HEADER STRUCTURAL PROTEIN 16-AUG-11 3J0I TITLE FITTING OF THE PHIKZ GP29PR STRUCTURE INTO THE CRYO-EM DENSITY MAP OF TITLE 2 THE PHIKZ POLYSHEATH COMPND MOL_ID: 1; COMPND 2 MOLECULE: PHIKZ029; COMPND 3 CHAIN: A, B, C, D, E, F; COMPND 4 FRAGMENT: PROTEASE-RESISTANT FRAGMENT OF GENE PRODUCT 29 (GP29PR, UNP COMPND 5 RESIDUES 96-390) SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PHAGE PHIKZ; SOURCE 3 ORGANISM_TAXID: 169683 KEYWDS BACTERIOPHAGE TAIL SHEATH, STRUCTURAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR A.A.AKSYUK,A.FOKINE,L.P.KUROCHKINA,V.V.MESYANZHINOV,M.G.ROSSMANN REVDAT 4 20-MAR-13 3J0I 1 SCALE1 SCALE2 SCALE3 REVDAT 3 25-JUL-12 3J0I 1 REMARK REVDAT 2 28-MAR-12 3J0I 1 JRNL REVDAT 1 14-DEC-11 3J0I 0 JRNL AUTH A.A.AKSYUK,L.P.KUROCHKINA,A.FOKINE,F.FOROUHAR, JRNL AUTH 2 V.V.MESYANZHINOV,L.TONG,M.G.ROSSMANN JRNL TITL STRUCTURAL CONSERVATION OF THE MYOVIRIDAE PHAGE TAIL SHEATH JRNL TITL 2 PROTEIN FOLD. JRNL REF STRUCTURE V. 19 1885 2011 JRNL REFN ISSN 0969-2126 JRNL PMID 22153511 JRNL DOI 10.1016/J.STR.2011.09.012 REMARK 2 REMARK 2 RESOLUTION. 19.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : EMFIT REMARK 3 RECONSTRUCTION SCHEMA : SPIDER SINGLE PARTICLE REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 3SPE REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : 2.490 REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : 2.490 REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 19.000 REMARK 3 NUMBER OF PARTICLES : NULL REMARK 3 CTF CORRECTION METHOD : NULL REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: FSC AT 0.5 CUT-OFF REMARK 4 REMARK 4 3J0I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-AUG-11. REMARK 100 THE RCSB ID CODE IS RCSB160096. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : VITREOUS ICE (CRYO EM) REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : CYCLIC REMARK 245 NAME OF SAMPLE : BACTERIOPHAGE PHIKZ POLYSHEATH REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : LIQUID ETHANE REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : NULL REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI/PHILIPS CM200FEG REMARK 245 DETECTOR TYPE : NULL REMARK 245 MINIMUM DEFOCUS (NM) : NULL REMARK 245 MAXIMUM DEFOCUS (NM) : NULL REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHTFIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : NULL REMARK 245 ILLUMINATION MODE : SPOTSCAN REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 200 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 LEU A 96 REMARK 465 ARG A 97 REMARK 465 PRO A 98 REMARK 465 GLU A 99 REMARK 465 ASP A 100 REMARK 465 ALA A 101 REMARK 465 ILE A 122 REMARK 465 ARG A 123 REMARK 465 ARG A 124 REMARK 465 LEU A 125 REMARK 465 SER A 126 REMARK 465 GLY A 127 REMARK 465 PHE A 128 REMARK 465 ASN A 129 REMARK 465 TYR A 130 REMARK 465 PRO A 131 REMARK 465 ASN A 132 REMARK 465 SER A 133 REMARK 465 VAL A 134 REMARK 465 ARG A 135 REMARK 465 ASP A 136 REMARK 465 ILE A 137 REMARK 465 GLY A 138 REMARK 465 ASN A 139 REMARK 465 ALA A 140 REMARK 465 PRO A 141 REMARK 465 VAL A 142 REMARK 465 PRO A 143 REMARK 465 THR A 144 REMARK 465 THR A 145 REMARK 465 ASP A 146 REMARK 465 VAL A 242 REMARK 465 GLY A 243 REMARK 465 THR A 244 REMARK 465 THR A 382 REMARK 465 THR A 383 REMARK 465 ASP A 384 REMARK 465 LEU A 385 REMARK 465 GLU A 386 REMARK 465 GLU A 387 REMARK 465 TYR A 388 REMARK 465 ALA A 389 REMARK 465 LYS A 390 REMARK 465 LEU B 96 REMARK 465 ARG B 97 REMARK 465 PRO B 98 REMARK 465 GLU B 99 REMARK 465 ASP B 100 REMARK 465 ALA B 101 REMARK 465 ILE B 122 REMARK 465 ARG B 123 REMARK 465 ARG B 124 REMARK 465 LEU B 125 REMARK 465 SER B 126 REMARK 465 GLY B 127 REMARK 465 PHE B 128 REMARK 465 ASN B 129 REMARK 465 TYR B 130 REMARK 465 PRO B 131 REMARK 465 ASN B 132 REMARK 465 SER B 133 REMARK 465 VAL B 134 REMARK 465 ARG B 135 REMARK 465 ASP B 136 REMARK 465 ILE B 137 REMARK 465 GLY B 138 REMARK 465 ASN B 139 REMARK 465 ALA B 140 REMARK 465 PRO B 141 REMARK 465 VAL B 142 REMARK 465 PRO B 143 REMARK 465 THR B 144 REMARK 465 THR B 145 REMARK 465 ASP B 146 REMARK 465 VAL B 242 REMARK 465 GLY B 243 REMARK 465 THR B 244 REMARK 465 THR B 382 REMARK 465 THR B 383 REMARK 465 ASP B 384 REMARK 465 LEU B 385 REMARK 465 GLU B 386 REMARK 465 GLU B 387 REMARK 465 TYR B 388 REMARK 465 ALA B 389 REMARK 465 LYS B 390 REMARK 465 LEU C 96 REMARK 465 ARG C 97 REMARK 465 PRO C 98 REMARK 465 GLU C 99 REMARK 465 ASP C 100 REMARK 465 ALA C 101 REMARK 465 ILE C 122 REMARK 465 ARG C 123 REMARK 465 ARG C 124 REMARK 465 LEU C 125 REMARK 465 SER C 126 REMARK 465 GLY C 127 REMARK 465 PHE C 128 REMARK 465 ASN C 129 REMARK 465 TYR C 130 REMARK 465 PRO C 131 REMARK 465 ASN C 132 REMARK 465 SER C 133 REMARK 465 VAL C 134 REMARK 465 ARG C 135 REMARK 465 ASP C 136 REMARK 465 ILE C 137 REMARK 465 GLY C 138 REMARK 465 ASN C 139 REMARK 465 ALA C 140 REMARK 465 PRO C 141 REMARK 465 VAL C 142 REMARK 465 PRO C 143 REMARK 465 THR C 144 REMARK 465 THR C 145 REMARK 465 ASP C 146 REMARK 465 VAL C 242 REMARK 465 GLY C 243 REMARK 465 THR C 244 REMARK 465 THR C 382 REMARK 465 THR C 383 REMARK 465 ASP C 384 REMARK 465 LEU C 385 REMARK 465 GLU C 386 REMARK 465 GLU C 387 REMARK 465 TYR C 388 REMARK 465 ALA C 389 REMARK 465 LYS C 390 REMARK 465 LEU D 96 REMARK 465 ARG D 97 REMARK 465 PRO D 98 REMARK 465 GLU D 99 REMARK 465 ASP D 100 REMARK 465 ALA D 101 REMARK 465 ILE D 122 REMARK 465 ARG D 123 REMARK 465 ARG D 124 REMARK 465 LEU D 125 REMARK 465 SER D 126 REMARK 465 GLY D 127 REMARK 465 PHE D 128 REMARK 465 ASN D 129 REMARK 465 TYR D 130 REMARK 465 PRO D 131 REMARK 465 ASN D 132 REMARK 465 SER D 133 REMARK 465 VAL D 134 REMARK 465 ARG D 135 REMARK 465 ASP D 136 REMARK 465 ILE D 137 REMARK 465 GLY D 138 REMARK 465 ASN D 139 REMARK 465 ALA D 140 REMARK 465 PRO D 141 REMARK 465 VAL D 142 REMARK 465 PRO D 143 REMARK 465 THR D 144 REMARK 465 THR D 145 REMARK 465 ASP D 146 REMARK 465 VAL D 242 REMARK 465 GLY D 243 REMARK 465 THR D 244 REMARK 465 THR D 382 REMARK 465 THR D 383 REMARK 465 ASP D 384 REMARK 465 LEU D 385 REMARK 465 GLU D 386 REMARK 465 GLU D 387 REMARK 465 TYR D 388 REMARK 465 ALA D 389 REMARK 465 LYS D 390 REMARK 465 LEU E 96 REMARK 465 ARG E 97 REMARK 465 PRO E 98 REMARK 465 GLU E 99 REMARK 465 ASP E 100 REMARK 465 ALA E 101 REMARK 465 ILE E 122 REMARK 465 ARG E 123 REMARK 465 ARG E 124 REMARK 465 LEU E 125 REMARK 465 SER E 126 REMARK 465 GLY E 127 REMARK 465 PHE E 128 REMARK 465 ASN E 129 REMARK 465 TYR E 130 REMARK 465 PRO E 131 REMARK 465 ASN E 132 REMARK 465 SER E 133 REMARK 465 VAL E 134 REMARK 465 ARG E 135 REMARK 465 ASP E 136 REMARK 465 ILE E 137 REMARK 465 GLY E 138 REMARK 465 ASN E 139 REMARK 465 ALA E 140 REMARK 465 PRO E 141 REMARK 465 VAL E 142 REMARK 465 PRO E 143 REMARK 465 THR E 144 REMARK 465 THR E 145 REMARK 465 ASP E 146 REMARK 465 VAL E 242 REMARK 465 GLY E 243 REMARK 465 THR E 244 REMARK 465 THR E 382 REMARK 465 THR E 383 REMARK 465 ASP E 384 REMARK 465 LEU E 385 REMARK 465 GLU E 386 REMARK 465 GLU E 387 REMARK 465 TYR E 388 REMARK 465 ALA E 389 REMARK 465 LYS E 390 REMARK 465 LEU F 96 REMARK 465 ARG F 97 REMARK 465 PRO F 98 REMARK 465 GLU F 99 REMARK 465 ASP F 100 REMARK 465 ALA F 101 REMARK 465 ILE F 122 REMARK 465 ARG F 123 REMARK 465 ARG F 124 REMARK 465 LEU F 125 REMARK 465 SER F 126 REMARK 465 GLY F 127 REMARK 465 PHE F 128 REMARK 465 ASN F 129 REMARK 465 TYR F 130 REMARK 465 PRO F 131 REMARK 465 ASN F 132 REMARK 465 SER F 133 REMARK 465 VAL F 134 REMARK 465 ARG F 135 REMARK 465 ASP F 136 REMARK 465 ILE F 137 REMARK 465 GLY F 138 REMARK 465 ASN F 139 REMARK 465 ALA F 140 REMARK 465 PRO F 141 REMARK 465 VAL F 142 REMARK 465 PRO F 143 REMARK 465 THR F 144 REMARK 465 THR F 145 REMARK 465 ASP F 146 REMARK 465 VAL F 242 REMARK 465 GLY F 243 REMARK 465 THR F 244 REMARK 465 THR F 382 REMARK 465 THR F 383 REMARK 465 ASP F 384 REMARK 465 LEU F 385 REMARK 465 GLU F 386 REMARK 465 GLU F 387 REMARK 465 TYR F 388 REMARK 465 ALA F 389 REMARK 465 LYS F 390 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 MET A 270 CG MET A 270 SD 0.168 REMARK 500 MET A 323 CG MET A 323 SD 0.157 REMARK 500 MET B 270 CG MET B 270 SD 0.168 REMARK 500 MET B 323 CG MET B 323 SD 0.157 REMARK 500 MET C 270 CG MET C 270 SD 0.169 REMARK 500 MET C 323 CG MET C 323 SD 0.157 REMARK 500 MET D 270 CG MET D 270 SD 0.168 REMARK 500 MET D 323 CG MET D 323 SD 0.157 REMARK 500 MET E 270 CG MET E 270 SD 0.168 REMARK 500 MET E 323 CG MET E 323 SD 0.157 REMARK 500 MET F 270 CG MET F 270 SD 0.169 REMARK 500 MET F 323 CG MET F 323 SD 0.157 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ALA A 214 CB - CA - C ANGL. DEV. = 9.6 DEGREES REMARK 500 ASP A 215 N - CA - CB ANGL. DEV. = -11.1 DEGREES REMARK 500 ASP A 215 N - CA - C ANGL. DEV. = 21.0 DEGREES REMARK 500 VAL A 290 N - CA - C ANGL. DEV. = 20.0 DEGREES REMARK 500 VAL A 291 N - CA - CB ANGL. DEV. = -18.7 DEGREES REMARK 500 VAL A 291 N - CA - C ANGL. DEV. = -18.0 DEGREES REMARK 500 ALA B 214 CB - CA - C ANGL. DEV. = 9.6 DEGREES REMARK 500 ASP B 215 N - CA - CB ANGL. DEV. = -11.2 DEGREES REMARK 500 ASP B 215 N - CA - C ANGL. DEV. = 21.1 DEGREES REMARK 500 VAL B 290 N - CA - C ANGL. DEV. = 19.9 DEGREES REMARK 500 VAL B 291 N - CA - CB ANGL. DEV. = -18.7 DEGREES REMARK 500 VAL B 291 N - CA - C ANGL. DEV. = -18.0 DEGREES REMARK 500 ALA C 214 CB - CA - C ANGL. DEV. = 9.6 DEGREES REMARK 500 ASP C 215 N - CA - CB ANGL. DEV. = -11.1 DEGREES REMARK 500 ASP C 215 N - CA - C ANGL. DEV. = 21.1 DEGREES REMARK 500 VAL C 290 N - CA - C ANGL. DEV. = 20.0 DEGREES REMARK 500 VAL C 291 N - CA - CB ANGL. DEV. = -18.8 DEGREES REMARK 500 VAL C 291 N - CA - C ANGL. DEV. = -18.0 DEGREES REMARK 500 ALA D 214 CB - CA - C ANGL. DEV. = 9.6 DEGREES REMARK 500 ASP D 215 N - CA - CB ANGL. DEV. = -11.1 DEGREES REMARK 500 ASP D 215 N - CA - C ANGL. DEV. = 21.0 DEGREES REMARK 500 VAL D 290 N - CA - C ANGL. DEV. = 20.0 DEGREES REMARK 500 VAL D 291 N - CA - CB ANGL. DEV. = -18.7 DEGREES REMARK 500 VAL D 291 N - CA - C ANGL. DEV. = -18.0 DEGREES REMARK 500 ALA E 214 CB - CA - C ANGL. DEV. = 9.6 DEGREES REMARK 500 ASP E 215 N - CA - CB ANGL. DEV. = -11.1 DEGREES REMARK 500 ASP E 215 N - CA - C ANGL. DEV. = 21.0 DEGREES REMARK 500 VAL E 290 N - CA - C ANGL. DEV. = 20.0 DEGREES REMARK 500 VAL E 291 N - CA - CB ANGL. DEV. = -18.8 DEGREES REMARK 500 VAL E 291 N - CA - C ANGL. DEV. = -18.0 DEGREES REMARK 500 ALA F 214 CB - CA - C ANGL. DEV. = 9.6 DEGREES REMARK 500 ASP F 215 N - CA - CB ANGL. DEV. = -11.1 DEGREES REMARK 500 ASP F 215 N - CA - C ANGL. DEV. = 21.1 DEGREES REMARK 500 VAL F 290 N - CA - C ANGL. DEV. = 20.0 DEGREES REMARK 500 VAL F 291 N - CA - CB ANGL. DEV. = -18.8 DEGREES REMARK 500 VAL F 291 N - CA - C ANGL. DEV. = -18.0 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 THR A 213 47.56 -80.24 REMARK 500 ASP A 253 5.94 -58.12 REMARK 500 GLN A 254 35.34 71.71 REMARK 500 ASN A 272 45.87 33.73 REMARK 500 ASP A 287 102.58 -164.26 REMARK 500 ALA A 329 -9.30 -57.40 REMARK 500 THR B 213 47.54 -80.21 REMARK 500 ASP B 253 5.98 -58.15 REMARK 500 GLN B 254 35.33 71.71 REMARK 500 ASN B 272 45.89 33.73 REMARK 500 ASP B 287 102.58 -164.24 REMARK 500 ALA B 329 -9.32 -57.45 REMARK 500 THR C 213 47.55 -80.24 REMARK 500 ASP C 253 5.94 -58.10 REMARK 500 GLN C 254 35.35 71.66 REMARK 500 ASN C 272 45.86 33.73 REMARK 500 ASP C 287 102.61 -164.25 REMARK 500 ALA C 329 -9.34 -57.37 REMARK 500 THR D 213 47.56 -80.24 REMARK 500 ASP D 253 5.94 -58.12 REMARK 500 GLN D 254 35.34 71.71 REMARK 500 ASN D 272 45.87 33.73 REMARK 500 ASP D 287 102.58 -164.26 REMARK 500 ALA D 329 -9.30 -57.40 REMARK 500 THR E 213 47.57 -80.27 REMARK 500 ASP E 253 5.93 -58.11 REMARK 500 GLN E 254 35.37 71.70 REMARK 500 ASN E 272 45.81 33.77 REMARK 500 ASP E 287 102.59 -164.28 REMARK 500 ALA E 329 -9.34 -57.35 REMARK 500 THR F 213 47.55 -80.24 REMARK 500 ASP F 253 5.91 -58.10 REMARK 500 GLN F 254 35.30 71.75 REMARK 500 ASN F 272 45.86 33.73 REMARK 500 ASP F 287 102.61 -164.26 REMARK 500 ALA F 329 -9.34 -57.37 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 ASP A 215 24.7 L L OUTSIDE RANGE REMARK 500 VAL A 290 9.2 L L EXPECTING SP3 REMARK 500 VAL A 291 55.2 L L OUTSIDE RANGE REMARK 500 ASP B 215 24.7 L L OUTSIDE RANGE REMARK 500 VAL B 290 9.2 L L EXPECTING SP3 REMARK 500 VAL B 291 55.2 L L OUTSIDE RANGE REMARK 500 ASP C 215 24.7 L L OUTSIDE RANGE REMARK 500 VAL C 290 9.2 L L EXPECTING SP3 REMARK 500 VAL C 291 55.2 L L OUTSIDE RANGE REMARK 500 ASP D 215 24.7 L L OUTSIDE RANGE REMARK 500 VAL D 290 9.2 L L EXPECTING SP3 REMARK 500 VAL D 291 55.2 L L OUTSIDE RANGE REMARK 500 ASP E 215 24.7 L L OUTSIDE RANGE REMARK 500 VAL E 290 9.2 L L EXPECTING SP3 REMARK 500 VAL E 291 55.2 L L OUTSIDE RANGE REMARK 500 ASP F 215 24.7 L L OUTSIDE RANGE REMARK 500 VAL F 290 9.2 L L EXPECTING SP3 REMARK 500 VAL F 291 55.2 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3SPE RELATED DB: PDB REMARK 900 RELATED ID: 5331 RELATED DB: EMDB REMARK 900 CRYO-EM DENSITY MAP OF THE PHIKZ POLYSHEATH USED FOR THE REMARK 900 FITTING REMARK 900 RELATED ID: 5332 RELATED DB: EMDB REMARK 900 CRYO-EM DENSITY MAP OF THE PHIKZ EXTENDED TAIL SHEATH REMARK 900 RELATED ID: 3J0H RELATED DB: PDB REMARK 900 FITTED COORDINATES INTO THE PHIKZ EXTENDED TAIL SHEATH MAP REMARK 900 RELATED ID: 3HXL RELATED DB: PDB REMARK 900 RELATED ID: 3LML RELATED DB: PDB DBREF 3J0I A 96 390 UNP Q8SDD3 Q8SDD3_BPDPK 96 390 DBREF 3J0I B 96 390 UNP Q8SDD3 Q8SDD3_BPDPK 96 390 DBREF 3J0I C 96 390 UNP Q8SDD3 Q8SDD3_BPDPK 96 390 DBREF 3J0I D 96 390 UNP Q8SDD3 Q8SDD3_BPDPK 96 390 DBREF 3J0I E 96 390 UNP Q8SDD3 Q8SDD3_BPDPK 96 390 DBREF 3J0I F 96 390 UNP Q8SDD3 Q8SDD3_BPDPK 96 390 SEQRES 1 A 295 LEU ARG PRO GLU ASP ALA ALA ASN PRO SER ARG LEU ILE SEQRES 2 A 295 VAL ALA ILE GLU ILE VAL GLU ASP GLU ILE PRO LEU THR SEQRES 3 A 295 ILE ARG ARG LEU SER GLY PHE ASN TYR PRO ASN SER VAL SEQRES 4 A 295 ARG ASP ILE GLY ASN ALA PRO VAL PRO THR THR ASP LYS SEQRES 5 A 295 VAL ASP GLY LEU LYS ALA ARG ILE ILE LEU ILE GLU ASP SEQRES 6 A 295 ASN THR SER GLU VAL GLY THR GLN ARG VAL LEU PRO GLY SEQRES 7 A 295 THR LEU VAL SER ASP LYS ASP GLY SER GLN SER LEU VAL SEQRES 8 A 295 TYR PRO LEU PHE GLU ALA PRO VAL SER PHE PHE GLY LYS SEQRES 9 A 295 LEU GLY ASP SER ASN GLY MET ARG VAL TRP SER THR THR SEQRES 10 A 295 THR ALA ASP ILE GLU GLU PHE ASP GLU ALA ALA MET ALA SEQRES 11 A 295 LYS PHE LYS THR ARG GLN PHE ARG ILE GLN LEU ILE GLU SEQRES 12 A 295 LYS PRO GLU VAL GLY THR SER PRO VAL ILE VAL LYS THR SEQRES 13 A 295 ALA ASP GLN GLN ASP TYR LEU ASN ILE THR PHE ASP LYS SEQRES 14 A 295 GLY VAL TYR SER ASP MET TYR ASN ALA ASP LEU TYR VAL SEQRES 15 A 295 GLY ASP VAL LEU VAL ASP SER TYR SER ASP ASP GLY VAL SEQRES 16 A 295 VAL SER GLY LEU SER PRO LEU TYR SER PRO PHE SER GLN SEQRES 17 A 295 PHE TYR VAL TYR HIS GLU ASN ILE ASP LEU VAL ARG GLN SEQRES 18 A 295 MET ILE TYR ASP THR GLU MET ARG VAL ASN PRO ALA ALA SEQRES 19 A 295 ALA ALA HIS THR THR ALA PRO GLY GLU ILE ASP PHE LEU SEQRES 20 A 295 THR PHE LEU ALA VAL ASP GLY ASP PRO TYR GLN GLY ILE SEQRES 21 A 295 GLN VAL LEU GLY PRO LEU ASP GLY GLY ILE THR LEU GLY SEQRES 22 A 295 LYS ASP GLY ASN ILE TYR ALA SER GLY GLY THR ASP GLY SEQRES 23 A 295 THR THR ASP LEU GLU GLU TYR ALA LYS SEQRES 1 B 295 LEU ARG PRO GLU ASP ALA ALA ASN PRO SER ARG LEU ILE SEQRES 2 B 295 VAL ALA ILE GLU ILE VAL GLU ASP GLU ILE PRO LEU THR SEQRES 3 B 295 ILE ARG ARG LEU SER GLY PHE ASN TYR PRO ASN SER VAL SEQRES 4 B 295 ARG ASP ILE GLY ASN ALA PRO VAL PRO THR THR ASP LYS SEQRES 5 B 295 VAL ASP GLY LEU LYS ALA ARG ILE ILE LEU ILE GLU ASP SEQRES 6 B 295 ASN THR SER GLU VAL GLY THR GLN ARG VAL LEU PRO GLY SEQRES 7 B 295 THR LEU VAL SER ASP LYS ASP GLY SER GLN SER LEU VAL SEQRES 8 B 295 TYR PRO LEU PHE GLU ALA PRO VAL SER PHE PHE GLY LYS SEQRES 9 B 295 LEU GLY ASP SER ASN GLY MET ARG VAL TRP SER THR THR SEQRES 10 B 295 THR ALA ASP ILE GLU GLU PHE ASP GLU ALA ALA MET ALA SEQRES 11 B 295 LYS PHE LYS THR ARG GLN PHE ARG ILE GLN LEU ILE GLU SEQRES 12 B 295 LYS PRO GLU VAL GLY THR SER PRO VAL ILE VAL LYS THR SEQRES 13 B 295 ALA ASP GLN GLN ASP TYR LEU ASN ILE THR PHE ASP LYS SEQRES 14 B 295 GLY VAL TYR SER ASP MET TYR ASN ALA ASP LEU TYR VAL SEQRES 15 B 295 GLY ASP VAL LEU VAL ASP SER TYR SER ASP ASP GLY VAL SEQRES 16 B 295 VAL SER GLY LEU SER PRO LEU TYR SER PRO PHE SER GLN SEQRES 17 B 295 PHE TYR VAL TYR HIS GLU ASN ILE ASP LEU VAL ARG GLN SEQRES 18 B 295 MET ILE TYR ASP THR GLU MET ARG VAL ASN PRO ALA ALA SEQRES 19 B 295 ALA ALA HIS THR THR ALA PRO GLY GLU ILE ASP PHE LEU SEQRES 20 B 295 THR PHE LEU ALA VAL ASP GLY ASP PRO TYR GLN GLY ILE SEQRES 21 B 295 GLN VAL LEU GLY PRO LEU ASP GLY GLY ILE THR LEU GLY SEQRES 22 B 295 LYS ASP GLY ASN ILE TYR ALA SER GLY GLY THR ASP GLY SEQRES 23 B 295 THR THR ASP LEU GLU GLU TYR ALA LYS SEQRES 1 C 295 LEU ARG PRO GLU ASP ALA ALA ASN PRO SER ARG LEU ILE SEQRES 2 C 295 VAL ALA ILE GLU ILE VAL GLU ASP GLU ILE PRO LEU THR SEQRES 3 C 295 ILE ARG ARG LEU SER GLY PHE ASN TYR PRO ASN SER VAL SEQRES 4 C 295 ARG ASP ILE GLY ASN ALA PRO VAL PRO THR THR ASP LYS SEQRES 5 C 295 VAL ASP GLY LEU LYS ALA ARG ILE ILE LEU ILE GLU ASP SEQRES 6 C 295 ASN THR SER GLU VAL GLY THR GLN ARG VAL LEU PRO GLY SEQRES 7 C 295 THR LEU VAL SER ASP LYS ASP GLY SER GLN SER LEU VAL SEQRES 8 C 295 TYR PRO LEU PHE GLU ALA PRO VAL SER PHE PHE GLY LYS SEQRES 9 C 295 LEU GLY ASP SER ASN GLY MET ARG VAL TRP SER THR THR SEQRES 10 C 295 THR ALA ASP ILE GLU GLU PHE ASP GLU ALA ALA MET ALA SEQRES 11 C 295 LYS PHE LYS THR ARG GLN PHE ARG ILE GLN LEU ILE GLU SEQRES 12 C 295 LYS PRO GLU VAL GLY THR SER PRO VAL ILE VAL LYS THR SEQRES 13 C 295 ALA ASP GLN GLN ASP TYR LEU ASN ILE THR PHE ASP LYS SEQRES 14 C 295 GLY VAL TYR SER ASP MET TYR ASN ALA ASP LEU TYR VAL SEQRES 15 C 295 GLY ASP VAL LEU VAL ASP SER TYR SER ASP ASP GLY VAL SEQRES 16 C 295 VAL SER GLY LEU SER PRO LEU TYR SER PRO PHE SER GLN SEQRES 17 C 295 PHE TYR VAL TYR HIS GLU ASN ILE ASP LEU VAL ARG GLN SEQRES 18 C 295 MET ILE TYR ASP THR GLU MET ARG VAL ASN PRO ALA ALA SEQRES 19 C 295 ALA ALA HIS THR THR ALA PRO GLY GLU ILE ASP PHE LEU SEQRES 20 C 295 THR PHE LEU ALA VAL ASP GLY ASP PRO TYR GLN GLY ILE SEQRES 21 C 295 GLN VAL LEU GLY PRO LEU ASP GLY GLY ILE THR LEU GLY SEQRES 22 C 295 LYS ASP GLY ASN ILE TYR ALA SER GLY GLY THR ASP GLY SEQRES 23 C 295 THR THR ASP LEU GLU GLU TYR ALA LYS SEQRES 1 D 295 LEU ARG PRO GLU ASP ALA ALA ASN PRO SER ARG LEU ILE SEQRES 2 D 295 VAL ALA ILE GLU ILE VAL GLU ASP GLU ILE PRO LEU THR SEQRES 3 D 295 ILE ARG ARG LEU SER GLY PHE ASN TYR PRO ASN SER VAL SEQRES 4 D 295 ARG ASP ILE GLY ASN ALA PRO VAL PRO THR THR ASP LYS SEQRES 5 D 295 VAL ASP GLY LEU LYS ALA ARG ILE ILE LEU ILE GLU ASP SEQRES 6 D 295 ASN THR SER GLU VAL GLY THR GLN ARG VAL LEU PRO GLY SEQRES 7 D 295 THR LEU VAL SER ASP LYS ASP GLY SER GLN SER LEU VAL SEQRES 8 D 295 TYR PRO LEU PHE GLU ALA PRO VAL SER PHE PHE GLY LYS SEQRES 9 D 295 LEU GLY ASP SER ASN GLY MET ARG VAL TRP SER THR THR SEQRES 10 D 295 THR ALA ASP ILE GLU GLU PHE ASP GLU ALA ALA MET ALA SEQRES 11 D 295 LYS PHE LYS THR ARG GLN PHE ARG ILE GLN LEU ILE GLU SEQRES 12 D 295 LYS PRO GLU VAL GLY THR SER PRO VAL ILE VAL LYS THR SEQRES 13 D 295 ALA ASP GLN GLN ASP TYR LEU ASN ILE THR PHE ASP LYS SEQRES 14 D 295 GLY VAL TYR SER ASP MET TYR ASN ALA ASP LEU TYR VAL SEQRES 15 D 295 GLY ASP VAL LEU VAL ASP SER TYR SER ASP ASP GLY VAL SEQRES 16 D 295 VAL SER GLY LEU SER PRO LEU TYR SER PRO PHE SER GLN SEQRES 17 D 295 PHE TYR VAL TYR HIS GLU ASN ILE ASP LEU VAL ARG GLN SEQRES 18 D 295 MET ILE TYR ASP THR GLU MET ARG VAL ASN PRO ALA ALA SEQRES 19 D 295 ALA ALA HIS THR THR ALA PRO GLY GLU ILE ASP PHE LEU SEQRES 20 D 295 THR PHE LEU ALA VAL ASP GLY ASP PRO TYR GLN GLY ILE SEQRES 21 D 295 GLN VAL LEU GLY PRO LEU ASP GLY GLY ILE THR LEU GLY SEQRES 22 D 295 LYS ASP GLY ASN ILE TYR ALA SER GLY GLY THR ASP GLY SEQRES 23 D 295 THR THR ASP LEU GLU GLU TYR ALA LYS SEQRES 1 E 295 LEU ARG PRO GLU ASP ALA ALA ASN PRO SER ARG LEU ILE SEQRES 2 E 295 VAL ALA ILE GLU ILE VAL GLU ASP GLU ILE PRO LEU THR SEQRES 3 E 295 ILE ARG ARG LEU SER GLY PHE ASN TYR PRO ASN SER VAL SEQRES 4 E 295 ARG ASP ILE GLY ASN ALA PRO VAL PRO THR THR ASP LYS SEQRES 5 E 295 VAL ASP GLY LEU LYS ALA ARG ILE ILE LEU ILE GLU ASP SEQRES 6 E 295 ASN THR SER GLU VAL GLY THR GLN ARG VAL LEU PRO GLY SEQRES 7 E 295 THR LEU VAL SER ASP LYS ASP GLY SER GLN SER LEU VAL SEQRES 8 E 295 TYR PRO LEU PHE GLU ALA PRO VAL SER PHE PHE GLY LYS SEQRES 9 E 295 LEU GLY ASP SER ASN GLY MET ARG VAL TRP SER THR THR SEQRES 10 E 295 THR ALA ASP ILE GLU GLU PHE ASP GLU ALA ALA MET ALA SEQRES 11 E 295 LYS PHE LYS THR ARG GLN PHE ARG ILE GLN LEU ILE GLU SEQRES 12 E 295 LYS PRO GLU VAL GLY THR SER PRO VAL ILE VAL LYS THR SEQRES 13 E 295 ALA ASP GLN GLN ASP TYR LEU ASN ILE THR PHE ASP LYS SEQRES 14 E 295 GLY VAL TYR SER ASP MET TYR ASN ALA ASP LEU TYR VAL SEQRES 15 E 295 GLY ASP VAL LEU VAL ASP SER TYR SER ASP ASP GLY VAL SEQRES 16 E 295 VAL SER GLY LEU SER PRO LEU TYR SER PRO PHE SER GLN SEQRES 17 E 295 PHE TYR VAL TYR HIS GLU ASN ILE ASP LEU VAL ARG GLN SEQRES 18 E 295 MET ILE TYR ASP THR GLU MET ARG VAL ASN PRO ALA ALA SEQRES 19 E 295 ALA ALA HIS THR THR ALA PRO GLY GLU ILE ASP PHE LEU SEQRES 20 E 295 THR PHE LEU ALA VAL ASP GLY ASP PRO TYR GLN GLY ILE SEQRES 21 E 295 GLN VAL LEU GLY PRO LEU ASP GLY GLY ILE THR LEU GLY SEQRES 22 E 295 LYS ASP GLY ASN ILE TYR ALA SER GLY GLY THR ASP GLY SEQRES 23 E 295 THR THR ASP LEU GLU GLU TYR ALA LYS SEQRES 1 F 295 LEU ARG PRO GLU ASP ALA ALA ASN PRO SER ARG LEU ILE SEQRES 2 F 295 VAL ALA ILE GLU ILE VAL GLU ASP GLU ILE PRO LEU THR SEQRES 3 F 295 ILE ARG ARG LEU SER GLY PHE ASN TYR PRO ASN SER VAL SEQRES 4 F 295 ARG ASP ILE GLY ASN ALA PRO VAL PRO THR THR ASP LYS SEQRES 5 F 295 VAL ASP GLY LEU LYS ALA ARG ILE ILE LEU ILE GLU ASP SEQRES 6 F 295 ASN THR SER GLU VAL GLY THR GLN ARG VAL LEU PRO GLY SEQRES 7 F 295 THR LEU VAL SER ASP LYS ASP GLY SER GLN SER LEU VAL SEQRES 8 F 295 TYR PRO LEU PHE GLU ALA PRO VAL SER PHE PHE GLY LYS SEQRES 9 F 295 LEU GLY ASP SER ASN GLY MET ARG VAL TRP SER THR THR SEQRES 10 F 295 THR ALA ASP ILE GLU GLU PHE ASP GLU ALA ALA MET ALA SEQRES 11 F 295 LYS PHE LYS THR ARG GLN PHE ARG ILE GLN LEU ILE GLU SEQRES 12 F 295 LYS PRO GLU VAL GLY THR SER PRO VAL ILE VAL LYS THR SEQRES 13 F 295 ALA ASP GLN GLN ASP TYR LEU ASN ILE THR PHE ASP LYS SEQRES 14 F 295 GLY VAL TYR SER ASP MET TYR ASN ALA ASP LEU TYR VAL SEQRES 15 F 295 GLY ASP VAL LEU VAL ASP SER TYR SER ASP ASP GLY VAL SEQRES 16 F 295 VAL SER GLY LEU SER PRO LEU TYR SER PRO PHE SER GLN SEQRES 17 F 295 PHE TYR VAL TYR HIS GLU ASN ILE ASP LEU VAL ARG GLN SEQRES 18 F 295 MET ILE TYR ASP THR GLU MET ARG VAL ASN PRO ALA ALA SEQRES 19 F 295 ALA ALA HIS THR THR ALA PRO GLY GLU ILE ASP PHE LEU SEQRES 20 F 295 THR PHE LEU ALA VAL ASP GLY ASP PRO TYR GLN GLY ILE SEQRES 21 F 295 GLN VAL LEU GLY PRO LEU ASP GLY GLY ILE THR LEU GLY SEQRES 22 F 295 LYS ASP GLY ASN ILE TYR ALA SER GLY GLY THR ASP GLY SEQRES 23 F 295 THR THR ASP LEU GLU GLU TYR ALA LYS HELIX 1 1 GLY A 198 ASP A 202 5 5 HELIX 2 2 ASP A 220 LYS A 228 1 9 HELIX 3 3 TYR A 276 TYR A 285 1 10 HELIX 4 4 TYR A 307 ASN A 326 1 20 HELIX 5 5 PRO A 327 HIS A 332 5 6 HELIX 6 6 ALA A 335 ILE A 339 5 5 HELIX 7 7 GLY A 359 GLY A 363 5 5 HELIX 8 8 GLY B 198 ASP B 202 5 5 HELIX 9 9 ASP B 220 LYS B 228 1 9 HELIX 10 10 TYR B 276 TYR B 285 1 10 HELIX 11 11 TYR B 307 ASN B 326 1 20 HELIX 12 12 PRO B 327 HIS B 332 5 6 HELIX 13 13 ALA B 335 ILE B 339 5 5 HELIX 14 14 GLY B 359 GLY B 363 5 5 HELIX 15 15 GLY C 198 ASP C 202 5 5 HELIX 16 16 ASP C 220 LYS C 228 1 9 HELIX 17 17 TYR C 276 TYR C 285 1 10 HELIX 18 18 TYR C 307 ASN C 326 1 20 HELIX 19 19 PRO C 327 HIS C 332 5 6 HELIX 20 20 ALA C 335 ILE C 339 5 5 HELIX 21 21 GLY C 359 GLY C 363 5 5 HELIX 22 22 GLY D 198 ASP D 202 5 5 HELIX 23 23 ASP D 220 LYS D 228 1 9 HELIX 24 24 TYR D 276 TYR D 285 1 10 HELIX 25 25 TYR D 307 ASN D 326 1 20 HELIX 26 26 PRO D 327 HIS D 332 5 6 HELIX 27 27 ALA D 335 ILE D 339 5 5 HELIX 28 28 GLY D 359 GLY D 363 5 5 HELIX 29 29 GLY E 198 ASP E 202 5 5 HELIX 30 30 ASP E 220 LYS E 228 1 9 HELIX 31 31 TYR E 276 TYR E 285 1 10 HELIX 32 32 TYR E 307 ASN E 326 1 20 HELIX 33 33 PRO E 327 HIS E 332 5 6 HELIX 34 34 ALA E 335 ILE E 339 5 5 HELIX 35 35 GLY E 359 GLY E 363 5 5 HELIX 36 36 GLY F 198 ASP F 202 5 5 HELIX 37 37 ASP F 220 LYS F 228 1 9 HELIX 38 38 TYR F 276 TYR F 285 1 10 HELIX 39 39 TYR F 307 ASN F 326 1 20 HELIX 40 40 PRO F 327 HIS F 332 5 6 HELIX 41 41 ALA F 335 ILE F 339 5 5 HELIX 42 42 GLY F 359 GLY F 363 5 5 SHEET 1 A 3 LEU A 171 VAL A 176 0 SHEET 2 A 3 GLN A 183 PRO A 193 -1 O VAL A 186 N LEU A 171 SHEET 3 A 3 TYR A 305 VAL A 306 -1 O TYR A 305 N GLU A 191 SHEET 1 B 5 LEU A 171 VAL A 176 0 SHEET 2 B 5 GLN A 183 PRO A 193 -1 O VAL A 186 N LEU A 171 SHEET 3 B 5 ARG A 106 ILE A 118 -1 N VAL A 109 O LEU A 189 SHEET 4 B 5 VAL A 148 LEU A 157 -1 O LYS A 152 N VAL A 114 SHEET 5 B 5 ILE A 355 VAL A 357 1 O GLN A 356 N ALA A 153 SHEET 1 C 3 VAL A 247 ILE A 248 0 SHEET 2 C 3 PHE A 232 GLU A 238 -1 N GLU A 238 O VAL A 247 SHEET 3 C 3 LEU A 258 ILE A 260 -1 O ILE A 260 N PHE A 232 SHEET 1 D 4 VAL A 247 ILE A 248 0 SHEET 2 D 4 PHE A 232 GLU A 238 -1 N GLU A 238 O VAL A 247 SHEET 3 D 4 ASN A 204 SER A 210 -1 N TRP A 209 O ARG A 233 SHEET 4 D 4 ILE A 373 TYR A 374 -1 O ILE A 373 N MET A 206 SHEET 1 E 2 TYR A 267 SER A 268 0 SHEET 2 E 2 ALA A 273 ASP A 274 -1 O ALA A 273 N SER A 268 SHEET 1 F 3 LEU B 171 VAL B 176 0 SHEET 2 F 3 GLN B 183 PRO B 193 -1 O VAL B 186 N LEU B 171 SHEET 3 F 3 TYR B 305 VAL B 306 -1 O TYR B 305 N GLU B 191 SHEET 1 G 5 LEU B 171 VAL B 176 0 SHEET 2 G 5 GLN B 183 PRO B 193 -1 O VAL B 186 N LEU B 171 SHEET 3 G 5 ARG B 106 ILE B 118 -1 N VAL B 109 O LEU B 189 SHEET 4 G 5 VAL B 148 LEU B 157 -1 O LYS B 152 N VAL B 114 SHEET 5 G 5 ILE B 355 VAL B 357 1 O GLN B 356 N ALA B 153 SHEET 1 H 3 VAL B 247 ILE B 248 0 SHEET 2 H 3 PHE B 232 GLU B 238 -1 N GLU B 238 O VAL B 247 SHEET 3 H 3 LEU B 258 ILE B 260 -1 O ILE B 260 N PHE B 232 SHEET 1 I 4 VAL B 247 ILE B 248 0 SHEET 2 I 4 PHE B 232 GLU B 238 -1 N GLU B 238 O VAL B 247 SHEET 3 I 4 ASN B 204 SER B 210 -1 N TRP B 209 O ARG B 233 SHEET 4 I 4 ILE B 373 TYR B 374 -1 O ILE B 373 N MET B 206 SHEET 1 J 2 TYR B 267 SER B 268 0 SHEET 2 J 2 ALA B 273 ASP B 274 -1 O ALA B 273 N SER B 268 SHEET 1 K 3 LEU C 171 VAL C 176 0 SHEET 2 K 3 GLN C 183 PRO C 193 -1 O VAL C 186 N LEU C 171 SHEET 3 K 3 TYR C 305 VAL C 306 -1 O TYR C 305 N GLU C 191 SHEET 1 L 5 LEU C 171 VAL C 176 0 SHEET 2 L 5 GLN C 183 PRO C 193 -1 O VAL C 186 N LEU C 171 SHEET 3 L 5 ARG C 106 ILE C 118 -1 N VAL C 109 O LEU C 189 SHEET 4 L 5 VAL C 148 LEU C 157 -1 O LYS C 152 N VAL C 114 SHEET 5 L 5 ILE C 355 VAL C 357 1 O GLN C 356 N ALA C 153 SHEET 1 M 3 VAL C 247 ILE C 248 0 SHEET 2 M 3 PHE C 232 GLU C 238 -1 N GLU C 238 O VAL C 247 SHEET 3 M 3 LEU C 258 ILE C 260 -1 O ILE C 260 N PHE C 232 SHEET 1 N 4 VAL C 247 ILE C 248 0 SHEET 2 N 4 PHE C 232 GLU C 238 -1 N GLU C 238 O VAL C 247 SHEET 3 N 4 ASN C 204 SER C 210 -1 N TRP C 209 O ARG C 233 SHEET 4 N 4 ILE C 373 TYR C 374 -1 O ILE C 373 N MET C 206 SHEET 1 O 2 TYR C 267 SER C 268 0 SHEET 2 O 2 ALA C 273 ASP C 274 -1 O ALA C 273 N SER C 268 SHEET 1 P 3 LEU D 171 VAL D 176 0 SHEET 2 P 3 GLN D 183 PRO D 193 -1 O VAL D 186 N LEU D 171 SHEET 3 P 3 TYR D 305 VAL D 306 -1 O TYR D 305 N GLU D 191 SHEET 1 Q 5 LEU D 171 VAL D 176 0 SHEET 2 Q 5 GLN D 183 PRO D 193 -1 O VAL D 186 N LEU D 171 SHEET 3 Q 5 ARG D 106 ILE D 118 -1 N VAL D 109 O LEU D 189 SHEET 4 Q 5 VAL D 148 LEU D 157 -1 O LYS D 152 N VAL D 114 SHEET 5 Q 5 ILE D 355 VAL D 357 1 O GLN D 356 N ALA D 153 SHEET 1 R 3 VAL D 247 ILE D 248 0 SHEET 2 R 3 PHE D 232 GLU D 238 -1 N GLU D 238 O VAL D 247 SHEET 3 R 3 LEU D 258 ILE D 260 -1 O ILE D 260 N PHE D 232 SHEET 1 S 4 VAL D 247 ILE D 248 0 SHEET 2 S 4 PHE D 232 GLU D 238 -1 N GLU D 238 O VAL D 247 SHEET 3 S 4 ASN D 204 SER D 210 -1 N TRP D 209 O ARG D 233 SHEET 4 S 4 ILE D 373 TYR D 374 -1 O ILE D 373 N MET D 206 SHEET 1 T 2 TYR D 267 SER D 268 0 SHEET 2 T 2 ALA D 273 ASP D 274 -1 O ALA D 273 N SER D 268 SHEET 1 U 3 LEU E 171 VAL E 176 0 SHEET 2 U 3 GLN E 183 PRO E 193 -1 O VAL E 186 N LEU E 171 SHEET 3 U 3 TYR E 305 VAL E 306 -1 O TYR E 305 N GLU E 191 SHEET 1 V 5 LEU E 171 VAL E 176 0 SHEET 2 V 5 GLN E 183 PRO E 193 -1 O VAL E 186 N LEU E 171 SHEET 3 V 5 ARG E 106 ILE E 118 -1 N VAL E 109 O LEU E 189 SHEET 4 V 5 VAL E 148 LEU E 157 -1 O LYS E 152 N VAL E 114 SHEET 5 V 5 ILE E 355 VAL E 357 1 O GLN E 356 N ALA E 153 SHEET 1 W 3 VAL E 247 ILE E 248 0 SHEET 2 W 3 PHE E 232 GLU E 238 -1 N GLU E 238 O VAL E 247 SHEET 3 W 3 LEU E 258 ILE E 260 -1 O ILE E 260 N PHE E 232 SHEET 1 X 4 VAL E 247 ILE E 248 0 SHEET 2 X 4 PHE E 232 GLU E 238 -1 N GLU E 238 O VAL E 247 SHEET 3 X 4 ASN E 204 SER E 210 -1 N TRP E 209 O ARG E 233 SHEET 4 X 4 ILE E 373 TYR E 374 -1 O ILE E 373 N MET E 206 SHEET 1 Y 2 TYR E 267 SER E 268 0 SHEET 2 Y 2 ALA E 273 ASP E 274 -1 O ALA E 273 N SER E 268 SHEET 1 Z 3 LEU F 171 VAL F 176 0 SHEET 2 Z 3 GLN F 183 PRO F 193 -1 O VAL F 186 N LEU F 171 SHEET 3 Z 3 TYR F 305 VAL F 306 -1 O TYR F 305 N GLU F 191 SHEET 1 AA 5 LEU F 171 VAL F 176 0 SHEET 2 AA 5 GLN F 183 PRO F 193 -1 O VAL F 186 N LEU F 171 SHEET 3 AA 5 ARG F 106 ILE F 118 -1 N VAL F 109 O LEU F 189 SHEET 4 AA 5 VAL F 148 LEU F 157 -1 O LYS F 152 N VAL F 114 SHEET 5 AA 5 ILE F 355 VAL F 357 1 O GLN F 356 N ALA F 153 SHEET 1 AB 3 VAL F 247 ILE F 248 0 SHEET 2 AB 3 PHE F 232 GLU F 238 -1 N GLU F 238 O VAL F 247 SHEET 3 AB 3 LEU F 258 ILE F 260 -1 O ILE F 260 N PHE F 232 SHEET 1 AC 4 VAL F 247 ILE F 248 0 SHEET 2 AC 4 PHE F 232 GLU F 238 -1 N GLU F 238 O VAL F 247 SHEET 3 AC 4 ASN F 204 SER F 210 -1 N TRP F 209 O ARG F 233 SHEET 4 AC 4 ILE F 373 TYR F 374 -1 O ILE F 373 N MET F 206 SHEET 1 AD 2 TYR F 267 SER F 268 0 SHEET 2 AD 2 ALA F 273 ASP F 274 -1 O ALA F 273 N SER F 268 CISPEP 1 LYS A 239 PRO A 240 0 8.81 CISPEP 2 LYS B 239 PRO B 240 0 8.83 CISPEP 3 LYS C 239 PRO C 240 0 8.79 CISPEP 4 LYS D 239 PRO D 240 0 8.81 CISPEP 5 LYS E 239 PRO E 240 0 8.84 CISPEP 6 LYS F 239 PRO F 240 0 8.79 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000 ATOM 1 N ALA A 102 -78.359 78.782 -27.033 1.00100.71 N ANISOU 1 N ALA A 102 13065 12694 12506 -330 -701 424 N ATOM 2 CA ALA A 102 -79.173 77.658 -27.487 1.00 93.80 C ANISOU 2 CA ALA A 102 12213 11808 11621 -341 -714 425 C ATOM 3 C ALA A 102 -80.646 78.034 -27.628 1.00 86.86 C ANISOU 3 C ALA A 102 11315 10942 10744 -290 -682 394 C ATOM 4 O ALA A 102 -81.314 77.591 -28.561 1.00110.24 O ANISOU 4 O ALA A 102 14282 13874 13729 -287 -704 388 O ATOM 5 CB ALA A 102 -79.012 76.461 -26.548 1.00 86.29 C ANISOU 5 CB ALA A 102 11294 10890 10604 -385 -704 441 C ATOM 6 N ASN A 103 -81.149 78.852 -26.706 1.00 50.14 N ANISOU 6 N ASN A 103 6644 6335 6070 -251 -631 377 N ATOM 7 CA ASN A 103 -82.587 79.134 -26.638 1.00 46.47 C ANISOU 7 CA ASN A 103 6167 5889 5599 -207 -598 352 C ATOM 8 C ASN A 103 -82.888 80.605 -26.425 1.00 41.31 C ANISOU 8 C ASN A 103 5477 5254 4965 -157 -567 333 C ATOM 9 O ASN A 103 -82.306 81.240 -25.549 1.00 70.84 O ANISOU 9 O ASN A 103 9205 9026 8687 -150 -544 336 O ATOM 10 CB ASN A 103 -83.232 78.337 -25.502 1.00 73.18 C ANISOU 10 CB ASN A 103 9572 9315 8918 -211 -564 352 C ATOM 11 CG ASN A 103 -83.480 76.893 -25.871 1.00101.46 C ANISOU 11 CG ASN A 103 13188 12882 12480 -253 -589 362 C ATOM 12 OD1 ASN A 103 -83.871 76.591 -27.000 1.00111.92 O ANISOU 12 OD1 ASN A 103 14518 14170 13839 -256 -621 360 O ATOM 13 ND2 ASN A 103 -83.256 75.987 -24.921 1.00103.25 N ANISOU 13 ND2 ASN A 103 13440 13139 12651 -289 -576 372 N ATOM 14 N PRO A 104 -83.802 81.160 -27.229 1.00 26.12 N ANISOU 14 N PRO A 104 3535 3313 3076 -126 -565 313 N ATOM 15 CA PRO A 104 -84.131 82.574 -27.046 1.00 23.05 C ANISOU 15 CA PRO A 104 3110 2945 2702 -84 -535 296 C ATOM 16 C PRO A 104 -84.878 82.789 -25.739 1.00 33.53 C ANISOU 16 C PRO A 104 4435 4326 3979 -53 -486 293 C ATOM 17 O PRO A 104 -85.488 81.854 -25.196 1.00 57.51 O ANISOU 17 O PRO A 104 7497 7376 6976 -58 -474 298 O ATOM 18 CB PRO A 104 -85.052 82.880 -28.233 1.00 34.60 C ANISOU 18 CB PRO A 104 4561 4376 4209 -67 -547 275 C ATOM 19 CG PRO A 104 -84.859 81.756 -29.192 1.00 34.14 C ANISOU 19 CG PRO A 104 4530 4272 4172 -101 -593 283 C ATOM 20 CD PRO A 104 -84.520 80.566 -28.366 1.00 30.88 C ANISOU 20 CD PRO A 104 4149 3877 3706 -132 -593 305 C ATOM 21 N SER A 105 -84.819 84.009 -25.226 1.00 13.48 N ANISOU 21 N SER A 105 1867 1815 1440 -21 -459 286 N ATOM 22 CA SER A 105 -85.604 84.368 -24.071 1.00 23.31 C ANISOU 22 CA SER A 105 3108 3104 2645 16 -415 283 C ATOM 23 C SER A 105 -87.015 84.443 -24.601 1.00 36.99 C ANISOU 23 C SER A 105 4837 4827 4389 41 -406 272 C ATOM 24 O SER A 105 -87.209 84.451 -25.808 1.00 40.18 O ANISOU 24 O SER A 105 5236 5195 4835 31 -432 263 O ATOM 25 CB SER A 105 -85.159 85.717 -23.524 1.00 31.73 C ANISOU 25 CB SER A 105 4145 4196 3713 42 -395 276 C ATOM 26 OG SER A 105 -83.776 85.700 -23.241 1.00 56.58 O ANISOU 26 OG SER A 105 7293 7346 6857 11 -410 286 O ATOM 27 N ARG A 106 -88.006 84.480 -23.722 1.00 20.24 N ANISOU 27 N ARG A 106 2722 2734 2233 73 -371 274 N ATOM 28 CA ARG A 106 -89.366 84.613 -24.201 1.00 27.02 C ANISOU 28 CA ARG A 106 3578 3584 3105 93 -362 269 C ATOM 29 C ARG A 106 -90.297 85.308 -23.189 1.00 31.16 C ANISOU 29 C ARG A 106 4095 4141 3603 139 -319 274 C ATOM 30 O ARG A 106 -90.109 85.218 -21.986 1.00 29.53 O ANISOU 30 O ARG A 106 3914 3942 3365 150 -298 272 O ATOM 31 CB ARG A 106 -89.915 83.247 -24.626 1.00 19.50 C ANISOU 31 CB ARG A 106 2662 2604 2143 65 -380 270 C ATOM 32 CG ARG A 106 -91.271 83.301 -25.313 1.00 26.83 C ANISOU 32 CG ARG A 106 3595 3510 3090 78 -380 260 C ATOM 33 CD ARG A 106 -91.778 81.909 -25.576 1.00 29.58 C ANISOU 33 CD ARG A 106 3986 3834 3417 50 -397 258 C ATOM 34 NE ARG A 106 -90.844 81.141 -26.388 1.00 17.70 N ANISOU 34 NE ARG A 106 2492 2302 1931 10 -439 256 N ATOM 35 CZ ARG A 106 -91.049 79.888 -26.771 1.00 34.45 C ANISOU 35 CZ ARG A 106 4648 4403 4037 -23 -462 255 C ATOM 36 NH1 ARG A 106 -92.168 79.267 -26.427 1.00 16.61 N ANISOU 36 NH1 ARG A 106 2419 2147 1743 -20 -446 252 N ATOM 37 NH2 ARG A 106 -90.141 79.257 -27.505 1.00 50.23 N ANISOU 37 NH2 ARG A 106 6652 6377 6055 -59 -502 260 N ATOM 38 N LEU A 107 -91.288 86.023 -23.703 1.00 31.48 N ANISOU 38 N LEU A 107 4111 4176 3674 151 -307 272 N ATOM 39 CA LEU A 107 -92.285 86.676 -22.874 1.00 19.63 C ANISOU 39 CA LEU A 107 2613 2649 2197 104 -308 296 C ATOM 40 C LEU A 107 -93.616 86.002 -23.170 1.00 13.14 C ANISOU 40 C LEU A 107 1813 1823 1355 136 -294 297 C ATOM 41 O LEU A 107 -94.068 85.993 -24.308 1.00 21.71 O ANISOU 41 O LEU A 107 2895 2892 2460 152 -304 281 O ATOM 42 CB LEU A 107 -92.362 88.151 -23.259 1.00 11.14 C ANISOU 42 CB LEU A 107 1532 1542 1158 123 -320 270 C ATOM 43 CG LEU A 107 -93.141 89.096 -22.370 1.00 13.38 C ANISOU 43 CG LEU A 107 1802 1853 1427 168 -280 273 C ATOM 44 CD1 LEU A 107 -92.685 88.896 -20.972 1.00 19.71 C ANISOU 44 CD1 LEU A 107 2604 2692 2193 179 -248 284 C ATOM 45 CD2 LEU A 107 -92.922 90.528 -22.787 1.00 7.26 C ANISOU 45 CD2 LEU A 107 993 1083 683 173 -283 259 C ATOM 46 N ILE A 108 -94.238 85.410 -22.164 1.00 40.34 N ANISOU 46 N ILE A 108 5302 5265 4760 153 -270 298 N ATOM 47 CA ILE A 108 -95.612 84.942 -22.328 1.00 21.85 C ANISOU 47 CA ILE A 108 2993 2903 2407 189 -245 287 C ATOM 48 C ILE A 108 -96.448 85.660 -21.294 1.00 27.89 C ANISOU 48 C ILE A 108 3751 3679 3166 241 -191 289 C ATOM 49 O ILE A 108 -96.120 85.609 -20.115 1.00 27.41 O ANISOU 49 O ILE A 108 3685 3650 3080 253 -163 300 O ATOM 50 CB ILE A 108 -95.721 83.431 -22.144 1.00 27.86 C ANISOU 50 CB ILE A 108 3803 3660 3122 174 -243 285 C ATOM 51 CG1 ILE A 108 -94.672 82.724 -23.010 1.00 30.30 C ANISOU 51 CG1 ILE A 108 4105 3971 3437 129 -288 283 C ATOM 52 CG2 ILE A 108 -97.124 82.957 -22.494 1.00 33.79 C ANISOU 52 CG2 ILE A 108 4601 4375 3864 203 -223 268 C ATOM 53 CD1 ILE A 108 -94.465 81.277 -22.672 1.00 22.67 C ANISOU 53 CD1 ILE A 108 3183 3008 2422 98 -290 280 C ATOM 54 N VAL A 109 -97.493 86.365 -21.733 1.00 44.50 N ANISOU 54 N VAL A 109 5849 5765 5295 272 -176 282 N ATOM 55 CA VAL A 109 -98.403 87.071 -20.817 1.00 15.65 C ANISOU 55 CA VAL A 109 2182 2122 1641 322 -123 292 C ATOM 56 C VAL A 109 -99.677 86.318 -20.704 1.00 13.84 C ANISOU 56 C VAL A 109 2000 1864 1393 358 -88 292 C ATOM 57 O VAL A 109 -100.234 85.896 -21.709 1.00 50.45 O ANISOU 57 O VAL A 109 6668 6465 6034 350 -105 277 O ATOM 58 CB VAL A 109 -98.761 88.466 -21.308 1.00 19.63 C ANISOU 58 CB VAL A 109 2651 2626 2182 328 -125 288 C ATOM 59 CG1 VAL A 109 -99.868 89.025 -20.459 1.00 23.13 C ANISOU 59 CG1 VAL A 109 3089 3075 2624 377 -74 302 C ATOM 60 CG2 VAL A 109 -97.524 89.382 -21.274 1.00 22.70 C ANISOU 60 CG2 VAL A 109 2997 3042 2586 299 -150 287 C ATOM 61 N ALA A 110 -100.150 86.144 -19.475 1.00 21.71 N ANISOU 61 N ALA A 110 3005 2875 2370 400 -37 307 N ATOM 62 CA ALA A 110 -101.381 85.399 -19.225 1.00 11.87 C ANISOU 62 CA ALA A 110 1803 1593 1115 429 9 302 C ATOM 63 C ALA A 110 -102.239 86.083 -18.167 1.00 16.46 C ANISOU 63 C ALA A 110 2367 2176 1711 487 62 323 C ATOM 64 O ALA A 110 -101.783 86.990 -17.483 1.00 31.47 O ANISOU 64 O ALA A 110 4223 4117 3616 506 63 345 O ATOM 65 CB ALA A 110 -101.062 83.978 -18.819 1.00 14.01 C ANISOU 65 CB ALA A 110 2104 1863 1356 397 22 280 C ATOM 66 N ILE A 111 -103.497 85.666 -18.055 1.00 22.07 N ANISOU 66 N ILE A 111 3106 2841 2439 506 106 309 N ATOM 67 CA ILE A 111 -104.378 86.214 -17.042 1.00 9.62 C ANISOU 67 CA ILE A 111 1516 1257 883 563 156 331 C ATOM 68 C ILE A 111 -104.998 85.109 -16.241 1.00 25.06 C ANISOU 68 C ILE A 111 3497 3184 2841 573 211 307 C ATOM 69 O ILE A 111 -105.541 84.161 -16.804 1.00 43.81 O ANISOU 69 O ILE A 111 5912 5518 5216 545 223 272 O ATOM 70 CB ILE A 111 -105.471 87.074 -17.657 1.00 20.10 C ANISOU 70 CB ILE A 111 2849 2550 2239 584 160 343 C ATOM 71 CG1 ILE A 111 -106.378 87.656 -16.574 1.00 18.01 C ANISOU 71 CG1 ILE A 111 2571 2274 1997 644 207 375 C ATOM 72 CG2 ILE A 111 -106.288 86.275 -18.651 1.00 28.84 C ANISOU 72 CG2 ILE A 111 4002 3602 3354 554 165 305 C ATOM 73 CD1 ILE A 111 -107.379 88.681 -17.121 1.00 26.85 C ANISOU 73 CD1 ILE A 111 3683 3373 3144 640 206 380 C ATOM 74 N GLU A 112 -104.892 85.212 -14.920 1.00 31.38 N ANISOU 74 N GLU A 112 4272 4008 3644 611 246 321 N ATOM 75 CA GLU A 112 -105.519 84.258 -14.022 1.00 10.90 C ANISOU 75 CA GLU A 112 1694 1388 1061 626 306 295 C ATOM 76 C GLU A 112 -106.845 84.856 -13.593 1.00 30.07 C ANISOU 76 C GLU A 112 4121 3770 3533 685 346 315 C ATOM 77 O GLU A 112 -106.882 85.976 -13.090 1.00 22.40 O ANISOU 77 O GLU A 112 3114 2820 2577 730 341 358 O ATOM 78 CB GLU A 112 -104.630 84.016 -12.807 1.00 11.15 C ANISOU 78 CB GLU A 112 1694 1470 1073 633 321 294 C ATOM 79 CG GLU A 112 -104.919 82.705 -12.109 1.00 35.16 C ANISOU 79 CG GLU A 112 4754 4494 4112 620 375 249 C ATOM 80 CD GLU A 112 -103.905 82.361 -11.036 1.00 38.39 C ANISOU 80 CD GLU A 112 5132 4959 4493 612 386 239 C ATOM 81 OE1 GLU A 112 -104.077 81.332 -10.353 1.00 39.51 O ANISOU 81 OE1 GLU A 112 5285 5096 4633 599 434 198 O ATOM 82 OE2 GLU A 112 -102.930 83.109 -10.870 1.00 33.27 O ANISOU 82 OE2 GLU A 112 4450 4365 3826 615 351 269 O ATOM 83 N ILE A 113 -107.936 84.126 -13.821 1.00 27.63 N ANISOU 83 N ILE A 113 3852 3400 3245 682 385 285 N ATOM 84 CA ILE A 113 -109.249 84.552 -13.347 1.00 18.87 C ANISOU 84 CA ILE A 113 2747 2239 2184 736 429 302 C ATOM 85 C ILE A 113 -110.012 83.457 -12.592 1.00 22.79 C ANISOU 85 C ILE A 113 3265 2690 2706 748 497 262 C ATOM 86 O ILE A 113 -109.887 82.277 -12.916 1.00 28.38 O ANISOU 86 O ILE A 113 4001 3389 3392 699 510 212 O ATOM 87 CB ILE A 113 -110.134 85.013 -14.487 1.00 21.34 C ANISOU 87 CB ILE A 113 3091 2508 2509 726 415 309 C ATOM 88 CG1 ILE A 113 -109.354 85.907 -15.439 1.00 31.06 C ANISOU 88 CG1 ILE A 113 4305 3782 3715 700 349 332 C ATOM 89 CG2 ILE A 113 -111.368 85.746 -13.938 1.00 26.55 C ANISOU 89 CG2 ILE A 113 3750 3121 3215 786 450 344 C ATOM 90 CD1 ILE A 113 -110.119 86.257 -16.685 1.00 18.13 C ANISOU 90 CD1 ILE A 113 2696 2108 2086 678 333 327 C ATOM 91 N VAL A 114 -110.795 83.876 -11.589 1.00 28.59 N ANISOU 91 N VAL A 114 3982 3394 3486 812 538 284 N ATOM 92 CA VAL A 114 -111.767 83.035 -10.877 1.00 13.59 C ANISOU 92 CA VAL A 114 2100 1436 1628 833 608 249 C ATOM 93 C VAL A 114 -113.020 83.829 -10.559 1.00 51.95 C ANISOU 93 C VAL A 114 6953 6247 6537 866 617 285 C ATOM 94 O VAL A 114 -112.950 85.050 -10.407 1.00 49.14 O ANISOU 94 O VAL A 114 6565 5922 6183 883 578 339 O ATOM 95 CB VAL A 114 -111.271 82.590 -9.506 1.00 24.72 C ANISOU 95 CB VAL A 114 3472 2873 3047 858 643 231 C ATOM 96 CG1 VAL A 114 -111.489 81.105 -9.334 1.00 38.41 C ANISOU 96 CG1 VAL A 114 5232 4582 4779 819 696 158 C ATOM 97 CG2 VAL A 114 -109.830 82.966 -9.308 1.00 57.49 C ANISOU 97 CG2 VAL A 114 7583 7109 7152 843 596 249 C ATOM 98 N GLU A 115 -114.154 83.129 -10.431 1.00 37.83 N ANISOU 98 N GLU A 115 5193 4396 4786 858 663 252 N ATOM 99 CA GLU A 115 -115.395 83.713 -9.907 1.00 19.11 C ANISOU 99 CA GLU A 115 2814 1982 2466 881 674 280 C ATOM 100 C GLU A 115 -115.310 83.868 -8.387 1.00 26.75 C ANISOU 100 C GLU A 115 3732 2961 3471 926 691 292 C ATOM 101 O GLU A 115 -114.995 82.909 -7.672 1.00 26.22 O ANISOU 101 O GLU A 115 3655 2894 3414 929 731 246 O ATOM 102 CB GLU A 115 -116.599 82.831 -10.233 1.00 31.78 C ANISOU 102 CB GLU A 115 4462 3515 4099 856 719 236 C ATOM 103 CG GLU A 115 -117.118 82.925 -11.657 1.00 59.63 C ANISOU 103 CG GLU A 115 8034 7019 7604 815 702 232 C ATOM 104 CD GLU A 115 -118.653 82.923 -11.728 1.00 83.02 C ANISOU 104 CD GLU A 115 11020 9915 10607 810 730 230 C ATOM 105 OE1 GLU A 115 -119.306 83.675 -10.958 1.00 50.80 O ANISOU 105 OE1 GLU A 115 6917 5818 6565 847 731 270 O ATOM 106 OE2 GLU A 115 -119.208 82.165 -12.557 1.00100.56 O ANISOU 106 OE2 GLU A 115 13284 12103 12821 768 751 187 O ATOM 107 N ASP A 116 -115.576 85.072 -7.886 1.00 40.45 N ANISOU 107 N ASP A 116 5434 4710 5225 957 662 349 N ATOM 108 CA ASP A 116 -115.687 85.263 -6.439 1.00 48.39 C ANISOU 108 CA ASP A 116 6394 5717 6275 1002 676 361 C ATOM 109 C ASP A 116 -116.516 86.490 -6.072 1.00 57.67 C ANISOU 109 C ASP A 116 7552 6879 7482 1029 651 419 C ATOM 110 O ASP A 116 -116.834 87.308 -6.943 1.00 46.91 O ANISOU 110 O ASP A 116 6207 5520 6098 1009 619 453 O ATOM 111 CB ASP A 116 -114.308 85.357 -5.788 1.00 33.80 C ANISOU 111 CB ASP A 116 4501 3942 4399 1016 661 363 C ATOM 112 CG ASP A 116 -114.252 84.655 -4.446 1.00 41.66 C ANISOU 112 CG ASP A 116 5462 4930 5435 1046 704 326 C ATOM 113 OD1 ASP A 116 -115.330 84.450 -3.843 1.00 66.57 O ANISOU 113 OD1 ASP A 116 8618 8026 8651 1066 733 316 O ATOM 114 OD2 ASP A 116 -113.132 84.304 -3.992 1.00 44.63 O ANISOU 114 OD2 ASP A 116 5810 5361 5785 1047 708 304 O ATOM 115 N GLU A 117 -116.879 86.581 -4.785 1.00 55.45 N ANISOU 115 N GLU A 117 7235 6581 7253 1072 667 426 N ATOM 116 CA GLU A 117 -117.459 87.777 -4.176 1.00 18.24 C ANISOU 116 CA GLU A 117 2494 1865 2569 1104 638 485 C ATOM 117 C GLU A 117 -116.364 88.837 -3.941 1.00 37.08 C ANISOU 117 C GLU A 117 4836 4337 4915 1109 589 527 C ATOM 118 O GLU A 117 -115.466 88.635 -3.127 1.00 39.93 O ANISOU 118 O GLU A 117 5157 4741 5273 1128 592 514 O ATOM 119 CB GLU A 117 -118.091 87.422 -2.826 1.00 46.25 C ANISOU 119 CB GLU A 117 6015 5369 6190 1151 670 472 C ATOM 120 CG GLU A 117 -119.122 86.297 -2.864 1.00 65.51 C ANISOU 120 CG GLU A 117 8490 7726 8675 1146 724 421 C ATOM 121 CD GLU A 117 -120.401 86.686 -3.594 1.00 66.36 C ANISOU 121 CD GLU A 117 8641 7775 8797 1133 721 447 C ATOM 122 OE1 GLU A 117 -120.965 87.762 -3.280 1.00 38.21 O ANISOU 122 OE1 GLU A 117 5062 4202 5253 1159 690 504 O ATOM 123 OE2 GLU A 117 -120.834 85.923 -4.491 1.00 72.82 O ANISOU 123 OE2 GLU A 117 9507 8557 9604 1096 748 409 O ATOM 124 N ILE A 118 -116.403 89.919 -4.665 1.00 43.52 N ANISOU 124 N ILE A 118 5656 5179 5700 1089 547 571 N ATOM 125 CA ILE A 118 -115.384 90.900 -4.500 1.00 41.00 C ANISOU 125 CA ILE A 118 5296 4943 5339 1083 502 606 C ATOM 126 C ILE A 118 -116.043 92.019 -3.771 1.00 48.41 C ANISOU 126 C ILE A 118 6206 5885 6303 1109 474 661 C ATOM 127 O ILE A 118 -117.259 92.065 -3.614 1.00 37.91 O ANISOU 127 O ILE A 118 4897 4494 5014 1123 482 679 O ATOM 128 CB ILE A 118 -114.862 91.382 -5.846 1.00 32.26 C ANISOU 128 CB ILE A 118 4210 3875 4172 1032 471 608 C ATOM 129 CG1 ILE A 118 -115.900 92.235 -6.543 1.00 37.80 C ANISOU 129 CG1 ILE A 118 4934 4550 4877 1013 451 639 C ATOM 130 CG2 ILE A 118 -114.640 90.226 -6.710 1.00 38.80 C ANISOU 130 CG2 ILE A 118 5078 4683 4981 1007 496 556 C ATOM 131 CD1 ILE A 118 -115.515 92.643 -7.877 1.00 39.97 C ANISOU 131 CD1 ILE A 118 5223 4864 5101 963 419 635 C ATOM 132 N PRO A 119 -115.327 93.105 -3.549 1.00 42.58 N ANISOU 132 N PRO A 119 5421 5218 5540 1113 442 689 N ATOM 133 CA PRO A 119 -115.967 94.317 -3.068 1.00 42.83 C ANISOU 133 CA PRO A 119 5421 5258 5594 1139 415 740 C ATOM 134 C PRO A 119 -116.413 95.246 -4.192 1.00 66.43 C ANISOU 134 C PRO A 119 8442 8202 8598 1129 401 775 C ATOM 135 O PRO A 119 -115.785 95.284 -5.216 1.00 95.13 O ANISOU 135 O PRO A 119 12087 11769 12289 1163 419 784 O ATOM 136 CB PRO A 119 -114.854 94.961 -2.278 1.00 52.60 C ANISOU 136 CB PRO A 119 6618 6589 6778 1118 379 757 C ATOM 137 CG PRO A 119 -114.035 93.906 -1.900 1.00 59.52 C ANISOU 137 CG PRO A 119 7484 7495 7636 1117 400 713 C ATOM 138 CD PRO A 119 -113.979 93.001 -3.018 1.00 55.09 C ANISOU 138 CD PRO A 119 6976 6878 7079 1100 432 671 C ATOM 139 N LEU A 120 -117.493 95.991 -4.029 1.00 30.00 N ATOM 140 CA LEU A 120 -117.914 96.830 -5.161 1.00 30.00 C ATOM 141 C LEU A 120 -117.657 98.323 -5.053 1.00 30.00 C ATOM 142 O LEU A 120 -118.126 99.107 -5.875 1.00 30.00 O ATOM 143 CB LEU A 120 -119.354 96.551 -5.641 1.00 20.00 C ATOM 144 CG LEU A 120 -119.194 96.470 -7.153 1.00 20.00 C ATOM 145 CD1 LEU A 120 -120.345 96.890 -7.970 1.00 20.00 C ATOM 146 CD2 LEU A 120 -118.069 97.377 -7.387 1.00 20.00 C ATOM 147 N THR A 121 -116.918 98.717 -4.036 1.00 30.00 N ATOM 148 CA THR A 121 -116.563 100.111 -3.887 1.00 30.00 C ATOM 149 C THR A 121 -115.738 100.561 -5.091 1.00 30.00 C ATOM 150 O THR A 121 -116.276 100.751 -6.192 1.00 30.00 O ATOM 151 CB THR A 121 -115.885 100.388 -2.523 1.00 20.00 C ATOM 152 OG1 THR A 121 -114.970 101.469 -2.647 1.00 20.00 O ATOM 153 CG2 THR A 121 -115.157 99.176 -2.019 1.00 20.00 C ATOM 154 N LYS A 147 -120.869 92.027 -0.413 1.00 52.41 N ANISOU 154 N LYS A 147 6709 6100 7103 1285 540 716 N ATOM 155 CA LYS A 147 -120.076 92.210 -1.621 1.00 43.06 C ANISOU 155 CA LYS A 147 5545 4974 5841 1230 524 712 C ATOM 156 C LYS A 147 -120.952 92.226 -2.867 1.00 45.55 C ANISOU 156 C LYS A 147 5918 5246 6141 1192 529 715 C ATOM 157 O LYS A 147 -121.905 92.994 -2.957 1.00 59.24 O ANISOU 157 O LYS A 147 7667 6948 7894 1197 510 759 O ATOM 158 CB LYS A 147 -119.031 91.102 -1.752 1.00 53.81 C ANISOU 158 CB LYS A 147 6904 6366 7177 1214 554 651 C ATOM 159 CG LYS A 147 -118.304 90.741 -0.462 1.00 71.84 C ANISOU 159 CG LYS A 147 9135 8676 9486 1253 565 630 C ATOM 160 CD LYS A 147 -117.434 91.879 0.041 1.00 86.49 C ANISOU 160 CD LYS A 147 10941 10612 11311 1263 519 674 C ATOM 161 CE LYS A 147 -116.509 91.407 1.156 1.00 93.10 C ANISOU 161 CE LYS A 147 11726 11486 12161 1291 532 643 C ATOM 162 NZ LYS A 147 -117.255 90.751 2.270 1.00 94.10 N ANISOU 162 NZ LYS A 147 11836 11549 12370 1340 566 616 N ATOM 163 N VAL A 148 -120.599 91.378 -3.829 1.00 55.83 N ANISOU 163 N VAL A 148 7254 6550 7409 1153 552 668 N ATOM 164 CA VAL A 148 -121.322 91.204 -5.093 1.00 43.81 C ANISOU 164 CA VAL A 148 5787 4989 5869 1113 562 657 C ATOM 165 C VAL A 148 -120.595 90.135 -5.895 1.00 39.59 C ANISOU 165 C VAL A 148 5277 4470 5297 1077 586 598 C ATOM 166 O VAL A 148 -119.428 89.847 -5.639 1.00 43.77 O ANISOU 166 O VAL A 148 5779 5052 5801 1078 582 580 O ATOM 167 CB VAL A 148 -121.371 92.482 -5.940 1.00 40.48 C ANISOU 167 CB VAL A 148 5371 4605 5405 1083 515 703 C ATOM 168 CG1 VAL A 148 -120.059 92.703 -6.629 1.00 44.23 C ANISOU 168 CG1 VAL A 148 5832 5160 5815 1048 490 691 C ATOM 169 CG2 VAL A 148 -122.479 92.382 -6.970 1.00 57.36 C ANISOU 169 CG2 VAL A 148 7564 6685 7544 1053 529 698 C ATOM 170 N ASP A 149 -121.275 89.537 -6.862 1.00 52.04 N ANISOU 170 N ASP A 149 6904 5999 6869 1045 611 569 N ATOM 171 CA ASP A 149 -120.674 88.431 -7.590 1.00 38.83 C ANISOU 171 CA ASP A 149 5256 4332 5165 1012 634 511 C ATOM 172 C ASP A 149 -120.076 88.905 -8.897 1.00 53.63 C ANISOU 172 C ASP A 149 7146 6254 6978 968 599 516 C ATOM 173 O ASP A 149 -120.793 89.398 -9.774 1.00 48.78 O ANISOU 173 O ASP A 149 6562 5619 6354 943 588 530 O ATOM 174 CB ASP A 149 -121.685 87.316 -7.831 1.00 50.00 C ANISOU 174 CB ASP A 149 6716 5670 6613 999 687 464 C ATOM 175 CG ASP A 149 -121.118 86.195 -8.660 1.00 65.36 C ANISOU 175 CG ASP A 149 8690 7622 8522 958 708 405 C ATOM 176 OD1 ASP A 149 -120.286 85.417 -8.139 1.00 93.04 O ANISOU 176 OD1 ASP A 149 12177 11149 12024 964 725 370 O ATOM 177 OD2 ASP A 149 -121.511 86.085 -9.839 1.00 56.88 O ANISOU 177 OD2 ASP A 149 7658 6532 7423 918 708 391 O ATOM 178 N GLY A 150 -118.752 88.757 -8.993 1.00 64.51 N ANISOU 178 N GLY A 150 8502 7693 8315 959 581 504 N ATOM 179 CA GLY A 150 -117.963 89.169 -10.142 1.00 52.25 C ANISOU 179 CA GLY A 150 6956 6191 6707 920 544 504 C ATOM 180 C GLY A 150 -116.707 88.320 -10.317 1.00 37.65 C ANISOU 180 C GLY A 150 5103 4377 4824 908 546 467 C ATOM 181 O GLY A 150 -116.768 87.095 -10.279 1.00 55.00 O ANISOU 181 O GLY A 150 7326 6541 7032 904 585 421 O ATOM 182 N LEU A 151 -115.558 88.966 -10.475 1.00 36.36 N ANISOU 182 N LEU A 151 4908 4285 4622 899 504 485 N ATOM 183 CA LEU A 151 -114.335 88.260 -10.852 1.00 34.36 C ANISOU 183 CA LEU A 151 4656 4067 4330 883 498 454 C ATOM 184 C LEU A 151 -113.081 88.719 -10.115 1.00 26.30 C ANISOU 184 C LEU A 151 3584 3121 3288 899 473 474 C ATOM 185 O LEU A 151 -112.907 89.906 -9.857 1.00 33.46 O ANISOU 185 O LEU A 151 4454 4070 4189 901 440 512 O ATOM 186 CB LEU A 151 -114.107 88.413 -12.356 1.00 25.92 C ANISOU 186 CB LEU A 151 3615 3008 3226 838 466 442 C ATOM 187 CG LEU A 151 -115.093 87.677 -13.262 1.00 31.22 C ANISOU 187 CG LEU A 151 4342 3612 3908 814 493 408 C ATOM 188 CD1 LEU A 151 -114.824 88.038 -14.680 1.00 41.34 C ANISOU 188 CD1 LEU A 151 5641 4909 5158 773 454 401 C ATOM 189 CD2 LEU A 151 -114.964 86.173 -13.070 1.00 35.42 C ANISOU 189 CD2 LEU A 151 4903 4110 4445 815 536 359 C ATOM 190 N LYS A 152 -112.209 87.763 -9.796 1.00 37.08 N ANISOU 190 N LYS A 152 4947 4501 4639 906 490 445 N ATOM 191 CA LYS A 152 -110.877 88.023 -9.235 1.00 23.44 C ANISOU 191 CA LYS A 152 3176 2846 2883 915 468 456 C ATOM 192 C LYS A 152 -109.843 87.739 -10.322 1.00 32.46 C ANISOU 192 C LYS A 152 4334 4020 3977 881 437 440 C ATOM 193 O LYS A 152 -109.743 86.620 -10.801 1.00 38.83 O ANISOU 193 O LYS A 152 5180 4798 4776 873 459 402 O ATOM 194 CB LYS A 152 -110.596 87.078 -8.071 1.00 45.52 C ANISOU 194 CB LYS A 152 5958 5641 5698 948 512 428 C ATOM 195 CG LYS A 152 -110.518 87.720 -6.690 1.00 65.59 C ANISOU 195 CG LYS A 152 8445 8212 8263 985 513 455 C ATOM 196 CD LYS A 152 -110.297 86.650 -5.607 1.00 69.00 C ANISOU 196 CD LYS A 152 8862 8638 8718 1010 561 413 C ATOM 197 CE LYS A 152 -110.124 87.258 -4.216 1.00 81.93 C ANISOU 197 CE LYS A 152 10441 10309 10381 1047 559 435 C ATOM 198 NZ LYS A 152 -111.375 87.871 -3.678 1.00 83.09 N ANISOU 198 NZ LYS A 152 10582 10406 10583 1074 562 463 N ATOM 199 N ALA A 153 -109.064 88.745 -10.702 1.00 33.41 N ANISOU 199 N ALA A 153 4425 4201 4068 857 388 464 N ATOM 200 CA ALA A 153 -108.134 88.583 -11.800 1.00 15.85 C ANISOU 200 CA ALA A 153 2213 2003 1806 818 350 450 C ATOM 201 C ALA A 153 -106.747 89.032 -11.432 1.00 44.63 C ANISOU 201 C ALA A 153 5813 5726 5419 809 319 462 C ATOM 202 O ALA A 153 -106.586 89.902 -10.581 1.00 38.54 O ANISOU 202 O ALA A 153 4997 4994 4653 822 316 485 O ATOM 203 CB ALA A 153 -108.602 89.348 -13.003 1.00 18.51 C ANISOU 203 CB ALA A 153 2561 2329 2142 777 317 451 C ATOM 204 N ARG A 154 -105.752 88.433 -12.093 1.00 44.75 N ANISOU 204 N ARG A 154 5843 5760 5399 783 293 446 N ATOM 205 CA ARG A 154 -104.383 88.900 -11.993 1.00 19.49 C ANISOU 205 CA ARG A 154 2604 2633 2169 755 255 451 C ATOM 206 C ARG A 154 -103.509 88.556 -13.204 1.00 21.61 C ANISOU 206 C ARG A 154 2892 2911 2408 695 209 429 C ATOM 207 O ARG A 154 -103.537 87.456 -13.723 1.00 32.78 O ANISOU 207 O ARG A 154 4349 4294 3810 667 211 400 O ATOM 208 CB ARG A 154 -103.753 88.396 -10.706 1.00 15.15 C ANISOU 208 CB ARG A 154 2030 2120 1606 787 282 453 C ATOM 209 CG ARG A 154 -103.442 86.941 -10.707 1.00 20.10 C ANISOU 209 CG ARG A 154 2690 2733 2215 745 301 401 C ATOM 210 CD ARG A 154 -102.745 86.596 -9.429 1.00 33.81 C ANISOU 210 CD ARG A 154 4392 4515 3938 756 326 390 C ATOM 211 NE ARG A 154 -102.648 85.161 -9.248 1.00 38.31 N ANISOU 211 NE ARG A 154 4992 5069 4493 718 356 339 N ATOM 212 CZ ARG A 154 -102.324 84.582 -8.104 1.00 35.09 C ANISOU 212 CZ ARG A 154 4564 4689 4080 724 394 314 C ATOM 213 NH1 ARG A 154 -102.085 85.329 -7.032 1.00 36.86 N ANISOU 213 NH1 ARG A 154 4735 4956 4316 773 406 337 N ATOM 214 NH2 ARG A 154 -102.265 83.262 -8.034 1.00 37.86 N ANISOU 214 NH2 ARG A 154 4945 5027 4414 680 422 263 N ATOM 215 N ILE A 155 -102.722 89.518 -13.655 1.00 39.45 N ANISOU 215 N ILE A 155 5113 5210 4668 649 169 422 N ATOM 216 CA ILE A 155 -101.823 89.276 -14.758 1.00 22.98 C ANISOU 216 CA ILE A 155 3035 3128 2569 589 123 397 C ATOM 217 C ILE A 155 -100.636 88.503 -14.239 1.00 22.74 C ANISOU 217 C ILE A 155 3004 3134 2503 576 115 394 C ATOM 218 O ILE A 155 -100.118 88.815 -13.171 1.00 27.11 O ANISOU 218 O ILE A 155 3522 3733 3045 597 130 408 O ATOM 219 CB ILE A 155 -101.354 90.580 -15.392 1.00 23.42 C ANISOU 219 CB ILE A 155 3050 3205 2644 548 88 388 C ATOM 220 CG1 ILE A 155 -102.552 91.388 -15.858 1.00 22.25 C ANISOU 220 CG1 ILE A 155 2905 3028 2522 556 96 394 C ATOM 221 CG2 ILE A 155 -100.460 90.284 -16.567 1.00 34.25 C ANISOU 221 CG2 ILE A 155 4432 4569 4014 491 41 363 C ATOM 222 CD1 ILE A 155 -103.429 90.617 -16.793 1.00 31.71 C ANISOU 222 CD1 ILE A 155 4153 4170 3725 555 97 381 C ATOM 223 N ILE A 156 -100.227 87.483 -14.992 1.00 25.47 N ANISOU 223 N ILE A 156 3389 3463 2826 537 92 375 N ATOM 224 CA ILE A 156 -99.062 86.672 -14.667 1.00 17.83 C ANISOU 224 CA ILE A 156 2427 2528 1818 504 80 367 C ATOM 225 C ILE A 156 -98.224 86.379 -15.903 1.00 38.61 C ANISOU 225 C ILE A 156 5071 5146 4453 434 22 345 C ATOM 226 O ILE A 156 -98.697 86.526 -17.024 1.00 56.46 O ANISOU 226 O ILE A 156 7346 7368 6738 420 -1 335 O ATOM 227 CB ILE A 156 -99.445 85.344 -14.027 1.00 18.64 C ANISOU 227 CB ILE A 156 2566 2617 1901 504 122 346 C ATOM 228 CG1 ILE A 156 -100.473 84.628 -14.877 1.00 40.00 C ANISOU 228 CG1 ILE A 156 5317 5258 4623 491 130 322 C ATOM 229 CG2 ILE A 156 -100.019 85.559 -12.631 1.00 47.20 C ANISOU 229 CG2 ILE A 156 6156 6246 5532 560 180 353 C ATOM 230 CD1 ILE A 156 -100.928 83.334 -14.266 1.00 56.62 C ANISOU 230 CD1 ILE A 156 7451 7344 6719 480 178 287 C ATOM 231 N LEU A 157 -96.972 85.979 -15.682 1.00 32.26 N ANISOU 231 N LEU A 157 4260 4371 3625 392 0 340 N ATOM 232 CA LEU A 157 -96.065 85.577 -16.749 1.00 22.26 C ANISOU 232 CA LEU A 157 3008 3088 2361 326 -56 326 C ATOM 233 C LEU A 157 -95.806 84.080 -16.709 1.00 17.89 C ANISOU 233 C LEU A 157 2503 2535 1759 293 -58 319 C ATOM 234 O LEU A 157 -95.540 83.520 -15.648 1.00 39.85 O ANISOU 234 O LEU A 157 5289 5351 4499 297 -26 320 O ATOM 235 CB LEU A 157 -94.709 86.296 -16.636 1.00 47.66 C ANISOU 235 CB LEU A 157 6188 6331 5590 292 -84 326 C ATOM 236 CG LEU A 157 -94.679 87.829 -16.580 1.00 63.12 C ANISOU 236 CG LEU A 157 8096 8301 7586 311 -81 328 C ATOM 237 CD1 LEU A 157 -93.240 88.349 -16.755 1.00 52.37 C ANISOU 237 CD1 LEU A 157 6713 6952 6232 267 -113 321 C ATOM 238 CD2 LEU A 157 -95.624 88.448 -17.612 1.00 39.87 C ANISOU 238 CD2 LEU A 157 5152 5320 4678 321 -89 321 C ATOM 239 N ILE A 158 -95.859 83.436 -17.870 1.00 27.00 N ANISOU 239 N ILE A 158 3690 3652 2916 257 -97 309 N ATOM 240 CA ILE A 158 -95.493 82.031 -17.971 1.00 22.12 C ANISOU 240 CA ILE A 158 3118 3035 2251 211 -109 301 C ATOM 241 C ILE A 158 -94.068 81.895 -18.477 1.00 33.25 C ANISOU 241 C ILE A 158 4517 4451 3665 144 -169 307 C ATOM 242 O ILE A 158 -93.716 82.489 -19.492 1.00 58.93 O ANISOU 242 O ILE A 158 7747 7681 6963 127 -214 311 O ATOM 243 CB ILE A 158 -96.413 81.261 -18.932 1.00 30.80 C ANISOU 243 CB ILE A 158 4264 4089 3351 204 -118 285 C ATOM 244 CG1 ILE A 158 -97.859 81.291 -18.449 1.00 52.04 C ANISOU 244 CG1 ILE A 158 6958 6754 6060 250 -52 267 C ATOM 245 CG2 ILE A 158 -95.948 79.832 -19.044 1.00 20.60 C ANISOU 245 CG2 ILE A 158 3011 2799 2017 140 -134 272 C ATOM 246 CD1 ILE A 158 -98.779 80.394 -19.255 1.00 49.78 C ANISOU 246 CD1 ILE A 158 6713 6422 5781 228 -49 238 C ATOM 247 N GLU A 159 -93.259 81.104 -17.779 1.00 38.31 N ANISOU 247 N GLU A 159 5175 5123 4260 104 -167 308 N ATOM 248 CA GLU A 159 -91.868 80.885 -18.170 1.00 23.87 C ANISOU 248 CA GLU A 159 3363 3273 2433 69 -213 301 C ATOM 249 C GLU A 159 -91.668 79.580 -18.923 1.00 26.26 C ANISOU 249 C GLU A 159 3663 3594 2720 41 -229 301 C ATOM 250 O GLU A 159 -91.536 78.518 -18.332 1.00 40.27 O ANISOU 250 O GLU A 159 5468 5383 4449 3 -215 294 O ATOM 251 CB GLU A 159 -90.938 80.959 -16.954 1.00 28.51 C ANISOU 251 CB GLU A 159 3942 3903 2988 58 -191 305 C ATOM 252 CG GLU A 159 -90.756 82.384 -16.446 1.00 47.94 C ANISOU 252 CG GLU A 159 6345 6384 5485 83 -177 313 C ATOM 253 CD GLU A 159 -90.065 82.452 -15.099 1.00 83.65 C ANISOU 253 CD GLU A 159 10847 10960 9977 81 -142 312 C ATOM 254 OE1 GLU A 159 -90.674 82.026 -14.094 1.00 90.04 O ANISOU 254 OE1 GLU A 159 11651 11810 10751 100 -91 308 O ATOM 255 OE2 GLU A 159 -88.912 82.937 -15.044 1.00 96.07 O ANISOU 255 OE2 GLU A 159 12407 12535 11561 66 -162 311 O ATOM 256 N ASP A 160 -91.648 79.685 -20.242 1.00 25.33 N ANISOU 256 N ASP A 160 3535 3439 2650 34 -270 298 N ATOM 257 CA ASP A 160 -91.411 78.559 -21.121 1.00 18.76 C ANISOU 257 CA ASP A 160 2729 2578 1823 -16 -306 290 C ATOM 258 C ASP A 160 -90.705 79.046 -22.397 1.00 46.59 C ANISOU 258 C ASP A 160 6225 6070 5407 -19 -352 289 C ATOM 259 O ASP A 160 -91.232 79.901 -23.108 1.00 53.27 O ANISOU 259 O ASP A 160 7049 6897 6295 11 -358 284 O ATOM 260 CB ASP A 160 -92.740 77.917 -21.480 1.00 21.12 C ANISOU 260 CB ASP A 160 3063 2854 2106 -21 -299 278 C ATOM 261 CG ASP A 160 -92.587 76.631 -22.277 1.00 38.00 C ANISOU 261 CG ASP A 160 5231 4969 4238 -75 -334 269 C ATOM 262 OD1 ASP A 160 -93.599 75.908 -22.413 1.00 30.40 O ANISOU 262 OD1 ASP A 160 4306 3994 3249 -88 -323 255 O ATOM 263 OD2 ASP A 160 -91.478 76.337 -22.757 1.00 46.00 O ANISOU 263 OD2 ASP A 160 6233 5976 5271 -105 -370 277 O ATOM 264 N ASN A 161 -89.505 78.522 -22.658 1.00 40.64 N ANISOU 264 N ASN A 161 5474 5309 4659 -59 -382 295 N ATOM 265 CA ASN A 161 -88.811 78.720 -23.929 1.00 16.42 C ANISOU 265 CA ASN A 161 2390 2203 1644 -73 -427 295 C ATOM 266 C ASN A 161 -88.671 77.413 -24.671 1.00 28.02 C ANISOU 266 C ASN A 161 3890 3645 3110 -123 -464 298 C ATOM 267 O ASN A 161 -88.097 77.359 -25.747 1.00 54.70 O ANISOU 267 O ASN A 161 7263 6990 6531 -140 -504 301 O ATOM 268 CB ASN A 161 -87.425 79.292 -23.709 1.00 35.20 C ANISOU 268 CB ASN A 161 4747 4589 4037 -80 -435 304 C ATOM 269 CG ASN A 161 -87.191 79.688 -22.296 1.00 51.64 C ANISOU 269 CG ASN A 161 6824 6717 6079 -63 -395 308 C ATOM 270 OD1 ASN A 161 -87.399 80.838 -21.921 1.00 68.08 O ANISOU 270 OD1 ASN A 161 8880 8816 8170 -19 -372 304 O ATOM 271 ND2 ASN A 161 -86.761 78.737 -21.486 1.00 55.82 N ANISOU 271 ND2 ASN A 161 7380 7268 6563 -99 -388 315 N ATOM 272 N THR A 162 -89.211 76.353 -24.089 1.00 42.02 N ANISOU 272 N THR A 162 5697 5436 4833 -148 -448 296 N ATOM 273 CA THR A 162 -89.203 75.028 -24.700 1.00 51.13 C ANISOU 273 CA THR A 162 6882 6571 5973 -199 -479 299 C ATOM 274 C THR A 162 -90.305 74.824 -25.749 1.00 33.66 C ANISOU 274 C THR A 162 4679 4327 3782 -191 -497 285 C ATOM 275 O THR A 162 -90.035 74.457 -26.890 1.00 31.10 O ANISOU 275 O THR A 162 4356 3969 3492 -211 -541 288 O ATOM 276 CB THR A 162 -89.373 73.944 -23.616 1.00 76.76 C ANISOU 276 CB THR A 162 10162 9853 9151 -236 -450 297 C ATOM 277 OG1 THR A 162 -88.391 74.134 -22.589 1.00 86.09 O ANISOU 277 OG1 THR A 162 11334 11065 10309 -245 -432 307 O ATOM 278 CG2 THR A 162 -89.231 72.540 -24.210 1.00 76.38 C ANISOU 278 CG2 THR A 162 10143 9791 9085 -298 -483 303 C ATOM 279 N SER A 163 -91.548 75.053 -25.352 1.00 32.84 N ANISOU 279 N SER A 163 4586 4233 3658 -162 -462 269 N ATOM 280 CA SER A 163 -92.678 74.753 -26.216 1.00 42.53 C ANISOU 280 CA SER A 163 5832 5433 4895 -160 -474 253 C ATOM 281 C SER A 163 -92.557 75.561 -27.472 1.00 32.72 C ANISOU 281 C SER A 163 4559 4153 3721 -137 -510 248 C ATOM 282 O SER A 163 -91.934 76.608 -27.468 1.00 35.39 O ANISOU 282 O SER A 163 4861 4492 4094 -111 -508 253 O ATOM 283 CB SER A 163 -93.977 75.108 -25.517 1.00 39.94 C ANISOU 283 CB SER A 163 5523 5116 4537 -127 -427 238 C ATOM 284 OG SER A 163 -93.969 74.581 -24.211 1.00 51.19 O ANISOU 284 OG SER A 163 6970 6578 5901 -142 -384 240 O ATOM 285 N GLU A 164 -93.152 75.074 -28.547 1.00 33.03 N ANISOU 285 N GLU A 164 4610 4162 3778 -149 -540 236 N ATOM 286 CA GLU A 164 -93.237 75.843 -29.774 1.00 23.49 C ANISOU 286 CA GLU A 164 3374 2917 2635 -127 -569 224 C ATOM 287 C GLU A 164 -94.131 77.021 -29.463 1.00 41.29 C ANISOU 287 C GLU A 164 5615 5175 4898 -78 -535 209 C ATOM 288 O GLU A 164 -95.057 76.902 -28.661 1.00 42.95 O ANISOU 288 O GLU A 164 5852 5401 5065 -66 -499 204 O ATOM 289 CB GLU A 164 -93.856 74.996 -30.876 1.00 43.25 C ANISOU 289 CB GLU A 164 5896 5392 5146 -150 -603 211 C ATOM 290 CG GLU A 164 -93.974 75.681 -32.216 1.00 59.71 C ANISOU 290 CG GLU A 164 7952 7437 7298 -130 -634 193 C ATOM 291 CD GLU A 164 -94.748 74.843 -33.229 1.00 65.98 C ANISOU 291 CD GLU A 164 8766 8208 8096 -148 -664 177 C ATOM 292 OE1 GLU A 164 -95.087 73.679 -32.923 1.00 60.22 O ANISOU 292 OE1 GLU A 164 8071 7494 7315 -182 -662 182 O ATOM 293 OE2 GLU A 164 -95.019 75.353 -34.334 1.00 67.96 O ANISOU 293 OE2 GLU A 164 8994 8427 8399 -131 -687 158 O ATOM 294 N VAL A 165 -93.837 78.167 -30.066 1.00 32.15 N ANISOU 294 N VAL A 165 4418 4003 3796 -52 -543 201 N ATOM 295 CA VAL A 165 -94.623 79.353 -29.824 1.00 26.88 C ANISOU 295 CA VAL A 165 3734 3341 3140 -9 -513 189 C ATOM 296 C VAL A 165 -96.048 79.046 -30.265 1.00 32.23 C ANISOU 296 C VAL A 165 4444 3996 3808 -1 -514 167 C ATOM 297 O VAL A 165 -96.237 78.362 -31.269 1.00 42.33 O ANISOU 297 O VAL A 165 5733 5247 5102 -24 -550 153 O ATOM 298 CB VAL A 165 -94.045 80.584 -30.595 1.00 30.28 C ANISOU 298 CB VAL A 165 4117 3758 3632 6 -526 179 C ATOM 299 CG1 VAL A 165 -94.976 81.805 -30.479 1.00 34.60 C ANISOU 299 CG1 VAL A 165 4646 4309 4191 46 -497 165 C ATOM 300 CG2 VAL A 165 -92.672 80.932 -30.084 1.00 26.34 C ANISOU 300 CG2 VAL A 165 3594 3280 3136 0 -521 198 C ATOM 301 N GLY A 166 -97.039 79.526 -29.505 1.00 32.73 N ANISOU 301 N GLY A 166 4524 4068 3843 32 -474 165 N ATOM 302 CA GLY A 166 -98.446 79.358 -29.841 1.00 25.53 C ANISOU 302 CA GLY A 166 3652 3130 2916 45 -468 142 C ATOM 303 C GLY A 166 -99.073 78.051 -29.381 1.00 43.21 C ANISOU 303 C GLY A 166 5954 5372 5093 21 -454 138 C ATOM 304 O GLY A 166 -100.095 77.609 -29.912 1.00 39.55 O ANISOU 304 O GLY A 166 5513 4885 4627 16 -442 107 O ATOM 305 N THR A 167 -98.460 77.418 -28.390 1.00 32.65 N ANISOU 305 N THR A 167 4627 4064 3714 1 -434 159 N ATOM 306 CA THR A 167 -98.961 76.148 -27.897 1.00 24.60 C ANISOU 306 CA THR A 167 3662 3053 2632 -33 -409 150 C ATOM 307 C THR A 167 -99.081 76.140 -26.387 1.00 33.23 C ANISOU 307 C THR A 167 4761 4175 3692 -17 -336 156 C ATOM 308 O THR A 167 -99.012 75.079 -25.759 1.00 30.39 O ANISOU 308 O THR A 167 4429 3835 3283 -54 -313 151 O ATOM 309 CB THR A 167 -98.044 75.020 -28.298 1.00 35.34 C ANISOU 309 CB THR A 167 5017 4425 3985 -91 -451 159 C ATOM 310 OG1 THR A 167 -96.944 74.966 -27.385 1.00 49.22 O ANISOU 310 OG1 THR A 167 6756 6217 5730 -102 -439 184 O ATOM 311 CG2 THR A 167 -97.526 75.266 -29.707 1.00 44.15 C ANISOU 311 CG2 THR A 167 6093 5514 5168 -96 -510 156 C ATOM 312 N GLN A 168 -99.242 77.318 -25.795 1.00 17.29 N ANISOU 312 N GLN A 168 2163 2055 2353 15 146 27 N ATOM 313 CA GLN A 168 -99.585 77.357 -24.387 1.00 19.93 C ANISOU 313 CA GLN A 168 2523 2432 2618 24 114 36 C ATOM 314 C GLN A 168 -101.052 76.963 -24.265 1.00 24.96 C ANISOU 314 C GLN A 168 3171 3069 3244 31 119 41 C ATOM 315 O GLN A 168 -101.835 77.135 -25.194 1.00 32.39 O ANISOU 315 O GLN A 168 4099 4007 4201 27 173 37 O ATOM 316 CB GLN A 168 -99.327 78.731 -23.772 1.00 15.94 C ANISOU 316 CB GLN A 168 2043 1922 2091 24 124 29 C ATOM 317 CG GLN A 168 -97.872 79.131 -23.714 1.00 30.70 C ANISOU 317 CG GLN A 168 3889 3818 3956 17 125 22 C ATOM 318 CD GLN A 168 -97.066 78.210 -22.835 1.00 35.89 C ANISOU 318 CD GLN A 168 4526 4497 4614 16 53 35 C ATOM 319 OE1 GLN A 168 -97.412 77.989 -21.682 1.00 35.01 O ANISOU 319 OE1 GLN A 168 4421 4410 4472 14 31 30 O ATOM 320 NE2 GLN A 168 -95.990 77.653 -23.382 1.00 22.58 N ANISOU 320 NE2 GLN A 168 2775 2803 3002 -1 -7 55 N ATOM 321 N ARG A 169 -101.430 76.358 -23.155 1.00 34.95 N ANISOU 321 N ARG A 169 4432 4365 4481 32 85 43 N ATOM 322 CA ARG A 169 -102.793 75.905 -22.927 1.00 29.13 C ANISOU 322 CA ARG A 169 3688 3644 3735 35 100 44 C ATOM 323 C ARG A 169 -103.446 76.696 -21.806 1.00 35.28 C ANISOU 323 C ARG A 169 4475 4429 4500 40 96 45 C ATOM 324 O ARG A 169 -102.756 77.145 -20.916 1.00 26.81 O ANISOU 324 O ARG A 169 3407 3355 3425 39 69 45 O ATOM 325 CB ARG A 169 -102.795 74.441 -22.516 1.00 35.11 C ANISOU 325 CB ARG A 169 4444 4403 4492 32 66 45 C ATOM 326 CG ARG A 169 -102.301 73.463 -23.515 1.00 63.22 C ANISOU 326 CG ARG A 169 7996 7952 8074 29 74 49 C ATOM 327 CD ARG A 169 -102.797 72.074 -23.211 1.00 83.25 C ANISOU 327 CD ARG A 169 10523 10506 10602 21 48 45 C ATOM 328 NE ARG A 169 -103.449 71.494 -24.376 1.00 93.56 N ANISOU 328 NE ARG A 169 11828 11811 11908 23 49 47 N ATOM 329 CZ ARG A 169 -104.742 71.239 -24.481 1.00114.54 C ANISOU 329 CZ ARG A 169 14491 14480 14547 21 39 41 C ATOM 330 NH1 ARG A 169 -105.573 71.478 -23.488 1.00129.09 N ANISOU 330 NH1 ARG A 169 16338 16333 16377 19 30 34 N ATOM 331 NH2 ARG A 169 -105.205 70.734 -25.593 1.00120.42 N ANISOU 331 NH2 ARG A 169 15235 15224 15294 23 42 44 N ATOM 332 N VAL A 170 -104.770 76.847 -21.850 1.00 31.40 N ANISOU 332 N VAL A 170 4001 3909 4019 53 105 57 N ATOM 333 CA VAL A 170 -105.545 77.294 -20.696 1.00 30.51 C ANISOU 333 CA VAL A 170 3889 3804 3898 60 101 63 C ATOM 334 C VAL A 170 -105.529 76.215 -19.613 1.00 32.25 C ANISOU 334 C VAL A 170 4092 4049 4111 53 74 60 C ATOM 335 O VAL A 170 -105.951 75.084 -19.844 1.00 40.40 O ANISOU 335 O VAL A 170 5112 5098 5139 46 78 54 O ATOM 336 CB VAL A 170 -106.984 77.576 -21.080 1.00 40.88 C ANISOU 336 CB VAL A 170 5205 5123 5206 66 143 66 C ATOM 337 CG1 VAL A 170 -107.774 78.053 -19.861 1.00 47.22 C ANISOU 337 CG1 VAL A 170 6018 5911 6014 82 125 81 C ATOM 338 CG2 VAL A 170 -107.022 78.587 -22.218 1.00 41.19 C ANISOU 338 CG2 VAL A 170 5266 5131 5253 66 187 64 C ATOM 339 N LEU A 171 -105.044 76.574 -18.430 1.00 33.00 N ANISOU 339 N LEU A 171 4179 4167 4195 43 69 60 N ATOM 340 CA LEU A 171 -104.805 75.609 -17.361 1.00 31.51 C ANISOU 340 CA LEU A 171 3975 3985 4011 46 48 53 C ATOM 341 C LEU A 171 -105.216 76.193 -16.008 1.00 29.76 C ANISOU 341 C LEU A 171 3752 3776 3781 45 57 74 C ATOM 342 O LEU A 171 -105.222 77.402 -15.841 1.00 47.89 O ANISOU 342 O LEU A 171 6048 6072 6074 52 64 80 O ATOM 343 CB LEU A 171 -103.325 75.218 -17.322 1.00 28.18 C ANISOU 343 CB LEU A 171 3556 3566 3585 29 30 47 C ATOM 344 CG LEU A 171 -102.831 73.958 -18.026 1.00 52.99 C ANISOU 344 CG LEU A 171 6699 6708 6726 20 22 36 C ATOM 345 CD1 LEU A 171 -102.968 72.752 -17.111 1.00 70.64 C ANISOU 345 CD1 LEU A 171 8931 8948 8960 17 20 40 C ATOM 346 CD2 LEU A 171 -103.553 73.729 -19.332 1.00 53.86 C ANISOU 346 CD2 LEU A 171 6808 6817 6839 22 35 34 C ATOM 347 N PRO A 172 -105.556 75.326 -15.036 1.00 38.47 N ANISOU 347 N PRO A 172 4848 4887 4884 46 54 82 N ATOM 348 CA PRO A 172 -105.911 75.761 -13.682 1.00 31.55 C ANISOU 348 CA PRO A 172 3943 4029 4015 65 60 95 C ATOM 349 C PRO A 172 -104.748 76.416 -12.971 1.00 40.11 C ANISOU 349 C PRO A 172 5013 5128 5099 59 51 105 C ATOM 350 O PRO A 172 -103.675 75.821 -12.928 1.00 41.79 O ANISOU 350 O PRO A 172 5241 5335 5303 42 36 112 O ATOM 351 CB PRO A 172 -106.222 74.449 -12.970 1.00 46.91 C ANISOU 351 CB PRO A 172 5901 5972 5952 59 54 114 C ATOM 352 CG PRO A 172 -105.487 73.412 -13.743 1.00 44.32 C ANISOU 352 CG PRO A 172 5579 5635 5627 46 44 93 C ATOM 353 CD PRO A 172 -105.588 73.859 -15.160 1.00 41.42 C ANISOU 353 CD PRO A 172 5212 5262 5263 42 51 69 C ATOM 354 N GLY A 173 -104.958 77.606 -12.412 1.00 43.73 N ANISOU 354 N GLY A 173 5459 5601 5556 67 56 121 N ATOM 355 CA GLY A 173 -103.908 78.314 -11.698 1.00 29.58 C ANISOU 355 CA GLY A 173 3671 3824 3745 52 40 151 C ATOM 356 C GLY A 173 -103.956 77.948 -10.236 1.00 39.34 C ANISOU 356 C GLY A 173 4883 5089 4976 51 38 186 C ATOM 357 O GLY A 173 -104.611 76.976 -9.873 1.00 38.78 O ANISOU 357 O GLY A 173 4813 5014 4908 59 45 190 O ATOM 358 N THR A 174 -103.289 78.730 -9.395 1.00 28.89 N ANISOU 358 N THR A 174 3536 3798 3644 38 26 215 N ATOM 359 CA THR A 174 -103.241 78.428 -7.973 1.00 35.81 C ANISOU 359 CA THR A 174 4385 4707 4513 33 23 256 C ATOM 360 C THR A 174 -104.336 79.120 -7.155 1.00 42.15 C ANISOU 360 C THR A 174 5124 5550 5341 53 35 257 C ATOM 361 O THR A 174 -104.457 78.902 -5.958 1.00 47.46 O ANISOU 361 O THR A 174 5767 6253 6012 53 35 290 O ATOM 362 CB THR A 174 -101.908 78.829 -7.390 1.00 43.02 C ANISOU 362 CB THR A 174 5227 5666 5453 0 0 261 C ATOM 363 OG1 THR A 174 -101.814 80.257 -7.398 1.00 49.47 O ANISOU 363 OG1 THR A 174 6088 6489 6222 -14 -9 293 O ATOM 364 CG2 THR A 174 -100.773 78.220 -8.205 1.00 38.58 C ANISOU 364 CG2 THR A 174 4682 5080 4896 -20 -14 243 C ATOM 365 N LEU A 175 -105.129 79.962 -7.798 1.00 47.46 N ANISOU 365 N LEU A 175 5859 6196 5977 62 41 265 N ATOM 366 CA LEU A 175 -106.135 80.728 -7.086 1.00 30.62 C ANISOU 366 CA LEU A 175 3713 4090 3834 75 49 290 C ATOM 367 C LEU A 175 -107.357 79.869 -6.783 1.00 51.07 C ANISOU 367 C LEU A 175 6258 6681 6466 108 73 267 C ATOM 368 O LEU A 175 -107.759 79.045 -7.598 1.00 73.58 O ANISOU 368 O LEU A 175 9140 9496 9323 116 82 241 O ATOM 369 CB LEU A 175 -106.543 81.956 -7.907 1.00 33.44 C ANISOU 369 CB LEU A 175 4027 4456 4222 88 56 252 C ATOM 370 CG LEU A 175 -106.748 83.242 -7.117 1.00 43.21 C ANISOU 370 CG LEU A 175 5229 5744 5446 78 47 282 C ATOM 371 CD1 LEU A 175 -105.495 83.566 -6.321 1.00 41.11 C ANISOU 371 CD1 LEU A 175 4995 5503 5123 33 19 334 C ATOM 372 CD2 LEU A 175 -107.112 84.389 -8.047 1.00 53.65 C ANISOU 372 CD2 LEU A 175 6617 7048 6719 74 43 292 C ATOM 373 N VAL A 176 -107.932 80.048 -5.598 1.00 43.88 N ANISOU 373 N VAL A 176 5377 5787 5508 108 72 330 N ATOM 374 CA VAL A 176 -109.202 79.428 -5.278 1.00 30.35 C ANISOU 374 CA VAL A 176 3611 4082 3839 143 97 305 C ATOM 375 C VAL A 176 -110.223 80.486 -4.930 1.00 44.29 C ANISOU 375 C VAL A 176 5362 5868 5597 159 105 323 C ATOM 376 O VAL A 176 -109.877 81.653 -4.741 1.00 71.33 O ANISOU 376 O VAL A 176 8833 9305 8964 135 87 370 O ATOM 377 CB VAL A 176 -109.173 78.399 -4.117 1.00 26.42 C ANISOU 377 CB VAL A 176 3157 3584 3299 135 92 364 C ATOM 378 CG1 VAL A 176 -108.143 77.302 -4.302 1.00 35.45 C ANISOU 378 CG1 VAL A 176 4304 4713 4451 120 83 350 C ATOM 379 CG2 VAL A 176 -109.231 79.042 -2.742 1.00 53.64 C ANISOU 379 CG2 VAL A 176 6569 7080 6732 137 91 412 C ATOM 380 N SER A 177 -111.485 80.080 -4.846 1.00 32.68 N ANISOU 380 N SER A 177 3903 4387 4129 181 123 324 N ATOM 381 CA SER A 177 -112.551 81.046 -4.658 1.00 42.00 C ANISOU 381 CA SER A 177 5073 5582 5302 198 132 339 C ATOM 382 C SER A 177 -113.208 80.929 -3.288 1.00 52.35 C ANISOU 382 C SER A 177 6353 6928 6610 213 141 376 C ATOM 383 O SER A 177 -113.681 79.862 -2.906 1.00 69.09 O ANISOU 383 O SER A 177 8479 9036 8735 226 153 379 O ATOM 384 CB SER A 177 -113.583 80.912 -5.773 1.00 42.63 C ANISOU 384 CB SER A 177 5247 5610 5339 186 146 346 C ATOM 385 OG SER A 177 -114.668 81.799 -5.572 1.00 38.92 O ANISOU 385 OG SER A 177 4712 5162 4912 236 143 334 O ATOM 386 N ASP A 178 -113.209 82.034 -2.548 1.00 32.47 N ANISOU 386 N ASP A 178 3799 4456 4083 210 135 406 N ATOM 387 CA ASP A 178 -113.766 82.076 -1.201 1.00 43.51 C ANISOU 387 CA ASP A 178 5252 5870 5410 205 131 492 C ATOM 388 C ASP A 178 -115.250 81.779 -1.219 1.00 34.62 C ANISOU 388 C ASP A 178 4051 4750 4353 253 164 447 C ATOM 389 O ASP A 178 -115.789 81.249 -0.255 1.00 54.08 O ANISOU 389 O ASP A 178 6594 7204 6750 248 162 522 O ATOM 390 CB ASP A 178 -113.554 83.450 -0.564 1.00 56.79 C ANISOU 390 CB ASP A 178 6899 7606 7072 191 117 525 C ATOM 391 CG ASP A 178 -112.094 83.774 -0.342 1.00 62.73 C ANISOU 391 CG ASP A 178 7531 8409 7892 173 104 486 C ATOM 392 OD1 ASP A 178 -111.359 82.897 0.158 1.00 60.62 O ANISOU 392 OD1 ASP A 178 7359 8116 7556 154 94 542 O ATOM 393 OD2 ASP A 178 -111.686 84.911 -0.663 1.00 72.91 O ANISOU 393 OD2 ASP A 178 8809 9723 9170 147 85 485 O ATOM 394 N LYS A 179 -115.904 82.139 -2.318 1.00 39.68 N ANISOU 394 N LYS A 179 4805 5338 4932 237 155 467 N ATOM 395 CA LYS A 179 -117.339 81.913 -2.470 1.00 47.92 C ANISOU 395 CA LYS A 179 5861 6371 5976 250 189 463 C ATOM 396 C LYS A 179 -117.723 80.429 -2.538 1.00 53.68 C ANISOU 396 C LYS A 179 6611 7067 6717 257 202 449 C ATOM 397 O LYS A 179 -118.421 79.918 -1.648 1.00 38.36 O ANISOU 397 O LYS A 179 4588 5144 4842 319 198 434 O ATOM 398 CB LYS A 179 -117.856 82.637 -3.715 1.00 34.16 C ANISOU 398 CB LYS A 179 4138 4607 4235 250 190 438 C ATOM 399 CG LYS A 179 -119.200 82.140 -4.200 1.00 43.09 C ANISOU 399 CG LYS A 179 5293 5709 5372 267 210 429 C ATOM 400 CD LYS A 179 -120.332 82.702 -3.368 1.00 62.68 C ANISOU 400 CD LYS A 179 7755 8218 7841 285 221 464 C ATOM 401 CE LYS A 179 -121.678 82.426 -4.033 1.00 84.42 C ANISOU 401 CE LYS A 179 10464 10943 10668 349 219 415 C ATOM 402 NZ LYS A 179 -121.680 82.826 -5.476 1.00 83.87 N ANISOU 402 NZ LYS A 179 10486 10843 10536 292 237 423 N ATOM 403 N ASP A 180 -117.250 79.742 -3.582 1.00 45.38 N ANISOU 403 N ASP A 180 5585 5980 5678 244 197 412 N ATOM 404 CA ASP A 180 -117.787 78.425 -3.945 1.00 48.78 C ANISOU 404 CA ASP A 180 5978 6380 6174 290 189 362 C ATOM 405 C ASP A 180 -116.757 77.314 -4.138 1.00 35.66 C ANISOU 405 C ASP A 180 4326 4705 4518 272 180 344 C ATOM 406 O ASP A 180 -117.090 76.258 -4.670 1.00 32.01 O ANISOU 406 O ASP A 180 3886 4215 4060 269 183 326 O ATOM 407 CB ASP A 180 -118.630 78.534 -5.224 1.00 64.52 C ANISOU 407 CB ASP A 180 8056 8341 8116 247 213 369 C ATOM 408 CG ASP A 180 -117.776 78.771 -6.465 1.00 66.19 C ANISOU 408 CG ASP A 180 8237 8529 8385 269 184 308 C ATOM 409 OD1 ASP A 180 -118.291 78.642 -7.600 1.00 72.41 O ANISOU 409 OD1 ASP A 180 9092 9292 9128 226 205 315 O ATOM 410 OD2 ASP A 180 -116.581 79.085 -6.298 1.00 41.30 O ANISOU 410 OD2 ASP A 180 5119 5390 5181 217 186 335 O ATOM 411 N GLY A 181 -115.515 77.544 -3.724 1.00 28.43 N ANISOU 411 N GLY A 181 3390 3810 3601 258 167 351 N ATOM 412 CA GLY A 181 -114.482 76.531 -3.868 1.00 21.60 C ANISOU 412 CA GLY A 181 2532 2935 2741 241 157 336 C ATOM 413 C GLY A 181 -113.985 76.286 -5.294 1.00 35.20 C ANISOU 413 C GLY A 181 4333 4618 4422 187 161 325 C ATOM 414 O GLY A 181 -113.193 75.375 -5.535 1.00 32.30 O ANISOU 414 O GLY A 181 3925 4244 4103 205 139 284 O ATOM 415 N SER A 182 -114.425 77.099 -6.253 1.00 40.23 N ANISOU 415 N SER A 182 4939 5243 5102 221 149 283 N ATOM 416 CA SER A 182 -113.933 76.928 -7.614 1.00 30.73 C ANISOU 416 CA SER A 182 3764 4011 3903 203 141 251 C ATOM 417 C SER A 182 -112.493 77.382 -7.752 1.00 34.78 C ANISOU 417 C SER A 182 4307 4528 4378 156 137 265 C ATOM 418 O SER A 182 -111.975 78.114 -6.921 1.00 43.19 O ANISOU 418 O SER A 182 5309 5626 5476 185 121 264 O ATOM 419 CB SER A 182 -114.809 77.622 -8.640 1.00 19.54 C ANISOU 419 CB SER A 182 2367 2573 2486 209 149 240 C ATOM 420 OG SER A 182 -114.899 79.002 -8.368 1.00 35.71 O ANISOU 420 OG SER A 182 4439 4641 4488 186 165 278 O ATOM 421 N GLN A 183 -111.869 76.917 -8.824 1.00 47.90 N ANISOU 421 N GLN A 183 5952 6167 6080 168 118 216 N ATOM 422 CA GLN A 183 -110.455 77.076 -9.062 1.00 35.10 C ANISOU 422 CA GLN A 183 4361 4546 4430 125 113 224 C ATOM 423 C GLN A 183 -110.248 78.053 -10.220 1.00 42.81 C ANISOU 423 C GLN A 183 5323 5509 5435 145 103 187 C ATOM 424 O GLN A 183 -111.048 78.077 -11.162 1.00 28.95 O ANISOU 424 O GLN A 183 3614 3733 3655 126 122 192 O ATOM 425 CB GLN A 183 -109.878 75.703 -9.425 1.00 32.91 C ANISOU 425 CB GLN A 183 4062 4257 4187 134 96 188 C ATOM 426 CG GLN A 183 -108.383 75.653 -9.505 1.00 33.49 C ANISOU 426 CG GLN A 183 4162 4326 4238 101 81 199 C ATOM 427 CD GLN A 183 -107.747 75.617 -8.134 1.00 61.19 C ANISOU 427 CD GLN A 183 7645 7864 7742 100 77 230 C ATOM 428 OE1 GLN A 183 -108.220 74.902 -7.249 1.00 75.98 O ANISOU 428 OE1 GLN A 183 9465 9763 9641 119 91 226 O ATOM 429 NE2 GLN A 183 -106.677 76.395 -7.942 1.00 48.31 N ANISOU 429 NE2 GLN A 183 5959 6262 6134 97 72 216 N ATOM 430 N SER A 184 -109.177 78.843 -10.153 1.00 38.31 N ANISOU 430 N SER A 184 4773 4948 4835 114 101 205 N ATOM 431 CA SER A 184 -108.863 79.799 -11.196 1.00 35.32 C ANISOU 431 CA SER A 184 4380 4557 4483 133 93 173 C ATOM 432 C SER A 184 -108.395 79.069 -12.437 1.00 23.20 C ANISOU 432 C SER A 184 2892 2992 2931 100 98 158 C ATOM 433 O SER A 184 -107.948 77.936 -12.358 1.00 51.03 O ANISOU 433 O SER A 184 6415 6514 6460 90 88 150 O ATOM 434 CB SER A 184 -107.784 80.775 -10.724 1.00 32.61 C ANISOU 434 CB SER A 184 4045 4236 4108 104 88 200 C ATOM 435 OG SER A 184 -106.545 80.117 -10.559 1.00 32.61 O ANISOU 435 OG SER A 184 4007 4248 4137 98 72 176 O ATOM 436 N LEU A 185 -108.526 79.717 -13.585 1.00 32.78 N ANISOU 436 N LEU A 185 4106 4181 4166 123 98 132 N ATOM 437 CA LEU A 185 -107.883 79.256 -14.809 1.00 30.04 C ANISOU 437 CA LEU A 185 3779 3813 3822 109 94 110 C ATOM 438 C LEU A 185 -106.866 80.312 -15.289 1.00 27.22 C ANISOU 438 C LEU A 185 3440 3455 3447 88 103 111 C ATOM 439 O LEU A 185 -106.982 81.501 -14.979 1.00 37.28 O ANISOU 439 O LEU A 185 4705 4725 4736 118 102 111 O ATOM 440 CB LEU A 185 -108.929 78.968 -15.893 1.00 29.27 C ANISOU 440 CB LEU A 185 3710 3702 3710 95 120 116 C ATOM 441 CG LEU A 185 -109.772 77.689 -15.789 1.00 36.82 C ANISOU 441 CG LEU A 185 4652 4651 4686 113 109 108 C ATOM 442 CD1 LEU A 185 -110.696 77.529 -16.997 1.00 33.04 C ANISOU 442 CD1 LEU A 185 4191 4152 4212 118 125 106 C ATOM 443 CD2 LEU A 185 -108.902 76.458 -15.652 1.00 32.04 C ANISOU 443 CD2 LEU A 185 4048 4060 4066 78 98 106 C ATOM 444 N VAL A 186 -105.875 79.866 -16.045 1.00 37.63 N ANISOU 444 N VAL A 186 4756 4757 4783 89 85 86 N ATOM 445 CA VAL A 186 -104.843 80.744 -16.556 1.00 10.81 C ANISOU 445 CA VAL A 186 1377 1358 1372 70 95 83 C ATOM 446 C VAL A 186 -104.900 80.740 -18.061 1.00 33.75 C ANISOU 446 C VAL A 186 4307 4223 4294 81 106 65 C ATOM 447 O VAL A 186 -104.749 79.689 -18.697 1.00 25.99 O ANISOU 447 O VAL A 186 3317 3257 3302 59 107 65 O ATOM 448 CB VAL A 186 -103.461 80.284 -16.100 1.00 26.89 C ANISOU 448 CB VAL A 186 3390 3407 3422 67 62 70 C ATOM 449 CG1 VAL A 186 -102.389 81.220 -16.641 1.00 39.32 C ANISOU 449 CG1 VAL A 186 4982 4974 4984 53 70 65 C ATOM 450 CG2 VAL A 186 -103.406 80.243 -14.580 1.00 28.70 C ANISOU 450 CG2 VAL A 186 3587 3670 3650 65 50 91 C ATOM 451 N TYR A 187 -105.112 81.916 -18.641 1.00 26.65 N ANISOU 451 N TYR A 187 3446 3287 3393 80 136 66 N ATOM 452 CA TYR A 187 -105.310 82.005 -20.072 1.00 26.35 C ANISOU 452 CA TYR A 187 3437 3213 3362 70 170 56 C ATOM 453 C TYR A 187 -104.116 82.686 -20.705 1.00 31.80 C ANISOU 453 C TYR A 187 4140 3916 4028 44 204 34 C ATOM 454 O TYR A 187 -103.912 83.876 -20.510 1.00 49.41 O ANISOU 454 O TYR A 187 6404 6126 6244 28 227 19 O ATOM 455 CB TYR A 187 -106.598 82.785 -20.404 1.00 26.66 C ANISOU 455 CB TYR A 187 3493 3257 3381 65 230 51 C ATOM 456 CG TYR A 187 -107.849 82.232 -19.777 1.00 34.84 C ANISOU 456 CG TYR A 187 4508 4310 4419 85 218 69 C ATOM 457 CD1 TYR A 187 -108.745 81.464 -20.512 1.00 48.84 C ANISOU 457 CD1 TYR A 187 6279 6079 6201 87 229 73 C ATOM 458 CD2 TYR A 187 -108.143 82.477 -18.447 1.00 42.58 C ANISOU 458 CD2 TYR A 187 5485 5281 5415 109 177 89 C ATOM 459 CE1 TYR A 187 -109.910 80.955 -19.926 1.00 15.82 C ANISOU 459 CE1 TYR A 187 2082 1912 2018 101 221 87 C ATOM 460 CE2 TYR A 187 -109.300 81.969 -17.857 1.00 40.39 C ANISOU 460 CE2 TYR A 187 5181 5050 5114 108 189 107 C ATOM 461 CZ TYR A 187 -110.168 81.217 -18.602 1.00 20.90 C ANISOU 461 CZ TYR A 187 2715 2573 2652 107 201 108 C ATOM 462 OH TYR A 187 -111.285 80.719 -18.006 1.00 53.97 O ANISOU 462 OH TYR A 187 6892 6775 6839 118 196 122 O ATOM 463 N PRO A 188 -103.313 81.931 -21.470 1.00 34.96 N ANISOU 463 N PRO A 188 4525 4321 4437 39 196 31 N ATOM 464 CA PRO A 188 -102.260 82.623 -22.195 1.00 21.84 C ANISOU 464 CA PRO A 188 2901 2600 2796 18 205 14 C ATOM 465 C PRO A 188 -102.928 83.655 -23.071 1.00 9.90 C ANISOU 465 C PRO A 188 1409 1088 1267 -10 291 -8 C ATOM 466 O PRO A 188 -103.917 83.339 -23.700 1.00 15.66 O ANISOU 466 O PRO A 188 2152 1751 2046 -10 290 -8 O ATOM 467 CB PRO A 188 -101.651 81.519 -23.051 1.00 24.26 C ANISOU 467 CB PRO A 188 3180 2918 3121 20 196 18 C ATOM 468 CG PRO A 188 -101.958 80.286 -22.353 1.00 19.24 C ANISOU 468 CG PRO A 188 2508 2323 2478 38 149 34 C ATOM 469 CD PRO A 188 -103.296 80.484 -21.737 1.00 43.20 C ANISOU 469 CD PRO A 188 5536 5385 5492 45 168 39 C ATOM 470 N LEU A 189 -102.387 84.867 -23.104 1.00 13.38 N ANISOU 470 N LEU A 189 1883 1511 1690 -46 323 -34 N ATOM 471 CA LEU A 189 -102.950 85.937 -23.892 1.00 7.74 C ANISOU 471 CA LEU A 189 1224 694 1023 -107 380 -79 C ATOM 472 C LEU A 189 -102.080 86.224 -25.098 1.00 25.42 C ANISOU 472 C LEU A 189 3455 2909 3296 -164 456 -123 C ATOM 473 O LEU A 189 -102.567 86.196 -26.229 1.00 36.58 O ANISOU 473 O LEU A 189 4846 4288 4764 -203 547 -173 O ATOM 474 CB LEU A 189 -103.105 87.190 -23.044 1.00 10.40 C ANISOU 474 CB LEU A 189 1636 1006 1309 -158 449 -111 C ATOM 475 CG LEU A 189 -104.057 87.025 -21.877 1.00 23.64 C ANISOU 475 CG LEU A 189 3324 2693 2965 -118 423 -80 C ATOM 476 CD1 LEU A 189 -104.046 88.264 -21.021 1.00 28.64 C ANISOU 476 CD1 LEU A 189 3988 3378 3517 -174 451 -92 C ATOM 477 CD2 LEU A 189 -105.473 86.694 -22.382 1.00 22.06 C ANISOU 477 CD2 LEU A 189 3115 2473 2793 -102 455 -73 C ATOM 478 N PHE A 190 -100.802 86.518 -24.861 1.00 36.91 N ANISOU 478 N PHE A 190 4916 4378 4731 -176 441 -125 N ATOM 479 CA PHE A 190 -99.834 86.626 -25.958 1.00 28.37 C ANISOU 479 CA PHE A 190 3804 3273 3701 -229 547 -194 C ATOM 480 C PHE A 190 -98.413 86.142 -25.649 1.00 21.14 C ANISOU 480 C PHE A 190 2880 2385 2767 -201 501 -165 C ATOM 481 O PHE A 190 -98.038 85.898 -24.505 1.00 29.56 O ANISOU 481 O PHE A 190 3955 3517 3760 -150 360 -77 O ATOM 482 CB PHE A 190 -99.800 88.029 -26.551 1.00 13.28 C ANISOU 482 CB PHE A 190 1902 1372 1773 -273 659 -333 C ATOM 483 CG PHE A 190 -99.335 89.069 -25.606 1.00 14.81 C ANISOU 483 CG PHE A 190 2174 1591 1862 -298 643 -326 C ATOM 484 CD1 PHE A 190 -98.013 89.469 -25.589 1.00 33.55 C ANISOU 484 CD1 PHE A 190 4573 3985 4189 -264 605 -382 C ATOM 485 CD2 PHE A 190 -100.222 89.672 -24.743 1.00 29.37 C ANISOU 485 CD2 PHE A 190 4071 3436 3650 -334 639 -290 C ATOM 486 CE1 PHE A 190 -97.583 90.454 -24.723 1.00 28.04 C ANISOU 486 CE1 PHE A 190 3957 3310 3386 -306 587 -370 C ATOM 487 CE2 PHE A 190 -99.799 90.649 -23.871 1.00 47.79 C ANISOU 487 CE2 PHE A 190 6462 5808 5890 -365 619 -287 C ATOM 488 CZ PHE A 190 -98.473 91.037 -23.859 1.00 42.66 C ANISOU 488 CZ PHE A 190 5843 5174 5191 -370 601 -311 C ATOM 489 N GLU A 191 -97.618 86.019 -26.696 1.00 27.45 N ANISOU 489 N GLU A 191 3629 3153 3648 -156 510 -296 N ATOM 490 CA GLU A 191 -96.343 85.345 -26.576 1.00 23.80 C ANISOU 490 CA GLU A 191 3182 2645 3215 -84 360 -306 C ATOM 491 C GLU A 191 -95.336 85.923 -27.550 1.00 12.51 C ANISOU 491 C GLU A 191 1791 1107 1854 -19 253 -463 C ATOM 492 O GLU A 191 -95.605 85.993 -28.737 1.00 42.12 O ANISOU 492 O GLU A 191 5477 4838 5688 8 299 -563 O ATOM 493 CB GLU A 191 -96.540 83.862 -26.849 1.00 14.32 C ANISOU 493 CB GLU A 191 1896 1458 2088 -63 335 -241 C ATOM 494 CG GLU A 191 -95.325 83.053 -26.583 1.00 40.36 C ANISOU 494 CG GLU A 191 5234 4691 5411 -21 149 -212 C ATOM 495 CD GLU A 191 -95.586 81.607 -26.803 1.00 37.79 C ANISOU 495 CD GLU A 191 4808 4407 5144 -10 138 -155 C ATOM 496 OE1 GLU A 191 -96.727 81.296 -27.180 1.00 40.50 O ANISOU 496 OE1 GLU A 191 5058 4819 5511 -35 271 -143 O ATOM 497 OE2 GLU A 191 -94.661 80.791 -26.609 1.00 54.56 O ANISOU 497 OE2 GLU A 191 6935 6504 7293 -1 12 -116 O ATOM 498 N ALA A 192 -94.178 86.332 -27.045 1.00 22.79 N ANISOU 498 N ALA A 192 3208 2331 3119 -13 111 -472 N ATOM 499 CA ALA A 192 -93.158 86.977 -27.874 1.00 29.38 C ANISOU 499 CA ALA A 192 4137 3048 3980 11 48 -593 C ATOM 500 C ALA A 192 -91.738 86.471 -27.584 1.00 33.67 C ANISOU 500 C ALA A 192 4748 3497 4549 -52 -27 -540 C ATOM 501 O ALA A 192 -91.196 86.731 -26.503 1.00 31.07 O ANISOU 501 O ALA A 192 4415 3204 4185 -138 -10 -482 O ATOM 502 CB ALA A 192 -93.231 88.480 -27.688 1.00 25.64 C ANISOU 502 CB ALA A 192 3716 2602 3425 8 76 -691 C ATOM 503 N PRO A 193 -91.145 85.726 -28.541 1.00 36.68 N ANISOU 503 N PRO A 193 5002 3835 5099 -1 -101 -586 N ATOM 504 CA PRO A 193 -89.738 85.303 -28.469 1.00 17.40 C ANISOU 504 CA PRO A 193 2520 1339 2752 2 -271 -561 C ATOM 505 C PRO A 193 -88.772 86.433 -28.857 1.00 16.23 C ANISOU 505 C PRO A 193 2447 1102 2619 -6 -318 -684 C ATOM 506 O PRO A 193 -89.059 87.216 -29.759 1.00 36.38 O ANISOU 506 O PRO A 193 5026 3618 5179 22 -240 -825 O ATOM 507 CB PRO A 193 -89.663 84.184 -29.507 1.00 34.25 C ANISOU 507 CB PRO A 193 4508 3460 5044 70 -351 -577 C ATOM 508 CG PRO A 193 -90.735 84.518 -30.491 1.00 36.69 C ANISOU 508 CG PRO A 193 4778 3783 5378 101 -210 -686 C ATOM 509 CD PRO A 193 -91.849 85.089 -29.668 1.00 38.67 C ANISOU 509 CD PRO A 193 5118 4109 5466 64 -69 -638 C ATOM 510 N VAL A 194 -87.648 86.516 -28.155 1.00 30.84 N ANISOU 510 N VAL A 194 4326 2928 4463 -34 -462 -621 N ATOM 511 CA VAL A 194 -86.542 87.405 -28.503 1.00 27.84 C ANISOU 511 CA VAL A 194 4007 2459 4113 -37 -550 -721 C ATOM 512 C VAL A 194 -85.815 86.924 -29.777 1.00 33.57 C ANISOU 512 C VAL A 194 4654 3097 5006 48 -671 -804 C ATOM 513 O VAL A 194 -85.780 85.738 -30.084 1.00 37.37 O ANISOU 513 O VAL A 194 5026 3591 5582 95 -758 -738 O ATOM 514 CB VAL A 194 -85.558 87.494 -27.329 1.00 28.14 C ANISOU 514 CB VAL A 194 4098 2505 4089 -80 -709 -590 C ATOM 515 CG1 VAL A 194 -84.310 88.310 -27.699 1.00 20.06 C ANISOU 515 CG1 VAL A 194 3139 1381 3103 -81 -828 -680 C ATOM 516 CG2 VAL A 194 -86.263 88.064 -26.099 1.00 22.25 C ANISOU 516 CG2 VAL A 194 3408 1854 3191 -159 -604 -517 C ATOM 517 N SER A 195 -85.246 87.866 -30.513 1.00 30.31 N ANISOU 517 N SER A 195 4290 2599 4627 62 -678 -956 N ATOM 518 CA SER A 195 -84.664 87.610 -31.826 1.00 28.14 C ANISOU 518 CA SER A 195 3937 2239 4515 144 -768 -1068 C ATOM 519 C SER A 195 -83.333 86.870 -31.778 1.00 39.68 C ANISOU 519 C SER A 195 5357 3640 6078 173 -1012 -989 C ATOM 520 O SER A 195 -82.940 86.246 -32.757 1.00 52.22 O ANISOU 520 O SER A 195 6846 5177 7817 239 -1108 -1039 O ATOM 521 CB SER A 195 -84.427 88.940 -32.550 1.00 41.32 C ANISOU 521 CB SER A 195 5688 3838 6172 152 -702 -1257 C ATOM 522 OG SER A 195 -85.635 89.603 -32.845 1.00 48.82 O ANISOU 522 OG SER A 195 6670 4843 7038 148 -498 -1341 O ATOM 523 N PHE A 196 -82.622 86.950 -30.659 1.00 40.76 N ANISOU 523 N PHE A 196 5569 3784 6133 124 -1124 -863 N ATOM 524 CA PHE A 196 -81.253 86.439 -30.620 1.00 27.40 C ANISOU 524 CA PHE A 196 3867 2026 4519 153 -1372 -788 C ATOM 525 C PHE A 196 -80.935 85.578 -29.410 1.00 47.52 C ANISOU 525 C PHE A 196 6419 4642 6995 126 -1506 -562 C ATOM 526 O PHE A 196 -81.470 85.804 -28.326 1.00 50.51 O ANISOU 526 O PHE A 196 6856 5103 7233 68 -1425 -464 O ATOM 527 CB PHE A 196 -80.267 87.594 -30.705 1.00 42.68 C ANISOU 527 CB PHE A 196 5910 3864 6441 135 -1437 -881 C ATOM 528 CG PHE A 196 -80.586 88.736 -29.795 1.00 29.25 C ANISOU 528 CG PHE A 196 4331 2205 4577 48 -1319 -885 C ATOM 529 CD1 PHE A 196 -80.197 88.713 -28.461 1.00 52.46 C ANISOU 529 CD1 PHE A 196 7338 5191 7404 -11 -1410 -707 C ATOM 530 CD2 PHE A 196 -81.232 89.856 -30.281 1.00 43.27 C ANISOU 530 CD2 PHE A 196 6158 3976 6305 23 -1128 -1063 C ATOM 531 CE1 PHE A 196 -80.476 89.785 -27.613 1.00 51.55 C ANISOU 531 CE1 PHE A 196 7323 5121 7143 -97 -1314 -709 C ATOM 532 CE2 PHE A 196 -81.520 90.924 -29.437 1.00 59.68 C ANISOU 532 CE2 PHE A 196 8340 6104 8231 -68 -1025 -1073 C ATOM 533 CZ PHE A 196 -81.137 90.889 -28.098 1.00 33.83 C ANISOU 533 CZ PHE A 196 5114 2879 4859 -129 -1123 -899 C ATOM 534 N PHE A 197 -80.045 84.604 -29.600 1.00 57.20 N ANISOU 534 N PHE A 197 7583 5838 8313 169 -1717 -480 N ATOM 535 CA PHE A 197 -79.680 83.670 -28.538 1.00 53.91 C ANISOU 535 CA PHE A 197 7165 5494 7825 151 -1865 -264 C ATOM 536 C PHE A 197 -79.156 84.423 -27.334 1.00 34.97 C ANISOU 536 C PHE A 197 4904 3103 5281 90 -1914 -153 C ATOM 537 O PHE A 197 -78.672 85.534 -27.465 1.00 47.52 O ANISOU 537 O PHE A 197 6583 4612 6862 71 -1905 -242 O ATOM 538 CB PHE A 197 -78.592 82.704 -29.013 1.00 73.44 C ANISOU 538 CB PHE A 197 9577 7921 10405 184 -2059 -219 C ATOM 539 CG PHE A 197 -79.103 81.537 -29.819 1.00104.92 C ANISOU 539 CG PHE A 197 13432 11950 14483 206 -1991 -252 C ATOM 540 CD1 PHE A 197 -80.374 81.024 -29.612 1.00115.14 C ANISOU 540 CD1 PHE A 197 14671 13355 15723 185 -1820 -231 C ATOM 541 CD2 PHE A 197 -78.297 80.944 -30.783 1.00120.76 C ANISOU 541 CD2 PHE A 197 15376 13882 16624 240 -2102 -301 C ATOM 542 CE1 PHE A 197 -80.835 79.945 -30.358 1.00121.31 C ANISOU 542 CE1 PHE A 197 15343 14171 16577 197 -1760 -256 C ATOM 543 CE2 PHE A 197 -78.752 79.867 -31.530 1.00126.09 C ANISOU 543 CE2 PHE A 197 15942 14593 17372 250 -2040 -324 C ATOM 544 CZ PHE A 197 -80.022 79.366 -31.317 1.00125.02 C ANISOU 544 CZ PHE A 197 15759 14567 17176 226 -1868 -300 C ATOM 545 N GLY A 198 -79.246 83.817 -26.159 1.00 51.66 N ANISOU 545 N GLY A 198 7033 5344 7253 16 -1824 3 N ATOM 546 CA GLY A 198 -78.476 84.305 -25.034 1.00 59.12 C ANISOU 546 CA GLY A 198 8074 6315 8072 -63 -1812 101 C ATOM 547 C GLY A 198 -79.251 84.826 -23.854 1.00 49.73 C ANISOU 547 C GLY A 198 6932 5240 6725 -131 -1653 166 C ATOM 548 O GLY A 198 -80.377 85.289 -23.987 1.00 57.97 O ANISOU 548 O GLY A 198 7989 6292 7744 -114 -1604 125 O ATOM 549 N LYS A 199 -78.621 84.756 -22.689 1.00 57.99 N ANISOU 549 N LYS A 199 7988 6375 7670 -202 -1573 257 N ATOM 550 CA LYS A 199 -79.224 85.249 -21.465 1.00 59.44 C ANISOU 550 CA LYS A 199 8183 6682 7720 -260 -1415 306 C ATOM 551 C LYS A 199 -79.424 86.754 -21.523 1.00 54.81 C ANISOU 551 C LYS A 199 7735 5998 7092 -284 -1495 287 C ATOM 552 O LYS A 199 -80.213 87.298 -20.747 1.00 46.98 O ANISOU 552 O LYS A 199 6757 5095 5998 -328 -1364 309 O ATOM 553 CB LYS A 199 -78.389 84.863 -20.240 1.00 49.01 C ANISOU 553 CB LYS A 199 6887 5266 6468 -393 -1250 333 C ATOM 554 CG LYS A 199 -78.512 83.405 -19.865 1.00 67.59 C ANISOU 554 CG LYS A 199 9172 7660 8849 -418 -1220 366 C ATOM 555 CD LYS A 199 -77.627 83.033 -18.691 1.00 87.08 C ANISOU 555 CD LYS A 199 11552 10361 11173 -465 -1383 405 C ATOM 556 CE LYS A 199 -77.682 81.535 -18.431 1.00102.19 C ANISOU 556 CE LYS A 199 13502 12074 13252 -521 -1235 471 C ATOM 557 NZ LYS A 199 -76.736 81.112 -17.366 1.00106.87 N ANISOU 557 NZ LYS A 199 14100 12663 13842 -603 -1280 545 N ATOM 558 N LEU A 200 -78.728 87.423 -22.442 1.00 29.07 N ANISOU 558 N LEU A 200 4576 2559 3910 -245 -1711 231 N ATOM 559 CA LEU A 200 -78.861 88.876 -22.557 1.00 40.81 C ANISOU 559 CA LEU A 200 6207 3953 5345 -265 -1769 172 C ATOM 560 C LEU A 200 -80.229 89.267 -23.105 1.00 51.95 C ANISOU 560 C LEU A 200 7557 5417 6766 -268 -1526 -8 C ATOM 561 O LEU A 200 -80.724 90.363 -22.833 1.00 69.06 O ANISOU 561 O LEU A 200 9777 7613 8849 -331 -1398 -85 O ATOM 562 CB LEU A 200 -77.715 89.499 -23.373 1.00 59.16 C ANISOU 562 CB LEU A 200 8572 6136 7770 -248 -1883 40 C ATOM 563 CG LEU A 200 -77.860 90.056 -24.795 1.00 85.09 C ANISOU 563 CG LEU A 200 11808 9343 11178 -209 -1788 -240 C ATOM 564 CD1 LEU A 200 -78.981 91.082 -24.942 1.00 83.75 C ANISOU 564 CD1 LEU A 200 11646 9231 10945 -258 -1548 -408 C ATOM 565 CD2 LEU A 200 -76.532 90.673 -25.234 1.00 93.09 C ANISOU 565 CD2 LEU A 200 12893 10228 12250 -204 -1946 -310 C ATOM 566 N GLY A 201 -80.845 88.364 -23.862 1.00 45.58 N ANISOU 566 N GLY A 201 6636 4626 6057 -202 -1466 -69 N ATOM 567 CA GLY A 201 -82.205 88.573 -24.340 1.00 30.44 C ANISOU 567 CA GLY A 201 4659 2759 4146 -203 -1234 -208 C ATOM 568 C GLY A 201 -83.178 88.842 -23.206 1.00 27.55 C ANISOU 568 C GLY A 201 4329 2514 3624 -267 -1116 -103 C ATOM 569 O GLY A 201 -84.247 89.394 -23.428 1.00 56.98 O ANISOU 569 O GLY A 201 8036 6283 7331 -289 -923 -222 O ATOM 570 N ASP A 202 -82.804 88.453 -21.990 1.00 41.78 N ANISOU 570 N ASP A 202 6184 4382 5308 -296 -1238 124 N ATOM 571 CA ASP A 202 -83.604 88.709 -20.788 1.00 31.45 C ANISOU 571 CA ASP A 202 4899 3211 3841 -362 -1122 235 C ATOM 572 C ASP A 202 -83.589 90.187 -20.410 1.00 33.31 C ANISOU 572 C ASP A 202 5260 3419 3978 -441 -1087 212 C ATOM 573 O ASP A 202 -84.251 90.608 -19.445 1.00 30.19 O ANISOU 573 O ASP A 202 4851 3141 3479 -500 -949 268 O ATOM 574 CB ASP A 202 -83.075 87.895 -19.604 1.00 42.26 C ANISOU 574 CB ASP A 202 6101 4739 5218 -374 -1002 295 C ATOM 575 CG ASP A 202 -83.265 86.402 -19.775 1.00 43.54 C ANISOU 575 CG ASP A 202 6119 4978 5445 -319 -948 281 C ATOM 576 OD1 ASP A 202 -83.661 85.970 -20.873 1.00 46.60 O ANISOU 576 OD1 ASP A 202 6517 5287 5903 -275 -1013 243 O ATOM 577 OD2 ASP A 202 -83.002 85.656 -18.806 1.00 59.03 O ANISOU 577 OD2 ASP A 202 8045 6869 7514 -406 -831 297 O ATOM 578 N SER A 203 -82.828 90.973 -21.166 1.00 24.41 N ANISOU 578 N SER A 203 4157 2184 2933 -441 -1125 49 N ATOM 579 CA SER A 203 -82.777 92.416 -20.957 1.00 28.41 C ANISOU 579 CA SER A 203 4742 2691 3362 -516 -1072 -40 C ATOM 580 C SER A 203 -83.841 93.109 -21.784 1.00 30.08 C ANISOU 580 C SER A 203 4892 2938 3601 -507 -874 -285 C ATOM 581 O SER A 203 -84.154 94.271 -21.555 1.00 32.51 O ANISOU 581 O SER A 203 5244 3293 3815 -562 -803 -363 O ATOM 582 CB SER A 203 -81.395 92.958 -21.280 1.00 51.21 C ANISOU 582 CB SER A 203 7695 5466 6298 -522 -1226 -94 C ATOM 583 OG SER A 203 -80.429 92.346 -20.449 1.00 68.40 O ANISOU 583 OG SER A 203 9933 7612 8444 -531 -1410 150 O ATOM 584 N ASN A 204 -84.404 92.369 -22.737 1.00 31.55 N ANISOU 584 N ASN A 204 4972 3106 3910 -437 -791 -396 N ATOM 585 CA ASN A 204 -85.571 92.812 -23.490 1.00 36.55 C ANISOU 585 CA ASN A 204 5530 3782 4574 -421 -590 -599 C ATOM 586 C ASN A 204 -86.873 92.571 -22.743 1.00 36.89 C ANISOU 586 C ASN A 204 5551 3947 4520 -432 -481 -486 C ATOM 587 O ASN A 204 -87.017 91.572 -22.051 1.00 33.34 O ANISOU 587 O ASN A 204 5103 3529 4034 -430 -523 -283 O ATOM 588 CB ASN A 204 -85.661 92.066 -24.804 1.00 42.58 C ANISOU 588 CB ASN A 204 6209 4471 5500 -354 -533 -729 C ATOM 589 CG ASN A 204 -84.483 92.314 -25.682 1.00 31.70 C ANISOU 589 CG ASN A 204 4872 2967 4207 -333 -631 -836 C ATOM 590 OD1 ASN A 204 -83.720 91.396 -25.982 1.00 42.33 O ANISOU 590 OD1 ASN A 204 6200 4241 5644 -276 -777 -756 O ATOM 591 ND2 ASN A 204 -84.329 93.553 -26.119 1.00 36.52 N ANISOU 591 ND2 ASN A 204 5529 3557 4788 -369 -566 -1020 N ATOM 592 N GLY A 205 -87.819 93.493 -22.906 1.00 35.14 N ANISOU 592 N GLY A 205 5316 3799 4238 -434 -353 -611 N ATOM 593 CA GLY A 205 -89.129 93.399 -22.291 1.00 27.76 C ANISOU 593 CA GLY A 205 4384 2979 3182 -446 -235 -499 C ATOM 594 C GLY A 205 -90.048 94.444 -22.889 1.00 24.95 C ANISOU 594 C GLY A 205 4019 2689 2771 -412 -108 -664 C ATOM 595 O GLY A 205 -89.688 95.087 -23.875 1.00 24.36 O ANISOU 595 O GLY A 205 3915 2562 2777 -349 -135 -881 O ATOM 596 N MET A 206 -91.233 94.629 -22.307 1.00 44.68 N ANISOU 596 N MET A 206 6550 5299 5128 -461 38 -547 N ATOM 597 CA MET A 206 -92.164 95.616 -22.842 1.00 18.87 C ANISOU 597 CA MET A 206 3255 2112 1802 -428 172 -659 C ATOM 598 C MET A 206 -93.169 96.220 -21.866 1.00 27.99 C ANISOU 598 C MET A 206 4429 3378 2826 -529 298 -508 C ATOM 599 O MET A 206 -93.223 95.843 -20.703 1.00 31.80 O ANISOU 599 O MET A 206 4929 3864 3290 -615 273 -320 O ATOM 600 CB MET A 206 -92.892 95.031 -24.042 1.00 16.18 C ANISOU 600 CB MET A 206 2821 1753 1574 -322 244 -765 C ATOM 601 CG MET A 206 -93.328 93.624 -23.835 1.00 43.39 C ANISOU 601 CG MET A 206 6205 5191 5092 -315 259 -634 C ATOM 602 SD MET A 206 -94.311 92.934 -25.358 1.00 74.14 S ANISOU 602 SD MET A 206 9983 9070 9118 -206 356 -736 S ATOM 603 CE MET A 206 -92.894 92.743 -26.672 1.00 38.17 C ANISOU 603 CE MET A 206 5462 4325 4716 -78 153 -930 C ATOM 604 N ARG A 207 -93.930 97.191 -22.372 1.00 27.82 N ANISOU 604 N ARG A 207 4389 3418 2761 -520 408 -605 N ATOM 605 CA ARG A 207 -95.037 97.810 -21.669 1.00 15.85 C ANISOU 605 CA ARG A 207 2854 1978 1189 -604 503 -508 C ATOM 606 C ARG A 207 -96.265 97.833 -22.579 1.00 35.54 C ANISOU 606 C ARG A 207 5263 4509 3732 -557 624 -584 C ATOM 607 O ARG A 207 -96.144 97.802 -23.804 1.00 34.40 O ANISOU 607 O ARG A 207 5092 4346 3632 -469 653 -733 O ATOM 608 CB ARG A 207 -94.707 99.236 -21.254 1.00 27.38 C ANISOU 608 CB ARG A 207 4394 3481 2528 -670 496 -538 C ATOM 609 CG ARG A 207 -93.777 99.353 -20.087 1.00 35.80 C ANISOU 609 CG ARG A 207 5536 4521 3547 -756 380 -416 C ATOM 610 CD ARG A 207 -93.092 100.706 -20.100 1.00 25.95 C ANISOU 610 CD ARG A 207 4382 3293 2186 -792 348 -501 C ATOM 611 NE ARG A 207 -92.090 100.801 -19.054 1.00 26.75 N ANISOU 611 NE ARG A 207 4558 3355 2253 -879 221 -379 N ATOM 612 CZ ARG A 207 -91.287 101.841 -18.865 1.00 38.16 C ANISOU 612 CZ ARG A 207 6095 4796 3607 -927 156 -418 C ATOM 613 NH1 ARG A 207 -91.352 102.894 -19.664 1.00 32.68 N ANISOU 613 NH1 ARG A 207 5434 4135 2846 -890 204 -596 N ATOM 614 NH2 ARG A 207 -90.408 101.815 -17.872 1.00 37.42 N ANISOU 614 NH2 ARG A 207 6059 4656 3505 -1016 36 -281 N ATOM 615 N VAL A 208 -97.442 97.906 -21.962 1.00 24.26 N ANISOU 615 N VAL A 208 3791 3117 2309 -610 667 -494 N ATOM 616 CA VAL A 208 -98.724 97.764 -22.643 1.00 21.23 C ANISOU 616 CA VAL A 208 3332 2757 1979 -580 753 -531 C ATOM 617 C VAL A 208 -99.761 98.460 -21.803 1.00 22.51 C ANISOU 617 C VAL A 208 3491 2971 2090 -641 766 -473 C ATOM 618 O VAL A 208 -99.808 98.279 -20.584 1.00 29.15 O ANISOU 618 O VAL A 208 4342 3809 2925 -676 690 -369 O ATOM 619 CB VAL A 208 -99.243 96.296 -22.665 1.00 30.64 C ANISOU 619 CB VAL A 208 4458 3896 3288 -540 727 -458 C ATOM 620 CG1 VAL A 208 -100.085 96.061 -23.897 1.00 32.13 C ANISOU 620 CG1 VAL A 208 4579 4091 3539 -491 809 -540 C ATOM 621 CG2 VAL A 208 -98.118 95.273 -22.544 1.00 37.66 C ANISOU 621 CG2 VAL A 208 5365 4719 4226 -513 650 -415 C ATOM 622 N TRP A 209 -100.633 99.206 -22.457 1.00 24.71 N ANISOU 622 N TRP A 209 3748 3301 2339 -644 854 -549 N ATOM 623 CA TRP A 209 -101.702 99.881 -21.759 1.00 20.43 C ANISOU 623 CA TRP A 209 3203 2813 1746 -694 868 -505 C ATOM 624 C TRP A 209 -102.824 100.223 -22.708 1.00 19.38 C ANISOU 624 C TRP A 209 3027 2719 1616 -679 964 -582 C ATOM 625 O TRP A 209 -102.602 100.401 -23.895 1.00 42.97 O ANISOU 625 O TRP A 209 6001 5711 4615 -646 1032 -696 O ATOM 626 CB TRP A 209 -101.171 101.123 -21.053 1.00 31.24 C ANISOU 626 CB TRP A 209 4642 4225 3002 -768 853 -503 C ATOM 627 CG TRP A 209 -100.613 102.204 -21.951 1.00 32.51 C ANISOU 627 CG TRP A 209 4851 4419 3084 -775 924 -635 C ATOM 628 CD1 TRP A 209 -101.297 103.249 -22.484 1.00 38.49 C ANISOU 628 CD1 TRP A 209 5610 5238 3776 -797 1012 -720 C ATOM 629 CD2 TRP A 209 -99.249 102.367 -22.368 1.00 31.67 C ANISOU 629 CD2 TRP A 209 4803 4284 2948 -748 898 -709 C ATOM 630 NE1 TRP A 209 -100.452 104.043 -23.216 1.00 24.29 N ANISOU 630 NE1 TRP A 209 3866 3451 1914 -781 1046 -849 N ATOM 631 CE2 TRP A 209 -99.195 103.519 -23.166 1.00 23.60 C ANISOU 631 CE2 TRP A 209 3816 3305 1847 -743 970 -851 C ATOM 632 CE3 TRP A 209 -98.074 101.634 -22.159 1.00 55.65 C ANISOU 632 CE3 TRP A 209 7870 7258 6015 -721 811 -679 C ATOM 633 CZ2 TRP A 209 -98.005 103.970 -23.754 1.00 48.44 C ANISOU 633 CZ2 TRP A 209 7030 6424 4949 -697 944 -981 C ATOM 634 CZ3 TRP A 209 -96.892 102.086 -22.746 1.00 38.27 C ANISOU 634 CZ3 TRP A 209 5740 5034 3768 -679 780 -802 C ATOM 635 CH2 TRP A 209 -96.870 103.242 -23.528 1.00 28.76 C ANISOU 635 CH2 TRP A 209 4572 3864 2493 -661 839 -958 C ATOM 636 N SER A 210 -104.040 100.287 -22.166 1.00 38.99 N ANISOU 636 N SER A 210 5488 5234 4092 -696 963 -525 N ATOM 637 CA SER A 210 -105.246 100.570 -22.938 1.00 26.61 C ANISOU 637 CA SER A 210 3882 3705 2522 -692 1045 -580 C ATOM 638 C SER A 210 -105.438 102.064 -23.083 1.00 22.18 C ANISOU 638 C SER A 210 3356 3219 1852 -753 1115 -650 C ATOM 639 O SER A 210 -104.898 102.838 -22.287 1.00 32.17 O ANISOU 639 O SER A 210 4675 4507 3040 -806 1085 -626 O ATOM 640 CB SER A 210 -106.446 100.001 -22.217 1.00 45.63 C ANISOU 640 CB SER A 210 6262 6116 4959 -677 1004 -487 C ATOM 641 OG SER A 210 -106.413 100.427 -20.868 1.00 63.32 O ANISOU 641 OG SER A 210 8530 8383 7145 -713 939 -408 O ATOM 642 N THR A 211 -106.191 102.469 -24.105 1.00 48.78 N ANISOU 642 N THR A 211 7617 5334 5583 2871 3003 2408 N ATOM 643 CA THR A 211 -106.515 103.875 -24.313 1.00 49.29 C ANISOU 643 CA THR A 211 7772 5362 5594 2879 3018 2403 C ATOM 644 C THR A 211 -107.783 104.271 -23.547 1.00 49.50 C ANISOU 644 C THR A 211 7859 5405 5544 2905 2967 2396 C ATOM 645 O THR A 211 -108.559 103.414 -23.121 1.00 58.59 O ANISOU 645 O THR A 211 8982 6587 6692 2910 2928 2392 O ATOM 646 CB THR A 211 -106.683 104.183 -25.789 1.00 49.31 C ANISOU 646 CB THR A 211 7787 5309 5637 2849 3074 2390 C ATOM 647 OG1 THR A 211 -107.551 103.218 -26.386 1.00 66.28 O ANISOU 647 OG1 THR A 211 9897 7462 7823 2830 3069 2378 O ATOM 648 CG2 THR A 211 -105.340 104.129 -26.485 1.00 49.25 C ANISOU 648 CG2 THR A 211 7738 5278 5695 2827 3126 2396 C ATOM 649 N THR A 212 -107.987 105.570 -23.365 1.00 50.01 N ANISOU 649 N THR A 212 8007 5449 5545 2920 2968 2395 N ATOM 650 CA THR A 212 -109.115 106.049 -22.578 1.00 50.27 C ANISOU 650 CA THR A 212 8101 5497 5501 2946 2917 2390 C ATOM 651 C THR A 212 -109.585 107.434 -23.012 1.00 52.86 C ANISOU 651 C THR A 212 8523 5784 5778 2946 2937 2383 C ATOM 652 O THR A 212 -108.761 108.307 -23.282 1.00 51.09 O ANISOU 652 O THR A 212 8331 5534 5546 2941 2973 2388 O ATOM 653 CB THR A 212 -108.751 106.067 -21.086 1.00 50.40 C ANISOU 653 CB THR A 212 8116 5564 5471 2983 2864 2404 C ATOM 654 OG1 THR A 212 -108.706 104.722 -20.585 1.00 68.58 O ANISOU 654 OG1 THR A 212 10339 7909 7810 2986 2834 2407 O ATOM 655 CG2 THR A 212 -109.761 106.828 -20.316 1.00 50.78 C ANISOU 655 CG2 THR A 212 8238 5621 5436 3012 2816 2400 C ATOM 656 N THR A 213 -110.904 107.637 -23.075 1.00 50.87 N ANISOU 656 N THR A 213 8315 5524 5488 2949 2914 2371 N ATOM 657 CA THR A 213 -111.444 108.942 -23.437 1.00 51.36 C ANISOU 657 CA THR A 213 8468 5549 5497 2949 2929 2364 C ATOM 658 C THR A 213 -111.366 109.760 -22.171 1.00 51.84 C ANISOU 658 C THR A 213 8589 5630 5478 2981 2892 2374 C ATOM 659 O THR A 213 -112.323 110.422 -21.792 1.00 96.54 O ANISOU 659 O THR A 213 14330 11276 11076 2989 2881 2369 O ATOM 660 CB THR A 213 -112.947 108.883 -23.790 1.00 51.34 C ANISOU 660 CB THR A 213 8496 5534 5476 2943 2912 2350 C ATOM 661 OG1 THR A 213 -113.669 108.260 -22.719 1.00 51.20 O ANISOU 661 OG1 THR A 213 8464 5561 5429 2967 2848 2351 O ATOM 662 CG2 THR A 213 -113.162 108.109 -25.079 1.00 50.94 C ANISOU 662 CG2 THR A 213 8397 5458 5500 2908 2953 2340 C ATOM 663 N ALA A 214 -110.215 109.719 -21.522 1.00 58.30 N ANISOU 663 N ALA A 214 9370 6484 6298 3000 2872 2388 N ATOM 664 CA ALA A 214 -109.976 110.502 -20.319 1.00 56.22 C ANISOU 664 CA ALA A 214 9155 6244 5960 3031 2836 2399 C ATOM 665 C ALA A 214 -108.588 111.126 -20.493 1.00 57.98 C ANISOU 665 C ALA A 214 9366 6465 6199 3026 2870 2412 C ATOM 666 O ALA A 214 -108.294 112.147 -19.881 1.00 57.97 O ANISOU 666 O ALA A 214 9370 6499 6158 3053 2836 2426 O ATOM 667 CB ALA A 214 -110.353 109.841 -18.981 1.00 52.12 C ANISOU 667 CB ALA A 214 8607 5782 5413 3066 2764 2405 C ATOM 668 N ASP A 215 -107.705 110.536 -21.284 1.00 52.25 N ANISOU 668 N ASP A 215 8622 5699 5533 2993 2935 2409 N ATOM 669 CA ASP A 215 -106.406 111.197 -21.395 1.00 80.90 C ANISOU 669 CA ASP A 215 12240 9326 9173 2988 2965 2423 C ATOM 670 C ASP A 215 -105.920 112.355 -22.260 1.00 52.81 C ANISOU 670 C ASP A 215 8744 5717 5604 2963 3025 2418 C ATOM 671 O ASP A 215 -106.474 112.660 -23.312 1.00 62.68 O ANISOU 671 O ASP A 215 10024 6924 6870 2939 3063 2403 O ATOM 672 CB ASP A 215 -105.517 109.971 -21.601 1.00 93.66 C ANISOU 672 CB ASP A 215 13757 10956 10875 2975 2983 2431 C ATOM 673 CG ASP A 215 -104.121 110.154 -21.017 1.00113.72 C ANISOU 673 CG ASP A 215 16279 13515 13415 2982 2988 2449 C ATOM 674 OD1 ASP A 215 -103.990 110.898 -20.023 1.00105.75 O ANISOU 674 OD1 ASP A 215 15315 12531 12332 3009 2953 2459 O ATOM 675 OD2 ASP A 215 -103.156 109.557 -21.545 1.00131.29 O ANISOU 675 OD2 ASP A 215 18441 15730 15712 2960 3027 2455 O ATOM 676 N ILE A 216 -104.875 113.000 -21.763 1.00 57.43 N ANISOU 676 N ILE A 216 9350 6311 6160 2968 3032 2430 N ATOM 677 CA ILE A 216 -104.059 113.904 -22.552 1.00 63.79 C ANISOU 677 CA ILE A 216 10196 7073 6970 2939 3096 2426 C ATOM 678 C ILE A 216 -103.845 113.611 -24.047 1.00 56.89 C ANISOU 678 C ILE A 216 9289 6148 6178 2903 3158 2412 C ATOM 679 O ILE A 216 -104.077 114.474 -24.886 1.00 76.70 O ANISOU 679 O ILE A 216 11848 8620 8675 2889 3180 2396 O ATOM 680 CB ILE A 216 -102.595 113.966 -21.987 1.00 77.31 C ANISOU 680 CB ILE A 216 11882 8807 8686 2940 3105 2444 C ATOM 681 CG1 ILE A 216 -101.840 112.637 -22.184 1.00 57.72 C ANISOU 681 CG1 ILE A 216 9294 6337 6299 2931 3117 2453 C ATOM 682 CG2 ILE A 216 -102.614 114.365 -20.506 1.00 71.76 C ANISOU 682 CG2 ILE A 216 11208 8158 7898 2978 3038 2459 C ATOM 683 CD1 ILE A 216 -101.197 112.064 -20.909 1.00 52.86 C ANISOU 683 CD1 ILE A 216 8630 5782 5674 2960 3067 2475 C ATOM 684 N GLU A 217 -103.434 112.396 -24.383 1.00 52.75 N ANISOU 684 N GLU A 217 8683 5623 5738 2888 3184 2418 N ATOM 685 CA GLU A 217 -103.338 111.992 -25.777 1.00 52.44 C ANISOU 685 CA GLU A 217 8601 5542 5781 2857 3234 2405 C ATOM 686 C GLU A 217 -104.758 111.646 -26.157 1.00 52.25 C ANISOU 686 C GLU A 217 8585 5514 5755 2859 3214 2391 C ATOM 687 O GLU A 217 -105.582 111.359 -25.287 1.00 52.52 O ANISOU 687 O GLU A 217 8622 5586 5746 2885 3156 2394 O ATOM 688 CB GLU A 217 -102.491 110.718 -25.870 1.00 51.92 C ANISOU 688 CB GLU A 217 8433 5494 5802 2848 3240 2415 C ATOM 689 CG GLU A 217 -101.030 110.981 -26.058 1.00 62.97 C ANISOU 689 CG GLU A 217 9816 6878 7234 2831 3284 2423 C ATOM 690 CD GLU A 217 -100.786 111.932 -27.205 1.00 77.58 C ANISOU 690 CD GLU A 217 11717 8665 9094 2801 3351 2409 C ATOM 691 OE1 GLU A 217 -101.152 113.132 -27.077 1.00 52.90 O ANISOU 691 OE1 GLU A 217 8681 5525 5894 2804 3355 2402 O ATOM 692 OE2 GLU A 217 -100.238 111.472 -28.233 1.00 76.12 O ANISOU 692 OE2 GLU A 217 11482 8447 8991 2774 3399 2403 O ATOM 693 N GLU A 218 -105.048 111.656 -27.453 1.00 52.19 N ANISOU 693 N GLU A 218 8575 5460 5793 2831 3263 2377 N ATOM 694 CA GLU A 218 -106.243 110.971 -27.918 1.00 53.97 C ANISOU 694 CA GLU A 218 8780 5686 6040 2828 3247 2366 C ATOM 695 C GLU A 218 -105.891 109.759 -28.759 1.00 73.64 C ANISOU 695 C GLU A 218 11179 8172 8630 2807 3273 2364 C ATOM 696 O GLU A 218 -104.717 109.420 -28.904 1.00 68.93 O ANISOU 696 O GLU A 218 10532 7573 8085 2796 3299 2371 O ATOM 697 CB GLU A 218 -107.221 111.900 -28.621 1.00 58.94 C ANISOU 697 CB GLU A 218 9488 6277 6632 2819 3267 2350 C ATOM 698 CG GLU A 218 -107.927 112.894 -27.670 1.00 91.64 C ANISOU 698 CG GLU A 218 13715 10433 10670 2844 3224 2352 C ATOM 699 CD GLU A 218 -108.389 112.275 -26.341 1.00 94.55 C ANISOU 699 CD GLU A 218 14063 10861 11003 2877 3149 2362 C ATOM 700 OE1 GLU A 218 -108.584 111.041 -26.276 1.00 96.42 O ANISOU 700 OE1 GLU A 218 14224 11122 11289 2878 3129 2363 O ATOM 701 OE2 GLU A 218 -108.558 113.033 -25.357 1.00 79.02 O ANISOU 701 OE2 GLU A 218 12154 8914 8956 2901 3111 2367 O ATOM 702 N PHE A 219 -106.913 109.088 -29.278 1.00 51.04 N ANISOU 702 N PHE A 219 8292 5310 5790 2799 3263 2353 N ATOM 703 CA PHE A 219 -106.731 107.805 -29.952 1.00 50.50 C ANISOU 703 CA PHE A 219 8133 5247 5808 2780 3276 2352 C ATOM 704 C PHE A 219 -107.825 107.666 -30.996 1.00 50.40 C ANISOU 704 C PHE A 219 8128 5209 5814 2763 3291 2336 C ATOM 705 O PHE A 219 -108.669 108.534 -31.081 1.00 50.74 O ANISOU 705 O PHE A 219 8245 5233 5802 2768 3288 2328 O ATOM 706 CB PHE A 219 -106.761 106.656 -28.932 1.00 50.09 C ANISOU 706 CB PHE A 219 8017 5253 5761 2796 3221 2362 C ATOM 707 CG PHE A 219 -108.118 106.392 -28.340 1.00 50.01 C ANISOU 707 CG PHE A 219 8029 5272 5702 2812 3167 2357 C ATOM 708 CD1 PHE A 219 -109.013 105.568 -28.982 1.00 49.66 C ANISOU 708 CD1 PHE A 219 7951 5228 5691 2796 3163 2346 C ATOM 709 CD2 PHE A 219 -108.480 106.950 -27.138 1.00 50.29 C ANISOU 709 CD2 PHE A 219 8116 5334 5658 2843 3120 2362 C ATOM 710 CE1 PHE A 219 -110.242 105.326 -28.456 1.00 49.61 C ANISOU 710 CE1 PHE A 219 7964 5244 5641 2809 3116 2341 C ATOM 711 CE2 PHE A 219 -109.715 106.706 -26.596 1.00 50.24 C ANISOU 711 CE2 PHE A 219 8128 5351 5608 2857 3071 2357 C ATOM 712 CZ PHE A 219 -110.599 105.894 -27.254 1.00 51.29 C ANISOU 712 CZ PHE A 219 8229 5481 5776 2839 3070 2346 C ATOM 713 N ASP A 220 -107.837 106.603 -31.789 1.00 49.96 N ANISOU 713 N ASP A 220 7999 5152 5832 2743 3305 2332 N ATOM 714 CA ASP A 220 -108.775 106.584 -32.908 1.00 49.93 C ANISOU 714 CA ASP A 220 8005 5118 5847 2725 3326 2318 C ATOM 715 C ASP A 220 -110.160 106.100 -32.506 1.00 51.92 C ANISOU 715 C ASP A 220 8264 5399 6063 2733 3276 2314 C ATOM 716 O ASP A 220 -110.512 104.936 -32.718 1.00 54.31 O ANISOU 716 O ASP A 220 8502 5723 6408 2722 3259 2312 O ATOM 717 CB ASP A 220 -108.235 105.813 -34.119 1.00 49.60 C ANISOU 717 CB ASP A 220 7891 5057 5900 2698 3368 2315 C ATOM 718 CG ASP A 220 -109.047 106.068 -35.384 1.00 49.69 C ANISOU 718 CG ASP A 220 7923 5028 5928 2680 3400 2301 C ATOM 719 OD1 ASP A 220 -110.165 106.605 -35.266 1.00 72.30 O ANISOU 719 OD1 ASP A 220 10847 7887 8734 2686 3382 2295 O ATOM 720 OD2 ASP A 220 -108.598 105.727 -36.495 1.00 49.55 O ANISOU 720 OD2 ASP A 220 7862 4985 5981 2659 3442 2297 O ATOM 721 N GLU A 221 -110.944 107.029 -31.952 1.00 50.13 N ANISOU 721 N GLU A 221 8120 5170 5758 2750 3253 2311 N ATOM 722 CA GLU A 221 -112.271 106.766 -31.403 1.00 50.06 C ANISOU 722 CA GLU A 221 8132 5186 5703 2761 3201 2307 C ATOM 723 C GLU A 221 -113.284 106.235 -32.429 1.00 49.84 C ANISOU 723 C GLU A 221 8086 5143 5707 2739 3211 2296 C ATOM 724 O GLU A 221 -114.136 105.405 -32.104 1.00 62.90 O ANISOU 724 O GLU A 221 9715 6825 7357 2740 3170 2294 O ATOM 725 CB GLU A 221 -112.803 108.021 -30.703 1.00 50.59 C ANISOU 725 CB GLU A 221 8294 5246 5679 2783 3180 2307 C ATOM 726 CG GLU A 221 -111.898 108.512 -29.566 1.00 67.63 C ANISOU 726 CG GLU A 221 10471 7426 7797 2807 3162 2319 C ATOM 727 CD GLU A 221 -112.616 109.438 -28.581 1.00 65.75 C ANISOU 727 CD GLU A 221 10316 7200 7465 2834 3119 2321 C ATOM 728 OE1 GLU A 221 -111.960 109.935 -27.633 1.00 57.49 O ANISOU 728 OE1 GLU A 221 9292 6173 6378 2855 3100 2331 O ATOM 729 OE2 GLU A 221 -113.832 109.666 -28.754 1.00 61.36 O ANISOU 729 OE2 GLU A 221 9801 6636 6877 2833 3102 2312 O ATOM 730 N ALA A 222 -113.179 106.698 -33.664 1.00 49.99 N ANISOU 730 N ALA A 222 8117 5116 5759 2719 3264 2289 N ATOM 731 CA ALA A 222 -114.039 106.213 -34.733 1.00 60.95 C ANISOU 731 CA ALA A 222 9486 6489 7184 2697 3277 2279 C ATOM 732 C ALA A 222 -113.601 104.830 -35.199 1.00 49.25 C ANISOU 732 C ALA A 222 7905 5025 5782 2679 3281 2281 C ATOM 733 O ALA A 222 -114.407 104.010 -35.612 1.00 58.74 O ANISOU 733 O ALA A 222 9074 6237 7006 2666 3266 2277 O ATOM 734 CB ALA A 222 -114.051 107.195 -35.901 1.00 68.97 C ANISOU 734 CB ALA A 222 10548 7449 8206 2682 3333 2271 C ATOM 735 N ALA A 223 -112.309 104.566 -35.128 1.00 49.13 N ANISOU 735 N ALA A 223 7843 5014 5810 2679 3301 2289 N ATOM 736 CA ALA A 223 -111.833 103.252 -35.489 1.00 48.63 C ANISOU 736 CA ALA A 223 7685 4971 5820 2663 3302 2291 C ATOM 737 C ALA A 223 -112.404 102.242 -34.517 1.00 49.72 C ANISOU 737 C ALA A 223 7790 5161 5940 2671 3243 2295 C ATOM 738 O ALA A 223 -112.934 101.202 -34.921 1.00 62.20 O ANISOU 738 O ALA A 223 9321 6757 7556 2654 3229 2292 O ATOM 739 CB ALA A 223 -110.321 103.208 -35.472 1.00 77.82 C ANISOU 739 CB ALA A 223 11342 8665 9562 2662 3331 2300 C ATOM 740 N MET A 224 -112.291 102.545 -33.228 1.00 48.41 N ANISOU 740 N MET A 224 7653 5022 5717 2696 3207 2302 N ATOM 741 CA MET A 224 -112.853 101.672 -32.213 1.00 48.12 C ANISOU 741 CA MET A 224 7593 5035 5658 2707 3149 2305 C ATOM 742 C MET A 224 -114.309 101.490 -32.497 1.00 48.08 C ANISOU 742 C MET A 224 7612 5027 5629 2699 3127 2295 C ATOM 743 O MET A 224 -114.794 100.371 -32.606 1.00 53.12 O ANISOU 743 O MET A 224 8200 5688 6296 2686 3106 2292 O ATOM 744 CB MET A 224 -112.726 102.276 -30.830 1.00 52.10 C ANISOU 744 CB MET A 224 8142 5561 6092 2738 3113 2312 C ATOM 745 CG MET A 224 -113.686 101.631 -29.850 1.00 73.31 C ANISOU 745 CG MET A 224 10826 8288 8738 2752 3053 2311 C ATOM 746 SD MET A 224 -113.277 102.013 -28.007 1.00105.94 S ANISOU 746 SD MET A 224 14988 12464 12801 2793 3002 2323 S ATOM 747 CE MET A 224 -113.410 103.959 -28.048 1.00 88.69 C ANISOU 747 CE MET A 224 12917 10236 10545 2811 3021 2322 C ATOM 748 N ALA A 225 -115.008 102.612 -32.597 1.00 48.50 N ANISOU 748 N ALA A 225 7747 5053 5630 2707 3132 2289 N ATOM 749 CA ALA A 225 -116.427 102.579 -32.872 1.00 61.51 C ANISOU 749 CA ALA A 225 9426 6694 7251 2700 3112 2280 C ATOM 750 C ALA A 225 -116.668 101.552 -33.967 1.00 58.79 C ANISOU 750 C ALA A 225 9018 6346 6975 2670 3129 2276 C ATOM 751 O ALA A 225 -117.261 100.497 -33.730 1.00 62.18 O ANISOU 751 O ALA A 225 9407 6803 7414 2663 3094 2274 O ATOM 752 CB ALA A 225 -116.919 103.955 -33.301 1.00 54.93 C ANISOU 752 CB ALA A 225 8679 5819 6372 2704 3135 2275 C ATOM 753 N LYS A 226 -116.161 101.858 -35.156 1.00 48.20 N ANISOU 753 N LYS A 226 7666 4967 5680 2653 3182 2273 N ATOM 754 CA LYS A 226 -116.424 101.051 -36.340 1.00 50.03 C ANISOU 754 CA LYS A 226 7845 5189 5975 2625 3202 2268 C ATOM 755 C LYS A 226 -116.204 99.563 -36.083 1.00 58.32 C ANISOU 755 C LYS A 226 8810 6280 7070 2615 3175 2272 C ATOM 756 O LYS A 226 -117.096 98.748 -36.330 1.00 57.80 O ANISOU 756 O LYS A 226 8721 6227 7014 2600 3152 2268 O ATOM 757 CB LYS A 226 -115.574 101.536 -37.513 1.00 48.04 C ANISOU 757 CB LYS A 226 7583 4896 5775 2613 3264 2267 C ATOM 758 CG LYS A 226 -115.936 100.927 -38.859 1.00 76.18 C ANISOU 758 CG LYS A 226 11105 8443 9399 2586 3288 2262 C ATOM 759 CD LYS A 226 -115.369 101.776 -39.998 1.00 90.41 C ANISOU 759 CD LYS A 226 12924 10195 11232 2578 3350 2259 C ATOM 760 CE LYS A 226 -115.580 101.136 -41.369 1.00 92.68 C ANISOU 760 CE LYS A 226 13162 10466 11586 2553 3376 2255 C ATOM 761 NZ LYS A 226 -114.592 100.055 -41.664 1.00 85.17 N ANISOU 761 NZ LYS A 226 12120 9532 10710 2542 3383 2260 N ATOM 762 N PHE A 227 -115.034 99.215 -35.553 1.00 47.21 N ANISOU 762 N PHE A 227 7359 4893 5687 2622 3177 2280 N ATOM 763 CA PHE A 227 -114.673 97.818 -35.385 1.00 46.72 C ANISOU 763 CA PHE A 227 7213 4866 5672 2610 3157 2285 C ATOM 764 C PHE A 227 -115.005 97.232 -34.017 1.00 46.55 C ANISOU 764 C PHE A 227 7186 4891 5610 2626 3101 2288 C ATOM 765 O PHE A 227 -114.764 96.057 -33.760 1.00 46.15 O ANISOU 765 O PHE A 227 7070 4873 5592 2617 3080 2292 O ATOM 766 CB PHE A 227 -113.195 97.644 -35.691 1.00 50.32 C ANISOU 766 CB PHE A 227 7615 5318 6187 2605 3191 2292 C ATOM 767 CG PHE A 227 -112.810 98.127 -37.054 1.00 57.02 C ANISOU 767 CG PHE A 227 8461 6120 7082 2590 3247 2288 C ATOM 768 CD1 PHE A 227 -113.074 97.356 -38.170 1.00 46.51 C ANISOU 768 CD1 PHE A 227 7081 4781 5809 2565 3261 2284 C ATOM 769 CD2 PHE A 227 -112.192 99.350 -37.218 1.00 59.13 C ANISOU 769 CD2 PHE A 227 8778 6352 7336 2601 3285 2288 C ATOM 770 CE1 PHE A 227 -112.734 97.795 -39.418 1.00 46.67 C ANISOU 770 CE1 PHE A 227 7099 4759 5873 2553 3311 2280 C ATOM 771 CE2 PHE A 227 -111.842 99.794 -38.470 1.00 66.22 C ANISOU 771 CE2 PHE A 227 9677 7207 8278 2587 3337 2284 C ATOM 772 CZ PHE A 227 -112.115 99.015 -39.574 1.00 70.56 C ANISOU 772 CZ PHE A 227 10174 7749 8886 2564 3350 2280 C ATOM 773 N LYS A 228 -115.560 98.048 -33.139 1.00 28.26 N ANISOU 773 N LYS A 228 3521 3547 3669 631 1594 1263 N ATOM 774 CA LYS A 228 -115.958 97.571 -31.821 1.00 36.50 C ANISOU 774 CA LYS A 228 4505 4557 4807 586 1590 1266 C ATOM 775 C LYS A 228 -114.828 96.811 -31.156 1.00 35.62 C ANISOU 775 C LYS A 228 4384 4435 4714 506 1559 1194 C ATOM 776 O LYS A 228 -115.015 95.686 -30.668 1.00 30.16 O ANISOU 776 O LYS A 228 3638 3709 4111 426 1542 1136 O ATOM 777 CB LYS A 228 -117.202 96.681 -31.914 1.00 50.08 C ANISOU 777 CB LYS A 228 6161 6234 6632 551 1594 1255 C ATOM 778 CG LYS A 228 -118.464 97.431 -32.333 1.00 61.52 C ANISOU 778 CG LYS A 228 7606 7688 8079 623 1630 1337 C ATOM 779 CD LYS A 228 -119.733 96.725 -31.864 1.00 79.98 C ANISOU 779 CD LYS A 228 9878 9978 10534 595 1636 1347 C ATOM 780 CE LYS A 228 -120.957 97.615 -32.047 1.00 91.08 C ANISOU 780 CE LYS A 228 11277 11390 11938 667 1675 1444 C ATOM 781 NZ LYS A 228 -120.838 98.894 -31.287 1.00 95.00 N ANISOU 781 NZ LYS A 228 11798 11915 12384 730 1696 1529 N ATOM 782 N THR A 229 -113.645 97.421 -31.150 1.00 35.41 N ANISOU 782 N THR A 229 4417 4442 4594 526 1549 1194 N ATOM 783 CA THR A 229 -112.535 96.849 -30.416 1.00 34.42 C ANISOU 783 CA THR A 229 4284 4311 4481 452 1523 1138 C ATOM 784 C THR A 229 -111.748 97.926 -29.711 1.00 30.76 C ANISOU 784 C THR A 229 3873 3876 3938 499 1525 1193 C ATOM 785 O THR A 229 -111.983 99.101 -29.930 1.00 45.26 O ANISOU 785 O THR A 229 5767 5741 5688 591 1538 1266 O ATOM 786 CB THR A 229 -111.604 96.054 -31.323 1.00 47.31 C ANISOU 786 CB THR A 229 5943 5951 6083 394 1492 1060 C ATOM 787 OG1 THR A 229 -110.659 95.348 -30.515 1.00 49.19 O ANISOU 787 OG1 THR A 229 6163 6180 6346 304 1467 1002 O ATOM 788 CG2 THR A 229 -110.870 96.978 -32.256 1.00 54.80 C ANISOU 788 CG2 THR A 229 6978 6935 6907 467 1494 1084 C ATOM 789 N ARG A 230 -110.806 97.511 -28.875 1.00 32.76 N ANISOU 789 N ARG A 230 4113 4124 4213 433 1508 1157 N ATOM 790 CA ARG A 230 -110.074 98.423 -28.000 1.00 25.76 C ANISOU 790 CA ARG A 230 3267 3255 3264 466 1503 1217 C ATOM 791 C ARG A 230 -108.673 98.755 -28.527 1.00 31.42 C ANISOU 791 C ARG A 230 4086 4002 3849 472 1454 1185 C ATOM 792 O ARG A 230 -108.001 97.909 -29.121 1.00 31.32 O ANISOU 792 O ARG A 230 4077 3986 3836 408 1452 1117 O ATOM 793 CB ARG A 230 -109.991 97.808 -26.600 1.00 24.51 C ANISOU 793 CB ARG A 230 3015 3063 3235 386 1510 1200 C ATOM 794 CG ARG A 230 -109.492 98.734 -25.531 1.00 30.03 C ANISOU 794 CG ARG A 230 3733 3759 3918 411 1399 1201 C ATOM 795 CD ARG A 230 -110.422 99.901 -25.325 1.00 25.98 C ANISOU 795 CD ARG A 230 3243 3250 3380 510 1388 1301 C ATOM 796 NE ARG A 230 -110.096 100.591 -24.080 1.00 43.25 N ANISOU 796 NE ARG A 230 5417 5419 5596 516 1277 1303 N ATOM 797 CZ ARG A 230 -110.565 100.269 -22.866 1.00 39.08 C ANISOU 797 CZ ARG A 230 4778 4847 5223 480 1274 1305 C ATOM 798 NH1 ARG A 230 -111.403 99.254 -22.687 1.00 26.51 N ANISOU 798 NH1 ARG A 230 3080 3222 3770 433 1379 1301 N ATOM 799 NH2 ARG A 230 -110.174 100.972 -21.815 1.00 46.99 N ANISOU 799 NH2 ARG A 230 5774 5834 6247 489 1162 1308 N ATOM 800 N GLN A 231 -108.240 99.989 -28.302 1.00 26.46 N ANISOU 800 N GLN A 231 3543 3393 3119 542 1363 1200 N ATOM 801 CA GLN A 231 -106.953 100.436 -28.782 1.00 25.16 C ANISOU 801 CA GLN A 231 3481 3247 2830 555 1274 1144 C ATOM 802 C GLN A 231 -105.961 100.425 -27.655 1.00 43.11 C ANISOU 802 C GLN A 231 5746 5503 5130 492 1157 1084 C ATOM 803 O GLN A 231 -106.247 100.902 -26.562 1.00 37.81 O ANISOU 803 O GLN A 231 5040 4819 4506 499 1111 1112 O ATOM 804 CB GLN A 231 -107.016 101.842 -29.365 1.00 34.39 C ANISOU 804 CB GLN A 231 4767 4450 3850 672 1245 1191 C ATOM 805 CG GLN A 231 -105.720 102.238 -30.061 1.00 32.17 C ANISOU 805 CG GLN A 231 4598 4183 3441 691 1167 1126 C ATOM 806 CD GLN A 231 -105.825 103.564 -30.779 1.00 54.65 C ANISOU 806 CD GLN A 231 7565 7064 6134 806 1160 1163 C ATOM 807 OE1 GLN A 231 -106.692 103.754 -31.630 1.00 61.37 O ANISOU 807 OE1 GLN A 231 8423 7938 6957 867 1264 1218 O ATOM 808 NE2 GLN A 231 -104.939 104.497 -30.432 1.00 73.92 N ANISOU 808 NE2 GLN A 231 10104 9510 8472 833 1038 1134 N ATOM 809 N PHE A 232 -104.784 99.883 -27.944 1.00 29.68 N ANISOU 809 N PHE A 232 4075 3800 3401 429 1107 1006 N ATOM 810 CA PHE A 232 -103.764 99.692 -26.945 1.00 24.60 C ANISOU 810 CA PHE A 232 3415 3141 2789 350 1005 943 C ATOM 811 C PHE A 232 -102.467 100.311 -27.420 1.00 44.25 C ANISOU 811 C PHE A 232 6023 5641 5148 371 892 898 C ATOM 812 O PHE A 232 -102.222 100.463 -28.615 1.00 47.49 O ANISOU 812 O PHE A 232 6511 6065 5468 416 909 891 O ATOM 813 CB PHE A 232 -103.526 98.198 -26.696 1.00 23.82 C ANISOU 813 CB PHE A 232 3227 3023 2802 221 1052 884 C ATOM 814 CG PHE A 232 -104.657 97.485 -25.986 1.00 23.70 C ANISOU 814 CG PHE A 232 3087 2987 2933 182 1151 910 C ATOM 815 CD1 PHE A 232 -104.679 97.398 -24.611 1.00 25.14 C ANISOU 815 CD1 PHE A 232 3187 3148 3216 136 1121 894 C ATOM 816 CD2 PHE A 232 -105.665 96.874 -26.700 1.00 30.65 C ANISOU 816 CD2 PHE A 232 3928 3864 3855 190 1272 945 C ATOM 817 CE1 PHE A 232 -105.694 96.728 -23.954 1.00 23.93 C ANISOU 817 CE1 PHE A 232 2918 2970 3204 102 1213 908 C ATOM 818 CE2 PHE A 232 -106.694 96.212 -26.050 1.00 29.98 C ANISOU 818 CE2 PHE A 232 3732 3753 3904 153 1359 964 C ATOM 819 CZ PHE A 232 -106.697 96.135 -24.671 1.00 29.75 C ANISOU 819 CZ PHE A 232 3625 3702 3976 110 1330 942 C ATOM 820 N ARG A 233 -101.628 100.652 -26.460 1.00 47.75 N ANISOU 820 N ARG A 233 6476 6076 5591 335 776 864 N ATOM 821 CA ARG A 233 -100.305 101.112 -26.753 1.00 25.19 C ANISOU 821 CA ARG A 233 3723 3221 2628 333 657 812 C ATOM 822 C ARG A 233 -99.303 100.141 -26.166 1.00 33.55 C ANISOU 822 C ARG A 233 4732 4261 3755 203 606 741 C ATOM 823 O ARG A 233 -99.367 99.815 -24.986 1.00 52.03 O ANISOU 823 O ARG A 233 6983 6590 6198 137 594 733 O ATOM 824 CB ARG A 233 -100.109 102.525 -26.210 1.00 31.78 C ANISOU 824 CB ARG A 233 4634 4061 3380 409 547 841 C ATOM 825 CG ARG A 233 -100.382 103.587 -27.273 1.00 56.17 C ANISOU 825 CG ARG A 233 7844 7173 6323 531 559 876 C ATOM 826 CD ARG A 233 -100.984 104.895 -26.735 1.00 52.83 C ANISOU 826 CD ARG A 233 7468 6761 5845 616 514 944 C ATOM 827 NE ARG A 233 -101.764 105.545 -27.793 1.00 41.85 N ANISOU 827 NE ARG A 233 6149 5399 4353 720 598 994 N ATOM 828 CZ ARG A 233 -102.497 106.644 -27.651 1.00 34.77 C ANISOU 828 CZ ARG A 233 5305 4519 3387 801 593 1065 C ATOM 829 NH1 ARG A 233 -102.574 107.277 -26.483 1.00 43.23 N ANISOU 829 NH1 ARG A 233 6366 5577 4481 796 497 1100 N ATOM 830 NH2 ARG A 233 -103.162 107.108 -28.689 1.00 29.25 N ANISOU 830 NH2 ARG A 233 4666 3849 2598 884 685 1104 N ATOM 831 N ILE A 234 -98.382 99.664 -26.994 1.00 29.44 N ANISOU 831 N ILE A 234 4268 3737 3182 162 578 689 N ATOM 832 CA ILE A 234 -97.301 98.813 -26.527 1.00 23.93 C ANISOU 832 CA ILE A 234 3542 3023 2525 33 516 623 C ATOM 833 C ILE A 234 -95.976 99.503 -26.786 1.00 29.49 C ANISOU 833 C ILE A 234 4363 3722 3121 45 372 584 C ATOM 834 O ILE A 234 -95.776 100.058 -27.862 1.00 39.80 O ANISOU 834 O ILE A 234 5768 5030 4324 127 356 584 O ATOM 835 CB ILE A 234 -97.318 97.474 -27.272 1.00 23.16 C ANISOU 835 CB ILE A 234 3409 2920 2472 -50 599 596 C ATOM 836 CG1 ILE A 234 -96.250 96.537 -26.737 1.00 22.84 C ANISOU 836 CG1 ILE A 234 3340 2866 2473 -197 542 533 C ATOM 837 CG2 ILE A 234 -97.115 97.689 -28.741 1.00 23.09 C ANISOU 837 CG2 ILE A 234 3493 2911 2369 18 602 598 C ATOM 838 CD1 ILE A 234 -96.512 95.129 -27.148 1.00 29.56 C ANISOU 838 CD1 ILE A 234 4132 3710 3388 -297 636 515 C ATOM 839 N GLN A 235 -95.070 99.478 -25.812 1.00 31.17 N ANISOU 839 N GLN A 235 4560 3924 3358 -34 269 547 N ATOM 840 CA GLN A 235 -93.716 99.944 -26.072 1.00 24.70 C ANISOU 840 CA GLN A 235 3848 3093 2446 -44 128 504 C ATOM 841 C GLN A 235 -92.650 98.970 -25.622 1.00 24.36 C ANISOU 841 C GLN A 235 3769 3035 2452 -193 72 448 C ATOM 842 O GLN A 235 -92.710 98.443 -24.525 1.00 56.99 O ANISOU 842 O GLN A 235 7801 7170 6683 -282 87 440 O ATOM 843 CB GLN A 235 -93.495 101.327 -25.458 1.00 42.07 C ANISOU 843 CB GLN A 235 6109 5292 4582 32 15 524 C ATOM 844 CG GLN A 235 -93.212 101.353 -23.983 1.00 28.40 C ANISOU 844 CG GLN A 235 4301 3556 2935 -40 -53 521 C ATOM 845 CD GLN A 235 -92.803 102.732 -23.517 1.00 38.31 C ANISOU 845 CD GLN A 235 5637 4805 4113 28 -191 538 C ATOM 846 OE1 GLN A 235 -92.633 103.645 -24.323 1.00 60.81 O ANISOU 846 OE1 GLN A 235 8614 7656 6835 123 -238 543 O ATOM 847 NE2 GLN A 235 -92.647 102.896 -22.211 1.00 51.21 N ANISOU 847 NE2 GLN A 235 7199 6432 5828 -21 -257 546 N ATOM 848 N LEU A 236 -91.675 98.727 -26.478 1.00 32.81 N ANISOU 848 N LEU A 236 4920 4088 3457 -223 8 409 N ATOM 849 CA LEU A 236 -90.533 97.875 -26.122 1.00 29.28 C ANISOU 849 CA LEU A 236 4458 3627 3039 -370 -63 359 C ATOM 850 C LEU A 236 -89.524 98.610 -25.254 1.00 24.58 C ANISOU 850 C LEU A 236 3900 3022 2416 -394 -214 339 C ATOM 851 O LEU A 236 -89.353 99.812 -25.383 1.00 49.62 O ANISOU 851 O LEU A 236 7159 6189 5506 -290 -296 351 O ATOM 852 CB LEU A 236 -89.840 97.343 -27.373 1.00 23.63 C ANISOU 852 CB LEU A 236 3819 2890 2271 -397 -89 331 C ATOM 853 CG LEU A 236 -90.711 96.613 -28.397 1.00 23.09 C ANISOU 853 CG LEU A 236 3723 2823 2225 -376 42 351 C ATOM 854 CD1 LEU A 236 -89.841 95.719 -29.245 1.00 54.15 C ANISOU 854 CD1 LEU A 236 7697 6730 6148 -465 -1 319 C ATOM 855 CD2 LEU A 236 -91.767 95.795 -27.729 1.00 27.78 C ANISOU 855 CD2 LEU A 236 4192 3438 2925 -432 175 372 C ATOM 856 N ILE A 237 -88.858 97.885 -24.372 1.00 24.51 N ANISOU 856 N ILE A 237 3827 3012 2474 -533 -249 310 N ATOM 857 CA ILE A 237 -87.915 98.487 -23.444 1.00 25.12 C ANISOU 857 CA ILE A 237 3919 3080 2544 -571 -389 294 C ATOM 858 C ILE A 237 -86.727 97.572 -23.263 1.00 24.95 C ANISOU 858 C ILE A 237 3892 3048 2541 -730 -452 249 C ATOM 859 O ILE A 237 -86.797 96.396 -23.592 1.00 35.81 O ANISOU 859 O ILE A 237 5226 4427 3952 -823 -370 233 O ATOM 860 CB ILE A 237 -88.533 98.708 -22.049 1.00 25.48 C ANISOU 860 CB ILE A 237 3850 3142 2691 -579 -358 318 C ATOM 861 CG1 ILE A 237 -88.978 97.379 -21.442 1.00 25.03 C ANISOU 861 CG1 ILE A 237 3654 3099 2756 -699 -230 301 C ATOM 862 CG2 ILE A 237 -89.707 99.673 -22.119 1.00 48.87 C ANISOU 862 CG2 ILE A 237 6819 6112 5637 -429 -310 371 C ATOM 863 CD1 ILE A 237 -89.552 97.513 -20.070 1.00 25.45 C ANISOU 863 CD1 ILE A 237 3583 3161 2926 -710 -196 317 C ATOM 864 N GLU A 238 -85.639 98.115 -22.729 1.00 26.29 N ANISOU 864 N GLU A 238 4104 3202 2681 -767 -601 232 N ATOM 865 CA GLU A 238 -84.450 97.328 -22.402 1.00 31.57 C ANISOU 865 CA GLU A 238 4765 3862 3370 -927 -673 194 C ATOM 866 C GLU A 238 -83.885 97.730 -21.043 1.00 26.16 C ANISOU 866 C GLU A 238 4024 3179 2736 -987 -763 191 C ATOM 867 O GLU A 238 -84.051 98.851 -20.611 1.00 32.29 O ANISOU 867 O GLU A 238 4819 3951 3497 -892 -829 214 O ATOM 868 CB GLU A 238 -83.371 97.491 -23.469 1.00 39.71 C ANISOU 868 CB GLU A 238 5933 4856 4297 -926 -795 172 C ATOM 869 CG GLU A 238 -83.390 96.423 -24.559 1.00 78.19 C ANISOU 869 CG GLU A 238 10826 9721 9160 -977 -727 160 C ATOM 870 CD GLU A 238 -82.347 96.669 -25.651 1.00107.21 C ANISOU 870 CD GLU A 238 14637 13351 12746 -960 -856 139 C ATOM 871 OE1 GLU A 238 -81.683 97.738 -25.637 1.00 99.69 O ANISOU 871 OE1 GLU A 238 13773 12375 11730 -894 -988 131 O ATOM 872 OE2 GLU A 238 -82.193 95.785 -26.527 1.00118.98 O ANISOU 872 OE2 GLU A 238 16147 14826 14234 -1014 -827 131 O ATOM 873 N LYS A 239 -83.215 96.806 -20.372 1.00 26.16 N ANISOU 873 N LYS A 239 3955 3186 2797 -1150 -767 164 N ATOM 874 CA LYS A 239 -82.400 97.153 -19.217 1.00 65.32 C ANISOU 874 CA LYS A 239 8875 8144 7799 -1223 -876 157 C ATOM 875 C LYS A 239 -81.015 97.573 -19.729 1.00 90.30 C ANISOU 875 C LYS A 239 12170 11274 10866 -1250 -1056 141 C ATOM 876 O LYS A 239 -80.655 97.259 -20.866 1.00 94.72 O ANISOU 876 O LYS A 239 12825 11814 11350 -1250 -1074 128 O ATOM 877 CB LYS A 239 -82.286 95.956 -18.271 1.00 52.34 C ANISOU 877 CB LYS A 239 7097 6527 6264 -1391 -789 132 C ATOM 878 CG LYS A 239 -83.596 95.491 -17.677 1.00 31.05 C ANISOU 878 CG LYS A 239 4264 3857 3674 -1373 -613 139 C ATOM 879 CD LYS A 239 -83.384 94.262 -16.816 1.00 30.65 C ANISOU 879 CD LYS A 239 4094 3832 3721 -1547 -523 102 C ATOM 880 CE LYS A 239 -84.709 93.614 -16.464 1.00 27.00 C ANISOU 880 CE LYS A 239 3512 3390 3356 -1533 -334 98 C ATOM 881 NZ LYS A 239 -84.617 92.594 -15.401 1.00 26.64 N ANISOU 881 NZ LYS A 239 3334 3369 3420 -1686 -237 57 N ATOM 882 N PRO A 240 -80.208 98.244 -18.883 1.00 97.21 N ANISOU 882 N PRO A 240 13047 12137 11752 -1281 -1194 142 N ATOM 883 CA PRO A 240 -80.427 98.473 -17.453 1.00 72.73 C ANISOU 883 CA PRO A 240 9819 9055 8760 -1312 -1188 155 C ATOM 884 C PRO A 240 -81.488 99.518 -17.145 1.00 54.41 C ANISOU 884 C PRO A 240 7479 6737 6457 -1157 -1167 194 C ATOM 885 O PRO A 240 -81.538 100.573 -17.773 1.00 49.82 O ANISOU 885 O PRO A 240 7017 6136 5778 -1029 -1249 212 O ATOM 886 CB PRO A 240 -79.062 98.976 -16.960 1.00 62.59 C ANISOU 886 CB PRO A 240 8582 7746 7455 -1384 -1378 148 C ATOM 887 CG PRO A 240 -78.103 98.719 -18.072 1.00 80.59 C ANISOU 887 CG PRO A 240 10997 9997 9628 -1422 -1462 125 C ATOM 888 CD PRO A 240 -78.920 98.808 -19.315 1.00 93.68 C ANISOU 888 CD PRO A 240 12730 11650 11213 -1294 -1380 129 C ATOM 889 N GLU A 241 -82.331 99.187 -16.174 1.00 66.70 N ANISOU 889 N GLU A 241 8886 8318 8140 -1174 -1055 206 N ATOM 890 CA GLU A 241 -83.163 100.151 -15.479 1.00 78.62 C ANISOU 890 CA GLU A 241 10345 9824 9701 -1063 -1062 248 C ATOM 891 C GLU A 241 -82.346 100.610 -14.275 1.00 91.81 C ANISOU 891 C GLU A 241 11960 11483 11440 -1130 -1196 253 C ATOM 892 O GLU A 241 -82.900 101.041 -13.266 1.00 74.89 O ANISOU 892 O GLU A 241 9713 9340 9402 -1099 -1192 282 O ATOM 893 CB GLU A 241 -84.467 99.492 -15.013 1.00 97.87 C ANISOU 893 CB GLU A 241 12641 12287 12260 -1054 -876 257 C ATOM 894 CG GLU A 241 -84.275 98.395 -13.950 1.00101.65 C ANISOU 894 CG GLU A 241 12960 12783 12880 -1207 -793 223 C ATOM 895 CD GLU A 241 -85.387 97.345 -13.938 1.00 79.37 C ANISOU 895 CD GLU A 241 10033 9983 10142 -1226 -587 208 C ATOM 896 OE1 GLU A 241 -86.037 97.128 -14.985 1.00 46.89 O ANISOU 896 OE1 GLU A 241 5985 5872 5959 -1162 -507 215 O ATOM 897 OE2 GLU A 241 -85.601 96.726 -12.872 1.00 82.96 O ANISOU 897 OE2 GLU A 241 10337 10448 10735 -1308 -503 186 O ATOM 898 N SER A 245 -85.112 104.203 -14.361 1.00 73.75 N ANISOU 898 N SER A 245 9799 9166 9058 -657 -1278 416 N ATOM 899 CA SER A 245 -86.038 103.686 -15.372 1.00 62.94 C ANISOU 899 CA SER A 245 8453 7816 7645 -597 -1116 414 C ATOM 900 C SER A 245 -85.385 102.859 -16.494 1.00 54.72 C ANISOU 900 C SER A 245 7491 6782 6518 -653 -1079 362 C ATOM 901 O SER A 245 -84.239 103.092 -16.874 1.00 49.14 O ANISOU 901 O SER A 245 6888 6058 5725 -687 -1205 334 O ATOM 902 CB SER A 245 -86.846 104.832 -15.987 1.00 74.95 C ANISOU 902 CB SER A 245 10082 9334 9061 -439 -1132 463 C ATOM 903 OG SER A 245 -87.761 104.344 -16.954 1.00 84.63 O ANISOU 903 OG SER A 245 11322 10580 10253 -382 -975 465 O ATOM 904 N PRO A 246 -86.129 101.886 -17.027 1.00 54.37 N ANISOU 904 N PRO A 246 7398 6758 6504 -663 -910 350 N ATOM 905 CA PRO A 246 -85.697 101.162 -18.221 1.00 39.20 C ANISOU 905 CA PRO A 246 5556 4838 4499 -697 -871 313 C ATOM 906 C PRO A 246 -85.512 102.108 -19.390 1.00 41.49 C ANISOU 906 C PRO A 246 6018 5114 4633 -577 -946 319 C ATOM 907 O PRO A 246 -86.011 103.236 -19.384 1.00 52.46 O ANISOU 907 O PRO A 246 7461 6499 5971 -458 -987 357 O ATOM 908 CB PRO A 246 -86.891 100.259 -18.536 1.00 43.58 C ANISOU 908 CB PRO A 246 6027 5415 5115 -688 -676 319 C ATOM 909 CG PRO A 246 -87.583 100.077 -17.242 1.00 68.69 C ANISOU 909 CG PRO A 246 9051 8604 8444 -716 -612 337 C ATOM 910 CD PRO A 246 -87.386 101.355 -16.476 1.00 71.35 C ANISOU 910 CD PRO A 246 9406 8925 8779 -654 -753 372 C ATOM 911 N VAL A 247 -84.836 101.611 -20.414 1.00 34.97 N ANISOU 911 N VAL A 247 5275 4278 3734 -611 -958 282 N ATOM 912 CA VAL A 247 -84.618 102.340 -21.641 1.00 28.01 C ANISOU 912 CA VAL A 247 4550 3379 2714 -504 -1011 275 C ATOM 913 C VAL A 247 -85.646 101.927 -22.683 1.00 37.44 C ANISOU 913 C VAL A 247 5746 4589 3891 -431 -855 287 C ATOM 914 O VAL A 247 -85.956 100.753 -22.816 1.00 51.12 O ANISOU 914 O VAL A 247 7397 6334 5693 -508 -741 278 O ATOM 915 CB VAL A 247 -83.209 102.068 -22.159 1.00 41.75 C ANISOU 915 CB VAL A 247 6379 5088 4396 -582 -1130 228 C ATOM 916 CG1 VAL A 247 -83.091 102.410 -23.635 1.00 42.07 C ANISOU 916 CG1 VAL A 247 6557 5108 4320 -484 -1138 210 C ATOM 917 CG2 VAL A 247 -82.213 102.850 -21.329 1.00 45.94 C ANISOU 917 CG2 VAL A 247 6946 5596 4912 -616 -1309 223 C ATOM 918 N ILE A 248 -86.178 102.908 -23.407 1.00 46.57 N ANISOU 918 N ILE A 248 6997 5746 4953 -286 -849 308 N ATOM 919 CA ILE A 248 -87.200 102.697 -24.434 1.00 27.17 C ANISOU 919 CA ILE A 248 4547 3304 2473 -201 -705 326 C ATOM 920 C ILE A 248 -86.589 102.478 -25.807 1.00 28.37 C ANISOU 920 C ILE A 248 4801 3434 2544 -181 -720 288 C ATOM 921 O ILE A 248 -85.834 103.318 -26.305 1.00 68.74 O ANISOU 921 O ILE A 248 10042 8521 7554 -124 -834 263 O ATOM 922 CB ILE A 248 -88.141 103.924 -24.536 1.00 60.40 C ANISOU 922 CB ILE A 248 8807 7528 6616 -51 -682 373 C ATOM 923 CG1 ILE A 248 -89.006 104.050 -23.276 1.00 63.13 C ANISOU 923 CG1 ILE A 248 9035 7892 7061 -60 -645 423 C ATOM 924 CG2 ILE A 248 -89.004 103.846 -25.793 1.00 56.45 C ANISOU 924 CG2 ILE A 248 8339 7040 6068 44 -551 387 C ATOM 925 CD1 ILE A 248 -89.819 105.331 -23.205 1.00 60.08 C ANISOU 925 CD1 ILE A 248 8704 7515 6607 71 -654 476 C ATOM 926 N VAL A 249 -86.918 101.349 -26.420 1.00 34.56 N ANISOU 926 N VAL A 249 4683 4861 3585 510 -280 -1027 N ATOM 927 CA VAL A 249 -86.537 101.103 -27.800 1.00 23.85 C ANISOU 927 CA VAL A 249 3319 3459 2283 506 -192 -1074 C ATOM 928 C VAL A 249 -87.519 101.782 -28.727 1.00 32.52 C ANISOU 928 C VAL A 249 4492 4639 3226 520 -76 -1067 C ATOM 929 O VAL A 249 -88.671 101.379 -28.806 1.00 49.90 O ANISOU 929 O VAL A 249 6707 6851 5404 522 -40 -963 O ATOM 930 CB VAL A 249 -86.600 99.640 -28.123 1.00 29.82 C ANISOU 930 CB VAL A 249 4013 4097 3221 485 -194 -992 C ATOM 931 CG1 VAL A 249 -86.326 99.442 -29.613 1.00 30.57 C ANISOU 931 CG1 VAL A 249 4106 4146 3364 478 -92 -1030 C ATOM 932 CG2 VAL A 249 -85.638 98.865 -27.230 1.00 48.37 C ANISOU 932 CG2 VAL A 249 6274 6375 5727 475 -298 -977 C ATOM 933 N LYS A 250 -87.077 102.821 -29.420 1.00 49.67 N ANISOU 933 N LYS A 250 6709 6871 5292 534 -8 -1172 N ATOM 934 CA LYS A 250 -87.955 103.513 -30.343 1.00 61.16 C ANISOU 934 CA LYS A 250 8229 8408 6600 554 122 -1162 C ATOM 935 C LYS A 250 -88.268 102.610 -31.528 1.00 52.24 C ANISOU 935 C LYS A 250 7067 7190 5594 564 227 -1121 C ATOM 936 O LYS A 250 -87.493 101.707 -31.867 1.00 40.28 O ANISOU 936 O LYS A 250 5502 5543 4261 540 213 -1132 O ATOM 937 CB LYS A 250 -87.333 104.830 -30.811 1.00 67.87 C ANISOU 937 CB LYS A 250 9136 9336 7314 568 175 -1294 C ATOM 938 CG LYS A 250 -87.481 105.980 -29.831 1.00 78.94 C ANISOU 938 CG LYS A 250 10590 10875 8527 569 103 -1317 C ATOM 939 CD LYS A 250 -86.893 107.270 -30.401 1.00 93.28 C ANISOU 939 CD LYS A 250 12472 12770 10201 581 167 -1453 C ATOM 940 CE LYS A 250 -87.228 108.488 -29.541 1.00 99.88 C ANISOU 940 CE LYS A 250 13371 13760 10820 579 108 -1462 C ATOM 941 NZ LYS A 250 -86.668 108.392 -28.161 1.00100.97 N ANISOU 941 NZ LYS A 250 13471 13886 11006 562 -48 -1469 N ATOM 942 N THR A 251 -89.419 102.836 -32.143 1.00 45.67 N ANISOU 942 N THR A 251 6241 6459 4655 622 318 -1069 N ATOM 943 CA THR A 251 -89.720 102.146 -33.379 1.00 40.16 C ANISOU 943 CA THR A 251 5505 5687 4068 640 441 -1038 C ATOM 944 C THR A 251 -88.817 102.691 -34.478 1.00 56.91 C ANISOU 944 C THR A 251 7654 7753 6216 631 553 -1149 C ATOM 945 O THR A 251 -88.146 103.703 -34.293 1.00 42.38 O ANISOU 945 O THR A 251 5870 5961 4271 624 541 -1248 O ATOM 946 CB THR A 251 -91.137 102.375 -33.811 1.00 30.05 C ANISOU 946 CB THR A 251 4219 4536 2664 707 530 -934 C ATOM 947 OG1 THR A 251 -91.367 101.620 -35.001 1.00 56.60 O ANISOU 947 OG1 THR A 251 7525 7806 6173 716 650 -898 O ATOM 948 CG2 THR A 251 -91.345 103.830 -34.138 1.00 28.13 C ANISOU 948 CG2 THR A 251 4036 4447 2205 736 609 -984 C ATOM 949 N ALA A 252 -88.811 102.019 -35.625 1.00 62.33 N ANISOU 949 N ALA A 252 8304 8332 7047 637 664 -1126 N ATOM 950 CA ALA A 252 -88.019 102.466 -36.766 1.00 41.36 C ANISOU 950 CA ALA A 252 5680 5607 4426 650 784 -1206 C ATOM 951 C ALA A 252 -88.313 103.935 -37.074 1.00 46.69 C ANISOU 951 C ALA A 252 6417 6437 4886 684 876 -1288 C ATOM 952 O ALA A 252 -87.423 104.777 -36.984 1.00 78.23 O ANISOU 952 O ALA A 252 10474 10443 8809 680 861 -1395 O ATOM 953 CB ALA A 252 -88.296 101.592 -37.974 1.00 37.16 C ANISOU 953 CB ALA A 252 5098 4958 4063 670 907 -1131 C ATOM 954 N ASP A 253 -89.562 104.243 -37.414 1.00 42.73 N ANISOU 954 N ASP A 253 5896 6064 4277 718 964 -1225 N ATOM 955 CA ASP A 253 -89.985 105.618 -37.682 1.00 45.96 C ANISOU 955 CA ASP A 253 6365 6637 4459 748 1050 -1271 C ATOM 956 C ASP A 253 -89.745 106.552 -36.496 1.00 45.94 C ANISOU 956 C ASP A 253 6434 6754 4266 738 922 -1320 C ATOM 957 O ASP A 253 -90.193 107.695 -36.512 1.00 53.30 O ANISOU 957 O ASP A 253 7423 7840 4987 759 968 -1338 O ATOM 958 CB ASP A 253 -91.480 105.673 -38.023 1.00 86.94 C ANISOU 958 CB ASP A 253 11514 11962 9558 789 1130 -1137 C ATOM 959 CG ASP A 253 -91.845 104.833 -39.234 1.00114.25 C ANISOU 959 CG ASP A 253 14878 15326 13206 793 1258 -1083 C ATOM 960 OD1 ASP A 253 -90.952 104.554 -40.066 1.00121.69 O ANISOU 960 OD1 ASP A 253 15806 16115 14315 767 1337 -1174 O ATOM 961 OD2 ASP A 253 -93.033 104.461 -39.357 1.00117.46 O ANISOU 961 OD2 ASP A 253 15228 15802 13600 829 1278 -930 O ATOM 962 N GLN A 254 -89.092 106.053 -35.451 1.00 48.86 N ANISOU 962 N GLN A 254 6795 7054 4716 701 762 -1330 N ATOM 963 CA GLN A 254 -88.676 106.901 -34.338 1.00 50.26 C ANISOU 963 CA GLN A 254 7027 7315 4755 679 641 -1386 C ATOM 964 C GLN A 254 -89.794 107.404 -33.422 1.00 52.50 C ANISOU 964 C GLN A 254 7326 7772 4849 701 572 -1287 C ATOM 965 O GLN A 254 -89.719 108.517 -32.920 1.00 56.94 O ANISOU 965 O GLN A 254 7952 8450 5232 697 537 -1334 O ATOM 966 CB GLN A 254 -87.890 108.090 -34.874 1.00 56.76 C ANISOU 966 CB GLN A 254 7927 8167 5472 680 715 -1529 C ATOM 967 CG GLN A 254 -86.530 107.706 -35.340 1.00 51.16 C ANISOU 967 CG GLN A 254 7210 7291 4939 661 721 -1621 C ATOM 968 CD GLN A 254 -85.672 107.291 -34.180 1.00 70.50 C ANISOU 968 CD GLN A 254 9608 9704 7474 634 537 -1649 C ATOM 969 OE1 GLN A 254 -84.974 106.273 -34.228 1.00 79.48 O ANISOU 969 OE1 GLN A 254 10671 10717 8813 623 485 -1642 O ATOM 970 NE2 GLN A 254 -85.715 108.083 -33.115 1.00 71.64 N ANISOU 970 NE2 GLN A 254 9787 9962 7470 621 439 -1672 N ATOM 971 N GLN A 255 -90.815 106.585 -33.198 1.00 61.02 N ANISOU 971 N GLN A 255 8352 8864 5968 727 553 -1140 N ATOM 972 CA GLN A 255 -91.852 106.888 -32.214 1.00 53.20 C ANISOU 972 CA GLN A 255 7372 8010 4833 750 473 -1011 C ATOM 973 C GLN A 255 -91.551 106.155 -30.921 1.00 36.48 C ANISOU 973 C GLN A 255 5224 5814 2822 716 309 -979 C ATOM 974 O GLN A 255 -90.832 105.155 -30.923 1.00 42.83 O ANISOU 974 O GLN A 255 5984 6462 3827 684 272 -1015 O ATOM 975 CB GLN A 255 -93.231 106.465 -32.721 1.00 76.08 C ANISOU 975 CB GLN A 255 10232 10965 7711 804 559 -839 C ATOM 976 CG GLN A 255 -93.934 107.486 -33.593 1.00 98.81 C ANISOU 976 CG GLN A 255 13145 13981 10416 840 701 -810 C ATOM 977 CD GLN A 255 -95.370 107.093 -33.879 1.00114.77 C ANISOU 977 CD GLN A 255 15123 16056 12427 890 767 -599 C ATOM 978 OE1 GLN A 255 -95.768 105.947 -33.654 1.00117.32 O ANISOU 978 OE1 GLN A 255 15388 16292 12895 900 729 -488 O ATOM 979 NE2 GLN A 255 -96.157 108.042 -34.370 1.00115.47 N ANISOU 979 NE2 GLN A 255 15242 16281 12351 918 867 -533 N ATOM 980 N ASP A 256 -92.107 106.639 -29.814 1.00 31.24 N ANISOU 980 N ASP A 256 4582 5252 2037 717 214 -901 N ATOM 981 CA ASP A 256 -91.830 106.041 -28.513 1.00 27.29 C ANISOU 981 CA ASP A 256 4054 4676 1640 679 67 -870 C ATOM 982 C ASP A 256 -92.675 104.795 -28.263 1.00 46.51 C ANISOU 982 C ASP A 256 6431 7047 4193 700 45 -723 C ATOM 983 O ASP A 256 -92.375 103.971 -27.385 1.00 33.72 O ANISOU 983 O ASP A 256 4778 5320 2714 666 -55 -704 O ATOM 984 CB ASP A 256 -92.038 107.047 -27.390 1.00 28.70 C ANISOU 984 CB ASP A 256 4276 4966 1660 662 -23 -845 C ATOM 985 CG ASP A 256 -90.987 108.128 -27.376 1.00 95.78 C ANISOU 985 CG ASP A 256 12830 13493 10070 628 -34 -1001 C ATOM 986 OD1 ASP A 256 -89.954 107.962 -28.060 1.00101.16 O ANISOU 986 OD1 ASP A 256 13508 14077 10850 610 11 -1127 O ATOM 987 OD2 ASP A 256 -91.186 109.141 -26.672 1.00 97.80 O ANISOU 987 OD2 ASP A 256 13135 13864 10162 618 -88 -990 O ATOM 988 N TYR A 257 -93.737 104.648 -29.038 1.00 37.53 N ANISOU 988 N TYR A 257 5284 5971 3007 755 147 -610 N ATOM 989 CA TYR A 257 -94.602 103.511 -28.833 1.00 24.30 C ANISOU 989 CA TYR A 257 3560 4237 1435 778 136 -455 C ATOM 990 C TYR A 257 -95.435 103.209 -30.075 1.00 24.90 C ANISOU 990 C TYR A 257 3614 4333 1516 831 284 -357 C ATOM 991 O TYR A 257 -95.521 104.015 -30.996 1.00 34.33 O ANISOU 991 O TYR A 257 4829 5608 2607 853 395 -392 O ATOM 992 CB TYR A 257 -95.487 103.763 -27.616 1.00 34.21 C ANISOU 992 CB TYR A 257 4820 5559 2619 772 51 -311 C ATOM 993 CG TYR A 257 -96.439 104.904 -27.815 1.00 26.06 C ANISOU 993 CG TYR A 257 3818 4693 1392 803 114 -215 C ATOM 994 CD1 TYR A 257 -96.234 106.119 -27.194 1.00 33.31 C ANISOU 994 CD1 TYR A 257 4786 5717 2153 780 60 -264 C ATOM 995 CD2 TYR A 257 -97.530 104.771 -28.658 1.00 31.14 C ANISOU 995 CD2 TYR A 257 4436 5378 2017 850 232 -69 C ATOM 996 CE1 TYR A 257 -97.117 107.179 -27.395 1.00 53.31 C ANISOU 996 CE1 TYR A 257 7351 8404 4502 806 117 -174 C ATOM 997 CE2 TYR A 257 -98.411 105.807 -28.867 1.00 39.29 C ANISOU 997 CE2 TYR A 257 5490 6552 2885 874 295 26 C ATOM 998 CZ TYR A 257 -98.208 107.011 -28.233 1.00 55.73 C ANISOU 998 CZ TYR A 257 7628 8747 4799 853 236 -28 C ATOM 999 OH TYR A 257 -99.102 108.040 -28.445 1.00 62.17 O ANISOU 999 OH TYR A 257 8469 9707 5446 876 297 70 O ATOM 1000 N LEU A 258 -96.049 102.033 -30.076 1.00 29.38 N ANISOU 1000 N LEU A 258 4137 4815 2212 847 290 -228 N ATOM 1001 CA LEU A 258 -96.793 101.533 -31.216 1.00 28.60 C ANISOU 1001 CA LEU A 258 4001 4694 2172 887 429 -115 C ATOM 1002 C LEU A 258 -98.246 101.407 -30.818 1.00 34.08 C ANISOU 1002 C LEU A 258 4669 5431 2848 905 441 124 C ATOM 1003 O LEU A 258 -98.545 100.858 -29.767 1.00 53.74 O ANISOU 1003 O LEU A 258 7147 7873 5400 879 339 204 O ATOM 1004 CB LEU A 258 -96.244 100.160 -31.623 1.00 19.77 C ANISOU 1004 CB LEU A 258 2844 3403 1265 874 435 -155 C ATOM 1005 CG LEU A 258 -96.844 99.544 -32.877 1.00 23.31 C ANISOU 1005 CG LEU A 258 3240 3788 1827 899 582 -48 C ATOM 1006 CD1 LEU A 258 -96.796 100.525 -34.020 1.00 26.62 C ANISOU 1006 CD1 LEU A 258 3665 4285 2165 915 709 -110 C ATOM 1007 CD2 LEU A 258 -96.128 98.253 -33.227 1.00 47.18 C ANISOU 1007 CD2 LEU A 258 6223 6625 5080 867 572 -112 C ATOM 1008 N ASN A 259 -99.141 101.939 -31.649 1.00 51.79 N ANISOU 1008 N ASN A 259 6898 7748 5033 937 562 232 N ATOM 1009 CA ASN A 259 -100.584 101.825 -31.448 1.00 23.59 C ANISOU 1009 CA ASN A 259 3283 4189 1490 942 585 460 C ATOM 1010 C ASN A 259 -101.096 100.536 -32.059 1.00 25.88 C ANISOU 1010 C ASN A 259 3505 4330 1997 937 644 581 C ATOM 1011 O ASN A 259 -100.890 100.300 -33.250 1.00 29.24 O ANISOU 1011 O ASN A 259 3912 4711 2486 955 752 554 O ATOM 1012 CB ASN A 259 -101.297 102.994 -32.122 1.00 32.75 C ANISOU 1012 CB ASN A 259 4456 5484 2504 973 687 514 C ATOM 1013 CG ASN A 259 -101.226 104.275 -31.312 1.00 39.13 C ANISOU 1013 CG ASN A 259 5323 6440 3105 967 619 465 C ATOM 1014 OD1 ASN A 259 -101.519 104.282 -30.120 1.00 54.03 O ANISOU 1014 OD1 ASN A 259 7209 8332 4989 939 508 523 O ATOM 1015 ND2 ASN A 259 -100.840 105.364 -31.960 1.00 29.83 N ANISOU 1015 ND2 ASN A 259 4195 5373 1765 983 689 356 N ATOM 1016 N ILE A 260 -101.768 99.699 -31.264 1.00 20.57 N ANISOU 1016 N ILE A 260 2787 3564 1463 898 573 706 N ATOM 1017 CA ILE A 260 -102.187 98.395 -31.743 1.00 18.95 C ANISOU 1017 CA ILE A 260 2513 3194 1492 871 607 798 C ATOM 1018 C ILE A 260 -103.567 97.986 -31.303 1.00 29.98 C ANISOU 1018 C ILE A 260 3836 4531 3023 824 583 944 C ATOM 1019 O ILE A 260 -104.102 98.525 -30.348 1.00 46.33 O ANISOU 1019 O ILE A 260 5915 6664 5026 805 522 979 O ATOM 1020 CB ILE A 260 -101.260 97.325 -31.209 1.00 26.52 C ANISOU 1020 CB ILE A 260 3482 4030 2564 832 525 720 C ATOM 1021 CG1 ILE A 260 -101.226 97.420 -29.691 1.00 30.44 C ANISOU 1021 CG1 ILE A 260 4000 4537 3031 783 383 696 C ATOM 1022 CG2 ILE A 260 -99.862 97.487 -31.787 1.00 43.74 C ANISOU 1022 CG2 ILE A 260 5719 6234 4667 871 557 537 C ATOM 1023 CD1 ILE A 260 -100.778 96.140 -29.010 1.00 45.09 C ANISOU 1023 CD1 ILE A 260 5839 6223 5069 704 289 659 C ATOM 1024 N THR A 261 -104.136 97.010 -31.997 1.00 24.78 N ANISOU 1024 N THR A 261 3103 3745 2568 798 626 1005 N ATOM 1025 CA THR A 261 -105.343 96.341 -31.530 1.00 22.42 C ANISOU 1025 CA THR A 261 2725 3365 2427 730 587 1072 C ATOM 1026 C THR A 261 -104.966 94.897 -31.470 1.00 30.52 C ANISOU 1026 C THR A 261 3709 4234 3651 644 537 995 C ATOM 1027 O THR A 261 -104.115 94.476 -32.257 1.00 34.31 O ANISOU 1027 O THR A 261 4195 4662 4178 663 574 951 O ATOM 1028 CB THR A 261 -106.472 96.436 -32.550 1.00 28.66 C ANISOU 1028 CB THR A 261 3453 4159 3278 765 676 1172 C ATOM 1029 OG1 THR A 261 -106.025 95.886 -33.791 1.00 23.72 O ANISOU 1029 OG1 THR A 261 2808 3457 2747 787 740 1154 O ATOM 1030 CG2 THR A 261 -106.882 97.884 -32.767 1.00 29.03 C ANISOU 1030 CG2 THR A 261 3541 4368 3121 839 740 1243 C ATOM 1031 N PHE A 262 -105.573 94.115 -30.584 1.00 13.88 N ANISOU 1031 N PHE A 262 1561 2060 1654 551 464 970 N ATOM 1032 CA PHE A 262 -105.280 92.679 -30.608 1.00 23.53 C ANISOU 1032 CA PHE A 262 2714 3178 3047 481 444 902 C ATOM 1033 C PHE A 262 -106.165 91.952 -31.601 1.00 32.16 C ANISOU 1033 C PHE A 262 3687 4246 4286 497 513 953 C ATOM 1034 O PHE A 262 -106.099 90.728 -31.721 1.00 34.91 O ANISOU 1034 O PHE A 262 3973 4531 4762 429 488 893 O ATOM 1035 CB PHE A 262 -105.412 92.028 -29.239 1.00 25.89 C ANISOU 1035 CB PHE A 262 2986 3451 3402 406 371 868 C ATOM 1036 CG PHE A 262 -104.331 92.413 -28.291 1.00 28.83 C ANISOU 1036 CG PHE A 262 3467 3813 3673 381 284 792 C ATOM 1037 CD1 PHE A 262 -103.203 91.629 -28.153 1.00 18.84 C ANISOU 1037 CD1 PHE A 262 2232 2471 2457 320 231 682 C ATOM 1038 CD2 PHE A 262 -104.448 93.561 -27.526 1.00 35.68 C ANISOU 1038 CD2 PHE A 262 4401 4758 4399 420 249 829 C ATOM 1039 CE1 PHE A 262 -102.216 91.977 -27.269 1.00 15.88 C ANISOU 1039 CE1 PHE A 262 1952 2078 2003 310 138 610 C ATOM 1040 CE2 PHE A 262 -103.459 93.928 -26.647 1.00 15.69 C ANISOU 1040 CE2 PHE A 262 1958 2222 1782 405 156 753 C ATOM 1041 CZ PHE A 262 -102.340 93.129 -26.518 1.00 31.69 C ANISOU 1041 CZ PHE A 262 4014 4156 3872 355 97 644 C ATOM 1042 N ASP A 263 -106.993 92.698 -32.319 1.00 20.23 N ANISOU 1042 N ASP A 263 2164 2786 2739 575 580 1052 N ATOM 1043 CA ASP A 263 -107.818 92.043 -33.308 1.00 23.62 C ANISOU 1043 CA ASP A 263 2485 3181 3309 600 635 1103 C ATOM 1044 C ASP A 263 -107.417 92.385 -34.722 1.00 29.83 C ANISOU 1044 C ASP A 263 3309 3944 4081 656 697 1111 C ATOM 1045 O ASP A 263 -106.989 93.509 -34.993 1.00 30.80 O ANISOU 1045 O ASP A 263 3531 4118 4052 699 727 1129 O ATOM 1046 CB ASP A 263 -109.293 92.356 -33.079 1.00 24.94 C ANISOU 1046 CB ASP A 263 2578 3402 3497 641 667 1223 C ATOM 1047 CG ASP A 263 -109.829 91.693 -31.844 1.00 32.85 C ANISOU 1047 CG ASP A 263 3538 4390 4554 562 600 1202 C ATOM 1048 OD1 ASP A 263 -109.813 90.442 -31.767 1.00 57.17 O ANISOU 1048 OD1 ASP A 263 6621 7386 7716 462 531 1103 O ATOM 1049 OD2 ASP A 263 -110.286 92.429 -30.952 1.00 57.71 O ANISOU 1049 OD2 ASP A 263 6684 7608 7635 586 599 1270 O ATOM 1050 N LYS A 264 -107.618 91.432 -35.616 1.00 27.05 N ANISOU 1050 N LYS A 264 2940 3505 3834 589 676 1059 N ATOM 1051 CA LYS A 264 -107.316 91.541 -37.025 1.00 26.82 C ANISOU 1051 CA LYS A 264 2932 3434 3825 623 730 1068 C ATOM 1052 C LYS A 264 -108.280 92.456 -37.736 1.00 44.51 C ANISOU 1052 C LYS A 264 5145 5727 6039 741 831 1217 C ATOM 1053 O LYS A 264 -109.336 92.747 -37.214 1.00 62.36 O ANISOU 1053 O LYS A 264 7354 8052 8287 780 847 1306 O ATOM 1054 CB LYS A 264 -107.433 90.182 -37.662 1.00 47.95 C ANISOU 1054 CB LYS A 264 5578 6030 6612 528 672 986 C ATOM 1055 CG LYS A 264 -106.427 89.184 -37.195 1.00 66.61 C ANISOU 1055 CG LYS A 264 7964 8357 8988 422 575 846 C ATOM 1056 CD LYS A 264 -106.327 88.025 -38.149 1.00 79.95 C ANISOU 1056 CD LYS A 264 9633 9998 10747 362 528 775 C ATOM 1057 CE LYS A 264 -105.115 87.185 -37.822 1.00 94.62 C ANISOU 1057 CE LYS A 264 11519 11843 12591 277 438 647 C ATOM 1058 NZ LYS A 264 -105.100 85.864 -38.496 1.00 96.80 N ANISOU 1058 NZ LYS A 264 11773 12101 12904 200 418 605 N ATOM 1059 N GLY A 265 -107.910 92.932 -38.917 1.00 44.27 N ANISOU 1059 N GLY A 265 5148 5672 6002 801 906 1250 N ATOM 1060 CA GLY A 265 -108.831 93.684 -39.753 1.00 47.86 C ANISOU 1060 CA GLY A 265 5579 6164 6441 895 1006 1383 C ATOM 1061 C GLY A 265 -109.045 95.150 -39.421 1.00 42.66 C ANISOU 1061 C GLY A 265 4987 5649 5571 937 1071 1450 C ATOM 1062 O GLY A 265 -109.753 95.863 -40.136 1.00 58.22 O ANISOU 1062 O GLY A 265 6955 7672 7494 987 1158 1539 O ATOM 1063 N VAL A 266 -108.433 95.620 -38.349 1.00 26.55 N ANISOU 1063 N VAL A 266 3005 3686 3398 920 1031 1402 N ATOM 1064 CA VAL A 266 -108.626 97.001 -37.968 1.00 22.39 C ANISOU 1064 CA VAL A 266 2535 3320 2652 960 1080 1446 C ATOM 1065 C VAL A 266 -107.669 97.885 -38.748 1.00 51.17 C ANISOU 1065 C VAL A 266 6257 7042 6143 998 1179 1393 C ATOM 1066 O VAL A 266 -106.457 97.711 -38.664 1.00 36.14 O ANISOU 1066 O VAL A 266 4399 5119 4214 979 1165 1284 O ATOM 1067 CB VAL A 266 -108.378 97.200 -36.476 1.00 37.87 C ANISOU 1067 CB VAL A 266 4526 5343 4519 927 988 1405 C ATOM 1068 CG1 VAL A 266 -108.466 98.680 -36.111 1.00 46.33 C ANISOU 1068 CG1 VAL A 266 5663 6595 5345 970 1027 1432 C ATOM 1069 CG2 VAL A 266 -109.383 96.376 -35.662 1.00 42.80 C ANISOU 1069 CG2 VAL A 266 5071 5903 5290 869 904 1427 C ATOM 1070 N TYR A 267 -108.216 98.823 -39.518 1.00 46.40 N ANISOU 1070 N TYR A 267 5662 6530 5439 1045 1285 1449 N ATOM 1071 CA TYR A 267 -107.386 99.825 -40.179 1.00 37.15 C ANISOU 1071 CA TYR A 267 4556 5467 4094 1071 1389 1359 C ATOM 1072 C TYR A 267 -107.756 101.236 -39.760 1.00 29.34 C ANISOU 1072 C TYR A 267 3615 4671 2860 1107 1426 1373 C ATOM 1073 O TYR A 267 -108.920 101.614 -39.764 1.00 60.32 O ANISOU 1073 O TYR A 267 7508 8640 6771 1131 1448 1497 O ATOM 1074 CB TYR A 267 -107.414 99.695 -41.703 1.00 46.41 C ANISOU 1074 CB TYR A 267 5700 6569 5364 1086 1501 1368 C ATOM 1075 CG TYR A 267 -106.691 100.832 -42.379 1.00 40.11 C ANISOU 1075 CG TYR A 267 4956 5897 4387 1109 1619 1253 C ATOM 1076 CD1 TYR A 267 -105.312 100.872 -42.417 1.00 57.45 C ANISOU 1076 CD1 TYR A 267 7190 8096 6541 1087 1622 1075 C ATOM 1077 CD2 TYR A 267 -107.386 101.875 -42.952 1.00 55.41 C ANISOU 1077 CD2 TYR A 267 6901 7951 6201 1151 1726 1305 C ATOM 1078 CE1 TYR A 267 -104.642 101.917 -43.022 1.00 66.96 C ANISOU 1078 CE1 TYR A 267 8435 9413 7595 1104 1725 934 C ATOM 1079 CE2 TYR A 267 -106.727 102.923 -43.559 1.00 64.13 C ANISOU 1079 CE2 TYR A 267 8052 9171 7142 1167 1834 1178 C ATOM 1080 CZ TYR A 267 -105.354 102.935 -43.588 1.00 52.22 C ANISOU 1080 CZ TYR A 267 6578 7661 5604 1142 1832 985 C ATOM 1081 OH TYR A 267 -104.683 103.964 -44.184 1.00 46.38 O ANISOU 1081 OH TYR A 267 5877 7029 4715 1152 1935 832 O ATOM 1082 N SER A 268 -106.736 102.007 -39.411 1.00 43.76 N ANISOU 1082 N SER A 268 5516 6612 4497 1107 1427 1233 N ATOM 1083 CA SER A 268 -106.891 103.313 -38.800 1.00 31.83 C ANISOU 1083 CA SER A 268 4066 5288 2741 1128 1428 1219 C ATOM 1084 C SER A 268 -106.566 104.425 -39.758 1.00 36.92 C ANISOU 1084 C SER A 268 4756 6050 3222 1155 1558 1132 C ATOM 1085 O SER A 268 -105.459 104.486 -40.279 1.00 65.22 O ANISOU 1085 O SER A 268 8368 9624 6788 1145 1601 968 O ATOM 1086 CB SER A 268 -105.956 103.427 -37.605 1.00 35.92 C ANISOU 1086 CB SER A 268 4641 5853 3153 1104 1313 1101 C ATOM 1087 OG SER A 268 -105.790 104.781 -37.239 1.00 45.75 O ANISOU 1087 OG SER A 268 5958 7280 4145 1119 1321 1037 O ATOM 1088 N ASP A 269 -107.521 105.321 -39.973 1.00 36.31 N ANISOU 1088 N ASP A 269 4683 6083 3031 1185 1623 1230 N ATOM 1089 CA ASP A 269 -107.295 106.474 -40.817 1.00 44.48 C ANISOU 1089 CA ASP A 269 5765 7242 3892 1206 1752 1149 C ATOM 1090 C ASP A 269 -106.484 107.549 -40.093 1.00 45.95 C ANISOU 1090 C ASP A 269 6046 7586 3827 1195 1713 998 C ATOM 1091 O ASP A 269 -105.911 108.435 -40.721 1.00 59.96 O ANISOU 1091 O ASP A 269 7872 9451 5458 1197 1806 863 O ATOM 1092 CB ASP A 269 -108.636 107.042 -41.287 1.00 70.82 C ANISOU 1092 CB ASP A 269 9074 10641 7194 1241 1835 1315 C ATOM 1093 CG ASP A 269 -109.402 106.072 -42.181 1.00 73.89 C ANISOU 1093 CG ASP A 269 9372 10872 7831 1254 1883 1443 C ATOM 1094 OD1 ASP A 269 -108.762 105.357 -42.987 1.00 65.25 O ANISOU 1094 OD1 ASP A 269 8252 9657 6884 1241 1920 1371 O ATOM 1095 OD2 ASP A 269 -110.647 106.030 -42.079 1.00 73.58 O ANISOU 1095 OD2 ASP A 269 9285 10826 7845 1275 1879 1611 O ATOM 1096 N MET A 270 -106.443 107.472 -38.768 1.00 41.54 N ANISOU 1096 N MET A 270 5508 7052 3223 1178 1571 1015 N ATOM 1097 CA MET A 270 -105.722 108.459 -37.972 1.00 39.98 C ANISOU 1097 CA MET A 270 5398 6994 2799 1163 1508 882 C ATOM 1098 C MET A 270 -104.215 108.246 -38.083 1.00 53.98 C ANISOU 1098 C MET A 270 7208 8720 4580 1138 1488 655 C ATOM 1099 O MET A 270 -103.429 109.199 -38.141 1.00 54.10 O ANISOU 1099 O MET A 270 7297 8835 4422 1127 1509 487 O ATOM 1100 CB MET A 270 -106.175 108.377 -36.501 1.00 43.04 C ANISOU 1100 CB MET A 270 5784 7404 3164 1149 1356 980 C ATOM 1101 CG MET A 270 -105.355 109.213 -35.510 1.00 53.36 C ANISOU 1101 CG MET A 270 7176 8826 4274 1126 1254 844 C ATOM 1102 SD MET A 270 -106.169 109.411 -33.721 1.00 82.21 S ANISOU 1102 SD MET A 270 10823 12532 7882 1106 1083 994 S ATOM 1103 CE MET A 270 -104.751 110.440 -32.846 1.00276.84 C ANISOU 1103 CE MET A 270 35586 37300 32300 1072 972 765 C ATOM 1104 N TYR A 271 -103.817 106.981 -38.110 1.00 41.66 N ANISOU 1104 N TYR A 271 5700 4591 5536 1038 2082 952 N ATOM 1105 CA TYR A 271 -102.417 106.624 -38.190 1.00 31.05 C ANISOU 1105 CA TYR A 271 4406 3262 4131 1040 2038 903 C ATOM 1106 C TYR A 271 -102.120 106.006 -39.555 1.00 37.28 C ANISOU 1106 C TYR A 271 5157 4055 4951 1048 2061 900 C ATOM 1107 O TYR A 271 -101.026 105.512 -39.802 1.00 54.34 O ANISOU 1107 O TYR A 271 7351 6221 7073 1048 2031 859 O ATOM 1108 CB TYR A 271 -102.067 105.649 -37.077 1.00 33.52 C ANISOU 1108 CB TYR A 271 4770 3537 4431 997 2008 860 C ATOM 1109 CG TYR A 271 -102.549 106.071 -35.702 1.00 45.52 C ANISOU 1109 CG TYR A 271 6315 5043 5936 985 1992 862 C ATOM 1110 CD1 TYR A 271 -103.693 105.522 -35.147 1.00 45.33 C ANISOU 1110 CD1 TYR A 271 6269 4978 5976 956 2024 877 C ATOM 1111 CD2 TYR A 271 -101.852 107.007 -34.956 1.00 63.30 C ANISOU 1111 CD2 TYR A 271 8612 7325 8113 1002 1942 846 C ATOM 1112 CE1 TYR A 271 -104.133 105.900 -33.897 1.00 48.91 C ANISOU 1112 CE1 TYR A 271 6745 5421 6417 947 2009 876 C ATOM 1113 CE2 TYR A 271 -102.286 107.390 -33.705 1.00 59.46 C ANISOU 1113 CE2 TYR A 271 8145 6827 7618 992 1926 846 C ATOM 1114 CZ TYR A 271 -103.426 106.840 -33.183 1.00 43.59 C ANISOU 1114 CZ TYR A 271 6113 4778 5669 966 1960 860 C ATOM 1115 OH TYR A 271 -103.849 107.220 -31.930 1.00 48.09 O ANISOU 1115 OH TYR A 271 6703 5339 6230 959 1944 857 O ATOM 1116 N ASN A 272 -103.100 106.075 -40.447 1.00 45.31 N ANISOU 1116 N ASN A 272 6103 5072 6041 1056 2113 945 N ATOM 1117 CA ASN A 272 -103.013 105.421 -41.742 1.00 32.40 C ANISOU 1117 CA ASN A 272 4418 3436 4455 1061 2141 947 C ATOM 1118 C ASN A 272 -102.256 104.111 -41.776 1.00 47.62 C ANISOU 1118 C ASN A 272 6384 5335 6375 1035 2117 892 C ATOM 1119 O ASN A 272 -101.391 103.878 -42.639 1.00 53.16 O ANISOU 1119 O ASN A 272 7110 6060 7028 1057 2087 856 O ATOM 1120 CB ASN A 272 -102.540 106.389 -42.831 1.00 52.25 C ANISOU 1120 CB ASN A 272 6912 6008 6935 1113 2138 958 C ATOM 1121 CG ASN A 272 -103.459 107.601 -42.973 1.00 59.57 C ANISOU 1121 CG ASN A 272 7800 6964 7870 1139 2165 1013 C ATOM 1122 OD1 ASN A 272 -103.153 108.684 -42.470 1.00 58.38 O ANISOU 1122 OD1 ASN A 272 7686 6844 7652 1163 2139 1014 O ATOM 1123 ND2 ASN A 272 -104.599 107.418 -43.647 1.00 48.82 N ANISOU 1123 ND2 ASN A 272 6364 5591 6594 1132 2217 1059 N ATOM 1124 N ALA A 273 -102.568 103.271 -40.793 1.00 30.58 N ANISOU 1124 N ALA A 273 4232 3125 4263 988 2128 883 N ATOM 1125 CA ALA A 273 -101.934 101.970 -40.668 1.00 26.72 C ANISOU 1125 CA ALA A 273 3779 2602 3770 957 2110 831 C ATOM 1126 C ALA A 273 -102.875 100.844 -40.273 1.00 37.15 C ANISOU 1126 C ALA A 273 5075 3863 5178 906 2145 836 C ATOM 1127 O ALA A 273 -103.959 101.089 -39.767 1.00 44.72 O ANISOU 1127 O ALA A 273 6009 4805 6177 892 2169 873 O ATOM 1128 CB ALA A 273 -100.879 102.167 -39.598 1.00 54.19 C ANISOU 1128 CB ALA A 273 7346 6095 7149 953 2049 787 C ATOM 1129 N ASP A 274 -102.463 99.605 -40.518 1.00 52.37 N ANISOU 1129 N ASP A 274 7006 5756 7135 880 2147 796 N ATOM 1130 CA ASP A 274 -103.109 98.466 -39.889 1.00 47.75 C ANISOU 1130 CA ASP A 274 6417 5113 6613 826 2168 787 C ATOM 1131 C ASP A 274 -102.667 98.488 -38.438 1.00 52.53 C ANISOU 1131 C ASP A 274 7106 5716 7137 807 2126 754 C ATOM 1132 O ASP A 274 -101.515 98.856 -38.144 1.00 33.14 O ANISOU 1132 O ASP A 274 4712 3292 4586 825 2075 719 O ATOM 1133 CB ASP A 274 -102.676 97.153 -40.535 1.00 56.26 C ANISOU 1133 CB ASP A 274 7489 6151 7738 786 2108 737 C ATOM 1134 CG ASP A 274 -103.412 96.871 -41.823 1.00 79.85 C ANISOU 1134 CG ASP A 274 10386 9121 10831 779 2118 768 C ATOM 1135 OD1 ASP A 274 -104.658 96.959 -41.813 1.00 77.47 O ANISOU 1135 OD1 ASP A 274 10027 8801 10607 765 2170 822 O ATOM 1136 OD2 ASP A 274 -102.746 96.570 -42.841 1.00 95.30 O ANISOU 1136 OD2 ASP A 274 12330 11084 12795 789 2073 741 O ATOM 1137 N LEU A 275 -103.572 98.102 -37.535 1.00 25.90 N ANISOU 1137 N LEU A 275 3732 2305 3804 769 2142 766 N ATOM 1138 CA LEU A 275 -103.293 98.181 -36.112 1.00 25.33 C ANISOU 1138 CA LEU A 275 3730 2232 3663 753 2102 737 C ATOM 1139 C LEU A 275 -103.034 96.832 -35.477 1.00 29.68 C ANISOU 1139 C LEU A 275 4319 2740 4216 702 2094 690 C ATOM 1140 O LEU A 275 -102.522 96.758 -34.356 1.00 34.95 O ANISOU 1140 O LEU A 275 5052 3412 4814 689 2052 654 O ATOM 1141 CB LEU A 275 -104.414 98.920 -35.365 1.00 29.34 C ANISOU 1141 CB LEU A 275 4218 2736 4193 758 2114 777 C ATOM 1142 CG LEU A 275 -104.229 100.418 -35.083 1.00 47.15 C ANISOU 1142 CG LEU A 275 6489 5042 6382 803 2087 796 C ATOM 1143 CD1 LEU A 275 -103.495 101.117 -36.208 1.00 52.00 C ANISOU 1143 CD1 LEU A 275 7091 5703 6964 844 2080 806 C ATOM 1144 CD2 LEU A 275 -105.570 101.088 -34.825 1.00 70.75 C ANISOU 1144 CD2 LEU A 275 9433 8024 9424 812 2119 846 C ATOM 1145 N TYR A 276 -103.377 95.757 -36.169 1.00 33.41 N ANISOU 1145 N TYR A 276 4753 3169 4772 662 2078 678 N ATOM 1146 CA TYR A 276 -103.233 94.439 -35.553 1.00 34.23 C ANISOU 1146 CA TYR A 276 4893 3225 4886 599 2008 623 C ATOM 1147 C TYR A 276 -101.779 94.124 -35.167 1.00 24.35 C ANISOU 1147 C TYR A 276 3721 1995 3536 596 1942 559 C ATOM 1148 O TYR A 276 -100.891 94.101 -36.007 1.00 33.88 O ANISOU 1148 O TYR A 276 4934 3221 4719 611 1904 537 O ATOM 1149 CB TYR A 276 -103.831 93.341 -36.434 1.00 38.14 C ANISOU 1149 CB TYR A 276 5333 3668 5492 553 1969 617 C ATOM 1150 CG TYR A 276 -103.613 91.944 -35.897 1.00 29.10 C ANISOU 1150 CG TYR A 276 4226 2476 4355 490 1892 556 C ATOM 1151 CD1 TYR A 276 -103.871 91.632 -34.568 1.00 24.85 C ANISOU 1151 CD1 TYR A 276 3730 1920 3790 463 1891 539 C ATOM 1152 CD2 TYR A 276 -103.149 90.937 -36.721 1.00 25.23 C ANISOU 1152 CD2 TYR A 276 3728 1961 3899 458 1821 515 C ATOM 1153 CE1 TYR A 276 -103.663 90.351 -34.073 1.00 25.49 C ANISOU 1153 CE1 TYR A 276 3846 1963 3876 408 1821 481 C ATOM 1154 CE2 TYR A 276 -102.938 89.656 -36.241 1.00 43.54 C ANISOU 1154 CE2 TYR A 276 6082 4239 6222 401 1750 459 C ATOM 1155 CZ TYR A 276 -103.195 89.361 -34.921 1.00 30.04 C ANISOU 1155 CZ TYR A 276 4415 2515 4484 376 1751 442 C ATOM 1156 OH TYR A 276 -102.982 88.068 -34.467 1.00 24.51 O ANISOU 1156 OH TYR A 276 3748 1777 3787 321 1680 385 O ATOM 1157 N VAL A 277 -101.565 93.863 -33.880 1.00 27.14 N ANISOU 1157 N VAL A 277 4133 2344 3833 574 1928 531 N ATOM 1158 CA VAL A 277 -100.249 93.631 -33.320 1.00 23.28 C ANISOU 1158 CA VAL A 277 3722 1879 3244 568 1872 476 C ATOM 1159 C VAL A 277 -99.446 92.591 -34.102 1.00 24.90 C ANISOU 1159 C VAL A 277 3936 2066 3460 536 1786 425 C ATOM 1160 O VAL A 277 -98.299 92.837 -34.464 1.00 36.72 O ANISOU 1160 O VAL A 277 5467 3594 4890 558 1752 402 O ATOM 1161 CB VAL A 277 -100.328 93.178 -31.857 1.00 22.88 C ANISOU 1161 CB VAL A 277 3723 1816 3155 535 1861 450 C ATOM 1162 CG1 VAL A 277 -99.074 93.614 -31.138 1.00 32.15 C ANISOU 1162 CG1 VAL A 277 4972 3035 4208 555 1840 420 C ATOM 1163 CG2 VAL A 277 -101.531 93.764 -31.182 1.00114.56 C ANISOU 1163 CG2 VAL A 277 15307 13418 14801 546 1935 499 C ATOM 1164 N GLY A 278 -100.051 91.424 -34.323 1.00 34.19 N ANISOU 1164 N GLY A 278 5084 3190 4718 483 1750 408 N ATOM 1165 CA GLY A 278 -99.399 90.308 -34.983 1.00 23.46 C ANISOU 1165 CA GLY A 278 3733 1806 3375 444 1667 358 C ATOM 1166 C GLY A 278 -98.826 90.697 -36.336 1.00 50.20 C ANISOU 1166 C GLY A 278 7091 5213 6768 479 1655 365 C ATOM 1167 O GLY A 278 -97.784 90.176 -36.780 1.00 42.18 O ANISOU 1167 O GLY A 278 6107 4201 5719 467 1585 321 O ATOM 1168 N ASP A 279 -99.499 91.636 -36.990 1.00 26.01 N ANISOU 1168 N ASP A 279 3970 2166 3748 523 1723 422 N ATOM 1169 CA ASP A 279 -99.153 92.009 -38.361 1.00 36.23 C ANISOU 1169 CA ASP A 279 5224 3478 5063 558 1719 433 C ATOM 1170 C ASP A 279 -98.177 93.168 -38.453 1.00 24.19 C ANISOU 1170 C ASP A 279 3733 2013 3443 621 1736 438 C ATOM 1171 O ASP A 279 -97.586 93.405 -39.502 1.00 60.59 O ANISOU 1171 O ASP A 279 8329 6643 8051 651 1716 433 O ATOM 1172 CB ASP A 279 -100.427 92.384 -39.145 1.00 39.86 C ANISOU 1172 CB ASP A 279 5594 3927 5625 573 1782 494 C ATOM 1173 CG ASP A 279 -101.169 91.172 -39.682 1.00 47.82 C ANISOU 1173 CG ASP A 279 6553 4873 6741 517 1745 485 C ATOM 1174 OD1 ASP A 279 -100.951 90.052 -39.171 1.00 48.21 O ANISOU 1174 OD1 ASP A 279 6640 4887 6791 463 1682 437 O ATOM 1175 OD2 ASP A 279 -101.970 91.351 -40.623 1.00 63.93 O ANISOU 1175 OD2 ASP A 279 8518 6906 8868 527 1779 527 O ATOM 1176 N VAL A 280 -98.016 93.899 -37.363 1.00 35.93 N ANISOU 1176 N VAL A 280 5268 3531 4855 642 1773 448 N ATOM 1177 CA VAL A 280 -97.367 95.194 -37.437 1.00 27.24 C ANISOU 1177 CA VAL A 280 4189 2487 3675 709 1808 466 C ATOM 1178 C VAL A 280 -96.195 95.441 -36.477 1.00 31.54 C ANISOU 1178 C VAL A 280 4821 3061 4102 717 1776 430 C ATOM 1179 O VAL A 280 -95.460 96.391 -36.675 1.00 26.08 O ANISOU 1179 O VAL A 280 4153 2413 3342 770 1787 436 O ATOM 1180 CB VAL A 280 -98.412 96.298 -37.215 1.00 48.24 C ANISOU 1180 CB VAL A 280 6806 5167 6355 749 1907 532 C ATOM 1181 CG1 VAL A 280 -97.755 97.674 -37.179 1.00 63.18 C ANISOU 1181 CG1 VAL A 280 8724 7120 8162 809 1918 551 C ATOM 1182 CG2 VAL A 280 -99.448 96.240 -38.312 1.00 64.21 C ANISOU 1182 CG2 VAL A 280 8740 7171 8487 751 1942 573 C ATOM 1183 N LEU A 281 -96.015 94.635 -35.431 1.00 22.63 N ANISOU 1183 N LEU A 281 3741 1911 2946 666 1737 395 N ATOM 1184 CA LEU A 281 -95.036 95.032 -34.424 1.00 27.42 C ANISOU 1184 CA LEU A 281 4425 2551 3442 677 1720 372 C ATOM 1185 C LEU A 281 -93.616 94.765 -34.883 1.00 21.78 C ANISOU 1185 C LEU A 281 3758 1852 2667 677 1641 327 C ATOM 1186 O LEU A 281 -92.828 95.693 -35.043 1.00 37.13 O ANISOU 1186 O LEU A 281 5730 3837 4542 727 1646 331 O ATOM 1187 CB LEU A 281 -95.296 94.420 -33.039 1.00 29.02 C ANISOU 1187 CB LEU A 281 4666 2735 3624 629 1714 353 C ATOM 1188 CG LEU A 281 -94.250 94.887 -32.013 1.00 21.13 C ANISOU 1188 CG LEU A 281 3733 1776 2519 629 1660 336 C ATOM 1189 CD1 LEU A 281 -94.836 95.231 -30.676 1.00 25.39 C ANISOU 1189 CD1 LEU A 281 4272 2319 3054 610 1652 354 C ATOM 1190 CD2 LEU A 281 -93.148 93.857 -31.852 1.00 47.66 C ANISOU 1190 CD2 LEU A 281 7158 5127 5823 596 1604 273 C ATOM 1191 N VAL A 282 -93.282 93.501 -35.071 1.00 21.72 N ANISOU 1191 N VAL A 282 3761 1809 2682 621 1567 282 N ATOM 1192 CA VAL A 282 -91.973 93.168 -35.611 1.00 24.92 C ANISOU 1192 CA VAL A 282 4206 2223 3039 617 1486 240 C ATOM 1193 C VAL A 282 -91.651 94.118 -36.750 1.00 28.62 C ANISOU 1193 C VAL A 282 4647 2720 3506 681 1504 261 C ATOM 1194 O VAL A 282 -90.683 94.864 -36.686 1.00 64.11 O ANISOU 1194 O VAL A 282 9187 7252 7919 721 1491 255 O ATOM 1195 CB VAL A 282 -91.945 91.764 -36.168 1.00 26.63 C ANISOU 1195 CB VAL A 282 4408 2395 3315 558 1415 202 C ATOM 1196 CG1 VAL A 282 -90.573 91.472 -36.730 1.00 47.36 C ANISOU 1196 CG1 VAL A 282 7077 5030 5889 556 1331 161 C ATOM 1197 CG2 VAL A 282 -92.327 90.775 -35.083 1.00 33.98 C ANISOU 1197 CG2 VAL A 282 5362 3297 4251 496 1398 180 C ATOM 1198 N ASP A 283 -92.482 94.099 -37.786 1.00 31.26 N ANISOU 1198 N ASP A 283 4907 3037 3931 693 1533 288 N ATOM 1199 CA ASP A 283 -92.293 94.982 -38.937 1.00 27.59 C ANISOU 1199 CA ASP A 283 4408 2601 3474 756 1555 310 C ATOM 1200 C ASP A 283 -91.971 96.419 -38.541 1.00 37.86 C ANISOU 1200 C ASP A 283 5736 3955 4696 823 1609 337 C ATOM 1201 O ASP A 283 -91.140 97.062 -39.174 1.00 65.86 O ANISOU 1201 O ASP A 283 9296 7532 8197 872 1591 330 O ATOM 1202 CB ASP A 283 -93.518 94.964 -39.858 1.00 44.12 C ANISOU 1202 CB ASP A 283 6410 4675 5678 763 1606 349 C ATOM 1203 CG ASP A 283 -93.541 93.757 -40.790 1.00 71.70 C ANISOU 1203 CG ASP A 283 9871 8125 9248 718 1541 320 C ATOM 1204 OD1 ASP A 283 -92.457 93.218 -41.098 1.00 75.03 O ANISOU 1204 OD1 ASP A 283 10333 8541 9633 703 1461 273 O ATOM 1205 OD2 ASP A 283 -94.645 93.350 -41.222 1.00 88.69 O ANISOU 1205 OD2 ASP A 283 11955 10245 11497 697 1570 345 O ATOM 1206 N SER A 284 -92.613 96.926 -37.496 1.00 28.66 N ANISOU 1206 N SER A 284 4577 2799 3512 827 1672 367 N ATOM 1207 CA SER A 284 -92.456 98.335 -37.143 1.00 38.48 C ANISOU 1207 CA SER A 284 5823 4097 4702 860 1669 407 C ATOM 1208 C SER A 284 -91.160 98.642 -36.390 1.00 46.61 C ANISOU 1208 C SER A 284 6923 5155 5632 852 1589 379 C ATOM 1209 O SER A 284 -90.687 99.777 -36.394 1.00 49.94 O ANISOU 1209 O SER A 284 7348 5618 6011 884 1561 398 O ATOM 1210 CB SER A 284 -93.662 98.832 -36.339 1.00 36.02 C ANISOU 1210 CB SER A 284 5476 3784 4426 845 1708 455 C ATOM 1211 OG SER A 284 -94.810 98.936 -37.159 1.00 45.72 O ANISOU 1211 OG SER A 284 6631 5000 5742 863 1778 494 O ATOM 1212 N TYR A 285 -90.592 97.639 -35.735 1.00 21.35 N ANISOU 1212 N TYR A 285 3779 1933 2400 807 1549 334 N ATOM 1213 CA TYR A 285 -89.356 97.855 -35.001 1.00 21.62 C ANISOU 1213 CA TYR A 285 3874 1993 2347 794 1469 310 C ATOM 1214 C TYR A 285 -88.185 97.378 -35.834 1.00 30.55 C ANISOU 1214 C TYR A 285 5047 3121 3440 807 1423 264 C ATOM 1215 O TYR A 285 -87.107 97.072 -35.321 1.00 46.30 O ANISOU 1215 O TYR A 285 7101 5123 5369 782 1353 231 O ATOM 1216 CB TYR A 285 -89.401 97.137 -33.647 1.00 31.38 C ANISOU 1216 CB TYR A 285 5145 3213 3565 735 1444 291 C ATOM 1217 CG TYR A 285 -90.214 97.888 -32.640 1.00 27.17 C ANISOU 1217 CG TYR A 285 4582 2691 3051 732 1460 329 C ATOM 1218 CD1 TYR A 285 -89.640 98.865 -31.849 1.00 48.09 C ANISOU 1218 CD1 TYR A 285 7243 5373 5655 741 1408 337 C ATOM 1219 CD2 TYR A 285 -91.559 97.648 -32.498 1.00 27.99 C ANISOU 1219 CD2 TYR A 285 4644 2767 3222 721 1525 353 C ATOM 1220 CE1 TYR A 285 -90.395 99.578 -30.926 1.00 47.93 C ANISOU 1220 CE1 TYR A 285 7195 5358 5657 742 1419 365 C ATOM 1221 CE2 TYR A 285 -92.326 98.365 -31.588 1.00 38.50 C ANISOU 1221 CE2 TYR A 285 5951 4105 4572 722 1535 384 C ATOM 1222 CZ TYR A 285 -91.739 99.325 -30.802 1.00 33.58 C ANISOU 1222 CZ TYR A 285 5343 3515 3903 733 1481 387 C ATOM 1223 OH TYR A 285 -92.507 100.024 -29.892 1.00 32.40 O ANISOU 1223 OH TYR A 285 5170 3369 3774 736 1490 412 O ATOM 1224 N SER A 286 -88.415 97.333 -37.137 1.00 20.91 N ANISOU 1224 N SER A 286 2210 2390 3346 915 1088 201 N ATOM 1225 CA SER A 286 -87.442 96.813 -38.074 1.00 26.95 C ANISOU 1225 CA SER A 286 3088 2996 4156 956 1215 249 C ATOM 1226 C SER A 286 -87.270 97.759 -39.255 1.00 23.63 C ANISOU 1226 C SER A 286 2795 2484 3700 1023 1363 200 C ATOM 1227 O SER A 286 -88.141 98.578 -39.526 1.00 56.98 O ANISOU 1227 O SER A 286 7006 6776 7866 1046 1353 173 O ATOM 1228 CB SER A 286 -87.876 95.429 -38.543 1.00 21.47 C ANISOU 1228 CB SER A 286 2365 2307 3485 960 1175 435 C ATOM 1229 OG SER A 286 -87.859 94.538 -37.443 1.00 43.47 O ANISOU 1229 OG SER A 286 5070 5149 6298 891 1065 469 O ATOM 1230 N ASP A 287 -86.143 97.643 -39.952 1.00 38.99 N ANISOU 1230 N ASP A 287 4872 4260 5683 1052 1524 206 N ATOM 1231 CA ASP A 287 -85.822 98.531 -41.076 1.00 33.60 C ANISOU 1231 CA ASP A 287 4349 3449 4969 1112 1707 172 C ATOM 1232 C ASP A 287 -84.701 97.938 -41.903 1.00 53.11 C ANISOU 1232 C ASP A 287 6923 5771 7484 1138 1827 226 C ATOM 1233 O ASP A 287 -83.531 98.027 -41.543 1.00 75.75 O ANISOU 1233 O ASP A 287 9904 8480 10398 1104 1971 171 O ATOM 1234 CB ASP A 287 -85.411 99.918 -40.575 1.00 36.08 C ANISOU 1234 CB ASP A 287 4808 3654 5246 1079 1890 13 C ATOM 1235 CG ASP A 287 -84.761 100.769 -41.649 1.00 45.68 C ANISOU 1235 CG ASP A 287 6250 4689 6416 1108 2103 -50 C ATOM 1236 OD1 ASP A 287 -84.150 101.789 -41.279 1.00 62.07 O ANISOU 1236 OD1 ASP A 287 8513 6634 8436 1029 2271 -216 O ATOM 1237 OD2 ASP A 287 -84.858 100.444 -42.855 1.00 42.11 O ANISOU 1237 OD2 ASP A 287 5807 4226 5969 1187 2106 51 O ATOM 1238 N ASP A 288 -85.083 97.366 -43.036 1.00 55.48 N ANISOU 1238 N ASP A 288 7217 6077 7786 1205 1857 380 N ATOM 1239 CA ASP A 288 -84.163 96.708 -43.945 1.00 52.30 C ANISOU 1239 CA ASP A 288 6896 5549 7425 1248 2006 485 C ATOM 1240 C ASP A 288 -83.105 97.668 -44.525 1.00 58.08 C ANISOU 1240 C ASP A 288 7822 6099 8145 1268 2195 374 C ATOM 1241 O ASP A 288 -82.101 97.221 -45.089 1.00 51.01 O ANISOU 1241 O ASP A 288 7011 5078 7291 1292 2335 432 O ATOM 1242 CB ASP A 288 -84.957 96.017 -45.063 1.00 44.19 C ANISOU 1242 CB ASP A 288 5825 4584 6382 1319 2020 681 C ATOM 1243 CG ASP A 288 -85.737 97.003 -45.927 1.00 75.18 C ANISOU 1243 CG ASP A 288 9802 8518 10244 1383 2065 675 C ATOM 1244 OD1 ASP A 288 -85.494 98.226 -45.822 1.00 74.15 O ANISOU 1244 OD1 ASP A 288 9767 8324 10083 1379 2117 518 O ATOM 1245 OD2 ASP A 288 -86.589 96.552 -46.722 1.00 97.31 O ANISOU 1245 OD2 ASP A 288 12558 11395 13021 1432 2053 823 O ATOM 1246 N GLY A 289 -83.339 98.976 -44.398 1.00 49.41 N ANISOU 1246 N GLY A 289 6812 4976 6986 1256 2232 228 N ATOM 1247 CA GLY A 289 -82.320 99.974 -44.693 1.00 36.73 C ANISOU 1247 CA GLY A 289 5449 3147 5359 1241 2476 116 C ATOM 1248 C GLY A 289 -82.339 100.536 -46.102 1.00 72.98 C ANISOU 1248 C GLY A 289 10158 7665 9907 1325 2607 152 C ATOM 1249 O GLY A 289 -81.518 101.389 -46.448 1.00 40.20 O ANISOU 1249 O GLY A 289 6228 3322 5723 1307 2813 55 O ATOM 1250 N VAL A 290 -83.260 100.052 -46.929 1.00 89.90 N ANISOU 1250 N VAL A 290 12174 9940 12045 1406 2513 294 N ATOM 1251 CA VAL A 290 -83.444 100.619 -48.259 1.00 83.41 C ANISOU 1251 CA VAL A 290 11460 9049 11184 1499 2658 355 C ATOM 1252 C VAL A 290 -83.635 102.052 -48.710 1.00 88.95 C ANISOU 1252 C VAL A 290 12146 9846 11804 1497 2585 253 C ATOM 1253 O VAL A 290 -82.850 102.565 -49.513 1.00 75.74 O ANISOU 1253 O VAL A 290 10318 8338 10120 1466 2407 247 O ATOM 1254 CB VAL A 290 -83.899 99.572 -49.293 1.00 72.04 C ANISOU 1254 CB VAL A 290 9940 7656 9774 1595 2685 605 C ATOM 1255 CG1 VAL A 290 -85.357 99.174 -49.057 1.00 70.57 C ANISOU 1255 CG1 VAL A 290 9576 7670 9567 1597 2497 692 C ATOM 1256 CG2 VAL A 290 -83.702 100.115 -50.706 1.00 67.62 C ANISOU 1256 CG2 VAL A 290 9525 6982 9186 1696 2883 672 C ATOM 1257 N VAL A 291 -84.686 102.688 -48.213 1.00104.68 N ANISOU 1257 N VAL A 291 14311 11725 13735 1531 2745 181 N ATOM 1258 CA VAL A 291 -85.074 103.998 -48.707 1.00118.78 C ANISOU 1258 CA VAL A 291 16133 13569 15431 1524 2739 75 C ATOM 1259 C VAL A 291 -84.641 104.699 -47.425 1.00124.08 C ANISOU 1259 C VAL A 291 16906 14187 16051 1401 2777 -118 C ATOM 1260 O VAL A 291 -84.784 105.914 -47.288 1.00136.14 O ANISOU 1260 O VAL A 291 18571 15687 17470 1356 2860 -263 O ATOM 1261 CB VAL A 291 -86.581 103.655 -48.652 1.00117.08 C ANISOU 1261 CB VAL A 291 15683 13590 15211 1556 2517 165 C ATOM 1262 CG1 VAL A 291 -87.421 104.924 -48.558 1.00123.41 C ANISOU 1262 CG1 VAL A 291 16519 14457 15914 1559 2527 65 C ATOM 1263 CG2 VAL A 291 -86.983 102.827 -49.865 1.00110.38 C ANISOU 1263 CG2 VAL A 291 14798 12738 14403 1665 2564 407 C ATOM 1264 N SER A 292 -84.095 103.926 -46.490 1.00112.11 N ANISOU 1264 N SER A 292 15333 12663 14602 1332 2720 -123 N ATOM 1265 CA SER A 292 -83.548 104.479 -45.257 1.00106.36 C ANISOU 1265 CA SER A 292 14714 11869 13828 1189 2769 -306 C ATOM 1266 C SER A 292 -82.061 104.752 -45.412 1.00 78.98 C ANISOU 1266 C SER A 292 11503 8147 10359 1108 2978 -405 C ATOM 1267 O SER A 292 -81.554 105.762 -44.932 1.00 84.35 O ANISOU 1267 O SER A 292 12394 8719 10936 965 3091 -604 O ATOM 1268 CB SER A 292 -83.782 103.534 -44.078 1.00121.06 C ANISOU 1268 CB SER A 292 16375 13859 15765 1148 2596 -264 C ATOM 1269 OG SER A 292 -83.160 104.029 -42.905 1.00130.28 O ANISOU 1269 OG SER A 292 17661 14952 16889 991 2662 -443 O ATOM 1270 N GLY A 293 -81.366 103.838 -46.079 1.00 82.58 N ANISOU 1270 N GLY A 293 11943 8519 10913 1178 3025 -270 N ATOM 1271 CA GLY A 293 -79.958 104.019 -46.401 1.00 91.72 C ANISOU 1271 CA GLY A 293 13333 9435 12081 1123 3235 -332 C ATOM 1272 C GLY A 293 -79.002 103.705 -45.268 1.00 66.36 C ANISOU 1272 C GLY A 293 10178 6128 8908 976 3255 -430 C ATOM 1273 O GLY A 293 -77.794 103.868 -45.397 1.00 61.55 O ANISOU 1273 O GLY A 293 9766 5316 8305 902 3423 -498 O ATOM 1274 N LEU A 294 -79.550 103.268 -44.144 1.00 71.17 N ANISOU 1274 N LEU A 294 10614 6884 9542 930 3085 -437 N ATOM 1275 CA LEU A 294 -78.741 102.912 -42.994 1.00 81.23 C ANISOU 1275 CA LEU A 294 11916 8086 10860 787 3086 -523 C ATOM 1276 C LEU A 294 -78.591 101.394 -42.876 1.00 94.60 C ANISOU 1276 C LEU A 294 13392 9855 12694 876 2977 -333 C ATOM 1277 O LEU A 294 -79.146 100.636 -43.675 1.00104.94 O ANISOU 1277 O LEU A 294 14541 11287 14047 1020 2888 -151 O ATOM 1278 CB LEU A 294 -79.351 103.490 -41.718 1.00 68.84 C ANISOU 1278 CB LEU A 294 10320 6622 9215 648 2991 -677 C ATOM 1279 CG LEU A 294 -79.547 105.003 -41.726 1.00 70.31 C ANISOU 1279 CG LEU A 294 10718 6778 9220 519 3075 -883 C ATOM 1280 CD1 LEU A 294 -79.715 105.509 -40.306 1.00 75.43 C ANISOU 1280 CD1 LEU A 294 11388 7505 9767 295 3008 -1074 C ATOM 1281 CD2 LEU A 294 -78.372 105.681 -42.395 1.00 81.40 C ANISOU 1281 CD2 LEU A 294 12419 7940 10569 432 3278 -988 C ATOM 1282 N SER A 295 -77.828 100.959 -41.879 1.00 68.48 N ANISOU 1282 N SER A 295 10093 6482 9445 764 2979 -388 N ATOM 1283 CA SER A 295 -77.639 99.544 -41.612 1.00 59.03 C ANISOU 1283 CA SER A 295 8695 5364 8368 825 2871 -227 C ATOM 1284 C SER A 295 -78.959 98.896 -41.226 1.00 55.50 C ANISOU 1284 C SER A 295 7972 5175 7939 901 2632 -112 C ATOM 1285 O SER A 295 -79.656 99.387 -40.340 1.00 41.27 O ANISOU 1285 O SER A 295 6117 3460 6103 841 2552 -201 O ATOM 1286 CB SER A 295 -76.627 99.372 -40.484 1.00 80.57 C ANISOU 1286 CB SER A 295 11494 7971 11149 672 2918 -332 C ATOM 1287 OG SER A 295 -76.793 100.390 -39.511 1.00 82.33 O ANISOU 1287 OG SER A 295 11829 8160 11292 497 2926 -543 O ATOM 1288 N PRO A 296 -79.311 97.788 -41.897 1.00 58.72 N ANISOU 1288 N PRO A 296 8211 5714 8385 1012 2516 75 N ATOM 1289 CA PRO A 296 -80.590 97.150 -41.587 1.00 36.47 C ANISOU 1289 CA PRO A 296 5156 3142 5559 1049 2271 169 C ATOM 1290 C PRO A 296 -80.797 97.073 -40.089 1.00 48.16 C ANISOU 1290 C PRO A 296 6538 4688 7073 966 2170 107 C ATOM 1291 O PRO A 296 -79.871 96.686 -39.376 1.00 42.33 O ANISOU 1291 O PRO A 296 5824 3854 6406 901 2223 80 O ATOM 1292 CB PRO A 296 -80.432 95.747 -42.174 1.00 32.95 C ANISOU 1292 CB PRO A 296 4596 2775 5148 1098 2186 331 C ATOM 1293 CG PRO A 296 -79.541 95.972 -43.363 1.00 49.82 C ANISOU 1293 CG PRO A 296 6896 4747 7287 1151 2394 355 C ATOM 1294 CD PRO A 296 -78.553 97.040 -42.917 1.00 57.94 C ANISOU 1294 CD PRO A 296 8142 5551 8323 1079 2601 195 C ATOM 1295 N LEU A 297 -81.995 97.466 -39.641 1.00 61.43 N ANISOU 1295 N LEU A 297 8105 6529 8706 969 2035 87 N ATOM 1296 CA LEU A 297 -82.408 97.456 -38.238 1.00 37.46 C ANISOU 1296 CA LEU A 297 4944 3593 5697 901 1931 43 C ATOM 1297 C LEU A 297 -83.350 96.300 -37.981 1.00 35.29 C ANISOU 1297 C LEU A 297 4444 3546 5420 926 1666 181 C ATOM 1298 O LEU A 297 -84.277 96.069 -38.770 1.00 35.54 O ANISOU 1298 O LEU A 297 4422 3697 5385 973 1549 246 O ATOM 1299 CB LEU A 297 -83.135 98.754 -37.894 1.00 60.56 C ANISOU 1299 CB LEU A 297 7902 6565 8543 871 1973 -84 C ATOM 1300 CG LEU A 297 -83.766 98.771 -36.497 1.00 74.18 C ANISOU 1300 CG LEU A 297 9446 8453 10287 808 1861 -109 C ATOM 1301 CD1 LEU A 297 -82.690 99.025 -35.451 1.00 87.02 C ANISOU 1301 CD1 LEU A 297 11157 9936 11968 662 2019 -261 C ATOM 1302 CD2 LEU A 297 -84.891 99.803 -36.381 1.00 52.57 C ANISOU 1302 CD2 LEU A 297 6659 5870 7445 808 1838 -167 C ATOM 1303 N TYR A 298 -83.136 95.584 -36.879 1.00 24.83 N ANISOU 1303 N TYR A 298 3011 2271 4154 870 1574 206 N ATOM 1304 CA TYR A 298 -83.977 94.420 -36.565 1.00 33.86 C ANISOU 1304 CA TYR A 298 3997 3614 5254 854 1320 301 C ATOM 1305 C TYR A 298 -84.643 94.514 -35.206 1.00 22.19 C ANISOU 1305 C TYR A 298 2385 2274 3773 796 1181 282 C ATOM 1306 O TYR A 298 -84.099 95.061 -34.258 1.00 45.05 O ANISOU 1306 O TYR A 298 5253 5112 6752 753 1278 228 O ATOM 1307 CB TYR A 298 -83.188 93.109 -36.625 1.00 36.72 C ANISOU 1307 CB TYR A 298 4355 3929 5666 838 1320 394 C ATOM 1308 CG TYR A 298 -82.686 92.715 -37.993 1.00 58.63 C ANISOU 1308 CG TYR A 298 7224 6597 8456 898 1468 483 C ATOM 1309 CD1 TYR A 298 -83.443 91.902 -38.822 1.00 68.79 C ANISOU 1309 CD1 TYR A 298 8478 7943 9717 929 1459 635 C ATOM 1310 CD2 TYR A 298 -81.444 93.135 -38.447 1.00 85.03 C ANISOU 1310 CD2 TYR A 298 10696 9780 11832 916 1628 417 C ATOM 1311 CE1 TYR A 298 -82.985 91.531 -40.077 1.00 73.07 C ANISOU 1311 CE1 TYR A 298 9091 8406 10267 990 1603 730 C ATOM 1312 CE2 TYR A 298 -80.979 92.767 -39.700 1.00 98.94 C ANISOU 1312 CE2 TYR A 298 12536 11451 13605 976 1776 515 C ATOM 1313 CZ TYR A 298 -81.755 91.964 -40.509 1.00 89.75 C ANISOU 1313 CZ TYR A 298 11316 10366 12417 1018 1761 676 C ATOM 1314 OH TYR A 298 -81.302 91.596 -41.753 1.00 99.60 O ANISOU 1314 OH TYR A 298 12632 11539 13671 1085 1914 784 O ATOM 1315 N SER A 299 -85.833 93.952 -35.125 1.00 38.03 N ANISOU 1315 N SER A 299 4314 4422 5715 780 1015 353 N ATOM 1316 CA SER A 299 -86.636 94.006 -33.923 1.00 22.98 C ANISOU 1316 CA SER A 299 2296 2657 3776 722 867 345 C ATOM 1317 C SER A 299 -86.053 93.090 -32.856 1.00 23.87 C ANISOU 1317 C SER A 299 2361 2774 3936 659 804 382 C ATOM 1318 O SER A 299 -85.546 92.017 -33.179 1.00 34.36 O ANISOU 1318 O SER A 299 3726 4024 5306 660 840 469 O ATOM 1319 CB SER A 299 -88.065 93.575 -34.284 1.00 23.02 C ANISOU 1319 CB SER A 299 2288 2731 3727 723 790 451 C ATOM 1320 OG SER A 299 -88.924 93.546 -33.158 1.00 44.81 O ANISOU 1320 OG SER A 299 4973 5605 6448 663 659 459 O ATOM 1321 N PRO A 300 -86.113 93.514 -31.579 1.00 21.00 N ANISOU 1321 N PRO A 300 1903 2519 3556 599 717 324 N ATOM 1322 CA PRO A 300 -85.696 92.656 -30.473 1.00 17.80 C ANISOU 1322 CA PRO A 300 1449 2129 3184 535 643 372 C ATOM 1323 C PRO A 300 -86.656 91.487 -30.264 1.00 20.78 C ANISOU 1323 C PRO A 300 1845 2520 3528 512 556 500 C ATOM 1324 O PRO A 300 -86.280 90.497 -29.633 1.00 35.89 O ANISOU 1324 O PRO A 300 3759 4411 5468 473 526 560 O ATOM 1325 CB PRO A 300 -85.706 93.601 -29.265 1.00 28.64 C ANISOU 1325 CB PRO A 300 2690 3625 4567 460 607 324 C ATOM 1326 CG PRO A 300 -86.589 94.721 -29.654 1.00 29.52 C ANISOU 1326 CG PRO A 300 2772 3816 4630 479 626 285 C ATOM 1327 CD PRO A 300 -86.419 94.879 -31.126 1.00 28.89 C ANISOU 1327 CD PRO A 300 2811 3595 4570 581 767 271 C ATOM 1328 N PHE A 301 -87.873 91.590 -30.776 1.00 25.03 N ANISOU 1328 N PHE A 301 2406 3099 4005 530 533 536 N ATOM 1329 CA PHE A 301 -88.783 90.448 -30.736 1.00 27.89 C ANISOU 1329 CA PHE A 301 2800 3471 4326 502 496 645 C ATOM 1330 C PHE A 301 -89.079 89.985 -32.138 1.00 29.36 C ANISOU 1330 C PHE A 301 3039 3613 4502 546 574 708 C ATOM 1331 O PHE A 301 -89.470 90.785 -32.983 1.00 28.20 O ANISOU 1331 O PHE A 301 2907 3473 4335 593 610 682 O ATOM 1332 CB PHE A 301 -90.081 90.778 -29.992 1.00 31.43 C ANISOU 1332 CB PHE A 301 3228 4014 4701 469 411 654 C ATOM 1333 CG PHE A 301 -89.893 90.969 -28.520 1.00 28.41 C ANISOU 1333 CG PHE A 301 2795 3685 4313 417 335 630 C ATOM 1334 CD1 PHE A 301 -89.840 89.887 -27.673 1.00 32.91 C ANISOU 1334 CD1 PHE A 301 3382 4240 4883 374 307 696 C ATOM 1335 CD2 PHE A 301 -89.728 92.227 -27.992 1.00 37.64 C ANISOU 1335 CD2 PHE A 301 3894 4934 5473 407 299 543 C ATOM 1336 CE1 PHE A 301 -89.633 90.058 -26.325 1.00 32.03 C ANISOU 1336 CE1 PHE A 301 3229 4178 4763 330 245 689 C ATOM 1337 CE2 PHE A 301 -89.528 92.398 -26.644 1.00 39.70 C ANISOU 1337 CE2 PHE A 301 4099 5263 5721 348 231 534 C ATOM 1338 CZ PHE A 301 -89.484 91.314 -25.810 1.00 28.14 C ANISOU 1338 CZ PHE A 301 2665 3770 4257 316 204 614 C ATOM 1339 N SER A 302 -88.880 88.691 -32.379 1.00 23.79 N ANISOU 1339 N SER A 302 2358 2873 3806 530 603 793 N ATOM 1340 CA SER A 302 -89.029 88.118 -33.716 1.00 25.55 C ANISOU 1340 CA SER A 302 2619 3070 4019 569 685 867 C ATOM 1341 C SER A 302 -90.489 87.796 -34.118 1.00 19.85 C ANISOU 1341 C SER A 302 1909 2411 3221 562 660 925 C ATOM 1342 O SER A 302 -90.796 87.668 -35.297 1.00 25.42 O ANISOU 1342 O SER A 302 2638 3113 3907 603 722 977 O ATOM 1343 CB SER A 302 -88.139 86.880 -33.868 1.00 34.05 C ANISOU 1343 CB SER A 302 3706 4097 5136 559 736 935 C ATOM 1344 OG SER A 302 -88.610 85.785 -33.092 1.00 51.49 O ANISOU 1344 OG SER A 302 5905 6344 7316 502 680 984 O ATOM 1345 N GLN A 303 -91.381 87.657 -33.148 1.00 32.83 N ANISOU 1345 N GLN A 303 3539 4110 4824 511 581 921 N ATOM 1346 CA GLN A 303 -92.798 87.488 -33.474 1.00 34.36 C ANISOU 1346 CA GLN A 303 3747 4357 4951 503 566 964 C ATOM 1347 C GLN A 303 -93.720 87.730 -32.297 1.00 25.62 C ANISOU 1347 C GLN A 303 2628 3301 3805 457 490 943 C ATOM 1348 O GLN A 303 -93.379 87.466 -31.152 1.00 39.15 O ANISOU 1348 O GLN A 303 4329 5014 5533 418 448 928 O ATOM 1349 CB GLN A 303 -93.092 86.108 -34.066 1.00 27.36 C ANISOU 1349 CB GLN A 303 2879 3470 4046 495 604 1052 C ATOM 1350 CG GLN A 303 -92.923 84.982 -33.109 1.00 25.25 C ANISOU 1350 CG GLN A 303 2610 3201 3785 443 575 1074 C ATOM 1351 CD GLN A 303 -93.420 83.688 -33.685 1.00 47.32 C ANISOU 1351 CD GLN A 303 5419 6020 6540 440 569 1080 C ATOM 1352 OE1 GLN A 303 -92.662 82.716 -33.814 1.00 51.23 O ANISOU 1352 OE1 GLN A 303 5915 6498 7053 441 584 1088 O ATOM 1353 NE2 GLN A 303 -94.710 83.654 -34.038 1.00 39.46 N ANISOU 1353 NE2 GLN A 303 4433 5067 5493 438 548 1074 N ATOM 1354 N PHE A 304 -94.900 88.245 -32.599 1.00 25.48 N ANISOU 1354 N PHE A 304 2616 3329 3738 465 479 950 N ATOM 1355 CA PHE A 304 -95.875 88.497 -31.577 1.00 14.82 C ANISOU 1355 CA PHE A 304 1258 2026 2347 428 425 945 C ATOM 1356 C PHE A 304 -97.077 87.599 -31.879 1.00 33.54 C ANISOU 1356 C PHE A 304 3653 4412 4677 408 440 1011 C ATOM 1357 O PHE A 304 -97.797 87.821 -32.840 1.00 33.08 O ANISOU 1357 O PHE A 304 3604 4372 4592 435 467 1036 O ATOM 1358 CB PHE A 304 -96.270 89.969 -31.591 1.00 18.79 C ANISOU 1358 CB PHE A 304 1740 2572 2828 454 401 895 C ATOM 1359 CG PHE A 304 -96.969 90.406 -30.325 1.00 22.72 C ANISOU 1359 CG PHE A 304 2220 3122 3292 417 346 888 C ATOM 1360 CD1 PHE A 304 -98.342 90.252 -30.180 1.00 12.77 C ANISOU 1360 CD1 PHE A 304 974 1894 1982 399 343 937 C ATOM 1361 CD2 PHE A 304 -96.248 90.928 -29.276 1.00 25.28 C ANISOU 1361 CD2 PHE A 304 2509 3462 3633 401 303 842 C ATOM 1362 CE1 PHE A 304 -98.971 90.618 -29.019 1.00 21.17 C ANISOU 1362 CE1 PHE A 304 2024 3003 3016 370 307 947 C ATOM 1363 CE2 PHE A 304 -96.871 91.305 -28.117 1.00 14.46 C ANISOU 1363 CE2 PHE A 304 1120 2147 2226 369 260 855 C ATOM 1364 CZ PHE A 304 -98.239 91.154 -27.991 1.00 37.58 C ANISOU 1364 CZ PHE A 304 4068 5103 5106 356 266 911 C ATOM 1365 N TYR A 305 -97.263 86.565 -31.063 1.00 34.38 N ANISOU 1365 N TYR A 305 3768 4513 4781 366 419 1023 N ATOM 1366 CA TYR A 305 -98.331 85.588 -31.242 1.00 16.21 C ANISOU 1366 CA TYR A 305 1487 2223 2447 349 401 1002 C ATOM 1367 C TYR A 305 -99.435 85.949 -30.321 1.00 16.49 C ANISOU 1367 C TYR A 305 1523 2287 2454 324 365 988 C ATOM 1368 O TYR A 305 -99.188 86.137 -29.137 1.00 34.56 O ANISOU 1368 O TYR A 305 3803 4578 4749 302 340 983 O ATOM 1369 CB TYR A 305 -97.873 84.202 -30.820 1.00 30.65 C ANISOU 1369 CB TYR A 305 3328 4030 4290 325 388 983 C ATOM 1370 CG TYR A 305 -98.917 83.154 -31.066 1.00 39.54 C ANISOU 1370 CG TYR A 305 4470 5167 5388 313 376 968 C ATOM 1371 CD1 TYR A 305 -99.910 82.904 -30.133 1.00 39.69 C ANISOU 1371 CD1 TYR A 305 4497 5196 5388 285 343 945 C ATOM 1372 CD2 TYR A 305 -98.929 82.434 -32.249 1.00 55.46 C ANISOU 1372 CD2 TYR A 305 6490 7184 7398 334 401 983 C ATOM 1373 CE1 TYR A 305 -100.882 81.954 -30.364 1.00 35.08 C ANISOU 1373 CE1 TYR A 305 3925 4617 4788 276 336 935 C ATOM 1374 CE2 TYR A 305 -99.893 81.483 -32.493 1.00 66.68 C ANISOU 1374 CE2 TYR A 305 7920 8618 8797 324 389 975 C ATOM 1375 CZ TYR A 305 -100.868 81.244 -31.551 1.00 61.05 C ANISOU 1375 CZ TYR A 305 7215 7909 8072 295 357 949 C ATOM 1376 OH TYR A 305 -101.827 80.288 -31.807 1.00 80.03 O ANISOU 1376 OH TYR A 305 9624 10322 10462 288 350 945 O ATOM 1377 N VAL A 306 -100.650 86.051 -30.851 1.00 31.97 N ANISOU 1377 N VAL A 306 3492 4269 4387 329 365 987 N ATOM 1378 CA VAL A 306 -101.822 86.410 -30.045 1.00 20.95 C ANISOU 1378 CA VAL A 306 2096 2897 2967 310 339 978 C ATOM 1379 C VAL A 306 -102.732 85.202 -29.915 1.00 20.06 C ANISOU 1379 C VAL A 306 2001 2770 2850 288 325 956 C ATOM 1380 O VAL A 306 -103.078 84.584 -30.922 1.00 27.14 O ANISOU 1380 O VAL A 306 2906 3662 3743 298 339 958 O ATOM 1381 CB VAL A 306 -102.621 87.568 -30.683 1.00 19.30 C ANISOU 1381 CB VAL A 306 1879 2723 2733 334 351 999 C ATOM 1382 CG1 VAL A 306 -103.924 87.753 -29.966 1.00 26.50 C ANISOU 1382 CG1 VAL A 306 2790 3653 3625 314 329 993 C ATOM 1383 CG2 VAL A 306 -101.835 88.848 -30.615 1.00 36.33 C ANISOU 1383 CG2 VAL A 306 4013 4905 4887 358 362 1024 C ATOM 1384 N TYR A 307 -103.089 84.851 -28.676 1.00 37.28 N ANISOU 1384 N TYR A 307 4186 4947 5032 261 301 942 N ATOM 1385 CA TYR A 307 -104.096 83.813 -28.411 1.00 25.14 C ANISOU 1385 CA TYR A 307 2662 3397 3492 244 291 925 C ATOM 1386 C TYR A 307 -105.512 84.382 -28.569 1.00 30.46 C ANISOU 1386 C TYR A 307 3333 4088 4153 247 291 934 C ATOM 1387 O TYR A 307 -106.146 84.795 -27.591 1.00 49.16 O ANISOU 1387 O TYR A 307 5696 6465 6519 236 279 939 O ATOM 1388 CB TYR A 307 -103.902 83.247 -27.006 1.00 22.41 C ANISOU 1388 CB TYR A 307 2320 3040 3156 222 273 913 C ATOM 1389 CG TYR A 307 -102.660 82.420 -26.880 1.00 28.19 C ANISOU 1389 CG TYR A 307 3056 3754 3902 218 273 904 C ATOM 1390 CD1 TYR A 307 -102.702 81.058 -27.088 1.00 36.00 C ANISOU 1390 CD1 TYR A 307 4057 4727 4893 214 274 891 C ATOM 1391 CD2 TYR A 307 -101.443 82.999 -26.593 1.00 27.85 C ANISOU 1391 CD2 TYR A 307 3001 3710 3870 221 274 914 C ATOM 1392 CE1 TYR A 307 -101.580 80.296 -27.003 1.00 28.94 C ANISOU 1392 CE1 TYR A 307 3166 3821 4011 212 277 887 C ATOM 1393 CE2 TYR A 307 -100.305 82.238 -26.491 1.00 31.58 C ANISOU 1393 CE2 TYR A 307 3476 4163 4360 218 276 908 C ATOM 1394 CZ TYR A 307 -100.377 80.885 -26.699 1.00 30.04 C ANISOU 1394 CZ TYR A 307 3295 3955 4164 214 278 894 C ATOM 1395 OH TYR A 307 -99.245 80.104 -26.603 1.00 26.41 O ANISOU 1395 OH TYR A 307 2835 3480 3719 213 282 893 O ATOM 1396 N HIS A 308 -105.998 84.415 -29.802 1.00 25.55 N ANISOU 1396 N HIS A 308 3349 2868 3489 -253 174 -261 N ATOM 1397 CA HIS A 308 -107.296 85.034 -30.098 1.00 36.07 C ANISOU 1397 CA HIS A 308 4713 4152 4839 -240 257 -210 C ATOM 1398 C HIS A 308 -108.436 84.405 -29.349 1.00 21.63 C ANISOU 1398 C HIS A 308 2879 2220 3121 -242 382 -192 C ATOM 1399 O HIS A 308 -109.238 85.106 -28.754 1.00 43.88 O ANISOU 1399 O HIS A 308 5708 4990 5975 -196 426 -100 O ATOM 1400 CB HIS A 308 -107.610 84.980 -31.584 1.00 34.61 C ANISOU 1400 CB HIS A 308 4555 3998 4599 -289 276 -282 C ATOM 1401 CG HIS A 308 -106.807 85.940 -32.392 1.00 31.45 C ANISOU 1401 CG HIS A 308 4170 3692 4086 -276 167 -274 C ATOM 1402 ND1 HIS A 308 -105.810 85.530 -33.260 1.00 33.22 N ANISOU 1402 ND1 HIS A 308 4390 3992 4242 -319 93 -364 N ATOM 1403 CD2 HIS A 308 -106.836 87.287 -32.466 1.00 36.55 C ANISOU 1403 CD2 HIS A 308 4840 4371 4677 -224 117 -187 C ATOM 1404 CE1 HIS A 308 -105.270 86.585 -33.831 1.00 51.77 C ANISOU 1404 CE1 HIS A 308 6756 6415 6499 -295 4 -333 C ATOM 1405 NE2 HIS A 308 -105.875 87.670 -33.367 1.00 62.29 N ANISOU 1405 NE2 HIS A 308 8107 7724 7837 -236 16 -225 N ATOM 1406 N GLU A 309 -108.510 83.080 -29.388 1.00 30.27 N ANISOU 1406 N GLU A 309 3956 3279 4267 -294 438 -282 N ATOM 1407 CA GLU A 309 -109.608 82.376 -28.744 1.00 29.50 C ANISOU 1407 CA GLU A 309 3853 3081 4275 -302 560 -276 C ATOM 1408 C GLU A 309 -109.602 82.677 -27.252 1.00 38.86 C ANISOU 1408 C GLU A 309 5020 4225 5521 -243 559 -180 C ATOM 1409 O GLU A 309 -110.628 83.062 -26.701 1.00 27.86 O ANISOU 1409 O GLU A 309 3636 2765 4184 -212 635 -106 O ATOM 1410 CB GLU A 309 -109.551 80.867 -29.010 1.00 25.21 C ANISOU 1410 CB GLU A 309 3293 2513 3773 -367 609 -393 C ATOM 1411 CG GLU A 309 -110.738 80.089 -28.449 1.00 80.83 C ANISOU 1411 CG GLU A 309 10333 9452 10927 -380 740 -395 C ATOM 1412 CD GLU A 309 -110.680 78.601 -28.767 1.00107.68 C ANISOU 1412 CD GLU A 309 13720 12830 14364 -444 786 -515 C ATOM 1413 OE1 GLU A 309 -109.580 78.011 -28.682 1.00116.19 O ANISOU 1413 OE1 GLU A 309 14774 13965 15409 -453 713 -564 O ATOM 1414 OE2 GLU A 309 -111.734 78.021 -29.110 1.00110.37 O ANISOU 1414 OE2 GLU A 309 14060 13142 14734 -460 873 -538 O ATOM 1415 N ASN A 310 -108.443 82.524 -26.604 1.00 35.88 N ANISOU 1415 N ASN A 310 4615 3887 5130 -226 473 -178 N ATOM 1416 CA ASN A 310 -108.352 82.831 -25.180 1.00 20.53 C ANISOU 1416 CA ASN A 310 2652 1908 3241 -169 465 -86 C ATOM 1417 C ASN A 310 -108.778 84.246 -24.857 1.00 21.71 C ANISOU 1417 C ASN A 310 2820 2057 3371 -105 447 32 C ATOM 1418 O ASN A 310 -109.437 84.467 -23.863 1.00 28.78 O ANISOU 1418 O ASN A 310 3712 2888 4335 -66 501 110 O ATOM 1419 CB ASN A 310 -106.949 82.608 -24.637 1.00 23.66 C ANISOU 1419 CB ASN A 310 3018 2359 3615 -158 361 -99 C ATOM 1420 CG ASN A 310 -106.533 81.171 -24.708 1.00 34.83 C ANISOU 1420 CG ASN A 310 4410 3763 5061 -212 384 -205 C ATOM 1421 OD1 ASN A 310 -107.350 80.309 -24.997 1.00 39.79 O ANISOU 1421 OD1 ASN A 310 5044 4335 5739 -254 482 -262 O ATOM 1422 ND2 ASN A 310 -105.261 80.896 -24.451 1.00 59.57 N ANISOU 1422 ND2 ASN A 310 7517 6950 8165 -211 293 -232 N ATOM 1423 N ILE A 311 -108.370 85.208 -25.680 1.00 31.86 N ANISOU 1423 N ILE A 311 4127 3416 4562 -93 369 46 N ATOM 1424 CA ILE A 311 -108.720 86.606 -25.442 1.00 28.98 C ANISOU 1424 CA ILE A 311 3784 3058 4170 -30 345 157 C ATOM 1425 C ILE A 311 -110.229 86.838 -25.535 1.00 19.29 C ANISOU 1425 C ILE A 311 2581 1755 2991 -25 464 197 C ATOM 1426 O ILE A 311 -110.816 87.529 -24.713 1.00 18.46 O ANISOU 1426 O ILE A 311 2482 1606 2924 29 492 296 O ATOM 1427 CB ILE A 311 -107.934 87.555 -26.376 1.00 25.64 C ANISOU 1427 CB ILE A 311 3378 2732 3630 -21 234 156 C ATOM 1428 CG1 ILE A 311 -106.472 87.604 -25.921 1.00 34.14 C ANISOU 1428 CG1 ILE A 311 4428 3875 4669 -3 111 153 C ATOM 1429 CG2 ILE A 311 -108.505 88.959 -26.355 1.00 17.14 C ANISOU 1429 CG2 ILE A 311 2333 1657 2523 38 227 261 C ATOM 1430 CD1 ILE A 311 -105.544 88.315 -26.860 1.00 22.53 C ANISOU 1430 CD1 ILE A 311 2970 2504 3086 -3 -3 133 C ATOM 1431 N ASP A 312 -110.847 86.247 -26.541 1.00 19.51 N ANISOU 1431 N ASP A 312 2625 1768 3021 -82 533 120 N ATOM 1432 CA ASP A 312 -112.276 86.353 -26.716 1.00 18.40 C ANISOU 1432 CA ASP A 312 2507 1555 2931 -84 651 147 C ATOM 1433 C ASP A 312 -113.012 85.731 -25.509 1.00 35.04 C ANISOU 1433 C ASP A 312 4595 3565 5152 -72 744 180 C ATOM 1434 O ASP A 312 -113.989 86.286 -25.010 1.00 47.34 O ANISOU 1434 O ASP A 312 6166 5065 6755 -34 810 263 O ATOM 1435 CB ASP A 312 -112.679 85.670 -28.014 1.00 18.12 C ANISOU 1435 CB ASP A 312 2486 1521 2879 -153 703 44 C ATOM 1436 CG ASP A 312 -112.442 86.536 -29.210 1.00 31.18 C ANISOU 1436 CG ASP A 312 4168 3247 4431 -155 644 38 C ATOM 1437 OD1 ASP A 312 -112.171 87.736 -29.007 1.00 51.18 O ANISOU 1437 OD1 ASP A 312 6714 5819 6913 -99 577 124 O ATOM 1438 OD2 ASP A 312 -112.541 86.035 -30.353 1.00 37.57 O ANISOU 1438 OD2 ASP A 312 4987 4075 5212 -212 664 -51 O ATOM 1439 N LEU A 313 -112.528 84.580 -25.055 1.00 28.59 N ANISOU 1439 N LEU A 313 3749 2733 4381 -103 749 116 N ATOM 1440 CA LEU A 313 -113.039 83.903 -23.887 1.00 19.08 C ANISOU 1440 CA LEU A 313 2524 1445 3282 -94 826 140 C ATOM 1441 C LEU A 313 -112.914 84.779 -22.655 1.00 27.56 C ANISOU 1441 C LEU A 313 3589 2506 4375 -20 791 259 C ATOM 1442 O LEU A 313 -113.855 84.881 -21.867 1.00 39.91 O ANISOU 1442 O LEU A 313 5155 3996 6015 8 872 325 O ATOM 1443 CB LEU A 313 -112.289 82.601 -23.672 1.00 29.92 C ANISOU 1443 CB LEU A 313 3866 2821 4681 -136 813 49 C ATOM 1444 CG LEU A 313 -113.100 81.336 -23.403 1.00 68.00 C ANISOU 1444 CG LEU A 313 8679 7559 9601 -177 931 -7 C ATOM 1445 CD1 LEU A 313 -114.405 81.342 -24.189 1.00 73.05 C ANISOU 1445 CD1 LEU A 313 9345 8150 10261 -204 1034 -23 C ATOM 1446 CD2 LEU A 313 -112.266 80.093 -23.720 1.00 71.24 C ANISOU 1446 CD2 LEU A 313 9068 7996 10004 -231 905 -122 C ATOM 1447 N VAL A 314 -111.769 85.429 -22.486 1.00 21.41 N ANISOU 1447 N VAL A 314 2802 1803 3531 12 669 289 N ATOM 1448 CA VAL A 314 -111.563 86.320 -21.349 1.00 19.52 C ANISOU 1448 CA VAL A 314 2555 1558 3304 84 624 401 C ATOM 1449 C VAL A 314 -112.449 87.576 -21.426 1.00 23.20 C ANISOU 1449 C VAL A 314 3053 2008 3754 133 650 498 C ATOM 1450 O VAL A 314 -113.005 88.014 -20.424 1.00 33.53 O ANISOU 1450 O VAL A 314 4360 3263 5118 182 686 588 O ATOM 1451 CB VAL A 314 -110.081 86.727 -21.174 1.00 18.92 C ANISOU 1451 CB VAL A 314 2461 1567 3161 108 482 408 C ATOM 1452 CG1 VAL A 314 -109.948 87.789 -20.107 1.00 21.30 C ANISOU 1452 CG1 VAL A 314 2758 1865 3470 185 434 528 C ATOM 1453 CG2 VAL A 314 -109.225 85.526 -20.812 1.00 18.36 C ANISOU 1453 CG2 VAL A 314 2354 1501 3120 72 461 331 C ATOM 1454 N ARG A 315 -112.591 88.167 -22.598 1.00 27.60 N ANISOU 1454 N ARG A 315 3641 2612 4236 120 632 481 N ATOM 1455 CA ARG A 315 -113.333 89.418 -22.669 1.00 38.38 C ANISOU 1455 CA ARG A 315 5037 3968 5578 171 646 575 C ATOM 1456 C ARG A 315 -114.792 89.191 -22.385 1.00 29.93 C ANISOU 1456 C ARG A 315 3978 2801 4593 170 784 605 C ATOM 1457 O ARG A 315 -115.416 89.986 -21.693 1.00 42.97 O ANISOU 1457 O ARG A 315 5640 4414 6272 226 812 706 O ATOM 1458 CB ARG A 315 -113.220 90.074 -24.038 1.00 35.02 C ANISOU 1458 CB ARG A 315 4643 3609 5054 157 604 548 C ATOM 1459 CG ARG A 315 -111.848 90.577 -24.401 1.00 40.97 C ANISOU 1459 CG ARG A 315 5392 4463 5710 167 462 534 C ATOM 1460 CD ARG A 315 -111.636 90.271 -25.851 1.00 40.11 C ANISOU 1460 CD ARG A 315 5299 4407 5534 109 449 438 C ATOM 1461 NE ARG A 315 -111.056 91.385 -26.568 1.00 48.05 N ANISOU 1461 NE ARG A 315 6328 5496 6434 135 351 464 N ATOM 1462 CZ ARG A 315 -110.894 91.408 -27.882 1.00 41.76 C ANISOU 1462 CZ ARG A 315 5550 4751 5565 95 330 397 C ATOM 1463 NH1 ARG A 315 -111.291 90.383 -28.631 1.00 20.50 N ANISOU 1463 NH1 ARG A 315 2856 2035 2896 27 402 301 N ATOM 1464 NH2 ARG A 315 -110.340 92.465 -28.441 1.00 53.24 N ANISOU 1464 NH2 ARG A 315 7025 6280 6923 125 238 428 N ATOM 1465 N GLN A 316 -115.334 88.122 -22.966 1.00 34.48 N ANISOU 1465 N GLN A 316 4552 3339 5209 106 870 516 N ATOM 1466 CA GLN A 316 -116.740 87.788 -22.825 1.00 29.08 C ANISOU 1466 CA GLN A 316 3878 2563 4608 96 1006 530 C ATOM 1467 C GLN A 316 -117.020 87.717 -21.347 1.00 32.16 C ANISOU 1467 C GLN A 316 4248 2888 5084 139 1041 605 C ATOM 1468 O GLN A 316 -117.907 88.381 -20.827 1.00 47.61 O ANISOU 1468 O GLN A 316 6219 4794 7077 183 1097 694 O ATOM 1469 CB GLN A 316 -117.025 86.432 -23.467 1.00 36.90 C ANISOU 1469 CB GLN A 316 4859 3524 5636 18 1077 412 C ATOM 1470 CG GLN A 316 -118.503 86.181 -23.777 1.00 44.19 C ANISOU 1470 CG GLN A 316 5800 4366 6625 -3 1213 410 C ATOM 1471 CD GLN A 316 -119.102 87.281 -24.626 1.00 44.90 C ANISOU 1471 CD GLN A 316 5926 4475 6659 17 1222 455 C ATOM 1472 OE1 GLN A 316 -118.492 87.728 -25.602 1.00 39.11 O ANISOU 1472 OE1 GLN A 316 5208 3818 5834 6 1147 425 O ATOM 1473 NE2 GLN A 316 -120.294 87.744 -24.243 1.00 53.48 N ANISOU 1473 NE2 GLN A 316 7029 5492 7801 49 1312 532 N ATOM 1474 N MET A 317 -116.212 86.919 -20.671 1.00 38.51 N ANISOU 1474 N MET A 317 5019 3696 5917 126 1005 569 N ATOM 1475 CA MET A 317 -116.320 86.728 -19.241 1.00 40.58 C ANISOU 1475 CA MET A 317 5257 3900 6260 163 1030 631 C ATOM 1476 C MET A 317 -116.453 88.057 -18.498 1.00 33.28 C ANISOU 1476 C MET A 317 4344 2977 5324 242 995 760 C ATOM 1477 O MET A 317 -117.339 88.215 -17.661 1.00 36.89 O ANISOU 1477 O MET A 317 4802 3362 5853 274 1071 831 O ATOM 1478 CB MET A 317 -115.110 85.942 -18.745 1.00 42.90 C ANISOU 1478 CB MET A 317 5517 4226 6558 147 960 580 C ATOM 1479 CG MET A 317 -115.351 85.120 -17.498 1.00 41.16 C ANISOU 1479 CG MET A 317 5268 3931 6441 153 1021 594 C ATOM 1480 SD MET A 317 -113.840 83.922 -17.171 1.00 96.16 S ANISOU 1480 SD MET A 317 12192 10939 13406 118 942 503 S ATOM 1481 CE MET A 317 -114.454 83.118 -15.498 1.00166.86 C ANISOU 1481 CE MET A 317 21118 19784 22499 138 1039 548 C ATOM 1482 N ILE A 318 -115.585 89.009 -18.803 1.00 22.79 N ANISOU 1482 N ILE A 318 3024 1731 3905 273 880 789 N ATOM 1483 CA ILE A 318 -115.576 90.294 -18.104 1.00 23.61 C ANISOU 1483 CA ILE A 318 3137 1843 3991 351 832 908 C ATOM 1484 C ILE A 318 -116.720 91.216 -18.551 1.00 35.12 C ANISOU 1484 C ILE A 318 4634 3275 5436 377 894 971 C ATOM 1485 O ILE A 318 -117.244 92.004 -17.766 1.00 43.66 O ANISOU 1485 O ILE A 318 5723 4321 6544 437 912 1073 O ATOM 1486 CB ILE A 318 -114.266 91.036 -18.325 1.00 26.68 C ANISOU 1486 CB ILE A 318 3525 2330 4285 376 685 918 C ATOM 1487 CG1 ILE A 318 -113.090 90.243 -17.748 1.00 44.98 C ANISOU 1487 CG1 ILE A 318 5802 4673 6617 360 618 870 C ATOM 1488 CG2 ILE A 318 -114.325 92.413 -17.704 1.00 39.03 C ANISOU 1488 CG2 ILE A 318 5102 3902 5824 457 637 1039 C ATOM 1489 CD1 ILE A 318 -111.722 90.671 -18.315 1.00 31.89 C ANISOU 1489 CD1 ILE A 318 4140 3118 4858 361 477 840 C ATOM 1490 N TYR A 319 -117.085 91.115 -19.821 1.00 31.73 N ANISOU 1490 N TYR A 319 4228 2864 4964 334 924 909 N ATOM 1491 CA TYR A 319 -118.208 91.855 -20.370 1.00 24.32 C ANISOU 1491 CA TYR A 319 3325 1898 4016 351 993 956 C ATOM 1492 C TYR A 319 -119.488 91.427 -19.666 1.00 33.37 C ANISOU 1492 C TYR A 319 4469 2939 5271 353 1127 991 C ATOM 1493 O TYR A 319 -120.220 92.267 -19.137 1.00 51.11 O ANISOU 1493 O TYR A 319 6732 5149 7539 408 1163 1089 O ATOM 1494 CB TYR A 319 -118.333 91.552 -21.852 1.00 25.27 C ANISOU 1494 CB TYR A 319 3465 2051 4084 291 1010 866 C ATOM 1495 CG TYR A 319 -119.448 92.278 -22.536 1.00 28.66 C ANISOU 1495 CG TYR A 319 3932 2457 4501 304 1080 906 C ATOM 1496 CD1 TYR A 319 -119.336 93.616 -22.829 1.00 41.33 C ANISOU 1496 CD1 TYR A 319 5566 4110 6028 357 1018 979 C ATOM 1497 CD2 TYR A 319 -120.607 91.622 -22.904 1.00 50.82 C ANISOU 1497 CD2 TYR A 319 6745 5192 7372 263 1207 870 C ATOM 1498 CE1 TYR A 319 -120.356 94.290 -23.457 1.00 41.80 C ANISOU 1498 CE1 TYR A 319 5661 4148 6075 371 1084 1018 C ATOM 1499 CE2 TYR A 319 -121.632 92.293 -23.540 1.00 45.08 C ANISOU 1499 CE2 TYR A 319 6052 4442 6636 276 1273 908 C ATOM 1500 CZ TYR A 319 -121.494 93.627 -23.811 1.00 27.87 C ANISOU 1500 CZ TYR A 319 3901 2311 4377 330 1212 983 C ATOM 1501 OH TYR A 319 -122.491 94.316 -24.446 1.00 52.26 O ANISOU 1501 OH TYR A 319 7024 5378 7453 345 1276 1023 O ATOM 1502 N ASP A 320 -119.744 90.118 -19.665 1.00 27.62 N ANISOU 1502 N ASP A 320 3721 2164 4610 295 1200 909 N ATOM 1503 CA ASP A 320 -120.909 89.536 -18.996 1.00 42.36 C ANISOU 1503 CA ASP A 320 5581 3929 6585 290 1329 928 C ATOM 1504 C ASP A 320 -120.970 89.951 -17.537 1.00 41.29 C ANISOU 1504 C ASP A 320 5424 3775 6489 351 1314 1016 C ATOM 1505 O ASP A 320 -121.908 90.655 -17.115 1.00 35.60 O ANISOU 1505 O ASP A 320 4709 3040 5777 391 1355 1081 O ATOM 1506 CB ASP A 320 -120.920 88.007 -19.100 1.00 35.72 C ANISOU 1506 CB ASP A 320 4716 3053 5804 220 1386 820 C ATOM 1507 CG ASP A 320 -121.009 87.522 -20.531 1.00 48.69 C ANISOU 1507 CG ASP A 320 6373 4723 7405 154 1403 717 C ATOM 1508 OD1 ASP A 320 -120.806 86.311 -20.775 1.00 59.22 O ANISOU 1508 OD1 ASP A 320 7687 6045 8767 95 1428 617 O ATOM 1509 OD2 ASP A 320 -121.271 88.362 -21.417 1.00 54.34 O ANISOU 1509 OD2 ASP A 320 7118 5472 8057 163 1392 735 O ATOM 1510 N THR A 321 -119.973 89.517 -16.772 1.00 28.25 N ANISOU 1510 N THR A 321 3743 2139 4850 355 1249 1007 N ATOM 1511 CA THR A 321 -119.873 89.902 -15.368 1.00 48.10 C ANISOU 1511 CA THR A 321 6230 4660 7387 409 1215 1076 C ATOM 1512 C THR A 321 -120.278 91.355 -15.188 1.00 45.71 C ANISOU 1512 C THR A 321 5950 4380 7040 473 1187 1175 C ATOM 1513 O THR A 321 -121.157 91.677 -14.394 1.00 36.94 O ANISOU 1513 O THR A 321 4829 3245 5961 503 1235 1222 O ATOM 1514 CB THR A 321 -118.434 89.740 -14.823 1.00 33.98 C ANISOU 1514 CB THR A 321 4417 2910 5583 421 1107 1074 C ATOM 1515 OG1 THR A 321 -118.142 88.353 -14.652 1.00 49.35 O ANISOU 1515 OG1 THR A 321 6336 4834 7583 368 1137 988 O ATOM 1516 CG2 THR A 321 -118.303 90.415 -13.484 1.00 42.74 C ANISOU 1516 CG2 THR A 321 5504 4037 6697 480 1058 1153 C ATOM 1517 N GLU A 322 -119.636 92.244 -15.928 1.00 30.38 N ANISOU 1517 N GLU A 322 4037 2487 5019 496 1107 1205 N ATOM 1518 CA GLU A 322 -119.906 93.642 -15.703 1.00 29.90 C ANISOU 1518 CA GLU A 322 3994 2458 4906 560 1067 1294 C ATOM 1519 C GLU A 322 -121.284 94.156 -16.153 1.00 27.55 C ANISOU 1519 C GLU A 322 3724 2130 4613 567 1159 1321 C ATOM 1520 O GLU A 322 -121.843 95.019 -15.513 1.00 33.70 O ANISOU 1520 O GLU A 322 4505 2913 5387 615 1160 1388 O ATOM 1521 CB GLU A 322 -118.790 94.488 -16.264 1.00 26.34 C ANISOU 1521 CB GLU A 322 3562 2080 4364 588 944 1319 C ATOM 1522 CG GLU A 322 -118.057 95.197 -15.173 1.00 26.44 C ANISOU 1522 CG GLU A 322 3553 2142 4351 640 840 1372 C ATOM 1523 CD GLU A 322 -118.063 96.681 -15.389 1.00 45.75 C ANISOU 1523 CD GLU A 322 6026 4643 6712 694 772 1436 C ATOM 1524 OE1 GLU A 322 -118.342 97.124 -16.526 1.00 51.84 O ANISOU 1524 OE1 GLU A 322 6835 5429 7433 691 784 1437 O ATOM 1525 OE2 GLU A 322 -117.800 97.409 -14.421 1.00 51.87 O ANISOU 1525 OE2 GLU A 322 6788 5450 7471 736 707 1480 O ATOM 1526 N MET A 323 -121.815 93.647 -17.254 1.00 27.41 N ANISOU 1526 N MET A 323 3727 2084 4602 519 1233 1266 N ATOM 1527 CA MET A 323 -123.140 94.055 -17.678 1.00 29.12 C ANISOU 1527 CA MET A 323 3966 2270 4828 523 1324 1286 C ATOM 1528 C MET A 323 -124.143 93.743 -16.585 1.00 47.48 C ANISOU 1528 C MET A 323 6263 4548 7231 534 1404 1302 C ATOM 1529 O MET A 323 -125.037 94.534 -16.299 1.00 62.70 O ANISOU 1529 O MET A 323 8199 6465 9158 573 1439 1362 O ATOM 1530 CB MET A 323 -123.524 93.323 -18.958 1.00 56.32 C ANISOU 1530 CB MET A 323 7429 5690 8279 458 1396 1206 C ATOM 1531 CG MET A 323 -122.690 93.750 -20.153 1.00 63.20 C ANISOU 1531 CG MET A 323 8337 6608 9069 449 1328 1196 C ATOM 1532 SD MET A 323 -122.445 95.699 -20.166 1.00 97.94 S ANISOU 1532 SD MET A 323 12771 11077 13365 540 1229 1315 S ATOM 1533 CE MET A 323 -120.627 95.778 -19.394 1.00 49.63 C ANISOU 1533 CE MET A 323 6622 5033 7202 567 1064 1320 C ATOM 1534 N ARG A 324 -123.979 92.575 -15.976 1.00 33.96 N ANISOU 1534 N ARG A 324 4514 2807 5582 499 1430 1247 N ATOM 1535 CA ARG A 324 -124.755 92.203 -14.826 1.00 33.53 C ANISOU 1535 CA ARG A 324 4428 2714 5598 510 1492 1262 C ATOM 1536 C ARG A 324 -124.509 93.121 -13.625 1.00 44.46 C ANISOU 1536 C ARG A 324 5801 4122 6970 573 1430 1348 C ATOM 1537 O ARG A 324 -125.441 93.733 -13.110 1.00 53.39 O ANISOU 1537 O ARG A 324 6933 5235 8117 608 1474 1403 O ATOM 1538 CB ARG A 324 -124.474 90.762 -14.438 1.00 28.86 C ANISOU 1538 CB ARG A 324 3802 2098 5067 461 1519 1182 C ATOM 1539 CG ARG A 324 -125.099 90.395 -13.111 1.00 38.43 C ANISOU 1539 CG ARG A 324 4977 3276 6346 478 1569 1203 C ATOM 1540 CD ARG A 324 -124.247 89.384 -12.411 1.00 44.49 C ANISOU 1540 CD ARG A 324 5711 4048 7147 455 1536 1157 C ATOM 1541 NE ARG A 324 -123.725 88.437 -13.384 1.00 51.06 N ANISOU 1541 NE ARG A 324 6546 4883 7971 396 1536 1063 N ATOM 1542 CZ ARG A 324 -122.789 87.540 -13.112 1.00 63.96 C ANISOU 1542 CZ ARG A 324 8156 6528 9619 368 1496 1009 C ATOM 1543 NH1 ARG A 324 -122.291 87.489 -11.886 1.00 44.83 N ANISOU 1543 NH1 ARG A 324 5703 4112 7217 395 1455 1044 N ATOM 1544 NH2 ARG A 324 -122.347 86.713 -14.061 1.00 73.20 N ANISOU 1544 NH2 ARG A 324 9330 7704 10778 312 1496 920 N ATOM 1545 N VAL A 325 -123.264 93.206 -13.174 1.00 50.53 N ANISOU 1545 N VAL A 325 6556 4931 7710 587 1327 1357 N ATOM 1546 CA VAL A 325 -122.923 94.000 -11.994 1.00 41.25 C ANISOU 1546 CA VAL A 325 5367 3784 6523 641 1258 1427 C ATOM 1547 C VAL A 325 -123.290 95.472 -12.121 1.00 47.24 C ANISOU 1547 C VAL A 325 6155 4572 7223 695 1227 1503 C ATOM 1548 O VAL A 325 -123.846 96.071 -11.190 1.00 58.51 O ANISOU 1548 O VAL A 325 7574 5992 8665 733 1239 1560 O ATOM 1549 CB VAL A 325 -121.424 93.926 -11.678 1.00 52.69 C ANISOU 1549 CB VAL A 325 6799 5281 7939 645 1141 1418 C ATOM 1550 CG1 VAL A 325 -121.007 95.130 -10.853 1.00 43.77 C ANISOU 1550 CG1 VAL A 325 5668 4197 6764 705 1049 1491 C ATOM 1551 CG2 VAL A 325 -121.098 92.622 -10.952 1.00 76.92 C ANISOU 1551 CG2 VAL A 325 9828 8322 11076 610 1164 1364 C ATOM 1552 N ASN A 326 -122.980 96.045 -13.278 1.00 46.68 N ANISOU 1552 N ASN A 326 7358 4079 6299 958 1781 2196 N ATOM 1553 CA ASN A 326 -123.066 97.489 -13.489 1.00 44.89 C ANISOU 1553 CA ASN A 326 7197 3947 5912 1067 1700 2323 C ATOM 1554 C ASN A 326 -123.616 97.800 -14.881 1.00 52.96 C ANISOU 1554 C ASN A 326 8258 4984 6880 1015 1790 2323 C ATOM 1555 O ASN A 326 -122.852 98.137 -15.795 1.00 43.78 O ANISOU 1555 O ASN A 326 7110 3961 5562 974 1683 2274 O ATOM 1556 CB ASN A 326 -121.670 98.077 -13.320 1.00 46.04 C ANISOU 1556 CB ASN A 326 7344 4277 5872 1101 1460 2304 C ATOM 1557 CG ASN A 326 -121.616 99.558 -13.569 1.00 51.86 C ANISOU 1557 CG ASN A 326 8132 5132 6441 1193 1355 2403 C ATOM 1558 OD1 ASN A 326 -120.529 100.130 -13.670 1.00 53.59 O ANISOU 1558 OD1 ASN A 326 8346 5513 6502 1201 1165 2370 O ATOM 1559 ND2 ASN A 326 -122.779 100.196 -13.661 1.00 46.39 N ANISOU 1559 ND2 ASN A 326 7481 4360 5785 1258 1476 2517 N ATOM 1560 N PRO A 327 -124.951 97.691 -15.050 1.00 46.90 N ANISOU 1560 N PRO A 327 7504 4075 6242 1016 1986 2373 N ATOM 1561 CA PRO A 327 -125.522 97.620 -16.399 1.00 46.95 C ANISOU 1561 CA PRO A 327 7530 4070 6239 936 2099 2335 C ATOM 1562 C PRO A 327 -125.501 98.950 -17.149 1.00 54.27 C ANISOU 1562 C PRO A 327 8521 5111 6988 1000 2023 2425 C ATOM 1563 O PRO A 327 -125.619 98.980 -18.383 1.00 51.45 O ANISOU 1563 O PRO A 327 8179 4793 6576 928 2059 2378 O ATOM 1564 CB PRO A 327 -126.949 97.128 -16.165 1.00 48.84 C ANISOU 1564 CB PRO A 327 7758 4120 6678 928 2322 2362 C ATOM 1565 CG PRO A 327 -126.995 96.721 -14.710 1.00 65.74 C ANISOU 1565 CG PRO A 327 9860 6174 8943 982 2324 2386 C ATOM 1566 CD PRO A 327 -125.983 97.564 -14.021 1.00 48.90 C ANISOU 1566 CD PRO A 327 7749 4172 6660 1084 2114 2454 C ATOM 1567 N ALA A 328 -125.328 100.043 -16.417 1.00 53.40 N ANISOU 1567 N ALA A 328 8441 5060 6787 1128 1911 2542 N ATOM 1568 CA ALA A 328 -125.065 101.320 -17.072 1.00 71.59 C ANISOU 1568 CA ALA A 328 10792 7500 8909 1179 1800 2602 C ATOM 1569 C ALA A 328 -123.797 101.259 -17.941 1.00 46.25 C ANISOU 1569 C ALA A 328 7564 4457 5551 1093 1642 2484 C ATOM 1570 O ALA A 328 -123.719 101.908 -18.973 1.00 46.05 O ANISOU 1570 O ALA A 328 7565 4522 5412 1072 1605 2482 O ATOM 1571 CB ALA A 328 -124.975 102.456 -16.043 1.00 76.04 C ANISOU 1571 CB ALA A 328 11378 8110 9403 1322 1689 2724 C ATOM 1572 N ALA A 329 -122.812 100.466 -17.530 1.00 44.48 N ANISOU 1572 N ALA A 329 7293 4274 5332 1040 1552 2383 N ATOM 1573 CA ALA A 329 -121.535 100.387 -18.255 1.00 42.21 C ANISOU 1573 CA ALA A 329 6983 4150 4905 961 1394 2268 C ATOM 1574 C ALA A 329 -121.693 99.979 -19.723 1.00 43.19 C ANISOU 1574 C ALA A 329 7108 4292 5009 846 1470 2184 C ATOM 1575 O ALA A 329 -120.742 100.038 -20.493 1.00 53.91 O ANISOU 1575 O ALA A 329 8448 5791 6243 780 1347 2095 O ATOM 1576 CB ALA A 329 -120.578 99.449 -17.547 1.00 40.56 C ANISOU 1576 CB ALA A 329 6723 3957 4730 919 1315 2172 C ATOM 1577 N ALA A 330 -122.894 99.568 -20.111 1.00 42.55 N ANISOU 1577 N ALA A 330 7041 4071 5054 818 1669 2205 N ATOM 1578 CA ALA A 330 -123.146 99.194 -21.498 1.00 48.84 C ANISOU 1578 CA ALA A 330 7836 4881 5841 710 1747 2123 C ATOM 1579 C ALA A 330 -123.162 100.413 -22.417 1.00 48.18 C ANISOU 1579 C ALA A 330 7793 4907 5606 742 1675 2180 C ATOM 1580 O ALA A 330 -123.252 100.271 -23.632 1.00 55.43 O ANISOU 1580 O ALA A 330 8709 5864 6489 659 1707 2117 O ATOM 1581 CB ALA A 330 -124.461 98.440 -21.609 1.00 65.04 C ANISOU 1581 CB ALA A 330 9882 6751 8078 668 1977 2120 C ATOM 1582 N ALA A 331 -123.069 101.605 -21.831 1.00 44.73 N ANISOU 1582 N ALA A 331 7387 4522 5085 859 1576 2293 N ATOM 1583 CA ALA A 331 -123.249 102.847 -22.572 1.00 44.14 C ANISOU 1583 CA ALA A 331 7350 4531 4890 899 1524 2359 C ATOM 1584 C ALA A 331 -122.047 103.133 -23.456 1.00 63.09 C ANISOU 1584 C ALA A 331 9722 7113 7137 826 1348 2258 C ATOM 1585 O ALA A 331 -122.173 103.620 -24.579 1.00 57.95 O ANISOU 1585 O ALA A 331 9083 6523 6415 788 1343 2247 O ATOM 1586 CB ALA A 331 -123.500 104.007 -21.620 1.00 45.87 C ANISOU 1586 CB ALA A 331 7603 4750 5075 1038 1471 2496 C ATOM 1587 N HIS A 332 -120.870 102.825 -22.939 1.00 66.62 N ANISOU 1587 N HIS A 332 10125 7648 7540 803 1203 2179 N ATOM 1588 CA HIS A 332 -119.658 102.961 -23.724 1.00 56.13 C ANISOU 1588 CA HIS A 332 8753 6488 6087 719 1037 2066 C ATOM 1589 C HIS A 332 -118.984 101.610 -23.960 1.00 47.06 C ANISOU 1589 C HIS A 332 7552 5355 4975 609 1039 1924 C ATOM 1590 O HIS A 332 -118.272 101.429 -24.939 1.00 48.70 O ANISOU 1590 O HIS A 332 7717 5675 5111 514 963 1818 O ATOM 1591 CB HIS A 332 -118.712 103.958 -23.064 1.00 75.72 C ANISOU 1591 CB HIS A 332 11229 9081 8462 801 865 2087 C ATOM 1592 CG HIS A 332 -119.348 105.286 -22.789 1.00 86.04 C ANISOU 1592 CG HIS A 332 12591 10373 9728 930 882 2226 C ATOM 1593 ND1 HIS A 332 -120.423 105.431 -21.940 1.00 80.77 N ANISOU 1593 ND1 HIS A 332 11957 9578 9154 1003 976 2346 N ATOM 1594 CD2 HIS A 332 -119.063 106.525 -23.255 1.00 87.04 C ANISOU 1594 CD2 HIS A 332 12742 10594 9734 999 821 2261 C ATOM 1595 CE1 HIS A 332 -120.770 106.705 -21.889 1.00 90.31 C ANISOU 1595 CE1 HIS A 332 13209 10810 10294 1114 971 2452 C ATOM 1596 NE2 HIS A 332 -119.963 107.389 -22.678 1.00 88.17 N ANISOU 1596 NE2 HIS A 332 12933 10672 9893 1113 878 2403 N ATOM 1597 N THR A 333 -119.210 100.656 -23.072 1.00 36.63 N ANISOU 1597 N THR A 333 6226 3920 3771 618 1126 1919 N ATOM 1598 CA THR A 333 -118.782 99.293 -23.346 1.00 34.93 C ANISOU 1598 CA THR A 333 5966 3694 3612 507 1165 1785 C ATOM 1599 C THR A 333 -119.914 98.500 -23.996 1.00 47.94 C ANISOU 1599 C THR A 333 7623 5208 5386 442 1376 1764 C ATOM 1600 O THR A 333 -120.700 97.843 -23.309 1.00 64.78 O ANISOU 1600 O THR A 333 9760 7182 7671 453 1523 1788 O ATOM 1601 CB THR A 333 -118.332 98.581 -22.071 1.00 34.45 C ANISOU 1601 CB THR A 333 5884 3583 3624 530 1143 1766 C ATOM 1602 OG1 THR A 333 -117.424 99.423 -21.359 1.00 47.36 O ANISOU 1602 OG1 THR A 333 7509 5330 5155 601 952 1796 O ATOM 1603 CG2 THR A 333 -117.628 97.276 -22.421 1.00 39.38 C ANISOU 1603 CG2 THR A 333 6455 4231 4276 407 1146 1609 C ATOM 1604 N THR A 334 -119.989 98.558 -25.325 1.00 38.82 N ANISOU 1604 N THR A 334 6459 4116 4174 368 1387 1708 N ATOM 1605 CA THR A 334 -121.129 98.010 -26.063 1.00 38.07 C ANISOU 1605 CA THR A 334 6371 3908 4186 309 1576 1690 C ATOM 1606 C THR A 334 -120.839 96.649 -26.670 1.00 34.34 C ANISOU 1606 C THR A 334 5836 3437 3773 172 1621 1520 C ATOM 1607 O THR A 334 -121.725 96.026 -27.247 1.00 36.99 O ANISOU 1607 O THR A 334 6160 3680 4213 107 1771 1473 O ATOM 1608 CB THR A 334 -121.537 98.948 -27.206 1.00 36.61 C ANISOU 1608 CB THR A 334 6214 3786 3910 315 1568 1736 C ATOM 1609 OG1 THR A 334 -120.407 99.160 -28.064 1.00 54.37 O ANISOU 1609 OG1 THR A 334 8420 6219 6020 254 1400 1648 O ATOM 1610 CG2 THR A 334 -121.962 100.277 -26.648 1.00 52.07 C ANISOU 1610 CG2 THR A 334 8231 5730 5822 446 1541 1897 C ATOM 1611 N ALA A 335 -119.590 96.207 -26.563 1.00 43.53 N ANISOU 1611 N ALA A 335 6952 4714 4872 126 1485 1420 N ATOM 1612 CA ALA A 335 -119.177 94.932 -27.147 1.00 36.63 C ANISOU 1612 CA ALA A 335 6009 3866 4042 -2 1505 1246 C ATOM 1613 C ALA A 335 -118.114 94.339 -26.274 1.00 32.26 C ANISOU 1613 C ALA A 335 5422 3351 3485 -14 1411 1178 C ATOM 1614 O ALA A 335 -117.356 95.083 -25.669 1.00 48.44 O ANISOU 1614 O ALA A 335 7487 5483 5434 62 1270 1243 O ATOM 1615 CB ALA A 335 -118.630 95.137 -28.534 1.00 39.54 C ANISOU 1615 CB ALA A 335 6337 4394 4293 -64 1406 1171 C ATOM 1616 N PRO A 336 -118.067 92.995 -26.189 1.00 39.91 N ANISOU 1616 N PRO A 336 6336 4260 4567 -111 1484 1038 N ATOM 1617 CA PRO A 336 -117.008 92.284 -25.457 1.00 26.78 C ANISOU 1617 CA PRO A 336 4633 2637 2904 -141 1399 948 C ATOM 1618 C PRO A 336 -115.665 92.609 -26.035 1.00 24.92 C ANISOU 1618 C PRO A 336 4363 2606 2500 -152 1204 889 C ATOM 1619 O PRO A 336 -114.655 92.513 -25.359 1.00 39.63 O ANISOU 1619 O PRO A 336 6210 4537 4312 -136 1089 861 O ATOM 1620 CB PRO A 336 -117.339 90.805 -25.689 1.00 31.96 C ANISOU 1620 CB PRO A 336 5219 3213 3713 -264 1513 775 C ATOM 1621 CG PRO A 336 -118.302 90.785 -26.837 1.00 50.88 C ANISOU 1621 CG PRO A 336 7610 5581 6143 -304 1611 755 C ATOM 1622 CD PRO A 336 -119.074 92.068 -26.730 1.00 35.08 C ANISOU 1622 CD PRO A 336 5692 3536 4103 -197 1650 948 C ATOM 1623 N GLY A 337 -115.655 93.009 -27.293 1.00 30.14 N ANISOU 1623 N GLY A 337 4999 3369 3083 -177 1163 868 N ATOM 1624 CA GLY A 337 -114.412 93.371 -27.951 1.00 39.45 C ANISOU 1624 CA GLY A 337 6106 4752 4130 -183 975 810 C ATOM 1625 C GLY A 337 -113.820 94.675 -27.463 1.00 33.97 C ANISOU 1625 C GLY A 337 5431 4154 3323 -91 830 919 C ATOM 1626 O GLY A 337 -112.693 95.025 -27.807 1.00 52.89 O ANISOU 1626 O GLY A 337 7797 6676 5622 -74 701 861 O ATOM 1627 N GLU A 338 -114.562 95.408 -26.656 1.00 25.01 N ANISOU 1627 N GLU A 338 4382 2916 2203 -8 880 1064 N ATOM 1628 CA GLU A 338 -114.074 96.685 -26.170 1.00 26.02 C ANISOU 1628 CA GLU A 338 4524 3125 2237 76 737 1156 C ATOM 1629 C GLU A 338 -113.461 96.608 -24.767 1.00 37.44 C ANISOU 1629 C GLU A 338 5975 4559 3692 131 660 1174 C ATOM 1630 O GLU A 338 -112.948 97.598 -24.239 1.00 29.04 O ANISOU 1630 O GLU A 338 4912 3560 2561 198 532 1229 O ATOM 1631 CB GLU A 338 -115.186 97.723 -26.248 1.00 27.60 C ANISOU 1631 CB GLU A 338 4804 3246 2435 150 811 1300 C ATOM 1632 CG GLU A 338 -115.647 97.889 -27.650 1.00 27.92 C ANISOU 1632 CG GLU A 338 4858 3304 2447 116 882 1279 C ATOM 1633 CD GLU A 338 -116.592 99.022 -27.803 1.00 43.24 C ANISOU 1633 CD GLU A 338 6874 5189 4366 197 939 1416 C ATOM 1634 OE1 GLU A 338 -116.949 99.608 -26.766 1.00 65.08 O ANISOU 1634 OE1 GLU A 338 9680 7895 7153 282 932 1526 O ATOM 1635 OE2 GLU A 338 -116.981 99.316 -28.954 1.00 58.03 O ANISOU 1635 OE2 GLU A 338 8765 7080 6206 179 991 1411 O ATOM 1636 N ILE A 339 -113.485 95.414 -24.190 1.00 30.44 N ANISOU 1636 N ILE A 339 5094 3581 2893 101 744 1115 N ATOM 1637 CA ILE A 339 -112.926 95.180 -22.871 1.00 24.50 C ANISOU 1637 CA ILE A 339 4347 2806 2158 150 681 1124 C ATOM 1638 C ILE A 339 -111.403 95.262 -22.815 1.00 23.32 C ANISOU 1638 C ILE A 339 4104 2838 1916 123 480 1024 C ATOM 1639 O ILE A 339 -110.716 94.537 -23.533 1.00 37.57 O ANISOU 1639 O ILE A 339 5829 4734 3711 38 451 887 O ATOM 1640 CB ILE A 339 -113.334 93.798 -22.359 1.00 40.99 C ANISOU 1640 CB ILE A 339 6450 4740 4385 96 835 1066 C ATOM 1641 CG1 ILE A 339 -114.847 93.763 -22.043 1.00 26.46 C ANISOU 1641 CG1 ILE A 339 4663 2699 2693 131 1035 1171 C ATOM 1642 CG2 ILE A 339 -112.474 93.420 -21.159 1.00 39.65 C ANISOU 1642 CG2 ILE A 339 6270 4579 4216 126 742 1042 C ATOM 1643 CD1 ILE A 339 -115.243 94.657 -20.913 1.00 28.14 C ANISOU 1643 CD1 ILE A 339 4921 2850 2922 271 1010 1332 C ATOM 1644 N ASP A 340 -110.873 96.136 -21.956 1.00 24.93 N ANISOU 1644 N ASP A 340 4297 3097 2077 194 344 1083 N ATOM 1645 CA ASP A 340 -109.436 96.141 -21.644 1.00 22.68 C ANISOU 1645 CA ASP A 340 3919 2952 1746 173 181 982 C ATOM 1646 C ASP A 340 -109.097 95.068 -20.625 1.00 30.40 C ANISOU 1646 C ASP A 340 4890 3882 2778 171 182 932 C ATOM 1647 O ASP A 340 -109.259 95.258 -19.418 1.00 47.29 O ANISOU 1647 O ASP A 340 7076 5947 4944 254 163 1011 O ATOM 1648 CB ASP A 340 -108.969 97.510 -21.141 1.00 26.13 C ANISOU 1648 CB ASP A 340 4380 3434 2113 269 70 1043 C ATOM 1649 CG ASP A 340 -107.656 97.450 -20.344 1.00 34.96 C ANISOU 1649 CG ASP A 340 5434 4631 3218 279 -59 958 C ATOM 1650 OD1 ASP A 340 -106.908 96.445 -20.404 1.00 34.16 O ANISOU 1650 OD1 ASP A 340 5262 4575 3142 214 -78 834 O ATOM 1651 OD2 ASP A 340 -107.358 98.445 -19.649 1.00 36.91 O ANISOU 1651 OD2 ASP A 340 5698 4894 3431 358 -135 1010 O ATOM 1652 N PHE A 341 -108.607 93.947 -21.129 1.00 23.95 N ANISOU 1652 N PHE A 341 4021 3100 1976 89 208 791 N ATOM 1653 CA PHE A 341 -108.259 92.805 -20.316 1.00 18.22 C ANISOU 1653 CA PHE A 341 3320 2311 1292 70 224 711 C ATOM 1654 C PHE A 341 -106.797 92.841 -19.854 1.00 29.80 C ANISOU 1654 C PHE A 341 4645 3941 2738 69 49 608 C ATOM 1655 O PHE A 341 -106.212 91.794 -19.596 1.00 43.31 O ANISOU 1655 O PHE A 341 6327 5650 4478 25 35 478 O ATOM 1656 CB PHE A 341 -108.465 91.559 -21.150 1.00 20.44 C ANISOU 1656 CB PHE A 341 3607 2539 1619 -46 346 577 C ATOM 1657 CG PHE A 341 -107.664 91.562 -22.415 1.00 26.94 C ANISOU 1657 CG PHE A 341 4281 3533 2424 -85 263 455 C ATOM 1658 CD1 PHE A 341 -106.415 90.965 -22.462 1.00 29.68 C ANISOU 1658 CD1 PHE A 341 4526 3957 2794 -106 160 298 C ATOM 1659 CD2 PHE A 341 -108.140 92.208 -23.545 1.00 28.49 C ANISOU 1659 CD2 PHE A 341 4466 3763 2595 -82 297 501 C ATOM 1660 CE1 PHE A 341 -105.666 90.984 -23.615 1.00 19.30 C ANISOU 1660 CE1 PHE A 341 3175 2675 1484 -133 113 203 C ATOM 1661 CE2 PHE A 341 -107.404 92.231 -24.691 1.00 23.40 C ANISOU 1661 CE2 PHE A 341 3786 3179 1925 -100 247 394 C ATOM 1662 CZ PHE A 341 -106.158 91.618 -24.730 1.00 31.28 C ANISOU 1662 CZ PHE A 341 4721 4205 2960 -127 156 251 C ATOM 1663 N LEU A 342 -106.189 94.018 -19.747 1.00 17.17 N ANISOU 1663 N LEU A 342 3000 2430 1094 114 -60 645 N ATOM 1664 CA LEU A 342 -104.810 94.074 -19.249 1.00 30.83 C ANISOU 1664 CA LEU A 342 4660 4236 2819 125 -175 541 C ATOM 1665 C LEU A 342 -104.672 94.982 -18.054 1.00 17.58 C ANISOU 1665 C LEU A 342 3005 2548 1128 200 -256 632 C ATOM 1666 O LEU A 342 -103.965 94.670 -17.097 1.00 30.38 O ANISOU 1666 O LEU A 342 4580 4183 2780 209 -320 581 O ATOM 1667 CB LEU A 342 -103.827 94.517 -20.344 1.00 16.04 C ANISOU 1667 CB LEU A 342 2741 2435 918 104 -211 451 C ATOM 1668 CG LEU A 342 -103.764 93.556 -21.512 1.00 14.84 C ANISOU 1668 CG LEU A 342 2552 2284 802 45 -149 342 C ATOM 1669 CD1 LEU A 342 -103.086 94.174 -22.704 1.00 27.64 C ANISOU 1669 CD1 LEU A 342 4142 3957 2401 39 -169 308 C ATOM 1670 CD2 LEU A 342 -103.098 92.283 -21.072 1.00 20.39 C ANISOU 1670 CD2 LEU A 342 3195 2962 1589 8 -163 214 C ATOM 1671 N THR A 343 -105.337 96.127 -18.130 1.00 25.41 N ANISOU 1671 N THR A 343 4067 3511 2079 259 -250 760 N ATOM 1672 CA THR A 343 -105.279 97.111 -17.060 1.00 21.39 C ANISOU 1672 CA THR A 343 3582 2989 1555 347 -321 846 C ATOM 1673 C THR A 343 -106.701 97.422 -16.590 1.00 32.44 C ANISOU 1673 C THR A 343 5060 4277 2989 407 -258 1013 C ATOM 1674 O THR A 343 -106.916 98.233 -15.684 1.00 32.06 O ANISOU 1674 O THR A 343 5040 4201 2941 495 -300 1105 O ATOM 1675 CB THR A 343 -104.542 98.376 -17.512 1.00 24.06 C ANISOU 1675 CB THR A 343 3927 3397 1818 384 -378 829 C ATOM 1676 OG1 THR A 343 -105.133 98.856 -18.729 1.00 27.27 O ANISOU 1676 OG1 THR A 343 4379 3801 2180 376 -318 867 O ATOM 1677 CG2 THR A 343 -103.058 98.066 -17.742 1.00 20.00 C ANISOU 1677 CG2 THR A 343 3334 2955 1311 331 -432 677 C ATOM 1678 N PHE A 344 -107.662 96.768 -17.237 1.00 21.95 N ANISOU 1678 N PHE A 344 3764 2875 1702 359 -145 1046 N ATOM 1679 CA PHE A 344 -109.016 96.677 -16.732 1.00 30.02 C ANISOU 1679 CA PHE A 344 4894 3728 2783 449 -24 1182 C ATOM 1680 C PHE A 344 -109.675 98.035 -16.546 1.00 39.60 C ANISOU 1680 C PHE A 344 6148 4919 3978 529 -35 1313 C ATOM 1681 O PHE A 344 -110.525 98.232 -15.681 1.00 37.74 O ANISOU 1681 O PHE A 344 5972 4568 3802 633 25 1430 O ATOM 1682 CB PHE A 344 -108.995 95.900 -15.433 1.00 26.62 C ANISOU 1682 CB PHE A 344 4478 3208 2429 509 -20 1192 C ATOM 1683 CG PHE A 344 -108.110 94.726 -15.488 1.00 21.80 C ANISOU 1683 CG PHE A 344 3821 2645 1817 431 -50 1046 C ATOM 1684 CD1 PHE A 344 -106.927 94.705 -14.784 1.00 24.96 C ANISOU 1684 CD1 PHE A 344 4122 3159 2204 414 -200 960 C ATOM 1685 CD2 PHE A 344 -108.432 93.654 -16.299 1.00 32.42 C ANISOU 1685 CD2 PHE A 344 5214 3922 3180 355 82 979 C ATOM 1686 CE1 PHE A 344 -106.102 93.615 -14.847 1.00 28.93 C ANISOU 1686 CE1 PHE A 344 4574 3711 2707 343 -227 809 C ATOM 1687 CE2 PHE A 344 -107.612 92.557 -16.371 1.00 24.10 C ANISOU 1687 CE2 PHE A 344 4133 2910 2115 272 51 824 C ATOM 1688 CZ PHE A 344 -106.442 92.535 -15.645 1.00 34.59 C ANISOU 1688 CZ PHE A 344 5362 4359 3424 276 -114 736 C ATOM 1689 N LEU A 345 -109.281 98.970 -17.386 1.00 29.48 N ANISOU 1689 N LEU A 345 4858 3738 2604 516 -82 1291 N ATOM 1690 CA LEU A 345 -109.967 100.220 -17.435 1.00 27.67 C ANISOU 1690 CA LEU A 345 4694 3485 2335 609 -60 1409 C ATOM 1691 C LEU A 345 -111.055 100.117 -18.482 1.00 28.96 C ANISOU 1691 C LEU A 345 4907 3580 2515 579 74 1458 C ATOM 1692 O LEU A 345 -110.865 99.478 -19.511 1.00 33.30 O ANISOU 1692 O LEU A 345 5436 4164 3054 488 113 1371 O ATOM 1693 CB LEU A 345 -108.983 101.312 -17.806 1.00 42.78 C ANISOU 1693 CB LEU A 345 6593 5525 4138 642 -155 1361 C ATOM 1694 CG LEU A 345 -107.778 101.330 -16.879 1.00 36.85 C ANISOU 1694 CG LEU A 345 5780 4844 3375 652 -274 1286 C ATOM 1695 CD1 LEU A 345 -106.913 102.550 -17.173 1.00 43.54 C ANISOU 1695 CD1 LEU A 345 6623 5791 4130 693 -347 1255 C ATOM 1696 CD2 LEU A 345 -108.241 101.341 -15.443 1.00 28.23 C ANISOU 1696 CD2 LEU A 345 4698 3681 2346 724 -292 1377 C ATOM 1697 N ALA A 346 -112.194 100.747 -18.218 1.00 30.06 N ANISOU 1697 N ALA A 346 5110 3626 2687 657 150 1593 N ATOM 1698 CA ALA A 346 -113.232 100.878 -19.225 1.00 50.69 C ANISOU 1698 CA ALA A 346 7772 6179 5309 642 280 1646 C ATOM 1699 C ALA A 346 -112.885 102.067 -20.096 1.00 35.16 C ANISOU 1699 C ALA A 346 5824 4316 3217 681 236 1647 C ATOM 1700 O ALA A 346 -112.107 102.926 -19.708 1.00 31.78 O ANISOU 1700 O ALA A 346 5385 3974 2716 741 127 1640 O ATOM 1701 CB ALA A 346 -114.618 101.080 -18.573 1.00 37.54 C ANISOU 1701 CB ALA A 346 6177 4357 3729 750 422 1795 C ATOM 1702 N VAL A 347 -113.489 102.123 -21.268 1.00 39.00 N ANISOU 1702 N VAL A 347 6341 4789 3690 645 328 1654 N ATOM 1703 CA VAL A 347 -113.256 103.239 -22.160 1.00 41.50 C ANISOU 1703 CA VAL A 347 6679 5190 3899 682 297 1661 C ATOM 1704 C VAL A 347 -113.414 104.586 -21.443 1.00 34.22 C ANISOU 1704 C VAL A 347 5794 4278 2929 812 252 1771 C ATOM 1705 O VAL A 347 -112.593 105.479 -21.627 1.00 60.48 O ANISOU 1705 O VAL A 347 9109 7706 6165 848 159 1741 O ATOM 1706 CB VAL A 347 -114.154 103.126 -23.400 1.00 40.91 C ANISOU 1706 CB VAL A 347 6638 5073 3833 639 422 1680 C ATOM 1707 CG1 VAL A 347 -114.150 104.421 -24.181 1.00 52.32 C ANISOU 1707 CG1 VAL A 347 8118 6582 5179 699 401 1720 C ATOM 1708 CG2 VAL A 347 -113.686 101.945 -24.268 1.00 33.33 C ANISOU 1708 CG2 VAL A 347 5627 4147 2891 510 437 1543 C ATOM 1709 N ASP A 348 -114.399 104.787 -20.596 1.00 65.48 N ANISOU 1709 N ASP A 348 9793 8130 6958 881 324 1893 N ATOM 1710 CA ASP A 348 -114.574 106.103 -19.976 1.00 67.04 C ANISOU 1710 CA ASP A 348 10024 8330 7118 1011 293 2006 C ATOM 1711 C ASP A 348 -113.422 106.467 -19.090 1.00 55.79 C ANISOU 1711 C ASP A 348 8556 7007 5633 1046 144 1953 C ATOM 1712 O ASP A 348 -113.224 107.614 -18.763 1.00 38.55 O ANISOU 1712 O ASP A 348 6389 4879 3379 1137 92 2006 O ATOM 1713 CB ASP A 348 -115.878 106.177 -19.189 1.00 83.79 C ANISOU 1713 CB ASP A 348 12176 10311 9348 1070 384 2126 C ATOM 1714 CG ASP A 348 -117.097 106.098 -20.084 1.00111.59 C ANISOU 1714 CG ASP A 348 15751 13726 12922 1075 544 2213 C ATOM 1715 OD1 ASP A 348 -117.457 104.971 -20.519 1.00120.81 O ANISOU 1715 OD1 ASP A 348 16914 14794 14195 996 647 2191 O ATOM 1716 OD2 ASP A 348 -117.693 107.161 -20.362 1.00118.61 O ANISOU 1716 OD2 ASP A 348 16684 14629 13752 1156 573 2302 O ATOM 1717 N GLY A 349 -112.652 105.473 -18.699 1.00 54.98 N ANISOU 1717 N GLY A 349 8398 6929 5564 972 80 1847 N ATOM 1718 CA GLY A 349 -111.464 105.699 -17.908 1.00 58.30 C ANISOU 1718 CA GLY A 349 8770 7439 5941 995 -53 1785 C ATOM 1719 C GLY A 349 -111.524 104.987 -16.597 1.00 51.77 C ANISOU 1719 C GLY A 349 7919 6553 5200 1009 -79 1801 C ATOM 1720 O GLY A 349 -110.539 104.879 -15.909 1.00 55.65 O ANISOU 1720 O GLY A 349 8357 7109 5680 993 -182 1721 O ATOM 1721 N ASP A 350 -112.705 104.497 -16.286 1.00 45.80 N ANISOU 1721 N ASP A 350 7199 5666 4538 1038 19 1902 N ATOM 1722 CA ASP A 350 -113.069 103.970 -14.995 1.00 54.13 C ANISOU 1722 CA ASP A 350 8233 6645 5690 1063 2 1930 C ATOM 1723 C ASP A 350 -112.844 102.474 -14.893 1.00 48.60 C ANISOU 1723 C ASP A 350 7497 5880 5089 955 34 1851 C ATOM 1724 O ASP A 350 -113.322 101.757 -15.719 1.00 59.88 O ANISOU 1724 O ASP A 350 8945 7257 6552 889 141 1834 O ATOM 1725 CB ASP A 350 -114.567 104.217 -14.854 1.00 84.38 C ANISOU 1725 CB ASP A 350 12117 10359 9584 1165 90 2084 C ATOM 1726 CG ASP A 350 -115.326 103.936 -16.150 1.00 99.69 C ANISOU 1726 CG ASP A 350 14072 12365 11441 1286 24 2160 C ATOM 1727 OD1 ASP A 350 -114.755 104.084 -17.234 1.00 93.92 O ANISOU 1727 OD1 ASP A 350 13303 11755 10628 1290 -99 2089 O ATOM 1728 OD2 ASP A 350 -116.507 103.568 -16.099 1.00101.59 O ANISOU 1728 OD2 ASP A 350 14362 12535 11702 1377 100 2289 O ATOM 1729 N PRO A 351 -112.172 101.990 -13.864 1.00 38.35 N ANISOU 1729 N PRO A 351 6148 4584 3838 948 -47 1803 N ATOM 1730 CA PRO A 351 -111.969 100.562 -13.699 1.00 31.99 C ANISOU 1730 CA PRO A 351 5319 3726 3109 898 -2 1730 C ATOM 1731 C PRO A 351 -113.233 99.778 -13.485 1.00 44.79 C ANISOU 1731 C PRO A 351 6999 5166 4853 951 201 1816 C ATOM 1732 O PRO A 351 -114.004 100.107 -12.629 1.00 67.92 O ANISOU 1732 O PRO A 351 9960 8000 7845 1051 264 1934 O ATOM 1733 CB PRO A 351 -111.151 100.501 -12.443 1.00 34.78 C ANISOU 1733 CB PRO A 351 5617 4111 3487 927 -127 1700 C ATOM 1734 CG PRO A 351 -111.515 101.617 -11.738 1.00 33.45 C ANISOU 1734 CG PRO A 351 5466 3945 3298 1018 -178 1802 C ATOM 1735 CD PRO A 351 -111.649 102.696 -12.707 1.00 52.21 C ANISOU 1735 CD PRO A 351 7885 6388 5564 1039 -153 1833 C ATOM 1736 N TYR A 352 -113.419 98.723 -14.248 1.00 40.70 N ANISOU 1736 N TYR A 352 6488 4595 4382 871 312 1751 N ATOM 1737 CA TYR A 352 -114.626 97.913 -14.201 1.00 52.33 C ANISOU 1737 CA TYR A 352 7998 5879 6007 881 527 1807 C ATOM 1738 C TYR A 352 -115.035 97.648 -12.754 1.00 34.30 C ANISOU 1738 C TYR A 352 5703 3475 3853 967 556 1874 C ATOM 1739 O TYR A 352 -114.185 97.460 -11.898 1.00 33.51 O ANISOU 1739 O TYR A 352 5560 3429 3743 985 424 1830 O ATOM 1740 CB TYR A 352 -114.385 96.599 -14.941 1.00 53.88 C ANISOU 1740 CB TYR A 352 8180 6043 6249 758 614 1688 C ATOM 1741 CG TYR A 352 -113.978 96.812 -16.371 1.00 47.30 C ANISOU 1741 CG TYR A 352 7349 5333 5291 670 584 1613 C ATOM 1742 CD1 TYR A 352 -114.854 97.409 -17.270 1.00 45.68 C ANISOU 1742 CD1 TYR A 352 7183 5104 5070 670 679 1673 C ATOM 1743 CD2 TYR A 352 -112.718 96.422 -16.835 1.00 42.85 C ANISOU 1743 CD2 TYR A 352 6737 4912 4631 584 456 1476 C ATOM 1744 CE1 TYR A 352 -114.486 97.619 -18.592 1.00 56.19 C ANISOU 1744 CE1 TYR A 352 8505 6550 6296 588 644 1601 C ATOM 1745 CE2 TYR A 352 -112.349 96.624 -18.162 1.00 27.12 C ANISOU 1745 CE2 TYR A 352 4727 3036 2541 499 426 1401 C ATOM 1746 CZ TYR A 352 -113.234 97.227 -19.026 1.00 28.25 C ANISOU 1746 CZ TYR A 352 4910 3152 2673 502 516 1465 C ATOM 1747 OH TYR A 352 -112.909 97.438 -20.333 1.00 50.43 O ANISOU 1747 OH TYR A 352 7692 6071 5399 419 483 1393 O ATOM 1748 N GLN A 353 -116.333 97.644 -12.481 1.00 36.18 N ANISOU 1748 N GLN A 353 5971 3557 4221 1017 725 1975 N ATOM 1749 CA GLN A 353 -116.841 97.430 -11.126 1.00 37.48 C ANISOU 1749 CA GLN A 353 6117 3599 4523 1098 765 2041 C ATOM 1750 C GLN A 353 -116.915 95.938 -10.789 1.00 43.73 C ANISOU 1750 C GLN A 353 6865 4257 5494 1023 872 1956 C ATOM 1751 O GLN A 353 -116.952 95.559 -9.622 1.00 55.39 O ANISOU 1751 O GLN A 353 8305 5659 7081 1068 861 1966 O ATOM 1752 CB GLN A 353 -118.198 98.102 -10.959 1.00 39.93 C ANISOU 1752 CB GLN A 353 6470 3803 4899 1180 900 2179 C ATOM 1753 CG GLN A 353 -118.149 99.328 -10.058 1.00 59.18 C ANISOU 1753 CG GLN A 353 8921 6308 7259 1308 776 2280 C ATOM 1754 CD GLN A 353 -119.383 100.235 -10.169 1.00 43.65 C ANISOU 1754 CD GLN A 353 7008 4274 5305 1388 891 2418 C ATOM 1755 OE1 GLN A 353 -120.082 100.247 -11.179 1.00 44.05 O ANISOU 1755 OE1 GLN A 353 7092 4279 5364 1348 1021 2435 O ATOM 1756 NE2 GLN A 353 -119.633 101.011 -9.123 1.00 77.62 N ANISOU 1756 NE2 GLN A 353 11315 8573 9603 1504 839 2515 N ATOM 1757 N GLY A 354 -116.908 95.099 -11.820 1.00 45.91 N ANISOU 1757 N GLY A 354 7137 4506 5800 898 972 1859 N ATOM 1758 CA GLY A 354 -116.972 93.657 -11.652 1.00 36.95 C ANISOU 1758 CA GLY A 354 5949 3246 4846 794 1084 1748 C ATOM 1759 C GLY A 354 -115.620 92.963 -11.575 1.00 32.32 C ANISOU 1759 C GLY A 354 5326 2747 4207 731 951 1622 C ATOM 1760 O GLY A 354 -115.545 91.746 -11.514 1.00 31.97 O ANISOU 1760 O GLY A 354 5230 2610 4307 625 1032 1504 O ATOM 1761 N ILE A 355 -114.539 93.726 -11.571 1.00 31.42 N ANISOU 1761 N ILE A 355 5228 2817 3893 785 743 1629 N ATOM 1762 CA ILE A 355 -113.237 93.108 -11.392 1.00 29.36 C ANISOU 1762 CA ILE A 355 4933 2647 3575 740 606 1512 C ATOM 1763 C ILE A 355 -112.549 93.596 -10.135 1.00 29.50 C ANISOU 1763 C ILE A 355 4917 2743 3550 846 418 1542 C ATOM 1764 O ILE A 355 -112.743 94.714 -9.699 1.00 59.81 O ANISOU 1764 O ILE A 355 8765 6639 7320 941 341 1638 O ATOM 1765 CB ILE A 355 -112.345 93.294 -12.614 1.00 30.10 C ANISOU 1765 CB ILE A 355 5047 2917 3474 665 515 1429 C ATOM 1766 CG1 ILE A 355 -113.088 92.828 -13.861 1.00 41.14 C ANISOU 1766 CG1 ILE A 355 6472 4242 4918 554 705 1393 C ATOM 1767 CG2 ILE A 355 -111.045 92.515 -12.445 1.00 54.22 C ANISOU 1767 CG2 ILE A 355 8071 6057 6472 609 390 1294 C ATOM 1768 CD1 ILE A 355 -112.208 92.700 -15.063 1.00 60.94 C ANISOU 1768 CD1 ILE A 355 8986 6906 7263 456 636 1278 C ATOM 1769 N GLN A 356 -111.798 92.719 -9.510 1.00 35.09 N ANISOU 1769 N GLN A 356 5577 3439 4315 822 354 1450 N ATOM 1770 CA GLN A 356 -110.999 93.113 -8.384 1.00 30.59 C ANISOU 1770 CA GLN A 356 4961 2970 3694 904 158 1449 C ATOM 1771 C GLN A 356 -109.618 92.655 -8.778 1.00 30.90 C ANISOU 1771 C GLN A 356 4973 3161 3607 833 12 1305 C ATOM 1772 O GLN A 356 -109.380 91.454 -8.873 1.00 25.08 O ANISOU 1772 O GLN A 356 4236 2336 2957 765 71 1207 O ATOM 1773 CB GLN A 356 -111.462 92.411 -7.105 1.00 31.64 C ANISOU 1773 CB GLN A 356 5045 2935 4041 948 217 1462 C ATOM 1774 CG GLN A 356 -110.367 92.356 -6.055 1.00 52.95 C ANISOU 1774 CG GLN A 356 7678 5739 6701 992 13 1401 C ATOM 1775 CD GLN A 356 -110.737 91.560 -4.823 1.00 42.52 C ANISOU 1775 CD GLN A 356 6297 4260 5600 1024 65 1390 C ATOM 1776 OE1 GLN A 356 -111.898 91.499 -4.448 1.00 51.35 O ANISOU 1776 OE1 GLN A 356 7419 5220 6872 1049 217 1465 O ATOM 1777 NE2 GLN A 356 -109.738 90.949 -4.180 1.00 40.31 N ANISOU 1777 NE2 GLN A 356 5950 4033 5333 1018 -68 1282 N ATOM 1778 N VAL A 357 -108.727 93.612 -9.052 1.00 31.13 N ANISOU 1778 N VAL A 357 4970 3407 3452 823 -161 1273 N ATOM 1779 CA VAL A 357 -107.390 93.305 -9.560 1.00 28.36 C ANISOU 1779 CA VAL A 357 4562 3234 2978 728 -292 1114 C ATOM 1780 C VAL A 357 -106.447 92.932 -8.429 1.00 25.09 C ANISOU 1780 C VAL A 357 4057 2884 2590 738 -431 1028 C ATOM 1781 O VAL A 357 -106.550 93.462 -7.330 1.00 43.06 O ANISOU 1781 O VAL A 357 6293 5149 4920 810 -484 1101 O ATOM 1782 CB VAL A 357 -106.785 94.512 -10.283 1.00 43.79 C ANISOU 1782 CB VAL A 357 6463 5377 4798 672 -380 1095 C ATOM 1783 CG1 VAL A 357 -105.533 94.099 -11.039 1.00 46.19 C ANISOU 1783 CG1 VAL A 357 6680 5844 5027 543 -445 920 C ATOM 1784 CG2 VAL A 357 -107.799 95.127 -11.220 1.00 23.99 C ANISOU 1784 CG2 VAL A 357 4039 2811 2266 685 -265 1195 C ATOM 1785 N LEU A 358 -105.528 92.020 -8.697 1.00 27.75 N ANISOU 1785 N LEU A 358 4361 3293 2891 653 -492 860 N ATOM 1786 CA LEU A 358 -104.567 91.599 -7.692 1.00 30.92 C ANISOU 1786 CA LEU A 358 4658 3769 3322 639 -615 747 C ATOM 1787 C LEU A 358 -103.174 92.063 -8.092 1.00 39.40 C ANISOU 1787 C LEU A 358 5592 5071 4307 515 -672 616 C ATOM 1788 O LEU A 358 -102.630 91.590 -9.094 1.00 47.26 O ANISOU 1788 O LEU A 358 6558 6134 5265 408 -646 490 O ATOM 1789 CB LEU A 358 -104.595 90.079 -7.528 1.00 18.45 C ANISOU 1789 CB LEU A 358 3131 2044 1834 610 -637 631 C ATOM 1790 CG LEU A 358 -105.861 89.445 -6.945 1.00 39.16 C ANISOU 1790 CG LEU A 358 5715 4432 4730 603 -440 673 C ATOM 1791 CD1 LEU A 358 -105.663 87.949 -6.698 1.00 38.17 C ANISOU 1791 CD1 LEU A 358 5460 4247 4797 442 -396 450 C ATOM 1792 CD2 LEU A 358 -106.263 90.139 -5.666 1.00 53.96 C ANISOU 1792 CD2 LEU A 358 7607 6241 6654 781 -477 847 C ATOM 1793 N GLY A 359 -102.605 92.988 -7.317 1.00 30.75 N ANISOU 1793 N GLY A 359 4404 4068 3213 514 -717 661 N ATOM 1794 CA GLY A 359 -101.291 93.539 -7.613 1.00 35.96 C ANISOU 1794 CA GLY A 359 5038 4832 3794 467 -753 537 C ATOM 1795 C GLY A 359 -100.106 92.689 -7.168 1.00 41.34 C ANISOU 1795 C GLY A 359 5662 5530 4515 411 -779 362 C ATOM 1796 O GLY A 359 -100.208 91.468 -7.022 1.00 29.56 O ANISOU 1796 O GLY A 359 4137 3999 3093 365 -762 286 O ATOM 1797 N PRO A 360 -98.952 93.327 -6.949 1.00 43.02 N ANISOU 1797 N PRO A 360 5866 5784 4697 415 -813 300 N ATOM 1798 CA PRO A 360 -97.829 92.492 -6.508 1.00 50.02 C ANISOU 1798 CA PRO A 360 6705 6653 5648 368 -818 160 C ATOM 1799 C PRO A 360 -98.054 91.987 -5.094 1.00 61.25 C ANISOU 1799 C PRO A 360 8097 8045 7130 400 -859 165 C ATOM 1800 O PRO A 360 -97.613 90.886 -4.759 1.00 79.25 O ANISOU 1800 O PRO A 360 10340 10282 9490 354 -847 61 O ATOM 1801 CB PRO A 360 -96.634 93.443 -6.575 1.00 60.96 C ANISOU 1801 CB PRO A 360 8096 8078 6987 384 -838 132 C ATOM 1802 CG PRO A 360 -97.045 94.472 -7.599 1.00 77.74 C ANISOU 1802 CG PRO A 360 10265 10241 9030 401 -826 208 C ATOM 1803 CD PRO A 360 -98.517 94.668 -7.364 1.00 66.58 C ANISOU 1803 CD PRO A 360 8882 8816 7598 448 -831 340 C ATOM 1804 N LEU A 361 -98.743 92.776 -4.277 1.00 52.18 N ANISOU 1804 N LEU A 361 6959 6909 5957 484 -901 297 N ATOM 1805 CA LEU A 361 -99.081 92.340 -2.933 1.00 50.06 C ANISOU 1805 CA LEU A 361 6652 6608 5759 527 -936 328 C ATOM 1806 C LEU A 361 -99.754 90.963 -2.972 1.00 60.36 C ANISOU 1806 C LEU A 361 7926 7847 7162 491 -904 294 C ATOM 1807 O LEU A 361 -99.628 90.178 -2.031 1.00 70.56 O ANISOU 1807 O LEU A 361 9172 9101 8537 487 -927 236 O ATOM 1808 CB LEU A 361 -100.007 93.353 -2.259 1.00 63.49 C ANISOU 1808 CB LEU A 361 8367 8306 7452 632 -962 522 C ATOM 1809 CG LEU A 361 -99.554 94.809 -2.137 1.00 84.32 C ANISOU 1809 CG LEU A 361 11038 11003 9995 679 -1004 572 C ATOM 1810 CD1 LEU A 361 -100.764 95.731 -2.029 1.00 90.18 C ANISOU 1810 CD1 LEU A 361 11819 11707 10738 764 -1004 772 C ATOM 1811 CD2 LEU A 361 -98.609 95.009 -0.957 1.00 80.12 C ANISOU 1811 CD2 LEU A 361 10476 10506 9461 699 -1062 510 C ATOM 1812 N ASP A 362 -100.455 90.670 -4.070 1.00 52.34 N ANISOU 1812 N ASP A 362 6935 6812 6140 462 -852 324 N ATOM 1813 CA ASP A 362 -101.295 89.472 -4.167 1.00 36.08 C ANISOU 1813 CA ASP A 362 4932 4608 4168 490 -883 278 C ATOM 1814 C ASP A 362 -100.915 88.452 -5.264 1.00 57.75 C ANISOU 1814 C ASP A 362 7670 7356 6918 356 -853 112 C ATOM 1815 O ASP A 362 -101.752 87.653 -5.697 1.00 52.98 O ANISOU 1815 O ASP A 362 7147 6613 6369 361 -905 85 O ATOM 1816 CB ASP A 362 -102.760 89.874 -4.336 1.00 54.45 C ANISOU 1816 CB ASP A 362 7384 6781 6523 631 -862 468 C ATOM 1817 CG ASP A 362 -103.372 90.394 -3.056 1.00 68.33 C ANISOU 1817 CG ASP A 362 9128 8466 8370 761 -855 622 C ATOM 1818 OD1 ASP A 362 -103.604 89.574 -2.137 1.00 55.03 O ANISOU 1818 OD1 ASP A 362 7414 6658 6837 800 -882 586 O ATOM 1819 OD2 ASP A 362 -103.633 91.616 -2.973 1.00 84.97 O ANISOU 1819 OD2 ASP A 362 11236 10626 10421 808 -828 770 O ATOM 1820 N GLY A 363 -99.660 88.469 -5.707 1.00 64.92 N ANISOU 1820 N GLY A 363 9420 7463 7783 280 524 -539 N ATOM 1821 CA GLY A 363 -99.190 87.475 -6.657 1.00 35.99 C ANISOU 1821 CA GLY A 363 5880 3675 4119 100 494 -577 C ATOM 1822 C GLY A 363 -99.333 87.912 -8.099 1.00 42.21 C ANISOU 1822 C GLY A 363 6669 4466 4903 48 420 -466 C ATOM 1823 O GLY A 363 -99.199 87.117 -9.021 1.00 45.68 O ANISOU 1823 O GLY A 363 7173 4825 5358 -87 379 -442 O ATOM 1824 N GLY A 364 -99.605 89.191 -8.298 1.00 34.19 N ANISOU 1824 N GLY A 364 5529 3592 3871 159 393 -374 N ATOM 1825 CA GLY A 364 -99.868 89.686 -9.627 1.00 23.38 C ANISOU 1825 CA GLY A 364 4151 2232 2499 128 323 -256 C ATOM 1826 C GLY A 364 -98.795 90.575 -10.231 1.00 29.83 C ANISOU 1826 C GLY A 364 4861 3229 3244 108 288 -290 C ATOM 1827 O GLY A 364 -97.720 90.820 -9.675 1.00 37.23 O ANISOU 1827 O GLY A 364 5728 4288 4128 101 317 -415 O ATOM 1828 N ILE A 365 -99.107 91.050 -11.421 1.00 23.29 N ANISOU 1828 N ILE A 365 4022 2414 2413 92 226 -176 N ATOM 1829 CA ILE A 365 -98.258 91.970 -12.113 1.00 15.59 C ANISOU 1829 CA ILE A 365 2948 1602 1376 83 189 -187 C ATOM 1830 C ILE A 365 -99.095 93.147 -12.577 1.00 15.83 C ANISOU 1830 C ILE A 365 2878 1730 1408 200 146 -37 C ATOM 1831 O ILE A 365 -100.112 92.967 -13.237 1.00 41.27 O ANISOU 1831 O ILE A 365 6159 4847 4674 198 113 95 O ATOM 1832 CB ILE A 365 -97.610 91.294 -13.322 1.00 19.18 C ANISOU 1832 CB ILE A 365 3497 1977 1813 -73 150 -205 C ATOM 1833 CG1 ILE A 365 -96.503 90.356 -12.848 1.00 31.40 C ANISOU 1833 CG1 ILE A 365 5112 3478 3339 -181 195 -367 C ATOM 1834 CG2 ILE A 365 -97.037 92.327 -14.259 1.00 31.68 C ANISOU 1834 CG2 ILE A 365 4985 3709 3344 -67 102 -175 C ATOM 1835 CD1 ILE A 365 -95.851 89.563 -13.965 1.00 53.71 C ANISOU 1835 CD1 ILE A 365 7941 6265 6202 -310 157 -329 C ATOM 1836 N THR A 366 -98.665 94.349 -12.220 1.00 30.36 N ANISOU 1836 N THR A 366 4561 3777 3196 298 149 -59 N ATOM 1837 CA THR A 366 -99.249 95.560 -12.761 1.00 35.56 C ANISOU 1837 CA THR A 366 5109 4563 3841 401 104 73 C ATOM 1838 C THR A 366 -98.671 95.895 -14.141 1.00 44.42 C ANISOU 1838 C THR A 366 6222 5733 4923 319 44 95 C ATOM 1839 O THR A 366 -97.486 96.189 -14.265 1.00 77.96 O ANISOU 1839 O THR A 366 10419 10086 9114 271 47 -17 O ATOM 1840 CB THR A 366 -99.027 96.746 -11.808 1.00 37.03 C ANISOU 1840 CB THR A 366 5120 4971 3978 544 132 38 C ATOM 1841 OG1 THR A 366 -99.530 96.415 -10.507 1.00 47.33 O ANISOU 1841 OG1 THR A 366 6432 6235 5316 628 192 17 O ATOM 1842 CG2 THR A 366 -99.759 97.960 -12.301 1.00 43.88 C ANISOU 1842 CG2 THR A 366 5873 5967 4832 662 89 186 C ATOM 1843 N LEU A 367 -99.507 95.817 -15.173 1.00 36.72 N ANISOU 1843 N LEU A 367 5300 4675 3978 300 -7 236 N ATOM 1844 CA LEU A 367 -99.179 96.375 -16.479 1.00 28.96 C ANISOU 1844 CA LEU A 367 4281 3767 2955 261 -68 289 C ATOM 1845 C LEU A 367 -99.560 97.854 -16.502 1.00 27.92 C ANISOU 1845 C LEU A 367 3985 3834 2791 403 -92 377 C ATOM 1846 O LEU A 367 -100.097 98.376 -15.543 1.00 62.66 O ANISOU 1846 O LEU A 367 8305 8303 7199 528 -62 403 O ATOM 1847 CB LEU A 367 -99.953 95.673 -17.576 1.00 13.95 C ANISOU 1847 CB LEU A 367 2498 1707 1095 181 -114 408 C ATOM 1848 CG LEU A 367 -99.561 94.297 -18.046 1.00 24.99 C ANISOU 1848 CG LEU A 367 4053 2931 2510 24 -113 350 C ATOM 1849 CD1 LEU A 367 -98.717 93.620 -17.014 1.00 44.54 C ANISOU 1849 CD1 LEU A 367 6567 5372 4982 -18 -52 186 C ATOM 1850 CD2 LEU A 367 -100.842 93.537 -18.338 1.00 24.58 C ANISOU 1850 CD2 LEU A 367 4110 2706 2524 -5 -127 467 C ATOM 1851 N GLY A 368 -99.320 98.507 -17.628 1.00 32.72 N ANISOU 1851 N GLY A 368 4542 4531 3358 388 -147 429 N ATOM 1852 CA GLY A 368 -99.513 99.936 -17.747 1.00 24.80 C ANISOU 1852 CA GLY A 368 3371 3723 2330 500 -169 486 C ATOM 1853 C GLY A 368 -98.238 100.656 -18.182 1.00 26.71 C ANISOU 1853 C GLY A 368 3518 4092 2539 450 -173 364 C ATOM 1854 O GLY A 368 -97.193 100.021 -18.356 1.00 20.25 O ANISOU 1854 O GLY A 368 2774 3238 1681 351 -164 255 O ATOM 1855 N LYS A 369 -98.330 101.981 -18.334 1.00 34.85 N ANISOU 1855 N LYS A 369 4394 5251 3598 515 -171 374 N ATOM 1856 CA LYS A 369 -97.232 102.830 -18.810 1.00 29.92 C ANISOU 1856 CA LYS A 369 3674 4727 2967 481 -163 277 C ATOM 1857 C LYS A 369 -95.926 102.646 -18.045 1.00 27.32 C ANISOU 1857 C LYS A 369 3329 4474 2578 454 -130 120 C ATOM 1858 O LYS A 369 -94.857 102.876 -18.599 1.00 35.67 O ANISOU 1858 O LYS A 369 4372 5529 3653 377 -126 36 O ATOM 1859 CB LYS A 369 -97.635 104.305 -18.785 1.00 22.41 C ANISOU 1859 CB LYS A 369 2562 3917 2035 575 -138 307 C ATOM 1860 CG LYS A 369 -98.671 104.686 -19.815 1.00 28.35 C ANISOU 1860 CG LYS A 369 3330 4582 2859 554 -159 413 C ATOM 1861 CD LYS A 369 -99.352 105.996 -19.413 1.00 38.65 C ANISOU 1861 CD LYS A 369 4509 6019 4158 652 -114 452 C ATOM 1862 CE LYS A 369 -99.971 106.710 -20.610 1.00 46.95 C ANISOU 1862 CE LYS A 369 5554 7024 5261 613 -124 506 C ATOM 1863 NZ LYS A 369 -100.185 108.167 -20.356 1.00 52.23 N ANISOU 1863 NZ LYS A 369 6097 7863 5885 691 -63 513 N ATOM 1864 N ASP A 370 -96.015 102.226 -16.785 1.00 23.73 N ANISOU 1864 N ASP A 370 2885 4064 2069 509 -99 74 N ATOM 1865 CA ASP A 370 -94.828 102.005 -15.961 1.00 15.89 C ANISOU 1865 CA ASP A 370 1879 3102 1056 454 -51 -98 C ATOM 1866 C ASP A 370 -94.687 100.550 -15.597 1.00 26.75 C ANISOU 1866 C ASP A 370 3425 4321 2418 369 -21 -159 C ATOM 1867 O ASP A 370 -93.923 100.214 -14.699 1.00 25.94 O ANISOU 1867 O ASP A 370 3322 4204 2330 325 30 -288 O ATOM 1868 CB ASP A 370 -94.891 102.818 -14.672 1.00 45.86 C ANISOU 1868 CB ASP A 370 5524 7077 4824 576 -19 -142 C ATOM 1869 CG ASP A 370 -94.200 104.168 -14.797 1.00102.14 C ANISOU 1869 CG ASP A 370 12473 14357 11978 597 -31 -184 C ATOM 1870 OD1 ASP A 370 -93.300 104.304 -15.659 1.00113.93 O ANISOU 1870 OD1 ASP A 370 13978 15793 13515 495 -42 -228 O ATOM 1871 OD2 ASP A 370 -94.548 105.091 -14.028 1.00118.19 O ANISOU 1871 OD2 ASP A 370 14356 16566 13986 721 -31 -169 O ATOM 1872 N GLY A 371 -95.423 99.688 -16.293 1.00 21.68 N ANISOU 1872 N GLY A 371 2921 3526 1790 331 -52 -56 N ATOM 1873 CA GLY A 371 -95.543 98.294 -15.888 1.00 36.13 C ANISOU 1873 CA GLY A 371 4905 5150 3674 248 -20 -91 C ATOM 1874 C GLY A 371 -94.631 97.412 -16.707 1.00 51.39 C ANISOU 1874 C GLY A 371 6958 6964 5602 92 -26 -161 C ATOM 1875 O GLY A 371 -95.007 96.924 -17.770 1.00 51.61 O ANISOU 1875 O GLY A 371 7077 6881 5651 33 -70 -68 O ATOM 1876 N ASN A 372 -93.428 97.199 -16.188 1.00 47.88 N ANISOU 1876 N ASN A 372 6513 6536 5144 24 22 -316 N ATOM 1877 CA ASN A 372 -92.357 96.590 -16.943 1.00 21.29 C ANISOU 1877 CA ASN A 372 3164 3061 1862 -45 7 -352 C ATOM 1878 C ASN A 372 -92.360 95.067 -16.879 1.00 24.83 C ANISOU 1878 C ASN A 372 3707 3338 2389 -151 27 -361 C ATOM 1879 O ASN A 372 -92.315 94.485 -15.805 1.00 30.05 O ANISOU 1879 O ASN A 372 4390 3959 3068 -155 66 -424 O ATOM 1880 CB ASN A 372 -91.010 97.125 -16.446 1.00 33.22 C ANISOU 1880 CB ASN A 372 4623 4581 3417 -43 35 -424 C ATOM 1881 CG ASN A 372 -90.956 98.655 -16.382 1.00 41.29 C ANISOU 1881 CG ASN A 372 5508 5762 4417 -12 42 -416 C ATOM 1882 OD1 ASN A 372 -91.660 99.358 -17.104 1.00 37.25 O ANISOU 1882 OD1 ASN A 372 4942 5333 3876 30 3 -339 O ATOM 1883 ND2 ASN A 372 -90.097 99.169 -15.520 1.00 55.67 N ANISOU 1883 ND2 ASN A 372 7236 7648 6267 -7 76 -488 N ATOM 1884 N ILE A 373 -92.391 94.421 -18.039 1.00 21.41 N ANISOU 1884 N ILE A 373 3336 2793 2007 -224 1 -286 N ATOM 1885 CA ILE A 373 -92.257 92.977 -18.093 1.00 33.75 C ANISOU 1885 CA ILE A 373 4987 4194 3643 -313 22 -272 C ATOM 1886 C ILE A 373 -91.128 92.560 -19.044 1.00 24.01 C ANISOU 1886 C ILE A 373 3712 2933 2475 -359 26 -251 C ATOM 1887 O ILE A 373 -90.988 93.108 -20.128 1.00 23.84 O ANISOU 1887 O ILE A 373 3666 2941 2452 -353 -2 -208 O ATOM 1888 CB ILE A 373 -93.590 92.294 -18.483 1.00 46.67 C ANISOU 1888 CB ILE A 373 6778 5693 5261 -353 -4 -176 C ATOM 1889 CG1 ILE A 373 -94.064 92.769 -19.852 1.00 47.35 C ANISOU 1889 CG1 ILE A 373 6871 5783 5335 -353 -64 -75 C ATOM 1890 CG2 ILE A 373 -94.669 92.590 -17.456 1.00 59.25 C ANISOU 1890 CG2 ILE A 373 8442 7290 6780 -289 3 -185 C ATOM 1891 CD1 ILE A 373 -95.280 92.016 -20.345 1.00 64.96 C ANISOU 1891 CD1 ILE A 373 9235 7872 7576 -397 -103 17 C ATOM 1892 N TYR A 374 -90.335 91.575 -18.639 1.00 27.46 N ANISOU 1892 N TYR A 374 4163 3317 2953 -408 68 -269 N ATOM 1893 CA TYR A 374 -89.155 91.193 -19.399 1.00 21.23 C ANISOU 1893 CA TYR A 374 3389 2502 2174 -477 100 -238 C ATOM 1894 C TYR A 374 -89.247 89.765 -19.870 1.00 15.95 C ANISOU 1894 C TYR A 374 2826 1741 1495 -548 128 -152 C ATOM 1895 O TYR A 374 -89.792 88.921 -19.181 1.00 25.74 O ANISOU 1895 O TYR A 374 4111 2942 2727 -555 142 -151 O ATOM 1896 CB TYR A 374 -87.904 91.380 -18.537 1.00 23.08 C ANISOU 1896 CB TYR A 374 3564 2789 2417 -487 143 -322 C ATOM 1897 CG TYR A 374 -87.573 92.850 -18.310 1.00 22.47 C ANISOU 1897 CG TYR A 374 3386 2826 2325 -416 118 -392 C ATOM 1898 CD1 TYR A 374 -87.999 93.511 -17.168 1.00 19.03 C ANISOU 1898 CD1 TYR A 374 2899 2467 1864 -335 103 -459 C ATOM 1899 CD2 TYR A 374 -86.856 93.570 -19.253 1.00 20.86 C ANISOU 1899 CD2 TYR A 374 3148 2659 2119 -423 112 -382 C ATOM 1900 CE1 TYR A 374 -87.715 94.834 -16.974 1.00 16.26 C ANISOU 1900 CE1 TYR A 374 2476 2224 1477 -265 88 -499 C ATOM 1901 CE2 TYR A 374 -86.559 94.900 -19.072 1.00 16.87 C ANISOU 1901 CE2 TYR A 374 2560 2260 1589 -358 93 -434 C ATOM 1902 CZ TYR A 374 -86.996 95.531 -17.931 1.00 26.83 C ANISOU 1902 CZ TYR A 374 3782 3595 2819 -283 83 -486 C ATOM 1903 OH TYR A 374 -86.709 96.857 -17.746 1.00 30.07 O ANISOU 1903 OH TYR A 374 4122 4105 3197 -234 79 -515 O ATOM 1904 N ALA A 375 -88.726 89.489 -21.057 1.00 15.15 N ANISOU 1904 N ALA A 375 2764 1618 1376 -590 135 -82 N ATOM 1905 CA ALA A 375 -88.565 88.107 -21.474 1.00 11.40 C ANISOU 1905 CA ALA A 375 2317 1124 891 -594 141 -46 C ATOM 1906 C ALA A 375 -87.619 87.389 -20.526 1.00 30.18 C ANISOU 1906 C ALA A 375 4720 3499 3249 -647 212 -84 C ATOM 1907 O ALA A 375 -86.940 88.020 -19.721 1.00 30.99 O ANISOU 1907 O ALA A 375 4783 3625 3365 -668 250 -147 O ATOM 1908 CB ALA A 375 -88.062 88.012 -22.881 1.00 9.45 C ANISOU 1908 CB ALA A 375 2023 897 669 -562 108 -18 C ATOM 1909 N SER A 376 -87.580 86.064 -20.626 1.00 32.75 N ANISOU 1909 N SER A 376 5066 3813 3564 -643 213 -72 N ATOM 1910 CA SER A 376 -86.791 85.279 -19.699 1.00 25.58 C ANISOU 1910 CA SER A 376 4181 2899 2639 -692 277 -107 C ATOM 1911 C SER A 376 -86.447 83.893 -20.248 1.00 36.20 C ANISOU 1911 C SER A 376 5539 4242 3974 -684 269 -89 C ATOM 1912 O SER A 376 -86.915 83.487 -21.325 1.00 17.81 O ANISOU 1912 O SER A 376 3199 1919 1648 -645 216 -53 O ATOM 1913 CB SER A 376 -87.547 85.135 -18.382 1.00 25.45 C ANISOU 1913 CB SER A 376 4209 2856 2604 -718 313 -134 C ATOM 1914 OG SER A 376 -88.794 84.516 -18.628 1.00 31.18 O ANISOU 1914 OG SER A 376 4973 3557 3318 -685 266 -102 O ATOM 1915 N GLY A 377 -85.612 83.178 -19.496 1.00 19.47 N ANISOU 1915 N GLY A 377 3436 2119 1842 -728 325 -119 N ATOM 1916 CA GLY A 377 -85.288 81.807 -19.825 1.00 22.70 C ANISOU 1916 CA GLY A 377 3866 2524 2236 -730 324 -107 C ATOM 1917 C GLY A 377 -84.221 81.642 -20.887 1.00 39.45 C ANISOU 1917 C GLY A 377 5958 4665 4367 -714 311 -92 C ATOM 1918 O GLY A 377 -84.076 80.549 -21.431 1.00 39.75 O ANISOU 1918 O GLY A 377 6009 4703 4392 -707 298 -76 O ATOM 1919 N GLY A 378 -83.488 82.721 -21.179 1.00 42.25 N ANISOU 1919 N GLY A 378 6278 5035 4741 -712 318 -99 N ATOM 1920 CA GLY A 378 -82.400 82.700 -22.144 1.00 20.19 C ANISOU 1920 CA GLY A 378 3463 2253 1955 -700 314 -89 C ATOM 1921 C GLY A 378 -81.287 81.759 -21.733 1.00 36.18 C ANISOU 1921 C GLY A 378 5507 4274 3965 -735 360 -109 C ATOM 1922 O GLY A 378 -80.856 81.765 -20.580 1.00 50.63 O ANISOU 1922 O GLY A 378 7346 6101 5792 -782 415 -148 O ATOM 1923 N THR A 379 -80.831 80.934 -22.675 1.00 44.22 N ANISOU 1923 N THR A 379 6530 5295 4978 -714 339 -86 N ATOM 1924 CA THR A 379 -79.773 79.961 -22.422 1.00 61.57 C ANISOU 1924 CA THR A 379 8749 7487 7159 -744 377 -101 C ATOM 1925 C THR A 379 -78.627 80.139 -23.433 1.00 88.14 C ANISOU 1925 C THR A 379 12102 10859 10530 -729 375 -91 C ATOM 1926 O THR A 379 -78.865 80.454 -24.602 1.00 93.87 O ANISOU 1926 O THR A 379 12803 11481 11380 -727 282 -125 O ATOM 1927 CB THR A 379 -80.320 78.516 -22.482 1.00 63.60 C ANISOU 1927 CB THR A 379 9036 7737 7394 -741 361 -87 C ATOM 1928 OG1 THR A 379 -81.450 78.394 -21.612 1.00 64.15 O ANISOU 1928 OG1 THR A 379 9125 7796 7456 -754 363 -95 O ATOM 1929 CG2 THR A 379 -79.255 77.504 -22.056 1.00 78.06 C ANISOU 1929 CG2 THR A 379 10892 9561 9207 -777 404 -105 C ATOM 1930 N ASP A 380 -77.389 79.943 -22.977 1.00 78.08 N ANISOU 1930 N ASP A 380 10840 9579 9248 -767 425 -118 N ATOM 1931 CA ASP A 380 -76.205 80.150 -23.816 1.00 71.53 C ANISOU 1931 CA ASP A 380 10009 8750 8420 -762 433 -115 C ATOM 1932 C ASP A 380 -75.673 78.855 -24.447 1.00 63.64 C ANISOU 1932 C ASP A 380 9042 7616 7525 -803 371 -167 C ATOM 1933 O ASP A 380 -75.460 78.779 -25.659 1.00 47.49 O ANISOU 1933 O ASP A 380 7017 5558 5470 -790 347 -152 O ATOM 1934 CB ASP A 380 -75.079 80.809 -23.004 1.00 82.95 C ANISOU 1934 CB ASP A 380 11453 10193 9869 -813 498 -159 C ATOM 1935 CG ASP A 380 -75.462 82.176 -22.453 1.00 73.84 C ANISOU 1935 CG ASP A 380 10269 9051 8736 -829 511 -184 C ATOM 1936 OD1 ASP A 380 -76.088 82.965 -23.188 1.00 48.68 O ANISOU 1936 OD1 ASP A 380 7064 5871 5563 -793 469 -161 O ATOM 1937 OD2 ASP A 380 -75.125 82.463 -21.282 1.00 81.11 O ANISOU 1937 OD2 ASP A 380 11179 9978 9661 -878 565 -230 O ATOM 1938 N GLY A 381 -75.436 77.847 -23.617 1.00 62.96 N ANISOU 1938 N GLY A 381 8973 7520 7428 -833 398 -181 N ATOM 1939 CA GLY A 381 -74.907 76.590 -24.104 1.00 74.58 C ANISOU 1939 CA GLY A 381 10492 8968 8878 -851 400 -179 C ATOM 1940 C GLY A 381 -73.576 76.758 -24.810 1.00 73.99 C ANISOU 1940 C GLY A 381 10464 9045 8605 -782 457 -203 C ATOM 1941 O GLY A 381 -72.526 76.403 -24.271 1.00 74.74 O ANISOU 1941 O GLY A 381 10573 9134 8689 -810 504 -226 O TER 1942 GLY A 381 ATOM 1943 N ALA B 102 -107.406 -28.470 -27.033 1.00100.71 N ANISOU 1943 N ALA B 102 13065 12694 12506 -330 -701 424 N ATOM 1944 CA ALA B 102 -106.841 -29.736 -27.487 1.00 93.80 C ANISOU 1944 CA ALA B 102 12213 11808 11621 -341 -714 425 C ATOM 1945 C ALA B 102 -107.902 -30.824 -27.628 1.00 86.86 C ANISOU 1945 C ALA B 102 11315 10942 10744 -290 -682 394 C ATOM 1946 O ALA B 102 -107.853 -31.624 -28.561 1.00110.24 O ANISOU 1946 O ALA B 102 14282 13874 13729 -287 -704 388 O ATOM 1947 CB ALA B 102 -105.723 -30.196 -26.548 1.00 86.29 C ANISOU 1947 CB ALA B 102 11294 10890 10604 -385 -704 441 C ATOM 1948 N ASN B 103 -108.863 -30.851 -26.706 1.00 50.14 N ANISOU 1948 N ASN B 103 6644 6335 6070 -251 -631 377 N ATOM 1949 CA ASN B 103 -109.826 -31.956 -26.638 1.00 46.47 C ANISOU 1949 CA ASN B 103 6167 5889 5599 -207 -598 352 C ATOM 1950 C ASN B 103 -111.250 -31.480 -26.425 1.00 41.31 C ANISOU 1950 C ASN B 103 5477 5254 4965 -157 -567 333 C ATOM 1951 O ASN B 103 -111.509 -30.659 -25.549 1.00 70.84 O ANISOU 1951 O ASN B 103 9205 9026 8687 -150 -544 336 O ATOM 1952 CB ASN B 103 -109.458 -32.912 -25.502 1.00 73.18 C ANISOU 1952 CB ASN B 103 9572 9315 8918 -211 -564 352 C ATOM 1953 CG ASN B 103 -108.331 -33.849 -25.871 1.00101.46 C ANISOU 1953 CG ASN B 103 13188 12882 12480 -253 -589 362 C ATOM 1954 OD1 ASN B 103 -108.265 -34.339 -27.001 1.00111.92 O ANISOU 1954 OD1 ASN B 103 14518 14170 13839 -256 -621 360 O ATOM 1955 ND2 ASN B 103 -107.435 -34.108 -24.921 1.00103.25 N ANISOU 1955 ND2 ASN B 103 13440 13139 12651 -289 -576 372 N ATOM 1956 N PRO B 104 -112.187 -31.994 -27.229 1.00 26.12 N ANISOU 1956 N PRO B 104 3535 3313 3076 -126 -565 313 N ATOM 1957 CA PRO B 104 -113.577 -31.573 -27.046 1.00 23.05 C ANISOU 1957 CA PRO B 104 3110 2945 2702 -84 -535 296 C ATOM 1958 C PRO B 104 -114.136 -32.112 -25.739 1.00 33.53 C ANISOU 1958 C PRO B 104 4435 4326 3979 -53 -486 293 C ATOM 1959 O PRO B 104 -113.632 -33.108 -25.196 1.00 57.51 O ANISOU 1959 O PRO B 104 7497 7376 6976 -58 -474 298 O ATOM 1960 CB PRO B 104 -114.302 -32.217 -28.233 1.00 34.60 C ANISOU 1960 CB PRO B 104 4561 4376 4209 -67 -547 275 C ATOM 1961 CG PRO B 104 -113.232 -32.612 -29.192 1.00 34.14 C ANISOU 1961 CG PRO B 104 4530 4272 4172 -101 -593 283 C ATOM 1962 CD PRO B 104 -112.032 -32.914 -28.366 1.00 30.88 C ANISOU 1962 CD PRO B 104 4149 3877 3706 -132 -593 305 C ATOM 1963 N SER B 105 -115.163 -31.451 -25.226 1.00 13.48 N ANISOU 1963 N SER B 105 1867 1815 1440 -21 -459 286 N ATOM 1964 CA SER B 105 -115.867 -31.951 -24.071 1.00 23.31 C ANISOU 1964 CA SER B 105 3108 3104 2645 16 -415 283 C ATOM 1965 C SER B 105 -116.638 -33.135 -24.601 1.00 36.99 C ANISOU 1965 C SER B 105 4837 4827 4389 41 -406 272 C ATOM 1966 O SER B 105 -116.741 -33.299 -25.808 1.00 40.18 O ANISOU 1966 O SER B 105 5236 5195 4835 31 -432 263 O ATOM 1967 CB SER B 105 -116.812 -30.892 -23.524 1.00 31.73 C ANISOU 1967 CB SER B 105 4145 4196 3713 42 -395 276 C ATOM 1968 OG SER B 105 -116.106 -29.702 -23.241 1.00 56.58 O ANISOU 1968 OG SER B 105 7293 7346 6857 11 -410 286 O ATOM 1969 N ARG B 106 -117.165 -33.975 -23.722 1.00 20.24 N ANISOU 1969 N ARG B 106 2722 2734 2233 73 -371 274 N ATOM 1970 CA ARG B 106 -117.960 -35.087 -24.201 1.00 27.02 C ANISOU 1970 CA ARG B 106 3578 3584 3105 93 -362 269 C ATOM 1971 C ARG B 106 -119.027 -35.545 -23.189 1.00 31.16 C ANISOU 1971 C ARG B 106 4095 4141 3603 139 -319 274 C ATOM 1972 O ARG B 106 -118.855 -35.428 -21.986 1.00 29.53 O ANISOU 1972 O ARG B 106 3914 3942 3365 150 -298 272 O ATOM 1973 CB ARG B 106 -117.051 -36.245 -24.626 1.00 19.50 C ANISOU 1973 CB ARG B 106 2662 2604 2143 65 -380 270 C ATOM 1974 CG ARG B 106 -117.777 -37.392 -25.313 1.00 26.83 C ANISOU 1974 CG ARG B 106 3595 3510 3090 78 -380 260 C ATOM 1975 CD ARG B 106 -116.824 -38.528 -25.576 1.00 29.58 C ANISOU 1975 CD ARG B 106 3986 3834 3417 50 -397 258 C ATOM 1976 NE ARG B 106 -115.693 -38.102 -26.388 1.00 17.70 N ANISOU 1976 NE ARG B 106 2492 2302 1931 10 -439 256 N ATOM 1977 CZ ARG B 106 -114.710 -38.907 -26.771 1.00 34.45 C ANISOU 1977 CZ ARG B 106 4648 4403 4037 -23 -462 255 C ATOM 1978 NH1 ARG B 106 -114.731 -40.186 -26.428 1.00 16.61 N ANISOU 1978 NH1 ARG B 106 2419 2147 1743 -20 -446 252 N ATOM 1979 NH2 ARG B 106 -113.709 -38.436 -27.505 1.00 50.23 N ANISOU 1979 NH2 ARG B 106 6652 6377 6055 -59 -502 260 N ATOM 1980 N LEU B 107 -120.142 -36.046 -23.703 1.00 31.48 N ANISOU 1980 N LEU B 107 4111 4176 3674 151 -307 272 N ATOM 1981 CA LEU B 107 -121.206 -36.583 -22.874 1.00 19.63 C ANISOU 1981 CA LEU B 107 2613 2649 2197 104 -308 296 C ATOM 1982 C LEU B 107 -121.288 -38.073 -23.170 1.00 13.14 C ANISOU 1982 C LEU B 107 1813 1823 1355 136 -294 297 C ATOM 1983 O LEU B 107 -121.507 -38.469 -24.308 1.00 21.71 O ANISOU 1983 O LEU B 107 2895 2892 2460 152 -304 281 O ATOM 1984 CB LEU B 107 -122.522 -35.912 -23.259 1.00 11.14 C ANISOU 1984 CB LEU B 107 1532 1542 1158 123 -320 270 C ATOM 1985 CG LEU B 107 -123.730 -36.115 -22.370 1.00 13.38 C ANISOU 1985 CG LEU B 107 1802 1853 1427 168 -280 273 C ATOM 1986 CD1 LEU B 107 -123.329 -35.820 -20.972 1.00 19.71 C ANISOU 1986 CD1 LEU B 107 2604 2692 2193 179 -248 284 C ATOM 1987 CD2 LEU B 107 -124.861 -35.208 -22.787 1.00 7.26 C ANISOU 1987 CD2 LEU B 107 993 1083 683 173 -283 259 C ATOM 1988 N ILE B 108 -121.086 -38.907 -22.164 1.00 40.34 N ANISOU 1988 N ILE B 108 5302 5265 4760 153 -270 298 N ATOM 1989 CA ILE B 108 -121.368 -40.332 -22.328 1.00 21.85 C ANISOU 1989 CA ILE B 108 2993 2903 2407 189 -245 287 C ATOM 1990 C ILE B 108 -122.407 -40.696 -21.294 1.00 27.89 C ANISOU 1990 C ILE B 108 3751 3679 3166 241 -191 289 C ATOM 1991 O ILE B 108 -122.199 -40.438 -20.115 1.00 27.41 O ANISOU 1991 O ILE B 108 3685 3650 3080 253 -163 300 O ATOM 1992 CB ILE B 108 -120.114 -41.182 -22.144 1.00 27.86 C ANISOU 1992 CB ILE B 108 3803 3660 3122 174 -243 285 C ATOM 1993 CG1 ILE B 108 -118.977 -40.626 -23.010 1.00 30.30 C ANISOU 1993 CG1 ILE B 108 4105 3971 3437 129 -288 283 C ATOM 1994 CG2 ILE B 108 -120.404 -42.634 -22.494 1.00 33.79 C ANISOU 1994 CG2 ILE B 108 4601 4375 3864 203 -223 268 C ATOM 1995 CD1 ILE B 108 -117.620 -41.170 -22.672 1.00 22.67 C ANISOU 1995 CD1 ILE B 108 3183 3008 2422 98 -290 280 C ATOM 1996 N VAL B 109 -123.541 -41.249 -21.733 1.00 44.50 N ANISOU 1996 N VAL B 109 5849 5765 5295 272 -176 282 N ATOM 1997 CA VAL B 109 -124.607 -41.684 -20.817 1.00 15.65 C ANISOU 1997 CA VAL B 109 2182 2122 1641 322 -123 292 C ATOM 1998 C VAL B 109 -124.592 -43.164 -20.704 1.00 13.84 C ANISOU 1998 C VAL B 109 2000 1864 1393 358 -88 292 C ATOM 1999 O VAL B 109 -124.505 -43.857 -21.709 1.00 50.45 O ANISOU 1999 O VAL B 109 6668 6465 6034 350 -105 277 O ATOM 2000 CB VAL B 109 -125.995 -41.297 -21.308 1.00 19.63 C ANISOU 2000 CB VAL B 109 2651 2626 2182 328 -125 288 C ATOM 2001 CG1 VAL B 109 -127.032 -41.975 -20.459 1.00 23.13 C ANISOU 2001 CG1 VAL B 109 3089 3075 2624 377 -74 302 C ATOM 2002 CG2 VAL B 109 -126.169 -39.767 -21.274 1.00 22.70 C ANISOU 2002 CG2 VAL B 109 2997 3042 2586 299 -150 287 C ATOM 2003 N ALA B 110 -124.678 -43.661 -19.475 1.00 21.71 N ANISOU 2003 N ALA B 110 3005 2875 2370 400 -37 307 N ATOM 2004 CA ALA B 110 -124.648 -45.099 -19.225 1.00 11.87 C ANISOU 2004 CA ALA B 110 1803 1593 1115 429 9 302 C ATOM 2005 C ALA B 110 -125.669 -45.500 -18.167 1.00 16.46 C ANISOU 2005 C ALA B 110 2367 2176 1711 487 62 323 C ATOM 2006 O ALA B 110 -126.227 -44.652 -17.483 1.00 31.47 O ANISOU 2006 O ALA B 110 4223 4117 3616 506 63 345 O ATOM 2007 CB ALA B 110 -123.258 -45.534 -18.819 1.00 14.01 C ANISOU 2007 CB ALA B 110 2104 1863 1356 397 22 280 C ATOM 2008 N ILE B 111 -125.937 -46.798 -18.055 1.00 22.07 N ANISOU 2008 N ILE B 111 3106 2841 2439 506 106 309 N ATOM 2009 CA ILE B 111 -126.853 -47.287 -17.042 1.00 9.62 C ANISOU 2009 CA ILE B 111 1516 1257 883 563 156 331 C ATOM 2010 C ILE B 111 -126.206 -48.377 -16.241 1.00 25.06 C ANISOU 2010 C ILE B 111 3497 3184 2841 573 211 307 C ATOM 2011 O ILE B 111 -125.657 -49.321 -16.804 1.00 43.81 O ANISOU 2011 O ILE B 111 5912 5518 5216 545 223 272 O ATOM 2012 CB ILE B 111 -128.144 -47.803 -17.657 1.00 20.10 C ANISOU 2012 CB ILE B 111 2849 2550 2239 584 160 343 C ATOM 2013 CG1 ILE B 111 -129.101 -48.298 -16.574 1.00 18.01 C ANISOU 2013 CG1 ILE B 111 2571 2274 1997 644 207 375 C ATOM 2014 CG2 ILE B 111 -127.860 -48.911 -18.651 1.00 28.84 C ANISOU 2014 CG2 ILE B 111 4002 3602 3354 554 165 305 C ATOM 2015 CD1 ILE B 111 -130.489 -48.652 -17.121 1.00 26.85 C ANISOU 2015 CD1 ILE B 111 3683 3373 3144 640 206 380 C ATOM 2016 N GLU B 112 -126.241 -48.233 -14.920 1.00 31.38 N ANISOU 2016 N GLU B 112 4272 4008 3644 611 246 321 N ATOM 2017 CA GLU B 112 -125.729 -49.253 -14.022 1.00 10.90 C ANISOU 2017 CA GLU B 112 1694 1388 1061 626 306 295 C ATOM 2018 C GLU B 112 -126.910 -50.103 -13.593 1.00 30.07 C ANISOU 2018 C GLU B 112 4121 3770 3533 685 346 315 C ATOM 2019 O GLU B 112 -127.899 -49.574 -13.090 1.00 22.40 O ANISOU 2019 O GLU B 112 3114 2820 2577 730 341 358 O ATOM 2020 CB GLU B 112 -125.074 -48.604 -12.807 1.00 11.15 C ANISOU 2020 CB GLU B 112 1694 1470 1073 633 321 294 C ATOM 2021 CG GLU B 112 -124.084 -49.510 -12.110 1.00 35.16 C ANISOU 2021 CG GLU B 112 4754 4494 4112 620 375 249 C ATOM 2022 CD GLU B 112 -123.279 -48.804 -11.036 1.00 38.39 C ANISOU 2022 CD GLU B 112 5132 4959 4493 612 386 239 C ATOM 2023 OE1 GLU B 112 -122.474 -49.467 -10.353 1.00 39.51 O ANISOU 2023 OE1 GLU B 112 5285 5096 4633 599 434 198 O ATOM 2024 OE2 GLU B 112 -123.439 -47.586 -10.870 1.00 33.27 O ANISOU 2024 OE2 GLU B 112 4450 4365 3826 615 351 269 O ATOM 2025 N ILE B 113 -126.823 -51.412 -13.821 1.00 27.63 N ANISOU 2025 N ILE B 113 3852 3400 3245 682 385 285 N ATOM 2026 CA ILE B 113 -127.849 -52.336 -13.347 1.00 18.87 C ANISOU 2026 CA ILE B 113 2747 2239 2184 736 429 302 C ATOM 2027 C ILE B 113 -127.282 -53.545 -12.592 1.00 22.79 C ANISOU 2027 C ILE B 113 3265 2690 2706 748 497 262 C ATOM 2028 O ILE B 113 -126.197 -54.027 -12.916 1.00 28.38 O ANISOU 2028 O ILE B 113 4001 3389 3392 699 510 212 O ATOM 2029 CB ILE B 113 -128.690 -52.873 -14.487 1.00 21.34 C ANISOU 2029 CB ILE B 113 3091 2508 2509 726 415 309 C ATOM 2030 CG1 ILE B 113 -129.074 -51.749 -15.439 1.00 31.06 C ANISOU 2030 CG1 ILE B 113 4305 3782 3715 700 349 332 C ATOM 2031 CG2 ILE B 113 -129.942 -53.574 -13.938 1.00 26.55 C ANISOU 2031 CG2 ILE B 113 3750 3121 3215 786 450 344 C ATOM 2032 CD1 ILE B 113 -129.760 -52.237 -16.685 1.00 18.13 C ANISOU 2032 CD1 ILE B 113 2696 2108 2086 678 333 327 C ATOM 2033 N VAL B 114 -128.036 -54.013 -11.589 1.00 28.59 N ANISOU 2033 N VAL B 114 3982 3394 3486 812 538 284 N ATOM 2034 CA VAL B 114 -127.794 -55.275 -10.877 1.00 13.59 C ANISOU 2034 CA VAL B 114 2100 1436 1628 833 608 249 C ATOM 2035 C VAL B 114 -129.107 -55.964 -10.559 1.00 51.95 C ANISOU 2035 C VAL B 114 6953 6247 6537 866 617 285 C ATOM 2036 O VAL B 114 -130.130 -55.292 -10.407 1.00 49.14 O ANISOU 2036 O VAL B 114 6565 5922 6183 883 578 339 O ATOM 2037 CB VAL B 114 -127.160 -55.068 -9.506 1.00 24.72 C ANISOU 2037 CB VAL B 114 3472 2873 3047 858 643 231 C ATOM 2038 CG1 VAL B 114 -125.984 -56.000 -9.334 1.00 38.41 C ANISOU 2038 CG1 VAL B 114 5232 4582 4779 819 696 158 C ATOM 2039 CG2 VAL B 114 -126.766 -53.633 -9.308 1.00 57.49 C ANISOU 2039 CG2 VAL B 114 7583 7109 7152 843 596 249 C ATOM 2040 N GLU B 115 -129.069 -57.296 -10.431 1.00 37.83 N ANISOU 2040 N GLU B 115 5193 4396 4786 858 663 252 N ATOM 2041 CA GLU B 115 -130.195 -58.078 -9.907 1.00 19.11 C ANISOU 2041 CA GLU B 115 2814 1982 2466 881 674 280 C ATOM 2042 C GLU B 115 -130.287 -57.928 -8.387 1.00 26.75 C ANISOU 2042 C GLU B 115 3732 2961 3471 926 691 292 C ATOM 2043 O GLU B 115 -129.299 -58.134 -7.672 1.00 26.22 O ANISOU 2043 O GLU B 115 3655 2894 3414 929 731 246 O ATOM 2044 CB GLU B 115 -130.033 -59.562 -10.233 1.00 31.78 C ANISOU 2044 CB GLU B 115 4462 3515 4099 856 719 236 C ATOM 2045 CG GLU B 115 -130.374 -59.965 -11.657 1.00 59.63 C ANISOU 2045 CG GLU B 115 8034 7019 7604 815 702 232 C ATOM 2046 CD GLU B 115 -131.140 -61.295 -11.728 1.00 83.02 C ANISOU 2046 CD GLU B 115 11020 9915 10607 810 730 230 C ATOM 2047 OE1 GLU B 115 -132.117 -61.485 -10.958 1.00 50.80 O ANISOU 2047 OE1 GLU B 115 6917 5818 6565 847 731 270 O ATOM 2048 OE2 GLU B 115 -130.761 -62.154 -12.557 1.00100.56 O ANISOU 2048 OE2 GLU B 115 13284 12103 12821 768 751 187 O ATOM 2049 N ASP B 116 -131.463 -57.556 -7.886 1.00 40.45 N ANISOU 2049 N ASP B 116 5434 4710 5225 957 662 349 N ATOM 2050 CA ASP B 116 -131.684 -57.556 -6.439 1.00 48.39 C ANISOU 2050 CA ASP B 116 6394 5717 6275 1002 676 361 C ATOM 2051 C ASP B 116 -133.161 -57.660 -6.072 1.00 57.67 C ANISOU 2051 C ASP B 116 7552 6879 7482 1029 651 419 C ATOM 2052 O ASP B 116 -134.028 -57.527 -6.943 1.00 46.91 O ANISOU 2052 O ASP B 116 6207 5520 6098 1009 619 453 O ATOM 2053 CB ASP B 116 -131.075 -56.315 -5.788 1.00 33.80 C ANISOU 2053 CB ASP B 116 4501 3942 4399 1016 661 363 C ATOM 2054 CG ASP B 116 -130.439 -56.618 -4.446 1.00 41.66 C ANISOU 2054 CG ASP B 116 5462 4930 5435 1046 704 326 C ATOM 2055 OD1 ASP B 116 -130.801 -57.654 -3.843 1.00 66.57 O ANISOU 2055 OD1 ASP B 116 8618 8026 8651 1066 733 316 O ATOM 2056 OD2 ASP B 116 -129.575 -55.824 -3.992 1.00 44.63 O ANISOU 2056 OD2 ASP B 116 5810 5361 5785 1047 708 304 O ATOM 2057 N GLU B 117 -133.421 -57.930 -4.785 1.00 55.45 N ANISOU 2057 N GLU B 117 7235 6581 7253 1072 667 426 N ATOM 2058 CA GLU B 117 -134.747 -57.834 -4.177 1.00 18.24 C ANISOU 2058 CA GLU B 117 2494 1865 2569 1104 638 485 C ATOM 2059 C GLU B 117 -135.117 -56.356 -3.941 1.00 37.08 C ANISOU 2059 C GLU B 117 4836 4337 4915 1109 589 527 C ATOM 2060 O GLU B 117 -134.493 -55.679 -3.127 1.00 39.93 O ANISOU 2060 O GLU B 117 5157 4741 5273 1128 592 514 O ATOM 2061 CB GLU B 117 -134.755 -58.558 -2.826 1.00 46.25 C ANISOU 2061 CB GLU B 117 6015 5369 6190 1151 670 472 C ATOM 2062 CG GLU B 117 -134.297 -60.014 -2.865 1.00 65.51 C ANISOU 2062 CG GLU B 117 8490 7726 8675 1146 724 421 C ATOM 2063 CD GLU B 117 -135.273 -60.927 -3.594 1.00 66.36 C ANISOU 2063 CD GLU B 117 8641 7775 8797 1133 721 447 C ATOM 2064 OE1 GLU B 117 -136.487 -60.878 -3.280 1.00 38.21 O ANISOU 2064 OE1 GLU B 117 5062 4202 5253 1159 690 504 O ATOM 2065 OE2 GLU B 117 -134.829 -61.684 -4.491 1.00 72.82 O ANISOU 2065 OE2 GLU B 117 9507 8557 9604 1096 748 409 O ATOM 2066 N ILE B 118 -136.073 -55.849 -4.665 1.00 43.52 N ANISOU 2066 N ILE B 118 5656 5179 5700 1089 547 571 N ATOM 2067 CA ILE B 118 -136.413 -54.475 -4.500 1.00 41.00 C ANISOU 2067 CA ILE B 118 5296 4943 5339 1083 502 606 C ATOM 2068 C ILE B 118 -137.712 -54.487 -3.771 1.00 48.41 C ANISOU 2068 C ILE B 118 6206 5885 6303 1109 474 661 C ATOM 2069 O ILE B 118 -138.360 -55.516 -3.614 1.00 37.91 O ANISOU 2069 O ILE B 118 4897 4494 5014 1123 482 679 O ATOM 2070 CB ILE B 118 -136.570 -53.782 -5.846 1.00 32.26 C ANISOU 2070 CB ILE B 118 4210 3875 4172 1032 471 608 C ATOM 2071 CG1 ILE B 118 -137.828 -54.254 -6.543 1.00 37.80 C ANISOU 2071 CG1 ILE B 118 4934 4550 4877 1013 451 639 C ATOM 2072 CG2 ILE B 118 -135.458 -54.168 -6.710 1.00 38.80 C ANISOU 2072 CG2 ILE B 118 5078 4683 4981 1007 496 556 C ATOM 2073 CD1 ILE B 118 -137.988 -53.718 -7.877 1.00 39.97 C ANISOU 2073 CD1 ILE B 118 5223 4864 5101 963 419 635 C ATOM 2074 N PRO B 119 -138.295 -53.324 -3.549 1.00 42.58 N ANISOU 2074 N PRO B 119 5421 5218 5540 1113 442 689 N ATOM 2075 CA PRO B 119 -139.664 -53.272 -3.068 1.00 42.83 C ANISOU 2075 CA PRO B 119 5421 5258 5594 1139 415 740 C ATOM 2076 C PRO B 119 -140.691 -53.193 -4.192 1.00 66.43 C ANISOU 2076 C PRO B 119 8442 8202 8598 1129 401 775 C ATOM 2077 O PRO B 119 -140.411 -52.630 -5.216 1.00 95.13 O ANISOU 2077 O PRO B 119 12087 11769 12289 1163 419 784 O ATOM 2078 CB PRO B 119 -139.666 -51.986 -2.278 1.00 52.60 C ANISOU 2078 CB PRO B 119 6618 6589 6778 1118 379 757 C ATOM 2079 CG PRO B 119 -138.342 -51.804 -1.900 1.00 59.52 C ANISOU 2079 CG PRO B 119 7484 7495 7636 1117 400 713 C ATOM 2080 CD PRO B 119 -137.531 -52.208 -3.018 1.00 55.09 C ANISOU 2080 CD PRO B 119 6976 6878 7079 1100 432 671 C ATOM 2081 N LEU B 120 -141.877 -53.757 -4.029 1.00 30.00 N ATOM 2082 CA LEU B 120 -142.815 -53.702 -5.161 1.00 30.00 C ATOM 2083 C LEU B 120 -143.979 -52.733 -5.053 1.00 30.00 C ATOM 2084 O LEU B 120 -144.892 -52.747 -5.875 1.00 30.00 O ATOM 2085 CB LEU B 120 -143.293 -55.088 -5.641 1.00 20.00 C ATOM 2086 CG LEU B 120 -143.143 -54.990 -7.153 1.00 20.00 C ATOM 2087 CD1 LEU B 120 -144.082 -55.777 -7.970 1.00 20.00 C ATOM 2088 CD2 LEU B 120 -143.365 -53.562 -7.387 1.00 20.00 C ATOM 2089 N THR B 121 -143.951 -51.895 -4.036 1.00 30.00 N ATOM 2090 CA THR B 121 -144.980 -50.892 -3.887 1.00 30.00 C ATOM 2091 C THR B 121 -144.958 -49.952 -5.090 1.00 30.00 C ATOM 2092 O THR B 121 -145.391 -50.323 -6.192 1.00 30.00 O ATOM 2093 CB THR B 121 -144.881 -50.165 -2.523 1.00 20.00 C ATOM 2094 OG1 THR B 121 -145.359 -48.832 -2.647 1.00 20.00 O ATOM 2095 CG2 THR B 121 -143.468 -50.141 -2.019 1.00 20.00 C ATOM 2096 N LYS B 147 -140.132 -58.662 -0.413 1.00 52.41 N ANISOU 2096 N LYS B 147 6709 6100 7103 1285 540 716 N ATOM 2097 CA LYS B 147 -139.894 -57.884 -1.621 1.00 43.06 C ANISOU 2097 CA LYS B 147 5545 4974 5841 1230 524 712 C ATOM 2098 C LYS B 147 -140.346 -58.635 -2.867 1.00 45.55 C ANISOU 2098 C LYS B 147 5918 5246 6141 1192 529 715 C ATOM 2099 O LYS B 147 -141.487 -59.076 -2.957 1.00 59.24 O ANISOU 2099 O LYS B 147 7667 6948 7894 1197 510 759 O ATOM 2100 CB LYS B 147 -138.412 -57.533 -1.752 1.00 53.81 C ANISOU 2100 CB LYS B 147 6904 6366 7177 1214 554 651 C ATOM 2101 CG LYS B 147 -137.736 -57.084 -0.462 1.00 71.84 C ANISOU 2101 CG LYS B 147 9135 8676 9486 1253 565 630 C ATOM 2102 CD LYS B 147 -138.286 -55.762 0.041 1.00 86.49 C ANISOU 2102 CD LYS B 147 10941 10612 11311 1263 519 674 C ATOM 2103 CE LYS B 147 -137.415 -55.197 1.156 1.00 93.10 C ANISOU 2103 CE LYS B 147 11726 11486 12161 1291 532 643 C ATOM 2104 NZ LYS B 147 -137.220 -56.171 2.270 1.00 94.10 N ANISOU 2104 NZ LYS B 147 11836 11549 12370 1340 566 616 N ATOM 2105 N VAL B 148 -139.435 -58.753 -3.829 1.00 55.83 N ANISOU 2105 N VAL B 148 7254 6550 7409 1153 552 668 N ATOM 2106 CA VAL B 148 -139.646 -59.466 -5.093 1.00 43.81 C ANISOU 2106 CA VAL B 148 5787 4989 5869 1113 562 657 C ATOM 2107 C VAL B 148 -138.357 -59.371 -5.895 1.00 39.59 C ANISOU 2107 C VAL B 148 5277 4470 5297 1077 586 598 C ATOM 2108 O VAL B 148 -137.524 -58.505 -5.639 1.00 43.77 O ANISOU 2108 O VAL B 148 5779 5052 5801 1078 582 580 O ATOM 2109 CB VAL B 148 -140.777 -58.869 -5.940 1.00 40.48 C ANISOU 2109 CB VAL B 148 5371 4605 5405 1083 515 703 C ATOM 2110 CG1 VAL B 148 -140.313 -57.622 -6.629 1.00 44.23 C ANISOU 2110 CG1 VAL B 148 5832 5160 5815 1048 490 691 C ATOM 2111 CG2 VAL B 148 -141.244 -59.879 -6.970 1.00 57.36 C ANISOU 2111 CG2 VAL B 148 7564 6685 7544 1053 529 698 C ATOM 2112 N ASP B 149 -138.179 -60.259 -6.862 1.00 52.04 N ANISOU 2112 N ASP B 149 6904 5999 6869 1045 611 569 N ATOM 2113 CA ASP B 149 -136.920 -60.291 -7.590 1.00 38.83 C ANISOU 2113 CA ASP B 149 5256 4332 5165 1012 634 511 C ATOM 2114 C ASP B 149 -137.032 -59.536 -8.897 1.00 53.63 C ANISOU 2114 C ASP B 149 7146 6254 6978 968 599 516 C ATOM 2115 O ASP B 149 -137.817 -59.911 -9.774 1.00 48.78 O ANISOU 2115 O ASP B 149 6562 5619 6354 943 588 530 O ATOM 2116 CB ASP B 149 -136.460 -61.724 -7.831 1.00 50.00 C ANISOU 2116 CB ASP B 149 6716 5670 6613 999 687 464 C ATOM 2117 CG ASP B 149 -135.206 -61.794 -8.660 1.00 65.36 C ANISOU 2117 CG ASP B 149 8690 7622 8522 958 708 405 C ATOM 2118 OD1 ASP B 149 -134.116 -61.463 -8.139 1.00 93.04 O ANISOU 2118 OD1 ASP B 149 12177 11149 12024 964 725 370 O ATOM 2119 OD2 ASP B 149 -135.307 -62.189 -9.839 1.00 56.88 O ANISOU 2119 OD2 ASP B 149 7658 6532 7423 918 708 391 O ATOM 2120 N GLY B 150 -136.242 -58.464 -8.993 1.00 64.51 N ANISOU 2120 N GLY B 150 8502 7693 8315 959 581 504 N ATOM 2121 CA GLY B 150 -136.204 -57.575 -10.142 1.00 52.25 C ANISOU 2121 CA GLY B 150 6956 6191 6707 920 544 504 C ATOM 2122 C GLY B 150 -134.841 -56.911 -10.317 1.00 37.65 C ANISOU 2122 C GLY B 150 5103 4377 4824 908 546 467 C ATOM 2123 O GLY B 150 -133.810 -57.577 -10.279 1.00 55.00 O ANISOU 2123 O GLY B 150 7326 6541 7032 904 585 421 O ATOM 2124 N LEU B 151 -134.826 -55.593 -10.475 1.00 36.36 N ANISOU 2124 N LEU B 151 4908 4285 4622 899 504 485 N ATOM 2125 CA LEU B 151 -133.603 -54.887 -10.852 1.00 34.36 C ANISOU 2125 CA LEU B 151 4656 4067 4330 883 498 454 C ATOM 2126 C LEU B 151 -133.373 -53.571 -10.115 1.00 26.30 C ANISOU 2126 C LEU B 151 3584 3121 3288 899 473 474 C ATOM 2127 O LEU B 151 -134.315 -52.828 -9.857 1.00 33.46 O ANISOU 2127 O LEU B 151 4454 4070 4189 901 440 512 O ATOM 2128 CB LEU B 151 -133.621 -54.613 -12.356 1.00 25.92 C ANISOU 2128 CB LEU B 151 3615 3008 3226 838 466 442 C ATOM 2129 CG LEU B 151 -133.477 -55.834 -13.262 1.00 31.22 C ANISOU 2129 CG LEU B 151 4342 3612 3908 814 493 408 C ATOM 2130 CD1 LEU B 151 -133.655 -55.421 -14.680 1.00 41.34 C ANISOU 2130 CD1 LEU B 151 5641 4909 5158 773 454 401 C ATOM 2131 CD2 LEU B 151 -132.110 -56.475 -13.070 1.00 35.42 C ANISOU 2131 CD2 LEU B 151 4903 4110 4445 815 536 359 C ATOM 2132 N LYS B 152 -132.109 -53.294 -9.796 1.00 37.08 N ANISOU 2132 N LYS B 152 4947 4501 4639 906 490 445 N ATOM 2133 CA LYS B 152 -131.668 -52.011 -9.235 1.00 23.44 C ANISOU 2133 CA LYS B 152 3176 2846 2883 915 468 456 C ATOM 2134 C LYS B 152 -130.906 -51.258 -10.322 1.00 32.46 C ANISOU 2134 C LYS B 152 4334 4020 3977 881 437 440 C ATOM 2135 O LYS B 152 -129.886 -51.730 -10.801 1.00 38.83 O ANISOU 2135 O LYS B 152 5180 4798 4776 873 459 402 O ATOM 2136 CB LYS B 152 -130.710 -52.240 -8.071 1.00 45.52 C ANISOU 2136 CB LYS B 152 5958 5641 5698 948 512 428 C ATOM 2137 CG LYS B 152 -131.227 -51.851 -6.690 1.00 65.59 C ANISOU 2137 CG LYS B 152 8445 8212 8263 985 513 455 C ATOM 2138 CD LYS B 152 -130.190 -52.195 -5.607 1.00 69.00 C ANISOU 2138 CD LYS B 152 8862 8638 8718 1010 561 413 C ATOM 2139 CE LYS B 152 -130.629 -51.741 -4.216 1.00 81.93 C ANISOU 2139 CE LYS B 152 10441 10309 10381 1047 559 435 C ATOM 2140 NZ LYS B 152 -131.786 -52.518 -3.678 1.00 83.09 N ANISOU 2140 NZ LYS B 152 10582 10406 10583 1074 562 463 N ATOM 2141 N ALA B 153 -131.387 -50.080 -10.702 1.00 33.41 N ANISOU 2141 N ALA B 153 4425 4201 4068 857 388 464 N ATOM 2142 CA ALA B 153 -130.782 -49.356 -11.800 1.00 15.85 C ANISOU 2142 CA ALA B 153 2213 2003 1806 818 350 450 C ATOM 2143 C ALA B 153 -130.477 -47.930 -11.432 1.00 44.63 C ANISOU 2143 C ALA B 153 5813 5726 5419 809 319 462 C ATOM 2144 O ALA B 153 -131.150 -47.355 -10.581 1.00 38.54 O ANISOU 2144 O ALA B 153 4997 4994 4653 822 316 485 O ATOM 2145 CB ALA B 153 -131.679 -49.378 -13.003 1.00 18.51 C ANISOU 2145 CB ALA B 153 2561 2329 2142 777 317 451 C ATOM 2146 N ARG B 154 -129.462 -47.368 -12.093 1.00 44.75 N ANISOU 2146 N ARG B 154 5843 5760 5399 783 293 446 N ATOM 2147 CA ARG B 154 -129.181 -45.948 -11.993 1.00 19.49 C ANISOU 2147 CA ARG B 154 2604 2633 2169 755 255 451 C ATOM 2148 C ARG B 154 -128.446 -45.363 -13.204 1.00 21.61 C ANISOU 2148 C ARG B 154 2892 2911 2408 695 209 429 C ATOM 2149 O ARG B 154 -127.508 -45.937 -13.723 1.00 32.78 O ANISOU 2149 O ARG B 154 4349 4294 3810 667 211 400 O ATOM 2150 CB ARG B 154 -128.429 -45.655 -10.706 1.00 15.15 C ANISOU 2150 CB ARG B 154 2030 2120 1606 787 282 453 C ATOM 2151 CG ARG B 154 -127.015 -46.113 -10.707 1.00 20.10 C ANISOU 2151 CG ARG B 154 2690 2733 2215 745 301 401 C ATOM 2152 CD ARG B 154 -126.367 -45.682 -9.429 1.00 33.81 C ANISOU 2152 CD ARG B 154 4392 4515 3938 756 326 390 C ATOM 2153 NE ARG B 154 -125.075 -46.316 -9.248 1.00 38.31 N ANISOU 2153 NE ARG B 154 4992 5069 4493 718 356 339 N ATOM 2154 CZ ARG B 154 -124.413 -46.324 -8.104 1.00 35.09 C ANISOU 2154 CZ ARG B 154 4564 4689 4080 724 394 314 C ATOM 2155 NH1 ARG B 154 -124.940 -45.744 -7.032 1.00 36.86 N ANISOU 2155 NH1 ARG B 154 4735 4956 4316 773 406 337 N ATOM 2156 NH2 ARG B 154 -123.240 -46.933 -8.034 1.00 37.86 N ANISOU 2156 NH2 ARG B 154 4945 5027 4414 680 422 263 N ATOM 2157 N ILE B 155 -128.886 -44.201 -13.655 1.00 39.45 N ANISOU 2157 N ILE B 155 5113 5210 4668 649 169 422 N ATOM 2158 CA ILE B 155 -128.227 -43.543 -14.758 1.00 22.98 C ANISOU 2158 CA ILE B 155 3035 3128 2569 589 123 397 C ATOM 2159 C ILE B 155 -126.964 -42.902 -14.239 1.00 22.74 C ANISOU 2159 C ILE B 155 3004 3134 2503 576 115 394 C ATOM 2160 O ILE B 155 -126.975 -42.297 -13.171 1.00 27.11 O ANISOU 2160 O ILE B 155 3522 3733 3045 597 130 408 O ATOM 2161 CB ILE B 155 -129.121 -42.485 -15.392 1.00 23.42 C ANISOU 2161 CB ILE B 155 3050 3205 2644 548 88 388 C ATOM 2162 CG1 ILE B 155 -130.421 -43.118 -15.858 1.00 22.25 C ANISOU 2162 CG1 ILE B 155 2905 3028 2522 556 96 394 C ATOM 2163 CG2 ILE B 155 -128.418 -41.859 -16.567 1.00 34.25 C ANISOU 2163 CG2 ILE B 155 4432 4569 4014 491 41 363 C ATOM 2164 CD1 ILE B 155 -130.191 -44.264 -16.793 1.00 31.71 C ANISOU 2164 CD1 ILE B 155 4153 4170 3725 555 97 381 C ATOM 2165 N ILE B 156 -125.876 -43.057 -14.992 1.00 25.47 N ANISOU 2165 N ILE B 156 3389 3463 2826 537 92 375 N ATOM 2166 CA ILE B 156 -124.591 -42.454 -14.667 1.00 17.83 C ANISOU 2166 CA ILE B 156 2427 2528 1818 504 80 367 C ATOM 2167 C ILE B 156 -123.918 -41.875 -15.903 1.00 38.61 C ANISOU 2167 C ILE B 156 5071 5146 4453 434 22 345 C ATOM 2168 O ILE B 156 -124.282 -42.211 -17.024 1.00 56.46 O ANISOU 2168 O ILE B 156 7346 7368 6738 420 -1 335 O ATOM 2169 CB ILE B 156 -123.632 -43.450 -14.027 1.00 18.64 C ANISOU 2169 CB ILE B 156 2566 2617 1901 504 122 346 C ATOM 2170 CG1 ILE B 156 -123.526 -44.698 -14.877 1.00 40.00 C ANISOU 2170 CG1 ILE B 156 5317 5258 4623 491 130 322 C ATOM 2171 CG2 ILE B 156 -124.106 -43.840 -12.631 1.00 47.20 C ANISOU 2171 CG2 ILE B 156 6156 6246 5532 560 180 353 C ATOM 2172 CD1 ILE B 156 -122.634 -45.740 -14.266 1.00 56.62 C ANISOU 2172 CD1 ILE B 156 7451 7344 6719 480 178 287 C ATOM 2173 N LEU B 157 -122.946 -40.991 -15.682 1.00 32.26 N ANISOU 2173 N LEU B 157 4260 4371 3625 392 0 340 N ATOM 2174 CA LEU B 157 -122.145 -40.406 -16.749 1.00 22.26 C ANISOU 2174 CA LEU B 157 3008 3088 2361 326 -56 326 C ATOM 2175 C LEU B 157 -120.718 -40.930 -16.709 1.00 17.89 C ANISOU 2175 C LEU B 157 2503 2535 1759 293 -58 319 C ATOM 2176 O LEU B 157 -120.101 -40.980 -15.648 1.00 39.85 O ANISOU 2176 O LEU B 157 5289 5351 4499 297 -26 320 O ATOM 2177 CB LEU B 157 -122.089 -38.872 -16.636 1.00 47.66 C ANISOU 2177 CB LEU B 157 6188 6331 5590 292 -84 326 C ATOM 2178 CG LEU B 157 -123.402 -38.080 -16.580 1.00 63.12 C ANISOU 2178 CG LEU B 157 8096 8301 7586 311 -81 328 C ATOM 2179 CD1 LEU B 157 -123.133 -36.574 -16.755 1.00 52.37 C ANISOU 2179 CD1 LEU B 157 6713 6952 6232 267 -113 321 C ATOM 2180 CD2 LEU B 157 -124.410 -38.589 -17.612 1.00 39.87 C ANISOU 2180 CD2 LEU B 157 5152 5320 4678 321 -89 321 C ATOM 2181 N ILE B 158 -120.187 -41.298 -17.870 1.00 27.00 N ANISOU 2181 N ILE B 158 3690 3652 2916 257 -97 309 N ATOM 2182 CA ILE B 158 -118.787 -41.684 -17.972 1.00 22.12 C ANISOU 2182 CA ILE B 158 3118 3035 2251 211 -109 301 C ATOM 2183 C ILE B 158 -117.957 -40.518 -18.477 1.00 33.25 C ANISOU 2183 C ILE B 158 4517 4451 3665 144 -169 307 C ATOM 2184 O ILE B 158 -118.295 -39.916 -19.492 1.00 58.93 O ANISOU 2184 O ILE B 158 7747 7681 6963 127 -214 311 O ATOM 2185 CB ILE B 158 -118.580 -42.866 -18.932 1.00 30.80 C ANISOU 2185 CB ILE B 158 4264 4089 3351 204 -118 285 C ATOM 2186 CG1 ILE B 158 -119.330 -44.103 -18.449 1.00 52.04 C ANISOU 2186 CG1 ILE B 158 6958 6754 6060 250 -52 267 C ATOM 2187 CG2 ILE B 158 -117.110 -43.177 -19.044 1.00 20.60 C ANISOU 2187 CG2 ILE B 158 3011 2799 2017 140 -134 272 C ATOM 2188 CD1 ILE B 158 -119.013 -45.348 -19.255 1.00 49.78 C ANISOU 2188 CD1 ILE B 158 6713 6422 5781 228 -49 238 C ATOM 2189 N GLU B 159 -116.867 -40.213 -17.779 1.00 38.31 N ANISOU 2189 N GLU B 159 5175 5123 4260 104 -167 308 N ATOM 2190 CA GLU B 159 -115.982 -39.117 -18.170 1.00 23.87 C ANISOU 2190 CA GLU B 159 3363 3273 2433 69 -213 301 C ATOM 2191 C GLU B 159 -114.753 -39.597 -18.923 1.00 26.26 C ANISOU 2191 C GLU B 159 3663 3594 2720 41 -229 301 C ATOM 2192 O GLU B 159 -113.766 -40.014 -18.332 1.00 40.27 O ANISOU 2192 O GLU B 159 5468 5383 4449 3 -215 294 O ATOM 2193 CB GLU B 159 -115.582 -38.275 -16.954 1.00 28.51 C ANISOU 2193 CB GLU B 159 3942 3903 2988 58 -191 305 C ATOM 2194 CG GLU B 159 -116.724 -37.405 -16.447 1.00 47.94 C ANISOU 2194 CG GLU B 159 6345 6384 5485 83 -177 313 C ATOM 2195 CD GLU B 159 -116.438 -36.772 -15.099 1.00 83.65 C ANISOU 2195 CD GLU B 159 10847 10960 9977 81 -142 312 C ATOM 2196 OE1 GLU B 159 -116.373 -37.513 -14.094 1.00 90.04 O ANISOU 2196 OE1 GLU B 159 11651 11810 10751 100 -91 308 O ATOM 2197 OE2 GLU B 159 -116.281 -35.531 -15.044 1.00 96.07 O ANISOU 2197 OE2 GLU B 159 12407 12535 11561 66 -162 311 O ATOM 2198 N ASP B 160 -114.833 -39.526 -20.242 1.00 25.33 N ANISOU 2198 N ASP B 160 3535 3439 2650 34 -270 298 N ATOM 2199 CA ASP B 160 -113.739 -39.885 -21.121 1.00 18.76 C ANISOU 2199 CA ASP B 160 2729 2578 1823 -16 -306 290 C ATOM 2200 C ASP B 160 -113.809 -39.030 -22.397 1.00 46.59 C ANISOU 2200 C ASP B 160 6225 6070 5407 -19 -352 289 C ATOM 2201 O ASP B 160 -114.812 -39.059 -23.108 1.00 53.27 O ANISOU 2201 O ASP B 160 7049 6897 6295 11 -358 284 O ATOM 2202 CB ASP B 160 -113.848 -41.357 -21.480 1.00 21.12 C ANISOU 2202 CB ASP B 160 3063 2854 2106 -21 -299 278 C ATOM 2203 CG ASP B 160 -112.658 -41.867 -22.277 1.00 38.00 C ANISOU 2203 CG ASP B 160 5231 4969 4238 -75 -334 269 C ATOM 2204 OD1 ASP B 160 -112.537 -43.106 -22.413 1.00 30.40 O ANISOU 2204 OD1 ASP B 160 4306 3994 3249 -88 -323 255 O ATOM 2205 OD2 ASP B 160 -111.848 -41.054 -22.757 1.00 46.00 O ANISOU 2205 OD2 ASP B 160 6233 5976 5271 -105 -370 277 O ATOM 2206 N ASN B 161 -112.754 -38.253 -22.658 1.00 40.64 N ANISOU 2206 N ASN B 161 5474 5309 4659 -59 -382 295 N ATOM 2207 CA ASN B 161 -112.579 -37.552 -23.929 1.00 16.42 C ANISOU 2207 CA ASN B 161 2390 2203 1644 -73 -427 295 C ATOM 2208 C ASN B 161 -111.377 -38.085 -24.671 1.00 28.02 C ANISOU 2208 C ASN B 161 3890 3645 3110 -123 -464 298 C ATOM 2209 O ASN B 161 -111.043 -37.615 -25.747 1.00 54.70 O ANISOU 2209 O ASN B 161 7263 6990 6531 -140 -504 301 O ATOM 2210 CB ASN B 161 -112.381 -36.066 -23.709 1.00 35.20 C ANISOU 2210 CB ASN B 161 4747 4589 4037 -80 -435 304 C ATOM 2211 CG ASN B 161 -112.607 -35.665 -22.296 1.00 51.64 C ANISOU 2211 CG ASN B 161 6824 6717 6079 -63 -395 308 C ATOM 2212 OD1 ASN B 161 -113.707 -35.271 -21.921 1.00 68.08 O ANISOU 2212 OD1 ASN B 161 8880 8816 8170 -19 -372 304 O ATOM 2213 ND2 ASN B 161 -111.569 -35.769 -21.486 1.00 55.82 N ANISOU 2213 ND2 ASN B 161 7380 7268 6563 -99 -388 315 N ATOM 2214 N THR B 162 -110.730 -39.082 -24.089 1.00 42.02 N ANISOU 2214 N THR B 162 5697 5436 4833 -148 -448 296 N ATOM 2215 CA THR B 162 -109.578 -39.739 -24.700 1.00 51.13 C ANISOU 2215 CA THR B 162 6882 6571 5973 -199 -479 299 C ATOM 2216 C THR B 162 -109.952 -40.794 -25.749 1.00 33.66 C ANISOU 2216 C THR B 162 4679 4327 3782 -191 -497 285 C ATOM 2217 O THR B 162 -109.499 -40.744 -26.890 1.00 31.10 O ANISOU 2217 O THR B 162 4356 3969 3492 -211 -541 288 O ATOM 2218 CB THR B 162 -108.724 -40.428 -23.616 1.00 76.76 C ANISOU 2218 CB THR B 162 10162 9853 9151 -236 -450 297 C ATOM 2219 OG1 THR B 162 -108.397 -39.482 -22.589 1.00 86.09 O ANISOU 2219 OG1 THR B 162 11334 11065 10309 -245 -432 307 O ATOM 2220 CG2 THR B 162 -107.437 -41.006 -24.211 1.00 76.38 C ANISOU 2220 CG2 THR B 162 10143 9791 9085 -298 -483 303 C ATOM 2221 N SER B 163 -110.772 -41.757 -25.352 1.00 32.84 N ANISOU 2221 N SER B 163 4586 4233 3658 -162 -462 269 N ATOM 2222 CA SER B 163 -111.077 -42.885 -26.216 1.00 42.53 C ANISOU 2222 CA SER B 163 5832 5433 4895 -160 -474 253 C ATOM 2223 C SER B 163 -111.716 -42.376 -27.472 1.00 32.72 C ANISOU 2223 C SER B 163 4559 4153 3721 -137 -510 248 C ATOM 2224 O SER B 163 -112.311 -41.313 -27.468 1.00 35.39 O ANISOU 2224 O SER B 163 4861 4492 4094 -111 -508 253 O ATOM 2225 CB SER B 163 -112.034 -43.832 -25.517 1.00 39.94 C ANISOU 2225 CB SER B 163 5523 5116 4537 -127 -427 238 C ATOM 2226 OG SER B 163 -111.574 -44.089 -24.211 1.00 51.19 O ANISOU 2226 OG SER B 163 6970 6578 5901 -142 -384 240 O ATOM 2227 N GLU B 164 -111.592 -43.135 -28.547 1.00 33.03 N ANISOU 2227 N GLU B 164 4610 4162 3778 -149 -540 236 N ATOM 2228 CA GLU B 164 -112.301 -42.824 -29.774 1.00 23.49 C ANISOU 2228 CA GLU B 164 3374 2917 2635 -127 -569 224 C ATOM 2229 C GLU B 164 -113.768 -43.009 -29.463 1.00 41.29 C ANISOU 2229 C GLU B 164 5615 5175 4898 -78 -535 209 C ATOM 2230 O GLU B 164 -114.127 -43.871 -28.661 1.00 42.95 O ANISOU 2230 O GLU B 164 5852 5401 5065 -66 -499 204 O ATOM 2231 CB GLU B 164 -111.877 -43.784 -30.876 1.00 43.25 C ANISOU 2231 CB GLU B 164 5896 5392 5146 -150 -603 211 C ATOM 2232 CG GLU B 164 -112.529 -43.543 -32.216 1.00 59.71 C ANISOU 2232 CG GLU B 164 7952 7437 7298 -130 -634 193 C ATOM 2233 CD GLU B 164 -112.190 -44.632 -33.229 1.00 65.98 C ANISOU 2233 CD GLU B 164 8766 8208 8096 -148 -664 177 C ATOM 2234 OE1 GLU B 164 -111.352 -45.508 -32.923 1.00 60.22 O ANISOU 2234 OE1 GLU B 164 8071 7494 7315 -182 -662 182 O ATOM 2235 OE2 GLU B 164 -112.767 -44.612 -34.334 1.00 67.96 O ANISOU 2235 OE2 GLU B 164 8994 8427 8399 -131 -687 158 O ATOM 2236 N VAL B 165 -114.613 -42.182 -30.066 1.00 32.15 N ANISOU 2236 N VAL B 165 4418 4003 3796 -52 -543 201 N ATOM 2237 CA VAL B 165 -116.034 -42.269 -29.824 1.00 26.88 C ANISOU 2237 CA VAL B 165 3734 3341 3140 -9 -513 189 C ATOM 2238 C VAL B 165 -116.480 -43.657 -30.265 1.00 32.23 C ANISOU 2238 C VAL B 165 4444 3996 3808 -1 -514 167 C ATOM 2239 O VAL B 165 -115.982 -44.163 -31.269 1.00 42.33 O ANISOU 2239 O VAL B 165 5733 5247 5102 -24 -550 153 O ATOM 2240 CB VAL B 165 -116.810 -41.153 -30.595 1.00 30.28 C ANISOU 2240 CB VAL B 165 4117 3758 3632 6 -526 179 C ATOM 2241 CG1 VAL B 165 -118.333 -41.349 -30.479 1.00 34.60 C ANISOU 2241 CG1 VAL B 165 4646 4309 4191 46 -497 165 C ATOM 2242 CG2 VAL B 165 -116.425 -39.791 -30.084 1.00 26.34 C ANISOU 2242 CG2 VAL B 165 3594 3280 3136 0 -521 198 C ATOM 2243 N GLY B 166 -117.391 -44.275 -29.505 1.00 32.73 N ANISOU 2243 N GLY B 166 4524 4068 3843 32 -474 165 N ATOM 2244 CA GLY B 166 -117.949 -45.578 -29.841 1.00 25.53 C ANISOU 2244 CA GLY B 166 3652 3130 2916 45 -468 142 C ATOM 2245 C GLY B 166 -117.131 -46.775 -29.381 1.00 43.21 C ANISOU 2245 C GLY B 166 5954 5372 5093 21 -454 138 C ATOM 2246 O GLY B 166 -117.259 -47.881 -29.912 1.00 39.55 O ANISOU 2246 O GLY B 166 5513 4885 4627 16 -442 107 O ATOM 2247 N THR B 167 -116.276 -46.560 -28.390 1.00 32.65 N ANISOU 2247 N THR B 167 4627 4064 3714 1 -434 159 N ATOM 2248 CA THR B 167 -115.426 -47.629 -27.897 1.00 24.60 C ANISOU 2248 CA THR B 167 3662 3053 2632 -33 -409 150 C ATOM 2249 C THR B 167 -115.480 -47.737 -26.387 1.00 33.23 C ANISOU 2249 C THR B 167 4761 4175 3692 -17 -336 156 C ATOM 2250 O THR B 167 -114.527 -48.207 -25.759 1.00 30.39 O ANISOU 2250 O THR B 167 4429 3835 3283 -54 -313 151 O ATOM 2251 CB THR B 167 -113.992 -47.399 -28.298 1.00 35.34 C ANISOU 2251 CB THR B 167 5017 4425 3985 -91 -451 159 C ATOM 2252 OG1 THR B 167 -113.395 -46.473 -27.385 1.00 49.22 O ANISOU 2252 OG1 THR B 167 6756 6217 5730 -102 -439 184 O ATOM 2253 CG2 THR B 167 -113.945 -46.827 -29.707 1.00 44.15 C ANISOU 2253 CG2 THR B 167 6093 5514 5168 -96 -510 156 C ATOM 2254 N GLN B 168 -116.580 -47.287 -25.795 1.00 17.29 N ANISOU 2254 N GLN B 168 2163 2055 2353 15 146 27 N ATOM 2255 CA GLN B 168 -116.786 -47.565 -24.387 1.00 19.93 C ANISOU 2255 CA GLN B 168 2523 2432 2618 24 114 36 C ATOM 2256 C GLN B 168 -117.178 -49.032 -24.265 1.00 24.96 C ANISOU 2256 C GLN B 168 3171 3069 3244 31 119 41 C ATOM 2257 O GLN B 168 -117.719 -49.624 -25.194 1.00 32.39 O ANISOU 2257 O GLN B 168 4099 4007 4201 27 173 37 O ATOM 2258 CB GLN B 168 -117.846 -46.654 -23.773 1.00 15.94 C ANISOU 2258 CB GLN B 168 2043 1922 2091 24 124 29 C ATOM 2259 CG GLN B 168 -117.465 -45.194 -23.714 1.00 30.70 C ANISOU 2259 CG GLN B 168 3889 3818 3956 17 125 22 C ATOM 2260 CD GLN B 168 -116.264 -44.956 -22.835 1.00 35.89 C ANISOU 2260 CD GLN B 168 4526 4497 4614 16 53 35 C ATOM 2261 OE1 GLN B 168 -116.246 -45.366 -21.682 1.00 35.01 O ANISOU 2261 OE1 GLN B 168 4421 4410 4472 14 31 30 O ATOM 2262 NE2 GLN B 168 -115.244 -44.303 -23.382 1.00 22.58 N ANISOU 2262 NE2 GLN B 168 2775 2803 3002 -1 -7 55 N ATOM 2263 N ARG B 169 -116.843 -49.662 -23.155 1.00 34.95 N ANISOU 2263 N ARG B 169 4432 4365 4481 32 85 43 N ATOM 2264 CA ARG B 169 -117.132 -51.069 -22.927 1.00 29.13 C ANISOU 2264 CA ARG B 169 3688 3644 3735 35 100 44 C ATOM 2265 C ARG B 169 -118.144 -51.239 -21.806 1.00 35.28 C ANISOU 2265 C ARG B 169 4475 4429 4500 40 96 45 C ATOM 2266 O ARG B 169 -118.187 -50.417 -20.916 1.00 26.81 O ANISOU 2266 O ARG B 169 3407 3355 3425 39 69 45 O ATOM 2267 CB ARG B 169 -115.865 -51.803 -22.516 1.00 35.11 C ANISOU 2267 CB ARG B 169 4444 4403 4492 32 66 45 C ATOM 2268 CG ARG B 169 -114.771 -51.864 -23.515 1.00 63.22 C ANISOU 2268 CG ARG B 169 7996 7952 8074 29 74 49 C ATOM 2269 CD ARG B 169 -113.816 -52.988 -23.211 1.00 83.25 C ANISOU 2269 CD ARG B 169 10523 10506 10602 21 48 45 C ATOM 2270 NE ARG B 169 -113.640 -53.842 -24.376 1.00 93.56 N ANISOU 2270 NE ARG B 169 11828 11811 11908 23 49 47 N ATOM 2271 CZ ARG B 169 -114.066 -55.090 -24.481 1.00114.54 C ANISOU 2271 CZ ARG B 169 14491 14480 14547 21 39 41 C ATOM 2272 NH1 ARG B 169 -114.688 -55.689 -23.488 1.00129.09 N ANISOU 2272 NH1 ARG B 169 16338 16333 16377 19 30 34 N ATOM 2273 NH2 ARG B 169 -113.860 -55.743 -25.593 1.00120.42 N ANISOU 2273 NH2 ARG B 169 15235 15224 15294 23 42 44 N ATOM 2274 N VAL B 170 -118.937 -52.310 -21.850 1.00 31.40 N ANISOU 2274 N VAL B 170 4001 3909 4019 53 105 57 N ATOM 2275 CA VAL B 170 -119.711 -52.758 -20.696 1.00 30.51 C ANISOU 2275 CA VAL B 170 3889 3804 3898 60 101 63 C ATOM 2276 C VAL B 170 -118.768 -53.283 -19.613 1.00 32.25 C ANISOU 2276 C VAL B 170 4092 4049 4111 53 74 60 C ATOM 2277 O VAL B 170 -118.000 -54.215 -19.844 1.00 40.40 O ANISOU 2277 O VAL B 170 5112 5098 5139 46 78 54 O ATOM 2278 CB VAL B 170 -120.674 -53.863 -21.080 1.00 40.88 C ANISOU 2278 CB VAL B 170 5205 5123 5206 66 143 66 C ATOM 2279 CG1 VAL B 170 -121.482 -54.309 -19.861 1.00 47.22 C ANISOU 2279 CG1 VAL B 170 6018 5911 6014 82 125 81 C ATOM 2280 CG2 VAL B 170 -121.569 -53.390 -22.218 1.00 41.19 C ANISOU 2280 CG2 VAL B 170 5266 5131 5253 66 187 64 C ATOM 2281 N LEU B 171 -118.837 -52.684 -18.430 1.00 33.00 N ANISOU 2281 N LEU B 171 4179 4167 4195 43 69 60 N ATOM 2282 CA LEU B 171 -117.882 -52.959 -17.361 1.00 31.51 C ANISOU 2282 CA LEU B 171 3975 3985 4011 46 48 53 C ATOM 2283 C LEU B 171 -118.593 -53.023 -16.008 1.00 29.76 C ANISOU 2283 C LEU B 171 3752 3776 3781 45 57 74 C ATOM 2284 O LEU B 171 -119.643 -52.424 -15.841 1.00 47.89 O ANISOU 2284 O LEU B 171 6048 6072 6074 52 64 80 O ATOM 2285 CB LEU B 171 -116.803 -51.873 -17.322 1.00 28.18 C ANISOU 2285 CB LEU B 171 3556 3566 3585 29 30 47 C ATOM 2286 CG LEU B 171 -115.465 -52.075 -18.026 1.00 52.99 C ANISOU 2286 CG LEU B 171 6699 6708 6726 20 22 36 C ATOM 2287 CD1 LEU B 171 -114.489 -52.797 -17.111 1.00 70.64 C ANISOU 2287 CD1 LEU B 171 8931 8948 8960 17 20 40 C ATOM 2288 CD2 LEU B 171 -115.628 -52.815 -19.332 1.00 53.86 C ANISOU 2288 CD2 LEU B 171 6808 6817 6839 22 35 34 C ATOM 2289 N PRO B 172 -118.013 -53.751 -15.037 1.00 38.47 N ANISOU 2289 N PRO B 172 4848 4887 4884 46 54 82 N ATOM 2290 CA PRO B 172 -118.567 -53.841 -13.682 1.00 31.55 C ANISOU 2290 CA PRO B 172 3943 4029 4015 65 60 95 C ATOM 2291 C PRO B 172 -118.552 -52.506 -12.971 1.00 40.11 C ANISOU 2291 C PRO B 172 5013 5128 5099 59 51 105 C ATOM 2292 O PRO B 172 -117.501 -51.875 -12.929 1.00 41.79 O ANISOU 2292 O PRO B 172 5241 5335 5303 42 36 112 O ATOM 2293 CB PRO B 172 -117.586 -54.766 -12.970 1.00 46.91 C ANISOU 2293 CB PRO B 172 5901 5972 5952 59 54 114 C ATOM 2294 CG PRO B 172 -116.320 -54.648 -13.743 1.00 44.32 C ANISOU 2294 CG PRO B 172 5579 5635 5627 46 44 93 C ATOM 2295 CD PRO B 172 -116.758 -54.513 -15.160 1.00 41.42 C ANISOU 2295 CD PRO B 172 5212 5262 5263 42 51 69 C ATOM 2296 N GLY B 173 -119.688 -52.093 -12.412 1.00 43.73 N ANISOU 2296 N GLY B 173 5459 5601 5556 67 56 121 N ATOM 2297 CA GLY B 173 -119.776 -50.830 -11.698 1.00 29.58 C ANISOU 2297 CA GLY B 173 3671 3824 3745 52 40 151 C ATOM 2298 C GLY B 173 -119.482 -51.054 -10.236 1.00 39.34 C ANISOU 2298 C GLY B 173 4883 5089 4976 51 38 186 C ATOM 2299 O GLY B 173 -118.969 -52.108 -9.873 1.00 38.78 O ANISOU 2299 O GLY B 173 4813 5014 4908 59 45 190 O ATOM 2300 N THR B 174 -119.827 -50.086 -9.395 1.00 28.89 N ANISOU 2300 N THR B 174 3536 3798 3644 38 26 215 N ATOM 2301 CA THR B 174 -119.541 -50.195 -7.973 1.00 35.81 C ANISOU 2301 CA THR B 174 4385 4707 4513 33 23 256 C ATOM 2302 C THR B 174 -120.688 -50.798 -7.155 1.00 42.15 C ANISOU 2302 C THR B 174 5124 5550 5341 53 35 257 C ATOM 2303 O THR B 174 -120.560 -51.011 -5.958 1.00 47.46 O ANISOU 2303 O THR B 174 5767 6253 6012 53 35 290 O ATOM 2304 CB THR B 174 -119.222 -48.841 -7.390 1.00 43.02 C ANISOU 2304 CB THR B 174 5227 5666 5453 0 0 261 C ATOM 2305 OG1 THR B 174 -120.412 -48.045 -7.398 1.00 49.47 O ANISOU 2305 OG1 THR B 174 6088 6489 6222 -14 -9 293 O ATOM 2306 CG2 THR B 174 -118.127 -48.162 -8.205 1.00 38.58 C ANISOU 2306 CG2 THR B 174 4682 5080 4896 -20 -14 243 C ATOM 2307 N LEU B 175 -121.813 -51.064 -7.799 1.00 47.46 N ANISOU 2307 N LEU B 175 5859 6196 5977 62 41 265 N ATOM 2308 CA LEU B 175 -122.980 -51.552 -7.086 1.00 30.62 C ANISOU 2308 CA LEU B 175 3713 4090 3834 75 49 290 C ATOM 2309 C LEU B 175 -122.847 -53.040 -6.783 1.00 51.07 C ANISOU 2309 C LEU B 175 6258 6681 6466 108 73 267 C ATOM 2310 O LEU B 175 -122.335 -53.799 -7.598 1.00 73.58 O ANISOU 2310 O LEU B 175 9140 9496 9323 116 82 241 O ATOM 2311 CB LEU B 175 -124.247 -51.291 -7.907 1.00 33.44 C ANISOU 2311 CB LEU B 175 4027 4456 4222 88 56 252 C ATOM 2312 CG LEU B 175 -125.464 -50.826 -7.117 1.00 43.21 C ANISOU 2312 CG LEU B 175 5229 5744 5446 78 47 282 C ATOM 2313 CD1 LEU B 175 -125.118 -49.578 -6.321 1.00 41.11 C ANISOU 2313 CD1 LEU B 175 4995 5503 5123 33 19 334 C ATOM 2314 CD2 LEU B 175 -126.639 -50.567 -8.047 1.00 53.65 C ANISOU 2314 CD2 LEU B 175 6617 7048 6719 74 43 292 C ATOM 2315 N VAL B 176 -123.290 -53.448 -5.598 1.00 43.88 N ANISOU 2315 N VAL B 176 5377 5787 5508 108 72 330 N ATOM 2316 CA VAL B 176 -123.387 -54.858 -5.278 1.00 30.35 C ANISOU 2316 CA VAL B 176 3611 4082 3839 143 97 305 C ATOM 2317 C VAL B 176 -124.814 -55.213 -4.930 1.00 44.29 C ANISOU 2317 C VAL B 176 5362 5868 5597 159 105 323 C ATOM 2318 O VAL B 176 -125.652 -54.330 -4.741 1.00 71.33 O ANISOU 2318 O VAL B 176 8833 9305 8964 135 87 370 O ATOM 2319 CB VAL B 176 -122.482 -55.347 -4.117 1.00 26.42 C ANISOU 2319 CB VAL B 176 3157 3584 3299 135 92 364 C ATOM 2320 CG1 VAL B 176 -121.017 -55.004 -4.302 1.00 35.45 C ANISOU 2320 CG1 VAL B 176 4304 4713 4451 120 83 350 C ATOM 2321 CG2 VAL B 176 -123.067 -55.076 -2.743 1.00 53.64 C ANISOU 2321 CG2 VAL B 176 6569 7080 6732 137 91 412 C ATOM 2322 N SER B 177 -125.094 -56.509 -4.846 1.00 32.68 N ANISOU 2322 N SER B 177 3903 4387 4129 181 123 324 N ATOM 2323 CA SER B 177 -126.464 -56.949 -4.658 1.00 42.00 C ANISOU 2323 CA SER B 177 5073 5582 5302 198 132 339 C ATOM 2324 C SER B 177 -126.690 -57.577 -3.288 1.00 52.35 C ANISOU 2324 C SER B 177 6353 6928 6610 213 141 376 C ATOM 2325 O SER B 177 -126.003 -58.520 -2.906 1.00 69.09 O ANISOU 2325 O SER B 177 8479 9036 8735 226 153 379 O ATOM 2326 CB SER B 177 -126.863 -57.910 -5.773 1.00 42.63 C ANISOU 2326 CB SER B 177 5247 5610 5339 186 146 346 C ATOM 2327 OG SER B 177 -128.174 -58.406 -5.572 1.00 38.92 O ANISOU 2327 OG SER B 177 4712 5162 4912 236 143 334 O ATOM 2328 N ASP B 178 -127.647 -57.025 -2.548 1.00 32.47 N ANISOU 2328 N ASP B 178 3799 4456 4083 210 135 406 N ATOM 2329 CA ASP B 178 -127.963 -57.487 -1.201 1.00 43.51 C ANISOU 2329 CA ASP B 178 5252 5870 5410 205 131 492 C ATOM 2330 C ASP B 178 -128.448 -58.920 -1.219 1.00 34.62 C ANISOU 2330 C ASP B 178 4051 4750 4353 253 164 447 C ATOM 2331 O ASP B 178 -128.258 -59.652 -0.255 1.00 54.08 O ANISOU 2331 O ASP B 178 6594 7204 6750 248 162 522 O ATOM 2332 CB ASP B 178 -129.047 -56.616 -0.564 1.00 56.79 C ANISOU 2332 CB ASP B 178 6899 7606 7072 191 117 525 C ATOM 2333 CG ASP B 178 -128.597 -55.189 -0.342 1.00 62.73 C ANISOU 2333 CG ASP B 178 7531 8409 7892 173 104 486 C ATOM 2334 OD1 ASP B 178 -127.470 -54.991 0.158 1.00 60.62 O ANISOU 2334 OD1 ASP B 178 7359 8116 7556 154 94 542 O ATOM 2335 OD2 ASP B 178 -129.378 -54.267 -0.663 1.00 72.91 O ANISOU 2335 OD2 ASP B 178 8809 9723 9170 147 85 485 O ATOM 2336 N LYS B 179 -129.086 -59.306 -2.318 1.00 39.68 N ANISOU 2336 N LYS B 179 4805 5338 4932 237 155 467 N ATOM 2337 CA LYS B 179 -129.608 -60.662 -2.470 1.00 47.92 C ANISOU 2337 CA LYS B 179 5861 6371 5976 250 189 463 C ATOM 2338 C LYS B 179 -128.515 -61.737 -2.538 1.00 53.68 C ANISOU 2338 C LYS B 179 6611 7067 6717 257 202 449 C ATOM 2339 O LYS B 179 -128.421 -62.596 -1.648 1.00 38.36 O ANISOU 2339 O LYS B 179 4588 5144 4842 319 198 434 O ATOM 2340 CB LYS B 179 -130.494 -60.748 -3.715 1.00 34.16 C ANISOU 2340 CB LYS B 179 4138 4607 4235 250 190 438 C ATOM 2341 CG LYS B 179 -130.735 -62.161 -4.200 1.00 43.09 C ANISOU 2341 CG LYS B 179 5293 5709 5372 267 210 429 C ATOM 2342 CD LYS B 179 -131.788 -62.860 -3.368 1.00 62.68 C ANISOU 2342 CD LYS B 179 7755 8218 7841 285 221 464 C ATOM 2343 CE LYS B 179 -132.222 -64.163 -4.033 1.00 84.42 C ANISOU 2343 CE LYS B 179 10464 10943 10668 349 219 415 C ATOM 2344 NZ LYS B 179 -132.569 -63.965 -5.476 1.00 83.87 N ANISOU 2344 NZ LYS B 179 10486 10843 10536 292 237 423 N ATOM 2345 N ASP B 180 -127.683 -61.670 -3.583 1.00 45.38 N ANISOU 2345 N ASP B 180 5585 5980 5678 244 197 412 N ATOM 2346 CA ASP B 180 -126.812 -62.793 -3.945 1.00 48.78 C ANISOU 2346 CA ASP B 180 5978 6380 6174 290 189 362 C ATOM 2347 C ASP B 180 -125.335 -62.458 -4.138 1.00 35.66 C ANISOU 2347 C ASP B 180 4326 4705 4518 272 180 344 C ATOM 2348 O ASP B 180 -124.586 -63.274 -4.670 1.00 32.01 O ANISOU 2348 O ASP B 180 3886 4215 4060 269 183 326 O ATOM 2349 CB ASP B 180 -127.327 -63.470 -5.224 1.00 64.52 C ANISOU 2349 CB ASP B 180 8056 8341 8116 247 213 369 C ATOM 2350 CG ASP B 180 -127.106 -62.612 -6.466 1.00 66.19 C ANISOU 2350 CG ASP B 180 8237 8529 8385 269 184 308 C ATOM 2351 OD1 ASP B 180 -127.251 -63.122 -7.600 1.00 72.41 O ANISOU 2351 OD1 ASP B 180 9092 9292 9128 226 205 315 O ATOM 2352 OD2 ASP B 180 -126.780 -61.420 -6.298 1.00 41.30 O ANISOU 2352 OD2 ASP B 180 5119 5390 5181 217 186 335 O ATOM 2353 N GLY B 181 -124.912 -61.267 -3.724 1.00 28.43 N ANISOU 2353 N GLY B 181 3390 3810 3601 258 167 351 N ATOM 2354 CA GLY B 181 -123.519 -60.879 -3.868 1.00 21.60 C ANISOU 2354 CA GLY B 181 2532 2935 2741 241 157 336 C ATOM 2355 C GLY B 181 -123.058 -60.571 -5.294 1.00 35.20 C ANISOU 2355 C GLY B 181 4333 4618 4422 187 161 325 C ATOM 2356 O GLY B 181 -121.873 -60.340 -5.535 1.00 32.30 O ANISOU 2356 O GLY B 181 3925 4244 4103 205 139 284 O ATOM 2357 N SER B 182 -123.982 -60.545 -6.253 1.00 40.23 N ANISOU 2357 N SER B 182 4939 5243 5102 221 149 283 N ATOM 2358 CA SER B 182 -123.588 -60.204 -7.614 1.00 30.73 C ANISOU 2358 CA SER B 182 3764 4011 3903 203 141 251 C ATOM 2359 C SER B 182 -123.261 -58.731 -7.752 1.00 34.78 C ANISOU 2359 C SER B 182 4307 4528 4378 156 137 265 C ATOM 2360 O SER B 182 -123.636 -57.916 -6.921 1.00 43.19 O ANISOU 2360 O SER B 182 5309 5626 5476 185 121 264 O ATOM 2361 CB SER B 182 -124.627 -60.616 -8.640 1.00 19.54 C ANISOU 2361 CB SER B 182 2367 2573 2486 209 149 240 C ATOM 2362 OG SER B 182 -125.867 -60.005 -8.368 1.00 35.71 O ANISOU 2362 OG SER B 182 4439 4641 4488 186 165 278 O ATOM 2363 N GLN B 183 -122.546 -58.423 -8.824 1.00 47.90 N ANISOU 2363 N GLN B 183 5952 6167 6080 168 118 216 N ATOM 2364 CA GLN B 183 -121.977 -57.118 -9.062 1.00 35.10 C ANISOU 2364 CA GLN B 183 4361 4546 4430 125 113 224 C ATOM 2365 C GLN B 183 -122.720 -56.452 -10.220 1.00 42.81 C ANISOU 2365 C GLN B 183 5323 5509 5435 145 103 187 C ATOM 2366 O GLN B 183 -123.141 -57.132 -11.162 1.00 28.95 O ANISOU 2366 O GLN B 183 3614 3733 3655 126 122 192 O ATOM 2367 CB GLN B 183 -120.500 -57.305 -9.425 1.00 32.91 C ANISOU 2367 CB GLN B 183 4062 4257 4187 134 96 188 C ATOM 2368 CG GLN B 183 -119.709 -56.036 -9.505 1.00 33.49 C ANISOU 2368 CG GLN B 183 4162 4326 4238 101 81 199 C ATOM 2369 CD GLN B 183 -119.360 -55.503 -8.134 1.00 61.19 C ANISOU 2369 CD GLN B 183 7645 7864 7742 100 77 230 C ATOM 2370 OE1 GLN B 183 -118.978 -56.270 -7.250 1.00 75.98 O ANISOU 2370 OE1 GLN B 183 9465 9763 9641 119 91 226 O ATOM 2371 NE2 GLN B 183 -119.499 -54.188 -7.942 1.00 48.31 N ANISOU 2371 NE2 GLN B 183 5959 6262 6134 97 72 216 N ATOM 2372 N SER B 184 -122.868 -55.128 -10.153 1.00 38.31 N ANISOU 2372 N SER B 184 4773 4948 4835 114 101 205 N ATOM 2373 CA SER B 184 -123.539 -54.379 -11.196 1.00 35.32 C ANISOU 2373 CA SER B 184 4380 4557 4483 133 93 173 C ATOM 2374 C SER B 184 -122.673 -54.338 -12.437 1.00 23.20 C ANISOU 2374 C SER B 184 2892 2992 2931 100 98 158 C ATOM 2375 O SER B 184 -121.468 -54.518 -12.358 1.00 51.03 O ANISOU 2375 O SER B 184 6415 6514 6460 90 88 150 O ATOM 2376 CB SER B 184 -123.845 -52.956 -10.724 1.00 32.61 C ANISOU 2376 CB SER B 184 4045 4236 4108 104 88 200 C ATOM 2377 OG SER B 184 -122.656 -52.212 -10.559 1.00 32.61 O ANISOU 2377 OG SER B 184 4007 4248 4137 98 72 176 O ATOM 2378 N LEU B 185 -123.299 -54.128 -13.585 1.00 32.78 N ANISOU 2378 N LEU B 185 4106 4181 4166 123 98 132 N ATOM 2379 CA LEU B 185 -122.579 -53.802 -14.809 1.00 30.04 C ANISOU 2379 CA LEU B 185 3779 3813 3822 109 94 110 C ATOM 2380 C LEU B 185 -122.985 -52.393 -15.289 1.00 27.22 C ANISOU 2380 C LEU B 185 3440 3455 3447 88 103 111 C ATOM 2381 O LEU B 185 -124.073 -51.898 -14.979 1.00 37.28 O ANISOU 2381 O LEU B 185 4705 4725 4736 118 102 111 O ATOM 2382 CB LEU B 185 -122.853 -54.851 -15.893 1.00 29.27 C ANISOU 2382 CB LEU B 185 3710 3702 3710 95 120 116 C ATOM 2383 CG LEU B 185 -122.166 -56.221 -15.789 1.00 36.82 C ANISOU 2383 CG LEU B 185 4652 4651 4686 113 109 108 C ATOM 2384 CD1 LEU B 185 -122.490 -57.101 -16.997 1.00 33.04 C ANISOU 2384 CD1 LEU B 185 4191 4152 4212 118 125 106 C ATOM 2385 CD2 LEU B 185 -120.665 -56.084 -15.652 1.00 32.04 C ANISOU 2385 CD2 LEU B 185 4048 4060 4066 78 98 106 C ATOM 2386 N VAL B 186 -122.104 -51.757 -16.045 1.00 37.63 N ANISOU 2386 N VAL B 186 4756 4757 4783 89 85 86 N ATOM 2387 CA VAL B 186 -122.348 -50.425 -16.556 1.00 10.81 C ANISOU 2387 CA VAL B 186 1377 1358 1372 70 95 83 C ATOM 2388 C VAL B 186 -122.373 -50.476 -18.061 1.00 33.75 C ANISOU 2388 C VAL B 186 4307 4223 4294 81 106 65 C ATOM 2389 O VAL B 186 -121.387 -50.871 -18.697 1.00 25.99 O ANISOU 2389 O VAL B 186 3317 3257 3302 59 107 65 O ATOM 2390 CB VAL B 186 -121.258 -49.458 -16.100 1.00 26.89 C ANISOU 2390 CB VAL B 186 3390 3407 3422 67 62 70 C ATOM 2391 CG1 VAL B 186 -121.533 -48.062 -16.641 1.00 39.32 C ANISOU 2391 CG1 VAL B 186 4982 4974 4984 53 70 65 C ATOM 2392 CG2 VAL B 186 -121.196 -49.431 -14.580 1.00 28.70 C ANISOU 2392 CG2 VAL B 186 3587 3670 3650 65 50 91 C ATOM 2393 N TYR B 187 -123.497 -50.072 -18.641 1.00 26.65 N ANISOU 2393 N TYR B 187 3446 3287 3393 80 136 66 N ATOM 2394 CA TYR B 187 -123.674 -50.199 -20.072 1.00 26.35 C ANISOU 2394 CA TYR B 187 3437 3213 3362 70 170 56 C ATOM 2395 C TYR B 187 -123.666 -48.824 -20.705 1.00 31.80 C ANISOU 2395 C TYR B 187 4140 3916 4028 44 204 34 C ATOM 2396 O TYR B 187 -124.595 -48.052 -20.510 1.00 49.41 O ANISOU 2396 O TYR B 187 6404 6126 6244 28 227 19 O ATOM 2397 CB TYR B 187 -124.993 -50.924 -20.404 1.00 26.66 C ANISOU 2397 CB TYR B 187 3493 3257 3381 65 230 51 C ATOM 2398 CG TYR B 187 -125.140 -52.284 -19.777 1.00 34.84 C ANISOU 2398 CG TYR B 187 4508 4310 4419 85 218 69 C ATOM 2399 CD1 TYR B 187 -124.922 -53.444 -20.512 1.00 48.84 C ANISOU 2399 CD1 TYR B 187 6279 6079 6201 87 229 73 C ATOM 2400 CD2 TYR B 187 -125.498 -52.416 -18.447 1.00 42.58 C ANISOU 2400 CD2 TYR B 187 5485 5281 5415 109 177 89 C ATOM 2401 CE1 TYR B 187 -125.064 -54.707 -19.926 1.00 15.82 C ANISOU 2401 CE1 TYR B 187 2082 1912 2018 101 221 87 C ATOM 2402 CE2 TYR B 187 -125.637 -53.673 -17.857 1.00 40.39 C ANISOU 2402 CE2 TYR B 187 5181 5050 5114 108 189 107 C ATOM 2403 CZ TYR B 187 -125.420 -54.800 -18.602 1.00 20.90 C ANISOU 2403 CZ TYR B 187 2715 2573 2652 107 201 108 C ATOM 2404 OH TYR B 187 -125.547 -56.016 -18.006 1.00 53.97 O ANISOU 2404 OH TYR B 187 6892 6775 6839 118 196 122 O ATOM 2405 N PRO B 188 -122.610 -48.506 -21.470 1.00 34.96 N ANISOU 2405 N PRO B 188 4525 4321 4437 39 196 31 N ATOM 2406 CA PRO B 188 -122.683 -47.248 -22.195 1.00 21.84 C ANISOU 2406 CA PRO B 188 2901 2600 2796 18 205 14 C ATOM 2407 C PRO B 188 -123.912 -47.311 -23.071 1.00 9.90 C ANISOU 2407 C PRO B 188 1409 1088 1267 -10 291 -8 C ATOM 2408 O PRO B 188 -124.132 -48.325 -23.700 1.00 15.66 O ANISOU 2408 O PRO B 188 2152 1751 2046 -10 290 -8 O ATOM 2409 CB PRO B 188 -121.423 -47.273 -23.051 1.00 24.26 C ANISOU 2409 CB PRO B 188 3180 2918 3121 20 196 18 C ATOM 2410 CG PRO B 188 -120.509 -48.155 -22.353 1.00 19.24 C ANISOU 2410 CG PRO B 188 2508 2323 2478 38 149 34 C ATOM 2411 CD PRO B 188 -121.349 -49.214 -21.737 1.00 43.20 C ANISOU 2411 CD PRO B 188 5536 5385 5492 45 168 39 C ATOM 2412 N LEU B 189 -124.690 -46.236 -23.104 1.00 13.38 N ANISOU 2412 N LEU B 189 1883 1511 1690 -46 323 -34 N ATOM 2413 CA LEU B 189 -125.899 -46.189 -23.892 1.00 7.74 C ANISOU 2413 CA LEU B 189 1224 694 1023 -107 380 -79 C ATOM 2414 C LEU B 189 -125.712 -45.292 -25.098 1.00 25.42 C ANISOU 2414 C LEU B 189 3455 2909 3296 -164 456 -123 C ATOM 2415 O LEU B 189 -125.931 -45.728 -26.229 1.00 36.58 O ANISOU 2415 O LEU B 189 4846 4288 4764 -203 547 -173 O ATOM 2416 CB LEU B 189 -127.061 -45.696 -23.044 1.00 10.40 C ANISOU 2416 CB LEU B 189 1636 1006 1309 -158 449 -111 C ATOM 2417 CG LEU B 189 -127.394 -46.603 -21.877 1.00 23.64 C ANISOU 2417 CG LEU B 189 3324 2693 2965 -118 423 -80 C ATOM 2418 CD1 LEU B 189 -128.462 -45.974 -21.021 1.00 28.64 C ANISOU 2418 CD1 LEU B 189 3988 3378 3517 -174 451 -92 C ATOM 2419 CD2 LEU B 189 -127.816 -47.996 -22.382 1.00 22.06 C ANISOU 2419 CD2 LEU B 189 3115 2473 2793 -102 455 -73 C ATOM 2420 N PHE B 190 -125.328 -44.038 -24.861 1.00 36.91 N ANISOU 2420 N PHE B 190 4916 4378 4731 -176 441 -125 N ATOM 2421 CA PHE B 190 -124.937 -43.146 -25.958 1.00 28.37 C ANISOU 2421 CA PHE B 190 3804 3273 3701 -229 547 -194 C ATOM 2422 C PHE B 190 -123.808 -42.157 -25.649 1.00 21.14 C ANISOU 2422 C PHE B 190 2880 2385 2767 -201 501 -165 C ATOM 2423 O PHE B 190 -123.409 -41.955 -24.505 1.00 29.56 O ANISOU 2423 O PHE B 190 3955 3517 3760 -150 360 -77 O ATOM 2424 CB PHE B 190 -126.135 -42.415 -26.551 1.00 13.28 C ANISOU 2424 CB PHE B 190 1902 1372 1773 -273 659 -333 C ATOM 2425 CG PHE B 190 -126.804 -41.492 -25.606 1.00 14.81 C ANISOU 2425 CG PHE B 190 2174 1591 1862 -298 643 -326 C ATOM 2426 CD1 PHE B 190 -126.489 -40.147 -25.589 1.00 33.55 C ANISOU 2426 CD1 PHE B 190 4573 3985 4189 -264 605 -382 C ATOM 2427 CD2 PHE B 190 -127.769 -41.959 -24.743 1.00 29.37 C ANISOU 2427 CD2 PHE B 190 4071 3436 3650 -334 639 -290 C ATOM 2428 CE1 PHE B 190 -127.127 -39.283 -24.723 1.00 28.04 C ANISOU 2428 CE1 PHE B 190 3957 3310 3386 -306 587 -370 C ATOM 2429 CE2 PHE B 190 -128.403 -41.104 -23.871 1.00 47.79 C ANISOU 2429 CE2 PHE B 190 6462 5808 5890 -365 619 -287 C ATOM 2430 CZ PHE B 190 -128.077 -39.762 -23.859 1.00 42.66 C ANISOU 2430 CZ PHE B 190 5843 5174 5191 -370 601 -311 C ATOM 2431 N GLU B 191 -123.303 -41.530 -26.696 1.00 27.45 N ANISOU 2431 N GLU B 191 3629 3153 3648 -156 510 -296 N ATOM 2432 CA GLU B 191 -122.082 -40.763 -26.576 1.00 23.80 C ANISOU 2432 CA GLU B 191 3182 2645 3215 -84 360 -306 C ATOM 2433 C GLU B 191 -122.079 -39.602 -27.550 1.00 12.51 C ANISOU 2433 C GLU B 191 1791 1107 1854 -19 253 -463 C ATOM 2434 O GLU B 191 -122.274 -39.800 -28.737 1.00 42.12 O ANISOU 2434 O GLU B 191 5477 4838 5688 8 299 -563 O ATOM 2435 CB GLU B 191 -120.897 -41.675 -26.850 1.00 14.32 C ANISOU 2435 CB GLU B 191 1896 1458 2088 -63 335 -241 C ATOM 2436 CG GLU B 191 -119.589 -41.028 -26.583 1.00 40.36 C ANISOU 2436 CG GLU B 191 5234 4691 5411 -21 149 -212 C ATOM 2437 CD GLU B 191 -118.467 -41.976 -26.803 1.00 37.79 C ANISOU 2437 CD GLU B 191 4808 4407 5144 -10 138 -155 C ATOM 2438 OE1 GLU B 191 -118.768 -43.120 -27.180 1.00 40.50 O ANISOU 2438 OE1 GLU B 191 5058 4819 5511 -35 271 -143 O ATOM 2439 OE2 GLU B 191 -117.298 -41.583 -26.609 1.00 54.56 O ANISOU 2439 OE2 GLU B 191 6935 6504 7293 -1 12 -116 O ATOM 2440 N ALA B 192 -121.855 -38.395 -27.045 1.00 22.79 N ANISOU 2440 N ALA B 192 3208 2331 3119 -13 111 -472 N ATOM 2441 CA ALA B 192 -121.903 -37.188 -27.874 1.00 29.38 C ANISOU 2441 CA ALA B 192 4137 3048 3980 11 48 -593 C ATOM 2442 C ALA B 192 -120.755 -36.212 -27.584 1.00 33.67 C ANISOU 2442 C ALA B 192 4748 3497 4549 -52 -27 -540 C ATOM 2443 O ALA B 192 -120.709 -35.612 -26.503 1.00 31.07 O ANISOU 2443 O ALA B 192 4415 3204 4185 -138 -10 -482 O ATOM 2444 CB ALA B 192 -123.242 -36.500 -27.688 1.00 25.64 C ANISOU 2444 CB ALA B 192 3716 2602 3425 8 76 -691 C ATOM 2445 N PRO B 193 -119.813 -36.071 -28.541 1.00 36.68 N ANISOU 2445 N PRO B 193 5002 3835 5099 -1 -101 -586 N ATOM 2446 CA PRO B 193 -118.743 -35.064 -28.469 1.00 17.40 C ANISOU 2446 CA PRO B 193 2520 1339 2752 2 -271 -561 C ATOM 2447 C PRO B 193 -119.239 -33.662 -28.857 1.00 16.23 C ANISOU 2447 C PRO B 193 2447 1102 2619 -6 -318 -684 C ATOM 2448 O PRO B 193 -120.061 -33.519 -29.759 1.00 36.38 O ANISOU 2448 O PRO B 193 5026 3618 5179 22 -240 -825 O ATOM 2449 CB PRO B 193 -117.737 -35.558 -29.507 1.00 34.25 C ANISOU 2449 CB PRO B 193 4508 3460 5044 70 -351 -577 C ATOM 2450 CG PRO B 193 -118.562 -36.320 -30.491 1.00 36.69 C ANISOU 2450 CG PRO B 193 4778 3783 5378 101 -210 -686 C ATOM 2451 CD PRO B 193 -119.614 -36.999 -29.668 1.00 38.67 C ANISOU 2451 CD PRO B 193 5118 4109 5466 64 -69 -638 C ATOM 2452 N VAL B 194 -118.750 -32.647 -28.155 1.00 30.84 N ANISOU 2452 N VAL B 194 4326 2928 4463 -34 -462 -621 N ATOM 2453 CA VAL B 194 -118.966 -31.245 -28.503 1.00 27.84 C ANISOU 2453 CA VAL B 194 4007 2459 4113 -37 -550 -721 C ATOM 2454 C VAL B 194 -118.186 -30.856 -29.777 1.00 33.57 C ANISOU 2454 C VAL B 194 4654 3097 5006 48 -671 -804 C ATOM 2455 O VAL B 194 -117.141 -31.419 -30.084 1.00 37.37 O ANISOU 2455 O VAL B 194 5026 3591 5582 95 -758 -738 O ATOM 2456 CB VAL B 194 -118.551 -30.348 -27.329 1.00 28.14 C ANISOU 2456 CB VAL B 194 4098 2505 4089 -80 -709 -590 C ATOM 2457 CG1 VAL B 194 -118.633 -28.860 -27.699 1.00 20.06 C ANISOU 2457 CG1 VAL B 194 3139 1381 3103 -81 -828 -680 C ATOM 2458 CG2 VAL B 194 -119.397 -30.674 -26.099 1.00 22.25 C ANISOU 2458 CG2 VAL B 194 3408 1854 3191 -159 -604 -517 C ATOM 2459 N SER B 195 -118.717 -29.892 -30.513 1.00 30.31 N ANISOU 2459 N SER B 195 4290 2599 4627 62 -678 -956 N ATOM 2460 CA SER B 195 -118.204 -29.516 -31.826 1.00 28.14 C ANISOU 2460 CA SER B 195 3937 2239 4515 144 -768 -1068 C ATOM 2461 C SER B 195 -116.898 -28.733 -31.778 1.00 39.68 C ANISOU 2461 C SER B 195 5357 3640 6078 173 -1012 -989 C ATOM 2462 O SER B 195 -116.161 -28.705 -32.757 1.00 52.22 O ANISOU 2462 O SER B 195 6846 5177 7817 239 -1108 -1039 O ATOM 2463 CB SER B 195 -119.237 -28.646 -32.550 1.00 41.32 C ANISOU 2463 CB SER B 195 5688 3838 6172 152 -702 -1257 C ATOM 2464 OG SER B 195 -120.416 -29.360 -32.845 1.00 48.82 O ANISOU 2464 OG SER B 195 6670 4843 7038 148 -498 -1341 O ATOM 2465 N PHE B 196 -116.612 -28.078 -30.659 1.00 40.76 N ANISOU 2465 N PHE B 196 5569 3784 6133 124 -1124 -863 N ATOM 2466 CA PHE B 196 -115.485 -27.147 -30.620 1.00 27.40 C ANISOU 2466 CA PHE B 196 3867 2026 4519 153 -1372 -788 C ATOM 2467 C PHE B 196 -114.580 -27.303 -29.410 1.00 47.52 C ANISOU 2467 C PHE B 196 6419 4642 6995 126 -1506 -562 C ATOM 2468 O PHE B 196 -115.043 -27.654 -28.326 1.00 50.51 O ANISOU 2468 O PHE B 196 6856 5103 7233 68 -1425 -464 O ATOM 2469 CB PHE B 196 -115.992 -25.716 -30.705 1.00 42.68 C ANISOU 2469 CB PHE B 196 5910 3864 6441 135 -1437 -881 C ATOM 2470 CG PHE B 196 -117.140 -25.421 -29.795 1.00 29.25 C ANISOU 2470 CG PHE B 196 4331 2205 4577 48 -1319 -885 C ATOM 2471 CD1 PHE B 196 -116.926 -25.096 -28.461 1.00 52.46 C ANISOU 2471 CD1 PHE B 196 7338 5191 7404 -11 -1410 -707 C ATOM 2472 CD2 PHE B 196 -118.434 -25.421 -30.281 1.00 43.27 C ANISOU 2472 CD2 PHE B 196 6158 3976 6305 23 -1128 -1063 C ATOM 2473 CE1 PHE B 196 -117.995 -24.802 -27.613 1.00 51.55 C ANISOU 2473 CE1 PHE B 196 7323 5121 7143 -97 -1314 -709 C ATOM 2474 CE2 PHE B 196 -119.502 -25.136 -29.437 1.00 59.68 C ANISOU 2474 CE2 PHE B 196 8340 6104 8231 -68 -1025 -1073 C ATOM 2475 CZ PHE B 196 -119.281 -24.822 -28.098 1.00 33.83 C ANISOU 2475 CZ PHE B 196 5114 2879 4859 -129 -1123 -899 C ATOM 2476 N PHE B 197 -113.292 -27.019 -29.600 1.00 57.20 N ANISOU 2476 N PHE B 197 7583 5838 8313 169 -1717 -480 N ATOM 2477 CA PHE B 197 -112.300 -27.169 -28.538 1.00 53.91 C ANISOU 2477 CA PHE B 197 7165 5494 7825 151 -1865 -264 C ATOM 2478 C PHE B 197 -112.691 -26.340 -27.334 1.00 34.97 C ANISOU 2478 C PHE B 197 4904 3103 5281 90 -1914 -153 C ATOM 2479 O PHE B 197 -113.411 -25.365 -27.465 1.00 47.52 O ANISOU 2479 O PHE B 197 6583 4612 6862 71 -1905 -242 O ATOM 2480 CB PHE B 197 -110.919 -26.711 -29.013 1.00 73.44 C ANISOU 2480 CB PHE B 197 9577 7921 10405 184 -2059 -219 C ATOM 2481 CG PHE B 197 -110.164 -27.737 -29.819 1.00104.92 C ANISOU 2481 CG PHE B 197 13432 11950 14483 206 -1991 -252 C ATOM 2482 CD1 PHE B 197 -110.356 -29.093 -29.612 1.00115.14 C ANISOU 2482 CD1 PHE B 197 14671 13355 15723 185 -1820 -231 C ATOM 2483 CD2 PHE B 197 -109.248 -27.335 -30.783 1.00120.76 C ANISOU 2483 CD2 PHE B 197 15376 13882 16624 240 -2102 -301 C ATOM 2484 CE1 PHE B 197 -109.652 -30.033 -30.358 1.00121.31 C ANISOU 2484 CE1 PHE B 197 15343 14171 16577 197 -1760 -256 C ATOM 2485 CE2 PHE B 197 -108.543 -28.268 -31.530 1.00126.09 C ANISOU 2485 CE2 PHE B 197 15942 14593 17372 250 -2040 -324 C ATOM 2486 CZ PHE B 197 -108.744 -29.618 -31.317 1.00125.02 C ANISOU 2486 CZ PHE B 197 15759 14567 17176 226 -1868 -300 C ATOM 2487 N GLY B 198 -112.211 -26.721 -26.159 1.00 51.66 N ANISOU 2487 N GLY B 198 7033 5344 7253 16 -1824 3 N ATOM 2488 CA GLY B 198 -112.249 -25.809 -25.034 1.00 59.12 C ANISOU 2488 CA GLY B 198 8074 6315 8072 -63 -1812 101 C ATOM 2489 C GLY B 198 -113.087 -26.220 -23.854 1.00 49.73 C ANISOU 2489 C GLY B 198 6932 5240 6725 -131 -1653 166 C ATOM 2490 O GLY B 198 -114.051 -26.964 -23.987 1.00 57.97 O ANISOU 2490 O GLY B 198 7989 6292 7744 -114 -1604 125 O ATOM 2491 N LYS B 199 -112.711 -25.710 -22.689 1.00 57.99 N ANISOU 2491 N LYS B 199 7988 6375 7670 -202 -1573 257 N ATOM 2492 CA LYS B 199 -113.440 -25.985 -21.465 1.00 59.44 C ANISOU 2492 CA LYS B 199 8183 6682 7720 -260 -1415 306 C ATOM 2493 C LYS B 199 -114.844 -25.406 -21.523 1.00 54.81 C ANISOU 2493 C LYS B 199 7735 5998 7092 -284 -1495 287 C ATOM 2494 O LYS B 199 -115.709 -25.817 -20.747 1.00 46.98 O ANISOU 2494 O LYS B 199 6757 5095 5998 -328 -1364 309 O ATOM 2495 CB LYS B 199 -112.688 -25.456 -20.240 1.00 49.01 C ANISOU 2495 CB LYS B 199 6887 5266 6468 -393 -1250 333 C ATOM 2496 CG LYS B 199 -111.487 -26.291 -19.865 1.00 67.59 C ANISOU 2496 CG LYS B 199 9172 7660 8849 -418 -1220 366 C ATOM 2497 CD LYS B 199 -110.722 -25.710 -18.691 1.00 87.08 C ANISOU 2497 CD LYS B 199 11552 10361 11173 -465 -1383 405 C ATOM 2498 CE LYS B 199 -109.452 -26.507 -18.431 1.00102.19 C ANISOU 2498 CE LYS B 199 13502 12074 13252 -521 -1235 471 C ATOM 2499 NZ LYS B 199 -108.613 -25.899 -17.366 1.00106.87 N ANISOU 2499 NZ LYS B 199 14100 12663 13842 -603 -1280 545 N ATOM 2500 N LEU B 200 -115.074 -24.469 -22.442 1.00 29.07 N ANISOU 2500 N LEU B 200 4576 2559 3910 -245 -1711 231 N ATOM 2501 CA LEU B 200 -116.399 -23.858 -22.557 1.00 40.81 C ANISOU 2501 CA LEU B 200 6207 3953 5345 -265 -1769 172 C ATOM 2502 C LEU B 200 -117.422 -24.847 -23.105 1.00 51.95 C ANISOU 2502 C LEU B 200 7557 5417 6766 -268 -1526 -8 C ATOM 2503 O LEU B 200 -118.618 -24.728 -22.833 1.00 69.06 O ANISOU 2503 O LEU B 200 9777 7613 8849 -331 -1398 -85 O ATOM 2504 CB LEU B 200 -116.366 -22.554 -23.373 1.00 59.16 C ANISOU 2504 CB LEU B 200 8572 6136 7770 -248 -1883 40 C ATOM 2505 CG LEU B 200 -116.921 -22.401 -24.795 1.00 85.09 C ANISOU 2505 CG LEU B 200 11808 9343 11178 -209 -1788 -240 C ATOM 2506 CD1 LEU B 200 -118.370 -22.858 -24.942 1.00 83.75 C ANISOU 2506 CD1 LEU B 200 11646 9231 10945 -258 -1548 -408 C ATOM 2507 CD2 LEU B 200 -116.791 -20.942 -25.234 1.00 93.09 C ANISOU 2507 CD2 LEU B 200 12893 10228 12250 -204 -1946 -310 C ATOM 2508 N GLY B 201 -116.948 -25.832 -23.862 1.00 45.58 N ANISOU 2508 N GLY B 201 6636 4626 6057 -202 -1466 -69 N ATOM 2509 CA GLY B 201 -117.809 -26.905 -24.340 1.00 30.44 C ANISOU 2509 CA GLY B 201 4659 2759 4146 -203 -1234 -208 C ATOM 2510 C GLY B 201 -118.528 -27.613 -23.206 1.00 27.55 C ANISOU 2510 C GLY B 201 4329 2514 3624 -267 -1116 -103 C ATOM 2511 O GLY B 201 -119.541 -28.264 -23.428 1.00 56.98 O ANISOU 2511 O GLY B 201 8036 6283 7331 -289 -923 -222 O ATOM 2512 N ASP B 202 -118.004 -27.484 -21.990 1.00 41.78 N ANISOU 2512 N ASP B 202 6184 4382 5308 -296 -1238 124 N ATOM 2513 CA ASP B 202 -118.626 -28.049 -20.788 1.00 31.45 C ANISOU 2513 CA ASP B 202 4899 3211 3841 -362 -1122 235 C ATOM 2514 C ASP B 202 -119.899 -27.297 -20.410 1.00 33.31 C ANISOU 2514 C ASP B 202 5260 3419 3978 -441 -1087 212 C ATOM 2515 O ASP B 202 -120.594 -27.660 -19.445 1.00 30.19 O ANISOU 2515 O ASP B 202 4851 3141 3479 -500 -949 268 O ATOM 2516 CB ASP B 202 -117.657 -27.997 -19.604 1.00 42.26 C ANISOU 2516 CB ASP B 202 6101 4739 5218 -374 -1002 295 C ATOM 2517 CG ASP B 202 -116.459 -28.908 -19.776 1.00 43.54 C ANISOU 2517 CG ASP B 202 6119 4978 5445 -319 -948 281 C ATOM 2518 OD1 ASP B 202 -116.283 -29.468 -20.873 1.00 46.60 O ANISOU 2518 OD1 ASP B 202 6517 5287 5903 -275 -1013 243 O ATOM 2519 OD2 ASP B 202 -115.682 -29.054 -18.806 1.00 59.03 O ANISOU 2519 OD2 ASP B 202 8045 6869 7514 -406 -831 297 O ATOM 2520 N SER B 203 -120.199 -26.244 -21.166 1.00 24.41 N ANISOU 2520 N SER B 203 4157 2184 2933 -441 -1125 49 N ATOM 2521 CA SER B 203 -121.423 -25.479 -20.957 1.00 28.41 C ANISOU 2521 CA SER B 203 4742 2691 3362 -516 -1072 -40 C ATOM 2522 C SER B 203 -122.555 -26.054 -21.784 1.00 30.08 C ANISOU 2522 C SER B 203 4892 2938 3601 -507 -874 -285 C ATOM 2523 O SER B 203 -123.718 -25.743 -21.555 1.00 32.51 O ANISOU 2523 O SER B 203 5244 3293 3815 -562 -803 -363 O ATOM 2524 CB SER B 203 -121.202 -24.011 -21.280 1.00 51.21 C ANISOU 2524 CB SER B 203 7695 5466 6298 -522 -1226 -94 C ATOM 2525 OG SER B 203 -120.188 -23.481 -20.449 1.00 68.40 O ANISOU 2525 OG SER B 203 9933 7612 8444 -531 -1410 150 O ATOM 2526 N ASN B 204 -122.196 -26.912 -22.737 1.00 31.55 N ANISOU 2526 N ASN B 204 4972 3106 3910 -437 -791 -396 N ATOM 2527 CA ASN B 204 -123.163 -27.701 -23.490 1.00 36.55 C ANISOU 2527 CA ASN B 204 5530 3782 4574 -421 -590 -599 C ATOM 2528 C ASN B 204 -123.606 -28.949 -22.743 1.00 36.89 C ANISOU 2528 C ASN B 204 5551 3947 4520 -432 -481 -486 C ATOM 2529 O ASN B 204 -122.812 -29.573 -22.051 1.00 33.34 O ANISOU 2529 O ASN B 204 5103 3529 4034 -430 -523 -283 O ATOM 2530 CB ASN B 204 -122.562 -28.152 -24.804 1.00 42.58 C ANISOU 2530 CB ASN B 204 6209 4471 5500 -354 -533 -729 C ATOM 2531 CG ASN B 204 -122.188 -27.007 -25.682 1.00 31.70 C ANISOU 2531 CG ASN B 204 4872 2967 4207 -333 -631 -836 C ATOM 2532 OD1 ASN B 204 -121.012 -26.806 -25.982 1.00 42.33 O ANISOU 2532 OD1 ASN B 204 6200 4241 5644 -276 -777 -756 O ATOM 2533 ND2 ASN B 204 -123.184 -26.254 -26.119 1.00 36.52 N ANISOU 2533 ND2 ASN B 204 5529 3557 4788 -369 -566 -1020 N ATOM 2534 N GLY B 205 -124.876 -29.307 -22.906 1.00 35.14 N ANISOU 2534 N GLY B 205 5316 3799 4238 -434 -353 -611 N ATOM 2535 CA GLY B 205 -125.451 -30.489 -22.291 1.00 27.76 C ANISOU 2535 CA GLY B 205 4384 2979 3182 -446 -235 -499 C ATOM 2536 C GLY B 205 -126.815 -30.762 -22.889 1.00 24.95 C ANISOU 2536 C GLY B 205 4019 2689 2771 -412 -108 -664 C ATOM 2537 O GLY B 205 -127.192 -30.129 -23.875 1.00 24.36 O ANISOU 2537 O GLY B 205 3915 2562 2777 -349 -135 -881 O ATOM 2538 N MET B 206 -127.568 -31.696 -22.307 1.00 44.68 N ANISOU 2538 N MET B 206 6550 5299 5128 -461 38 -547 N ATOM 2539 CA MET B 206 -128.887 -32.008 -22.842 1.00 18.87 C ANISOU 2539 CA MET B 206 3255 2112 1802 -428 172 -659 C ATOM 2540 C MET B 206 -129.914 -32.576 -21.866 1.00 27.99 C ANISOU 2540 C MET B 206 4429 3378 2826 -529 298 -508 C ATOM 2541 O MET B 206 -129.614 -32.812 -20.703 1.00 31.80 O ANISOU 2541 O MET B 206 4929 3864 3290 -615 273 -320 O ATOM 2542 CB MET B 206 -128.745 -32.931 -24.042 1.00 16.18 C ANISOU 2542 CB MET B 206 2821 1753 1574 -322 244 -765 C ATOM 2543 CG MET B 206 -127.744 -34.013 -23.835 1.00 43.39 C ANISOU 2543 CG MET B 206 6205 5191 5092 -315 259 -634 C ATOM 2544 SD MET B 206 -127.639 -35.209 -25.358 1.00 74.14 S ANISOU 2544 SD MET B 206 9983 9070 9118 -206 356 -736 S ATOM 2545 CE MET B 206 -126.765 -34.077 -26.672 1.00 38.17 C ANISOU 2545 CE MET B 206 5462 4325 4716 -78 153 -930 C ATOM 2546 N ARG B 207 -131.135 -32.750 -22.371 1.00 27.82 N ANISOU 2546 N ARG B 207 4389 3418 2761 -520 408 -605 N ATOM 2547 CA ARG B 207 -132.224 -33.399 -21.669 1.00 15.85 C ANISOU 2547 CA ARG B 207 2854 1978 1189 -604 503 -508 C ATOM 2548 C ARG B 207 -132.858 -34.451 -22.579 1.00 35.54 C ANISOU 2548 C ARG B 207 5263 4509 3732 -557 624 -584 C ATOM 2549 O ARG B 207 -132.771 -34.362 -23.804 1.00 34.40 O ANISOU 2549 O ARG B 207 5092 4346 3632 -469 653 -733 O ATOM 2550 CB ARG B 207 -133.295 -32.401 -21.254 1.00 27.38 C ANISOU 2550 CB ARG B 207 4394 3481 2528 -670 496 -538 C ATOM 2551 CG ARG B 207 -132.931 -31.537 -20.087 1.00 35.80 C ANISOU 2551 CG ARG B 207 5536 4521 3547 -756 380 -416 C ATOM 2552 CD ARG B 207 -133.760 -30.267 -20.100 1.00 25.95 C ANISOU 2552 CD ARG B 207 4382 3293 2186 -792 348 -501 C ATOM 2553 NE ARG B 207 -133.341 -29.352 -19.054 1.00 26.75 N ANISOU 2553 NE ARG B 207 4558 3355 2253 -879 221 -379 N ATOM 2554 CZ ARG B 207 -133.840 -28.137 -18.865 1.00 38.16 C ANISOU 2554 CZ ARG B 207 6095 4796 3607 -927 156 -418 C ATOM 2555 NH1 ARG B 207 -134.785 -27.666 -19.664 1.00 32.68 N ANISOU 2555 NH1 ARG B 207 5434 4135 2846 -890 204 -596 N ATOM 2556 NH2 ARG B 207 -133.379 -27.388 -17.872 1.00 37.42 N ANISOU 2556 NH2 ARG B 207 6059 4656 3505 -1016 36 -281 N ATOM 2557 N VAL B 208 -133.510 -35.434 -21.962 1.00 24.26 N ANISOU 2557 N VAL B 208 3791 3117 2309 -610 667 -494 N ATOM 2558 CA VAL B 208 -134.028 -36.615 -22.643 1.00 21.23 C ANISOU 2558 CA VAL B 208 3332 2757 1979 -580 753 -531 C ATOM 2559 C VAL B 208 -135.149 -37.165 -21.803 1.00 22.51 C ANISOU 2559 C VAL B 208 3491 2971 2090 -641 766 -473 C ATOM 2560 O VAL B 208 -135.016 -37.296 -20.584 1.00 29.15 O ANISOU 2560 O VAL B 208 4342 3809 2925 -676 690 -369 O ATOM 2561 CB VAL B 208 -133.016 -37.799 -22.665 1.00 30.64 C ANISOU 2561 CB VAL B 208 4458 3896 3288 -540 727 -458 C ATOM 2562 CG1 VAL B 208 -133.233 -38.645 -23.897 1.00 32.13 C ANISOU 2562 CG1 VAL B 208 4579 4091 3539 -491 809 -540 C ATOM 2563 CG2 VAL B 208 -131.568 -37.336 -22.544 1.00 37.66 C ANISOU 2563 CG2 VAL B 208 5365 4719 4226 -513 650 -415 C ATOM 2564 N TRP B 209 -136.231 -37.548 -22.457 1.00 24.71 N ANISOU 2564 N TRP B 209 3748 3301 2339 -644 854 -549 N ATOM 2565 CA TRP B 209 -137.350 -38.136 -21.759 1.00 20.43 C ANISOU 2565 CA TRP B 209 3203 2813 1746 -694 868 -505 C ATOM 2566 C TRP B 209 -138.208 -38.937 -22.708 1.00 19.38 C ANISOU 2566 C TRP B 209 3027 2719 1616 -679 964 -582 C ATOM 2567 O TRP B 209 -138.251 -38.655 -23.895 1.00 42.97 O ANISOU 2567 O TRP B 209 6001 5711 4615 -646 1032 -696 O ATOM 2568 CB TRP B 209 -138.161 -37.055 -21.053 1.00 31.24 C ANISOU 2568 CB TRP B 209 4642 4225 3002 -768 853 -503 C ATOM 2569 CG TRP B 209 -138.818 -36.031 -21.951 1.00 32.51 C ANISOU 2569 CG TRP B 209 4851 4419 3084 -775 924 -635 C ATOM 2570 CD1 TRP B 209 -140.065 -36.101 -22.484 1.00 38.49 C ANISOU 2570 CD1 TRP B 209 5610 5238 3776 -797 1012 -720 C ATOM 2571 CD2 TRP B 209 -138.277 -34.769 -22.368 1.00 31.67 C ANISOU 2571 CD2 TRP B 209 4803 4284 2948 -748 898 -709 C ATOM 2572 NE1 TRP B 209 -140.331 -34.973 -23.216 1.00 24.29 N ANISOU 2572 NE1 TRP B 209 3866 3451 1914 -781 1046 -849 N ATOM 2573 CE2 TRP B 209 -139.248 -34.146 -23.166 1.00 23.60 C ANISOU 2573 CE2 TRP B 209 3816 3305 1847 -743 970 -851 C ATOM 2574 CE3 TRP B 209 -137.055 -34.118 -22.159 1.00 55.65 C ANISOU 2574 CE3 TRP B 209 7870 7258 6015 -721 811 -679 C ATOM 2575 CZ2 TRP B 209 -139.043 -32.890 -23.754 1.00 48.44 C ANISOU 2575 CZ2 TRP B 209 7030 6424 4949 -697 944 -981 C ATOM 2576 CZ3 TRP B 209 -136.855 -32.868 -22.746 1.00 38.27 C ANISOU 2576 CZ3 TRP B 209 5740 5034 3768 -679 780 -802 C ATOM 2577 CH2 TRP B 209 -137.846 -32.271 -23.528 1.00 28.76 C ANISOU 2577 CH2 TRP B 209 4572 3864 2493 -661 839 -958 C ATOM 2578 N SER B 210 -138.871 -39.958 -22.166 1.00 38.99 N ANISOU 2578 N SER B 210 5488 5234 4092 -696 963 -525 N ATOM 2579 CA SER B 210 -139.719 -40.860 -22.938 1.00 26.61 C ANISOU 2579 CA SER B 210 3882 3705 2522 -692 1045 -580 C ATOM 2580 C SER B 210 -141.109 -40.280 -23.083 1.00 22.18 C ANISOU 2580 C SER B 210 3356 3219 1852 -753 1115 -650 C ATOM 2581 O SER B 210 -141.509 -39.425 -22.287 1.00 32.17 O ANISOU 2581 O SER B 210 4675 4507 3040 -806 1085 -626 O ATOM 2582 CB SER B 210 -139.827 -42.185 -22.217 1.00 45.63 C ANISOU 2582 CB SER B 210 6262 6116 4959 -677 1004 -487 C ATOM 2583 OG SER B 210 -140.179 -41.943 -20.868 1.00 63.32 O ANISOU 2583 OG SER B 210 8530 8383 7145 -713 939 -408 O ATOM 2584 N THR B 211 -141.836 -40.730 -24.105 1.00 48.78 N ANISOU 2584 N THR B 211 7617 5334 5583 2871 3003 2408 N ATOM 2585 CA THR B 211 -143.216 -40.307 -24.313 1.00 49.29 C ANISOU 2585 CA THR B 211 7772 5362 5594 2879 3018 2403 C ATOM 2586 C THR B 211 -144.193 -41.207 -23.547 1.00 49.50 C ANISOU 2586 C THR B 211 7859 5405 5544 2905 2967 2396 C ATOM 2587 O THR B 211 -143.839 -42.307 -23.121 1.00 58.59 O ANISOU 2587 O THR B 211 8982 6587 6692 2910 2928 2392 O ATOM 2588 CB THR B 211 -143.566 -40.299 -25.789 1.00 49.31 C ANISOU 2588 CB THR B 211 7787 5309 5637 2849 3074 2390 C ATOM 2589 OG1 THR B 211 -143.165 -41.533 -26.386 1.00 66.28 O ANISOU 2589 OG1 THR B 211 9897 7462 7823 2830 3069 2378 O ATOM 2590 CG2 THR B 211 -142.848 -39.163 -26.485 1.00 49.25 C ANISOU 2590 CG2 THR B 211 7738 5278 5695 2827 3126 2396 C ATOM 2591 N THR B 212 -145.420 -40.735 -23.365 1.00 50.01 N ANISOU 2591 N THR B 212 8007 5449 5545 2920 2968 2395 N ATOM 2592 CA THR B 212 -146.399 -41.472 -22.578 1.00 50.27 C ANISOU 2592 CA THR B 212 8101 5497 5501 2946 2917 2390 C ATOM 2593 C THR B 212 -147.833 -41.186 -23.012 1.00 52.86 C ANISOU 2593 C THR B 212 8523 5784 5778 2946 2937 2383 C ATOM 2594 O THR B 212 -148.177 -40.036 -23.282 1.00 51.09 O ANISOU 2594 O THR B 212 8331 5534 5546 2941 2973 2388 O ATOM 2595 CB THR B 212 -146.232 -41.147 -21.086 1.00 50.40 C ANISOU 2595 CB THR B 212 8116 5564 5471 2983 2864 2404 C ATOM 2596 OG1 THR B 212 -145.045 -41.781 -20.585 1.00 68.58 O ANISOU 2596 OG1 THR B 212 10339 7909 7810 2986 2834 2407 O ATOM 2597 CG2 THR B 212 -147.396 -41.642 -20.316 1.00 50.78 C ANISOU 2597 CG2 THR B 212 8238 5621 5436 3012 2816 2400 C ATOM 2598 N THR B 213 -148.668 -42.227 -23.075 1.00 50.87 N ANISOU 2598 N THR B 213 8315 5524 5488 2949 2914 2371 N ATOM 2599 CA THR B 213 -150.069 -42.043 -23.437 1.00 51.36 C ANISOU 2599 CA THR B 213 8468 5549 5497 2949 2929 2364 C ATOM 2600 C THR B 213 -150.738 -41.566 -22.171 1.00 51.84 C ANISOU 2600 C THR B 213 8589 5630 5478 2981 2892 2374 C ATOM 2601 O THR B 213 -151.790 -42.064 -21.792 1.00 96.54 O ANISOU 2601 O THR B 213 14330 11276 11076 2989 2881 2369 O ATOM 2602 CB THR B 213 -150.769 -43.373 -23.790 1.00 51.34 C ANISOU 2602 CB THR B 213 8496 5534 5476 2943 2912 2350 C ATOM 2603 OG1 THR B 213 -150.590 -44.310 -22.718 1.00 51.20 O ANISOU 2603 OG1 THR B 213 8464 5561 5429 2967 2848 2351 O ATOM 2604 CG2 THR B 213 -150.206 -43.947 -25.079 1.00 50.94 C ANISOU 2604 CG2 THR B 213 8397 5458 5500 2908 2953 2340 C ATOM 2605 N ALA B 214 -150.127 -40.589 -21.522 1.00 58.30 N ANISOU 2605 N ALA B 214 9370 6484 6298 3000 2872 2388 N ATOM 2606 CA ALA B 214 -150.685 -39.991 -20.319 1.00 56.22 C ANISOU 2606 CA ALA B 214 9155 6244 5960 3031 2836 2399 C ATOM 2607 C ALA B 214 -150.532 -38.477 -20.493 1.00 57.98 C ANISOU 2607 C ALA B 214 9366 6465 6199 3026 2870 2412 C ATOM 2608 O ALA B 214 -151.269 -37.712 -19.881 1.00 57.97 O ANISOU 2608 O ALA B 214 9370 6499 6158 3053 2836 2426 O ATOM 2609 CB ALA B 214 -150.302 -40.648 -18.981 1.00 52.12 C ANISOU 2609 CB ALA B 214 8607 5782 5413 3066 2764 2405 C ATOM 2610 N ASP B 215 -149.580 -38.007 -21.284 1.00 52.25 N ANISOU 2610 N ASP B 215 8622 5699 5533 2993 2935 2409 N ATOM 2611 CA ASP B 215 -149.503 -36.551 -21.395 1.00 80.90 C ANISOU 2611 CA ASP B 215 12240 9326 9173 2988 2965 2423 C ATOM 2612 C ASP B 215 -150.262 -35.551 -22.260 1.00 52.81 C ANISOU 2612 C ASP B 215 8744 5717 5604 2963 3025 2418 C ATOM 2613 O ASP B 215 -150.804 -35.879 -23.312 1.00 62.68 O ANISOU 2613 O ASP B 215 10024 6924 6870 2939 3063 2403 O ATOM 2614 CB ASP B 215 -147.996 -36.395 -21.601 1.00 93.66 C ANISOU 2614 CB ASP B 215 13757 10956 10875 2975 2983 2431 C ATOM 2615 CG ASP B 215 -147.456 -35.095 -21.017 1.00113.72 C ANISOU 2615 CG ASP B 215 16279 13515 13415 2982 2988 2449 C ATOM 2616 OD1 ASP B 215 -148.035 -34.609 -20.023 1.00105.75 O ANISOU 2616 OD1 ASP B 215 15315 12531 12332 3009 2953 2459 O ATOM 2617 OD2 ASP B 215 -146.458 -34.557 -21.545 1.00131.29 O ANISOU 2617 OD2 ASP B 215 18441 15730 15712 2960 3027 2455 O ATOM 2618 N ILE B 216 -150.298 -34.324 -21.763 1.00 57.43 N ANISOU 2618 N ILE B 216 9350 6311 6160 2968 3032 2430 N ATOM 2619 CA ILE B 216 -150.673 -33.165 -22.552 1.00 63.79 C ANISOU 2619 CA ILE B 216 10196 7073 6970 2939 3096 2426 C ATOM 2620 C ILE B 216 -150.313 -33.127 -24.047 1.00 56.89 C ANISOU 2620 C ILE B 216 9289 6148 6178 2903 3158 2412 C ATOM 2621 O ILE B 216 -151.176 -32.896 -24.886 1.00 76.70 O ANISOU 2621 O ILE B 216 11848 8620 8675 2889 3180 2396 O ATOM 2622 CB ILE B 216 -149.995 -31.866 -21.987 1.00 77.31 C ANISOU 2622 CB ILE B 216 11882 8807 8686 2940 3105 2444 C ATOM 2623 CG1 ILE B 216 -148.467 -31.877 -22.184 1.00 57.72 C ANISOU 2623 CG1 ILE B 216 9294 6337 6299 2931 3117 2453 C ATOM 2624 CG2 ILE B 216 -150.350 -31.683 -20.506 1.00 71.76 C ANISOU 2624 CG2 ILE B 216 11208 8158 7898 2978 3038 2459 C ATOM 2625 CD1 ILE B 216 -147.649 -31.608 -20.909 1.00 52.86 C ANISOU 2625 CD1 ILE B 216 8630 5782 5674 2960 3067 2475 C ATOM 2626 N GLU B 217 -149.055 -33.378 -24.383 1.00 52.75 N ANISOU 2626 N GLU B 217 8683 5623 5738 2888 3184 2418 N ATOM 2627 CA GLU B 217 -148.657 -33.498 -25.776 1.00 52.44 C ANISOU 2627 CA GLU B 217 8601 5542 5781 2857 3234 2405 C ATOM 2628 C GLU B 217 -149.067 -34.899 -26.157 1.00 52.25 C ANISOU 2628 C GLU B 217 8585 5514 5755 2859 3214 2391 C ATOM 2629 O GLU B 217 -149.231 -35.757 -25.286 1.00 52.52 O ANISOU 2629 O GLU B 217 8622 5586 5746 2885 3156 2394 O ATOM 2630 CB GLU B 217 -147.130 -33.401 -25.870 1.00 51.92 C ANISOU 2630 CB GLU B 217 8433 5494 5802 2848 3240 2415 C ATOM 2631 CG GLU B 217 -146.627 -32.004 -26.058 1.00 62.97 C ANISOU 2631 CG GLU B 217 9816 6878 7234 2831 3284 2423 C ATOM 2632 CD GLU B 217 -147.329 -31.317 -27.205 1.00 77.58 C ANISOU 2632 CD GLU B 217 11717 8665 9094 2801 3351 2409 C ATOM 2633 OE1 GLU B 217 -148.551 -31.035 -27.077 1.00 52.90 O ANISOU 2633 OE1 GLU B 217 8681 5525 5894 2804 3355 2402 O ATOM 2634 OE2 GLU B 217 -146.656 -31.073 -28.233 1.00 76.12 O ANISOU 2634 OE2 GLU B 217 11482 8447 8991 2774 3399 2403 O ATOM 2635 N GLU B 218 -149.221 -35.146 -27.453 1.00 52.19 N ANISOU 2635 N GLU B 218 8575 5460 5793 2831 3263 2377 N ATOM 2636 CA GLU B 218 -149.225 -36.524 -27.917 1.00 53.97 C ANISOU 2636 CA GLU B 218 8780 5686 6040 2828 3247 2366 C ATOM 2637 C GLU B 218 -147.999 -36.825 -28.759 1.00 73.64 C ANISOU 2637 C GLU B 218 11179 8172 8630 2807 3273 2364 C ATOM 2638 O GLU B 218 -147.119 -35.977 -28.904 1.00 68.93 O ANISOU 2638 O GLU B 218 10532 7573 8085 2796 3299 2371 O ATOM 2639 CB GLU B 218 -150.519 -36.907 -28.621 1.00 58.94 C ANISOU 2639 CB GLU B 218 9488 6277 6632 2819 3267 2350 C ATOM 2640 CG GLU B 218 -151.732 -37.020 -27.670 1.00 91.64 C ANISOU 2640 CG GLU B 218 13715 10433 10670 2844 3224 2352 C ATOM 2641 CD GLU B 218 -151.427 -37.730 -26.341 1.00 94.55 C ANISOU 2641 CD GLU B 218 14063 10861 11003 2877 3149 2362 C ATOM 2642 OE1 GLU B 218 -150.456 -38.517 -26.276 1.00 96.42 O ANISOU 2642 OE1 GLU B 218 14224 11122 11289 2878 3129 2363 O ATOM 2643 OE2 GLU B 218 -152.169 -37.498 -25.357 1.00 79.02 O ANISOU 2643 OE2 GLU B 218 12154 8914 8956 2901 3111 2367 O ATOM 2644 N PHE B 219 -147.929 -38.046 -29.278 1.00 51.04 N ANISOU 2644 N PHE B 219 8292 5310 5790 2799 3263 2353 N ATOM 2645 CA PHE B 219 -146.728 -38.529 -29.952 1.00 50.50 C ANISOU 2645 CA PHE B 219 8133 5247 5808 2780 3276 2352 C ATOM 2646 C PHE B 219 -147.154 -39.546 -30.996 1.00 50.40 C ANISOU 2646 C PHE B 219 8128 5209 5814 2763 3291 2336 C ATOM 2647 O PHE B 219 -148.327 -39.843 -31.081 1.00 50.74 O ANISOU 2647 O PHE B 219 8245 5233 5802 2768 3288 2328 O ATOM 2648 CB PHE B 219 -145.747 -39.130 -28.932 1.00 50.09 C ANISOU 2648 CB PHE B 219 8017 5253 5761 2796 3221 2362 C ATOM 2649 CG PHE B 219 -146.197 -40.437 -28.340 1.00 50.01 C ANISOU 2649 CG PHE B 219 8029 5272 5702 2812 3167 2357 C ATOM 2650 CD1 PHE B 219 -145.931 -41.624 -28.982 1.00 49.66 C ANISOU 2650 CD1 PHE B 219 7951 5228 5691 2796 3163 2346 C ATOM 2651 CD2 PHE B 219 -146.862 -40.472 -27.138 1.00 50.29 C ANISOU 2651 CD2 PHE B 219 8116 5334 5658 2843 3120 2362 C ATOM 2652 CE1 PHE B 219 -146.336 -42.809 -28.456 1.00 49.61 C ANISOU 2652 CE1 PHE B 219 7964 5244 5641 2809 3116 2341 C ATOM 2653 CE2 PHE B 219 -147.268 -41.663 -26.596 1.00 50.24 C ANISOU 2653 CE2 PHE B 219 8128 5351 5608 2857 3071 2357 C ATOM 2654 CZ PHE B 219 -147.006 -42.834 -27.254 1.00 51.29 C ANISOU 2654 CZ PHE B 219 8229 5481 5776 2839 3070 2346 C ATOM 2655 N ASP B 220 -146.239 -40.088 -31.789 1.00 49.96 N ANISOU 2655 N ASP B 220 7999 5152 5832 2743 3305 2332 N ATOM 2656 CA ASP B 220 -146.692 -40.910 -32.908 1.00 49.93 C ANISOU 2656 CA ASP B 220 8005 5118 5847 2725 3326 2318 C ATOM 2657 C ASP B 220 -146.965 -42.352 -32.506 1.00 51.92 C ANISOU 2657 C ASP B 220 8264 5399 6063 2733 3276 2314 C ATOM 2658 O ASP B 220 -146.133 -43.238 -32.718 1.00 54.31 O ANISOU 2658 O ASP B 220 8502 5723 6408 2722 3259 2312 O ATOM 2659 CB ASP B 220 -145.754 -40.828 -34.119 1.00 49.60 C ANISOU 2659 CB ASP B 220 7891 5057 5900 2698 3368 2315 C ATOM 2660 CG ASP B 220 -146.381 -41.403 -35.384 1.00 49.69 C ANISOU 2660 CG ASP B 220 7923 5028 5928 2680 3400 2301 C ATOM 2661 OD1 ASP B 220 -147.405 -42.103 -35.266 1.00 72.30 O ANISOU 2661 OD1 ASP B 220 10847 7887 8734 2686 3382 2295 O ATOM 2662 OD2 ASP B 220 -145.861 -41.185 -36.495 1.00 49.55 O ANISOU 2662 OD2 ASP B 220 7862 4985 5981 2659 3442 2297 O ATOM 2663 N GLU B 221 -148.162 -42.565 -31.952 1.00 50.13 N ANISOU 2663 N GLU B 221 8120 5170 5758 2750 3253 2311 N ATOM 2664 CA GLU B 221 -148.598 -43.846 -31.403 1.00 50.06 C ANISOU 2664 CA GLU B 221 8132 5186 5703 2761 3201 2307 C ATOM 2665 C GLU B 221 -148.644 -44.989 -32.428 1.00 49.84 C ANISOU 2665 C GLU B 221 8086 5143 5707 2739 3211 2296 C ATOM 2666 O GLU B 221 -148.351 -46.142 -32.104 1.00 62.90 O ANISOU 2666 O GLU B 221 9715 6825 7357 2740 3170 2294 O ATOM 2667 CB GLU B 221 -149.951 -43.680 -30.703 1.00 50.59 C ANISOU 2667 CB GLU B 221 8294 5246 5679 2783 3180 2307 C ATOM 2668 CG GLU B 221 -149.923 -42.650 -29.566 1.00 67.63 C ANISOU 2668 CG GLU B 221 10471 7426 7797 2807 3162 2319 C ATOM 2669 CD GLU B 221 -151.084 -42.809 -28.581 1.00 65.75 C ANISOU 2669 CD GLU B 221 10316 7200 7465 2834 3119 2321 C ATOM 2670 OE1 GLU B 221 -151.187 -41.993 -27.633 1.00 57.49 O ANISOU 2670 OE1 GLU B 221 9292 6173 6378 2855 3100 2331 O ATOM 2671 OE2 GLU B 221 -151.889 -43.749 -28.754 1.00 61.36 O ANISOU 2671 OE2 GLU B 221 9801 6636 6877 2833 3102 2312 O ATOM 2672 N ALA B 222 -148.992 -44.667 -33.664 1.00 49.99 N ANISOU 2672 N ALA B 222 8117 5116 5759 2719 3264 2289 N ATOM 2673 CA ALA B 222 -149.002 -45.654 -34.733 1.00 60.95 C ANISOU 2673 CA ALA B 222 9486 6489 7184 2697 3277 2279 C ATOM 2674 C ALA B 222 -147.586 -45.966 -35.199 1.00 49.25 C ANISOU 2674 C ALA B 222 7905 5025 5782 2679 3281 2281 C ATOM 2675 O ALA B 222 -147.279 -47.075 -35.612 1.00 58.74 O ANISOU 2675 O ALA B 222 9074 6237 7006 2666 3266 2277 O ATOM 2676 CB ALA B 222 -149.860 -45.174 -35.901 1.00 68.97 C ANISOU 2676 CB ALA B 222 10548 7449 8206 2682 3333 2271 C ATOM 2677 N ALA B 223 -146.711 -44.980 -35.128 1.00 49.13 N ANISOU 2677 N ALA B 223 7843 5014 5810 2679 3301 2289 N ATOM 2678 CA ALA B 223 -145.335 -45.225 -35.489 1.00 48.63 C ANISOU 2678 CA ALA B 223 7685 4971 5820 2663 3302 2291 C ATOM 2679 C ALA B 223 -144.746 -46.224 -34.517 1.00 49.72 C ANISOU 2679 C ALA B 223 7790 5161 5940 2671 3243 2295 C ATOM 2680 O ALA B 223 -144.111 -47.203 -34.921 1.00 62.20 O ANISOU 2680 O ALA B 223 9321 6757 7556 2654 3229 2292 O ATOM 2681 CB ALA B 223 -144.541 -43.937 -35.472 1.00 77.82 C ANISOU 2681 CB ALA B 223 11342 8665 9562 2662 3331 2300 C ATOM 2682 N MET B 224 -144.952 -45.974 -33.228 1.00 48.41 N ANISOU 2682 N MET B 224 7653 5022 5717 2696 3207 2302 N ATOM 2683 CA MET B 224 -144.477 -46.898 -32.213 1.00 48.12 C ANISOU 2683 CA MET B 224 7593 5035 5658 2707 3149 2305 C ATOM 2684 C MET B 224 -145.047 -48.249 -32.497 1.00 48.08 C ANISOU 2684 C MET B 224 7612 5027 5629 2699 3127 2295 C ATOM 2685 O MET B 224 -144.321 -49.229 -32.606 1.00 53.12 O ANISOU 2685 O MET B 224 8200 5688 6296 2686 3106 2292 O ATOM 2686 CB MET B 224 -144.937 -46.486 -30.830 1.00 52.10 C ANISOU 2686 CB MET B 224 8142 5561 6092 2738 3113 2312 C ATOM 2687 CG MET B 224 -144.858 -47.640 -29.850 1.00 73.31 C ANISOU 2687 CG MET B 224 10826 8288 8738 2752 3053 2311 C ATOM 2688 SD MET B 224 -144.984 -47.094 -28.007 1.00105.94 S ANISOU 2688 SD MET B 224 14988 12464 12801 2793 3002 2323 S ATOM 2689 CE MET B 224 -146.736 -46.237 -28.047 1.00 88.69 C ANISOU 2689 CE MET B 224 12917 10236 10545 2811 3021 2322 C ATOM 2690 N ALA B 225 -146.368 -48.294 -32.597 1.00 48.50 N ANISOU 2690 N ALA B 225 7747 5053 5630 2707 3132 2289 N ATOM 2691 CA ALA B 225 -147.049 -49.539 -32.872 1.00 61.51 C ANISOU 2691 CA ALA B 225 9426 6694 7251 2700 3112 2280 C ATOM 2692 C ALA B 225 -146.281 -50.261 -33.967 1.00 58.79 C ANISOU 2692 C ALA B 225 9018 6346 6975 2670 3129 2276 C ATOM 2693 O ALA B 225 -145.663 -51.302 -33.730 1.00 62.18 O ANISOU 2693 O ALA B 225 9407 6803 7414 2663 3094 2274 O ATOM 2694 CB ALA B 225 -148.487 -49.278 -33.301 1.00 54.93 C ANISOU 2694 CB ALA B 225 8679 5819 6372 2704 3135 2275 C ATOM 2695 N LYS B 226 -146.292 -49.669 -35.156 1.00 48.20 N ANISOU 2695 N LYS B 226 7666 4967 5680 2653 3182 2273 N ATOM 2696 CA LYS B 226 -145.725 -50.301 -36.340 1.00 50.03 C ANISOU 2696 CA LYS B 226 7845 5189 5975 2625 3202 2268 C ATOM 2697 C LYS B 226 -144.326 -50.854 -36.083 1.00 58.32 C ANISOU 2697 C LYS B 226 8810 6280 7070 2615 3175 2272 C ATOM 2698 O LYS B 226 -144.066 -52.034 -36.330 1.00 57.80 O ANISOU 2698 O LYS B 226 8721 6227 7014 2600 3152 2268 O ATOM 2699 CB LYS B 226 -145.720 -49.322 -37.513 1.00 48.04 C ANISOU 2699 CB LYS B 226 7583 4896 5775 2613 3264 2267 C ATOM 2700 CG LYS B 226 -145.374 -49.939 -38.859 1.00 76.18 C ANISOU 2700 CG LYS B 226 11105 8443 9399 2586 3288 2262 C ATOM 2701 CD LYS B 226 -145.825 -49.025 -39.998 1.00 90.41 C ANISOU 2701 CD LYS B 226 12924 10195 11232 2578 3350 2259 C ATOM 2702 CE LYS B 226 -145.377 -49.527 -41.369 1.00 92.68 C ANISOU 2702 CE LYS B 226 13162 10466 11586 2553 3376 2255 C ATOM 2703 NZ LYS B 226 -143.946 -49.212 -41.664 1.00 85.17 N ANISOU 2703 NZ LYS B 226 12120 9532 10710 2542 3383 2260 N ATOM 2704 N PHE B 227 -143.440 -50.015 -35.553 1.00 47.21 N ANISOU 2704 N PHE B 227 7359 4893 5687 2622 3177 2280 N ATOM 2705 CA PHE B 227 -142.049 -50.401 -35.385 1.00 46.72 C ANISOU 2705 CA PHE B 227 7213 4866 5672 2610 3157 2285 C ATOM 2706 C PHE B 227 -141.708 -50.981 -34.017 1.00 46.55 C ANISOU 2706 C PHE B 227 7186 4891 5610 2626 3101 2288 C ATOM 2707 O PHE B 227 -140.570 -51.360 -33.760 1.00 46.15 O ANISOU 2707 O PHE B 227 7070 4873 5592 2617 3080 2292 O ATOM 2708 CB PHE B 227 -141.159 -49.208 -35.691 1.00 50.32 C ANISOU 2708 CB PHE B 227 7615 5318 6187 2605 3191 2292 C ATOM 2709 CG PHE B 227 -141.385 -48.633 -37.054 1.00 57.02 C ANISOU 2709 CG PHE B 227 8461 6120 7082 2590 3247 2288 C ATOM 2710 CD1 PHE B 227 -140.850 -49.247 -38.170 1.00 46.51 C ANISOU 2710 CD1 PHE B 227 7081 4781 5809 2565 3261 2284 C ATOM 2711 CD2 PHE B 227 -142.136 -47.486 -37.218 1.00 59.13 C ANISOU 2711 CD2 PHE B 227 8778 6352 7336 2601 3285 2288 C ATOM 2712 CE1 PHE B 227 -141.060 -48.733 -39.418 1.00 46.67 C ANISOU 2712 CE1 PHE B 227 7099 4759 5873 2553 3311 2280 C ATOM 2713 CE2 PHE B 227 -142.345 -46.961 -38.470 1.00 66.22 C ANISOU 2713 CE2 PHE B 227 9677 7207 8278 2587 3337 2284 C ATOM 2714 CZ PHE B 227 -141.807 -47.587 -39.574 1.00 70.56 C ANISOU 2714 CZ PHE B 227 10174 7749 8886 2564 3350 2280 C ATOM 2715 N LYS B 228 -142.692 -51.053 -33.139 1.00 28.26 N ANISOU 2715 N LYS B 228 3521 3547 3669 631 1594 1263 N ATOM 2716 CA LYS B 228 -142.478 -51.637 -31.821 1.00 36.50 C ANISOU 2716 CA LYS B 228 4505 4557 4807 586 1590 1266 C ATOM 2717 C LYS B 228 -141.255 -51.038 -31.156 1.00 35.62 C ANISOU 2717 C LYS B 228 4384 4435 4714 506 1559 1194 C ATOM 2718 O LYS B 228 -140.374 -51.763 -30.668 1.00 30.16 O ANISOU 2718 O LYS B 228 3638 3709 4111 426 1542 1136 O ATOM 2719 CB LYS B 228 -142.329 -53.160 -31.914 1.00 50.08 C ANISOU 2719 CB LYS B 228 6161 6234 6632 551 1594 1255 C ATOM 2720 CG LYS B 228 -143.609 -53.877 -32.333 1.00 61.52 C ANISOU 2720 CG LYS B 228 7606 7688 8079 623 1630 1337 C ATOM 2721 CD LYS B 228 -143.633 -55.330 -31.864 1.00 79.98 C ANISOU 2721 CD LYS B 228 9878 9978 10534 595 1636 1347 C ATOM 2722 CE LYS B 228 -145.016 -55.944 -32.047 1.00 91.08 C ANISOU 2722 CE LYS B 228 11277 11390 11938 667 1675 1444 C ATOM 2723 NZ LYS B 228 -146.063 -55.202 -31.287 1.00 95.00 N ANISOU 2723 NZ LYS B 228 11798 11915 12384 730 1696 1529 N ATOM 2724 N THR B 229 -141.191 -49.709 -31.150 1.00 35.41 N ANISOU 2724 N THR B 229 4417 4442 4594 526 1549 1194 N ATOM 2725 CA THR B 229 -140.141 -49.034 -30.416 1.00 34.42 C ANISOU 2725 CA THR B 229 4284 4311 4481 452 1523 1138 C ATOM 2726 C THR B 229 -140.681 -47.814 -29.711 1.00 30.76 C ANISOU 2726 C THR B 229 3873 3876 3938 499 1525 1193 C ATOM 2727 O THR B 229 -141.815 -47.430 -29.930 1.00 45.26 O ANISOU 2727 O THR B 229 5767 5741 5688 591 1538 1266 O ATOM 2728 CB THR B 229 -138.987 -48.625 -31.323 1.00 47.31 C ANISOU 2728 CB THR B 229 5943 5951 6083 394 1492 1060 C ATOM 2729 OG1 THR B 229 -137.904 -48.160 -30.515 1.00 49.19 O ANISOU 2729 OG1 THR B 229 6163 6180 6346 304 1467 1002 O ATOM 2730 CG2 THR B 229 -139.420 -47.527 -32.256 1.00 54.80 C ANISOU 2730 CG2 THR B 229 6978 6935 6907 467 1494 1084 C ATOM 2731 N ARG B 230 -139.850 -47.205 -28.875 1.00 32.76 N ANISOU 2731 N ARG B 230 4113 4124 4213 433 1508 1157 N ATOM 2732 CA ARG B 230 -140.274 -46.115 -28.000 1.00 25.76 C ANISOU 2732 CA ARG B 230 3267 3255 3264 466 1503 1217 C ATOM 2733 C ARG B 230 -139.861 -44.737 -28.527 1.00 31.42 C ANISOU 2733 C ARG B 230 4086 4002 3849 472 1454 1185 C ATOM 2734 O ARG B 230 -138.792 -44.577 -29.121 1.00 31.32 O ANISOU 2734 O ARG B 230 4077 3986 3836 408 1452 1117 O ATOM 2735 CB ARG B 230 -139.700 -46.351 -26.600 1.00 24.51 C ANISOU 2735 CB ARG B 230 3015 3063 3235 386 1510 1200 C ATOM 2736 CG ARG B 230 -140.252 -45.456 -25.531 1.00 30.03 C ANISOU 2736 CG ARG B 230 3733 3759 3918 411 1399 1201 C ATOM 2737 CD ARG B 230 -141.728 -45.678 -25.325 1.00 25.98 C ANISOU 2737 CD ARG B 230 3243 3250 3380 510 1388 1301 C ATOM 2738 NE ARG B 230 -142.163 -45.050 -24.080 1.00 43.25 N ANISOU 2738 NE ARG B 230 5417 5419 5596 516 1277 1303 N ATOM 2739 CZ ARG B 230 -142.118 -45.617 -22.866 1.00 39.08 C ANISOU 2739 CZ ARG B 230 4778 4847 5223 480 1274 1305 C ATOM 2740 NH1 ARG B 230 -141.658 -46.851 -22.687 1.00 26.51 N ANISOU 2740 NH1 ARG B 230 3080 3222 3770 433 1379 1301 N ATOM 2741 NH2 ARG B 230 -142.531 -44.928 -21.815 1.00 46.99 N ANISOU 2741 NH2 ARG B 230 5774 5834 6247 489 1162 1308 N ATOM 2742 N GLN B 231 -140.713 -43.744 -28.302 1.00 26.46 N ANISOU 2742 N GLN B 231 3543 3393 3119 542 1363 1200 N ATOM 2743 CA GLN B 231 -140.456 -42.406 -28.782 1.00 25.16 C ANISOU 2743 CA GLN B 231 3481 3247 2830 555 1274 1144 C ATOM 2744 C GLN B 231 -139.951 -41.552 -27.655 1.00 43.11 C ANISOU 2744 C GLN B 231 5746 5503 5130 492 1157 1084 C ATOM 2745 O GLN B 231 -140.507 -41.562 -26.562 1.00 37.81 O ANISOU 2745 O GLN B 231 5040 4819 4506 499 1111 1112 O ATOM 2746 CB GLN B 231 -141.706 -41.757 -29.365 1.00 34.39 C ANISOU 2746 CB GLN B 231 4767 4450 3850 672 1245 1191 C ATOM 2747 CG GLN B 231 -141.400 -40.437 -30.061 1.00 32.17 C ANISOU 2747 CG GLN B 231 4598 4183 3441 691 1167 1126 C ATOM 2748 CD GLN B 231 -142.602 -39.865 -30.778 1.00 54.65 C ANISOU 2748 CD GLN B 231 7565 7064 6134 806 1160 1163 C ATOM 2749 OE1 GLN B 231 -143.200 -40.521 -31.630 1.00 61.37 O ANISOU 2749 OE1 GLN B 231 8423 7938 6957 867 1264 1218 O ATOM 2750 NE2 GLN B 231 -142.967 -38.632 -30.432 1.00 73.92 N ANISOU 2750 NE2 GLN B 231 10104 9510 8472 833 1038 1134 N ATOM 2751 N PHE B 232 -138.893 -40.804 -27.944 1.00 29.68 N ANISOU 2751 N PHE B 232 4075 3800 3401 429 1107 1006 N ATOM 2752 CA PHE B 232 -138.218 -40.016 -26.945 1.00 24.60 C ANISOU 2752 CA PHE B 232 3415 3141 2789 350 1005 943 C ATOM 2753 C PHE B 232 -138.106 -38.584 -27.420 1.00 44.25 C ANISOU 2753 C PHE B 232 6023 5641 5148 371 892 898 C ATOM 2754 O PHE B 232 -138.114 -38.296 -28.615 1.00 47.49 O ANISOU 2754 O PHE B 232 6511 6065 5468 416 909 891 O ATOM 2755 CB PHE B 232 -136.805 -40.557 -26.696 1.00 23.82 C ANISOU 2755 CB PHE B 232 3227 3023 2802 221 1052 884 C ATOM 2756 CG PHE B 232 -136.753 -41.893 -25.986 1.00 23.70 C ANISOU 2756 CG PHE B 232 3087 2987 2933 182 1151 910 C ATOM 2757 CD1 PHE B 232 -136.688 -41.956 -24.611 1.00 25.14 C ANISOU 2757 CD1 PHE B 232 3187 3148 3216 136 1121 894 C ATOM 2758 CD2 PHE B 232 -136.728 -43.072 -26.700 1.00 30.65 C ANISOU 2758 CD2 PHE B 232 3928 3864 3855 190 1272 945 C ATOM 2759 CE1 PHE B 232 -136.615 -43.170 -23.954 1.00 23.93 C ANISOU 2759 CE1 PHE B 232 2918 2970 3204 102 1213 908 C ATOM 2760 CE2 PHE B 232 -136.669 -44.294 -26.050 1.00 29.98 C ANISOU 2760 CE2 PHE B 232 3732 3753 3904 153 1359 964 C ATOM 2761 CZ PHE B 232 -136.604 -44.335 -24.671 1.00 29.75 C ANISOU 2761 CZ PHE B 232 3625 3702 3976 110 1330 942 C ATOM 2762 N ARG B 233 -137.981 -37.686 -26.460 1.00 47.75 N ANISOU 2762 N ARG B 233 6476 6076 5591 335 776 864 N ATOM 2763 CA ARG B 233 -137.718 -36.310 -26.753 1.00 25.19 C ANISOU 2763 CA ARG B 233 3723 3221 2628 333 657 812 C ATOM 2764 C ARG B 233 -136.376 -35.928 -26.166 1.00 33.55 C ANISOU 2764 C ARG B 233 4732 4261 3755 203 606 741 C ATOM 2765 O ARG B 233 -136.126 -36.147 -24.986 1.00 52.03 O ANISOU 2765 O ARG B 233 6983 6590 6198 137 594 733 O ATOM 2766 CB ARG B 233 -138.844 -35.434 -26.210 1.00 31.78 C ANISOU 2766 CB ARG B 233 4634 4061 3380 409 547 841 C ATOM 2767 CG ARG B 233 -139.900 -35.140 -27.273 1.00 56.17 C ANISOU 2767 CG ARG B 233 7844 7173 6323 531 559 876 C ATOM 2768 CD ARG B 233 -141.334 -35.007 -26.735 1.00 52.83 C ANISOU 2768 CD ARG B 233 7468 6761 5845 616 514 944 C ATOM 2769 NE ARG B 233 -142.287 -35.358 -27.793 1.00 41.85 N ANISOU 2769 NE ARG B 233 6149 5399 4353 720 598 994 N ATOM 2770 CZ ARG B 233 -143.605 -35.443 -27.651 1.00 34.77 C ANISOU 2770 CZ ARG B 233 5305 4519 3387 801 593 1065 C ATOM 2771 NH1 ARG B 233 -144.191 -35.193 -26.483 1.00 43.23 N ANISOU 2771 NH1 ARG B 233 6366 5577 4481 796 497 1100 N ATOM 2772 NH2 ARG B 233 -144.339 -35.787 -28.689 1.00 29.25 N ANISOU 2772 NH2 ARG B 233 4666 3849 2598 884 685 1104 N ATOM 2773 N ILE B 234 -135.503 -35.369 -26.994 1.00 29.44 N ANISOU 2773 N ILE B 234 4268 3737 3182 162 578 689 N ATOM 2774 CA ILE B 234 -134.224 -34.858 -26.527 1.00 23.93 C ANISOU 2774 CA ILE B 234 3542 3023 2525 33 516 623 C ATOM 2775 C ILE B 234 -134.160 -33.367 -26.786 1.00 29.49 C ANISOU 2775 C ILE B 234 4363 3722 3121 45 372 584 C ATOM 2776 O ILE B 234 -134.541 -32.915 -27.862 1.00 39.80 O ANISOU 2776 O ILE B 234 5768 5030 4324 127 356 584 O ATOM 2777 CB ILE B 234 -133.074 -35.543 -27.272 1.00 23.16 C ANISOU 2777 CB ILE B 234 3409 2920 2472 -50 599 596 C ATOM 2778 CG1 ILE B 234 -131.729 -35.086 -26.737 1.00 22.84 C ANISOU 2778 CG1 ILE B 234 3340 2866 2473 -197 542 533 C ATOM 2779 CG2 ILE B 234 -133.158 -35.260 -28.741 1.00 23.09 C ANISOU 2779 CG2 ILE B 234 3493 2911 2369 18 602 598 C ATOM 2780 CD1 ILE B 234 -130.640 -36.018 -27.148 1.00 29.56 C ANISOU 2780 CD1 ILE B 234 4132 3710 3388 -297 636 515 C ATOM 2781 N GLN B 235 -133.685 -32.595 -25.812 1.00 31.17 N ANISOU 2781 N GLN B 235 4560 3924 3358 -34 269 547 N ATOM 2782 CA GLN B 235 -133.412 -31.188 -26.072 1.00 24.70 C ANISOU 2782 CA GLN B 235 3848 3093 2446 -44 128 504 C ATOM 2783 C GLN B 235 -132.036 -30.752 -25.622 1.00 24.36 C ANISOU 2783 C GLN B 235 3769 3035 2452 -193 72 448 C ATOM 2784 O GLN B 235 -131.609 -31.068 -24.525 1.00 56.99 O ANISOU 2784 O GLN B 235 7801 7170 6683 -282 87 440 O ATOM 2785 CB GLN B 235 -134.499 -30.306 -25.458 1.00 42.07 C ANISOU 2785 CB GLN B 235 6109 5292 4582 32 15 524 C ATOM 2786 CG GLN B 235 -134.380 -30.047 -23.983 1.00 28.40 C ANISOU 2786 CG GLN B 235 4301 3556 2935 -40 -53 521 C ATOM 2787 CD GLN B 235 -135.370 -29.003 -23.516 1.00 38.31 C ANISOU 2787 CD GLN B 235 5637 4805 4113 28 -191 538 C ATOM 2788 OE1 GLN B 235 -136.076 -28.400 -24.323 1.00 60.81 O ANISOU 2788 OE1 GLN B 235 8614 7656 6835 123 -238 543 O ATOM 2789 NE2 GLN B 235 -135.434 -28.787 -22.211 1.00 51.21 N ANISOU 2789 NE2 GLN B 235 7199 6432 5828 -21 -257 546 N ATOM 2790 N LEU B 236 -131.338 -30.030 -26.478 1.00 32.81 N ANISOU 2790 N LEU B 236 4920 4088 3457 -223 8 409 N ATOM 2791 CA LEU B 236 -130.029 -29.467 -26.122 1.00 29.28 C ANISOU 2791 CA LEU B 236 4458 3627 3039 -370 -63 359 C ATOM 2792 C LEU B 236 -130.161 -28.225 -25.254 1.00 24.58 C ANISOU 2792 C LEU B 236 3900 3022 2416 -394 -214 339 C ATOM 2793 O LEU B 236 -131.117 -27.476 -25.383 1.00 49.62 O ANISOU 2793 O LEU B 236 7159 6189 5506 -290 -296 351 O ATOM 2794 CB LEU B 236 -129.221 -29.133 -27.373 1.00 23.63 C ANISOU 2794 CB LEU B 236 3819 2890 2271 -397 -89 331 C ATOM 2795 CG LEU B 236 -129.025 -30.251 -28.397 1.00 23.09 C ANISOU 2795 CG LEU B 236 3723 2823 2225 -376 42 351 C ATOM 2796 CD1 LEU B 236 -127.815 -29.945 -29.245 1.00 54.15 C ANISOU 2796 CD1 LEU B 236 7697 6730 6148 -465 -1 319 C ATOM 2797 CD2 LEU B 236 -128.844 -31.575 -27.729 1.00 27.78 C ANISOU 2797 CD2 LEU B 236 4192 3438 2925 -432 175 372 C ATOM 2798 N ILE B 237 -129.200 -28.010 -24.372 1.00 24.51 N ANISOU 2798 N ILE B 237 3827 3012 2474 -533 -249 310 N ATOM 2799 CA ILE B 237 -129.250 -26.894 -23.444 1.00 25.12 C ANISOU 2799 CA ILE B 237 3919 3080 2544 -571 -389 294 C ATOM 2800 C ILE B 237 -127.864 -26.322 -23.263 1.00 24.95 C ANISOU 2800 C ILE B 237 3892 3048 2541 -730 -452 249 C ATOM 2801 O ILE B 237 -126.880 -26.970 -23.592 1.00 35.81 O ANISOU 2801 O ILE B 237 5226 4427 3952 -823 -370 233 O ATOM 2802 CB ILE B 237 -129.750 -27.318 -22.049 1.00 25.48 C ANISOU 2802 CB ILE B 237 3850 3142 2691 -579 -358 318 C ATOM 2803 CG1 ILE B 237 -128.822 -28.367 -21.442 1.00 25.03 C ANISOU 2803 CG1 ILE B 237 3654 3099 2756 -699 -230 301 C ATOM 2804 CG2 ILE B 237 -131.173 -27.852 -22.119 1.00 48.87 C ANISOU 2804 CG2 ILE B 237 6819 6112 5637 -429 -310 371 C ATOM 2805 CD1 ILE B 237 -129.225 -28.798 -20.070 1.00 25.45 C ANISOU 2805 CD1 ILE B 237 3583 3161 2926 -710 -196 317 C ATOM 2806 N GLU B 238 -127.790 -25.108 -22.729 1.00 26.29 N ANISOU 2806 N GLU B 238 4104 3202 2681 -767 -601 232 N ATOM 2807 CA GLU B 238 -126.514 -24.472 -22.402 1.00 31.57 C ANISOU 2807 CA GLU B 238 4765 3862 3370 -927 -673 194 C ATOM 2808 C GLU B 238 -126.579 -23.782 -21.043 1.00 26.16 C ANISOU 2808 C GLU B 238 4024 3179 2736 -987 -763 191 C ATOM 2809 O GLU B 238 -127.633 -23.365 -20.611 1.00 32.29 O ANISOU 2809 O GLU B 238 4819 3951 3497 -892 -829 214 O ATOM 2810 CB GLU B 238 -126.115 -23.456 -23.469 1.00 39.71 C ANISOU 2810 CB GLU B 238 5933 4856 4297 -926 -795 172 C ATOM 2811 CG GLU B 238 -125.199 -24.006 -24.559 1.00 78.19 C ANISOU 2811 CG GLU B 238 10826 9721 9160 -977 -727 160 C ATOM 2812 CD GLU B 238 -124.891 -22.980 -25.651 1.00107.21 C ANISOU 2812 CD GLU B 238 14637 13351 12746 -960 -856 139 C ATOM 2813 OE1 GLU B 238 -125.485 -21.871 -25.637 1.00 99.69 O ANISOU 2813 OE1 GLU B 238 13773 12375 11730 -894 -988 131 O ATOM 2814 OE2 GLU B 238 -124.049 -23.289 -26.527 1.00118.98 O ANISOU 2814 OE2 GLU B 238 16147 14826 14234 -1014 -827 131 O ATOM 2815 N LYS B 239 -125.444 -23.663 -20.372 1.00 26.16 N ANISOU 2815 N LYS B 239 3955 3186 2797 -1150 -767 164 N ATOM 2816 CA LYS B 239 -125.337 -22.784 -19.217 1.00 65.32 C ANISOU 2816 CA LYS B 239 8875 8144 7799 -1223 -876 157 C ATOM 2817 C LYS B 239 -125.008 -21.374 -19.729 1.00 90.30 C ANISOU 2817 C LYS B 239 12170 11274 10866 -1250 -1056 141 C ATOM 2818 O LYS B 239 -124.556 -21.220 -20.866 1.00 94.72 O ANISOU 2818 O LYS B 239 12825 11814 11350 -1250 -1074 128 O ATOM 2819 CB LYS B 239 -124.243 -23.284 -18.271 1.00 52.34 C ANISOU 2819 CB LYS B 239 7097 6527 6264 -1391 -789 132 C ATOM 2820 CG LYS B 239 -124.495 -24.651 -17.677 1.00 31.05 C ANISOU 2820 CG LYS B 239 4264 3857 3674 -1373 -613 139 C ATOM 2821 CD LYS B 239 -123.326 -25.082 -16.816 1.00 30.65 C ANISOU 2821 CD LYS B 239 4094 3832 3721 -1547 -523 102 C ATOM 2822 CE LYS B 239 -123.427 -26.553 -16.464 1.00 27.00 C ANISOU 2822 CE LYS B 239 3512 3390 3356 -1533 -334 98 C ATOM 2823 NZ LYS B 239 -122.497 -26.984 -15.401 1.00 26.64 N ANISOU 2823 NZ LYS B 239 3334 3369 3420 -1686 -237 57 N ATOM 2824 N PRO B 240 -125.186 -20.340 -18.883 1.00 97.21 N ANISOU 2824 N PRO B 240 13047 12137 11752 -1281 -1194 142 N ATOM 2825 CA PRO B 240 -125.494 -20.416 -17.453 1.00 72.73 C ANISOU 2825 CA PRO B 240 9819 9055 8760 -1312 -1188 155 C ATOM 2826 C PRO B 240 -126.929 -20.812 -17.145 1.00 54.41 C ANISOU 2826 C PRO B 240 7479 6737 6457 -1157 -1167 194 C ATOM 2827 O PRO B 240 -127.868 -20.328 -17.773 1.00 49.82 O ANISOU 2827 O PRO B 240 7017 6136 5778 -1029 -1249 212 O ATOM 2828 CB PRO B 240 -125.246 -18.982 -16.960 1.00 62.59 C ANISOU 2828 CB PRO B 240 8582 7746 7455 -1384 -1378 148 C ATOM 2829 CG PRO B 240 -124.545 -18.280 -18.072 1.00 80.59 C ANISOU 2829 CG PRO B 240 10997 9997 9628 -1422 -1462 125 C ATOM 2830 CD PRO B 240 -125.030 -18.942 -19.315 1.00 93.68 C ANISOU 2830 CD PRO B 240 12730 11650 11213 -1294 -1380 129 C ATOM 2831 N GLU B 241 -127.064 -21.708 -16.174 1.00 66.70 N ANISOU 2831 N GLU B 241 8886 8318 8140 -1174 -1055 206 N ATOM 2832 CA GLU B 241 -128.314 -21.946 -15.479 1.00 78.62 C ANISOU 2832 CA GLU B 241 10345 9824 9701 -1063 -1062 248 C ATOM 2833 C GLU B 241 -128.304 -21.009 -14.275 1.00 91.81 C ANISOU 2833 C GLU B 241 11960 11483 11440 -1130 -1196 253 C ATOM 2834 O GLU B 241 -128.954 -21.273 -13.266 1.00 74.89 O ANISOU 2834 O GLU B 241 9713 9340 9402 -1099 -1192 282 O ATOM 2835 CB GLU B 241 -128.396 -23.404 -15.013 1.00 97.87 C ANISOU 2835 CB GLU B 241 12641 12287 12260 -1054 -876 257 C ATOM 2836 CG GLU B 241 -127.350 -23.787 -13.950 1.00101.65 C ANISOU 2836 CG GLU B 241 12960 12783 12880 -1207 -793 223 C ATOM 2837 CD GLU B 241 -126.997 -25.275 -13.938 1.00 79.37 C ANISOU 2837 CD GLU B 241 10033 9983 10142 -1226 -587 208 C ATOM 2838 OE1 GLU B 241 -127.133 -25.946 -14.985 1.00 46.89 O ANISOU 2838 OE1 GLU B 241 5985 5872 5959 -1162 -507 215 O ATOM 2839 OE2 GLU B 241 -126.568 -25.770 -12.872 1.00 82.96 O ANISOU 2839 OE2 GLU B 241 10337 10448 10735 -1308 -503 186 O ATOM 2840 N SER B 245 -132.799 -21.608 -14.361 1.00 73.75 N ANISOU 2840 N SER B 245 9799 9166 9058 -657 -1278 416 N ATOM 2841 CA SER B 245 -132.813 -22.669 -15.372 1.00 62.94 C ANISOU 2841 CA SER B 245 8453 7816 7645 -597 -1116 414 C ATOM 2842 C SER B 245 -131.771 -22.516 -16.494 1.00 54.72 C ANISOU 2842 C SER B 245 7491 6782 6518 -653 -1079 362 C ATOM 2843 O SER B 245 -131.400 -21.407 -16.874 1.00 49.14 O ANISOU 2843 O SER B 245 6888 6058 5725 -687 -1205 334 O ATOM 2844 CB SER B 245 -134.210 -22.794 -15.987 1.00 74.95 C ANISOU 2844 CB SER B 245 10082 9334 9061 -439 -1132 463 C ATOM 2845 OG SER B 245 -134.245 -23.831 -16.954 1.00 84.63 O ANISOU 2845 OG SER B 245 11322 10580 10253 -382 -975 465 O ATOM 2846 N PRO B 246 -131.300 -23.647 -17.027 1.00 54.37 N ANISOU 2846 N PRO B 246 7398 6758 6504 -663 -910 350 N ATOM 2847 CA PRO B 246 -130.457 -23.635 -18.221 1.00 39.20 C ANISOU 2847 CA PRO B 246 5556 4838 4499 -697 -871 313 C ATOM 2848 C PRO B 246 -131.185 -23.001 -19.390 1.00 41.49 C ANISOU 2848 C PRO B 246 6018 5114 4633 -577 -946 319 C ATOM 2849 O PRO B 246 -132.411 -22.869 -19.384 1.00 52.46 O ANISOU 2849 O PRO B 246 7461 6499 5971 -458 -987 357 O ATOM 2850 CB PRO B 246 -130.272 -25.121 -18.536 1.00 43.58 C ANISOU 2850 CB PRO B 246 6027 5415 5115 -688 -676 319 C ATOM 2851 CG PRO B 246 -130.461 -25.811 -17.242 1.00 68.69 C ANISOU 2851 CG PRO B 246 9051 8604 8444 -716 -612 337 C ATOM 2852 CD PRO B 246 -131.469 -25.001 -16.476 1.00 71.35 C ANISOU 2852 CD PRO B 246 9406 8925 8779 -654 -753 372 C ATOM 2853 N VAL B 247 -130.416 -22.664 -20.413 1.00 34.97 N ANISOU 2853 N VAL B 247 5275 4278 3734 -611 -958 282 N ATOM 2854 CA VAL B 247 -130.938 -22.111 -21.641 1.00 28.01 C ANISOU 2854 CA VAL B 247 4550 3379 2714 -504 -1011 275 C ATOM 2855 C VAL B 247 -131.095 -23.208 -22.683 1.00 37.44 C ANISOU 2855 C VAL B 247 5746 4589 3891 -431 -855 287 C ATOM 2856 O VAL B 247 -130.232 -24.064 -22.816 1.00 51.12 O ANISOU 2856 O VAL B 247 7397 6334 5693 -508 -741 278 O ATOM 2857 CB VAL B 247 -129.998 -21.027 -22.159 1.00 41.75 C ANISOU 2857 CB VAL B 247 6379 5088 4396 -582 -1130 228 C ATOM 2858 CG1 VAL B 247 -130.235 -20.754 -23.635 1.00 42.07 C ANISOU 2858 CG1 VAL B 247 6557 5108 4320 -484 -1138 210 C ATOM 2859 CG2 VAL B 247 -130.177 -19.774 -21.329 1.00 45.94 C ANISOU 2859 CG2 VAL B 247 6946 5596 4912 -616 -1309 223 C ATOM 2860 N ILE B 248 -132.210 -23.178 -23.407 1.00 46.57 N ANISOU 2860 N ILE B 248 6997 5746 4953 -286 -849 308 N ATOM 2861 CA ILE B 248 -132.538 -24.169 -24.434 1.00 27.17 C ANISOU 2861 CA ILE B 248 4547 3304 2473 -201 -705 326 C ATOM 2862 C ILE B 248 -132.043 -23.749 -25.807 1.00 28.37 C ANISOU 2862 C ILE B 248 4801 3434 2544 -181 -720 288 C ATOM 2863 O ILE B 248 -132.393 -22.676 -26.305 1.00 68.74 O ANISOU 2863 O ILE B 248 10042 8521 7554 -124 -834 263 O ATOM 2864 CB ILE B 248 -134.071 -24.371 -24.536 1.00 60.40 C ANISOU 2864 CB ILE B 248 8807 7528 6616 -51 -682 373 C ATOM 2865 CG1 ILE B 248 -134.613 -25.056 -23.276 1.00 63.13 C ANISOU 2865 CG1 ILE B 248 9035 7892 7061 -60 -645 423 C ATOM 2866 CG2 ILE B 248 -134.435 -25.157 -25.793 1.00 56.45 C ANISOU 2866 CG2 ILE B 248 8339 7040 6068 44 -551 387 C ATOM 2867 CD1 ILE B 248 -136.129 -25.120 -23.205 1.00 60.08 C ANISOU 2867 CD1 ILE B 248 8704 7515 6607 71 -654 476 C ATOM 2868 N VAL B 249 -131.230 -24.598 -26.420 1.00 34.56 N ANISOU 2868 N VAL B 249 4683 4861 3585 510 -280 -1027 N ATOM 2869 CA VAL B 249 -130.826 -24.392 -27.800 1.00 23.85 C ANISOU 2869 CA VAL B 249 3319 3459 2283 506 -192 -1074 C ATOM 2870 C VAL B 249 -131.906 -24.903 -28.727 1.00 32.52 C ANISOU 2870 C VAL B 249 4492 4639 3226 520 -76 -1067 C ATOM 2871 O VAL B 249 -132.132 -26.102 -28.806 1.00 49.90 O ANISOU 2871 O VAL B 249 6707 6851 5404 522 -40 -963 O ATOM 2872 CB VAL B 249 -129.590 -25.178 -28.123 1.00 29.82 C ANISOU 2872 CB VAL B 249 4013 4097 3221 485 -194 -992 C ATOM 2873 CG1 VAL B 249 -129.283 -25.040 -29.613 1.00 30.57 C ANISOU 2873 CG1 VAL B 249 4106 4146 3364 478 -92 -1030 C ATOM 2874 CG2 VAL B 249 -128.439 -24.732 -27.230 1.00 48.37 C ANISOU 2874 CG2 VAL B 249 6274 6375 5727 475 -298 -977 C ATOM 2875 N LYS B 250 -132.584 -24.000 -29.420 1.00 49.67 N ANISOU 2875 N LYS B 250 6709 6871 5292 534 -8 -1172 N ATOM 2876 CA LYS B 250 -133.622 -24.415 -30.343 1.00 61.16 C ANISOU 2876 CA LYS B 250 8229 8408 6600 554 122 -1162 C ATOM 2877 C LYS B 250 -132.997 -25.137 -31.528 1.00 52.24 C ANISOU 2877 C LYS B 250 7067 7190 5594 564 227 -1121 C ATOM 2878 O LYS B 250 -131.828 -24.918 -31.866 1.00 40.28 O ANISOU 2878 O LYS B 250 5502 5543 4261 540 213 -1132 O ATOM 2879 CB LYS B 250 -134.452 -23.217 -30.811 1.00 67.87 C ANISOU 2879 CB LYS B 250 9136 9336 7314 568 175 -1294 C ATOM 2880 CG LYS B 250 -135.522 -22.771 -29.831 1.00 78.94 C ANISOU 2880 CG LYS B 250 10590 10875 8527 569 103 -1317 C ATOM 2881 CD LYS B 250 -136.346 -21.617 -30.401 1.00 93.28 C ANISOU 2881 CD LYS B 250 12472 12770 10201 581 167 -1453 C ATOM 2882 CE LYS B 250 -137.567 -21.297 -29.540 1.00 99.88 C ANISOU 2882 CE LYS B 250 13371 13760 10820 579 108 -1462 C ATOM 2883 NZ LYS B 250 -137.204 -20.860 -28.161 1.00100.97 N ANISOU 2883 NZ LYS B 250 13471 13886 11006 562 -48 -1469 N ATOM 2884 N THR B 251 -133.768 -26.021 -32.143 1.00 45.67 N ANISOU 2884 N THR B 251 6241 6459 4655 622 318 -1069 N ATOM 2885 CA THR B 251 -133.321 -26.626 -33.379 1.00 40.16 C ANISOU 2885 CA THR B 251 5505 5687 4068 640 441 -1038 C ATOM 2886 C THR B 251 -133.342 -25.572 -34.478 1.00 56.91 C ANISOU 2886 C THR B 251 7654 7753 6216 631 553 -1149 C ATOM 2887 O THR B 251 -133.883 -24.486 -34.293 1.00 42.38 O ANISOU 2887 O THR B 251 5870 5961 4271 624 541 -1248 O ATOM 2888 CB THR B 251 -134.228 -27.740 -33.811 1.00 30.05 C ANISOU 2888 CB THR B 251 4219 4536 2664 707 530 -934 C ATOM 2889 OG1 THR B 251 -133.689 -28.315 -35.001 1.00 56.60 O ANISOU 2889 OG1 THR B 251 7525 7806 6173 716 650 -898 O ATOM 2890 CG2 THR B 251 -135.592 -27.192 -34.138 1.00 28.13 C ANISOU 2890 CG2 THR B 251 4036 4447 2205 736 609 -984 C ATOM 2891 N ALA B 252 -132.756 -25.903 -35.625 1.00 62.33 N ANISOU 2891 N ALA B 252 8304 8332 7047 637 664 -1126 N ATOM 2892 CA ALA B 252 -132.748 -24.994 -36.766 1.00 41.36 C ANISOU 2892 CA ALA B 252 5680 5607 4426 650 784 -1206 C ATOM 2893 C ALA B 252 -134.167 -24.514 -37.074 1.00 46.69 C ANISOU 2893 C ALA B 252 6417 6437 4886 684 876 -1288 C ATOM 2894 O ALA B 252 -134.451 -23.322 -36.984 1.00 78.23 O ANISOU 2894 O ALA B 252 10474 10443 8809 680 861 -1395 O ATOM 2895 CB ALA B 252 -132.129 -25.671 -37.974 1.00 37.16 C ANISOU 2895 CB ALA B 252 5098 4958 4063 670 907 -1131 C ATOM 2896 N ASP B 253 -135.058 -25.441 -37.414 1.00 42.73 N ANISOU 2896 N ASP B 253 5896 6064 4277 718 964 -1225 N ATOM 2897 CA ASP B 253 -136.460 -25.120 -37.682 1.00 45.96 C ANISOU 2897 CA ASP B 253 6365 6637 4459 748 1050 -1271 C ATOM 2898 C ASP B 253 -137.150 -24.446 -36.496 1.00 45.94 C ANISOU 2898 C ASP B 253 6434 6754 4266 738 922 -1320 C ATOM 2899 O ASP B 253 -138.363 -24.262 -36.512 1.00 53.30 O ANISOU 2899 O ASP B 253 7423 7840 4987 759 968 -1338 O ATOM 2900 CB ASP B 253 -137.255 -26.387 -38.023 1.00 86.94 C ANISOU 2900 CB ASP B 253 11514 11962 9558 789 1130 -1137 C ATOM 2901 CG ASP B 253 -136.710 -27.123 -39.234 1.00114.25 C ANISOU 2901 CG ASP B 253 14878 15326 13206 793 1258 -1083 C ATOM 2902 OD1 ASP B 253 -136.022 -26.490 -40.066 1.00121.69 O ANISOU 2902 OD1 ASP B 253 15806 16115 14315 767 1337 -1174 O ATOM 2903 OD2 ASP B 253 -136.982 -28.339 -39.357 1.00117.46 O ANISOU 2903 OD2 ASP B 253 15228 15802 13600 829 1278 -930 O ATOM 2904 N GLN B 254 -136.390 -24.130 -35.451 1.00 48.86 N ANISOU 2904 N GLN B 254 6795 7054 4716 701 762 -1330 N ATOM 2905 CA GLN B 254 -136.917 -23.345 -34.338 1.00 50.26 C ANISOU 2905 CA GLN B 254 7027 7315 4755 679 641 -1386 C ATOM 2906 C GLN B 254 -137.912 -24.062 -33.422 1.00 52.50 C ANISOU 2906 C GLN B 254 7326 7772 4849 701 572 -1287 C ATOM 2907 O GLN B 254 -138.838 -23.440 -32.920 1.00 56.94 O ANISOU 2907 O GLN B 254 7952 8450 5232 697 537 -1334 O ATOM 2908 CB GLN B 254 -137.553 -22.070 -34.874 1.00 56.76 C ANISOU 2908 CB GLN B 254 7927 8167 5472 680 715 -1529 C ATOM 2909 CG GLN B 254 -136.541 -21.084 -35.340 1.00 51.16 C ANISOU 2909 CG GLN B 254 7210 7291 4939 661 721 -1621 C ATOM 2910 CD GLN B 254 -135.753 -20.548 -34.180 1.00 70.50 C ANISOU 2910 CD GLN B 254 9608 9704 7474 634 537 -1649 C ATOM 2911 OE1 GLN B 254 -134.522 -20.453 -34.227 1.00 79.48 O ANISOU 2911 OE1 GLN B 254 10671 10717 8813 623 485 -1642 O ATOM 2912 NE2 GLN B 254 -136.460 -20.190 -33.115 1.00 71.64 N ANISOU 2912 NE2 GLN B 254 9787 9962 7470 621 439 -1672 N ATOM 2913 N GLN B 255 -137.713 -25.355 -33.198 1.00 61.02 N ANISOU 2913 N GLN B 255 8352 8864 5968 727 553 -1140 N ATOM 2914 CA GLN B 255 -138.493 -26.102 -32.214 1.00 53.20 C ANISOU 2914 CA GLN B 255 7372 8010 4833 750 473 -1011 C ATOM 2915 C GLN B 255 -137.709 -26.208 -30.921 1.00 36.48 C ANISOU 2915 C GLN B 255 5224 5814 2822 716 309 -979 C ATOM 2916 O GLN B 255 -136.483 -26.086 -30.923 1.00 42.83 O ANISOU 2916 O GLN B 255 5984 6462 3827 684 272 -1015 O ATOM 2917 CB GLN B 255 -138.817 -27.508 -32.721 1.00 76.08 C ANISOU 2917 CB GLN B 255 10232 10965 7711 804 559 -839 C ATOM 2918 CG GLN B 255 -140.052 -27.606 -33.593 1.00 98.81 C ANISOU 2918 CG GLN B 255 13145 13981 10416 840 701 -810 C ATOM 2919 CD GLN B 255 -140.430 -29.046 -33.879 1.00114.77 C ANISOU 2919 CD GLN B 255 15123 16056 12427 890 767 -599 C ATOM 2920 OE1 GLN B 255 -139.637 -29.963 -33.654 1.00117.32 O ANISOU 2920 OE1 GLN B 255 15388 16292 12895 900 729 -488 O ATOM 2921 NE2 GLN B 255 -141.645 -29.253 -34.370 1.00115.47 N ANISOU 2921 NE2 GLN B 255 15242 16281 12351 918 867 -533 N ATOM 2922 N ASP B 256 -138.405 -26.448 -29.814 1.00 31.24 N ANISOU 2922 N ASP B 256 4582 5252 2037 717 214 -901 N ATOM 2923 CA ASP B 256 -137.749 -26.507 -28.513 1.00 27.29 C ANISOU 2923 CA ASP B 256 4054 4676 1640 679 67 -870 C ATOM 2924 C ASP B 256 -137.093 -27.861 -28.263 1.00 46.51 C ANISOU 2924 C ASP B 256 6431 7047 4193 700 45 -723 C ATOM 2925 O ASP B 256 -136.229 -28.014 -27.385 1.00 33.72 O ANISOU 2925 O ASP B 256 4778 5320 2714 666 -55 -704 O ATOM 2926 CB ASP B 256 -138.724 -26.184 -27.390 1.00 28.70 C ANISOU 2926 CB ASP B 256 4276 4966 1660 662 -23 -845 C ATOM 2927 CG ASP B 256 -139.135 -24.733 -27.376 1.00 95.78 C ANISOU 2927 CG ASP B 256 12830 13493 10070 628 -34 -1001 C ATOM 2928 OD1 ASP B 256 -138.475 -23.922 -28.059 1.00101.16 O ANISOU 2928 OD1 ASP B 256 13508 14077 10850 610 11 -1127 O ATOM 2929 OD2 ASP B 256 -140.111 -24.399 -26.672 1.00 97.80 O ANISOU 2929 OD2 ASP B 256 13135 13864 10162 618 -88 -990 O ATOM 2930 N TYR B 257 -137.496 -28.855 -29.038 1.00 37.53 N ANISOU 2930 N TYR B 257 5284 5971 3007 755 147 -610 N ATOM 2931 CA TYR B 257 -136.944 -30.172 -28.833 1.00 24.30 C ANISOU 2931 CA TYR B 257 3560 4237 1435 778 136 -455 C ATOM 2932 C TYR B 257 -137.100 -31.045 -30.075 1.00 24.90 C ANISOU 2932 C TYR B 257 3614 4333 1516 831 284 -357 C ATOM 2933 O TYR B 257 -137.840 -30.716 -30.996 1.00 34.33 O ANISOU 2933 O TYR B 257 4829 5608 2607 853 395 -392 O ATOM 2934 CB TYR B 257 -137.606 -30.813 -27.616 1.00 34.21 C ANISOU 2934 CB TYR B 257 4820 5559 2619 772 51 -311 C ATOM 2935 CG TYR B 257 -139.069 -31.067 -27.815 1.00 26.06 C ANISOU 2935 CG TYR B 257 3818 4693 1392 803 114 -215 C ATOM 2936 CD1 TYR B 257 -140.018 -30.281 -27.194 1.00 33.31 C ANISOU 2936 CD1 TYR B 257 4786 5717 2153 780 60 -264 C ATOM 2937 CD2 TYR B 257 -139.499 -32.078 -28.658 1.00 31.14 C ANISOU 2937 CD2 TYR B 257 4436 5378 2017 850 232 -69 C ATOM 2938 CE1 TYR B 257 -141.378 -30.516 -27.395 1.00 53.31 C ANISOU 2938 CE1 TYR B 257 7351 8404 4502 806 117 -174 C ATOM 2939 CE2 TYR B 257 -140.837 -32.323 -28.867 1.00 39.29 C ANISOU 2939 CE2 TYR B 257 5490 6552 2885 874 295 26 C ATOM 2940 CZ TYR B 257 -141.778 -31.545 -28.233 1.00 55.73 C ANISOU 2940 CZ TYR B 257 7628 8747 4799 853 236 -28 C ATOM 2941 OH TYR B 257 -143.117 -31.805 -28.445 1.00 62.17 O ANISOU 2941 OH TYR B 257 8469 9707 5446 876 297 70 O ATOM 2942 N LEU B 258 -136.387 -32.164 -30.076 1.00 29.38 N ANISOU 2942 N LEU B 258 4137 4815 2212 847 290 -228 N ATOM 2943 CA LEU B 258 -136.326 -33.058 -31.216 1.00 28.60 C ANISOU 2943 CA LEU B 258 4001 4694 2172 887 429 -115 C ATOM 2944 C LEU B 258 -136.944 -34.380 -30.817 1.00 34.08 C ANISOU 2944 C LEU B 258 4669 5431 2848 905 441 124 C ATOM 2945 O LEU B 258 -136.618 -34.913 -29.767 1.00 53.74 O ANISOU 2945 O LEU B 258 7147 7873 5400 879 339 204 O ATOM 2946 CB LEU B 258 -134.863 -33.269 -31.623 1.00 19.77 C ANISOU 2946 CB LEU B 258 2844 3403 1265 874 435 -155 C ATOM 2947 CG LEU B 258 -134.630 -34.098 -32.877 1.00 23.31 C ANISOU 2947 CG LEU B 258 3240 3788 1827 899 582 -48 C ATOM 2948 CD1 LEU B 258 -135.455 -33.565 -34.020 1.00 26.62 C ANISOU 2948 CD1 LEU B 258 3665 4285 2165 915 709 -110 C ATOM 2949 CD2 LEU B 258 -133.153 -34.122 -33.227 1.00 47.18 C ANISOU 2949 CD2 LEU B 258 6223 6625 5080 867 572 -112 C ATOM 2950 N ASN B 259 -137.852 -34.889 -31.649 1.00 51.79 N ANISOU 2950 N ASN B 259 6898 7748 5033 937 562 232 N ATOM 2951 CA ASN B 259 -138.475 -36.196 -31.448 1.00 23.59 C ANISOU 2951 CA ASN B 259 3283 4189 1490 942 585 460 C ATOM 2952 C ASN B 259 -137.614 -37.284 -32.059 1.00 25.88 C ANISOU 2952 C ASN B 259 3505 4330 1997 937 644 581 C ATOM 2953 O ASN B 259 -137.308 -37.223 -33.250 1.00 29.24 O ANISOU 2953 O ASN B 259 3912 4711 2486 955 752 554 O ATOM 2954 CB ASN B 259 -139.844 -36.228 -32.122 1.00 32.75 C ANISOU 2954 CB ASN B 259 4456 5484 2504 973 687 514 C ATOM 2955 CG ASN B 259 -140.918 -35.527 -31.312 1.00 39.13 C ANISOU 2955 CG ASN B 259 5323 6440 3105 967 619 465 C ATOM 2956 OD1 ASN B 259 -141.070 -35.776 -30.120 1.00 54.03 O ANISOU 2956 OD1 ASN B 259 7209 8332 4989 939 508 523 O ATOM 2957 ND2 ASN B 259 -141.668 -34.648 -31.960 1.00 29.83 N ANISOU 2957 ND2 ASN B 259 4195 5373 1765 983 689 356 N ATOM 2958 N ILE B 260 -137.226 -38.285 -31.263 1.00 20.57 N ANISOU 2958 N ILE B 260 2787 3564 1463 898 573 706 N ATOM 2959 CA ILE B 260 -136.306 -39.299 -31.743 1.00 18.95 C ANISOU 2959 CA ILE B 260 2513 3194 1492 871 607 798 C ATOM 2960 C ILE B 260 -136.642 -40.699 -31.303 1.00 29.98 C ANISOU 2960 C ILE B 260 3836 4531 3023 824 583 944 C ATOM 2961 O ILE B 260 -137.376 -40.892 -30.348 1.00 46.33 O ANISOU 2961 O ILE B 260 5915 6664 5026 805 522 979 O ATOM 2962 CB ILE B 260 -134.916 -39.031 -31.209 1.00 26.52 C ANISOU 2962 CB ILE B 260 3482 4030 2564 832 525 720 C ATOM 2963 CG1 ILE B 260 -134.982 -38.954 -29.691 1.00 30.44 C ANISOU 2963 CG1 ILE B 260 4000 4537 3031 783 383 696 C ATOM 2964 CG2 ILE B 260 -134.357 -37.739 -31.787 1.00 43.74 C ANISOU 2964 CG2 ILE B 260 5719 6234 4667 871 557 537 C ATOM 2965 CD1 ILE B 260 -133.648 -39.207 -29.010 1.00 45.09 C ANISOU 2965 CD1 ILE B 260 5839 6223 5069 704 289 659 C ATOM 2966 N THR B 261 -136.081 -41.679 -31.997 1.00 24.78 N ANISOU 2966 N THR B 261 3103 3745 2568 798 626 1005 N ATOM 2967 CA THR B 261 -136.105 -43.059 -31.530 1.00 22.42 C ANISOU 2967 CA THR B 261 2725 3365 2427 730 587 1072 C ATOM 2968 C THR B 261 -134.666 -43.454 -31.470 1.00 30.52 C ANISOU 2968 C THR B 261 3709 4234 3651 644 537 995 C ATOM 2969 O THR B 261 -133.876 -42.928 -32.257 1.00 34.31 O ANISOU 2969 O THR B 261 4195 4662 4178 663 574 951 O ATOM 2970 CB THR B 261 -136.752 -43.989 -32.550 1.00 28.66 C ANISOU 2970 CB THR B 261 3453 4159 3278 765 676 1172 C ATOM 2971 OG1 THR B 261 -136.053 -43.877 -33.791 1.00 23.72 O ANISOU 2971 OG1 THR B 261 2808 3457 2747 787 740 1154 O ATOM 2972 CG2 THR B 261 -138.212 -43.620 -32.767 1.00 29.03 C ANISOU 2972 CG2 THR B 261 3541 4368 3121 839 740 1243 C ATOM 2973 N PHE B 262 -134.292 -44.371 -30.584 1.00 13.88 N ANISOU 2973 N PHE B 262 1561 2060 1654 551 464 970 N ATOM 2974 CA PHE B 262 -132.902 -44.836 -30.608 1.00 23.53 C ANISOU 2974 CA PHE B 262 2714 3178 3047 481 444 902 C ATOM 2975 C PHE B 262 -132.715 -45.965 -31.601 1.00 32.16 C ANISOU 2975 C PHE B 262 3687 4246 4286 497 513 953 C ATOM 2976 O PHE B 262 -131.622 -46.520 -31.721 1.00 34.91 O ANISOU 2976 O PHE B 262 3973 4531 4762 429 488 893 O ATOM 2977 CB PHE B 262 -132.405 -45.275 -29.239 1.00 25.89 C ANISOU 2977 CB PHE B 262 2986 3451 3402 406 371 868 C ATOM 2978 CG PHE B 262 -132.197 -44.147 -28.291 1.00 28.83 C ANISOU 2978 CG PHE B 262 3467 3813 3673 381 284 792 C ATOM 2979 CD1 PHE B 262 -130.955 -43.562 -28.153 1.00 18.84 C ANISOU 2979 CD1 PHE B 262 2232 2471 2457 320 231 682 C ATOM 2980 CD2 PHE B 262 -133.250 -43.674 -27.526 1.00 35.68 C ANISOU 2980 CD2 PHE B 262 4401 4758 4399 420 249 829 C ATOM 2981 CE1 PHE B 262 -130.762 -42.533 -27.269 1.00 15.88 C ANISOU 2981 CE1 PHE B 262 1952 2078 2003 310 138 610 C ATOM 2982 CE2 PHE B 262 -133.073 -42.634 -26.647 1.00 15.69 C ANISOU 2982 CE2 PHE B 262 1958 2222 1782 405 156 753 C ATOM 2983 CZ PHE B 262 -131.822 -42.064 -26.518 1.00 31.69 C ANISOU 2983 CZ PHE B 262 4014 4156 3872 355 97 644 C ATOM 2984 N ASP B 263 -133.775 -46.310 -32.319 1.00 20.23 N ANISOU 2984 N ASP B 263 2164 2786 2739 575 580 1052 N ATOM 2985 CA ASP B 263 -133.620 -47.352 -33.308 1.00 23.62 C ANISOU 2985 CA ASP B 263 2485 3181 3309 600 635 1103 C ATOM 2986 C ASP B 263 -133.716 -46.834 -34.722 1.00 29.83 C ANISOU 2986 C ASP B 263 3309 3944 4081 656 697 1111 C ATOM 2987 O ASP B 263 -134.476 -45.900 -34.993 1.00 30.80 O ANISOU 2987 O ASP B 263 3531 4118 4052 699 727 1129 O ATOM 2988 CB ASP B 263 -134.629 -48.472 -33.079 1.00 24.94 C ANISOU 2988 CB ASP B 263 2578 3402 3497 641 667 1223 C ATOM 2989 CG ASP B 263 -134.323 -49.268 -31.844 1.00 32.85 C ANISOU 2989 CG ASP B 263 3538 4390 4554 562 600 1202 C ATOM 2990 OD1 ASP B 263 -133.232 -49.880 -31.767 1.00 57.17 O ANISOU 2990 OD1 ASP B 263 6621 7386 7716 462 531 1103 O ATOM 2991 OD2 ASP B 263 -135.188 -49.296 -30.952 1.00 57.71 O ANISOU 2991 OD2 ASP B 263 6684 7608 7635 586 599 1270 O ATOM 2992 N LYS B 264 -132.992 -47.484 -35.616 1.00 27.05 N ANISOU 2992 N LYS B 264 2940 3505 3834 589 676 1059 N ATOM 2993 CA LYS B 264 -132.935 -47.168 -37.025 1.00 26.82 C ANISOU 2993 CA LYS B 264 2932 3434 3825 623 730 1068 C ATOM 2994 C LYS B 264 -134.209 -47.545 -37.736 1.00 44.51 C ANISOU 2994 C LYS B 264 5145 5727 6039 741 831 1217 C ATOM 2995 O LYS B 264 -134.989 -48.315 -37.214 1.00 62.36 O ANISOU 2995 O LYS B 264 7354 8052 8287 780 847 1306 O ATOM 2996 CB LYS B 264 -131.816 -47.948 -37.662 1.00 47.95 C ANISOU 2996 CB LYS B 264 5578 6030 6612 528 672 986 C ATOM 2997 CG LYS B 264 -130.449 -47.577 -37.195 1.00 66.61 C ANISOU 2997 CG LYS B 264 7964 8357 8988 422 575 846 C ATOM 2998 CD LYS B 264 -129.396 -48.069 -38.149 1.00 79.95 C ANISOU 2998 CD LYS B 264 9633 9998 10747 362 528 775 C ATOM 2999 CE LYS B 264 -128.062 -47.440 -37.822 1.00 94.62 C ANISOU 2999 CE LYS B 264 11519 11843 12591 277 438 647 C ATOM 3000 NZ LYS B 264 -126.910 -48.087 -38.496 1.00 96.80 N ANISOU 3000 NZ LYS B 264 11773 12101 12904 200 418 605 N ATOM 3001 N GLY B 265 -134.436 -46.987 -38.917 1.00 44.27 N ANISOU 3001 N GLY B 265 5148 5672 6002 801 906 1250 N ATOM 3002 CA GLY B 265 -135.548 -47.408 -39.753 1.00 47.86 C ANISOU 3002 CA GLY B 265 5579 6164 6441 895 1006 1383 C ATOM 3003 C GLY B 265 -136.925 -46.861 -39.421 1.00 42.66 C ANISOU 3003 C GLY B 265 4987 5649 5571 937 1071 1450 C ATOM 3004 O GLY B 265 -137.896 -47.117 -40.136 1.00 58.22 O ANISOU 3004 O GLY B 265 6955 7672 7494 987 1158 1539 O ATOM 3005 N VAL B 266 -137.026 -46.096 -38.349 1.00 26.55 N ANISOU 3005 N VAL B 266 3005 3686 3398 920 1031 1402 N ATOM 3006 CA VAL B 266 -138.319 -45.573 -37.968 1.00 22.39 C ANISOU 3006 CA VAL B 266 2535 3320 2652 960 1080 1446 C ATOM 3007 C VAL B 266 -138.605 -44.302 -38.748 1.00 51.17 C ANISOU 3007 C VAL B 266 6257 7042 6143 998 1179 1393 C ATOM 3008 O VAL B 266 -137.849 -43.339 -38.664 1.00 36.14 O ANISOU 3008 O VAL B 266 4399 5119 4214 979 1165 1284 O ATOM 3009 CB VAL B 266 -138.367 -45.258 -36.476 1.00 37.87 C ANISOU 3009 CB VAL B 266 4526 5343 4519 927 988 1405 C ATOM 3010 CG1 VAL B 266 -139.693 -44.594 -36.111 1.00 46.33 C ANISOU 3010 CG1 VAL B 266 5663 6595 5345 970 1027 1432 C ATOM 3011 CG2 VAL B 266 -138.156 -46.540 -35.662 1.00 42.80 C ANISOU 3011 CG2 VAL B 266 5071 5903 5290 869 904 1427 C ATOM 3012 N TYR B 267 -139.691 -44.306 -39.518 1.00 46.40 N ANISOU 3012 N TYR B 267 5662 6530 5439 1045 1285 1449 N ATOM 3013 CA TYR B 267 -140.144 -43.086 -40.179 1.00 37.15 C ANISOU 3013 CA TYR B 267 4556 5467 4094 1071 1389 1359 C ATOM 3014 C TYR B 267 -141.551 -42.701 -39.760 1.00 29.34 C ANISOU 3014 C TYR B 267 3615 4671 2860 1107 1426 1373 C ATOM 3015 O TYR B 267 -142.460 -43.520 -39.764 1.00 60.32 O ANISOU 3015 O TYR B 267 7508 8640 6771 1131 1448 1497 O ATOM 3016 CB TYR B 267 -140.045 -43.176 -41.703 1.00 46.41 C ANISOU 3016 CB TYR B 267 5700 6569 5364 1086 1501 1368 C ATOM 3017 CG TYR B 267 -140.669 -41.980 -42.379 1.00 40.11 C ANISOU 3017 CG TYR B 267 4956 5897 4387 1109 1619 1253 C ATOM 3018 CD1 TYR B 267 -140.014 -40.767 -42.417 1.00 57.45 C ANISOU 3018 CD1 TYR B 267 7190 8096 6541 1087 1622 1075 C ATOM 3019 CD2 TYR B 267 -141.920 -42.062 -42.952 1.00 55.41 C ANISOU 3019 CD2 TYR B 267 6901 7951 6201 1151 1726 1305 C ATOM 3020 CE1 TYR B 267 -140.584 -39.664 -43.021 1.00 66.96 C ANISOU 3020 CE1 TYR B 267 8435 9413 7595 1104 1725 934 C ATOM 3021 CE2 TYR B 267 -142.498 -40.967 -43.559 1.00 64.13 C ANISOU 3021 CE2 TYR B 267 8052 9171 7142 1167 1834 1178 C ATOM 3022 CZ TYR B 267 -141.821 -39.771 -43.588 1.00 52.22 C ANISOU 3022 CZ TYR B 267 6578 7661 5604 1142 1832 985 C ATOM 3023 OH TYR B 267 -142.377 -38.676 -44.184 1.00 46.38 O ANISOU 3023 OH TYR B 267 5877 7029 4715 1152 1935 832 O ATOM 3024 N SER B 268 -141.708 -41.432 -39.411 1.00 43.76 N ANISOU 3024 N SER B 268 5516 6612 4497 1107 1427 1233 N ATOM 3025 CA SER B 268 -142.917 -40.914 -38.800 1.00 31.83 C ANISOU 3025 CA SER B 268 4066 5288 2741 1128 1428 1219 C ATOM 3026 C SER B 268 -143.718 -40.077 -39.758 1.00 36.92 C ANISOU 3026 C SER B 268 4756 6050 3222 1155 1558 1132 C ATOM 3027 O SER B 268 -143.217 -39.087 -40.279 1.00 65.22 O ANISOU 3027 O SER B 268 8368 9624 6788 1145 1601 968 O ATOM 3028 CB SER B 268 -142.548 -40.047 -37.605 1.00 35.92 C ANISOU 3028 CB SER B 268 4641 5853 3153 1104 1313 1101 C ATOM 3029 OG SER B 268 -143.638 -39.226 -37.239 1.00 45.75 O ANISOU 3029 OG SER B 268 5958 7280 4145 1119 1321 1037 O ATOM 3030 N ASP B 269 -144.971 -40.456 -39.973 1.00 36.31 N ANISOU 3030 N ASP B 269 4683 6083 3031 1185 1623 1230 N ATOM 3031 CA ASP B 269 -145.857 -39.684 -40.817 1.00 44.48 C ANISOU 3031 CA ASP B 269 5765 7242 3892 1206 1752 1149 C ATOM 3032 C ASP B 269 -146.382 -38.443 -40.093 1.00 45.95 C ANISOU 3032 C ASP B 269 6046 7586 3827 1195 1713 998 C ATOM 3033 O ASP B 269 -146.863 -37.504 -40.721 1.00 59.96 O ANISOU 3033 O ASP B 269 7872 9451 5458 1197 1806 863 O ATOM 3034 CB ASP B 269 -147.019 -40.561 -41.287 1.00 70.82 C ANISOU 3034 CB ASP B 269 9074 10641 7194 1241 1835 1315 C ATOM 3035 CG ASP B 269 -146.562 -41.709 -42.181 1.00 73.89 C ANISOU 3035 CG ASP B 269 9372 10872 7831 1254 1883 1443 C ATOM 3036 OD1 ASP B 269 -145.623 -41.513 -42.987 1.00 65.25 O ANISOU 3036 OD1 ASP B 269 8252 9657 6884 1241 1920 1371 O ATOM 3037 OD2 ASP B 269 -147.148 -42.808 -42.079 1.00 73.58 O ANISOU 3037 OD2 ASP B 269 9285 10826 7845 1275 1879 1611 O ATOM 3038 N MET B 270 -146.295 -38.447 -38.768 1.00 41.54 N ANISOU 3038 N MET B 270 5508 7052 3223 1178 1571 1015 N ATOM 3039 CA MET B 270 -146.790 -37.328 -37.972 1.00 39.98 C ANISOU 3039 CA MET B 270 5398 6994 2799 1163 1508 882 C ATOM 3040 C MET B 270 -145.851 -36.130 -38.083 1.00 53.98 C ANISOU 3040 C MET B 270 7208 8720 4580 1138 1488 655 C ATOM 3041 O MET B 270 -146.284 -34.972 -38.141 1.00 54.10 O ANISOU 3041 O MET B 270 7297 8835 4422 1127 1509 487 O ATOM 3042 CB MET B 270 -146.944 -37.762 -36.501 1.00 43.04 C ANISOU 3042 CB MET B 270 5784 7404 3164 1149 1356 980 C ATOM 3043 CG MET B 270 -147.259 -36.634 -35.510 1.00 53.36 C ANISOU 3043 CG MET B 270 7176 8826 4274 1126 1254 844 C ATOM 3044 SD MET B 270 -147.837 -37.239 -33.721 1.00 82.21 S ANISOU 3044 SD MET B 270 10823 12532 7882 1106 1083 994 S ATOM 3045 CE MET B 270 -148.019 -35.497 -32.846 1.00276.84 C ANISOU 3045 CE MET B 270 35586 37300 32300 1072 972 765 C ATOM 3046 N TYR B 271 -144.557 -36.418 -38.110 1.00 41.66 N ANISOU 3046 N TYR B 271 5700 4591 5536 1038 2082 952 N ATOM 3047 CA TYR B 271 -143.547 -35.384 -38.190 1.00 31.05 C ANISOU 3047 CA TYR B 271 4406 3262 4131 1040 2038 903 C ATOM 3048 C TYR B 271 -142.864 -35.435 -39.555 1.00 37.28 C ANISOU 3048 C TYR B 271 5157 4055 4951 1048 2061 900 C ATOM 3049 O TYR B 271 -141.889 -34.735 -39.802 1.00 54.34 O ANISOU 3049 O TYR B 271 7351 6221 7073 1048 2031 859 O ATOM 3050 CB TYR B 271 -142.528 -35.568 -37.077 1.00 33.52 C ANISOU 3050 CB TYR B 271 4770 3537 4431 997 2008 860 C ATOM 3051 CG TYR B 271 -143.135 -35.775 -35.702 1.00 45.52 C ANISOU 3051 CG TYR B 271 6315 5043 5936 985 1992 862 C ATOM 3052 CD1 TYR B 271 -143.232 -37.040 -35.147 1.00 45.33 C ANISOU 3052 CD1 TYR B 271 6269 4978 5976 956 2024 877 C ATOM 3053 CD2 TYR B 271 -143.597 -34.703 -34.956 1.00 63.30 C ANISOU 3053 CD2 TYR B 271 8612 7325 8113 1002 1942 846 C ATOM 3054 CE1 TYR B 271 -143.778 -37.232 -33.896 1.00 48.91 C ANISOU 3054 CE1 TYR B 271 6745 5421 6417 947 2009 876 C ATOM 3055 CE2 TYR B 271 -144.145 -34.887 -33.705 1.00 59.46 C ANISOU 3055 CE2 TYR B 271 8145 6827 7618 992 1926 846 C ATOM 3056 CZ TYR B 271 -144.239 -36.149 -33.183 1.00 43.59 C ANISOU 3056 CZ TYR B 271 6113 4778 5669 966 1960 860 C ATOM 3057 OH TYR B 271 -144.780 -36.326 -31.930 1.00 48.09 O ANISOU 3057 OH TYR B 271 6703 5339 6230 959 1944 857 O ATOM 3058 N ASN B 272 -143.414 -36.250 -40.447 1.00 45.31 N ANISOU 3058 N ASN B 272 6103 5072 6041 1056 2113 945 N ATOM 3059 CA ASN B 272 -142.804 -36.502 -41.742 1.00 32.40 C ANISOU 3059 CA ASN B 272 4418 3436 4455 1061 2141 947 C ATOM 3060 C ASN B 272 -141.291 -36.501 -41.776 1.00 47.62 C ANISOU 3060 C ASN B 272 6384 5335 6375 1035 2117 892 C ATOM 3061 O ASN B 272 -140.657 -35.868 -42.639 1.00 53.16 O ANISOU 3061 O ASN B 272 7110 6060 7028 1057 2087 856 O ATOM 3062 CB ASN B 272 -143.406 -35.607 -42.831 1.00 52.25 C ANISOU 3062 CB ASN B 272 6912 6008 6935 1113 2138 958 C ATOM 3063 CG ASN B 272 -144.915 -35.797 -42.973 1.00 59.57 C ANISOU 3063 CG ASN B 272 7800 6964 7870 1139 2165 1013 C ATOM 3064 OD1 ASN B 272 -145.700 -34.991 -42.470 1.00 58.38 O ANISOU 3064 OD1 ASN B 272 7686 6844 7652 1163 2139 1014 O ATOM 3065 ND2 ASN B 272 -145.327 -36.876 -43.647 1.00 48.82 N ANISOU 3065 ND2 ASN B 272 6364 5591 6594 1132 2217 1059 N ATOM 3066 N ALA B 273 -140.720 -37.191 -40.793 1.00 30.58 N ANISOU 3066 N ALA B 273 4232 3125 4263 988 2128 883 N ATOM 3067 CA ALA B 273 -139.276 -37.292 -40.668 1.00 26.72 C ANISOU 3067 CA ALA B 273 3779 2602 3770 957 2110 831 C ATOM 3068 C ALA B 273 -138.771 -38.670 -40.273 1.00 37.15 C ANISOU 3068 C ALA B 273 5075 3863 5178 906 2145 836 C ATOM 3069 O ALA B 273 -139.525 -39.486 -39.767 1.00 44.72 O ANISOU 3069 O ALA B 273 6009 4805 6177 892 2169 873 O ATOM 3070 CB ALA B 273 -138.919 -36.280 -39.598 1.00 54.19 C ANISOU 3070 CB ALA B 273 7346 6095 7149 953 2049 787 C ATOM 3071 N ASP B 274 -137.492 -38.933 -40.518 1.00 52.37 N ANISOU 3071 N ASP B 274 7006 5756 7135 880 2147 796 N ATOM 3072 CA ASP B 274 -136.828 -40.062 -39.889 1.00 47.75 C ANISOU 3072 CA ASP B 274 6417 5113 6613 826 2168 787 C ATOM 3073 C ASP B 274 -136.627 -39.668 -38.438 1.00 52.53 C ANISOU 3073 C ASP B 274 7106 5716 7137 807 2126 754 C ATOM 3074 O ASP B 274 -136.370 -38.487 -38.144 1.00 33.14 O ANISOU 3074 O ASP B 274 4712 3292 4586 825 2075 719 O ATOM 3075 CB ASP B 274 -135.475 -40.344 -40.535 1.00 56.26 C ANISOU 3075 CB ASP B 274 7489 6151 7738 786 2108 737 C ATOM 3076 CG ASP B 274 -135.598 -41.122 -41.823 1.00 79.85 C ANISOU 3076 CG ASP B 274 10386 9121 10831 779 2118 768 C ATOM 3077 OD1 ASP B 274 -136.298 -42.157 -41.813 1.00 77.47 O ANISOU 3077 OD1 ASP B 274 10027 8801 10607 765 2170 822 O ATOM 3078 OD2 ASP B 274 -135.005 -40.695 -42.841 1.00 95.30 O ANISOU 3078 OD2 ASP B 274 12330 11084 12795 789 2073 741 O ATOM 3079 N LEU B 275 -136.745 -40.645 -37.535 1.00 25.90 N ANISOU 3079 N LEU B 275 3732 2305 3804 769 2142 766 N ATOM 3080 CA LEU B 275 -136.674 -40.364 -36.112 1.00 25.33 C ANISOU 3080 CA LEU B 275 3730 2232 3663 753 2102 737 C ATOM 3081 C LEU B 275 -135.377 -40.814 -35.477 1.00 29.68 C ANISOU 3081 C LEU B 275 4319 2740 4216 702 2094 690 C ATOM 3082 O LEU B 275 -135.055 -40.408 -34.356 1.00 34.95 O ANISOU 3082 O LEU B 275 5052 3412 4814 689 2052 654 O ATOM 3083 CB LEU B 275 -137.874 -40.965 -35.365 1.00 29.34 C ANISOU 3083 CB LEU B 275 4218 2736 4193 758 2114 777 C ATOM 3084 CG LEU B 275 -139.079 -40.056 -35.083 1.00 47.15 C ANISOU 3084 CG LEU B 275 6489 5042 6382 803 2087 796 C ATOM 3085 CD1 LEU B 275 -139.317 -39.071 -36.207 1.00 52.00 C ANISOU 3085 CD1 LEU B 275 7091 5703 6964 844 2080 806 C ATOM 3086 CD2 LEU B 275 -140.330 -40.882 -34.825 1.00 70.75 C ANISOU 3086 CD2 LEU B 275 9433 8024 9424 812 2119 846 C ATOM 3087 N TYR B 276 -134.617 -41.649 -36.169 1.00 33.41 N ANISOU 3087 N TYR B 276 4753 3169 4772 662 2078 678 N ATOM 3088 CA TYR B 276 -133.403 -42.183 -35.553 1.00 34.23 C ANISOU 3088 CA TYR B 276 4893 3225 4886 599 2008 623 C ATOM 3089 C TYR B 276 -132.403 -41.082 -35.167 1.00 24.35 C ANISOU 3089 C TYR B 276 3721 1995 3536 596 1942 559 C ATOM 3090 O TYR B 276 -131.940 -40.324 -36.007 1.00 33.88 O ANISOU 3090 O TYR B 276 4934 3221 4719 611 1904 537 O ATOM 3091 CB TYR B 276 -132.751 -43.250 -36.434 1.00 38.14 C ANISOU 3091 CB TYR B 276 5333 3668 5492 553 1969 617 C ATOM 3092 CG TYR B 276 -131.432 -43.760 -35.897 1.00 29.10 C ANISOU 3092 CG TYR B 276 4226 2476 4355 490 1892 556 C ATOM 3093 CD1 TYR B 276 -131.291 -44.139 -34.568 1.00 24.85 C ANISOU 3093 CD1 TYR B 276 3730 1920 3790 463 1891 539 C ATOM 3094 CD2 TYR B 276 -130.328 -43.861 -36.721 1.00 25.23 C ANISOU 3094 CD2 TYR B 276 3728 1961 3899 458 1821 515 C ATOM 3095 CE1 TYR B 276 -130.078 -44.599 -34.073 1.00 25.49 C ANISOU 3095 CE1 TYR B 276 3846 1963 3876 408 1821 481 C ATOM 3096 CE2 TYR B 276 -129.113 -44.319 -36.241 1.00 43.54 C ANISOU 3096 CE2 TYR B 276 6082 4239 6222 401 1750 459 C ATOM 3097 CZ TYR B 276 -128.986 -44.689 -34.921 1.00 30.04 C ANISOU 3097 CZ TYR B 276 4415 2515 4484 376 1751 442 C ATOM 3098 OH TYR B 276 -127.760 -45.151 -34.467 1.00 24.51 O ANISOU 3098 OH TYR B 276 3748 1777 3787 321 1680 385 O ATOM 3099 N VAL B 277 -132.070 -41.026 -33.880 1.00 27.14 N ANISOU 3099 N VAL B 277 4133 2344 3833 574 1928 531 N ATOM 3100 CA VAL B 277 -131.212 -40.003 -33.320 1.00 23.28 C ANISOU 3100 CA VAL B 277 3722 1879 3244 568 1872 476 C ATOM 3101 C VAL B 277 -129.909 -39.827 -34.102 1.00 24.90 C ANISOU 3101 C VAL B 277 3936 2066 3460 536 1786 425 C ATOM 3102 O VAL B 277 -129.549 -38.711 -34.464 1.00 36.72 O ANISOU 3102 O VAL B 277 5467 3594 4890 558 1752 402 O ATOM 3103 CB VAL B 277 -130.858 -40.297 -31.857 1.00 22.88 C ANISOU 3103 CB VAL B 277 3723 1816 3155 535 1861 450 C ATOM 3104 CG1 VAL B 277 -130.609 -38.993 -31.138 1.00 32.15 C ANISOU 3104 CG1 VAL B 277 4972 3035 4208 555 1840 420 C ATOM 3105 CG2 VAL B 277 -131.967 -41.046 -31.182 1.00114.56 C ANISOU 3105 CG2 VAL B 277 15307 13418 14801 546 1935 499 C ATOM 3106 N GLY B 278 -129.201 -40.935 -34.323 1.00 34.19 N ANISOU 3106 N GLY B 278 5084 3190 4718 483 1750 408 N ATOM 3107 CA GLY B 278 -127.909 -40.928 -34.983 1.00 23.46 C ANISOU 3107 CA GLY B 278 3733 1806 3375 444 1667 358 C ATOM 3108 C GLY B 278 -127.959 -40.237 -36.336 1.00 50.20 C ANISOU 3108 C GLY B 278 7091 5213 6768 479 1655 365 C ATOM 3109 O GLY B 278 -126.986 -39.596 -36.780 1.00 42.18 O ANISOU 3109 O GLY B 278 6107 4201 5719 467 1585 321 O ATOM 3110 N ASP B 279 -129.109 -40.351 -36.990 1.00 26.01 N ANISOU 3110 N ASP B 279 3970 2166 3748 523 1723 422 N ATOM 3111 CA ASP B 279 -129.259 -39.864 -38.361 1.00 36.23 C ANISOU 3111 CA ASP B 279 5224 3478 5063 558 1719 433 C ATOM 3112 C ASP B 279 -129.774 -38.439 -38.453 1.00 24.19 C ANISOU 3112 C ASP B 279 3733 2013 3443 621 1736 438 C ATOM 3113 O ASP B 279 -129.684 -37.809 -39.502 1.00 60.59 O ANISOU 3113 O ASP B 279 8329 6643 8051 651 1716 433 O ATOM 3114 CB ASP B 279 -130.220 -40.780 -39.145 1.00 39.86 C ANISOU 3114 CB ASP B 279 5594 3927 5625 573 1782 494 C ATOM 3115 CG ASP B 279 -129.542 -42.029 -39.682 1.00 47.82 C ANISOU 3115 CG ASP B 279 6553 4873 6741 517 1745 485 C ATOM 3116 OD1 ASP B 279 -128.463 -42.400 -39.171 1.00 48.21 O ANISOU 3116 OD1 ASP B 279 6640 4887 6791 463 1682 437 O ATOM 3117 OD2 ASP B 279 -130.097 -42.633 -40.623 1.00 63.93 O ANISOU 3117 OD2 ASP B 279 8518 6906 8868 527 1779 527 O ATOM 3118 N VAL B 280 -130.327 -37.934 -37.363 1.00 35.93 N ANISOU 3118 N VAL B 280 5268 3531 4855 642 1773 448 N ATOM 3119 CA VAL B 280 -131.124 -36.726 -37.437 1.00 27.24 C ANISOU 3119 CA VAL B 280 4189 2487 3675 709 1808 466 C ATOM 3120 C VAL B 280 -130.752 -35.587 -36.477 1.00 31.54 C ANISOU 3120 C VAL B 280 4821 3061 4102 717 1776 430 C ATOM 3121 O VAL B 280 -131.207 -34.475 -36.675 1.00 26.08 O ANISOU 3121 O VAL B 280 4153 2413 3342 770 1787 436 O ATOM 3122 CB VAL B 280 -132.602 -37.078 -37.215 1.00 48.24 C ANISOU 3122 CB VAL B 280 6806 5167 6355 749 1907 532 C ATOM 3123 CG1 VAL B 280 -133.465 -35.821 -37.179 1.00 63.18 C ANISOU 3123 CG1 VAL B 280 8724 7120 8162 809 1918 551 C ATOM 3124 CG2 VAL B 280 -133.071 -38.004 -38.312 1.00 64.21 C ANISOU 3124 CG2 VAL B 280 8740 7171 8487 751 1942 573 C ATOM 3125 N LEU B 281 -129.964 -35.834 -35.431 1.00 22.63 N ANISOU 3125 N LEU B 281 3741 1911 2946 666 1737 395 N ATOM 3126 CA LEU B 281 -129.818 -34.788 -34.424 1.00 27.42 C ANISOU 3126 CA LEU B 281 4425 2551 3442 677 1720 372 C ATOM 3127 C LEU B 281 -128.877 -33.691 -34.883 1.00 21.78 C ANISOU 3127 C LEU B 281 3758 1852 2667 677 1641 327 C ATOM 3128 O LEU B 281 -129.286 -32.545 -35.043 1.00 37.13 O ANISOU 3128 O LEU B 281 5730 3837 4542 727 1646 331 O ATOM 3129 CB LEU B 281 -129.418 -35.318 -33.039 1.00 29.02 C ANISOU 3129 CB LEU B 281 4666 2735 3624 629 1714 353 C ATOM 3130 CG LEU B 281 -129.300 -34.179 -32.013 1.00 21.13 C ANISOU 3130 CG LEU B 281 3733 1776 2519 629 1660 336 C ATOM 3131 CD1 LEU B 281 -129.890 -34.515 -30.676 1.00 25.39 C ANISOU 3131 CD1 LEU B 281 4272 2319 3054 610 1652 354 C ATOM 3132 CD2 LEU B 281 -127.856 -33.740 -31.852 1.00 47.66 C ANISOU 3132 CD2 LEU B 281 7158 5127 5823 596 1604 273 C ATOM 3133 N VAL B 282 -127.615 -34.034 -35.071 1.00 21.72 N ANISOU 3133 N VAL B 282 3761 1809 2682 621 1567 282 N ATOM 3134 CA VAL B 282 -126.672 -33.067 -35.611 1.00 24.92 C ANISOU 3134 CA VAL B 282 4206 2223 3039 617 1486 240 C ATOM 3135 C VAL B 282 -127.334 -32.313 -36.750 1.00 28.62 C ANISOU 3135 C VAL B 282 4647 2720 3506 681 1504 261 C ATOM 3136 O VAL B 282 -127.496 -31.102 -36.686 1.00 64.11 O ANISOU 3136 O VAL B 282 9187 7252 7919 721 1491 255 O ATOM 3137 CB VAL B 282 -125.443 -33.745 -36.168 1.00 26.63 C ANISOU 3137 CB VAL B 282 4408 2395 3315 558 1415 202 C ATOM 3138 CG1 VAL B 282 -124.504 -32.702 -36.730 1.00 47.36 C ANISOU 3138 CG1 VAL B 282 7077 5030 5889 556 1331 161 C ATOM 3139 CG2 VAL B 282 -124.777 -34.570 -35.083 1.00 33.98 C ANISOU 3139 CG2 VAL B 282 5362 3297 4251 496 1398 180 C ATOM 3140 N ASP B 283 -127.733 -33.042 -37.786 1.00 31.26 N ANISOU 3140 N ASP B 283 4907 3037 3931 693 1533 288 N ATOM 3141 CA ASP B 283 -128.404 -32.437 -38.937 1.00 27.59 C ANISOU 3141 CA ASP B 283 4408 2601 3474 756 1555 310 C ATOM 3142 C ASP B 283 -129.487 -31.440 -38.541 1.00 37.86 C ANISOU 3142 C ASP B 283 5736 3955 4696 823 1609 337 C ATOM 3143 O ASP B 283 -129.628 -30.399 -39.174 1.00 65.86 O ANISOU 3143 O ASP B 283 9296 7532 8197 872 1591 330 O ATOM 3144 CB ASP B 283 -129.000 -33.507 -39.858 1.00 44.12 C ANISOU 3144 CB ASP B 283 6410 4675 5678 763 1606 349 C ATOM 3145 CG ASP B 283 -127.967 -34.130 -40.790 1.00 71.70 C ANISOU 3145 CG ASP B 283 9871 8125 9248 718 1541 320 C ATOM 3146 OD1 ASP B 283 -126.958 -33.461 -41.098 1.00 75.03 O ANISOU 3146 OD1 ASP B 283 10333 8541 9633 703 1461 273 O ATOM 3147 OD2 ASP B 283 -128.166 -35.290 -41.222 1.00 88.69 O ANISOU 3147 OD2 ASP B 283 11955 10245 11497 697 1570 345 O ATOM 3148 N SER B 284 -130.246 -31.742 -37.496 1.00 28.66 N ANISOU 3148 N SER B 284 4577 2799 3512 827 1672 367 N ATOM 3149 CA SER B 284 -131.389 -30.902 -37.143 1.00 38.48 C ANISOU 3149 CA SER B 284 5823 4097 4702 860 1669 407 C ATOM 3150 C SER B 284 -131.007 -29.626 -36.390 1.00 46.61 C ANISOU 3150 C SER B 284 6923 5155 5632 852 1589 379 C ATOM 3151 O SER B 284 -131.753 -28.649 -36.394 1.00 49.94 O ANISOU 3151 O SER B 284 7348 5618 6011 884 1561 398 O ATOM 3152 CB SER B 284 -132.422 -31.698 -36.339 1.00 36.02 C ANISOU 3152 CB SER B 284 5476 3784 4426 845 1708 455 C ATOM 3153 OG SER B 284 -133.086 -32.640 -37.159 1.00 45.72 O ANISOU 3153 OG SER B 284 6631 5000 5742 863 1778 494 O ATOM 3154 N TYR B 285 -129.854 -29.635 -35.735 1.00 21.35 N ANISOU 3154 N TYR B 285 3779 1933 2400 807 1549 334 N ATOM 3155 CA TYR B 285 -129.423 -28.457 -35.001 1.00 21.62 C ANISOU 3155 CA TYR B 285 3874 1993 2347 794 1469 310 C ATOM 3156 C TYR B 285 -128.425 -27.681 -35.834 1.00 30.55 C ANISOU 3156 C TYR B 285 5047 3121 3440 807 1423 264 C ATOM 3157 O TYR B 285 -127.620 -26.901 -35.321 1.00 46.30 O ANISOU 3157 O TYR B 285 7101 5123 5369 782 1353 231 O ATOM 3158 CB TYR B 285 -128.823 -28.856 -33.647 1.00 31.38 C ANISOU 3158 CB TYR B 285 5145 3213 3565 735 1444 291 C ATOM 3159 CG TYR B 285 -129.881 -29.183 -32.640 1.00 27.17 C ANISOU 3159 CG TYR B 285 4582 2691 3051 732 1460 329 C ATOM 3160 CD1 TYR B 285 -130.440 -28.198 -31.849 1.00 48.09 C ANISOU 3160 CD1 TYR B 285 7243 5373 5655 741 1408 337 C ATOM 3161 CD2 TYR B 285 -130.346 -30.468 -32.498 1.00 27.99 C ANISOU 3161 CD2 TYR B 285 4644 2767 3222 721 1525 353 C ATOM 3162 CE1 TYR B 285 -131.434 -28.495 -30.926 1.00 47.93 C ANISOU 3162 CE1 TYR B 285 7195 5358 5657 742 1419 365 C ATOM 3163 CE2 TYR B 285 -131.350 -30.774 -31.588 1.00 38.50 C ANISOU 3163 CE2 TYR B 285 5951 4105 4572 722 1535 384 C ATOM 3164 CZ TYR B 285 -131.887 -29.785 -30.802 1.00 33.58 C ANISOU 3164 CZ TYR B 285 5343 3515 3903 733 1481 387 C ATOM 3165 OH TYR B 285 -132.877 -30.101 -29.892 1.00 32.40 O ANISOU 3165 OH TYR B 285 5170 3369 3774 736 1490 412 O ATOM 3166 N SER B 286 -128.500 -27.903 -37.137 1.00 20.91 N ANISOU 3166 N SER B 286 2210 2390 3346 915 1088 201 N ATOM 3167 CA SER B 286 -127.564 -27.321 -38.074 1.00 26.95 C ANISOU 3167 CA SER B 286 3088 2996 4156 956 1215 249 C ATOM 3168 C SER B 286 -128.297 -26.699 -39.255 1.00 23.63 C ANISOU 3168 C SER B 286 2795 2484 3700 1023 1363 200 C ATOM 3169 O SER B 286 -129.441 -27.044 -39.526 1.00 56.98 O ANISOU 3169 O SER B 286 7006 6776 7866 1046 1353 173 O ATOM 3170 CB SER B 286 -126.582 -28.389 -38.543 1.00 21.47 C ANISOU 3170 CB SER B 286 2365 2307 3485 960 1175 435 C ATOM 3171 OG SER B 286 -125.802 -28.819 -37.443 1.00 43.47 O ANISOU 3171 OG SER B 286 5070 5149 6298 891 1065 469 O ATOM 3172 N ASP B 287 -127.633 -25.780 -39.952 1.00 38.99 N ANISOU 3172 N ASP B 287 4872 4260 5683 1052 1524 206 N ATOM 3173 CA ASP B 287 -128.241 -25.059 -41.076 1.00 33.60 C ANISOU 3173 CA ASP B 287 4349 3449 4969 1112 1707 172 C ATOM 3174 C ASP B 287 -127.168 -24.384 -41.903 1.00 53.11 C ANISOU 3174 C ASP B 287 6923 5771 7484 1138 1827 226 C ATOM 3175 O ASP B 287 -126.660 -23.326 -41.543 1.00 75.75 O ANISOU 3175 O ASP B 287 9904 8480 10398 1104 1971 171 O ATOM 3176 CB ASP B 287 -129.237 -24.009 -40.575 1.00 36.08 C ANISOU 3176 CB ASP B 287 4808 3654 5246 1079 1890 13 C ATOM 3177 CG ASP B 287 -129.649 -23.021 -41.649 1.00 45.68 C ANISOU 3177 CG ASP B 287 6250 4689 6416 1108 2103 -50 C ATOM 3178 OD1 ASP B 287 -130.227 -21.982 -41.279 1.00 62.07 O ANISOU 3178 OD1 ASP B 287 8513 6634 8436 1029 2271 -216 O ATOM 3179 OD2 ASP B 287 -129.416 -23.267 -42.855 1.00 42.11 O ANISOU 3179 OD2 ASP B 287 5807 4226 5969 1187 2106 51 O ATOM 3180 N ASP B 288 -126.863 -25.001 -43.036 1.00 55.48 N ANISOU 3180 N ASP B 288 7217 6077 7786 1205 1857 380 N ATOM 3181 CA ASP B 288 -125.833 -24.534 -43.945 1.00 52.30 C ANISOU 3181 CA ASP B 288 6896 5549 7425 1248 2006 485 C ATOM 3182 C ASP B 288 -126.136 -23.137 -44.525 1.00 58.08 C ANISOU 3182 C ASP B 288 7822 6099 8145 1268 2195 374 C ATOM 3183 O ASP B 288 -125.247 -22.491 -45.089 1.00 51.01 O ANISOU 3183 O ASP B 288 7011 5078 7291 1292 2335 432 O ATOM 3184 CB ASP B 288 -125.631 -25.567 -45.063 1.00 44.19 C ANISOU 3184 CB ASP B 288 5825 4584 6382 1319 2020 681 C ATOM 3185 CG ASP B 288 -126.875 -25.749 -45.927 1.00 75.18 C ANISOU 3185 CG ASP B 288 9802 8518 10244 1383 2065 675 C ATOM 3186 OD1 ASP B 288 -127.814 -24.927 -45.822 1.00 74.15 O ANISOU 3186 OD1 ASP B 288 9767 8324 10083 1379 2117 518 O ATOM 3187 OD2 ASP B 288 -126.911 -26.713 -46.722 1.00 97.31 O ANISOU 3187 OD2 ASP B 288 12558 11395 13021 1432 2053 823 O ATOM 3188 N GLY B 289 -127.385 -22.686 -44.398 1.00 49.41 N ANISOU 3188 N GLY B 289 6812 4976 6986 1256 2232 228 N ATOM 3189 CA GLY B 289 -127.739 -21.304 -44.693 1.00 36.73 C ANISOU 3189 CA GLY B 289 5449 3147 5359 1241 2476 116 C ATOM 3190 C GLY B 289 -128.236 -21.040 -46.102 1.00 72.98 C ANISOU 3190 C GLY B 289 10158 7665 9907 1325 2607 152 C ATOM 3191 O GLY B 289 -128.565 -19.902 -46.448 1.00 40.20 O ANISOU 3191 O GLY B 289 6228 3322 5723 1307 2813 55 O ATOM 3192 N VAL B 290 -128.278 -22.079 -46.929 1.00 89.90 N ANISOU 3192 N VAL B 290 12174 9940 12045 1406 2513 294 N ATOM 3193 CA VAL B 290 -128.860 -21.955 -48.259 1.00 83.41 C ANISOU 3193 CA VAL B 290 11460 9049 11184 1499 2658 355 C ATOM 3194 C VAL B 290 -130.197 -21.404 -48.710 1.00 88.95 C ANISOU 3194 C VAL B 290 12146 9846 11804 1497 2585 253 C ATOM 3195 O VAL B 290 -130.249 -20.468 -49.513 1.00 75.74 O ANISOU 3195 O VAL B 290 10318 8338 10120 1466 2407 247 O ATOM 3196 CB VAL B 290 -128.181 -22.872 -49.293 1.00 72.04 C ANISOU 3196 CB VAL B 290 9940 7656 9774 1595 2685 605 C ATOM 3197 CG1 VAL B 290 -128.566 -24.334 -49.057 1.00 70.57 C ANISOU 3197 CG1 VAL B 290 9576 7670 9567 1597 2497 692 C ATOM 3198 CG2 VAL B 290 -128.553 -22.430 -50.705 1.00 67.62 C ANISOU 3198 CG2 VAL B 290 9525 6982 9186 1696 2883 672 C ATOM 3199 N VAL B 291 -131.273 -21.996 -48.213 1.00104.68 N ANISOU 3199 N VAL B 291 14311 11725 13735 1531 2745 181 N ATOM 3200 CA VAL B 291 -132.602 -21.678 -48.707 1.00118.78 C ANISOU 3200 CA VAL B 291 16133 13569 15431 1524 2739 75 C ATOM 3201 C VAL B 291 -132.993 -20.951 -47.425 1.00124.08 C ANISOU 3201 C VAL B 291 16906 14187 16051 1401 2777 -118 C ATOM 3202 O VAL B 291 -134.116 -20.468 -47.288 1.00136.14 O ANISOU 3202 O VAL B 291 18571 15687 17470 1356 2860 -263 O ATOM 3203 CB VAL B 291 -133.059 -23.154 -48.652 1.00117.08 C ANISOU 3203 CB VAL B 291 15683 13590 15211 1556 2517 165 C ATOM 3204 CG1 VAL B 291 -134.577 -23.247 -48.558 1.00123.41 C ANISOU 3204 CG1 VAL B 291 16519 14457 15914 1559 2527 65 C ATOM 3205 CG2 VAL B 291 -132.543 -23.916 -49.865 1.00110.38 C ANISOU 3205 CG2 VAL B 291 14798 12738 14403 1665 2564 407 C ATOM 3206 N SER B 292 -132.050 -20.866 -46.490 1.00112.11 N ANISOU 3206 N SER B 292 15333 12663 14602 1332 2720 -123 N ATOM 3207 CA SER B 292 -132.255 -20.115 -45.257 1.00106.36 C ANISOU 3207 CA SER B 292 14714 11869 13828 1189 2769 -306 C ATOM 3208 C SER B 292 -131.748 -18.691 -45.412 1.00 78.98 C ANISOU 3208 C SER B 292 11503 8147 10359 1108 2978 -405 C ATOM 3209 O SER B 292 -132.370 -17.746 -44.932 1.00 84.35 O ANISOU 3209 O SER B 292 12394 8719 10936 965 3091 -604 O ATOM 3210 CB SER B 292 -131.554 -20.791 -44.078 1.00121.06 C ANISOU 3210 CB SER B 292 16375 13859 15765 1148 2596 -264 C ATOM 3211 OG SER B 292 -131.672 -20.004 -42.905 1.00130.28 O ANISOU 3211 OG SER B 292 17661 14952 16889 991 2662 -443 O ATOM 3212 N GLY B 293 -130.610 -18.546 -46.079 1.00 82.58 N ANISOU 3212 N GLY B 293 11943 8519 10913 1178 3025 -270 N ATOM 3213 CA GLY B 293 -130.062 -17.236 -46.401 1.00 91.72 C ANISOU 3213 CA GLY B 293 13333 9435 12081 1123 3235 -332 C ATOM 3214 C GLY B 293 -129.312 -16.565 -45.268 1.00 66.36 C ANISOU 3214 C GLY B 293 10178 6128 8908 976 3255 -430 C ATOM 3215 O GLY B 293 -128.849 -15.437 -45.396 1.00 61.55 O ANISOU 3215 O GLY B 293 9766 5316 8305 902 3423 -498 O ATOM 3216 N LEU B 294 -129.208 -17.259 -44.144 1.00 71.17 N ANISOU 3216 N LEU B 294 10614 6884 9542 930 3085 -437 N ATOM 3217 CA LEU B 294 -128.495 -16.735 -42.994 1.00 81.23 C ANISOU 3217 CA LEU B 294 11916 8086 10860 787 3086 -523 C ATOM 3218 C LEU B 294 -127.105 -17.365 -42.876 1.00 94.60 C ANISOU 3218 C LEU B 294 13392 9855 12694 876 2977 -333 C ATOM 3219 O LEU B 294 -126.726 -18.225 -43.675 1.00104.94 O ANISOU 3219 O LEU B 294 14541 11287 14047 1020 2888 -151 O ATOM 3220 CB LEU B 294 -129.301 -16.975 -41.718 1.00 68.84 C ANISOU 3220 CB LEU B 294 10320 6622 9215 648 2991 -677 C ATOM 3221 CG LEU B 294 -130.709 -16.388 -41.726 1.00 70.31 C ANISOU 3221 CG LEU B 294 10718 6778 9220 519 3075 -883 C ATOM 3222 CD1 LEU B 294 -131.231 -16.281 -40.306 1.00 75.43 C ANISOU 3222 CD1 LEU B 294 11388 7505 9767 295 3008 -1074 C ATOM 3223 CD2 LEU B 294 -130.709 -15.031 -42.395 1.00 81.40 C ANISOU 3223 CD2 LEU B 294 12419 7940 10569 432 3278 -988 C ATOM 3224 N SER B 295 -126.347 -16.921 -41.879 1.00 68.48 N ANISOU 3224 N SER B 295 10093 6482 9445 764 2979 -388 N ATOM 3225 CA SER B 295 -125.027 -17.465 -41.612 1.00 59.03 C ANISOU 3225 CA SER B 295 8695 5364 8368 825 2871 -227 C ATOM 3226 C SER B 295 -125.126 -18.932 -41.226 1.00 55.50 C ANISOU 3226 C SER B 295 7972 5175 7939 901 2632 -112 C ATOM 3227 O SER B 295 -125.900 -19.291 -40.340 1.00 41.27 O ANISOU 3227 O SER B 295 6117 3460 6103 841 2552 -201 O ATOM 3228 CB SER B 295 -124.372 -16.675 -40.484 1.00 80.57 C ANISOU 3228 CB SER B 295 11494 7971 11149 672 2918 -332 C ATOM 3229 OG SER B 295 -125.336 -16.310 -39.511 1.00 82.33 O ANISOU 3229 OG SER B 295 11829 8160 11292 497 2926 -543 O ATOM 3230 N PRO B 296 -124.343 -19.792 -41.897 1.00 58.72 N ANISOU 3230 N PRO B 296 8211 5714 8385 1012 2516 75 N ATOM 3231 CA PRO B 296 -124.430 -21.218 -41.587 1.00 36.47 C ANISOU 3231 CA PRO B 296 5156 3142 5559 1049 2271 169 C ATOM 3232 C PRO B 296 -124.467 -21.436 -40.089 1.00 48.16 C ANISOU 3232 C PRO B 296 6538 4688 7073 966 2170 107 C ATOM 3233 O PRO B 296 -123.668 -20.827 -39.376 1.00 42.33 O ANISOU 3233 O PRO B 296 5824 3854 6406 901 2223 80 O ATOM 3234 CB PRO B 296 -123.135 -21.783 -42.174 1.00 32.95 C ANISOU 3234 CB PRO B 296 4596 2775 5148 1098 2186 331 C ATOM 3235 CG PRO B 296 -122.884 -20.898 -43.363 1.00 49.82 C ANISOU 3235 CG PRO B 296 6896 4747 7287 1151 2394 355 C ATOM 3236 CD PRO B 296 -123.315 -19.509 -42.917 1.00 57.94 C ANISOU 3236 CD PRO B 296 8142 5551 8323 1079 2601 195 C ATOM 3237 N LEU B 297 -125.405 -22.277 -39.641 1.00 61.43 N ANISOU 3237 N LEU B 297 8105 6529 8706 969 2035 87 N ATOM 3238 CA LEU B 297 -125.603 -22.639 -38.238 1.00 37.46 C ANISOU 3238 CA LEU B 297 4944 3593 5697 901 1931 43 C ATOM 3239 C LEU B 297 -125.073 -24.034 -37.981 1.00 35.29 C ANISOU 3239 C LEU B 297 4444 3546 5420 926 1666 181 C ATOM 3240 O LEU B 297 -125.337 -24.952 -38.770 1.00 35.54 O ANISOU 3240 O LEU B 297 4422 3697 5385 973 1549 246 O ATOM 3241 CB LEU B 297 -127.091 -22.620 -37.894 1.00 60.56 C ANISOU 3241 CB LEU B 297 7902 6565 8543 871 1973 -84 C ATOM 3242 CG LEU B 297 -127.421 -23.158 -36.497 1.00 74.18 C ANISOU 3242 CG LEU B 297 9446 8453 10287 808 1861 -109 C ATOM 3243 CD1 LEU B 297 -127.104 -22.099 -35.451 1.00 87.02 C ANISOU 3243 CD1 LEU B 297 11157 9936 11968 662 2019 -261 C ATOM 3244 CD2 LEU B 297 -128.877 -23.616 -36.381 1.00 52.57 C ANISOU 3244 CD2 LEU B 297 6659 5870 7445 808 1838 -167 C ATOM 3245 N TYR B 298 -124.347 -24.206 -36.879 1.00 24.83 N ANISOU 3245 N TYR B 298 3011 2271 4154 870 1574 206 N ATOM 3246 CA TYR B 298 -123.759 -25.517 -36.565 1.00 33.86 C ANISOU 3246 CA TYR B 298 3997 3614 5254 854 1320 301 C ATOM 3247 C TYR B 298 -124.173 -26.046 -35.206 1.00 22.19 C ANISOU 3247 C TYR B 298 2385 2274 3773 796 1181 282 C ATOM 3248 O TYR B 298 -124.375 -25.302 -34.258 1.00 45.05 O ANISOU 3248 O TYR B 298 5253 5112 6752 753 1278 228 O ATOM 3249 CB TYR B 298 -122.229 -25.488 -36.625 1.00 36.72 C ANISOU 3249 CB TYR B 298 4355 3929 5666 838 1320 394 C ATOM 3250 CG TYR B 298 -121.637 -25.251 -37.993 1.00 58.63 C ANISOU 3250 CG TYR B 298 7224 6597 8456 898 1468 483 C ATOM 3251 CD1 TYR B 298 -121.311 -26.313 -38.822 1.00 68.79 C ANISOU 3251 CD1 TYR B 298 8478 7943 9717 929 1459 635 C ATOM 3252 CD2 TYR B 298 -121.379 -23.965 -38.447 1.00 85.03 C ANISOU 3252 CD2 TYR B 298 10696 9780 11832 916 1628 417 C ATOM 3253 CE1 TYR B 298 -120.761 -26.102 -40.077 1.00 73.07 C ANISOU 3253 CE1 TYR B 298 9091 8406 10267 990 1603 730 C ATOM 3254 CE2 TYR B 298 -120.828 -23.746 -39.700 1.00 98.94 C ANISOU 3254 CE2 TYR B 298 12536 11451 13605 976 1776 515 C ATOM 3255 CZ TYR B 298 -120.521 -24.820 -40.509 1.00 89.75 C ANISOU 3255 CZ TYR B 298 11316 10366 12417 1018 1761 676 C ATOM 3256 OH TYR B 298 -119.975 -24.612 -41.753 1.00 99.60 O ANISOU 3256 OH TYR B 298 12632 11539 13671 1085 1914 784 O ATOM 3257 N SER B 299 -124.281 -27.358 -35.125 1.00 38.03 N ANISOU 3257 N SER B 299 4314 4422 5715 780 1015 353 N ATOM 3258 CA SER B 299 -124.730 -28.026 -33.923 1.00 22.98 C ANISOU 3258 CA SER B 299 2296 2657 3776 722 867 345 C ATOM 3259 C SER B 299 -123.644 -27.979 -32.856 1.00 23.87 C ANISOU 3259 C SER B 299 2361 2774 3936 659 804 382 C ATOM 3260 O SER B 299 -122.462 -28.076 -33.179 1.00 34.36 O ANISOU 3260 O SER B 299 3726 4024 5306 660 840 469 O ATOM 3261 CB SER B 299 -125.071 -29.479 -34.284 1.00 23.02 C ANISOU 3261 CB SER B 299 2288 2731 3727 723 790 451 C ATOM 3262 OG SER B 299 -125.475 -30.238 -33.158 1.00 44.81 O ANISOU 3262 OG SER B 299 4973 5605 6448 663 659 459 O ATOM 3263 N PRO B 300 -124.042 -27.819 -31.579 1.00 21.00 N ANISOU 3263 N PRO B 300 1903 2519 3556 599 717 324 N ATOM 3264 CA PRO B 300 -123.091 -27.887 -30.473 1.00 17.80 C ANISOU 3264 CA PRO B 300 1449 2129 3184 535 643 372 C ATOM 3265 C PRO B 300 -122.558 -29.303 -30.264 1.00 20.78 C ANISOU 3265 C PRO B 300 1845 2520 3528 512 556 500 C ATOM 3266 O PRO B 300 -121.513 -29.472 -29.633 1.00 35.89 O ANISOU 3266 O PRO B 300 3759 4411 5468 473 526 560 O ATOM 3267 CB PRO B 300 -123.914 -27.423 -29.265 1.00 28.64 C ANISOU 3267 CB PRO B 300 2690 3625 4567 460 607 324 C ATOM 3268 CG PRO B 300 -125.325 -27.628 -29.654 1.00 29.52 C ANISOU 3268 CG PRO B 300 2772 3816 4630 479 626 285 C ATOM 3269 CD PRO B 300 -125.378 -27.401 -31.126 1.00 28.89 C ANISOU 3269 CD PRO B 300 2811 3595 4570 581 767 271 C ATOM 3270 N PHE B 301 -123.256 -30.305 -30.776 1.00 25.03 N ANISOU 3270 N PHE B 301 2406 3099 4005 530 533 536 N ATOM 3271 CA PHE B 301 -122.722 -31.664 -30.736 1.00 27.89 C ANISOU 3271 CA PHE B 301 2800 3471 4326 502 496 645 C ATOM 3272 C PHE B 301 -122.469 -32.152 -32.138 1.00 29.36 C ANISOU 3272 C PHE B 301 3039 3613 4502 546 574 708 C ATOM 3273 O PHE B 301 -123.357 -32.091 -32.983 1.00 28.20 O ANISOU 3273 O PHE B 301 2907 3473 4335 593 610 682 O ATOM 3274 CB PHE B 301 -123.656 -32.624 -29.992 1.00 31.43 C ANISOU 3274 CB PHE B 301 3228 4014 4701 469 411 654 C ATOM 3275 CG PHE B 301 -123.728 -32.365 -28.520 1.00 28.41 C ANISOU 3275 CG PHE B 301 2795 3685 4313 417 335 630 C ATOM 3276 CD1 PHE B 301 -122.764 -32.860 -27.673 1.00 32.91 C ANISOU 3276 CD1 PHE B 301 3382 4240 4883 374 307 696 C ATOM 3277 CD2 PHE B 301 -124.735 -31.593 -27.992 1.00 37.64 C ANISOU 3277 CD2 PHE B 301 3894 4934 5473 407 299 543 C ATOM 3278 CE1 PHE B 301 -122.809 -32.595 -26.325 1.00 32.03 C ANISOU 3278 CE1 PHE B 301 3229 4178 4763 330 245 689 C ATOM 3279 CE2 PHE B 301 -124.783 -31.335 -26.644 1.00 39.70 C ANISOU 3279 CE2 PHE B 301 4099 5263 5721 348 231 534 C ATOM 3280 CZ PHE B 301 -123.822 -31.838 -25.810 1.00 28.14 C ANISOU 3280 CZ PHE B 301 2665 3770 4257 316 204 614 C ATOM 3281 N SER B 302 -121.249 -32.626 -32.379 1.00 23.79 N ANISOU 3281 N SER B 302 2358 2873 3806 530 603 793 N ATOM 3282 CA SER B 302 -120.827 -33.043 -33.716 1.00 25.55 C ANISOU 3282 CA SER B 302 2619 3070 4019 569 685 867 C ATOM 3283 C SER B 302 -121.278 -34.467 -34.118 1.00 19.85 C ANISOU 3283 C SER B 302 1909 2411 3221 562 660 925 C ATOM 3284 O SER B 302 -121.320 -34.798 -35.297 1.00 25.42 O ANISOU 3284 O SER B 302 2638 3113 3907 603 722 977 O ATOM 3285 CB SER B 302 -119.310 -32.891 -33.868 1.00 34.05 C ANISOU 3285 CB SER B 302 3706 4097 5136 559 736 935 C ATOM 3286 OG SER B 302 -118.597 -33.846 -33.092 1.00 51.49 O ANISOU 3286 OG SER B 302 5905 6344 7316 502 680 984 O ATOM 3287 N GLN B 303 -121.604 -35.310 -33.148 1.00 32.83 N ANISOU 3287 N GLN B 303 3539 4110 4824 511 581 921 N ATOM 3288 CA GLN B 303 -122.166 -36.621 -33.474 1.00 34.36 C ANISOU 3288 CA GLN B 303 3747 4357 4951 503 566 964 C ATOM 3289 C GLN B 303 -122.837 -37.299 -32.297 1.00 25.62 C ANISOU 3289 C GLN B 303 2628 3301 3805 457 490 943 C ATOM 3290 O GLN B 303 -122.438 -37.136 -31.152 1.00 39.15 O ANISOU 3290 O GLN B 303 4329 5014 5533 418 448 928 O ATOM 3291 CB GLN B 303 -121.117 -37.566 -34.066 1.00 27.36 C ANISOU 3291 CB GLN B 303 2879 3470 4046 495 604 1052 C ATOM 3292 CG GLN B 303 -120.058 -37.983 -33.109 1.00 25.25 C ANISOU 3292 CG GLN B 303 2610 3201 3785 443 575 1074 C ATOM 3293 CD GLN B 303 -119.186 -39.060 -33.685 1.00 47.32 C ANISOU 3293 CD GLN B 303 5419 6020 6540 440 569 1080 C ATOM 3294 OE1 GLN B 303 -117.965 -38.889 -33.814 1.00 51.23 O ANISOU 3294 OE1 GLN B 303 5915 6498 7053 441 584 1088 O ATOM 3295 NE2 GLN B 303 -119.802 -40.194 -34.038 1.00 39.46 N ANISOU 3295 NE2 GLN B 303 4433 5067 5493 438 548 1074 N ATOM 3296 N PHE B 304 -123.873 -38.063 -32.599 1.00 25.48 N ANISOU 3296 N PHE B 304 2616 3329 3738 465 479 950 N ATOM 3297 CA PHE B 304 -124.578 -38.782 -31.577 1.00 14.82 C ANISOU 3297 CA PHE B 304 1258 2026 2347 428 425 945 C ATOM 3298 C PHE B 304 -124.401 -40.271 -31.879 1.00 33.54 C ANISOU 3298 C PHE B 304 3653 4412 4677 408 440 1011 C ATOM 3299 O PHE B 304 -124.954 -40.784 -32.840 1.00 33.08 O ANISOU 3299 O PHE B 304 3604 4372 4592 435 467 1036 O ATOM 3300 CB PHE B 304 -126.050 -38.388 -31.591 1.00 18.79 C ANISOU 3300 CB PHE B 304 1740 2572 2828 454 401 895 C ATOM 3301 CG PHE B 304 -126.778 -38.775 -30.325 1.00 22.72 C ANISOU 3301 CG PHE B 304 2220 3122 3292 417 346 888 C ATOM 3302 CD1 PHE B 304 -127.331 -40.040 -30.180 1.00 12.77 C ANISOU 3302 CD1 PHE B 304 974 1894 1982 399 343 937 C ATOM 3303 CD2 PHE B 304 -126.870 -37.889 -29.276 1.00 25.28 C ANISOU 3303 CD2 PHE B 304 2509 3462 3633 401 303 842 C ATOM 3304 CE1 PHE B 304 -127.963 -40.403 -29.019 1.00 21.17 C ANISOU 3304 CE1 PHE B 304 2024 3003 3016 370 307 947 C ATOM 3305 CE2 PHE B 304 -127.508 -38.240 -28.117 1.00 14.46 C ANISOU 3305 CE2 PHE B 304 1120 2147 2226 369 260 855 C ATOM 3306 CZ PHE B 304 -128.061 -39.500 -27.991 1.00 37.58 C ANISOU 3306 CZ PHE B 304 4068 5103 5106 356 266 911 C ATOM 3307 N TYR B 305 -123.599 -40.950 -31.063 1.00 34.38 N ANISOU 3307 N TYR B 305 3768 4513 4781 366 419 1023 N ATOM 3308 CA TYR B 305 -123.287 -42.363 -31.242 1.00 16.21 C ANISOU 3308 CA TYR B 305 1487 2223 2447 349 401 1002 C ATOM 3309 C TYR B 305 -124.151 -43.139 -30.321 1.00 16.49 C ANISOU 3309 C TYR B 305 1523 2287 2454 324 365 988 C ATOM 3310 O TYR B 305 -124.191 -42.830 -29.137 1.00 34.56 O ANISOU 3310 O TYR B 305 3803 4578 4749 302 340 983 O ATOM 3311 CB TYR B 305 -121.857 -42.659 -30.820 1.00 30.65 C ANISOU 3311 CB TYR B 305 3328 4030 4290 325 388 983 C ATOM 3312 CG TYR B 305 -121.472 -44.088 -31.066 1.00 39.54 C ANISOU 3312 CG TYR B 305 4470 5167 5388 313 376 968 C ATOM 3313 CD1 TYR B 305 -121.752 -45.072 -30.133 1.00 39.69 C ANISOU 3313 CD1 TYR B 305 4497 5196 5388 285 343 945 C ATOM 3314 CD2 TYR B 305 -120.854 -44.458 -32.249 1.00 55.46 C ANISOU 3314 CD2 TYR B 305 6490 7184 7398 334 401 983 C ATOM 3315 CE1 TYR B 305 -121.415 -46.390 -30.364 1.00 35.08 C ANISOU 3315 CE1 TYR B 305 3925 4617 4788 276 336 935 C ATOM 3316 CE2 TYR B 305 -120.512 -45.768 -32.493 1.00 66.68 C ANISOU 3316 CE2 TYR B 305 7920 8618 8797 324 389 975 C ATOM 3317 CZ TYR B 305 -120.793 -46.732 -31.551 1.00 61.05 C ANISOU 3317 CZ TYR B 305 7215 7909 8072 295 357 949 C ATOM 3318 OH TYR B 305 -120.445 -48.041 -31.807 1.00 80.03 O ANISOU 3318 OH TYR B 305 9624 10322 10462 288 350 945 O ATOM 3319 N VAL B 306 -124.847 -44.140 -30.851 1.00 31.97 N ANISOU 3319 N VAL B 306 3492 4269 4387 329 365 987 N ATOM 3320 CA VAL B 306 -125.744 -44.975 -30.045 1.00 20.95 C ANISOU 3320 CA VAL B 306 2096 2897 2967 310 339 978 C ATOM 3321 C VAL B 306 -125.153 -46.367 -29.915 1.00 20.06 C ANISOU 3321 C VAL B 306 2001 2770 2850 288 325 956 C ATOM 3322 O VAL B 306 -124.791 -46.976 -30.922 1.00 27.14 O ANISOU 3322 O VAL B 306 2906 3662 3743 298 339 958 O ATOM 3323 CB VAL B 306 -127.147 -45.088 -30.683 1.00 19.30 C ANISOU 3323 CB VAL B 306 1879 2723 2733 334 351 999 C ATOM 3324 CG1 VAL B 306 -127.958 -46.124 -29.967 1.00 26.50 C ANISOU 3324 CG1 VAL B 306 2790 3653 3625 314 329 993 C ATOM 3325 CG2 VAL B 306 -127.862 -43.767 -30.615 1.00 36.33 C ANISOU 3325 CG2 VAL B 306 4013 4905 4887 358 362 1024 C ATOM 3326 N TYR B 307 -125.027 -46.853 -28.676 1.00 37.28 N ANISOU 3326 N TYR B 307 4186 4947 5032 261 301 942 N ATOM 3327 CA TYR B 307 -124.632 -48.243 -28.411 1.00 25.14 C ANISOU 3327 CA TYR B 307 2662 3397 3492 244 291 925 C ATOM 3328 C TYR B 307 -125.833 -49.186 -28.569 1.00 30.46 C ANISOU 3328 C TYR B 307 3333 4088 4153 247 291 934 C ATOM 3329 O TYR B 307 -126.508 -49.527 -27.591 1.00 49.16 O ANISOU 3329 O TYR B 307 5696 6465 6519 236 279 939 O ATOM 3330 CB TYR B 307 -124.045 -48.359 -27.006 1.00 22.41 C ANISOU 3330 CB TYR B 307 2320 3040 3156 222 273 913 C ATOM 3331 CG TYR B 307 -122.708 -47.696 -26.880 1.00 28.19 C ANISOU 3331 CG TYR B 307 3056 3754 3902 218 273 904 C ATOM 3332 CD1 TYR B 307 -121.550 -48.414 -27.088 1.00 36.00 C ANISOU 3332 CD1 TYR B 307 4057 4727 4893 214 274 891 C ATOM 3333 CD2 TYR B 307 -122.601 -46.353 -26.593 1.00 27.85 C ANISOU 3333 CD2 TYR B 307 3001 3710 3870 221 274 914 C ATOM 3334 CE1 TYR B 307 -120.328 -47.823 -27.003 1.00 28.94 C ANISOU 3334 CE1 TYR B 307 3166 3821 4011 212 277 887 C ATOM 3335 CE2 TYR B 307 -121.373 -45.748 -26.491 1.00 31.58 C ANISOU 3335 CE2 TYR B 307 3476 4163 4360 218 276 908 C ATOM 3336 CZ TYR B 307 -120.237 -46.486 -26.699 1.00 30.04 C ANISOU 3336 CZ TYR B 307 3295 3955 4164 214 278 894 C ATOM 3337 OH TYR B 307 -118.994 -45.897 -26.604 1.00 26.41 O ANISOU 3337 OH TYR B 307 2835 3480 3719 213 282 893 O ATOM 3338 N HIS B 308 -126.105 -49.589 -29.802 1.00 25.55 N ANISOU 3338 N HIS B 308 3349 2868 3489 -253 174 -261 N ATOM 3339 CA HIS B 308 -127.290 -50.404 -30.098 1.00 36.07 C ANISOU 3339 CA HIS B 308 4713 4152 4839 -240 257 -210 C ATOM 3340 C HIS B 308 -127.315 -51.706 -29.349 1.00 21.63 C ANISOU 3340 C HIS B 308 2879 2220 3121 -242 382 -192 C ATOM 3341 O HIS B 308 -128.323 -52.050 -28.754 1.00 43.88 O ANISOU 3341 O HIS B 308 5708 4990 5975 -196 426 -100 O ATOM 3342 CB HIS B 308 -127.400 -50.703 -31.584 1.00 34.61 C ANISOU 3342 CB HIS B 308 4555 3998 4599 -289 276 -282 C ATOM 3343 CG HIS B 308 -127.829 -49.527 -32.392 1.00 31.45 C ANISOU 3343 CG HIS B 308 4170 3692 4086 -276 167 -274 C ATOM 3344 ND1 HIS B 308 -126.976 -48.869 -33.260 1.00 33.22 N ANISOU 3344 ND1 HIS B 308 4390 3992 4242 -319 93 -364 N ATOM 3345 CD2 HIS B 308 -129.011 -48.879 -32.466 1.00 36.55 C ANISOU 3345 CD2 HIS B 308 4840 4371 4677 -224 117 -187 C ATOM 3346 CE1 HIS B 308 -127.620 -47.874 -33.831 1.00 51.77 C ANISOU 3346 CE1 HIS B 308 6756 6415 6499 -295 4 -333 C ATOM 3347 NE2 HIS B 308 -128.862 -47.855 -33.367 1.00 62.29 N ANISOU 3347 NE2 HIS B 308 8107 7724 7837 -236 16 -225 N ATOM 3348 N GLU B 309 -126.205 -52.432 -29.388 1.00 30.27 N ANISOU 3348 N GLU B 309 3956 3279 4267 -294 438 -282 N ATOM 3349 CA GLU B 309 -126.144 -53.736 -28.744 1.00 29.50 C ANISOU 3349 CA GLU B 309 3853 3081 4275 -302 560 -276 C ATOM 3350 C GLU B 309 -126.402 -53.579 -27.252 1.00 38.86 C ANISOU 3350 C GLU B 309 5020 4225 5521 -243 559 -180 C ATOM 3351 O GLU B 309 -127.248 -54.276 -26.702 1.00 27.86 O ANISOU 3351 O GLU B 309 3636 2765 4184 -212 635 -106 O ATOM 3352 CB GLU B 309 -124.809 -54.440 -29.010 1.00 25.21 C ANISOU 3352 CB GLU B 309 3293 2513 3773 -367 609 -393 C ATOM 3353 CG GLU B 309 -124.728 -55.858 -28.449 1.00 80.83 C ANISOU 3353 CG GLU B 309 10333 9452 10927 -380 740 -395 C ATOM 3354 CD GLU B 309 -123.411 -56.551 -28.767 1.00107.68 C ANISOU 3354 CD GLU B 309 13720 12830 14364 -444 786 -515 C ATOM 3355 OE1 GLU B 309 -122.349 -55.893 -28.682 1.00116.19 O ANISOU 3355 OE1 GLU B 309 14774 13965 15409 -453 713 -564 O ATOM 3356 OE2 GLU B 309 -123.436 -57.754 -29.110 1.00110.37 O ANISOU 3356 OE2 GLU B 309 14060 13142 14734 -460 873 -538 O ATOM 3357 N ASN B 310 -125.689 -52.653 -26.604 1.00 35.88 N ANISOU 3357 N ASN B 310 4615 3887 5130 -226 473 -178 N ATOM 3358 CA ASN B 310 -125.910 -52.420 -25.180 1.00 20.53 C ANISOU 3358 CA ASN B 310 2652 1908 3241 -169 465 -86 C ATOM 3359 C ASN B 310 -127.349 -52.082 -24.857 1.00 21.71 C ANISOU 3359 C ASN B 310 2820 2057 3371 -105 447 32 C ATOM 3360 O ASN B 310 -127.869 -52.542 -23.863 1.00 28.78 O ANISOU 3360 O ASN B 310 3712 2888 4335 -66 501 110 O ATOM 3361 CB ASN B 310 -125.015 -51.316 -24.637 1.00 23.66 C ANISOU 3361 CB ASN B 310 3018 2359 3615 -158 361 -99 C ATOM 3362 CG ASN B 310 -123.563 -51.675 -24.708 1.00 34.83 C ANISOU 3362 CG ASN B 310 4410 3763 5061 -212 384 -205 C ATOM 3363 OD1 ASN B 310 -123.225 -52.814 -24.997 1.00 39.79 O ANISOU 3363 OD1 ASN B 310 5044 4335 5739 -254 482 -262 O ATOM 3364 ND2 ASN B 310 -122.688 -50.710 -24.451 1.00 59.57 N ANISOU 3364 ND2 ASN B 310 7517 6950 8165 -211 293 -232 N ATOM 3365 N ILE B 311 -127.977 -51.248 -25.681 1.00 31.86 N ANISOU 3365 N ILE B 311 4127 3416 4562 -93 369 46 N ATOM 3366 CA ILE B 311 -129.363 -50.851 -25.442 1.00 28.98 C ANISOU 3366 CA ILE B 311 3784 3058 4170 -30 345 157 C ATOM 3367 C ILE B 311 -130.319 -52.042 -25.535 1.00 19.29 C ANISOU 3367 C ILE B 311 2581 1755 2991 -25 464 197 C ATOM 3368 O ILE B 311 -131.210 -52.205 -24.713 1.00 18.46 O ANISOU 3368 O ILE B 311 2482 1606 2924 29 492 296 O ATOM 3369 CB ILE B 311 -129.792 -49.696 -26.376 1.00 25.64 C ANISOU 3369 CB ILE B 311 3378 2732 3630 -21 234 156 C ATOM 3370 CG1 ILE B 311 -129.103 -48.405 -25.921 1.00 34.14 C ANISOU 3370 CG1 ILE B 311 4428 3875 4669 -3 111 153 C ATOM 3371 CG2 ILE B 311 -131.293 -49.489 -26.355 1.00 17.14 C ANISOU 3371 CG2 ILE B 311 2333 1657 2523 38 227 261 C ATOM 3372 CD1 ILE B 311 -129.255 -47.246 -26.860 1.00 22.53 C ANISOU 3372 CD1 ILE B 311 2970 2504 3086 -3 -3 133 C ATOM 3373 N ASP B 312 -130.115 -52.873 -26.541 1.00 19.51 N ANISOU 3373 N ASP B 312 2625 1768 3021 -82 533 120 N ATOM 3374 CA ASP B 312 -130.921 -54.058 -26.716 1.00 18.40 C ANISOU 3374 CA ASP B 312 2507 1555 2931 -84 651 147 C ATOM 3375 C ASP B 312 -130.751 -55.006 -25.509 1.00 35.04 C ANISOU 3375 C ASP B 312 4595 3565 5152 -72 744 180 C ATOM 3376 O ASP B 312 -131.720 -55.575 -25.010 1.00 47.34 O ANISOU 3376 O ASP B 312 6166 5065 6755 -34 810 263 O ATOM 3377 CB ASP B 312 -130.532 -54.748 -28.014 1.00 18.12 C ANISOU 3377 CB ASP B 312 2486 1521 2879 -153 703 44 C ATOM 3378 CG ASP B 312 -131.164 -54.110 -29.210 1.00 31.18 C ANISOU 3378 CG ASP B 312 4168 3247 4431 -155 644 38 C ATOM 3379 OD1 ASP B 312 -132.067 -53.275 -29.007 1.00 51.18 O ANISOU 3379 OD1 ASP B 312 6714 5819 6913 -99 577 124 O ATOM 3380 OD2 ASP B 312 -130.780 -54.446 -30.353 1.00 37.57 O ANISOU 3380 OD2 ASP B 312 4987 4075 5212 -212 664 -51 O ATOM 3381 N LEU B 313 -129.512 -55.162 -25.055 1.00 28.59 N ANISOU 3381 N LEU B 313 3749 2733 4381 -103 749 116 N ATOM 3382 CA LEU B 313 -129.182 -55.943 -23.887 1.00 19.08 C ANISOU 3382 CA LEU B 313 2524 1445 3282 -94 826 140 C ATOM 3383 C LEU B 313 -129.877 -55.397 -22.655 1.00 27.56 C ANISOU 3383 C LEU B 313 3589 2506 4375 -20 791 259 C ATOM 3384 O LEU B 313 -130.436 -56.161 -21.867 1.00 39.91 O ANISOU 3384 O LEU B 313 5155 3996 6015 8 872 325 O ATOM 3385 CB LEU B 313 -127.679 -55.944 -23.673 1.00 29.92 C ANISOU 3385 CB LEU B 313 3866 2821 4681 -136 813 49 C ATOM 3386 CG LEU B 313 -126.989 -57.279 -23.403 1.00 68.00 C ANISOU 3386 CG LEU B 313 8679 7559 9601 -177 931 -7 C ATOM 3387 CD1 LEU B 313 -127.647 -58.406 -24.189 1.00 73.05 C ANISOU 3387 CD1 LEU B 313 9345 8150 10261 -204 1034 -23 C ATOM 3388 CD2 LEU B 313 -125.496 -57.178 -23.720 1.00 71.24 C ANISOU 3388 CD2 LEU B 313 9068 7996 10004 -231 905 -122 C ATOM 3389 N VAL B 314 -129.868 -54.080 -22.486 1.00 21.41 N ANISOU 3389 N VAL B 314 2802 1803 3531 12 669 289 N ATOM 3390 CA VAL B 314 -130.537 -53.456 -21.349 1.00 19.52 C ANISOU 3390 CA VAL B 314 2555 1558 3304 84 624 401 C ATOM 3391 C VAL B 314 -132.067 -53.596 -21.426 1.00 23.20 C ANISOU 3391 C VAL B 314 3053 2008 3754 133 650 498 C ATOM 3392 O VAL B 314 -132.724 -53.858 -20.424 1.00 33.53 O ANISOU 3392 O VAL B 314 4360 3263 5118 182 686 588 O ATOM 3393 CB VAL B 314 -130.149 -51.969 -21.174 1.00 18.92 C ANISOU 3393 CB VAL B 314 2461 1567 3161 108 482 408 C ATOM 3394 CG1 VAL B 314 -131.002 -51.323 -20.107 1.00 21.30 C ANISOU 3394 CG1 VAL B 314 2758 1865 3470 185 434 528 C ATOM 3395 CG2 VAL B 314 -128.680 -51.828 -20.812 1.00 18.36 C ANISOU 3395 CG2 VAL B 314 2354 1501 3120 72 461 331 C ATOM 3396 N ARG B 315 -132.650 -53.423 -22.598 1.00 27.60 N ANISOU 3396 N ARG B 315 3641 2612 4236 120 632 481 N ATOM 3397 CA ARG B 315 -134.105 -53.440 -22.669 1.00 38.38 C ANISOU 3397 CA ARG B 315 5037 3968 5578 171 646 575 C ATOM 3398 C ARG B 315 -134.637 -54.817 -22.385 1.00 29.93 C ANISOU 3398 C ARG B 315 3978 2801 4593 170 784 605 C ATOM 3399 O ARG B 315 -135.639 -54.960 -21.693 1.00 42.97 O ANISOU 3399 O ARG B 315 5640 4414 6272 226 812 706 O ATOM 3400 CB ARG B 315 -134.617 -53.014 -24.038 1.00 35.02 C ANISOU 3400 CB ARG B 315 4643 3609 5054 157 604 548 C ATOM 3401 CG ARG B 315 -134.366 -51.575 -24.401 1.00 40.97 C ANISOU 3401 CG ARG B 315 5392 4463 5710 167 462 534 C ATOM 3402 CD ARG B 315 -133.995 -51.544 -25.851 1.00 40.11 C ANISOU 3402 CD ARG B 315 5299 4407 5534 109 449 438 C ATOM 3403 NE ARG B 315 -134.669 -50.485 -26.568 1.00 48.05 N ANISOU 3403 NE ARG B 315 6328 5496 6434 135 351 464 N ATOM 3404 CZ ARG B 315 -134.609 -50.333 -27.882 1.00 41.76 C ANISOU 3404 CZ ARG B 315 5550 4751 5565 95 330 397 C ATOM 3405 NH1 ARG B 315 -133.919 -51.189 -28.631 1.00 20.50 N ANISOU 3405 NH1 ARG B 315 2856 2035 2896 27 402 301 N ATOM 3406 NH2 ARG B 315 -135.246 -49.325 -28.441 1.00 53.24 N ANISOU 3406 NH2 ARG B 315 7025 6280 6923 125 238 428 N ATOM 3407 N GLN B 316 -133.982 -55.821 -22.966 1.00 34.48 N ANISOU 3407 N GLN B 316 4552 3339 5209 106 870 516 N ATOM 3408 CA GLN B 316 -134.397 -57.206 -22.825 1.00 29.08 C ANISOU 3408 CA GLN B 316 3878 2563 4608 96 1006 530 C ATOM 3409 C GLN B 316 -134.475 -57.483 -21.347 1.00 32.16 C ANISOU 3409 C GLN B 316 4248 2888 5084 139 1041 605 C ATOM 3410 O GLN B 316 -135.494 -57.920 -20.827 1.00 47.61 O ANISOU 3410 O GLN B 316 6219 4794 7077 183 1097 694 O ATOM 3411 CB GLN B 316 -133.365 -58.130 -23.467 1.00 36.90 C ANISOU 3411 CB GLN B 316 4859 3524 5636 18 1077 412 C ATOM 3412 CG GLN B 316 -133.887 -59.536 -23.777 1.00 44.19 C ANISOU 3412 CG GLN B 316 5800 4366 6625 -3 1213 410 C ATOM 3413 CD GLN B 316 -135.139 -59.505 -24.626 1.00 44.90 C ANISOU 3413 CD GLN B 316 5926 4475 6659 17 1222 455 C ATOM 3414 OE1 GLN B 316 -135.221 -58.753 -25.602 1.00 39.11 O ANISOU 3414 OE1 GLN B 316 5208 3818 5834 6 1147 425 O ATOM 3415 NE2 GLN B 316 -136.136 -60.305 -24.243 1.00 53.48 N ANISOU 3415 NE2 GLN B 316 7029 5492 7801 49 1312 532 N ATOM 3416 N MET B 317 -133.380 -57.183 -20.671 1.00 38.51 N ANISOU 3416 N MET B 317 5019 3696 5917 126 1005 569 N ATOM 3417 CA MET B 317 -133.268 -57.372 -19.241 1.00 40.58 C ANISOU 3417 CA MET B 317 5257 3900 6260 163 1030 631 C ATOM 3418 C MET B 317 -134.486 -56.822 -18.498 1.00 33.28 C ANISOU 3418 C MET B 317 4344 2977 5324 242 995 760 C ATOM 3419 O MET B 317 -135.065 -57.511 -17.661 1.00 36.89 O ANISOU 3419 O MET B 317 4802 3362 5853 274 1071 831 O ATOM 3420 CB MET B 317 -131.983 -56.717 -18.745 1.00 42.90 C ANISOU 3420 CB MET B 317 5517 4226 6558 147 960 580 C ATOM 3421 CG MET B 317 -131.391 -57.337 -17.498 1.00 41.16 C ANISOU 3421 CG MET B 317 5268 3931 6441 153 1021 594 C ATOM 3422 SD MET B 317 -129.598 -56.628 -17.171 1.00 96.16 S ANISOU 3422 SD MET B 317 12192 10939 13406 118 942 503 S ATOM 3423 CE MET B 317 -129.209 -57.561 -15.498 1.00166.86 C ANISOU 3423 CE MET B 317 21118 19784 22499 138 1039 548 C ATOM 3424 N ILE B 318 -134.876 -55.595 -18.803 1.00 22.79 N ANISOU 3424 N ILE B 318 3024 1731 3905 273 880 789 N ATOM 3425 CA ILE B 318 -135.985 -54.945 -18.104 1.00 23.61 C ANISOU 3425 CA ILE B 318 3137 1843 3991 351 832 908 C ATOM 3426 C ILE B 318 -137.355 -55.475 -18.551 1.00 35.12 C ANISOU 3426 C ILE B 318 4634 3275 5436 377 894 971 C ATOM 3427 O ILE B 318 -138.300 -55.534 -17.766 1.00 43.66 O ANISOU 3427 O ILE B 318 5723 4321 6544 437 912 1073 O ATOM 3428 CB ILE B 318 -135.973 -53.439 -18.325 1.00 26.68 C ANISOU 3428 CB ILE B 318 3525 2330 4285 376 685 918 C ATOM 3429 CG1 ILE B 318 -134.697 -52.817 -17.748 1.00 44.98 C ANISOU 3429 CG1 ILE B 318 5802 4673 6617 360 618 870 C ATOM 3430 CG2 ILE B 318 -137.195 -52.802 -17.704 1.00 39.03 C ANISOU 3430 CG2 ILE B 318 5102 3902 5824 457 637 1039 C ATOM 3431 CD1 ILE B 318 -134.384 -51.418 -18.315 1.00 31.89 C ANISOU 3431 CD1 ILE B 318 4140 3118 4858 361 477 840 C ATOM 3432 N TYR B 319 -137.450 -55.841 -19.821 1.00 31.73 N ANISOU 3432 N TYR B 319 4228 2864 4964 334 924 909 N ATOM 3433 CA TYR B 319 -138.653 -56.444 -20.370 1.00 24.32 C ANISOU 3433 CA TYR B 319 3325 1898 4016 351 993 956 C ATOM 3434 C TYR B 319 -138.922 -57.766 -19.666 1.00 33.37 C ANISOU 3434 C TYR B 319 4469 2939 5271 353 1127 991 C ATOM 3435 O TYR B 319 -140.015 -57.980 -19.137 1.00 51.11 O ANISOU 3435 O TYR B 319 6732 5149 7539 408 1163 1089 O ATOM 3436 CB TYR B 319 -138.453 -56.704 -21.852 1.00 25.27 C ANISOU 3436 CB TYR B 319 3465 2051 4084 291 1010 866 C ATOM 3437 CG TYR B 319 -139.639 -57.306 -22.536 1.00 28.66 C ANISOU 3437 CG TYR B 319 3932 2457 4501 304 1080 906 C ATOM 3438 CD1 TYR B 319 -140.742 -56.540 -22.829 1.00 41.33 C ANISOU 3438 CD1 TYR B 319 5566 4110 6028 357 1018 979 C ATOM 3439 CD2 TYR B 319 -139.650 -58.638 -22.904 1.00 50.82 C ANISOU 3439 CD2 TYR B 319 6745 5192 7372 263 1207 870 C ATOM 3440 CE1 TYR B 319 -141.835 -57.086 -23.457 1.00 41.80 C ANISOU 3440 CE1 TYR B 319 5661 4148 6075 371 1084 1018 C ATOM 3441 CE2 TYR B 319 -140.744 -59.190 -23.540 1.00 45.08 C ANISOU 3441 CE2 TYR B 319 6052 4442 6636 276 1273 908 C ATOM 3442 CZ TYR B 319 -141.830 -58.403 -23.811 1.00 27.87 C ANISOU 3442 CZ TYR B 319 3901 2311 4377 330 1212 983 C ATOM 3443 OH TYR B 319 -142.925 -58.922 -24.446 1.00 52.26 O ANISOU 3443 OH TYR B 319 7024 5378 7453 345 1276 1023 O ATOM 3444 N ASP B 320 -137.916 -58.642 -19.665 1.00 27.62 N ANISOU 3444 N ASP B 320 3721 2164 4610 295 1200 909 N ATOM 3445 CA ASP B 320 -137.994 -59.942 -18.996 1.00 42.36 C ANISOU 3445 CA ASP B 320 5581 3929 6585 290 1329 928 C ATOM 3446 C ASP B 320 -138.385 -59.787 -17.537 1.00 41.29 C ANISOU 3446 C ASP B 320 5424 3775 6489 351 1314 1016 C ATOM 3447 O ASP B 320 -139.464 -60.248 -17.115 1.00 35.60 O ANISOU 3447 O ASP B 320 4709 3040 5777 391 1355 1081 O ATOM 3448 CB ASP B 320 -136.677 -60.717 -19.100 1.00 35.72 C ANISOU 3448 CB ASP B 320 4716 3053 5804 220 1386 820 C ATOM 3449 CG ASP B 320 -136.301 -61.036 -20.531 1.00 48.69 C ANISOU 3449 CG ASP B 320 6373 4723 7405 154 1403 717 C ATOM 3450 OD1 ASP B 320 -135.150 -61.465 -20.775 1.00 59.22 O ANISOU 3450 OD1 ASP B 320 7687 6045 8767 95 1428 617 O ATOM 3451 OD2 ASP B 320 -137.159 -60.843 -21.417 1.00 54.34 O ANISOU 3451 OD2 ASP B 320 7118 5472 8057 163 1392 735 O ATOM 3452 N THR B 321 -137.511 -59.141 -16.772 1.00 28.25 N ANISOU 3452 N THR B 321 3743 2139 4850 355 1249 1007 N ATOM 3453 CA THR B 321 -137.793 -58.862 -15.368 1.00 48.10 C ANISOU 3453 CA THR B 321 6230 4660 7387 409 1215 1076 C ATOM 3454 C THR B 321 -139.254 -58.487 -15.188 1.00 45.71 C ANISOU 3454 C THR B 321 5950 4380 7040 473 1187 1175 C ATOM 3455 O THR B 321 -139.973 -59.086 -14.394 1.00 36.94 O ANISOU 3455 O THR B 321 4829 3245 5961 503 1235 1222 O ATOM 3456 CB THR B 321 -136.934 -57.697 -14.823 1.00 33.98 C ANISOU 3456 CB THR B 321 4417 2910 5583 421 1107 1074 C ATOM 3457 OG1 THR B 321 -135.587 -58.137 -14.652 1.00 49.35 O ANISOU 3457 OG1 THR B 321 6336 4834 7583 368 1137 988 O ATOM 3458 CG2 THR B 321 -137.453 -57.246 -13.484 1.00 42.74 C ANISOU 3458 CG2 THR B 321 5504 4037 6697 480 1058 1153 C ATOM 3459 N GLU B 322 -139.703 -57.485 -15.928 1.00 30.38 N ANISOU 3459 N GLU B 322 4037 2487 5019 496 1107 1205 N ATOM 3460 CA GLU B 322 -141.049 -57.021 -15.703 1.00 29.90 C ANISOU 3460 CA GLU B 322 3994 2458 4906 560 1067 1294 C ATOM 3461 C GLU B 322 -142.183 -57.957 -16.153 1.00 27.55 C ANISOU 3461 C GLU B 322 3724 2130 4613 567 1159 1321 C ATOM 3462 O GLU B 322 -143.210 -58.009 -15.513 1.00 33.70 O ANISOU 3462 O GLU B 322 4505 2913 5387 615 1160 1388 O ATOM 3463 CB GLU B 322 -141.224 -55.632 -16.264 1.00 26.34 C ANISOU 3463 CB GLU B 322 3562 2080 4364 588 944 1319 C ATOM 3464 CG GLU B 322 -141.472 -54.642 -15.173 1.00 26.44 C ANISOU 3464 CG GLU B 322 3553 2142 4351 640 840 1372 C ATOM 3465 CD GLU B 322 -142.759 -53.905 -15.389 1.00 45.75 C ANISOU 3465 CD GLU B 322 6026 4643 6712 694 772 1436 C ATOM 3466 OE1 GLU B 322 -143.283 -53.925 -16.526 1.00 51.84 O ANISOU 3466 OE1 GLU B 322 6835 5429 7433 691 784 1437 O ATOM 3467 OE2 GLU B 322 -143.259 -53.313 -14.421 1.00 51.87 O ANISOU 3467 OE2 GLU B 322 6788 5450 7471 736 707 1480 O ATOM 3468 N MET B 323 -142.008 -58.672 -17.254 1.00 27.41 N ANISOU 3468 N MET B 323 3727 2084 4602 519 1233 1266 N ATOM 3469 CA MET B 323 -143.025 -59.615 -17.678 1.00 29.12 C ANISOU 3469 CA MET B 323 3966 2270 4828 523 1324 1286 C ATOM 3470 C MET B 323 -143.255 -60.640 -16.585 1.00 47.48 C ANISOU 3470 C MET B 323 6263 4548 7231 534 1404 1302 C ATOM 3471 O MET B 323 -144.387 -61.018 -16.299 1.00 62.70 O ANISOU 3471 O MET B 323 8199 6465 9158 573 1439 1362 O ATOM 3472 CB MET B 323 -142.582 -60.313 -18.958 1.00 56.32 C ANISOU 3472 CB MET B 323 7429 5690 8279 458 1396 1206 C ATOM 3473 CG MET B 323 -142.535 -59.378 -20.153 1.00 63.20 C ANISOU 3473 CG MET B 323 8337 6608 9069 449 1328 1196 C ATOM 3474 SD MET B 323 -144.100 -58.191 -20.166 1.00 97.94 S ANISOU 3474 SD MET B 323 12771 11077 13365 540 1229 1315 S ATOM 3475 CE MET B 323 -143.260 -56.577 -19.394 1.00 49.63 C ANISOU 3475 CE MET B 323 6622 5033 7202 567 1064 1320 C ATOM 3476 N ARG B 324 -142.162 -61.082 -15.976 1.00 33.96 N ANISOU 3476 N ARG B 324 4514 2807 5582 499 1430 1247 N ATOM 3477 CA ARG B 324 -142.228 -61.940 -14.826 1.00 33.53 C ANISOU 3477 CA ARG B 324 4428 2714 5598 510 1492 1262 C ATOM 3478 C ARG B 324 -142.899 -61.268 -13.625 1.00 44.46 C ANISOU 3478 C ARG B 324 5801 4122 6970 573 1430 1348 C ATOM 3479 O ARG B 324 -143.895 -61.769 -13.110 1.00 53.39 O ANISOU 3479 O ARG B 324 6933 5235 8117 608 1474 1403 O ATOM 3480 CB ARG B 324 -140.839 -62.417 -14.438 1.00 28.86 C ANISOU 3480 CB ARG B 324 3802 2098 5067 461 1519 1182 C ATOM 3481 CG ARG B 324 -140.834 -63.142 -13.111 1.00 38.43 C ANISOU 3481 CG ARG B 324 4977 3276 6346 478 1569 1203 C ATOM 3482 CD ARG B 324 -139.533 -62.909 -12.411 1.00 44.49 C ANISOU 3482 CD ARG B 324 5711 4048 7147 455 1536 1157 C ATOM 3483 NE ARG B 324 -138.451 -62.931 -13.384 1.00 51.06 N ANISOU 3483 NE ARG B 324 6546 4883 7971 396 1536 1063 N ATOM 3484 CZ ARG B 324 -137.206 -62.569 -13.112 1.00 63.96 C ANISOU 3484 CZ ARG B 324 8156 6528 9619 368 1496 1009 C ATOM 3485 NH1 ARG B 324 -136.913 -62.162 -11.886 1.00 44.83 N ANISOU 3485 NH1 ARG B 324 5703 4112 7217 395 1455 1044 N ATOM 3486 NH2 ARG B 324 -136.269 -62.599 -14.061 1.00 73.20 N ANISOU 3486 NH2 ARG B 324 9330 7704 10778 312 1496 920 N ATOM 3487 N VAL B 325 -142.350 -60.146 -13.174 1.00 50.53 N ANISOU 3487 N VAL B 325 6556 4931 7710 587 1327 1357 N ATOM 3488 CA VAL B 325 -142.868 -59.454 -11.994 1.00 41.25 C ANISOU 3488 CA VAL B 325 5367 3784 6523 641 1258 1427 C ATOM 3489 C VAL B 325 -144.326 -59.036 -12.121 1.00 47.24 C ANISOU 3489 C VAL B 325 6155 4572 7223 695 1227 1503 C ATOM 3490 O VAL B 325 -145.122 -59.218 -11.190 1.00 58.51 O ANISOU 3490 O VAL B 325 7574 5992 8665 733 1239 1560 O ATOM 3491 CB VAL B 325 -142.054 -58.194 -11.678 1.00 52.69 C ANISOU 3491 CB VAL B 325 6799 5281 7939 645 1141 1418 C ATOM 3492 CG1 VAL B 325 -142.888 -57.230 -10.853 1.00 43.77 C ANISOU 3492 CG1 VAL B 325 5668 4197 6764 705 1049 1491 C ATOM 3493 CG2 VAL B 325 -140.762 -58.563 -10.952 1.00 76.92 C ANISOU 3493 CG2 VAL B 325 9828 8322 11076 610 1164 1364 C ATOM 3494 N ASN B 326 -144.668 -58.481 -13.278 1.00 46.68 N ANISOU 3494 N ASN B 326 7358 4079 6299 958 1781 2196 N ATOM 3495 CA ASN B 326 -145.961 -57.834 -13.489 1.00 44.89 C ANISOU 3495 CA ASN B 326 7197 3947 5912 1067 1700 2323 C ATOM 3496 C ASN B 326 -146.505 -58.154 -14.881 1.00 52.96 C ANISOU 3496 C ASN B 326 8258 4984 6880 1015 1790 2323 C ATOM 3497 O ASN B 326 -146.415 -57.324 -15.795 1.00 43.78 O ANISOU 3497 O ASN B 326 7110 3961 5562 974 1683 2274 O ATOM 3498 CB ASN B 326 -145.772 -56.331 -13.320 1.00 46.04 C ANISOU 3498 CB ASN B 326 7344 4277 5872 1101 1460 2304 C ATOM 3499 CG ASN B 326 -147.027 -55.543 -13.569 1.00 51.86 C ANISOU 3499 CG ASN B 326 8132 5132 6441 1193 1355 2403 C ATOM 3500 OD1 ASN B 326 -146.979 -54.316 -13.669 1.00 53.59 O ANISOU 3500 OD1 ASN B 326 8346 5513 6502 1201 1165 2370 O ATOM 3501 ND2 ASN B 326 -148.162 -56.232 -13.661 1.00 46.39 N ANISOU 3501 ND2 ASN B 326 7481 4360 5785 1258 1476 2517 N ATOM 3502 N PRO B 327 -147.078 -59.365 -15.050 1.00 46.90 N ANISOU 3502 N PRO B 327 7504 4075 6242 1016 1986 2373 N ATOM 3503 CA PRO B 327 -147.302 -59.895 -16.399 1.00 46.95 C ANISOU 3503 CA PRO B 327 7530 4070 6239 936 2099 2335 C ATOM 3504 C PRO B 327 -148.444 -59.212 -17.148 1.00 54.27 C ANISOU 3504 C PRO B 327 8521 5111 6988 1000 2023 2425 C ATOM 3505 O PRO B 327 -148.529 -59.299 -18.382 1.00 51.45 O ANISOU 3505 O PRO B 327 8179 4793 6576 928 2059 2378 O ATOM 3506 CB PRO B 327 -147.589 -61.377 -16.165 1.00 48.84 C ANISOU 3506 CB PRO B 327 7758 4120 6678 928 2322 2362 C ATOM 3507 CG PRO B 327 -147.260 -61.621 -14.710 1.00 65.74 C ANISOU 3507 CG PRO B 327 9860 6174 8943 982 2324 2386 C ATOM 3508 CD PRO B 327 -147.484 -60.322 -14.021 1.00 48.90 C ANISOU 3508 CD PRO B 327 7749 4172 6660 1084 2114 2454 C ATOM 3509 N ALA B 328 -149.304 -58.516 -16.417 1.00 53.40 N ANISOU 3509 N ALA B 328 8441 5060 6787 1128 1911 2542 N ATOM 3510 CA ALA B 328 -150.279 -57.650 -17.072 1.00 71.59 C ANISOU 3510 CA ALA B 328 10792 7500 8909 1179 1800 2602 C ATOM 3511 C ALA B 328 -149.591 -56.581 -17.941 1.00 46.25 C ANISOU 3511 C ALA B 328 7564 4457 5551 1093 1642 2484 C ATOM 3512 O ALA B 328 -150.114 -56.190 -18.973 1.00 46.05 O ANISOU 3512 O ALA B 328 7565 4522 5412 1072 1605 2482 O ATOM 3513 CB ALA B 328 -151.217 -57.004 -16.043 1.00 76.04 C ANISOU 3513 CB ALA B 328 11378 8110 9403 1322 1689 2724 C ATOM 3514 N ALA B 329 -148.412 -56.126 -17.530 1.00 44.48 N ANISOU 3514 N ALA B 329 7293 4274 5332 1040 1552 2383 N ATOM 3515 CA ALA B 329 -147.705 -55.059 -18.255 1.00 42.21 C ANISOU 3515 CA ALA B 329 6983 4150 4905 961 1394 2268 C ATOM 3516 C ALA B 329 -147.431 -55.400 -19.723 1.00 43.19 C ANISOU 3516 C ALA B 329 7108 4292 5009 846 1470 2184 C ATOM 3517 O ALA B 329 -147.007 -54.547 -20.493 1.00 53.91 O ANISOU 3517 O ALA B 329 8448 5791 6243 780 1347 2095 O ATOM 3518 CB ALA B 329 -146.415 -54.699 -17.547 1.00 40.56 C ANISOU 3518 CB ALA B 329 6723 3957 4730 919 1315 2172 C ATOM 3519 N ALA B 330 -147.675 -56.645 -20.111 1.00 42.55 N ANISOU 3519 N ALA B 330 7041 4071 5054 818 1669 2205 N ATOM 3520 CA ALA B 330 -147.477 -57.051 -21.498 1.00 48.84 C ANISOU 3520 CA ALA B 330 7836 4881 5841 710 1747 2123 C ATOM 3521 C ALA B 330 -148.541 -56.455 -22.417 1.00 48.18 C ANISOU 3521 C ALA B 330 7793 4907 5606 742 1675 2180 C ATOM 3522 O ALA B 330 -148.463 -56.604 -23.632 1.00 55.43 O ANISOU 3522 O ALA B 330 8709 5864 6489 659 1707 2117 O ATOM 3523 CB ALA B 330 -147.482 -58.566 -21.609 1.00 65.04 C ANISOU 3523 CB ALA B 330 9882 6751 8078 668 1977 2120 C ATOM 3524 N ALA B 331 -149.527 -55.779 -21.831 1.00 44.73 N ANISOU 3524 N ALA B 331 7387 4522 5085 859 1576 2293 N ATOM 3525 CA ALA B 331 -150.693 -55.313 -22.572 1.00 44.14 C ANISOU 3525 CA ALA B 331 7350 4531 4890 899 1524 2359 C ATOM 3526 C ALA B 331 -150.339 -54.130 -23.455 1.00 63.09 C ANISOU 3526 C ALA B 331 9722 7113 7137 826 1348 2258 C ATOM 3527 O ALA B 331 -150.824 -53.995 -24.579 1.00 57.95 O ANISOU 3527 O ALA B 331 9083 6523 6415 788 1343 2247 O ATOM 3528 CB ALA B 331 -151.823 -54.951 -21.620 1.00 45.87 C ANISOU 3528 CB ALA B 331 7603 4750 5075 1038 1471 2496 C ATOM 3529 N HIS B 332 -149.484 -53.264 -22.939 1.00 66.62 N ANISOU 3529 N HIS B 332 10125 7648 7540 803 1203 2179 N ATOM 3530 CA HIS B 332 -148.995 -52.147 -23.724 1.00 56.13 C ANISOU 3530 CA HIS B 332 8753 6488 6087 719 1037 2066 C ATOM 3531 C HIS B 332 -147.488 -52.238 -23.960 1.00 47.06 C ANISOU 3531 C HIS B 332 7552 5355 4975 609 1039 1924 C ATOM 3532 O HIS B 332 -146.976 -51.712 -24.939 1.00 48.70 O ANISOU 3532 O HIS B 332 7717 5675 5111 514 963 1818 O ATOM 3533 CB HIS B 332 -149.386 -50.829 -23.064 1.00 75.72 C ANISOU 3533 CB HIS B 332 11229 9081 8462 801 865 2087 C ATOM 3534 CG HIS B 332 -150.855 -50.715 -22.789 1.00 86.04 C ANISOU 3534 CG HIS B 332 12591 10373 9728 930 882 2226 C ATOM 3535 ND1 HIS B 332 -151.518 -51.574 -21.940 1.00 80.77 N ANISOU 3535 ND1 HIS B 332 11957 9578 9154 1003 976 2346 N ATOM 3536 CD2 HIS B 332 -151.785 -49.849 -23.255 1.00 87.04 C ANISOU 3536 CD2 HIS B 332 12742 10594 9734 999 821 2261 C ATOM 3537 CE1 HIS B 332 -152.794 -51.238 -21.889 1.00 90.31 C ANISOU 3537 CE1 HIS B 332 13209 10810 10294 1114 971 2452 C ATOM 3538 NE2 HIS B 332 -152.983 -50.197 -22.678 1.00 88.17 N ANISOU 3538 NE2 HIS B 332 12933 10672 9893 1113 878 2403 N ATOM 3539 N THR B 333 -146.776 -52.911 -23.071 1.00 36.63 N ANISOU 3539 N THR B 333 6226 3920 3771 618 1126 1919 N ATOM 3540 CA THR B 333 -145.381 -53.222 -23.346 1.00 34.93 C ANISOU 3540 CA THR B 333 5966 3694 3612 507 1165 1785 C ATOM 3541 C THR B 333 -145.261 -54.599 -23.996 1.00 47.94 C ANISOU 3541 C THR B 333 7623 5208 5386 442 1376 1764 C ATOM 3542 O THR B 333 -145.085 -55.608 -23.309 1.00 64.78 O ANISOU 3542 O THR B 333 9760 7182 7671 453 1523 1788 O ATOM 3543 CB THR B 333 -144.539 -53.188 -22.071 1.00 34.45 C ANISOU 3543 CB THR B 333 5884 3583 3624 530 1143 1766 C ATOM 3544 OG1 THR B 333 -144.815 -51.981 -21.359 1.00 47.36 O ANISOU 3544 OG1 THR B 333 7509 5330 5155 601 952 1796 O ATOM 3545 CG2 THR B 333 -143.058 -53.231 -22.421 1.00 39.38 C ANISOU 3545 CG2 THR B 333 6455 4231 4276 407 1146 1609 C ATOM 3546 N THR B 334 -145.348 -54.634 -25.325 1.00 38.82 N ANISOU 3546 N THR B 334 6459 4116 4174 368 1387 1708 N ATOM 3547 CA THR B 334 -145.444 -55.896 -26.063 1.00 38.07 C ANISOU 3547 CA THR B 334 6371 3908 4186 309 1576 1690 C ATOM 3548 C THR B 334 -144.120 -56.325 -26.670 1.00 34.34 C ANISOU 3548 C THR B 334 5836 3437 3773 172 1621 1520 C ATOM 3549 O THR B 334 -144.024 -57.404 -27.247 1.00 36.99 O ANISOU 3549 O THR B 334 6160 3680 4213 107 1771 1473 O ATOM 3550 CB THR B 334 -146.460 -55.780 -27.206 1.00 36.61 C ANISOU 3550 CB THR B 334 6214 3786 3910 315 1568 1736 C ATOM 3551 OG1 THR B 334 -146.079 -54.695 -28.064 1.00 54.37 O ANISOU 3551 OG1 THR B 334 8420 6219 6020 254 1400 1648 O ATOM 3552 CG2 THR B 334 -147.823 -55.483 -26.648 1.00 52.07 C ANISOU 3552 CG2 THR B 334 8231 5730 5822 446 1541 1897 C ATOM 3553 N ALA B 335 -143.113 -55.465 -26.563 1.00 43.53 N ANISOU 3553 N ALA B 335 6952 4714 4872 126 1485 1420 N ATOM 3554 CA ALA B 335 -141.802 -55.744 -27.147 1.00 36.63 C ANISOU 3554 CA ALA B 335 6009 3866 4042 -2 1505 1246 C ATOM 3555 C ALA B 335 -140.757 -55.120 -26.274 1.00 32.26 C ANISOU 3555 C ALA B 335 5422 3351 3485 -14 1411 1178 C ATOM 3556 O ALA B 335 -141.022 -54.092 -25.669 1.00 48.44 O ANISOU 3556 O ALA B 335 7487 5483 5434 62 1270 1243 O ATOM 3557 CB ALA B 335 -141.706 -55.168 -28.534 1.00 39.54 C ANISOU 3557 CB ALA B 335 6337 4394 4293 -64 1406 1171 C ATOM 3558 N PRO B 336 -139.569 -55.752 -26.189 1.00 39.91 N ANISOU 3558 N PRO B 336 6336 4260 4567 -111 1484 1038 N ATOM 3559 CA PRO B 336 -138.424 -55.190 -25.457 1.00 26.78 C ANISOU 3559 CA PRO B 336 4633 2637 2904 -141 1399 948 C ATOM 3560 C PRO B 336 -138.035 -53.864 -26.035 1.00 24.92 C ANISOU 3560 C PRO B 336 4363 2606 2500 -152 1204 889 C ATOM 3561 O PRO B 336 -137.446 -53.037 -25.359 1.00 39.63 O ANISOU 3561 O PRO B 336 6210 4537 4312 -136 1089 861 O ATOM 3562 CB PRO B 336 -137.309 -56.216 -25.689 1.00 31.96 C ANISOU 3562 CB PRO B 336 5219 3213 3713 -264 1513 775 C ATOM 3563 CG PRO B 336 -137.774 -57.060 -26.837 1.00 50.88 C ANISOU 3563 CG PRO B 336 7610 5581 6143 -304 1611 755 C ATOM 3564 CD PRO B 336 -139.270 -57.088 -26.730 1.00 35.08 C ANISOU 3564 CD PRO B 336 5692 3536 4103 -197 1650 948 C ATOM 3565 N GLY B 337 -138.376 -53.655 -27.293 1.00 30.14 N ANISOU 3565 N GLY B 337 4999 3369 3083 -177 1163 868 N ATOM 3566 CA GLY B 337 -138.067 -52.398 -27.951 1.00 39.45 C ANISOU 3566 CA GLY B 337 6106 4752 4130 -183 975 810 C ATOM 3567 C GLY B 337 -138.901 -51.233 -27.463 1.00 33.97 C ANISOU 3567 C GLY B 337 5431 4154 3323 -91 830 919 C ATOM 3568 O GLY B 337 -138.640 -50.083 -27.807 1.00 52.89 O ANISOU 3568 O GLY B 337 7797 6676 5622 -74 701 861 O ATOM 3569 N GLU B 338 -139.907 -51.510 -26.656 1.00 25.01 N ANISOU 3569 N GLU B 338 4382 2916 2203 -8 880 1064 N ATOM 3570 CA GLU B 338 -140.768 -50.449 -26.170 1.00 26.02 C ANISOU 3570 CA GLU B 338 4524 3125 2237 76 737 1156 C ATOM 3571 C GLU B 338 -140.395 -49.956 -24.767 1.00 37.44 C ANISOU 3571 C GLU B 338 5975 4559 3692 131 660 1174 C ATOM 3572 O GLU B 338 -140.996 -49.017 -24.239 1.00 29.04 O ANISOU 3572 O GLU B 338 4912 3560 2561 198 532 1229 O ATOM 3573 CB GLU B 338 -142.223 -50.893 -26.248 1.00 27.60 C ANISOU 3573 CB GLU B 338 4804 3246 2435 150 811 1300 C ATOM 3574 CG GLU B 338 -142.598 -51.209 -27.650 1.00 27.92 C ANISOU 3574 CG GLU B 338 4858 3304 2447 116 882 1279 C ATOM 3575 CD GLU B 338 -144.051 -51.461 -27.803 1.00 43.24 C ANISOU 3575 CD GLU B 338 6874 5189 4366 197 939 1416 C ATOM 3576 OE1 GLU B 338 -144.737 -51.477 -26.766 1.00 65.08 O ANISOU 3576 OE1 GLU B 338 9680 7895 7153 282 932 1526 O ATOM 3577 OE2 GLU B 338 -144.501 -51.651 -28.954 1.00 58.03 O ANISOU 3577 OE2 GLU B 338 8765 7080 6206 179 991 1411 O ATOM 3578 N ILE B 339 -139.373 -50.574 -24.190 1.00 30.44 N ANISOU 3578 N ILE B 339 5094 3581 2893 101 744 1115 N ATOM 3579 CA ILE B 339 -138.891 -50.207 -22.871 1.00 24.50 C ANISOU 3579 CA ILE B 339 4347 2806 2158 150 681 1124 C ATOM 3580 C ILE B 339 -138.201 -48.846 -22.815 1.00 23.32 C ANISOU 3580 C ILE B 339 4104 2838 1916 123 480 1024 C ATOM 3581 O ILE B 339 -137.230 -48.614 -23.533 1.00 37.57 O ANISOU 3581 O ILE B 339 5829 4734 3711 38 451 887 O ATOM 3582 CB ILE B 339 -137.899 -51.251 -22.359 1.00 40.99 C ANISOU 3582 CB ILE B 339 6450 4740 4385 96 835 1066 C ATOM 3583 CG1 ILE B 339 -138.624 -52.579 -22.043 1.00 26.46 C ANISOU 3583 CG1 ILE B 339 4663 2699 2693 131 1035 1171 C ATOM 3584 CG2 ILE B 339 -137.142 -50.696 -21.159 1.00 39.65 C ANISOU 3584 CG2 ILE B 339 6270 4579 4216 126 742 1042 C ATOM 3585 CD1 ILE B 339 -139.596 -52.475 -20.913 1.00 28.14 C ANISOU 3585 CD1 ILE B 339 4921 2850 2922 271 1010 1332 C ATOM 3586 N ASP B 340 -138.692 -47.951 -21.956 1.00 24.93 N ANISOU 3586 N ASP B 340 4297 3097 2077 194 344 1083 N ATOM 3587 CA ASP B 340 -137.978 -46.704 -21.644 1.00 22.68 C ANISOU 3587 CA ASP B 340 3919 2952 1746 173 181 982 C ATOM 3588 C ASP B 340 -136.880 -46.947 -20.625 1.00 30.40 C ANISOU 3588 C ASP B 340 4890 3882 2778 171 182 932 C ATOM 3589 O ASP B 340 -137.125 -46.992 -19.418 1.00 47.29 O ANISOU 3589 O ASP B 340 7076 5947 4944 254 163 1011 O ATOM 3590 CB ASP B 340 -138.930 -45.615 -21.141 1.00 26.13 C ANISOU 3590 CB ASP B 340 4380 3434 2113 269 70 1043 C ATOM 3591 CG ASP B 340 -138.222 -44.508 -20.344 1.00 34.96 C ANISOU 3591 CG ASP B 340 5434 4631 3218 279 -59 958 C ATOM 3592 OD1 ASP B 340 -136.978 -44.362 -20.404 1.00 34.16 O ANISOU 3592 OD1 ASP B 340 5262 4575 3142 214 -78 834 O ATOM 3593 OD2 ASP B 340 -138.935 -43.752 -19.649 1.00 36.91 O ANISOU 3593 OD2 ASP B 340 5698 4894 3431 358 -135 1010 O ATOM 3594 N PHE B 341 -135.664 -47.083 -21.129 1.00 23.95 N ANISOU 3594 N PHE B 341 4021 3100 1976 89 208 791 N ATOM 3595 CA PHE B 341 -134.501 -47.352 -20.316 1.00 18.22 C ANISOU 3595 CA PHE B 341 3320 2311 1292 70 224 711 C ATOM 3596 C PHE B 341 -133.801 -46.068 -19.854 1.00 29.80 C ANISOU 3596 C PHE B 341 4645 3941 2738 69 49 608 C ATOM 3597 O PHE B 341 -132.602 -46.086 -19.596 1.00 43.31 O ANISOU 3597 O PHE B 341 6327 5650 4478 25 35 478 O ATOM 3598 CB PHE B 341 -133.525 -48.154 -21.150 1.00 20.44 C ANISOU 3598 CB PHE B 341 3607 2539 1619 -46 346 577 C ATOM 3599 CG PHE B 341 -133.127 -47.459 -22.415 1.00 26.94 C ANISOU 3599 CG PHE B 341 4281 3533 2424 -85 263 455 C ATOM 3600 CD1 PHE B 341 -131.985 -46.675 -22.462 1.00 29.68 C ANISOU 3600 CD1 PHE B 341 4526 3957 2794 -106 160 298 C ATOM 3601 CD2 PHE B 341 -133.925 -47.548 -23.545 1.00 28.49 C ANISOU 3601 CD2 PHE B 341 4466 3763 2595 -82 297 501 C ATOM 3602 CE1 PHE B 341 -131.628 -46.017 -23.615 1.00 19.30 C ANISOU 3602 CE1 PHE B 341 3175 2675 1484 -133 113 203 C ATOM 3603 CE2 PHE B 341 -133.576 -46.899 -24.691 1.00 23.40 C ANISOU 3603 CE2 PHE B 341 3786 3179 1925 -100 247 394 C ATOM 3604 CZ PHE B 341 -132.423 -46.127 -24.730 1.00 31.28 C ANISOU 3604 CZ PHE B 341 4721 4205 2960 -127 156 251 C ATOM 3605 N LEU B 342 -134.517 -44.953 -19.747 1.00 17.17 N ANISOU 3605 N LEU B 342 3000 2430 1094 114 -60 645 N ATOM 3606 CA LEU B 342 -133.875 -43.731 -19.249 1.00 30.83 C ANISOU 3606 CA LEU B 342 4660 4236 2819 125 -175 541 C ATOM 3607 C LEU B 342 -134.593 -43.158 -18.054 1.00 17.58 C ANISOU 3607 C LEU B 342 3005 2548 1128 200 -256 632 C ATOM 3608 O LEU B 342 -133.969 -42.701 -17.097 1.00 30.38 O ANISOU 3608 O LEU B 342 4580 4183 2780 209 -320 581 O ATOM 3609 CB LEU B 342 -133.767 -42.658 -20.344 1.00 16.04 C ANISOU 3609 CB LEU B 342 2741 2435 918 104 -211 451 C ATOM 3610 CG LEU B 342 -132.904 -43.085 -21.512 1.00 14.84 C ANISOU 3610 CG LEU B 342 2552 2284 802 45 -149 342 C ATOM 3611 CD1 LEU B 342 -133.100 -42.188 -22.704 1.00 27.64 C ANISOU 3611 CD1 LEU B 342 4142 3957 2401 39 -169 308 C ATOM 3612 CD2 LEU B 342 -131.469 -43.144 -21.072 1.00 20.39 C ANISOU 3612 CD2 LEU B 342 3195 2962 1589 8 -163 214 C ATOM 3613 N THR B 343 -135.917 -43.162 -18.130 1.00 25.41 N ANISOU 3613 N THR B 343 4067 3511 2079 259 -250 760 N ATOM 3614 CA THR B 343 -136.740 -42.619 -17.060 1.00 21.39 C ANISOU 3614 CA THR B 343 3582 2989 1555 347 -321 846 C ATOM 3615 C THR B 343 -137.721 -43.694 -16.590 1.00 32.44 C ANISOU 3615 C THR B 343 5060 4277 2989 407 -258 1013 C ATOM 3616 O THR B 343 -138.530 -43.476 -15.684 1.00 32.06 O ANISOU 3616 O THR B 343 5040 4201 2941 495 -300 1105 O ATOM 3617 CB THR B 343 -137.468 -41.348 -17.512 1.00 24.06 C ANISOU 3617 CB THR B 343 3927 3397 1818 384 -378 829 C ATOM 3618 OG1 THR B 343 -138.178 -41.620 -18.729 1.00 27.27 O ANISOU 3618 OG1 THR B 343 4379 3801 2180 376 -318 867 O ATOM 3619 CG2 THR B 343 -136.457 -40.218 -17.742 1.00 20.00 C ANISOU 3619 CG2 THR B 343 3334 2955 1311 331 -432 677 C ATOM 3620 N PHE B 344 -137.635 -44.854 -17.237 1.00 21.95 N ANISOU 3620 N PHE B 344 3764 2875 1702 359 -145 1046 N ATOM 3621 CA PHE B 344 -138.233 -46.072 -16.732 1.00 30.02 C ANISOU 3621 CA PHE B 344 4894 3728 2783 449 -24 1182 C ATOM 3622 C PHE B 344 -139.738 -45.964 -16.546 1.00 39.60 C ANISOU 3622 C PHE B 344 6148 4919 3978 529 -35 1313 C ATOM 3623 O PHE B 344 -140.334 -46.601 -15.681 1.00 37.74 O ANISOU 3623 O PHE B 344 5972 4568 3802 633 25 1430 O ATOM 3624 CB PHE B 344 -137.549 -46.443 -15.433 1.00 26.62 C ANISOU 3624 CB PHE B 344 4478 3208 2429 509 -20 1192 C ATOM 3625 CG PHE B 344 -136.090 -46.263 -15.488 1.00 21.80 C ANISOU 3625 CG PHE B 344 3821 2645 1817 431 -50 1046 C ATOM 3626 CD1 PHE B 344 -135.480 -45.249 -14.784 1.00 24.96 C ANISOU 3626 CD1 PHE B 344 4122 3159 2204 414 -200 960 C ATOM 3627 CD2 PHE B 344 -135.323 -47.078 -16.299 1.00 32.42 C ANISOU 3627 CD2 PHE B 344 5214 3922 3180 355 82 979 C ATOM 3628 CE1 PHE B 344 -134.124 -45.080 -14.847 1.00 28.93 C ANISOU 3628 CE1 PHE B 344 4574 3711 2707 343 -227 809 C ATOM 3629 CE2 PHE B 344 -133.962 -46.916 -16.371 1.00 24.10 C ANISOU 3629 CE2 PHE B 344 4133 2910 2115 272 51 824 C ATOM 3630 CZ PHE B 344 -133.358 -45.914 -15.645 1.00 34.59 C ANISOU 3630 CZ PHE B 344 5362 4359 3424 276 -114 736 C ATOM 3631 N LEU B 345 -140.351 -45.155 -17.386 1.00 29.48 N ANISOU 3631 N LEU B 345 4858 3738 2604 516 -82 1291 N ATOM 3632 CA LEU B 345 -141.777 -45.124 -17.435 1.00 27.67 C ANISOU 3632 CA LEU B 345 4694 3485 2335 609 -60 1409 C ATOM 3633 C LEU B 345 -142.231 -46.118 -18.482 1.00 28.96 C ANISOU 3633 C LEU B 345 4907 3580 2515 579 74 1458 C ATOM 3634 O LEU B 345 -141.583 -46.273 -19.511 1.00 33.30 O ANISOU 3634 O LEU B 345 5436 4164 3054 488 113 1371 O ATOM 3635 CB LEU B 345 -142.230 -43.726 -17.806 1.00 42.78 C ANISOU 3635 CB LEU B 345 6593 5525 4138 642 -155 1361 C ATOM 3636 CG LEU B 345 -141.643 -42.674 -16.879 1.00 36.85 C ANISOU 3636 CG LEU B 345 5780 4844 3375 652 -274 1286 C ATOM 3637 CD1 LEU B 345 -142.268 -41.315 -17.173 1.00 43.54 C ANISOU 3637 CD1 LEU B 345 6623 5791 4130 693 -347 1255 C ATOM 3638 CD2 LEU B 345 -141.884 -43.070 -15.443 1.00 28.23 C ANISOU 3638 CD2 LEU B 345 4698 3681 2346 724 -292 1377 C ATOM 3639 N ALA B 346 -143.347 -46.789 -18.218 1.00 30.06 N ANISOU 3639 N ALA B 346 5110 3626 2687 657 150 1593 N ATOM 3640 CA ALA B 346 -143.979 -47.623 -19.225 1.00 50.69 C ANISOU 3640 CA ALA B 346 7772 6179 5309 642 280 1646 C ATOM 3641 C ALA B 346 -144.835 -46.728 -20.096 1.00 35.16 C ANISOU 3641 C ALA B 346 5824 4316 3217 681 236 1647 C ATOM 3642 O ALA B 346 -145.190 -45.625 -19.708 1.00 31.78 O ANISOU 3642 O ALA B 346 5385 3974 2716 741 127 1640 O ATOM 3643 CB ALA B 346 -144.847 -48.722 -18.573 1.00 37.54 C ANISOU 3643 CB ALA B 346 6177 4357 3729 750 422 1795 C ATOM 3644 N VAL B 347 -145.185 -47.223 -21.268 1.00 39.00 N ANISOU 3644 N VAL B 347 6341 4789 3690 645 328 1654 N ATOM 3645 CA VAL B 347 -146.036 -46.463 -22.160 1.00 41.50 C ANISOU 3645 CA VAL B 347 6679 5190 3899 682 297 1661 C ATOM 3646 C VAL B 347 -147.281 -45.926 -21.443 1.00 34.22 C ANISOU 3646 C VAL B 347 5794 4278 2929 812 252 1771 C ATOM 3647 O VAL B 347 -147.644 -44.769 -21.627 1.00 60.48 O ANISOU 3647 O VAL B 347 9109 7706 6165 848 159 1741 O ATOM 3648 CB VAL B 347 -146.387 -47.297 -23.400 1.00 40.91 C ANISOU 3648 CB VAL B 347 6638 5073 3833 639 422 1680 C ATOM 3649 CG1 VAL B 347 -147.506 -46.646 -24.181 1.00 52.32 C ANISOU 3649 CG1 VAL B 347 8118 6582 5179 699 401 1720 C ATOM 3650 CG2 VAL B 347 -145.130 -47.482 -24.268 1.00 33.33 C ANISOU 3650 CG2 VAL B 347 5627 4147 2891 510 437 1543 C ATOM 3651 N ASP B 348 -147.948 -46.679 -20.596 1.00 65.48 N ANISOU 3651 N ASP B 348 9793 8130 6958 881 324 1893 N ATOM 3652 CA ASP B 348 -149.175 -46.172 -19.976 1.00 67.04 C ANISOU 3652 CA ASP B 348 10024 8330 7118 1011 293 2006 C ATOM 3653 C ASP B 348 -148.914 -44.992 -19.090 1.00 55.79 C ANISOU 3653 C ASP B 348 8556 7007 5633 1046 144 1953 C ATOM 3654 O ASP B 348 -149.809 -44.248 -18.763 1.00 38.55 O ANISOU 3654 O ASP B 348 6389 4879 3379 1137 92 2006 O ATOM 3655 CB ASP B 348 -149.891 -47.265 -19.189 1.00 83.79 C ANISOU 3655 CB ASP B 348 12176 10311 9348 1070 384 2126 C ATOM 3656 CG ASP B 348 -150.432 -48.360 -20.084 1.00111.59 C ANISOU 3656 CG ASP B 348 15751 13726 12922 1075 544 2213 C ATOM 3657 OD1 ASP B 348 -149.636 -49.235 -20.519 1.00120.81 O ANISOU 3657 OD1 ASP B 348 16914 14794 14195 996 647 2191 O ATOM 3658 OD2 ASP B 348 -151.650 -48.345 -20.362 1.00118.61 O ANISOU 3658 OD2 ASP B 348 16684 14629 13752 1156 573 2302 O ATOM 3659 N GLY B 349 -147.668 -44.823 -18.699 1.00 54.98 N ANISOU 3659 N GLY B 349 8398 6929 5564 972 80 1847 N ATOM 3660 CA GLY B 349 -147.270 -43.681 -17.908 1.00 58.30 C ANISOU 3660 CA GLY B 349 8770 7439 5941 995 -53 1785 C ATOM 3661 C GLY B 349 -146.684 -44.089 -16.597 1.00 51.77 C ANISOU 3661 C GLY B 349 7919 6553 5200 1009 -79 1801 C ATOM 3662 O GLY B 349 -146.097 -43.290 -15.909 1.00 55.65 O ANISOU 3662 O GLY B 349 8357 7109 5680 993 -182 1721 O ATOM 3663 N ASP B 350 -146.849 -45.357 -16.286 1.00 45.80 N ANISOU 3663 N ASP B 350 7199 5666 4538 1038 19 1902 N ATOM 3664 CA ASP B 350 -146.575 -45.936 -14.995 1.00 54.13 C ANISOU 3664 CA ASP B 350 8233 6645 5690 1063 2 1930 C ATOM 3665 C ASP B 350 -145.168 -46.489 -14.893 1.00 48.60 C ANISOU 3665 C ASP B 350 7497 5880 5089 955 34 1851 C ATOM 3666 O ASP B 350 -144.785 -47.262 -15.719 1.00 59.88 O ANISOU 3666 O ASP B 350 8945 7257 6552 889 141 1834 O ATOM 3667 CB ASP B 350 -147.538 -47.110 -14.854 1.00 84.38 C ANISOU 3667 CB ASP B 350 12117 10359 9584 1165 90 2084 C ATOM 3668 CG ASP B 350 -147.675 -47.907 -16.150 1.00 99.69 C ANISOU 3668 CG ASP B 350 14072 12365 11441 1286 24 2160 C ATOM 3669 OD1 ASP B 350 -147.517 -47.339 -17.234 1.00 93.92 O ANISOU 3669 OD1 ASP B 350 13303 11755 10628 1290 -99 2089 O ATOM 3670 OD2 ASP B 350 -147.946 -49.114 -16.098 1.00101.59 O ANISOU 3670 OD2 ASP B 350 14362 12535 11702 1377 100 2289 O ATOM 3671 N PRO B 351 -144.412 -46.148 -13.864 1.00 38.35 N ANISOU 3671 N PRO B 351 6148 4584 3838 948 -47 1803 N ATOM 3672 CA PRO B 351 -143.074 -46.687 -13.699 1.00 31.99 C ANISOU 3672 CA PRO B 351 5319 3726 3109 898 -2 1730 C ATOM 3673 C PRO B 351 -143.027 -48.174 -13.485 1.00 44.79 C ANISOU 3673 C PRO B 351 6999 5166 4853 951 201 1816 C ATOM 3674 O PRO B 351 -143.697 -48.677 -12.629 1.00 67.92 O ANISOU 3674 O PRO B 351 9960 8000 7845 1051 264 1934 O ATOM 3675 CB PRO B 351 -142.612 -46.009 -12.443 1.00 34.78 C ANISOU 3675 CB PRO B 351 5617 4111 3487 927 -127 1700 C ATOM 3676 CG PRO B 351 -143.760 -45.767 -11.738 1.00 33.45 C ANISOU 3676 CG PRO B 351 5466 3945 3298 1018 -178 1802 C ATOM 3677 CD PRO B 351 -144.762 -45.343 -12.707 1.00 52.21 C ANISOU 3677 CD PRO B 351 7885 6388 5564 1039 -153 1833 C ATOM 3678 N TYR B 352 -142.206 -48.863 -14.248 1.00 40.70 N ANISOU 3678 N TYR B 352 6488 4595 4382 871 312 1751 N ATOM 3679 CA TYR B 352 -142.108 -50.313 -14.201 1.00 52.33 C ANISOU 3679 CA TYR B 352 7998 5879 6007 881 527 1807 C ATOM 3680 C TYR B 352 -142.083 -50.800 -12.754 1.00 34.30 C ANISOU 3680 C TYR B 352 5703 3475 3853 967 556 1874 C ATOM 3681 O TYR B 352 -141.495 -50.157 -11.898 1.00 33.51 O ANISOU 3681 O TYR B 352 5560 3429 3743 985 424 1830 O ATOM 3682 CB TYR B 352 -140.850 -50.760 -14.941 1.00 53.88 C ANISOU 3682 CB TYR B 352 8180 6043 6249 758 614 1688 C ATOM 3683 CG TYR B 352 -140.831 -50.302 -16.371 1.00 47.30 C ANISOU 3683 CG TYR B 352 7349 5333 5291 670 584 1613 C ATOM 3684 CD1 TYR B 352 -141.786 -50.762 -17.270 1.00 45.68 C ANISOU 3684 CD1 TYR B 352 7183 5104 5070 670 679 1673 C ATOM 3685 CD2 TYR B 352 -139.863 -49.405 -16.835 1.00 42.85 C ANISOU 3685 CD2 TYR B 352 6737 4912 4631 584 456 1476 C ATOM 3686 CE1 TYR B 352 -141.783 -50.338 -18.592 1.00 56.19 C ANISOU 3686 CE1 TYR B 352 8505 6550 6296 588 644 1601 C ATOM 3687 CE2 TYR B 352 -139.853 -48.986 -18.162 1.00 27.12 C ANISOU 3687 CE2 TYR B 352 4727 3036 2541 499 426 1401 C ATOM 3688 CZ TYR B 352 -140.818 -49.450 -19.026 1.00 28.25 C ANISOU 3688 CZ TYR B 352 4910 3152 2673 502 516 1465 C ATOM 3689 OH TYR B 352 -140.838 -49.063 -20.333 1.00 50.43 O ANISOU 3689 OH TYR B 352 7692 6071 5399 419 483 1393 O ATOM 3690 N GLN B 353 -142.729 -51.925 -12.481 1.00 36.18 N ANISOU 3690 N GLN B 353 5971 3557 4221 1017 725 1975 N ATOM 3691 CA GLN B 353 -142.797 -52.472 -11.126 1.00 37.48 C ANISOU 3691 CA GLN B 353 6117 3599 4523 1098 765 2041 C ATOM 3692 C GLN B 353 -141.543 -53.282 -10.789 1.00 43.73 C ANISOU 3692 C GLN B 353 6865 4257 5494 1023 872 1956 C ATOM 3693 O GLN B 353 -141.233 -53.504 -9.622 1.00 55.39 O ANISOU 3693 O GLN B 353 8305 5659 7081 1068 861 1966 O ATOM 3694 CB GLN B 353 -144.058 -53.312 -10.959 1.00 39.93 C ANISOU 3694 CB GLN B 353 6470 3803 4899 1180 900 2179 C ATOM 3695 CG GLN B 353 -145.096 -52.656 -10.058 1.00 59.18 C ANISOU 3695 CG GLN B 353 8921 6308 7259 1308 776 2280 C ATOM 3696 CD GLN B 353 -146.497 -53.271 -10.169 1.00 43.65 C ANISOU 3696 CD GLN B 353 7008 4274 5305 1388 891 2418 C ATOM 3697 OE1 GLN B 353 -146.857 -53.871 -11.179 1.00 44.05 O ANISOU 3697 OE1 GLN B 353 7092 4279 5364 1348 1021 2435 O ATOM 3698 NE2 GLN B 353 -147.294 -53.100 -9.123 1.00 77.62 N ANISOU 3698 NE2 GLN B 353 11315 8573 9603 1504 839 2515 N ATOM 3699 N GLY B 354 -140.812 -53.696 -11.820 1.00 45.91 N ANISOU 3699 N GLY B 354 7137 4506 5800 898 972 1859 N ATOM 3700 CA GLY B 354 -139.595 -54.473 -11.652 1.00 36.95 C ANISOU 3700 CA GLY B 354 5949 3246 4846 794 1084 1748 C ATOM 3701 C GLY B 354 -138.318 -53.648 -11.575 1.00 32.32 C ANISOU 3701 C GLY B 354 5326 2747 4207 731 951 1622 C ATOM 3702 O GLY B 354 -137.227 -54.191 -11.514 1.00 31.97 O ANISOU 3702 O GLY B 354 5230 2610 4307 625 1032 1504 O ATOM 3703 N ILE B 355 -138.439 -52.331 -11.571 1.00 31.42 N ANISOU 3703 N ILE B 355 5228 2817 3893 785 743 1629 N ATOM 3704 CA ILE B 355 -137.253 -51.512 -11.392 1.00 29.36 C ANISOU 3704 CA ILE B 355 4933 2647 3575 740 606 1512 C ATOM 3705 C ILE B 355 -137.331 -50.672 -10.135 1.00 29.50 C ANISOU 3705 C ILE B 355 4917 2743 3550 846 418 1542 C ATOM 3706 O ILE B 355 -138.396 -50.281 -9.699 1.00 59.81 O ANISOU 3706 O ILE B 355 8765 6639 7320 941 341 1638 O ATOM 3707 CB ILE B 355 -136.968 -50.646 -12.614 1.00 30.10 C ANISOU 3707 CB ILE B 355 5047 2917 3474 665 515 1429 C ATOM 3708 CG1 ILE B 355 -136.936 -51.523 -13.861 1.00 41.14 C ANISOU 3708 CG1 ILE B 355 6472 4242 4918 554 705 1393 C ATOM 3709 CG2 ILE B 355 -135.643 -49.911 -12.445 1.00 54.22 C ANISOU 3709 CG2 ILE B 355 8071 6057 6472 609 390 1294 C ATOM 3710 CD1 ILE B 355 -136.384 -50.826 -15.063 1.00 60.94 C ANISOU 3710 CD1 ILE B 355 8986 6906 7263 456 636 1278 C ATOM 3711 N GLN B 356 -136.196 -50.461 -9.510 1.00 35.09 N ANISOU 3711 N GLN B 356 5577 3439 4315 822 354 1450 N ATOM 3712 CA GLN B 356 -136.138 -49.571 -8.384 1.00 30.59 C ANISOU 3712 CA GLN B 356 4961 2970 3694 904 158 1449 C ATOM 3713 C GLN B 356 -135.050 -48.605 -8.778 1.00 30.90 C ANISOU 3713 C GLN B 356 4973 3161 3607 833 12 1305 C ATOM 3714 O GLN B 356 -133.892 -48.999 -8.873 1.00 25.08 O ANISOU 3714 O GLN B 356 4236 2336 2957 765 71 1207 O ATOM 3715 CB GLN B 356 -135.761 -50.324 -7.105 1.00 31.64 C ANISOU 3715 CB GLN B 356 5045 2935 4041 948 217 1462 C ATOM 3716 CG GLN B 356 -135.166 -49.403 -6.055 1.00 52.95 C ANISOU 3716 CG GLN B 356 7678 5739 6701 992 13 1401 C ATOM 3717 CD GLN B 356 -134.662 -50.122 -4.823 1.00 42.52 C ANISOU 3717 CD GLN B 356 6297 4260 5600 1024 65 1390 C ATOM 3718 OE1 GLN B 356 -135.189 -51.157 -4.448 1.00 51.35 O ANISOU 3718 OE1 GLN B 356 7419 5220 6872 1049 217 1465 O ATOM 3719 NE2 GLN B 356 -133.633 -49.561 -4.180 1.00 40.31 N ANISOU 3719 NE2 GLN B 356 5950 4033 5333 1018 -68 1282 N ATOM 3720 N VAL B 357 -135.434 -47.355 -9.052 1.00 31.13 N ANISOU 3720 N VAL B 357 4970 3407 3452 823 -161 1273 N ATOM 3721 CA VAL B 357 -134.500 -46.350 -9.560 1.00 28.36 C ANISOU 3721 CA VAL B 357 4562 3234 2978 728 -292 1114 C ATOM 3722 C VAL B 357 -133.705 -45.720 -8.429 1.00 25.09 C ANISOU 3722 C VAL B 357 4057 2884 2590 738 -431 1028 C ATOM 3723 O VAL B 357 -134.215 -45.544 -7.330 1.00 43.06 O ANISOU 3723 O VAL B 357 6293 5149 4920 810 -484 1101 O ATOM 3724 CB VAL B 357 -135.242 -45.223 -10.283 1.00 43.79 C ANISOU 3724 CB VAL B 357 6463 5377 4798 672 -380 1095 C ATOM 3725 CG1 VAL B 357 -134.258 -44.345 -11.039 1.00 46.19 C ANISOU 3725 CG1 VAL B 357 6680 5844 5027 543 -445 920 C ATOM 3726 CG2 VAL B 357 -136.281 -45.793 -11.220 1.00 23.99 C ANISOU 3726 CG2 VAL B 357 4039 2811 2266 685 -265 1195 C ATOM 3727 N LEU B 358 -132.456 -45.380 -8.697 1.00 27.75 N ANISOU 3727 N LEU B 358 4361 3293 2891 653 -492 860 N ATOM 3728 CA LEU B 358 -131.610 -44.759 -7.692 1.00 30.92 C ANISOU 3728 CA LEU B 358 4658 3769 3322 639 -615 747 C ATOM 3729 C LEU B 358 -131.315 -43.320 -8.092 1.00 39.40 C ANISOU 3729 C LEU B 358 5592 5071 4307 515 -672 616 C ATOM 3730 O LEU B 358 -130.634 -43.085 -9.094 1.00 47.26 O ANISOU 3730 O LEU B 358 6558 6134 5265 408 -646 490 O ATOM 3731 CB LEU B 358 -130.308 -45.542 -7.528 1.00 18.45 C ANISOU 3731 CB LEU B 358 3131 2044 1834 610 -637 631 C ATOM 3732 CG LEU B 358 -130.392 -46.956 -6.945 1.00 39.16 C ANISOU 3732 CG LEU B 358 5715 4432 4730 603 -440 673 C ATOM 3733 CD1 LEU B 358 -128.997 -47.532 -6.698 1.00 38.17 C ANISOU 3733 CD1 LEU B 358 5460 4247 4797 442 -396 450 C ATOM 3734 CD2 LEU B 358 -131.194 -46.957 -5.666 1.00 53.96 C ANISOU 3734 CD2 LEU B 358 7607 6241 6654 781 -477 847 C ATOM 3735 N GLY B 359 -131.832 -42.364 -7.317 1.00 30.75 N ANISOU 3735 N GLY B 359 4404 4068 3213 514 -717 661 N ATOM 3736 CA GLY B 359 -131.652 -40.951 -7.613 1.00 35.96 C ANISOU 3736 CA GLY B 359 5038 4832 3794 467 -753 537 C ATOM 3737 C GLY B 359 -130.324 -40.350 -7.168 1.00 41.34 C ANISOU 3737 C GLY B 359 5662 5530 4515 411 -779 362 C ATOM 3738 O GLY B 359 -129.317 -41.049 -7.022 1.00 29.56 O ANISOU 3738 O GLY B 359 4137 3999 3093 365 -762 286 O ATOM 3739 N PRO B 360 -130.299 -39.032 -6.949 1.00 43.02 N ANISOU 3739 N PRO B 360 5866 5784 4697 415 -813 300 N ATOM 3740 CA PRO B 360 -129.015 -38.476 -6.508 1.00 50.02 C ANISOU 3740 CA PRO B 360 6705 6653 5648 368 -818 160 C ATOM 3741 C PRO B 360 -128.690 -38.924 -5.094 1.00 61.25 C ANISOU 3741 C PRO B 360 8097 8045 7130 400 -859 165 C ATOM 3742 O PRO B 360 -127.516 -39.092 -4.759 1.00 79.25 O ANISOU 3742 O PRO B 360 10340 10282 9490 354 -847 61 O ATOM 3743 CB PRO B 360 -129.241 -36.966 -6.575 1.00 60.96 C ANISOU 3743 CB PRO B 360 8096 8078 6987 384 -838 132 C ATOM 3744 CG PRO B 360 -130.337 -36.807 -7.599 1.00 77.74 C ANISOU 3744 CG PRO B 360 10265 10241 9030 401 -826 208 C ATOM 3745 CD PRO B 360 -131.243 -37.985 -7.364 1.00 66.58 C ANISOU 3745 CD PRO B 360 8882 8816 7598 448 -831 340 C ATOM 3746 N LEU B 361 -129.718 -39.126 -4.277 1.00 52.18 N ANISOU 3746 N LEU B 361 6959 6909 5957 484 -901 297 N ATOM 3747 CA LEU B 361 -129.509 -39.636 -2.933 1.00 50.06 C ANISOU 3747 CA LEU B 361 6652 6608 5759 527 -936 328 C ATOM 3748 C LEU B 361 -128.653 -40.908 -2.972 1.00 60.36 C ANISOU 3748 C LEU B 361 7926 7847 7162 491 -904 294 C ATOM 3749 O LEU B 361 -127.910 -41.191 -2.031 1.00 70.56 O ANISOU 3749 O LEU B 361 9172 9101 8537 487 -927 236 O ATOM 3750 CB LEU B 361 -130.850 -39.932 -2.259 1.00 63.49 C ANISOU 3750 CB LEU B 361 8367 8306 7452 632 -962 522 C ATOM 3751 CG LEU B 361 -131.884 -38.812 -2.137 1.00 84.32 C ANISOU 3751 CG LEU B 361 11038 11003 9995 679 -1004 572 C ATOM 3752 CD1 LEU B 361 -133.287 -39.399 -2.029 1.00 90.18 C ANISOU 3752 CD1 LEU B 361 11819 11707 10738 764 -1004 772 C ATOM 3753 CD2 LEU B 361 -131.584 -37.893 -0.957 1.00 80.12 C ANISOU 3753 CD2 LEU B 361 10476 10506 9461 699 -1062 510 C ATOM 3754 N ASP B 362 -128.749 -41.662 -4.070 1.00 52.34 N ANISOU 3754 N ASP B 362 6935 6812 6140 462 -852 324 N ATOM 3755 CA ASP B 362 -128.132 -42.989 -4.167 1.00 36.08 C ANISOU 3755 CA ASP B 362 4932 4608 4168 490 -883 278 C ATOM 3756 C ASP B 362 -127.059 -43.169 -5.264 1.00 57.75 C ANISOU 3756 C ASP B 362 7670 7356 6918 356 -853 112 C ATOM 3757 O ASP B 362 -126.786 -44.293 -5.697 1.00 52.98 O ANISOU 3757 O ASP B 362 7147 6613 6369 361 -905 85 O ATOM 3758 CB ASP B 362 -129.213 -44.056 -4.336 1.00 54.45 C ANISOU 3758 CB ASP B 362 7384 6781 6523 631 -862 468 C ATOM 3759 CG ASP B 362 -129.970 -44.325 -3.056 1.00 68.33 C ANISOU 3759 CG ASP B 362 9128 8466 8370 761 -855 622 C ATOM 3760 OD1 ASP B 362 -129.376 -44.936 -2.137 1.00 55.03 O ANISOU 3760 OD1 ASP B 362 7414 6658 6837 800 -882 586 O ATOM 3761 OD2 ASP B 362 -131.158 -43.941 -2.973 1.00 84.97 O ANISOU 3761 OD2 ASP B 362 11236 10626 10421 808 -828 770 O ATOM 3762 N GLY B 363 -126.446 -42.074 -5.707 1.00 64.92 N ANISOU 3762 N GLY B 363 9420 7463 7783 280 524 -539 N ATOM 3763 CA GLY B 363 -125.350 -42.164 -6.657 1.00 35.99 C ANISOU 3763 CA GLY B 363 5880 3675 4119 100 494 -577 C ATOM 3764 C GLY B 363 -125.801 -42.069 -8.099 1.00 42.21 C ANISOU 3764 C GLY B 363 6669 4466 4903 48 420 -466 C ATOM 3765 O GLY B 363 -125.045 -42.350 -9.021 1.00 45.68 O ANISOU 3765 O GLY B 363 7173 4825 5358 -87 379 -442 O ATOM 3766 N GLY B 364 -127.044 -41.665 -8.298 1.00 34.19 N ANISOU 3766 N GLY B 364 5529 3592 3871 159 393 -374 N ATOM 3767 CA GLY B 364 -127.605 -41.645 -9.627 1.00 23.38 C ANISOU 3767 CA GLY B 364 4151 2232 2499 128 323 -256 C ATOM 3768 C GLY B 364 -127.838 -40.271 -10.231 1.00 29.83 C ANISOU 3768 C GLY B 364 4861 3229 3244 108 288 -290 C ATOM 3769 O GLY B 364 -127.513 -39.218 -9.675 1.00 37.23 O ANISOU 3769 O GLY B 364 5728 4288 4128 101 317 -415 O ATOM 3770 N ILE B 365 -128.406 -40.304 -11.421 1.00 23.29 N ANISOU 3770 N ILE B 365 4022 2414 2413 92 226 -176 N ATOM 3771 CA ILE B 365 -128.777 -39.109 -12.113 1.00 15.59 C ANISOU 3771 CA ILE B 365 2948 1602 1376 83 189 -187 C ATOM 3772 C ILE B 365 -130.215 -39.246 -12.577 1.00 15.83 C ANISOU 3772 C ILE B 365 2878 1730 1408 200 146 -37 C ATOM 3773 O ILE B 365 -130.568 -40.216 -13.237 1.00 41.27 O ANISOU 3773 O ILE B 365 6159 4847 4674 198 113 95 O ATOM 3774 CB ILE B 365 -127.867 -38.886 -13.322 1.00 19.18 C ANISOU 3774 CB ILE B 365 3497 1977 1813 -73 150 -205 C ATOM 3775 CG1 ILE B 365 -126.502 -38.396 -12.848 1.00 31.40 C ANISOU 3775 CG1 ILE B 365 5112 3478 3339 -181 195 -367 C ATOM 3776 CG2 ILE B 365 -128.476 -37.873 -14.259 1.00 31.68 C ANISOU 3776 CG2 ILE B 365 4985 3709 3344 -67 102 -175 C ATOM 3777 CD1 ILE B 365 -125.489 -38.228 -13.965 1.00 53.71 C ANISOU 3777 CD1 ILE B 365 7941 6265 6202 -310 157 -329 C ATOM 3778 N THR B 366 -131.041 -38.272 -12.220 1.00 30.36 N ANISOU 3778 N THR B 366 4561 3777 3196 298 149 -59 N ATOM 3779 CA THR B 366 -132.382 -38.172 -12.761 1.00 35.56 C ANISOU 3779 CA THR B 366 5109 4563 3841 401 104 73 C ATOM 3780 C THR B 366 -132.383 -37.504 -14.141 1.00 44.42 C ANISOU 3780 C THR B 366 6222 5733 4923 319 44 95 C ATOM 3781 O THR B 366 -132.045 -36.331 -14.265 1.00 77.96 O ANISOU 3781 O THR B 366 10419 10086 9114 271 47 -17 O ATOM 3782 CB THR B 366 -133.298 -37.387 -11.808 1.00 37.03 C ANISOU 3782 CB THR B 366 5120 4971 3978 544 132 38 C ATOM 3783 OG1 THR B 366 -133.263 -37.989 -10.507 1.00 47.33 O ANISOU 3783 OG1 THR B 366 6432 6235 5316 628 192 17 O ATOM 3784 CG2 THR B 366 -134.715 -37.414 -12.301 1.00 43.88 C ANISOU 3784 CG2 THR B 366 5873 5967 4832 662 89 186 C ATOM 3785 N LEU B 367 -132.733 -38.267 -15.173 1.00 36.72 N ANISOU 3785 N LEU B 367 5300 4675 3978 300 -7 236 N ATOM 3786 CA LEU B 367 -133.052 -37.704 -16.479 1.00 28.96 C ANISOU 3786 CA LEU B 367 4281 3767 2955 261 -68 289 C ATOM 3787 C LEU B 367 -134.524 -37.295 -16.502 1.00 27.92 C ANISOU 3787 C LEU B 367 3985 3834 2791 403 -92 377 C ATOM 3788 O LEU B 367 -135.245 -37.499 -15.543 1.00 62.66 O ANISOU 3788 O LEU B 367 8305 8303 7199 528 -62 403 O ATOM 3789 CB LEU B 367 -132.832 -38.725 -17.576 1.00 13.95 C ANISOU 3789 CB LEU B 367 2498 1707 1095 181 -114 408 C ATOM 3790 CG LEU B 367 -131.444 -39.073 -18.046 1.00 24.99 C ANISOU 3790 CG LEU B 367 4053 2931 2510 24 -113 350 C ATOM 3791 CD1 LEU B 367 -130.436 -38.681 -17.014 1.00 44.54 C ANISOU 3791 CD1 LEU B 367 6567 5372 4982 -18 -52 186 C ATOM 3792 CD2 LEU B 367 -131.426 -40.563 -18.338 1.00 24.58 C ANISOU 3792 CD2 LEU B 367 4110 2706 2524 -5 -127 467 C ATOM 3793 N GLY B 368 -134.969 -36.760 -17.628 1.00 32.72 N ANISOU 3793 N GLY B 368 4542 4531 3358 388 -147 429 N ATOM 3794 CA GLY B 368 -136.304 -36.213 -17.747 1.00 24.80 C ANISOU 3794 CA GLY B 368 3371 3723 2330 500 -169 486 C ATOM 3795 C GLY B 368 -136.290 -34.749 -18.182 1.00 26.71 C ANISOU 3795 C GLY B 368 3518 4092 2539 450 -173 364 C ATOM 3796 O GLY B 368 -135.217 -34.161 -18.356 1.00 20.25 O ANISOU 3796 O GLY B 368 2774 3238 1681 351 -164 255 O ATOM 3797 N LYS B 369 -137.483 -34.166 -18.334 1.00 34.85 N ANISOU 3797 N LYS B 369 4394 5251 3598 515 -171 374 N ATOM 3798 CA LYS B 369 -137.670 -32.791 -18.810 1.00 29.92 C ANISOU 3798 CA LYS B 369 3674 4727 2967 481 -163 277 C ATOM 3799 C LYS B 369 -136.857 -31.752 -18.045 1.00 27.32 C ANISOU 3799 C LYS B 369 3329 4474 2578 454 -130 120 C ATOM 3800 O LYS B 369 -136.522 -30.711 -18.599 1.00 35.67 O ANISOU 3800 O LYS B 369 4372 5529 3653 377 -126 36 O ATOM 3801 CB LYS B 369 -139.148 -32.401 -18.785 1.00 22.41 C ANISOU 3801 CB LYS B 369 2562 3917 2035 575 -138 307 C ATOM 3802 CG LYS B 369 -139.997 -33.109 -19.815 1.00 28.35 C ANISOU 3802 CG LYS B 369 3330 4582 2859 554 -159 413 C ATOM 3803 CD LYS B 369 -141.472 -33.043 -19.413 1.00 38.65 C ANISOU 3803 CD LYS B 369 4509 6019 4158 652 -114 452 C ATOM 3804 CE LYS B 369 -142.399 -33.222 -20.609 1.00 46.95 C ANISOU 3804 CE LYS B 369 5554 7024 5261 613 -124 506 C ATOM 3805 NZ LYS B 369 -143.768 -32.680 -20.355 1.00 52.23 N ANISOU 3805 NZ LYS B 369 6097 7863 5885 691 -63 513 N ATOM 3806 N ASP B 370 -136.538 -32.039 -16.785 1.00 23.73 N ANISOU 3806 N ASP B 370 2885 4064 2069 509 -99 74 N ATOM 3807 CA ASP B 370 -135.753 -31.121 -15.961 1.00 15.89 C ANISOU 3807 CA ASP B 370 1879 3102 1056 454 -51 -98 C ATOM 3808 C ASP B 370 -134.422 -31.727 -15.597 1.00 26.75 C ANISOU 3808 C ASP B 370 3425 4321 2418 369 -21 -159 C ATOM 3809 O ASP B 370 -133.750 -31.233 -14.699 1.00 25.94 O ANISOU 3809 O ASP B 370 3322 4204 2330 325 30 -288 O ATOM 3810 CB ASP B 370 -136.489 -30.768 -14.672 1.00 45.86 C ANISOU 3810 CB ASP B 370 5524 7077 4824 576 -19 -142 C ATOM 3811 CG ASP B 370 -137.312 -29.496 -14.797 1.00102.14 C ANISOU 3811 CG ASP B 370 12473 14357 11978 597 -31 -184 C ATOM 3812 OD1 ASP B 370 -136.980 -28.648 -15.659 1.00113.93 O ANISOU 3812 OD1 ASP B 370 13978 15793 13515 495 -42 -228 O ATOM 3813 OD2 ASP B 370 -138.286 -29.336 -14.028 1.00118.19 O ANISOU 3813 OD2 ASP B 370 14356 16566 13986 721 -31 -169 O ATOM 3814 N GLY B 371 -134.044 -32.795 -16.293 1.00 21.68 N ANISOU 3814 N GLY B 371 2921 3526 1790 331 -52 -56 N ATOM 3815 CA GLY B 371 -132.896 -33.595 -15.888 1.00 36.13 C ANISOU 3815 CA GLY B 371 4905 5150 3674 248 -20 -91 C ATOM 3816 C GLY B 371 -131.676 -33.247 -16.707 1.00 51.39 C ANISOU 3816 C GLY B 371 6958 6964 5602 92 -26 -161 C ATOM 3817 O GLY B 371 -131.442 -33.816 -17.770 1.00 51.61 O ANISOU 3817 O GLY B 371 7077 6881 5651 33 -70 -68 O ATOM 3818 N ASN B 372 -130.890 -32.312 -16.188 1.00 47.88 N ANISOU 3818 N ASN B 372 6513 6536 5144 24 22 -316 N ATOM 3819 CA ASN B 372 -129.828 -31.688 -16.943 1.00 21.29 C ANISOU 3819 CA ASN B 372 3164 3061 1862 -45 7 -352 C ATOM 3820 C ASN B 372 -128.510 -32.453 -16.879 1.00 24.83 C ANISOU 3820 C ASN B 372 3707 3338 2389 -151 27 -361 C ATOM 3821 O ASN B 372 -127.984 -32.705 -15.805 1.00 30.05 O ANISOU 3821 O ASN B 372 4390 3959 3068 -155 66 -424 O ATOM 3822 CB ASN B 372 -129.618 -30.255 -16.446 1.00 33.22 C ANISOU 3822 CB ASN B 372 4623 4581 3417 -43 35 -424 C ATOM 3823 CG ASN B 372 -130.916 -29.442 -16.382 1.00 41.29 C ANISOU 3823 CG ASN B 372 5508 5762 4417 -12 42 -416 C ATOM 3824 OD1 ASN B 372 -131.876 -29.701 -17.104 1.00 37.25 O ANISOU 3824 OD1 ASN B 372 4942 5333 3876 30 3 -339 O ATOM 3825 ND2 ASN B 372 -130.931 -28.442 -15.520 1.00 55.67 N ANISOU 3825 ND2 ASN B 372 7236 7648 6267 -7 76 -488 N ATOM 3826 N ILE B 373 -127.967 -32.802 -18.039 1.00 21.41 N ANISOU 3826 N ILE B 373 3336 2793 2007 -224 1 -286 N ATOM 3827 CA ILE B 373 -126.649 -33.408 -18.093 1.00 33.75 C ANISOU 3827 CA ILE B 373 4987 4194 3643 -313 22 -272 C ATOM 3828 C ILE B 373 -125.723 -32.640 -19.044 1.00 24.01 C ANISOU 3828 C ILE B 373 3712 2933 2475 -359 26 -251 C ATOM 3829 O ILE B 373 -126.128 -32.244 -20.128 1.00 23.84 O ANISOU 3829 O ILE B 373 3666 2941 2452 -353 -2 -208 O ATOM 3830 CB ILE B 373 -126.724 -34.904 -18.483 1.00 46.67 C ANISOU 3830 CB ILE B 373 6778 5693 5261 -353 -4 -176 C ATOM 3831 CG1 ILE B 373 -127.372 -35.077 -19.852 1.00 47.35 C ANISOU 3831 CG1 ILE B 373 6871 5783 5335 -353 -64 -75 C ATOM 3832 CG2 ILE B 373 -127.519 -35.691 -17.456 1.00 59.25 C ANISOU 3832 CG2 ILE B 373 8442 7290 6780 -289 3 -185 C ATOM 3833 CD1 ILE B 373 -127.328 -36.507 -20.345 1.00 64.96 C ANISOU 3833 CD1 ILE B 373 9235 7872 7576 -397 -103 17 C ATOM 3834 N TYR B 374 -124.474 -32.445 -18.639 1.00 27.46 N ANISOU 3834 N TYR B 374 4163 3317 2953 -408 68 -269 N ATOM 3835 CA TYR B 374 -123.552 -31.614 -19.399 1.00 21.23 C ANISOU 3835 CA TYR B 374 3389 2502 2174 -477 100 -238 C ATOM 3836 C TYR B 374 -122.362 -32.407 -19.870 1.00 15.95 C ANISOU 3836 C TYR B 374 2826 1741 1495 -548 128 -152 C ATOM 3837 O TYR B 374 -121.904 -33.301 -19.181 1.00 25.74 O ANISOU 3837 O TYR B 374 4111 2942 2727 -555 142 -151 O ATOM 3838 CB TYR B 374 -123.090 -30.437 -18.537 1.00 23.08 C ANISOU 3838 CB TYR B 374 3564 2789 2417 -487 143 -322 C ATOM 3839 CG TYR B 374 -124.197 -29.416 -18.310 1.00 22.47 C ANISOU 3839 CG TYR B 374 3386 2826 2325 -416 118 -392 C ATOM 3840 CD1 TYR B 374 -124.982 -29.454 -17.168 1.00 19.03 C ANISOU 3840 CD1 TYR B 374 2899 2467 1864 -335 103 -459 C ATOM 3841 CD2 TYR B 374 -124.462 -28.434 -19.253 1.00 20.86 C ANISOU 3841 CD2 TYR B 374 3148 2659 2119 -423 112 -382 C ATOM 3842 CE1 TYR B 374 -125.987 -28.547 -16.974 1.00 16.26 C ANISOU 3842 CE1 TYR B 374 2476 2224 1477 -265 88 -499 C ATOM 3843 CE2 TYR B 374 -125.466 -27.513 -19.072 1.00 16.87 C ANISOU 3843 CE2 TYR B 374 2560 2260 1589 -358 93 -434 C ATOM 3844 CZ TYR B 374 -126.230 -27.575 -17.931 1.00 26.83 C ANISOU 3844 CZ TYR B 374 3782 3595 2819 -283 83 -486 C ATOM 3845 OH TYR B 374 -127.235 -26.663 -17.746 1.00 30.07 O ANISOU 3845 OH TYR B 374 4122 4105 3197 -234 79 -515 O ATOM 3846 N ALA B 375 -121.862 -32.094 -21.057 1.00 15.15 N ANISOU 3846 N ALA B 375 2764 1618 1376 -590 135 -82 N ATOM 3847 CA ALA B 375 -120.585 -32.646 -21.474 1.00 11.40 C ANISOU 3847 CA ALA B 375 2317 1124 891 -594 141 -46 C ATOM 3848 C ALA B 375 -119.491 -32.186 -20.526 1.00 30.18 C ANISOU 3848 C ALA B 375 4720 3499 3249 -647 212 -84 C ATOM 3849 O ALA B 375 -119.698 -31.282 -19.721 1.00 30.99 O ANISOU 3849 O ALA B 375 4783 3625 3365 -668 250 -147 O ATOM 3850 CB ALA B 375 -120.251 -32.258 -22.881 1.00 9.45 C ANISOU 3850 CB ALA B 375 2023 897 669 -562 108 -18 C ATOM 3851 N SER B 376 -118.324 -32.815 -20.626 1.00 32.75 N ANISOU 3851 N SER B 376 5066 3813 3564 -643 213 -72 N ATOM 3852 CA SER B 376 -117.249 -32.523 -19.699 1.00 25.58 C ANISOU 3852 CA SER B 376 4181 2899 2639 -692 277 -107 C ATOM 3853 C SER B 376 -115.877 -32.918 -20.248 1.00 36.20 C ANISOU 3853 C SER B 376 5539 4242 3974 -684 269 -89 C ATOM 3854 O SER B 376 -115.760 -33.527 -21.325 1.00 17.81 O ANISOU 3854 O SER B 376 3199 1919 1648 -645 216 -53 O ATOM 3855 CB SER B 376 -117.503 -33.251 -18.382 1.00 25.45 C ANISOU 3855 CB SER B 376 4209 2856 2604 -718 313 -134 C ATOM 3856 OG SER B 376 -117.591 -34.640 -18.628 1.00 31.18 O ANISOU 3856 OG SER B 376 4973 3557 3318 -685 266 -102 O ATOM 3857 N GLY B 377 -114.840 -32.553 -19.496 1.00 19.47 N ANISOU 3857 N GLY B 377 3436 2119 1842 -728 325 -119 N ATOM 3858 CA GLY B 377 -113.491 -32.959 -19.825 1.00 22.70 C ANISOU 3858 CA GLY B 377 3866 2524 2236 -730 324 -107 C ATOM 3859 C GLY B 377 -112.815 -32.117 -20.887 1.00 39.45 C ANISOU 3859 C GLY B 377 5958 4665 4367 -714 311 -92 C ATOM 3860 O GLY B 377 -111.795 -32.537 -21.431 1.00 39.75 O ANISOU 3860 O GLY B 377 6009 4703 4392 -707 298 -76 O ATOM 3861 N GLY B 378 -113.382 -30.942 -21.180 1.00 42.25 N ANISOU 3861 N GLY B 378 6278 5035 4741 -712 318 -99 N ATOM 3862 CA GLY B 378 -112.820 -30.010 -22.144 1.00 20.19 C ANISOU 3862 CA GLY B 378 3463 2253 1955 -700 314 -89 C ATOM 3863 C GLY B 378 -111.449 -29.517 -21.733 1.00 36.18 C ANISOU 3863 C GLY B 378 5507 4274 3965 -735 360 -109 C ATOM 3864 O GLY B 378 -111.239 -29.141 -20.580 1.00 50.63 O ANISOU 3864 O GLY B 378 7346 6101 5792 -782 415 -148 O ATOM 3865 N THR B 379 -110.506 -29.534 -22.675 1.00 44.22 N ANISOU 3865 N THR B 379 6530 5295 4978 -714 339 -86 N ATOM 3866 CA THR B 379 -109.134 -29.105 -22.422 1.00 61.57 C ANISOU 3866 CA THR B 379 8749 7487 7159 -744 377 -101 C ATOM 3867 C THR B 379 -108.716 -28.023 -23.433 1.00 88.14 C ANISOU 3867 C THR B 379 12102 10859 10530 -729 375 -91 C ATOM 3868 O THR B 379 -109.108 -28.072 -24.602 1.00 93.87 O ANISOU 3868 O THR B 379 12803 11481 11380 -727 282 -125 O ATOM 3869 CB THR B 379 -108.157 -30.301 -22.482 1.00 63.60 C ANISOU 3869 CB THR B 379 9036 7737 7394 -741 361 -87 C ATOM 3870 OG1 THR B 379 -108.616 -31.341 -21.612 1.00 64.15 O ANISOU 3870 OG1 THR B 379 9125 7796 7456 -754 363 -95 O ATOM 3871 CG2 THR B 379 -106.748 -29.885 -22.056 1.00 78.06 C ANISOU 3871 CG2 THR B 379 10892 9561 9207 -777 404 -105 C ATOM 3872 N ASP B 380 -107.927 -27.049 -22.977 1.00 78.08 N ANISOU 3872 N ASP B 380 10840 9579 9248 -767 425 -118 N ATOM 3873 CA ASP B 380 -107.515 -25.921 -23.816 1.00 71.53 C ANISOU 3873 CA ASP B 380 10009 8750 8420 -762 433 -115 C ATOM 3874 C ASP B 380 -106.127 -26.107 -24.447 1.00 63.64 C ANISOU 3874 C ASP B 380 9042 7616 7525 -803 371 -167 C ATOM 3875 O ASP B 380 -105.954 -25.961 -25.659 1.00 47.49 O ANISOU 3875 O ASP B 380 7017 5558 5470 -790 347 -152 O ATOM 3876 CB ASP B 380 -107.522 -24.616 -23.004 1.00 82.95 C ANISOU 3876 CB ASP B 380 11453 10193 9869 -813 498 -159 C ATOM 3877 CG ASP B 380 -108.897 -24.264 -22.453 1.00 73.84 C ANISOU 3877 CG ASP B 380 10269 9051 8736 -829 511 -184 C ATOM 3878 OD1 ASP B 380 -109.894 -24.412 -23.188 1.00 48.68 O ANISOU 3878 OD1 ASP B 380 7064 5871 5563 -793 469 -161 O ATOM 3879 OD2 ASP B 380 -108.978 -23.829 -21.282 1.00 81.11 O ANISOU 3879 OD2 ASP B 380 11179 9978 9661 -878 565 -230 O ATOM 3880 N GLY B 381 -105.135 -26.406 -23.617 1.00 62.96 N ANISOU 3880 N GLY B 381 8973 7520 7428 -833 398 -181 N ATOM 3881 CA GLY B 381 -103.782 -26.576 -24.104 1.00 74.58 C ANISOU 3881 CA GLY B 381 10492 8968 8878 -851 400 -179 C ATOM 3882 C GLY B 381 -103.262 -25.340 -24.810 1.00 73.99 C ANISOU 3882 C GLY B 381 10464 9045 8605 -782 457 -203 C ATOM 3883 O GLY B 381 -102.430 -24.607 -24.271 1.00 74.74 O ANISOU 3883 O GLY B 381 10573 9134 8689 -810 504 -226 O TER 3884 GLY B 381 ATOM 3885 N ALA C 102 -29.048-107.252 -27.033 1.00100.71 N ANISOU 3885 N ALA C 102 13065 12694 12506 -330 -701 424 N ATOM 3886 CA ALA C 102 -27.667-107.395 -27.487 1.00 93.80 C ANISOU 3886 CA ALA C 102 12213 11808 11621 -341 -714 425 C ATOM 3887 C ALA C 102 -27.256-108.858 -27.628 1.00 86.86 C ANISOU 3887 C ALA C 102 11315 10942 10744 -290 -682 394 C ATOM 3888 O ALA C 102 -26.539-109.215 -28.561 1.00110.24 O ANISOU 3888 O ALA C 102 14282 13874 13729 -287 -704 388 O ATOM 3889 CB ALA C 102 -26.711-106.657 -26.548 1.00 86.29 C ANISOU 3889 CB ALA C 102 11294 10890 10604 -385 -704 441 C ATOM 3890 N ASN C 103 -27.713-109.703 -26.706 1.00 50.14 N ANISOU 3890 N ASN C 103 6644 6335 6070 -251 -631 377 N ATOM 3891 CA ASN C 103 -27.238-111.089 -26.638 1.00 46.47 C ANISOU 3891 CA ASN C 103 6167 5889 5599 -207 -598 352 C ATOM 3892 C ASN C 103 -28.362-112.086 -26.425 1.00 41.31 C ANISOU 3892 C ASN C 103 5477 5254 4965 -157 -567 333 C ATOM 3893 O ASN C 103 -29.203-111.899 -25.549 1.00 70.84 O ANISOU 3893 O ASN C 103 9205 9026 8687 -150 -544 336 O ATOM 3894 CB ASN C 103 -26.226-111.250 -25.502 1.00 73.18 C ANISOU 3894 CB ASN C 103 9572 9315 8918 -211 -564 352 C ATOM 3895 CG ASN C 103 -24.851-110.742 -25.871 1.00101.46 C ANISOU 3895 CG ASN C 103 13188 12882 12480 -253 -589 362 C ATOM 3896 OD1 ASN C 103 -24.394-110.930 -27.000 1.00111.92 O ANISOU 3896 OD1 ASN C 103 14518 14170 13839 -256 -621 360 O ATOM 3897 ND2 ASN C 103 -24.179-110.095 -24.921 1.00103.25 N ANISOU 3897 ND2 ASN C 103 13440 13139 12651 -289 -576 372 N ATOM 3898 N PRO C 104 -28.386-113.155 -27.229 1.00 26.12 N ANISOU 3898 N PRO C 104 3535 3313 3076 -126 -565 313 N ATOM 3899 CA PRO C 104 -29.446-114.147 -27.046 1.00 23.05 C ANISOU 3899 CA PRO C 104 3110 2945 2702 -84 -535 296 C ATOM 3900 C PRO C 104 -29.258-114.901 -25.739 1.00 33.53 C ANISOU 3900 C PRO C 104 4435 4326 3979 -53 -486 293 C ATOM 3901 O PRO C 104 -28.144-114.962 -25.196 1.00 57.51 O ANISOU 3901 O PRO C 104 7497 7376 6976 -58 -474 298 O ATOM 3902 CB PRO C 104 -29.250-115.097 -28.233 1.00 34.60 C ANISOU 3902 CB PRO C 104 4561 4376 4209 -67 -547 275 C ATOM 3903 CG PRO C 104 -28.373-114.368 -29.192 1.00 34.14 C ANISOU 3903 CG PRO C 104 4530 4272 4172 -101 -593 283 C ATOM 3904 CD PRO C 104 -27.512-113.479 -28.366 1.00 30.88 C ANISOU 3904 CD PRO C 104 4149 3877 3706 -132 -593 305 C ATOM 3905 N SER C 105 -30.344-115.460 -25.226 1.00 13.48 N ANISOU 3905 N SER C 105 1867 1815 1440 -21 -459 286 N ATOM 3906 CA SER C 105 -30.263-116.319 -24.071 1.00 23.31 C ANISOU 3906 CA SER C 105 3108 3104 2645 16 -415 283 C ATOM 3907 C SER C 105 -29.622-117.579 -24.601 1.00 36.99 C ANISOU 3907 C SER C 105 4837 4827 4389 41 -406 272 C ATOM 3908 O SER C 105 -29.532-117.751 -25.808 1.00 40.18 O ANISOU 3908 O SER C 105 5236 5195 4835 31 -432 263 O ATOM 3909 CB SER C 105 -31.654-116.608 -23.524 1.00 31.73 C ANISOU 3909 CB SER C 105 4145 4196 3713 42 -395 276 C ATOM 3910 OG SER C 105 -32.330-115.402 -23.241 1.00 56.58 O ANISOU 3910 OG SER C 105 7293 7346 6857 11 -410 286 O ATOM 3911 N ARG C 106 -29.159-118.455 -23.722 1.00 20.24 N ANISOU 3911 N ARG C 106 2722 2734 2233 73 -371 274 N ATOM 3912 CA ARG C 106 -28.594-119.700 -24.201 1.00 27.02 C ANISOU 3912 CA ARG C 106 3578 3584 3105 93 -362 269 C ATOM 3913 C ARG C 106 -28.730-120.853 -23.189 1.00 31.16 C ANISOU 3913 C ARG C 106 4095 4141 3603 139 -319 274 C ATOM 3914 O ARG C 106 -28.746-120.646 -21.986 1.00 29.53 O ANISOU 3914 O ARG C 106 3914 3942 3365 150 -298 272 O ATOM 3915 CB ARG C 106 -27.136-119.492 -24.626 1.00 19.50 C ANISOU 3915 CB ARG C 106 2662 2604 2143 65 -380 270 C ATOM 3916 CG ARG C 106 -26.505-120.693 -25.313 1.00 26.83 C ANISOU 3916 CG ARG C 106 3595 3510 3090 78 -380 260 C ATOM 3917 CD ARG C 106 -25.046-120.437 -25.576 1.00 29.58 C ANISOU 3917 CD ARG C 106 3986 3834 3417 50 -397 258 C ATOM 3918 NE ARG C 106 -24.848-119.244 -26.388 1.00 17.70 N ANISOU 3918 NE ARG C 106 2492 2302 1931 10 -439 256 N ATOM 3919 CZ ARG C 106 -23.660-118.795 -26.771 1.00 34.45 C ANISOU 3919 CZ ARG C 106 4648 4403 4037 -23 -462 255 C ATOM 3920 NH1 ARG C 106 -22.563-119.453 -26.427 1.00 16.61 N ANISOU 3920 NH1 ARG C 106 2419 2147 1743 -20 -446 252 N ATOM 3921 NH2 ARG C 106 -23.568-117.693 -27.505 1.00 50.23 N ANISOU 3921 NH2 ARG C 106 6652 6377 6055 -59 -502 260 N ATOM 3922 N LEU C 107 -28.854-122.069 -23.703 1.00 31.48 N ANISOU 3922 N LEU C 107 4111 4176 3674 151 -307 272 N ATOM 3923 CA LEU C 107 -28.921-123.259 -22.874 1.00 19.63 C ANISOU 3923 CA LEU C 107 2613 2649 2197 104 -308 296 C ATOM 3924 C LEU C 107 -27.672-124.075 -23.170 1.00 13.14 C ANISOU 3924 C LEU C 107 1813 1823 1355 136 -294 297 C ATOM 3925 O LEU C 107 -27.438-124.462 -24.308 1.00 21.71 O ANISOU 3925 O LEU C 107 2895 2892 2460 152 -304 281 O ATOM 3926 CB LEU C 107 -30.160-124.063 -23.259 1.00 11.14 C ANISOU 3926 CB LEU C 107 1532 1542 1158 123 -320 270 C ATOM 3927 CG LEU C 107 -30.589-125.210 -22.370 1.00 13.38 C ANISOU 3927 CG LEU C 107 1802 1853 1427 168 -280 273 C ATOM 3928 CD1 LEU C 107 -30.644-124.716 -20.972 1.00 19.71 C ANISOU 3928 CD1 LEU C 107 2604 2692 2193 179 -248 284 C ATOM 3929 CD2 LEU C 107 -31.938-125.737 -22.787 1.00 7.26 C ANISOU 3929 CD2 LEU C 107 993 1083 683 173 -283 259 C ATOM 3930 N ILE C 108 -26.848-124.317 -22.164 1.00 40.34 N ANISOU 3930 N ILE C 108 5302 5265 4760 153 -270 298 N ATOM 3931 CA ILE C 108 -25.756-125.273 -22.328 1.00 21.85 C ANISOU 3931 CA ILE C 108 2993 2903 2407 189 -245 287 C ATOM 3932 C ILE C 108 -25.960-126.356 -21.294 1.00 27.89 C ANISOU 3932 C ILE C 108 3751 3679 3166 241 -191 289 C ATOM 3933 O ILE C 108 -26.080-126.047 -20.115 1.00 27.41 O ANISOU 3933 O ILE C 108 3685 3650 3080 253 -163 300 O ATOM 3934 CB ILE C 108 -24.393-124.612 -22.144 1.00 27.86 C ANISOU 3934 CB ILE C 108 3803 3660 3122 174 -243 285 C ATOM 3935 CG1 ILE C 108 -24.305-123.350 -23.010 1.00 30.30 C ANISOU 3935 CG1 ILE C 108 4105 3971 3437 129 -288 283 C ATOM 3936 CG2 ILE C 108 -23.281-125.590 -22.494 1.00 33.79 C ANISOU 3936 CG2 ILE C 108 4601 4375 3864 203 -223 268 C ATOM 3937 CD1 ILE C 108 -23.155-122.448 -22.672 1.00 22.67 C ANISOU 3937 CD1 ILE C 108 3183 3008 2422 98 -290 280 C ATOM 3938 N VAL C 109 -26.048-127.614 -21.733 1.00 44.50 N ANISOU 3938 N VAL C 109 5849 5765 5295 272 -176 282 N ATOM 3939 CA VAL C 109 -26.204-128.755 -20.817 1.00 15.65 C ANISOU 3939 CA VAL C 109 2182 2122 1641 322 -123 292 C ATOM 3940 C VAL C 109 -24.915-129.482 -20.704 1.00 13.84 C ANISOU 3940 C VAL C 109 2000 1864 1393 358 -88 292 C ATOM 3941 O VAL C 109 -24.271-129.753 -21.709 1.00 50.45 O ANISOU 3941 O VAL C 109 6668 6465 6034 350 -105 277 O ATOM 3942 CB VAL C 109 -27.233-129.763 -21.308 1.00 19.63 C ANISOU 3942 CB VAL C 109 2651 2626 2182 328 -125 288 C ATOM 3943 CG1 VAL C 109 -27.164-131.001 -20.459 1.00 23.13 C ANISOU 3943 CG1 VAL C 109 3089 3075 2624 377 -74 302 C ATOM 3944 CG2 VAL C 109 -28.645-129.149 -21.274 1.00 22.70 C ANISOU 3944 CG2 VAL C 109 2997 3042 2586 299 -150 287 C ATOM 3945 N ALA C 110 -24.528-129.804 -19.475 1.00 21.71 N ANISOU 3945 N ALA C 110 3005 2875 2370 400 -37 307 N ATOM 3946 CA ALA C 110 -23.267-130.498 -19.225 1.00 11.87 C ANISOU 3946 CA ALA C 110 1803 1593 1115 429 9 302 C ATOM 3947 C ALA C 110 -23.431-131.583 -18.167 1.00 16.46 C ANISOU 3947 C ALA C 110 2367 2176 1711 487 62 323 C ATOM 3948 O ALA C 110 -24.444-131.642 -17.483 1.00 31.47 O ANISOU 3948 O ALA C 110 4223 4117 3616 506 63 345 O ATOM 3949 CB ALA C 110 -22.196-129.511 -18.819 1.00 14.01 C ANISOU 3949 CB ALA C 110 2104 1863 1356 397 22 280 C ATOM 3950 N ILE C 111 -22.440-132.464 -18.055 1.00 22.07 N ANISOU 3950 N ILE C 111 3106 2841 2439 506 106 309 N ATOM 3951 CA ILE C 111 -22.474-133.501 -17.042 1.00 9.62 C ANISOU 3951 CA ILE C 111 1516 1257 883 563 156 331 C ATOM 3952 C ILE C 111 -21.207-133.485 -16.241 1.00 25.06 C ANISOU 3952 C ILE C 111 3497 3184 2841 573 211 307 C ATOM 3953 O ILE C 111 -20.115-133.482 -16.804 1.00 43.81 O ANISOU 3953 O ILE C 111 5912 5518 5216 545 223 272 O ATOM 3954 CB ILE C 111 -22.673-134.878 -17.657 1.00 20.10 C ANISOU 3954 CB ILE C 111 2849 2550 2239 584 160 343 C ATOM 3955 CG1 ILE C 111 -22.723-135.954 -16.574 1.00 18.01 C ANISOU 3955 CG1 ILE C 111 2571 2274 1997 644 207 375 C ATOM 3956 CG2 ILE C 111 -21.572-135.186 -18.651 1.00 28.84 C ANISOU 3956 CG2 ILE C 111 4002 3602 3354 554 165 305 C ATOM 3957 CD1 ILE C 111 -23.110-137.333 -17.121 1.00 26.85 C ANISOU 3957 CD1 ILE C 111 3683 3373 3144 640 206 380 C ATOM 3958 N GLU C 112 -21.350-133.445 -14.920 1.00 31.38 N ANISOU 3958 N GLU C 112 4272 4008 3644 611 246 321 N ATOM 3959 CA GLU C 112 -20.210-133.511 -14.022 1.00 10.90 C ANISOU 3959 CA GLU C 112 1694 1388 1061 626 306 295 C ATOM 3960 C GLU C 112 -20.065-134.958 -13.593 1.00 30.07 C ANISOU 3960 C GLU C 112 4121 3770 3533 685 346 315 C ATOM 3961 O GLU C 112 -21.016-135.551 -13.090 1.00 22.40 O ANISOU 3961 O GLU C 112 3114 2820 2577 730 341 358 O ATOM 3962 CB GLU C 112 -20.445-132.620 -12.807 1.00 11.15 C ANISOU 3962 CB GLU C 112 1694 1470 1073 633 321 294 C ATOM 3963 CG GLU C 112 -19.165-132.215 -12.109 1.00 35.16 C ANISOU 3963 CG GLU C 112 4754 4494 4112 620 375 249 C ATOM 3964 CD GLU C 112 -19.374-131.165 -11.036 1.00 38.39 C ANISOU 3964 CD GLU C 112 5132 4959 4493 612 386 239 C ATOM 3965 OE1 GLU C 112 -18.397-130.799 -10.353 1.00 39.51 O ANISOU 3965 OE1 GLU C 112 5285 5096 4633 599 434 198 O ATOM 3966 OE2 GLU C 112 -20.509-130.694 -10.870 1.00 33.27 O ANISOU 3966 OE2 GLU C 112 4450 4365 3826 615 351 269 O ATOM 3967 N ILE C 113 -18.887-135.538 -13.821 1.00 27.63 N ANISOU 3967 N ILE C 113 3852 3400 3245 682 385 285 N ATOM 3968 CA ILE C 113 -18.600-136.888 -13.347 1.00 18.87 C ANISOU 3968 CA ILE C 113 2747 2239 2184 736 429 302 C ATOM 3969 C ILE C 113 -17.270-137.002 -12.592 1.00 22.79 C ANISOU 3969 C ILE C 113 3265 2690 2706 748 497 262 C ATOM 3970 O ILE C 113 -16.310-136.303 -12.916 1.00 28.38 O ANISOU 3970 O ILE C 113 4001 3389 3392 699 510 212 O ATOM 3971 CB ILE C 113 -18.556-137.885 -14.487 1.00 21.34 C ANISOU 3971 CB ILE C 113 3091 2508 2509 726 415 309 C ATOM 3972 CG1 ILE C 113 -19.721-137.657 -15.439 1.00 31.06 C ANISOU 3972 CG1 ILE C 113 4305 3782 3715 700 349 332 C ATOM 3973 CG2 ILE C 113 -18.574-139.320 -13.938 1.00 26.55 C ANISOU 3973 CG2 ILE C 113 3750 3121 3215 786 450 344 C ATOM 3974 CD1 ILE C 113 -19.641-138.494 -16.685 1.00 18.13 C ANISOU 3974 CD1 ILE C 113 2696 2108 2086 678 333 327 C ATOM 3975 N VAL C 114 -17.241-137.889 -11.589 1.00 28.59 N ANISOU 3975 N VAL C 114 3982 3394 3486 812 538 284 N ATOM 3976 CA VAL C 114 -16.027-138.311 -10.877 1.00 13.59 C ANISOU 3976 CA VAL C 114 2100 1436 1628 833 608 249 C ATOM 3977 C VAL C 114 -16.088-139.793 -10.559 1.00 51.95 C ANISOU 3977 C VAL C 114 6953 6247 6537 866 617 285 C ATOM 3978 O VAL C 114 -17.180-140.343 -10.407 1.00 49.14 O ANISOU 3978 O VAL C 114 6565 5922 6183 883 578 339 O ATOM 3979 CB VAL C 114 -15.889-137.658 -9.506 1.00 24.72 C ANISOU 3979 CB VAL C 114 3472 2873 3047 858 643 231 C ATOM 3980 CG1 VAL C 114 -14.494-137.105 -9.334 1.00 38.41 C ANISOU 3980 CG1 VAL C 114 5232 4582 4779 819 696 158 C ATOM 3981 CG2 VAL C 114 -16.936-136.599 -9.308 1.00 57.49 C ANISOU 3981 CG2 VAL C 114 7583 7109 7152 843 596 249 C ATOM 3982 N GLU C 115 -14.915-140.425 -10.431 1.00 37.83 N ANISOU 3982 N GLU C 115 5193 4396 4786 858 663 252 N ATOM 3983 CA GLU C 115 -14.800-141.791 -9.907 1.00 19.11 C ANISOU 3983 CA GLU C 115 2814 1982 2466 881 674 280 C ATOM 3984 C GLU C 115 -14.977-141.795 -8.387 1.00 26.75 C ANISOU 3984 C GLU C 115 3732 2961 3471 926 691 292 C ATOM 3985 O GLU C 115 -14.304-141.043 -7.672 1.00 26.22 O ANISOU 3985 O GLU C 115 3655 2894 3414 929 731 246 O ATOM 3986 CB GLU C 115 -13.434-142.393 -10.233 1.00 31.78 C ANISOU 3986 CB GLU C 115 4462 3515 4099 856 719 236 C ATOM 3987 CG GLU C 115 -13.256-142.890 -11.657 1.00 59.63 C ANISOU 3987 CG GLU C 115 8034 7019 7604 815 702 232 C ATOM 3988 CD GLU C 115 -12.487-144.218 -11.728 1.00 83.02 C ANISOU 3988 CD GLU C 115 11020 9915 10607 810 730 230 C ATOM 3989 OE1 GLU C 115 -12.812-145.160 -10.958 1.00 50.80 O ANISOU 3989 OE1 GLU C 115 6917 5818 6565 847 731 270 O ATOM 3990 OE2 GLU C 115 -11.553-144.320 -12.557 1.00100.56 O ANISOU 3990 OE2 GLU C 115 13284 12103 12821 768 751 187 O ATOM 3991 N ASP C 116 -15.886-142.628 -7.886 1.00 40.45 N ANISOU 3991 N ASP C 116 5434 4710 5225 957 662 349 N ATOM 3992 CA ASP C 116 -15.996-142.819 -6.439 1.00 48.39 C ANISOU 3992 CA ASP C 116 6394 5717 6275 1002 676 361 C ATOM 3993 C ASP C 116 -16.644-144.151 -6.072 1.00 57.67 C ANISOU 3993 C ASP C 116 7552 6879 7482 1029 651 419 C ATOM 3994 O ASP C 116 -17.194-144.835 -6.943 1.00 46.91 O ANISOU 3994 O ASP C 116 6207 5520 6098 1009 619 453 O ATOM 3995 CB ASP C 116 -16.767-141.672 -5.788 1.00 33.80 C ANISOU 3995 CB ASP C 116 4501 3942 4399 1016 661 363 C ATOM 3996 CG ASP C 116 -16.187-141.273 -4.446 1.00 41.66 C ANISOU 3996 CG ASP C 116 5462 4930 5435 1046 704 326 C ATOM 3997 OD1 ASP C 116 -15.471-142.104 -3.843 1.00 66.57 O ANISOU 3997 OD1 ASP C 116 8618 8026 8651 1066 733 316 O ATOM 3998 OD2 ASP C 116 -16.443-140.127 -3.992 1.00 44.63 O ANISOU 3998 OD2 ASP C 116 5810 5361 5785 1047 708 304 O ATOM 3999 N GLU C 117 -16.542-144.511 -4.785 1.00 55.45 N ANISOU 3999 N GLU C 117 7235 6581 7253 1072 667 426 N ATOM 4000 CA GLU C 117 -17.288-145.611 -4.176 1.00 18.24 C ANISOU 4000 CA GLU C 117 2494 1865 2569 1104 638 485 C ATOM 4001 C GLU C 117 -18.753-145.193 -3.941 1.00 37.08 C ANISOU 4001 C GLU C 117 4836 4337 4915 1109 589 527 C ATOM 4002 O GLU C 117 -19.027-144.314 -3.127 1.00 39.93 O ANISOU 4002 O GLU C 117 5157 4741 5273 1128 592 514 O ATOM 4003 CB GLU C 117 -16.664-145.981 -2.826 1.00 46.25 C ANISOU 4003 CB GLU C 117 6015 5369 6190 1151 670 472 C ATOM 4004 CG GLU C 117 -15.174-146.311 -2.864 1.00 65.51 C ANISOU 4004 CG GLU C 117 8490 7726 8675 1146 724 421 C ATOM 4005 CD GLU C 117 -14.872-147.613 -3.594 1.00 66.36 C ANISOU 4005 CD GLU C 117 8641 7775 8797 1133 721 447 C ATOM 4006 OE1 GLU C 117 -15.522-148.640 -3.280 1.00 38.21 O ANISOU 4006 OE1 GLU C 117 5062 4202 5253 1159 690 504 O ATOM 4007 OE2 GLU C 117 -13.994-147.607 -4.491 1.00 72.82 O ANISOU 4007 OE2 GLU C 117 9507 8557 9604 1096 748 409 O ATOM 4008 N ILE C 118 -19.671-145.767 -4.665 1.00 43.52 N ANISOU 4008 N ILE C 118 5656 5179 5700 1089 547 571 N ATOM 4009 CA ILE C 118 -21.030-145.375 -4.500 1.00 41.00 C ANISOU 4009 CA ILE C 118 5296 4943 5339 1083 502 606 C ATOM 4010 C ILE C 118 -21.669-146.506 -3.771 1.00 48.41 C ANISOU 4010 C ILE C 118 6206 5885 6303 1109 474 661 C ATOM 4011 O ILE C 118 -21.101-147.582 -3.614 1.00 37.91 O ANISOU 4011 O ILE C 118 4897 4494 5014 1123 482 679 O ATOM 4012 CB ILE C 118 -21.708-145.164 -5.846 1.00 32.26 C ANISOU 4012 CB ILE C 118 4210 3875 4172 1032 471 608 C ATOM 4013 CG1 ILE C 118 -21.928-146.490 -6.543 1.00 37.80 C ANISOU 4013 CG1 ILE C 118 4934 4550 4877 1013 451 639 C ATOM 4014 CG2 ILE C 118 -20.818-144.394 -6.710 1.00 38.80 C ANISOU 4014 CG2 ILE C 118 5078 4683 4981 1007 496 556 C ATOM 4015 CD1 ILE C 118 -22.474-146.360 -7.877 1.00 39.97 C ANISOU 4015 CD1 ILE C 118 5223 4864 5101 963 419 635 C ATOM 4016 N PRO C 119 -22.968-146.429 -3.549 1.00 42.58 N ANISOU 4016 N PRO C 119 5421 5218 5540 1113 442 689 N ATOM 4017 CA PRO C 119 -23.697-147.589 -3.068 1.00 42.83 C ANISOU 4017 CA PRO C 119 5421 5258 5594 1139 415 740 C ATOM 4018 C PRO C 119 -24.279-148.440 -4.192 1.00 66.43 C ANISOU 4018 C PRO C 119 8442 8202 8598 1129 401 775 C ATOM 4019 O PRO C 119 -24.626-147.915 -5.216 1.00 95.13 O ANISOU 4019 O PRO C 119 12087 11769 12289 1163 419 784 O ATOM 4020 CB PRO C 119 -24.812-146.947 -2.278 1.00 52.60 C ANISOU 4020 CB PRO C 119 6618 6589 6778 1118 379 757 C ATOM 4021 CG PRO C 119 -24.307-145.710 -1.900 1.00 59.52 C ANISOU 4021 CG PRO C 119 7484 7495 7636 1117 400 713 C ATOM 4022 CD PRO C 119 -23.552-145.209 -3.018 1.00 55.09 C ANISOU 4022 CD PRO C 119 6976 6878 7079 1100 432 671 C ATOM 4023 N LEU C 120 -24.384-149.747 -4.029 1.00 30.00 N ATOM 4024 CA LEU C 120 -24.900-150.532 -5.161 1.00 30.00 C ATOM 4025 C LEU C 120 -26.322-151.055 -5.053 1.00 30.00 C ATOM 4026 O LEU C 120 -26.766-151.854 -5.875 1.00 30.00 O ATOM 4027 CB LEU C 120 -23.939-151.639 -5.641 1.00 20.00 C ATOM 4028 CG LEU C 120 -23.948-151.460 -7.153 1.00 20.00 C ATOM 4029 CD1 LEU C 120 -23.737-152.667 -7.970 1.00 20.00 C ATOM 4030 CD2 LEU C 120 -25.296-150.939 -7.387 1.00 20.00 C ATOM 4031 N THR C 121 -27.032-150.612 -4.036 1.00 30.00 N ATOM 4032 CA THR C 121 -28.417-151.002 -3.887 1.00 30.00 C ATOM 4033 C THR C 121 -29.219-150.513 -5.091 1.00 30.00 C ATOM 4034 O THR C 121 -29.115-151.073 -6.192 1.00 30.00 O ATOM 4035 CB THR C 121 -28.996-150.553 -2.523 1.00 20.00 C ATOM 4036 OG1 THR C 121 -30.390-150.301 -2.647 1.00 20.00 O ATOM 4037 CG2 THR C 121 -28.310-149.317 -2.019 1.00 20.00 C ATOM 4038 N LYS C 147 -19.263-150.689 -0.413 1.00 52.41 N ANISOU 4038 N LYS C 147 6709 6100 7103 1285 540 716 N ATOM 4039 CA LYS C 147 -19.818-150.094 -1.621 1.00 43.06 C ANISOU 4039 CA LYS C 147 5545 4974 5841 1230 524 712 C ATOM 4040 C LYS C 147 -19.394-150.860 -2.867 1.00 45.55 C ANISOU 4040 C LYS C 147 5918 5246 6141 1192 529 715 C ATOM 4041 O LYS C 147 -19.583-152.070 -2.957 1.00 59.24 O ANISOU 4041 O LYS C 147 7667 6948 7894 1197 510 759 O ATOM 4042 CB LYS C 147 -19.381-148.635 -1.752 1.00 53.81 C ANISOU 4042 CB LYS C 147 6904 6366 7177 1214 554 651 C ATOM 4043 CG LYS C 147 -19.432-147.825 -0.462 1.00 71.84 C ANISOU 4043 CG LYS C 147 9135 8676 9486 1253 565 630 C ATOM 4044 CD LYS C 147 -20.852-147.640 0.041 1.00 86.49 C ANISOU 4044 CD LYS C 147 10941 10612 11311 1263 519 674 C ATOM 4045 CE LYS C 147 -20.906-146.603 1.156 1.00 93.10 C ANISOU 4045 CE LYS C 147 11726 11486 12161 1291 532 643 C ATOM 4046 NZ LYS C 147 -19.965-146.921 2.270 1.00 94.10 N ANISOU 4046 NZ LYS C 147 11836 11549 12370 1340 566 616 N ATOM 4047 N VAL C 148 -18.836-150.131 -3.829 1.00 55.83 N ANISOU 4047 N VAL C 148 7254 6550 7409 1153 552 668 N ATOM 4048 CA VAL C 148 -18.324-150.670 -5.093 1.00 43.81 C ANISOU 4048 CA VAL C 148 5787 4989 5869 1113 562 657 C ATOM 4049 C VAL C 148 -17.762-149.506 -5.895 1.00 39.59 C ANISOU 4049 C VAL C 148 5277 4470 5297 1077 586 598 C ATOM 4050 O VAL C 148 -18.096-148.351 -5.639 1.00 43.77 O ANISOU 4050 O VAL C 148 5779 5052 5801 1078 582 580 O ATOM 4051 CB VAL C 148 -19.406-151.351 -5.940 1.00 40.48 C ANISOU 4051 CB VAL C 148 5371 4605 5405 1083 515 703 C ATOM 4052 CG1 VAL C 148 -20.254-150.326 -6.629 1.00 44.23 C ANISOU 4052 CG1 VAL C 148 5832 5160 5815 1048 490 691 C ATOM 4053 CG2 VAL C 148 -18.766-152.261 -6.970 1.00 57.36 C ANISOU 4053 CG2 VAL C 148 7564 6685 7544 1053 529 698 C ATOM 4054 N ASP C 149 -16.904-149.796 -6.862 1.00 52.04 N ANISOU 4054 N ASP C 149 6904 5999 6869 1045 611 569 N ATOM 4055 CA ASP C 149 -16.246-148.722 -7.590 1.00 38.83 C ANISOU 4055 CA ASP C 149 5256 4332 5165 1012 634 511 C ATOM 4056 C ASP C 149 -16.956-148.441 -8.897 1.00 53.63 C ANISOU 4056 C ASP C 149 7146 6254 6978 968 599 516 C ATOM 4057 O ASP C 149 -17.024-149.309 -9.774 1.00 48.78 O ANISOU 4057 O ASP C 149 6562 5619 6354 943 588 530 O ATOM 4058 CB ASP C 149 -14.775-149.040 -7.831 1.00 50.00 C ANISOU 4058 CB ASP C 149 6716 5670 6613 999 687 464 C ATOM 4059 CG ASP C 149 -14.088-147.989 -8.660 1.00 65.36 C ANISOU 4059 CG ASP C 149 8690 7622 8522 958 708 405 C ATOM 4060 OD1 ASP C 149 -13.830-146.879 -8.139 1.00 93.04 O ANISOU 4060 OD1 ASP C 149 12177 11149 12024 964 725 370 O ATOM 4061 OD2 ASP C 149 -13.796-148.274 -9.839 1.00 56.88 O ANISOU 4061 OD2 ASP C 149 7658 6532 7423 918 708 391 O ATOM 4062 N GLY C 150 -17.490-147.221 -8.993 1.00 64.51 N ANISOU 4062 N GLY C 150 8502 7693 8315 959 581 504 N ATOM 4063 CA GLY C 150 -18.241-146.743 -10.142 1.00 52.25 C ANISOU 4063 CA GLY C 150 6956 6191 6707 920 544 504 C ATOM 4064 C GLY C 150 -18.134-145.231 -10.317 1.00 37.65 C ANISOU 4064 C GLY C 150 5103 4377 4824 908 546 467 C ATOM 4065 O GLY C 150 -17.042-144.672 -10.279 1.00 55.00 O ANISOU 4065 O GLY C 150 7326 6541 7032 904 585 421 O ATOM 4066 N LEU C 151 -19.268-144.559 -10.475 1.00 36.36 N ANISOU 4066 N LEU C 151 4908 4285 4622 899 504 485 N ATOM 4067 CA LEU C 151 -19.268-143.147 -10.852 1.00 34.36 C ANISOU 4067 CA LEU C 151 4656 4067 4330 883 498 454 C ATOM 4068 C LEU C 151 -20.292-142.291 -10.115 1.00 26.30 C ANISOU 4068 C LEU C 151 3584 3121 3288 899 473 474 C ATOM 4069 O LEU C 151 -21.407-142.733 -9.857 1.00 33.46 O ANISOU 4069 O LEU C 151 4454 4070 4189 901 440 512 O ATOM 4070 CB LEU C 151 -19.514-143.026 -12.356 1.00 25.92 C ANISOU 4070 CB LEU C 151 3615 3008 3226 838 466 442 C ATOM 4071 CG LEU C 151 -18.384-143.512 -13.262 1.00 31.22 C ANISOU 4071 CG LEU C 151 4342 3612 3908 814 493 408 C ATOM 4072 CD1 LEU C 151 -18.831-143.459 -14.680 1.00 41.34 C ANISOU 4072 CD1 LEU C 151 5641 4909 5158 773 454 401 C ATOM 4073 CD2 LEU C 151 -17.146-142.648 -13.070 1.00 35.42 C ANISOU 4073 CD2 LEU C 151 4903 4110 4445 815 536 359 C ATOM 4074 N LYS C 152 -19.900-141.057 -9.796 1.00 37.08 N ANISOU 4074 N LYS C 152 4947 4501 4639 906 490 445 N ATOM 4075 CA LYS C 152 -20.792-140.034 -9.235 1.00 23.44 C ANISOU 4075 CA LYS C 152 3176 2846 2883 915 468 456 C ATOM 4076 C LYS C 152 -21.063-138.996 -10.322 1.00 32.46 C ANISOU 4076 C LYS C 152 4334 4020 3977 881 437 440 C ATOM 4077 O LYS C 152 -20.144-138.350 -10.801 1.00 38.83 O ANISOU 4077 O LYS C 152 5180 4798 4776 873 459 402 O ATOM 4078 CB LYS C 152 -20.114-139.318 -8.071 1.00 45.52 C ANISOU 4078 CB LYS C 152 5958 5641 5698 948 512 428 C ATOM 4079 CG LYS C 152 -20.709-139.571 -6.690 1.00 65.59 C ANISOU 4079 CG LYS C 152 8445 8212 8263 985 513 455 C ATOM 4080 CD LYS C 152 -19.893-138.845 -5.607 1.00 69.00 C ANISOU 4080 CD LYS C 152 8862 8638 8718 1010 561 413 C ATOM 4081 CE LYS C 152 -20.506-138.999 -4.216 1.00 81.93 C ANISOU 4081 CE LYS C 152 10441 10309 10381 1047 559 435 C ATOM 4082 NZ LYS C 152 -20.411-140.389 -3.678 1.00 83.09 N ANISOU 4082 NZ LYS C 152 10582 10406 10583 1074 562 463 N ATOM 4083 N ALA C 153 -22.323-138.825 -10.702 1.00 33.41 N ANISOU 4083 N ALA C 153 4425 4201 4068 857 388 464 N ATOM 4084 CA ALA C 153 -22.648-137.938 -11.800 1.00 15.85 C ANISOU 4084 CA ALA C 153 2213 2003 1806 818 350 450 C ATOM 4085 C ALA C 153 -23.730-136.962 -11.432 1.00 44.63 C ANISOU 4085 C ALA C 153 5813 5726 5419 809 319 462 C ATOM 4086 O ALA C 153 -24.564-137.257 -10.581 1.00 38.54 O ANISOU 4086 O ALA C 153 4997 4994 4653 822 316 485 O ATOM 4087 CB ALA C 153 -23.077-138.726 -13.003 1.00 18.51 C ANISOU 4087 CB ALA C 153 2561 2329 2142 777 317 451 C ATOM 4088 N ARG C 154 -23.709-135.800 -12.093 1.00 44.75 N ANISOU 4088 N ARG C 154 5843 5760 5399 783 293 446 N ATOM 4089 CA ARG C 154 -24.798-134.848 -11.993 1.00 19.49 C ANISOU 4089 CA ARG C 154 2604 2633 2169 755 255 451 C ATOM 4090 C ARG C 154 -24.937-133.919 -13.204 1.00 21.61 C ANISOU 4090 C ARG C 154 2892 2911 2408 695 209 429 C ATOM 4091 O ARG C 154 -23.971-133.394 -13.723 1.00 32.78 O ANISOU 4091 O ARG C 154 4349 4294 3810 667 211 400 O ATOM 4092 CB ARG C 154 -24.677-134.051 -10.706 1.00 15.15 C ANISOU 4092 CB ARG C 154 2030 2120 1606 787 282 453 C ATOM 4093 CG ARG C 154 -23.572-133.054 -10.707 1.00 20.10 C ANISOU 4093 CG ARG C 154 2690 2733 2215 745 301 401 C ATOM 4094 CD ARG C 154 -23.622-132.278 -9.429 1.00 33.81 C ANISOU 4094 CD ARG C 154 4392 4515 3938 756 326 390 C ATOM 4095 NE ARG C 154 -22.428-131.476 -9.248 1.00 38.31 N ANISOU 4095 NE ARG C 154 4992 5069 4493 718 356 339 N ATOM 4096 CZ ARG C 154 -22.088-130.906 -8.104 1.00 35.09 C ANISOU 4096 CZ ARG C 154 4564 4689 4080 724 394 314 C ATOM 4097 NH1 ARG C 154 -22.855-131.073 -7.032 1.00 36.86 N ANISOU 4097 NH1 ARG C 154 4735 4956 4316 773 406 337 N ATOM 4098 NH2 ARG C 154 -20.974-130.195 -8.034 1.00 37.86 N ANISOU 4098 NH2 ARG C 154 4945 5027 4414 680 422 263 N ATOM 4099 N ILE C 155 -26.164-133.719 -13.655 1.00 39.45 N ANISOU 4099 N ILE C 155 5113 5210 4668 649 169 422 N ATOM 4100 CA ILE C 155 -26.404-132.819 -14.758 1.00 22.98 C ANISOU 4100 CA ILE C 155 3035 3128 2569 589 123 397 C ATOM 4101 C ILE C 155 -26.328-131.405 -14.239 1.00 22.74 C ANISOU 4101 C ILE C 155 3004 3134 2503 576 115 394 C ATOM 4102 O ILE C 155 -26.857-131.112 -13.171 1.00 27.11 O ANISOU 4102 O ILE C 155 3522 3733 3045 597 130 408 O ATOM 4103 CB ILE C 155 -27.768-133.065 -15.392 1.00 23.42 C ANISOU 4103 CB ILE C 155 3050 3205 2644 548 88 388 C ATOM 4104 CG1 ILE C 155 -27.868-134.507 -15.858 1.00 22.25 C ANISOU 4104 CG1 ILE C 155 2905 3028 2522 556 96 394 C ATOM 4105 CG2 ILE C 155 -27.958-132.143 -16.567 1.00 34.25 C ANISOU 4105 CG2 ILE C 155 4432 4569 4014 491 41 363 C ATOM 4106 CD1 ILE C 155 -26.762-134.881 -16.793 1.00 31.71 C ANISOU 4106 CD1 ILE C 155 4153 4170 3725 555 97 381 C ATOM 4107 N ILE C 156 -25.649-130.541 -14.992 1.00 25.47 N ANISOU 4107 N ILE C 156 3389 3463 2826 537 92 375 N ATOM 4108 CA ILE C 156 -25.529-129.126 -14.667 1.00 17.83 C ANISOU 4108 CA ILE C 156 2427 2528 1818 504 80 367 C ATOM 4109 C ILE C 156 -25.694-128.254 -15.903 1.00 38.61 C ANISOU 4109 C ILE C 156 5071 5146 4453 434 22 345 C ATOM 4110 O ILE C 156 -25.585-128.737 -17.024 1.00 56.46 O ANISOU 4110 O ILE C 156 7346 7368 6738 420 -1 335 O ATOM 4111 CB ILE C 156 -24.188-128.794 -14.027 1.00 18.64 C ANISOU 4111 CB ILE C 156 2566 2617 1901 504 122 346 C ATOM 4112 CG1 ILE C 156 -23.053-129.326 -14.877 1.00 40.00 C ANISOU 4112 CG1 ILE C 156 5317 5258 4623 491 130 322 C ATOM 4113 CG2 ILE C 156 -24.087-129.398 -12.631 1.00 47.20 C ANISOU 4113 CG2 ILE C 156 6156 6246 5532 560 180 353 C ATOM 4114 CD1 ILE C 156 -21.705-129.073 -14.266 1.00 56.62 C ANISOU 4114 CD1 ILE C 156 7451 7344 6719 480 178 287 C ATOM 4115 N LEU C 157 -25.974-126.970 -15.682 1.00 32.26 N ANISOU 4115 N LEU C 157 4260 4371 3625 392 0 340 N ATOM 4116 CA LEU C 157 -26.079-125.983 -16.749 1.00 22.26 C ANISOU 4116 CA LEU C 157 3008 3088 2361 326 -56 326 C ATOM 4117 C LEU C 157 -24.912-125.010 -16.709 1.00 17.89 C ANISOU 4117 C LEU C 157 2503 2535 1759 293 -58 319 C ATOM 4118 O LEU C 157 -24.560-124.500 -15.648 1.00 39.85 O ANISOU 4118 O LEU C 157 5289 5351 4499 297 -26 320 O ATOM 4119 CB LEU C 157 -27.380-125.168 -16.636 1.00 47.66 C ANISOU 4119 CB LEU C 157 6188 6331 5590 292 -84 326 C ATOM 4120 CG LEU C 157 -28.723-125.909 -16.580 1.00 63.12 C ANISOU 4120 CG LEU C 157 8096 8301 7586 311 -81 328 C ATOM 4121 CD1 LEU C 157 -29.892-124.923 -16.755 1.00 52.37 C ANISOU 4121 CD1 LEU C 157 6713 6952 6232 267 -113 321 C ATOM 4122 CD2 LEU C 157 -28.786-127.037 -17.612 1.00 39.87 C ANISOU 4122 CD2 LEU C 157 5152 5320 4678 321 -89 321 C ATOM 4123 N ILE C 158 -24.328-124.734 -17.870 1.00 27.00 N ANISOU 4123 N ILE C 158 3690 3652 2916 257 -97 309 N ATOM 4124 CA ILE C 158 -23.294-123.715 -17.971 1.00 22.12 C ANISOU 4124 CA ILE C 158 3118 3035 2251 211 -109 301 C ATOM 4125 C ILE C 158 -23.889-122.413 -18.477 1.00 33.25 C ANISOU 4125 C ILE C 158 4517 4451 3665 144 -169 307 C ATOM 4126 O ILE C 158 -24.580-122.405 -19.492 1.00 58.93 O ANISOU 4126 O ILE C 158 7747 7681 6963 127 -214 311 O ATOM 4127 CB ILE C 158 -22.168-124.127 -18.932 1.00 30.80 C ANISOU 4127 CB ILE C 158 4264 4089 3351 204 -118 285 C ATOM 4128 CG1 ILE C 158 -21.471-125.394 -18.449 1.00 52.04 C ANISOU 4128 CG1 ILE C 158 6958 6754 6060 250 -52 267 C ATOM 4129 CG2 ILE C 158 -21.162-123.009 -19.044 1.00 20.60 C ANISOU 4129 CG2 ILE C 158 3011 2799 2017 140 -134 272 C ATOM 4130 CD1 ILE C 158 -20.234-125.742 -19.255 1.00 49.78 C ANISOU 4130 CD1 ILE C 158 6713 6422 5781 228 -49 238 C ATOM 4131 N GLU C 159 -23.609-121.317 -17.779 1.00 38.31 N ANISOU 4131 N GLU C 159 5175 5123 4260 104 -167 308 N ATOM 4132 CA GLU C 159 -24.114-120.003 -18.170 1.00 23.87 C ANISOU 4132 CA GLU C 159 3363 3273 2433 69 -213 301 C ATOM 4133 C GLU C 159 -23.084-119.177 -18.923 1.00 26.26 C ANISOU 4133 C GLU C 159 3663 3594 2720 41 -229 301 C ATOM 4134 O GLU C 159 -22.231-118.531 -18.332 1.00 40.27 O ANISOU 4134 O GLU C 159 5468 5383 4449 3 -215 294 O ATOM 4135 CB GLU C 159 -24.643-119.234 -16.954 1.00 28.51 C ANISOU 4135 CB GLU C 159 3942 3903 2988 58 -191 305 C ATOM 4136 CG GLU C 159 -25.969-119.789 -16.446 1.00 47.94 C ANISOU 4136 CG GLU C 159 6345 6384 5485 83 -177 313 C ATOM 4137 CD GLU C 159 -26.373-119.225 -15.099 1.00 83.65 C ANISOU 4137 CD GLU C 159 10847 10960 9977 81 -142 312 C ATOM 4138 OE1 GLU C 159 -25.700-119.539 -14.094 1.00 90.04 O ANISOU 4138 OE1 GLU C 159 11651 11810 10751 100 -91 308 O ATOM 4139 OE2 GLU C 159 -27.369-118.469 -15.044 1.00 96.07 O ANISOU 4139 OE2 GLU C 159 12407 12535 11561 66 -162 311 O ATOM 4140 N ASP C 160 -23.185-119.212 -20.242 1.00 25.33 N ANISOU 4140 N ASP C 160 3535 3439 2650 34 -270 298 N ATOM 4141 CA ASP C 160 -22.329-118.444 -21.121 1.00 18.76 C ANISOU 4141 CA ASP C 160 2729 2578 1823 -16 -306 290 C ATOM 4142 C ASP C 160 -23.103-118.076 -22.397 1.00 46.59 C ANISOU 4142 C ASP C 160 6225 6070 5407 -19 -352 289 C ATOM 4143 O ASP C 160 -23.580-118.960 -23.108 1.00 53.27 O ANISOU 4143 O ASP C 160 7049 6897 6295 11 -358 284 O ATOM 4144 CB ASP C 160 -21.108-119.274 -21.480 1.00 21.12 C ANISOU 4144 CB ASP C 160 3063 2854 2106 -21 -299 278 C ATOM 4145 CG ASP C 160 -20.071-118.498 -22.277 1.00 38.00 C ANISOU 4145 CG ASP C 160 5231 4969 4238 -75 -334 269 C ATOM 4146 OD1 ASP C 160 -18.939-119.013 -22.413 1.00 30.40 O ANISOU 4146 OD1 ASP C 160 4306 3994 3249 -88 -323 255 O ATOM 4147 OD2 ASP C 160 -20.371-117.391 -22.757 1.00 46.00 O ANISOU 4147 OD2 ASP C 160 6233 5976 5271 -105 -370 277 O ATOM 4148 N ASN C 161 -23.249-116.775 -22.658 1.00 40.64 N ANISOU 4148 N ASN C 161 5474 5309 4659 -59 -382 295 N ATOM 4149 CA ASN C 161 -23.768-116.273 -23.929 1.00 16.42 C ANISOU 4149 CA ASN C 161 2390 2203 1644 -73 -427 295 C ATOM 4150 C ASN C 161 -22.706-115.498 -24.671 1.00 28.02 C ANISOU 4150 C ASN C 161 3890 3645 3110 -123 -464 298 C ATOM 4151 O ASN C 161 -22.946-114.974 -25.747 1.00 54.70 O ANISOU 4151 O ASN C 161 7263 6990 6531 -140 -504 301 O ATOM 4152 CB ASN C 161 -24.956-115.358 -23.709 1.00 35.20 C ANISOU 4152 CB ASN C 161 4747 4589 4037 -80 -435 304 C ATOM 4153 CG ASN C 161 -25.416-115.354 -22.296 1.00 51.64 C ANISOU 4153 CG ASN C 161 6824 6717 6079 -63 -395 308 C ATOM 4154 OD1 ASN C 161 -26.308-116.109 -21.921 1.00 68.08 O ANISOU 4154 OD1 ASN C 161 8880 8816 8170 -19 -372 304 O ATOM 4155 ND2 ASN C 161 -24.808-114.506 -21.486 1.00 55.82 N ANISOU 4155 ND2 ASN C 161 7380 7268 6563 -99 -388 315 N ATOM 4156 N THR C 162 -21.518-115.435 -24.089 1.00 42.02 N ANISOU 4156 N THR C 162 5697 5436 4833 -148 -448 296 N ATOM 4157 CA THR C 162 -20.375-114.766 -24.700 1.00 51.13 C ANISOU 4157 CA THR C 162 6882 6571 5973 -199 -479 299 C ATOM 4158 C THR C 162 -19.647-115.618 -25.749 1.00 33.66 C ANISOU 4158 C THR C 162 4679 4327 3782 -191 -497 285 C ATOM 4159 O THR C 162 -19.464-115.201 -26.890 1.00 31.10 O ANISOU 4159 O THR C 162 4356 3969 3492 -211 -541 288 O ATOM 4160 CB THR C 162 -19.351-114.371 -23.616 1.00 76.76 C ANISOU 4160 CB THR C 162 10162 9853 9151 -236 -450 297 C ATOM 4161 OG1 THR C 162 -20.006-113.616 -22.589 1.00 86.09 O ANISOU 4161 OG1 THR C 162 11334 11065 10309 -245 -432 307 O ATOM 4162 CG2 THR C 162 -18.206-113.546 -24.210 1.00 76.38 C ANISOU 4162 CG2 THR C 162 10143 9791 9085 -298 -483 303 C ATOM 4163 N SER C 163 -19.224-116.809 -25.352 1.00 32.84 N ANISOU 4163 N SER C 163 4586 4233 3658 -162 -462 269 N ATOM 4164 CA SER C 163 -18.399-117.638 -26.216 1.00 42.53 C ANISOU 4164 CA SER C 163 5832 5433 4895 -160 -474 253 C ATOM 4165 C SER C 163 -19.159-117.937 -27.472 1.00 32.72 C ANISOU 4165 C SER C 163 4559 4153 3721 -137 -510 248 C ATOM 4166 O SER C 163 -20.377-117.921 -27.468 1.00 35.39 O ANISOU 4166 O SER C 163 4861 4492 4094 -111 -508 253 O ATOM 4167 CB SER C 163 -18.057-118.940 -25.517 1.00 39.94 C ANISOU 4167 CB SER C 163 5523 5116 4537 -127 -427 238 C ATOM 4168 OG SER C 163 -17.604-118.670 -24.211 1.00 51.19 O ANISOU 4168 OG SER C 163 6970 6578 5901 -142 -384 240 O ATOM 4169 N GLU C 164 -18.440-118.209 -28.547 1.00 33.03 N ANISOU 4169 N GLU C 164 4610 4162 3778 -149 -540 236 N ATOM 4170 CA GLU C 164 -19.063-118.667 -29.774 1.00 23.49 C ANISOU 4170 CA GLU C 164 3374 2917 2635 -127 -569 224 C ATOM 4171 C GLU C 164 -19.637-120.030 -29.463 1.00 41.29 C ANISOU 4171 C GLU C 164 5615 5175 4898 -78 -535 209 C ATOM 4172 O GLU C 164 -19.071-120.773 -28.661 1.00 42.95 O ANISOU 4172 O GLU C 164 5852 5401 5065 -66 -499 204 O ATOM 4173 CB GLU C 164 -18.020-118.780 -30.876 1.00 43.25 C ANISOU 4173 CB GLU C 164 5896 5392 5146 -150 -603 211 C ATOM 4174 CG GLU C 164 -18.555-119.224 -32.216 1.00 59.71 C ANISOU 4174 CG GLU C 164 7952 7437 7298 -130 -634 193 C ATOM 4175 CD GLU C 164 -17.442-119.476 -33.229 1.00 65.98 C ANISOU 4175 CD GLU C 164 8766 8208 8096 -148 -664 177 C ATOM 4176 OE1 GLU C 164 -16.264-119.187 -32.923 1.00 60.22 O ANISOU 4176 OE1 GLU C 164 8071 7494 7315 -182 -662 182 O ATOM 4177 OE2 GLU C 164 -17.748-119.965 -34.334 1.00 67.96 O ANISOU 4177 OE2 GLU C 164 8994 8427 8399 -131 -687 158 O ATOM 4178 N VAL C 165 -20.776-120.349 -30.066 1.00 32.15 N ANISOU 4178 N VAL C 165 4418 4003 3796 -52 -543 201 N ATOM 4179 CA VAL C 165 -21.410-121.622 -29.824 1.00 26.88 C ANISOU 4179 CA VAL C 165 3734 3341 3140 -9 -513 189 C ATOM 4180 C VAL C 165 -20.432-122.703 -30.265 1.00 32.23 C ANISOU 4180 C VAL C 165 4444 3996 3808 -1 -514 167 C ATOM 4181 O VAL C 165 -19.745-122.525 -31.269 1.00 42.33 O ANISOU 4181 O VAL C 165 5733 5247 5102 -24 -550 153 O ATOM 4182 CB VAL C 165 -22.765-121.737 -30.595 1.00 30.28 C ANISOU 4182 CB VAL C 165 4117 3758 3632 6 -526 179 C ATOM 4183 CG1 VAL C 165 -23.357-123.154 -30.479 1.00 34.60 C ANISOU 4183 CG1 VAL C 165 4646 4309 4191 46 -497 165 C ATOM 4184 CG2 VAL C 165 -23.753-120.722 -30.084 1.00 26.34 C ANISOU 4184 CG2 VAL C 165 3594 3280 3136 0 -521 198 C ATOM 4185 N GLY C 166 -20.352-123.801 -29.505 1.00 32.73 N ANISOU 4185 N GLY C 166 4524 4068 3843 32 -474 165 N ATOM 4186 CA GLY C 166 -19.503-124.936 -29.841 1.00 25.53 C ANISOU 4186 CA GLY C 166 3652 3130 2916 45 -468 142 C ATOM 4187 C GLY C 166 -18.058-124.825 -29.381 1.00 43.21 C ANISOU 4187 C GLY C 166 5954 5372 5093 21 -454 138 C ATOM 4188 O GLY C 166 -17.164-125.489 -29.912 1.00 39.55 O ANISOU 4188 O GLY C 166 5513 4885 4627 16 -442 107 O ATOM 4189 N THR C 167 -17.816-123.978 -28.390 1.00 32.65 N ANISOU 4189 N THR C 167 4627 4064 3714 1 -434 159 N ATOM 4190 CA THR C 167 -16.466-123.777 -27.897 1.00 24.60 C ANISOU 4190 CA THR C 167 3662 3053 2632 -33 -409 150 C ATOM 4191 C THR C 167 -16.399-123.877 -26.387 1.00 33.23 C ANISOU 4191 C THR C 167 4761 4175 3692 -17 -336 156 C ATOM 4192 O THR C 167 -15.514-123.286 -25.759 1.00 30.39 O ANISOU 4192 O THR C 167 4429 3835 3283 -54 -313 151 O ATOM 4193 CB THR C 167 -15.947-122.419 -28.298 1.00 35.34 C ANISOU 4193 CB THR C 167 5017 4425 3985 -91 -451 159 C ATOM 4194 OG1 THR C 167 -16.450-121.439 -27.385 1.00 49.22 O ANISOU 4194 OG1 THR C 167 6756 6217 5730 -102 -439 184 O ATOM 4195 CG2 THR C 167 -16.419-122.093 -29.707 1.00 44.15 C ANISOU 4195 CG2 THR C 167 6093 5514 5168 -96 -510 156 C ATOM 4196 N GLN C 168 -17.338-124.605 -25.795 1.00 17.29 N ANISOU 4196 N GLN C 168 2163 2055 2353 15 146 27 N ATOM 4197 CA GLN C 168 -17.201-124.922 -24.387 1.00 19.93 C ANISOU 4197 CA GLN C 168 2523 2432 2618 24 114 36 C ATOM 4198 C GLN C 168 -16.126-125.995 -24.265 1.00 24.96 C ANISOU 4198 C GLN C 168 3171 3069 3244 31 119 41 C ATOM 4199 O GLN C 168 -15.883-126.759 -25.194 1.00 32.39 O ANISOU 4199 O GLN C 168 4099 4007 4201 27 173 37 O ATOM 4200 CB GLN C 168 -18.519-125.385 -23.772 1.00 15.94 C ANISOU 4200 CB GLN C 168 2043 1922 2091 24 124 29 C ATOM 4201 CG GLN C 168 -19.593-124.325 -23.714 1.00 30.70 C ANISOU 4201 CG GLN C 168 3889 3818 3956 17 125 22 C ATOM 4202 CD GLN C 168 -19.199-123.167 -22.835 1.00 35.89 C ANISOU 4202 CD GLN C 168 4526 4497 4614 16 53 35 C ATOM 4203 OE1 GLN C 168 -18.834-123.356 -21.682 1.00 35.01 O ANISOU 4203 OE1 GLN C 168 4421 4410 4472 14 31 30 O ATOM 4204 NE2 GLN C 168 -19.254-121.956 -23.382 1.00 22.58 N ANISOU 4204 NE2 GLN C 168 2775 2803 3002 -1 -7 55 N ATOM 4205 N ARG C 169 -15.413-126.020 -23.155 1.00 34.95 N ANISOU 4205 N ARG C 169 4432 4365 4481 32 85 43 N ATOM 4206 CA ARG C 169 -14.339-126.974 -22.927 1.00 29.13 C ANISOU 4206 CA ARG C 169 3688 3644 3735 35 100 44 C ATOM 4207 C ARG C 169 -14.698-127.935 -21.806 1.00 35.28 C ANISOU 4207 C ARG C 169 4475 4429 4500 40 96 45 C ATOM 4208 O ARG C 169 -15.431-127.562 -20.916 1.00 26.81 O ANISOU 4208 O ARG C 169 3407 3355 3425 39 69 45 O ATOM 4209 CB ARG C 169 -13.070-126.244 -22.516 1.00 35.11 C ANISOU 4209 CB ARG C 169 4444 4403 4492 32 66 45 C ATOM 4210 CG ARG C 169 -12.470-125.327 -23.515 1.00 63.22 C ANISOU 4210 CG ARG C 169 7996 7952 8074 29 74 49 C ATOM 4211 CD ARG C 169 -11.019-125.062 -23.211 1.00 83.25 C ANISOU 4211 CD ARG C 169 10523 10506 10602 21 48 45 C ATOM 4212 NE ARG C 169 -10.191-125.336 -24.376 1.00 93.56 N ANISOU 4212 NE ARG C 169 11828 11811 11908 23 49 47 N ATOM 4213 CZ ARG C 169 -9.324-126.329 -24.481 1.00114.54 C ANISOU 4213 CZ ARG C 169 14491 14480 14547 21 39 41 C ATOM 4214 NH1 ARG C 169 -9.115-127.168 -23.488 1.00129.09 N ANISOU 4214 NH1 ARG C 169 16338 16333 16377 19 30 34 N ATOM 4215 NH2 ARG C 169 -8.655-126.477 -25.593 1.00120.42 N ANISOU 4215 NH2 ARG C 169 15235 15224 15294 23 42 44 N ATOM 4216 N VAL C 170 -14.166-129.157 -21.850 1.00 31.40 N ANISOU 4216 N VAL C 170 4001 3909 4019 53 105 57 N ATOM 4217 CA VAL C 170 -14.166-130.052 -20.696 1.00 30.51 C ANISOU 4217 CA VAL C 170 3889 3804 3898 60 101 63 C ATOM 4218 C VAL C 170 -13.240-129.498 -19.613 1.00 32.25 C ANISOU 4218 C VAL C 170 4092 4049 4111 53 74 60 C ATOM 4219 O VAL C 170 -12.049-129.298 -19.844 1.00 40.40 O ANISOU 4219 O VAL C 170 5112 5098 5139 46 78 54 O ATOM 4220 CB VAL C 170 -13.691-131.439 -21.080 1.00 40.88 C ANISOU 4220 CB VAL C 170 5205 5123 5206 66 143 66 C ATOM 4221 CG1 VAL C 170 -13.709-132.362 -19.861 1.00 47.22 C ANISOU 4221 CG1 VAL C 170 6018 5911 6014 82 125 81 C ATOM 4222 CG2 VAL C 170 -14.547-131.977 -22.218 1.00 41.19 C ANISOU 4222 CG2 VAL C 170 5266 5131 5253 66 187 64 C ATOM 4223 N LEU C 171 -13.793-129.258 -18.430 1.00 33.00 N ANISOU 4223 N LEU C 171 4179 4167 4195 43 69 60 N ATOM 4224 CA LEU C 171 -13.077-128.568 -17.361 1.00 31.51 C ANISOU 4224 CA LEU C 171 3975 3985 4011 46 48 53 C ATOM 4225 C LEU C 171 -13.377-129.216 -16.008 1.00 29.76 C ANISOU 4225 C LEU C 171 3752 3776 3781 45 57 74 C ATOM 4226 O LEU C 171 -14.421-129.826 -15.841 1.00 47.89 O ANISOU 4226 O LEU C 171 6048 6072 6074 52 64 80 O ATOM 4227 CB LEU C 171 -13.478-127.091 -17.322 1.00 28.18 C ANISOU 4227 CB LEU C 171 3556 3566 3585 29 30 47 C ATOM 4228 CG LEU C 171 -12.634-126.033 -18.026 1.00 52.99 C ANISOU 4228 CG LEU C 171 6699 6708 6726 20 22 36 C ATOM 4229 CD1 LEU C 171 -11.521-125.549 -17.111 1.00 70.64 C ANISOU 4229 CD1 LEU C 171 8931 8948 8960 17 20 40 C ATOM 4230 CD2 LEU C 171 -12.075-126.544 -19.332 1.00 53.86 C ANISOU 4230 CD2 LEU C 171 6808 6817 6839 22 35 34 C ATOM 4231 N PRO C 172 -12.456-129.077 -15.036 1.00 38.47 N ANISOU 4231 N PRO C 172 4848 4887 4884 46 54 82 N ATOM 4232 CA PRO C 172 -12.655-129.602 -13.682 1.00 31.55 C ANISOU 4232 CA PRO C 172 3943 4029 4015 65 60 95 C ATOM 4233 C PRO C 172 -13.804-128.922 -12.971 1.00 40.11 C ANISOU 4233 C PRO C 172 5013 5128 5099 59 51 105 C ATOM 4234 O PRO C 172 -13.825-127.696 -12.928 1.00 41.79 O ANISOU 4234 O PRO C 172 5241 5335 5303 42 36 112 O ATOM 4235 CB PRO C 172 -11.364-129.215 -12.970 1.00 46.91 C ANISOU 4235 CB PRO C 172 5901 5972 5952 59 54 114 C ATOM 4236 CG PRO C 172 -10.833-128.060 -13.743 1.00 44.32 C ANISOU 4236 CG PRO C 172 5579 5635 5627 46 44 93 C ATOM 4237 CD PRO C 172 -11.170-128.371 -15.160 1.00 41.42 C ANISOU 4237 CD PRO C 172 5212 5262 5263 42 51 69 C ATOM 4238 N GLY C 173 -14.730-129.699 -12.412 1.00 43.73 N ANISOU 4238 N GLY C 173 5459 5601 5556 67 56 121 N ATOM 4239 CA GLY C 173 -15.868-129.144 -11.698 1.00 29.58 C ANISOU 4239 CA GLY C 173 3671 3824 3745 52 40 151 C ATOM 4240 C GLY C 173 -15.527-129.003 -10.236 1.00 39.34 C ANISOU 4240 C GLY C 173 4883 5089 4976 51 38 186 C ATOM 4241 O GLY C 173 -14.358-129.084 -9.873 1.00 38.78 O ANISOU 4241 O GLY C 173 4813 5014 4908 59 45 190 O ATOM 4242 N THR C 174 -16.538-128.816 -9.395 1.00 28.89 N ANISOU 4242 N THR C 174 3536 3798 3644 38 26 215 N ATOM 4243 CA THR C 174 -16.300-128.623 -7.973 1.00 35.81 C ANISOU 4243 CA THR C 174 4385 4707 4513 33 23 256 C ATOM 4244 C THR C 174 -16.352-129.918 -7.155 1.00 42.15 C ANISOU 4244 C THR C 174 5124 5550 5341 53 35 257 C ATOM 4245 O THR C 174 -16.103-129.913 -5.958 1.00 47.46 O ANISOU 4245 O THR C 174 5767 6253 6012 53 35 290 O ATOM 4246 CB THR C 174 -17.314-127.669 -7.390 1.00 43.02 C ANISOU 4246 CB THR C 174 5227 5666 5453 0 0 261 C ATOM 4247 OG1 THR C 174 -18.598-128.302 -7.398 1.00 49.47 O ANISOU 4247 OG1 THR C 174 6088 6489 6222 -14 -9 293 O ATOM 4248 CG2 THR C 174 -17.354-126.382 -8.205 1.00 38.58 C ANISOU 4248 CG2 THR C 174 4682 5080 4896 -20 -14 243 C ATOM 4249 N LEU C 175 -16.685-131.025 -7.798 1.00 47.46 N ANISOU 4249 N LEU C 175 5859 6196 5977 62 41 265 N ATOM 4250 CA LEU C 175 -16.845-132.280 -7.086 1.00 30.62 C ANISOU 4250 CA LEU C 175 3713 4090 3834 75 49 290 C ATOM 4251 C LEU C 175 -15.490-132.908 -6.783 1.00 51.07 C ANISOU 4251 C LEU C 175 6258 6681 6466 108 73 267 C ATOM 4252 O LEU C 175 -14.575-132.845 -7.598 1.00 73.58 O ANISOU 4252 O LEU C 175 9140 9496 9323 116 82 241 O ATOM 4253 CB LEU C 175 -17.704-133.247 -7.907 1.00 33.44 C ANISOU 4253 CB LEU C 175 4027 4456 4222 88 56 252 C ATOM 4254 CG LEU C 175 -18.716-134.067 -7.117 1.00 43.21 C ANISOU 4254 CG LEU C 175 5229 5744 5446 78 47 282 C ATOM 4255 CD1 LEU C 175 -19.623-133.144 -6.321 1.00 41.11 C ANISOU 4255 CD1 LEU C 175 4995 5503 5123 33 19 334 C ATOM 4256 CD2 LEU C 175 -19.527-134.956 -8.047 1.00 53.65 C ANISOU 4256 CD2 LEU C 175 6617 7048 6719 74 43 292 C ATOM 4257 N VAL C 176 -15.358-133.496 -5.598 1.00 43.88 N ANISOU 4257 N VAL C 176 5377 5787 5508 108 72 330 N ATOM 4258 CA VAL C 176 -14.186-134.286 -5.278 1.00 30.35 C ANISOU 4258 CA VAL C 176 3611 4082 3839 143 97 305 C ATOM 4259 C VAL C 176 -14.591-135.699 -4.930 1.00 44.29 C ANISOU 4259 C VAL C 176 5362 5868 5597 159 105 323 C ATOM 4260 O VAL C 176 -15.775-135.983 -4.741 1.00 71.33 O ANISOU 4260 O VAL C 176 8833 9305 8964 135 87 370 O ATOM 4261 CB VAL C 176 -13.309-133.746 -4.117 1.00 26.42 C ANISOU 4261 CB VAL C 176 3157 3584 3299 135 92 364 C ATOM 4262 CG1 VAL C 176 -12.874-132.306 -4.302 1.00 35.45 C ANISOU 4262 CG1 VAL C 176 4304 4713 4451 120 83 350 C ATOM 4263 CG2 VAL C 176 -13.837-134.118 -2.742 1.00 53.64 C ANISOU 4263 CG2 VAL C 176 6569 7080 6732 137 91 412 C ATOM 4264 N SER C 177 -13.609-136.589 -4.846 1.00 32.68 N ANISOU 4264 N SER C 177 3903 4387 4129 181 123 324 N ATOM 4265 CA SER C 177 -13.912-137.995 -4.658 1.00 42.00 C ANISOU 4265 CA SER C 177 5073 5582 5302 198 132 339 C ATOM 4266 C SER C 177 -13.483-138.505 -3.288 1.00 52.35 C ANISOU 4266 C SER C 177 6353 6928 6610 213 141 376 C ATOM 4267 O SER C 177 -12.322-138.382 -2.906 1.00 69.09 O ANISOU 4267 O SER C 177 8479 9036 8735 226 153 379 O ATOM 4268 CB SER C 177 -13.280-138.822 -5.773 1.00 42.63 C ANISOU 4268 CB SER C 177 5247 5610 5339 186 146 346 C ATOM 4269 OG SER C 177 -13.506-140.205 -5.572 1.00 38.92 O ANISOU 4269 OG SER C 177 4712 5162 4912 236 143 334 O ATOM 4270 N ASP C 178 -14.439-139.059 -2.548 1.00 32.47 N ANISOU 4270 N ASP C 178 3799 4456 4083 210 135 406 N ATOM 4271 CA ASP C 178 -14.197-139.562 -1.201 1.00 43.51 C ANISOU 4271 CA ASP C 178 5252 5870 5410 205 131 492 C ATOM 4272 C ASP C 178 -13.198-140.699 -1.219 1.00 34.62 C ANISOU 4272 C ASP C 178 4051 4750 4353 253 164 447 C ATOM 4273 O ASP C 178 -12.469-140.901 -0.255 1.00 54.08 O ANISOU 4273 O ASP C 178 6594 7204 6750 248 162 522 O ATOM 4274 CB ASP C 178 -15.493-140.066 -0.564 1.00 56.79 C ANISOU 4274 CB ASP C 178 6899 7606 7072 191 117 525 C ATOM 4275 CG ASP C 178 -16.503-138.963 -0.342 1.00 62.73 C ANISOU 4275 CG ASP C 178 7531 8409 7892 173 104 486 C ATOM 4276 OD1 ASP C 178 -16.111-137.888 0.158 1.00 60.62 O ANISOU 4276 OD1 ASP C 178 7359 8116 7556 154 94 542 O ATOM 4277 OD2 ASP C 178 -17.692-139.178 -0.663 1.00 72.91 O ANISOU 4277 OD2 ASP C 178 8809 9723 9170 147 85 485 O ATOM 4278 N LYS C 179 -13.182-141.445 -2.318 1.00 39.68 N ANISOU 4278 N LYS C 179 4805 5338 4932 237 155 467 N ATOM 4279 CA LYS C 179 -12.269-142.575 -2.470 1.00 47.92 C ANISOU 4279 CA LYS C 179 5861 6371 5976 250 189 463 C ATOM 4280 C LYS C 179 -10.792-142.166 -2.538 1.00 53.68 C ANISOU 4280 C LYS C 179 6611 7067 6717 257 202 449 C ATOM 4281 O LYS C 179 -10.000-142.515 -1.648 1.00 38.36 O ANISOU 4281 O LYS C 179 4588 5144 4842 319 198 434 O ATOM 4282 CB LYS C 179 -12.638-143.385 -3.715 1.00 34.16 C ANISOU 4282 CB LYS C 179 4138 4607 4235 250 190 438 C ATOM 4283 CG LYS C 179 -11.535-144.300 -4.200 1.00 43.09 C ANISOU 4283 CG LYS C 179 5293 5709 5372 267 210 429 C ATOM 4284 CD LYS C 179 -11.456-145.562 -3.368 1.00 62.68 C ANISOU 4284 CD LYS C 179 7755 8218 7841 285 221 464 C ATOM 4285 CE LYS C 179 -10.544-146.589 -4.033 1.00 84.42 C ANISOU 4285 CE LYS C 179 10464 10943 10668 349 219 415 C ATOM 4286 NZ LYS C 179 -10.889-146.791 -5.476 1.00 83.87 N ANISOU 4286 NZ LYS C 179 10486 10843 10536 292 237 423 N ATOM 4287 N ASP C 180 -10.434-141.412 -3.582 1.00 45.38 N ANISOU 4287 N ASP C 180 5585 5980 5678 244 197 412 N ATOM 4288 CA ASP C 180 -9.024-141.219 -3.945 1.00 48.78 C ANISOU 4288 CA ASP C 180 5978 6380 6174 290 189 362 C ATOM 4289 C ASP C 180 -8.577-139.772 -4.138 1.00 35.66 C ANISOU 4289 C ASP C 180 4326 4705 4518 272 180 344 C ATOM 4290 O ASP C 180 -7.496-139.532 -4.670 1.00 32.01 O ANISOU 4290 O ASP C 180 3886 4215 4060 269 183 326 O ATOM 4291 CB ASP C 180 -8.697-142.004 -5.224 1.00 64.52 C ANISOU 4291 CB ASP C 180 8056 8341 8116 247 213 369 C ATOM 4292 CG ASP C 180 -9.330-141.382 -6.465 1.00 66.19 C ANISOU 4292 CG ASP C 180 8237 8529 8385 269 184 308 C ATOM 4293 OD1 ASP C 180 -8.960-141.764 -7.600 1.00 72.41 O ANISOU 4293 OD1 ASP C 180 9092 9292 9128 226 205 315 O ATOM 4294 OD2 ASP C 180 -10.199-140.505 -6.298 1.00 41.30 O ANISOU 4294 OD2 ASP C 180 5119 5390 5181 217 186 335 O ATOM 4295 N GLY C 181 -9.398-138.811 -3.724 1.00 28.43 N ANISOU 4295 N GLY C 181 3390 3810 3601 258 167 351 N ATOM 4296 CA GLY C 181 -9.037-137.410 -3.868 1.00 21.60 C ANISOU 4296 CA GLY C 181 2532 2935 2741 241 157 336 C ATOM 4297 C GLY C 181 -9.073-136.857 -5.294 1.00 35.20 C ANISOU 4297 C GLY C 181 4333 4618 4422 187 161 325 C ATOM 4298 O GLY C 181 -8.680-135.716 -5.535 1.00 32.30 O ANISOU 4298 O GLY C 181 3925 4244 4103 205 139 284 O ATOM 4299 N SER C 182 -9.557-137.644 -6.253 1.00 40.23 N ANISOU 4299 N SER C 182 4939 5243 5102 221 149 283 N ATOM 4300 CA SER C 182 -9.655-137.133 -7.614 1.00 30.73 C ANISOU 4300 CA SER C 182 3764 4011 3903 203 141 251 C ATOM 4301 C SER C 182 -10.768-136.113 -7.752 1.00 34.78 C ANISOU 4301 C SER C 182 4307 4528 4378 156 137 265 C ATOM 4302 O SER C 182 -11.661-136.030 -6.921 1.00 43.19 O ANISOU 4302 O SER C 182 5309 5626 5476 185 121 264 O ATOM 4303 CB SER C 182 -9.818-138.238 -8.640 1.00 19.54 C ANISOU 4303 CB SER C 182 2367 2573 2486 209 149 240 C ATOM 4304 OG SER C 182 -10.968-139.006 -8.368 1.00 35.71 O ANISOU 4304 OG SER C 182 4439 4641 4488 186 165 278 O ATOM 4305 N GLN C 183 -10.678-135.340 -8.824 1.00 47.90 N ANISOU 4305 N GLN C 183 5952 6167 6080 168 118 216 N ATOM 4306 CA GLN C 183 -11.522-134.195 -9.062 1.00 35.10 C ANISOU 4306 CA GLN C 183 4361 4546 4430 125 113 224 C ATOM 4307 C GLN C 183 -12.472-134.504 -10.220 1.00 42.81 C ANISOU 4307 C GLN C 183 5323 5509 5435 145 103 187 C ATOM 4308 O GLN C 183 -12.093-135.209 -11.162 1.00 28.95 O ANISOU 4308 O GLN C 183 3614 3733 3655 126 122 192 O ATOM 4309 CB GLN C 183 -10.622-133.009 -9.425 1.00 32.91 C ANISOU 4309 CB GLN C 183 4062 4257 4187 134 96 188 C ATOM 4310 CG GLN C 183 -11.326-131.689 -9.505 1.00 33.49 C ANISOU 4310 CG GLN C 183 4162 4326 4238 101 81 199 C ATOM 4311 CD GLN C 183 -11.613-131.120 -8.134 1.00 61.19 C ANISOU 4311 CD GLN C 183 7645 7864 7742 100 77 230 C ATOM 4312 OE1 GLN C 183 -10.757-131.172 -7.249 1.00 75.98 O ANISOU 4312 OE1 GLN C 183 9465 9763 9641 119 91 226 O ATOM 4313 NE2 GLN C 183 -12.821-130.582 -7.942 1.00 48.31 N ANISOU 4313 NE2 GLN C 183 5959 6262 6134 97 72 216 N ATOM 4314 N SER C 184 -13.691-133.972 -10.153 1.00 38.31 N ANISOU 4314 N SER C 184 4773 4948 4835 114 101 205 N ATOM 4315 CA SER C 184 -14.676-134.178 -11.196 1.00 35.32 C ANISOU 4315 CA SER C 184 4380 4557 4483 133 93 173 C ATOM 4316 C SER C 184 -14.278-133.407 -12.437 1.00 23.20 C ANISOU 4316 C SER C 184 2892 2992 2931 100 98 158 C ATOM 4317 O SER C 184 -13.520-132.454 -12.358 1.00 51.03 O ANISOU 4317 O SER C 184 6415 6514 6460 90 88 150 O ATOM 4318 CB SER C 184 -16.061-133.731 -10.724 1.00 32.61 C ANISOU 4318 CB SER C 184 4045 4236 4108 104 88 200 C ATOM 4319 OG SER C 184 -16.111-132.329 -10.559 1.00 32.61 O ANISOU 4319 OG SER C 184 4007 4248 4137 98 72 176 O ATOM 4320 N LEU C 185 -14.774-133.845 -13.585 1.00 32.78 N ANISOU 4320 N LEU C 185 4106 4181 4166 123 98 132 N ATOM 4321 CA LEU C 185 -14.696-133.057 -14.809 1.00 30.04 C ANISOU 4321 CA LEU C 185 3779 3813 3822 109 94 110 C ATOM 4322 C LEU C 185 -16.119-132.705 -15.289 1.00 27.22 C ANISOU 4322 C LEU C 185 3440 3455 3447 88 103 111 C ATOM 4323 O LEU C 185 -17.091-133.400 -14.979 1.00 37.28 O ANISOU 4323 O LEU C 185 4705 4725 4736 118 102 111 O ATOM 4324 CB LEU C 185 -13.924-133.819 -15.893 1.00 29.27 C ANISOU 4324 CB LEU C 185 3710 3702 3710 95 120 116 C ATOM 4325 CG LEU C 185 -12.395-133.910 -15.789 1.00 36.82 C ANISOU 4325 CG LEU C 185 4652 4651 4686 113 109 108 C ATOM 4326 CD1 LEU C 185 -11.794-134.630 -16.997 1.00 33.04 C ANISOU 4326 CD1 LEU C 185 4191 4152 4212 118 125 106 C ATOM 4327 CD2 LEU C 185 -11.764-132.541 -15.652 1.00 32.04 C ANISOU 4327 CD2 LEU C 185 4048 4060 4066 78 98 106 C ATOM 4328 N VAL C 186 -16.228-131.623 -16.045 1.00 37.63 N ANISOU 4328 N VAL C 186 4756 4757 4783 89 85 86 N ATOM 4329 CA VAL C 186 -17.505-131.169 -16.556 1.00 10.81 C ANISOU 4329 CA VAL C 186 1377 1358 1372 70 95 83 C ATOM 4330 C VAL C 186 -17.473-131.216 -18.061 1.00 33.75 C ANISOU 4330 C VAL C 186 4307 4223 4294 81 106 65 C ATOM 4331 O VAL C 186 -16.638-130.560 -18.697 1.00 25.99 O ANISOU 4331 O VAL C 186 3317 3257 3302 59 107 65 O ATOM 4332 CB VAL C 186 -17.797-129.742 -16.100 1.00 26.89 C ANISOU 4332 CB VAL C 186 3390 3407 3422 67 62 70 C ATOM 4333 CG1 VAL C 186 -19.144-129.281 -16.641 1.00 39.32 C ANISOU 4333 CG1 VAL C 186 4982 4974 4984 53 70 65 C ATOM 4334 CG2 VAL C 186 -17.789-129.674 -14.580 1.00 28.70 C ANISOU 4334 CG2 VAL C 186 3587 3670 3650 65 50 91 C ATOM 4335 N TYR C 187 -18.385-131.988 -18.641 1.00 26.65 N ANISOU 4335 N TYR C 187 3446 3287 3393 80 136 66 N ATOM 4336 CA TYR C 187 -18.363-132.204 -20.072 1.00 26.35 C ANISOU 4336 CA TYR C 187 3437 3213 3362 70 170 56 C ATOM 4337 C TYR C 187 -19.550-131.510 -20.705 1.00 31.80 C ANISOU 4337 C TYR C 187 4140 3916 4028 44 204 34 C ATOM 4338 O TYR C 187 -20.683-131.928 -20.510 1.00 49.41 O ANISOU 4338 O TYR C 187 6404 6126 6244 28 227 19 O ATOM 4339 CB TYR C 187 -18.395-133.709 -20.404 1.00 26.66 C ANISOU 4339 CB TYR C 187 3493 3257 3381 65 230 51 C ATOM 4340 CG TYR C 187 -17.290-134.516 -19.777 1.00 34.84 C ANISOU 4340 CG TYR C 187 4508 4310 4419 85 218 69 C ATOM 4341 CD1 TYR C 187 -16.177-134.908 -20.512 1.00 48.84 C ANISOU 4341 CD1 TYR C 187 6279 6079 6201 87 229 73 C ATOM 4342 CD2 TYR C 187 -17.356-134.893 -18.447 1.00 42.58 C ANISOU 4342 CD2 TYR C 187 5485 5281 5415 109 177 89 C ATOM 4343 CE1 TYR C 187 -15.154-135.662 -19.926 1.00 15.82 C ANISOU 4343 CE1 TYR C 187 2082 1912 2018 101 221 87 C ATOM 4344 CE2 TYR C 187 -16.337-135.641 -17.857 1.00 40.39 C ANISOU 4344 CE2 TYR C 187 5181 5050 5114 108 189 107 C ATOM 4345 CZ TYR C 187 -15.252-136.017 -18.602 1.00 20.90 C ANISOU 4345 CZ TYR C 187 2715 2573 2652 107 201 108 C ATOM 4346 OH TYR C 187 -14.262-136.735 -18.006 1.00 53.97 O ANISOU 4346 OH TYR C 187 6892 6775 6839 118 196 122 O ATOM 4347 N PRO C 188 -19.298-130.437 -21.470 1.00 34.96 N ANISOU 4347 N PRO C 188 4525 4321 4437 39 196 31 N ATOM 4348 CA PRO C 188 -20.424-129.871 -22.195 1.00 21.84 C ANISOU 4348 CA PRO C 188 2901 2600 2796 18 205 14 C ATOM 4349 C PRO C 188 -20.983-130.966 -23.071 1.00 9.90 C ANISOU 4349 C PRO C 188 1409 1088 1267 -10 291 -8 C ATOM 4350 O PRO C 188 -20.215-131.664 -23.700 1.00 15.66 O ANISOU 4350 O PRO C 188 2152 1751 2046 -10 290 -8 O ATOM 4351 CB PRO C 188 -19.772-128.792 -23.051 1.00 24.26 C ANISOU 4351 CB PRO C 188 3180 2918 3121 20 196 18 C ATOM 4352 CG PRO C 188 -18.551-128.441 -22.353 1.00 19.24 C ANISOU 4352 CG PRO C 188 2508 2323 2478 38 149 34 C ATOM 4353 CD PRO C 188 -18.053-129.699 -21.737 1.00 43.20 C ANISOU 4353 CD PRO C 188 5536 5385 5492 45 168 39 C ATOM 4354 N LEU C 189 -22.303-131.103 -23.104 1.00 13.38 N ANISOU 4354 N LEU C 189 1883 1511 1690 -46 323 -34 N ATOM 4355 CA LEU C 189 -22.949-132.126 -23.892 1.00 7.74 C ANISOU 4355 CA LEU C 189 1224 694 1023 -107 380 -79 C ATOM 4356 C LEU C 189 -23.632-131.516 -25.098 1.00 25.42 C ANISOU 4356 C LEU C 189 3455 2909 3296 -164 456 -123 C ATOM 4357 O LEU C 189 -23.364-131.924 -26.229 1.00 36.58 O ANISOU 4357 O LEU C 189 4846 4288 4764 -203 547 -173 O ATOM 4358 CB LEU C 189 -23.956-132.887 -23.044 1.00 10.40 C ANISOU 4358 CB LEU C 189 1636 1006 1309 -158 449 -111 C ATOM 4359 CG LEU C 189 -23.337-133.628 -21.877 1.00 23.64 C ANISOU 4359 CG LEU C 189 3324 2693 2965 -118 423 -80 C ATOM 4360 CD1 LEU C 189 -24.416-134.238 -21.021 1.00 28.64 C ANISOU 4360 CD1 LEU C 189 3988 3378 3517 -174 451 -92 C ATOM 4361 CD2 LEU C 189 -22.343-134.689 -22.382 1.00 22.06 C ANISOU 4361 CD2 LEU C 189 3115 2473 2793 -102 455 -73 C ATOM 4362 N PHE C 190 -24.526-130.556 -24.861 1.00 36.91 N ANISOU 4362 N PHE C 190 4916 4378 4731 -176 441 -125 N ATOM 4363 CA PHE C 190 -25.103-129.772 -25.958 1.00 28.37 C ANISOU 4363 CA PHE C 190 3804 3273 3701 -229 547 -194 C ATOM 4364 C PHE C 190 -25.395-128.299 -25.649 1.00 21.14 C ANISOU 4364 C PHE C 190 2880 2385 2767 -201 501 -165 C ATOM 4365 O PHE C 190 -25.371-127.852 -24.505 1.00 29.56 O ANISOU 4365 O PHE C 190 3955 3517 3760 -150 360 -77 O ATOM 4366 CB PHE C 190 -26.335-130.444 -26.551 1.00 13.28 C ANISOU 4366 CB PHE C 190 1902 1372 1773 -273 659 -333 C ATOM 4367 CG PHE C 190 -27.468-130.561 -25.606 1.00 14.81 C ANISOU 4367 CG PHE C 190 2174 1591 1862 -298 643 -326 C ATOM 4368 CD1 PHE C 190 -28.476-129.616 -25.589 1.00 33.55 C ANISOU 4368 CD1 PHE C 190 4573 3985 4189 -264 605 -382 C ATOM 4369 CD2 PHE C 190 -27.547-131.631 -24.743 1.00 29.37 C ANISOU 4369 CD2 PHE C 190 4071 3436 3650 -334 639 -290 C ATOM 4370 CE1 PHE C 190 -29.544-129.736 -24.723 1.00 28.04 C ANISOU 4370 CE1 PHE C 190 3957 3310 3386 -306 587 -370 C ATOM 4371 CE2 PHE C 190 -28.605-131.753 -23.871 1.00 47.79 C ANISOU 4371 CE2 PHE C 190 6462 5808 5890 -365 619 -287 C ATOM 4372 CZ PHE C 190 -29.604-130.799 -23.859 1.00 42.66 C ANISOU 4372 CZ PHE C 190 5843 5174 5191 -370 601 -311 C ATOM 4373 N GLU C 191 -25.686-127.549 -26.696 1.00 27.45 N ANISOU 4373 N GLU C 191 3629 3153 3648 -156 510 -296 N ATOM 4374 CA GLU C 191 -25.739-126.108 -26.576 1.00 23.80 C ANISOU 4374 CA GLU C 191 3182 2645 3215 -84 360 -306 C ATOM 4375 C GLU C 191 -26.743-125.525 -27.550 1.00 12.51 C ANISOU 4375 C GLU C 191 1791 1107 1854 -19 253 -463 C ATOM 4376 O GLU C 191 -26.670-125.793 -28.737 1.00 42.12 O ANISOU 4376 O GLU C 191 5477 4838 5688 8 299 -563 O ATOM 4377 CB GLU C 191 -24.357-125.537 -26.849 1.00 14.32 C ANISOU 4377 CB GLU C 191 1896 1458 2088 -63 335 -241 C ATOM 4378 CG GLU C 191 -24.263-124.080 -26.583 1.00 40.36 C ANISOU 4378 CG GLU C 191 5234 4691 5411 -21 149 -212 C ATOM 4379 CD GLU C 191 -22.881-123.583 -26.803 1.00 37.79 C ANISOU 4379 CD GLU C 191 4808 4407 5144 -10 138 -155 C ATOM 4380 OE1 GLU C 191 -22.041-124.416 -27.180 1.00 40.50 O ANISOU 4380 OE1 GLU C 191 5058 4819 5511 -35 271 -143 O ATOM 4381 OE2 GLU C 191 -22.636-122.374 -26.609 1.00 54.56 O ANISOU 4381 OE2 GLU C 191 6935 6504 7293 -1 12 -116 O ATOM 4382 N ALA C 192 -27.677-124.727 -27.045 1.00 22.79 N ANISOU 4382 N ALA C 192 3208 2331 3119 -13 111 -472 N ATOM 4383 CA ALA C 192 -28.745-124.166 -27.874 1.00 29.38 C ANISOU 4383 CA ALA C 192 4137 3048 3980 11 48 -593 C ATOM 4384 C ALA C 192 -29.017-122.683 -27.584 1.00 33.67 C ANISOU 4384 C ALA C 192 4748 3497 4549 -52 -27 -540 C ATOM 4385 O ALA C 192 -29.513-122.344 -26.503 1.00 31.07 O ANISOU 4385 O ALA C 192 4415 3204 4185 -138 -10 -482 O ATOM 4386 CB ALA C 192 -30.010-124.980 -27.688 1.00 25.64 C ANISOU 4386 CB ALA C 192 3716 2602 3425 8 76 -691 C ATOM 4387 N PRO C 193 -28.668-121.797 -28.541 1.00 36.68 N ANISOU 4387 N PRO C 193 5002 3835 5099 -1 -101 -586 N ATOM 4388 CA PRO C 193 -29.006-120.367 -28.469 1.00 17.40 C ANISOU 4388 CA PRO C 193 2520 1339 2752 2 -271 -561 C ATOM 4389 C PRO C 193 -30.467-120.095 -28.857 1.00 16.23 C ANISOU 4389 C PRO C 193 2447 1102 2619 -6 -318 -684 C ATOM 4390 O PRO C 193 -31.002-120.735 -29.759 1.00 36.38 O ANISOU 4390 O PRO C 193 5026 3618 5179 22 -240 -825 O ATOM 4391 CB PRO C 193 -28.074-119.742 -29.507 1.00 34.25 C ANISOU 4391 CB PRO C 193 4508 3460 5044 70 -351 -577 C ATOM 4392 CG PRO C 193 -27.827-120.838 -30.491 1.00 36.69 C ANISOU 4392 CG PRO C 193 4778 3783 5378 101 -210 -686 C ATOM 4393 CD PRO C 193 -27.765-122.088 -29.668 1.00 38.67 C ANISOU 4393 CD PRO C 193 5118 4109 5466 64 -69 -638 C ATOM 4394 N VAL C 194 -31.101-119.163 -28.155 1.00 30.84 N ANISOU 4394 N VAL C 194 4326 2928 4463 -34 -462 -621 N ATOM 4395 CA VAL C 194 -32.424-118.650 -28.503 1.00 27.84 C ANISOU 4395 CA VAL C 194 4007 2459 4113 -37 -550 -721 C ATOM 4396 C VAL C 194 -32.371-117.780 -29.777 1.00 33.57 C ANISOU 4396 C VAL C 194 4654 3097 5006 48 -671 -804 C ATOM 4397 O VAL C 194 -31.361-117.157 -30.084 1.00 37.37 O ANISOU 4397 O VAL C 194 5026 3591 5582 95 -758 -738 O ATOM 4398 CB VAL C 194 -32.993-117.842 -27.329 1.00 28.14 C ANISOU 4398 CB VAL C 194 4098 2505 4089 -80 -709 -590 C ATOM 4399 CG1 VAL C 194 -34.324-117.170 -27.699 1.00 20.06 C ANISOU 4399 CG1 VAL C 194 3139 1381 3103 -81 -828 -680 C ATOM 4400 CG2 VAL C 194 -33.134-118.738 -26.099 1.00 22.25 C ANISOU 4400 CG2 VAL C 194 3408 1854 3191 -159 -604 -517 C ATOM 4401 N SER C 195 -33.471-117.758 -30.513 1.00 30.31 N ANISOU 4401 N SER C 195 4290 2599 4627 62 -678 -956 N ATOM 4402 CA SER C 195 -33.540-117.126 -31.826 1.00 28.14 C ANISOU 4402 CA SER C 195 3937 2239 4515 144 -768 -1068 C ATOM 4403 C SER C 195 -33.565-115.603 -31.778 1.00 39.68 C ANISOU 4403 C SER C 195 5357 3640 6078 173 -1012 -989 C ATOM 4404 O SER C 195 -33.221-114.951 -32.757 1.00 52.22 O ANISOU 4404 O SER C 195 6846 5177 7817 239 -1108 -1039 O ATOM 4405 CB SER C 195 -34.811-117.586 -32.550 1.00 41.32 C ANISOU 4405 CB SER C 195 5688 3838 6172 152 -702 -1257 C ATOM 4406 OG SER C 195 -34.781-118.964 -32.845 1.00 48.82 O ANISOU 4406 OG SER C 195 6670 4843 7038 148 -498 -1341 O ATOM 4407 N PHE C 196 -33.990-115.028 -30.659 1.00 40.76 N ANISOU 4407 N PHE C 196 5569 3784 6133 124 -1124 -863 N ATOM 4408 CA PHE C 196 -34.232-113.587 -30.620 1.00 27.40 C ANISOU 4408 CA PHE C 196 3867 2026 4519 153 -1372 -788 C ATOM 4409 C PHE C 196 -33.645-112.881 -29.410 1.00 47.52 C ANISOU 4409 C PHE C 196 6419 4642 6995 126 -1506 -562 C ATOM 4410 O PHE C 196 -33.573-113.457 -28.326 1.00 50.51 O ANISOU 4410 O PHE C 196 6856 5103 7233 68 -1425 -464 O ATOM 4411 CB PHE C 196 -35.725-113.310 -30.705 1.00 42.68 C ANISOU 4411 CB PHE C 196 5910 3864 6441 135 -1437 -881 C ATOM 4412 CG PHE C 196 -36.555-114.157 -29.795 1.00 29.25 C ANISOU 4412 CG PHE C 196 4331 2205 4577 48 -1319 -885 C ATOM 4413 CD1 PHE C 196 -36.729-113.809 -28.461 1.00 52.46 C ANISOU 4413 CD1 PHE C 196 7338 5191 7404 -11 -1410 -707 C ATOM 4414 CD2 PHE C 196 -37.202-115.277 -30.281 1.00 43.27 C ANISOU 4414 CD2 PHE C 196 6158 3976 6305 23 -1128 -1063 C ATOM 4415 CE1 PHE C 196 -37.518-114.587 -27.613 1.00 51.55 C ANISOU 4415 CE1 PHE C 196 7323 5121 7143 -97 -1314 -709 C ATOM 4416 CE2 PHE C 196 -37.982-116.060 -29.437 1.00 59.68 C ANISOU 4416 CE2 PHE C 196 8340 6104 8231 -68 -1025 -1073 C ATOM 4417 CZ PHE C 196 -38.144-115.711 -28.098 1.00 33.83 C ANISOU 4417 CZ PHE C 196 5114 2879 4859 -129 -1123 -899 C ATOM 4418 N PHE C 197 -33.247-111.623 -29.600 1.00 57.20 N ANISOU 4418 N PHE C 197 7583 5838 8313 169 -1717 -480 N ATOM 4419 CA PHE C 197 -32.620-110.840 -28.538 1.00 53.91 C ANISOU 4419 CA PHE C 197 7165 5494 7825 151 -1865 -264 C ATOM 4420 C PHE C 197 -33.534-110.763 -27.334 1.00 34.97 C ANISOU 4420 C PHE C 197 4904 3103 5281 90 -1914 -153 C ATOM 4421 O PHE C 197 -34.739-110.899 -27.465 1.00 47.52 O ANISOU 4421 O PHE C 197 6583 4612 6862 71 -1905 -242 O ATOM 4422 CB PHE C 197 -32.328-109.415 -29.013 1.00 73.44 C ANISOU 4422 CB PHE C 197 9577 7921 10405 184 -2059 -219 C ATOM 4423 CG PHE C 197 -31.062-109.274 -29.819 1.00104.92 C ANISOU 4423 CG PHE C 197 13432 11950 14483 206 -1991 -252 C ATOM 4424 CD1 PHE C 197 -29.982-110.118 -29.612 1.00115.14 C ANISOU 4424 CD1 PHE C 197 14671 13355 15723 185 -1820 -231 C ATOM 4425 CD2 PHE C 197 -30.951-108.279 -30.783 1.00120.76 C ANISOU 4425 CD2 PHE C 197 15376 13882 16624 240 -2102 -301 C ATOM 4426 CE1 PHE C 197 -28.817-109.978 -30.358 1.00121.31 C ANISOU 4426 CE1 PHE C 197 15343 14171 16577 197 -1760 -256 C ATOM 4427 CE2 PHE C 197 -29.791-108.135 -31.530 1.00126.09 C ANISOU 4427 CE2 PHE C 197 15942 14593 17372 250 -2040 -324 C ATOM 4428 CZ PHE C 197 -28.722-108.984 -31.317 1.00125.02 C ANISOU 4428 CZ PHE C 197 15759 14567 17176 226 -1868 -300 C ATOM 4429 N GLY C 198 -32.965-110.538 -26.159 1.00 51.66 N ANISOU 4429 N GLY C 198 7033 5344 7253 16 -1824 3 N ATOM 4430 CA GLY C 198 -33.772-110.115 -25.034 1.00 59.12 C ANISOU 4430 CA GLY C 198 8074 6315 8072 -63 -1812 101 C ATOM 4431 C GLY C 198 -33.836-111.046 -23.854 1.00 49.73 C ANISOU 4431 C GLY C 198 6932 5240 6725 -131 -1653 166 C ATOM 4432 O GLY C 198 -33.674-112.253 -23.987 1.00 57.97 O ANISOU 4432 O GLY C 198 7989 6292 7744 -114 -1604 125 O ATOM 4433 N LYS C 199 -34.090-110.466 -22.689 1.00 57.99 N ANISOU 4433 N LYS C 199 7988 6375 7670 -202 -1573 257 N ATOM 4434 CA LYS C 199 -34.216-111.234 -21.465 1.00 59.44 C ANISOU 4434 CA LYS C 199 8183 6682 7720 -260 -1415 306 C ATOM 4435 C LYS C 199 -35.419-112.160 -21.523 1.00 54.81 C ANISOU 4435 C LYS C 199 7735 5998 7092 -284 -1495 287 C ATOM 4436 O LYS C 199 -35.496-113.115 -20.747 1.00 46.98 O ANISOU 4436 O LYS C 199 6757 5095 5998 -328 -1364 309 O ATOM 4437 CB LYS C 199 -34.299-110.318 -20.240 1.00 49.01 C ANISOU 4437 CB LYS C 199 6887 5266 6468 -393 -1250 333 C ATOM 4438 CG LYS C 199 -32.975-109.696 -19.865 1.00 67.59 C ANISOU 4438 CG LYS C 199 9172 7660 8849 -418 -1220 366 C ATOM 4439 CD LYS C 199 -33.095-108.743 -18.691 1.00 87.08 C ANISOU 4439 CD LYS C 199 11552 10361 11173 -465 -1383 405 C ATOM 4440 CE LYS C 199 -31.770-108.042 -18.431 1.00102.19 C ANISOU 4440 CE LYS C 199 13502 12074 13252 -521 -1235 471 C ATOM 4441 NZ LYS C 199 -31.877-107.011 -17.366 1.00106.87 N ANISOU 4441 NZ LYS C 199 14100 12663 13842 -603 -1280 545 N ATOM 4442 N LEU C 200 -36.346-111.892 -22.442 1.00 29.07 N ANISOU 4442 N LEU C 200 4576 2559 3910 -245 -1711 231 N ATOM 4443 CA LEU C 200 -37.538-112.734 -22.557 1.00 40.81 C ANISOU 4443 CA LEU C 200 6207 3953 5345 -265 -1769 172 C ATOM 4444 C LEU C 200 -37.193-114.114 -23.105 1.00 51.95 C ANISOU 4444 C LEU C 200 7557 5417 6766 -268 -1526 -8 C ATOM 4445 O LEU C 200 -37.895-115.091 -22.833 1.00 69.06 O ANISOU 4445 O LEU C 200 9777 7613 8849 -331 -1398 -85 O ATOM 4446 CB LEU C 200 -38.651-112.053 -23.373 1.00 59.16 C ANISOU 4446 CB LEU C 200 8572 6136 7770 -248 -1883 40 C ATOM 4447 CG LEU C 200 -39.061-112.457 -24.795 1.00 85.09 C ANISOU 4447 CG LEU C 200 11808 9343 11178 -209 -1788 -240 C ATOM 4448 CD1 LEU C 200 -39.389-113.941 -24.942 1.00 83.75 C ANISOU 4448 CD1 LEU C 200 11646 9231 10945 -258 -1548 -408 C ATOM 4449 CD2 LEU C 200 -40.259-111.615 -25.234 1.00 93.09 C ANISOU 4449 CD2 LEU C 200 12893 10228 12250 -204 -1946 -310 C ATOM 4450 N GLY C 201 -36.103-114.196 -23.862 1.00 45.58 N ANISOU 4450 N GLY C 201 6636 4626 6057 -202 -1466 -69 N ATOM 4451 CA GLY C 201 -35.604-115.478 -24.340 1.00 30.44 C ANISOU 4451 CA GLY C 201 4659 2759 4146 -203 -1234 -208 C ATOM 4452 C GLY C 201 -35.350-116.455 -23.206 1.00 27.55 C ANISOU 4452 C GLY C 201 4329 2514 3624 -267 -1116 -103 C ATOM 4453 O GLY C 201 -35.294-117.657 -23.428 1.00 56.98 O ANISOU 4453 O GLY C 201 8036 6283 7331 -289 -923 -222 O ATOM 4454 N ASP C 202 -35.200-115.937 -21.990 1.00 41.78 N ANISOU 4454 N ASP C 202 6184 4382 5308 -296 -1238 124 N ATOM 4455 CA ASP C 202 -35.022-116.758 -20.788 1.00 31.45 C ANISOU 4455 CA ASP C 202 4899 3211 3841 -362 -1122 235 C ATOM 4456 C ASP C 202 -36.310-117.484 -20.410 1.00 33.31 C ANISOU 4456 C ASP C 202 5260 3419 3978 -441 -1087 212 C ATOM 4457 O ASP C 202 -36.343-118.267 -19.445 1.00 30.19 O ANISOU 4457 O ASP C 202 4851 3141 3479 -500 -949 268 O ATOM 4458 CB ASP C 202 -34.582-115.893 -19.604 1.00 42.26 C ANISOU 4458 CB ASP C 202 6101 4739 5218 -374 -1002 295 C ATOM 4459 CG ASP C 202 -33.194-115.311 -19.775 1.00 43.54 C ANISOU 4459 CG ASP C 202 6119 4978 5445 -319 -948 281 C ATOM 4460 OD1 ASP C 202 -32.622-115.438 -20.873 1.00 46.60 O ANISOU 4460 OD1 ASP C 202 6517 5287 5903 -275 -1013 243 O ATOM 4461 OD2 ASP C 202 -32.679-114.710 -18.806 1.00 59.03 O ANISOU 4461 OD2 ASP C 202 8045 6869 7514 -406 -831 297 O ATOM 4462 N SER C 203 -37.371-117.218 -21.166 1.00 24.41 N ANISOU 4462 N SER C 203 4157 2184 2933 -441 -1125 49 N ATOM 4463 CA SER C 203 -38.646-117.895 -20.957 1.00 28.41 C ANISOU 4463 CA SER C 203 4742 2691 3362 -516 -1072 -40 C ATOM 4464 C SER C 203 -38.714-119.163 -21.784 1.00 30.08 C ANISOU 4464 C SER C 203 4892 2938 3601 -507 -874 -285 C ATOM 4465 O SER C 203 -39.564-120.015 -21.555 1.00 32.51 O ANISOU 4465 O SER C 203 5244 3293 3815 -562 -803 -363 O ATOM 4466 CB SER C 203 -39.806-116.969 -21.280 1.00 51.21 C ANISOU 4466 CB SER C 203 7695 5466 6298 -522 -1226 -94 C ATOM 4467 OG SER C 203 -39.759-115.827 -20.449 1.00 68.40 O ANISOU 4467 OG SER C 203 9933 7612 8444 -531 -1410 150 O ATOM 4468 N ASN C 204 -37.792-119.280 -22.737 1.00 31.55 N ANISOU 4468 N ASN C 204 4972 3106 3910 -437 -791 -396 N ATOM 4469 CA ASN C 204 -37.592-120.513 -23.490 1.00 36.55 C ANISOU 4469 CA ASN C 204 5530 3782 4574 -421 -590 -599 C ATOM 4470 C ASN C 204 -36.732-121.520 -22.743 1.00 36.89 C ANISOU 4470 C ASN C 204 5551 3947 4520 -432 -481 -486 C ATOM 4471 O ASN C 204 -35.795-121.145 -22.051 1.00 33.34 O ANISOU 4471 O ASN C 204 5103 3529 4034 -430 -523 -283 O ATOM 4472 CB ASN C 204 -36.901-120.218 -24.804 1.00 42.58 C ANISOU 4472 CB ASN C 204 6209 4471 5500 -354 -533 -729 C ATOM 4473 CG ASN C 204 -37.705-119.321 -25.682 1.00 31.70 C ANISOU 4473 CG ASN C 204 4872 2967 4207 -333 -631 -836 C ATOM 4474 OD1 ASN C 204 -37.291-118.202 -25.982 1.00 42.33 O ANISOU 4474 OD1 ASN C 204 6200 4241 5644 -276 -777 -756 O ATOM 4475 ND2 ASN C 204 -38.855-119.808 -26.119 1.00 36.52 N ANISOU 4475 ND2 ASN C 204 5529 3557 4788 -369 -566 -1020 N ATOM 4476 N GLY C 205 -37.058-122.800 -22.906 1.00 35.14 N ANISOU 4476 N GLY C 205 5316 3799 4238 -434 -353 -611 N ATOM 4477 CA GLY C 205 -36.321-123.887 -22.291 1.00 27.76 C ANISOU 4477 CA GLY C 205 4384 2979 3182 -446 -235 -499 C ATOM 4478 C GLY C 205 -36.767-125.206 -22.889 1.00 24.95 C ANISOU 4478 C GLY C 205 4019 2689 2771 -412 -108 -664 C ATOM 4479 O GLY C 205 -37.504-125.216 -23.875 1.00 24.36 O ANISOU 4479 O GLY C 205 3915 2562 2777 -349 -135 -881 O ATOM 4480 N MET C 206 -36.335-126.325 -22.307 1.00 44.68 N ANISOU 4480 N MET C 206 6550 5299 5128 -461 38 -547 N ATOM 4481 CA MET C 206 -36.724-127.624 -22.842 1.00 18.87 C ANISOU 4481 CA MET C 206 3255 2112 1802 -428 172 -659 C ATOM 4482 C MET C 206 -36.744-128.797 -21.866 1.00 27.99 C ANISOU 4482 C MET C 206 4429 3378 2826 -529 298 -508 C ATOM 4483 O MET C 206 -36.391-128.655 -20.703 1.00 31.80 O ANISOU 4483 O MET C 206 4929 3864 3290 -615 273 -320 O ATOM 4484 CB MET C 206 -35.853-127.962 -24.042 1.00 16.18 C ANISOU 4484 CB MET C 206 2821 1753 1574 -322 244 -765 C ATOM 4485 CG MET C 206 -34.417-127.636 -23.835 1.00 43.39 C ANISOU 4485 CG MET C 206 6205 5191 5092 -315 259 -634 C ATOM 4486 SD MET C 206 -33.328-128.143 -25.358 1.00 74.14 S ANISOU 4486 SD MET C 206 9983 9070 9118 -206 356 -736 S ATOM 4487 CE MET C 206 -33.871-126.820 -26.672 1.00 38.17 C ANISOU 4487 CE MET C 206 5462 4325 4716 -78 153 -930 C ATOM 4488 N ARG C 207 -37.205-129.941 -22.372 1.00 27.82 N ANISOU 4488 N ARG C 207 4389 3418 2761 -520 408 -605 N ATOM 4489 CA ARG C 207 -37.187-131.209 -21.669 1.00 15.85 C ANISOU 4489 CA ARG C 207 2854 1978 1189 -604 503 -508 C ATOM 4490 C ARG C 207 -36.593-132.284 -22.579 1.00 35.54 C ANISOU 4490 C ARG C 207 5263 4509 3732 -557 624 -584 C ATOM 4491 O ARG C 207 -36.627-132.164 -23.804 1.00 34.40 O ANISOU 4491 O ARG C 207 5092 4346 3632 -469 653 -733 O ATOM 4492 CB ARG C 207 -38.587-131.637 -21.254 1.00 27.38 C ANISOU 4492 CB ARG C 207 4394 3481 2528 -670 496 -538 C ATOM 4493 CG ARG C 207 -39.154-130.890 -20.087 1.00 35.80 C ANISOU 4493 CG ARG C 207 5536 4521 3547 -756 380 -416 C ATOM 4494 CD ARG C 207 -40.668-130.973 -20.100 1.00 25.95 C ANISOU 4494 CD ARG C 207 4382 3293 2186 -792 348 -501 C ATOM 4495 NE ARG C 207 -41.251-130.153 -19.054 1.00 26.75 N ANISOU 4495 NE ARG C 207 4558 3355 2253 -879 221 -379 N ATOM 4496 CZ ARG C 207 -42.553-129.977 -18.865 1.00 38.16 C ANISOU 4496 CZ ARG C 207 6095 4796 3607 -927 156 -418 C ATOM 4497 NH1 ARG C 207 -43.433-130.560 -19.664 1.00 32.68 N ANISOU 4497 NH1 ARG C 207 5434 4135 2846 -890 204 -596 N ATOM 4498 NH2 ARG C 207 -42.970-129.203 -17.872 1.00 37.42 N ANISOU 4498 NH2 ARG C 207 6059 4656 3505 -1016 36 -281 N ATOM 4499 N VAL C 208 -36.068-133.340 -21.962 1.00 24.26 N ANISOU 4499 N VAL C 208 3791 3117 2309 -610 667 -494 N ATOM 4500 CA VAL C 208 -35.304-134.379 -22.643 1.00 21.23 C ANISOU 4500 CA VAL C 208 3332 2757 1979 -580 753 -531 C ATOM 4501 C VAL C 208 -35.388-135.626 -21.803 1.00 22.51 C ANISOU 4501 C VAL C 208 3491 2971 2090 -641 766 -473 C ATOM 4502 O VAL C 208 -35.208-135.576 -20.584 1.00 29.15 O ANISOU 4502 O VAL C 208 4342 3809 2925 -676 690 -369 O ATOM 4503 CB VAL C 208 -33.773-134.095 -22.665 1.00 30.64 C ANISOU 4503 CB VAL C 208 4458 3896 3288 -540 727 -458 C ATOM 4504 CG1 VAL C 208 -33.149-134.707 -23.897 1.00 32.13 C ANISOU 4504 CG1 VAL C 208 4579 4091 3539 -491 809 -540 C ATOM 4505 CG2 VAL C 208 -33.450-132.609 -22.544 1.00 37.66 C ANISOU 4505 CG2 VAL C 208 5365 4719 4226 -513 650 -415 C ATOM 4506 N TRP C 209 -35.598-136.754 -22.457 1.00 24.71 N ANISOU 4506 N TRP C 209 3748 3301 2339 -644 854 -549 N ATOM 4507 CA TRP C 209 -35.648-138.017 -21.759 1.00 20.43 C ANISOU 4507 CA TRP C 209 3203 2813 1746 -694 868 -505 C ATOM 4508 C TRP C 209 -35.384-139.160 -22.708 1.00 19.38 C ANISOU 4508 C TRP C 209 3027 2719 1616 -679 964 -582 C ATOM 4509 O TRP C 209 -35.649-139.056 -23.895 1.00 42.97 O ANISOU 4509 O TRP C 209 6001 5711 4615 -646 1032 -696 O ATOM 4510 CB TRP C 209 -36.990-138.178 -21.053 1.00 31.24 C ANISOU 4510 CB TRP C 209 4642 4225 3002 -768 853 -503 C ATOM 4511 CG TRP C 209 -38.205-138.235 -21.951 1.00 32.51 C ANISOU 4511 CG TRP C 209 4851 4419 3084 -775 924 -635 C ATOM 4512 CD1 TRP C 209 -38.768-139.350 -22.484 1.00 38.49 C ANISOU 4512 CD1 TRP C 209 5610 5238 3776 -797 1012 -720 C ATOM 4513 CD2 TRP C 209 -39.028-137.136 -22.368 1.00 31.67 C ANISOU 4513 CD2 TRP C 209 4803 4284 2948 -748 898 -709 C ATOM 4514 NE1 TRP C 209 -39.878-139.015 -23.216 1.00 24.29 N ANISOU 4514 NE1 TRP C 209 3866 3451 1914 -781 1046 -849 N ATOM 4515 CE2 TRP C 209 -40.053-137.665 -23.166 1.00 23.60 C ANISOU 4515 CE2 TRP C 209 3816 3305 1847 -743 970 -851 C ATOM 4516 CE3 TRP C 209 -38.981-135.752 -22.159 1.00 55.65 C ANISOU 4516 CE3 TRP C 209 7870 7258 6015 -721 811 -679 C ATOM 4517 CZ2 TRP C 209 -41.038-136.860 -23.754 1.00 48.44 C ANISOU 4517 CZ2 TRP C 209 7030 6424 4949 -697 944 -981 C ATOM 4518 CZ3 TRP C 209 -39.963-134.954 -22.746 1.00 38.27 C ANISOU 4518 CZ3 TRP C 209 5740 5034 3768 -679 780 -802 C ATOM 4519 CH2 TRP C 209 -40.975-135.513 -23.528 1.00 28.76 C ANISOU 4519 CH2 TRP C 209 4572 3864 2493 -661 839 -958 C ATOM 4520 N SER C 210 -34.831-140.245 -22.166 1.00 38.99 N ANISOU 4520 N SER C 210 5488 5234 4092 -696 963 -525 N ATOM 4521 CA SER C 210 -34.473-141.431 -22.938 1.00 26.61 C ANISOU 4521 CA SER C 210 3882 3705 2522 -692 1045 -580 C ATOM 4522 C SER C 210 -35.671-142.344 -23.083 1.00 22.18 C ANISOU 4522 C SER C 210 3356 3219 1852 -753 1115 -650 C ATOM 4523 O SER C 210 -36.611-142.263 -22.287 1.00 32.17 O ANISOU 4523 O SER C 210 4675 4507 3040 -806 1085 -626 O ATOM 4524 CB SER C 210 -33.380-142.185 -22.217 1.00 45.63 C ANISOU 4524 CB SER C 210 6262 6116 4959 -677 1004 -487 C ATOM 4525 OG SER C 210 -33.766-142.370 -20.868 1.00 63.32 O ANISOU 4525 OG SER C 210 8530 8383 7145 -713 939 -408 O ATOM 4526 N THR C 211 -35.645-143.199 -24.105 1.00 48.78 N ANISOU 4526 N THR C 211 7617 5334 5583 2871 3003 2408 N ATOM 4527 CA THR C 211 -36.701-144.182 -24.313 1.00 49.29 C ANISOU 4527 CA THR C 211 7772 5362 5594 2879 3018 2403 C ATOM 4528 C THR C 211 -36.410-145.478 -23.547 1.00 49.50 C ANISOU 4528 C THR C 211 7859 5405 5544 2905 2967 2396 C ATOM 4529 O THR C 211 -35.280-145.722 -23.121 1.00 58.59 O ANISOU 4529 O THR C 211 8982 6587 6692 2910 2928 2392 O ATOM 4530 CB THR C 211 -36.884-144.482 -25.789 1.00 49.31 C ANISOU 4530 CB THR C 211 7787 5309 5637 2849 3074 2390 C ATOM 4531 OG1 THR C 211 -35.614-144.751 -26.386 1.00 66.28 O ANISOU 4531 OG1 THR C 211 9897 7462 7823 2830 3069 2378 O ATOM 4532 CG2 THR C 211 -37.508-143.292 -26.485 1.00 49.25 C ANISOU 4532 CG2 THR C 211 7738 5278 5695 2827 3126 2396 C ATOM 4533 N THR C 212 -37.433-146.304 -23.365 1.00 50.01 N ANISOU 4533 N THR C 212 8007 5449 5545 2920 2968 2395 N ATOM 4534 CA THR C 212 -37.284-147.521 -22.578 1.00 50.27 C ANISOU 4534 CA THR C 212 8101 5497 5501 2946 2917 2390 C ATOM 4535 C THR C 212 -38.248-148.620 -23.012 1.00 52.86 C ANISOU 4535 C THR C 212 8523 5784 5778 2946 2937 2383 C ATOM 4536 O THR C 212 -39.416-148.343 -23.282 1.00 51.09 O ANISOU 4536 O THR C 212 8331 5534 5546 2941 2973 2388 O ATOM 4537 CB THR C 212 -37.481-147.215 -21.086 1.00 50.40 C ANISOU 4537 CB THR C 212 8116 5564 5471 2983 2864 2404 C ATOM 4538 OG1 THR C 212 -36.339-146.503 -20.585 1.00 68.58 O ANISOU 4538 OG1 THR C 212 10339 7909 7810 2986 2834 2407 O ATOM 4539 CG2 THR C 212 -37.635-148.470 -20.316 1.00 50.78 C ANISOU 4539 CG2 THR C 212 8238 5621 5436 3012 2816 2400 C ATOM 4540 N THR C 213 -37.764-149.864 -23.075 1.00 50.87 N ANISOU 4540 N THR C 213 8315 5524 5488 2949 2914 2371 N ATOM 4541 CA THR C 213 -38.624-150.984 -23.437 1.00 51.36 C ANISOU 4541 CA THR C 213 8468 5549 5497 2949 2929 2364 C ATOM 4542 C THR C 213 -39.372-151.326 -22.171 1.00 51.84 C ANISOU 4542 C THR C 213 8589 5630 5478 2981 2892 2374 C ATOM 4543 O THR C 213 -39.467-152.486 -21.792 1.00 96.54 O ANISOU 4543 O THR C 213 14330 11276 11076 2989 2881 2369 O ATOM 4544 CB THR C 213 -37.822-152.256 -23.790 1.00 51.34 C ANISOU 4544 CB THR C 213 8496 5534 5476 2943 2912 2350 C ATOM 4545 OG1 THR C 213 -36.921-152.570 -22.719 1.00 51.20 O ANISOU 4545 OG1 THR C 213 8464 5561 5429 2967 2848 2351 O ATOM 4546 CG2 THR C 213 -37.044-152.056 -25.079 1.00 50.94 C ANISOU 4546 CG2 THR C 213 8397 5458 5500 2908 2953 2340 C ATOM 4547 N ALA C 214 -39.912-150.308 -21.522 1.00 58.30 N ANISOU 4547 N ALA C 214 9370 6484 6298 3000 2872 2388 N ATOM 4548 CA ALA C 214 -40.709-150.493 -20.319 1.00 56.22 C ANISOU 4548 CA ALA C 214 9155 6244 5960 3031 2836 2399 C ATOM 4549 C ALA C 214 -41.944-149.603 -20.493 1.00 57.98 C ANISOU 4549 C ALA C 214 9366 6465 6199 3026 2870 2412 C ATOM 4550 O ALA C 214 -42.975-149.859 -19.881 1.00 57.97 O ANISOU 4550 O ALA C 214 9370 6499 6158 3053 2836 2426 O ATOM 4551 CB ALA C 214 -39.949-150.489 -18.981 1.00 52.12 C ANISOU 4551 CB ALA C 214 8607 5782 5413 3066 2764 2405 C ATOM 4552 N ASP C 215 -41.874-148.543 -21.284 1.00 52.25 N ANISOU 4552 N ASP C 215 8622 5699 5533 2993 2935 2409 N ATOM 4553 CA ASP C 215 -43.096-147.749 -21.395 1.00 80.90 C ANISOU 4553 CA ASP C 215 12240 9326 9173 2988 2965 2423 C ATOM 4554 C ASP C 215 -44.342-147.907 -22.260 1.00 52.81 C ANISOU 4554 C ASP C 215 8744 5717 5604 2963 3025 2418 C ATOM 4555 O ASP C 215 -44.329-148.539 -23.312 1.00 62.68 O ANISOU 4555 O ASP C 215 10024 6924 6870 2939 3063 2403 O ATOM 4556 CB ASP C 215 -42.479-146.366 -21.601 1.00 93.66 C ANISOU 4556 CB ASP C 215 13757 10956 10875 2975 2983 2431 C ATOM 4557 CG ASP C 215 -43.336-145.248 -21.017 1.00113.72 C ANISOU 4557 CG ASP C 215 16279 13515 13415 2982 2988 2449 C ATOM 4558 OD1 ASP C 215 -44.045-145.507 -20.023 1.00105.75 O ANISOU 4558 OD1 ASP C 215 15315 12531 12332 3009 2953 2459 O ATOM 4559 OD2 ASP C 215 -43.301-144.114 -21.545 1.00131.29 O ANISOU 4559 OD2 ASP C 215 18441 15730 15712 2960 3027 2455 O ATOM 4560 N ILE C 216 -45.423-147.324 -21.763 1.00 57.43 N ANISOU 4560 N ILE C 216 9350 6311 6160 2968 3032 2430 N ATOM 4561 CA ILE C 216 -46.614-147.070 -22.552 1.00 63.79 C ANISOU 4561 CA ILE C 216 10196 7073 6970 2939 3096 2426 C ATOM 4562 C ILE C 216 -46.467-146.738 -24.047 1.00 56.89 C ANISOU 4562 C ILE C 216 9289 6148 6178 2903 3158 2412 C ATOM 4563 O ILE C 216 -47.099-147.370 -24.886 1.00 76.70 O ANISOU 4563 O ILE C 216 11848 8620 8675 2889 3180 2396 O ATOM 4564 CB ILE C 216 -47.400-145.833 -21.987 1.00 77.31 C ANISOU 4564 CB ILE C 216 11882 8807 8686 2940 3105 2444 C ATOM 4565 CG1 ILE C 216 -46.626-144.514 -22.184 1.00 57.72 C ANISOU 4565 CG1 ILE C 216 9294 6337 6299 2931 3117 2453 C ATOM 4566 CG2 ILE C 216 -47.736-146.049 -20.506 1.00 71.76 C ANISOU 4566 CG2 ILE C 216 11208 8158 7898 2978 3038 2459 C ATOM 4567 CD1 ILE C 216 -46.452-143.671 -20.909 1.00 52.86 C ANISOU 4567 CD1 ILE C 216 8630 5782 5674 2960 3067 2475 C ATOM 4568 N GLU C 217 -45.621-145.774 -24.383 1.00 52.75 N ANISOU 4568 N GLU C 217 8683 5623 5738 2888 3184 2418 N ATOM 4569 CA GLU C 217 -45.319-145.489 -25.777 1.00 52.44 C ANISOU 4569 CA GLU C 217 8601 5542 5781 2857 3234 2405 C ATOM 4570 C GLU C 217 -44.309-146.546 -26.157 1.00 52.25 C ANISOU 4570 C GLU C 217 8585 5514 5755 2859 3214 2391 C ATOM 4571 O GLU C 217 -43.649-147.116 -25.287 1.00 52.52 O ANISOU 4571 O GLU C 217 8622 5586 5746 2885 3156 2394 O ATOM 4572 CB GLU C 217 -44.639-144.119 -25.870 1.00 51.92 C ANISOU 4572 CB GLU C 217 8433 5494 5802 2848 3240 2415 C ATOM 4573 CG GLU C 217 -45.597-142.985 -26.058 1.00 62.97 C ANISOU 4573 CG GLU C 217 9816 6878 7234 2831 3284 2423 C ATOM 4574 CD GLU C 217 -46.543-143.249 -27.205 1.00 77.58 C ANISOU 4574 CD GLU C 217 11717 8665 9094 2801 3351 2409 C ATOM 4575 OE1 GLU C 217 -47.399-144.166 -27.077 1.00 52.90 O ANISOU 4575 OE1 GLU C 217 8681 5525 5894 2804 3355 2402 O ATOM 4576 OE2 GLU C 217 -46.419-142.545 -28.233 1.00 76.12 O ANISOU 4576 OE2 GLU C 217 11482 8447 8991 2774 3399 2403 O ATOM 4577 N GLU C 218 -44.173-146.802 -27.453 1.00 52.19 N ANISOU 4577 N GLU C 218 8575 5460 5793 2831 3263 2377 N ATOM 4578 CA GLU C 218 -42.982-147.495 -27.918 1.00 53.97 C ANISOU 4578 CA GLU C 218 8780 5686 6040 2828 3247 2366 C ATOM 4579 C GLU C 218 -42.109-146.584 -28.759 1.00 73.64 C ANISOU 4579 C GLU C 218 11179 8172 8630 2807 3273 2364 C ATOM 4580 O GLU C 218 -42.402-145.398 -28.904 1.00 68.93 O ANISOU 4580 O GLU C 218 10532 7573 8085 2796 3299 2371 O ATOM 4581 CB GLU C 218 -43.298-148.806 -28.621 1.00 58.94 C ANISOU 4581 CB GLU C 218 9488 6277 6632 2819 3267 2350 C ATOM 4582 CG GLU C 218 -43.806-149.914 -27.670 1.00 91.64 C ANISOU 4582 CG GLU C 218 13715 10433 10670 2844 3224 2352 C ATOM 4583 CD GLU C 218 -43.038-150.005 -26.341 1.00 94.55 C ANISOU 4583 CD GLU C 218 14063 10861 11003 2877 3149 2362 C ATOM 4584 OE1 GLU C 218 -41.872-149.557 -26.276 1.00 96.42 O ANISOU 4584 OE1 GLU C 218 14224 11122 11289 2878 3129 2363 O ATOM 4585 OE2 GLU C 218 -43.610-150.530 -25.357 1.00 79.02 O ANISOU 4585 OE2 GLU C 218 12154 8914 8956 2901 3111 2367 O ATOM 4586 N PHE C 219 -41.016-147.133 -29.278 1.00 51.04 N ANISOU 4586 N PHE C 219 8292 5310 5790 2799 3263 2353 N ATOM 4587 CA PHE C 219 -39.996-146.334 -29.952 1.00 50.50 C ANISOU 4587 CA PHE C 219 8133 5247 5808 2780 3276 2352 C ATOM 4588 C PHE C 219 -39.329-147.212 -30.996 1.00 50.40 C ANISOU 4588 C PHE C 219 8128 5209 5814 2763 3291 2336 C ATOM 4589 O PHE C 219 -39.659-148.377 -31.081 1.00 50.74 O ANISOU 4589 O PHE C 219 8245 5233 5802 2768 3288 2328 O ATOM 4590 CB PHE C 219 -38.986-145.786 -28.932 1.00 50.09 C ANISOU 4590 CB PHE C 219 8017 5253 5761 2796 3221 2362 C ATOM 4591 CG PHE C 219 -38.079-146.829 -28.340 1.00 50.01 C ANISOU 4591 CG PHE C 219 8029 5272 5702 2812 3167 2357 C ATOM 4592 CD1 PHE C 219 -36.918-147.192 -28.982 1.00 49.66 C ANISOU 4592 CD1 PHE C 219 7951 5228 5691 2796 3163 2346 C ATOM 4593 CD2 PHE C 219 -38.381-147.421 -27.138 1.00 50.29 C ANISOU 4593 CD2 PHE C 219 8116 5334 5658 2843 3120 2362 C ATOM 4594 CE1 PHE C 219 -36.094-148.135 -28.456 1.00 49.61 C ANISOU 4594 CE1 PHE C 219 7964 5244 5641 2809 3116 2341 C ATOM 4595 CE2 PHE C 219 -37.553-148.369 -26.596 1.00 50.24 C ANISOU 4595 CE2 PHE C 219 8128 5351 5608 2857 3071 2357 C ATOM 4596 CZ PHE C 219 -36.407-148.729 -27.254 1.00 51.29 C ANISOU 4596 CZ PHE C 219 8229 5481 5776 2839 3070 2346 C ATOM 4597 N ASP C 220 -38.402-146.691 -31.789 1.00 49.96 N ANISOU 4597 N ASP C 220 7999 5152 5832 2743 3305 2332 N ATOM 4598 CA ASP C 220 -37.917-147.494 -32.908 1.00 49.93 C ANISOU 4598 CA ASP C 220 8005 5118 5847 2725 3326 2318 C ATOM 4599 C ASP C 220 -36.805-148.451 -32.506 1.00 51.92 C ANISOU 4599 C ASP C 220 8264 5399 6063 2733 3276 2314 C ATOM 4600 O ASP C 220 -35.621-148.174 -32.718 1.00 54.31 O ANISOU 4600 O ASP C 220 8502 5723 6408 2722 3259 2312 O ATOM 4601 CB ASP C 220 -37.519-146.641 -34.119 1.00 49.60 C ANISOU 4601 CB ASP C 220 7891 5057 5900 2698 3368 2315 C ATOM 4602 CG ASP C 220 -37.334-147.471 -35.384 1.00 49.69 C ANISOU 4602 CG ASP C 220 7923 5028 5928 2680 3400 2301 C ATOM 4603 OD1 ASP C 220 -37.240-148.708 -35.266 1.00 72.30 O ANISOU 4603 OD1 ASP C 220 10847 7887 8734 2686 3382 2295 O ATOM 4604 OD2 ASP C 220 -37.263-146.912 -36.495 1.00 49.55 O ANISOU 4604 OD2 ASP C 220 7862 4985 5981 2659 3442 2297 O ATOM 4605 N GLU C 221 -37.218-149.595 -31.952 1.00 50.13 N ANISOU 4605 N GLU C 221 8120 5170 5758 2750 3253 2311 N ATOM 4606 CA GLU C 221 -36.327-150.613 -31.403 1.00 50.06 C ANISOU 4606 CA GLU C 221 8132 5186 5703 2761 3201 2307 C ATOM 4607 C GLU C 221 -35.360-151.224 -32.429 1.00 49.84 C ANISOU 4607 C GLU C 221 8086 5143 5707 2739 3211 2296 C ATOM 4608 O GLU C 221 -34.215-151.547 -32.104 1.00 62.90 O ANISOU 4608 O GLU C 221 9715 6825 7357 2740 3170 2294 O ATOM 4609 CB GLU C 221 -37.147-151.701 -30.703 1.00 50.59 C ANISOU 4609 CB GLU C 221 8294 5246 5679 2783 3180 2307 C ATOM 4610 CG GLU C 221 -38.025-151.162 -29.566 1.00 67.63 C ANISOU 4610 CG GLU C 221 10471 7426 7797 2807 3162 2319 C ATOM 4611 CD GLU C 221 -38.468-152.247 -28.581 1.00 65.75 C ANISOU 4611 CD GLU C 221 10316 7200 7465 2834 3119 2321 C ATOM 4612 OE1 GLU C 221 -39.226-151.928 -27.633 1.00 57.49 O ANISOU 4612 OE1 GLU C 221 9292 6173 6378 2855 3100 2331 O ATOM 4613 OE2 GLU C 221 -38.057-153.414 -28.754 1.00 61.36 O ANISOU 4613 OE2 GLU C 221 9801 6636 6877 2833 3102 2312 O ATOM 4614 N ALA C 222 -35.814-151.365 -33.664 1.00 49.99 N ANISOU 4614 N ALA C 222 8117 5116 5759 2719 3264 2289 N ATOM 4615 CA ALA C 222 -34.964-151.867 -34.733 1.00 60.95 C ANISOU 4615 CA ALA C 222 9486 6489 7184 2697 3277 2279 C ATOM 4616 C ALA C 222 -33.985-150.796 -35.199 1.00 49.25 C ANISOU 4616 C ALA C 222 7905 5025 5782 2679 3281 2281 C ATOM 4617 O ALA C 222 -32.872-151.084 -35.612 1.00 58.74 O ANISOU 4617 O ALA C 222 9074 6237 7006 2666 3266 2277 O ATOM 4618 CB ALA C 222 -35.808-152.369 -35.901 1.00 68.97 C ANISOU 4618 CB ALA C 222 10548 7449 8206 2682 3333 2271 C ATOM 4619 N ALA C 223 -34.402-149.545 -35.128 1.00 49.13 N ANISOU 4619 N ALA C 223 7843 5014 5810 2679 3301 2289 N ATOM 4620 CA ALA C 223 -33.502-148.476 -35.489 1.00 48.63 C ANISOU 4620 CA ALA C 223 7685 4971 5820 2663 3302 2291 C ATOM 4621 C ALA C 223 -32.342-148.466 -34.517 1.00 49.72 C ANISOU 4621 C ALA C 223 7790 5161 5940 2671 3243 2295 C ATOM 4622 O ALA C 223 -31.176-148.405 -34.921 1.00 62.20 O ANISOU 4622 O ALA C 223 9321 6757 7556 2654 3229 2292 O ATOM 4623 CB ALA C 223 -34.220-147.145 -35.472 1.00 77.82 C ANISOU 4623 CB ALA C 223 11342 8665 9562 2662 3331 2300 C ATOM 4624 N MET C 224 -32.661-148.519 -33.228 1.00 48.41 N ANISOU 4624 N MET C 224 7653 5022 5717 2696 3207 2302 N ATOM 4625 CA MET C 224 -31.624-148.570 -32.213 1.00 48.12 C ANISOU 4625 CA MET C 224 7593 5035 5658 2707 3149 2305 C ATOM 4626 C MET C 224 -30.738-149.739 -32.497 1.00 48.08 C ANISOU 4626 C MET C 224 7612 5027 5629 2699 3127 2295 C ATOM 4627 O MET C 224 -29.527-149.600 -32.606 1.00 53.12 O ANISOU 4627 O MET C 224 8200 5688 6296 2686 3106 2292 O ATOM 4628 CB MET C 224 -32.211-148.762 -30.830 1.00 52.10 C ANISOU 4628 CB MET C 224 8142 5561 6092 2738 3113 2312 C ATOM 4629 CG MET C 224 -31.172-149.270 -29.850 1.00 73.31 C ANISOU 4629 CG MET C 224 10826 8288 8738 2752 3053 2311 C ATOM 4630 SD MET C 224 -31.707-149.107 -28.007 1.00105.94 S ANISOU 4630 SD MET C 224 14988 12464 12801 2793 3002 2323 S ATOM 4631 CE MET C 224 -33.326-150.195 -28.048 1.00 88.69 C ANISOU 4631 CE MET C 224 12917 10236 10545 2811 3021 2322 C ATOM 4632 N ALA C 225 -31.361-150.906 -32.597 1.00 48.50 N ANISOU 4632 N ALA C 225 7747 5053 5630 2707 3132 2289 N ATOM 4633 CA ALA C 225 -30.622-152.118 -32.872 1.00 61.51 C ANISOU 4633 CA ALA C 225 9426 6694 7251 2700 3112 2280 C ATOM 4634 C ALA C 225 -29.613-151.813 -33.967 1.00 58.79 C ANISOU 4634 C ALA C 225 9018 6346 6975 2670 3129 2276 C ATOM 4635 O ALA C 225 -28.402-151.799 -33.730 1.00 62.18 O ANISOU 4635 O ALA C 225 9407 6803 7414 2663 3094 2274 O ATOM 4636 CB ALA C 225 -31.568-153.232 -33.301 1.00 54.93 C ANISOU 4636 CB ALA C 225 8679 5819 6372 2704 3135 2275 C ATOM 4637 N LYS C 226 -30.131-151.527 -35.156 1.00 48.20 N ANISOU 4637 N LYS C 226 7666 4967 5680 2653 3182 2273 N ATOM 4638 CA LYS C 226 -29.301-151.352 -36.340 1.00 50.03 C ANISOU 4638 CA LYS C 226 7845 5189 5975 2625 3202 2268 C ATOM 4639 C LYS C 226 -28.122-150.417 -36.083 1.00 58.32 C ANISOU 4639 C LYS C 226 8810 6280 7070 2615 3175 2272 C ATOM 4640 O LYS C 226 -26.970-150.782 -36.330 1.00 57.80 O ANISOU 4640 O LYS C 226 8721 6227 7014 2600 3152 2268 O ATOM 4641 CB LYS C 226 -30.146-150.858 -37.513 1.00 48.04 C ANISOU 4641 CB LYS C 226 7583 4896 5775 2613 3264 2267 C ATOM 4642 CG LYS C 226 -29.437-150.867 -38.859 1.00 76.18 C ANISOU 4642 CG LYS C 226 11105 8443 9399 2586 3288 2262 C ATOM 4643 CD LYS C 226 -30.456-150.800 -39.998 1.00 90.41 C ANISOU 4643 CD LYS C 226 12924 10195 11232 2578 3350 2259 C ATOM 4644 CE LYS C 226 -29.796-150.663 -41.369 1.00 92.68 C ANISOU 4644 CE LYS C 226 13162 10466 11586 2553 3376 2255 C ATOM 4645 NZ LYS C 226 -29.354-149.267 -41.664 1.00 85.17 N ANISOU 4645 NZ LYS C 226 12120 9532 10710 2542 3383 2260 N ATOM 4646 N PHE C 227 -28.406-149.230 -35.553 1.00 47.21 N ANISOU 4646 N PHE C 227 7359 4893 5687 2622 3177 2280 N ATOM 4647 CA PHE C 227 -27.376-148.219 -35.385 1.00 46.72 C ANISOU 4647 CA PHE C 227 7213 4866 5672 2610 3157 2285 C ATOM 4648 C PHE C 227 -26.703-148.213 -34.017 1.00 46.55 C ANISOU 4648 C PHE C 227 7186 4891 5610 2626 3101 2288 C ATOM 4649 O PHE C 227 -25.806-147.417 -33.760 1.00 46.15 O ANISOU 4649 O PHE C 227 7070 4873 5592 2617 3080 2292 O ATOM 4650 CB PHE C 227 -27.965-146.852 -35.691 1.00 50.32 C ANISOU 4650 CB PHE C 227 7615 5318 6187 2605 3191 2292 C ATOM 4651 CG PHE C 227 -28.575-146.760 -37.054 1.00 57.02 C ANISOU 4651 CG PHE C 227 8461 6120 7082 2590 3247 2288 C ATOM 4652 CD1 PHE C 227 -27.776-146.603 -38.170 1.00 46.51 C ANISOU 4652 CD1 PHE C 227 7081 4781 5809 2565 3261 2284 C ATOM 4653 CD2 PHE C 227 -29.944-146.836 -37.218 1.00 59.13 C ANISOU 4653 CD2 PHE C 227 8778 6352 7336 2601 3285 2288 C ATOM 4654 CE1 PHE C 227 -28.326-146.528 -39.418 1.00 46.67 C ANISOU 4654 CE1 PHE C 227 7099 4759 5873 2553 3311 2280 C ATOM 4655 CE2 PHE C 227 -30.503-146.755 -38.470 1.00 66.22 C ANISOU 4655 CE2 PHE C 227 9677 7207 8278 2587 3337 2284 C ATOM 4656 CZ PHE C 227 -29.692-146.602 -39.574 1.00 70.56 C ANISOU 4656 CZ PHE C 227 10174 7749 8886 2564 3350 2280 C ATOM 4657 N LYS C 228 -27.132-149.102 -33.139 1.00 28.26 N ANISOU 4657 N LYS C 228 3521 3547 3669 631 1594 1263 N ATOM 4658 CA LYS C 228 -26.520-149.208 -31.821 1.00 36.50 C ANISOU 4658 CA LYS C 228 4505 4557 4807 586 1590 1266 C ATOM 4659 C LYS C 228 -26.427-147.849 -31.156 1.00 35.62 C ANISOU 4659 C LYS C 228 4384 4435 4714 506 1559 1194 C ATOM 4660 O LYS C 228 -25.359-147.449 -30.668 1.00 30.16 O ANISOU 4660 O LYS C 228 3638 3709 4111 426 1542 1136 O ATOM 4661 CB LYS C 228 -25.127-149.840 -31.914 1.00 50.08 C ANISOU 4661 CB LYS C 228 6161 6234 6632 551 1594 1255 C ATOM 4662 CG LYS C 228 -25.146-151.308 -32.333 1.00 61.52 C ANISOU 4662 CG LYS C 228 7606 7688 8079 623 1630 1337 C ATOM 4663 CD LYS C 228 -23.900-152.054 -31.864 1.00 79.98 C ANISOU 4663 CD LYS C 228 9878 9978 10534 595 1636 1347 C ATOM 4664 CE LYS C 228 -24.059-153.559 -32.047 1.00 91.08 C ANISOU 4664 CE LYS C 228 11277 11390 11938 667 1675 1444 C ATOM 4665 NZ LYS C 228 -25.226-154.096 -31.287 1.00 95.00 N ANISOU 4665 NZ LYS C 228 11798 11915 12384 730 1696 1529 N ATOM 4666 N THR C 229 -27.547-147.130 -31.150 1.00 35.41 N ANISOU 4666 N THR C 229 4417 4442 4594 526 1549 1194 N ATOM 4667 CA THR C 229 -27.606-145.883 -30.416 1.00 34.42 C ANISOU 4667 CA THR C 229 4284 4311 4481 452 1523 1138 C ATOM 4668 C THR C 229 -28.932-145.740 -29.711 1.00 30.76 C ANISOU 4668 C THR C 229 3873 3876 3938 499 1525 1193 C ATOM 4669 O THR C 229 -29.832-146.531 -29.930 1.00 45.26 O ANISOU 4669 O THR C 229 5767 5741 5688 591 1538 1266 O ATOM 4670 CB THR C 229 -27.383-144.679 -31.323 1.00 47.31 C ANISOU 4670 CB THR C 229 5943 5951 6083 394 1492 1060 C ATOM 4671 OG1 THR C 229 -27.244-143.507 -30.515 1.00 49.19 O ANISOU 4671 OG1 THR C 229 6163 6180 6346 304 1467 1002 O ATOM 4672 CG2 THR C 229 -28.550-144.505 -32.256 1.00 54.80 C ANISOU 4672 CG2 THR C 229 6978 6935 6907 467 1494 1084 C ATOM 4673 N ARG C 230 -29.044-144.716 -28.875 1.00 32.76 N ANISOU 4673 N ARG C 230 4113 4124 4213 433 1508 1157 N ATOM 4674 CA ARG C 230 -30.200-144.538 -28.000 1.00 25.76 C ANISOU 4674 CA ARG C 230 3267 3255 3264 466 1503 1217 C ATOM 4675 C ARG C 230 -31.188-143.491 -28.527 1.00 31.42 C ANISOU 4675 C ARG C 230 4086 4002 3849 472 1454 1185 C ATOM 4676 O ARG C 230 -30.791-142.486 -29.121 1.00 31.32 O ANISOU 4676 O ARG C 230 4077 3986 3836 408 1452 1117 O ATOM 4677 CB ARG C 230 -29.709-144.159 -26.600 1.00 24.51 C ANISOU 4677 CB ARG C 230 3015 3063 3235 386 1510 1200 C ATOM 4678 CG ARG C 230 -30.760-144.190 -25.531 1.00 30.03 C ANISOU 4678 CG ARG C 230 3733 3759 3918 411 1399 1201 C ATOM 4679 CD ARG C 230 -31.306-145.579 -25.325 1.00 25.98 C ANISOU 4679 CD ARG C 230 3243 3250 3380 510 1388 1301 C ATOM 4680 NE ARG C 230 -32.066-145.641 -24.080 1.00 43.25 N ANISOU 4680 NE ARG C 230 5417 5419 5596 516 1277 1303 N ATOM 4681 CZ ARG C 230 -31.553-145.887 -22.866 1.00 39.08 C ANISOU 4681 CZ ARG C 230 4778 4847 5223 480 1274 1305 C ATOM 4682 NH1 ARG C 230 -30.255-146.105 -22.687 1.00 26.51 N ANISOU 4682 NH1 ARG C 230 3080 3222 3770 433 1379 1301 N ATOM 4683 NH2 ARG C 230 -32.357-145.899 -21.815 1.00 46.99 N ANISOU 4683 NH2 ARG C 230 5774 5834 6247 489 1162 1308 N ATOM 4684 N GLN C 231 -32.473-143.733 -28.302 1.00 26.46 N ANISOU 4684 N GLN C 231 3543 3393 3119 542 1363 1200 N ATOM 4685 CA GLN C 231 -33.504-142.842 -28.782 1.00 25.16 C ANISOU 4685 CA GLN C 231 3481 3247 2830 555 1274 1144 C ATOM 4686 C GLN C 231 -33.990-141.977 -27.655 1.00 43.11 C ANISOU 4686 C GLN C 231 5746 5503 5130 492 1157 1084 C ATOM 4687 O GLN C 231 -34.260-142.464 -26.562 1.00 37.81 O ANISOU 4687 O GLN C 231 5040 4819 4506 499 1111 1112 O ATOM 4688 CB GLN C 231 -34.690-143.600 -29.365 1.00 34.39 C ANISOU 4688 CB GLN C 231 4767 4450 3850 672 1245 1191 C ATOM 4689 CG GLN C 231 -35.681-142.675 -30.061 1.00 32.17 C ANISOU 4689 CG GLN C 231 4598 4183 3441 691 1167 1126 C ATOM 4690 CD GLN C 231 -36.777-143.429 -30.779 1.00 54.65 C ANISOU 4690 CD GLN C 231 7565 7064 6134 806 1160 1163 C ATOM 4691 OE1 GLN C 231 -36.508-144.275 -31.630 1.00 61.37 O ANISOU 4691 OE1 GLN C 231 8423 7938 6957 867 1264 1218 O ATOM 4692 NE2 GLN C 231 -38.028-143.128 -30.432 1.00 73.92 N ANISOU 4692 NE2 GLN C 231 10104 9510 8472 833 1038 1134 N ATOM 4693 N PHE C 232 -34.109-140.687 -27.944 1.00 29.68 N ANISOU 4693 N PHE C 232 4075 3800 3401 429 1107 1006 N ATOM 4694 CA PHE C 232 -34.454-139.708 -26.945 1.00 24.60 C ANISOU 4694 CA PHE C 232 3415 3141 2789 350 1005 943 C ATOM 4695 C PHE C 232 -35.638-138.894 -27.420 1.00 44.25 C ANISOU 4695 C PHE C 232 6023 5641 5148 371 892 898 C ATOM 4696 O PHE C 232 -35.892-138.758 -28.615 1.00 47.49 O ANISOU 4696 O PHE C 232 6511 6065 5468 416 909 891 O ATOM 4697 CB PHE C 232 -33.279-138.755 -26.696 1.00 23.82 C ANISOU 4697 CB PHE C 232 3227 3023 2802 221 1052 884 C ATOM 4698 CG PHE C 232 -32.096-139.378 -25.986 1.00 23.70 C ANISOU 4698 CG PHE C 232 3087 2987 2933 182 1151 910 C ATOM 4699 CD1 PHE C 232 -32.010-139.354 -24.611 1.00 25.14 C ANISOU 4699 CD1 PHE C 232 3187 3148 3216 136 1121 894 C ATOM 4700 CD2 PHE C 232 -31.063-139.946 -26.700 1.00 30.65 C ANISOU 4700 CD2 PHE C 232 3928 3864 3855 190 1272 945 C ATOM 4701 CE1 PHE C 232 -30.922-139.898 -23.954 1.00 23.93 C ANISOU 4701 CE1 PHE C 232 2918 2970 3204 102 1213 908 C ATOM 4702 CE2 PHE C 232 -29.975-140.506 -26.050 1.00 29.98 C ANISOU 4702 CE2 PHE C 232 3732 3753 3904 153 1359 964 C ATOM 4703 CZ PHE C 232 -29.907-140.470 -24.671 1.00 29.75 C ANISOU 4703 CZ PHE C 232 3625 3702 3976 110 1330 942 C ATOM 4704 N ARG C 233 -36.353-138.338 -26.460 1.00 47.75 N ANISOU 4704 N ARG C 233 6476 6076 5591 335 776 864 N ATOM 4705 CA ARG C 233 -37.413-137.423 -26.753 1.00 25.19 C ANISOU 4705 CA ARG C 233 3723 3221 2628 333 657 812 C ATOM 4706 C ARG C 233 -37.073-136.069 -26.166 1.00 33.55 C ANISOU 4706 C ARG C 233 4732 4261 3755 203 606 741 C ATOM 4707 O ARG C 233 -36.759-135.962 -24.986 1.00 52.03 O ANISOU 4707 O ARG C 233 6983 6590 6198 137 594 733 O ATOM 4708 CB ARG C 233 -38.735-137.959 -26.210 1.00 31.78 C ANISOU 4708 CB ARG C 233 4634 4061 3380 409 547 841 C ATOM 4709 CG ARG C 233 -39.518-138.727 -27.273 1.00 56.17 C ANISOU 4709 CG ARG C 233 7844 7173 6323 531 559 876 C ATOM 4710 CD ARG C 233 -40.350-139.902 -26.735 1.00 52.83 C ANISOU 4710 CD ARG C 233 7468 6761 5845 616 514 944 C ATOM 4711 NE ARG C 233 -40.523-140.903 -27.793 1.00 41.85 N ANISOU 4711 NE ARG C 233 6149 5399 4353 720 598 994 N ATOM 4712 CZ ARG C 233 -41.108-142.087 -27.651 1.00 34.77 C ANISOU 4712 CZ ARG C 233 5305 4519 3387 801 593 1065 C ATOM 4713 NH1 ARG C 233 -41.618-142.470 -26.483 1.00 43.23 N ANISOU 4713 NH1 ARG C 233 6366 5577 4481 796 497 1100 N ATOM 4714 NH2 ARG C 233 -41.177-142.895 -28.689 1.00 29.25 N ANISOU 4714 NH2 ARG C 233 4666 3849 2598 884 685 1104 N ATOM 4715 N ILE C 234 -37.121-135.033 -26.994 1.00 29.44 N ANISOU 4715 N ILE C 234 4268 3737 3182 162 578 689 N ATOM 4716 CA ILE C 234 -36.924-133.672 -26.527 1.00 23.93 C ANISOU 4716 CA ILE C 234 3542 3023 2525 33 516 623 C ATOM 4717 C ILE C 234 -38.184-132.869 -26.786 1.00 29.49 C ANISOU 4717 C ILE C 234 4363 3722 3121 45 372 584 C ATOM 4718 O ILE C 234 -38.765-132.973 -27.862 1.00 39.80 O ANISOU 4718 O ILE C 234 5768 5030 4324 127 356 584 O ATOM 4719 CB ILE C 234 -35.756-133.017 -27.272 1.00 23.16 C ANISOU 4719 CB ILE C 234 3409 2920 2472 -50 599 596 C ATOM 4720 CG1 ILE C 234 -35.478-131.623 -26.737 1.00 22.84 C ANISOU 4720 CG1 ILE C 234 3340 2866 2473 -197 542 533 C ATOM 4721 CG2 ILE C 234 -36.044-132.949 -28.741 1.00 23.09 C ANISOU 4721 CG2 ILE C 234 3493 2911 2369 18 602 598 C ATOM 4722 CD1 ILE C 234 -34.128-131.146 -27.148 1.00 29.56 C ANISOU 4722 CD1 ILE C 234 4132 3710 3388 -297 636 515 C ATOM 4723 N GLN C 235 -38.615-132.072 -25.812 1.00 31.17 N ANISOU 4723 N GLN C 235 4560 3924 3358 -34 269 547 N ATOM 4724 CA GLN C 235 -39.696-131.132 -26.072 1.00 24.70 C ANISOU 4724 CA GLN C 235 3848 3093 2446 -44 128 504 C ATOM 4725 C GLN C 235 -39.385-129.722 -25.622 1.00 24.36 C ANISOU 4725 C GLN C 235 3769 3035 2452 -193 72 448 C ATOM 4726 O GLN C 235 -38.899-129.511 -24.525 1.00 56.99 O ANISOU 4726 O GLN C 235 7801 7170 6683 -282 87 440 O ATOM 4727 CB GLN C 235 -41.004-131.633 -25.458 1.00 42.07 C ANISOU 4727 CB GLN C 235 6109 5292 4582 32 15 524 C ATOM 4728 CG GLN C 235 -41.168-131.400 -23.983 1.00 28.40 C ANISOU 4728 CG GLN C 235 4301 3556 2935 -40 -53 521 C ATOM 4729 CD GLN C 235 -42.567-131.736 -23.517 1.00 38.31 C ANISOU 4729 CD GLN C 235 5637 4805 4113 28 -191 538 C ATOM 4730 OE1 GLN C 235 -43.443-132.045 -24.323 1.00 60.81 O ANISOU 4730 OE1 GLN C 235 8614 7656 6835 123 -238 543 O ATOM 4731 NE2 GLN C 235 -42.787-131.683 -22.211 1.00 51.21 N ANISOU 4731 NE2 GLN C 235 7199 6432 5828 -21 -257 546 N ATOM 4732 N LEU C 236 -39.663-128.756 -26.478 1.00 32.81 N ANISOU 4732 N LEU C 236 4920 4088 3457 -223 8 409 N ATOM 4733 CA LEU C 236 -39.496-127.341 -26.122 1.00 29.28 C ANISOU 4733 CA LEU C 236 4458 3627 3039 -370 -63 359 C ATOM 4734 C LEU C 236 -40.637-126.835 -25.254 1.00 24.58 C ANISOU 4734 C LEU C 236 3900 3022 2416 -394 -214 339 C ATOM 4735 O LEU C 236 -41.763-127.288 -25.383 1.00 49.62 O ANISOU 4735 O LEU C 236 7159 6189 5506 -290 -296 351 O ATOM 4736 CB LEU C 236 -39.381-126.475 -27.373 1.00 23.63 C ANISOU 4736 CB LEU C 236 3819 2890 2271 -397 -89 331 C ATOM 4737 CG LEU C 236 -38.314-126.865 -28.397 1.00 23.09 C ANISOU 4737 CG LEU C 236 3723 2823 2225 -376 42 351 C ATOM 4738 CD1 LEU C 236 -37.975-125.664 -29.245 1.00 54.15 C ANISOU 4738 CD1 LEU C 236 7697 6730 6148 -465 -1 319 C ATOM 4739 CD2 LEU C 236 -37.077-127.370 -27.729 1.00 27.78 C ANISOU 4739 CD2 LEU C 236 4192 3438 2925 -432 175 372 C ATOM 4740 N ILE C 237 -40.342-125.896 -24.372 1.00 24.51 N ANISOU 4740 N ILE C 237 3827 3012 2474 -533 -249 310 N ATOM 4741 CA ILE C 237 -41.335-125.380 -23.444 1.00 25.12 C ANISOU 4741 CA ILE C 237 3919 3080 2544 -571 -389 294 C ATOM 4742 C ILE C 237 -41.136-123.894 -23.263 1.00 24.95 C ANISOU 4742 C ILE C 237 3892 3048 2541 -730 -452 249 C ATOM 4743 O ILE C 237 -40.083-123.366 -23.592 1.00 35.81 O ANISOU 4743 O ILE C 237 5226 4427 3952 -823 -370 233 O ATOM 4744 CB ILE C 237 -41.217-126.026 -22.049 1.00 25.48 C ANISOU 4744 CB ILE C 237 3850 3142 2691 -579 -358 318 C ATOM 4745 CG1 ILE C 237 -39.844-125.747 -21.442 1.00 25.03 C ANISOU 4745 CG1 ILE C 237 3654 3099 2756 -699 -230 301 C ATOM 4746 CG2 ILE C 237 -41.466-127.525 -22.119 1.00 48.87 C ANISOU 4746 CG2 ILE C 237 6819 6112 5637 -429 -310 371 C ATOM 4747 CD1 ILE C 237 -39.673-126.311 -20.070 1.00 25.45 C ANISOU 4747 CD1 ILE C 237 3583 3161 2926 -710 -196 317 C ATOM 4748 N GLU C 238 -42.151-123.223 -22.729 1.00 26.29 N ANISOU 4748 N GLU C 238 4104 3202 2681 -767 -601 232 N ATOM 4749 CA GLU C 238 -42.063-121.800 -22.402 1.00 31.57 C ANISOU 4749 CA GLU C 238 4765 3862 3370 -927 -673 194 C ATOM 4750 C GLU C 238 -42.694-121.512 -21.043 1.00 26.16 C ANISOU 4750 C GLU C 238 4024 3179 2736 -987 -763 191 C ATOM 4751 O GLU C 238 -43.582-122.216 -20.611 1.00 32.29 O ANISOU 4751 O GLU C 238 4819 3951 3497 -892 -829 214 O ATOM 4752 CB GLU C 238 -42.744-120.947 -23.469 1.00 39.71 C ANISOU 4752 CB GLU C 238 5933 4856 4297 -926 -795 172 C ATOM 4753 CG GLU C 238 -41.810-120.429 -24.559 1.00 78.19 C ANISOU 4753 CG GLU C 238 10826 9721 9160 -977 -727 160 C ATOM 4754 CD GLU C 238 -42.544-119.649 -25.651 1.00107.21 C ANISOU 4754 CD GLU C 238 14637 13351 12746 -960 -856 139 C ATOM 4755 OE1 GLU C 238 -43.802-119.609 -25.637 1.00 99.69 O ANISOU 4755 OE1 GLU C 238 13773 12375 11730 -894 -988 131 O ATOM 4756 OE2 GLU C 238 -41.856-119.074 -26.527 1.00118.98 O ANISOU 4756 OE2 GLU C 238 16147 14826 14234 -1014 -827 131 O ATOM 4757 N LYS C 239 -42.229-120.469 -20.372 1.00 26.16 N ANISOU 4757 N LYS C 239 3955 3186 2797 -1150 -767 164 N ATOM 4758 CA LYS C 239 -42.937-119.937 -19.217 1.00 65.32 C ANISOU 4758 CA LYS C 239 8875 8144 7799 -1223 -876 157 C ATOM 4759 C LYS C 239 -43.993-118.948 -19.729 1.00 90.30 C ANISOU 4759 C LYS C 239 12170 11274 10866 -1250 -1056 141 C ATOM 4760 O LYS C 239 -43.901-118.479 -20.866 1.00 94.72 O ANISOU 4760 O LYS C 239 12825 11814 11350 -1250 -1074 128 O ATOM 4761 CB LYS C 239 -41.957-119.240 -18.271 1.00 52.34 C ANISOU 4761 CB LYS C 239 7097 6527 6264 -1391 -789 132 C ATOM 4762 CG LYS C 239 -40.900-120.142 -17.677 1.00 31.05 C ANISOU 4762 CG LYS C 239 4264 3857 3674 -1373 -613 139 C ATOM 4763 CD LYS C 239 -39.941-119.344 -16.816 1.00 30.65 C ANISOU 4763 CD LYS C 239 4094 3832 3721 -1547 -523 102 C ATOM 4764 CE LYS C 239 -38.718-120.167 -16.464 1.00 27.00 C ANISOU 4764 CE LYS C 239 3512 3390 3356 -1533 -334 98 C ATOM 4765 NZ LYS C 239 -37.880-119.577 -15.401 1.00 26.64 N ANISOU 4765 NZ LYS C 239 3334 3369 3420 -1686 -237 57 N ATOM 4766 N PRO C 240 -44.978-118.584 -18.883 1.00 97.21 N ANISOU 4766 N PRO C 240 13047 12137 11752 -1281 -1194 142 N ATOM 4767 CA PRO C 240 -45.067-118.888 -17.453 1.00 72.73 C ANISOU 4767 CA PRO C 240 9819 9055 8760 -1312 -1188 155 C ATOM 4768 C PRO C 240 -45.441-120.330 -17.145 1.00 54.41 C ANISOU 4768 C PRO C 240 7479 6737 6457 -1157 -1167 194 C ATOM 4769 O PRO C 240 -46.330-120.900 -17.773 1.00 49.82 O ANISOU 4769 O PRO C 240 7017 6136 5778 -1029 -1249 212 O ATOM 4770 CB PRO C 240 -46.185-117.958 -16.960 1.00 62.59 C ANISOU 4770 CB PRO C 240 8582 7746 7455 -1384 -1378 148 C ATOM 4771 CG PRO C 240 -46.442-116.999 -18.072 1.00 80.59 C ANISOU 4771 CG PRO C 240 10997 9997 9628 -1422 -1462 125 C ATOM 4772 CD PRO C 240 -46.110-117.751 -19.315 1.00 93.68 C ANISOU 4772 CD PRO C 240 12730 11650 11213 -1294 -1380 129 C ATOM 4773 N GLU C 241 -44.733-120.894 -16.174 1.00 66.70 N ANISOU 4773 N GLU C 241 8886 8318 8140 -1174 -1055 206 N ATOM 4774 CA GLU C 241 -45.152-122.097 -15.479 1.00 78.62 C ANISOU 4774 CA GLU C 241 10345 9824 9701 -1063 -1062 248 C ATOM 4775 C GLU C 241 -45.958-121.619 -14.275 1.00 91.81 C ANISOU 4775 C GLU C 241 11960 11483 11440 -1130 -1196 253 C ATOM 4776 O GLU C 241 -46.054-122.314 -13.266 1.00 74.89 O ANISOU 4776 O GLU C 241 9713 9340 9402 -1099 -1192 282 O ATOM 4777 CB GLU C 241 -43.929-122.897 -15.013 1.00 97.87 C ANISOU 4777 CB GLU C 241 12641 12287 12260 -1054 -876 257 C ATOM 4778 CG GLU C 241 -43.075-122.182 -13.950 1.00101.65 C ANISOU 4778 CG GLU C 241 12960 12783 12880 -1207 -793 223 C ATOM 4779 CD GLU C 241 -41.610-122.620 -13.938 1.00 79.37 C ANISOU 4779 CD GLU C 241 10033 9983 10142 -1226 -587 208 C ATOM 4780 OE1 GLU C 241 -41.097-123.074 -14.985 1.00 46.89 O ANISOU 4780 OE1 GLU C 241 5985 5872 5959 -1162 -507 215 O ATOM 4781 OE2 GLU C 241 -40.967-122.496 -12.872 1.00 82.96 O ANISOU 4781 OE2 GLU C 241 10337 10448 10735 -1308 -503 186 O ATOM 4782 N SER C 245 -47.686-125.811 -14.361 1.00 73.75 N ANISOU 4782 N SER C 245 9799 9166 9058 -657 -1278 416 N ATOM 4783 CA SER C 245 -46.776-126.354 -15.372 1.00 62.94 C ANISOU 4783 CA SER C 245 8453 7816 7645 -597 -1116 414 C ATOM 4784 C SER C 245 -46.386-125.375 -16.494 1.00 54.72 C ANISOU 4784 C SER C 245 7491 6782 6518 -653 -1079 362 C ATOM 4785 O SER C 245 -47.161-124.499 -16.874 1.00 49.14 O ANISOU 4785 O SER C 245 6888 6058 5725 -687 -1205 334 O ATOM 4786 CB SER C 245 -47.364-127.627 -15.987 1.00 74.95 C ANISOU 4786 CB SER C 245 10082 9334 9061 -439 -1132 463 C ATOM 4787 OG SER C 245 -46.484-128.175 -16.954 1.00 84.63 O ANISOU 4787 OG SER C 245 11322 10580 10253 -382 -975 465 O ATOM 4788 N PRO C 246 -45.171-125.533 -17.027 1.00 54.37 N ANISOU 4788 N PRO C 246 7398 6758 6504 -663 -910 350 N ATOM 4789 CA PRO C 246 -44.760-124.797 -18.221 1.00 39.20 C ANISOU 4789 CA PRO C 246 5556 4838 4499 -697 -871 313 C ATOM 4790 C PRO C 246 -45.672-125.110 -19.390 1.00 41.49 C ANISOU 4790 C PRO C 246 6018 5114 4633 -577 -946 319 C ATOM 4791 O PRO C 246 -46.399-126.106 -19.384 1.00 52.46 O ANISOU 4791 O PRO C 246 7461 6499 5971 -458 -987 357 O ATOM 4792 CB PRO C 246 -43.381-125.379 -18.536 1.00 43.58 C ANISOU 4792 CB PRO C 246 6027 5415 5115 -688 -676 319 C ATOM 4793 CG PRO C 246 -42.878-125.888 -17.242 1.00 68.69 C ANISOU 4793 CG PRO C 246 9051 8604 8444 -716 -612 337 C ATOM 4794 CD PRO C 246 -44.083-126.356 -16.476 1.00 71.35 C ANISOU 4794 CD PRO C 246 9406 8925 8779 -654 -753 372 C ATOM 4795 N VAL C 247 -45.580-124.276 -20.414 1.00 34.97 N ANISOU 4795 N VAL C 247 5275 4278 3734 -611 -958 282 N ATOM 4796 CA VAL C 247 -46.320-124.451 -21.641 1.00 28.01 C ANISOU 4796 CA VAL C 247 4550 3379 2714 -504 -1011 275 C ATOM 4797 C VAL C 247 -45.448-125.135 -22.683 1.00 37.44 C ANISOU 4797 C VAL C 247 5746 4589 3891 -431 -855 287 C ATOM 4798 O VAL C 247 -44.277-124.817 -22.816 1.00 51.12 O ANISOU 4798 O VAL C 247 7397 6334 5693 -508 -741 278 O ATOM 4799 CB VAL C 247 -46.789-123.095 -22.159 1.00 41.75 C ANISOU 4799 CB VAL C 247 6379 5088 4396 -582 -1130 228 C ATOM 4800 CG1 VAL C 247 -47.144-123.164 -23.635 1.00 42.07 C ANISOU 4800 CG1 VAL C 247 6557 5108 4320 -484 -1138 210 C ATOM 4801 CG2 VAL C 247 -47.964-122.624 -21.329 1.00 45.94 C ANISOU 4801 CG2 VAL C 247 6946 5596 4912 -616 -1309 223 C ATOM 4802 N ILE C 248 -46.032-126.086 -23.407 1.00 46.57 N ANISOU 4802 N ILE C 248 6997 5746 4953 -286 -849 308 N ATOM 4803 CA ILE C 248 -45.338-126.866 -24.434 1.00 27.17 C ANISOU 4803 CA ILE C 248 4547 3304 2473 -201 -705 326 C ATOM 4804 C ILE C 248 -45.454-126.227 -25.807 1.00 28.37 C ANISOU 4804 C ILE C 248 4801 3434 2544 -181 -720 288 C ATOM 4805 O ILE C 248 -46.559-125.993 -26.305 1.00 68.74 O ANISOU 4805 O ILE C 248 10042 8521 7554 -124 -834 263 O ATOM 4806 CB ILE C 248 -45.930-128.294 -24.536 1.00 60.40 C ANISOU 4806 CB ILE C 248 8807 7528 6616 -51 -682 373 C ATOM 4807 CG1 ILE C 248 -45.607-129.106 -23.276 1.00 63.13 C ANISOU 4807 CG1 ILE C 248 9035 7892 7061 -60 -645 423 C ATOM 4808 CG2 ILE C 248 -45.431-129.003 -25.793 1.00 56.45 C ANISOU 4808 CG2 ILE C 248 8339 7040 6068 44 -551 387 C ATOM 4809 CD1 ILE C 248 -46.310-130.451 -23.205 1.00 60.08 C ANISOU 4809 CD1 ILE C 248 8704 7515 6607 71 -654 476 C ATOM 4810 N VAL C 249 -44.312-125.948 -26.420 1.00 34.56 N ANISOU 4810 N VAL C 249 4683 4861 3585 510 -280 -1027 N ATOM 4811 CA VAL C 249 -44.289-125.495 -27.800 1.00 23.85 C ANISOU 4811 CA VAL C 249 3319 3459 2283 506 -192 -1074 C ATOM 4812 C VAL C 249 -44.386-126.685 -28.727 1.00 32.52 C ANISOU 4812 C VAL C 249 4492 4639 3226 520 -76 -1067 C ATOM 4813 O VAL C 249 -43.461-127.481 -28.806 1.00 49.90 O ANISOU 4813 O VAL C 249 6707 6851 5404 522 -40 -963 O ATOM 4814 CB VAL C 249 -42.991-124.818 -28.123 1.00 29.82 C ANISOU 4814 CB VAL C 249 4013 4097 3221 485 -194 -992 C ATOM 4815 CG1 VAL C 249 -42.956-124.481 -29.613 1.00 30.57 C ANISOU 4815 CG1 VAL C 249 4106 4146 3364 478 -92 -1030 C ATOM 4816 CG2 VAL C 249 -42.801-123.597 -27.230 1.00 48.37 C ANISOU 4816 CG2 VAL C 249 6274 6375 5727 475 -298 -977 C ATOM 4817 N LYS C 250 -45.507-126.821 -29.420 1.00 49.67 N ANISOU 4817 N LYS C 250 6709 6871 5292 534 -8 -1172 N ATOM 4818 CA LYS C 250 -45.667-127.928 -30.343 1.00 61.16 C ANISOU 4818 CA LYS C 250 8229 8408 6600 554 122 -1162 C ATOM 4819 C LYS C 250 -44.729-127.747 -31.528 1.00 52.24 C ANISOU 4819 C LYS C 250 7067 7190 5594 564 227 -1121 C ATOM 4820 O LYS C 250 -44.334-126.625 -31.867 1.00 40.28 O ANISOU 4820 O LYS C 250 5502 5543 4261 540 213 -1132 O ATOM 4821 CB LYS C 250 -47.119-128.048 -30.811 1.00 67.87 C ANISOU 4821 CB LYS C 250 9136 9336 7314 568 175 -1294 C ATOM 4822 CG LYS C 250 -48.041-128.751 -29.831 1.00 78.94 C ANISOU 4822 CG LYS C 250 10590 10875 8527 569 103 -1317 C ATOM 4823 CD LYS C 250 -49.452-128.887 -30.401 1.00 93.28 C ANISOU 4823 CD LYS C 250 12472 12770 10201 581 167 -1453 C ATOM 4824 CE LYS C 250 -50.339-129.786 -29.541 1.00 99.88 C ANISOU 4824 CE LYS C 250 13371 13760 10820 579 108 -1462 C ATOM 4825 NZ LYS C 250 -50.536-129.253 -28.161 1.00100.97 N ANISOU 4825 NZ LYS C 250 13471 13886 11006 562 -48 -1469 N ATOM 4826 N THR C 251 -44.349-128.857 -32.143 1.00 45.67 N ANISOU 4826 N THR C 251 6241 6459 4655 622 318 -1069 N ATOM 4827 CA THR C 251 -43.601-128.773 -33.379 1.00 40.16 C ANISOU 4827 CA THR C 251 5505 5687 4068 640 441 -1038 C ATOM 4828 C THR C 251 -44.524-128.263 -34.478 1.00 56.91 C ANISOU 4828 C THR C 251 7654 7753 6216 631 553 -1149 C ATOM 4829 O THR C 251 -45.736-128.188 -34.293 1.00 42.38 O ANISOU 4829 O THR C 251 5870 5961 4271 624 541 -1248 O ATOM 4830 CB THR C 251 -43.091-130.114 -33.811 1.00 30.05 C ANISOU 4830 CB THR C 251 4219 4536 2664 707 530 -934 C ATOM 4831 OG1 THR C 251 -42.322-129.936 -35.001 1.00 56.60 O ANISOU 4831 OG1 THR C 251 7525 7806 6173 716 650 -898 O ATOM 4832 CG2 THR C 251 -44.247-131.022 -34.138 1.00 28.13 C ANISOU 4832 CG2 THR C 251 4036 4447 2205 736 609 -984 C ATOM 4833 N ALA C 252 -43.945-127.922 -35.625 1.00 62.33 N ANISOU 4833 N ALA C 252 8304 8332 7047 637 664 -1126 N ATOM 4834 CA ALA C 252 -44.729-127.460 -36.766 1.00 41.36 C ANISOU 4834 CA ALA C 252 5680 5607 4426 650 784 -1206 C ATOM 4835 C ALA C 252 -45.854-128.449 -37.074 1.00 46.69 C ANISOU 4835 C ALA C 252 6417 6437 4886 684 876 -1288 C ATOM 4836 O ALA C 252 -47.028-128.099 -36.984 1.00 78.23 O ANISOU 4836 O ALA C 252 10474 10443 8809 680 861 -1395 O ATOM 4837 CB ALA C 252 -43.833-127.263 -37.974 1.00 37.16 C ANISOU 4837 CB ALA C 252 5098 4958 4063 670 907 -1131 C ATOM 4838 N ASP C 253 -45.496-129.684 -37.414 1.00 42.73 N ANISOU 4838 N ASP C 253 5896 6064 4277 718 964 -1225 N ATOM 4839 CA ASP C 253 -46.475-130.738 -37.682 1.00 45.96 C ANISOU 4839 CA ASP C 253 6365 6637 4459 748 1050 -1271 C ATOM 4840 C ASP C 253 -47.404-130.997 -36.496 1.00 45.94 C ANISOU 4840 C ASP C 253 6434 6754 4266 738 922 -1320 C ATOM 4841 O ASP C 253 -48.170-131.957 -36.512 1.00 53.30 O ANISOU 4841 O ASP C 253 7423 7840 4987 759 968 -1338 O ATOM 4842 CB ASP C 253 -45.775-132.060 -38.023 1.00 86.94 C ANISOU 4842 CB ASP C 253 11514 11962 9558 789 1130 -1137 C ATOM 4843 CG ASP C 253 -44.865-131.957 -39.234 1.00114.25 C ANISOU 4843 CG ASP C 253 14878 15326 13206 793 1258 -1083 C ATOM 4844 OD1 ASP C 253 -45.070-131.044 -40.066 1.00121.69 O ANISOU 4844 OD1 ASP C 253 15806 16115 14315 767 1337 -1174 O ATOM 4845 OD2 ASP C 253 -43.949-132.799 -39.357 1.00117.46 O ANISOU 4845 OD2 ASP C 253 15228 15802 13600 829 1278 -930 O ATOM 4846 N GLN C 254 -47.299-130.182 -35.451 1.00 48.86 N ANISOU 4846 N GLN C 254 6795 7054 4716 701 762 -1330 N ATOM 4847 CA GLN C 254 -48.241-130.246 -34.338 1.00 50.26 C ANISOU 4847 CA GLN C 254 7027 7315 4755 679 641 -1386 C ATOM 4848 C GLN C 254 -48.118-131.466 -33.422 1.00 52.50 C ANISOU 4848 C GLN C 254 7326 7772 4849 701 572 -1287 C ATOM 4849 O GLN C 254 -49.119-131.957 -32.920 1.00 56.94 O ANISOU 4849 O GLN C 254 7952 8450 5232 697 537 -1334 O ATOM 4850 CB GLN C 254 -49.664-130.160 -34.874 1.00 56.76 C ANISOU 4850 CB GLN C 254 7927 8167 5472 680 715 -1529 C ATOM 4851 CG GLN C 254 -50.011-128.790 -35.340 1.00 51.16 C ANISOU 4851 CG GLN C 254 7210 7291 4939 661 721 -1621 C ATOM 4852 CD GLN C 254 -50.081-127.840 -34.180 1.00 70.50 C ANISOU 4852 CD GLN C 254 9608 9704 7474 634 537 -1649 C ATOM 4853 OE1 GLN C 254 -49.548-126.726 -34.228 1.00 79.48 O ANISOU 4853 OE1 GLN C 254 10671 10717 8813 623 485 -1642 O ATOM 4854 NE2 GLN C 254 -50.745-128.273 -33.115 1.00 71.64 N ANISOU 4854 NE2 GLN C 254 9787 9962 7470 621 439 -1672 N ATOM 4855 N GLN C 255 -46.898-131.941 -33.198 1.00 61.02 N ANISOU 4855 N GLN C 255 8352 8864 5968 727 553 -1140 N ATOM 4856 CA GLN C 255 -46.642-132.990 -32.214 1.00 53.20 C ANISOU 4856 CA GLN C 255 7372 8010 4833 750 473 -1011 C ATOM 4857 C GLN C 255 -46.157-132.363 -30.921 1.00 36.48 C ANISOU 4857 C GLN C 255 5224 5814 2822 716 309 -979 C ATOM 4858 O GLN C 255 -45.651-131.240 -30.923 1.00 42.83 O ANISOU 4858 O GLN C 255 5984 6462 3827 684 272 -1015 O ATOM 4859 CB GLN C 255 -45.586-133.973 -32.721 1.00 76.08 C ANISOU 4859 CB GLN C 255 10232 10965 7711 804 559 -839 C ATOM 4860 CG GLN C 255 -46.119-135.092 -33.593 1.00 98.81 C ANISOU 4860 CG GLN C 255 13145 13981 10416 840 701 -810 C ATOM 4861 CD GLN C 255 -45.060-136.139 -33.879 1.00114.77 C ANISOU 4861 CD GLN C 255 15123 16056 12427 890 767 -599 C ATOM 4862 OE1 GLN C 255 -43.869-135.911 -33.654 1.00117.32 O ANISOU 4862 OE1 GLN C 255 15388 16292 12895 900 729 -488 O ATOM 4863 NE2 GLN C 255 -45.489-137.295 -34.370 1.00115.47 N ANISOU 4863 NE2 GLN C 255 15242 16281 12351 918 867 -533 N ATOM 4864 N ASP C 256 -46.299-133.086 -29.814 1.00 31.24 N ANISOU 4864 N ASP C 256 4582 5252 2037 717 214 -901 N ATOM 4865 CA ASP C 256 -45.919-132.548 -28.513 1.00 27.29 C ANISOU 4865 CA ASP C 256 4054 4676 1640 679 67 -870 C ATOM 4866 C ASP C 256 -44.418-132.656 -28.263 1.00 46.51 C ANISOU 4866 C ASP C 256 6431 7047 4193 700 45 -723 C ATOM 4867 O ASP C 256 -43.854-131.985 -27.385 1.00 33.72 O ANISOU 4867 O ASP C 256 4778 5320 2714 666 -55 -704 O ATOM 4868 CB ASP C 256 -46.686-133.231 -27.390 1.00 28.70 C ANISOU 4868 CB ASP C 256 4276 4966 1660 662 -23 -845 C ATOM 4869 CG ASP C 256 -48.148-132.861 -27.376 1.00 95.78 C ANISOU 4869 CG ASP C 256 12830 13493 10070 628 -34 -1001 C ATOM 4870 OD1 ASP C 256 -48.521-131.883 -28.060 1.00101.16 O ANISOU 4870 OD1 ASP C 256 13508 14077 10850 610 11 -1127 O ATOM 4871 OD2 ASP C 256 -48.926-133.540 -26.672 1.00 97.80 O ANISOU 4871 OD2 ASP C 256 13135 13864 10162 618 -88 -990 O ATOM 4872 N TYR C 257 -43.759-133.503 -29.038 1.00 37.53 N ANISOU 4872 N TYR C 257 5284 5971 3007 755 147 -610 N ATOM 4873 CA TYR C 257 -42.342-133.683 -28.833 1.00 24.30 C ANISOU 4873 CA TYR C 257 3560 4237 1435 778 136 -455 C ATOM 4874 C TYR C 257 -41.664-134.254 -30.075 1.00 24.90 C ANISOU 4874 C TYR C 257 3614 4333 1516 831 284 -357 C ATOM 4875 O TYR C 257 -42.319-134.731 -30.996 1.00 34.33 O ANISOU 4875 O TYR C 257 4829 5608 2607 853 395 -392 O ATOM 4876 CB TYR C 257 -42.118-134.576 -27.616 1.00 34.21 C ANISOU 4876 CB TYR C 257 4820 5559 2619 772 51 -311 C ATOM 4877 CG TYR C 257 -42.630-135.971 -27.815 1.00 26.06 C ANISOU 4877 CG TYR C 257 3818 4693 1392 803 114 -215 C ATOM 4878 CD1 TYR C 257 -43.785-136.401 -27.194 1.00 33.31 C ANISOU 4878 CD1 TYR C 257 4786 5717 2153 780 60 -264 C ATOM 4879 CD2 TYR C 257 -41.969-136.849 -28.658 1.00 31.14 C ANISOU 4879 CD2 TYR C 257 4436 5378 2017 850 232 -69 C ATOM 4880 CE1 TYR C 257 -44.261-137.695 -27.395 1.00 53.31 C ANISOU 4880 CE1 TYR C 257 7351 8404 4502 806 117 -174 C ATOM 4881 CE2 TYR C 257 -42.426-138.130 -28.867 1.00 39.29 C ANISOU 4881 CE2 TYR C 257 5490 6552 2885 874 295 26 C ATOM 4882 CZ TYR C 257 -43.570-138.556 -28.233 1.00 55.73 C ANISOU 4882 CZ TYR C 257 7628 8747 4799 853 236 -28 C ATOM 4883 OH TYR C 257 -44.014-139.845 -28.445 1.00 62.17 O ANISOU 4883 OH TYR C 257 8469 9707 5446 876 297 70 O ATOM 4884 N LEU C 258 -40.339-134.197 -30.076 1.00 29.38 N ANISOU 4884 N LEU C 258 4137 4815 2212 847 290 -228 N ATOM 4885 CA LEU C 258 -39.534-134.592 -31.216 1.00 28.60 C ANISOU 4885 CA LEU C 258 4001 4694 2172 887 429 -115 C ATOM 4886 C LEU C 258 -38.698-135.787 -30.818 1.00 34.08 C ANISOU 4886 C LEU C 258 4669 5431 2848 905 441 124 C ATOM 4887 O LEU C 258 -38.073-135.771 -29.767 1.00 53.74 O ANISOU 4887 O LEU C 258 7147 7873 5400 879 339 204 O ATOM 4888 CB LEU C 258 -38.619-133.430 -31.623 1.00 19.77 C ANISOU 4888 CB LEU C 258 2844 3403 1265 874 435 -155 C ATOM 4889 CG LEU C 258 -37.786-133.641 -32.877 1.00 23.31 C ANISOU 4889 CG LEU C 258 3240 3788 1827 899 582 -48 C ATOM 4890 CD1 LEU C 258 -38.659-134.090 -34.020 1.00 26.62 C ANISOU 4890 CD1 LEU C 258 3665 4285 2165 915 709 -110 C ATOM 4891 CD2 LEU C 258 -37.026-132.376 -33.227 1.00 47.18 C ANISOU 4891 CD2 LEU C 258 6223 6625 5080 867 572 -112 C ATOM 4892 N ASN C 259 -38.711-136.828 -31.649 1.00 51.79 N ANISOU 4892 N ASN C 259 6898 7748 5033 937 562 232 N ATOM 4893 CA ASN C 259 -37.891-138.021 -31.448 1.00 23.59 C ANISOU 4893 CA ASN C 259 3283 4189 1490 942 585 460 C ATOM 4894 C ASN C 259 -36.519-137.820 -32.059 1.00 25.88 C ANISOU 4894 C ASN C 259 3505 4330 1997 937 644 581 C ATOM 4895 O ASN C 259 -36.417-137.523 -33.250 1.00 29.24 O ANISOU 4895 O ASN C 259 3912 4711 2486 955 752 554 O ATOM 4896 CB ASN C 259 -38.547-139.223 -32.122 1.00 32.75 C ANISOU 4896 CB ASN C 259 4456 5484 2504 973 687 514 C ATOM 4897 CG ASN C 259 -39.692-139.802 -31.312 1.00 39.13 C ANISOU 4897 CG ASN C 259 5323 6440 3105 967 619 465 C ATOM 4898 OD1 ASN C 259 -39.551-140.059 -30.120 1.00 54.03 O ANISOU 4898 OD1 ASN C 259 7209 8332 4989 939 508 523 O ATOM 4899 ND2 ASN C 259 -40.828-140.012 -31.960 1.00 29.83 N ANISOU 4899 ND2 ASN C 259 4195 5373 1765 983 689 356 N ATOM 4900 N ILE C 260 -35.458-137.983 -31.264 1.00 20.57 N ANISOU 4900 N ILE C 260 2787 3564 1463 898 573 706 N ATOM 4901 CA ILE C 260 -34.119-137.694 -31.743 1.00 18.95 C ANISOU 4901 CA ILE C 260 2513 3194 1492 871 607 798 C ATOM 4902 C ILE C 260 -33.075-138.685 -31.303 1.00 29.98 C ANISOU 4902 C ILE C 260 3836 4531 3023 824 583 944 C ATOM 4903 O ILE C 260 -33.274-139.417 -30.348 1.00 46.33 O ANISOU 4903 O ILE C 260 5915 6664 5026 805 522 979 O ATOM 4904 CB ILE C 260 -33.656-136.356 -31.209 1.00 26.52 C ANISOU 4904 CB ILE C 260 3482 4030 2564 832 525 720 C ATOM 4905 CG1 ILE C 260 -33.755-136.374 -29.691 1.00 30.44 C ANISOU 4905 CG1 ILE C 260 4000 4537 3031 783 383 696 C ATOM 4906 CG2 ILE C 260 -34.495-135.226 -31.787 1.00 43.74 C ANISOU 4906 CG2 ILE C 260 5719 6234 4667 871 557 537 C ATOM 4907 CD1 ILE C 260 -32.871-135.346 -29.010 1.00 45.09 C ANISOU 4907 CD1 ILE C 260 5839 6223 5069 704 289 659 C ATOM 4908 N THR C 261 -31.945-138.689 -31.997 1.00 24.78 N ANISOU 4908 N THR C 261 3103 3745 2568 798 626 1005 N ATOM 4909 CA THR C 261 -30.762-139.400 -31.530 1.00 22.42 C ANISOU 4909 CA THR C 261 2725 3365 2427 730 587 1072 C ATOM 4910 C THR C 261 -29.700-138.352 -31.470 1.00 30.52 C ANISOU 4910 C THR C 261 3709 4234 3651 644 537 995 C ATOM 4911 O THR C 261 -29.761-137.404 -32.257 1.00 34.31 O ANISOU 4911 O THR C 261 4195 4662 4178 663 574 951 O ATOM 4912 CB THR C 261 -30.280-140.425 -32.550 1.00 28.66 C ANISOU 4912 CB THR C 261 3453 4159 3278 765 676 1172 C ATOM 4913 OG1 THR C 261 -30.027-139.763 -33.791 1.00 23.72 O ANISOU 4913 OG1 THR C 261 2808 3457 2747 787 740 1154 O ATOM 4914 CG2 THR C 261 -31.329-141.504 -32.767 1.00 29.03 C ANISOU 4914 CG2 THR C 261 3541 4368 3121 839 740 1243 C ATOM 4915 N PHE C 262 -28.719-138.486 -30.584 1.00 13.88 N ANISOU 4915 N PHE C 262 1561 2060 1654 551 464 970 N ATOM 4916 CA PHE C 262 -27.622-137.515 -30.608 1.00 23.53 C ANISOU 4916 CA PHE C 262 2714 3178 3047 481 444 902 C ATOM 4917 C PHE C 262 -26.550-137.918 -31.601 1.00 32.16 C ANISOU 4917 C PHE C 262 3687 4246 4286 497 513 953 C ATOM 4918 O PHE C 262 -25.523-137.248 -31.721 1.00 34.91 O ANISOU 4918 O PHE C 262 3973 4531 4762 429 488 893 O ATOM 4919 CB PHE C 262 -26.993-137.303 -29.239 1.00 25.89 C ANISOU 4919 CB PHE C 262 2986 3451 3402 406 371 868 C ATOM 4920 CG PHE C 262 -27.866-136.560 -28.291 1.00 28.83 C ANISOU 4920 CG PHE C 262 3467 3813 3673 381 284 792 C ATOM 4921 CD1 PHE C 262 -27.751-135.191 -28.153 1.00 18.84 C ANISOU 4921 CD1 PHE C 262 2232 2471 2457 320 231 682 C ATOM 4922 CD2 PHE C 262 -28.802-137.235 -27.526 1.00 35.68 C ANISOU 4922 CD2 PHE C 262 4401 4758 4399 420 249 829 C ATOM 4923 CE1 PHE C 262 -28.546-134.510 -27.269 1.00 15.88 C ANISOU 4923 CE1 PHE C 262 1952 2078 2003 310 138 610 C ATOM 4924 CE2 PHE C 262 -29.614-136.562 -26.647 1.00 15.69 C ANISOU 4924 CE2 PHE C 262 1958 2222 1782 405 156 753 C ATOM 4925 CZ PHE C 262 -29.482-135.194 -26.518 1.00 31.69 C ANISOU 4925 CZ PHE C 262 4014 4156 3872 355 97 644 C ATOM 4926 N ASP C 263 -26.782-139.008 -32.319 1.00 20.23 N ANISOU 4926 N ASP C 263 2164 2786 2739 575 580 1052 N ATOM 4927 CA ASP C 263 -25.803-139.395 -33.308 1.00 23.62 C ANISOU 4927 CA ASP C 263 2485 3181 3309 600 635 1103 C ATOM 4928 C ASP C 263 -26.299-139.218 -34.722 1.00 29.83 C ANISOU 4928 C ASP C 263 3309 3944 4081 656 697 1111 C ATOM 4929 O ASP C 263 -27.487-139.410 -34.993 1.00 30.80 O ANISOU 4929 O ASP C 263 3531 4118 4052 699 727 1129 O ATOM 4930 CB ASP C 263 -25.336-140.828 -33.079 1.00 24.94 C ANISOU 4930 CB ASP C 263 2578 3402 3497 641 667 1223 C ATOM 4931 CG ASP C 263 -24.494-140.961 -31.844 1.00 32.85 C ANISOU 4931 CG ASP C 263 3538 4390 4554 562 600 1202 C ATOM 4932 OD1 ASP C 263 -23.419-140.322 -31.767 1.00 57.17 O ANISOU 4932 OD1 ASP C 263 6621 7386 7716 462 531 1103 O ATOM 4933 OD2 ASP C 263 -24.903-141.725 -30.952 1.00 57.71 O ANISOU 4933 OD2 ASP C 263 6684 7608 7635 586 599 1270 O ATOM 4934 N LYS C 264 -25.373-138.916 -35.616 1.00 27.05 N ANISOU 4934 N LYS C 264 2940 3505 3834 589 676 1059 N ATOM 4935 CA LYS C 264 -25.619-138.709 -37.025 1.00 26.82 C ANISOU 4935 CA LYS C 264 2932 3434 3825 623 730 1068 C ATOM 4936 C LYS C 264 -25.929-140.001 -37.736 1.00 44.51 C ANISOU 4936 C LYS C 264 5145 5727 6039 741 831 1217 C ATOM 4937 O LYS C 264 -25.653-141.061 -37.214 1.00 62.36 O ANISOU 4937 O LYS C 264 7354 8052 8287 780 847 1306 O ATOM 4938 CB LYS C 264 -24.383-138.131 -37.662 1.00 47.95 C ANISOU 4938 CB LYS C 264 5578 6030 6612 528 672 986 C ATOM 4939 CG LYS C 264 -24.022-136.760 -37.195 1.00 66.61 C ANISOU 4939 CG LYS C 264 7964 8357 8988 422 575 846 C ATOM 4940 CD LYS C 264 -23.068-136.094 -38.149 1.00 79.95 C ANISOU 4940 CD LYS C 264 9633 9998 10747 362 528 775 C ATOM 4941 CE LYS C 264 -22.947-134.625 -37.822 1.00 94.62 C ANISOU 4941 CE LYS C 264 11519 11843 12591 277 438 647 C ATOM 4942 NZ LYS C 264 -21.810-133.951 -38.496 1.00 96.80 N ANISOU 4942 NZ LYS C 264 11773 12101 12904 200 418 605 N ATOM 4943 N GLY C 265 -26.526-139.919 -38.917 1.00 44.27 N ANISOU 4943 N GLY C 265 5148 5672 6002 801 906 1250 N ATOM 4944 CA GLY C 265 -26.717-141.092 -39.753 1.00 47.86 C ANISOU 4944 CA GLY C 265 5579 6164 6441 895 1006 1383 C ATOM 4945 C GLY C 265 -27.880-142.011 -39.421 1.00 42.66 C ANISOU 4945 C GLY C 265 4987 5649 5571 937 1071 1450 C ATOM 4946 O GLY C 265 -28.143-142.980 -40.136 1.00 58.22 O ANISOU 4946 O GLY C 265 6955 7672 7494 987 1158 1539 O ATOM 4947 N VAL C 266 -28.593-141.716 -38.349 1.00 26.55 N ANISOU 4947 N VAL C 266 3005 3686 3398 920 1031 1402 N ATOM 4948 CA VAL C 266 -29.692-142.573 -37.968 1.00 22.39 C ANISOU 4948 CA VAL C 266 2535 3320 2652 960 1080 1446 C ATOM 4949 C VAL C 266 -30.936-142.187 -38.748 1.00 51.17 C ANISOU 4949 C VAL C 266 6257 7042 6143 998 1179 1393 C ATOM 4950 O VAL C 266 -31.392-141.050 -38.664 1.00 36.14 O ANISOU 4950 O VAL C 266 4399 5119 4214 979 1165 1284 O ATOM 4951 CB VAL C 266 -29.989-142.458 -36.476 1.00 37.87 C ANISOU 4951 CB VAL C 266 4526 5343 4519 927 988 1405 C ATOM 4952 CG1 VAL C 266 -31.226-143.274 -36.111 1.00 46.33 C ANISOU 4952 CG1 VAL C 266 5663 6595 5345 970 1027 1432 C ATOM 4953 CG2 VAL C 266 -28.773-142.916 -35.662 1.00 42.80 C ANISOU 4953 CG2 VAL C 266 5071 5903 5290 869 904 1427 C ATOM 4954 N TYR C 267 -31.475-143.129 -39.518 1.00 46.40 N ANISOU 4954 N TYR C 267 5662 6530 5439 1045 1285 1449 N ATOM 4955 CA TYR C 267 -32.758-142.911 -40.179 1.00 37.15 C ANISOU 4955 CA TYR C 267 4556 5467 4094 1071 1389 1359 C ATOM 4956 C TYR C 267 -33.795-143.937 -39.760 1.00 29.34 C ANISOU 4956 C TYR C 267 3615 4671 2860 1107 1426 1373 C ATOM 4957 O TYR C 267 -33.540-145.134 -39.764 1.00 60.32 O ANISOU 4957 O TYR C 267 7508 8640 6771 1131 1448 1497 O ATOM 4958 CB TYR C 267 -32.631-142.871 -41.703 1.00 46.41 C ANISOU 4958 CB TYR C 267 5700 6569 5364 1086 1501 1368 C ATOM 4959 CG TYR C 267 -33.978-142.813 -42.379 1.00 40.11 C ANISOU 4959 CG TYR C 267 4956 5897 4387 1109 1619 1253 C ATOM 4960 CD1 TYR C 267 -34.702-141.639 -42.417 1.00 57.45 C ANISOU 4960 CD1 TYR C 267 7190 8096 6541 1087 1622 1075 C ATOM 4961 CD2 TYR C 267 -34.533-143.936 -42.952 1.00 55.41 C ANISOU 4961 CD2 TYR C 267 6901 7951 6201 1151 1726 1305 C ATOM 4962 CE1 TYR C 267 -35.942-141.581 -43.022 1.00 66.96 C ANISOU 4962 CE1 TYR C 267 8435 9413 7595 1104 1725 934 C ATOM 4963 CE2 TYR C 267 -35.770-143.890 -43.559 1.00 64.13 C ANISOU 4963 CE2 TYR C 267 8052 9171 7142 1167 1834 1178 C ATOM 4964 CZ TYR C 267 -36.467-142.707 -43.588 1.00 52.22 C ANISOU 4964 CZ TYR C 267 6578 7661 5604 1142 1832 985 C ATOM 4965 OH TYR C 267 -37.694-142.640 -44.184 1.00 46.38 O ANISOU 4965 OH TYR C 267 5877 7029 4715 1152 1935 832 O ATOM 4966 N SER C 268 -34.973-143.440 -39.411 1.00 43.76 N ANISOU 4966 N SER C 268 5516 6612 4497 1107 1427 1233 N ATOM 4967 CA SER C 268 -36.026-144.227 -38.800 1.00 31.83 C ANISOU 4967 CA SER C 268 4066 5288 2741 1128 1428 1219 C ATOM 4968 C SER C 268 -37.152-144.501 -39.758 1.00 36.92 C ANISOU 4968 C SER C 268 4756 6050 3222 1155 1558 1132 C ATOM 4969 O SER C 268 -37.758-143.573 -40.279 1.00 65.22 O ANISOU 4969 O SER C 268 8368 9624 6788 1145 1601 968 O ATOM 4970 CB SER C 268 -36.592-143.474 -37.605 1.00 35.92 C ANISOU 4970 CB SER C 268 4641 5853 3153 1104 1313 1101 C ATOM 4971 OG SER C 268 -37.848-144.007 -37.239 1.00 45.75 O ANISOU 4971 OG SER C 268 5958 7280 4145 1119 1321 1037 O ATOM 4972 N ASP C 269 -37.450-145.776 -39.973 1.00 36.31 N ANISOU 4972 N ASP C 269 4683 6083 3031 1185 1623 1230 N ATOM 4973 CA ASP C 269 -38.562-146.157 -40.817 1.00 44.48 C ANISOU 4973 CA ASP C 269 5765 7242 3892 1206 1752 1149 C ATOM 4974 C ASP C 269 -39.898-145.992 -40.093 1.00 45.95 C ANISOU 4974 C ASP C 269 6046 7586 3827 1195 1713 998 C ATOM 4975 O ASP C 269 -40.952-145.939 -40.721 1.00 59.96 O ANISOU 4975 O ASP C 269 7872 9451 5458 1197 1806 863 O ATOM 4976 CB ASP C 269 -38.383-147.603 -41.287 1.00 70.82 C ANISOU 4976 CB ASP C 269 9074 10641 7194 1241 1835 1315 C ATOM 4977 CG ASP C 269 -37.160-147.781 -42.181 1.00 73.89 C ANISOU 4977 CG ASP C 269 9372 10872 7831 1254 1883 1443 C ATOM 4978 OD1 ASP C 269 -36.861-146.869 -42.987 1.00 65.25 O ANISOU 4978 OD1 ASP C 269 8252 9657 6884 1241 1920 1371 O ATOM 4979 OD2 ASP C 269 -36.501-148.838 -42.079 1.00 73.58 O ANISOU 4979 OD2 ASP C 269 9285 10826 7845 1275 1879 1611 O ATOM 4980 N MET C 270 -39.852-145.918 -38.768 1.00 41.54 N ANISOU 4980 N MET C 270 5508 7052 3223 1178 1571 1015 N ATOM 4981 CA MET C 270 -41.067-145.787 -37.972 1.00 39.98 C ANISOU 4981 CA MET C 270 5398 6994 2799 1163 1508 882 C ATOM 4982 C MET C 270 -41.636-144.376 -38.083 1.00 53.98 C ANISOU 4982 C MET C 270 7208 8720 4580 1138 1488 655 C ATOM 4983 O MET C 270 -42.855-144.172 -38.141 1.00 54.10 O ANISOU 4983 O MET C 270 7297 8835 4422 1127 1509 487 O ATOM 4984 CB MET C 270 -40.770-146.139 -36.501 1.00 43.04 C ANISOU 4984 CB MET C 270 5784 7404 3164 1149 1356 980 C ATOM 4985 CG MET C 270 -41.904-145.847 -35.510 1.00 53.36 C ANISOU 4985 CG MET C 270 7176 8826 4274 1126 1254 844 C ATOM 4986 SD MET C 270 -41.668-146.651 -33.721 1.00 82.21 S ANISOU 4986 SD MET C 270 10823 12532 7882 1106 1083 994 S ATOM 4987 CE MET C 270 -43.268-145.937 -32.846 1.00276.84 C ANISOU 4987 CE MET C 270 35586 37300 32300 1072 972 765 C ATOM 4988 N TYR C 271 -40.740-143.399 -38.110 1.00 41.66 N ANISOU 4988 N TYR C 271 5700 4591 5536 1038 2082 952 N ATOM 4989 CA TYR C 271 -41.131-142.008 -38.190 1.00 31.05 C ANISOU 4989 CA TYR C 271 4406 3262 4131 1040 2038 903 C ATOM 4990 C TYR C 271 -40.744-141.441 -39.555 1.00 37.28 C ANISOU 4990 C TYR C 271 5157 4055 4951 1048 2061 900 C ATOM 4991 O TYR C 271 -40.863-140.247 -39.802 1.00 54.34 O ANISOU 4991 O TYR C 271 7351 6221 7073 1048 2031 859 O ATOM 4992 CB TYR C 271 -40.461-141.217 -37.077 1.00 33.52 C ANISOU 4992 CB TYR C 271 4770 3537 4431 997 2008 860 C ATOM 4993 CG TYR C 271 -40.586-141.846 -35.702 1.00 45.52 C ANISOU 4993 CG TYR C 271 6315 5043 5936 985 1992 862 C ATOM 4994 CD1 TYR C 271 -39.538-142.562 -35.147 1.00 45.33 C ANISOU 4994 CD1 TYR C 271 6269 4978 5976 956 2024 877 C ATOM 4995 CD2 TYR C 271 -41.745-141.710 -34.956 1.00 63.30 C ANISOU 4995 CD2 TYR C 271 8612 7325 8113 1002 1942 846 C ATOM 4996 CE1 TYR C 271 -39.646-143.132 -33.897 1.00 48.91 C ANISOU 4996 CE1 TYR C 271 6745 5421 6417 947 2009 876 C ATOM 4997 CE2 TYR C 271 -41.859-142.277 -33.705 1.00 59.46 C ANISOU 4997 CE2 TYR C 271 8145 6827 7618 992 1926 846 C ATOM 4998 CZ TYR C 271 -40.813-142.990 -33.183 1.00 43.59 C ANISOU 4998 CZ TYR C 271 6113 4778 5669 966 1960 860 C ATOM 4999 OH TYR C 271 -40.931-143.546 -31.930 1.00 48.09 O ANISOU 4999 OH TYR C 271 6703 5339 6230 959 1944 857 O ATOM 5000 N ASN C 272 -40.314-142.325 -40.447 1.00 45.31 N ANISOU 5000 N ASN C 272 6103 5072 6041 1056 2113 945 N ATOM 5001 CA ASN C 272 -39.791-141.922 -41.742 1.00 32.40 C ANISOU 5001 CA ASN C 272 4418 3436 4455 1061 2141 947 C ATOM 5002 C ASN C 272 -39.035-140.612 -41.776 1.00 47.62 C ANISOU 5002 C ASN C 272 6384 5335 6375 1035 2117 892 C ATOM 5003 O ASN C 272 -39.265-139.746 -42.639 1.00 53.16 O ANISOU 5003 O ASN C 272 7110 6060 7028 1057 2087 856 O ATOM 5004 CB ASN C 272 -40.866-141.997 -42.831 1.00 52.25 C ANISOU 5004 CB ASN C 272 6912 6008 6935 1113 2138 958 C ATOM 5005 CG ASN C 272 -41.456-143.399 -42.973 1.00 59.57 C ANISOU 5005 CG ASN C 272 7800 6964 7870 1139 2165 1013 C ATOM 5006 OD1 ASN C 272 -42.547-143.675 -42.470 1.00 58.38 O ANISOU 5006 OD1 ASN C 272 7686 6844 7652 1163 2139 1014 O ATOM 5007 ND2 ASN C 272 -40.727-144.294 -43.647 1.00 48.82 N ANISOU 5007 ND2 ASN C 272 6364 5591 6594 1132 2217 1059 N ATOM 5008 N ALA C 273 -38.151-140.462 -40.793 1.00 30.58 N ANISOU 5008 N ALA C 273 4232 3125 4263 988 2128 883 N ATOM 5009 CA ALA C 273 -37.342-139.262 -40.668 1.00 26.72 C ANISOU 5009 CA ALA C 273 3779 2602 3770 957 2110 831 C ATOM 5010 C ALA C 273 -35.896-139.514 -40.273 1.00 37.15 C ANISOU 5010 C ALA C 273 5075 3863 5178 906 2145 836 C ATOM 5011 O ALA C 273 -35.566-140.576 -39.767 1.00 44.72 O ANISOU 5011 O ALA C 273 6009 4805 6177 892 2169 873 O ATOM 5012 CB ALA C 273 -38.040-138.447 -39.598 1.00 54.19 C ANISOU 5012 CB ALA C 273 7346 6095 7149 953 2049 787 C ATOM 5013 N ASP C 274 -35.029-138.538 -40.518 1.00 52.37 N ANISOU 5013 N ASP C 274 7006 5756 7135 880 2147 796 N ATOM 5014 CA ASP C 274 -33.720-138.528 -39.889 1.00 47.75 C ANISOU 5014 CA ASP C 274 6417 5113 6613 826 2168 787 C ATOM 5015 C ASP C 274 -33.960-138.156 -38.438 1.00 52.53 C ANISOU 5015 C ASP C 274 7106 5716 7137 807 2126 754 C ATOM 5016 O ASP C 274 -34.854-137.343 -38.144 1.00 33.14 O ANISOU 5016 O ASP C 274 4712 3292 4586 825 2075 719 O ATOM 5017 CB ASP C 274 -32.799-137.496 -40.535 1.00 56.26 C ANISOU 5017 CB ASP C 274 7489 6151 7738 786 2108 737 C ATOM 5018 CG ASP C 274 -32.187-137.993 -41.823 1.00 79.85 C ANISOU 5018 CG ASP C 274 10386 9121 10831 779 2118 768 C ATOM 5019 OD1 ASP C 274 -31.640-139.116 -41.813 1.00 77.47 O ANISOU 5019 OD1 ASP C 274 10027 8801 10607 765 2170 822 O ATOM 5020 OD2 ASP C 274 -32.259-137.266 -42.841 1.00 95.30 O ANISOU 5020 OD2 ASP C 274 12330 11084 12795 789 2073 741 O ATOM 5021 N LEU C 275 -33.173-138.747 -37.535 1.00 25.90 N ANISOU 5021 N LEU C 275 3732 2305 3804 769 2142 766 N ATOM 5022 CA LEU C 275 -33.381-138.545 -36.112 1.00 25.33 C ANISOU 5022 CA LEU C 275 3730 2232 3663 753 2102 737 C ATOM 5023 C LEU C 275 -32.342-137.646 -35.477 1.00 29.68 C ANISOU 5023 C LEU C 275 4319 2740 4216 702 2094 690 C ATOM 5024 O LEU C 275 -32.534-137.166 -34.356 1.00 34.95 O ANISOU 5024 O LEU C 275 5052 3412 4814 689 2052 654 O ATOM 5025 CB LEU C 275 -33.460-139.885 -35.365 1.00 29.34 C ANISOU 5025 CB LEU C 275 4218 2736 4193 758 2114 777 C ATOM 5026 CG LEU C 275 -34.850-140.474 -35.083 1.00 47.15 C ANISOU 5026 CG LEU C 275 6489 5042 6382 803 2087 796 C ATOM 5027 CD1 LEU C 275 -35.822-140.188 -36.208 1.00 52.00 C ANISOU 5027 CD1 LEU C 275 7091 5703 6964 844 2080 806 C ATOM 5028 CD2 LEU C 275 -34.760-141.970 -34.825 1.00 70.75 C ANISOU 5028 CD2 LEU C 275 9433 8024 9424 812 2119 846 C ATOM 5029 N TYR C 276 -31.239-137.406 -36.169 1.00 33.41 N ANISOU 5029 N TYR C 276 4753 3169 4772 662 2078 678 N ATOM 5030 CA TYR C 276 -30.170-136.622 -35.553 1.00 34.23 C ANISOU 5030 CA TYR C 276 4893 3225 4886 599 2008 623 C ATOM 5031 C TYR C 276 -30.624-135.205 -35.167 1.00 24.35 C ANISOU 5031 C TYR C 276 3721 1995 3536 596 1942 559 C ATOM 5032 O TYR C 276 -31.048-134.425 -36.007 1.00 33.88 O ANISOU 5032 O TYR C 276 4934 3221 4719 611 1904 537 O ATOM 5033 CB TYR C 276 -28.920-136.591 -36.434 1.00 38.14 C ANISOU 5033 CB TYR C 276 5333 3668 5492 553 1969 617 C ATOM 5034 CG TYR C 276 -27.819-135.703 -35.897 1.00 29.10 C ANISOU 5034 CG TYR C 276 4226 2476 4355 490 1892 556 C ATOM 5035 CD1 TYR C 276 -27.420-135.771 -34.568 1.00 24.85 C ANISOU 5035 CD1 TYR C 276 3730 1920 3790 463 1891 539 C ATOM 5036 CD2 TYR C 276 -27.179-134.798 -36.721 1.00 25.23 C ANISOU 5036 CD2 TYR C 276 3728 1961 3899 458 1821 515 C ATOM 5037 CE1 TYR C 276 -26.415-134.950 -34.073 1.00 25.49 C ANISOU 5037 CE1 TYR C 276 3846 1963 3876 408 1821 481 C ATOM 5038 CE2 TYR C 276 -26.175-133.975 -36.241 1.00 43.54 C ANISOU 5038 CE2 TYR C 276 6082 4239 6222 401 1750 459 C ATOM 5039 CZ TYR C 276 -25.791-134.050 -34.921 1.00 30.04 C ANISOU 5039 CZ TYR C 276 4415 2515 4484 376 1751 442 C ATOM 5040 OH TYR C 276 -24.778-133.219 -34.467 1.00 24.51 O ANISOU 5040 OH TYR C 276 3748 1777 3787 321 1680 385 O ATOM 5041 N VAL C 277 -30.505-134.889 -33.880 1.00 27.14 N ANISOU 5041 N VAL C 277 4133 2344 3833 574 1928 531 N ATOM 5042 CA VAL C 277 -30.962-133.634 -33.320 1.00 23.28 C ANISOU 5042 CA VAL C 277 3722 1879 3244 568 1872 476 C ATOM 5043 C VAL C 277 -30.463-132.418 -34.102 1.00 24.90 C ANISOU 5043 C VAL C 277 3936 2066 3460 536 1786 425 C ATOM 5044 O VAL C 277 -31.250-131.548 -34.464 1.00 36.72 O ANISOU 5044 O VAL C 277 5467 3594 4890 558 1752 402 O ATOM 5045 CB VAL C 277 -30.530-133.476 -31.857 1.00 22.88 C ANISOU 5045 CB VAL C 277 3723 1816 3155 535 1861 450 C ATOM 5046 CG1 VAL C 277 -31.535-132.608 -31.138 1.00 32.15 C ANISOU 5046 CG1 VAL C 277 4972 3035 4208 555 1840 420 C ATOM 5047 CG2 VAL C 277 -30.436-134.810 -31.182 1.00114.56 C ANISOU 5047 CG2 VAL C 277 15307 13418 14801 546 1935 499 C ATOM 5048 N GLY C 278 -29.150-132.359 -34.323 1.00 34.19 N ANISOU 5048 N GLY C 278 5084 3190 4718 483 1750 408 N ATOM 5049 CA GLY C 278 -28.509-131.236 -34.983 1.00 23.46 C ANISOU 5049 CA GLY C 278 3733 1806 3375 444 1667 358 C ATOM 5050 C GLY C 278 -29.133-130.934 -36.336 1.00 50.20 C ANISOU 5050 C GLY C 278 7091 5213 6768 479 1655 365 C ATOM 5051 O GLY C 278 -29.203-129.771 -36.780 1.00 42.18 O ANISOU 5051 O GLY C 278 6107 4201 5719 467 1585 321 O ATOM 5052 N ASP C 279 -29.610-131.987 -36.990 1.00 26.01 N ANISOU 5052 N ASP C 279 3970 2166 3748 523 1723 422 N ATOM 5053 CA ASP C 279 -30.106-131.873 -38.361 1.00 36.23 C ANISOU 5053 CA ASP C 279 5224 3478 5063 558 1719 433 C ATOM 5054 C ASP C 279 -31.597-131.608 -38.453 1.00 24.19 C ANISOU 5054 C ASP C 279 3733 2013 3443 621 1736 438 C ATOM 5055 O ASP C 279 -32.098-131.214 -39.502 1.00 60.59 O ANISOU 5055 O ASP C 279 8329 6643 8051 651 1716 433 O ATOM 5056 CB ASP C 279 -29.793-133.164 -39.145 1.00 39.86 C ANISOU 5056 CB ASP C 279 5594 3927 5625 573 1782 494 C ATOM 5057 CG ASP C 279 -28.373-133.201 -39.682 1.00 47.82 C ANISOU 5057 CG ASP C 279 6553 4873 6741 517 1745 485 C ATOM 5058 OD1 ASP C 279 -27.512-132.452 -39.171 1.00 48.21 O ANISOU 5058 OD1 ASP C 279 6640 4887 6791 463 1682 437 O ATOM 5059 OD2 ASP C 279 -28.127-133.984 -40.623 1.00 63.93 O ANISOU 5059 OD2 ASP C 279 8518 6906 8868 527 1779 527 O ATOM 5060 N VAL C 280 -32.311-131.834 -37.363 1.00 35.93 N ANISOU 5060 N VAL C 280 5268 3531 4855 642 1773 448 N ATOM 5061 CA VAL C 280 -33.757-131.919 -37.437 1.00 27.24 C ANISOU 5061 CA VAL C 280 4189 2487 3675 709 1808 466 C ATOM 5062 C VAL C 280 -34.557-131.028 -36.477 1.00 31.54 C ANISOU 5062 C VAL C 280 4821 3061 4102 717 1776 430 C ATOM 5063 O VAL C 280 -35.747-130.866 -36.675 1.00 26.08 O ANISOU 5063 O VAL C 280 4153 2413 3342 770 1787 436 O ATOM 5064 CB VAL C 280 -34.190-133.376 -37.215 1.00 48.24 C ANISOU 5064 CB VAL C 280 6806 5167 6355 749 1907 532 C ATOM 5065 CG1 VAL C 280 -35.711-133.495 -37.179 1.00 63.18 C ANISOU 5065 CG1 VAL C 280 8724 7120 8162 809 1918 551 C ATOM 5066 CG2 VAL C 280 -33.622-134.244 -38.312 1.00 64.21 C ANISOU 5066 CG2 VAL C 280 8740 7171 8487 751 1942 573 C ATOM 5067 N LEU C 281 -33.949-130.469 -35.431 1.00 22.63 N ANISOU 5067 N LEU C 281 3741 1911 2946 666 1737 395 N ATOM 5068 CA LEU C 281 -34.782-129.820 -34.424 1.00 27.42 C ANISOU 5068 CA LEU C 281 4425 2551 3442 677 1720 372 C ATOM 5069 C LEU C 281 -35.261-128.456 -34.883 1.00 21.78 C ANISOU 5069 C LEU C 281 3758 1852 2667 677 1641 327 C ATOM 5070 O LEU C 281 -36.459-128.238 -35.043 1.00 37.13 O ANISOU 5070 O LEU C 281 5730 3837 4542 727 1646 331 O ATOM 5071 CB LEU C 281 -34.122-129.739 -33.039 1.00 29.02 C ANISOU 5071 CB LEU C 281 4666 2735 3624 629 1714 353 C ATOM 5072 CG LEU C 281 -35.049-129.066 -32.013 1.00 21.13 C ANISOU 5072 CG LEU C 281 3733 1776 2519 629 1660 336 C ATOM 5073 CD1 LEU C 281 -35.054-129.746 -30.676 1.00 25.39 C ANISOU 5073 CD1 LEU C 281 4272 2319 3054 610 1652 354 C ATOM 5074 CD2 LEU C 281 -34.708-127.597 -31.852 1.00 47.66 C ANISOU 5074 CD2 LEU C 281 7158 5127 5823 596 1604 273 C ATOM 5075 N VAL C 282 -34.333-127.535 -35.071 1.00 21.72 N ANISOU 5075 N VAL C 282 3761 1809 2682 621 1567 282 N ATOM 5076 CA VAL C 282 -34.699-126.235 -35.611 1.00 24.92 C ANISOU 5076 CA VAL C 282 4206 2223 3039 617 1486 240 C ATOM 5077 C VAL C 282 -35.683-126.431 -36.750 1.00 28.62 C ANISOU 5077 C VAL C 282 4647 2720 3506 681 1504 261 C ATOM 5078 O VAL C 282 -36.813-125.966 -36.686 1.00 64.11 O ANISOU 5078 O VAL C 282 9187 7252 7919 721 1491 255 O ATOM 5079 CB VAL C 282 -33.497-125.509 -36.168 1.00 26.63 C ANISOU 5079 CB VAL C 282 4408 2395 3315 558 1415 202 C ATOM 5080 CG1 VAL C 282 -33.931-124.174 -36.730 1.00 47.36 C ANISOU 5080 CG1 VAL C 282 7077 5030 5889 556 1331 161 C ATOM 5081 CG2 VAL C 282 -32.450-125.345 -35.083 1.00 33.98 C ANISOU 5081 CG2 VAL C 282 5362 3297 4251 496 1398 180 C ATOM 5082 N ASP C 283 -35.251-127.141 -37.786 1.00 31.26 N ANISOU 5082 N ASP C 283 4907 3037 3931 693 1533 288 N ATOM 5083 CA ASP C 283 -36.110-127.419 -38.937 1.00 27.59 C ANISOU 5083 CA ASP C 283 4408 2601 3474 756 1555 310 C ATOM 5084 C ASP C 283 -37.516-127.859 -38.541 1.00 37.86 C ANISOU 5084 C ASP C 283 5736 3955 4696 823 1609 337 C ATOM 5085 O ASP C 283 -38.488-127.461 -39.174 1.00 65.86 O ANISOU 5085 O ASP C 283 9296 7532 8197 872 1591 330 O ATOM 5086 CB ASP C 283 -35.482-128.471 -39.858 1.00 44.12 C ANISOU 5086 CB ASP C 283 6410 4675 5678 763 1606 349 C ATOM 5087 CG ASP C 283 -34.425-127.887 -40.790 1.00 71.70 C ANISOU 5087 CG ASP C 283 9871 8125 9248 718 1541 320 C ATOM 5088 OD1 ASP C 283 -34.501-126.679 -41.098 1.00 75.03 O ANISOU 5088 OD1 ASP C 283 10333 8541 9633 703 1461 273 O ATOM 5089 OD2 ASP C 283 -33.521-128.640 -41.222 1.00 88.69 O ANISOU 5089 OD2 ASP C 283 11955 10245 11497 697 1570 345 O ATOM 5090 N SER C 284 -37.634-128.668 -37.496 1.00 28.66 N ANISOU 5090 N SER C 284 4577 2799 3512 827 1672 367 N ATOM 5091 CA SER C 284 -38.933-129.237 -37.143 1.00 38.48 C ANISOU 5091 CA SER C 284 5823 4097 4702 860 1669 407 C ATOM 5092 C SER C 284 -39.846-128.268 -36.390 1.00 46.61 C ANISOU 5092 C SER C 284 6923 5155 5632 852 1589 379 C ATOM 5093 O SER C 284 -41.066-128.426 -36.394 1.00 49.94 O ANISOU 5093 O SER C 284 7348 5618 6011 884 1561 398 O ATOM 5094 CB SER C 284 -38.760-130.530 -36.339 1.00 36.02 C ANISOU 5094 CB SER C 284 5476 3784 4426 845 1708 455 C ATOM 5095 OG SER C 284 -38.276-131.576 -37.159 1.00 45.72 O ANISOU 5095 OG SER C 284 6631 5000 5742 863 1778 494 O ATOM 5096 N TYR C 285 -39.262-127.274 -35.735 1.00 21.35 N ANISOU 5096 N TYR C 285 3779 1933 2400 807 1549 334 N ATOM 5097 CA TYR C 285 -40.067-126.312 -35.001 1.00 21.62 C ANISOU 5097 CA TYR C 285 3874 1993 2347 794 1469 310 C ATOM 5098 C TYR C 285 -40.239-125.059 -35.834 1.00 30.55 C ANISOU 5098 C TYR C 285 5047 3121 3440 807 1423 264 C ATOM 5099 O TYR C 285 -40.513-123.973 -35.321 1.00 46.30 O ANISOU 5099 O TYR C 285 7101 5123 5369 782 1353 231 O ATOM 5100 CB TYR C 285 -39.423-125.992 -33.647 1.00 31.38 C ANISOU 5100 CB TYR C 285 5145 3213 3565 735 1444 291 C ATOM 5101 CG TYR C 285 -39.666-127.072 -32.640 1.00 27.17 C ANISOU 5101 CG TYR C 285 4582 2691 3051 732 1460 329 C ATOM 5102 CD1 TYR C 285 -40.800-127.063 -31.849 1.00 48.09 C ANISOU 5102 CD1 TYR C 285 7243 5373 5655 741 1408 337 C ATOM 5103 CD2 TYR C 285 -38.786-128.116 -32.498 1.00 27.99 C ANISOU 5103 CD2 TYR C 285 4644 2767 3222 721 1525 353 C ATOM 5104 CE1 TYR C 285 -41.040-128.073 -30.926 1.00 47.93 C ANISOU 5104 CE1 TYR C 285 7195 5358 5657 742 1419 365 C ATOM 5105 CE2 TYR C 285 -39.024-129.139 -31.588 1.00 38.50 C ANISOU 5105 CE2 TYR C 285 5951 4105 4572 722 1535 384 C ATOM 5106 CZ TYR C 285 -40.148-129.111 -30.802 1.00 33.58 C ANISOU 5106 CZ TYR C 285 5343 3515 3903 733 1481 387 C ATOM 5107 OH TYR C 285 -40.370-130.125 -29.892 1.00 32.40 O ANISOU 5107 OH TYR C 285 5170 3369 3774 736 1490 412 O ATOM 5108 N SER C 286 -40.085-125.236 -37.137 1.00 20.91 N ANISOU 5108 N SER C 286 2210 2390 3346 915 1088 201 N ATOM 5109 CA SER C 286 -40.121-124.133 -38.074 1.00 26.95 C ANISOU 5109 CA SER C 286 3088 2996 4156 956 1215 249 C ATOM 5110 C SER C 286 -41.027-124.458 -39.255 1.00 23.63 C ANISOU 5110 C SER C 286 2795 2484 3700 1023 1363 200 C ATOM 5111 O SER C 286 -41.300-125.621 -39.526 1.00 56.98 O ANISOU 5111 O SER C 286 7006 6776 7866 1046 1353 173 O ATOM 5112 CB SER C 286 -38.706-123.817 -38.543 1.00 21.47 C ANISOU 5112 CB SER C 286 2365 2307 3485 960 1175 435 C ATOM 5113 OG SER C 286 -37.943-123.357 -37.443 1.00 43.47 O ANISOU 5113 OG SER C 286 5070 5149 6298 891 1065 469 O ATOM 5114 N ASP C 287 -41.490-123.423 -39.952 1.00 38.99 N ANISOU 5114 N ASP C 287 4872 4260 5683 1052 1524 206 N ATOM 5115 CA ASP C 287 -42.419-123.589 -41.076 1.00 33.60 C ANISOU 5115 CA ASP C 287 4349 3449 4969 1112 1707 172 C ATOM 5116 C ASP C 287 -42.466-122.322 -41.903 1.00 53.11 C ANISOU 5116 C ASP C 287 6923 5771 7484 1138 1827 226 C ATOM 5117 O ASP C 287 -43.128-121.353 -41.543 1.00 75.75 O ANISOU 5117 O ASP C 287 9904 8480 10398 1104 1971 171 O ATOM 5118 CB ASP C 287 -43.826-123.927 -40.575 1.00 36.08 C ANISOU 5118 CB ASP C 287 4808 3654 5246 1079 1890 13 C ATOM 5119 CG ASP C 287 -44.888-123.790 -41.649 1.00 45.68 C ANISOU 5119 CG ASP C 287 6250 4689 6416 1108 2103 -50 C ATOM 5120 OD1 ASP C 287 -46.077-123.771 -41.279 1.00 62.07 O ANISOU 5120 OD1 ASP C 287 8513 6634 8436 1029 2271 -216 O ATOM 5121 OD2 ASP C 287 -44.558-123.711 -42.855 1.00 42.11 O ANISOU 5121 OD2 ASP C 287 5807 4226 5969 1187 2106 51 O ATOM 5122 N ASP C 288 -41.780-122.367 -43.036 1.00 55.48 N ANISOU 5122 N ASP C 288 7217 6077 7786 1205 1857 380 N ATOM 5123 CA ASP C 288 -41.670-121.241 -43.945 1.00 52.30 C ANISOU 5123 CA ASP C 288 6896 5549 7425 1248 2006 485 C ATOM 5124 C ASP C 288 -43.030-120.805 -44.525 1.00 58.08 C ANISOU 5124 C ASP C 288 7822 6099 8145 1268 2195 374 C ATOM 5125 O ASP C 288 -43.145-119.712 -45.089 1.00 51.01 O ANISOU 5125 O ASP C 288 7011 5078 7291 1292 2335 432 O ATOM 5126 CB ASP C 288 -40.675-121.583 -45.063 1.00 44.19 C ANISOU 5126 CB ASP C 288 5825 4584 6382 1319 2020 681 C ATOM 5127 CG ASP C 288 -41.139-122.752 -45.927 1.00 75.18 C ANISOU 5127 CG ASP C 288 9802 8518 10244 1383 2065 675 C ATOM 5128 OD1 ASP C 288 -42.319-123.153 -45.822 1.00 74.15 O ANISOU 5128 OD1 ASP C 288 9767 8324 10083 1379 2117 518 O ATOM 5129 OD2 ASP C 288 -40.322-123.264 -46.722 1.00 97.31 O ANISOU 5129 OD2 ASP C 288 12558 11395 13021 1432 2053 823 O ATOM 5130 N GLY C 289 -44.046-121.662 -44.398 1.00 49.41 N ANISOU 5130 N GLY C 289 6812 4976 6986 1256 2232 228 N ATOM 5131 CA GLY C 289 -45.420-121.278 -44.693 1.00 36.73 C ANISOU 5131 CA GLY C 289 5449 3147 5359 1241 2476 116 C ATOM 5132 C GLY C 289 -45.897-121.576 -46.102 1.00 72.98 C ANISOU 5132 C GLY C 289 10158 7665 9907 1325 2607 152 C ATOM 5133 O GLY C 289 -47.046-121.291 -46.448 1.00 40.20 O ANISOU 5133 O GLY C 289 6228 3322 5723 1307 2813 55 O ATOM 5134 N VAL C 290 -45.018-122.131 -46.929 1.00 89.90 N ANISOU 5134 N VAL C 290 12174 9940 12045 1406 2513 294 N ATOM 5135 CA VAL C 290 -45.417-122.574 -48.259 1.00 83.41 C ANISOU 5135 CA VAL C 290 11460 9049 11184 1499 2658 355 C ATOM 5136 C VAL C 290 -46.562-123.456 -48.710 1.00 88.95 C ANISOU 5136 C VAL C 290 12146 9846 11804 1497 2585 253 C ATOM 5137 O VAL C 290 -47.399-123.033 -49.513 1.00 75.74 O ANISOU 5137 O VAL C 290 10318 8338 10120 1466 2407 247 O ATOM 5138 CB VAL C 290 -44.282-122.445 -49.293 1.00 72.04 C ANISOU 5138 CB VAL C 290 9940 7656 9774 1595 2685 605 C ATOM 5139 CG1 VAL C 290 -43.209-123.508 -49.057 1.00 70.57 C ANISOU 5139 CG1 VAL C 290 9576 7670 9567 1597 2497 692 C ATOM 5140 CG2 VAL C 290 -44.851-122.546 -50.706 1.00 67.62 C ANISOU 5140 CG2 VAL C 290 9525 6982 9186 1696 2883 672 C ATOM 5141 N VAL C 291 -46.587-124.684 -48.213 1.00104.68 N ANISOU 5141 N VAL C 291 14311 11725 13735 1531 2745 181 N ATOM 5142 CA VAL C 291 -47.528-125.675 -48.707 1.00118.78 C ANISOU 5142 CA VAL C 291 16133 13569 15431 1524 2739 75 C ATOM 5143 C VAL C 291 -48.351-125.651 -47.425 1.00124.08 C ANISOU 5143 C VAL C 291 16906 14187 16051 1401 2777 -118 C ATOM 5144 O VAL C 291 -49.332-126.382 -47.288 1.00136.14 O ANISOU 5144 O VAL C 291 18571 15687 17470 1356 2860 -263 O ATOM 5145 CB VAL C 291 -46.477-126.809 -48.652 1.00117.08 C ANISOU 5145 CB VAL C 291 15683 13590 15211 1556 2517 165 C ATOM 5146 CG1 VAL C 291 -47.156-128.171 -48.558 1.00123.41 C ANISOU 5146 CG1 VAL C 291 16519 14457 15914 1559 2527 65 C ATOM 5147 CG2 VAL C 291 -45.559-126.743 -49.865 1.00110.38 C ANISOU 5147 CG2 VAL C 291 14798 12738 14403 1665 2564 407 C ATOM 5148 N SER C 292 -47.955-124.791 -46.490 1.00112.11 N ANISOU 5148 N SER C 292 15333 12663 14602 1332 2720 -123 N ATOM 5149 CA SER C 292 -48.707-124.594 -45.257 1.00106.36 C ANISOU 5149 CA SER C 292 14714 11869 13828 1189 2769 -306 C ATOM 5150 C SER C 292 -49.687-123.443 -45.412 1.00 78.98 C ANISOU 5150 C SER C 292 11503 8147 10359 1108 2978 -405 C ATOM 5151 O SER C 292 -50.816-123.509 -44.932 1.00 84.35 O ANISOU 5151 O SER C 292 12394 8719 10936 965 3091 -604 O ATOM 5152 CB SER C 292 -47.772-124.324 -44.078 1.00121.06 C ANISOU 5152 CB SER C 292 16375 13859 15765 1148 2596 -264 C ATOM 5153 OG SER C 292 -48.512-124.033 -42.905 1.00130.28 O ANISOU 5153 OG SER C 292 17661 14952 16889 991 2662 -443 O ATOM 5154 N GLY C 293 -49.243-122.384 -46.079 1.00 82.58 N ANISOU 5154 N GLY C 293 11943 8519 10913 1178 3025 -270 N ATOM 5155 CA GLY C 293 -50.104-121.255 -46.401 1.00 91.72 C ANISOU 5155 CA GLY C 293 13333 9435 12081 1123 3235 -332 C ATOM 5156 C GLY C 293 -50.310-120.270 -45.268 1.00 66.36 C ANISOU 5156 C GLY C 293 10178 6128 8908 976 3255 -430 C ATOM 5157 O GLY C 293 -51.055-119.306 -45.397 1.00 61.55 O ANISOU 5157 O GLY C 293 9766 5316 8305 902 3423 -498 O ATOM 5158 N LEU C 294 -49.658-120.526 -44.144 1.00 71.17 N ANISOU 5158 N LEU C 294 10614 6884 9542 930 3085 -437 N ATOM 5159 CA LEU C 294 -49.754-119.648 -42.994 1.00 81.23 C ANISOU 5159 CA LEU C 294 11916 8086 10860 787 3086 -523 C ATOM 5160 C LEU C 294 -48.514-118.759 -42.876 1.00 94.60 C ANISOU 5160 C LEU C 294 13392 9855 12694 876 2977 -333 C ATOM 5161 O LEU C 294 -47.580-118.860 -43.675 1.00104.94 O ANISOU 5161 O LEU C 294 14541 11287 14047 1020 2888 -151 O ATOM 5162 CB LEU C 294 -49.949-120.465 -41.718 1.00 68.84 C ANISOU 5162 CB LEU C 294 10320 6622 9215 648 2991 -677 C ATOM 5163 CG LEU C 294 -51.162-121.391 -41.726 1.00 70.31 C ANISOU 5163 CG LEU C 294 10718 6778 9220 519 3075 -883 C ATOM 5164 CD1 LEU C 294 -51.516-121.790 -40.306 1.00 75.43 C ANISOU 5164 CD1 LEU C 294 11388 7505 9767 295 3008 -1074 C ATOM 5165 CD2 LEU C 294 -52.336-120.713 -42.395 1.00 81.40 C ANISOU 5165 CD2 LEU C 294 12419 7940 10569 432 3278 -988 C ATOM 5166 N SER C 295 -48.519-117.880 -41.879 1.00 68.48 N ANISOU 5166 N SER C 295 10093 6482 9445 764 2979 -388 N ATOM 5167 CA SER C 295 -47.388-117.009 -41.612 1.00 59.03 C ANISOU 5167 CA SER C 295 8695 5364 8368 825 2871 -227 C ATOM 5168 C SER C 295 -46.167-117.828 -41.226 1.00 55.50 C ANISOU 5168 C SER C 295 7972 5175 7939 901 2632 -112 C ATOM 5169 O SER C 295 -46.244-118.678 -40.340 1.00 41.27 O ANISOU 5169 O SER C 295 6117 3460 6103 841 2552 -201 O ATOM 5170 CB SER C 295 -47.745-116.047 -40.484 1.00 80.57 C ANISOU 5170 CB SER C 295 11494 7971 11149 672 2918 -332 C ATOM 5171 OG SER C 295 -48.544-116.700 -39.511 1.00 82.33 O ANISOU 5171 OG SER C 295 11829 8160 11292 497 2926 -543 O ATOM 5172 N PRO C 296 -45.031-117.579 -41.897 1.00 58.72 N ANISOU 5172 N PRO C 296 8211 5714 8385 1012 2516 75 N ATOM 5173 CA PRO C 296 -43.839-118.368 -41.587 1.00 36.47 C ANISOU 5173 CA PRO C 296 5156 3142 5559 1049 2271 169 C ATOM 5174 C PRO C 296 -43.669-118.509 -40.089 1.00 48.16 C ANISOU 5174 C PRO C 296 6538 4688 7073 966 2170 107 C ATOM 5175 O PRO C 296 -43.797-117.513 -39.376 1.00 42.33 O ANISOU 5175 O PRO C 296 5824 3854 6406 901 2223 80 O ATOM 5176 CB PRO C 296 -42.703-117.530 -42.174 1.00 32.95 C ANISOU 5176 CB PRO C 296 4596 2775 5148 1098 2186 331 C ATOM 5177 CG PRO C 296 -43.344-116.870 -43.363 1.00 49.82 C ANISOU 5177 CG PRO C 296 6896 4747 7287 1151 2394 355 C ATOM 5178 CD PRO C 296 -44.763-116.549 -42.917 1.00 57.94 C ANISOU 5178 CD PRO C 296 8142 5551 8323 1079 2601 195 C ATOM 5179 N LEU C 297 -43.410-119.743 -39.641 1.00 61.43 N ANISOU 5179 N LEU C 297 8105 6529 8706 969 2035 87 N ATOM 5180 CA LEU C 297 -43.195-120.095 -38.238 1.00 37.46 C ANISOU 5180 CA LEU C 297 4944 3593 5697 901 1931 43 C ATOM 5181 C LEU C 297 -41.723-120.333 -37.981 1.00 35.29 C ANISOU 5181 C LEU C 297 4444 3546 5420 926 1666 181 C ATOM 5182 O LEU C 297 -41.060-121.020 -38.770 1.00 35.54 O ANISOU 5182 O LEU C 297 4422 3697 5385 973 1549 246 O ATOM 5183 CB LEU C 297 -43.956-121.374 -37.894 1.00 60.56 C ANISOU 5183 CB LEU C 297 7902 6565 8543 871 1973 -84 C ATOM 5184 CG LEU C 297 -43.655-121.929 -36.497 1.00 74.18 C ANISOU 5184 CG LEU C 297 9446 8453 10287 808 1861 -109 C ATOM 5185 CD1 LEU C 297 -44.413-121.124 -35.451 1.00 87.02 C ANISOU 5185 CD1 LEU C 297 11157 9936 11968 662 2019 -261 C ATOM 5186 CD2 LEU C 297 -43.986-123.419 -36.381 1.00 52.57 C ANISOU 5186 CD2 LEU C 297 6659 5870 7445 808 1838 -167 C ATOM 5187 N TYR C 298 -41.210-119.790 -36.879 1.00 24.83 N ANISOU 5187 N TYR C 298 3011 2271 4154 870 1574 206 N ATOM 5188 CA TYR C 298 -39.782-119.936 -36.565 1.00 33.86 C ANISOU 5188 CA TYR C 298 3997 3614 5254 854 1320 301 C ATOM 5189 C TYR C 298 -39.530-120.560 -35.206 1.00 22.19 C ANISOU 5189 C TYR C 298 2385 2274 3773 796 1181 282 C ATOM 5190 O TYR C 298 -40.276-120.362 -34.258 1.00 45.05 O ANISOU 5190 O TYR C 298 5253 5112 6752 753 1278 228 O ATOM 5191 CB TYR C 298 -39.041-118.597 -36.625 1.00 36.72 C ANISOU 5191 CB TYR C 298 4355 3929 5666 838 1320 394 C ATOM 5192 CG TYR C 298 -38.950-117.966 -37.993 1.00 58.63 C ANISOU 5192 CG TYR C 298 7224 6597 8456 898 1468 483 C ATOM 5193 CD1 TYR C 298 -37.868-118.215 -38.822 1.00 68.79 C ANISOU 5193 CD1 TYR C 298 8478 7943 9717 929 1459 635 C ATOM 5194 CD2 TYR C 298 -39.935-117.100 -38.447 1.00 85.03 C ANISOU 5194 CD2 TYR C 298 10696 9780 11832 916 1628 417 C ATOM 5195 CE1 TYR C 298 -37.776-117.633 -40.077 1.00 73.07 C ANISOU 5195 CE1 TYR C 298 9091 8406 10267 990 1603 730 C ATOM 5196 CE2 TYR C 298 -39.849-116.513 -39.700 1.00 98.94 C ANISOU 5196 CE2 TYR C 298 12536 11451 13605 976 1776 515 C ATOM 5197 CZ TYR C 298 -38.766-116.784 -40.509 1.00 89.75 C ANISOU 5197 CZ TYR C 298 11316 10366 12417 1018 1761 676 C ATOM 5198 OH TYR C 298 -38.673-116.208 -41.753 1.00 99.60 O ANISOU 5198 OH TYR C 298 12632 11539 13671 1085 1914 784 O ATOM 5199 N SER C 299 -38.448-121.310 -35.125 1.00 38.03 N ANISOU 5199 N SER C 299 4314 4422 5715 780 1015 353 N ATOM 5200 CA SER C 299 -38.094-122.032 -33.923 1.00 22.98 C ANISOU 5200 CA SER C 299 2296 2657 3776 722 867 345 C ATOM 5201 C SER C 299 -37.592-121.069 -32.856 1.00 23.87 C ANISOU 5201 C SER C 299 2361 2774 3936 659 804 382 C ATOM 5202 O SER C 299 -36.916-120.093 -33.179 1.00 34.36 O ANISOU 5202 O SER C 299 3726 4024 5306 660 840 469 O ATOM 5203 CB SER C 299 -37.006-123.054 -34.284 1.00 23.02 C ANISOU 5203 CB SER C 299 2288 2731 3727 723 790 451 C ATOM 5204 OG SER C 299 -36.551-123.783 -33.158 1.00 44.81 O ANISOU 5204 OG SER C 299 4973 5605 6448 663 659 459 O ATOM 5205 N PRO C 300 -37.929-121.333 -31.579 1.00 21.00 N ANISOU 5205 N PRO C 300 1903 2519 3556 599 717 324 N ATOM 5206 CA PRO C 300 -37.394-120.543 -30.473 1.00 17.80 C ANISOU 5206 CA PRO C 300 1449 2129 3184 535 643 372 C ATOM 5207 C PRO C 300 -35.902-120.790 -30.264 1.00 20.78 C ANISOU 5207 C PRO C 300 1845 2520 3528 512 556 500 C ATOM 5208 O PRO C 300 -35.233-119.969 -29.633 1.00 35.89 O ANISOU 5208 O PRO C 300 3759 4411 5468 473 526 560 O ATOM 5209 CB PRO C 300 -38.208-121.024 -29.265 1.00 28.64 C ANISOU 5209 CB PRO C 300 2690 3625 4567 460 607 324 C ATOM 5210 CG PRO C 300 -38.736-122.349 -29.654 1.00 29.52 C ANISOU 5210 CG PRO C 300 2772 3816 4630 479 626 285 C ATOM 5211 CD PRO C 300 -38.958-122.281 -31.126 1.00 28.89 C ANISOU 5211 CD PRO C 300 2811 3595 4570 581 767 271 C ATOM 5212 N PHE C 301 -35.383-121.895 -30.776 1.00 25.03 N ANISOU 5212 N PHE C 301 2406 3099 4005 530 533 536 N ATOM 5213 CA PHE C 301 -33.939-122.112 -30.736 1.00 27.89 C ANISOU 5213 CA PHE C 301 2800 3471 4326 502 496 645 C ATOM 5214 C PHE C 301 -33.390-122.137 -32.138 1.00 29.36 C ANISOU 5214 C PHE C 301 3039 3613 4502 546 574 708 C ATOM 5215 O PHE C 301 -33.887-122.876 -32.983 1.00 28.20 O ANISOU 5215 O PHE C 301 2907 3473 4335 593 610 682 O ATOM 5216 CB PHE C 301 -33.575-123.401 -29.992 1.00 31.43 C ANISOU 5216 CB PHE C 301 3228 4014 4701 469 411 654 C ATOM 5217 CG PHE C 301 -33.835-123.334 -28.520 1.00 28.41 C ANISOU 5217 CG PHE C 301 2795 3685 4313 417 335 630 C ATOM 5218 CD1 PHE C 301 -32.924-122.747 -27.673 1.00 32.91 C ANISOU 5218 CD1 PHE C 301 3382 4240 4883 374 307 696 C ATOM 5219 CD2 PHE C 301 -35.007-123.820 -27.992 1.00 37.64 C ANISOU 5219 CD2 PHE C 301 3894 4934 5473 407 299 543 C ATOM 5220 CE1 PHE C 301 -33.176-122.653 -26.325 1.00 32.03 C ANISOU 5220 CE1 PHE C 301 3229 4178 4763 330 245 689 C ATOM 5221 CE2 PHE C 301 -35.255-123.732 -26.644 1.00 39.70 C ANISOU 5221 CE2 PHE C 301 4099 5263 5721 348 231 534 C ATOM 5222 CZ PHE C 301 -34.338-123.152 -25.810 1.00 28.14 C ANISOU 5222 CZ PHE C 301 2665 3770 4257 316 204 614 C ATOM 5223 N SER C 302 -32.369-121.318 -32.379 1.00 23.79 N ANISOU 5223 N SER C 302 2358 2873 3806 530 603 793 N ATOM 5224 CA SER C 302 -31.798-121.160 -33.716 1.00 25.55 C ANISOU 5224 CA SER C 302 2619 3070 4019 569 685 867 C ATOM 5225 C SER C 302 -30.789-122.264 -34.118 1.00 19.85 C ANISOU 5225 C SER C 302 1909 2411 3221 562 660 925 C ATOM 5226 O SER C 302 -30.525-122.466 -35.297 1.00 25.42 O ANISOU 5226 O SER C 302 2638 3113 3907 603 722 977 O ATOM 5227 CB SER C 302 -31.171-119.771 -33.868 1.00 34.05 C ANISOU 5227 CB SER C 302 3706 4097 5136 559 736 935 C ATOM 5228 OG SER C 302 -29.987-119.631 -33.092 1.00 51.49 O ANISOU 5228 OG SER C 302 5905 6344 7316 502 680 984 O ATOM 5229 N GLN C 303 -30.223-122.967 -33.148 1.00 32.83 N ANISOU 5229 N GLN C 303 3539 4110 4824 511 581 921 N ATOM 5230 CA GLN C 303 -29.368-124.109 -33.474 1.00 34.36 C ANISOU 5230 CA GLN C 303 3747 4357 4951 503 566 964 C ATOM 5231 C GLN C 303 -29.116-125.029 -32.297 1.00 25.62 C ANISOU 5231 C GLN C 303 2628 3301 3805 457 490 943 C ATOM 5232 O GLN C 303 -29.058-124.602 -31.152 1.00 39.15 O ANISOU 5232 O GLN C 303 4329 5014 5533 418 448 928 O ATOM 5233 CB GLN C 303 -28.026-123.674 -34.066 1.00 27.36 C ANISOU 5233 CB GLN C 303 2879 3470 4046 495 604 1052 C ATOM 5234 CG GLN C 303 -27.135-122.965 -33.109 1.00 25.25 C ANISOU 5234 CG GLN C 303 2610 3201 3785 443 575 1074 C ATOM 5235 CD GLN C 303 -25.766-122.748 -33.685 1.00 47.32 C ANISOU 5235 CD GLN C 303 5419 6020 6540 440 569 1080 C ATOM 5236 OE1 GLN C 303 -25.303-121.606 -33.814 1.00 51.23 O ANISOU 5236 OE1 GLN C 303 5915 6498 7053 441 584 1088 O ATOM 5237 NE2 GLN C 303 -25.091-123.848 -34.038 1.00 39.46 N ANISOU 5237 NE2 GLN C 303 4433 5067 5493 438 548 1074 N ATOM 5238 N PHE C 304 -28.972-126.308 -32.599 1.00 25.48 N ANISOU 5238 N PHE C 304 2616 3329 3738 465 479 950 N ATOM 5239 CA PHE C 304 -28.703-127.279 -31.577 1.00 14.82 C ANISOU 5239 CA PHE C 304 1258 2026 2347 428 425 945 C ATOM 5240 C PHE C 304 -27.324-127.871 -31.879 1.00 33.54 C ANISOU 5240 C PHE C 304 3653 4412 4677 408 440 1011 C ATOM 5241 O PHE C 304 -27.157-128.605 -32.840 1.00 33.08 O ANISOU 5241 O PHE C 304 3604 4372 4592 435 467 1036 O ATOM 5242 CB PHE C 304 -29.780-128.357 -31.591 1.00 18.79 C ANISOU 5242 CB PHE C 304 1740 2572 2828 454 401 895 C ATOM 5243 CG PHE C 304 -29.809-129.181 -30.325 1.00 22.72 C ANISOU 5243 CG PHE C 304 2220 3122 3292 417 346 888 C ATOM 5244 CD1 PHE C 304 -28.989-130.293 -30.180 1.00 12.77 C ANISOU 5244 CD1 PHE C 304 974 1894 1982 399 343 937 C ATOM 5245 CD2 PHE C 304 -30.622-128.817 -29.276 1.00 25.28 C ANISOU 5245 CD2 PHE C 304 2509 3462 3633 401 303 842 C ATOM 5246 CE1 PHE C 304 -28.992-131.020 -29.019 1.00 21.17 C ANISOU 5246 CE1 PHE C 304 2024 3003 3016 370 307 947 C ATOM 5247 CE2 PHE C 304 -30.637-129.545 -28.117 1.00 14.46 C ANISOU 5247 CE2 PHE C 304 1120 2147 2226 369 260 855 C ATOM 5248 CZ PHE C 304 -29.822-130.654 -27.991 1.00 37.58 C ANISOU 5248 CZ PHE C 304 4068 5103 5106 356 266 911 C ATOM 5249 N TYR C 305 -26.336-127.515 -31.063 1.00 34.38 N ANISOU 5249 N TYR C 305 3768 4513 4781 366 419 1023 N ATOM 5250 CA TYR C 305 -24.956-127.951 -31.242 1.00 16.21 C ANISOU 5250 CA TYR C 305 1487 2223 2447 349 401 1002 C ATOM 5251 C TYR C 305 -24.716-129.088 -30.321 1.00 16.49 C ANISOU 5251 C TYR C 305 1523 2287 2454 324 365 988 C ATOM 5252 O TYR C 305 -25.003-128.968 -29.137 1.00 34.56 O ANISOU 5252 O TYR C 305 3803 4578 4749 302 340 983 O ATOM 5253 CB TYR C 305 -23.985-126.861 -30.820 1.00 30.65 C ANISOU 5253 CB TYR C 305 3328 4030 4290 325 388 983 C ATOM 5254 CG TYR C 305 -22.555-127.242 -31.066 1.00 39.54 C ANISOU 5254 CG TYR C 305 4470 5167 5388 313 376 968 C ATOM 5255 CD1 TYR C 305 -21.842-127.977 -30.133 1.00 39.69 C ANISOU 5255 CD1 TYR C 305 4497 5196 5388 285 343 945 C ATOM 5256 CD2 TYR C 305 -21.925-126.892 -32.249 1.00 55.46 C ANISOU 5256 CD2 TYR C 305 6490 7184 7398 334 401 983 C ATOM 5257 CE1 TYR C 305 -20.533-128.343 -30.364 1.00 35.08 C ANISOU 5257 CE1 TYR C 305 3925 4617 4788 276 336 935 C ATOM 5258 CE2 TYR C 305 -20.620-127.251 -32.493 1.00 66.68 C ANISOU 5258 CE2 TYR C 305 7920 8618 8797 324 389 975 C ATOM 5259 CZ TYR C 305 -19.925-127.976 -31.551 1.00 61.05 C ANISOU 5259 CZ TYR C 305 7215 7909 8072 295 357 949 C ATOM 5260 OH TYR C 305 -18.618-128.329 -31.807 1.00 80.03 O ANISOU 5260 OH TYR C 305 9624 10322 10462 288 350 945 O ATOM 5261 N VAL C 306 -24.197-130.191 -30.851 1.00 31.97 N ANISOU 5261 N VAL C 306 3492 4269 4387 329 365 987 N ATOM 5262 CA VAL C 306 -23.922-131.385 -30.045 1.00 20.95 C ANISOU 5262 CA VAL C 306 2096 2897 2967 310 339 978 C ATOM 5263 C VAL C 306 -22.421-131.569 -29.915 1.00 20.06 C ANISOU 5263 C VAL C 306 2001 2770 2850 288 325 956 C ATOM 5264 O VAL C 306 -21.713-131.560 -30.922 1.00 27.14 O ANISOU 5264 O VAL C 306 2906 3662 3743 298 339 958 O ATOM 5265 CB VAL C 306 -24.526-132.656 -30.683 1.00 19.30 C ANISOU 5265 CB VAL C 306 1879 2723 2733 334 351 999 C ATOM 5266 CG1 VAL C 306 -24.034-133.877 -29.966 1.00 26.50 C ANISOU 5266 CG1 VAL C 306 2790 3653 3625 314 329 993 C ATOM 5267 CG2 VAL C 306 -26.027-132.616 -30.615 1.00 36.33 C ANISOU 5267 CG2 VAL C 306 4013 4905 4887 358 362 1024 C ATOM 5268 N TYR C 307 -21.939-131.703 -28.676 1.00 37.28 N ANISOU 5268 N TYR C 307 4186 4947 5032 261 301 942 N ATOM 5269 CA TYR C 307 -20.536-132.056 -28.411 1.00 25.14 C ANISOU 5269 CA TYR C 307 2662 3397 3492 244 291 925 C ATOM 5270 C TYR C 307 -20.321-133.567 -28.569 1.00 30.46 C ANISOU 5270 C TYR C 307 3333 4088 4153 247 291 934 C ATOM 5271 O TYR C 307 -20.362-134.323 -27.591 1.00 49.16 O ANISOU 5271 O TYR C 307 5696 6465 6519 236 279 939 O ATOM 5272 CB TYR C 307 -20.143-131.605 -27.006 1.00 22.41 C ANISOU 5272 CB TYR C 307 2320 3040 3156 222 273 913 C ATOM 5273 CG TYR C 307 -20.048-130.116 -26.880 1.00 28.19 C ANISOU 5273 CG TYR C 307 3056 3754 3902 218 273 904 C ATOM 5274 CD1 TYR C 307 -18.847-129.472 -27.088 1.00 36.00 C ANISOU 5274 CD1 TYR C 307 4057 4727 4893 214 274 891 C ATOM 5275 CD2 TYR C 307 -21.158-129.352 -26.593 1.00 27.85 C ANISOU 5275 CD2 TYR C 307 3001 3710 3870 221 274 914 C ATOM 5276 CE1 TYR C 307 -18.748-128.119 -27.003 1.00 28.94 C ANISOU 5276 CE1 TYR C 307 3166 3821 4011 212 277 887 C ATOM 5277 CE2 TYR C 307 -21.068-127.986 -26.491 1.00 31.58 C ANISOU 5277 CE2 TYR C 307 3476 4163 4360 218 276 908 C ATOM 5278 CZ TYR C 307 -19.860-127.372 -26.699 1.00 30.04 C ANISOU 5278 CZ TYR C 307 3295 3955 4164 214 278 894 C ATOM 5279 OH TYR C 307 -19.750-126.001 -26.603 1.00 26.41 O ANISOU 5279 OH TYR C 307 2835 3480 3719 213 282 893 O ATOM 5280 N HIS C 308 -20.106-134.004 -29.802 1.00 25.55 N ANISOU 5280 N HIS C 308 3349 2868 3489 -253 174 -261 N ATOM 5281 CA HIS C 308 -19.994-135.438 -30.098 1.00 36.07 C ANISOU 5281 CA HIS C 308 4713 4152 4839 -240 257 -210 C ATOM 5282 C HIS C 308 -18.879-136.111 -29.349 1.00 21.63 C ANISOU 5282 C HIS C 308 2879 2220 3121 -242 382 -192 C ATOM 5283 O HIS C 308 -19.085-137.156 -28.754 1.00 43.88 O ANISOU 5283 O HIS C 308 5708 4990 5975 -196 426 -100 O ATOM 5284 CB HIS C 308 -19.790-135.683 -31.584 1.00 34.61 C ANISOU 5284 CB HIS C 308 4555 3998 4599 -289 276 -282 C ATOM 5285 CG HIS C 308 -21.023-135.468 -32.392 1.00 31.45 C ANISOU 5285 CG HIS C 308 4170 3692 4086 -276 167 -274 C ATOM 5286 ND1 HIS C 308 -21.166-134.399 -33.260 1.00 33.22 N ANISOU 5286 ND1 HIS C 308 4390 3992 4242 -319 93 -364 N ATOM 5287 CD2 HIS C 308 -22.175-136.166 -32.466 1.00 36.55 C ANISOU 5287 CD2 HIS C 308 4840 4371 4677 -224 117 -187 C ATOM 5288 CE1 HIS C 308 -22.350-134.459 -33.831 1.00 51.77 C ANISOU 5288 CE1 HIS C 308 6756 6415 6499 -295 4 -333 C ATOM 5289 NE2 HIS C 308 -22.987-135.525 -33.367 1.00 62.29 N ANISOU 5289 NE2 HIS C 308 8107 7724 7837 -236 16 -225 N ATOM 5290 N GLU C 309 -17.694-135.512 -29.388 1.00 30.27 N ANISOU 5290 N GLU C 309 3956 3279 4267 -294 438 -282 N ATOM 5291 CA GLU C 309 -16.536-136.111 -28.744 1.00 29.50 C ANISOU 5291 CA GLU C 309 3853 3081 4275 -302 560 -276 C ATOM 5292 C GLU C 309 -16.799-136.257 -27.252 1.00 38.86 C ANISOU 5292 C GLU C 309 5020 4225 5521 -243 559 -180 C ATOM 5293 O GLU C 309 -16.620-137.338 -26.701 1.00 27.86 O ANISOU 5293 O GLU C 309 3636 2765 4184 -212 635 -106 O ATOM 5294 CB GLU C 309 -15.257-135.307 -29.010 1.00 25.21 C ANISOU 5294 CB GLU C 309 3293 2513 3773 -367 609 -393 C ATOM 5295 CG GLU C 309 -13.990-135.946 -28.449 1.00 80.83 C ANISOU 5295 CG GLU C 309 10333 9452 10927 -380 740 -395 C ATOM 5296 CD GLU C 309 -12.730-135.152 -28.767 1.00107.68 C ANISOU 5296 CD GLU C 309 13720 12830 14364 -444 786 -515 C ATOM 5297 OE1 GLU C 309 -12.769-133.905 -28.682 1.00116.19 O ANISOU 5297 OE1 GLU C 309 14774 13965 15409 -453 713 -564 O ATOM 5298 OE2 GLU C 309 -11.701-135.775 -29.110 1.00110.37 O ANISOU 5298 OE2 GLU C 309 14060 13142 14734 -460 873 -538 O ATOM 5299 N ASN C 310 -17.246-135.176 -26.604 1.00 35.88 N ANISOU 5299 N ASN C 310 4615 3887 5130 -226 473 -178 N ATOM 5300 CA ASN C 310 -17.558-135.251 -25.180 1.00 20.53 C ANISOU 5300 CA ASN C 310 2652 1908 3241 -169 465 -86 C ATOM 5301 C ASN C 310 -18.570-136.327 -24.857 1.00 21.71 C ANISOU 5301 C ASN C 310 2820 2057 3371 -105 447 32 C ATOM 5302 O ASN C 310 -18.432-137.009 -23.863 1.00 28.78 O ANISOU 5302 O ASN C 310 3712 2888 4335 -66 501 110 O ATOM 5303 CB ASN C 310 -18.066-133.925 -24.637 1.00 23.66 C ANISOU 5303 CB ASN C 310 3018 2359 3615 -158 361 -99 C ATOM 5304 CG ASN C 310 -17.030-132.846 -24.708 1.00 34.83 C ANISOU 5304 CG ASN C 310 4410 3763 5061 -212 384 -205 C ATOM 5305 OD1 ASN C 310 -15.875-133.122 -24.997 1.00 39.79 O ANISOU 5305 OD1 ASN C 310 5044 4335 5739 -254 482 -262 O ATOM 5306 ND2 ASN C 310 -17.427-131.607 -24.451 1.00 59.57 N ANISOU 5306 ND2 ASN C 310 7517 6950 8165 -211 293 -232 N ATOM 5307 N ILE C 311 -19.607-136.455 -25.680 1.00 31.86 N ANISOU 5307 N ILE C 311 4127 3416 4562 -93 369 46 N ATOM 5308 CA ILE C 311 -20.643-137.457 -25.442 1.00 28.98 C ANISOU 5308 CA ILE C 311 3784 3058 4170 -30 345 157 C ATOM 5309 C ILE C 311 -20.089-138.880 -25.535 1.00 19.29 C ANISOU 5309 C ILE C 311 2581 1755 2991 -25 464 197 C ATOM 5310 O ILE C 311 -20.394-139.734 -24.713 1.00 18.46 O ANISOU 5310 O ILE C 311 2482 1606 2924 29 492 296 O ATOM 5311 CB ILE C 311 -21.858-137.251 -26.376 1.00 25.64 C ANISOU 5311 CB ILE C 311 3378 2732 3630 -21 234 156 C ATOM 5312 CG1 ILE C 311 -22.631-136.009 -25.921 1.00 34.14 C ANISOU 5312 CG1 ILE C 311 4428 3875 4669 -3 111 153 C ATOM 5313 CG2 ILE C 311 -22.788-138.448 -26.355 1.00 17.14 C ANISOU 5313 CG2 ILE C 311 2333 1657 2523 38 227 261 C ATOM 5314 CD1 ILE C 311 -23.711-135.561 -26.860 1.00 22.53 C ANISOU 5314 CD1 ILE C 311 2970 2504 3086 -3 -3 133 C ATOM 5315 N ASP C 312 -19.269-139.120 -26.541 1.00 19.51 N ANISOU 5315 N ASP C 312 2625 1768 3021 -82 533 120 N ATOM 5316 CA ASP C 312 -18.646-140.410 -26.716 1.00 18.40 C ANISOU 5316 CA ASP C 312 2507 1555 2931 -84 651 147 C ATOM 5317 C ASP C 312 -17.739-140.737 -25.509 1.00 35.04 C ANISOU 5317 C ASP C 312 4595 3565 5152 -72 744 180 C ATOM 5318 O ASP C 312 -17.731-141.860 -25.010 1.00 47.34 O ANISOU 5318 O ASP C 312 6166 5065 6755 -34 810 263 O ATOM 5319 CB ASP C 312 -17.853-140.418 -28.014 1.00 18.12 C ANISOU 5319 CB ASP C 312 2486 1521 2879 -153 703 44 C ATOM 5320 CG ASP C 312 -18.721-140.646 -29.210 1.00 31.18 C ANISOU 5320 CG ASP C 312 4168 3247 4431 -155 644 38 C ATOM 5321 OD1 ASP C 312 -19.896-141.011 -29.007 1.00 51.18 O ANISOU 5321 OD1 ASP C 312 6714 5819 6913 -99 577 124 O ATOM 5322 OD2 ASP C 312 -18.238-140.481 -30.353 1.00 37.57 O ANISOU 5322 OD2 ASP C 312 4987 4075 5212 -212 664 -51 O ATOM 5323 N LEU C 313 -16.984-139.742 -25.055 1.00 28.59 N ANISOU 5323 N LEU C 313 3749 2733 4381 -103 749 116 N ATOM 5324 CA LEU C 313 -16.143-139.846 -23.887 1.00 19.08 C ANISOU 5324 CA LEU C 313 2524 1445 3282 -94 826 140 C ATOM 5325 C LEU C 313 -16.964-140.176 -22.655 1.00 27.56 C ANISOU 5325 C LEU C 313 3589 2506 4375 -20 791 259 C ATOM 5326 O LEU C 313 -16.582-141.042 -21.867 1.00 39.91 O ANISOU 5326 O LEU C 313 5155 3996 6015 8 872 325 O ATOM 5327 CB LEU C 313 -15.390-138.546 -23.672 1.00 29.92 C ANISOU 5327 CB LEU C 313 3866 2821 4681 -136 813 49 C ATOM 5328 CG LEU C 313 -13.889-138.615 -23.403 1.00 68.00 C ANISOU 5328 CG LEU C 313 8679 7559 9601 -177 931 -7 C ATOM 5329 CD1 LEU C 313 -13.242-139.749 -24.189 1.00 73.05 C ANISOU 5329 CD1 LEU C 313 9345 8150 10261 -204 1034 -23 C ATOM 5330 CD2 LEU C 313 -13.230-137.272 -23.720 1.00 71.24 C ANISOU 5330 CD2 LEU C 313 9068 7996 10004 -231 905 -122 C ATOM 5331 N VAL C 314 -18.099-139.509 -22.486 1.00 21.41 N ANISOU 5331 N VAL C 314 2802 1803 3531 12 669 289 N ATOM 5332 CA VAL C 314 -18.974-139.776 -21.349 1.00 19.52 C ANISOU 5332 CA VAL C 314 2555 1558 3304 84 624 401 C ATOM 5333 C VAL C 314 -19.618-141.172 -21.426 1.00 23.20 C ANISOU 5333 C VAL C 314 3053 2008 3754 133 650 498 C ATOM 5334 O VAL C 314 -19.720-141.872 -20.424 1.00 33.53 O ANISOU 5334 O VAL C 314 4360 3263 5118 182 686 588 O ATOM 5335 CB VAL C 314 -20.067-138.696 -21.174 1.00 18.92 C ANISOU 5335 CB VAL C 314 2461 1567 3161 108 482 408 C ATOM 5336 CG1 VAL C 314 -21.053-139.112 -20.107 1.00 21.30 C ANISOU 5336 CG1 VAL C 314 2758 1865 3470 185 434 528 C ATOM 5337 CG2 VAL C 314 -19.455-137.355 -20.812 1.00 18.36 C ANISOU 5337 CG2 VAL C 314 2354 1501 3120 72 461 331 C ATOM 5338 N ARG C 315 -20.059-141.590 -22.598 1.00 27.60 N ANISOU 5338 N ARG C 315 3641 2612 4236 120 632 481 N ATOM 5339 CA ARG C 315 -20.772-142.858 -22.669 1.00 38.38 C ANISOU 5339 CA ARG C 315 5037 3968 5578 171 646 575 C ATOM 5340 C ARG C 315 -19.846-144.008 -22.385 1.00 29.93 C ANISOU 5340 C ARG C 315 3978 2801 4593 170 784 605 C ATOM 5341 O ARG C 315 -20.222-144.946 -21.693 1.00 42.97 O ANISOU 5341 O ARG C 315 5640 4414 6272 226 812 706 O ATOM 5342 CB ARG C 315 -21.396-143.088 -24.038 1.00 35.02 C ANISOU 5342 CB ARG C 315 4643 3609 5054 157 604 548 C ATOM 5343 CG ARG C 315 -22.518-142.152 -24.401 1.00 40.97 C ANISOU 5343 CG ARG C 315 5392 4463 5710 167 462 534 C ATOM 5344 CD ARG C 315 -22.359-141.815 -25.851 1.00 40.11 C ANISOU 5344 CD ARG C 315 5299 4407 5534 109 449 438 C ATOM 5345 NE ARG C 315 -23.614-141.870 -26.568 1.00 48.05 N ANISOU 5345 NE ARG C 315 6328 5496 6434 135 351 464 N ATOM 5346 CZ ARG C 315 -23.715-141.741 -27.882 1.00 41.76 C ANISOU 5346 CZ ARG C 315 5550 4751 5565 95 330 397 C ATOM 5347 NH1 ARG C 315 -22.628-141.572 -28.631 1.00 20.50 N ANISOU 5347 NH1 ARG C 315 2856 2035 2896 27 402 301 N ATOM 5348 NH2 ARG C 315 -24.907-141.790 -28.441 1.00 53.24 N ANISOU 5348 NH2 ARG C 315 7025 6280 6923 125 238 428 N ATOM 5349 N GLN C 316 -18.649-143.943 -22.966 1.00 34.48 N ANISOU 5349 N GLN C 316 4552 3339 5209 106 870 516 N ATOM 5350 CA GLN C 316 -17.657-144.994 -22.825 1.00 29.08 C ANISOU 5350 CA GLN C 316 3878 2563 4608 96 1006 530 C ATOM 5351 C GLN C 316 -17.455-145.201 -21.347 1.00 32.16 C ANISOU 5351 C GLN C 316 4248 2888 5084 139 1041 605 C ATOM 5352 O GLN C 316 -17.587-146.301 -20.827 1.00 47.61 O ANISOU 5352 O GLN C 316 6219 4794 7077 183 1097 694 O ATOM 5353 CB GLN C 316 -16.340-144.563 -23.467 1.00 36.90 C ANISOU 5353 CB GLN C 316 4859 3524 5636 18 1077 412 C ATOM 5354 CG GLN C 316 -15.383-145.717 -23.777 1.00 44.19 C ANISOU 5354 CG GLN C 316 5800 4366 6625 -3 1213 410 C ATOM 5355 CD GLN C 316 -16.037-146.786 -24.626 1.00 44.90 C ANISOU 5355 CD GLN C 316 5926 4475 6659 17 1222 455 C ATOM 5356 OE1 GLN C 316 -16.729-146.481 -25.602 1.00 39.11 O ANISOU 5356 OE1 GLN C 316 5208 3818 5834 6 1147 425 O ATOM 5357 NE2 GLN C 316 -15.841-148.050 -24.243 1.00 53.48 N ANISOU 5357 NE2 GLN C 316 7029 5492 7801 49 1312 532 N ATOM 5358 N MET C 317 -17.168-144.102 -20.671 1.00 38.51 N ANISOU 5358 N MET C 317 5019 3696 5917 126 1005 569 N ATOM 5359 CA MET C 317 -16.949-144.100 -19.241 1.00 40.58 C ANISOU 5359 CA MET C 317 5257 3900 6260 163 1030 631 C ATOM 5360 C MET C 317 -18.033-144.880 -18.498 1.00 33.28 C ANISOU 5360 C MET C 317 4344 2977 5324 242 995 760 C ATOM 5361 O MET C 317 -17.727-145.726 -17.661 1.00 36.89 O ANISOU 5361 O MET C 317 4802 3362 5853 274 1071 831 O ATOM 5362 CB MET C 317 -16.873-142.659 -18.745 1.00 42.90 C ANISOU 5362 CB MET C 317 5517 4226 6558 147 960 580 C ATOM 5363 CG MET C 317 -16.041-142.457 -17.498 1.00 41.16 C ANISOU 5363 CG MET C 317 5268 3931 6441 153 1021 594 C ATOM 5364 SD MET C 317 -15.759-140.549 -17.171 1.00 96.16 S ANISOU 5364 SD MET C 317 12192 10939 13406 118 942 503 S ATOM 5365 CE MET C 317 -14.755-140.679 -15.498 1.00166.86 C ANISOU 5365 CE MET C 317 21118 19784 22499 138 1039 548 C ATOM 5366 N ILE C 318 -19.292-144.604 -18.803 1.00 22.79 N ANISOU 5366 N ILE C 318 3024 1731 3905 273 880 789 N ATOM 5367 CA ILE C 318 -20.409-145.239 -18.104 1.00 23.61 C ANISOU 5367 CA ILE C 318 3137 1843 3991 351 832 908 C ATOM 5368 C ILE C 318 -20.635-146.690 -18.551 1.00 35.12 C ANISOU 5368 C ILE C 318 4634 3275 5436 377 894 971 C ATOM 5369 O ILE C 318 -21.056-147.538 -17.766 1.00 43.66 O ANISOU 5369 O ILE C 318 5723 4321 6544 437 912 1073 O ATOM 5370 CB ILE C 318 -21.706-144.475 -18.325 1.00 26.68 C ANISOU 5370 CB ILE C 318 3525 2330 4285 376 685 918 C ATOM 5371 CG1 ILE C 318 -21.608-143.060 -17.748 1.00 44.98 C ANISOU 5371 CG1 ILE C 318 5802 4673 6617 360 618 870 C ATOM 5372 CG2 ILE C 318 -22.869-145.215 -17.704 1.00 39.03 C ANISOU 5372 CG2 ILE C 318 5102 3902 5824 457 637 1039 C ATOM 5373 CD1 ILE C 318 -22.662-142.090 -18.315 1.00 31.89 C ANISOU 5373 CD1 ILE C 318 4140 3118 4858 361 477 840 C ATOM 5374 N TYR C 319 -20.365-146.956 -19.821 1.00 31.73 N ANISOU 5374 N TYR C 319 4228 2864 4964 334 924 909 N ATOM 5375 CA TYR C 319 -20.445-148.299 -20.370 1.00 24.32 C ANISOU 5375 CA TYR C 319 3325 1898 4016 351 993 956 C ATOM 5376 C TYR C 319 -19.434-149.193 -19.666 1.00 33.37 C ANISOU 5376 C TYR C 319 4469 2939 5271 353 1127 991 C ATOM 5377 O TYR C 319 -19.796-150.247 -19.137 1.00 51.11 O ANISOU 5377 O TYR C 319 6732 5149 7539 408 1163 1089 O ATOM 5378 CB TYR C 319 -20.120-148.255 -21.852 1.00 25.27 C ANISOU 5378 CB TYR C 319 3465 2051 4084 291 1010 866 C ATOM 5379 CG TYR C 319 -20.191-149.584 -22.536 1.00 28.66 C ANISOU 5379 CG TYR C 319 3932 2457 4501 304 1080 906 C ATOM 5380 CD1 TYR C 319 -21.406-150.156 -22.829 1.00 41.33 C ANISOU 5380 CD1 TYR C 319 5566 4110 6028 357 1018 979 C ATOM 5381 CD2 TYR C 319 -19.043-150.260 -22.904 1.00 50.82 C ANISOU 5381 CD2 TYR C 319 6745 5192 7372 263 1207 870 C ATOM 5382 CE1 TYR C 319 -21.479-151.376 -23.457 1.00 41.80 C ANISOU 5382 CE1 TYR C 319 5661 4148 6075 371 1084 1018 C ATOM 5383 CE2 TYR C 319 -19.112-151.483 -23.540 1.00 45.08 C ANISOU 5383 CE2 TYR C 319 6052 4442 6636 276 1273 908 C ATOM 5384 CZ TYR C 319 -20.336-152.030 -23.811 1.00 27.87 C ANISOU 5384 CZ TYR C 319 3901 2311 4377 330 1212 983 C ATOM 5385 OH TYR C 319 -20.435-153.238 -24.446 1.00 52.26 O ANISOU 5385 OH TYR C 319 7024 5378 7453 345 1276 1023 O ATOM 5386 N ASP C 320 -18.172-148.760 -19.665 1.00 27.62 N ANISOU 5386 N ASP C 320 3721 2164 4610 295 1200 909 N ATOM 5387 CA ASP C 320 -17.086-149.478 -18.996 1.00 42.36 C ANISOU 5387 CA ASP C 320 5581 3929 6585 290 1329 928 C ATOM 5388 C ASP C 320 -17.415-149.739 -17.537 1.00 41.29 C ANISOU 5388 C ASP C 320 5424 3775 6489 351 1314 1016 C ATOM 5389 O ASP C 320 -17.555-150.903 -17.115 1.00 35.60 O ANISOU 5389 O ASP C 320 4709 3040 5777 391 1355 1081 O ATOM 5390 CB ASP C 320 -15.756-148.723 -19.100 1.00 35.72 C ANISOU 5390 CB ASP C 320 4716 3053 5804 220 1386 820 C ATOM 5391 CG ASP C 320 -15.292-148.558 -20.531 1.00 48.69 C ANISOU 5391 CG ASP C 320 6373 4723 7405 154 1403 717 C ATOM 5392 OD1 ASP C 320 -14.344-147.777 -20.775 1.00 59.22 O ANISOU 5392 OD1 ASP C 320 7687 6045 8767 95 1428 617 O ATOM 5393 OD2 ASP C 320 -15.888-149.205 -21.417 1.00 54.34 O ANISOU 5393 OD2 ASP C 320 7118 5472 8057 163 1392 735 O ATOM 5394 N THR C 321 -17.537-148.658 -16.772 1.00 28.25 N ANISOU 5394 N THR C 321 3743 2139 4850 355 1249 1007 N ATOM 5395 CA THR C 321 -17.921-148.764 -15.368 1.00 48.10 C ANISOU 5395 CA THR C 321 6230 4660 7387 409 1215 1076 C ATOM 5396 C THR C 321 -18.977-149.841 -15.188 1.00 45.71 C ANISOU 5396 C THR C 321 5950 4380 7040 473 1187 1175 C ATOM 5397 O THR C 321 -18.816-150.764 -14.394 1.00 36.94 O ANISOU 5397 O THR C 321 4829 3245 5961 503 1235 1222 O ATOM 5398 CB THR C 321 -18.500-147.437 -14.823 1.00 33.98 C ANISOU 5398 CB THR C 321 4417 2910 5583 421 1107 1074 C ATOM 5399 OG1 THR C 321 -17.445-146.490 -14.652 1.00 49.35 O ANISOU 5399 OG1 THR C 321 6336 4834 7583 368 1137 988 O ATOM 5400 CG2 THR C 321 -19.150-147.661 -13.484 1.00 42.74 C ANISOU 5400 CG2 THR C 321 5504 4037 6697 480 1058 1153 C ATOM 5401 N GLU C 322 -20.068-149.730 -15.928 1.00 30.38 N ANISOU 5401 N GLU C 322 4037 2487 5019 496 1107 1205 N ATOM 5402 CA GLU C 322 -21.143-150.663 -15.703 1.00 29.90 C ANISOU 5402 CA GLU C 322 3994 2458 4906 560 1067 1294 C ATOM 5403 C GLU C 322 -20.899-152.113 -16.153 1.00 27.55 C ANISOU 5403 C GLU C 322 3724 2130 4613 567 1159 1321 C ATOM 5404 O GLU C 322 -21.367-153.029 -15.513 1.00 33.70 O ANISOU 5404 O GLU C 322 4505 2913 5387 615 1160 1388 O ATOM 5405 CB GLU C 322 -22.434-150.119 -16.264 1.00 26.34 C ANISOU 5405 CB GLU C 322 3562 2080 4364 588 944 1319 C ATOM 5406 CG GLU C 322 -23.414-149.839 -15.173 1.00 26.44 C ANISOU 5406 CG GLU C 322 3553 2142 4351 640 840 1372 C ATOM 5407 CD GLU C 322 -24.697-150.586 -15.389 1.00 45.75 C ANISOU 5407 CD GLU C 322 6026 4643 6712 694 772 1436 C ATOM 5408 OE1 GLU C 322 -24.941-151.049 -16.526 1.00 51.84 O ANISOU 5408 OE1 GLU C 322 6835 5429 7433 691 784 1437 O ATOM 5409 OE2 GLU C 322 -25.459-150.722 -14.421 1.00 51.87 O ANISOU 5409 OE2 GLU C 322 6788 5450 7471 736 707 1480 O ATOM 5410 N MET C 323 -20.193-152.318 -17.254 1.00 27.41 N ANISOU 5410 N MET C 323 3727 2084 4602 519 1233 1266 N ATOM 5411 CA MET C 323 -19.884-153.670 -17.678 1.00 29.12 C ANISOU 5411 CA MET C 323 3966 2270 4828 523 1324 1286 C ATOM 5412 C MET C 323 -19.112-154.382 -16.585 1.00 47.48 C ANISOU 5412 C MET C 323 6263 4548 7231 534 1404 1302 C ATOM 5413 O MET C 323 -19.350-155.552 -16.299 1.00 62.70 O ANISOU 5413 O MET C 323 8199 6465 9158 573 1439 1362 O ATOM 5414 CB MET C 323 -19.058-153.636 -18.958 1.00 56.32 C ANISOU 5414 CB MET C 323 7429 5690 8279 458 1396 1206 C ATOM 5415 CG MET C 323 -19.845-153.128 -20.153 1.00 63.20 C ANISOU 5415 CG MET C 323 8337 6608 9069 449 1328 1196 C ATOM 5416 SD MET C 323 -21.655-153.890 -20.166 1.00 97.94 S ANISOU 5416 SD MET C 323 12771 11077 13365 540 1229 1315 S ATOM 5417 CE MET C 323 -22.633-152.355 -19.394 1.00 49.63 C ANISOU 5417 CE MET C 323 6622 5033 7202 567 1064 1320 C ATOM 5418 N ARG C 324 -18.183-153.656 -15.976 1.00 33.96 N ANISOU 5418 N ARG C 324 4514 2807 5582 499 1430 1247 N ATOM 5419 CA ARG C 324 -17.473-154.142 -14.826 1.00 33.53 C ANISOU 5419 CA ARG C 324 4428 2714 5598 510 1492 1262 C ATOM 5420 C ARG C 324 -18.391-154.388 -13.625 1.00 44.46 C ANISOU 5420 C ARG C 324 5801 4122 6970 573 1430 1348 C ATOM 5421 O ARG C 324 -18.455-155.502 -13.110 1.00 53.39 O ANISOU 5421 O ARG C 324 6933 5235 8117 608 1474 1403 O ATOM 5422 CB ARG C 324 -16.365-153.179 -14.438 1.00 28.86 C ANISOU 5422 CB ARG C 324 3802 2098 5067 461 1519 1182 C ATOM 5423 CG ARG C 324 -15.735-153.536 -13.111 1.00 38.43 C ANISOU 5423 CG ARG C 324 4977 3276 6346 478 1569 1203 C ATOM 5424 CD ARG C 324 -15.285-152.293 -12.411 1.00 44.49 C ANISOU 5424 CD ARG C 324 5711 4048 7147 455 1536 1157 C ATOM 5425 NE ARG C 324 -14.726-151.367 -13.384 1.00 51.06 N ANISOU 5425 NE ARG C 324 6546 4883 7971 396 1536 1063 N ATOM 5426 CZ ARG C 324 -14.417-150.108 -13.112 1.00 63.96 C ANISOU 5426 CZ ARG C 324 8156 6528 9619 368 1496 1009 C ATOM 5427 NH1 ARG C 324 -14.622-149.652 -11.886 1.00 44.83 N ANISOU 5427 NH1 ARG C 324 5703 4112 7217 395 1455 1044 N ATOM 5428 NH2 ARG C 324 -13.922-149.312 -14.061 1.00 73.20 N ANISOU 5428 NH2 ARG C 324 9330 7704 10778 312 1496 920 N ATOM 5429 N VAL C 325 -19.087-153.353 -13.174 1.00 50.53 N ANISOU 5429 N VAL C 325 6556 4931 7710 587 1327 1357 N ATOM 5430 CA VAL C 325 -19.945-153.454 -11.994 1.00 41.25 C ANISOU 5430 CA VAL C 325 5367 3784 6523 641 1258 1427 C ATOM 5431 C VAL C 325 -21.036-154.508 -12.121 1.00 47.24 C ANISOU 5431 C VAL C 325 6155 4572 7223 695 1227 1503 C ATOM 5432 O VAL C 325 -21.277-155.289 -11.190 1.00 58.51 O ANISOU 5432 O VAL C 325 7574 5992 8665 733 1239 1560 O ATOM 5433 CB VAL C 325 -20.630-152.119 -11.678 1.00 52.69 C ANISOU 5433 CB VAL C 325 6799 5281 7939 645 1141 1418 C ATOM 5434 CG1 VAL C 325 -21.881-152.360 -10.853 1.00 43.77 C ANISOU 5434 CG1 VAL C 325 5668 4197 6764 705 1049 1491 C ATOM 5435 CG2 VAL C 325 -19.664-151.185 -10.952 1.00 76.92 C ANISOU 5435 CG2 VAL C 325 9828 8322 11076 610 1164 1364 C ATOM 5436 N ASN C 326 -21.687-154.526 -13.278 1.00 46.68 N ANISOU 5436 N ASN C 326 7358 4079 6299 958 1781 2196 N ATOM 5437 CA ASN C 326 -22.895-155.323 -13.489 1.00 44.89 C ANISOU 5437 CA ASN C 326 7197 3947 5912 1067 1700 2323 C ATOM 5438 C ASN C 326 -22.889-155.955 -14.881 1.00 52.96 C ANISOU 5438 C ASN C 326 8258 4984 6880 1015 1790 2323 C ATOM 5439 O ASN C 326 -23.563-155.461 -15.795 1.00 43.78 O ANISOU 5439 O ASN C 326 7110 3961 5562 974 1683 2274 O ATOM 5440 CB ASN C 326 -24.102-154.408 -13.320 1.00 46.04 C ANISOU 5440 CB ASN C 326 7344 4277 5872 1101 1460 2304 C ATOM 5441 CG ASN C 326 -25.412-155.102 -13.569 1.00 51.86 C ANISOU 5441 CG ASN C 326 8132 5132 6441 1193 1355 2403 C ATOM 5442 OD1 ASN C 326 -26.451-154.446 -13.670 1.00 53.59 O ANISOU 5442 OD1 ASN C 326 8346 5513 6502 1201 1165 2370 O ATOM 5443 ND2 ASN C 326 -25.383-156.428 -13.661 1.00 46.39 N ANISOU 5443 ND2 ASN C 326 7481 4360 5785 1258 1476 2517 N ATOM 5444 N PRO C 327 -22.127-157.056 -15.050 1.00 46.90 N ANISOU 5444 N PRO C 327 7504 4075 6242 1016 1986 2373 N ATOM 5445 CA PRO C 327 -21.780-157.515 -16.399 1.00 46.95 C ANISOU 5445 CA PRO C 327 7530 4070 6239 936 2099 2335 C ATOM 5446 C PRO C 327 -22.943-158.162 -17.149 1.00 54.27 C ANISOU 5446 C PRO C 327 8521 5111 6988 1000 2023 2425 C ATOM 5447 O PRO C 327 -22.910-158.279 -18.383 1.00 51.45 O ANISOU 5447 O PRO C 327 8179 4793 6576 928 2059 2378 O ATOM 5448 CB PRO C 327 -20.641-158.505 -16.165 1.00 48.84 C ANISOU 5448 CB PRO C 327 7758 4120 6678 928 2322 2362 C ATOM 5449 CG PRO C 327 -20.265-158.341 -14.710 1.00 65.74 C ANISOU 5449 CG PRO C 327 9860 6174 8943 982 2324 2386 C ATOM 5450 CD PRO C 327 -21.501-157.886 -14.021 1.00 48.90 C ANISOU 5450 CD PRO C 327 7749 4172 6660 1084 2114 2454 C ATOM 5451 N ALA C 328 -23.976-158.559 -16.417 1.00 53.40 N ANISOU 5451 N ALA C 328 8441 5060 6787 1128 1911 2542 N ATOM 5452 CA ALA C 328 -25.213-158.969 -17.072 1.00 71.59 C ANISOU 5452 CA ALA C 328 10792 7500 8909 1179 1800 2602 C ATOM 5453 C ALA C 328 -25.794-157.841 -17.941 1.00 46.25 C ANISOU 5453 C ALA C 328 7564 4457 5551 1093 1642 2484 C ATOM 5454 O ALA C 328 -26.395-158.098 -18.973 1.00 46.05 O ANISOU 5454 O ALA C 328 7565 4522 5412 1072 1605 2482 O ATOM 5455 CB ALA C 328 -26.242-159.460 -16.043 1.00 76.04 C ANISOU 5455 CB ALA C 328 11378 8110 9403 1322 1689 2724 C ATOM 5456 N ALA C 329 -25.600-156.591 -17.530 1.00 44.48 N ANISOU 5456 N ALA C 329 7293 4274 5332 1040 1552 2383 N ATOM 5457 CA ALA C 329 -26.170-155.446 -18.255 1.00 42.21 C ANISOU 5457 CA ALA C 329 6983 4150 4905 961 1394 2268 C ATOM 5458 C ALA C 329 -25.738-155.379 -19.723 1.00 43.19 C ANISOU 5458 C ALA C 329 7108 4292 5009 846 1470 2184 C ATOM 5459 O ALA C 329 -26.264-154.585 -20.493 1.00 53.91 O ANISOU 5459 O ALA C 329 8448 5791 6243 780 1347 2095 O ATOM 5460 CB ALA C 329 -25.836-154.148 -17.547 1.00 40.56 C ANISOU 5460 CB ALA C 329 6723 3957 4730 919 1315 2172 C ATOM 5461 N ALA C 330 -24.781-156.213 -20.111 1.00 42.55 N ANISOU 5461 N ALA C 330 7041 4071 5054 818 1669 2205 N ATOM 5462 CA ALA C 330 -24.331-156.245 -21.498 1.00 48.84 C ANISOU 5462 CA ALA C 330 7836 4881 5841 710 1747 2123 C ATOM 5463 C ALA C 330 -25.379-156.868 -22.417 1.00 48.18 C ANISOU 5463 C ALA C 330 7793 4907 5606 742 1675 2180 C ATOM 5464 O ALA C 330 -25.211-156.875 -23.632 1.00 55.43 O ANISOU 5464 O ALA C 330 8709 5864 6489 659 1707 2117 O ATOM 5465 CB ALA C 330 -23.021-157.006 -21.609 1.00 65.04 C ANISOU 5465 CB ALA C 330 9882 6751 8078 668 1977 2120 C ATOM 5466 N ALA C 331 -26.458-157.383 -21.831 1.00 44.73 N ANISOU 5466 N ALA C 331 7387 4522 5085 859 1576 2293 N ATOM 5467 CA ALA C 331 -27.444-158.160 -22.572 1.00 44.14 C ANISOU 5467 CA ALA C 331 7350 4531 4890 899 1524 2359 C ATOM 5468 C ALA C 331 -28.292-157.262 -23.456 1.00 63.09 C ANISOU 5468 C ALA C 331 9722 7113 7137 826 1348 2258 C ATOM 5469 O ALA C 331 -28.651-157.615 -24.579 1.00 57.95 O ANISOU 5469 O ALA C 331 9083 6523 6415 788 1343 2247 O ATOM 5470 CB ALA C 331 -28.323-158.958 -21.620 1.00 45.87 C ANISOU 5470 CB ALA C 331 7603 4750 5075 1038 1471 2496 C ATOM 5471 N HIS C 332 -28.614-156.089 -22.939 1.00 66.62 N ANISOU 5471 N HIS C 332 10125 7648 7540 803 1203 2179 N ATOM 5472 CA HIS C 332 -29.338-155.107 -23.724 1.00 56.13 C ANISOU 5472 CA HIS C 332 8753 6488 6087 719 1037 2066 C ATOM 5473 C HIS C 332 -28.505-153.848 -23.960 1.00 47.06 C ANISOU 5473 C HIS C 332 7552 5355 4975 609 1039 1924 C ATOM 5474 O HIS C 332 -28.704-153.141 -24.939 1.00 48.70 O ANISOU 5474 O HIS C 332 7717 5675 5111 514 963 1818 O ATOM 5475 CB HIS C 332 -30.674-154.787 -23.064 1.00 75.72 C ANISOU 5475 CB HIS C 332 11229 9081 8462 801 865 2087 C ATOM 5476 CG HIS C 332 -31.506-156.001 -22.789 1.00 86.04 C ANISOU 5476 CG HIS C 332 12591 10373 9728 930 882 2226 C ATOM 5477 ND1 HIS C 332 -31.094-157.005 -21.940 1.00 80.77 N ANISOU 5477 ND1 HIS C 332 11957 9578 9154 1003 976 2346 N ATOM 5478 CD2 HIS C 332 -32.722-156.374 -23.255 1.00 87.04 C ANISOU 5478 CD2 HIS C 332 12742 10594 9734 999 821 2261 C ATOM 5479 CE1 HIS C 332 -32.024-157.942 -21.889 1.00 90.31 C ANISOU 5479 CE1 HIS C 332 13209 10810 10294 1114 971 2452 C ATOM 5480 NE2 HIS C 332 -33.020-157.585 -22.678 1.00 88.17 N ANISOU 5480 NE2 HIS C 332 12933 10672 9893 1113 878 2403 N ATOM 5481 N THR C 333 -27.566-153.567 -23.072 1.00 36.63 N ANISOU 5481 N THR C 333 6226 3920 3771 618 1126 1919 N ATOM 5482 CA THR C 333 -26.599-152.515 -23.346 1.00 34.93 C ANISOU 5482 CA THR C 333 5966 3694 3612 507 1165 1785 C ATOM 5483 C THR C 333 -25.346-153.099 -23.996 1.00 47.94 C ANISOU 5483 C THR C 333 7623 5208 5386 442 1376 1764 C ATOM 5484 O THR C 333 -24.384-153.451 -23.309 1.00 64.78 O ANISOU 5484 O THR C 333 9760 7182 7671 453 1523 1788 O ATOM 5485 CB THR C 333 -26.208-151.769 -22.071 1.00 34.45 C ANISOU 5485 CB THR C 333 5884 3583 3624 530 1143 1766 C ATOM 5486 OG1 THR C 333 -27.391-151.404 -21.359 1.00 47.36 O ANISOU 5486 OG1 THR C 333 7509 5330 5155 601 952 1796 O ATOM 5487 CG2 THR C 333 -25.429-150.507 -22.421 1.00 39.38 C ANISOU 5487 CG2 THR C 333 6455 4231 4276 407 1146 1609 C ATOM 5488 N THR C 334 -25.359-153.192 -25.325 1.00 38.82 N ANISOU 5488 N THR C 334 6459 4116 4174 368 1387 1708 N ATOM 5489 CA THR C 334 -24.315-153.906 -26.063 1.00 38.07 C ANISOU 5489 CA THR C 334 6371 3908 4186 309 1576 1690 C ATOM 5490 C THR C 334 -23.281-152.974 -26.670 1.00 34.34 C ANISOU 5490 C THR C 334 5836 3437 3773 172 1621 1520 C ATOM 5491 O THR C 334 -22.298-153.430 -27.247 1.00 36.99 O ANISOU 5491 O THR C 334 6160 3680 4213 107 1771 1473 O ATOM 5492 CB THR C 334 -24.923-154.728 -27.206 1.00 36.61 C ANISOU 5492 CB THR C 334 6214 3786 3910 315 1568 1736 C ATOM 5493 OG1 THR C 334 -25.672-153.855 -28.064 1.00 54.37 O ANISOU 5493 OG1 THR C 334 8420 6219 6020 254 1400 1648 O ATOM 5494 CG2 THR C 334 -25.861-155.761 -26.648 1.00 52.07 C ANISOU 5494 CG2 THR C 334 8231 5730 5822 446 1541 1897 C ATOM 5495 N ALA C 335 -23.523-151.671 -26.563 1.00 43.53 N ANISOU 5495 N ALA C 335 6952 4714 4872 126 1485 1420 N ATOM 5496 CA ALA C 335 -22.625-150.676 -27.147 1.00 36.63 C ANISOU 5496 CA ALA C 335 6009 3866 4042 -2 1505 1246 C ATOM 5497 C ALA C 335 -22.643-149.459 -26.274 1.00 32.26 C ANISOU 5497 C ALA C 335 5422 3351 3485 -14 1411 1178 C ATOM 5498 O ALA C 335 -23.666-149.175 -25.669 1.00 48.44 O ANISOU 5498 O ALA C 335 7487 5483 5434 62 1270 1243 O ATOM 5499 CB ALA C 335 -23.076-150.305 -28.534 1.00 39.54 C ANISOU 5499 CB ALA C 335 6337 4394 4293 -64 1406 1171 C ATOM 5500 N PRO C 336 -21.502-148.746 -26.189 1.00 39.91 N ANISOU 5500 N PRO C 336 6336 4260 4567 -111 1484 1038 N ATOM 5501 CA PRO C 336 -21.416-147.474 -25.457 1.00 26.78 C ANISOU 5501 CA PRO C 336 4633 2637 2904 -141 1399 948 C ATOM 5502 C PRO C 336 -22.369-146.473 -26.035 1.00 24.92 C ANISOU 5502 C PRO C 336 4363 2606 2500 -152 1204 889 C ATOM 5503 O PRO C 336 -22.791-145.551 -25.359 1.00 39.63 O ANISOU 5503 O PRO C 336 6210 4537 4312 -136 1089 861 O ATOM 5504 CB PRO C 336 -19.970-147.021 -25.689 1.00 31.96 C ANISOU 5504 CB PRO C 336 5219 3213 3713 -264 1513 775 C ATOM 5505 CG PRO C 336 -19.471-147.845 -26.837 1.00 50.88 C ANISOU 5505 CG PRO C 336 7610 5581 6143 -304 1611 755 C ATOM 5506 CD PRO C 336 -20.196-149.155 -26.730 1.00 35.08 C ANISOU 5506 CD PRO C 336 5692 3536 4103 -197 1650 948 C ATOM 5507 N GLY C 337 -22.721-146.665 -27.293 1.00 30.14 N ANISOU 5507 N GLY C 337 4999 3369 3083 -177 1163 868 N ATOM 5508 CA GLY C 337 -23.656-145.769 -27.951 1.00 39.45 C ANISOU 5508 CA GLY C 337 6106 4752 4130 -183 975 810 C ATOM 5509 C GLY C 337 -25.081-145.908 -27.463 1.00 33.97 C ANISOU 5509 C GLY C 337 5431 4154 3323 -91 830 919 C ATOM 5510 O GLY C 337 -25.948-145.107 -27.807 1.00 52.89 O ANISOU 5510 O GLY C 337 7797 6676 5622 -74 701 861 O ATOM 5511 N GLU C 338 -25.345-146.918 -26.656 1.00 25.01 N ANISOU 5511 N GLU C 338 4382 2916 2203 -8 880 1064 N ATOM 5512 CA GLU C 338 -26.695-147.133 -26.170 1.00 26.02 C ANISOU 5512 CA GLU C 338 4524 3125 2237 76 737 1156 C ATOM 5513 C GLU C 338 -26.934-146.564 -24.767 1.00 37.44 C ANISOU 5513 C GLU C 338 5975 4559 3692 131 660 1174 C ATOM 5514 O GLU C 338 -28.048-146.615 -24.239 1.00 29.04 O ANISOU 5514 O GLU C 338 4912 3560 2561 198 532 1229 O ATOM 5515 CB GLU C 338 -27.038-148.615 -26.248 1.00 27.60 C ANISOU 5515 CB GLU C 338 4804 3246 2435 150 811 1300 C ATOM 5516 CG GLU C 338 -26.951-149.098 -27.650 1.00 27.92 C ANISOU 5516 CG GLU C 338 4858 3304 2447 116 882 1279 C ATOM 5517 CD GLU C 338 -27.460-150.483 -27.803 1.00 43.24 C ANISOU 5517 CD GLU C 338 6874 5189 4366 197 939 1416 C ATOM 5518 OE1 GLU C 338 -27.789-151.085 -26.766 1.00 65.08 O ANISOU 5518 OE1 GLU C 338 9680 7895 7153 282 932 1526 O ATOM 5519 OE2 GLU C 338 -27.520-150.966 -28.954 1.00 58.03 O ANISOU 5519 OE2 GLU C 338 8765 7080 6206 179 991 1411 O ATOM 5520 N ILE C 339 -25.888-145.988 -24.190 1.00 30.44 N ANISOU 5520 N ILE C 339 5094 3581 2893 101 744 1115 N ATOM 5521 CA ILE C 339 -25.965-145.387 -22.871 1.00 24.50 C ANISOU 5521 CA ILE C 339 4347 2806 2158 150 681 1124 C ATOM 5522 C ILE C 339 -26.798-144.109 -22.815 1.00 23.32 C ANISOU 5522 C ILE C 339 4104 2838 1916 123 480 1024 C ATOM 5523 O ILE C 339 -26.513-143.151 -23.533 1.00 37.57 O ANISOU 5523 O ILE C 339 5829 4734 3711 38 451 887 O ATOM 5524 CB ILE C 339 -24.564-145.049 -22.359 1.00 40.99 C ANISOU 5524 CB ILE C 339 6450 4740 4385 96 835 1066 C ATOM 5525 CG1 ILE C 339 -23.778-146.342 -22.043 1.00 26.46 C ANISOU 5525 CG1 ILE C 339 4663 2699 2693 131 1035 1171 C ATOM 5526 CG2 ILE C 339 -24.667-144.115 -21.159 1.00 39.65 C ANISOU 5526 CG2 ILE C 339 6270 4579 4216 126 742 1042 C ATOM 5527 CD1 ILE C 339 -24.354-147.132 -20.913 1.00 28.14 C ANISOU 5527 CD1 ILE C 339 4921 2850 2922 271 1010 1332 C ATOM 5528 N ASP C 340 -27.820-144.087 -21.956 1.00 24.93 N ANISOU 5528 N ASP C 340 4297 3097 2077 194 344 1083 N ATOM 5529 CA ASP C 340 -28.542-142.845 -21.644 1.00 22.68 C ANISOU 5529 CA ASP C 340 3919 2952 1746 173 181 982 C ATOM 5530 C ASP C 340 -27.783-142.015 -20.625 1.00 30.40 C ANISOU 5530 C ASP C 340 4890 3882 2778 171 182 932 C ATOM 5531 O ASP C 340 -27.866-142.250 -19.418 1.00 47.29 O ANISOU 5531 O ASP C 340 7076 5947 4944 254 163 1011 O ATOM 5532 CB ASP C 340 -29.962-143.125 -21.141 1.00 26.13 C ANISOU 5532 CB ASP C 340 4380 3434 2113 269 70 1043 C ATOM 5533 CG ASP C 340 -30.566-141.958 -20.344 1.00 34.96 C ANISOU 5533 CG ASP C 340 5434 4631 3218 279 -59 958 C ATOM 5534 OD1 ASP C 340 -30.070-140.808 -20.404 1.00 34.16 O ANISOU 5534 OD1 ASP C 340 5262 4575 3142 214 -78 834 O ATOM 5535 OD2 ASP C 340 -31.577-142.197 -19.649 1.00 36.91 O ANISOU 5535 OD2 ASP C 340 5698 4894 3431 358 -135 1010 O ATOM 5536 N PHE C 341 -27.057-141.030 -21.129 1.00 23.95 N ANISOU 5536 N PHE C 341 4021 3100 1976 89 208 791 N ATOM 5537 CA PHE C 341 -26.242-140.158 -20.316 1.00 18.22 C ANISOU 5537 CA PHE C 341 3320 2311 1292 70 224 711 C ATOM 5538 C PHE C 341 -27.004-138.909 -19.854 1.00 29.80 C ANISOU 5538 C PHE C 341 4645 3941 2738 69 49 608 C ATOM 5539 O PHE C 341 -26.390-137.879 -19.596 1.00 43.31 O ANISOU 5539 O PHE C 341 6327 5650 4478 25 35 478 O ATOM 5540 CB PHE C 341 -25.060-139.713 -21.150 1.00 20.44 C ANISOU 5540 CB PHE C 341 3607 2539 1619 -46 346 577 C ATOM 5541 CG PHE C 341 -25.463-139.021 -22.415 1.00 26.94 C ANISOU 5541 CG PHE C 341 4281 3533 2424 -85 263 455 C ATOM 5542 CD1 PHE C 341 -25.570-137.641 -22.462 1.00 29.68 C ANISOU 5542 CD1 PHE C 341 4526 3957 2794 -106 160 298 C ATOM 5543 CD2 PHE C 341 -25.784-139.756 -23.545 1.00 28.49 C ANISOU 5543 CD2 PHE C 341 4466 3763 2595 -82 297 501 C ATOM 5544 CE1 PHE C 341 -25.961-137.001 -23.615 1.00 19.30 C ANISOU 5544 CE1 PHE C 341 3175 2675 1484 -133 113 203 C ATOM 5545 CE2 PHE C 341 -26.172-139.130 -24.691 1.00 23.40 C ANISOU 5545 CE2 PHE C 341 3786 3179 1925 -100 247 394 C ATOM 5546 CZ PHE C 341 -26.264-137.745 -24.730 1.00 31.28 C ANISOU 5546 CZ PHE C 341 4721 4205 2960 -127 156 251 C ATOM 5547 N LEU C 342 -28.327-138.971 -19.747 1.00 17.17 N ANISOU 5547 N LEU C 342 3000 2430 1094 114 -60 645 N ATOM 5548 CA LEU C 342 -29.065-137.805 -19.249 1.00 30.83 C ANISOU 5548 CA LEU C 342 4660 4236 2819 125 -175 541 C ATOM 5549 C LEU C 342 -29.921-138.140 -18.054 1.00 17.58 C ANISOU 5549 C LEU C 342 3005 2548 1128 200 -256 632 C ATOM 5550 O LEU C 342 -30.004-137.371 -17.097 1.00 30.38 O ANISOU 5550 O LEU C 342 4580 4183 2780 209 -320 581 O ATOM 5551 CB LEU C 342 -29.941-137.175 -20.344 1.00 16.04 C ANISOU 5551 CB LEU C 342 2741 2435 918 104 -211 451 C ATOM 5552 CG LEU C 342 -29.140-136.640 -21.512 1.00 14.84 C ANISOU 5552 CG LEU C 342 2552 2284 802 45 -149 342 C ATOM 5553 CD1 LEU C 342 -30.014-136.362 -22.704 1.00 27.64 C ANISOU 5553 CD1 LEU C 342 4142 3957 2401 39 -169 308 C ATOM 5554 CD2 LEU C 342 -28.370-135.427 -21.072 1.00 20.39 C ANISOU 5554 CD2 LEU C 342 3195 2962 1589 8 -163 214 C ATOM 5555 N THR C 343 -30.580-139.288 -18.130 1.00 25.41 N ANISOU 5555 N THR C 343 4067 3511 2079 259 -250 760 N ATOM 5556 CA THR C 343 -31.461-139.730 -17.060 1.00 21.39 C ANISOU 5556 CA THR C 343 3582 2989 1555 347 -321 846 C ATOM 5557 C THR C 343 -31.019-141.117 -16.590 1.00 32.44 C ANISOU 5557 C THR C 343 5060 4277 2989 407 -258 1013 C ATOM 5558 O THR C 343 -31.614-141.708 -15.684 1.00 32.06 O ANISOU 5558 O THR C 343 5040 4201 2941 495 -300 1105 O ATOM 5559 CB THR C 343 -32.925-139.724 -17.512 1.00 24.06 C ANISOU 5559 CB THR C 343 3927 3397 1818 384 -378 829 C ATOM 5560 OG1 THR C 343 -33.045-140.476 -18.729 1.00 27.27 O ANISOU 5560 OG1 THR C 343 4379 3801 2180 376 -318 867 O ATOM 5561 CG2 THR C 343 -33.399-138.284 -17.742 1.00 20.00 C ANISOU 5561 CG2 THR C 343 3334 2955 1311 331 -432 677 C ATOM 5562 N PHE C 344 -29.972-141.622 -17.237 1.00 21.95 N ANISOU 5562 N PHE C 344 3764 2875 1702 359 -145 1046 N ATOM 5563 CA PHE C 344 -29.217-142.749 -16.732 1.00 30.02 C ANISOU 5563 CA PHE C 344 4894 3728 2783 449 -24 1182 C ATOM 5564 C PHE C 344 -30.063-143.999 -16.546 1.00 39.60 C ANISOU 5564 C PHE C 344 6148 4919 3978 529 -35 1313 C ATOM 5565 O PHE C 344 -29.809-144.833 -15.681 1.00 37.74 O ANISOU 5565 O PHE C 344 5972 4568 3802 633 25 1430 O ATOM 5566 CB PHE C 344 -28.554-142.342 -15.433 1.00 26.62 C ANISOU 5566 CB PHE C 344 4478 3208 2429 509 -20 1192 C ATOM 5567 CG PHE C 344 -27.980-140.989 -15.488 1.00 21.80 C ANISOU 5567 CG PHE C 344 3821 2645 1817 431 -50 1046 C ATOM 5568 CD1 PHE C 344 -28.553-139.954 -14.784 1.00 24.96 C ANISOU 5568 CD1 PHE C 344 4122 3159 2204 414 -200 960 C ATOM 5569 CD2 PHE C 344 -26.891-140.732 -16.299 1.00 32.42 C ANISOU 5569 CD2 PHE C 344 5214 3922 3180 355 82 979 C ATOM 5570 CE1 PHE C 344 -28.022-138.695 -14.847 1.00 28.93 C ANISOU 5570 CE1 PHE C 344 4574 3711 2707 343 -227 809 C ATOM 5571 CE2 PHE C 344 -26.351-139.473 -16.371 1.00 24.10 C ANISOU 5571 CE2 PHE C 344 4133 2910 2115 272 51 824 C ATOM 5572 CZ PHE C 344 -26.917-138.449 -15.645 1.00 34.59 C ANISOU 5572 CZ PHE C 344 5362 4359 3424 276 -114 736 C ATOM 5573 N LEU C 345 -31.070-144.125 -17.386 1.00 29.48 N ANISOU 5573 N LEU C 345 4858 3738 2604 516 -82 1291 N ATOM 5574 CA LEU C 345 -31.810-145.344 -17.435 1.00 27.67 C ANISOU 5574 CA LEU C 345 4694 3485 2335 609 -60 1409 C ATOM 5575 C LEU C 345 -31.176-146.235 -18.482 1.00 28.96 C ANISOU 5575 C LEU C 345 4907 3580 2515 579 74 1458 C ATOM 5576 O LEU C 345 -30.718-145.751 -19.511 1.00 33.30 O ANISOU 5576 O LEU C 345 5436 4164 3054 488 113 1371 O ATOM 5577 CB LEU C 345 -33.247-145.038 -17.806 1.00 42.78 C ANISOU 5577 CB LEU C 345 6593 5525 4138 642 -155 1361 C ATOM 5578 CG LEU C 345 -33.865-144.003 -16.879 1.00 36.85 C ANISOU 5578 CG LEU C 345 5780 4844 3375 652 -274 1286 C ATOM 5579 CD1 LEU C 345 -35.354-143.864 -17.173 1.00 43.54 C ANISOU 5579 CD1 LEU C 345 6623 5791 4130 693 -347 1255 C ATOM 5580 CD2 LEU C 345 -33.643-144.410 -15.443 1.00 28.23 C ANISOU 5580 CD2 LEU C 345 4698 3681 2346 724 -292 1377 C ATOM 5581 N ALA C 346 -31.152-147.536 -18.218 1.00 30.06 N ANISOU 5581 N ALA C 346 5110 3626 2687 657 150 1593 N ATOM 5582 CA ALA C 346 -30.747-148.501 -19.225 1.00 50.69 C ANISOU 5582 CA ALA C 346 7772 6179 5309 642 280 1646 C ATOM 5583 C ALA C 346 -31.950-148.795 -20.096 1.00 35.16 C ANISOU 5583 C ALA C 346 5824 4316 3217 681 236 1647 C ATOM 5584 O ALA C 346 -33.083-148.550 -19.708 1.00 31.78 O ANISOU 5584 O ALA C 346 5385 3974 2716 741 127 1640 O ATOM 5585 CB ALA C 346 -30.229-149.802 -18.573 1.00 37.54 C ANISOU 5585 CB ALA C 346 6177 4357 3729 750 422 1795 C ATOM 5586 N VAL C 347 -31.697-149.346 -21.268 1.00 39.00 N ANISOU 5586 N VAL C 347 6341 4789 3690 645 328 1654 N ATOM 5587 CA VAL C 347 -32.780-149.702 -22.160 1.00 41.50 C ANISOU 5587 CA VAL C 347 6679 5190 3899 682 297 1661 C ATOM 5588 C VAL C 347 -33.867-150.512 -21.443 1.00 34.22 C ANISOU 5588 C VAL C 347 5794 4278 2929 812 252 1771 C ATOM 5589 O VAL C 347 -35.051-150.248 -21.627 1.00 60.48 O ANISOU 5589 O VAL C 347 9109 7706 6165 848 159 1741 O ATOM 5590 CB VAL C 347 -32.233-150.423 -23.400 1.00 40.91 C ANISOU 5590 CB VAL C 347 6638 5073 3833 639 422 1680 C ATOM 5591 CG1 VAL C 347 -33.356-151.067 -24.181 1.00 52.32 C ANISOU 5591 CG1 VAL C 347 8118 6582 5179 699 401 1720 C ATOM 5592 CG2 VAL C 347 -31.444-149.427 -24.268 1.00 33.33 C ANISOU 5592 CG2 VAL C 347 5627 4147 2891 510 437 1543 C ATOM 5593 N ASP C 348 -33.549-151.466 -20.596 1.00 65.48 N ANISOU 5593 N ASP C 348 9793 8130 6958 881 324 1893 N ATOM 5594 CA ASP C 348 -34.601-152.275 -19.976 1.00 67.04 C ANISOU 5594 CA ASP C 348 10024 8330 7118 1011 293 2006 C ATOM 5595 C ASP C 348 -35.492-151.460 -19.090 1.00 55.79 C ANISOU 5595 C ASP C 348 8556 7007 5633 1046 144 1953 C ATOM 5596 O ASP C 348 -36.584-151.862 -18.763 1.00 38.55 O ANISOU 5596 O ASP C 348 6389 4879 3379 1137 92 2006 O ATOM 5597 CB ASP C 348 -34.013-153.442 -19.189 1.00 83.79 C ANISOU 5597 CB ASP C 348 12176 10311 9348 1070 384 2126 C ATOM 5598 CG ASP C 348 -33.335-154.458 -20.084 1.00111.59 C ANISOU 5598 CG ASP C 348 15751 13726 12922 1075 544 2213 C ATOM 5599 OD1 ASP C 348 -32.179-154.206 -20.519 1.00120.81 O ANISOU 5599 OD1 ASP C 348 16914 14794 14195 996 647 2191 O ATOM 5600 OD2 ASP C 348 -33.958-155.506 -20.362 1.00118.61 O ANISOU 5600 OD2 ASP C 348 16684 14629 13752 1156 573 2302 O ATOM 5601 N GLY C 349 -35.016-150.296 -18.699 1.00 54.98 N ANISOU 5601 N GLY C 349 8398 6929 5564 972 80 1847 N ATOM 5602 CA GLY C 349 -35.806-149.380 -17.908 1.00 58.30 C ANISOU 5602 CA GLY C 349 8770 7439 5941 995 -53 1785 C ATOM 5603 C GLY C 349 -35.159-149.076 -16.597 1.00 51.77 C ANISOU 5603 C GLY C 349 7919 6553 5200 1009 -79 1801 C ATOM 5604 O GLY C 349 -35.558-148.169 -15.909 1.00 55.65 O ANISOU 5604 O GLY C 349 8357 7109 5680 993 -182 1721 O ATOM 5605 N ASP C 350 -34.145-149.854 -16.286 1.00 45.80 N ANISOU 5605 N ASP C 350 7199 5666 4538 1038 19 1902 N ATOM 5606 CA ASP C 350 -33.506-149.906 -14.995 1.00 54.13 C ANISOU 5606 CA ASP C 350 8233 6645 5690 1063 2 1930 C ATOM 5607 C ASP C 350 -32.323-148.963 -14.893 1.00 48.60 C ANISOU 5607 C ASP C 350 7497 5880 5089 955 34 1851 C ATOM 5608 O ASP C 350 -31.463-149.018 -15.719 1.00 59.88 O ANISOU 5608 O ASP C 350 8945 7257 6552 889 141 1834 O ATOM 5609 CB ASP C 350 -32.971-151.326 -14.854 1.00 84.38 C ANISOU 5609 CB ASP C 350 12117 10359 9584 1165 90 2084 C ATOM 5610 CG ASP C 350 -32.348-151.843 -16.150 1.00 99.69 C ANISOU 5610 CG ASP C 350 14072 12365 11441 1286 24 2160 C ATOM 5611 OD1 ASP C 350 -32.762-151.423 -17.234 1.00 93.92 O ANISOU 5611 OD1 ASP C 350 13303 11755 10628 1290 -99 2089 O ATOM 5612 OD2 ASP C 350 -31.439-152.682 -16.099 1.00101.59 O ANISOU 5612 OD2 ASP C 350 14362 12535 11702 1377 100 2289 O ATOM 5613 N PRO C 351 -32.240-148.139 -13.864 1.00 38.35 N ANISOU 5613 N PRO C 351 6148 4584 3838 948 -47 1803 N ATOM 5614 CA PRO C 351 -31.105-147.249 -13.699 1.00 31.99 C ANISOU 5614 CA PRO C 351 5319 3726 3109 898 -2 1730 C ATOM 5615 C PRO C 351 -29.794-147.952 -13.485 1.00 44.79 C ANISOU 5615 C PRO C 351 6999 5166 4853 951 201 1816 C ATOM 5616 O PRO C 351 -29.693-148.784 -12.629 1.00 67.92 O ANISOU 5616 O PRO C 351 9960 8000 7845 1051 264 1934 O ATOM 5617 CB PRO C 351 -31.461-146.510 -12.443 1.00 34.78 C ANISOU 5617 CB PRO C 351 5617 4111 3487 927 -127 1700 C ATOM 5618 CG PRO C 351 -32.245-147.383 -11.738 1.00 33.45 C ANISOU 5618 CG PRO C 351 5466 3945 3298 1018 -178 1802 C ATOM 5619 CD PRO C 351 -33.113-148.039 -12.707 1.00 52.21 C ANISOU 5619 CD PRO C 351 7885 6388 5564 1039 -153 1833 C ATOM 5620 N TYR C 352 -28.787-147.585 -14.248 1.00 40.70 N ANISOU 5620 N TYR C 352 6488 4595 4382 871 312 1751 N ATOM 5621 CA TYR C 352 -27.482-148.226 -14.201 1.00 52.33 C ANISOU 5621 CA TYR C 352 7998 5879 6007 881 527 1807 C ATOM 5622 C TYR C 352 -27.048-148.447 -12.754 1.00 34.30 C ANISOU 5622 C TYR C 352 5703 3475 3853 967 556 1874 C ATOM 5623 O TYR C 352 -27.310-147.617 -11.898 1.00 33.51 O ANISOU 5623 O TYR C 352 5560 3429 3743 985 424 1830 O ATOM 5624 CB TYR C 352 -26.465-147.360 -14.941 1.00 53.88 C ANISOU 5624 CB TYR C 352 8180 6043 6249 758 614 1688 C ATOM 5625 CG TYR C 352 -26.853-147.114 -16.371 1.00 47.30 C ANISOU 5625 CG TYR C 352 7349 5333 5291 670 584 1613 C ATOM 5626 CD1 TYR C 352 -26.932-148.171 -17.270 1.00 45.68 C ANISOU 5626 CD1 TYR C 352 7183 5104 5070 670 679 1673 C ATOM 5627 CD2 TYR C 352 -27.145-145.828 -16.835 1.00 42.85 C ANISOU 5627 CD2 TYR C 352 6737 4912 4631 584 456 1476 C ATOM 5628 CE1 TYR C 352 -27.297-147.957 -18.592 1.00 56.19 C ANISOU 5628 CE1 TYR C 352 8505 6550 6296 588 644 1601 C ATOM 5629 CE2 TYR C 352 -27.504-145.609 -18.162 1.00 27.12 C ANISOU 5629 CE2 TYR C 352 4727 3036 2541 499 426 1401 C ATOM 5630 CZ TYR C 352 -27.584-146.677 -19.026 1.00 28.25 C ANISOU 5630 CZ TYR C 352 4910 3152 2673 502 516 1465 C ATOM 5631 OH TYR C 352 -27.929-146.501 -20.333 1.00 50.43 O ANISOU 5631 OH TYR C 352 7692 6071 5399 419 483 1393 O ATOM 5632 N GLN C 353 -26.396-149.569 -12.481 1.00 36.18 N ANISOU 5632 N GLN C 353 5971 3557 4221 1017 725 1975 N ATOM 5633 CA GLN C 353 -25.956-149.902 -11.126 1.00 37.48 C ANISOU 5633 CA GLN C 353 6117 3599 4523 1098 765 2041 C ATOM 5634 C GLN C 353 -24.627-149.220 -10.789 1.00 43.73 C ANISOU 5634 C GLN C 353 6865 4257 5494 1023 872 1956 C ATOM 5635 O GLN C 353 -24.280-149.063 -9.622 1.00 55.39 O ANISOU 5635 O GLN C 353 8305 5659 7081 1068 861 1966 O ATOM 5636 CB GLN C 353 -25.860-151.413 -10.959 1.00 39.93 C ANISOU 5636 CB GLN C 353 6470 3803 4899 1180 900 2179 C ATOM 5637 CG GLN C 353 -26.946-151.984 -10.058 1.00 59.18 C ANISOU 5637 CG GLN C 353 8921 6308 7259 1308 776 2280 C ATOM 5638 CD GLN C 353 -27.115-153.506 -10.169 1.00 43.65 C ANISOU 5638 CD GLN C 353 7008 4274 5305 1388 891 2418 C ATOM 5639 OE1 GLN C 353 -26.775-154.118 -11.179 1.00 44.05 O ANISOU 5639 OE1 GLN C 353 7092 4279 5364 1348 1021 2435 O ATOM 5640 NE2 GLN C 353 -27.662-154.111 -9.123 1.00 77.62 N ANISOU 5640 NE2 GLN C 353 11315 8573 9603 1504 839 2515 N ATOM 5641 N GLY C 354 -23.904-148.795 -11.820 1.00 45.91 N ANISOU 5641 N GLY C 354 7137 4506 5800 898 972 1859 N ATOM 5642 CA GLY C 354 -22.623-148.129 -11.652 1.00 36.95 C ANISOU 5642 CA GLY C 354 5949 3246 4846 794 1084 1748 C ATOM 5643 C GLY C 354 -22.698-146.611 -11.575 1.00 32.32 C ANISOU 5643 C GLY C 354 5326 2747 4207 731 951 1622 C ATOM 5644 O GLY C 354 -21.682-145.938 -11.514 1.00 31.97 O ANISOU 5644 O GLY C 354 5230 2610 4307 625 1032 1504 O ATOM 5645 N ILE C 355 -23.900-146.057 -11.571 1.00 31.42 N ANISOU 5645 N ILE C 355 5228 2817 3893 785 743 1629 N ATOM 5646 CA ILE C 355 -24.015-144.620 -11.392 1.00 29.36 C ANISOU 5646 CA ILE C 355 4933 2647 3575 740 606 1512 C ATOM 5647 C ILE C 355 -24.782-144.268 -10.135 1.00 29.50 C ANISOU 5647 C ILE C 355 4917 2743 3550 846 418 1542 C ATOM 5648 O ILE C 355 -25.653-144.995 -9.699 1.00 59.81 O ANISOU 5648 O ILE C 355 8765 6639 7320 941 341 1638 O ATOM 5649 CB ILE C 355 -24.622-143.941 -12.614 1.00 30.10 C ANISOU 5649 CB ILE C 355 5047 2917 3474 665 515 1429 C ATOM 5650 CG1 ILE C 355 -23.847-144.351 -13.861 1.00 41.14 C ANISOU 5650 CG1 ILE C 355 6472 4242 4918 554 705 1393 C ATOM 5651 CG2 ILE C 355 -24.598-142.425 -12.445 1.00 54.22 C ANISOU 5651 CG2 ILE C 355 8071 6057 6472 609 390 1294 C ATOM 5652 CD1 ILE C 355 -24.176-143.525 -15.063 1.00 60.94 C ANISOU 5652 CD1 ILE C 355 8986 6906 7263 456 636 1278 C ATOM 5653 N GLN C 356 -24.398-143.179 -9.510 1.00 35.09 N ANISOU 5653 N GLN C 356 5577 3439 4315 822 354 1450 N ATOM 5654 CA GLN C 356 -25.139-142.684 -8.384 1.00 30.59 C ANISOU 5654 CA GLN C 356 4961 2970 3694 904 158 1449 C ATOM 5655 C GLN C 356 -25.433-141.259 -8.778 1.00 30.90 C ANISOU 5655 C GLN C 356 4973 3161 3607 833 12 1305 C ATOM 5656 O GLN C 356 -24.511-140.453 -8.873 1.00 25.08 O ANISOU 5656 O GLN C 356 4236 2336 2957 765 71 1207 O ATOM 5657 CB GLN C 356 -24.299-142.734 -7.105 1.00 31.64 C ANISOU 5657 CB GLN C 356 5045 2935 4041 948 217 1462 C ATOM 5658 CG GLN C 356 -24.799-141.759 -6.055 1.00 52.95 C ANISOU 5658 CG GLN C 356 7678 5739 6701 992 13 1401 C ATOM 5659 CD GLN C 356 -23.925-141.681 -4.823 1.00 42.52 C ANISOU 5659 CD GLN C 356 6297 4260 5600 1024 65 1390 C ATOM 5660 OE1 GLN C 356 -23.291-142.656 -4.448 1.00 51.35 O ANISOU 5660 OE1 GLN C 356 7419 5220 6872 1049 217 1465 O ATOM 5661 NE2 GLN C 356 -23.895-140.510 -4.180 1.00 40.31 N ANISOU 5661 NE2 GLN C 356 5950 4033 5333 1018 -68 1282 N ATOM 5662 N VAL C 357 -26.707-140.966 -9.052 1.00 31.13 N ANISOU 5662 N VAL C 357 4970 3407 3452 823 -161 1273 N ATOM 5663 CA VAL C 357 -27.109-139.655 -9.560 1.00 28.36 C ANISOU 5663 CA VAL C 357 4562 3234 2978 728 -292 1114 C ATOM 5664 C VAL C 357 -27.258-138.652 -8.429 1.00 25.09 C ANISOU 5664 C VAL C 357 4057 2884 2590 738 -431 1028 C ATOM 5665 O VAL C 357 -27.665-139.006 -7.330 1.00 43.06 O ANISOU 5665 O VAL C 357 6293 5149 4920 810 -484 1101 O ATOM 5666 CB VAL C 357 -28.457-139.735 -10.283 1.00 43.79 C ANISOU 5666 CB VAL C 357 6463 5377 4798 672 -380 1095 C ATOM 5667 CG1 VAL C 357 -28.726-138.444 -11.039 1.00 46.19 C ANISOU 5667 CG1 VAL C 357 6680 5844 5027 543 -445 920 C ATOM 5668 CG2 VAL C 357 -28.483-140.920 -11.220 1.00 23.99 C ANISOU 5668 CG2 VAL C 357 4039 2811 2266 685 -265 1195 C ATOM 5669 N LEU C 358 -26.928-137.400 -8.697 1.00 27.75 N ANISOU 5669 N LEU C 358 4361 3293 2891 653 -492 860 N ATOM 5670 CA LEU C 358 -27.044-136.357 -7.692 1.00 30.92 C ANISOU 5670 CA LEU C 358 4658 3769 3322 639 -615 747 C ATOM 5671 C LEU C 358 -28.142-135.383 -8.092 1.00 39.40 C ANISOU 5671 C LEU C 358 5592 5071 4307 515 -672 616 C ATOM 5672 O LEU C 358 -28.004-134.675 -9.094 1.00 47.26 O ANISOU 5672 O LEU C 358 6558 6134 5265 408 -646 490 O ATOM 5673 CB LEU C 358 -25.713-135.621 -7.528 1.00 18.45 C ANISOU 5673 CB LEU C 358 3131 2044 1834 610 -637 631 C ATOM 5674 CG LEU C 358 -24.531-136.401 -6.945 1.00 39.16 C ANISOU 5674 CG LEU C 358 5715 4432 4730 603 -440 673 C ATOM 5675 CD1 LEU C 358 -23.335-135.481 -6.698 1.00 38.17 C ANISOU 5675 CD1 LEU C 358 5460 4247 4797 442 -396 450 C ATOM 5676 CD2 LEU C 358 -24.931-137.096 -5.666 1.00 53.96 C ANISOU 5676 CD2 LEU C 358 7607 6241 6654 781 -477 847 C ATOM 5677 N GLY C 359 -29.227-135.353 -7.317 1.00 30.75 N ANISOU 5677 N GLY C 359 4404 4068 3213 514 -717 661 N ATOM 5678 CA GLY C 359 -30.362-134.490 -7.613 1.00 35.96 C ANISOU 5678 CA GLY C 359 5038 4832 3794 467 -753 537 C ATOM 5679 C GLY C 359 -30.218-133.039 -7.168 1.00 41.34 C ANISOU 5679 C GLY C 359 5662 5530 4515 411 -779 362 C ATOM 5680 O GLY C 359 -29.110-132.517 -7.022 1.00 29.56 O ANISOU 5680 O GLY C 359 4137 3999 3093 365 -762 286 O ATOM 5681 N PRO C 360 -31.347-132.358 -6.949 1.00 43.02 N ANISOU 5681 N PRO C 360 5866 5784 4697 415 -813 300 N ATOM 5682 CA PRO C 360 -31.186-130.968 -6.508 1.00 50.02 C ANISOU 5682 CA PRO C 360 6705 6653 5648 368 -818 160 C ATOM 5683 C PRO C 360 -30.636-130.911 -5.094 1.00 61.25 C ANISOU 5683 C PRO C 360 8097 8045 7130 400 -859 165 C ATOM 5684 O PRO C 360 -29.903-129.978 -4.759 1.00 79.25 O ANISOU 5684 O PRO C 360 10340 10282 9490 354 -847 61 O ATOM 5685 CB PRO C 360 -32.607-130.409 -6.575 1.00 60.96 C ANISOU 5685 CB PRO C 360 8096 8078 6987 384 -838 132 C ATOM 5686 CG PRO C 360 -33.293-131.279 -7.599 1.00 77.74 C ANISOU 5686 CG PRO C 360 10265 10241 9030 401 -826 208 C ATOM 5687 CD PRO C 360 -32.726-132.652 -7.364 1.00 66.58 C ANISOU 5687 CD PRO C 360 8882 8816 7598 448 -831 340 C ATOM 5688 N LEU C 361 -30.975-131.902 -4.277 1.00 52.18 N ANISOU 5688 N LEU C 361 6959 6909 5957 484 -901 297 N ATOM 5689 CA LEU C 361 -30.428-131.977 -2.933 1.00 50.06 C ANISOU 5689 CA LEU C 361 6652 6608 5759 527 -936 328 C ATOM 5690 C LEU C 361 -28.899-131.871 -2.972 1.00 60.36 C ANISOU 5690 C LEU C 361 7926 7847 7162 491 -904 294 C ATOM 5691 O LEU C 361 -28.282-131.369 -2.031 1.00 70.56 O ANISOU 5691 O LEU C 361 9172 9101 8537 487 -927 236 O ATOM 5692 CB LEU C 361 -30.843-133.285 -2.259 1.00 63.49 C ANISOU 5692 CB LEU C 361 8367 8306 7452 632 -962 522 C ATOM 5693 CG LEU C 361 -32.330-133.621 -2.137 1.00 84.32 C ANISOU 5693 CG LEU C 361 11038 11003 9995 679 -1004 572 C ATOM 5694 CD1 LEU C 361 -32.523-135.130 -2.029 1.00 90.18 C ANISOU 5694 CD1 LEU C 361 11819 11707 10738 764 -1004 772 C ATOM 5695 CD2 LEU C 361 -32.976-132.902 -0.957 1.00 80.12 C ANISOU 5695 CD2 LEU C 361 10476 10506 9461 699 -1062 510 C ATOM 5696 N ASP C 362 -28.295-132.332 -4.070 1.00 52.34 N ANISOU 5696 N ASP C 362 6935 6812 6140 462 -852 324 N ATOM 5697 CA ASP C 362 -26.837-132.460 -4.167 1.00 36.08 C ANISOU 5697 CA ASP C 362 4932 4608 4168 490 -883 278 C ATOM 5698 C ASP C 362 -26.144-131.621 -5.264 1.00 57.75 C ANISOU 5698 C ASP C 362 7670 7356 6918 356 -853 112 C ATOM 5699 O ASP C 362 -25.034-131.946 -5.697 1.00 52.98 O ANISOU 5699 O ASP C 362 7147 6613 6369 361 -905 85 O ATOM 5700 CB ASP C 362 -26.453-133.930 -4.336 1.00 54.45 C ANISOU 5700 CB ASP C 362 7384 6781 6523 631 -862 468 C ATOM 5701 CG ASP C 362 -26.597-134.720 -3.056 1.00 68.33 C ANISOU 5701 CG ASP C 362 9128 8466 8370 761 -855 622 C ATOM 5702 OD1 ASP C 362 -25.771-134.511 -2.137 1.00 55.03 O ANISOU 5702 OD1 ASP C 362 7414 6658 6837 800 -882 586 O ATOM 5703 OD2 ASP C 362 -27.525-135.557 -2.973 1.00 84.97 O ANISOU 5703 OD2 ASP C 362 11236 10626 10421 808 -828 770 O ATOM 5704 N GLY C 363 -26.786-130.543 -5.707 1.00 64.92 N ANISOU 5704 N GLY C 363 9420 7463 7783 280 524 -539 N ATOM 5705 CA GLY C 363 -26.161-129.639 -6.657 1.00 35.99 C ANISOU 5705 CA GLY C 363 5880 3675 4119 100 494 -577 C ATOM 5706 C GLY C 363 -26.467-129.981 -8.099 1.00 42.21 C ANISOU 5706 C GLY C 363 6669 4466 4903 48 420 -466 C ATOM 5707 O GLY C 363 -25.846-129.467 -9.021 1.00 45.68 O ANISOU 5707 O GLY C 363 7173 4825 5358 -87 379 -442 O ATOM 5708 N GLY C 364 -27.439-130.856 -8.298 1.00 34.19 N ANISOU 5708 N GLY C 364 5529 3592 3871 159 393 -374 N ATOM 5709 CA GLY C 364 -27.736-131.331 -9.627 1.00 23.38 C ANISOU 5709 CA GLY C 364 4151 2232 2499 128 323 -256 C ATOM 5710 C GLY C 364 -29.043-130.846 -10.231 1.00 29.83 C ANISOU 5710 C GLY C 364 4861 3229 3244 108 288 -290 C ATOM 5711 O GLY C 364 -29.792-130.038 -9.675 1.00 37.23 O ANISOU 5711 O GLY C 364 5728 4288 4128 101 317 -415 O ATOM 5712 N ILE C 365 -29.298-131.354 -11.421 1.00 23.29 N ANISOU 5712 N ILE C 365 4022 2414 2413 92 226 -176 N ATOM 5713 CA ILE C 365 -30.519-131.079 -12.113 1.00 15.59 C ANISOU 5713 CA ILE C 365 2948 1602 1376 83 189 -187 C ATOM 5714 C ILE C 365 -31.120-132.392 -12.577 1.00 15.83 C ANISOU 5714 C ILE C 365 2878 1730 1408 200 146 -37 C ATOM 5715 O ILE C 365 -30.456-133.183 -13.237 1.00 41.27 O ANISOU 5715 O ILE C 365 6159 4847 4674 198 113 95 O ATOM 5716 CB ILE C 365 -30.258-130.180 -13.322 1.00 19.18 C ANISOU 5716 CB ILE C 365 3497 1977 1813 -73 150 -205 C ATOM 5717 CG1 ILE C 365 -29.999-128.752 -12.848 1.00 31.40 C ANISOU 5717 CG1 ILE C 365 5112 3478 3339 -181 195 -367 C ATOM 5718 CG2 ILE C 365 -31.439-130.200 -14.259 1.00 31.68 C ANISOU 5718 CG2 ILE C 365 4985 3709 3344 -67 102 -175 C ATOM 5719 CD1 ILE C 365 -29.638-127.791 -13.965 1.00 53.71 C ANISOU 5719 CD1 ILE C 365 7941 6265 6202 -310 157 -329 C ATOM 5720 N THR C 366 -32.376-132.621 -12.220 1.00 30.36 N ANISOU 5720 N THR C 366 4561 3777 3196 298 149 -59 N ATOM 5721 CA THR C 366 -33.133-133.732 -12.761 1.00 35.56 C ANISOU 5721 CA THR C 366 5109 4563 3841 401 104 73 C ATOM 5722 C THR C 366 -33.712-133.399 -14.141 1.00 44.42 C ANISOU 5722 C THR C 366 6222 5733 4923 319 44 95 C ATOM 5723 O THR C 366 -34.559-132.520 -14.265 1.00 77.96 O ANISOU 5723 O THR C 366 10419 10086 9114 271 47 -17 O ATOM 5724 CB THR C 366 -34.271-134.133 -11.808 1.00 37.03 C ANISOU 5724 CB THR C 366 5120 4971 3978 544 132 38 C ATOM 5725 OG1 THR C 366 -33.733-134.403 -10.507 1.00 47.33 O ANISOU 5725 OG1 THR C 366 6432 6235 5316 628 192 17 O ATOM 5726 CG2 THR C 366 -34.956-135.374 -12.301 1.00 43.88 C ANISOU 5726 CG2 THR C 366 5873 5967 4832 662 89 186 C ATOM 5727 N LEU C 367 -33.226-134.084 -15.173 1.00 36.72 N ANISOU 5727 N LEU C 367 5300 4675 3978 300 -7 236 N ATOM 5728 CA LEU C 367 -33.874-134.079 -16.479 1.00 28.96 C ANISOU 5728 CA LEU C 367 4281 3767 2955 261 -68 289 C ATOM 5729 C LEU C 367 -34.964-135.148 -16.502 1.00 27.92 C ANISOU 5729 C LEU C 367 3985 3834 2791 403 -92 377 C ATOM 5730 O LEU C 367 -35.148-135.875 -15.543 1.00 62.66 O ANISOU 5730 O LEU C 367 8305 8303 7199 528 -62 403 O ATOM 5731 CB LEU C 367 -32.879-134.398 -17.576 1.00 13.95 C ANISOU 5731 CB LEU C 367 2498 1707 1095 181 -114 408 C ATOM 5732 CG LEU C 367 -31.883-133.371 -18.046 1.00 24.99 C ANISOU 5732 CG LEU C 367 4053 2931 2510 24 -113 350 C ATOM 5733 CD1 LEU C 367 -31.719-132.301 -17.014 1.00 44.54 C ANISOU 5733 CD1 LEU C 367 6567 5372 4982 -18 -52 186 C ATOM 5734 CD2 LEU C 367 -30.584-134.100 -18.338 1.00 24.58 C ANISOU 5734 CD2 LEU C 367 4110 2706 2524 -5 -127 467 C ATOM 5735 N GLY C 368 -35.650-135.267 -17.628 1.00 32.72 N ANISOU 5735 N GLY C 368 4542 4531 3358 388 -147 429 N ATOM 5736 CA GLY C 368 -36.791-136.149 -17.747 1.00 24.80 C ANISOU 5736 CA GLY C 368 3371 3723 2330 500 -169 486 C ATOM 5737 C GLY C 368 -38.052-135.405 -18.182 1.00 26.71 C ANISOU 5737 C GLY C 368 3518 4092 2539 450 -173 364 C ATOM 5738 O GLY C 368 -38.024-134.182 -18.356 1.00 20.25 O ANISOU 5738 O GLY C 368 2774 3238 1681 351 -164 255 O ATOM 5739 N LYS C 369 -39.153-136.147 -18.334 1.00 34.85 N ANISOU 5739 N LYS C 369 4394 5251 3598 515 -171 374 N ATOM 5740 CA LYS C 369 -40.437-135.620 -18.810 1.00 29.92 C ANISOU 5740 CA LYS C 369 3674 4727 2967 481 -163 277 C ATOM 5741 C LYS C 369 -40.931-134.397 -18.045 1.00 27.32 C ANISOU 5741 C LYS C 369 3329 4474 2578 454 -130 120 C ATOM 5742 O LYS C 369 -41.665-133.587 -18.599 1.00 35.67 O ANISOU 5742 O LYS C 369 4372 5529 3653 377 -126 36 O ATOM 5743 CB LYS C 369 -41.513-136.707 -18.785 1.00 22.41 C ANISOU 5743 CB LYS C 369 2562 3917 2035 575 -138 307 C ATOM 5744 CG LYS C 369 -41.325-137.795 -19.815 1.00 28.35 C ANISOU 5744 CG LYS C 369 3330 4582 2859 554 -159 413 C ATOM 5745 CD LYS C 369 -42.119-139.039 -19.413 1.00 38.65 C ANISOU 5745 CD LYS C 369 4509 6019 4158 652 -114 452 C ATOM 5746 CE LYS C 369 -42.428-139.932 -20.610 1.00 46.95 C ANISOU 5746 CE LYS C 369 5554 7024 5261 613 -124 506 C ATOM 5747 NZ LYS C 369 -43.583-140.846 -20.356 1.00 52.23 N ANISOU 5747 NZ LYS C 369 6097 7863 5885 691 -63 513 N ATOM 5748 N ASP C 370 -40.523-134.264 -16.785 1.00 23.73 N ANISOU 5748 N ASP C 370 2885 4064 2069 509 -99 74 N ATOM 5749 CA ASP C 370 -40.925-133.126 -15.961 1.00 15.89 C ANISOU 5749 CA ASP C 370 1879 3102 1056 454 -51 -98 C ATOM 5750 C ASP C 370 -39.735-132.276 -15.597 1.00 26.75 C ANISOU 5750 C ASP C 370 3425 4321 2418 369 -21 -159 C ATOM 5751 O ASP C 370 -39.826-131.447 -14.699 1.00 25.94 O ANISOU 5751 O ASP C 370 3322 4204 2330 325 30 -288 O ATOM 5752 CB ASP C 370 -41.597-133.587 -14.672 1.00 45.86 C ANISOU 5752 CB ASP C 370 5524 7077 4824 576 -19 -142 C ATOM 5753 CG ASP C 370 -43.112-133.664 -14.797 1.00102.14 C ANISOU 5753 CG ASP C 370 12473 14357 11978 597 -31 -184 C ATOM 5754 OD1 ASP C 370 -43.680-132.952 -15.659 1.00113.93 O ANISOU 5754 OD1 ASP C 370 13978 15793 13515 495 -42 -228 O ATOM 5755 OD2 ASP C 370 -43.737-134.426 -14.028 1.00118.19 O ANISOU 5755 OD2 ASP C 370 14356 16566 13986 721 -31 -169 O ATOM 5756 N GLY C 371 -38.621-132.483 -16.293 1.00 21.68 N ANISOU 5756 N GLY C 371 2921 3526 1790 331 -52 -56 N ATOM 5757 CA GLY C 371 -37.354-131.890 -15.888 1.00 36.13 C ANISOU 5757 CA GLY C 371 4905 5150 3674 248 -20 -91 C ATOM 5758 C GLY C 371 -37.046-130.659 -16.707 1.00 51.39 C ANISOU 5758 C GLY C 371 6958 6964 5602 92 -26 -161 C ATOM 5759 O GLY C 371 -36.435-130.740 -17.770 1.00 51.61 O ANISOU 5759 O GLY C 371 7077 6881 5651 33 -70 -68 O ATOM 5760 N ASN C 372 -37.463-129.510 -16.188 1.00 47.88 N ANISOU 5760 N ASN C 372 6513 6536 5144 24 22 -316 N ATOM 5761 CA ASN C 372 -37.471-128.278 -16.943 1.00 21.29 C ANISOU 5761 CA ASN C 372 3164 3061 1862 -45 7 -352 C ATOM 5762 C ASN C 372 -36.150-127.520 -16.879 1.00 24.83 C ANISOU 5762 C ASN C 372 3707 3338 2389 -151 27 -361 C ATOM 5763 O ASN C 372 -35.669-127.190 -15.805 1.00 30.05 O ANISOU 5763 O ASN C 372 4390 3959 3068 -155 66 -424 O ATOM 5764 CB ASN C 372 -38.608-127.379 -16.446 1.00 33.22 C ANISOU 5764 CB ASN C 372 4623 4581 3417 -43 35 -424 C ATOM 5765 CG ASN C 372 -39.960-128.098 -16.382 1.00 41.29 C ANISOU 5765 CG ASN C 372 5508 5762 4417 -12 42 -416 C ATOM 5766 OD1 ASN C 372 -40.216-129.059 -17.104 1.00 37.25 O ANISOU 5766 OD1 ASN C 372 4942 5333 3876 30 3 -339 O ATOM 5767 ND2 ASN C 372 -40.834-127.611 -15.520 1.00 55.67 N ANISOU 5767 ND2 ASN C 372 7236 7648 6267 -7 76 -488 N ATOM 5768 N ILE C 373 -35.575-127.223 -18.039 1.00 21.41 N ANISOU 5768 N ILE C 373 3336 2793 2007 -224 1 -286 N ATOM 5769 CA ILE C 373 -34.392-126.385 -18.093 1.00 33.75 C ANISOU 5769 CA ILE C 373 4987 4194 3643 -313 22 -272 C ATOM 5770 C ILE C 373 -34.595-125.199 -19.044 1.00 24.01 C ANISOU 5770 C ILE C 373 3712 2933 2475 -359 26 -251 C ATOM 5771 O ILE C 373 -35.140-125.352 -20.128 1.00 23.84 O ANISOU 5771 O ILE C 373 3666 2941 2452 -353 -2 -208 O ATOM 5772 CB ILE C 373 -33.134-127.198 -18.483 1.00 46.67 C ANISOU 5772 CB ILE C 373 6778 5693 5261 -353 -4 -176 C ATOM 5773 CG1 ILE C 373 -33.308-127.846 -19.852 1.00 47.35 C ANISOU 5773 CG1 ILE C 373 6871 5783 5335 -353 -64 -75 C ATOM 5774 CG2 ILE C 373 -32.851-128.281 -17.456 1.00 59.25 C ANISOU 5774 CG2 ILE C 373 8442 7290 6780 -289 3 -185 C ATOM 5775 CD1 ILE C 373 -32.048-128.523 -20.345 1.00 64.96 C ANISOU 5775 CD1 ILE C 373 9235 7872 7576 -397 -103 17 C ATOM 5776 N TYR C 374 -34.139-124.020 -18.639 1.00 27.46 N ANISOU 5776 N TYR C 374 4163 3317 2953 -408 68 -269 N ATOM 5777 CA TYR C 374 -34.398-122.807 -19.399 1.00 21.23 C ANISOU 5777 CA TYR C 374 3389 2502 2174 -477 100 -238 C ATOM 5778 C TYR C 374 -33.115-122.173 -19.870 1.00 15.95 C ANISOU 5778 C TYR C 374 2826 1741 1495 -548 128 -152 C ATOM 5779 O TYR C 374 -32.112-122.223 -19.181 1.00 25.74 O ANISOU 5779 O TYR C 374 4111 2942 2727 -555 142 -151 O ATOM 5780 CB TYR C 374 -35.185-121.817 -18.537 1.00 23.08 C ANISOU 5780 CB TYR C 374 3564 2789 2417 -487 143 -322 C ATOM 5781 CG TYR C 374 -36.624-122.265 -18.310 1.00 22.47 C ANISOU 5781 CG TYR C 374 3386 2826 2325 -416 118 -392 C ATOM 5782 CD1 TYR C 374 -36.983-122.965 -17.168 1.00 19.03 C ANISOU 5782 CD1 TYR C 374 2899 2467 1864 -335 103 -459 C ATOM 5783 CD2 TYR C 374 -37.606-122.004 -19.253 1.00 20.86 C ANISOU 5783 CD2 TYR C 374 3148 2659 2119 -423 112 -382 C ATOM 5784 CE1 TYR C 374 -38.271-123.380 -16.974 1.00 16.26 C ANISOU 5784 CE1 TYR C 374 2476 2224 1477 -265 88 -499 C ATOM 5785 CE2 TYR C 374 -38.906-122.412 -19.072 1.00 16.87 C ANISOU 5785 CE2 TYR C 374 2560 2260 1589 -358 93 -434 C ATOM 5786 CZ TYR C 374 -39.234-123.106 -17.931 1.00 26.83 C ANISOU 5786 CZ TYR C 374 3782 3595 2819 -283 83 -486 C ATOM 5787 OH TYR C 374 -40.526-123.521 -17.746 1.00 30.07 O ANISOU 5787 OH TYR C 374 4122 4105 3197 -234 79 -515 O ATOM 5788 N ALA C 375 -33.137-121.583 -21.057 1.00 15.15 N ANISOU 5788 N ALA C 375 2764 1618 1376 -590 135 -82 N ATOM 5789 CA ALA C 375 -32.020-120.753 -21.474 1.00 11.40 C ANISOU 5789 CA ALA C 375 2317 1124 891 -594 141 -46 C ATOM 5790 C ALA C 375 -31.872-119.575 -20.526 1.00 30.18 C ANISOU 5790 C ALA C 375 4720 3499 3249 -647 212 -84 C ATOM 5791 O ALA C 375 -32.757-119.302 -19.721 1.00 30.99 O ANISOU 5791 O ALA C 375 4783 3625 3365 -668 250 -147 O ATOM 5792 CB ALA C 375 -32.190-120.270 -22.881 1.00 9.45 C ANISOU 5792 CB ALA C 375 2023 897 669 -562 108 -18 C ATOM 5793 N SER C 376 -30.744-118.878 -20.626 1.00 32.75 N ANISOU 5793 N SER C 376 5066 3813 3564 -643 213 -72 N ATOM 5794 CA SER C 376 -30.458-117.803 -19.699 1.00 25.58 C ANISOU 5794 CA SER C 376 4181 2899 2639 -692 277 -107 C ATOM 5795 C SER C 376 -29.430-116.812 -20.248 1.00 36.20 C ANISOU 5795 C SER C 376 5539 4242 3974 -684 269 -89 C ATOM 5796 O SER C 376 -28.844-117.014 -21.325 1.00 17.81 O ANISOU 5796 O SER C 376 3199 1919 1648 -645 216 -53 O ATOM 5797 CB SER C 376 -29.956-118.385 -18.382 1.00 25.45 C ANISOU 5797 CB SER C 376 4209 2856 2604 -718 313 -134 C ATOM 5798 OG SER C 376 -28.796-119.156 -18.628 1.00 31.18 O ANISOU 5798 OG SER C 376 4973 3557 3318 -685 266 -102 O ATOM 5799 N GLY C 377 -29.228-115.731 -19.496 1.00 19.47 N ANISOU 5799 N GLY C 377 3436 2119 1842 -728 325 -119 N ATOM 5800 CA GLY C 377 -28.203-114.765 -19.825 1.00 22.70 C ANISOU 5800 CA GLY C 377 3866 2524 2236 -730 324 -107 C ATOM 5801 C GLY C 377 -28.593-113.759 -20.887 1.00 39.45 C ANISOU 5801 C GLY C 377 5958 4665 4367 -714 311 -92 C ATOM 5802 O GLY C 377 -27.719-113.086 -21.431 1.00 39.75 O ANISOU 5802 O GLY C 377 6009 4703 4392 -707 298 -76 O ATOM 5803 N GLY C 378 -29.894-113.663 -21.179 1.00 42.25 N ANISOU 5803 N GLY C 378 6278 5035 4741 -712 318 -99 N ATOM 5804 CA GLY C 378 -30.420-112.710 -22.144 1.00 20.19 C ANISOU 5804 CA GLY C 378 3463 2253 1955 -700 314 -89 C ATOM 5805 C GLY C 378 -30.162-111.276 -21.733 1.00 36.18 C ANISOU 5805 C GLY C 378 5507 4274 3965 -735 360 -109 C ATOM 5806 O GLY C 378 -30.383-110.906 -20.580 1.00 50.63 O ANISOU 5806 O GLY C 378 7346 6101 5792 -782 415 -148 O ATOM 5807 N THR C 379 -29.675-110.469 -22.675 1.00 44.22 N ANISOU 5807 N THR C 379 6530 5295 4978 -714 339 -86 N ATOM 5808 CA THR C 379 -29.362-109.066 -22.422 1.00 61.57 C ANISOU 5808 CA THR C 379 8749 7487 7159 -744 377 -101 C ATOM 5809 C THR C 379 -30.089-108.162 -23.433 1.00 88.14 C ANISOU 5809 C THR C 379 12102 10859 10530 -729 375 -91 C ATOM 5810 O THR C 379 -30.243-108.526 -24.602 1.00 93.87 O ANISOU 5810 O THR C 379 12803 11481 11380 -727 282 -125 O ATOM 5811 CB THR C 379 -27.837-108.817 -22.482 1.00 63.60 C ANISOU 5811 CB THR C 379 9036 7737 7394 -741 361 -87 C ATOM 5812 OG1 THR C 379 -27.166-109.735 -21.612 1.00 64.15 O ANISOU 5812 OG1 THR C 379 9125 7796 7456 -754 363 -95 O ATOM 5813 CG2 THR C 379 -27.493-107.389 -22.056 1.00 78.06 C ANISOU 5813 CG2 THR C 379 10892 9561 9207 -777 404 -105 C ATOM 5814 N ASP C 380 -30.538-106.992 -22.977 1.00 78.08 N ANISOU 5814 N ASP C 380 10840 9579 9248 -767 425 -118 N ATOM 5815 CA ASP C 380 -31.309-106.070 -23.816 1.00 71.53 C ANISOU 5815 CA ASP C 380 10009 8750 8420 -762 433 -115 C ATOM 5816 C ASP C 380 -30.454-104.962 -24.447 1.00 63.64 C ANISOU 5816 C ASP C 380 9042 7616 7525 -803 371 -167 C ATOM 5817 O ASP C 380 -30.495-104.740 -25.659 1.00 47.49 O ANISOU 5817 O ASP C 380 7017 5558 5470 -790 347 -152 O ATOM 5818 CB ASP C 380 -32.443-105.425 -23.004 1.00 82.95 C ANISOU 5818 CB ASP C 380 11453 10193 9869 -813 498 -159 C ATOM 5819 CG ASP C 380 -33.435-106.440 -22.453 1.00 73.84 C ANISOU 5819 CG ASP C 380 10269 9051 8736 -829 511 -184 C ATOM 5820 OD1 ASP C 380 -33.806-107.377 -23.188 1.00 48.68 O ANISOU 5820 OD1 ASP C 380 7064 5871 5563 -793 469 -161 O ATOM 5821 OD2 ASP C 380 -33.852-106.292 -21.282 1.00 81.11 O ANISOU 5821 OD2 ASP C 380 11179 9978 9661 -878 565 -230 O ATOM 5822 N GLY C 381 -29.699-104.253 -23.617 1.00 62.96 N ANISOU 5822 N GLY C 381 8973 7520 7428 -833 398 -181 N ATOM 5823 CA GLY C 381 -28.875-103.166 -24.104 1.00 74.58 C ANISOU 5823 CA GLY C 381 10492 8968 8878 -851 400 -179 C ATOM 5824 C GLY C 381 -29.686-102.098 -24.810 1.00 73.99 C ANISOU 5824 C GLY C 381 10464 9045 8605 -782 457 -203 C ATOM 5825 O GLY C 381 -29.904-101.011 -24.271 1.00 74.74 O ANISOU 5825 O GLY C 381 10573 9134 8689 -810 504 -226 O TER 5826 GLY C 381 ATOM 5827 N ALA D 102 78.359 -78.782 -27.033 1.00100.71 N ANISOU 5827 N ALA D 102 13065 12694 12506 -330 -701 424 N ATOM 5828 CA ALA D 102 79.173 -77.658 -27.487 1.00 93.80 C ANISOU 5828 CA ALA D 102 12213 11808 11621 -341 -714 425 C ATOM 5829 C ALA D 102 80.646 -78.034 -27.628 1.00 86.86 C ANISOU 5829 C ALA D 102 11315 10942 10744 -290 -682 394 C ATOM 5830 O ALA D 102 81.314 -77.591 -28.561 1.00110.24 O ANISOU 5830 O ALA D 102 14282 13874 13729 -287 -704 388 O ATOM 5831 CB ALA D 102 79.012 -76.461 -26.548 1.00 86.29 C ANISOU 5831 CB ALA D 102 11294 10890 10604 -385 -704 441 C ATOM 5832 N ASN D 103 81.149 -78.852 -26.706 1.00 50.14 N ANISOU 5832 N ASN D 103 6644 6335 6070 -251 -631 377 N ATOM 5833 CA ASN D 103 82.587 -79.134 -26.638 1.00 46.47 C ANISOU 5833 CA ASN D 103 6167 5889 5599 -207 -598 352 C ATOM 5834 C ASN D 103 82.888 -80.605 -26.425 1.00 41.31 C ANISOU 5834 C ASN D 103 5477 5254 4965 -157 -567 333 C ATOM 5835 O ASN D 103 82.306 -81.240 -25.549 1.00 70.84 O ANISOU 5835 O ASN D 103 9205 9026 8687 -150 -544 336 O ATOM 5836 CB ASN D 103 83.232 -78.337 -25.502 1.00 73.18 C ANISOU 5836 CB ASN D 103 9572 9315 8918 -211 -564 352 C ATOM 5837 CG ASN D 103 83.480 -76.893 -25.871 1.00101.46 C ANISOU 5837 CG ASN D 103 13188 12882 12480 -253 -589 362 C ATOM 5838 OD1 ASN D 103 83.871 -76.591 -27.000 1.00111.92 O ANISOU 5838 OD1 ASN D 103 14518 14170 13839 -256 -621 360 O ATOM 5839 ND2 ASN D 103 83.256 -75.987 -24.921 1.00103.25 N ANISOU 5839 ND2 ASN D 103 13440 13139 12651 -289 -576 372 N ATOM 5840 N PRO D 104 83.802 -81.160 -27.229 1.00 26.12 N ANISOU 5840 N PRO D 104 3535 3313 3076 -126 -565 313 N ATOM 5841 CA PRO D 104 84.131 -82.574 -27.046 1.00 23.05 C ANISOU 5841 CA PRO D 104 3110 2945 2702 -84 -535 296 C ATOM 5842 C PRO D 104 84.878 -82.789 -25.739 1.00 33.53 C ANISOU 5842 C PRO D 104 4435 4326 3979 -53 -486 293 C ATOM 5843 O PRO D 104 85.488 -81.854 -25.196 1.00 57.51 O ANISOU 5843 O PRO D 104 7497 7376 6976 -58 -474 298 O ATOM 5844 CB PRO D 104 85.052 -82.880 -28.233 1.00 34.60 C ANISOU 5844 CB PRO D 104 4561 4376 4209 -67 -547 275 C ATOM 5845 CG PRO D 104 84.859 -81.756 -29.192 1.00 34.14 C ANISOU 5845 CG PRO D 104 4530 4272 4172 -101 -593 283 C ATOM 5846 CD PRO D 104 84.520 -80.566 -28.366 1.00 30.88 C ANISOU 5846 CD PRO D 104 4149 3877 3706 -132 -593 305 C ATOM 5847 N SER D 105 84.819 -84.009 -25.226 1.00 13.48 N ANISOU 5847 N SER D 105 1867 1815 1440 -21 -459 286 N ATOM 5848 CA SER D 105 85.604 -84.368 -24.071 1.00 23.31 C ANISOU 5848 CA SER D 105 3108 3104 2645 16 -415 283 C ATOM 5849 C SER D 105 87.015 -84.443 -24.601 1.00 36.99 C ANISOU 5849 C SER D 105 4837 4827 4389 41 -406 272 C ATOM 5850 O SER D 105 87.209 -84.451 -25.808 1.00 40.18 O ANISOU 5850 O SER D 105 5236 5195 4835 31 -432 263 O ATOM 5851 CB SER D 105 85.159 -85.717 -23.524 1.00 31.73 C ANISOU 5851 CB SER D 105 4145 4196 3713 42 -395 276 C ATOM 5852 OG SER D 105 83.776 -85.700 -23.241 1.00 56.58 O ANISOU 5852 OG SER D 105 7293 7346 6857 11 -410 286 O ATOM 5853 N ARG D 106 88.006 -84.480 -23.722 1.00 20.24 N ANISOU 5853 N ARG D 106 2722 2734 2233 73 -371 274 N ATOM 5854 CA ARG D 106 89.366 -84.613 -24.201 1.00 27.02 C ANISOU 5854 CA ARG D 106 3578 3584 3105 93 -362 269 C ATOM 5855 C ARG D 106 90.297 -85.308 -23.189 1.00 31.16 C ANISOU 5855 C ARG D 106 4095 4141 3603 139 -319 274 C ATOM 5856 O ARG D 106 90.109 -85.218 -21.986 1.00 29.53 O ANISOU 5856 O ARG D 106 3914 3942 3365 150 -298 272 O ATOM 5857 CB ARG D 106 89.915 -83.247 -24.626 1.00 19.50 C ANISOU 5857 CB ARG D 106 2662 2604 2143 65 -380 270 C ATOM 5858 CG ARG D 106 91.271 -83.301 -25.313 1.00 26.83 C ANISOU 5858 CG ARG D 106 3595 3510 3090 78 -380 260 C ATOM 5859 CD ARG D 106 91.778 -81.909 -25.576 1.00 29.58 C ANISOU 5859 CD ARG D 106 3986 3834 3417 50 -397 258 C ATOM 5860 NE ARG D 106 90.844 -81.141 -26.388 1.00 17.70 N ANISOU 5860 NE ARG D 106 2492 2302 1931 10 -439 256 N ATOM 5861 CZ ARG D 106 91.049 -79.888 -26.771 1.00 34.45 C ANISOU 5861 CZ ARG D 106 4648 4403 4037 -23 -462 255 C ATOM 5862 NH1 ARG D 106 92.168 -79.267 -26.427 1.00 16.61 N ANISOU 5862 NH1 ARG D 106 2419 2147 1743 -20 -446 252 N ATOM 5863 NH2 ARG D 106 90.141 -79.257 -27.505 1.00 50.23 N ANISOU 5863 NH2 ARG D 106 6652 6377 6055 -59 -502 260 N ATOM 5864 N LEU D 107 91.288 -86.023 -23.703 1.00 31.48 N ANISOU 5864 N LEU D 107 4111 4176 3674 151 -307 272 N ATOM 5865 CA LEU D 107 92.285 -86.676 -22.874 1.00 19.63 C ANISOU 5865 CA LEU D 107 2613 2649 2197 104 -308 296 C ATOM 5866 C LEU D 107 93.616 -86.002 -23.170 1.00 13.14 C ANISOU 5866 C LEU D 107 1813 1823 1355 136 -294 297 C ATOM 5867 O LEU D 107 94.068 -85.993 -24.308 1.00 21.71 O ANISOU 5867 O LEU D 107 2895 2892 2460 152 -304 281 O ATOM 5868 CB LEU D 107 92.362 -88.151 -23.259 1.00 11.14 C ANISOU 5868 CB LEU D 107 1532 1542 1158 123 -320 270 C ATOM 5869 CG LEU D 107 93.141 -89.096 -22.370 1.00 13.38 C ANISOU 5869 CG LEU D 107 1802 1853 1427 168 -280 273 C ATOM 5870 CD1 LEU D 107 92.685 -88.896 -20.972 1.00 19.71 C ANISOU 5870 CD1 LEU D 107 2604 2692 2193 179 -248 284 C ATOM 5871 CD2 LEU D 107 92.922 -90.528 -22.787 1.00 7.26 C ANISOU 5871 CD2 LEU D 107 993 1083 683 173 -283 259 C ATOM 5872 N ILE D 108 94.238 -85.410 -22.164 1.00 40.34 N ANISOU 5872 N ILE D 108 5302 5265 4760 153 -270 298 N ATOM 5873 CA ILE D 108 95.612 -84.942 -22.328 1.00 21.85 C ANISOU 5873 CA ILE D 108 2993 2903 2407 189 -245 287 C ATOM 5874 C ILE D 108 96.448 -85.660 -21.294 1.00 27.89 C ANISOU 5874 C ILE D 108 3751 3679 3166 241 -191 289 C ATOM 5875 O ILE D 108 96.120 -85.609 -20.115 1.00 27.41 O ANISOU 5875 O ILE D 108 3685 3650 3080 253 -163 300 O ATOM 5876 CB ILE D 108 95.721 -83.431 -22.144 1.00 27.86 C ANISOU 5876 CB ILE D 108 3803 3660 3122 174 -243 285 C ATOM 5877 CG1 ILE D 108 94.672 -82.724 -23.010 1.00 30.30 C ANISOU 5877 CG1 ILE D 108 4105 3971 3437 129 -288 283 C ATOM 5878 CG2 ILE D 108 97.124 -82.957 -22.494 1.00 33.79 C ANISOU 5878 CG2 ILE D 108 4601 4375 3864 203 -223 268 C ATOM 5879 CD1 ILE D 108 94.465 -81.277 -22.672 1.00 22.67 C ANISOU 5879 CD1 ILE D 108 3183 3008 2422 98 -290 280 C ATOM 5880 N VAL D 109 97.493 -86.365 -21.733 1.00 44.50 N ANISOU 5880 N VAL D 109 5849 5765 5295 272 -176 282 N ATOM 5881 CA VAL D 109 98.403 -87.071 -20.817 1.00 15.65 C ANISOU 5881 CA VAL D 109 2182 2122 1641 322 -123 292 C ATOM 5882 C VAL D 109 99.677 -86.318 -20.704 1.00 13.84 C ANISOU 5882 C VAL D 109 2000 1864 1393 358 -88 292 C ATOM 5883 O VAL D 109 100.234 -85.896 -21.709 1.00 50.45 O ANISOU 5883 O VAL D 109 6668 6465 6034 350 -105 277 O ATOM 5884 CB VAL D 109 98.761 -88.466 -21.308 1.00 19.63 C ANISOU 5884 CB VAL D 109 2651 2626 2182 328 -125 288 C ATOM 5885 CG1 VAL D 109 99.868 -89.025 -20.459 1.00 23.13 C ANISOU 5885 CG1 VAL D 109 3089 3075 2624 377 -74 302 C ATOM 5886 CG2 VAL D 109 97.524 -89.382 -21.274 1.00 22.70 C ANISOU 5886 CG2 VAL D 109 2997 3042 2586 299 -150 287 C ATOM 5887 N ALA D 110 100.150 -86.144 -19.475 1.00 21.71 N ANISOU 5887 N ALA D 110 3005 2875 2370 400 -37 307 N ATOM 5888 CA ALA D 110 101.381 -85.399 -19.225 1.00 11.87 C ANISOU 5888 CA ALA D 110 1803 1593 1115 429 9 302 C ATOM 5889 C ALA D 110 102.239 -86.083 -18.167 1.00 16.46 C ANISOU 5889 C ALA D 110 2367 2176 1711 487 62 323 C ATOM 5890 O ALA D 110 101.783 -86.990 -17.483 1.00 31.47 O ANISOU 5890 O ALA D 110 4223 4117 3616 506 63 345 O ATOM 5891 CB ALA D 110 101.062 -83.978 -18.819 1.00 14.01 C ANISOU 5891 CB ALA D 110 2104 1863 1356 397 22 280 C ATOM 5892 N ILE D 111 103.497 -85.666 -18.055 1.00 22.07 N ANISOU 5892 N ILE D 111 3106 2841 2439 506 106 309 N ATOM 5893 CA ILE D 111 104.378 -86.214 -17.042 1.00 9.62 C ANISOU 5893 CA ILE D 111 1516 1257 883 563 156 331 C ATOM 5894 C ILE D 111 104.998 -85.109 -16.241 1.00 25.06 C ANISOU 5894 C ILE D 111 3497 3184 2841 573 211 307 C ATOM 5895 O ILE D 111 105.541 -84.161 -16.804 1.00 43.81 O ANISOU 5895 O ILE D 111 5912 5518 5216 545 223 272 O ATOM 5896 CB ILE D 111 105.471 -87.074 -17.657 1.00 20.10 C ANISOU 5896 CB ILE D 111 2849 2550 2239 584 160 343 C ATOM 5897 CG1 ILE D 111 106.378 -87.656 -16.574 1.00 18.01 C ANISOU 5897 CG1 ILE D 111 2571 2274 1997 644 207 375 C ATOM 5898 CG2 ILE D 111 106.288 -86.275 -18.651 1.00 28.84 C ANISOU 5898 CG2 ILE D 111 4002 3602 3354 554 165 305 C ATOM 5899 CD1 ILE D 111 107.379 -88.681 -17.121 1.00 26.85 C ANISOU 5899 CD1 ILE D 111 3683 3373 3144 640 206 380 C ATOM 5900 N GLU D 112 104.892 -85.212 -14.920 1.00 31.38 N ANISOU 5900 N GLU D 112 4272 4008 3644 611 246 321 N ATOM 5901 CA GLU D 112 105.519 -84.258 -14.022 1.00 10.90 C ANISOU 5901 CA GLU D 112 1694 1388 1061 626 306 295 C ATOM 5902 C GLU D 112 106.845 -84.856 -13.593 1.00 30.07 C ANISOU 5902 C GLU D 112 4121 3770 3533 685 346 315 C ATOM 5903 O GLU D 112 106.882 -85.976 -13.090 1.00 22.40 O ANISOU 5903 O GLU D 112 3114 2820 2577 730 341 358 O ATOM 5904 CB GLU D 112 104.630 -84.016 -12.807 1.00 11.15 C ANISOU 5904 CB GLU D 112 1694 1470 1073 633 321 294 C ATOM 5905 CG GLU D 112 104.919 -82.705 -12.109 1.00 35.16 C ANISOU 5905 CG GLU D 112 4754 4494 4112 620 375 249 C ATOM 5906 CD GLU D 112 103.905 -82.361 -11.036 1.00 38.39 C ANISOU 5906 CD GLU D 112 5132 4959 4493 612 386 239 C ATOM 5907 OE1 GLU D 112 104.077 -81.332 -10.353 1.00 39.51 O ANISOU 5907 OE1 GLU D 112 5285 5096 4633 599 434 198 O ATOM 5908 OE2 GLU D 112 102.930 -83.109 -10.870 1.00 33.27 O ANISOU 5908 OE2 GLU D 112 4450 4365 3826 615 351 269 O ATOM 5909 N ILE D 113 107.936 -84.126 -13.821 1.00 27.63 N ANISOU 5909 N ILE D 113 3852 3400 3245 682 385 285 N ATOM 5910 CA ILE D 113 109.249 -84.552 -13.347 1.00 18.87 C ANISOU 5910 CA ILE D 113 2747 2239 2184 736 429 302 C ATOM 5911 C ILE D 113 110.012 -83.457 -12.592 1.00 22.79 C ANISOU 5911 C ILE D 113 3265 2690 2706 748 497 262 C ATOM 5912 O ILE D 113 109.887 -82.277 -12.916 1.00 28.38 O ANISOU 5912 O ILE D 113 4001 3389 3392 699 510 212 O ATOM 5913 CB ILE D 113 110.134 -85.013 -14.487 1.00 21.34 C ANISOU 5913 CB ILE D 113 3091 2508 2509 726 415 309 C ATOM 5914 CG1 ILE D 113 109.354 -85.907 -15.439 1.00 31.06 C ANISOU 5914 CG1 ILE D 113 4305 3782 3715 700 349 332 C ATOM 5915 CG2 ILE D 113 111.368 -85.746 -13.938 1.00 26.55 C ANISOU 5915 CG2 ILE D 113 3750 3121 3215 786 450 344 C ATOM 5916 CD1 ILE D 113 110.119 -86.257 -16.685 1.00 18.13 C ANISOU 5916 CD1 ILE D 113 2696 2108 2086 678 333 327 C ATOM 5917 N VAL D 114 110.795 -83.876 -11.589 1.00 28.59 N ANISOU 5917 N VAL D 114 3982 3394 3486 812 538 284 N ATOM 5918 CA VAL D 114 111.767 -83.035 -10.877 1.00 13.59 C ANISOU 5918 CA VAL D 114 2100 1436 1628 833 608 249 C ATOM 5919 C VAL D 114 113.020 -83.829 -10.559 1.00 51.95 C ANISOU 5919 C VAL D 114 6953 6247 6537 866 617 285 C ATOM 5920 O VAL D 114 112.950 -85.050 -10.407 1.00 49.14 O ANISOU 5920 O VAL D 114 6565 5922 6183 883 578 339 O ATOM 5921 CB VAL D 114 111.271 -82.590 -9.506 1.00 24.72 C ANISOU 5921 CB VAL D 114 3472 2873 3047 858 643 231 C ATOM 5922 CG1 VAL D 114 111.489 -81.105 -9.334 1.00 38.41 C ANISOU 5922 CG1 VAL D 114 5232 4582 4779 819 696 158 C ATOM 5923 CG2 VAL D 114 109.830 -82.966 -9.308 1.00 57.49 C ANISOU 5923 CG2 VAL D 114 7583 7109 7152 843 596 249 C ATOM 5924 N GLU D 115 114.154 -83.129 -10.431 1.00 37.83 N ANISOU 5924 N GLU D 115 5193 4396 4786 858 663 252 N ATOM 5925 CA GLU D 115 115.395 -83.713 -9.907 1.00 19.11 C ANISOU 5925 CA GLU D 115 2814 1982 2466 881 674 280 C ATOM 5926 C GLU D 115 115.310 -83.868 -8.387 1.00 26.75 C ANISOU 5926 C GLU D 115 3732 2961 3471 926 691 292 C ATOM 5927 O GLU D 115 114.995 -82.909 -7.672 1.00 26.22 O ANISOU 5927 O GLU D 115 3655 2894 3414 929 731 246 O ATOM 5928 CB GLU D 115 116.599 -82.831 -10.233 1.00 31.78 C ANISOU 5928 CB GLU D 115 4462 3515 4099 856 719 236 C ATOM 5929 CG GLU D 115 117.118 -82.925 -11.657 1.00 59.63 C ANISOU 5929 CG GLU D 115 8034 7019 7604 815 702 232 C ATOM 5930 CD GLU D 115 118.653 -82.923 -11.728 1.00 83.02 C ANISOU 5930 CD GLU D 115 11020 9915 10607 810 730 230 C ATOM 5931 OE1 GLU D 115 119.306 -83.675 -10.958 1.00 50.80 O ANISOU 5931 OE1 GLU D 115 6917 5818 6565 847 731 270 O ATOM 5932 OE2 GLU D 115 119.208 -82.165 -12.557 1.00100.56 O ANISOU 5932 OE2 GLU D 115 13284 12103 12821 768 751 187 O ATOM 5933 N ASP D 116 115.576 -85.072 -7.886 1.00 40.45 N ANISOU 5933 N ASP D 116 5434 4710 5225 957 662 349 N ATOM 5934 CA ASP D 116 115.687 -85.263 -6.439 1.00 48.39 C ANISOU 5934 CA ASP D 116 6394 5717 6275 1002 676 361 C ATOM 5935 C ASP D 116 116.516 -86.490 -6.072 1.00 57.67 C ANISOU 5935 C ASP D 116 7552 6879 7482 1029 651 419 C ATOM 5936 O ASP D 116 116.834 -87.308 -6.943 1.00 46.91 O ANISOU 5936 O ASP D 116 6207 5520 6098 1009 619 453 O ATOM 5937 CB ASP D 116 114.308 -85.357 -5.788 1.00 33.80 C ANISOU 5937 CB ASP D 116 4501 3942 4399 1016 661 363 C ATOM 5938 CG ASP D 116 114.252 -84.655 -4.446 1.00 41.66 C ANISOU 5938 CG ASP D 116 5462 4930 5435 1046 704 326 C ATOM 5939 OD1 ASP D 116 115.330 -84.450 -3.843 1.00 66.57 O ANISOU 5939 OD1 ASP D 116 8618 8026 8651 1066 733 316 O ATOM 5940 OD2 ASP D 116 113.132 -84.304 -3.992 1.00 44.63 O ANISOU 5940 OD2 ASP D 116 5810 5361 5785 1047 708 304 O ATOM 5941 N GLU D 117 116.879 -86.581 -4.785 1.00 55.45 N ANISOU 5941 N GLU D 117 7235 6581 7253 1072 667 426 N ATOM 5942 CA GLU D 117 117.459 -87.777 -4.176 1.00 18.24 C ANISOU 5942 CA GLU D 117 2494 1865 2569 1104 638 485 C ATOM 5943 C GLU D 117 116.364 -88.837 -3.941 1.00 37.08 C ANISOU 5943 C GLU D 117 4836 4337 4915 1109 589 527 C ATOM 5944 O GLU D 117 115.466 -88.635 -3.127 1.00 39.93 O ANISOU 5944 O GLU D 117 5157 4741 5273 1128 592 514 O ATOM 5945 CB GLU D 117 118.091 -87.422 -2.826 1.00 46.25 C ANISOU 5945 CB GLU D 117 6015 5369 6190 1151 670 472 C ATOM 5946 CG GLU D 117 119.122 -86.297 -2.864 1.00 65.51 C ANISOU 5946 CG GLU D 117 8490 7726 8675 1146 724 421 C ATOM 5947 CD GLU D 117 120.401 -86.686 -3.594 1.00 66.36 C ANISOU 5947 CD GLU D 117 8641 7775 8797 1133 721 447 C ATOM 5948 OE1 GLU D 117 120.965 -87.762 -3.280 1.00 38.21 O ANISOU 5948 OE1 GLU D 117 5062 4202 5253 1159 690 504 O ATOM 5949 OE2 GLU D 117 120.834 -85.923 -4.491 1.00 72.82 O ANISOU 5949 OE2 GLU D 117 9507 8557 9604 1096 748 409 O ATOM 5950 N ILE D 118 116.403 -89.919 -4.665 1.00 43.52 N ANISOU 5950 N ILE D 118 5656 5179 5700 1089 547 571 N ATOM 5951 CA ILE D 118 115.384 -90.900 -4.500 1.00 41.00 C ANISOU 5951 CA ILE D 118 5296 4943 5339 1083 502 606 C ATOM 5952 C ILE D 118 116.043 -92.019 -3.771 1.00 48.41 C ANISOU 5952 C ILE D 118 6206 5885 6303 1109 474 661 C ATOM 5953 O ILE D 118 117.259 -92.065 -3.614 1.00 37.91 O ANISOU 5953 O ILE D 118 4897 4494 5014 1123 482 679 O ATOM 5954 CB ILE D 118 114.862 -91.382 -5.846 1.00 32.26 C ANISOU 5954 CB ILE D 118 4210 3875 4172 1032 471 608 C ATOM 5955 CG1 ILE D 118 115.900 -92.235 -6.543 1.00 37.80 C ANISOU 5955 CG1 ILE D 118 4934 4550 4877 1013 451 639 C ATOM 5956 CG2 ILE D 118 114.640 -90.226 -6.710 1.00 38.80 C ANISOU 5956 CG2 ILE D 118 5078 4683 4981 1007 496 556 C ATOM 5957 CD1 ILE D 118 115.515 -92.643 -7.877 1.00 39.97 C ANISOU 5957 CD1 ILE D 118 5223 4864 5101 963 419 635 C ATOM 5958 N PRO D 119 115.327 -93.105 -3.549 1.00 42.58 N ANISOU 5958 N PRO D 119 5421 5218 5540 1113 442 689 N ATOM 5959 CA PRO D 119 115.967 -94.317 -3.068 1.00 42.83 C ANISOU 5959 CA PRO D 119 5421 5258 5594 1139 415 740 C ATOM 5960 C PRO D 119 116.413 -95.246 -4.192 1.00 66.43 C ANISOU 5960 C PRO D 119 8442 8202 8598 1129 401 775 C ATOM 5961 O PRO D 119 115.785 -95.284 -5.216 1.00 95.13 O ANISOU 5961 O PRO D 119 12087 11769 12289 1163 419 784 O ATOM 5962 CB PRO D 119 114.854 -94.961 -2.278 1.00 52.60 C ANISOU 5962 CB PRO D 119 6618 6589 6778 1118 379 757 C ATOM 5963 CG PRO D 119 114.035 -93.906 -1.900 1.00 59.52 C ANISOU 5963 CG PRO D 119 7484 7495 7636 1117 400 713 C ATOM 5964 CD PRO D 119 113.979 -93.001 -3.018 1.00 55.09 C ANISOU 5964 CD PRO D 119 6976 6878 7079 1100 432 671 C ATOM 5965 N LEU D 120 117.493 -95.991 -4.029 1.00 30.00 N ATOM 5966 CA LEU D 120 117.914 -96.830 -5.161 1.00 30.00 C ATOM 5967 C LEU D 120 117.657 -98.323 -5.053 1.00 30.00 C ATOM 5968 O LEU D 120 118.126 -99.107 -5.875 1.00 30.00 O ATOM 5969 CB LEU D 120 119.354 -96.551 -5.641 1.00 20.00 C ATOM 5970 CG LEU D 120 119.194 -96.470 -7.153 1.00 20.00 C ATOM 5971 CD1 LEU D 120 120.345 -96.890 -7.970 1.00 20.00 C ATOM 5972 CD2 LEU D 120 118.069 -97.377 -7.387 1.00 20.00 C ATOM 5973 N THR D 121 116.918 -98.717 -4.036 1.00 30.00 N ATOM 5974 CA THR D 121 116.563-100.111 -3.887 1.00 30.00 C ATOM 5975 C THR D 121 115.738-100.561 -5.091 1.00 30.00 C ATOM 5976 O THR D 121 116.276-100.751 -6.192 1.00 30.00 O ATOM 5977 CB THR D 121 115.885-100.388 -2.523 1.00 20.00 C ATOM 5978 OG1 THR D 121 114.970-101.469 -2.647 1.00 20.00 O ATOM 5979 CG2 THR D 121 115.157 -99.176 -2.019 1.00 20.00 C ATOM 5980 N LYS D 147 120.869 -92.027 -0.413 1.00 52.41 N ANISOU 5980 N LYS D 147 6709 6100 7103 1285 540 716 N ATOM 5981 CA LYS D 147 120.076 -92.210 -1.621 1.00 43.06 C ANISOU 5981 CA LYS D 147 5545 4974 5841 1230 524 712 C ATOM 5982 C LYS D 147 120.952 -92.226 -2.867 1.00 45.55 C ANISOU 5982 C LYS D 147 5918 5246 6141 1192 529 715 C ATOM 5983 O LYS D 147 121.905 -92.994 -2.957 1.00 59.24 O ANISOU 5983 O LYS D 147 7667 6948 7894 1197 510 759 O ATOM 5984 CB LYS D 147 119.031 -91.102 -1.752 1.00 53.81 C ANISOU 5984 CB LYS D 147 6904 6366 7177 1214 554 651 C ATOM 5985 CG LYS D 147 118.304 -90.741 -0.462 1.00 71.84 C ANISOU 5985 CG LYS D 147 9135 8676 9486 1253 565 630 C ATOM 5986 CD LYS D 147 117.434 -91.879 0.041 1.00 86.49 C ANISOU 5986 CD LYS D 147 10941 10612 11311 1263 519 674 C ATOM 5987 CE LYS D 147 116.509 -91.407 1.156 1.00 93.10 C ANISOU 5987 CE LYS D 147 11726 11486 12161 1291 532 643 C ATOM 5988 NZ LYS D 147 117.255 -90.751 2.270 1.00 94.10 N ANISOU 5988 NZ LYS D 147 11836 11549 12370 1340 566 616 N ATOM 5989 N VAL D 148 120.599 -91.378 -3.829 1.00 55.83 N ANISOU 5989 N VAL D 148 7254 6550 7409 1153 552 668 N ATOM 5990 CA VAL D 148 121.322 -91.204 -5.093 1.00 43.81 C ANISOU 5990 CA VAL D 148 5787 4989 5869 1113 562 657 C ATOM 5991 C VAL D 148 120.595 -90.135 -5.895 1.00 39.59 C ANISOU 5991 C VAL D 148 5277 4470 5297 1077 586 598 C ATOM 5992 O VAL D 148 119.428 -89.847 -5.639 1.00 43.77 O ANISOU 5992 O VAL D 148 5779 5052 5801 1078 582 580 O ATOM 5993 CB VAL D 148 121.371 -92.482 -5.940 1.00 40.48 C ANISOU 5993 CB VAL D 148 5371 4605 5405 1083 515 703 C ATOM 5994 CG1 VAL D 148 120.059 -92.703 -6.629 1.00 44.23 C ANISOU 5994 CG1 VAL D 148 5832 5160 5815 1048 490 691 C ATOM 5995 CG2 VAL D 148 122.479 -92.382 -6.970 1.00 57.36 C ANISOU 5995 CG2 VAL D 148 7564 6685 7544 1053 529 698 C ATOM 5996 N ASP D 149 121.275 -89.537 -6.862 1.00 52.04 N ANISOU 5996 N ASP D 149 6904 5999 6869 1045 611 569 N ATOM 5997 CA ASP D 149 120.674 -88.431 -7.590 1.00 38.83 C ANISOU 5997 CA ASP D 149 5256 4332 5165 1012 634 511 C ATOM 5998 C ASP D 149 120.076 -88.905 -8.897 1.00 53.63 C ANISOU 5998 C ASP D 149 7146 6254 6978 968 599 516 C ATOM 5999 O ASP D 149 120.793 -89.398 -9.774 1.00 48.78 O ANISOU 5999 O ASP D 149 6562 5619 6354 943 588 530 O ATOM 6000 CB ASP D 149 121.685 -87.316 -7.831 1.00 50.00 C ANISOU 6000 CB ASP D 149 6716 5670 6613 999 687 464 C ATOM 6001 CG ASP D 149 121.118 -86.195 -8.660 1.00 65.36 C ANISOU 6001 CG ASP D 149 8690 7622 8522 958 708 405 C ATOM 6002 OD1 ASP D 149 120.286 -85.417 -8.139 1.00 93.04 O ANISOU 6002 OD1 ASP D 149 12177 11149 12024 964 725 370 O ATOM 6003 OD2 ASP D 149 121.511 -86.085 -9.839 1.00 56.88 O ANISOU 6003 OD2 ASP D 149 7658 6532 7423 918 708 391 O ATOM 6004 N GLY D 150 118.752 -88.757 -8.993 1.00 64.51 N ANISOU 6004 N GLY D 150 8502 7693 8315 959 581 504 N ATOM 6005 CA GLY D 150 117.963 -89.169 -10.142 1.00 52.25 C ANISOU 6005 CA GLY D 150 6956 6191 6707 920 544 504 C ATOM 6006 C GLY D 150 116.707 -88.320 -10.317 1.00 37.65 C ANISOU 6006 C GLY D 150 5103 4377 4824 908 546 467 C ATOM 6007 O GLY D 150 116.768 -87.095 -10.279 1.00 55.00 O ANISOU 6007 O GLY D 150 7326 6541 7032 904 585 421 O ATOM 6008 N LEU D 151 115.558 -88.966 -10.475 1.00 36.36 N ANISOU 6008 N LEU D 151 4908 4285 4622 899 504 485 N ATOM 6009 CA LEU D 151 114.335 -88.260 -10.852 1.00 34.36 C ANISOU 6009 CA LEU D 151 4656 4067 4330 883 498 454 C ATOM 6010 C LEU D 151 113.081 -88.719 -10.115 1.00 26.30 C ANISOU 6010 C LEU D 151 3584 3121 3288 899 473 474 C ATOM 6011 O LEU D 151 112.907 -89.906 -9.857 1.00 33.46 O ANISOU 6011 O LEU D 151 4454 4070 4189 901 440 512 O ATOM 6012 CB LEU D 151 114.107 -88.413 -12.356 1.00 25.92 C ANISOU 6012 CB LEU D 151 3615 3008 3226 838 466 442 C ATOM 6013 CG LEU D 151 115.093 -87.677 -13.262 1.00 31.22 C ANISOU 6013 CG LEU D 151 4342 3612 3908 814 493 408 C ATOM 6014 CD1 LEU D 151 114.824 -88.038 -14.680 1.00 41.34 C ANISOU 6014 CD1 LEU D 151 5641 4909 5158 773 454 401 C ATOM 6015 CD2 LEU D 151 114.964 -86.173 -13.070 1.00 35.42 C ANISOU 6015 CD2 LEU D 151 4903 4110 4445 815 536 359 C ATOM 6016 N LYS D 152 112.209 -87.763 -9.796 1.00 37.08 N ANISOU 6016 N LYS D 152 4947 4501 4639 906 490 445 N ATOM 6017 CA LYS D 152 110.877 -88.023 -9.235 1.00 23.44 C ANISOU 6017 CA LYS D 152 3176 2846 2883 915 468 456 C ATOM 6018 C LYS D 152 109.843 -87.739 -10.322 1.00 32.46 C ANISOU 6018 C LYS D 152 4334 4020 3977 881 437 440 C ATOM 6019 O LYS D 152 109.743 -86.620 -10.801 1.00 38.83 O ANISOU 6019 O LYS D 152 5180 4798 4776 873 459 402 O ATOM 6020 CB LYS D 152 110.596 -87.078 -8.071 1.00 45.52 C ANISOU 6020 CB LYS D 152 5958 5641 5698 948 512 428 C ATOM 6021 CG LYS D 152 110.518 -87.720 -6.690 1.00 65.59 C ANISOU 6021 CG LYS D 152 8445 8212 8263 985 513 455 C ATOM 6022 CD LYS D 152 110.297 -86.650 -5.607 1.00 69.00 C ANISOU 6022 CD LYS D 152 8862 8638 8718 1010 561 413 C ATOM 6023 CE LYS D 152 110.124 -87.258 -4.216 1.00 81.93 C ANISOU 6023 CE LYS D 152 10441 10309 10381 1047 559 435 C ATOM 6024 NZ LYS D 152 111.375 -87.871 -3.678 1.00 83.09 N ANISOU 6024 NZ LYS D 152 10582 10406 10583 1074 562 463 N ATOM 6025 N ALA D 153 109.064 -88.745 -10.702 1.00 33.41 N ANISOU 6025 N ALA D 153 4425 4201 4068 857 388 464 N ATOM 6026 CA ALA D 153 108.134 -88.583 -11.800 1.00 15.85 C ANISOU 6026 CA ALA D 153 2213 2003 1806 818 350 450 C ATOM 6027 C ALA D 153 106.747 -89.032 -11.432 1.00 44.63 C ANISOU 6027 C ALA D 153 5813 5726 5419 809 319 462 C ATOM 6028 O ALA D 153 106.586 -89.902 -10.581 1.00 38.54 O ANISOU 6028 O ALA D 153 4997 4994 4653 822 316 485 O ATOM 6029 CB ALA D 153 108.602 -89.348 -13.003 1.00 18.51 C ANISOU 6029 CB ALA D 153 2561 2329 2142 777 317 451 C ATOM 6030 N ARG D 154 105.752 -88.433 -12.093 1.00 44.75 N ANISOU 6030 N ARG D 154 5843 5760 5399 783 293 446 N ATOM 6031 CA ARG D 154 104.383 -88.900 -11.993 1.00 19.49 C ANISOU 6031 CA ARG D 154 2604 2633 2169 755 255 451 C ATOM 6032 C ARG D 154 103.509 -88.556 -13.204 1.00 21.61 C ANISOU 6032 C ARG D 154 2892 2911 2408 695 209 429 C ATOM 6033 O ARG D 154 103.537 -87.456 -13.723 1.00 32.78 O ANISOU 6033 O ARG D 154 4349 4294 3810 667 211 400 O ATOM 6034 CB ARG D 154 103.753 -88.396 -10.706 1.00 15.15 C ANISOU 6034 CB ARG D 154 2030 2120 1606 787 282 453 C ATOM 6035 CG ARG D 154 103.442 -86.941 -10.707 1.00 20.10 C ANISOU 6035 CG ARG D 154 2690 2733 2215 745 301 401 C ATOM 6036 CD ARG D 154 102.745 -86.596 -9.429 1.00 33.81 C ANISOU 6036 CD ARG D 154 4392 4515 3938 756 326 390 C ATOM 6037 NE ARG D 154 102.648 -85.161 -9.248 1.00 38.31 N ANISOU 6037 NE ARG D 154 4992 5069 4493 718 356 339 N ATOM 6038 CZ ARG D 154 102.324 -84.582 -8.104 1.00 35.09 C ANISOU 6038 CZ ARG D 154 4564 4689 4080 724 394 314 C ATOM 6039 NH1 ARG D 154 102.085 -85.329 -7.032 1.00 36.86 N ANISOU 6039 NH1 ARG D 154 473