HEADER VIRAL PROTEIN 30-DEC-08 3FOH TITLE FITTING OF GP18M CRYSTAL STRUCTURE INTO 3D CRYO-EM RECONSTRUCTION OF TITLE 2 BACTERIOPHAGE T4 EXTENDED TAIL COMPND MOL_ID: 1; COMPND 2 MOLECULE: TAIL SHEATH PROTEIN GP18; COMPND 3 CHAIN: A, B, C, D, E, F; COMPND 4 FRAGMENT: DELETION MUTANT GP18M: UNP RESIDUES 1-510; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE T4; SOURCE 3 ORGANISM_COMMON: BACTERIOPHAGE T4; SOURCE 4 ORGANISM_TAXID: 10665; SOURCE 5 GENE: 18, GB AAA32541; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22 KEYWDS ALPHA-BETA, VIRAL STRUCTURAL PROTEIN, BACTERIOPHAGE T4, TAIL SHEATH, KEYWDS 2 VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR A.A.AKSYUK,P.G.LEIMAN,L.P.KUROCHKINA,M.M.SHNEIDER,V.A.KOSTYUCHENKO, AUTHOR 2 V.V.MESYANZHINOV,M.G.ROSSMANN REVDAT 3 30-MAY-12 3FOH 1 REMARK VERSN REVDAT 2 21-APR-09 3FOH 1 JRNL REVDAT 1 10-MAR-09 3FOH 0 JRNL AUTH A.A.AKSYUK,P.G.LEIMAN,L.P.KUROCHKINA,M.M.SHNEIDER, JRNL AUTH 2 V.A.KOSTYUCHENKO,V.V.MESYANZHINOV,M.G.ROSSMANN JRNL TITL THE TAIL SHEATH STRUCTURE OF BACTERIOPHAGE T4: A MOLECULAR JRNL TITL 2 MACHINE FOR INFECTING BACTERIA. JRNL REF EMBO J. V. 28 821 2009 JRNL REFN ISSN 0261-4189 JRNL PMID 19229296 JRNL DOI 10.1038/EMBOJ.2009.36 REMARK 2 REMARK 2 RESOLUTION. 15.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : SITUS FROM COLORES REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 3FOA REMARK 3 REFINEMENT SPACE : NULL 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) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 15.000 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: NULL REMARK 4 REMARK 4 3FOH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-09. REMARK 100 THE RCSB ID CODE IS RCSB050843. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : NULL REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : NULL REMARK 245 PARTICLE TYPE : NULL REMARK 245 NAME OF SAMPLE : NULL REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL 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 : NULL 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 : NULL REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : NULL REMARK 245 ILLUMINATION MODE : NULL REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : NULL REMARK 245 ACCELERATION VOLTAGE (KV) : NULL 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 MET A 1 REMARK 465 THR A 2 REMARK 465 LEU A 3 REMARK 465 LEU A 4 REMARK 465 SER A 5 REMARK 465 PRO A 6 REMARK 465 GLY A 7 REMARK 465 ILE A 8 REMARK 465 GLU A 9 REMARK 465 LEU A 10 REMARK 465 LYS A 11 REMARK 465 GLU A 12 REMARK 465 THR A 13 REMARK 465 THR A 14 REMARK 465 VAL A 15 REMARK 465 GLN A 16 REMARK 465 SER A 17 REMARK 465 THR A 18 REMARK 465 VAL A 19 REMARK 465 VAL A 20 REMARK 465 SER A 485 REMARK 465 GLN A 486 REMARK 465 THR A 487 REMARK 465 TRP A 488 REMARK 465 MET A 489 REMARK 465 SER A 490 REMARK 465 PRO A 491 REMARK 465 ALA A 492 REMARK 465 GLY A 493 REMARK 465 TYR A 494 REMARK 465 ASN A 495 REMARK 465 MET B 1 REMARK 465 THR B 2 REMARK 465 LEU B 3 REMARK 465 LEU B 4 REMARK 465 SER B 5 REMARK 465 PRO B 6 REMARK 465 GLY B 7 REMARK 465 ILE B 8 REMARK 465 GLU B 9 REMARK 465 LEU B 10 REMARK 465 LYS B 11 REMARK 465 GLU B 12 REMARK 465 THR B 13 REMARK 465 THR B 14 REMARK 465 VAL B 15 REMARK 465 GLN B 16 REMARK 465 SER B 17 REMARK 465 THR B 18 REMARK 465 VAL B 19 REMARK 465 VAL B 20 REMARK 465 SER B 485 REMARK 465 GLN B 486 REMARK 465 THR B 487 REMARK 465 TRP B 488 REMARK 465 MET B 489 REMARK 465 SER B 490 REMARK 465 PRO B 491 REMARK 465 ALA B 492 REMARK 465 GLY B 493 REMARK 465 TYR B 494 REMARK 465 ASN B 495 REMARK 465 MET C 1 REMARK 465 THR C 2 REMARK 465 LEU C 3 REMARK 465 LEU C 4 REMARK 465 SER C 5 REMARK 465 PRO C 6 REMARK 465 GLY C 7 REMARK 465 ILE C 8 REMARK 465 GLU C 9 REMARK 465 LEU C 10 REMARK 465 LYS C 11 REMARK 465 GLU C 12 REMARK 465 THR C 13 REMARK 465 THR C 14 REMARK 465 VAL C 15 REMARK 465 GLN C 16 REMARK 465 SER C 17 REMARK 465 THR C 18 REMARK 465 VAL C 19 REMARK 465 VAL C 20 REMARK 465 SER C 485 REMARK 465 GLN C 486 REMARK 465 THR C 487 REMARK 465 TRP C 488 REMARK 465 MET C 489 REMARK 465 SER C 490 REMARK 465 PRO C 491 REMARK 465 ALA C 492 REMARK 465 GLY C 493 REMARK 465 TYR C 494 REMARK 465 ASN C 495 REMARK 465 MET D 1 REMARK 465 THR D 2 REMARK 465 LEU D 3 REMARK 465 LEU D 4 REMARK 465 SER D 5 REMARK 465 PRO D 6 REMARK 465 GLY D 7 REMARK 465 ILE D 8 REMARK 465 GLU D 9 REMARK 465 LEU D 10 REMARK 465 LYS D 11 REMARK 465 GLU D 12 REMARK 465 THR D 13 REMARK 465 THR D 14 REMARK 465 VAL D 15 REMARK 465 GLN D 16 REMARK 465 SER D 17 REMARK 465 THR D 18 REMARK 465 VAL D 19 REMARK 465 VAL D 20 REMARK 465 SER D 485 REMARK 465 GLN D 486 REMARK 465 THR D 487 REMARK 465 TRP D 488 REMARK 465 MET D 489 REMARK 465 SER D 490 REMARK 465 PRO D 491 REMARK 465 ALA D 492 REMARK 465 GLY D 493 REMARK 465 TYR D 494 REMARK 465 ASN D 495 REMARK 465 MET E 1 REMARK 465 THR E 2 REMARK 465 LEU E 3 REMARK 465 LEU E 4 REMARK 465 SER E 5 REMARK 465 PRO E 6 REMARK 465 GLY E 7 REMARK 465 ILE E 8 REMARK 465 GLU E 9 REMARK 465 LEU E 10 REMARK 465 LYS E 11 REMARK 465 GLU E 12 REMARK 465 THR E 13 REMARK 465 THR E 14 REMARK 465 VAL E 15 REMARK 465 GLN E 16 REMARK 465 SER E 17 REMARK 465 THR E 18 REMARK 465 VAL E 19 REMARK 465 VAL E 20 REMARK 465 SER E 485 REMARK 465 GLN E 486 REMARK 465 THR E 487 REMARK 465 TRP E 488 REMARK 465 MET E 489 REMARK 465 SER E 490 REMARK 465 PRO E 491 REMARK 465 ALA E 492 REMARK 465 GLY E 493 REMARK 465 TYR E 494 REMARK 465 ASN E 495 REMARK 465 MET F 1 REMARK 465 THR F 2 REMARK 465 LEU F 3 REMARK 465 LEU F 4 REMARK 465 SER F 5 REMARK 465 PRO F 6 REMARK 465 GLY F 7 REMARK 465 ILE F 8 REMARK 465 GLU F 9 REMARK 465 LEU F 10 REMARK 465 LYS F 11 REMARK 465 GLU F 12 REMARK 465 THR F 13 REMARK 465 THR F 14 REMARK 465 VAL F 15 REMARK 465 GLN F 16 REMARK 465 SER F 17 REMARK 465 THR F 18 REMARK 465 VAL F 19 REMARK 465 VAL F 20 REMARK 465 SER F 485 REMARK 465 GLN F 486 REMARK 465 THR F 487 REMARK 465 TRP F 488 REMARK 465 MET F 489 REMARK 465 SER F 490 REMARK 465 PRO F 491 REMARK 465 ALA F 492 REMARK 465 GLY F 493 REMARK 465 TYR F 494 REMARK 465 ASN F 495 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 CG2 THR B 351 OD2 ASP B 354 1.13 REMARK 500 CG2 THR C 351 OD2 ASP C 354 1.13 REMARK 500 CG2 THR F 351 OD2 ASP F 354 1.13 REMARK 500 CG2 THR A 351 OD2 ASP A 354 1.13 REMARK 500 CG2 THR D 351 OD2 ASP D 354 1.13 REMARK 500 CG2 THR E 351 OD2 ASP E 354 1.13 REMARK 500 O PRO E 409 CE1 TYR E 454 1.65 REMARK 500 O PRO C 409 CE1 TYR C 454 1.65 REMARK 500 O PRO F 409 CE1 TYR F 454 1.65 REMARK 500 O PRO D 409 CE1 TYR D 454 1.65 REMARK 500 O PRO A 409 CE1 TYR A 454 1.65 REMARK 500 O PRO B 409 CE1 TYR B 454 1.65 REMARK 500 CD PRO B 409 O ASP B 451 1.75 REMARK 500 CD PRO E 409 O ASP E 451 1.75 REMARK 500 CD PRO D 409 O ASP D 451 1.75 REMARK 500 CD PRO A 409 O ASP A 451 1.75 REMARK 500 CD PRO C 409 O ASP C 451 1.75 REMARK 500 CD PRO F 409 O ASP F 451 1.75 REMARK 500 CB ALA B 379 OH TYR B 454 1.84 REMARK 500 CB ALA C 379 OH TYR C 454 1.84 REMARK 500 CB ALA F 379 OH TYR F 454 1.84 REMARK 500 CB ALA D 379 OH TYR D 454 1.84 REMARK 500 CB ALA A 379 OH TYR A 454 1.84 REMARK 500 CB ALA E 379 OH TYR E 454 1.84 REMARK 500 O THR B 24 OE1 GLN B 371 2.04 REMARK 500 O THR D 24 OE1 GLN D 371 2.04 REMARK 500 O THR E 24 OE1 GLN E 371 2.04 REMARK 500 O THR F 24 OE1 GLN F 371 2.04 REMARK 500 O THR A 24 OE1 GLN A 371 2.04 REMARK 500 O THR C 24 OE1 GLN C 371 2.04 REMARK 500 O VAL A 112 O ILE A 131 2.04 REMARK 500 O VAL E 112 O ILE E 131 2.04 REMARK 500 O VAL C 112 O ILE C 131 2.04 REMARK 500 O VAL B 112 O ILE B 131 2.04 REMARK 500 O VAL D 112 O ILE D 131 2.04 REMARK 500 O VAL F 112 O ILE F 131 2.04 REMARK 500 O PRO D 409 CZ TYR D 454 2.06 REMARK 500 O PRO E 409 CZ TYR E 454 2.06 REMARK 500 O PRO B 409 CZ TYR B 454 2.06 REMARK 500 O PRO C 409 CZ TYR C 454 2.06 REMARK 500 O PRO F 409 CZ TYR F 454 2.06 REMARK 500 O PRO A 409 CZ TYR A 454 2.06 REMARK 500 O PRO A 409 OH TYR A 454 2.06 REMARK 500 O PRO F 409 OH TYR F 454 2.06 REMARK 500 O PRO B 409 OH TYR B 454 2.06 REMARK 500 O PRO D 409 OH TYR D 454 2.06 REMARK 500 O PRO E 409 OH TYR E 454 2.06 REMARK 500 O PRO C 409 OH TYR C 454 2.06 REMARK 500 OG SER D 23 CB ASN D 483 2.19 REMARK 500 OG SER C 23 CB ASN C 483 2.19 REMARK 500 REMARK 500 THIS ENTRY HAS 54 CLOSE CONTACTS 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 GLY A 55 N - CA - C ANGL. DEV. = 45.0 DEGREES REMARK 500 GLN A 56 N - CA - CB ANGL. DEV. = -20.5 DEGREES REMARK 500 ASP A 85 N - CA - C ANGL. DEV. = -17.7 DEGREES REMARK 500 ALA A 111 CB - CA - C ANGL. DEV. = 14.3 DEGREES REMARK 500 VAL A 112 CB - CA - C ANGL. DEV. = -14.5 DEGREES REMARK 500 VAL A 112 N - CA - C ANGL. DEV. = 25.7 DEGREES REMARK 500 GLU A 366 CB - CA - C ANGL. DEV. = 14.8 DEGREES REMARK 500 SER A 367 N - CA - CB ANGL. DEV. = -16.0 DEGREES REMARK 500 LEU A 404 CB - CA - C ANGL. DEV. = 13.0 DEGREES REMARK 500 LEU A 404 N - CA - C ANGL. DEV. = -20.4 DEGREES REMARK 500 VAL A 405 N - CA - C ANGL. DEV. = -25.9 DEGREES REMARK 500 LEU A 406 CB - CA - C ANGL. DEV. = 11.7 DEGREES REMARK 500 CYS A 407 CB - CA - C ANGL. DEV. = -19.0 DEGREES REMARK 500 SER A 408 N - CA - CB ANGL. DEV. = -13.3 DEGREES REMARK 500 ALA A 449 CB - CA - C ANGL. DEV. = 10.1 DEGREES REMARK 500 GLY B 55 N - CA - C ANGL. DEV. = 45.0 DEGREES REMARK 500 GLN B 56 N - CA - CB ANGL. DEV. = -20.4 DEGREES REMARK 500 ASP B 85 N - CA - C ANGL. DEV. = -17.6 DEGREES REMARK 500 ALA B 111 CB - CA - C ANGL. DEV. = 14.4 DEGREES REMARK 500 VAL B 112 CB - CA - C ANGL. DEV. = -14.5 DEGREES REMARK 500 VAL B 112 N - CA - C ANGL. DEV. = 25.7 DEGREES REMARK 500 GLU B 366 CB - CA - C ANGL. DEV. = 14.8 DEGREES REMARK 500 SER B 367 N - CA - CB ANGL. DEV. = -15.9 DEGREES REMARK 500 LEU B 404 CB - CA - C ANGL. DEV. = 13.0 DEGREES REMARK 500 LEU B 404 N - CA - C ANGL. DEV. = -20.3 DEGREES REMARK 500 VAL B 405 N - CA - C ANGL. DEV. = -25.9 DEGREES REMARK 500 LEU B 406 CB - CA - C ANGL. DEV. = 11.7 DEGREES REMARK 500 CYS B 407 CB - CA - C ANGL. DEV. = -19.0 DEGREES REMARK 500 SER B 408 N - CA - CB ANGL. DEV. = -13.3 DEGREES REMARK 500 ALA B 449 CB - CA - C ANGL. DEV. = 10.0 DEGREES REMARK 500 GLY C 55 N - CA - C ANGL. DEV. = 45.0 DEGREES REMARK 500 GLN C 56 N - CA - CB ANGL. DEV. = -20.4 DEGREES REMARK 500 ASP C 85 N - CA - C ANGL. DEV. = -17.6 DEGREES REMARK 500 ALA C 111 CB - CA - C ANGL. DEV. = 14.3 DEGREES REMARK 500 VAL C 112 CB - CA - C ANGL. DEV. = -14.4 DEGREES REMARK 500 VAL C 112 N - CA - C ANGL. DEV. = 25.7 DEGREES REMARK 500 GLU C 366 CB - CA - C ANGL. DEV. = 14.9 DEGREES REMARK 500 SER C 367 N - CA - CB ANGL. DEV. = -15.9 DEGREES REMARK 500 LEU C 404 CB - CA - C ANGL. DEV. = 13.0 DEGREES REMARK 500 LEU C 404 N - CA - C ANGL. DEV. = -20.3 DEGREES REMARK 500 VAL C 405 N - CA - C ANGL. DEV. = -25.9 DEGREES REMARK 500 LEU C 406 CB - CA - C ANGL. DEV. = 11.7 DEGREES REMARK 500 CYS C 407 CB - CA - C ANGL. DEV. = -19.0 DEGREES REMARK 500 SER C 408 N - CA - CB ANGL. DEV. = -13.3 DEGREES REMARK 500 ALA C 449 CB - CA - C ANGL. DEV. = 10.1 DEGREES REMARK 500 GLY D 55 N - CA - C ANGL. DEV. = 45.0 DEGREES REMARK 500 GLN D 56 N - CA - CB ANGL. DEV. = -20.4 DEGREES REMARK 500 ASP D 85 N - CA - C ANGL. DEV. = -17.6 DEGREES REMARK 500 ALA D 111 CB - CA - C ANGL. DEV. = 14.4 DEGREES REMARK 500 VAL D 112 CB - CA - C ANGL. DEV. = -14.5 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 90 ANGLE DEVIATIONS. 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 ASN A 22 30.35 77.58 REMARK 500 SER A 23 36.67 82.07 REMARK 500 VAL A 48 -8.27 -59.27 REMARK 500 PHE A 54 35.84 -140.18 REMARK 500 ALA A 62 -70.65 -19.80 REMARK 500 LEU A 72 -4.88 -55.24 REMARK 500 ASN A 76 -69.87 -93.75 REMARK 500 THR A 88 12.25 -141.80 REMARK 500 ALA A 96 27.06 -78.22 REMARK 500 ASN A 98 -172.48 -51.24 REMARK 500 GLU A 100 140.66 -39.14 REMARK 500 ILE A 103 81.28 -68.75 REMARK 500 VAL A 121 73.71 53.71 REMARK 500 LYS A 130 129.38 -171.83 REMARK 500 ASP A 135 -150.78 -99.75 REMARK 500 GLU A 159 52.18 -90.04 REMARK 500 THR A 162 -70.66 -36.65 REMARK 500 LEU A 163 -151.40 63.34 REMARK 500 SER A 173 73.36 -115.71 REMARK 500 LEU A 178 -163.24 -115.24 REMARK 500 ALA A 179 -6.56 74.49 REMARK 500 ALA A 196 -99.91 -116.97 REMARK 500 ALA A 201 -101.75 -14.68 REMARK 500 ALA A 242 -71.53 -69.60 REMARK 500 ALA A 250 115.58 -38.13 REMARK 500 THR A 264 -7.54 -141.87 REMARK 500 VAL A 268 -27.35 -145.02 REMARK 500 TYR A 271 99.28 -60.89 REMARK 500 GLN A 274 -75.66 -83.01 REMARK 500 ASP A 287 -6.66 72.72 REMARK 500 ASP A 303 -168.11 -79.42 REMARK 500 ILE A 304 22.97 -75.05 REMARK 500 ASN A 308 103.08 -54.05 REMARK 500 ASN A 329 15.90 59.73 REMARK 500 LEU A 344 94.13 -160.82 REMARK 500 ALA A 348 -65.65 -19.30 REMARK 500 ALA A 363 33.11 -83.02 REMARK 500 GLU A 381 171.95 -58.66 REMARK 500 GLU A 384 -72.22 -41.99 REMARK 500 CYS A 403 -160.88 171.04 REMARK 500 THR A 431 -69.82 -127.36 REMARK 500 ALA A 432 -76.47 166.80 REMARK 500 ALA A 433 -117.88 44.04 REMARK 500 SER A 444 77.30 -150.92 REMARK 500 ASN A 453 -146.57 -133.74 REMARK 500 ARG A 480 -107.88 -74.33 REMARK 500 THR A 481 128.13 -39.43 REMARK 500 ASP A 482 -153.80 41.91 REMARK 500 GLN A 498 151.01 -45.71 REMARK 500 LYS A 504 137.85 165.94 REMARK 500 REMARK 500 THIS ENTRY HAS 301 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ASN A 21 ASN A 22 -141.58 REMARK 500 ILE A 450 ASP A 451 -142.60 REMARK 500 ASP A 451 GLY A 452 -113.25 REMARK 500 GLY A 452 ASN A 453 147.04 REMARK 500 ASN B 21 ASN B 22 -141.57 REMARK 500 ILE B 450 ASP B 451 -142.70 REMARK 500 ASP B 451 GLY B 452 -113.18 REMARK 500 GLY B 452 ASN B 453 147.08 REMARK 500 ASN C 21 ASN C 22 -141.54 REMARK 500 ILE C 450 ASP C 451 -142.70 REMARK 500 ASP C 451 GLY C 452 -113.20 REMARK 500 GLY C 452 ASN C 453 147.06 REMARK 500 ASN D 21 ASN D 22 -141.56 REMARK 500 ILE D 450 ASP D 451 -142.65 REMARK 500 ASP D 451 GLY D 452 -113.13 REMARK 500 GLY D 452 ASN D 453 147.07 REMARK 500 ASN E 21 ASN E 22 -141.56 REMARK 500 ILE E 450 ASP E 451 -142.62 REMARK 500 ASP E 451 GLY E 452 -113.19 REMARK 500 GLY E 452 ASN E 453 147.07 REMARK 500 ASN F 21 ASN F 22 -141.56 REMARK 500 ILE F 450 ASP F 451 -142.69 REMARK 500 ASP F 451 GLY F 452 -113.18 REMARK 500 GLY F 452 ASN F 453 147.06 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 GLN A 56 49.0 L L OUTSIDE RANGE REMARK 500 VAL A 112 17.5 L L OUTSIDE RANGE REMARK 500 ALA A 179 24.2 L L OUTSIDE RANGE REMARK 500 LEU A 404 46.5 L L OUTSIDE RANGE REMARK 500 GLN B 56 48.9 L L OUTSIDE RANGE REMARK 500 VAL B 112 17.5 L L OUTSIDE RANGE REMARK 500 ALA B 179 24.2 L L OUTSIDE RANGE REMARK 500 LEU B 404 46.5 L L OUTSIDE RANGE REMARK 500 GLN C 56 49.0 L L OUTSIDE RANGE REMARK 500 VAL C 112 17.5 L L OUTSIDE RANGE REMARK 500 ALA C 179 24.2 L L OUTSIDE RANGE REMARK 500 LEU C 404 46.5 L L OUTSIDE RANGE REMARK 500 GLN D 56 48.9 L L OUTSIDE RANGE REMARK 500 VAL D 112 17.5 L L OUTSIDE RANGE REMARK 500 ALA D 179 24.3 L L OUTSIDE RANGE REMARK 500 LEU D 404 46.5 L L OUTSIDE RANGE REMARK 500 GLN E 56 48.9 L L OUTSIDE RANGE REMARK 500 VAL E 112 17.5 L L OUTSIDE RANGE REMARK 500 ALA E 179 24.3 L L OUTSIDE RANGE REMARK 500 LEU E 404 46.5 L L OUTSIDE RANGE REMARK 500 GLN F 56 48.9 L L OUTSIDE RANGE REMARK 500 VAL F 112 17.5 L L OUTSIDE RANGE REMARK 500 ALA F 179 24.3 L L OUTSIDE RANGE REMARK 500 LEU F 404 46.5 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3FOA RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 TAIL SHEATH PROTEIN, REMARK 900 GP18M, THAT WAS USED FOR THE FITTING REMARK 900 RELATED ID: 3FO8 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE PROTEASE RESISTANT FRAGMENT OF REMARK 900 BACTERIOPHAGE T4 TAIL SHEATH PROTEIN, GP18PR REMARK 900 RELATED ID: EMD-1126 RELATED DB: EMDB REMARK 900 3D CRYO-EM MAP OF THE BACTERIOPHAGE T4 TAIL IN THE EXTENDED REMARK 900 CONFORMATION THAT WAS USED FOR THE FITTING REMARK 900 RELATED ID: 3FOI RELATED DB: PDB REMARK 900 FITTING OF GP18M CRYSTAL STRUCTURE INTO 3D CRYO-EM REMARK 900 RECONSTRUCTION OF CONTRACTED CONFORMATION OF BACTERIOPHAGE REMARK 900 T4 TAIL SHEATH PROTEIN REMARK 999 REMARK 999 SEQUENCE REMARK 999 AUTHORS STATE THAT THE SEQUENCE COMPLETELY AGREES WITH REMARK 999 THE GENBANK ENTRY AAA32541, PUBMED REPORT 2964531. REMARK 999 THE SEQUENCE DIFFERENCES MAY REFLECT THE SEQUENCE REMARK 999 VARIATION BETWEEN THE VIRUS STRAINS. DBREF 3FOH A 1 510 UNP P13332 VG18_BPT4 1 510 DBREF 3FOH B 1 510 UNP P13332 VG18_BPT4 1 510 DBREF 3FOH C 1 510 UNP P13332 VG18_BPT4 1 510 DBREF 3FOH D 1 510 UNP P13332 VG18_BPT4 1 510 DBREF 3FOH E 1 510 UNP P13332 VG18_BPT4 1 510 DBREF 3FOH F 1 510 UNP P13332 VG18_BPT4 1 510 SEQADV 3FOH GLU A 100 UNP P13332 ASP 100 SEE REMARK 999 SEQADV 3FOH ALA A 148 UNP P13332 GLY 148 SEE REMARK 999 SEQADV 3FOH ILE A 150 UNP P13332 ASN 150 SEE REMARK 999 SEQADV 3FOH ILE A 151 UNP P13332 TYR 151 SEE REMARK 999 SEQADV 3FOH GLY A 301 UNP P13332 GLU 301 SEE REMARK 999 SEQADV 3FOH VAL A 399 UNP P13332 ALA 399 SEE REMARK 999 SEQADV 3FOH TYR A 454 UNP P13332 HIS 454 SEE REMARK 999 SEQADV 3FOH PRO A 510 UNP P13332 ARG 510 ENGINEERED SEQADV 3FOH GLU B 100 UNP P13332 ASP 100 SEE REMARK 999 SEQADV 3FOH ALA B 148 UNP P13332 GLY 148 SEE REMARK 999 SEQADV 3FOH ILE B 150 UNP P13332 ASN 150 SEE REMARK 999 SEQADV 3FOH ILE B 151 UNP P13332 TYR 151 SEE REMARK 999 SEQADV 3FOH GLY B 301 UNP P13332 GLU 301 SEE REMARK 999 SEQADV 3FOH VAL B 399 UNP P13332 ALA 399 SEE REMARK 999 SEQADV 3FOH TYR B 454 UNP P13332 HIS 454 SEE REMARK 999 SEQADV 3FOH PRO B 510 UNP P13332 ARG 510 ENGINEERED SEQADV 3FOH GLU C 100 UNP P13332 ASP 100 SEE REMARK 999 SEQADV 3FOH ALA C 148 UNP P13332 GLY 148 SEE REMARK 999 SEQADV 3FOH ILE C 150 UNP P13332 ASN 150 SEE REMARK 999 SEQADV 3FOH ILE C 151 UNP P13332 TYR 151 SEE REMARK 999 SEQADV 3FOH GLY C 301 UNP P13332 GLU 301 SEE REMARK 999 SEQADV 3FOH VAL C 399 UNP P13332 ALA 399 SEE REMARK 999 SEQADV 3FOH TYR C 454 UNP P13332 HIS 454 SEE REMARK 999 SEQADV 3FOH PRO C 510 UNP P13332 ARG 510 ENGINEERED SEQADV 3FOH GLU D 100 UNP P13332 ASP 100 SEE REMARK 999 SEQADV 3FOH ALA D 148 UNP P13332 GLY 148 SEE REMARK 999 SEQADV 3FOH ILE D 150 UNP P13332 ASN 150 SEE REMARK 999 SEQADV 3FOH ILE D 151 UNP P13332 TYR 151 SEE REMARK 999 SEQADV 3FOH GLY D 301 UNP P13332 GLU 301 SEE REMARK 999 SEQADV 3FOH VAL D 399 UNP P13332 ALA 399 SEE REMARK 999 SEQADV 3FOH TYR D 454 UNP P13332 HIS 454 SEE REMARK 999 SEQADV 3FOH PRO D 510 UNP P13332 ARG 510 ENGINEERED SEQADV 3FOH GLU E 100 UNP P13332 ASP 100 SEE REMARK 999 SEQADV 3FOH ALA E 148 UNP P13332 GLY 148 SEE REMARK 999 SEQADV 3FOH ILE E 150 UNP P13332 ASN 150 SEE REMARK 999 SEQADV 3FOH ILE E 151 UNP P13332 TYR 151 SEE REMARK 999 SEQADV 3FOH GLY E 301 UNP P13332 GLU 301 SEE REMARK 999 SEQADV 3FOH VAL E 399 UNP P13332 ALA 399 SEE REMARK 999 SEQADV 3FOH TYR E 454 UNP P13332 HIS 454 SEE REMARK 999 SEQADV 3FOH PRO E 510 UNP P13332 ARG 510 ENGINEERED SEQADV 3FOH GLU F 100 UNP P13332 ASP 100 SEE REMARK 999 SEQADV 3FOH ALA F 148 UNP P13332 GLY 148 SEE REMARK 999 SEQADV 3FOH ILE F 150 UNP P13332 ASN 150 SEE REMARK 999 SEQADV 3FOH ILE F 151 UNP P13332 TYR 151 SEE REMARK 999 SEQADV 3FOH GLY F 301 UNP P13332 GLU 301 SEE REMARK 999 SEQADV 3FOH VAL F 399 UNP P13332 ALA 399 SEE REMARK 999 SEQADV 3FOH TYR F 454 UNP P13332 HIS 454 SEE REMARK 999 SEQADV 3FOH PRO F 510 UNP P13332 ARG 510 ENGINEERED SEQRES 1 A 510 MET THR LEU LEU SER PRO GLY ILE GLU LEU LYS GLU THR SEQRES 2 A 510 THR VAL GLN SER THR VAL VAL ASN ASN SER THR GLY THR SEQRES 3 A 510 ALA ALA LEU ALA GLY LYS PHE GLN TRP GLY PRO ALA PHE SEQRES 4 A 510 GLN ILE LYS GLN VAL THR ASN GLU VAL ASP LEU VAL ASN SEQRES 5 A 510 THR PHE GLY GLN PRO THR ALA GLU THR ALA ASP TYR PHE SEQRES 6 A 510 MET SER ALA MET ASN PHE LEU GLN TYR GLY ASN ASP LEU SEQRES 7 A 510 ARG VAL VAL ARG ALA VAL ASP ARG ASP THR ALA LYS ASN SEQRES 8 A 510 SER SER PRO ILE ALA GLY ASN ILE GLU TYR THR ILE SER SEQRES 9 A 510 THR PRO GLY SER ASN TYR ALA VAL GLY ASP LYS ILE THR SEQRES 10 A 510 VAL LYS TYR VAL SER ASP ASP ILE GLU THR GLU GLY LYS SEQRES 11 A 510 ILE THR GLU VAL ASP ALA ASP GLY LYS ILE LYS LYS ILE SEQRES 12 A 510 ASN ILE PRO THR ALA LYS ILE ILE ALA LYS ALA LYS GLU SEQRES 13 A 510 VAL GLY GLU TYR PRO THR LEU GLY SER ASN TRP THR ALA SEQRES 14 A 510 GLU ILE SER SER SER SER SER GLY LEU ALA ALA VAL ILE SEQRES 15 A 510 THR LEU GLY LYS ILE ILE THR ASP SER GLY ILE LEU LEU SEQRES 16 A 510 ALA GLU ILE GLU ASN ALA GLU ALA ALA MET THR ALA VAL SEQRES 17 A 510 ASP PHE GLN ALA ASN LEU LYS LYS TYR GLY ILE PRO GLY SEQRES 18 A 510 VAL VAL ALA LEU TYR PRO GLY GLU LEU GLY ASP LYS ILE SEQRES 19 A 510 GLU ILE GLU ILE VAL SER LYS ALA ASP TYR ALA LYS GLY SEQRES 20 A 510 ALA SER ALA LEU LEU PRO ILE TYR PRO GLY GLY GLY THR SEQRES 21 A 510 ARG ALA SER THR ALA LYS ALA VAL PHE GLY TYR GLY PRO SEQRES 22 A 510 GLN THR ASP SER GLN TYR ALA ILE ILE VAL ARG ARG ASN SEQRES 23 A 510 ASP ALA ILE VAL GLN SER VAL VAL LEU SER THR LYS ARG SEQRES 24 A 510 GLY GLY LYS ASP ILE TYR ASP SER ASN ILE TYR ILE ASP SEQRES 25 A 510 ASP PHE PHE ALA LYS GLY GLY SER GLU TYR ILE PHE ALA SEQRES 26 A 510 THR ALA GLN ASN TRP PRO GLU GLY PHE SER GLY ILE LEU SEQRES 27 A 510 THR LEU SER GLY GLY LEU SER SER ASN ALA GLU VAL THR SEQRES 28 A 510 ALA GLY ASP LEU MET GLU ALA TRP ASP PHE PHE ALA ASP SEQRES 29 A 510 ARG GLU SER VAL ASP VAL GLN LEU PHE ILE ALA GLY SER SEQRES 30 A 510 CYS ALA GLY GLU SER LEU GLU THR ALA SER THR VAL GLN SEQRES 31 A 510 LYS HIS VAL VAL SER ILE GLY ASP VAL ARG GLN ASP CYS SEQRES 32 A 510 LEU VAL LEU CYS SER PRO PRO ARG GLU THR VAL VAL GLY SEQRES 33 A 510 ILE PRO VAL THR ARG ALA VAL ASP ASN LEU VAL ASN TRP SEQRES 34 A 510 ARG THR ALA ALA GLY SER TYR THR ASP ASN ASN PHE ASN SEQRES 35 A 510 ILE SER SER THR TYR ALA ALA ILE ASP GLY ASN TYR LYS SEQRES 36 A 510 TYR GLN TYR ASP LYS TYR ASN ASP VAL ASN ARG TRP VAL SEQRES 37 A 510 PRO LEU ALA ALA ASP ILE ALA GLY LEU CYS ALA ARG THR SEQRES 38 A 510 ASP ASN VAL SER GLN THR TRP MET SER PRO ALA GLY TYR SEQRES 39 A 510 ASN ARG GLY GLN ILE LEU ASN VAL ILE LYS LEU ALA ILE SEQRES 40 A 510 GLU THR PRO SEQRES 1 B 510 MET THR LEU LEU SER PRO GLY ILE GLU LEU LYS GLU THR SEQRES 2 B 510 THR VAL GLN SER THR VAL VAL ASN ASN SER THR GLY THR SEQRES 3 B 510 ALA ALA LEU ALA GLY LYS PHE GLN TRP GLY PRO ALA PHE SEQRES 4 B 510 GLN ILE LYS GLN VAL THR ASN GLU VAL ASP LEU VAL ASN SEQRES 5 B 510 THR PHE GLY GLN PRO THR ALA GLU THR ALA ASP TYR PHE SEQRES 6 B 510 MET SER ALA MET ASN PHE LEU GLN TYR GLY ASN ASP LEU SEQRES 7 B 510 ARG VAL VAL ARG ALA VAL ASP ARG ASP THR ALA LYS ASN SEQRES 8 B 510 SER SER PRO ILE ALA GLY ASN ILE GLU TYR THR ILE SER SEQRES 9 B 510 THR PRO GLY SER ASN TYR ALA VAL GLY ASP LYS ILE THR SEQRES 10 B 510 VAL LYS TYR VAL SER ASP ASP ILE GLU THR GLU GLY LYS SEQRES 11 B 510 ILE THR GLU VAL ASP ALA ASP GLY LYS ILE LYS LYS ILE SEQRES 12 B 510 ASN ILE PRO THR ALA LYS ILE ILE ALA LYS ALA LYS GLU SEQRES 13 B 510 VAL GLY GLU TYR PRO THR LEU GLY SER ASN TRP THR ALA SEQRES 14 B 510 GLU ILE SER SER SER SER SER GLY LEU ALA ALA VAL ILE SEQRES 15 B 510 THR LEU GLY LYS ILE ILE THR ASP SER GLY ILE LEU LEU SEQRES 16 B 510 ALA GLU ILE GLU ASN ALA GLU ALA ALA MET THR ALA VAL SEQRES 17 B 510 ASP PHE GLN ALA ASN LEU LYS LYS TYR GLY ILE PRO GLY SEQRES 18 B 510 VAL VAL ALA LEU TYR PRO GLY GLU LEU GLY ASP LYS ILE SEQRES 19 B 510 GLU ILE GLU ILE VAL SER LYS ALA ASP TYR ALA LYS GLY SEQRES 20 B 510 ALA SER ALA LEU LEU PRO ILE TYR PRO GLY GLY GLY THR SEQRES 21 B 510 ARG ALA SER THR ALA LYS ALA VAL PHE GLY TYR GLY PRO SEQRES 22 B 510 GLN THR ASP SER GLN TYR ALA ILE ILE VAL ARG ARG ASN SEQRES 23 B 510 ASP ALA ILE VAL GLN SER VAL VAL LEU SER THR LYS ARG SEQRES 24 B 510 GLY GLY LYS ASP ILE TYR ASP SER ASN ILE TYR ILE ASP SEQRES 25 B 510 ASP PHE PHE ALA LYS GLY GLY SER GLU TYR ILE PHE ALA SEQRES 26 B 510 THR ALA GLN ASN TRP PRO GLU GLY PHE SER GLY ILE LEU SEQRES 27 B 510 THR LEU SER GLY GLY LEU SER SER ASN ALA GLU VAL THR SEQRES 28 B 510 ALA GLY ASP LEU MET GLU ALA TRP ASP PHE PHE ALA ASP SEQRES 29 B 510 ARG GLU SER VAL ASP VAL GLN LEU PHE ILE ALA GLY SER SEQRES 30 B 510 CYS ALA GLY GLU SER LEU GLU THR ALA SER THR VAL GLN SEQRES 31 B 510 LYS HIS VAL VAL SER ILE GLY ASP VAL ARG GLN ASP CYS SEQRES 32 B 510 LEU VAL LEU CYS SER PRO PRO ARG GLU THR VAL VAL GLY SEQRES 33 B 510 ILE PRO VAL THR ARG ALA VAL ASP ASN LEU VAL ASN TRP SEQRES 34 B 510 ARG THR ALA ALA GLY SER TYR THR ASP ASN ASN PHE ASN SEQRES 35 B 510 ILE SER SER THR TYR ALA ALA ILE ASP GLY ASN TYR LYS SEQRES 36 B 510 TYR GLN TYR ASP LYS TYR ASN ASP VAL ASN ARG TRP VAL SEQRES 37 B 510 PRO LEU ALA ALA ASP ILE ALA GLY LEU CYS ALA ARG THR SEQRES 38 B 510 ASP ASN VAL SER GLN THR TRP MET SER PRO ALA GLY TYR SEQRES 39 B 510 ASN ARG GLY GLN ILE LEU ASN VAL ILE LYS LEU ALA ILE SEQRES 40 B 510 GLU THR PRO SEQRES 1 C 510 MET THR LEU LEU SER PRO GLY ILE GLU LEU LYS GLU THR SEQRES 2 C 510 THR VAL GLN SER THR VAL VAL ASN ASN SER THR GLY THR SEQRES 3 C 510 ALA ALA LEU ALA GLY LYS PHE GLN TRP GLY PRO ALA PHE SEQRES 4 C 510 GLN ILE LYS GLN VAL THR ASN GLU VAL ASP LEU VAL ASN SEQRES 5 C 510 THR PHE GLY GLN PRO THR ALA GLU THR ALA ASP TYR PHE SEQRES 6 C 510 MET SER ALA MET ASN PHE LEU GLN TYR GLY ASN ASP LEU SEQRES 7 C 510 ARG VAL VAL ARG ALA VAL ASP ARG ASP THR ALA LYS ASN SEQRES 8 C 510 SER SER PRO ILE ALA GLY ASN ILE GLU TYR THR ILE SER SEQRES 9 C 510 THR PRO GLY SER ASN TYR ALA VAL GLY ASP LYS ILE THR SEQRES 10 C 510 VAL LYS TYR VAL SER ASP ASP ILE GLU THR GLU GLY LYS SEQRES 11 C 510 ILE THR GLU VAL ASP ALA ASP GLY LYS ILE LYS LYS ILE SEQRES 12 C 510 ASN ILE PRO THR ALA LYS ILE ILE ALA LYS ALA LYS GLU SEQRES 13 C 510 VAL GLY GLU TYR PRO THR LEU GLY SER ASN TRP THR ALA SEQRES 14 C 510 GLU ILE SER SER SER SER SER GLY LEU ALA ALA VAL ILE SEQRES 15 C 510 THR LEU GLY LYS ILE ILE THR ASP SER GLY ILE LEU LEU SEQRES 16 C 510 ALA GLU ILE GLU ASN ALA GLU ALA ALA MET THR ALA VAL SEQRES 17 C 510 ASP PHE GLN ALA ASN LEU LYS LYS TYR GLY ILE PRO GLY SEQRES 18 C 510 VAL VAL ALA LEU TYR PRO GLY GLU LEU GLY ASP LYS ILE SEQRES 19 C 510 GLU ILE GLU ILE VAL SER LYS ALA ASP TYR ALA LYS GLY SEQRES 20 C 510 ALA SER ALA LEU LEU PRO ILE TYR PRO GLY GLY GLY THR SEQRES 21 C 510 ARG ALA SER THR ALA LYS ALA VAL PHE GLY TYR GLY PRO SEQRES 22 C 510 GLN THR ASP SER GLN TYR ALA ILE ILE VAL ARG ARG ASN SEQRES 23 C 510 ASP ALA ILE VAL GLN SER VAL VAL LEU SER THR LYS ARG SEQRES 24 C 510 GLY GLY LYS ASP ILE TYR ASP SER ASN ILE TYR ILE ASP SEQRES 25 C 510 ASP PHE PHE ALA LYS GLY GLY SER GLU TYR ILE PHE ALA SEQRES 26 C 510 THR ALA GLN ASN TRP PRO GLU GLY PHE SER GLY ILE LEU SEQRES 27 C 510 THR LEU SER GLY GLY LEU SER SER ASN ALA GLU VAL THR SEQRES 28 C 510 ALA GLY ASP LEU MET GLU ALA TRP ASP PHE PHE ALA ASP SEQRES 29 C 510 ARG GLU SER VAL ASP VAL GLN LEU PHE ILE ALA GLY SER SEQRES 30 C 510 CYS ALA GLY GLU SER LEU GLU THR ALA SER THR VAL GLN SEQRES 31 C 510 LYS HIS VAL VAL SER ILE GLY ASP VAL ARG GLN ASP CYS SEQRES 32 C 510 LEU VAL LEU CYS SER PRO PRO ARG GLU THR VAL VAL GLY SEQRES 33 C 510 ILE PRO VAL THR ARG ALA VAL ASP ASN LEU VAL ASN TRP SEQRES 34 C 510 ARG THR ALA ALA GLY SER TYR THR ASP ASN ASN PHE ASN SEQRES 35 C 510 ILE SER SER THR TYR ALA ALA ILE ASP GLY ASN TYR LYS SEQRES 36 C 510 TYR GLN TYR ASP LYS TYR ASN ASP VAL ASN ARG TRP VAL SEQRES 37 C 510 PRO LEU ALA ALA ASP ILE ALA GLY LEU CYS ALA ARG THR SEQRES 38 C 510 ASP ASN VAL SER GLN THR TRP MET SER PRO ALA GLY TYR SEQRES 39 C 510 ASN ARG GLY GLN ILE LEU ASN VAL ILE LYS LEU ALA ILE SEQRES 40 C 510 GLU THR PRO SEQRES 1 D 510 MET THR LEU LEU SER PRO GLY ILE GLU LEU LYS GLU THR SEQRES 2 D 510 THR VAL GLN SER THR VAL VAL ASN ASN SER THR GLY THR SEQRES 3 D 510 ALA ALA LEU ALA GLY LYS PHE GLN TRP GLY PRO ALA PHE SEQRES 4 D 510 GLN ILE LYS GLN VAL THR ASN GLU VAL ASP LEU VAL ASN SEQRES 5 D 510 THR PHE GLY GLN PRO THR ALA GLU THR ALA ASP TYR PHE SEQRES 6 D 510 MET SER ALA MET ASN PHE LEU GLN TYR GLY ASN ASP LEU SEQRES 7 D 510 ARG VAL VAL ARG ALA VAL ASP ARG ASP THR ALA LYS ASN SEQRES 8 D 510 SER SER PRO ILE ALA GLY ASN ILE GLU TYR THR ILE SER SEQRES 9 D 510 THR PRO GLY SER ASN TYR ALA VAL GLY ASP LYS ILE THR SEQRES 10 D 510 VAL LYS TYR VAL SER ASP ASP ILE GLU THR GLU GLY LYS SEQRES 11 D 510 ILE THR GLU VAL ASP ALA ASP GLY LYS ILE LYS LYS ILE SEQRES 12 D 510 ASN ILE PRO THR ALA LYS ILE ILE ALA LYS ALA LYS GLU SEQRES 13 D 510 VAL GLY GLU TYR PRO THR LEU GLY SER ASN TRP THR ALA SEQRES 14 D 510 GLU ILE SER SER SER SER SER GLY LEU ALA ALA VAL ILE SEQRES 15 D 510 THR LEU GLY LYS ILE ILE THR ASP SER GLY ILE LEU LEU SEQRES 16 D 510 ALA GLU ILE GLU ASN ALA GLU ALA ALA MET THR ALA VAL SEQRES 17 D 510 ASP PHE GLN ALA ASN LEU LYS LYS TYR GLY ILE PRO GLY SEQRES 18 D 510 VAL VAL ALA LEU TYR PRO GLY GLU LEU GLY ASP LYS ILE SEQRES 19 D 510 GLU ILE GLU ILE VAL SER LYS ALA ASP TYR ALA LYS GLY SEQRES 20 D 510 ALA SER ALA LEU LEU PRO ILE TYR PRO GLY GLY GLY THR SEQRES 21 D 510 ARG ALA SER THR ALA LYS ALA VAL PHE GLY TYR GLY PRO SEQRES 22 D 510 GLN THR ASP SER GLN TYR ALA ILE ILE VAL ARG ARG ASN SEQRES 23 D 510 ASP ALA ILE VAL GLN SER VAL VAL LEU SER THR LYS ARG SEQRES 24 D 510 GLY GLY LYS ASP ILE TYR ASP SER ASN ILE TYR ILE ASP SEQRES 25 D 510 ASP PHE PHE ALA LYS GLY GLY SER GLU TYR ILE PHE ALA SEQRES 26 D 510 THR ALA GLN ASN TRP PRO GLU GLY PHE SER GLY ILE LEU SEQRES 27 D 510 THR LEU SER GLY GLY LEU SER SER ASN ALA GLU VAL THR SEQRES 28 D 510 ALA GLY ASP LEU MET GLU ALA TRP ASP PHE PHE ALA ASP SEQRES 29 D 510 ARG GLU SER VAL ASP VAL GLN LEU PHE ILE ALA GLY SER SEQRES 30 D 510 CYS ALA GLY GLU SER LEU GLU THR ALA SER THR VAL GLN SEQRES 31 D 510 LYS HIS VAL VAL SER ILE GLY ASP VAL ARG GLN ASP CYS SEQRES 32 D 510 LEU VAL LEU CYS SER PRO PRO ARG GLU THR VAL VAL GLY SEQRES 33 D 510 ILE PRO VAL THR ARG ALA VAL ASP ASN LEU VAL ASN TRP SEQRES 34 D 510 ARG THR ALA ALA GLY SER TYR THR ASP ASN ASN PHE ASN SEQRES 35 D 510 ILE SER SER THR TYR ALA ALA ILE ASP GLY ASN TYR LYS SEQRES 36 D 510 TYR GLN TYR ASP LYS TYR ASN ASP VAL ASN ARG TRP VAL SEQRES 37 D 510 PRO LEU ALA ALA ASP ILE ALA GLY LEU CYS ALA ARG THR SEQRES 38 D 510 ASP ASN VAL SER GLN THR TRP MET SER PRO ALA GLY TYR SEQRES 39 D 510 ASN ARG GLY GLN ILE LEU ASN VAL ILE LYS LEU ALA ILE SEQRES 40 D 510 GLU THR PRO SEQRES 1 E 510 MET THR LEU LEU SER PRO GLY ILE GLU LEU LYS GLU THR SEQRES 2 E 510 THR VAL GLN SER THR VAL VAL ASN ASN SER THR GLY THR SEQRES 3 E 510 ALA ALA LEU ALA GLY LYS PHE GLN TRP GLY PRO ALA PHE SEQRES 4 E 510 GLN ILE LYS GLN VAL THR ASN GLU VAL ASP LEU VAL ASN SEQRES 5 E 510 THR PHE GLY GLN PRO THR ALA GLU THR ALA ASP TYR PHE SEQRES 6 E 510 MET SER ALA MET ASN PHE LEU GLN TYR GLY ASN ASP LEU SEQRES 7 E 510 ARG VAL VAL ARG ALA VAL ASP ARG ASP THR ALA LYS ASN SEQRES 8 E 510 SER SER PRO ILE ALA GLY ASN ILE GLU TYR THR ILE SER SEQRES 9 E 510 THR PRO GLY SER ASN TYR ALA VAL GLY ASP LYS ILE THR SEQRES 10 E 510 VAL LYS TYR VAL SER ASP ASP ILE GLU THR GLU GLY LYS SEQRES 11 E 510 ILE THR GLU VAL ASP ALA ASP GLY LYS ILE LYS LYS ILE SEQRES 12 E 510 ASN ILE PRO THR ALA LYS ILE ILE ALA LYS ALA LYS GLU SEQRES 13 E 510 VAL GLY GLU TYR PRO THR LEU GLY SER ASN TRP THR ALA SEQRES 14 E 510 GLU ILE SER SER SER SER SER GLY LEU ALA ALA VAL ILE SEQRES 15 E 510 THR LEU GLY LYS ILE ILE THR ASP SER GLY ILE LEU LEU SEQRES 16 E 510 ALA GLU ILE GLU ASN ALA GLU ALA ALA MET THR ALA VAL SEQRES 17 E 510 ASP PHE GLN ALA ASN LEU LYS LYS TYR GLY ILE PRO GLY SEQRES 18 E 510 VAL VAL ALA LEU TYR PRO GLY GLU LEU GLY ASP LYS ILE SEQRES 19 E 510 GLU ILE GLU ILE VAL SER LYS ALA ASP TYR ALA LYS GLY SEQRES 20 E 510 ALA SER ALA LEU LEU PRO ILE TYR PRO GLY GLY GLY THR SEQRES 21 E 510 ARG ALA SER THR ALA LYS ALA VAL PHE GLY TYR GLY PRO SEQRES 22 E 510 GLN THR ASP SER GLN TYR ALA ILE ILE VAL ARG ARG ASN SEQRES 23 E 510 ASP ALA ILE VAL GLN SER VAL VAL LEU SER THR LYS ARG SEQRES 24 E 510 GLY GLY LYS ASP ILE TYR ASP SER ASN ILE TYR ILE ASP SEQRES 25 E 510 ASP PHE PHE ALA LYS GLY GLY SER GLU TYR ILE PHE ALA SEQRES 26 E 510 THR ALA GLN ASN TRP PRO GLU GLY PHE SER GLY ILE LEU SEQRES 27 E 510 THR LEU SER GLY GLY LEU SER SER ASN ALA GLU VAL THR SEQRES 28 E 510 ALA GLY ASP LEU MET GLU ALA TRP ASP PHE PHE ALA ASP SEQRES 29 E 510 ARG GLU SER VAL ASP VAL GLN LEU PHE ILE ALA GLY SER SEQRES 30 E 510 CYS ALA GLY GLU SER LEU GLU THR ALA SER THR VAL GLN SEQRES 31 E 510 LYS HIS VAL VAL SER ILE GLY ASP VAL ARG GLN ASP CYS SEQRES 32 E 510 LEU VAL LEU CYS SER PRO PRO ARG GLU THR VAL VAL GLY SEQRES 33 E 510 ILE PRO VAL THR ARG ALA VAL ASP ASN LEU VAL ASN TRP SEQRES 34 E 510 ARG THR ALA ALA GLY SER TYR THR ASP ASN ASN PHE ASN SEQRES 35 E 510 ILE SER SER THR TYR ALA ALA ILE ASP GLY ASN TYR LYS SEQRES 36 E 510 TYR GLN TYR ASP LYS TYR ASN ASP VAL ASN ARG TRP VAL SEQRES 37 E 510 PRO LEU ALA ALA ASP ILE ALA GLY LEU CYS ALA ARG THR SEQRES 38 E 510 ASP ASN VAL SER GLN THR TRP MET SER PRO ALA GLY TYR SEQRES 39 E 510 ASN ARG GLY GLN ILE LEU ASN VAL ILE LYS LEU ALA ILE SEQRES 40 E 510 GLU THR PRO SEQRES 1 F 510 MET THR LEU LEU SER PRO GLY ILE GLU LEU LYS GLU THR SEQRES 2 F 510 THR VAL GLN SER THR VAL VAL ASN ASN SER THR GLY THR SEQRES 3 F 510 ALA ALA LEU ALA GLY LYS PHE GLN TRP GLY PRO ALA PHE SEQRES 4 F 510 GLN ILE LYS GLN VAL THR ASN GLU VAL ASP LEU VAL ASN SEQRES 5 F 510 THR PHE GLY GLN PRO THR ALA GLU THR ALA ASP TYR PHE SEQRES 6 F 510 MET SER ALA MET ASN PHE LEU GLN TYR GLY ASN ASP LEU SEQRES 7 F 510 ARG VAL VAL ARG ALA VAL ASP ARG ASP THR ALA LYS ASN SEQRES 8 F 510 SER SER PRO ILE ALA GLY ASN ILE GLU TYR THR ILE SER SEQRES 9 F 510 THR PRO GLY SER ASN TYR ALA VAL GLY ASP LYS ILE THR SEQRES 10 F 510 VAL LYS TYR VAL SER ASP ASP ILE GLU THR GLU GLY LYS SEQRES 11 F 510 ILE THR GLU VAL ASP ALA ASP GLY LYS ILE LYS LYS ILE SEQRES 12 F 510 ASN ILE PRO THR ALA LYS ILE ILE ALA LYS ALA LYS GLU SEQRES 13 F 510 VAL GLY GLU TYR PRO THR LEU GLY SER ASN TRP THR ALA SEQRES 14 F 510 GLU ILE SER SER SER SER SER GLY LEU ALA ALA VAL ILE SEQRES 15 F 510 THR LEU GLY LYS ILE ILE THR ASP SER GLY ILE LEU LEU SEQRES 16 F 510 ALA GLU ILE GLU ASN ALA GLU ALA ALA MET THR ALA VAL SEQRES 17 F 510 ASP PHE GLN ALA ASN LEU LYS LYS TYR GLY ILE PRO GLY SEQRES 18 F 510 VAL VAL ALA LEU TYR PRO GLY GLU LEU GLY ASP LYS ILE SEQRES 19 F 510 GLU ILE GLU ILE VAL SER LYS ALA ASP TYR ALA LYS GLY SEQRES 20 F 510 ALA SER ALA LEU LEU PRO ILE TYR PRO GLY GLY GLY THR SEQRES 21 F 510 ARG ALA SER THR ALA LYS ALA VAL PHE GLY TYR GLY PRO SEQRES 22 F 510 GLN THR ASP SER GLN TYR ALA ILE ILE VAL ARG ARG ASN SEQRES 23 F 510 ASP ALA ILE VAL GLN SER VAL VAL LEU SER THR LYS ARG SEQRES 24 F 510 GLY GLY LYS ASP ILE TYR ASP SER ASN ILE TYR ILE ASP SEQRES 25 F 510 ASP PHE PHE ALA LYS GLY GLY SER GLU TYR ILE PHE ALA SEQRES 26 F 510 THR ALA GLN ASN TRP PRO GLU GLY PHE SER GLY ILE LEU SEQRES 27 F 510 THR LEU SER GLY GLY LEU SER SER ASN ALA GLU VAL THR SEQRES 28 F 510 ALA GLY ASP LEU MET GLU ALA TRP ASP PHE PHE ALA ASP SEQRES 29 F 510 ARG GLU SER VAL ASP VAL GLN LEU PHE ILE ALA GLY SER SEQRES 30 F 510 CYS ALA GLY GLU SER LEU GLU THR ALA SER THR VAL GLN SEQRES 31 F 510 LYS HIS VAL VAL SER ILE GLY ASP VAL ARG GLN ASP CYS SEQRES 32 F 510 LEU VAL LEU CYS SER PRO PRO ARG GLU THR VAL VAL GLY SEQRES 33 F 510 ILE PRO VAL THR ARG ALA VAL ASP ASN LEU VAL ASN TRP SEQRES 34 F 510 ARG THR ALA ALA GLY SER TYR THR ASP ASN ASN PHE ASN SEQRES 35 F 510 ILE SER SER THR TYR ALA ALA ILE ASP GLY ASN TYR LYS SEQRES 36 F 510 TYR GLN TYR ASP LYS TYR ASN ASP VAL ASN ARG TRP VAL SEQRES 37 F 510 PRO LEU ALA ALA ASP ILE ALA GLY LEU CYS ALA ARG THR SEQRES 38 F 510 ASP ASN VAL SER GLN THR TRP MET SER PRO ALA GLY TYR SEQRES 39 F 510 ASN ARG GLY GLN ILE LEU ASN VAL ILE LYS LEU ALA ILE SEQRES 40 F 510 GLU THR PRO HELIX 1 1 GLU A 47 GLY A 55 1 9 HELIX 2 2 THR A 61 ASN A 70 1 10 HELIX 3 3 THR A 147 VAL A 157 1 11 HELIX 4 4 ASN A 200 MET A 205 1 6 HELIX 5 5 ALA A 207 TYR A 217 1 11 HELIX 6 6 GLY A 228 ASP A 232 5 5 HELIX 7 7 LYS A 241 LYS A 246 1 6 HELIX 8 8 GLY A 247 SER A 249 5 3 HELIX 9 9 THR A 264 VAL A 268 5 5 HELIX 10 10 TYR A 310 LYS A 317 1 8 HELIX 11 11 THR A 351 ASP A 360 1 10 HELIX 12 12 PHE A 361 ALA A 363 5 3 HELIX 13 13 GLY A 376 ALA A 379 5 4 HELIX 14 14 SER A 382 GLN A 401 1 20 HELIX 15 15 PRO A 410 VAL A 415 1 6 HELIX 16 16 PRO A 418 ARG A 430 1 13 HELIX 17 17 LEU A 470 THR A 481 1 12 HELIX 18 18 GLU B 47 GLY B 55 1 9 HELIX 19 19 THR B 61 ASN B 70 1 10 HELIX 20 20 THR B 147 VAL B 157 1 11 HELIX 21 21 ASN B 200 MET B 205 1 6 HELIX 22 22 ALA B 207 TYR B 217 1 11 HELIX 23 23 GLY B 228 ASP B 232 5 5 HELIX 24 24 LYS B 241 LYS B 246 1 6 HELIX 25 25 GLY B 247 SER B 249 5 3 HELIX 26 26 THR B 264 VAL B 268 5 5 HELIX 27 27 TYR B 310 LYS B 317 1 8 HELIX 28 28 THR B 351 ASP B 360 1 10 HELIX 29 29 PHE B 361 ALA B 363 5 3 HELIX 30 30 GLY B 376 ALA B 379 5 4 HELIX 31 31 SER B 382 GLN B 401 1 20 HELIX 32 32 PRO B 410 VAL B 415 1 6 HELIX 33 33 PRO B 418 ARG B 430 1 13 HELIX 34 34 LEU B 470 THR B 481 1 12 HELIX 35 35 GLU C 47 GLY C 55 1 9 HELIX 36 36 THR C 61 ASN C 70 1 10 HELIX 37 37 THR C 147 VAL C 157 1 11 HELIX 38 38 ASN C 200 MET C 205 1 6 HELIX 39 39 ALA C 207 TYR C 217 1 11 HELIX 40 40 GLY C 228 ASP C 232 5 5 HELIX 41 41 LYS C 241 LYS C 246 1 6 HELIX 42 42 GLY C 247 SER C 249 5 3 HELIX 43 43 THR C 264 VAL C 268 5 5 HELIX 44 44 TYR C 310 LYS C 317 1 8 HELIX 45 45 THR C 351 ASP C 360 1 10 HELIX 46 46 PHE C 361 ALA C 363 5 3 HELIX 47 47 GLY C 376 ALA C 379 5 4 HELIX 48 48 SER C 382 GLN C 401 1 20 HELIX 49 49 PRO C 410 VAL C 415 1 6 HELIX 50 50 PRO C 418 ARG C 430 1 13 HELIX 51 51 LEU C 470 THR C 481 1 12 HELIX 52 52 GLU D 47 GLY D 55 1 9 HELIX 53 53 THR D 61 ASN D 70 1 10 HELIX 54 54 THR D 147 VAL D 157 1 11 HELIX 55 55 ASN D 200 MET D 205 1 6 HELIX 56 56 ALA D 207 TYR D 217 1 11 HELIX 57 57 GLY D 228 ASP D 232 5 5 HELIX 58 58 LYS D 241 LYS D 246 1 6 HELIX 59 59 GLY D 247 SER D 249 5 3 HELIX 60 60 THR D 264 VAL D 268 5 5 HELIX 61 61 TYR D 310 LYS D 317 1 8 HELIX 62 62 THR D 351 ASP D 360 1 10 HELIX 63 63 PHE D 361 ALA D 363 5 3 HELIX 64 64 GLY D 376 ALA D 379 5 4 HELIX 65 65 SER D 382 GLN D 401 1 20 HELIX 66 66 PRO D 410 VAL D 415 1 6 HELIX 67 67 PRO D 418 ARG D 430 1 13 HELIX 68 68 LEU D 470 THR D 481 1 12 HELIX 69 69 GLU E 47 GLY E 55 1 9 HELIX 70 70 THR E 61 ASN E 70 1 10 HELIX 71 71 THR E 147 VAL E 157 1 11 HELIX 72 72 ASN E 200 MET E 205 1 6 HELIX 73 73 ALA E 207 TYR E 217 1 11 HELIX 74 74 GLY E 228 ASP E 232 5 5 HELIX 75 75 LYS E 241 LYS E 246 1 6 HELIX 76 76 GLY E 247 SER E 249 5 3 HELIX 77 77 THR E 264 VAL E 268 5 5 HELIX 78 78 TYR E 310 LYS E 317 1 8 HELIX 79 79 THR E 351 ASP E 360 1 10 HELIX 80 80 PHE E 361 ALA E 363 5 3 HELIX 81 81 GLY E 376 ALA E 379 5 4 HELIX 82 82 SER E 382 GLN E 401 1 20 HELIX 83 83 PRO E 410 VAL E 415 1 6 HELIX 84 84 PRO E 418 ARG E 430 1 13 HELIX 85 85 LEU E 470 THR E 481 1 12 HELIX 86 86 GLU F 47 GLY F 55 1 9 HELIX 87 87 THR F 61 ASN F 70 1 10 HELIX 88 88 THR F 147 VAL F 157 1 11 HELIX 89 89 ASN F 200 MET F 205 1 6 HELIX 90 90 ALA F 207 TYR F 217 1 11 HELIX 91 91 GLY F 228 ASP F 232 5 5 HELIX 92 92 LYS F 241 LYS F 246 1 6 HELIX 93 93 GLY F 247 SER F 249 5 3 HELIX 94 94 THR F 264 VAL F 268 5 5 HELIX 95 95 TYR F 310 LYS F 317 1 8 HELIX 96 96 THR F 351 ASP F 360 1 10 HELIX 97 97 PHE F 361 ALA F 363 5 3 HELIX 98 98 GLY F 376 ALA F 379 5 4 HELIX 99 99 SER F 382 GLN F 401 1 20 HELIX 100 100 PRO F 410 VAL F 415 1 6 HELIX 101 101 PRO F 418 ARG F 430 1 13 HELIX 102 102 LEU F 470 THR F 481 1 12 SHEET 1 A 3 THR A 26 GLY A 31 0 SHEET 2 A 3 ASP A 77 ARG A 82 1 O ARG A 79 N LEU A 29 SHEET 3 A 3 LYS A 42 VAL A 44 -1 N VAL A 44 O LEU A 78 SHEET 1 B 2 ILE A 99 THR A 105 0 SHEET 2 B 2 VAL A 181 ILE A 187 -1 O LYS A 186 N GLU A 100 SHEET 1 C 4 ILE A 140 ASN A 144 0 SHEET 2 C 4 ASP A 124 VAL A 134 -1 N THR A 132 O LYS A 142 SHEET 3 C 4 LYS A 115 TYR A 120 -1 N VAL A 118 O GLU A 126 SHEET 4 C 4 TRP A 167 ILE A 171 -1 O GLU A 170 N THR A 117 SHEET 1 D 2 GLY A 221 ALA A 224 0 SHEET 2 D 2 ILE A 323 THR A 326 -1 O PHE A 324 N VAL A 223 SHEET 1 E 6 THR A 260 ALA A 262 0 SHEET 2 E 6 LEU A 251 TYR A 255 -1 N LEU A 252 O ARG A 261 SHEET 3 E 6 GLY A 336 THR A 339 1 O ILE A 337 N PRO A 253 SHEET 4 E 6 ILE A 234 SER A 240 -1 N ILE A 238 O GLY A 336 SHEET 5 E 6 GLN A 278 ARG A 285 -1 O ALA A 280 N VAL A 239 SHEET 6 E 6 ALA A 288 SER A 296 -1 O LEU A 295 N TYR A 279 SHEET 1 F 3 PHE A 373 ILE A 374 0 SHEET 2 F 3 VAL A 405 LEU A 406 1 O LEU A 406 N PHE A 373 SHEET 3 F 3 ALA A 448 ALA A 449 1 O ALA A 449 N VAL A 405 SHEET 1 G 2 TYR A 454 ASP A 459 0 SHEET 2 G 2 VAL A 464 PRO A 469 -1 O VAL A 468 N LYS A 455 SHEET 1 H 3 THR B 26 GLY B 31 0 SHEET 2 H 3 ASP B 77 ARG B 82 1 O ARG B 79 N LEU B 29 SHEET 3 H 3 LYS B 42 VAL B 44 -1 N VAL B 44 O LEU B 78 SHEET 1 I 2 ILE B 99 THR B 105 0 SHEET 2 I 2 VAL B 181 ILE B 187 -1 O LYS B 186 N GLU B 100 SHEET 1 J 4 ILE B 140 ASN B 144 0 SHEET 2 J 4 ASP B 124 VAL B 134 -1 N THR B 132 O LYS B 142 SHEET 3 J 4 LYS B 115 TYR B 120 -1 N VAL B 118 O GLU B 126 SHEET 4 J 4 TRP B 167 ILE B 171 -1 O GLU B 170 N THR B 117 SHEET 1 K 2 GLY B 221 ALA B 224 0 SHEET 2 K 2 ILE B 323 THR B 326 -1 O PHE B 324 N VAL B 223 SHEET 1 L 6 THR B 260 ALA B 262 0 SHEET 2 L 6 LEU B 251 TYR B 255 -1 N LEU B 252 O ARG B 261 SHEET 3 L 6 GLY B 336 THR B 339 1 O ILE B 337 N PRO B 253 SHEET 4 L 6 ILE B 234 SER B 240 -1 N ILE B 238 O GLY B 336 SHEET 5 L 6 GLN B 278 ARG B 285 -1 O ALA B 280 N VAL B 239 SHEET 6 L 6 ALA B 288 SER B 296 -1 O LEU B 295 N TYR B 279 SHEET 1 M 3 PHE B 373 ILE B 374 0 SHEET 2 M 3 VAL B 405 LEU B 406 1 O LEU B 406 N PHE B 373 SHEET 3 M 3 ALA B 448 ALA B 449 1 O ALA B 449 N VAL B 405 SHEET 1 N 2 TYR B 454 ASP B 459 0 SHEET 2 N 2 VAL B 464 PRO B 469 -1 O VAL B 468 N LYS B 455 SHEET 1 O 3 THR C 26 GLY C 31 0 SHEET 2 O 3 ASP C 77 ARG C 82 1 O ARG C 79 N LEU C 29 SHEET 3 O 3 LYS C 42 VAL C 44 -1 N VAL C 44 O LEU C 78 SHEET 1 P 2 ILE C 99 THR C 105 0 SHEET 2 P 2 VAL C 181 ILE C 187 -1 O LYS C 186 N GLU C 100 SHEET 1 Q 4 ILE C 140 ASN C 144 0 SHEET 2 Q 4 ASP C 124 VAL C 134 -1 N THR C 132 O LYS C 142 SHEET 3 Q 4 LYS C 115 TYR C 120 -1 N VAL C 118 O GLU C 126 SHEET 4 Q 4 TRP C 167 ILE C 171 -1 O GLU C 170 N THR C 117 SHEET 1 R 2 GLY C 221 ALA C 224 0 SHEET 2 R 2 ILE C 323 THR C 326 -1 O PHE C 324 N VAL C 223 SHEET 1 S 6 THR C 260 ALA C 262 0 SHEET 2 S 6 LEU C 251 TYR C 255 -1 N LEU C 252 O ARG C 261 SHEET 3 S 6 GLY C 336 THR C 339 1 O ILE C 337 N PRO C 253 SHEET 4 S 6 ILE C 234 SER C 240 -1 N ILE C 238 O GLY C 336 SHEET 5 S 6 GLN C 278 ARG C 285 -1 O ALA C 280 N VAL C 239 SHEET 6 S 6 ALA C 288 SER C 296 -1 O LEU C 295 N TYR C 279 SHEET 1 T 3 PHE C 373 ILE C 374 0 SHEET 2 T 3 VAL C 405 LEU C 406 1 O LEU C 406 N PHE C 373 SHEET 3 T 3 ALA C 448 ALA C 449 1 O ALA C 449 N VAL C 405 SHEET 1 U 2 TYR C 454 ASP C 459 0 SHEET 2 U 2 VAL C 464 PRO C 469 -1 O VAL C 468 N LYS C 455 SHEET 1 V 3 THR D 26 GLY D 31 0 SHEET 2 V 3 ASP D 77 ARG D 82 1 O ARG D 79 N LEU D 29 SHEET 3 V 3 LYS D 42 VAL D 44 -1 N VAL D 44 O LEU D 78 SHEET 1 W 2 ILE D 99 THR D 105 0 SHEET 2 W 2 VAL D 181 ILE D 187 -1 O LYS D 186 N GLU D 100 SHEET 1 X 4 ILE D 140 ASN D 144 0 SHEET 2 X 4 ASP D 124 VAL D 134 -1 N THR D 132 O LYS D 142 SHEET 3 X 4 LYS D 115 TYR D 120 -1 N VAL D 118 O GLU D 126 SHEET 4 X 4 TRP D 167 ILE D 171 -1 O GLU D 170 N THR D 117 SHEET 1 Y 2 GLY D 221 ALA D 224 0 SHEET 2 Y 2 ILE D 323 THR D 326 -1 O PHE D 324 N VAL D 223 SHEET 1 Z 6 THR D 260 ALA D 262 0 SHEET 2 Z 6 LEU D 251 TYR D 255 -1 N LEU D 252 O ARG D 261 SHEET 3 Z 6 GLY D 336 THR D 339 1 O ILE D 337 N PRO D 253 SHEET 4 Z 6 ILE D 234 SER D 240 -1 N ILE D 238 O GLY D 336 SHEET 5 Z 6 GLN D 278 ARG D 285 -1 O ALA D 280 N VAL D 239 SHEET 6 Z 6 ALA D 288 SER D 296 -1 O LEU D 295 N TYR D 279 SHEET 1 AA 3 PHE D 373 ILE D 374 0 SHEET 2 AA 3 VAL D 405 LEU D 406 1 O LEU D 406 N PHE D 373 SHEET 3 AA 3 ALA D 448 ALA D 449 1 O ALA D 449 N VAL D 405 SHEET 1 AB 2 TYR D 454 ASP D 459 0 SHEET 2 AB 2 VAL D 464 PRO D 469 -1 O VAL D 468 N LYS D 455 SHEET 1 AC 3 THR E 26 GLY E 31 0 SHEET 2 AC 3 ASP E 77 ARG E 82 1 O ARG E 79 N LEU E 29 SHEET 3 AC 3 LYS E 42 VAL E 44 -1 N VAL E 44 O LEU E 78 SHEET 1 AD 2 ILE E 99 THR E 105 0 SHEET 2 AD 2 VAL E 181 ILE E 187 -1 O LYS E 186 N GLU E 100 SHEET 1 AE 4 ILE E 140 ASN E 144 0 SHEET 2 AE 4 ASP E 124 VAL E 134 -1 N THR E 132 O LYS E 142 SHEET 3 AE 4 LYS E 115 TYR E 120 -1 N VAL E 118 O GLU E 126 SHEET 4 AE 4 TRP E 167 ILE E 171 -1 O GLU E 170 N THR E 117 SHEET 1 AF 2 GLY E 221 ALA E 224 0 SHEET 2 AF 2 ILE E 323 THR E 326 -1 O PHE E 324 N VAL E 223 SHEET 1 AG 6 THR E 260 ALA E 262 0 SHEET 2 AG 6 LEU E 251 TYR E 255 -1 N LEU E 252 O ARG E 261 SHEET 3 AG 6 GLY E 336 THR E 339 1 O ILE E 337 N PRO E 253 SHEET 4 AG 6 ILE E 234 SER E 240 -1 N ILE E 238 O GLY E 336 SHEET 5 AG 6 GLN E 278 ARG E 285 -1 O ALA E 280 N VAL E 239 SHEET 6 AG 6 ALA E 288 SER E 296 -1 O LEU E 295 N TYR E 279 SHEET 1 AH 3 PHE E 373 ILE E 374 0 SHEET 2 AH 3 VAL E 405 LEU E 406 1 O LEU E 406 N PHE E 373 SHEET 3 AH 3 ALA E 448 ALA E 449 1 O ALA E 449 N VAL E 405 SHEET 1 AI 2 TYR E 454 ASP E 459 0 SHEET 2 AI 2 VAL E 464 PRO E 469 -1 O VAL E 468 N LYS E 455 SHEET 1 AJ 3 THR F 26 GLY F 31 0 SHEET 2 AJ 3 ASP F 77 ARG F 82 1 O ARG F 79 N LEU F 29 SHEET 3 AJ 3 LYS F 42 VAL F 44 -1 N VAL F 44 O LEU F 78 SHEET 1 AK 2 ILE F 99 THR F 105 0 SHEET 2 AK 2 VAL F 181 ILE F 187 -1 O LYS F 186 N GLU F 100 SHEET 1 AL 4 ILE F 140 ASN F 144 0 SHEET 2 AL 4 ASP F 124 VAL F 134 -1 N THR F 132 O LYS F 142 SHEET 3 AL 4 LYS F 115 TYR F 120 -1 N VAL F 118 O GLU F 126 SHEET 4 AL 4 TRP F 167 ILE F 171 -1 O GLU F 170 N THR F 117 SHEET 1 AM 2 GLY F 221 ALA F 224 0 SHEET 2 AM 2 ILE F 323 THR F 326 -1 O PHE F 324 N VAL F 223 SHEET 1 AN 6 THR F 260 ALA F 262 0 SHEET 2 AN 6 LEU F 251 TYR F 255 -1 N LEU F 252 O ARG F 261 SHEET 3 AN 6 GLY F 336 THR F 339 1 O ILE F 337 N PRO F 253 SHEET 4 AN 6 ILE F 234 SER F 240 -1 N ILE F 238 O GLY F 336 SHEET 5 AN 6 GLN F 278 ARG F 285 -1 O ALA F 280 N VAL F 239 SHEET 6 AN 6 ALA F 288 SER F 296 -1 O LEU F 295 N TYR F 279 SHEET 1 AO 3 PHE F 373 ILE F 374 0 SHEET 2 AO 3 VAL F 405 LEU F 406 1 O LEU F 406 N PHE F 373 SHEET 3 AO 3 ALA F 448 ALA F 449 1 O ALA F 449 N VAL F 405 SHEET 1 AP 2 TYR F 454 ASP F 459 0 SHEET 2 AP 2 VAL F 464 PRO F 469 -1 O VAL F 468 N LYS F 455 CISPEP 1 GLY A 36 PRO A 37 0 17.07 CISPEP 2 TYR A 160 PRO A 161 0 -4.65 CISPEP 3 SER A 173 SER A 174 0 -1.58 CISPEP 4 TYR A 255 PRO A 256 0 -3.90 CISPEP 5 GLU A 508 THR A 509 0 -21.10 CISPEP 6 THR A 509 PRO A 510 0 -21.59 CISPEP 7 GLY B 36 PRO B 37 0 17.05 CISPEP 8 TYR B 160 PRO B 161 0 -4.68 CISPEP 9 SER B 173 SER B 174 0 -1.60 CISPEP 10 TYR B 255 PRO B 256 0 -3.93 CISPEP 11 GLU B 508 THR B 509 0 -21.14 CISPEP 12 THR B 509 PRO B 510 0 -21.64 CISPEP 13 GLY C 36 PRO C 37 0 17.07 CISPEP 14 TYR C 160 PRO C 161 0 -4.64 CISPEP 15 SER C 173 SER C 174 0 -1.58 CISPEP 16 TYR C 255 PRO C 256 0 -3.88 CISPEP 17 GLU C 508 THR C 509 0 -21.12 CISPEP 18 THR C 509 PRO C 510 0 -21.59 CISPEP 19 GLY D 36 PRO D 37 0 17.03 CISPEP 20 TYR D 160 PRO D 161 0 -4.58 CISPEP 21 SER D 173 SER D 174 0 -1.57 CISPEP 22 TYR D 255 PRO D 256 0 -3.90 CISPEP 23 GLU D 508 THR D 509 0 -21.13 CISPEP 24 THR D 509 PRO D 510 0 -21.62 CISPEP 25 GLY E 36 PRO E 37 0 17.05 CISPEP 26 TYR E 160 PRO E 161 0 -4.54 CISPEP 27 SER E 173 SER E 174 0 -1.54 CISPEP 28 TYR E 255 PRO E 256 0 -3.86 CISPEP 29 GLU E 508 THR E 509 0 -21.11 CISPEP 30 THR E 509 PRO E 510 0 -21.53 CISPEP 31 GLY F 36 PRO F 37 0 17.13 CISPEP 32 TYR F 160 PRO F 161 0 -4.68 CISPEP 33 SER F 173 SER F 174 0 -1.69 CISPEP 34 TYR F 255 PRO F 256 0 -3.86 CISPEP 35 GLU F 508 THR F 509 0 -21.13 CISPEP 36 THR F 509 PRO F 510 0 -21.64 CRYST1 714.600 714.600 1508.600 90.00 90.00 90.00 P 1 6 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 0.001399 0.000000 0.000000 0.00000 SCALE2 0.000000 0.001399 0.000000 0.00000 SCALE3 0.000000 0.000000 0.000663 0.00000 ATOM 1 N ASN A 21 40.116 41.211-381.173 1.00197.86 N ANISOU 1 N ASN A 21 24661 26429 24087 2495 2157 811 N ATOM 2 CA ASN A 21 39.453 41.249-382.469 1.00197.34 C ANISOU 2 CA ASN A 21 24318 26496 24167 2489 2234 1084 C ATOM 3 C ASN A 21 39.999 40.494-383.681 1.00195.79 C ANISOU 3 C ASN A 21 24054 26410 23928 2308 2221 1166 C ATOM 4 O ASN A 21 40.137 41.068-384.769 1.00193.89 O ANISOU 4 O ASN A 21 23800 26047 23823 2096 2111 1224 O ATOM 5 CB ASN A 21 39.226 42.716-382.863 1.00196.39 C ANISOU 5 CB ASN A 21 24139 26174 24305 2396 2133 1184 C ATOM 6 CG ASN A 21 38.331 42.871-384.065 1.00196.45 C ANISOU 6 CG ASN A 21 23856 26290 24496 2408 2196 1454 C ATOM 7 OD1 ASN A 21 37.821 41.889-384.598 1.00197.29 O ANISOU 7 OD1 ASN A 21 23792 26618 24550 2493 2331 1592 O ATOM 8 ND2 ASN A 21 38.133 44.113-384.502 1.00195.76 N ANISOU 8 ND2 ASN A 21 23705 26048 24628 2319 2091 1540 N ATOM 9 N ASN A 22 40.357 39.245-383.436 1.00 20.00 N ATOM 10 CA ASN A 22 41.452 38.392-383.884 1.00 20.00 C ATOM 11 C ASN A 22 42.761 38.712-383.168 1.00 20.00 C ATOM 12 O ASN A 22 43.860 38.462-383.826 1.00254.18 O ANISOU 12 O ASN A 22 31650 33792 31136 1860 2028 1018 O ATOM 13 CB ASN A 22 41.639 38.510-385.398 1.00 20.00 C ATOM 14 CG ASN A 22 40.507 37.867-386.176 1.00 20.00 C ATOM 15 OD1 ASN A 22 39.813 36.986-385.669 1.00 20.00 O ATOM 16 ND2 ASN A 22 40.316 38.306-387.414 1.00 20.00 N ATOM 17 N SER A 23 42.722 39.142-382.014 1.00 20.00 N ATOM 18 CA SER A 23 43.820 39.710-381.241 1.00 20.00 C ATOM 19 C SER A 23 44.038 41.179-381.588 1.00 20.00 C ATOM 20 O SER A 23 45.278 41.603-381.421 1.00208.55 O ANISOU 20 O SER A 23 26321 27532 25386 1610 1732 647 O ATOM 21 CB SER A 23 45.108 38.917-381.474 1.00 20.00 C ATOM 22 OG SER A 23 45.541 39.039-382.818 1.00 20.00 O ATOM 23 N THR A 24 43.076 41.922-381.837 1.00174.40 N ANISOU 23 N THR A 24 21903 23194 21167 1942 1862 707 N ATOM 24 CA THR A 24 43.093 43.381-381.830 1.00173.40 C ANISOU 24 CA THR A 24 21796 22849 21241 1843 1757 759 C ATOM 25 C THR A 24 44.178 43.991-382.718 1.00171.27 C ANISOU 25 C THR A 24 21516 22530 21027 1598 1654 820 C ATOM 26 O THR A 24 45.066 44.687-382.241 1.00276.83 O ANISOU 26 O THR A 24 35042 35792 34348 1455 1557 709 O ATOM 27 CB THR A 24 43.141 44.047-380.425 1.00174.52 C ANISOU 27 CB THR A 24 22160 22769 21382 1888 1683 581 C ATOM 28 OG1 THR A 24 43.356 45.459-380.535 1.00173.61 O ANISOU 28 OG1 THR A 24 22071 22452 21439 1784 1575 641 O ATOM 29 CG2 THR A 24 44.237 43.420-379.559 1.00174.83 C ANISOU 29 CG2 THR A 24 22401 22766 21262 1787 1616 379 C ATOM 30 N GLY A 25 44.123 43.684-384.012 1.00 91.93 N ANISOU 30 N GLY A 25 11277 12568 11084 1555 1679 1001 N ATOM 31 CA GLY A 25 45.129 44.161-384.942 1.00 83.53 C ANISOU 31 CA GLY A 25 10198 11473 10065 1357 1593 1056 C ATOM 32 C GLY A 25 45.071 45.675-385.007 1.00 73.33 C ANISOU 32 C GLY A 25 8951 9991 8921 1266 1469 1077 C ATOM 33 O GLY A 25 44.461 46.242-385.915 1.00 65.50 O ANISOU 33 O GLY A 25 7850 8986 8050 1195 1423 1192 O ATOM 34 N THR A 26 45.703 46.336-384.041 1.00 73.25 N ANISOU 34 N THR A 26 9104 9827 8900 1274 1409 966 N ATOM 35 CA THR A 26 45.684 47.793-383.989 1.00 65.31 C ANISOU 35 CA THR A 26 8148 8653 8014 1208 1294 995 C ATOM 36 C THR A 26 46.998 48.143-384.653 1.00 62.16 C ANISOU 36 C THR A 26 7785 8241 7593 1022 1209 1011 C ATOM 37 O THR A 26 48.063 47.792-384.145 1.00 69.73 O ANISOU 37 O THR A 26 8861 9196 8436 923 1188 927 O ATOM 38 CB THR A 26 45.701 48.414-382.579 1.00 65.78 C ANISOU 38 CB THR A 26 8390 8538 8064 1249 1249 886 C ATOM 39 OG1 THR A 26 44.488 48.101-381.884 1.00 72.50 O ANISOU 39 OG1 THR A 26 9226 9395 8925 1452 1333 853 O ATOM 40 CG2 THR A 26 45.840 49.919-382.683 1.00 60.36 C ANISOU 40 CG2 THR A 26 7735 7704 7495 1196 1138 949 C ATOM 41 N ALA A 27 46.931 48.830-385.789 1.00 71.87 N ANISOU 41 N ALA A 27 8910 9469 8930 978 1153 1116 N ATOM 42 CA ALA A 27 48.146 49.288-386.450 1.00 70.71 C ANISOU 42 CA ALA A 27 8803 9311 8753 833 1072 1126 C ATOM 43 C ALA A 27 48.543 50.634-385.879 1.00 73.47 C ANISOU 43 C ALA A 27 9274 9517 9123 793 969 1108 C ATOM 44 O ALA A 27 47.842 51.190-385.035 1.00 78.59 O ANISOU 44 O ALA A 27 9971 10065 9826 876 957 1096 O ATOM 45 CB ALA A 27 47.951 49.383-387.954 1.00 66.58 C ANISOU 45 CB ALA A 27 8131 8839 8326 812 1047 1224 C ATOM 46 N ALA A 28 49.674 51.149-386.337 1.00 69.64 N ANISOU 46 N ALA A 28 8838 9033 8588 681 900 1119 N ATOM 47 CA ALA A 28 50.148 52.455-385.915 1.00 69.74 C ANISOU 47 CA ALA A 28 8955 8939 8603 643 807 1131 C ATOM 48 C ALA A 28 50.997 53.021-387.032 1.00 68.44 C ANISOU 48 C ALA A 28 8768 8829 8406 572 739 1171 C ATOM 49 O ALA A 28 51.901 52.353-387.538 1.00 68.77 O ANISOU 49 O ALA A 28 8799 8967 8362 503 770 1160 O ATOM 50 CB ALA A 28 50.955 52.351-384.630 1.00 73.97 C ANISOU 50 CB ALA A 28 9641 9412 9054 576 815 1076 C ATOM 51 N LEU A 29 50.695 54.254-387.418 1.00 46.03 N ANISOU 51 N LEU A 29 5924 5936 5629 604 643 1213 N ATOM 52 CA LEU A 29 51.356 54.886-388.547 1.00 46.41 C ANISOU 52 CA LEU A 29 5957 6033 5642 569 564 1231 C ATOM 53 C LEU A 29 51.580 56.354-388.272 1.00 44.18 C ANISOU 53 C LEU A 29 5756 5696 5336 583 463 1264 C ATOM 54 O LEU A 29 50.712 57.041-387.741 1.00 44.45 O ANISOU 54 O LEU A 29 5791 5647 5450 650 421 1292 O ATOM 55 CB LEU A 29 50.505 54.736-389.805 1.00 46.36 C ANISOU 55 CB LEU A 29 5811 6045 5758 611 529 1245 C ATOM 56 CG LEU A 29 50.913 55.595-390.997 1.00 43.23 C ANISOU 56 CG LEU A 29 5409 5660 5357 600 410 1239 C ATOM 57 CD1 LEU A 29 51.887 54.827-391.882 1.00 44.10 C ANISOU 57 CD1 LEU A 29 5513 5852 5392 553 448 1212 C ATOM 58 CD2 LEU A 29 49.670 56.013-391.777 1.00 45.71 C ANISOU 58 CD2 LEU A 29 5599 5924 5846 648 320 1262 C ATOM 59 N ALA A 30 52.752 56.839-388.640 1.00 57.04 N ANISOU 59 N ALA A 30 7445 7386 6841 535 427 1272 N ATOM 60 CA ALA A 30 53.037 58.252-388.507 1.00 59.36 C ANISOU 60 CA ALA A 30 7809 7662 7082 561 333 1318 C ATOM 61 C ALA A 30 53.790 58.711-389.737 1.00 60.56 C ANISOU 61 C ALA A 30 7958 7913 7139 567 267 1297 C ATOM 62 O ALA A 30 54.713 58.038-390.201 1.00 57.12 O ANISOU 62 O ALA A 30 7522 7565 6617 523 323 1274 O ATOM 63 CB ALA A 30 53.840 58.521-387.248 1.00 59.38 C ANISOU 63 CB ALA A 30 7925 7634 7003 507 373 1372 C ATOM 64 N GLY A 31 53.383 59.856-390.272 1.00 54.02 N ANISOU 64 N GLY A 31 7129 7076 6322 634 141 1299 N ATOM 65 CA GLY A 31 54.015 60.396-391.458 1.00 51.43 C ANISOU 65 CA GLY A 31 6814 6832 5894 665 56 1254 C ATOM 66 C GLY A 31 53.360 61.670-391.944 1.00 54.65 C ANISOU 66 C GLY A 31 7218 7222 6326 743 -107 1241 C ATOM 67 O GLY A 31 52.439 62.195-391.317 1.00 53.26 O ANISOU 67 O GLY A 31 7020 6976 6241 774 -150 1289 O ATOM 68 N LYS A 32 53.835 62.152-393.086 1.00 66.31 N ANISOU 68 N LYS A 32 8716 8765 7715 783 -204 1169 N ATOM 69 CA LYS A 32 53.408 63.431-393.634 1.00 65.53 C ANISOU 69 CA LYS A 32 8628 8675 7594 861 -383 1136 C ATOM 70 C LYS A 32 52.111 63.294-394.423 1.00 60.63 C ANISOU 70 C LYS A 32 7888 7958 7192 857 -498 1077 C ATOM 71 O LYS A 32 51.961 62.382-395.232 1.00 60.40 O ANISOU 71 O LYS A 32 7792 7886 7270 814 -479 1019 O ATOM 72 CB LYS A 32 54.519 63.990-394.525 1.00 66.68 C ANISOU 72 CB LYS A 32 8862 8938 7534 922 -444 1063 C ATOM 73 CG LYS A 32 55.894 63.432-394.169 1.00 64.40 C ANISOU 73 CG LYS A 32 8635 8752 7081 896 -284 1107 C ATOM 74 CD LYS A 32 57.032 64.290-394.696 1.00 69.81 C ANISOU 74 CD LYS A 32 9416 9594 7515 991 -325 1082 C ATOM 75 CE LYS A 32 57.175 64.177-396.202 1.00 76.20 C ANISOU 75 CE LYS A 32 10234 10409 8310 1054 -422 919 C ATOM 76 NZ LYS A 32 58.215 65.114-396.704 1.00 74.78 N ANISOU 76 NZ LYS A 32 10158 10394 7861 1182 -470 879 N ATOM 77 N PHE A 33 51.174 64.207-394.185 1.00 57.78 N ANISOU 77 N PHE A 33 7486 7564 6902 899 -620 1109 N ATOM 78 CA PHE A 33 49.892 64.179-394.886 1.00 62.37 C ANISOU 78 CA PHE A 33 7927 8065 7704 887 -742 1077 C ATOM 79 C PHE A 33 49.454 65.543-395.414 1.00 59.43 C ANISOU 79 C PHE A 33 7551 7717 7312 949 -971 1035 C ATOM 80 O PHE A 33 49.977 66.579-395.007 1.00 60.60 O ANISOU 80 O PHE A 33 7802 7950 7273 1021 -1022 1057 O ATOM 81 CB PHE A 33 48.797 63.592-393.997 1.00 56.76 C ANISOU 81 CB PHE A 33 7105 7285 7177 870 -643 1177 C ATOM 82 CG PHE A 33 49.049 62.175-393.598 1.00 50.53 C ANISOU 82 CG PHE A 33 6303 6476 6419 813 -442 1199 C ATOM 83 CD1 PHE A 33 49.143 61.827-392.264 1.00 51.47 C ANISOU 83 CD1 PHE A 33 6470 6586 6500 820 -296 1270 C ATOM 84 CD2 PHE A 33 49.200 61.190-394.561 1.00 50.51 C ANISOU 84 CD2 PHE A 33 6246 6462 6484 758 -409 1146 C ATOM 85 CE1 PHE A 33 49.377 60.519-391.894 1.00 53.30 C ANISOU 85 CE1 PHE A 33 6694 6813 6744 771 -130 1274 C ATOM 86 CE2 PHE A 33 49.435 59.875-394.201 1.00 51.62 C ANISOU 86 CE2 PHE A 33 6369 6607 6636 716 -230 1171 C ATOM 87 CZ PHE A 33 49.525 59.539-392.866 1.00 51.16 C ANISOU 87 CZ PHE A 33 6360 6558 6522 723 -95 1228 C ATOM 88 N GLN A 34 48.483 65.520-396.321 1.00 53.51 N ANISOU 88 N GLN A 34 6672 6899 6761 918 -1114 984 N ATOM 89 CA GLN A 34 47.996 66.728-396.972 1.00 53.84 C ANISOU 89 CA GLN A 34 6691 6958 6808 960 -1364 921 C ATOM 90 C GLN A 34 47.106 67.518-396.027 1.00 55.25 C ANISOU 90 C GLN A 34 6802 7159 7030 1014 -1406 1042 C ATOM 91 O GLN A 34 46.815 68.690-396.266 1.00 58.79 O ANISOU 91 O GLN A 34 7250 7661 7428 1072 -1604 1018 O ATOM 92 CB GLN A 34 47.209 66.355-398.230 1.00 54.02 C ANISOU 92 CB GLN A 34 6577 6878 7070 882 -1509 840 C ATOM 93 CG GLN A 34 47.015 67.489-399.225 1.00 57.38 C ANISOU 93 CG GLN A 34 7012 7311 7478 908 -1801 710 C ATOM 94 CD GLN A 34 46.145 67.084-400.402 1.00 61.91 C ANISOU 94 CD GLN A 34 7433 7751 8340 804 -1953 649 C ATOM 95 OE1 GLN A 34 44.970 66.750-400.235 1.00 63.70 O ANISOU 95 OE1 GLN A 34 7463 7923 8816 742 -1950 763 O ATOM 96 NE2 GLN A 34 46.716 67.120-401.601 1.00 61.92 N ANISOU 96 NE2 GLN A 34 7520 7695 8313 790 -2088 476 N ATOM 97 N TRP A 35 46.690 66.873-394.943 1.00 57.48 N ANISOU 97 N TRP A 35 7035 7405 7398 1008 -1222 1167 N ATOM 98 CA TRP A 35 45.664 67.437-394.074 1.00 59.25 C ANISOU 98 CA TRP A 35 7171 7626 7716 1070 -1246 1287 C ATOM 99 C TRP A 35 45.802 66.933-392.633 1.00 57.78 C ANISOU 99 C TRP A 35 7042 7411 7500 1100 -1023 1398 C ATOM 100 O TRP A 35 45.974 65.738-392.401 1.00 56.79 O ANISOU 100 O TRP A 35 6914 7241 7422 1046 -850 1396 O ATOM 101 CB TRP A 35 44.286 67.086-394.649 1.00 54.85 C ANISOU 101 CB TRP A 35 6389 7013 7439 1026 -1325 1310 C ATOM 102 CG TRP A 35 43.131 67.904-394.139 1.00 56.15 C ANISOU 102 CG TRP A 35 6426 7199 7711 1101 -1422 1415 C ATOM 103 CD1 TRP A 35 41.985 67.430-393.587 1.00 61.54 C ANISOU 103 CD1 TRP A 35 6940 7851 8591 1125 -1334 1532 C ATOM 104 CD2 TRP A 35 43.009 69.332-394.157 1.00 60.50 C ANISOU 104 CD2 TRP A 35 6996 7823 8167 1177 -1627 1420 C ATOM 105 NE1 TRP A 35 41.152 68.469-393.252 1.00 64.01 N ANISOU 105 NE1 TRP A 35 7161 8208 8951 1211 -1467 1614 N ATOM 106 CE2 TRP A 35 41.756 69.646-393.586 1.00 60.63 C ANISOU 106 CE2 TRP A 35 6845 7844 8346 1240 -1653 1549 C ATOM 107 CE3 TRP A 35 43.831 70.372-394.586 1.00 67.17 C ANISOU 107 CE3 TRP A 35 7981 8748 8791 1215 -1786 1333 C ATOM 108 CZ2 TRP A 35 41.312 70.952-393.438 1.00 66.09 C ANISOU 108 CZ2 TRP A 35 7503 8613 8997 1329 -1839 1599 C ATOM 109 CZ3 TRP A 35 43.390 71.672-394.438 1.00 70.10 C ANISOU 109 CZ3 TRP A 35 8326 9204 9106 1305 -1972 1377 C ATOM 110 CH2 TRP A 35 42.138 71.950-393.867 1.00 72.69 C ANISOU 110 CH2 TRP A 35 8480 9528 9610 1357 -2001 1511 C ATOM 111 N GLY A 36 45.738 67.851-391.671 1.00 55.52 N ANISOU 111 N GLY A 36 6815 7145 7134 1190 -1039 1492 N ATOM 112 CA GLY A 36 45.852 67.516-390.259 1.00 60.23 C ANISOU 112 CA GLY A 36 7485 7685 7716 1224 -857 1590 C ATOM 113 C GLY A 36 44.637 66.727-389.828 1.00 52.43 C ANISOU 113 C GLY A 36 6352 6623 6945 1243 -765 1638 C ATOM 114 O GLY A 36 43.757 66.486-390.646 1.00 62.08 O ANISOU 114 O GLY A 36 7406 7855 8327 1221 -839 1618 O ATOM 115 N PRO A 37 44.533 66.375-388.535 1.00 52.91 N ANISOU 115 N PRO A 37 6472 6610 7020 1293 -612 1707 N ATOM 116 CA PRO A 37 45.217 66.872-387.340 1.00 53.13 C ANISOU 116 CA PRO A 37 6669 6591 6926 1336 -550 1775 C ATOM 117 C PRO A 37 46.709 66.663-387.340 1.00 52.20 C ANISOU 117 C PRO A 37 6709 6498 6625 1246 -488 1735 C ATOM 118 O PRO A 37 47.195 65.613-387.758 1.00 48.68 O ANISOU 118 O PRO A 37 6264 6062 6169 1155 -401 1653 O ATOM 119 CB PRO A 37 44.616 65.997-386.242 1.00 53.01 C ANISOU 119 CB PRO A 37 6649 6466 7026 1380 -385 1802 C ATOM 120 CG PRO A 37 44.495 64.693-386.927 1.00 52.36 C ANISOU 120 CG PRO A 37 6479 6408 7008 1300 -302 1714 C ATOM 121 CD PRO A 37 43.809 65.135-388.204 1.00 50.70 C ANISOU 121 CD PRO A 37 6100 6278 6886 1293 -460 1705 C ATOM 122 N ALA A 38 47.418 67.667-386.838 1.00 54.32 N ANISOU 122 N ALA A 38 7099 6787 6753 1279 -528 1814 N ATOM 123 CA ALA A 38 48.854 67.582-386.642 1.00 54.02 C ANISOU 123 CA ALA A 38 7201 6783 6541 1204 -457 1820 C ATOM 124 C ALA A 38 49.149 67.108-385.225 1.00 51.97 C ANISOU 124 C ALA A 38 7040 6390 6315 1178 -310 1889 C ATOM 125 O ALA A 38 48.565 67.596-384.262 1.00 54.80 O ANISOU 125 O ALA A 38 7424 6647 6751 1259 -310 1982 O ATOM 126 CB ALA A 38 49.507 68.939-386.898 1.00 58.48 C ANISOU 126 CB ALA A 38 7834 7463 6922 1257 -575 1888 C ATOM 127 N PHE A 39 50.053 66.148-385.112 1.00 49.61 N ANISOU 127 N PHE A 39 6797 6087 5965 1067 -195 1839 N ATOM 128 CA PHE A 39 50.451 65.629-383.816 1.00 50.26 C ANISOU 128 CA PHE A 39 6979 6038 6079 1016 -75 1882 C ATOM 129 C PHE A 39 49.249 65.272-382.955 1.00 51.00 C ANISOU 129 C PHE A 39 7051 5979 6349 1096 -35 1874 C ATOM 130 O PHE A 39 49.124 65.727-381.822 1.00 51.85 O ANISOU 130 O PHE A 39 7244 5951 6504 1143 -20 1962 O ATOM 131 CB PHE A 39 51.361 66.625-383.103 1.00 53.05 C ANISOU 131 CB PHE A 39 7449 6382 6325 1007 -88 2030 C ATOM 132 CG PHE A 39 52.658 66.858-383.815 1.00 50.78 C ANISOU 132 CG PHE A 39 7188 6262 5845 939 -94 2046 C ATOM 133 CD1 PHE A 39 52.838 67.969-384.616 1.00 52.46 C ANISOU 133 CD1 PHE A 39 7387 6624 5921 1016 -205 2085 C ATOM 134 CD2 PHE A 39 53.690 65.951-383.707 1.00 49.89 C ANISOU 134 CD2 PHE A 39 7106 6171 5678 811 9 2016 C ATOM 135 CE1 PHE A 39 54.035 68.175-385.278 1.00 52.63 C ANISOU 135 CE1 PHE A 39 7437 6814 5746 983 -200 2092 C ATOM 136 CE2 PHE A 39 54.888 66.155-384.368 1.00 53.24 C ANISOU 136 CE2 PHE A 39 7541 6767 5920 768 16 2040 C ATOM 137 CZ PHE A 39 55.059 67.267-385.154 1.00 55.35 C ANISOU 137 CZ PHE A 39 7805 7182 6045 863 -82 2076 C ATOM 138 N GLN A 40 48.376 64.439-383.504 1.00 71.60 N ANISOU 138 N GLN A 40 9542 8609 9053 1119 -11 1777 N ATOM 139 CA GLN A 40 47.246 63.909-382.759 1.00 78.26 C ANISOU 139 CA GLN A 40 10352 9340 10044 1210 53 1757 C ATOM 140 C GLN A 40 47.021 62.460-383.144 1.00 75.17 C ANISOU 140 C GLN A 40 9888 8986 9687 1164 151 1643 C ATOM 141 O GLN A 40 47.113 62.110-384.317 1.00 70.35 O ANISOU 141 O GLN A 40 9179 8496 9055 1110 128 1598 O ATOM 142 CB GLN A 40 45.985 64.722-383.043 1.00 83.16 C ANISOU 142 CB GLN A 40 10851 9980 10767 1350 -41 1816 C ATOM 143 CG GLN A 40 45.979 66.096-382.403 1.00 91.06 C ANISOU 143 CG GLN A 40 11921 10926 11750 1436 -125 1946 C ATOM 144 CD GLN A 40 44.662 66.815-382.600 1.00101.26 C ANISOU 144 CD GLN A 40 13077 12245 13153 1583 -216 2007 C ATOM 145 OE1 GLN A 40 43.688 66.225-383.074 1.00101.13 O ANISOU 145 OE1 GLN A 40 12908 12269 13246 1623 -200 1960 O ATOM 146 NE2 GLN A 40 44.621 68.094-382.236 1.00 99.37 N ANISOU 146 NE2 GLN A 40 12876 11994 12885 1668 -312 2130 N ATOM 147 N ILE A 41 46.731 61.620-382.154 1.00 90.15 N ANISOU 147 N ILE A 41 11840 10779 11635 1193 258 1594 N ATOM 148 CA ILE A 41 46.478 60.210-382.414 1.00 93.60 C ANISOU 148 CA ILE A 41 12211 11268 12085 1171 360 1494 C ATOM 149 C ILE A 41 45.045 60.007-382.890 1.00100.71 C ANISOU 149 C ILE A 41 12937 12223 13106 1297 372 1506 C ATOM 150 O ILE A 41 44.278 59.258-382.285 1.00110.27 O ANISOU 150 O ILE A 41 14127 13400 14370 1394 469 1468 O ATOM 151 CB ILE A 41 46.709 59.335-381.161 1.00101.68 C ANISOU 151 CB ILE A 41 13365 12172 13095 1165 462 1417 C ATOM 152 CG1 ILE A 41 48.024 59.698-380.473 1.00104.79 C ANISOU 152 CG1 ILE A 41 13924 12480 13411 1040 438 1439 C ATOM 153 CG2 ILE A 41 46.710 57.847-381.530 1.00 99.28 C ANISOU 153 CG2 ILE A 41 13003 11966 12754 1125 560 1314 C ATOM 154 CD1 ILE A 41 49.175 58.798-380.867 1.00 96.77 C ANISOU 154 CD1 ILE A 41 12925 11560 12285 879 478 1377 C ATOM 155 N LYS A 42 44.678 60.683-383.970 1.00 52.89 N ANISOU 155 N LYS A 42 6749 6255 7091 1300 269 1561 N ATOM 156 CA LYS A 42 43.369 60.466-384.563 1.00 53.00 C ANISOU 156 CA LYS A 42 6564 6336 7239 1388 271 1593 C ATOM 157 C LYS A 42 43.300 59.042-385.116 1.00 52.19 C ANISOU 157 C LYS A 42 6375 6315 7139 1339 381 1537 C ATOM 158 O LYS A 42 44.243 58.569-385.753 1.00 52.32 O ANISOU 158 O LYS A 42 6426 6381 7072 1212 384 1488 O ATOM 159 CB LYS A 42 43.101 61.496-385.665 1.00 55.23 C ANISOU 159 CB LYS A 42 6728 6687 7570 1370 107 1652 C ATOM 160 CG LYS A 42 41.687 61.455-386.260 1.00 56.31 C ANISOU 160 CG LYS A 42 6632 6886 7876 1449 81 1715 C ATOM 161 CD LYS A 42 40.597 61.566-385.192 1.00 53.19 C ANISOU 161 CD LYS A 42 6198 6444 7568 1626 150 1777 C ATOM 162 CE LYS A 42 39.252 61.912-385.814 1.00 61.77 C ANISOU 162 CE LYS A 42 7034 7612 8824 1704 84 1877 C ATOM 163 NZ LYS A 42 38.977 61.117-387.044 1.00 66.18 N ANISOU 163 NZ LYS A 42 7415 8266 9465 1606 90 1880 N ATOM 164 N GLN A 43 42.193 58.353-384.857 1.00 58.99 N ANISOU 164 N GLN A 43 7122 7203 8087 1453 479 1555 N ATOM 165 CA GLN A 43 42.024 56.994-385.355 1.00 54.94 C ANISOU 165 CA GLN A 43 6514 6789 7573 1428 594 1529 C ATOM 166 C GLN A 43 41.298 56.981-386.691 1.00 59.87 C ANISOU 166 C GLN A 43 6907 7510 8330 1402 543 1615 C ATOM 167 O GLN A 43 40.470 57.849-386.969 1.00 71.56 O ANISOU 167 O GLN A 43 8265 8992 9932 1456 450 1696 O ATOM 168 CB GLN A 43 41.263 56.139-384.345 1.00 59.84 C ANISOU 168 CB GLN A 43 7137 7408 8190 1579 745 1503 C ATOM 169 CG GLN A 43 41.022 54.713-384.811 1.00 61.20 C ANISOU 169 CG GLN A 43 7203 7711 8340 1578 875 1494 C ATOM 170 CD GLN A 43 40.404 53.845-383.735 1.00 62.83 C ANISOU 170 CD GLN A 43 7447 7932 8495 1743 1024 1440 C ATOM 171 OE1 GLN A 43 39.353 54.170-383.181 1.00 61.84 O ANISOU 171 OE1 GLN A 43 7262 7794 8442 1916 1058 1485 O ATOM 172 NE2 GLN A 43 41.055 52.727-383.435 1.00 60.88 N ANISOU 172 NE2 GLN A 43 7298 7723 8111 1704 1111 1340 N ATOM 173 N VAL A 44 41.604 55.983-387.510 1.00 55.39 N ANISOU 173 N VAL A 44 6276 7019 7749 1315 599 1603 N ATOM 174 CA VAL A 44 41.041 55.879-388.849 1.00 55.57 C ANISOU 174 CA VAL A 44 6090 7107 7916 1261 545 1687 C ATOM 175 C VAL A 44 40.582 54.453-389.122 1.00 55.61 C ANISOU 175 C VAL A 44 5969 7214 7947 1284 702 1734 C ATOM 176 O VAL A 44 41.268 53.504-388.758 1.00 64.64 O ANISOU 176 O VAL A 44 7219 8388 8952 1268 810 1664 O ATOM 177 CB VAL A 44 42.089 56.267-389.908 1.00 54.49 C ANISOU 177 CB VAL A 44 6011 6947 7745 1109 415 1638 C ATOM 178 CG1 VAL A 44 41.649 55.799-391.289 1.00 54.69 C ANISOU 178 CG1 VAL A 44 5845 7014 7920 1038 383 1705 C ATOM 179 CG2 VAL A 44 42.361 57.773-389.881 1.00 54.85 C ANISOU 179 CG2 VAL A 44 6136 6928 7775 1100 241 1618 C ATOM 180 N THR A 45 39.434 54.301-389.775 1.00 72.51 N ANISOU 180 N THR A 45 7871 9417 10261 1320 711 1864 N ATOM 181 CA THR A 45 38.881 52.969-390.018 1.00 78.03 C ANISOU 181 CA THR A 45 8425 10235 10988 1362 875 1947 C ATOM 182 C THR A 45 38.591 52.667-391.491 1.00 80.78 C ANISOU 182 C THR A 45 8570 10613 11510 1249 826 2066 C ATOM 183 O THR A 45 38.787 51.541-391.948 1.00 77.30 O ANISOU 183 O THR A 45 8082 10241 11046 1217 932 2106 O ATOM 184 CB THR A 45 37.613 52.736-389.186 1.00 80.17 C ANISOU 184 CB THR A 45 8577 10587 11297 1556 1003 2029 C ATOM 185 OG1 THR A 45 37.955 52.755-387.794 1.00 70.27 O ANISOU 185 OG1 THR A 45 7536 9287 9875 1665 1066 1900 O ATOM 186 CG2 THR A 45 36.985 51.396-389.532 1.00 81.13 C ANISOU 186 CG2 THR A 45 8523 10863 11441 1611 1176 2144 C ATOM 187 N ASN A 46 38.128 53.670-392.230 1.00117.11 N ANISOU 187 N ASN A 46 13052 15155 16290 1187 656 2123 N ATOM 188 CA ASN A 46 37.845 53.495-393.651 1.00117.67 C ANISOU 188 CA ASN A 46 12937 15212 16559 1062 575 2226 C ATOM 189 C ASN A 46 38.915 54.132-394.521 1.00116.68 C ANISOU 189 C ASN A 46 12946 14968 16419 915 389 2107 C ATOM 190 O ASN A 46 39.789 54.840-394.025 1.00170.68 O ANISOU 190 O ASN A 46 19997 21757 23098 915 320 1967 O ATOM 191 CB ASN A 46 36.493 54.105-394.013 1.00119.71 C ANISOU 191 CB ASN A 46 12934 15490 17059 1083 493 2380 C ATOM 192 CG ASN A 46 35.438 53.854-392.960 1.00120.91 C ANISOU 192 CG ASN A 46 12979 15762 17201 1272 654 2478 C ATOM 193 OD1 ASN A 46 35.565 52.949-392.135 1.00120.47 O ANISOU 193 OD1 ASN A 46 13007 15785 16982 1385 847 2450 O ATOM 194 ND2 ASN A 46 34.381 54.659-392.983 1.00122.65 N ANISOU 194 ND2 ASN A 46 13010 16002 17590 1318 569 2587 N ATOM 195 N GLU A 47 38.845 53.877-395.823 1.00105.86 N ANISOU 195 N GLU A 47 11452 13552 15218 797 311 2168 N ATOM 196 CA GLU A 47 39.685 54.592-396.770 1.00103.53 C ANISOU 196 CA GLU A 47 11263 13136 14937 676 110 2051 C ATOM 197 C GLU A 47 39.048 55.950-396.993 1.00100.50 C ANISOU 197 C GLU A 47 10803 12698 14683 659 -105 2047 C ATOM 198 O GLU A 47 39.679 56.983-396.789 1.00 97.14 O ANISOU 198 O GLU A 47 10543 12231 14133 663 -238 1915 O ATOM 199 CB GLU A 47 39.782 53.838-398.096 1.00113.43 C ANISOU 199 CB GLU A 47 12418 14332 16350 564 91 2113 C ATOM 200 CG GLU A 47 40.765 54.446-399.086 1.00105.59 C ANISOU 200 CG GLU A 47 11566 13207 15345 464 -102 1964 C ATOM 201 CD GLU A 47 40.453 54.066-400.523 1.00112.68 C ANISOU 201 CD GLU A 47 12316 13994 16503 346 -196 2041 C ATOM 202 OE1 GLU A 47 41.201 53.249-401.101 1.00113.80 O ANISOU 202 OE1 GLU A 47 12525 14099 16613 313 -133 2025 O ATOM 203 OE2 GLU A 47 39.453 54.576-401.075 1.00110.50 O ANISOU 203 OE2 GLU A 47 11850 13660 16474 285 -337 2127 O ATOM 204 N VAL A 48 37.780 55.929-397.399 1.00 85.60 N ANISOU 204 N VAL A 48 8651 10831 13044 644 -135 2209 N ATOM 205 CA VAL A 48 37.004 57.145-397.637 1.00 88.24 C ANISOU 205 CA VAL A 48 8861 11136 13532 624 -345 2233 C ATOM 206 C VAL A 48 36.918 57.990-396.374 1.00 78.87 C ANISOU 206 C VAL A 48 7775 10006 12186 762 -334 2188 C ATOM 207 O VAL A 48 36.439 59.124-396.402 1.00 78.56 O ANISOU 207 O VAL A 48 7675 9957 12217 770 -513 2189 O ATOM 208 CB VAL A 48 35.580 56.818-398.123 1.00 89.16 C ANISOU 208 CB VAL A 48 8637 11293 13946 594 -338 2456 C ATOM 209 CG1 VAL A 48 34.829 58.080-398.503 1.00 95.54 C ANISOU 209 CG1 VAL A 48 9300 12070 14930 549 -589 2477 C ATOM 210 CG2 VAL A 48 35.633 55.855-399.300 1.00 98.52 C ANISOU 210 CG2 VAL A 48 9715 12413 15305 462 -319 2537 C ATOM 211 N ASP A 49 37.388 57.427-395.266 1.00 62.79 N ANISOU 211 N ASP A 49 5894 8023 9940 870 -133 2150 N ATOM 212 CA ASP A 49 37.380 58.126-393.990 1.00 58.50 C ANISOU 212 CA ASP A 49 5472 7505 9251 1004 -106 2108 C ATOM 213 C ASP A 49 38.746 58.702-393.646 1.00 54.77 C ANISOU 213 C ASP A 49 5291 6973 8547 984 -166 1939 C ATOM 214 O ASP A 49 38.855 59.585-392.806 1.00 56.74 O ANISOU 214 O ASP A 49 5649 7213 8696 1064 -208 1906 O ATOM 215 CB ASP A 49 36.905 57.199-392.873 1.00 62.78 C ANISOU 215 CB ASP A 49 5994 8132 9726 1149 143 2174 C ATOM 216 CG ASP A 49 36.438 57.958-391.649 1.00 68.25 C ANISOU 216 CG ASP A 49 6733 8837 10360 1308 158 2180 C ATOM 217 OD1 ASP A 49 36.049 59.141-391.803 1.00 65.95 O ANISOU 217 OD1 ASP A 49 6383 8525 10151 1311 -19 2204 O ATOM 218 OD2 ASP A 49 36.453 57.374-390.540 1.00 75.35 O ANISOU 218 OD2 ASP A 49 7730 9763 11135 1434 337 2158 O ATOM 219 N LEU A 50 39.792 58.189-394.276 1.00 50.05 N ANISOU 219 N LEU A 50 4810 6340 7865 886 -159 1849 N ATOM 220 CA LEU A 50 41.101 58.791-394.095 1.00 55.98 C ANISOU 220 CA LEU A 50 5809 7054 8406 863 -225 1708 C ATOM 221 C LEU A 50 41.292 59.898-395.121 1.00 50.60 C ANISOU 221 C LEU A 50 5130 6323 7771 793 -474 1643 C ATOM 222 O LEU A 50 41.910 60.919-394.827 1.00 52.51 O ANISOU 222 O LEU A 50 5523 6563 7866 821 -577 1567 O ATOM 223 CB LEU A 50 42.236 57.760-394.141 1.00 54.72 C ANISOU 223 CB LEU A 50 5787 6902 8101 816 -90 1639 C ATOM 224 CG LEU A 50 42.837 57.257-395.451 1.00 53.52 C ANISOU 224 CG LEU A 50 5627 6717 7990 709 -139 1596 C ATOM 225 CD1 LEU A 50 43.591 58.345-396.167 1.00 53.87 C ANISOU 225 CD1 LEU A 50 5787 6710 7970 665 -342 1480 C ATOM 226 CD2 LEU A 50 43.782 56.105-395.152 1.00 54.63 C ANISOU 226 CD2 LEU A 50 5879 6900 7978 700 38 1563 C ATOM 227 N VAL A 51 40.759 59.703-396.325 1.00 54.03 N ANISOU 227 N VAL A 51 5399 6719 8410 705 -578 1675 N ATOM 228 CA VAL A 51 40.766 60.766-397.324 1.00 52.42 C ANISOU 228 CA VAL A 51 5182 6458 8276 640 -844 1600 C ATOM 229 C VAL A 51 40.037 61.972-396.758 1.00 57.73 C ANISOU 229 C VAL A 51 5797 7171 8965 714 -970 1640 C ATOM 230 O VAL A 51 40.544 63.086-396.764 1.00 60.09 O ANISOU 230 O VAL A 51 6225 7476 9131 738 -1128 1546 O ATOM 231 CB VAL A 51 40.091 60.337-398.625 1.00 58.23 C ANISOU 231 CB VAL A 51 5717 7122 9286 524 -944 1651 C ATOM 232 CG1 VAL A 51 40.134 61.466-399.622 1.00 61.70 C ANISOU 232 CG1 VAL A 51 6165 7489 9788 458 -1245 1540 C ATOM 233 CG2 VAL A 51 40.783 59.126-399.189 1.00 59.82 C ANISOU 233 CG2 VAL A 51 5969 7281 9478 465 -815 1633 C ATOM 234 N ASN A 52 38.837 61.738-396.254 1.00 83.30 N ANISOU 234 N ASN A 52 8837 10456 12359 766 -892 1790 N ATOM 235 CA ASN A 52 38.100 62.776-395.560 1.00 91.48 C ANISOU 235 CA ASN A 52 9808 11542 13408 865 -976 1852 C ATOM 236 C ASN A 52 39.013 63.570-394.622 1.00 82.53 C ANISOU 236 C ASN A 52 8927 10421 12010 955 -973 1768 C ATOM 237 O ASN A 52 38.871 64.785-394.489 1.00 86.01 O ANISOU 237 O ASN A 52 9384 10886 12411 1003 -1140 1761 O ATOM 238 CB ASN A 52 36.940 62.142-394.779 1.00 97.06 C ANISOU 238 CB ASN A 52 10325 12313 14240 961 -794 2021 C ATOM 239 CG ASN A 52 36.157 63.150-393.953 1.00109.84 C ANISOU 239 CG ASN A 52 11877 13986 15873 1093 -855 2098 C ATOM 240 OD1 ASN A 52 36.051 64.322-394.317 1.00119.71 O ANISOU 240 OD1 ASN A 52 13107 15239 17140 1076 -1084 2072 O ATOM 241 ND2 ASN A 52 35.593 62.690-392.838 1.00105.47 N ANISOU 241 ND2 ASN A 52 11288 13479 15307 1237 -653 2191 N ATOM 242 N THR A 53 39.969 62.884-394.001 1.00 53.80 N ANISOU 242 N THR A 53 5477 6770 8195 971 -789 1715 N ATOM 243 CA THR A 53 40.708 63.452-392.879 1.00 53.31 C ANISOU 243 CA THR A 53 5626 6714 7916 1058 -738 1684 C ATOM 244 C THR A 53 42.163 63.799-393.185 1.00 51.24 C ANISOU 244 C THR A 53 5584 6444 7439 1006 -791 1559 C ATOM 245 O THR A 53 42.693 64.757-392.640 1.00 54.57 O ANISOU 245 O THR A 53 6145 6885 7705 1062 -849 1547 O ATOM 246 CB THR A 53 40.665 62.522-391.645 1.00 52.15 C ANISOU 246 CB THR A 53 5533 6560 7723 1133 -489 1729 C ATOM 247 OG1 THR A 53 39.307 62.199-391.327 1.00 53.15 O ANISOU 247 OG1 THR A 53 5454 6715 8025 1215 -422 1847 O ATOM 248 CG2 THR A 53 41.294 63.197-390.441 1.00 51.51 C ANISOU 248 CG2 THR A 53 5652 6453 7465 1215 -457 1718 C ATOM 249 N PHE A 54 42.818 63.029-394.041 1.00 54.08 N ANISOU 249 N PHE A 54 5974 6787 7788 911 -764 1483 N ATOM 250 CA PHE A 54 44.200 63.319-394.396 1.00 51.66 C ANISOU 250 CA PHE A 54 5861 6491 7275 879 -804 1369 C ATOM 251 C PHE A 54 44.349 63.057-395.881 1.00 52.87 C ANISOU 251 C PHE A 54 5967 6613 7508 796 -950 1278 C ATOM 252 O PHE A 54 45.393 62.606-396.358 1.00 53.48 O ANISOU 252 O PHE A 54 6179 6694 7446 770 -961 1175 O ATOM 253 CB PHE A 54 45.124 62.291-393.761 1.00 49.68 C ANISOU 253 CB PHE A 54 5733 6247 6895 863 -588 1358 C ATOM 254 CG PHE A 54 44.908 62.103-392.289 1.00 51.87 C ANISOU 254 CG PHE A 54 6052 6521 7135 931 -437 1434 C ATOM 255 CD1 PHE A 54 45.724 62.742-391.363 1.00 52.46 C ANISOU 255 CD1 PHE A 54 6299 6603 7032 969 -415 1437 C ATOM 256 CD2 PHE A 54 43.910 61.273-391.828 1.00 52.42 C ANISOU 256 CD2 PHE A 54 5994 6577 7348 964 -315 1506 C ATOM 257 CE1 PHE A 54 45.538 62.561-389.999 1.00 48.79 C ANISOU 257 CE1 PHE A 54 5888 6098 6553 1026 -289 1497 C ATOM 258 CE2 PHE A 54 43.720 61.087-390.473 1.00 52.36 C ANISOU 258 CE2 PHE A 54 6045 6549 7302 1042 -184 1549 C ATOM 259 CZ PHE A 54 44.531 61.735-389.557 1.00 51.74 C ANISOU 259 CZ PHE A 54 6148 6444 7065 1068 -178 1538 C ATOM 260 N GLY A 55 43.289 63.374-396.606 1.00 51.98 N ANISOU 260 N GLY A 55 5656 6463 7630 759 -1066 1321 N ATOM 261 CA GLY A 55 43.040 62.818-397.922 1.00 51.65 C ANISOU 261 CA GLY A 55 5521 6349 7756 657 -1160 1272 C ATOM 262 C GLY A 55 43.351 62.282-399.295 1.00 51.61 C ANISOU 262 C GLY A 55 5654 6304 7653 622 -1313 1107 C ATOM 263 O GLY A 55 42.886 61.225-399.693 1.00 55.34 O ANISOU 263 O GLY A 55 6287 6829 7911 683 -1405 1014 O ATOM 264 N GLN A 56 44.153 63.063-400.013 1.00 64.09 N ANISOU 264 N GLN A 56 7167 7792 9393 534 -1332 1080 N ATOM 265 CA GLN A 56 44.707 62.684-401.301 1.00 54.87 C ANISOU 265 CA GLN A 56 6106 6549 8193 502 -1496 915 C ATOM 266 C GLN A 56 46.206 62.587-401.083 1.00 54.43 C ANISOU 266 C GLN A 56 6281 6558 7842 570 -1386 818 C ATOM 267 O GLN A 56 46.743 63.198-400.162 1.00 54.88 O ANISOU 267 O GLN A 56 6457 6724 7670 650 -1334 819 O ATOM 268 CB GLN A 56 44.338 64.056-401.867 1.00 64.39 C ANISOU 268 CB GLN A 56 7308 7739 9419 506 -1797 812 C ATOM 269 CG GLN A 56 42.843 64.288-402.072 1.00 61.98 C ANISOU 269 CG GLN A 56 6752 7389 9410 434 -1934 916 C ATOM 270 CD GLN A 56 42.278 63.519-403.252 1.00 61.12 C ANISOU 270 CD GLN A 56 6485 7123 9613 299 -2004 936 C ATOM 271 OE1 GLN A 56 42.840 63.531-404.349 1.00 62.71 O ANISOU 271 OE1 GLN A 56 6782 7211 9835 256 -2142 785 O ATOM 272 NE2 GLN A 56 41.152 62.847-403.030 1.00 71.96 N ANISOU 272 NE2 GLN A 56 7616 8490 11235 240 -1908 1132 N ATOM 273 N PRO A 57 46.887 61.802-401.929 1.00 50.84 N ANISOU 273 N PRO A 57 5881 6036 7401 539 -1345 750 N ATOM 274 CA PRO A 57 48.332 61.620-401.810 1.00 56.25 C ANISOU 274 CA PRO A 57 6760 6795 7816 607 -1232 671 C ATOM 275 C PRO A 57 49.092 62.604-402.692 1.00 52.45 C ANISOU 275 C PRO A 57 6435 6308 7186 670 -1433 480 C ATOM 276 O PRO A 57 49.033 62.479-403.911 1.00 52.95 O ANISOU 276 O PRO A 57 6493 6241 7385 637 -1572 375 O ATOM 277 CB PRO A 57 48.546 60.197-402.357 1.00 49.04 C ANISOU 277 CB PRO A 57 5799 5811 7023 553 -1089 711 C ATOM 278 CG PRO A 57 47.162 59.677-402.749 1.00 49.88 C ANISOU 278 CG PRO A 57 5682 5805 7465 455 -1127 824 C ATOM 279 CD PRO A 57 46.325 60.893-402.936 1.00 51.71 C ANISOU 279 CD PRO A 57 5853 6005 7790 442 -1365 784 C ATOM 280 N THR A 58 49.794 63.563-402.097 1.00 60.08 N ANISOU 280 N THR A 58 7540 7410 7877 767 -1448 438 N ATOM 281 CA THR A 58 50.624 64.464-402.884 1.00 64.00 C ANISOU 281 CA THR A 58 8198 7941 8178 860 -1613 255 C ATOM 282 C THR A 58 51.930 63.738-403.119 1.00 62.50 C ANISOU 282 C THR A 58 8129 7795 7824 912 -1451 214 C ATOM 283 O THR A 58 52.196 62.739-402.458 1.00 56.90 O ANISOU 283 O THR A 58 7381 7119 7118 875 -1224 337 O ATOM 284 CB THR A 58 50.896 65.803-402.162 1.00 68.63 C ANISOU 284 CB THR A 58 8879 8686 8511 961 -1683 252 C ATOM 285 OG1 THR A 58 52.183 65.774-401.533 1.00 66.68 O ANISOU 285 OG1 THR A 58 8769 8589 7976 1045 -1504 284 O ATOM 286 CG2 THR A 58 49.824 66.076-401.117 1.00 67.22 C ANISOU 286 CG2 THR A 58 8570 8523 8448 919 -1664 411 C ATOM 287 N ALA A 59 52.741 64.233-404.052 1.00 57.47 N ANISOU 287 N ALA A 59 7634 7167 7036 1008 -1571 36 N ATOM 288 CA ALA A 59 54.020 63.596-404.385 1.00 53.16 C ANISOU 288 CA ALA A 59 7198 6674 6328 1083 -1426 -9 C ATOM 289 C ALA A 59 55.009 63.673-403.229 1.00 52.83 C ANISOU 289 C ALA A 59 7222 6847 6005 1145 -1218 104 C ATOM 290 O ALA A 59 56.118 63.154-403.310 1.00 51.56 O ANISOU 290 O ALA A 59 7130 6770 5691 1205 -1075 102 O ATOM 291 CB ALA A 59 54.619 64.219-405.636 1.00 54.07 C ANISOU 291 CB ALA A 59 7459 6754 6331 1202 -1613 -239 C ATOM 292 N GLU A 60 54.584 64.325-402.155 1.00 53.54 N ANISOU 292 N GLU A 60 7281 7018 6045 1127 -1209 213 N ATOM 293 CA GLU A 60 55.381 64.468-400.955 1.00 53.44 C ANISOU 293 CA GLU A 60 7318 7178 5810 1160 -1031 344 C ATOM 294 C GLU A 60 54.697 63.692-399.838 1.00 51.89 C ANISOU 294 C GLU A 60 7001 6935 5779 1040 -880 513 C ATOM 295 O GLU A 60 55.245 63.518-398.752 1.00 50.22 O ANISOU 295 O GLU A 60 6811 6820 5451 1028 -716 634 O ATOM 296 CB GLU A 60 55.482 65.949-400.588 1.00 51.13 C ANISOU 296 CB GLU A 60 7105 7011 5310 1257 -1151 337 C ATOM 297 CG GLU A 60 56.376 66.268-399.397 1.00 55.92 C ANISOU 297 CG GLU A 60 7770 7795 5682 1296 -984 488 C ATOM 298 CD GLU A 60 57.853 66.245-399.750 1.00 51.94 C ANISOU 298 CD GLU A 60 7372 7449 4912 1402 -890 452 C ATOM 299 OE1 GLU A 60 58.408 67.330-400.031 1.00 53.11 O ANISOU 299 OE1 GLU A 60 7623 7741 4817 1542 -979 395 O ATOM 300 OE2 GLU A 60 58.455 65.147-399.761 1.00 49.73 O ANISOU 300 OE2 GLU A 60 7068 7169 4659 1359 -726 484 O ATOM 301 N THR A 61 53.487 63.225-400.124 1.00 52.32 N ANISOU 301 N THR A 61 6929 6840 6112 955 -940 521 N ATOM 302 CA THR A 61 52.675 62.512-399.147 1.00 52.14 C ANISOU 302 CA THR A 61 6786 6773 6251 866 -811 665 C ATOM 303 C THR A 61 52.506 61.046-399.531 1.00 46.27 C ANISOU 303 C THR A 61 5951 5950 5678 792 -689 693 C ATOM 304 O THR A 61 52.459 60.168-398.672 1.00 49.53 O ANISOU 304 O THR A 61 6316 6387 6115 746 -513 798 O ATOM 305 CB THR A 61 51.286 63.158-399.031 1.00 52.00 C ANISOU 305 CB THR A 61 6662 6681 6415 843 -958 694 C ATOM 306 OG1 THR A 61 51.428 64.479-398.504 1.00 53.00 O ANISOU 306 OG1 THR A 61 6867 6898 6371 919 -1052 699 O ATOM 307 CG2 THR A 61 50.385 62.348-398.117 1.00 46.56 C ANISOU 307 CG2 THR A 61 5843 5948 5898 778 -817 833 C ATOM 308 N ALA A 62 52.436 60.798-400.833 1.00 74.24 N ANISOU 308 N ALA A 62 9477 9396 9334 787 -793 595 N ATOM 309 CA ALA A 62 52.148 59.478-401.389 1.00 75.77 C ANISOU 309 CA ALA A 62 9571 9496 9722 721 -706 634 C ATOM 310 C ALA A 62 52.384 58.293-400.455 1.00 71.40 C ANISOU 310 C ALA A 62 8973 9017 9138 685 -465 762 C ATOM 311 O ALA A 62 51.439 57.652-400.001 1.00 73.77 O ANISOU 311 O ALA A 62 9146 9284 9601 628 -392 866 O ATOM 312 CB ALA A 62 52.916 59.283-402.683 1.00 79.21 C ANISOU 312 CB ALA A 62 10085 9876 10137 765 -770 509 C ATOM 313 N ASP A 63 53.644 58.002-400.173 1.00 57.07 N ANISOU 313 N ASP A 63 7257 7316 7110 724 -345 753 N ATOM 314 CA ASP A 63 53.981 56.764-399.486 1.00 44.95 C ANISOU 314 CA ASP A 63 5681 5850 5548 684 -139 850 C ATOM 315 C ASP A 63 53.323 56.599-398.124 1.00 43.74 C ANISOU 315 C ASP A 63 5476 5726 5419 640 -46 951 C ATOM 316 O ASP A 63 53.378 55.520-397.548 1.00 46.34 O ANISOU 316 O ASP A 63 5759 6099 5748 605 105 1019 O ATOM 317 CB ASP A 63 55.499 56.599-399.371 1.00 49.44 C ANISOU 317 CB ASP A 63 6354 6555 5877 730 -42 830 C ATOM 318 CG ASP A 63 56.139 56.162-400.683 1.00 56.51 C ANISOU 318 CG ASP A 63 7274 7422 6776 784 -64 756 C ATOM 319 OD1 ASP A 63 55.392 55.966-401.671 1.00 50.89 O ANISOU 319 OD1 ASP A 63 6505 6562 6270 770 -160 721 O ATOM 320 OD2 ASP A 63 57.384 56.014-400.726 1.00 60.79 O ANISOU 320 OD2 ASP A 63 7886 8086 7127 840 15 743 O ATOM 321 N TYR A 64 52.705 57.654-397.604 1.00 54.03 N ANISOU 321 N TYR A 64 6790 7005 6734 653 -141 954 N ATOM 322 CA TYR A 64 52.035 57.562-396.308 1.00 53.81 C ANISOU 322 CA TYR A 64 6723 6983 6738 633 -61 1041 C ATOM 323 C TYR A 64 50.544 57.371-396.484 1.00 53.60 C ANISOU 323 C TYR A 64 6549 6868 6950 617 -102 1088 C ATOM 324 O TYR A 64 49.906 56.665-395.717 1.00 53.60 O ANISOU 324 O TYR A 64 6477 6872 7017 608 13 1163 O ATOM 325 CB TYR A 64 52.299 58.793-395.448 1.00 57.72 C ANISOU 325 CB TYR A 64 7317 7515 7098 669 -115 1048 C ATOM 326 CG TYR A 64 53.758 59.068-395.204 1.00 53.90 C ANISOU 326 CG TYR A 64 6962 7139 6379 684 -67 1034 C ATOM 327 CD1 TYR A 64 54.497 59.810-396.113 1.00 48.75 C ANISOU 327 CD1 TYR A 64 6383 6536 5604 742 -167 957 C ATOM 328 CD2 TYR A 64 54.396 58.594-394.068 1.00 53.67 C ANISOU 328 CD2 TYR A 64 6976 7167 6251 644 75 1099 C ATOM 329 CE1 TYR A 64 55.833 60.072-395.905 1.00 52.52 C ANISOU 329 CE1 TYR A 64 6959 7138 5857 772 -109 966 C ATOM 330 CE2 TYR A 64 55.737 58.850-393.846 1.00 46.75 C ANISOU 330 CE2 TYR A 64 6189 6400 5173 647 121 1114 C ATOM 331 CZ TYR A 64 56.451 59.591-394.771 1.00 53.59 C ANISOU 331 CZ TYR A 64 7113 7337 5912 717 38 1058 C ATOM 332 OH TYR A 64 57.791 59.860-394.572 1.00 57.05 O ANISOU 332 OH TYR A 64 7625 7913 6140 737 98 1091 O ATOM 333 N PHE A 65 49.980 58.018-397.489 1.00 44.66 N ANISOU 333 N PHE A 65 5365 5660 5943 619 -272 1045 N ATOM 334 CA PHE A 65 48.591 57.771-397.815 1.00 49.58 C ANISOU 334 CA PHE A 65 5815 6205 6817 590 -314 1111 C ATOM 335 C PHE A 65 48.465 56.298-398.162 1.00 49.99 C ANISOU 335 C PHE A 65 5772 6251 6970 552 -172 1176 C ATOM 336 O PHE A 65 47.738 55.561-397.499 1.00 48.97 O ANISOU 336 O PHE A 65 5543 6152 6912 554 -44 1275 O ATOM 337 CB PHE A 65 48.134 58.620-398.994 1.00 50.79 C ANISOU 337 CB PHE A 65 5926 6268 7104 575 -542 1044 C ATOM 338 CG PHE A 65 46.666 58.541-399.247 1.00 47.75 C ANISOU 338 CG PHE A 65 5341 5814 6989 534 -604 1134 C ATOM 339 CD1 PHE A 65 45.823 59.536-398.796 1.00 48.39 C ANISOU 339 CD1 PHE A 65 5363 5900 7122 560 -715 1162 C ATOM 340 CD2 PHE A 65 46.126 57.464-399.919 1.00 52.95 C ANISOU 340 CD2 PHE A 65 5855 6414 7850 476 -544 1212 C ATOM 341 CE1 PHE A 65 44.469 59.464-399.021 1.00 48.33 C ANISOU 341 CE1 PHE A 65 5147 5849 7367 525 -768 1263 C ATOM 342 CE2 PHE A 65 44.773 57.383-400.145 1.00 55.45 C ANISOU 342 CE2 PHE A 65 5963 6684 8422 436 -590 1324 C ATOM 343 CZ PHE A 65 43.945 58.382-399.695 1.00 48.52 C ANISOU 343 CZ PHE A 65 5018 5820 7596 459 -702 1348 C ATOM 344 N MET A 66 49.181 55.871-399.199 1.00 46.43 N ANISOU 344 N MET A 66 5356 5770 6515 534 -190 1123 N ATOM 345 CA MET A 66 49.221 54.463-399.569 1.00 48.21 C ANISOU 345 CA MET A 66 5503 6001 6812 508 -52 1196 C ATOM 346 C MET A 66 49.424 53.589-398.347 1.00 47.71 C ANISOU 346 C MET A 66 5448 6060 6620 524 151 1261 C ATOM 347 O MET A 66 48.632 52.685-398.079 1.00 53.67 O ANISOU 347 O MET A 66 6078 6838 7475 520 261 1366 O ATOM 348 CB MET A 66 50.351 54.207-400.559 1.00 52.74 C ANISOU 348 CB MET A 66 6169 6554 7315 518 -73 1116 C ATOM 349 CG MET A 66 49.907 53.993-401.993 1.00 60.16 C ANISOU 349 CG MET A 66 7027 7343 8487 482 -185 1114 C ATOM 350 SD MET A 66 49.000 55.382-402.680 1.00 87.55 S ANISOU 350 SD MET A 66 10461 10669 12134 451 -458 1037 S ATOM 351 CE MET A 66 47.319 54.924-402.266 1.00 62.38 C ANISOU 351 CE MET A 66 7030 7467 9206 389 -407 1225 C ATOM 352 N SER A 67 50.494 53.866-397.612 1.00 46.60 N ANISOU 352 N SER A 67 5453 6000 6253 544 194 1201 N ATOM 353 CA SER A 67 50.843 53.091-396.428 1.00 46.55 C ANISOU 353 CA SER A 67 5477 6097 6114 545 358 1238 C ATOM 354 C SER A 67 49.582 52.728-395.660 1.00 47.32 C ANISOU 354 C SER A 67 5468 6189 6321 561 426 1315 C ATOM 355 O SER A 67 49.332 51.559-395.375 1.00 44.29 O ANISOU 355 O SER A 67 5017 5867 5943 568 561 1374 O ATOM 356 CB SER A 67 51.794 53.891-395.534 1.00 43.21 C ANISOU 356 CB SER A 67 5204 5724 5488 551 348 1183 C ATOM 357 OG SER A 67 52.857 53.091-395.048 1.00 43.70 O ANISOU 357 OG SER A 67 5323 5888 5392 528 469 1183 O ATOM 358 N ALA A 68 48.784 53.739-395.338 1.00 42.16 N ANISOU 358 N ALA A 68 4797 5478 5745 584 332 1318 N ATOM 359 CA ALA A 68 47.496 53.520-394.701 1.00 42.78 C ANISOU 359 CA ALA A 68 4761 5554 5941 624 387 1397 C ATOM 360 C ALA A 68 46.549 52.810-395.656 1.00 43.50 C ANISOU 360 C ALA A 68 4662 5627 6238 612 401 1493 C ATOM 361 O ALA A 68 46.210 51.653-395.443 1.00 44.39 O ANISOU 361 O ALA A 68 4695 5810 6363 633 548 1567 O ATOM 362 CB ALA A 68 46.899 54.823-394.238 1.00 50.03 C ANISOU 362 CB ALA A 68 5692 6418 6899 660 271 1390 C ATOM 363 N MET A 69 46.128 53.499-396.713 1.00 47.23 N ANISOU 363 N MET A 69 5062 6010 6874 576 245 1497 N ATOM 364 CA MET A 69 45.129 52.948-397.626 1.00 50.85 C ANISOU 364 CA MET A 69 5319 6429 7573 545 238 1613 C ATOM 365 C MET A 69 45.277 51.448-397.838 1.00 51.13 C ANISOU 365 C MET A 69 5292 6531 7603 544 409 1698 C ATOM 366 O MET A 69 44.406 50.674-397.441 1.00 58.31 O ANISOU 366 O MET A 69 6066 7514 8574 585 539 1820 O ATOM 367 CB MET A 69 45.148 53.646-398.985 1.00 51.98 C ANISOU 367 CB MET A 69 5437 6443 7869 476 35 1569 C ATOM 368 CG MET A 69 43.951 53.277-399.856 1.00 57.44 C ANISOU 368 CG MET A 69 5898 7069 8858 423 -3 1709 C ATOM 369 SD MET A 69 44.216 53.429-401.641 1.00 72.42 S ANISOU 369 SD MET A 69 7777 8785 10955 323 -196 1664 S ATOM 370 CE MET A 69 45.064 51.896-402.020 1.00 63.26 C ANISOU 370 CE MET A 69 6652 7658 9727 329 -8 1716 C ATOM 371 N ASN A 70 46.378 51.032-398.459 1.00 57.21 N ANISOU 371 N ASN A 70 6157 7292 8289 513 414 1641 N ATOM 372 CA ASN A 70 46.530 49.623-398.806 1.00 59.56 C ANISOU 372 CA ASN A 70 6386 7652 8593 515 560 1736 C ATOM 373 C ASN A 70 46.818 48.741-397.592 1.00 59.23 C ANISOU 373 C ASN A 70 6391 7769 8344 574 743 1742 C ATOM 374 O ASN A 70 47.232 47.592-397.728 1.00 62.48 O ANISOU 374 O ASN A 70 6784 8267 8687 585 862 1794 O ATOM 375 CB ASN A 70 47.558 49.418-399.925 1.00 58.94 C ANISOU 375 CB ASN A 70 6378 7507 8508 480 506 1686 C ATOM 376 CG ASN A 70 48.976 49.445-399.426 1.00 55.94 C ANISOU 376 CG ASN A 70 6183 7209 7864 503 543 1565 C ATOM 377 OD1 ASN A 70 49.243 49.868-398.303 1.00 56.26 O ANISOU 377 OD1 ASN A 70 6315 7319 7742 523 569 1503 O ATOM 378 ND2 ASN A 70 49.903 48.993-400.261 1.00 54.90 N ANISOU 378 ND2 ASN A 70 6099 7063 7697 502 546 1544 N ATOM 379 N PHE A 71 46.596 49.293-396.405 1.00 41.69 N ANISOU 379 N PHE A 71 4235 5580 6026 613 753 1687 N ATOM 380 CA PHE A 71 46.588 48.498-395.183 1.00 41.94 C ANISOU 380 CA PHE A 71 4299 5737 5898 674 907 1685 C ATOM 381 C PHE A 71 45.154 48.275-394.746 1.00 42.00 C ANISOU 381 C PHE A 71 4158 5783 6017 750 980 1789 C ATOM 382 O PHE A 71 44.793 47.179-394.351 1.00 44.31 O ANISOU 382 O PHE A 71 4386 6195 6253 814 1129 1854 O ATOM 383 CB PHE A 71 47.357 49.188-394.053 1.00 40.90 C ANISOU 383 CB PHE A 71 4354 5601 5586 675 879 1553 C ATOM 384 CG PHE A 71 46.912 48.766-392.671 1.00 41.92 C ANISOU 384 CG PHE A 71 4513 5796 5619 748 988 1536 C ATOM 385 CD1 PHE A 71 47.677 47.896-391.915 1.00 42.17 C ANISOU 385 CD1 PHE A 71 4638 5920 5465 748 1082 1477 C ATOM 386 CD2 PHE A 71 45.729 49.243-392.127 1.00 42.22 C ANISOU 386 CD2 PHE A 71 4486 5802 5753 824 987 1572 C ATOM 387 CE1 PHE A 71 47.270 47.506-390.652 1.00 40.73 C ANISOU 387 CE1 PHE A 71 4501 5779 5195 820 1164 1434 C ATOM 388 CE2 PHE A 71 45.322 48.851-390.865 1.00 43.33 C ANISOU 388 CE2 PHE A 71 4671 5991 5803 914 1086 1539 C ATOM 389 CZ PHE A 71 46.094 47.981-390.131 1.00 42.29 C ANISOU 389 CZ PHE A 71 4649 5933 5486 911 1170 1460 C ATOM 390 N LEU A 72 44.346 49.327-394.798 1.00 44.09 N ANISOU 390 N LEU A 72 4364 5963 6426 756 874 1807 N ATOM 391 CA LEU A 72 42.946 49.218-394.430 1.00 44.42 C ANISOU 391 CA LEU A 72 4241 6049 6586 839 939 1921 C ATOM 392 C LEU A 72 42.265 48.123-395.244 1.00 45.61 C ANISOU 392 C LEU A 72 4187 6273 6871 844 1041 2096 C ATOM 393 O LEU A 72 41.092 47.815-395.025 1.00 49.11 O ANISOU 393 O LEU A 72 4460 6791 7407 923 1128 2227 O ATOM 394 CB LEU A 72 42.218 50.546-394.640 1.00 46.75 C ANISOU 394 CB LEU A 72 4471 6243 7047 827 782 1935 C ATOM 395 CG LEU A 72 42.434 51.676-393.637 1.00 46.73 C ANISOU 395 CG LEU A 72 4621 6191 6942 866 706 1821 C ATOM 396 CD1 LEU A 72 42.447 51.119-392.233 1.00 44.92 C ANISOU 396 CD1 LEU A 72 4487 6037 6544 971 857 1776 C ATOM 397 CD2 LEU A 72 43.719 52.422-393.922 1.00 44.48 C ANISOU 397 CD2 LEU A 72 4520 5830 6550 783 578 1690 C ATOM 398 N GLN A 73 43.001 47.544-396.188 1.00 83.03 N ANISOU 398 N GLN A 73 8934 10993 11619 768 1035 2113 N ATOM 399 CA GLN A 73 42.518 46.408-396.966 1.00 84.97 C ANISOU 399 CA GLN A 73 9001 11305 11978 770 1141 2296 C ATOM 400 C GLN A 73 42.448 45.138-396.108 1.00 88.28 C ANISOU 400 C GLN A 73 9416 11924 12204 882 1350 2337 C ATOM 401 O GLN A 73 41.582 44.284-396.318 1.00 94.18 O ANISOU 401 O GLN A 73 9980 12781 13024 942 1476 2519 O ATOM 402 CB GLN A 73 43.423 46.184-398.179 1.00 84.15 C ANISOU 402 CB GLN A 73 8935 11108 11930 672 1069 2291 C ATOM 403 CG GLN A 73 43.560 47.399-399.083 1.00 85.39 C ANISOU 403 CG GLN A 73 9119 11068 12257 573 849 2220 C ATOM 404 CD GLN A 73 42.314 47.657-399.905 1.00 91.59 C ANISOU 404 CD GLN A 73 9679 11768 13354 523 775 2380 C ATOM 405 OE1 GLN A 73 41.581 46.729-400.253 1.00 95.10 O ANISOU 405 OE1 GLN A 73 9934 12274 13924 534 890 2581 O ATOM 406 NE2 GLN A 73 42.070 48.923-400.226 1.00 88.80 N ANISOU 406 NE2 GLN A 73 9333 11281 13125 464 576 2303 N ATOM 407 N TYR A 74 43.370 45.021-395.152 1.00 55.03 N ANISOU 407 N TYR A 74 5404 7762 7744 909 1379 2171 N ATOM 408 CA TYR A 74 43.348 43.960-394.144 1.00 54.01 C ANISOU 408 CA TYR A 74 5307 7811 7402 1020 1543 2154 C ATOM 409 C TYR A 74 43.084 44.579-392.778 1.00 51.61 C ANISOU 409 C TYR A 74 5119 7497 6994 1096 1538 2020 C ATOM 410 O TYR A 74 43.220 43.920-391.751 1.00 54.21 O ANISOU 410 O TYR A 74 5536 7934 7128 1182 1635 1939 O ATOM 411 CB TYR A 74 44.697 43.244-394.078 1.00 51.22 C ANISOU 411 CB TYR A 74 5094 7520 6848 978 1566 2061 C ATOM 412 CG TYR A 74 45.492 43.250-395.360 1.00 50.97 C ANISOU 412 CG TYR A 74 5053 7407 6906 873 1490 2100 C ATOM 413 CD1 TYR A 74 45.598 42.106-396.137 1.00 52.54 C ANISOU 413 CD1 TYR A 74 5148 7697 7118 883 1580 2240 C ATOM 414 CD2 TYR A 74 46.152 44.397-395.789 1.00 50.96 C ANISOU 414 CD2 TYR A 74 5153 7242 6966 780 1330 1998 C ATOM 415 CE1 TYR A 74 46.333 42.101-397.313 1.00 55.26 C ANISOU 415 CE1 TYR A 74 5495 7948 7553 803 1511 2271 C ATOM 416 CE2 TYR A 74 46.887 44.407-396.965 1.00 50.89 C ANISOU 416 CE2 TYR A 74 5152 7154 7030 709 1259 2014 C ATOM 417 CZ TYR A 74 46.975 43.255-397.725 1.00 52.71 C ANISOU 417 CZ TYR A 74 5283 7454 7290 721 1349 2148 C ATOM 418 OH TYR A 74 47.700 43.246-398.902 1.00 54.01 O ANISOU 418 OH TYR A 74 5463 7523 7536 667 1281 2163 O ATOM 419 N GLY A 75 42.709 45.854-392.771 1.00 91.21 N ANISOU 419 N GLY A 75 10139 12375 12142 1069 1415 1994 N ATOM 420 CA GLY A 75 42.735 46.638-391.552 1.00 94.95 C ANISOU 420 CA GLY A 75 10760 12792 12524 1120 1378 1856 C ATOM 421 C GLY A 75 41.404 46.925-390.894 1.00101.27 C ANISOU 421 C GLY A 75 11461 13618 13398 1258 1430 1914 C ATOM 422 O GLY A 75 40.407 47.220-391.553 1.00101.30 O ANISOU 422 O GLY A 75 11268 13621 13600 1272 1414 2061 O ATOM 423 N ASN A 76 41.405 46.829-389.570 1.00127.26 N ANISOU 423 N ASN A 76 14889 16929 16535 1363 1489 1796 N ATOM 424 CA ASN A 76 40.265 47.223-388.767 1.00129.13 C ANISOU 424 CA ASN A 76 15076 17171 16818 1519 1533 1817 C ATOM 425 C ASN A 76 40.474 48.665-388.332 1.00121.13 C ANISOU 425 C ASN A 76 14181 15984 15858 1483 1384 1735 C ATOM 426 O ASN A 76 39.793 49.574-388.803 1.00122.85 O ANISOU 426 O ASN A 76 14277 16149 16251 1479 1299 1826 O ATOM 427 CB ASN A 76 40.141 46.323-387.531 1.00135.66 C ANISOU 427 CB ASN A 76 16006 18094 17443 1675 1672 1715 C ATOM 428 CG ASN A 76 40.588 44.890-387.792 1.00142.71 C ANISOU 428 CG ASN A 76 16885 19150 18187 1669 1784 1724 C ATOM 429 OD1 ASN A 76 40.302 44.319-388.845 1.00148.40 O ANISOU 429 OD1 ASN A 76 17424 19972 18991 1641 1835 1888 O ATOM 430 ND2 ASN A 76 41.290 44.302-386.826 1.00136.66 N ANISOU 430 ND2 ASN A 76 16309 18408 17208 1695 1813 1553 N ATOM 431 N ASP A 77 41.441 48.867-387.443 1.00 69.26 N ANISOU 431 N ASP A 77 7844 9332 9140 1449 1347 1574 N ATOM 432 CA ASP A 77 41.733 50.195-386.922 1.00 67.25 C ANISOU 432 CA ASP A 77 7719 8918 8915 1421 1218 1509 C ATOM 433 C ASP A 77 43.189 50.611-387.157 1.00 65.91 C ANISOU 433 C ASP A 77 7704 8671 8666 1252 1111 1427 C ATOM 434 O ASP A 77 44.108 49.800-387.060 1.00 68.52 O ANISOU 434 O ASP A 77 8123 9048 8862 1185 1155 1358 O ATOM 435 CB ASP A 77 41.358 50.306-385.433 1.00 68.85 C ANISOU 435 CB ASP A 77 8052 9062 9046 1568 1269 1417 C ATOM 436 CG ASP A 77 42.511 49.963-384.497 1.00 71.70 C ANISOU 436 CG ASP A 77 8649 9359 9236 1507 1267 1256 C ATOM 437 OD1 ASP A 77 43.392 49.170-384.885 1.00 74.07 O ANISOU 437 OD1 ASP A 77 8977 9731 9435 1399 1287 1221 O ATOM 438 OD2 ASP A 77 42.525 50.485-383.360 1.00 70.21 O ANISOU 438 OD2 ASP A 77 8612 9042 9024 1568 1241 1173 O ATOM 439 N LEU A 78 43.376 51.886-387.478 1.00 46.51 N ANISOU 439 N LEU A 78 5270 6115 6286 1193 971 1444 N ATOM 440 CA LEU A 78 44.691 52.451-387.701 1.00 46.23 C ANISOU 440 CA LEU A 78 5373 6022 6171 1059 872 1383 C ATOM 441 C LEU A 78 44.784 53.734-386.904 1.00 45.37 C ANISOU 441 C LEU A 78 5384 5793 6063 1082 779 1361 C ATOM 442 O LEU A 78 43.897 54.575-386.966 1.00 53.45 O ANISOU 442 O LEU A 78 6328 6779 7202 1154 717 1423 O ATOM 443 CB LEU A 78 44.886 52.752-389.187 1.00 47.08 C ANISOU 443 CB LEU A 78 5375 6149 6364 968 780 1439 C ATOM 444 CG LEU A 78 46.223 53.375-389.595 1.00 47.91 C ANISOU 444 CG LEU A 78 5607 6221 6376 856 679 1382 C ATOM 445 CD1 LEU A 78 47.270 52.295-389.802 1.00 48.51 C ANISOU 445 CD1 LEU A 78 5731 6373 6327 784 758 1340 C ATOM 446 CD2 LEU A 78 46.072 54.202-390.862 1.00 46.99 C ANISOU 446 CD2 LEU A 78 5406 6077 6371 815 539 1417 C ATOM 447 N ARG A 79 45.846 53.885-386.137 1.00 49.43 N ANISOU 447 N ARG A 79 6078 6249 6454 1020 768 1288 N ATOM 448 CA ARG A 79 46.038 55.120-385.412 1.00 51.80 C ANISOU 448 CA ARG A 79 6495 6433 6755 1033 682 1292 C ATOM 449 C ARG A 79 47.161 55.874-386.102 1.00 43.46 C ANISOU 449 C ARG A 79 5492 5386 5634 915 579 1303 C ATOM 450 O ARG A 79 48.251 55.323-386.278 1.00 45.37 O ANISOU 450 O ARG A 79 5792 5678 5768 815 608 1263 O ATOM 451 CB ARG A 79 46.419 54.825-383.970 1.00 46.96 C ANISOU 451 CB ARG A 79 6049 5728 6067 1047 738 1220 C ATOM 452 CG ARG A 79 45.637 53.680-383.346 1.00 48.92 C ANISOU 452 CG ARG A 79 6273 6002 6312 1155 860 1162 C ATOM 453 CD ARG A 79 44.292 54.138-382.812 1.00 49.57 C ANISOU 453 CD ARG A 79 6304 6027 6503 1334 876 1199 C ATOM 454 NE ARG A 79 43.635 53.099-382.022 1.00 51.37 N ANISOU 454 NE ARG A 79 6546 6275 6696 1464 999 1125 N ATOM 455 CZ ARG A 79 43.944 52.809-380.762 1.00 54.39 C ANISOU 455 CZ ARG A 79 7110 6546 7011 1494 1024 1010 C ATOM 456 NH1 ARG A 79 44.909 53.476-380.142 1.00 58.50 N ANISOU 456 NH1 ARG A 79 7798 6919 7511 1385 940 981 N ATOM 457 NH2 ARG A 79 43.290 51.849-380.122 1.00 55.96 N ANISOU 457 NH2 ARG A 79 7322 6780 7162 1636 1129 926 N ATOM 458 N VAL A 80 46.904 57.123-386.500 1.00 44.92 N ANISOU 458 N VAL A 80 5652 5543 5873 939 460 1357 N ATOM 459 CA VAL A 80 47.908 57.921-387.210 1.00 43.11 C ANISOU 459 CA VAL A 80 5474 5343 5561 859 358 1362 C ATOM 460 C VAL A 80 48.280 59.197-386.474 1.00 47.41 C ANISOU 460 C VAL A 80 6138 5820 6055 878 282 1405 C ATOM 461 O VAL A 80 47.580 59.634-385.571 1.00 47.58 O ANISOU 461 O VAL A 80 6183 5756 6141 963 282 1442 O ATOM 462 CB VAL A 80 47.447 58.290-388.627 1.00 46.90 C ANISOU 462 CB VAL A 80 5821 5875 6124 859 255 1376 C ATOM 463 CG1 VAL A 80 46.573 57.186-389.199 1.00 49.26 C ANISOU 463 CG1 VAL A 80 5961 6212 6542 873 328 1385 C ATOM 464 CG2 VAL A 80 46.693 59.599-388.607 1.00 48.27 C ANISOU 464 CG2 VAL A 80 5960 6010 6372 933 127 1429 C ATOM 465 N VAL A 81 49.400 59.782-386.871 1.00 54.37 N ANISOU 465 N VAL A 81 7093 6750 6816 812 224 1411 N ATOM 466 CA VAL A 81 49.844 61.058-386.330 1.00 53.65 C ANISOU 466 CA VAL A 81 7103 6626 6655 832 150 1479 C ATOM 467 C VAL A 81 50.519 61.844-387.447 1.00 52.51 C ANISOU 467 C VAL A 81 6957 6588 6406 816 45 1478 C ATOM 468 O VAL A 81 51.559 61.432-387.964 1.00 52.60 O ANISOU 468 O VAL A 81 6998 6680 6308 747 77 1442 O ATOM 469 CB VAL A 81 50.844 60.861-385.181 1.00 54.44 C ANISOU 469 CB VAL A 81 7341 6672 6671 762 228 1504 C ATOM 470 CG1 VAL A 81 51.452 62.187-384.767 1.00 54.87 C ANISOU 470 CG1 VAL A 81 7488 6715 6644 772 159 1608 C ATOM 471 CG2 VAL A 81 50.170 60.200-384.001 1.00 56.56 C ANISOU 471 CG2 VAL A 81 7641 6813 7037 794 309 1482 C ATOM 472 N ARG A 82 49.931 62.972-387.828 1.00 59.49 N ANISOU 472 N ARG A 82 7806 7481 7316 893 -86 1510 N ATOM 473 CA ARG A 82 50.485 63.747-388.930 1.00 61.14 C ANISOU 473 CA ARG A 82 8022 7793 7415 899 -206 1481 C ATOM 474 C ARG A 82 51.722 64.525-388.509 1.00 61.29 C ANISOU 474 C ARG A 82 8172 7875 7240 893 -204 1545 C ATOM 475 O ARG A 82 51.696 65.257-387.523 1.00 65.20 O ANISOU 475 O ARG A 82 8730 8325 7718 930 -206 1649 O ATOM 476 CB ARG A 82 49.449 64.716-389.494 1.00 67.78 C ANISOU 476 CB ARG A 82 8778 8637 8337 980 -370 1486 C ATOM 477 CG ARG A 82 49.948 65.482-390.718 1.00 66.50 C ANISOU 477 CG ARG A 82 8630 8577 8061 995 -519 1420 C ATOM 478 CD ARG A 82 49.179 66.769-390.923 1.00 68.18 C ANISOU 478 CD ARG A 82 8802 8811 8294 1082 -700 1447 C ATOM 479 NE ARG A 82 49.173 67.191-392.318 1.00 66.77 N ANISOU 479 NE ARG A 82 8587 8693 8090 1088 -871 1335 N ATOM 480 CZ ARG A 82 48.799 68.399-392.721 1.00 67.68 C ANISOU 480 CZ ARG A 82 8689 8863 8163 1160 -1064 1326 C ATOM 481 NH1 ARG A 82 48.418 69.302-391.829 1.00 65.98 N ANISOU 481 NH1 ARG A 82 8486 8660 7922 1238 -1097 1443 N ATOM 482 NH2 ARG A 82 48.813 68.705-394.009 1.00 71.97 N ANISOU 482 NH2 ARG A 82 9212 9444 8690 1158 -1232 1196 N ATOM 483 N ALA A 83 52.802 64.372-389.266 1.00103.40 N ANISOU 483 N ALA A 83 13540 13318 12431 856 -195 1498 N ATOM 484 CA ALA A 83 54.007 65.149-389.019 1.00108.34 C ANISOU 484 CA ALA A 83 14267 14043 12855 865 -189 1574 C ATOM 485 C ALA A 83 53.947 66.470-389.774 1.00107.03 C ANISOU 485 C ALA A 83 14117 13974 12576 970 -348 1566 C ATOM 486 O ALA A 83 53.881 66.498-391.001 1.00108.14 O ANISOU 486 O ALA A 83 14224 14171 12694 1000 -441 1447 O ATOM 487 CB ALA A 83 55.242 64.364-389.414 1.00101.87 C ANISOU 487 CB ALA A 83 13470 13319 11917 797 -90 1539 C ATOM 488 N VAL A 84 53.957 67.562-389.023 1.00 53.58 N ANISOU 488 N VAL A 84 7402 7216 5740 1030 -387 1692 N ATOM 489 CA VAL A 84 53.976 68.902-389.581 1.00 54.72 C ANISOU 489 CA VAL A 84 7573 7479 5739 1143 -538 1702 C ATOM 490 C VAL A 84 55.297 69.539-389.195 1.00 53.28 C ANISOU 490 C VAL A 84 7488 7433 5322 1166 -477 1826 C ATOM 491 O VAL A 84 55.910 69.116-388.223 1.00 58.04 O ANISOU 491 O VAL A 84 8126 7992 5935 1086 -337 1941 O ATOM 492 CB VAL A 84 52.827 69.737-389.000 1.00 51.24 C ANISOU 492 CB VAL A 84 7100 6963 5406 1216 -637 1782 C ATOM 493 CG1 VAL A 84 53.337 71.070-388.467 1.00 57.63 C ANISOU 493 CG1 VAL A 84 7991 7871 6033 1307 -679 1938 C ATOM 494 CG2 VAL A 84 51.722 69.918-390.033 1.00 59.08 C ANISOU 494 CG2 VAL A 84 7990 7951 6508 1259 -805 1655 C ATOM 495 N ASP A 85 55.757 70.539-389.940 1.00 52.65 N ANISOU 495 N ASP A 85 7449 7524 5030 1274 -582 1809 N ATOM 496 CA ASP A 85 56.954 71.250-389.503 1.00 53.41 C ANISOU 496 CA ASP A 85 7624 7777 4893 1317 -515 1966 C ATOM 497 C ASP A 85 56.180 72.173-388.591 1.00 58.25 C ANISOU 497 C ASP A 85 8268 8386 5479 1390 -564 2152 C ATOM 498 O ASP A 85 55.175 72.735-388.999 1.00 56.65 O ANISOU 498 O ASP A 85 8089 8322 5115 1523 -696 2159 O ATOM 499 CB ASP A 85 57.780 71.780-390.668 1.00 54.29 C ANISOU 499 CB ASP A 85 7779 8110 4740 1428 -579 1873 C ATOM 500 CG ASP A 85 58.958 72.621-390.199 1.00 56.28 C ANISOU 500 CG ASP A 85 8095 8557 4730 1498 -503 2067 C ATOM 501 OD1 ASP A 85 60.007 72.048-389.808 1.00 57.00 O ANISOU 501 OD1 ASP A 85 8190 8700 4769 1422 -338 2162 O ATOM 502 OD2 ASP A 85 58.827 73.862-390.219 1.00 57.84 O ANISOU 502 OD2 ASP A 85 8330 8872 4774 1629 -610 2136 O ATOM 503 N ARG A 86 56.661 72.336-387.364 1.00 63.87 N ANISOU 503 N ARG A 86 8984 8937 6346 1309 -463 2298 N ATOM 504 CA ARG A 86 55.974 73.125-386.337 1.00 61.53 C ANISOU 504 CA ARG A 86 8717 8587 6074 1375 -500 2491 C ATOM 505 C ARG A 86 56.408 74.567-386.612 1.00 62.68 C ANISOU 505 C ARG A 86 8906 8950 5959 1524 -591 2608 C ATOM 506 O ARG A 86 55.727 75.513-386.218 1.00 76.07 O ANISOU 506 O ARG A 86 10604 10632 7666 1623 -687 2712 O ATOM 507 CB ARG A 86 56.443 72.719-384.938 1.00 71.50 C ANISOU 507 CB ARG A 86 10022 9701 7445 1262 -346 2671 C ATOM 508 CG ARG A 86 55.405 71.994-384.113 1.00 60.80 C ANISOU 508 CG ARG A 86 8648 8082 6372 1202 -318 2634 C ATOM 509 CD ARG A 86 56.064 71.125-383.052 1.00 61.33 C ANISOU 509 CD ARG A 86 8758 8002 6542 1049 -166 2710 C ATOM 510 NE ARG A 86 55.407 71.290-381.757 1.00 63.65 N ANISOU 510 NE ARG A 86 9097 8062 7024 1052 -152 2824 N ATOM 511 CZ ARG A 86 54.264 70.704-381.411 1.00 61.68 C ANISOU 511 CZ ARG A 86 8826 7628 6980 1067 -161 2715 C ATOM 512 NH1 ARG A 86 53.640 69.902-382.262 1.00 67.67 N ANISOU 512 NH1 ARG A 86 9506 8415 7790 1066 -181 2510 N ATOM 513 NH2 ARG A 86 53.745 70.927-380.209 1.00 65.79 N ANISOU 513 NH2 ARG A 86 9404 7935 7657 1093 -146 2822 N ATOM 514 N ASP A 87 57.546 74.728-387.273 1.00 62.35 N ANISOU 514 N ASP A 87 8896 9123 5672 1557 -557 2596 N ATOM 515 CA ASP A 87 58.133 76.043-387.476 1.00 68.03 C ANISOU 515 CA ASP A 87 9664 10084 6101 1711 -615 2723 C ATOM 516 C ASP A 87 57.546 76.775-388.680 1.00 68.01 C ANISOU 516 C ASP A 87 9658 10218 5965 1861 -827 2535 C ATOM 517 O ASP A 87 57.645 77.997-388.773 1.00 68.81 O ANISOU 517 O ASP A 87 9795 10499 5849 2013 -922 2629 O ATOM 518 CB ASP A 87 59.655 75.930-387.634 1.00 68.54 C ANISOU 518 CB ASP A 87 9758 10346 5937 1703 -474 2807 C ATOM 519 CG ASP A 87 60.340 75.425-386.375 1.00 77.06 C ANISOU 519 CG ASP A 87 10834 11318 7129 1551 -286 3036 C ATOM 520 OD1 ASP A 87 60.132 76.033-385.302 1.00 72.35 O ANISOU 520 OD1 ASP A 87 10256 10631 6601 1547 -271 3263 O ATOM 521 OD2 ASP A 87 61.096 74.425-386.465 1.00 87.65 O ANISOU 521 OD2 ASP A 87 12150 12659 8493 1434 -163 2992 O ATOM 522 N THR A 88 56.950 76.042-389.611 1.00 62.19 N ANISOU 522 N THR A 88 7107 9691 6833 437 -580 -412 N ATOM 523 CA THR A 88 56.484 76.677-390.835 1.00 60.24 C ANISOU 523 CA THR A 88 7038 9402 6449 635 -630 -313 C ATOM 524 C THR A 88 55.161 76.147-391.361 1.00 63.59 C ANISOU 524 C THR A 88 7738 9527 6897 706 -663 -351 C ATOM 525 O THR A 88 54.785 76.434-392.491 1.00 57.93 O ANISOU 525 O THR A 88 7179 8760 6072 877 -738 -312 O ATOM 526 CB THR A 88 57.520 76.562-391.955 1.00 61.50 C ANISOU 526 CB THR A 88 7172 9909 6287 898 -752 -381 C ATOM 527 OG1 THR A 88 57.721 75.182-392.273 1.00 62.53 O ANISOU 527 OG1 THR A 88 7386 10124 6247 1024 -840 -595 O ATOM 528 CG2 THR A 88 58.836 77.187-391.527 1.00 64.43 C ANISOU 528 CG2 THR A 88 7241 10632 6608 851 -708 -304 C ATOM 529 N ALA A 89 54.452 75.370-390.560 1.00 61.28 N ANISOU 529 N ALA A 89 7494 9042 6747 587 -616 -426 N ATOM 530 CA ALA A 89 53.142 74.926-390.979 1.00 59.73 C ANISOU 530 CA ALA A 89 7529 8586 6581 646 -619 -416 C ATOM 531 C ALA A 89 52.201 76.054-390.642 1.00 62.17 C ANISOU 531 C ALA A 89 7865 8653 7102 509 -535 -243 C ATOM 532 O ALA A 89 52.467 76.818-389.717 1.00 62.52 O ANISOU 532 O ALA A 89 7764 8690 7299 345 -459 -167 O ATOM 533 CB ALA A 89 52.748 73.691-390.252 1.00 63.03 C ANISOU 533 CB ALA A 89 7973 8941 7033 623 -604 -560 C ATOM 534 N LYS A 90 51.106 76.158-391.390 1.00 60.23 N ANISOU 534 N LYS A 90 7801 8213 6872 578 -547 -174 N ATOM 535 CA LYS A 90 50.128 77.220-391.188 1.00 57.96 C ANISOU 535 CA LYS A 90 7545 7716 6763 480 -479 -29 C ATOM 536 C LYS A 90 48.689 76.754-391.426 1.00 59.50 C ANISOU 536 C LYS A 90 7904 7676 7028 484 -457 1 C ATOM 537 O LYS A 90 48.408 76.047-392.393 1.00 62.42 O ANISOU 537 O LYS A 90 8401 8020 7296 610 -519 -20 O ATOM 538 CB LYS A 90 50.457 78.421-392.081 1.00 59.29 C ANISOU 538 CB LYS A 90 7696 7956 6877 580 -533 61 C ATOM 539 CG LYS A 90 51.759 79.129-391.711 1.00 61.55 C ANISOU 539 CG LYS A 90 7786 8495 7105 575 -517 95 C ATOM 540 CD LYS A 90 51.714 79.614-390.275 1.00 59.77 C ANISOU 540 CD LYS A 90 7435 8195 7079 358 -379 178 C ATOM 541 CE LYS A 90 53.082 80.024-389.780 1.00 62.31 C ANISOU 541 CE LYS A 90 7534 8775 7366 313 -343 226 C ATOM 542 NZ LYS A 90 53.034 80.384-388.335 1.00 64.60 N ANISOU 542 NZ LYS A 90 7714 8938 7892 76 -215 312 N ATOM 543 N ASN A 91 47.791 77.144-390.522 1.00 55.06 N ANISOU 543 N ASN A 91 7334 6949 6637 352 -365 63 N ATOM 544 CA ASN A 91 46.357 76.962-390.699 1.00 54.15 C ANISOU 544 CA ASN A 91 7337 6642 6596 349 -327 127 C ATOM 545 C ASN A 91 45.812 78.174-391.415 1.00 52.80 C ANISOU 545 C ASN A 91 7191 6376 6494 355 -338 239 C ATOM 546 O ASN A 91 46.045 79.293-390.977 1.00 52.51 O ANISOU 546 O ASN A 91 7074 6352 6525 303 -305 289 O ATOM 547 CB ASN A 91 45.669 76.896-389.343 1.00 55.44 C ANISOU 547 CB ASN A 91 7473 6702 6888 236 -241 121 C ATOM 548 CG ASN A 91 45.932 75.612-388.617 1.00 54.64 C ANISOU 548 CG ASN A 91 7356 6669 6736 260 -251 -20 C ATOM 549 OD1 ASN A 91 46.837 75.532-387.793 1.00 57.06 O ANISOU 549 OD1 ASN A 91 7553 7053 7074 192 -265 -116 O ATOM 550 ND2 ASN A 91 45.140 74.590-388.912 1.00 55.63 N ANISOU 550 ND2 ASN A 91 7576 6773 6786 366 -245 -33 N ATOM 551 N SER A 92 45.085 77.978-392.507 1.00 55.54 N ANISOU 551 N SER A 92 7641 6625 6835 423 -386 281 N ATOM 552 CA SER A 92 44.496 79.116-393.193 1.00 52.02 C ANISOU 552 CA SER A 92 7204 6081 6482 431 -421 353 C ATOM 553 C SER A 92 43.781 80.003-392.178 1.00 55.80 C ANISOU 553 C SER A 92 7624 6489 7088 327 -315 411 C ATOM 554 O SER A 92 43.233 79.505-391.198 1.00 58.19 O ANISOU 554 O SER A 92 7930 6746 7433 249 -226 415 O ATOM 555 CB SER A 92 43.522 78.636-394.257 1.00 54.79 C ANISOU 555 CB SER A 92 7660 6279 6879 459 -465 403 C ATOM 556 OG SER A 92 44.007 77.464-394.870 1.00 53.45 O ANISOU 556 OG SER A 92 7575 6148 6587 548 -521 365 O ATOM 557 N SER A 93 43.789 81.315-392.406 1.00 70.41 N ANISOU 557 N SER A 93 9427 8343 8984 358 -336 445 N ATOM 558 CA SER A 93 43.181 82.259-391.463 1.00 68.90 C ANISOU 558 CA SER A 93 9192 8098 8890 293 -236 502 C ATOM 559 C SER A 93 42.676 83.535-392.140 1.00 66.85 C ANISOU 559 C SER A 93 8912 7809 8680 374 -280 528 C ATOM 560 O SER A 93 42.946 83.772-393.315 1.00 66.35 O ANISOU 560 O SER A 93 8856 7771 8584 484 -408 489 O ATOM 561 CB SER A 93 44.174 82.612-390.354 1.00 66.74 C ANISOU 561 CB SER A 93 8836 7920 8601 247 -167 517 C ATOM 562 OG SER A 93 45.116 83.565-390.809 1.00 67.46 O ANISOU 562 OG SER A 93 8851 8154 8625 350 -208 545 O ATOM 563 N PRO A 94 41.936 84.369-391.392 1.00 52.46 N ANISOU 563 N PRO A 94 7068 5934 6932 344 -192 575 N ATOM 564 CA PRO A 94 41.360 85.582-391.970 1.00 51.92 C ANISOU 564 CA PRO A 94 6970 5853 6904 444 -234 574 C ATOM 565 C PRO A 94 42.358 86.724-391.944 1.00 52.92 C ANISOU 565 C PRO A 94 7025 6129 6954 582 -246 593 C ATOM 566 O PRO A 94 42.125 87.751-392.573 1.00 52.40 O ANISOU 566 O PRO A 94 6923 6101 6886 728 -313 564 O ATOM 567 CB PRO A 94 40.192 85.911-391.024 1.00 50.83 C ANISOU 567 CB PRO A 94 6843 5629 6840 377 -118 614 C ATOM 568 CG PRO A 94 40.158 84.821-389.997 1.00 51.17 C ANISOU 568 CG PRO A 94 6931 5628 6883 252 -35 630 C ATOM 569 CD PRO A 94 41.514 84.191-389.998 1.00 51.20 C ANISOU 569 CD PRO A 94 6920 5715 6817 239 -66 608 C ATOM 570 N ILE A 95 43.446 86.557-391.204 1.00 51.80 N ANISOU 570 N ILE A 95 6845 6086 6750 548 -181 643 N ATOM 571 CA ILE A 95 44.490 87.573-391.173 1.00 52.73 C ANISOU 571 CA ILE A 95 6870 6386 6778 686 -171 704 C ATOM 572 C ILE A 95 45.220 87.636-392.506 1.00 54.93 C ANISOU 572 C ILE A 95 7121 6812 6939 867 -338 627 C ATOM 573 O ILE A 95 45.600 88.707-392.968 1.00 53.95 O ANISOU 573 O ILE A 95 6931 6835 6734 1076 -390 635 O ATOM 574 CB ILE A 95 45.527 87.290-390.066 1.00 54.94 C ANISOU 574 CB ILE A 95 7088 6739 7047 571 -58 794 C ATOM 575 CG1 ILE A 95 45.130 87.980-388.761 1.00 55.86 C ANISOU 575 CG1 ILE A 95 7206 6758 7262 493 96 907 C ATOM 576 CG2 ILE A 95 46.900 87.778-390.486 1.00 54.15 C ANISOU 576 CG2 ILE A 95 6871 6895 6807 716 -92 843 C ATOM 577 CD1 ILE A 95 44.448 87.081-387.778 1.00 53.40 C ANISOU 577 CD1 ILE A 95 6972 6251 7068 297 151 874 C ATOM 578 N ALA A 96 45.379 86.478-393.132 1.00 58.84 N ANISOU 578 N ALA A 96 7675 7269 7413 819 -432 546 N ATOM 579 CA ALA A 96 46.381 86.296-394.171 1.00 59.69 C ANISOU 579 CA ALA A 96 7766 7535 7377 982 -586 475 C ATOM 580 C ALA A 96 46.018 86.861-395.539 1.00 55.93 C ANISOU 580 C ALA A 96 7323 7029 6897 1178 -782 372 C ATOM 581 O ALA A 96 46.513 86.381-396.555 1.00 58.08 O ANISOU 581 O ALA A 96 7642 7336 7088 1290 -948 280 O ATOM 582 CB ALA A 96 46.749 84.825-394.290 1.00 61.19 C ANISOU 582 CB ALA A 96 8021 7702 7527 884 -614 423 C ATOM 583 N GLY A 97 45.179 87.884-395.577 1.00 53.70 N ANISOU 583 N GLY A 97 7018 6683 6702 1238 -779 370 N ATOM 584 CA GLY A 97 44.959 88.596-396.826 1.00 54.90 C ANISOU 584 CA GLY A 97 7168 6834 6858 1457 -989 244 C ATOM 585 C GLY A 97 45.222 90.087-396.688 1.00 54.61 C ANISOU 585 C GLY A 97 7023 6993 6735 1699 -985 256 C ATOM 586 O GLY A 97 45.593 90.773-397.643 1.00 57.14 O ANISOU 586 O GLY A 97 7306 7435 6969 1977 -1175 143 O ATOM 587 N ASN A 98 45.017 90.578-395.475 1.00 56.66 N ANISOU 587 N ASN A 98 8891 5857 6782 -352 554 577 N ATOM 588 CA ASN A 98 45.150 91.982-395.174 1.00 55.19 C ANISOU 588 CA ASN A 98 8581 5843 6547 -303 568 641 C ATOM 589 C ASN A 98 46.463 92.548-395.647 1.00 57.15 C ANISOU 589 C ASN A 98 8689 6149 6875 -442 516 646 C ATOM 590 O ASN A 98 47.227 91.873-396.326 1.00 57.67 O ANISOU 590 O ASN A 98 8737 6143 7033 -579 484 602 O ATOM 591 CB ASN A 98 45.000 92.190-393.679 1.00 58.67 C ANISOU 591 CB ASN A 98 9232 6153 6908 -171 528 750 C ATOM 592 CG ASN A 98 43.581 92.057-393.237 1.00 60.15 C ANISOU 592 CG ASN A 98 9520 6357 6977 18 622 778 C ATOM 593 OD1 ASN A 98 42.693 92.662-393.829 1.00 57.09 O ANISOU 593 OD1 ASN A 98 8949 6194 6549 77 728 774 O ATOM 594 ND2 ASN A 98 43.344 91.261-392.204 1.00 58.13 N ANISOU 594 ND2 ASN A 98 9571 5855 6659 122 579 827 N ATOM 595 N ILE A 99 46.718 93.795-395.266 1.00 55.29 N ANISOU 595 N ILE A 99 8357 6045 6605 -393 518 712 N ATOM 596 CA ILE A 99 47.892 94.531-395.712 1.00 56.11 C ANISOU 596 CA ILE A 99 8315 6238 6768 -477 488 739 C ATOM 597 C ILE A 99 48.522 95.290-394.551 1.00 54.49 C ANISOU 597 C ILE A 99 8144 5999 6561 -418 420 872 C ATOM 598 O ILE A 99 47.850 96.062-393.878 1.00 55.22 O ANISOU 598 O ILE A 99 8226 6181 6574 -304 451 902 O ATOM 599 CB ILE A 99 47.511 95.534-396.804 1.00 54.88 C ANISOU 599 CB ILE A 99 7939 6346 6568 -476 569 670 C ATOM 600 CG1 ILE A 99 48.633 96.557-396.999 1.00 53.70 C ANISOU 600 CG1 ILE A 99 7667 6293 6442 -499 550 725 C ATOM 601 CG2 ILE A 99 46.204 96.223-396.446 1.00 54.54 C ANISOU 601 CG2 ILE A 99 7857 6438 6426 -353 635 683 C ATOM 602 CD1 ILE A 99 48.470 97.449-398.223 1.00 53.77 C ANISOU 602 CD1 ILE A 99 7505 6521 6404 -515 605 653 C ATOM 603 N GLU A 100 49.808 95.057-394.313 1.00 80.54 N ANISOU 603 N GLU A 100 11474 9172 9956 -496 325 969 N ATOM 604 CA GLU A 100 50.541 95.798-393.298 1.00 81.00 C ANISOU 604 CA GLU A 100 11530 9211 10035 -448 238 1120 C ATOM 605 C GLU A 100 50.103 97.252-393.321 1.00 81.29 C ANISOU 605 C GLU A 100 11387 9502 9997 -347 319 1100 C ATOM 606 O GLU A 100 49.884 97.819-394.387 1.00100.05 O ANISOU 606 O GLU A 100 13601 12068 12346 -359 414 1011 O ATOM 607 CB GLU A 100 52.038 95.748-393.596 1.00 80.70 C ANISOU 607 CB GLU A 100 11420 9123 10118 -542 170 1243 C ATOM 608 CG GLU A 100 52.639 94.361-393.711 1.00 80.33 C ANISOU 608 CG GLU A 100 11518 8834 10169 -674 92 1290 C ATOM 609 CD GLU A 100 53.125 93.839-392.386 1.00 80.85 C ANISOU 609 CD GLU A 100 11785 8644 10289 -689 -87 1465 C ATOM 610 OE1 GLU A 100 52.286 93.705-391.468 1.00 81.38 O ANISOU 610 OE1 GLU A 100 12026 8621 10272 -607 -130 1438 O ATOM 611 OE2 GLU A 100 54.341 93.569-392.268 1.00 80.82 O ANISOU 611 OE2 GLU A 100 11776 8525 10408 -778 -191 1649 O ATOM 612 N TYR A 101 49.974 97.859-392.151 1.00 60.38 N ANISOU 612 N TYR A 101 8777 6850 7313 -254 272 1187 N ATOM 613 CA TYR A 101 49.729 99.293-392.083 1.00 60.76 C ANISOU 613 CA TYR A 101 8641 7134 7311 -172 340 1190 C ATOM 614 C TYR A 101 49.894 99.795-390.665 1.00 60.76 C ANISOU 614 C TYR A 101 8696 7089 7302 -89 253 1311 C ATOM 615 O TYR A 101 49.519 99.119-389.711 1.00 57.26 O ANISOU 615 O TYR A 101 8470 6464 6821 -54 182 1349 O ATOM 616 CB TYR A 101 48.338 99.647-392.603 1.00 60.43 C ANISOU 616 CB TYR A 101 8540 7256 7166 -124 476 1074 C ATOM 617 CG TYR A 101 47.225 99.482-391.592 1.00 56.68 C ANISOU 617 CG TYR A 101 8210 6728 6599 -18 502 1096 C ATOM 618 CD1 TYR A 101 46.399 98.368-391.615 1.00 56.91 C ANISOU 618 CD1 TYR A 101 8414 6624 6584 2 528 1053 C ATOM 619 CD2 TYR A 101 46.991 100.446-390.621 1.00 57.17 C ANISOU 619 CD2 TYR A 101 8237 6875 6610 77 510 1167 C ATOM 620 CE1 TYR A 101 45.378 98.214-390.701 1.00 56.97 C ANISOU 620 CE1 TYR A 101 8579 6578 6488 132 568 1093 C ATOM 621 CE2 TYR A 101 45.975 100.296-389.701 1.00 58.94 C ANISOU 621 CE2 TYR A 101 8614 7049 6732 191 550 1201 C ATOM 622 CZ TYR A 101 45.172 99.178-389.747 1.00 58.14 C ANISOU 622 CZ TYR A 101 8706 6809 6576 228 582 1170 C ATOM 623 OH TYR A 101 44.157 99.023-388.834 1.00 58.07 O ANISOU 623 OH TYR A 101 8873 6744 6447 374 637 1224 O ATOM 624 N THR A 102 50.446 100.990-390.529 1.00 61.87 N ANISOU 624 N THR A 102 8649 7392 7468 -50 253 1374 N ATOM 625 CA THR A 102 50.723 101.540-389.213 1.00 65.30 C ANISOU 625 CA THR A 102 9100 7802 7909 22 156 1498 C ATOM 626 C THR A 102 50.345 103.013-389.179 1.00 65.85 C ANISOU 626 C THR A 102 8954 8134 7932 100 256 1473 C ATOM 627 O THR A 102 50.893 103.817-389.929 1.00 66.16 O ANISOU 627 O THR A 102 8793 8334 8010 93 304 1466 O ATOM 628 CB THR A 102 52.212 101.393-388.865 1.00 62.58 C ANISOU 628 CB THR A 102 8736 7344 7699 -20 -6 1675 C ATOM 629 OG1 THR A 102 52.771 100.302-389.610 1.00 57.58 O ANISOU 629 OG1 THR A 102 8183 6561 7135 -128 -35 1680 O ATOM 630 CG2 THR A 102 52.393 101.149-387.371 1.00 64.51 C ANISOU 630 CG2 THR A 102 9148 7409 7952 14 -186 1817 C ATOM 631 N ILE A 103 49.401 103.365-388.316 1.00 60.93 N ANISOU 631 N ILE A 103 8386 7546 7218 180 291 1467 N ATOM 632 CA ILE A 103 48.967 104.750-388.197 1.00 59.57 C ANISOU 632 CA ILE A 103 8011 7616 7005 243 390 1453 C ATOM 633 C ILE A 103 50.075 105.607-387.591 1.00 58.29 C ANISOU 633 C ILE A 103 7699 7517 6932 273 291 1569 C ATOM 634 O ILE A 103 50.073 105.893-386.392 1.00 59.73 O ANISOU 634 O ILE A 103 7917 7672 7106 333 214 1651 O ATOM 635 CB ILE A 103 47.678 104.853-387.366 1.00 59.35 C ANISOU 635 CB ILE A 103 8088 7606 6857 327 466 1445 C ATOM 636 CG1 ILE A 103 46.548 104.087-388.059 1.00 57.76 C ANISOU 636 CG1 ILE A 103 7997 7373 6576 319 579 1361 C ATOM 637 CG2 ILE A 103 47.279 106.305-387.162 1.00 60.00 C ANISOU 637 CG2 ILE A 103 7951 7937 6911 376 565 1451 C ATOM 638 CD1 ILE A 103 45.227 104.187-387.347 1.00 57.95 C ANISOU 638 CD1 ILE A 103 8119 7427 6474 427 684 1388 C ATOM 639 N SER A 104 51.020 106.009-388.436 1.00 56.17 N ANISOU 639 N SER A 104 7265 7331 6745 244 292 1585 N ATOM 640 CA SER A 104 52.194 106.761-388.003 1.00 56.68 C ANISOU 640 CA SER A 104 7169 7455 6910 290 201 1724 C ATOM 641 C SER A 104 51.833 108.009-387.213 1.00 55.75 C ANISOU 641 C SER A 104 6897 7517 6767 370 234 1738 C ATOM 642 O SER A 104 52.501 108.353-386.241 1.00 56.45 O ANISOU 642 O SER A 104 6928 7595 6926 419 111 1874 O ATOM 643 CB SER A 104 53.061 107.135-389.206 1.00 56.84 C ANISOU 643 CB SER A 104 7041 7572 6985 282 252 1728 C ATOM 644 OG SER A 104 53.777 106.005-389.683 1.00 56.06 O ANISOU 644 OG SER A 104 7060 7293 6947 214 186 1783 O ATOM 645 N THR A 105 50.774 108.688-387.634 1.00 58.46 N ANISOU 645 N THR A 105 7166 8028 7018 377 392 1614 N ATOM 646 CA THR A 105 50.308 109.863-386.916 1.00 57.84 C ANISOU 646 CA THR A 105 6939 8125 6911 438 446 1622 C ATOM 647 C THR A 105 48.798 109.936-386.900 1.00 57.43 C ANISOU 647 C THR A 105 6948 8136 6737 432 586 1535 C ATOM 648 O THR A 105 48.178 110.243-387.913 1.00 56.75 O ANISOU 648 O THR A 105 6798 8158 6606 391 706 1450 O ATOM 649 CB THR A 105 50.851 111.139-387.532 1.00 56.30 C ANISOU 649 CB THR A 105 6489 8141 6763 466 505 1617 C ATOM 650 OG1 THR A 105 52.283 111.123-387.463 1.00 56.74 O ANISOU 650 OG1 THR A 105 6473 8150 6935 505 385 1743 O ATOM 651 CG2 THR A 105 50.323 112.344-386.776 1.00 58.08 C ANISOU 651 CG2 THR A 105 6551 8550 6966 515 567 1621 C ATOM 652 N PRO A 106 48.199 109.650-385.739 1.00 66.94 N ANISOU 652 N PRO A 106 8288 9265 7883 481 564 1578 N ATOM 653 CA PRO A 106 46.746 109.727-385.616 1.00 70.53 C ANISOU 653 CA PRO A 106 8801 9782 8215 505 714 1541 C ATOM 654 C PRO A 106 46.349 111.147-385.930 1.00 74.32 C ANISOU 654 C PRO A 106 9021 10524 8695 497 843 1521 C ATOM 655 O PRO A 106 46.954 112.076-385.396 1.00 77.76 O ANISOU 655 O PRO A 106 9288 11069 9190 525 805 1559 O ATOM 656 CB PRO A 106 46.497 109.455-384.129 1.00 76.81 C ANISOU 656 CB PRO A 106 9767 10467 8952 590 649 1619 C ATOM 657 CG PRO A 106 47.736 108.813-383.626 1.00 79.46 C ANISOU 657 CG PRO A 106 10206 10612 9375 581 430 1687 C ATOM 658 CD PRO A 106 48.854 109.366-384.453 1.00 74.77 C ANISOU 658 CD PRO A 106 9376 10121 8912 528 393 1689 C ATOM 659 N GLY A 107 45.365 111.331-386.794 1.00 87.87 N ANISOU 659 N GLY A 107 10697 12336 10352 455 980 1478 N ATOM 660 CA GLY A 107 44.928 112.676-387.100 1.00 86.27 C ANISOU 660 CA GLY A 107 10265 12364 10149 429 1090 1478 C ATOM 661 C GLY A 107 44.165 113.236-385.920 1.00 87.35 C ANISOU 661 C GLY A 107 10371 12588 10231 492 1173 1552 C ATOM 662 O GLY A 107 44.342 112.806-384.783 1.00 89.26 O ANISOU 662 O GLY A 107 10741 12723 10451 567 1108 1596 O ATOM 663 N SER A 108 43.318 114.213-386.197 1.00 61.22 N ANISOU 663 N SER A 108 6901 9466 6895 457 1310 1579 N ATOM 664 CA SER A 108 42.349 114.676-385.224 1.00 62.03 C ANISOU 664 CA SER A 108 6982 9659 6929 510 1432 1669 C ATOM 665 C SER A 108 41.097 114.991-386.022 1.00 66.11 C ANISOU 665 C SER A 108 7433 10288 7397 450 1582 1730 C ATOM 666 O SER A 108 41.161 115.122-387.242 1.00 68.87 O ANISOU 666 O SER A 108 7718 10668 7783 357 1561 1687 O ATOM 667 CB SER A 108 42.871 115.917-384.507 1.00 64.37 C ANISOU 667 CB SER A 108 7060 10112 7284 520 1427 1677 C ATOM 668 OG SER A 108 42.746 117.062-385.335 1.00 68.76 O ANISOU 668 OG SER A 108 7386 10853 7887 431 1497 1661 O ATOM 669 N ASN A 109 39.956 115.088-385.352 1.00 99.91 N ANISOU 669 N ASN A 109 11744 14623 11594 507 1726 1853 N ATOM 670 CA ASN A 109 38.720 115.477-386.024 1.00104.70 C ANISOU 670 CA ASN A 109 12261 15352 12170 450 1869 1971 C ATOM 671 C ASN A 109 38.343 114.635-387.246 1.00106.29 C ANISOU 671 C ASN A 109 12552 15469 12366 399 1838 1969 C ATOM 672 O ASN A 109 37.578 115.091-388.097 1.00112.05 O ANISOU 672 O ASN A 109 13165 16302 13105 311 1894 2059 O ATOM 673 CB ASN A 109 38.768 116.958-386.411 1.00104.73 C ANISOU 673 CB ASN A 109 11988 15560 12243 335 1905 1981 C ATOM 674 CG ASN A 109 38.763 117.874-385.203 1.00110.52 C ANISOU 674 CG ASN A 109 12597 16419 12976 379 1983 2024 C ATOM 675 OD1 ASN A 109 37.931 117.728-384.307 1.00114.55 O ANISOU 675 OD1 ASN A 109 13177 16944 13403 467 2109 2146 O ATOM 676 ND2 ASN A 109 39.691 118.829-385.174 1.00110.07 N ANISOU 676 ND2 ASN A 109 12357 16457 13007 332 1915 1933 N ATOM 677 N TYR A 110 38.881 113.422-387.338 1.00 59.62 N ANISOU 677 N TYR A 110 6841 9365 6446 446 1735 1879 N ATOM 678 CA TYR A 110 38.419 112.467-388.342 1.00 60.84 C ANISOU 678 CA TYR A 110 7097 9431 6588 420 1718 1884 C ATOM 679 C TYR A 110 37.164 111.792-387.809 1.00 60.15 C ANISOU 679 C TYR A 110 7149 9305 6400 544 1852 2045 C ATOM 680 O TYR A 110 36.788 112.002-386.660 1.00 61.51 O ANISOU 680 O TYR A 110 7373 9496 6503 655 1948 2132 O ATOM 681 CB TYR A 110 39.484 111.415-388.639 1.00 58.49 C ANISOU 681 CB TYR A 110 6954 8945 6326 417 1567 1732 C ATOM 682 CG TYR A 110 40.638 111.917-389.480 1.00 59.49 C ANISOU 682 CG TYR A 110 6961 9102 6542 309 1449 1604 C ATOM 683 CD1 TYR A 110 41.778 112.433-388.889 1.00 59.26 C ANISOU 683 CD1 TYR A 110 6873 9078 6565 325 1375 1543 C ATOM 684 CD2 TYR A 110 40.590 111.865-390.867 1.00 62.16 C ANISOU 684 CD2 TYR A 110 7255 9459 6904 206 1406 1562 C ATOM 685 CE1 TYR A 110 42.832 112.887-389.651 1.00 59.21 C ANISOU 685 CE1 TYR A 110 6769 9098 6629 262 1285 1454 C ATOM 686 CE2 TYR A 110 41.644 112.320-391.636 1.00 57.85 C ANISOU 686 CE2 TYR A 110 6637 8929 6414 135 1309 1454 C ATOM 687 CZ TYR A 110 42.759 112.828-391.023 1.00 57.30 C ANISOU 687 CZ TYR A 110 6512 8867 6391 173 1261 1406 C ATOM 688 OH TYR A 110 43.812 113.281-391.783 1.00 58.89 O ANISOU 688 OH TYR A 110 6651 9085 6638 136 1182 1326 O ATOM 689 N ALA A 111 36.515 110.977-388.631 1.00 65.90 N ANISOU 689 N ALA A 111 7944 9980 7116 542 1862 2095 N ATOM 690 CA ALA A 111 35.319 110.254-388.196 1.00 66.15 C ANISOU 690 CA ALA A 111 8115 9968 7050 692 1997 2270 C ATOM 691 C ALA A 111 35.405 108.826-388.724 1.00 64.48 C ANISOU 691 C ALA A 111 8038 9619 6841 710 1942 2241 C ATOM 692 O ALA A 111 36.429 108.431-389.266 1.00 65.42 O ANISOU 692 O ALA A 111 8070 9745 7041 573 1831 2145 O ATOM 693 CB ALA A 111 34.102 111.134-388.314 1.00 93.67 C ANISOU 693 CB ALA A 111 11423 13649 10520 682 2153 2507 C ATOM 694 N VAL A 112 34.328 108.059-388.576 1.00 66.29 N ANISOU 694 N VAL A 112 8489 9722 6977 888 2020 2327 N ATOM 695 CA VAL A 112 34.307 106.663-389.015 1.00 64.53 C ANISOU 695 CA VAL A 112 8401 9361 6755 926 1976 2302 C ATOM 696 C VAL A 112 34.136 105.913-390.340 1.00 65.37 C ANISOU 696 C VAL A 112 8297 9598 6944 797 1956 2373 C ATOM 697 O VAL A 112 34.513 104.750-390.448 1.00 70.71 O ANISOU 697 O VAL A 112 8760 10458 7648 715 2003 2502 O ATOM 698 CB VAL A 112 33.357 105.776-388.174 1.00 69.63 C ANISOU 698 CB VAL A 112 9290 9896 7269 1170 2113 2460 C ATOM 699 CG1 VAL A 112 33.249 104.394-388.760 1.00 67.18 C ANISOU 699 CG1 VAL A 112 9130 9428 6966 1217 2061 2412 C ATOM 700 CG2 VAL A 112 33.852 105.689-386.738 1.00 65.18 C ANISOU 700 CG2 VAL A 112 8961 9198 6607 1294 2111 2406 C ATOM 701 N GLY A 113 33.548 106.559-391.341 1.00 88.16 N ANISOU 701 N GLY A 113 11242 12384 9870 767 1869 2294 N ATOM 702 CA GLY A 113 33.359 105.932-392.641 1.00 86.81 C ANISOU 702 CA GLY A 113 10890 12320 9772 646 1817 2364 C ATOM 703 C GLY A 113 34.007 106.953-393.570 1.00 88.91 C ANISOU 703 C GLY A 113 10982 12676 10125 423 1677 2234 C ATOM 704 O GLY A 113 33.517 107.174-394.681 1.00 90.39 O ANISOU 704 O GLY A 113 11075 12902 10367 311 1583 2242 O ATOM 705 N ASP A 114 35.086 107.598-393.131 1.00 65.81 N ANISOU 705 N ASP A 114 8018 9783 7204 370 1657 2128 N ATOM 706 CA ASP A 114 35.816 108.494-394.019 1.00 63.00 C ANISOU 706 CA ASP A 114 7538 9487 6912 193 1528 1993 C ATOM 707 C ASP A 114 36.613 107.526-394.865 1.00 60.76 C ANISOU 707 C ASP A 114 7346 9071 6668 132 1397 1807 C ATOM 708 O ASP A 114 37.261 106.634-394.333 1.00 60.23 O ANISOU 708 O ASP A 114 7437 8852 6595 199 1382 1692 O ATOM 709 CB ASP A 114 36.754 109.400-393.230 1.00 62.10 C ANISOU 709 CB ASP A 114 7394 9402 6801 186 1529 1895 C ATOM 710 CG ASP A 114 36.017 110.515-392.526 1.00 70.46 C ANISOU 710 CG ASP A 114 8325 10614 7832 213 1654 2068 C ATOM 711 OD1 ASP A 114 34.876 110.815-392.938 1.00 69.77 O ANISOU 711 OD1 ASP A 114 8137 10632 7739 190 1716 2269 O ATOM 712 OD2 ASP A 114 36.573 111.092-391.566 1.00 73.98 O ANISOU 712 OD2 ASP A 114 8762 11080 8268 254 1687 2019 O ATOM 713 N LYS A 115 36.550 107.692-396.180 1.00 63.38 N ANISOU 713 N LYS A 115 7590 9454 7037 0 1294 1791 N ATOM 714 CA LYS A 115 37.124 106.714-397.094 1.00 62.20 C ANISOU 714 CA LYS A 115 7520 9194 6920 -59 1181 1639 C ATOM 715 C LYS A 115 38.620 106.909-397.309 1.00 61.09 C ANISOU 715 C LYS A 115 7421 8990 6801 -125 1093 1431 C ATOM 716 O LYS A 115 39.133 108.018-397.230 1.00 60.53 O ANISOU 716 O LYS A 115 7276 8995 6726 -162 1080 1410 O ATOM 717 CB LYS A 115 36.366 106.706-398.428 1.00 68.59 C ANISOU 717 CB LYS A 115 8235 10074 7751 -162 1093 1726 C ATOM 718 CG LYS A 115 34.889 106.377-398.269 1.00 65.16 C ANISOU 718 CG LYS A 115 7746 9699 7311 -79 1178 1976 C ATOM 719 CD LYS A 115 34.327 105.644-399.472 1.00 65.45 C ANISOU 719 CD LYS A 115 7746 9734 7389 -141 1073 2024 C ATOM 720 CE LYS A 115 32.956 105.071-399.143 1.00 70.52 C ANISOU 720 CE LYS A 115 8351 10413 8030 -5 1179 2284 C ATOM 721 NZ LYS A 115 32.385 104.264-400.258 1.00 69.77 N ANISOU 721 NZ LYS A 115 8201 10319 7988 -46 1072 2348 N ATOM 722 N ILE A 116 39.306 105.803-397.571 1.00 70.10 N ANISOU 722 N ILE A 116 8678 9989 7966 -129 1039 1296 N ATOM 723 CA ILE A 116 40.746 105.806-397.759 1.00 66.42 C ANISOU 723 CA ILE A 116 8261 9448 7526 -174 968 1137 C ATOM 724 C ILE A 116 41.065 105.331-399.168 1.00 63.43 C ANISOU 724 C ILE A 116 7897 9041 7164 -280 867 1038 C ATOM 725 O ILE A 116 40.334 104.523-399.742 1.00 66.44 O ANISOU 725 O ILE A 116 8289 9402 7554 -302 848 1059 O ATOM 726 CB ILE A 116 41.435 104.885-396.740 1.00 68.19 C ANISOU 726 CB ILE A 116 8627 9509 7772 -96 986 1084 C ATOM 727 CG1 ILE A 116 41.015 105.259-395.318 1.00 73.72 C ANISOU 727 CG1 ILE A 116 9348 10224 8439 20 1074 1187 C ATOM 728 CG2 ILE A 116 42.942 104.959-396.882 1.00 67.99 C ANISOU 728 CG2 ILE A 116 8629 9418 7787 -136 916 976 C ATOM 729 CD1 ILE A 116 41.594 104.350-394.252 1.00 72.46 C ANISOU 729 CD1 ILE A 116 9365 9880 8287 98 1060 1160 C ATOM 730 N THR A 117 42.157 105.835-399.725 1.00 58.27 N ANISOU 730 N THR A 117 7245 8387 6509 -332 805 941 N ATOM 731 CA THR A 117 42.512 105.531-401.100 1.00 59.27 C ANISOU 731 CA THR A 117 7402 8491 6627 -426 710 849 C ATOM 732 C THR A 117 43.967 105.123-401.223 1.00 58.08 C ANISOU 732 C THR A 117 7335 8235 6498 -424 690 735 C ATOM 733 O THR A 117 44.861 105.847-400.792 1.00 58.43 O ANISOU 733 O THR A 117 7369 8292 6540 -378 707 735 O ATOM 734 CB THR A 117 42.255 106.737-402.010 1.00 61.53 C ANISOU 734 CB THR A 117 7626 8894 6857 -494 638 881 C ATOM 735 OG1 THR A 117 40.854 107.045-402.011 1.00 65.65 O ANISOU 735 OG1 THR A 117 8059 9511 7375 -516 641 1028 O ATOM 736 CG2 THR A 117 42.707 106.444-403.430 1.00 58.36 C ANISOU 736 CG2 THR A 117 7295 8453 6425 -579 525 781 C ATOM 737 N VAL A 118 44.197 103.957-401.816 1.00 59.98 N ANISOU 737 N VAL A 118 7647 8376 6766 -472 658 658 N ATOM 738 CA VAL A 118 45.544 103.447-402.003 1.00 56.69 C ANISOU 738 CA VAL A 118 7308 7853 6378 -482 648 580 C ATOM 739 C VAL A 118 45.956 103.666-403.443 1.00 59.76 C ANISOU 739 C VAL A 118 7724 8270 6713 -550 579 506 C ATOM 740 O VAL A 118 45.314 103.171-404.364 1.00 57.66 O ANISOU 740 O VAL A 118 7463 8013 6432 -625 522 465 O ATOM 741 CB VAL A 118 45.637 101.942-401.701 1.00 59.24 C ANISOU 741 CB VAL A 118 7709 8029 6772 -500 661 545 C ATOM 742 CG1 VAL A 118 47.088 101.503-401.690 1.00 55.74 C ANISOU 742 CG1 VAL A 118 7332 7473 6373 -511 657 516 C ATOM 743 CG2 VAL A 118 44.972 101.613-400.373 1.00 56.96 C ANISOU 743 CG2 VAL A 118 7441 7693 6507 -423 713 620 C ATOM 744 N LYS A 119 47.033 104.408-403.637 1.00 58.84 N ANISOU 744 N LYS A 119 7632 8164 6560 -510 581 500 N ATOM 745 CA LYS A 119 47.481 104.742-404.976 1.00 70.55 C ANISOU 745 CA LYS A 119 9182 9663 7959 -544 520 439 C ATOM 746 C LYS A 119 48.774 104.012-405.317 1.00 72.32 C ANISOU 746 C LYS A 119 9491 9784 8204 -534 549 400 C ATOM 747 O LYS A 119 49.598 103.731-404.443 1.00 72.88 O ANISOU 747 O LYS A 119 9553 9791 8348 -478 609 457 O ATOM 748 CB LYS A 119 47.669 106.260-405.114 1.00 80.60 C ANISOU 748 CB LYS A 119 10447 11029 9147 -485 504 477 C ATOM 749 CG LYS A 119 46.431 107.079-404.737 1.00 78.01 C ANISOU 749 CG LYS A 119 10024 10807 8808 -507 484 544 C ATOM 750 CD LYS A 119 46.714 108.583-404.678 1.00 80.98 C ANISOU 750 CD LYS A 119 10384 11265 9118 -447 480 586 C ATOM 751 CE LYS A 119 46.516 109.261-406.031 1.00 90.01 C ANISOU 751 CE LYS A 119 11628 12427 10143 -502 361 558 C ATOM 752 NZ LYS A 119 46.545 110.752-405.937 1.00 88.13 N ANISOU 752 NZ LYS A 119 11378 12264 9843 -458 347 609 N ATOM 753 N TYR A 120 48.937 103.692-406.595 1.00 75.72 N ANISOU 753 N TYR A 120 10004 10196 8571 -592 497 324 N ATOM 754 CA TYR A 120 50.197 103.160-407.089 1.00 79.46 C ANISOU 754 CA TYR A 120 10564 10586 9040 -575 536 306 C ATOM 755 C TYR A 120 50.865 104.216-407.955 1.00 86.87 C ANISOU 755 C TYR A 120 11604 11565 9839 -496 518 310 C ATOM 756 O TYR A 120 50.499 104.405-409.114 1.00 87.78 O ANISOU 756 O TYR A 120 11809 11698 9845 -544 432 239 O ATOM 757 CB TYR A 120 49.962 101.879-407.884 1.00 77.68 C ANISOU 757 CB TYR A 120 10375 10298 8842 -692 505 214 C ATOM 758 CG TYR A 120 51.227 101.214-408.382 1.00 75.81 C ANISOU 758 CG TYR A 120 10220 9974 8611 -689 562 211 C ATOM 759 CD1 TYR A 120 52.435 101.386-407.717 1.00 74.74 C ANISOU 759 CD1 TYR A 120 10090 9791 8516 -594 648 327 C ATOM 760 CD2 TYR A 120 51.207 100.392-409.501 1.00 72.84 C ANISOU 760 CD2 TYR A 120 9904 9565 8208 -783 528 115 C ATOM 761 CE1 TYR A 120 53.588 100.772-408.168 1.00 74.67 C ANISOU 761 CE1 TYR A 120 10147 9705 8519 -588 710 369 C ATOM 762 CE2 TYR A 120 52.355 99.775-409.955 1.00 70.33 C ANISOU 762 CE2 TYR A 120 9657 9171 7895 -784 597 129 C ATOM 763 CZ TYR A 120 53.540 99.967-409.286 1.00 70.81 C ANISOU 763 CZ TYR A 120 9724 9185 7995 -685 694 267 C ATOM 764 OH TYR A 120 54.681 99.349-409.740 1.00 70.36 O ANISOU 764 OH TYR A 120 9730 9055 7949 -682 772 323 O ATOM 765 N VAL A 121 51.839 104.909-407.379 1.00 79.91 N ANISOU 765 N VAL A 121 10717 10690 8957 -366 590 405 N ATOM 766 CA VAL A 121 52.492 106.013-408.066 1.00 80.89 C ANISOU 766 CA VAL A 121 10947 10847 8939 -249 588 427 C ATOM 767 C VAL A 121 51.458 107.020-408.555 1.00 84.17 C ANISOU 767 C VAL A 121 11391 11341 9249 -284 482 376 C ATOM 768 O VAL A 121 51.164 107.093-409.750 1.00 82.62 O ANISOU 768 O VAL A 121 11328 11130 8933 -335 387 305 O ATOM 769 CB VAL A 121 53.317 105.522-409.262 1.00 76.04 C ANISOU 769 CB VAL A 121 10495 10165 8232 -233 601 395 C ATOM 770 CG1 VAL A 121 54.240 106.623-409.747 1.00 78.34 C ANISOU 770 CG1 VAL A 121 10917 10471 8378 -55 635 459 C ATOM 771 CG2 VAL A 121 54.118 104.296-408.879 1.00 77.85 C ANISOU 771 CG2 VAL A 121 10684 10309 8587 -256 690 450 C ATOM 772 N SER A 122 50.901 107.785-407.619 1.00 95.00 N ANISOU 772 N SER A 122 12640 12788 10668 -265 489 427 N ATOM 773 CA SER A 122 49.917 108.819-407.933 1.00 96.80 C ANISOU 773 CA SER A 122 12872 13091 10818 -306 394 420 C ATOM 774 C SER A 122 48.834 108.319-408.889 1.00100.06 C ANISOU 774 C SER A 122 13331 13493 11193 -460 263 357 C ATOM 775 O SER A 122 48.358 109.063-409.748 1.00101.79 O ANISOU 775 O SER A 122 13648 13728 11298 -500 139 350 O ATOM 776 CB SER A 122 50.606 110.060-408.509 1.00 92.93 C ANISOU 776 CB SER A 122 12515 12611 10183 -185 377 437 C ATOM 777 OG SER A 122 51.545 110.595-407.593 1.00 85.02 O ANISOU 777 OG SER A 122 11438 11637 9228 -31 492 519 O ATOM 778 N ASP A 123 48.450 107.056-408.730 1.00 91.77 N ANISOU 778 N ASP A 123 12215 12410 10243 -544 278 326 N ATOM 779 CA ASP A 123 47.427 106.456-409.575 1.00 91.38 C ANISOU 779 CA ASP A 123 12176 12361 10185 -680 156 284 C ATOM 780 C ASP A 123 46.508 105.582-408.731 1.00 83.10 C ANISOU 780 C ASP A 123 10969 11329 9276 -736 198 315 C ATOM 781 O ASP A 123 46.971 104.693-408.020 1.00 81.41 O ANISOU 781 O ASP A 123 10718 11059 9155 -708 300 300 O ATOM 782 CB ASP A 123 48.074 105.630-410.689 1.00 92.78 C ANISOU 782 CB ASP A 123 12489 12458 10306 -711 121 190 C ATOM 783 CG ASP A 123 47.265 105.643-411.972 1.00 99.80 C ANISOU 783 CG ASP A 123 13459 13352 11107 -824 -65 154 C ATOM 784 OD1 ASP A 123 46.017 105.656-411.887 1.00100.68 O ANISOU 784 OD1 ASP A 123 13462 13522 11271 -913 -154 210 O ATOM 785 OD2 ASP A 123 47.879 105.643-413.064 1.00 97.33 O ANISOU 785 OD2 ASP A 123 13326 12985 10670 -818 -128 89 O ATOM 786 N ASP A 124 45.206 105.832-408.816 1.00 87.73 N ANISOU 786 N ASP A 124 11478 11984 9873 -807 115 381 N ATOM 787 CA ASP A 124 44.238 105.157-407.955 1.00 88.23 C ANISOU 787 CA ASP A 124 11402 12072 10048 -821 171 446 C ATOM 788 C ASP A 124 44.061 103.668-408.255 1.00 87.01 C ANISOU 788 C ASP A 124 11240 11855 9964 -873 169 382 C ATOM 789 O ASP A 124 43.786 103.285-409.392 1.00 92.96 O ANISOU 789 O ASP A 124 12029 12604 10688 -958 52 339 O ATOM 790 CB ASP A 124 42.881 105.858-408.038 1.00 97.26 C ANISOU 790 CB ASP A 124 12456 13314 11184 -872 88 581 C ATOM 791 CG ASP A 124 42.913 107.257-407.463 1.00102.32 C ANISOU 791 CG ASP A 124 13071 14022 11785 -825 118 659 C ATOM 792 OD1 ASP A 124 44.024 107.796-407.275 1.00104.50 O ANISOU 792 OD1 ASP A 124 13415 14272 12017 -752 171 596 O ATOM 793 OD2 ASP A 124 41.826 107.815-407.199 1.00102.69 O ANISOU 793 OD2 ASP A 124 13018 14151 11849 -857 95 800 O ATOM 794 N ILE A 125 44.206 102.835-407.226 1.00 61.44 N ANISOU 794 N ILE A 125 7965 8561 6819 -823 288 378 N ATOM 795 CA ILE A 125 43.985 101.396-407.352 1.00 58.31 C ANISOU 795 CA ILE A 125 7561 8095 6500 -864 299 324 C ATOM 796 C ILE A 125 42.764 100.981-406.538 1.00 60.90 C ANISOU 796 C ILE A 125 7798 8449 6893 -825 342 424 C ATOM 797 O ILE A 125 41.822 100.377-407.057 1.00 57.91 O ANISOU 797 O ILE A 125 7360 8098 6544 -865 286 454 O ATOM 798 CB ILE A 125 45.186 100.586-406.836 1.00 55.78 C ANISOU 798 CB ILE A 125 7310 7650 6234 -839 391 252 C ATOM 799 CG1 ILE A 125 46.491 101.120-407.419 1.00 61.62 C ANISOU 799 CG1 ILE A 125 8138 8370 6906 -831 388 204 C ATOM 800 CG2 ILE A 125 45.013 99.119-407.175 1.00 56.94 C ANISOU 800 CG2 ILE A 125 7460 7718 6455 -904 388 181 C ATOM 801 CD1 ILE A 125 46.727 100.715-408.855 1.00 59.96 C ANISOU 801 CD1 ILE A 125 7994 8147 6642 -915 307 110 C ATOM 802 N GLU A 126 42.795 101.310-405.252 1.00 65.44 N ANISOU 802 N GLU A 126 8365 9015 7485 -732 444 491 N ATOM 803 CA GLU A 126 41.713 100.967-404.341 1.00 65.28 C ANISOU 803 CA GLU A 126 8294 9007 7502 -659 511 601 C ATOM 804 C GLU A 126 41.163 102.234-403.706 1.00 65.73 C ANISOU 804 C GLU A 126 8285 9173 7517 -603 545 733 C ATOM 805 O GLU A 126 41.919 103.125-403.325 1.00 62.80 O ANISOU 805 O GLU A 126 7928 8817 7115 -582 566 717 O ATOM 806 CB GLU A 126 42.216 100.004-403.265 1.00 66.49 C ANISOU 806 CB GLU A 126 8536 9018 7708 -592 601 564 C ATOM 807 CG GLU A 126 41.180 99.621-402.220 1.00 67.40 C ANISOU 807 CG GLU A 126 8656 9118 7835 -481 682 676 C ATOM 808 CD GLU A 126 40.002 98.867-402.805 1.00 69.53 C ANISOU 808 CD GLU A 126 8868 9422 8128 -479 663 731 C ATOM 809 OE1 GLU A 126 39.958 97.624-402.660 1.00 67.20 O ANISOU 809 OE1 GLU A 126 8641 9012 7879 -455 686 682 O ATOM 810 OE2 GLU A 126 39.124 99.516-403.413 1.00 69.82 O ANISOU 810 OE2 GLU A 126 8789 9596 8144 -502 616 838 O ATOM 811 N THR A 127 39.844 102.316-403.599 1.00 60.63 N ANISOU 811 N THR A 127 7554 8609 6875 -576 555 882 N ATOM 812 CA THR A 127 39.202 103.526-403.104 1.00 62.54 C ANISOU 812 CA THR A 127 7714 8966 7082 -543 588 1034 C ATOM 813 C THR A 127 38.053 103.205-402.163 1.00 63.03 C ANISOU 813 C THR A 127 7736 9054 7160 -428 699 1203 C ATOM 814 O THR A 127 37.154 104.021-401.966 1.00 63.12 O ANISOU 814 O THR A 127 7651 9180 7153 -411 725 1384 O ATOM 815 CB THR A 127 38.646 104.371-404.264 1.00 66.53 C ANISOU 815 CB THR A 127 8141 9578 7558 -652 453 1116 C ATOM 816 OG1 THR A 127 37.506 103.713-404.834 1.00 67.40 O ANISOU 816 OG1 THR A 127 8179 9724 7706 -673 397 1238 O ATOM 817 CG2 THR A 127 39.707 104.569-405.336 1.00 68.27 C ANISOU 817 CG2 THR A 127 8445 9758 7738 -746 336 952 C ATOM 818 N GLU A 128 38.080 102.013-401.585 1.00 90.22 N ANISOU 818 N GLU A 128 11267 12384 10630 -345 767 1159 N ATOM 819 CA GLU A 128 36.993 101.585-400.718 1.00 96.03 C ANISOU 819 CA GLU A 128 12007 13121 11358 -202 881 1323 C ATOM 820 C GLU A 128 37.448 101.368-399.286 1.00 94.17 C ANISOU 820 C GLU A 128 11910 12775 11094 -80 989 1292 C ATOM 821 O GLU A 128 36.682 100.904-398.440 1.00 96.30 O ANISOU 821 O GLU A 128 12246 13009 11335 66 1091 1408 O ATOM 822 CB GLU A 128 36.312 100.339-401.282 1.00100.25 C ANISOU 822 CB GLU A 128 12539 13615 11935 -178 861 1349 C ATOM 823 CG GLU A 128 35.486 100.650-402.508 1.00103.77 C ANISOU 823 CG GLU A 128 12825 14193 12408 -269 750 1470 C ATOM 824 CD GLU A 128 34.764 101.977-402.373 1.00108.66 C ANISOU 824 CD GLU A 128 13328 14960 12996 -275 761 1681 C ATOM 825 OE1 GLU A 128 33.958 102.121-401.429 1.00108.03 O ANISOU 825 OE1 GLU A 128 13234 14918 12894 -137 896 1868 O ATOM 826 OE2 GLU A 128 35.009 102.880-403.204 1.00109.98 O ANISOU 826 OE2 GLU A 128 13433 15197 13156 -416 636 1667 O ATOM 827 N GLY A 129 38.700 101.714-399.017 1.00 59.30 N ANISOU 827 N GLY A 129 7549 8301 6680 -130 957 1153 N ATOM 828 CA GLY A 129 39.206 101.691-397.660 1.00 59.87 C ANISOU 828 CA GLY A 129 7741 8277 6731 -32 1021 1144 C ATOM 829 C GLY A 129 38.417 102.699-396.859 1.00 64.54 C ANISOU 829 C GLY A 129 8266 8989 7267 55 1115 1306 C ATOM 830 O GLY A 129 37.721 103.536-397.428 1.00 65.19 O ANISOU 830 O GLY A 129 8199 9228 7343 10 1117 1411 O ATOM 831 N LYS A 130 38.512 102.623-395.540 1.00 63.33 N ANISOU 831 N LYS A 130 8231 8756 7074 174 1183 1339 N ATOM 832 CA LYS A 130 37.758 103.537-394.699 1.00 60.07 C ANISOU 832 CA LYS A 130 7764 8456 6602 267 1289 1496 C ATOM 833 C LYS A 130 38.142 103.432-393.233 1.00 60.62 C ANISOU 833 C LYS A 130 7996 8413 6622 386 1330 1497 C ATOM 834 O LYS A 130 38.182 102.339-392.674 1.00 63.06 O ANISOU 834 O LYS A 130 8511 8544 6906 475 1328 1475 O ATOM 835 CB LYS A 130 36.257 103.292-394.863 1.00 62.41 C ANISOU 835 CB LYS A 130 8021 8828 6864 357 1385 1691 C ATOM 836 CG LYS A 130 35.888 101.830-395.017 1.00 62.59 C ANISOU 836 CG LYS A 130 8184 8711 6887 437 1390 1680 C ATOM 837 CD LYS A 130 34.381 101.638-395.088 1.00 76.65 C ANISOU 837 CD LYS A 130 9914 10577 8633 565 1499 1919 C ATOM 838 CE LYS A 130 33.733 101.854-393.728 1.00 83.31 C ANISOU 838 CE LYS A 130 10872 11411 9372 766 1656 2084 C ATOM 839 NZ LYS A 130 32.329 101.348-393.689 1.00 87.76 N ANISOU 839 NZ LYS A 130 11444 12011 9890 946 1784 2333 N ATOM 840 N ILE A 131 38.431 104.578-392.622 1.00 59.95 N ANISOU 840 N ILE A 131 7826 8426 6525 383 1352 1525 N ATOM 841 CA ILE A 131 38.640 104.655-391.185 1.00 60.42 C ANISOU 841 CA ILE A 131 8019 8408 6529 500 1385 1557 C ATOM 842 C ILE A 131 37.488 103.940-390.508 1.00 60.64 C ANISOU 842 C ILE A 131 8214 8367 6460 674 1500 1693 C ATOM 843 O ILE A 131 36.352 104.027-390.968 1.00 65.58 O ANISOU 843 O ILE A 131 8753 9105 7061 713 1600 1829 O ATOM 844 CB ILE A 131 38.667 106.108-390.710 1.00 60.97 C ANISOU 844 CB ILE A 131 7922 8651 6592 487 1433 1615 C ATOM 845 CG1 ILE A 131 39.875 106.840-391.301 1.00 60.65 C ANISOU 845 CG1 ILE A 131 7738 8669 6639 350 1325 1490 C ATOM 846 CG2 ILE A 131 38.699 106.169-389.195 1.00 65.95 C ANISOU 846 CG2 ILE A 131 8694 9212 7153 620 1471 1669 C ATOM 847 CD1 ILE A 131 39.891 108.331-391.011 1.00 64.34 C ANISOU 847 CD1 ILE A 131 8014 9321 7110 325 1369 1539 C ATOM 848 N THR A 132 37.769 103.220-389.429 1.00 64.05 N ANISOU 848 N THR A 132 8900 8605 6831 789 1478 1677 N ATOM 849 CA THR A 132 36.734 102.413-388.796 1.00 65.97 C ANISOU 849 CA THR A 132 9360 8745 6959 985 1585 1800 C ATOM 850 C THR A 132 36.677 102.568-387.284 1.00 65.28 C ANISOU 850 C THR A 132 9483 8568 6754 1141 1621 1870 C ATOM 851 O THR A 132 35.755 102.073-386.648 1.00 73.47 O ANISOU 851 O THR A 132 10720 9532 7665 1338 1733 1999 O ATOM 852 CB THR A 132 36.879 100.921-389.146 1.00 66.55 C ANISOU 852 CB THR A 132 9635 8605 7046 1005 1517 1720 C ATOM 853 OG1 THR A 132 38.227 100.501-388.906 1.00 65.19 O ANISOU 853 OG1 THR A 132 9579 8257 6934 905 1349 1567 O ATOM 854 CG2 THR A 132 36.531 100.684-390.604 1.00 64.73 C ANISOU 854 CG2 THR A 132 9210 8481 6902 899 1517 1698 C ATOM 855 N GLU A 133 37.654 103.249-386.705 1.00 62.97 N ANISOU 855 N GLU A 133 9153 8278 6496 1069 1524 1800 N ATOM 856 CA GLU A 133 37.607 103.510-385.276 1.00 65.07 C ANISOU 856 CA GLU A 133 9597 8475 6651 1205 1540 1870 C ATOM 857 C GLU A 133 38.396 104.747-384.909 1.00 71.83 C ANISOU 857 C GLU A 133 10252 9468 7572 1106 1481 1834 C ATOM 858 O GLU A 133 39.611 104.803-385.105 1.00 67.38 O ANISOU 858 O GLU A 133 9626 8858 7118 977 1320 1722 O ATOM 859 CB GLU A 133 38.124 102.315-384.477 1.00 71.78 C ANISOU 859 CB GLU A 133 10821 9011 7441 1285 1404 1824 C ATOM 860 CG GLU A 133 38.026 102.507-382.967 1.00 80.40 C ANISOU 860 CG GLU A 133 12154 10002 8394 1440 1395 1906 C ATOM 861 CD GLU A 133 38.761 101.434-382.177 1.00 84.20 C ANISOU 861 CD GLU A 133 13012 10149 8833 1477 1194 1861 C ATOM 862 OE1 GLU A 133 38.568 100.227-382.465 1.00 80.09 O ANISOU 862 OE1 GLU A 133 12714 9433 8284 1523 1171 1838 O ATOM 863 OE2 GLU A 133 39.525 101.805-381.255 1.00 82.72 O ANISOU 863 OE2 GLU A 133 12896 9889 8643 1458 1048 1861 O ATOM 864 N VAL A 134 37.693 105.739-384.379 1.00 68.72 N ANISOU 864 N VAL A 134 9748 9248 7113 1174 1621 1949 N ATOM 865 CA VAL A 134 38.328 106.937-383.858 1.00 64.44 C ANISOU 865 CA VAL A 134 9023 8840 6620 1108 1582 1929 C ATOM 866 C VAL A 134 37.982 107.053-382.382 1.00 67.19 C ANISOU 866 C VAL A 134 9574 9125 6830 1274 1623 2024 C ATOM 867 O VAL A 134 37.136 106.313-381.879 1.00 67.45 O ANISOU 867 O VAL A 134 9877 9034 6718 1447 1711 2119 O ATOM 868 CB VAL A 134 37.839 108.187-384.593 1.00 61.38 C ANISOU 868 CB VAL A 134 8289 8740 6293 1012 1709 1978 C ATOM 869 CG1 VAL A 134 38.430 108.243-385.989 1.00 60.69 C ANISOU 869 CG1 VAL A 134 8016 8706 6338 838 1624 1865 C ATOM 870 CG2 VAL A 134 36.320 108.199-384.658 1.00 65.20 C ANISOU 870 CG2 VAL A 134 8778 9317 6677 1122 1920 2162 C ATOM 871 N ASP A 135 38.640 107.969-381.684 1.00 73.58 N ANISOU 871 N ASP A 135 10266 10015 7676 1235 1556 2004 N ATOM 872 CA ASP A 135 38.301 108.227-380.292 1.00 72.31 C ANISOU 872 CA ASP A 135 10272 9822 7381 1382 1593 2095 C ATOM 873 C ASP A 135 37.423 109.466-380.184 1.00 72.83 C ANISOU 873 C ASP A 135 10090 10164 7419 1397 1809 2205 C ATOM 874 O ASP A 135 36.677 109.792-381.103 1.00 78.03 O ANISOU 874 O ASP A 135 10554 10984 8109 1349 1961 2264 O ATOM 875 CB ASP A 135 39.559 108.381-379.434 1.00 77.09 C ANISOU 875 CB ASP A 135 10926 10325 8041 1343 1360 2029 C ATOM 876 CG ASP A 135 40.468 109.492-379.916 1.00 76.45 C ANISOU 876 CG ASP A 135 10461 10447 8138 1178 1297 1957 C ATOM 877 OD1 ASP A 135 40.151 110.119-380.946 1.00 73.99 O ANISOU 877 OD1 ASP A 135 9878 10336 7899 1085 1422 1939 O ATOM 878 OD2 ASP A 135 41.505 109.734-379.262 1.00 73.42 O ANISOU 878 OD2 ASP A 135 10060 10015 7820 1149 1112 1933 O ATOM 879 N ALA A 136 37.518 110.162-379.060 1.00 66.73 N ANISOU 879 N ALA A 136 9318 9443 6592 1455 1812 2245 N ATOM 880 CA ALA A 136 36.683 111.329-378.838 1.00 69.91 C ANISOU 880 CA ALA A 136 9496 10102 6965 1469 2026 2362 C ATOM 881 C ALA A 136 37.174 112.542-379.619 1.00 73.94 C ANISOU 881 C ALA A 136 9582 10856 7655 1269 2021 2294 C ATOM 882 O ALA A 136 36.403 113.456-379.908 1.00 73.80 O ANISOU 882 O ALA A 136 9333 11059 7649 1228 2203 2394 O ATOM 883 CB ALA A 136 36.613 111.646-377.358 1.00 63.49 C ANISOU 883 CB ALA A 136 8836 9262 6027 1600 2032 2423 C ATOM 884 N ASP A 137 38.456 112.546-379.965 1.00 85.38 N ANISOU 884 N ASP A 137 10943 12257 9241 1153 1812 2144 N ATOM 885 CA ASP A 137 39.065 113.703-380.615 1.00 83.23 C ANISOU 885 CA ASP A 137 10306 12193 9125 995 1790 2074 C ATOM 886 C ASP A 137 39.188 113.515-382.121 1.00 82.26 C ANISOU 886 C ASP A 137 10072 12090 9094 871 1774 2010 C ATOM 887 O ASP A 137 39.640 114.415-382.828 1.00 83.43 O ANISOU 887 O ASP A 137 9957 12389 9354 748 1757 1954 O ATOM 888 CB ASP A 137 40.450 113.982-380.030 1.00 81.50 C ANISOU 888 CB ASP A 137 10029 11935 9002 966 1579 1983 C ATOM 889 CG ASP A 137 40.459 113.972-378.513 1.00 86.02 C ANISOU 889 CG ASP A 137 10765 12438 9480 1088 1532 2040 C ATOM 890 OD1 ASP A 137 39.379 114.146-377.903 1.00 84.49 O ANISOU 890 OD1 ASP A 137 10652 12299 9152 1185 1708 2145 O ATOM 891 OD2 ASP A 137 41.551 113.790-377.928 1.00 90.56 O ANISOU 891 OD2 ASP A 137 11393 12901 10114 1089 1312 2000 O ATOM 892 N GLY A 138 38.795 112.344-382.606 1.00 88.16 N ANISOU 892 N GLY A 138 11033 12677 9787 911 1772 2017 N ATOM 893 CA GLY A 138 38.905 112.042-384.019 1.00 90.83 C ANISOU 893 CA GLY A 138 11293 13016 10203 798 1739 1954 C ATOM 894 C GLY A 138 40.251 111.442-384.370 1.00 89.34 C ANISOU 894 C GLY A 138 11164 12677 10104 739 1534 1811 C ATOM 895 O GLY A 138 40.556 111.225-385.542 1.00 90.89 O ANISOU 895 O GLY A 138 11296 12870 10368 642 1488 1739 O ATOM 896 N LYS A 139 41.063 111.182-383.350 1.00 83.11 N ANISOU 896 N LYS A 139 10500 11763 9316 797 1404 1789 N ATOM 897 CA LYS A 139 42.347 110.526-383.543 1.00 81.48 C ANISOU 897 CA LYS A 139 10368 11393 9198 749 1203 1704 C ATOM 898 C LYS A 139 42.097 109.164-384.164 1.00 84.49 C ANISOU 898 C LYS A 139 10972 11584 9546 751 1182 1675 C ATOM 899 O LYS A 139 41.319 108.373-383.629 1.00 89.40 O ANISOU 899 O LYS A 139 11839 12076 10052 858 1230 1730 O ATOM 900 CB LYS A 139 43.068 110.371-382.203 1.00 86.57 C ANISOU 900 CB LYS A 139 11148 11908 9836 819 1050 1739 C ATOM 901 CG LYS A 139 43.542 111.683-381.590 1.00 85.59 C ANISOU 901 CG LYS A 139 10776 11970 9775 812 1034 1760 C ATOM 902 CD LYS A 139 43.890 111.524-380.115 1.00 87.35 C ANISOU 902 CD LYS A 139 11163 12072 9955 902 898 1826 C ATOM 903 CE LYS A 139 44.943 110.445-379.903 1.00 91.07 C ANISOU 903 CE LYS A 139 11846 12277 10478 889 652 1834 C ATOM 904 NZ LYS A 139 45.054 110.028-378.473 1.00 97.92 N ANISOU 904 NZ LYS A 139 12978 12963 11266 981 497 1916 N ATOM 905 N ILE A 140 42.745 108.891-385.294 1.00 62.08 N ANISOU 905 N ILE A 140 8058 8730 6801 645 1116 1591 N ATOM 906 CA ILE A 140 42.527 107.625-386.001 1.00 61.60 C ANISOU 906 CA ILE A 140 8173 8507 6724 629 1099 1552 C ATOM 907 C ILE A 140 43.105 106.424-385.251 1.00 61.91 C ANISOU 907 C ILE A 140 8504 8269 6750 675 950 1554 C ATOM 908 O ILE A 140 44.318 106.325-385.049 1.00 58.33 O ANISOU 908 O ILE A 140 8049 7726 6387 624 789 1541 O ATOM 909 CB ILE A 140 43.103 107.654-387.428 1.00 60.42 C ANISOU 909 CB ILE A 140 7874 8411 6671 500 1064 1462 C ATOM 910 CG1 ILE A 140 42.724 108.959-388.133 1.00 59.10 C ANISOU 910 CG1 ILE A 140 7439 8496 6522 442 1164 1464 C ATOM 911 CG2 ILE A 140 42.601 106.461-388.217 1.00 58.55 C ANISOU 911 CG2 ILE A 140 7780 8055 6411 482 1080 1426 C ATOM 912 CD1 ILE A 140 43.046 108.970-389.616 1.00 58.10 C ANISOU 912 CD1 ILE A 140 7213 8413 6449 330 1137 1383 C ATOM 913 N LYS A 141 42.230 105.508-384.846 1.00 71.94 N ANISOU 913 N LYS A 141 10031 9396 7907 777 1001 1593 N ATOM 914 CA LYS A 141 42.663 104.334-384.098 1.00 73.91 C ANISOU 914 CA LYS A 141 10606 9353 8124 826 853 1604 C ATOM 915 C LYS A 141 42.691 103.065-384.952 1.00 71.09 C ANISOU 915 C LYS A 141 10382 8834 7794 776 822 1540 C ATOM 916 O LYS A 141 43.542 102.203-384.750 1.00 67.58 O ANISOU 916 O LYS A 141 10111 8166 7399 730 656 1525 O ATOM 917 CB LYS A 141 41.789 104.125-382.857 1.00 76.62 C ANISOU 917 CB LYS A 141 11215 9599 8300 1003 906 1696 C ATOM 918 CG LYS A 141 41.875 105.244-381.824 1.00 78.79 C ANISOU 918 CG LYS A 141 11400 9995 8543 1052 905 1760 C ATOM 919 CD LYS A 141 43.272 105.366-381.221 1.00 82.07 C ANISOU 919 CD LYS A 141 11812 10310 9060 981 663 1760 C ATOM 920 CE LYS A 141 43.297 106.384-380.081 1.00 87.94 C ANISOU 920 CE LYS A 141 12491 11158 9763 1046 648 1828 C ATOM 921 NZ LYS A 141 44.674 106.654-379.567 1.00 93.58 N ANISOU 921 NZ LYS A 141 13132 11819 10604 974 406 1857 N ATOM 922 N LYS A 142 41.773 102.951-385.906 1.00 65.16 N ANISOU 922 N LYS A 142 9541 8194 7021 777 972 1518 N ATOM 923 CA LYS A 142 41.712 101.753-386.743 1.00 63.13 C ANISOU 923 CA LYS A 142 9390 7803 6793 735 952 1455 C ATOM 924 C LYS A 142 41.091 102.000-388.118 1.00 62.06 C ANISOU 924 C LYS A 142 9023 7862 6696 667 1069 1420 C ATOM 925 O LYS A 142 40.121 102.742-388.245 1.00 60.72 O ANISOU 925 O LYS A 142 8717 7880 6475 719 1208 1494 O ATOM 926 CB LYS A 142 40.950 100.643-386.013 1.00 64.12 C ANISOU 926 CB LYS A 142 9861 7709 6791 892 975 1508 C ATOM 927 CG LYS A 142 40.726 99.380-386.829 1.00 64.03 C ANISOU 927 CG LYS A 142 9958 7566 6803 869 974 1449 C ATOM 928 CD LYS A 142 39.671 98.494-386.176 1.00 67.82 C ANISOU 928 CD LYS A 142 10750 7885 7133 1073 1054 1527 C ATOM 929 CE LYS A 142 39.950 98.309-384.687 1.00 73.07 C ANISOU 929 CE LYS A 142 11742 8332 7689 1187 952 1586 C ATOM 930 NZ LYS A 142 38.856 97.580-383.975 1.00 70.50 N ANISOU 930 NZ LYS A 142 11754 7852 7179 1428 1049 1679 N ATOM 931 N ILE A 143 41.656 101.366-389.141 1.00 67.55 N ANISOU 931 N ILE A 143 9680 8504 7483 545 1000 1323 N ATOM 932 CA ILE A 143 41.127 101.460-390.497 1.00 68.18 C ANISOU 932 CA ILE A 143 9572 8736 7597 472 1070 1286 C ATOM 933 C ILE A 143 40.963 100.072-391.101 1.00 58.81 C ANISOU 933 C ILE A 143 8519 7395 6430 455 1046 1229 C ATOM 934 O ILE A 143 41.363 99.075-390.499 1.00 59.56 O ANISOU 934 O ILE A 143 8851 7260 6520 486 972 1210 O ATOM 935 CB ILE A 143 42.055 102.261-391.405 1.00 67.13 C ANISOU 935 CB ILE A 143 9213 8735 7559 322 1012 1209 C ATOM 936 CG1 ILE A 143 43.254 101.413-391.823 1.00 68.91 C ANISOU 936 CG1 ILE A 143 9512 8798 7872 221 888 1117 C ATOM 937 CG2 ILE A 143 42.528 103.510-390.701 1.00 71.31 C ANISOU 937 CG2 ILE A 143 9628 9375 8090 337 1006 1251 C ATOM 938 CD1 ILE A 143 44.310 102.182-392.588 1.00 66.49 C ANISOU 938 CD1 ILE A 143 9023 8599 7643 112 837 1065 C ATOM 939 N ASN A 144 40.372 100.000-392.290 1.00 81.80 N ANISOU 939 N ASN A 144 11285 10428 9369 401 1095 1209 N ATOM 940 CA ASN A 144 40.253 98.727-392.997 1.00 78.48 C ANISOU 940 CA ASN A 144 10946 9887 8984 370 1069 1143 C ATOM 941 C ASN A 144 40.346 98.892-394.506 1.00 75.68 C ANISOU 941 C ASN A 144 10381 9670 8703 225 1042 1068 C ATOM 942 O ASN A 144 39.428 99.403-395.143 1.00 78.60 O ANISOU 942 O ASN A 144 10596 10213 9056 230 1099 1136 O ATOM 943 CB ASN A 144 38.961 97.999-392.619 1.00 83.47 C ANISOU 943 CB ASN A 144 11716 10466 9533 542 1170 1244 C ATOM 944 CG ASN A 144 38.945 96.558-393.100 1.00 85.27 C ANISOU 944 CG ASN A 144 12071 10528 9799 531 1134 1171 C ATOM 945 OD1 ASN A 144 38.773 96.287-394.291 1.00 81.95 O ANISOU 945 OD1 ASN A 144 11499 10193 9446 438 1124 1119 O ATOM 946 ND2 ASN A 144 39.118 95.623-392.172 1.00 78.50 N ANISOU 946 ND2 ASN A 144 11503 9426 8896 623 1104 1168 N ATOM 947 N ILE A 145 41.469 98.451-395.065 1.00 57.11 N ANISOU 947 N ILE A 145 8036 7232 6430 95 947 947 N ATOM 948 CA ILE A 145 41.716 98.524-396.499 1.00 57.16 C ANISOU 948 CA ILE A 145 7886 7339 6493 -42 908 861 C ATOM 949 C ILE A 145 41.533 97.166-397.177 1.00 58.19 C ANISOU 949 C ILE A 145 8080 7361 6668 -83 887 789 C ATOM 950 O ILE A 145 42.240 96.206-396.863 1.00 55.66 O ANISOU 950 O ILE A 145 7909 6849 6391 -111 843 731 O ATOM 951 CB ILE A 145 43.142 99.016-396.786 1.00 56.28 C ANISOU 951 CB ILE A 145 7726 7224 6432 -150 834 789 C ATOM 952 CG1 ILE A 145 43.444 100.281-395.978 1.00 62.17 C ANISOU 952 CG1 ILE A 145 8416 8059 7148 -98 848 859 C ATOM 953 CG2 ILE A 145 43.336 99.249-398.273 1.00 59.24 C ANISOU 953 CG2 ILE A 145 7966 7711 6831 -268 801 710 C ATOM 954 CD1 ILE A 145 44.870 100.786-396.129 1.00 56.24 C ANISOU 954 CD1 ILE A 145 7617 7303 6448 -164 784 825 C ATOM 955 N PRO A 146 40.577 97.080-398.113 1.00 56.56 N ANISOU 955 N PRO A 146 7755 7276 6461 -92 908 807 N ATOM 956 CA PRO A 146 40.374 95.853-398.887 1.00 57.14 C ANISOU 956 CA PRO A 146 7846 7277 6587 -138 883 735 C ATOM 957 C PRO A 146 41.553 95.629-399.829 1.00 55.24 C ANISOU 957 C PRO A 146 7569 7006 6414 -308 800 590 C ATOM 958 O PRO A 146 42.037 96.596-400.411 1.00 56.15 O ANISOU 958 O PRO A 146 7576 7239 6518 -383 765 569 O ATOM 959 CB PRO A 146 39.112 96.160-399.703 1.00 56.70 C ANISOU 959 CB PRO A 146 7622 7403 6517 -114 901 829 C ATOM 960 CG PRO A 146 38.463 97.309-399.013 1.00 57.93 C ANISOU 960 CG PRO A 146 7727 7680 6602 -16 968 983 C ATOM 961 CD PRO A 146 39.590 98.113-398.460 1.00 59.19 C ANISOU 961 CD PRO A 146 7922 7817 6750 -63 946 922 C ATOM 962 N THR A 147 42.003 94.386-399.989 1.00 54.85 N ANISOU 962 N THR A 147 7617 6798 6427 -363 775 502 N ATOM 963 CA THR A 147 43.198 94.121-400.785 1.00 54.92 C ANISOU 963 CA THR A 147 7604 6764 6498 -518 717 388 C ATOM 964 C THR A 147 42.932 93.399-402.098 1.00 52.90 C ANISOU 964 C THR A 147 7259 6553 6288 -615 687 295 C ATOM 965 O THR A 147 43.867 93.051-402.816 1.00 53.42 O ANISOU 965 O THR A 147 7317 6579 6401 -740 651 201 O ATOM 966 CB THR A 147 44.230 93.311-399.994 1.00 56.49 C ANISOU 966 CB THR A 147 7975 6736 6752 -548 695 373 C ATOM 967 OG1 THR A 147 43.632 92.087-399.562 1.00 52.67 O ANISOU 967 OG1 THR A 147 7625 6099 6288 -496 710 367 O ATOM 968 CG2 THR A 147 44.690 94.092-398.785 1.00 53.85 C ANISOU 968 CG2 THR A 147 7717 6363 6382 -473 691 468 C ATOM 969 N ALA A 148 41.667 93.172-402.417 1.00 53.24 N ANISOU 969 N ALA A 148 7227 6681 6320 -552 701 339 N ATOM 970 CA ALA A 148 41.333 92.488-403.657 1.00 52.66 C ANISOU 970 CA ALA A 148 7049 6661 6297 -640 654 263 C ATOM 971 C ALA A 148 42.034 93.144-404.836 1.00 52.39 C ANISOU 971 C ALA A 148 6922 6732 6252 -780 579 184 C ATOM 972 O ALA A 148 42.773 92.495-405.577 1.00 63.07 O ANISOU 972 O ALA A 148 8280 8031 7651 -897 549 67 O ATOM 973 CB ALA A 148 39.832 92.495-403.873 1.00 53.34 C ANISOU 973 CB ALA A 148 7027 6871 6370 -539 663 380 C ATOM 974 N LYS A 149 41.801 94.442-404.993 1.00 70.36 N ANISOU 974 N LYS A 149 9127 9149 8457 -761 554 257 N ATOM 975 CA LYS A 149 42.311 95.186-406.135 1.00 71.41 C ANISOU 975 CA LYS A 149 9203 9380 8549 -867 471 200 C ATOM 976 C LYS A 149 43.828 95.311-406.098 1.00 70.10 C ANISOU 976 C LYS A 149 9129 9127 8378 -920 491 118 C ATOM 977 O LYS A 149 44.494 95.155-407.118 1.00 69.20 O ANISOU 977 O LYS A 149 9019 9015 8257 -1016 447 28 O ATOM 978 CB LYS A 149 41.673 96.578-406.196 1.00 74.23 C ANISOU 978 CB LYS A 149 9487 9888 8830 -828 435 315 C ATOM 979 CG LYS A 149 40.153 96.580-406.353 1.00 82.72 C ANISOU 979 CG LYS A 149 10447 11069 9914 -781 405 453 C ATOM 980 CD LYS A 149 39.594 98.003-406.269 1.00 86.31 C ANISOU 980 CD LYS A 149 10835 11656 10302 -756 377 596 C ATOM 981 CE LYS A 149 38.065 98.031-406.235 1.00 79.88 C ANISOU 981 CE LYS A 149 9899 10944 9506 -692 368 798 C ATOM 982 NZ LYS A 149 37.453 97.962-407.595 1.00 71.96 N ANISOU 982 NZ LYS A 149 8789 10029 8523 -794 207 840 N ATOM 983 N ILE A 150 44.375 95.588-404.922 1.00 60.27 N ANISOU 983 N ILE A 150 7959 7806 7136 -849 554 172 N ATOM 984 CA ILE A 150 45.800 95.886-404.836 1.00 60.02 C ANISOU 984 CA ILE A 150 7989 7712 7103 -878 568 152 C ATOM 985 C ILE A 150 46.698 94.673-405.048 1.00 59.01 C ANISOU 985 C ILE A 150 7929 7437 7057 -966 581 85 C ATOM 986 O ILE A 150 47.670 94.760-405.796 1.00101.50 O ANISOU 986 O ILE A 150 13319 12817 12428 -1029 576 48 O ATOM 987 CB ILE A 150 46.189 96.672-403.554 1.00 60.51 C ANISOU 987 CB ILE A 150 8088 7752 7152 -781 608 253 C ATOM 988 CG1 ILE A 150 45.126 96.519-402.471 1.00 60.91 C ANISOU 988 CG1 ILE A 150 8156 7783 7203 -685 641 326 C ATOM 989 CG2 ILE A 150 46.360 98.161-403.865 1.00 61.23 C ANISOU 989 CG2 ILE A 150 8118 7986 7159 -747 593 287 C ATOM 990 CD1 ILE A 150 45.216 97.593-401.385 1.00 61.55 C ANISOU 990 CD1 ILE A 150 8239 7902 7244 -587 669 425 C ATOM 991 N ILE A 151 46.387 93.544-404.417 1.00 50.87 N ANISOU 991 N ILE A 151 6954 6274 6100 -966 600 81 N ATOM 992 CA ILE A 151 47.222 92.356-404.620 1.00 49.88 C ANISOU 992 CA ILE A 151 6891 5998 6063 -1071 607 28 C ATOM 993 C ILE A 151 47.188 91.980-406.101 1.00 49.27 C ANISOU 993 C ILE A 151 6736 5999 5986 -1177 583 -86 C ATOM 994 O ILE A 151 48.156 91.442-406.644 1.00 51.15 O ANISOU 994 O ILE A 151 6996 6171 6266 -1276 598 -127 O ATOM 995 CB ILE A 151 46.817 91.137-403.741 1.00 49.51 C ANISOU 995 CB ILE A 151 6946 5775 6091 -1057 618 36 C ATOM 996 CG1 ILE A 151 45.645 90.395-404.374 1.00 49.19 C ANISOU 996 CG1 ILE A 151 6840 5785 6065 -1059 615 -42 C ATOM 997 CG2 ILE A 151 46.523 91.553-402.300 1.00 50.33 C ANISOU 997 CG2 ILE A 151 7146 5814 6162 -927 626 147 C ATOM 998 CD1 ILE A 151 45.632 88.913-404.071 1.00 48.39 C ANISOU 998 CD1 ILE A 151 6833 5497 6056 -1101 625 -84 C ATOM 999 N ALA A 152 46.074 92.285-406.756 1.00 50.80 N ANISOU 999 N ALA A 152 6835 6334 6132 -1157 540 -118 N ATOM 1000 CA ALA A 152 45.967 92.075-408.189 1.00 49.39 C ANISOU 1000 CA ALA A 152 6584 6244 5939 -1254 484 -215 C ATOM 1001 C ALA A 152 47.020 92.914-408.902 1.00 50.62 C ANISOU 1001 C ALA A 152 6775 6446 6014 -1286 473 -229 C ATOM 1002 O ALA A 152 47.973 92.382-409.468 1.00 49.79 O ANISOU 1002 O ALA A 152 6708 6280 5930 -1368 499 -282 O ATOM 1003 CB ALA A 152 44.585 92.447-408.668 1.00 50.48 C ANISOU 1003 CB ALA A 152 6614 6527 6039 -1218 410 -192 C ATOM 1004 N LYS A 153 46.844 94.230-408.858 1.00 52.03 N ANISOU 1004 N LYS A 153 6947 6727 6094 -1212 444 -167 N ATOM 1005 CA LYS A 153 47.800 95.155-409.444 1.00 55.71 C ANISOU 1005 CA LYS A 153 7473 7233 6463 -1203 439 -163 C ATOM 1006 C LYS A 153 49.232 94.801-409.034 1.00 54.98 C ANISOU 1006 C LYS A 153 7454 7021 6416 -1204 531 -127 C ATOM 1007 O LYS A 153 50.154 94.884-409.843 1.00 56.58 O ANISOU 1007 O LYS A 153 7710 7219 6567 -1228 549 -146 O ATOM 1008 CB LYS A 153 47.468 96.587-409.021 1.00 56.83 C ANISOU 1008 CB LYS A 153 7605 7468 6518 -1104 416 -78 C ATOM 1009 CG LYS A 153 48.387 97.654-409.597 1.00 53.17 C ANISOU 1009 CG LYS A 153 7220 7045 5939 -1063 410 -66 C ATOM 1010 CD LYS A 153 48.118 97.845-411.073 1.00 59.67 C ANISOU 1010 CD LYS A 153 8081 7931 6660 -1127 300 -144 C ATOM 1011 CE LYS A 153 48.754 99.118-411.594 1.00 65.82 C ANISOU 1011 CE LYS A 153 8969 8749 7289 -1055 274 -118 C ATOM 1012 NZ LYS A 153 48.127 99.558-412.876 1.00 70.92 N ANISOU 1012 NZ LYS A 153 9671 9457 7818 -1110 116 -168 N ATOM 1013 N ALA A 154 49.412 94.405-407.777 1.00 55.27 N ANISOU 1013 N ALA A 154 7503 6953 6544 -1173 582 -53 N ATOM 1014 CA ALA A 154 50.742 94.116-407.248 1.00 57.18 C ANISOU 1014 CA ALA A 154 7805 7073 6848 -1177 644 36 C ATOM 1015 C ALA A 154 51.342 92.873-407.893 1.00 58.92 C ANISOU 1015 C ALA A 154 8047 7196 7143 -1303 673 -15 C ATOM 1016 O ALA A 154 52.501 92.871-408.311 1.00 55.94 O ANISOU 1016 O ALA A 154 7705 6787 6761 -1321 723 42 O ATOM 1017 CB ALA A 154 50.693 93.964-405.739 1.00 56.43 C ANISOU 1017 CB ALA A 154 7737 6874 6830 -1126 652 138 C ATOM 1018 N LYS A 155 50.553 91.807-407.960 1.00 71.99 N ANISOU 1018 N LYS A 155 9677 8806 8870 -1381 651 -107 N ATOM 1019 CA LYS A 155 50.988 90.605-408.653 1.00 71.58 C ANISOU 1019 CA LYS A 155 9626 8678 8895 -1515 677 -175 C ATOM 1020 C LYS A 155 51.346 90.983-410.078 1.00 65.13 C ANISOU 1020 C LYS A 155 8797 7972 7979 -1548 675 -246 C ATOM 1021 O LYS A 155 52.340 90.527-410.634 1.00 66.36 O ANISOU 1021 O LYS A 155 8983 8077 8152 -1617 733 -233 O ATOM 1022 CB LYS A 155 49.882 89.540-408.646 1.00 69.86 C ANISOU 1022 CB LYS A 155 9364 8428 8752 -1571 644 -280 C ATOM 1023 CG LYS A 155 49.874 88.648-407.410 1.00 63.72 C ANISOU 1023 CG LYS A 155 8659 7465 8088 -1578 660 -221 C ATOM 1024 CD LYS A 155 48.720 87.660-407.435 1.00 65.24 C ANISOU 1024 CD LYS A 155 8820 7633 8336 -1593 638 -318 C ATOM 1025 CE LYS A 155 48.715 86.786-406.186 1.00 70.68 C ANISOU 1025 CE LYS A 155 9634 8108 9112 -1582 644 -258 C ATOM 1026 NZ LYS A 155 47.486 85.940-406.070 1.00 67.43 N ANISOU 1026 NZ LYS A 155 9215 7673 8733 -1540 634 -330 N ATOM 1027 N GLU A 156 50.525 91.846-410.651 1.00 65.51 N ANISOU 1027 N GLU A 156 8814 8163 7914 -1494 602 -303 N ATOM 1028 CA GLU A 156 50.652 92.237-412.044 1.00 68.62 C ANISOU 1028 CA GLU A 156 9229 8654 8190 -1520 558 -381 C ATOM 1029 C GLU A 156 51.943 92.992-412.358 1.00 71.12 C ANISOU 1029 C GLU A 156 9649 8966 8407 -1452 623 -299 C ATOM 1030 O GLU A 156 52.329 93.106-413.520 1.00 70.60 O ANISOU 1030 O GLU A 156 9647 8939 8237 -1472 613 -354 O ATOM 1031 CB GLU A 156 49.433 93.068-412.444 1.00 68.37 C ANISOU 1031 CB GLU A 156 9155 8755 8067 -1479 435 -418 C ATOM 1032 CG GLU A 156 49.644 94.005-413.607 1.00 67.98 C ANISOU 1032 CG GLU A 156 9188 8792 7850 -1458 360 -447 C ATOM 1033 CD GLU A 156 48.464 94.930-413.804 1.00 88.97 C ANISOU 1033 CD GLU A 156 11811 11560 10433 -1424 222 -433 C ATOM 1034 OE1 GLU A 156 47.334 94.518-413.445 1.00 84.05 O ANISOU 1034 OE1 GLU A 156 11070 10969 9897 -1449 175 -429 O ATOM 1035 OE2 GLU A 156 48.666 96.061-414.307 1.00 93.92 O ANISOU 1035 OE2 GLU A 156 12537 12235 10914 -1367 163 -409 O ATOM 1036 N VAL A 157 52.615 93.500-411.330 1.00 49.67 N ANISOU 1036 N VAL A 157 6957 6200 5715 -1360 689 -157 N ATOM 1037 CA VAL A 157 53.826 94.295-411.546 1.00 49.68 C ANISOU 1037 CA VAL A 157 7044 6207 5625 -1259 758 -42 C ATOM 1038 C VAL A 157 55.005 93.878-410.655 1.00 49.62 C ANISOU 1038 C VAL A 157 7039 6080 5736 -1245 860 138 C ATOM 1039 O VAL A 157 55.819 94.709-410.257 1.00 52.32 O ANISOU 1039 O VAL A 157 7410 6429 6039 -1119 907 292 O ATOM 1040 CB VAL A 157 53.548 95.810-411.387 1.00 51.06 C ANISOU 1040 CB VAL A 157 7248 6482 5671 -1116 713 -6 C ATOM 1041 CG1 VAL A 157 52.561 96.285-412.441 1.00 51.39 C ANISOU 1041 CG1 VAL A 157 7315 6626 5585 -1140 593 -141 C ATOM 1042 CG2 VAL A 157 53.018 96.111-409.997 1.00 51.49 C ANISOU 1042 CG2 VAL A 157 7223 6529 5812 -1072 698 61 C ATOM 1043 N GLY A 158 55.091 92.589-410.347 1.00127.12 N ANISOU 1043 N GLY A 158 16820 15780 15698 -1377 881 136 N ATOM 1044 CA GLY A 158 56.236 92.048-409.634 1.00131.58 C ANISOU 1044 CA GLY A 158 17396 16211 16389 -1401 953 330 C ATOM 1045 C GLY A 158 56.360 92.462-408.181 1.00137.78 C ANISOU 1045 C GLY A 158 18168 16934 17248 -1326 921 486 C ATOM 1046 O GLY A 158 57.155 91.888-407.431 1.00140.62 O ANISOU 1046 O GLY A 158 18536 17156 17737 -1371 936 662 O ATOM 1047 N GLU A 159 55.574 93.457-407.776 1.00 80.20 N ANISOU 1047 N GLU A 159 10857 9739 9878 -1220 865 436 N ATOM 1048 CA GLU A 159 55.628 93.959-406.405 1.00 81.62 C ANISOU 1048 CA GLU A 159 11022 9879 10111 -1139 830 571 C ATOM 1049 C GLU A 159 54.662 93.228-405.469 1.00 76.75 C ANISOU 1049 C GLU A 159 10412 9169 9581 -1202 763 509 C ATOM 1050 O GLU A 159 53.873 93.855-404.767 1.00 76.90 O ANISOU 1050 O GLU A 159 10416 9239 9563 -1122 721 489 O ATOM 1051 CB GLU A 159 55.357 95.467-406.365 1.00 79.98 C ANISOU 1051 CB GLU A 159 10792 9822 9776 -984 819 571 C ATOM 1052 CG GLU A 159 56.320 96.306-407.189 1.00 77.68 C ANISOU 1052 CG GLU A 159 10528 9609 9377 -879 885 649 C ATOM 1053 CD GLU A 159 56.200 97.792-406.900 1.00 77.68 C ANISOU 1053 CD GLU A 159 10509 9728 9276 -719 871 685 C ATOM 1054 OE1 GLU A 159 56.104 98.172-405.715 1.00 79.46 O ANISOU 1054 OE1 GLU A 159 10680 9944 9567 -668 841 775 O ATOM 1055 OE2 GLU A 159 56.212 98.581-407.862 1.00 75.08 O ANISOU 1055 OE2 GLU A 159 10232 9497 8799 -646 884 625 O ATOM 1056 N TYR A 160 54.732 91.902-405.455 1.00 58.66 N ANISOU 1056 N TYR A 160 8154 6736 7398 -1336 760 489 N ATOM 1057 CA TYR A 160 53.904 91.115-404.557 1.00 58.46 C ANISOU 1057 CA TYR A 160 8175 6591 7446 -1378 700 445 C ATOM 1058 C TYR A 160 54.738 90.066-403.828 1.00 63.55 C ANISOU 1058 C TYR A 160 8900 7009 8236 -1481 673 593 C ATOM 1059 O TYR A 160 55.460 89.301-404.461 1.00 67.42 O ANISOU 1059 O TYR A 160 9387 7434 8796 -1599 714 621 O ATOM 1060 CB TYR A 160 52.768 90.439-405.327 1.00 58.41 C ANISOU 1060 CB TYR A 160 8140 6633 7419 -1440 699 236 C ATOM 1061 CG TYR A 160 51.951 89.485-404.479 1.00 57.89 C ANISOU 1061 CG TYR A 160 8144 6428 7425 -1464 656 200 C ATOM 1062 CD1 TYR A 160 50.750 89.883-403.915 1.00 55.96 C ANISOU 1062 CD1 TYR A 160 7903 6240 7118 -1353 629 156 C ATOM 1063 CD2 TYR A 160 52.389 88.191-404.235 1.00 57.19 C ANISOU 1063 CD2 TYR A 160 8130 6141 7458 -1588 646 227 C ATOM 1064 CE1 TYR A 160 50.003 89.013-403.137 1.00 56.01 C ANISOU 1064 CE1 TYR A 160 8004 6110 7168 -1339 602 138 C ATOM 1065 CE2 TYR A 160 51.655 87.317-403.460 1.00 57.20 C ANISOU 1065 CE2 TYR A 160 8233 5994 7508 -1590 603 195 C ATOM 1066 CZ TYR A 160 50.462 87.729-402.913 1.00 56.41 C ANISOU 1066 CZ TYR A 160 8152 5953 7329 -1453 585 150 C ATOM 1067 OH TYR A 160 49.726 86.857-402.137 1.00 51.17 O ANISOU 1067 OH TYR A 160 7618 5133 6692 -1422 554 132 O ATOM 1068 N PRO A 161 54.651 90.032-402.489 1.00 57.89 N ANISOU 1068 N PRO A 161 8266 6163 7566 -1442 594 703 N ATOM 1069 CA PRO A 161 53.902 90.971-401.652 1.00 55.16 C ANISOU 1069 CA PRO A 161 7926 5891 7140 -1298 555 697 C ATOM 1070 C PRO A 161 54.808 92.085-401.122 1.00 59.78 C ANISOU 1070 C PRO A 161 8469 6528 7717 -1202 540 887 C ATOM 1071 O PRO A 161 54.408 92.843-400.239 1.00 62.41 O ANISOU 1071 O PRO A 161 8808 6898 8007 -1094 499 923 O ATOM 1072 CB PRO A 161 53.420 90.094-400.485 1.00 48.98 C ANISOU 1072 CB PRO A 161 7296 4898 6416 -1319 470 724 C ATOM 1073 CG PRO A 161 53.971 88.699-400.750 1.00 48.65 C ANISOU 1073 CG PRO A 161 7325 4665 6495 -1488 456 744 C ATOM 1074 CD PRO A 161 55.096 88.871-401.709 1.00 52.01 C ANISOU 1074 CD PRO A 161 7643 5164 6955 -1556 523 818 C ATOM 1075 N THR A 162 56.021 92.168-401.652 1.00 91.52 N ANISOU 1075 N THR A 162 12442 10553 11778 -1232 581 1020 N ATOM 1076 CA THR A 162 56.944 93.223-401.272 1.00 88.66 C ANISOU 1076 CA THR A 162 12019 10254 11412 -1120 580 1222 C ATOM 1077 C THR A 162 56.230 94.564-401.023 1.00 90.40 C ANISOU 1077 C THR A 162 12179 10654 11513 -967 584 1143 C ATOM 1078 O THR A 162 56.125 95.008-399.870 1.00 91.53 O ANISOU 1078 O THR A 162 12333 10768 11675 -899 512 1236 O ATOM 1079 CB THR A 162 58.070 93.363-402.307 1.00 92.61 C ANISOU 1079 CB THR A 162 12463 10815 11911 -1119 676 1325 C ATOM 1080 OG1 THR A 162 57.658 92.773-403.547 1.00 93.36 O ANISOU 1080 OG1 THR A 162 12564 10953 11955 -1206 747 1125 O ATOM 1081 CG2 THR A 162 59.316 92.640-401.829 1.00 96.64 C ANISOU 1081 CG2 THR A 162 12996 11146 12576 -1199 641 1609 C ATOM 1082 N LEU A 163 55.738 95.194-402.091 1.00 51.69 N ANISOU 1082 N LEU A 163 7221 5928 6489 -923 657 982 N ATOM 1083 CA LEU A 163 55.021 96.467-401.971 1.00 51.90 C ANISOU 1083 CA LEU A 163 7190 6124 6405 -801 661 911 C ATOM 1084 C LEU A 163 55.876 97.620-401.428 1.00 52.86 C ANISOU 1084 C LEU A 163 7250 6313 6523 -666 662 1091 C ATOM 1085 O LEU A 163 57.087 97.673-401.638 1.00 53.04 O ANISOU 1085 O LEU A 163 7255 6310 6587 -637 692 1259 O ATOM 1086 CB LEU A 163 53.809 96.316-401.057 1.00 56.80 C ANISOU 1086 CB LEU A 163 7842 6716 7023 -796 608 834 C ATOM 1087 CG LEU A 163 52.542 95.657-401.558 1.00 51.96 C ANISOU 1087 CG LEU A 163 7253 6115 6373 -859 615 646 C ATOM 1088 CD1 LEU A 163 51.386 96.048-400.641 1.00 52.66 C ANISOU 1088 CD1 LEU A 163 7350 6239 6419 -780 593 623 C ATOM 1089 CD2 LEU A 163 52.278 96.101-402.965 1.00 52.57 C ANISOU 1089 CD2 LEU A 163 7269 6347 6357 -870 657 522 C ATOM 1090 N GLY A 164 55.212 98.564-400.760 1.00112.65 N ANISOU 1090 N GLY A 164 14776 13981 14044 -576 638 1066 N ATOM 1091 CA GLY A 164 55.876 99.577-399.959 1.00120.23 C ANISOU 1091 CA GLY A 164 15664 14993 15024 -452 619 1234 C ATOM 1092 C GLY A 164 56.355 100.842-400.654 1.00120.15 C ANISOU 1092 C GLY A 164 15581 15148 14922 -325 686 1257 C ATOM 1093 O GLY A 164 55.999 101.953-400.247 1.00107.93 O ANISOU 1093 O GLY A 164 13964 13721 13324 -229 684 1248 O ATOM 1094 N SER A 165 57.163 100.683-401.698 1.00 98.43 N ANISOU 1094 N SER A 165 12858 12398 12143 -317 749 1292 N ATOM 1095 CA SER A 165 57.941 101.802-402.224 1.00 90.77 C ANISOU 1095 CA SER A 165 11853 11542 11092 -159 813 1381 C ATOM 1096 C SER A 165 57.075 102.828-402.959 1.00 87.88 C ANISOU 1096 C SER A 165 11499 11325 10566 -109 831 1194 C ATOM 1097 O SER A 165 57.115 104.019-402.649 1.00 93.17 O ANISOU 1097 O SER A 165 12108 12101 11190 16 837 1234 O ATOM 1098 CB SER A 165 59.084 101.294-403.113 1.00 89.47 C ANISOU 1098 CB SER A 165 11742 11322 10929 -144 888 1500 C ATOM 1099 OG SER A 165 60.167 102.207-403.122 1.00 92.05 O ANISOU 1099 OG SER A 165 12026 11715 11235 44 944 1707 O ATOM 1100 N ASN A 166 56.292 102.356-403.925 1.00 67.74 N ANISOU 1100 N ASN A 166 9024 8776 7939 -214 827 1003 N ATOM 1101 CA ASN A 166 55.467 103.231-404.745 1.00 69.19 C ANISOU 1101 CA ASN A 166 9239 9077 7974 -194 813 850 C ATOM 1102 C ASN A 166 54.020 103.135-404.293 1.00 71.28 C ANISOU 1102 C ASN A 166 9457 9373 8253 -288 752 726 C ATOM 1103 O ASN A 166 53.114 103.727-404.887 1.00 68.25 O ANISOU 1103 O ASN A 166 9085 9076 7770 -308 717 617 O ATOM 1104 CB ASN A 166 55.571 102.822-406.212 1.00 69.00 C ANISOU 1104 CB ASN A 166 9335 9037 7846 -240 826 749 C ATOM 1105 CG ASN A 166 56.939 102.286-406.571 1.00 70.29 C ANISOU 1105 CG ASN A 166 9550 9122 8034 -193 906 887 C ATOM 1106 OD1 ASN A 166 57.958 102.882-406.232 1.00 71.62 O ANISOU 1106 OD1 ASN A 166 9697 9303 8211 -44 961 1068 O ATOM 1107 ND2 ASN A 166 56.968 101.153-407.260 1.00 74.70 N ANISOU 1107 ND2 ASN A 166 10166 9606 8612 -315 917 820 N ATOM 1108 N TRP A 167 53.807 102.366-403.237 1.00 78.59 N ANISOU 1108 N TRP A 167 10346 10216 9300 -343 735 767 N ATOM 1109 CA TRP A 167 52.468 102.164-402.720 1.00 77.55 C ANISOU 1109 CA TRP A 167 10186 10101 9180 -404 699 681 C ATOM 1110 C TRP A 167 52.186 103.149-401.597 1.00 73.65 C ANISOU 1110 C TRP A 167 9611 9680 8694 -316 695 753 C ATOM 1111 O TRP A 167 52.944 103.241-400.628 1.00 78.18 O ANISOU 1111 O TRP A 167 10154 10209 9343 -255 692 883 O ATOM 1112 CB TRP A 167 52.300 100.720-402.259 1.00 77.79 C ANISOU 1112 CB TRP A 167 10262 9981 9312 -500 682 673 C ATOM 1113 CG TRP A 167 52.430 99.752-403.396 1.00 72.50 C ANISOU 1113 CG TRP A 167 9651 9257 8639 -601 688 583 C ATOM 1114 CD1 TRP A 167 53.573 99.151-403.836 1.00 71.70 C ANISOU 1114 CD1 TRP A 167 9593 9070 8581 -630 718 642 C ATOM 1115 CD2 TRP A 167 51.379 99.294-404.251 1.00 70.68 C ANISOU 1115 CD2 TRP A 167 9430 9061 8364 -686 665 436 C ATOM 1116 NE1 TRP A 167 53.295 98.339-404.909 1.00 66.93 N ANISOU 1116 NE1 TRP A 167 9029 8446 7956 -734 720 519 N ATOM 1117 CE2 TRP A 167 51.956 98.409-405.184 1.00 68.67 C ANISOU 1117 CE2 TRP A 167 9226 8741 8126 -768 679 389 C ATOM 1118 CE3 TRP A 167 50.005 99.542-404.319 1.00 72.36 C ANISOU 1118 CE3 TRP A 167 9602 9359 8532 -697 633 365 C ATOM 1119 CZ2 TRP A 167 51.207 97.770-406.167 1.00 71.40 C ANISOU 1119 CZ2 TRP A 167 9578 9106 8446 -863 648 253 C ATOM 1120 CZ3 TRP A 167 49.261 98.909-405.298 1.00 69.45 C ANISOU 1120 CZ3 TRP A 167 9237 9008 8144 -785 598 257 C ATOM 1121 CH2 TRP A 167 49.865 98.033-406.208 1.00 71.84 C ANISOU 1121 CH2 TRP A 167 9586 9246 8465 -868 600 192 C ATOM 1122 N THR A 168 51.098 103.896-401.740 1.00 61.38 N ANISOU 1122 N THR A 168 8014 8241 7065 -315 689 686 N ATOM 1123 CA THR A 168 50.802 104.984-400.820 1.00 62.94 C ANISOU 1123 CA THR A 168 8123 8535 7256 -236 699 747 C ATOM 1124 C THR A 168 49.328 105.020-400.440 1.00 62.94 C ANISOU 1124 C THR A 168 8091 8588 7237 -274 699 710 C ATOM 1125 O THR A 168 48.483 104.492-401.157 1.00 56.50 O ANISOU 1125 O THR A 168 7306 7772 6391 -351 682 637 O ATOM 1126 CB THR A 168 51.199 106.326-401.435 1.00 59.02 C ANISOU 1126 CB THR A 168 7593 8157 6675 -161 710 755 C ATOM 1127 OG1 THR A 168 50.568 106.472-402.715 1.00 57.24 O ANISOU 1127 OG1 THR A 168 7426 7975 6349 -226 679 653 O ATOM 1128 CG2 THR A 168 52.707 106.384-401.618 1.00 67.49 C ANISOU 1128 CG2 THR A 168 8690 9185 7767 -73 733 842 C ATOM 1129 N ALA A 169 49.021 105.642-399.308 1.00 56.46 N ANISOU 1129 N ALA A 169 7201 7817 6433 -212 719 778 N ATOM 1130 CA ALA A 169 47.644 105.696-398.837 1.00 59.33 C ANISOU 1130 CA ALA A 169 7536 8232 6773 -225 742 781 C ATOM 1131 C ALA A 169 47.288 107.081-398.356 1.00 59.98 C ANISOU 1131 C ALA A 169 7506 8461 6822 -172 772 834 C ATOM 1132 O ALA A 169 47.962 107.626-397.488 1.00 58.38 O ANISOU 1132 O ALA A 169 7254 8274 6655 -98 781 894 O ATOM 1133 CB ALA A 169 47.428 104.696-397.724 1.00 56.49 C ANISOU 1133 CB ALA A 169 7249 7746 6467 -205 747 819 C ATOM 1134 N GLU A 170 46.220 107.642-398.914 1.00 78.76 N ANISOU 1134 N GLU A 170 9837 10947 9142 -216 780 830 N ATOM 1135 CA GLU A 170 45.730 108.954-398.506 1.00 86.65 C ANISOU 1135 CA GLU A 170 10723 12087 10112 -188 814 891 C ATOM 1136 C GLU A 170 44.274 108.858-398.054 1.00 86.42 C ANISOU 1136 C GLU A 170 10657 12109 10070 -204 862 964 C ATOM 1137 O GLU A 170 43.604 107.857-398.301 1.00 86.48 O ANISOU 1137 O GLU A 170 10725 12054 10079 -233 859 962 O ATOM 1138 CB GLU A 170 45.861 109.963-399.651 1.00 92.01 C ANISOU 1138 CB GLU A 170 11382 12849 10727 -228 768 862 C ATOM 1139 CG GLU A 170 44.940 109.683-400.834 1.00101.87 C ANISOU 1139 CG GLU A 170 12673 14106 11927 -333 706 843 C ATOM 1140 CD GLU A 170 45.037 110.736-401.927 1.00114.36 C ANISOU 1140 CD GLU A 170 14276 15747 13429 -375 630 826 C ATOM 1141 OE1 GLU A 170 46.153 111.239-402.178 1.00120.02 O ANISOU 1141 OE1 GLU A 170 15038 16448 14115 -312 623 782 O ATOM 1142 OE2 GLU A 170 43.997 111.056-402.543 1.00113.59 O ANISOU 1142 OE2 GLU A 170 14162 15700 13296 -464 569 877 O ATOM 1143 N ILE A 171 43.790 109.906-397.395 1.00 58.94 N ANISOU 1143 N ILE A 171 7070 8746 6577 -176 916 1043 N ATOM 1144 CA ILE A 171 42.420 109.945-396.898 1.00 60.15 C ANISOU 1144 CA ILE A 171 7177 8964 6713 -172 986 1153 C ATOM 1145 C ILE A 171 41.464 110.559-397.925 1.00 59.32 C ANISOU 1145 C ILE A 171 7004 8960 6573 -268 955 1220 C ATOM 1146 O ILE A 171 41.875 110.955-399.014 1.00 59.77 O ANISOU 1146 O ILE A 171 7075 9026 6609 -339 864 1160 O ATOM 1147 CB ILE A 171 42.336 110.747-395.584 1.00 60.34 C ANISOU 1147 CB ILE A 171 7118 9066 6744 -97 1069 1228 C ATOM 1148 CG1 ILE A 171 43.446 110.324-394.628 1.00 59.60 C ANISOU 1148 CG1 ILE A 171 7085 8870 6689 -15 1052 1180 C ATOM 1149 CG2 ILE A 171 40.998 110.527-394.903 1.00 58.42 C ANISOU 1149 CG2 ILE A 171 6867 8859 6472 -57 1166 1359 C ATOM 1150 CD1 ILE A 171 43.091 109.088-393.814 1.00 63.35 C ANISOU 1150 CD1 ILE A 171 7702 9209 7161 46 1073 1205 C ATOM 1151 N SER A 172 40.185 110.624-397.573 1.00 70.11 N ANISOU 1151 N SER A 172 8311 10395 7931 -265 1022 1366 N ATOM 1152 CA SER A 172 39.189 111.263-398.412 1.00 73.60 C ANISOU 1152 CA SER A 172 8671 10937 8356 -363 982 1489 C ATOM 1153 C SER A 172 39.645 112.691-398.630 1.00 78.72 C ANISOU 1153 C SER A 172 9246 11673 8992 -416 947 1476 C ATOM 1154 O SER A 172 40.407 113.223-397.824 1.00 80.91 O ANISOU 1154 O SER A 172 9492 11971 9280 -351 1001 1418 O ATOM 1155 CB SER A 172 37.837 111.249-397.702 1.00 77.50 C ANISOU 1155 CB SER A 172 9091 11505 8849 -319 1097 1697 C ATOM 1156 OG SER A 172 36.768 111.404-398.619 1.00 88.09 O ANISOU 1156 OG SER A 172 10368 12909 10194 -412 1037 1858 O ATOM 1157 N SER A 173 39.195 113.314-399.716 1.00158.77 N ANISOU 1157 N SER A 173 19364 21855 19107 -534 843 1536 N ATOM 1158 CA SER A 173 39.505 114.721-399.959 1.00160.58 C ANISOU 1158 CA SER A 173 19543 22156 19314 -587 802 1539 C ATOM 1159 C SER A 173 38.238 115.576-399.941 1.00161.24 C ANISOU 1159 C SER A 173 19504 22352 19409 -679 815 1762 C ATOM 1160 O SER A 173 37.759 116.020-400.982 1.00162.15 O ANISOU 1160 O SER A 173 19636 22471 19503 -804 680 1846 O ATOM 1161 CB SER A 173 40.269 114.904-401.273 1.00154.77 C ANISOU 1161 CB SER A 173 18934 21348 18524 -646 644 1417 C ATOM 1162 OG SER A 173 39.424 114.717-402.394 1.00157.55 O ANISOU 1162 OG SER A 173 19327 21682 18854 -768 508 1508 O ATOM 1163 N SER A 174 37.698 115.787-398.745 1.00107.64 N ANISOU 1163 N SER A 174 12601 15647 12650 -618 972 1874 N ATOM 1164 CA SER A 174 38.276 115.199-397.543 1.00106.78 C ANISOU 1164 CA SER A 174 12509 15507 12554 -473 1095 1778 C ATOM 1165 C SER A 174 37.250 114.859-396.465 1.00106.88 C ANISOU 1165 C SER A 174 12464 15571 12574 -396 1250 1947 C ATOM 1166 O SER A 174 36.078 115.235-396.548 1.00107.57 O ANISOU 1166 O SER A 174 12461 15746 12666 -449 1293 2164 O ATOM 1167 CB SER A 174 39.398 116.085-396.968 1.00106.08 C ANISOU 1167 CB SER A 174 12379 15452 12474 -424 1119 1655 C ATOM 1168 OG SER A 174 39.011 117.446-396.880 1.00106.28 O ANISOU 1168 OG SER A 174 12274 15602 12506 -493 1143 1754 O ATOM 1169 N SER A 175 37.705 114.118-395.465 1.00 90.81 N ANISOU 1169 N SER A 175 10501 13469 10535 -265 1327 1865 N ATOM 1170 CA SER A 175 36.925 113.899-394.264 1.00 79.24 C ANISOU 1170 CA SER A 175 9021 12036 9049 -158 1482 2002 C ATOM 1171 C SER A 175 36.819 115.235-393.552 1.00 79.93 C ANISOU 1171 C SER A 175 8959 12266 9146 -173 1567 2075 C ATOM 1172 O SER A 175 37.479 116.198-393.935 1.00 83.64 O ANISOU 1172 O SER A 175 9349 12788 9641 -252 1500 1993 O ATOM 1173 CB SER A 175 37.652 112.916-393.360 1.00 73.59 C ANISOU 1173 CB SER A 175 8452 11190 8320 -25 1501 1875 C ATOM 1174 OG SER A 175 38.739 113.554-392.712 1.00 63.78 O ANISOU 1174 OG SER A 175 7172 9960 7100 -2 1483 1758 O ATOM 1175 N SER A 176 36.006 115.293-392.506 1.00110.41 N ANISOU 1175 N SER A 176 12787 16186 12978 -87 1721 2231 N ATOM 1176 CA SER A 176 35.910 116.504-391.706 1.00107.67 C ANISOU 1176 CA SER A 176 12291 15978 12640 -97 1819 2298 C ATOM 1177 C SER A 176 37.289 116.937-391.212 1.00102.73 C ANISOU 1177 C SER A 176 11650 15339 12044 -70 1760 2088 C ATOM 1178 O SER A 176 37.652 118.109-391.311 1.00 94.49 O ANISOU 1178 O SER A 176 10464 14399 11039 -143 1745 2061 O ATOM 1179 CB SER A 176 34.985 116.276-390.514 1.00101.63 C ANISOU 1179 CB SER A 176 11545 15251 11820 33 2001 2474 C ATOM 1180 OG SER A 176 33.794 115.633-390.922 1.00 99.60 O ANISOU 1180 OG SER A 176 11326 14984 11532 56 2060 2682 O ATOM 1181 N GLY A 177 38.059 115.982-390.700 1.00 61.86 N ANISOU 1181 N GLY A 177 6621 10027 6856 37 1717 1958 N ATOM 1182 CA GLY A 177 39.297 116.284-390.007 1.00 57.85 C ANISOU 1182 CA GLY A 177 6095 9504 6383 89 1664 1819 C ATOM 1183 C GLY A 177 40.619 115.957-390.665 1.00 58.35 C ANISOU 1183 C GLY A 177 6172 9505 6495 50 1520 1657 C ATOM 1184 O GLY A 177 40.675 115.216-391.646 1.00 60.79 O ANISOU 1184 O GLY A 177 6495 9799 6804 -38 1454 1629 O ATOM 1185 N LEU A 178 41.690 116.507-390.091 1.00110.63 N ANISOU 1185 N LEU A 178 12796 16083 13154 125 1466 1571 N ATOM 1186 CA LEU A 178 43.018 116.503-390.709 1.00115.93 C ANISOU 1186 CA LEU A 178 13445 16725 13877 121 1354 1458 C ATOM 1187 C LEU A 178 44.180 115.738-390.056 1.00106.82 C ANISOU 1187 C LEU A 178 12342 15474 12772 220 1277 1416 C ATOM 1188 O LEU A 178 43.967 114.876-389.205 1.00101.22 O ANISOU 1188 O LEU A 178 11664 14738 12056 287 1297 1465 O ATOM 1189 CB LEU A 178 43.212 118.003-390.935 1.00113.55 C ANISOU 1189 CB LEU A 178 12953 16585 13604 81 1375 1458 C ATOM 1190 CG LEU A 178 43.495 118.823-389.669 1.00114.16 C ANISOU 1190 CG LEU A 178 12875 16773 13726 147 1423 1489 C ATOM 1191 CD1 LEU A 178 43.526 120.304-389.998 1.00113.38 C ANISOU 1191 CD1 LEU A 178 12589 16837 13655 95 1455 1492 C ATOM 1192 CD2 LEU A 178 42.478 118.541-388.571 1.00109.68 C ANISOU 1192 CD2 LEU A 178 12327 16228 13119 176 1527 1587 C ATOM 1193 N ALA A 179 45.402 116.067-390.481 1.00 73.69 N ANISOU 1193 N ALA A 179 8163 11218 8619 231 1181 1349 N ATOM 1194 CA ALA A 179 46.645 115.649-389.815 1.00 80.14 C ANISOU 1194 CA ALA A 179 8975 11968 9507 318 1091 1353 C ATOM 1195 C ALA A 179 47.244 114.238-389.866 1.00 68.36 C ANISOU 1195 C ALA A 179 7669 10272 8032 333 998 1344 C ATOM 1196 O ALA A 179 48.367 114.027-389.397 1.00 66.37 O ANISOU 1196 O ALA A 179 7413 9953 7851 392 904 1384 O ATOM 1197 CB ALA A 179 46.592 116.148-388.366 1.00 83.48 C ANISOU 1197 CB ALA A 179 9299 12462 9959 382 1107 1419 C ATOM 1198 N ALA A 180 46.520 113.289-390.455 1.00 73.78 N ANISOU 1198 N ALA A 180 8508 10863 8663 276 1017 1310 N ATOM 1199 CA ALA A 180 46.854 111.874-390.309 1.00 68.19 C ANISOU 1199 CA ALA A 180 7989 9953 7966 282 943 1306 C ATOM 1200 C ALA A 180 47.937 111.346-391.243 1.00 67.23 C ANISOU 1200 C ALA A 180 7917 9738 7891 259 866 1267 C ATOM 1201 O ALA A 180 48.228 111.944-392.277 1.00 71.11 O ANISOU 1201 O ALA A 180 8336 10309 8373 236 882 1224 O ATOM 1202 CB ALA A 180 45.601 111.037-390.457 1.00 66.67 C ANISOU 1202 CB ALA A 180 7934 9698 7700 252 1004 1297 C ATOM 1203 N VAL A 181 48.506 110.182-390.860 1.00 20.00 N ATOM 1204 CA VAL A 181 49.580 109.553-391.620 1.00 20.00 C ATOM 1205 C VAL A 181 49.495 108.032-391.540 1.00 20.00 C ATOM 1206 O VAL A 181 49.993 107.431-390.592 1.00 64.47 O ANISOU 1206 O VAL A 181 8055 8748 7692 217 564 1367 O ATOM 1207 CB VAL A 181 50.965 110.008-391.121 1.00 20.00 C ATOM 1208 CG1 VAL A 181 52.067 109.265-391.859 1.00 20.00 C ATOM 1209 CG2 VAL A 181 51.123 111.511-391.286 1.00 20.00 C ATOM 1210 N ILE A 182 48.941 107.394-392.566 1.00 58.74 N ANISOU 1210 N ILE A 182 7316 8130 6872 126 701 1192 N ATOM 1211 CA ILE A 182 48.917 105.935-392.608 1.00 58.81 C ANISOU 1211 CA ILE A 182 7506 7942 6896 79 655 1175 C ATOM 1212 C ILE A 182 50.065 105.438-393.469 1.00 55.61 C ANISOU 1212 C ILE A 182 7115 7461 6554 30 607 1175 C ATOM 1213 O ILE A 182 50.294 105.966-394.553 1.00 58.34 O ANISOU 1213 O ILE A 182 7380 7910 6876 14 649 1124 O ATOM 1214 CB ILE A 182 47.621 105.406-393.210 1.00 57.70 C ANISOU 1214 CB ILE A 182 7433 7809 6683 38 727 1091 C ATOM 1215 CG1 ILE A 182 46.410 106.078-392.555 1.00 64.28 C ANISOU 1215 CG1 ILE A 182 8221 8757 7444 96 808 1122 C ATOM 1216 CG2 ILE A 182 47.560 103.901-393.052 1.00 57.37 C ANISOU 1216 CG2 ILE A 182 7584 7555 6659 9 681 1078 C ATOM 1217 CD1 ILE A 182 45.109 105.883-393.323 1.00 64.42 C ANISOU 1217 CD1 ILE A 182 8239 8839 7398 66 888 1086 C ATOM 1218 N THR A 183 50.781 104.422-392.997 1.00 56.76 N ANISOU 1218 N THR A 183 7379 7416 6772 6 517 1246 N ATOM 1219 CA THR A 183 51.968 103.932-393.705 1.00 57.16 C ANISOU 1219 CA THR A 183 7436 7389 6895 -38 479 1291 C ATOM 1220 C THR A 183 51.865 102.457-394.111 1.00 56.87 C ANISOU 1220 C THR A 183 7560 7169 6880 -136 455 1242 C ATOM 1221 O THR A 183 51.678 101.578-393.263 1.00 59.89 O ANISOU 1221 O THR A 183 8089 7379 7287 -156 383 1281 O ATOM 1222 CB THR A 183 53.233 104.118-392.864 1.00 55.56 C ANISOU 1222 CB THR A 183 7190 7124 6795 9 377 1481 C ATOM 1223 OG1 THR A 183 53.554 105.510-392.786 1.00 57.42 O ANISOU 1223 OG1 THR A 183 7245 7549 7024 106 412 1524 O ATOM 1224 CG2 THR A 183 54.383 103.369-393.492 1.00 55.97 C ANISOU 1224 CG2 THR A 183 7275 7062 6930 -42 341 1571 C ATOM 1225 N LEU A 184 52.021 102.186-395.403 1.00 54.86 N ANISOU 1225 N LEU A 184 7291 6944 6611 -195 507 1160 N ATOM 1226 CA LEU A 184 51.738 100.859-395.948 1.00 54.55 C ANISOU 1226 CA LEU A 184 7375 6767 6584 -294 504 1081 C ATOM 1227 C LEU A 184 52.945 99.928-396.011 1.00 56.38 C ANISOU 1227 C LEU A 184 7673 6827 6922 -363 442 1186 C ATOM 1228 O LEU A 184 53.988 100.290-396.547 1.00 55.03 O ANISOU 1228 O LEU A 184 7425 6700 6785 -350 456 1267 O ATOM 1229 CB LEU A 184 51.125 100.992-397.343 1.00 56.44 C ANISOU 1229 CB LEU A 184 7566 7128 6750 -335 582 933 C ATOM 1230 CG LEU A 184 49.750 101.653-397.440 1.00 54.71 C ANISOU 1230 CG LEU A 184 7295 7055 6438 -302 633 849 C ATOM 1231 CD1 LEU A 184 49.278 101.648-398.880 1.00 57.44 C ANISOU 1231 CD1 LEU A 184 7609 7489 6727 -365 663 734 C ATOM 1232 CD2 LEU A 184 48.734 100.957-396.545 1.00 55.39 C ANISOU 1232 CD2 LEU A 184 7481 7051 6515 -284 630 848 C ATOM 1233 N GLY A 185 52.790 98.721-395.480 1.00 56.62 N ANISOU 1233 N GLY A 185 7856 6656 7000 -430 377 1200 N ATOM 1234 CA GLY A 185 53.822 97.705-395.588 1.00 61.35 C ANISOU 1234 CA GLY A 185 8529 7073 7708 -525 314 1305 C ATOM 1235 C GLY A 185 53.488 96.685-396.663 1.00 53.07 C ANISOU 1235 C GLY A 185 7531 5977 6655 -632 371 1164 C ATOM 1236 O GLY A 185 52.992 97.050-397.727 1.00 56.89 O ANISOU 1236 O GLY A 185 7933 6616 7065 -629 461 1023 O ATOM 1237 N LYS A 186 53.742 95.407-396.384 1.00 73.60 N ANISOU 1237 N LYS A 186 10271 8357 9337 -733 303 1206 N ATOM 1238 CA LYS A 186 53.533 94.346-397.370 1.00 69.10 C ANISOU 1238 CA LYS A 186 9739 7730 8784 -846 352 1082 C ATOM 1239 C LYS A 186 52.205 93.625-397.179 1.00 67.50 C ANISOU 1239 C LYS A 186 9648 7467 8531 -844 359 933 C ATOM 1240 O LYS A 186 51.524 93.818-396.179 1.00 68.23 O ANISOU 1240 O LYS A 186 9827 7523 8574 -755 323 949 O ATOM 1241 CB LYS A 186 54.653 93.308-397.295 1.00 75.72 C ANISOU 1241 CB LYS A 186 10655 8360 9756 -972 285 1229 C ATOM 1242 CG LYS A 186 55.910 93.743-396.562 1.00 82.84 C ANISOU 1242 CG LYS A 186 11530 9201 10745 -951 197 1496 C ATOM 1243 CD LYS A 186 56.964 92.643-396.651 1.00 90.18 C ANISOU 1243 CD LYS A 186 12525 9925 11815 -1098 138 1665 C ATOM 1244 CE LYS A 186 57.898 92.629-395.450 1.00 79.95 C ANISOU 1244 CE LYS A 186 11287 8461 10631 -1107 -29 1966 C ATOM 1245 NZ LYS A 186 58.786 91.430-395.487 1.00 64.62 N ANISOU 1245 NZ LYS A 186 9430 6288 8834 -1276 -105 2147 N ATOM 1246 N ILE A 187 51.847 92.782-398.142 1.00 59.24 N ANISOU 1246 N ILE A 187 8602 6412 7496 -929 410 800 N ATOM 1247 CA ILE A 187 50.653 91.960-398.031 1.00 60.38 C ANISOU 1247 CA ILE A 187 8846 6489 7607 -918 421 681 C ATOM 1248 C ILE A 187 50.959 90.794-397.105 1.00 59.73 C ANISOU 1248 C ILE A 187 8977 6117 7599 -973 324 763 C ATOM 1249 O ILE A 187 51.828 89.984-397.413 1.00 58.59 O ANISOU 1249 O ILE A 187 8865 5840 7558 -1108 291 809 O ATOM 1250 CB ILE A 187 50.238 91.407-399.393 1.00 55.50 C ANISOU 1250 CB ILE A 187 8140 5956 6991 -997 491 524 C ATOM 1251 CG1 ILE A 187 50.036 92.541-400.384 1.00 56.68 C ANISOU 1251 CG1 ILE A 187 8110 6362 7062 -961 552 459 C ATOM 1252 CG2 ILE A 187 48.956 90.630-399.273 1.00 56.09 C ANISOU 1252 CG2 ILE A 187 8291 5983 7036 -955 507 427 C ATOM 1253 CD1 ILE A 187 48.894 93.452-400.020 1.00 58.96 C ANISOU 1253 CD1 ILE A 187 8355 6795 7251 -831 575 443 C ATOM 1254 N ILE A 188 50.261 90.702-395.972 1.00 55.54 N ANISOU 1254 N ILE A 188 8613 5480 7011 -870 276 793 N ATOM 1255 CA ILE A 188 50.574 89.673-394.977 1.00 55.81 C ANISOU 1255 CA ILE A 188 8903 5208 7096 -911 151 889 C ATOM 1256 C ILE A 188 50.267 88.306-395.540 1.00 52.05 C ANISOU 1256 C ILE A 188 8514 4595 6668 -1004 170 783 C ATOM 1257 O ILE A 188 49.130 88.030-395.913 1.00 52.80 O ANISOU 1257 O ILE A 188 8602 4762 6697 -929 255 648 O ATOM 1258 CB ILE A 188 49.766 89.814-393.673 1.00 57.56 C ANISOU 1258 CB ILE A 188 9330 5329 7211 -755 99 930 C ATOM 1259 CG1 ILE A 188 49.067 91.169-393.598 1.00 53.66 C ANISOU 1259 CG1 ILE A 188 8683 5097 6610 -608 190 904 C ATOM 1260 CG2 ILE A 188 50.663 89.571-392.457 1.00 59.63 C ANISOU 1260 CG2 ILE A 188 9799 5334 7524 -793 -88 1120 C ATOM 1261 CD1 ILE A 188 48.136 91.312-392.406 1.00 54.77 C ANISOU 1261 CD1 ILE A 188 9018 5165 6627 -438 176 940 C ATOM 1262 N THR A 189 51.282 87.450-395.595 1.00 56.62 N ANISOU 1262 N THR A 189 7006 8266 6240 1726 -847 482 N ATOM 1263 CA THR A 189 51.113 86.095-396.095 1.00 57.50 C ANISOU 1263 CA THR A 189 7254 8227 6365 1628 -947 351 C ATOM 1264 C THR A 189 51.207 85.078-394.961 1.00 55.62 C ANISOU 1264 C THR A 189 6999 7923 6210 1338 -778 402 C ATOM 1265 O THR A 189 50.955 83.892-395.157 1.00 58.65 O ANISOU 1265 O THR A 189 7494 8177 6614 1246 -818 312 O ATOM 1266 CB THR A 189 52.140 85.782-397.191 1.00 58.62 C ANISOU 1266 CB THR A 189 7403 8603 6267 1888 -1152 233 C ATOM 1267 OG1 THR A 189 53.315 86.564-396.967 1.00 58.94 O ANISOU 1267 OG1 THR A 189 7254 9028 6114 2068 -1118 321 O ATOM 1268 CG2 THR A 189 51.582 86.140-398.557 1.00 58.60 C ANISOU 1268 CG2 THR A 189 7526 8470 6268 2110 -1396 91 C ATOM 1269 N ASP A 190 51.556 85.548-393.769 1.00 66.87 N ANISOU 1269 N ASP A 190 8286 9429 7691 1210 -595 546 N ATOM 1270 CA ASP A 190 51.625 84.675-392.604 1.00 66.62 C ANISOU 1270 CA ASP A 190 8225 9311 7775 937 -457 572 C ATOM 1271 C ASP A 190 50.270 84.650-391.909 1.00 61.43 C ANISOU 1271 C ASP A 190 7673 8329 7338 753 -362 597 C ATOM 1272 O ASP A 190 49.881 85.620-391.262 1.00 60.27 O ANISOU 1272 O ASP A 190 7490 8120 7290 717 -253 716 O ATOM 1273 CB ASP A 190 52.716 85.154-391.635 1.00 71.32 C ANISOU 1273 CB ASP A 190 8612 10129 8359 867 -320 720 C ATOM 1274 CG ASP A 190 52.948 84.186-390.486 1.00 73.26 C ANISOU 1274 CG ASP A 190 8805 10294 8736 593 -224 704 C ATOM 1275 OD1 ASP A 190 52.081 83.320-390.254 1.00 80.12 O ANISOU 1275 OD1 ASP A 190 9809 10918 9715 470 -236 598 O ATOM 1276 OD2 ASP A 190 53.997 84.291-389.811 1.00 73.24 O ANISOU 1276 OD2 ASP A 190 8613 10483 8732 510 -142 795 O ATOM 1277 N SER A 191 49.550 83.545-392.055 1.00 54.73 N ANISOU 1277 N SER A 191 6955 7296 6545 663 -401 492 N ATOM 1278 CA SER A 191 48.250 83.397-391.420 1.00 54.72 C ANISOU 1278 CA SER A 191 7044 7028 6719 513 -319 509 C ATOM 1279 C SER A 191 48.372 83.691-389.939 1.00 60.09 C ANISOU 1279 C SER A 191 7641 7666 7523 344 -168 599 C ATOM 1280 O SER A 191 47.425 84.147-389.310 1.00 58.67 O ANISOU 1280 O SER A 191 7510 7312 7470 272 -89 652 O ATOM 1281 CB SER A 191 47.726 81.983-391.612 1.00 59.40 C ANISOU 1281 CB SER A 191 7749 7502 7318 454 -358 407 C ATOM 1282 OG SER A 191 48.393 81.086-390.745 1.00 54.64 O ANISOU 1282 OG SER A 191 7088 6968 6706 349 -313 356 O ATOM 1283 N GLY A 192 49.546 83.415-389.385 1.00 54.86 N ANISOU 1283 N GLY A 192 6852 7162 6829 279 -136 611 N ATOM 1284 CA GLY A 192 49.845 83.757-388.008 1.00 56.15 C ANISOU 1284 CA GLY A 192 6917 7276 7141 105 -7 712 C ATOM 1285 C GLY A 192 49.245 82.816-386.988 1.00 55.96 C ANISOU 1285 C GLY A 192 6954 7040 7269 -74 18 623 C ATOM 1286 O GLY A 192 48.955 83.219-385.864 1.00 60.49 O ANISOU 1286 O GLY A 192 7518 7456 8008 -205 106 695 O ATOM 1287 N ILE A 193 49.068 81.557-387.370 1.00 60.15 N ANISOU 1287 N ILE A 193 7552 7569 7733 -54 -66 464 N ATOM 1288 CA ILE A 193 48.482 80.576-386.466 1.00 58.48 C ANISOU 1288 CA ILE A 193 7394 7196 7628 -163 -62 354 C ATOM 1289 C ILE A 193 48.703 79.146-386.935 1.00 56.49 C ANISOU 1289 C ILE A 193 7173 7039 7252 -94 -152 184 C ATOM 1290 O ILE A 193 48.551 78.843-388.117 1.00 61.67 O ANISOU 1290 O ILE A 193 7909 7762 7760 48 -212 164 O ATOM 1291 CB ILE A 193 46.974 80.816-386.297 1.00 56.33 C ANISOU 1291 CB ILE A 193 7264 6710 7430 -152 -29 384 C ATOM 1292 CG1 ILE A 193 46.412 79.931-385.188 1.00 57.07 C ANISOU 1292 CG1 ILE A 193 7398 6661 7626 -234 -30 274 C ATOM 1293 CG2 ILE A 193 46.245 80.578-387.609 1.00 55.01 C ANISOU 1293 CG2 ILE A 193 7204 6554 7144 -12 -84 371 C ATOM 1294 CD1 ILE A 193 47.092 80.136-383.860 1.00 59.05 C ANISOU 1294 CD1 ILE A 193 7548 6843 8045 -394 -2 271 C ATOM 1295 N LEU A 194 49.071 78.274-385.999 1.00 57.44 N ANISOU 1295 N LEU A 194 7230 7156 7438 -183 -168 56 N ATOM 1296 CA LEU A 194 49.215 76.841-386.267 1.00 58.22 C ANISOU 1296 CA LEU A 194 7358 7351 7413 -89 -247 -126 C ATOM 1297 C LEU A 194 48.610 76.031-385.129 1.00 57.80 C ANISOU 1297 C LEU A 194 7328 7161 7474 -138 -260 -259 C ATOM 1298 O LEU A 194 49.039 76.145-383.986 1.00 60.48 O ANISOU 1298 O LEU A 194 7559 7436 7983 -285 -262 -310 O ATOM 1299 CB LEU A 194 50.686 76.456-386.430 1.00 59.39 C ANISOU 1299 CB LEU A 194 7353 7750 7461 -81 -299 -215 C ATOM 1300 CG LEU A 194 51.011 75.095-387.052 1.00 59.74 C ANISOU 1300 CG LEU A 194 7436 7959 7302 84 -387 -395 C ATOM 1301 CD1 LEU A 194 52.506 74.864-387.025 1.00 60.33 C ANISOU 1301 CD1 LEU A 194 7325 8304 7294 74 -433 -489 C ATOM 1302 CD2 LEU A 194 50.304 73.957-386.349 1.00 61.13 C ANISOU 1302 CD2 LEU A 194 7673 8037 7515 116 -410 -553 C ATOM 1303 N LEU A 195 47.623 75.201-385.450 1.00 57.95 N ANISOU 1303 N LEU A 195 7479 7138 7401 -3 -277 -312 N ATOM 1304 CA LEU A 195 46.989 74.348-384.455 1.00 61.14 C ANISOU 1304 CA LEU A 195 7909 7457 7863 23 -307 -454 C ATOM 1305 C LEU A 195 47.497 72.907-384.551 1.00 59.29 C ANISOU 1305 C LEU A 195 7647 7397 7482 168 -388 -663 C ATOM 1306 O LEU A 195 47.400 72.264-385.602 1.00 59.35 O ANISOU 1306 O LEU A 195 7736 7523 7292 336 -392 -651 O ATOM 1307 CB LEU A 195 45.473 74.383-384.621 1.00 63.15 C ANISOU 1307 CB LEU A 195 8307 7589 8099 108 -258 -360 C ATOM 1308 CG LEU A 195 44.873 75.767-384.855 1.00 60.73 C ANISOU 1308 CG LEU A 195 8041 7153 7881 21 -182 -160 C ATOM 1309 CD1 LEU A 195 43.359 75.681-384.907 1.00 56.07 C ANISOU 1309 CD1 LEU A 195 7560 6473 7271 103 -139 -93 C ATOM 1310 CD2 LEU A 195 45.321 76.722-383.767 1.00 61.90 C ANISOU 1310 CD2 LEU A 195 8111 7188 8221 -149 -162 -137 C ATOM 1311 N ALA A 196 48.044 72.402-383.451 1.00 62.95 N ANISOU 1311 N ALA A 196 7998 7870 8051 113 -461 -860 N ATOM 1312 CA ALA A 196 48.563 71.045-383.418 1.00 61.73 C ANISOU 1312 CA ALA A 196 7796 7901 7759 272 -552 -1099 C ATOM 1313 C ALA A 196 47.765 70.244-382.414 1.00 66.63 C ANISOU 1313 C ALA A 196 8447 8442 8426 380 -618 -1274 C ATOM 1314 O ALA A 196 46.663 69.799-382.710 1.00 61.79 O ANISOU 1314 O ALA A 196 7968 7821 7689 561 -583 -1221 O ATOM 1315 CB ALA A 196 50.034 71.045-383.045 1.00 62.84 C ANISOU 1315 CB ALA A 196 7734 8171 7971 141 -613 -1231 C ATOM 1316 N GLU A 197 48.318 70.073-381.218 1.00 65.31 N ANISOU 1316 N GLU A 197 8147 8222 8447 275 -720 -1480 N ATOM 1317 CA GLU A 197 47.626 69.342-380.169 1.00 70.67 C ANISOU 1317 CA GLU A 197 8847 8821 9183 401 -824 -1690 C ATOM 1318 C GLU A 197 46.462 70.178-379.682 1.00 67.66 C ANISOU 1318 C GLU A 197 8583 8199 8926 338 -772 -1530 C ATOM 1319 O GLU A 197 46.273 71.303-380.144 1.00 66.73 O ANISOU 1319 O GLU A 197 8514 7983 8857 190 -654 -1273 O ATOM 1320 CB GLU A 197 48.567 69.051-379.007 1.00 71.47 C ANISOU 1320 CB GLU A 197 8765 8883 9507 274 -975 -1966 C ATOM 1321 CG GLU A 197 49.906 68.456-379.401 1.00 70.34 C ANISOU 1321 CG GLU A 197 8457 8989 9281 275 -1024 -2121 C ATOM 1322 CD GLU A 197 50.859 69.493-379.960 1.00 71.35 C ANISOU 1322 CD GLU A 197 8489 9152 9469 27 -922 -1901 C ATOM 1323 OE1 GLU A 197 51.904 69.096-380.511 1.00 71.51 O ANISOU 1323 OE1 GLU A 197 8389 9421 9359 56 -941 -1982 O ATOM 1324 OE2 GLU A 197 50.558 70.702-379.849 1.00 68.95 O ANISOU 1324 OE2 GLU A 197 8227 8651 9319 -167 -825 -1652 O ATOM 1325 N ILE A 198 45.683 69.638-378.749 1.00 71.16 N ANISOU 1325 N ILE A 198 9068 8566 9402 481 -870 -1698 N ATOM 1326 CA ILE A 198 44.580 70.400-378.172 1.00 78.96 C ANISOU 1326 CA ILE A 198 10166 9341 10493 448 -842 -1578 C ATOM 1327 C ILE A 198 44.946 70.929-376.786 1.00 77.96 C ANISOU 1327 C ILE A 198 9980 8954 10688 249 -958 -1706 C ATOM 1328 O ILE A 198 44.315 71.855-376.274 1.00 75.83 O ANISOU 1328 O ILE A 198 9795 8468 10549 154 -925 -1578 O ATOM 1329 CB ILE A 198 43.259 69.593-378.144 1.00 81.23 C ANISOU 1329 CB ILE A 198 10566 9727 10572 772 -858 -1622 C ATOM 1330 CG1 ILE A 198 42.827 69.234-379.568 1.00 81.04 C ANISOU 1330 CG1 ILE A 198 10608 9908 10277 921 -714 -1419 C ATOM 1331 CG2 ILE A 198 42.148 70.390-377.473 1.00 74.09 C ANISOU 1331 CG2 ILE A 198 9763 8629 9760 753 -845 -1524 C ATOM 1332 CD1 ILE A 198 42.512 70.439-380.450 1.00 66.69 C ANISOU 1332 CD1 ILE A 198 8851 7999 8489 738 -555 -1099 C ATOM 1333 N GLU A 199 45.983 70.356-376.187 1.00120.33 N ANISOU 1333 N GLU A 199 15195 14333 16191 182 -1096 -1957 N ATOM 1334 CA GLU A 199 46.505 70.906-374.943 1.00126.94 C ANISOU 1334 CA GLU A 199 15952 14892 17389 -67 -1203 -2050 C ATOM 1335 C GLU A 199 46.883 72.365-375.181 1.00118.83 C ANISOU 1335 C GLU A 199 14918 13719 16514 -368 -1038 -1720 C ATOM 1336 O GLU A 199 46.808 73.200-374.278 1.00121.62 O ANISOU 1336 O GLU A 199 15294 13785 17131 -550 -1054 -1652 O ATOM 1337 CB GLU A 199 47.714 70.111-374.439 1.00138.95 C ANISOU 1337 CB GLU A 199 17265 16477 19053 -137 -1364 -2350 C ATOM 1338 CG GLU A 199 48.805 69.866-375.470 1.00134.59 C ANISOU 1338 CG GLU A 199 16575 16209 18353 -185 -1278 -2303 C ATOM 1339 CD GLU A 199 48.771 68.459-376.043 1.00137.04 C ANISOU 1339 CD GLU A 199 16882 16834 18354 153 -1346 -2533 C ATOM 1340 OE1 GLU A 199 49.858 67.882-376.272 1.00132.77 O ANISOU 1340 OE1 GLU A 199 16175 16495 17777 140 -1398 -2694 O ATOM 1341 OE2 GLU A 199 47.660 67.930-376.261 1.00135.02 O ANISOU 1341 OE2 GLU A 199 16782 16640 17878 447 -1341 -2542 O ATOM 1342 N ASN A 200 47.280 72.661-376.412 1.00110.63 N ANISOU 1342 N ASN A 200 13855 12884 15294 -389 -886 -1516 N ATOM 1343 CA ASN A 200 47.618 74.017-376.803 1.00110.96 C ANISOU 1343 CA ASN A 200 13887 12857 15416 -601 -727 -1203 C ATOM 1344 C ASN A 200 46.483 74.696-377.557 1.00105.28 C ANISOU 1344 C ASN A 200 13344 12132 14524 -487 -595 -971 C ATOM 1345 O ASN A 200 46.536 75.891-377.814 1.00104.06 O ANISOU 1345 O ASN A 200 13206 11908 14424 -611 -473 -725 O ATOM 1346 CB ASN A 200 48.885 74.018-377.657 1.00107.87 C ANISOU 1346 CB ASN A 200 13335 12707 14945 -687 -668 -1142 C ATOM 1347 CG ASN A 200 50.077 73.436-376.936 1.00112.93 C ANISOU 1347 CG ASN A 200 13760 13381 15769 -828 -788 -1359 C ATOM 1348 OD1 ASN A 200 50.004 73.137-375.750 1.00111.69 O ANISOU 1348 OD1 ASN A 200 13569 13019 15849 -897 -922 -1549 O ATOM 1349 ND2 ASN A 200 51.188 73.269-377.655 1.00116.71 N ANISOU 1349 ND2 ASN A 200 14083 14123 16140 -864 -756 -1347 N ATOM 1350 N ALA A 201 45.462 73.916-377.897 1.00 91.29 N ANISOU 1350 N ALA A 201 11688 10452 12547 -239 -621 -1051 N ATOM 1351 CA ALA A 201 44.301 74.380-378.660 1.00 91.35 C ANISOU 1351 CA ALA A 201 11838 10481 12391 -122 -507 -853 C ATOM 1352 C ALA A 201 44.132 75.900-378.766 1.00 82.57 C ANISOU 1352 C ALA A 201 10766 9228 11379 -274 -387 -598 C ATOM 1353 O ALA A 201 44.800 76.558-379.560 1.00 77.73 O ANISOU 1353 O ALA A 201 10096 8694 10742 -366 -300 -440 O ATOM 1354 CB ALA A 201 43.022 73.748-378.112 1.00 98.93 C ANISOU 1354 CB ALA A 201 12907 11411 13270 93 -573 -966 C ATOM 1355 N GLU A 202 43.225 76.448-377.965 1.00123.51 N ANISOU 1355 N GLU A 202 16052 14226 16651 -263 -390 -570 N ATOM 1356 CA GLU A 202 42.911 77.874-378.020 1.00123.92 C ANISOU 1356 CA GLU A 202 16160 14157 16767 -352 -275 -342 C ATOM 1357 C GLU A 202 44.011 78.739-377.403 1.00119.42 C ANISOU 1357 C GLU A 202 15502 13443 16428 -580 -247 -252 C ATOM 1358 O GLU A 202 43.906 79.963-377.372 1.00119.07 O ANISOU 1358 O GLU A 202 15495 13306 16441 -642 -144 -52 O ATOM 1359 CB GLU A 202 41.558 78.158-377.352 1.00126.31 C ANISOU 1359 CB GLU A 202 16606 14328 17059 -234 -290 -349 C ATOM 1360 CG GLU A 202 41.371 77.468-376.010 1.00131.74 C ANISOU 1360 CG GLU A 202 17328 14865 17864 -186 -451 -580 C ATOM 1361 CD GLU A 202 42.355 77.956-374.963 1.00140.60 C ANISOU 1361 CD GLU A 202 18398 15741 19283 -408 -504 -603 C ATOM 1362 OE1 GLU A 202 42.112 79.028-374.370 1.00139.19 O ANISOU 1362 OE1 GLU A 202 18301 15353 19232 -482 -457 -472 O ATOM 1363 OE2 GLU A 202 43.367 77.264-374.732 1.00136.81 O ANISOU 1363 OE2 GLU A 202 17789 15279 18913 -505 -590 -747 O ATOM 1364 N ALA A 203 45.065 78.099-376.917 1.00 67.15 N ANISOU 1364 N ALA A 203 8754 6822 9939 -695 -333 -393 N ATOM 1365 CA ALA A 203 46.195 78.826-376.358 1.00 66.56 C ANISOU 1365 CA ALA A 203 8555 6635 10100 -934 -296 -283 C ATOM 1366 C ALA A 203 47.018 79.449-377.473 1.00 66.39 C ANISOU 1366 C ALA A 203 8428 6835 9964 -976 -167 -79 C ATOM 1367 O ALA A 203 47.750 80.408-377.254 1.00 67.46 O ANISOU 1367 O ALA A 203 8475 6926 10230 -1127 -76 116 O ATOM 1368 CB ALA A 203 47.056 77.908-375.517 1.00 69.08 C ANISOU 1368 CB ALA A 203 8737 6900 10609 -1052 -442 -515 C ATOM 1369 N ALA A 204 46.905 78.891-378.670 1.00 66.23 N ANISOU 1369 N ALA A 204 8415 7057 9693 -824 -166 -119 N ATOM 1370 CA ALA A 204 47.534 79.480-379.837 1.00 64.14 C ANISOU 1370 CA ALA A 204 8082 7004 9285 -804 -75 49 C ATOM 1371 C ALA A 204 46.556 80.479-380.420 1.00 62.57 C ANISOU 1371 C ALA A 204 8014 6769 8992 -698 16 222 C ATOM 1372 O ALA A 204 46.948 81.465-381.033 1.00 65.64 O ANISOU 1372 O ALA A 204 8359 7250 9331 -690 100 403 O ATOM 1373 CB ALA A 204 47.867 78.418-380.851 1.00 66.73 C ANISOU 1373 CB ALA A 204 8378 7576 9402 -679 -136 -85 C ATOM 1374 N MET A 205 45.273 80.208-380.216 1.00 65.36 N ANISOU 1374 N MET A 205 8511 7011 9311 -596 -11 155 N ATOM 1375 CA MET A 205 44.207 81.097-380.654 1.00 61.71 C ANISOU 1375 CA MET A 205 8161 6511 8774 -497 63 287 C ATOM 1376 C MET A 205 44.185 82.339-379.780 1.00 63.82 C ANISOU 1376 C MET A 205 8453 6602 9193 -576 138 432 C ATOM 1377 O MET A 205 43.472 83.295-380.064 1.00 58.66 O ANISOU 1377 O MET A 205 7873 5930 8486 -492 209 552 O ATOM 1378 CB MET A 205 42.855 80.390-380.562 1.00 61.44 C ANISOU 1378 CB MET A 205 8248 6437 8660 -367 16 177 C ATOM 1379 CG MET A 205 42.715 79.190-381.472 1.00 59.50 C ANISOU 1379 CG MET A 205 7997 6360 8249 -258 -32 78 C ATOM 1380 SD MET A 205 42.527 79.707-383.177 1.00 56.04 S ANISOU 1380 SD MET A 205 7565 6064 7663 -184 25 224 S ATOM 1381 CE MET A 205 41.018 80.655-383.050 1.00 57.47 C ANISOU 1381 CE MET A 205 7840 6141 7854 -124 89 325 C ATOM 1382 N THR A 206 44.967 82.315-378.710 1.00 65.73 N ANISOU 1382 N THR A 206 8630 6710 9635 -735 119 420 N ATOM 1383 CA THR A 206 44.997 83.413-377.758 1.00 63.39 C ANISOU 1383 CA THR A 206 8368 6204 9512 -821 192 576 C ATOM 1384 C THR A 206 46.435 83.818-377.480 1.00 65.36 C ANISOU 1384 C THR A 206 8446 6475 9913 -1003 251 716 C ATOM 1385 O THR A 206 46.865 83.917-376.331 1.00 73.85 O ANISOU 1385 O THR A 206 9491 7333 11235 -1171 239 740 O ATOM 1386 CB THR A 206 44.287 83.030-376.451 1.00 70.10 C ANISOU 1386 CB THR A 206 9338 6782 10515 -841 97 437 C ATOM 1387 OG1 THR A 206 42.941 82.633-376.745 1.00 67.71 O ANISOU 1387 OG1 THR A 206 9169 6518 10038 -649 52 324 O ATOM 1388 CG2 THR A 206 44.263 84.204-375.479 1.00 75.64 C ANISOU 1388 CG2 THR A 206 10110 7233 11395 -915 172 614 C ATOM 1389 N ALA A 207 47.184 84.033-378.550 1.00 64.83 N ANISOU 1389 N ALA A 207 8258 6675 9700 -964 306 809 N ATOM 1390 CA ALA A 207 48.546 84.509-378.433 1.00 66.69 C ANISOU 1390 CA ALA A 207 8303 7009 10028 -1100 384 979 C ATOM 1391 C ALA A 207 48.545 85.993-378.721 1.00 68.51 C ANISOU 1391 C ALA A 207 8542 7293 10196 -1006 535 1259 C ATOM 1392 O ALA A 207 47.935 86.434-379.689 1.00 66.41 O ANISOU 1392 O ALA A 207 8351 7160 9723 -803 552 1274 O ATOM 1393 CB ALA A 207 49.438 83.792-379.413 1.00 64.96 C ANISOU 1393 CB ALA A 207 7936 7095 9651 -1071 335 893 C ATOM 1394 N VAL A 208 49.222 86.765-377.880 1.00 80.81 N ANISOU 1394 N VAL A 208 10016 8746 11942 -1143 644 1481 N ATOM 1395 CA VAL A 208 49.261 88.210-378.046 1.00 82.86 C ANISOU 1395 CA VAL A 208 10281 9067 12136 -1022 804 1770 C ATOM 1396 C VAL A 208 49.434 88.593-379.511 1.00 75.60 C ANISOU 1396 C VAL A 208 9302 8506 10918 -786 820 1799 C ATOM 1397 O VAL A 208 48.681 89.405-380.036 1.00 70.45 O ANISOU 1397 O VAL A 208 8755 7895 10117 -571 857 1847 O ATOM 1398 CB VAL A 208 50.378 88.847-377.203 1.00 94.14 C ANISOU 1398 CB VAL A 208 11547 10444 13777 -1207 939 2053 C ATOM 1399 CG1 VAL A 208 50.059 88.715-375.722 1.00 93.46 C ANISOU 1399 CG1 VAL A 208 11561 9933 14017 -1417 916 2047 C ATOM 1400 CG2 VAL A 208 51.721 88.204-377.523 1.00 73.00 C ANISOU 1400 CG2 VAL A 208 8610 8019 11109 -1341 917 2044 C ATOM 1401 N ASP A 209 50.414 87.989-380.172 1.00 86.29 N ANISOU 1401 N ASP A 209 10487 10117 12182 -810 771 1745 N ATOM 1402 CA ASP A 209 50.709 88.313-381.563 1.00 82.99 C ANISOU 1402 CA ASP A 209 10010 10037 11485 -573 754 1757 C ATOM 1403 C ASP A 209 49.518 88.053-382.489 1.00 74.95 C ANISOU 1403 C ASP A 209 9170 9000 10309 -391 645 1559 C ATOM 1404 O ASP A 209 49.151 88.907-383.290 1.00 73.06 O ANISOU 1404 O ASP A 209 8967 8880 9912 -167 659 1614 O ATOM 1405 CB ASP A 209 51.956 87.560-382.032 1.00 93.00 C ANISOU 1405 CB ASP A 209 11080 11575 12680 -629 698 1700 C ATOM 1406 CG ASP A 209 53.233 88.103-381.405 1.00105.45 C ANISOU 1406 CG ASP A 209 12425 13278 14364 -760 830 1961 C ATOM 1407 OD1 ASP A 209 53.714 89.167-381.848 1.00107.29 O ANISOU 1407 OD1 ASP A 209 12562 13748 14454 -585 935 2191 O ATOM 1408 OD2 ASP A 209 53.758 87.463-380.467 1.00104.93 O ANISOU 1408 OD2 ASP A 209 12257 13083 14529 -1029 827 1936 O ATOM 1409 N PHE A 210 48.910 86.879-382.375 1.00 68.11 N ANISOU 1409 N PHE A 210 8399 7990 9488 -477 536 1331 N ATOM 1410 CA PHE A 210 47.734 86.557-383.180 1.00 63.05 C ANISOU 1410 CA PHE A 210 7911 7318 8729 -336 450 1175 C ATOM 1411 C PHE A 210 46.573 87.478-382.835 1.00 63.17 C ANISOU 1411 C PHE A 210 8059 7167 8774 -254 512 1243 C ATOM 1412 O PHE A 210 46.102 88.237-383.678 1.00 63.85 O ANISOU 1412 O PHE A 210 8176 7351 8733 -66 513 1272 O ATOM 1413 CB PHE A 210 47.323 85.102-382.970 1.00 61.91 C ANISOU 1413 CB PHE A 210 7829 7068 8625 -431 346 955 C ATOM 1414 CG PHE A 210 46.159 84.665-383.813 1.00 58.06 C ANISOU 1414 CG PHE A 210 7473 6564 8023 -304 274 832 C ATOM 1415 CD1 PHE A 210 46.247 84.664-385.193 1.00 56.56 C ANISOU 1415 CD1 PHE A 210 7274 6546 7669 -160 215 807 C ATOM 1416 CD2 PHE A 210 44.988 84.218-383.223 1.00 59.67 C ANISOU 1416 CD2 PHE A 210 7801 6582 8290 -324 258 745 C ATOM 1417 CE1 PHE A 210 45.181 84.244-385.969 1.00 58.78 C ANISOU 1417 CE1 PHE A 210 7661 6785 7887 -75 154 719 C ATOM 1418 CE2 PHE A 210 43.920 83.794-383.994 1.00 59.22 C ANISOU 1418 CE2 PHE A 210 7834 6531 8136 -221 211 666 C ATOM 1419 CZ PHE A 210 44.017 83.808-385.368 1.00 58.56 C ANISOU 1419 CZ PHE A 210 7734 6591 7926 -115 165 664 C ATOM 1420 N GLN A 211 46.121 87.406-381.586 1.00 61.15 N ANISOU 1420 N GLN A 211 7882 6666 8688 -379 546 1248 N ATOM 1421 CA GLN A 211 45.006 88.215-381.108 1.00 60.90 C ANISOU 1421 CA GLN A 211 7990 6472 8677 -294 601 1298 C ATOM 1422 C GLN A 211 45.196 89.688-381.432 1.00 61.43 C ANISOU 1422 C GLN A 211 8025 6655 8660 -129 711 1499 C ATOM 1423 O GLN A 211 44.228 90.437-381.522 1.00 61.41 O ANISOU 1423 O GLN A 211 8122 6617 8593 24 739 1509 O ATOM 1424 CB GLN A 211 44.817 88.027-379.601 1.00 61.19 C ANISOU 1424 CB GLN A 211 8103 6224 8921 -449 615 1300 C ATOM 1425 CG GLN A 211 44.073 86.760-379.225 1.00 62.74 C ANISOU 1425 CG GLN A 211 8388 6295 9156 -503 490 1065 C ATOM 1426 CD GLN A 211 42.579 86.891-379.418 1.00 59.78 C ANISOU 1426 CD GLN A 211 8158 5884 8670 -346 470 987 C ATOM 1427 OE1 GLN A 211 42.013 87.954-379.189 1.00 60.05 O ANISOU 1427 OE1 GLN A 211 8272 5864 8682 -243 543 1091 O ATOM 1428 NE2 GLN A 211 41.933 85.811-379.835 1.00 59.43 N ANISOU 1428 NE2 GLN A 211 8143 5892 8547 -312 376 813 N ATOM 1429 N ALA A 212 46.446 90.097-381.607 1.00 62.38 N ANISOU 1429 N ALA A 212 7992 6946 8765 -137 774 1657 N ATOM 1430 CA ALA A 212 46.747 91.481-381.932 1.00 66.52 C ANISOU 1430 CA ALA A 212 8463 7633 9179 65 883 1863 C ATOM 1431 C ALA A 212 46.091 91.881-383.240 1.00 65.15 C ANISOU 1431 C ALA A 212 8318 7634 8803 324 804 1749 C ATOM 1432 O ALA A 212 45.351 92.859-383.297 1.00 60.57 O ANISOU 1432 O ALA A 212 7808 7048 8158 509 848 1788 O ATOM 1433 CB ALA A 212 48.238 91.686-382.021 1.00 65.11 C ANISOU 1433 CB ALA A 212 8083 7670 8985 33 951 2043 C ATOM 1434 N ASN A 213 46.365 91.120-384.291 1.00 65.00 N ANISOU 1434 N ASN A 213 8244 7762 8692 341 676 1599 N ATOM 1435 CA ASN A 213 45.860 91.442-385.614 1.00 57.45 C ANISOU 1435 CA ASN A 213 7301 6948 7579 568 570 1482 C ATOM 1436 C ASN A 213 44.360 91.248-385.734 1.00 62.23 C ANISOU 1436 C ASN A 213 8045 7383 8218 575 514 1331 C ATOM 1437 O ASN A 213 43.710 91.893-386.551 1.00 56.18 O ANISOU 1437 O ASN A 213 7291 6687 7369 766 459 1266 O ATOM 1438 CB ASN A 213 46.588 90.635-386.678 1.00 62.96 C ANISOU 1438 CB ASN A 213 7923 7817 8182 582 438 1369 C ATOM 1439 CG ASN A 213 48.037 91.016-386.788 1.00 64.18 C ANISOU 1439 CG ASN A 213 7913 8229 8244 652 480 1514 C ATOM 1440 OD1 ASN A 213 48.592 91.080-387.880 1.00 65.74 O ANISOU 1440 OD1 ASN A 213 8042 8655 8281 831 375 1458 O ATOM 1441 ND2 ASN A 213 48.663 91.290-385.652 1.00 67.70 N ANISOU 1441 ND2 ASN A 213 8289 8641 8792 517 631 1709 N ATOM 1442 N LEU A 214 43.805 90.363-384.917 1.00 59.82 N ANISOU 1442 N LEU A 214 7826 6870 8033 379 521 1269 N ATOM 1443 CA LEU A 214 42.363 90.182-384.908 1.00 60.54 C ANISOU 1443 CA LEU A 214 8030 6830 8141 393 487 1153 C ATOM 1444 C LEU A 214 41.695 91.496-384.512 1.00 55.29 C ANISOU 1444 C LEU A 214 7415 6145 7449 552 571 1232 C ATOM 1445 O LEU A 214 40.545 91.754-384.870 1.00 55.26 O ANISOU 1445 O LEU A 214 7459 6129 7407 649 537 1140 O ATOM 1446 CB LEU A 214 41.963 89.059-383.955 1.00 58.64 C ANISOU 1446 CB LEU A 214 7868 6404 8009 204 481 1083 C ATOM 1447 CG LEU A 214 42.428 87.660-384.349 1.00 58.66 C ANISOU 1447 CG LEU A 214 7834 6437 8016 85 392 974 C ATOM 1448 CD1 LEU A 214 41.955 86.641-383.326 1.00 54.64 C ANISOU 1448 CD1 LEU A 214 7399 5763 7597 -44 377 886 C ATOM 1449 CD2 LEU A 214 41.921 87.303-385.733 1.00 57.56 C ANISOU 1449 CD2 LEU A 214 7692 6393 7786 173 298 880 C ATOM 1450 N LYS A 215 42.429 92.320-383.767 1.00 57.05 N ANISOU 1450 N LYS A 215 7615 6372 7688 582 689 1412 N ATOM 1451 CA LYS A 215 41.967 93.647-383.393 1.00 57.75 C ANISOU 1451 CA LYS A 215 7753 6467 7724 776 786 1515 C ATOM 1452 C LYS A 215 42.250 94.597-384.541 1.00 66.45 C ANISOU 1452 C LYS A 215 8754 7825 8669 1045 757 1523 C ATOM 1453 O LYS A 215 41.359 95.297-385.018 1.00 65.22 O ANISOU 1453 O LYS A 215 8622 7727 8432 1244 724 1434 O ATOM 1454 CB LYS A 215 42.698 94.134-382.139 1.00 61.37 C ANISOU 1454 CB LYS A 215 8228 6815 8274 706 934 1742 C ATOM 1455 CG LYS A 215 42.202 93.549-380.823 1.00 62.26 C ANISOU 1455 CG LYS A 215 8477 6631 8549 511 950 1723 C ATOM 1456 CD LYS A 215 43.264 93.677-379.725 1.00 65.85 C ANISOU 1456 CD LYS A 215 8904 6949 9166 349 1057 1937 C ATOM 1457 CE LYS A 215 42.717 93.324-378.339 1.00 66.73 C ANISOU 1457 CE LYS A 215 9174 6727 9452 203 1054 1913 C ATOM 1458 NZ LYS A 215 43.783 92.951-377.356 1.00 71.04 N ANISOU 1458 NZ LYS A 215 9667 7093 10232 -51 1091 2044 N ATOM 1459 N LYS A 216 43.503 94.598-384.983 1.00 58.68 N ANISOU 1459 N LYS A 216 7645 7013 7639 1065 755 1611 N ATOM 1460 CA LYS A 216 43.989 95.527-385.997 1.00 59.30 C ANISOU 1460 CA LYS A 216 7614 7368 7550 1361 717 1630 C ATOM 1461 C LYS A 216 43.123 95.552-387.244 1.00 61.35 C ANISOU 1461 C LYS A 216 7879 7687 7746 1512 543 1392 C ATOM 1462 O LYS A 216 42.849 96.613-387.792 1.00 57.65 O ANISOU 1462 O LYS A 216 7375 7367 7164 1804 513 1356 O ATOM 1463 CB LYS A 216 45.418 95.166-386.384 1.00 59.03 C ANISOU 1463 CB LYS A 216 7441 7521 7465 1332 699 1713 C ATOM 1464 CG LYS A 216 46.125 96.218-387.208 1.00 63.63 C ANISOU 1464 CG LYS A 216 7897 8429 7849 1678 681 1781 C ATOM 1465 CD LYS A 216 47.555 95.788-387.501 1.00 64.26 C ANISOU 1465 CD LYS A 216 7832 8722 7863 1646 667 1871 C ATOM 1466 CE LYS A 216 48.465 96.981-387.770 1.00 66.66 C ANISOU 1466 CE LYS A 216 7988 9371 7967 1983 739 2062 C ATOM 1467 NZ LYS A 216 49.870 96.557-388.029 1.00 72.36 N ANISOU 1467 NZ LYS A 216 8545 10344 8603 1960 731 2159 N ATOM 1468 N TYR A 217 42.701 94.382-387.699 1.00 60.51 N ANISOU 1468 N TYR A 217 7807 7463 7720 1321 424 1230 N ATOM 1469 CA TYR A 217 41.914 94.299-388.916 1.00 55.01 C ANISOU 1469 CA TYR A 217 7104 6786 7011 1415 254 1025 C ATOM 1470 C TYR A 217 40.469 93.940-388.611 1.00 54.27 C ANISOU 1470 C TYR A 217 7098 6506 7015 1293 257 928 C ATOM 1471 O TYR A 217 39.757 93.417-389.464 1.00 54.20 O ANISOU 1471 O TYR A 217 7085 6449 7058 1247 133 782 O ATOM 1472 CB TYR A 217 42.536 93.295-389.880 1.00 54.37 C ANISOU 1472 CB TYR A 217 6987 6740 6932 1334 109 933 C ATOM 1473 CG TYR A 217 43.977 93.605-390.187 1.00 60.86 C ANISOU 1473 CG TYR A 217 7708 7788 7627 1474 97 1020 C ATOM 1474 CD1 TYR A 217 44.314 94.589-391.103 1.00 61.54 C ANISOU 1474 CD1 TYR A 217 7714 8092 7577 1798 -5 973 C ATOM 1475 CD2 TYR A 217 45.002 92.924-389.552 1.00 56.97 C ANISOU 1475 CD2 TYR A 217 7185 7317 7143 1302 179 1140 C ATOM 1476 CE1 TYR A 217 45.631 94.882-391.383 1.00 57.06 C ANISOU 1476 CE1 TYR A 217 7040 7780 6859 1963 -16 1062 C ATOM 1477 CE2 TYR A 217 46.324 93.208-389.824 1.00 57.55 C ANISOU 1477 CE2 TYR A 217 7140 7641 7087 1433 177 1233 C ATOM 1478 CZ TYR A 217 46.637 94.190-390.741 1.00 60.45 C ANISOU 1478 CZ TYR A 217 7431 8245 7294 1773 84 1204 C ATOM 1479 OH TYR A 217 47.960 94.476-391.016 1.00 59.54 O ANISOU 1479 OH TYR A 217 7182 8425 7014 1940 81 1306 O ATOM 1480 N GLY A 218 40.047 94.229-387.385 1.00 55.54 N ANISOU 1480 N GLY A 218 7337 6566 7200 1248 400 1023 N ATOM 1481 CA GLY A 218 38.661 94.076-386.970 1.00 55.38 C ANISOU 1481 CA GLY A 218 7394 6419 7227 1193 414 943 C ATOM 1482 C GLY A 218 37.906 92.856-387.477 1.00 56.22 C ANISOU 1482 C GLY A 218 7510 6437 7415 1012 319 819 C ATOM 1483 O GLY A 218 36.844 92.989-388.085 1.00 57.80 O ANISOU 1483 O GLY A 218 7682 6650 7629 1059 254 708 O ATOM 1484 N ILE A 219 38.450 91.671-387.217 1.00 53.35 N ANISOU 1484 N ILE A 219 7171 5994 7105 813 318 846 N ATOM 1485 CA ILE A 219 37.788 90.417-387.565 1.00 53.34 C ANISOU 1485 CA ILE A 219 7187 5918 7162 659 256 765 C ATOM 1486 C ILE A 219 37.841 89.448-386.390 1.00 52.60 C ANISOU 1486 C ILE A 219 7170 5708 7107 499 321 799 C ATOM 1487 O ILE A 219 38.600 89.667-385.444 1.00 53.39 O ANISOU 1487 O ILE A 219 7298 5765 7222 469 390 878 O ATOM 1488 CB ILE A 219 38.419 89.749-388.804 1.00 52.72 C ANISOU 1488 CB ILE A 219 7054 5886 7092 627 136 715 C ATOM 1489 CG1 ILE A 219 39.944 89.751-388.698 1.00 52.24 C ANISOU 1489 CG1 ILE A 219 6963 5901 6983 636 143 780 C ATOM 1490 CG2 ILE A 219 37.967 90.444-390.072 1.00 54.63 C ANISOU 1490 CG2 ILE A 219 7228 6189 7339 766 21 627 C ATOM 1491 CD1 ILE A 219 40.640 89.211-389.927 1.00 52.81 C ANISOU 1491 CD1 ILE A 219 6995 6045 7026 657 11 719 C ATOM 1492 N PRO A 220 37.024 88.380-386.441 1.00 52.56 N ANISOU 1492 N PRO A 220 7191 5656 7125 408 293 741 N ATOM 1493 CA PRO A 220 36.939 87.389-385.364 1.00 52.32 C ANISOU 1493 CA PRO A 220 7229 5536 7115 304 324 733 C ATOM 1494 C PRO A 220 38.057 86.371-385.469 1.00 52.09 C ANISOU 1494 C PRO A 220 7180 5507 7105 200 286 721 C ATOM 1495 O PRO A 220 38.717 86.300-386.505 1.00 55.09 O ANISOU 1495 O PRO A 220 7504 5963 7466 209 232 720 O ATOM 1496 CB PRO A 220 35.602 86.687-385.631 1.00 53.04 C ANISOU 1496 CB PRO A 220 7322 5645 7186 302 307 687 C ATOM 1497 CG PRO A 220 34.942 87.445-386.740 1.00 51.94 C ANISOU 1497 CG PRO A 220 7110 5576 7049 374 278 679 C ATOM 1498 CD PRO A 220 36.041 88.102-387.497 1.00 52.07 C ANISOU 1498 CD PRO A 220 7082 5628 7075 416 231 687 C ATOM 1499 N GLY A 221 38.258 85.584-384.420 1.00 56.34 N ANISOU 1499 N GLY A 221 7764 5968 7675 122 295 691 N ATOM 1500 CA GLY A 221 39.298 84.572-384.434 1.00 56.69 C ANISOU 1500 CA GLY A 221 7777 6030 7733 34 253 651 C ATOM 1501 C GLY A 221 38.822 83.250-384.999 1.00 55.54 C ANISOU 1501 C GLY A 221 7639 5930 7534 37 203 582 C ATOM 1502 O GLY A 221 38.644 82.286-384.259 1.00 59.79 O ANISOU 1502 O GLY A 221 8209 6438 8069 22 186 510 O ATOM 1503 N VAL A 222 38.621 83.200-386.311 1.00 52.49 N ANISOU 1503 N VAL A 222 7223 5612 7107 73 172 604 N ATOM 1504 CA VAL A 222 38.146 81.984-386.962 1.00 51.76 C ANISOU 1504 CA VAL A 222 7143 5556 6969 82 142 584 C ATOM 1505 C VAL A 222 39.171 81.459-387.966 1.00 51.91 C ANISOU 1505 C VAL A 222 7142 5632 6948 81 77 568 C ATOM 1506 O VAL A 222 39.478 82.119-388.950 1.00 52.00 O ANISOU 1506 O VAL A 222 7129 5664 6966 109 31 593 O ATOM 1507 CB VAL A 222 36.810 82.223-387.685 1.00 59.36 C ANISOU 1507 CB VAL A 222 8093 6519 7941 115 158 640 C ATOM 1508 CG1 VAL A 222 36.237 80.916-388.187 1.00 51.74 C ANISOU 1508 CG1 VAL A 222 7136 5587 6934 123 159 667 C ATOM 1509 CG2 VAL A 222 35.824 82.911-386.759 1.00 53.31 C ANISOU 1509 CG2 VAL A 222 7341 5732 7183 147 216 646 C ATOM 1510 N VAL A 223 39.697 80.264-387.722 1.00 54.25 N ANISOU 1510 N VAL A 223 7453 5968 7193 77 56 506 N ATOM 1511 CA VAL A 223 40.727 79.704-388.589 1.00 54.05 C ANISOU 1511 CA VAL A 223 7419 6018 7100 101 -10 475 C ATOM 1512 C VAL A 223 40.381 78.288-389.017 1.00 52.28 C ANISOU 1512 C VAL A 223 7242 5825 6796 158 -21 459 C ATOM 1513 O VAL A 223 39.573 77.624-388.373 1.00 54.41 O ANISOU 1513 O VAL A 223 7533 6091 7051 184 25 454 O ATOM 1514 CB VAL A 223 42.085 79.665-387.876 1.00 54.67 C ANISOU 1514 CB VAL A 223 7444 6160 7169 61 -26 403 C ATOM 1515 CG1 VAL A 223 42.449 81.050-387.350 1.00 54.22 C ANISOU 1515 CG1 VAL A 223 7335 6077 7190 12 13 462 C ATOM 1516 CG2 VAL A 223 42.052 78.652-386.742 1.00 54.08 C ANISOU 1516 CG2 VAL A 223 7375 6076 7098 41 -18 304 C ATOM 1517 N ALA A 224 40.992 77.828-390.103 1.00 54.78 N ANISOU 1517 N ALA A 224 7583 6186 7045 208 -84 455 N ATOM 1518 CA ALA A 224 40.842 76.442-390.530 1.00 55.65 C ANISOU 1518 CA ALA A 224 7749 6336 7058 290 -87 452 C ATOM 1519 C ALA A 224 41.408 75.528-389.450 1.00 53.72 C ANISOU 1519 C ALA A 224 7486 6188 6737 328 -82 323 C ATOM 1520 O ALA A 224 42.391 75.869-388.796 1.00 53.33 O ANISOU 1520 O ALA A 224 7375 6181 6706 276 -111 228 O ATOM 1521 CB ALA A 224 41.553 76.207-391.852 1.00 56.47 C ANISOU 1521 CB ALA A 224 7901 6458 7097 353 -174 456 C ATOM 1522 N LEU A 225 40.794 74.369-389.262 1.00 56.23 N ANISOU 1522 N LEU A 225 7840 6550 6974 427 -48 320 N ATOM 1523 CA LEU A 225 41.160 73.496-388.157 1.00 57.12 C ANISOU 1523 CA LEU A 225 7925 6754 7024 495 -64 164 C ATOM 1524 C LEU A 225 42.499 72.791-388.359 1.00 55.74 C ANISOU 1524 C LEU A 225 7734 6703 6743 557 -136 25 C ATOM 1525 O LEU A 225 43.188 72.478-387.395 1.00 57.02 O ANISOU 1525 O LEU A 225 7828 6926 6910 551 -180 -142 O ATOM 1526 CB LEU A 225 40.053 72.471-387.925 1.00 57.93 C ANISOU 1526 CB LEU A 225 8063 6910 7038 642 -10 201 C ATOM 1527 CG LEU A 225 40.305 71.400-386.862 1.00 56.85 C ANISOU 1527 CG LEU A 225 7901 6890 6808 783 -51 11 C ATOM 1528 CD1 LEU A 225 40.183 72.008-385.478 1.00 58.09 C ANISOU 1528 CD1 LEU A 225 8011 6969 7091 700 -85 -101 C ATOM 1529 CD2 LEU A 225 39.347 70.224-387.025 1.00 58.86 C ANISOU 1529 CD2 LEU A 225 8195 7263 6908 1004 7 80 C ATOM 1530 N TYR A 226 42.866 72.542-389.610 1.00 54.75 N ANISOU 1530 N TYR A 226 7666 6610 6527 620 -161 83 N ATOM 1531 CA TYR A 226 44.051 71.749-389.904 1.00 55.69 C ANISOU 1531 CA TYR A 226 7783 6880 6498 726 -230 -51 C ATOM 1532 C TYR A 226 45.049 72.509-390.748 1.00 55.37 C ANISOU 1532 C TYR A 226 7730 6862 6446 681 -298 -42 C ATOM 1533 O TYR A 226 44.674 73.162-391.718 1.00 58.46 O ANISOU 1533 O TYR A 226 8182 7149 6883 660 -308 88 O ATOM 1534 CB TYR A 226 43.655 70.468-390.629 1.00 55.84 C ANISOU 1534 CB TYR A 226 7907 6958 6353 926 -210 -9 C ATOM 1535 CG TYR A 226 42.806 69.550-389.794 1.00 62.04 C ANISOU 1535 CG TYR A 226 8688 7796 7088 1044 -150 -35 C ATOM 1536 CD1 TYR A 226 43.169 69.237-388.496 1.00 57.61 C ANISOU 1536 CD1 TYR A 226 8038 7320 6533 1063 -191 -242 C ATOM 1537 CD2 TYR A 226 41.646 68.993-390.301 1.00 59.31 C ANISOU 1537 CD2 TYR A 226 8417 7423 6694 1149 -62 148 C ATOM 1538 CE1 TYR A 226 42.401 68.403-387.725 1.00 59.39 C ANISOU 1538 CE1 TYR A 226 8258 7611 6695 1218 -167 -295 C ATOM 1539 CE2 TYR A 226 40.870 68.153-389.535 1.00 59.10 C ANISOU 1539 CE2 TYR A 226 8374 7494 6587 1304 -8 131 C ATOM 1540 CZ TYR A 226 41.256 67.861-388.248 1.00 59.34 C ANISOU 1540 CZ TYR A 226 8326 7620 6602 1356 -72 -107 C ATOM 1541 OH TYR A 226 40.496 67.024-387.467 1.00 61.26 O ANISOU 1541 OH TYR A 226 8551 7976 6748 1556 -48 -156 O ATOM 1542 N PRO A 227 46.334 72.421-390.389 1.00 57.63 N ANISOU 1542 N PRO A 227 7926 7301 6670 681 -358 -192 N ATOM 1543 CA PRO A 227 47.361 73.097-391.182 1.00 55.37 C ANISOU 1543 CA PRO A 227 7611 7098 6328 684 -429 -187 C ATOM 1544 C PRO A 227 47.217 72.627-392.615 1.00 55.88 C ANISOU 1544 C PRO A 227 7826 7145 6262 843 -483 -130 C ATOM 1545 O PRO A 227 46.876 71.466-392.816 1.00 58.09 O ANISOU 1545 O PRO A 227 8196 7440 6435 973 -467 -148 O ATOM 1546 CB PRO A 227 48.667 72.569-390.590 1.00 58.12 C ANISOU 1546 CB PRO A 227 7836 7667 6581 707 -476 -371 C ATOM 1547 CG PRO A 227 48.310 72.102-389.215 1.00 57.94 C ANISOU 1547 CG PRO A 227 7742 7608 6665 633 -434 -467 C ATOM 1548 CD PRO A 227 46.900 71.611-389.300 1.00 62.45 C ANISOU 1548 CD PRO A 227 8443 8037 7247 704 -376 -383 C ATOM 1549 N GLY A 228 47.435 73.498-393.590 1.00 54.74 N ANISOU 1549 N GLY A 228 7714 6958 6127 852 -552 -61 N ATOM 1550 CA GLY A 228 47.330 73.075-394.973 1.00 56.24 C ANISOU 1550 CA GLY A 228 8061 7087 6221 999 -634 -17 C ATOM 1551 C GLY A 228 46.687 74.061-395.914 1.00 56.85 C ANISOU 1551 C GLY A 228 8197 6968 6434 960 -687 105 C ATOM 1552 O GLY A 228 45.729 74.736-395.561 1.00 54.73 O ANISOU 1552 O GLY A 228 7891 6558 6346 824 -616 201 O ATOM 1553 N GLU A 229 47.218 74.126-397.129 1.00 55.35 N ANISOU 1553 N GLU A 229 8101 6776 6152 1099 -830 80 N ATOM 1554 CA GLU A 229 46.687 75.002-398.159 1.00 58.14 C ANISOU 1554 CA GLU A 229 8514 6934 6641 1093 -930 154 C ATOM 1555 C GLU A 229 45.281 74.563-398.522 1.00 59.03 C ANISOU 1555 C GLU A 229 8721 6787 6921 1008 -861 307 C ATOM 1556 O GLU A 229 44.543 75.284-399.175 1.00 60.39 O ANISOU 1556 O GLU A 229 8909 6763 7275 943 -915 380 O ATOM 1557 CB GLU A 229 47.572 74.967-399.406 1.00 60.32 C ANISOU 1557 CB GLU A 229 8897 7252 6769 1297 -1130 70 C ATOM 1558 CG GLU A 229 49.069 75.048-399.127 1.00 57.26 C ANISOU 1558 CG GLU A 229 8418 7190 6147 1428 -1191 -77 C ATOM 1559 CD GLU A 229 49.676 73.700-398.769 1.00 58.30 C ANISOU 1559 CD GLU A 229 8580 7496 6075 1518 -1145 -159 C ATOM 1560 OE1 GLU A 229 48.921 72.704-398.674 1.00 61.89 O ANISOU 1560 OE1 GLU A 229 9132 7825 6560 1499 -1055 -96 O ATOM 1561 OE2 GLU A 229 50.909 73.636-398.583 1.00 57.61 O ANISOU 1561 OE2 GLU A 229 8406 7695 5787 1626 -1198 -286 O ATOM 1562 N LEU A 230 44.911 73.366-398.099 1.00 61.71 N ANISOU 1562 N LEU A 230 9104 7146 7196 1023 -744 355 N ATOM 1563 CA LEU A 230 43.575 72.872-398.363 1.00 62.07 C ANISOU 1563 CA LEU A 230 9212 6994 7379 955 -648 538 C ATOM 1564 C LEU A 230 42.558 73.683-397.592 1.00 60.99 C ANISOU 1564 C LEU A 230 8950 6793 7430 773 -543 611 C ATOM 1565 O LEU A 230 41.376 73.663-397.913 1.00 56.61 O ANISOU 1565 O LEU A 230 8405 6075 7031 686 -482 770 O ATOM 1566 CB LEU A 230 43.459 71.402-397.974 1.00 62.95 C ANISOU 1566 CB LEU A 230 9382 7204 7333 1067 -535 571 C ATOM 1567 CG LEU A 230 43.632 70.400-399.112 1.00 64.83 C ANISOU 1567 CG LEU A 230 9803 7369 7462 1237 -589 638 C ATOM 1568 CD1 LEU A 230 43.703 68.983-398.570 1.00 59.94 C ANISOU 1568 CD1 LEU A 230 9221 6922 6632 1404 -475 631 C ATOM 1569 CD2 LEU A 230 42.484 70.560-400.091 1.00 62.09 C ANISOU 1569 CD2 LEU A 230 9528 6724 7341 1137 -582 864 C ATOM 1570 N GLY A 231 43.023 74.391-396.569 1.00 60.15 N ANISOU 1570 N GLY A 231 8722 6821 7310 717 -519 505 N ATOM 1571 CA GLY A 231 42.149 75.199-395.737 1.00 59.39 C ANISOU 1571 CA GLY A 231 8522 6680 7364 573 -425 556 C ATOM 1572 C GLY A 231 41.721 76.482-396.417 1.00 54.11 C ANISOU 1572 C GLY A 231 7823 5874 6862 506 -501 591 C ATOM 1573 O GLY A 231 40.738 77.102-396.035 1.00 59.30 O ANISOU 1573 O GLY A 231 8414 6460 7656 401 -431 657 O ATOM 1574 N ASP A 232 42.469 76.876-397.434 1.00 55.10 N ANISOU 1574 N ASP A 232 7994 5980 6961 594 -661 526 N ATOM 1575 CA ASP A 232 42.169 78.090-398.165 1.00 54.61 C ANISOU 1575 CA ASP A 232 7901 5804 7046 580 -774 516 C ATOM 1576 C ASP A 232 40.816 78.008-398.849 1.00 56.09 C ANISOU 1576 C ASP A 232 8111 5759 7443 478 -766 642 C ATOM 1577 O ASP A 232 40.265 79.028-399.263 1.00 57.65 O ANISOU 1577 O ASP A 232 8248 5853 7804 433 -837 630 O ATOM 1578 CB ASP A 232 43.254 78.366-399.202 1.00 55.79 C ANISOU 1578 CB ASP A 232 8110 5987 7102 745 -980 403 C ATOM 1579 CG ASP A 232 44.578 78.737-398.569 1.00 55.08 C ANISOU 1579 CG ASP A 232 7944 6163 6820 841 -989 296 C ATOM 1580 OD1 ASP A 232 44.617 78.878-397.327 1.00 53.50 O ANISOU 1580 OD1 ASP A 232 7646 6076 6605 750 -842 312 O ATOM 1581 OD2 ASP A 232 45.572 78.892-399.309 1.00 55.33 O ANISOU 1581 OD2 ASP A 232 8010 6293 6721 1010 -1149 200 O ATOM 1582 N LYS A 233 40.279 76.800-398.972 1.00 61.97 N ANISOU 1582 N LYS A 233 8926 6436 8182 450 -677 767 N ATOM 1583 CA LYS A 233 39.005 76.607-399.656 1.00 65.44 C ANISOU 1583 CA LYS A 233 9371 6665 8830 339 -648 932 C ATOM 1584 C LYS A 233 37.799 76.877-398.751 1.00 64.15 C ANISOU 1584 C LYS A 233 9079 6536 8758 208 -479 1029 C ATOM 1585 O LYS A 233 36.667 76.938-399.220 1.00 67.72 O ANISOU 1585 O LYS A 233 9482 6850 9398 95 -446 1166 O ATOM 1586 CB LYS A 233 38.936 75.206-400.267 1.00 65.37 C ANISOU 1586 CB LYS A 233 9493 6577 8769 392 -614 1067 C ATOM 1587 CG LYS A 233 39.825 75.027-401.491 1.00 66.71 C ANISOU 1587 CG LYS A 233 9810 6630 8907 515 -815 996 C ATOM 1588 CD LYS A 233 40.044 73.557-401.830 1.00 70.94 C ANISOU 1588 CD LYS A 233 10497 7158 9300 628 -759 1103 C ATOM 1589 CE LYS A 233 38.757 72.869-402.273 1.00 71.16 C ANISOU 1589 CE LYS A 233 10539 6995 9503 519 -634 1379 C ATOM 1590 NZ LYS A 233 38.892 71.379-402.363 1.00 72.61 N ANISOU 1590 NZ LYS A 233 10855 7228 9504 664 -525 1513 N ATOM 1591 N ILE A 234 38.051 77.056-397.458 1.00 63.16 N ANISOU 1591 N ILE A 234 8896 6596 8507 224 -382 957 N ATOM 1592 CA ILE A 234 36.992 77.361-396.504 1.00 60.95 C ANISOU 1592 CA ILE A 234 8512 6368 8278 139 -242 1018 C ATOM 1593 C ILE A 234 36.624 78.847-396.497 1.00 60.85 C ANISOU 1593 C ILE A 234 8404 6317 8400 80 -296 953 C ATOM 1594 O ILE A 234 37.484 79.712-396.636 1.00 61.56 O ANISOU 1594 O ILE A 234 8492 6430 8469 139 -406 823 O ATOM 1595 CB ILE A 234 37.387 76.950-395.080 1.00 59.62 C ANISOU 1595 CB ILE A 234 8334 6378 7939 192 -141 950 C ATOM 1596 CG1 ILE A 234 37.649 75.448-395.005 1.00 62.49 C ANISOU 1596 CG1 ILE A 234 8776 6814 8154 288 -87 991 C ATOM 1597 CG2 ILE A 234 36.297 77.321-394.101 1.00 55.09 C ANISOU 1597 CG2 ILE A 234 7674 5851 7405 136 -24 995 C ATOM 1598 CD1 ILE A 234 37.882 74.947-393.588 1.00 62.69 C ANISOU 1598 CD1 ILE A 234 8778 7003 8039 348 -8 903 C ATOM 1599 N GLU A 235 35.337 79.130-396.324 1.00 56.07 N ANISOU 1599 N GLU A 235 7707 5685 7911 -10 -214 1045 N ATOM 1600 CA GLU A 235 34.833 80.502-396.302 1.00 55.74 C ANISOU 1600 CA GLU A 235 7565 5626 7986 -45 -256 977 C ATOM 1601 C GLU A 235 33.709 80.648-395.290 1.00 59.28 C ANISOU 1601 C GLU A 235 7928 6172 8424 -87 -107 1039 C ATOM 1602 O GLU A 235 32.578 80.242-395.547 1.00 58.55 O ANISOU 1602 O GLU A 235 7768 6060 8418 -164 -36 1175 O ATOM 1603 CB GLU A 235 34.313 80.908-397.684 1.00 59.66 C ANISOU 1603 CB GLU A 235 8018 5944 8707 -111 -387 996 C ATOM 1604 CG GLU A 235 33.944 82.386-397.804 1.00 58.98 C ANISOU 1604 CG GLU A 235 7823 5854 8733 -102 -472 873 C ATOM 1605 CD GLU A 235 32.712 82.620-398.661 1.00 71.22 C ANISOU 1605 CD GLU A 235 9255 7270 10535 -229 -514 935 C ATOM 1606 OE1 GLU A 235 31.611 82.171-398.263 1.00 71.28 O ANISOU 1606 OE1 GLU A 235 9183 7323 10576 -332 -363 1083 O ATOM 1607 OE2 GLU A 235 32.840 83.269-399.722 1.00 73.77 O ANISOU 1607 OE2 GLU A 235 9552 7453 11024 -218 -708 827 O ATOM 1608 N ILE A 236 34.017 81.240-394.147 1.00 58.61 N ANISOU 1608 N ILE A 236 7843 6195 8232 -30 -61 948 N ATOM 1609 CA ILE A 236 33.022 81.426-393.103 1.00 60.82 C ANISOU 1609 CA ILE A 236 8067 6570 8473 -33 58 979 C ATOM 1610 C ILE A 236 32.093 82.603-393.394 1.00 62.11 C ANISOU 1610 C ILE A 236 8119 6724 8755 -59 36 956 C ATOM 1611 O ILE A 236 32.539 83.656-393.844 1.00 65.45 O ANISOU 1611 O ILE A 236 8524 7106 9237 -22 -67 851 O ATOM 1612 CB ILE A 236 33.689 81.657-391.737 1.00 62.85 C ANISOU 1612 CB ILE A 236 8379 6905 8595 37 101 889 C ATOM 1613 CG1 ILE A 236 34.630 80.501-391.392 1.00 67.57 C ANISOU 1613 CG1 ILE A 236 9060 7529 9085 66 108 875 C ATOM 1614 CG2 ILE A 236 32.642 81.821-390.656 1.00 58.03 C ANISOU 1614 CG2 ILE A 236 7736 6378 7934 64 200 907 C ATOM 1615 CD1 ILE A 236 35.988 80.598-392.050 1.00 61.98 C ANISOU 1615 CD1 ILE A 236 8395 6788 8368 82 5 808 C ATOM 1616 N GLU A 237 30.802 82.418-393.141 1.00 56.34 N ANISOU 1616 N GLU A 237 7302 6061 8044 -97 129 1048 N ATOM 1617 CA GLU A 237 29.845 83.515-393.205 1.00 56.34 C ANISOU 1617 CA GLU A 237 7181 6100 8125 -104 122 1006 C ATOM 1618 C GLU A 237 29.310 83.770-391.803 1.00 56.60 C ANISOU 1618 C GLU A 237 7222 6281 8002 -14 228 982 C ATOM 1619 O GLU A 237 28.770 82.864-391.174 1.00 60.67 O ANISOU 1619 O GLU A 237 7744 6891 8417 3 325 1074 O ATOM 1620 CB GLU A 237 28.699 83.182-394.162 1.00 62.24 C ANISOU 1620 CB GLU A 237 7788 6818 9042 -229 133 1134 C ATOM 1621 CG GLU A 237 27.690 84.315-394.344 1.00 59.98 C ANISOU 1621 CG GLU A 237 7342 6586 8860 -244 107 1067 C ATOM 1622 CD GLU A 237 26.646 84.021-395.417 1.00 63.12 C ANISOU 1622 CD GLU A 237 7570 6930 9483 -408 99 1195 C ATOM 1623 OE1 GLU A 237 26.720 84.622-396.511 1.00 67.76 O ANISOU 1623 OE1 GLU A 237 8091 7367 10289 -477 -51 1113 O ATOM 1624 OE2 GLU A 237 25.749 83.187-395.168 1.00 68.25 O ANISOU 1624 OE2 GLU A 237 8144 7690 10099 -462 237 1382 O ATOM 1625 N ILE A 238 29.473 84.995-391.310 1.00 55.16 N ANISOU 1625 N ILE A 238 7050 6124 7786 74 201 859 N ATOM 1626 CA ILE A 238 29.021 85.340-389.964 1.00 55.50 C ANISOU 1626 CA ILE A 238 7131 6274 7682 178 283 826 C ATOM 1627 C ILE A 238 27.936 86.408-389.961 1.00 55.84 C ANISOU 1627 C ILE A 238 7063 6415 7737 235 291 773 C ATOM 1628 O ILE A 238 28.090 87.464-390.570 1.00 55.75 O ANISOU 1628 O ILE A 238 7000 6376 7806 266 214 681 O ATOM 1629 CB ILE A 238 30.177 85.830-389.085 1.00 56.02 C ANISOU 1629 CB ILE A 238 7329 6289 7667 258 274 746 C ATOM 1630 CG1 ILE A 238 31.300 84.800-389.059 1.00 53.57 C ANISOU 1630 CG1 ILE A 238 7105 5907 7342 204 258 773 C ATOM 1631 CG2 ILE A 238 29.693 86.094-387.670 1.00 56.13 C ANISOU 1631 CG2 ILE A 238 7408 6367 7552 362 344 718 C ATOM 1632 CD1 ILE A 238 32.503 85.237-388.251 1.00 52.89 C ANISOU 1632 CD1 ILE A 238 7114 5772 7209 247 252 716 C ATOM 1633 N VAL A 239 26.840 86.128-389.266 1.00 58.02 N ANISOU 1633 N VAL A 239 7298 6833 7913 278 374 816 N ATOM 1634 CA VAL A 239 25.757 87.088-389.123 1.00 58.30 C ANISOU 1634 CA VAL A 239 7227 7005 7919 358 389 755 C ATOM 1635 C VAL A 239 25.290 87.130-387.669 1.00 56.90 C ANISOU 1635 C VAL A 239 7142 6946 7531 516 458 728 C ATOM 1636 O VAL A 239 25.120 86.085-387.038 1.00 56.92 O ANISOU 1636 O VAL A 239 7195 6999 7434 533 506 799 O ATOM 1637 CB VAL A 239 24.575 86.747-390.051 1.00 61.80 C ANISOU 1637 CB VAL A 239 7458 7545 8480 242 405 847 C ATOM 1638 CG1 VAL A 239 23.379 87.632-389.745 1.00 65.08 C ANISOU 1638 CG1 VAL A 239 7745 8154 8829 339 429 775 C ATOM 1639 CG2 VAL A 239 24.984 86.898-391.505 1.00 60.31 C ANISOU 1639 CG2 VAL A 239 7185 7196 8534 96 300 841 C ATOM 1640 N SER A 240 25.094 88.340-387.143 1.00 58.60 N ANISOU 1640 N SER A 240 7388 7207 7669 659 451 616 N ATOM 1641 CA SER A 240 24.707 88.536-385.745 1.00 60.44 C ANISOU 1641 CA SER A 240 7743 7517 7706 834 494 572 C ATOM 1642 C SER A 240 23.201 88.651-385.596 1.00 60.64 C ANISOU 1642 C SER A 240 7634 7787 7618 926 533 565 C ATOM 1643 O SER A 240 22.487 88.780-386.587 1.00 61.39 O ANISOU 1643 O SER A 240 7525 7987 7813 840 530 588 O ATOM 1644 CB SER A 240 25.353 89.799-385.186 1.00 57.61 C ANISOU 1644 CB SER A 240 7513 7070 7305 968 479 476 C ATOM 1645 OG SER A 240 24.992 90.929-385.960 1.00 56.33 O ANISOU 1645 OG SER A 240 7227 6985 7189 1024 450 398 O ATOM 1646 N LYS A 241 22.720 88.619-384.357 1.00 58.78 N ANISOU 1646 N LYS A 241 7507 7644 7181 1105 557 527 N ATOM 1647 CA LYS A 241 21.293 88.769-384.114 1.00 60.17 C ANISOU 1647 CA LYS A 241 7560 8098 7202 1235 590 510 C ATOM 1648 C LYS A 241 20.813 90.060-384.754 1.00 66.81 C ANISOU 1648 C LYS A 241 8268 9029 8087 1272 575 414 C ATOM 1649 O LYS A 241 19.624 90.232-385.033 1.00 65.72 O ANISOU 1649 O LYS A 241 7938 9140 7894 1310 597 404 O ATOM 1650 CB LYS A 241 20.982 88.779-382.616 1.00 66.63 C ANISOU 1650 CB LYS A 241 8562 8975 7781 1475 583 439 C ATOM 1651 CG LYS A 241 19.480 88.821-382.301 1.00 73.40 C ANISOU 1651 CG LYS A 241 9292 10171 8427 1650 610 420 C ATOM 1652 CD LYS A 241 19.216 89.267-380.862 1.00 62.28 C ANISOU 1652 CD LYS A 241 8097 8790 6776 1937 572 298 C ATOM 1653 CE LYS A 241 17.727 89.482-380.588 1.00 70.01 C ANISOU 1653 CE LYS A 241 8944 10144 7513 2149 590 255 C ATOM 1654 NZ LYS A 241 17.169 90.612-381.375 1.00 66.45 N ANISOU 1654 NZ LYS A 241 8312 9836 7100 2140 616 195 N ATOM 1655 N ALA A 242 21.755 90.968-384.982 1.00 84.82 N ANISOU 1655 N ALA A 242 10637 11132 10460 1277 534 339 N ATOM 1656 CA ALA A 242 21.457 92.264-385.576 1.00 84.49 C ANISOU 1656 CA ALA A 242 10482 11169 10450 1361 500 215 C ATOM 1657 C ALA A 242 21.062 92.131-387.043 1.00 81.44 C ANISOU 1657 C ALA A 242 9831 10828 10285 1167 455 228 C ATOM 1658 O ALA A 242 19.897 92.302-387.398 1.00 81.92 O ANISOU 1658 O ALA A 242 9681 11103 10340 1170 461 197 O ATOM 1659 CB ALA A 242 22.664 93.197-385.433 1.00 86.77 C ANISOU 1659 CB ALA A 242 10935 11272 10763 1451 472 156 C ATOM 1660 N ASP A 243 22.039 91.816-387.888 1.00 94.75 N ANISOU 1660 N ASP A 243 11523 12306 12172 998 403 273 N ATOM 1661 CA ASP A 243 21.816 91.734-389.327 1.00 96.55 C ANISOU 1661 CA ASP A 243 11531 12504 12648 812 329 274 C ATOM 1662 C ASP A 243 21.109 90.436-389.714 1.00 95.61 C ANISOU 1662 C ASP A 243 11277 12437 12614 607 386 456 C ATOM 1663 O ASP A 243 21.057 90.084-390.892 1.00 94.03 O ANISOU 1663 O ASP A 243 10927 12146 12654 407 333 513 O ATOM 1664 CB ASP A 243 23.140 91.856-390.096 1.00 95.96 C ANISOU 1664 CB ASP A 243 11531 12193 12736 740 234 251 C ATOM 1665 CG ASP A 243 23.888 93.151-389.793 1.00 99.76 C ANISOU 1665 CG ASP A 243 12123 12654 13128 965 190 104 C ATOM 1666 OD1 ASP A 243 24.152 93.928-390.739 1.00102.92 O ANISOU 1666 OD1 ASP A 243 12425 13027 13653 1006 72 -22 O ATOM 1667 OD2 ASP A 243 24.223 93.391-388.614 1.00 95.72 O ANISOU 1667 OD2 ASP A 243 11795 12150 12424 1116 267 120 O ATOM 1668 N TYR A 244 20.568 89.725-388.729 1.00 61.95 N ANISOU 1668 N TYR A 244 7067 8319 8152 676 487 551 N ATOM 1669 CA TYR A 244 19.896 88.460-389.006 1.00 64.66 C ANISOU 1669 CA TYR A 244 7280 8757 8529 534 563 752 C ATOM 1670 C TYR A 244 18.456 88.649-389.462 1.00 65.51 C ANISOU 1670 C TYR A 244 7095 9122 8672 491 598 785 C ATOM 1671 O TYR A 244 17.969 87.909-390.315 1.00 67.94 O ANISOU 1671 O TYR A 244 7212 9449 9152 290 634 958 O ATOM 1672 CB TYR A 244 19.926 87.550-387.784 1.00 68.73 C ANISOU 1672 CB TYR A 244 7960 9351 8803 664 639 831 C ATOM 1673 CG TYR A 244 19.145 86.262-387.958 1.00 69.16 C ANISOU 1673 CG TYR A 244 7872 9575 8830 592 732 1046 C ATOM 1674 CD1 TYR A 244 19.639 85.223-388.734 1.00 70.31 C ANISOU 1674 CD1 TYR A 244 8003 9577 9135 410 752 1214 C ATOM 1675 CD2 TYR A 244 17.918 86.080-387.335 1.00 69.64 C ANISOU 1675 CD2 TYR A 244 7815 9963 8681 738 805 1092 C ATOM 1676 CE1 TYR A 244 18.931 84.045-388.890 1.00 71.63 C ANISOU 1676 CE1 TYR A 244 8041 9914 9260 375 856 1441 C ATOM 1677 CE2 TYR A 244 17.209 84.908-387.485 1.00 74.09 C ANISOU 1677 CE2 TYR A 244 8233 10722 9194 706 904 1316 C ATOM 1678 CZ TYR A 244 17.719 83.894-388.263 1.00 72.66 C ANISOU 1678 CZ TYR A 244 8039 10387 9181 525 937 1500 C ATOM 1679 OH TYR A 244 17.012 82.726-388.416 1.00 75.23 O ANISOU 1679 OH TYR A 244 8219 10923 9443 521 1055 1752 O ATOM 1680 N ALA A 245 17.772 89.626-388.874 1.00 72.93 N ANISOU 1680 N ALA A 245 7997 10267 9447 685 594 631 N ATOM 1681 CA ALA A 245 16.413 89.958-389.287 1.00 75.78 C ANISOU 1681 CA ALA A 245 8054 10906 9832 660 616 626 C ATOM 1682 C ALA A 245 16.440 90.518-390.704 1.00 74.14 C ANISOU 1682 C ALA A 245 7639 10562 9970 453 513 557 C ATOM 1683 O ALA A 245 15.648 90.133-391.562 1.00 71.58 O ANISOU 1683 O ALA A 245 7038 10312 9849 244 531 678 O ATOM 1684 CB ALA A 245 15.797 90.960-388.329 1.00 78.31 C ANISOU 1684 CB ALA A 245 8409 11470 9874 953 617 439 C ATOM 1685 N LYS A 246 17.366 91.433-390.941 1.00116.78 N ANISOU 1685 N LYS A 246 13168 15760 15442 523 396 365 N ATOM 1686 CA LYS A 246 17.620 91.915-392.283 1.00119.07 C ANISOU 1686 CA LYS A 246 13308 15873 16061 362 255 268 C ATOM 1687 C LYS A 246 18.357 90.835-393.057 1.00117.50 C ANISOU 1687 C LYS A 246 13162 15396 16087 115 240 456 C ATOM 1688 O LYS A 246 18.873 91.084-394.139 1.00113.22 O ANISOU 1688 O LYS A 246 12574 14632 15813 -6 100 383 O ATOM 1689 CB LYS A 246 18.458 93.189-392.237 1.00114.40 C ANISOU 1689 CB LYS A 246 12853 15189 15426 576 136 13 C ATOM 1690 CG LYS A 246 17.647 94.450-391.995 1.00120.30 C ANISOU 1690 CG LYS A 246 13467 16190 16051 800 101 -217 C ATOM 1691 CD LYS A 246 18.535 95.682-392.039 1.00129.58 C ANISOU 1691 CD LYS A 246 14773 17280 17181 1041 -11 -447 C ATOM 1692 CE LYS A 246 17.772 96.906-392.521 1.00133.02 C ANISOU 1692 CE LYS A 246 14975 17910 17655 1193 -121 -717 C ATOM 1693 NZ LYS A 246 16.538 97.157-391.730 1.00127.27 N ANISOU 1693 NZ LYS A 246 14144 17518 16694 1332 -21 -751 N ATOM 1694 N GLY A 247 18.395 89.633-392.488 1.00143.01 N ANISOU 1694 N GLY A 247 16497 18650 19192 72 372 682 N ATOM 1695 CA GLY A 247 19.136 88.517-393.047 1.00140.56 C ANISOU 1695 CA GLY A 247 16276 18105 19027 -110 379 867 C ATOM 1696 C GLY A 247 19.091 88.413-394.556 1.00139.27 C ANISOU 1696 C GLY A 247 15938 17737 19242 -365 274 910 C ATOM 1697 O GLY A 247 20.026 87.909-395.178 1.00138.48 O ANISOU 1697 O GLY A 247 15961 17374 19281 -466 209 963 O ATOM 1698 N ALA A 248 18.005 88.884-395.153 1.00 76.64 N ANISOU 1698 N ALA A 248 7714 9920 11486 -469 245 879 N ATOM 1699 CA ALA A 248 17.878 88.830-396.601 1.00 77.34 C ANISOU 1699 CA ALA A 248 7618 9784 11985 -731 120 907 C ATOM 1700 C ALA A 248 18.551 90.028-397.268 1.00 74.59 C ANISOU 1700 C ALA A 248 7293 9253 11795 -655 -116 587 C ATOM 1701 O ALA A 248 19.298 89.880-398.239 1.00 76.27 O ANISOU 1701 O ALA A 248 7564 9165 12251 -766 -264 563 O ATOM 1702 CB ALA A 248 16.402 88.766-396.992 1.00 78.94 C ANISOU 1702 CB ALA A 248 7460 10185 12349 -905 185 1023 C ATOM 1703 N SER A 249 18.291 91.215-396.726 1.00 90.42 N ANISOU 1703 N SER A 249 9261 11459 13637 -428 -156 336 N ATOM 1704 CA SER A 249 18.801 92.454-397.299 1.00 92.57 C ANISOU 1704 CA SER A 249 9523 11633 14018 -289 -376 15 C ATOM 1705 C SER A 249 20.247 92.703-396.895 1.00 91.60 C ANISOU 1705 C SER A 249 9714 11382 13706 -78 -418 -68 C ATOM 1706 O SER A 249 21.070 93.084-397.725 1.00 92.63 O ANISOU 1706 O SER A 249 9890 11308 13997 -52 -607 -211 O ATOM 1707 CB SER A 249 17.930 93.628-396.856 1.00 94.79 C ANISOU 1707 CB SER A 249 9636 12213 14167 -89 -387 -215 C ATOM 1708 OG SER A 249 16.552 93.294-396.932 1.00109.02 O ANISOU 1708 OG SER A 249 11149 14216 16056 -261 -295 -99 O ATOM 1709 N ALA A 250 20.546 92.489-395.617 1.00104.88 N ANISOU 1709 N ALA A 250 11602 13193 15053 77 -251 20 N ATOM 1710 CA ALA A 250 21.882 92.729-395.074 1.00101.72 C ANISOU 1710 CA ALA A 250 11482 12702 14466 266 -261 -28 C ATOM 1711 C ALA A 250 22.980 92.331-396.051 1.00 95.06 C ANISOU 1711 C ALA A 250 10723 11579 13815 162 -398 -16 C ATOM 1712 O ALA A 250 23.129 91.157-396.390 1.00 93.90 O ANISOU 1712 O ALA A 250 10614 11290 13774 -46 -357 184 O ATOM 1713 CB ALA A 250 22.062 91.995-393.753 1.00104.78 C ANISOU 1713 CB ALA A 250 12067 13168 14575 315 -67 148 C ATOM 1714 N LEU A 251 23.745 93.321-396.496 1.00 66.41 N ANISOU 1714 N LEU A 251 7129 7896 10206 344 -564 -231 N ATOM 1715 CA LEU A 251 24.795 93.092-397.478 1.00 68.05 C ANISOU 1715 CA LEU A 251 7412 7870 10575 303 -732 -263 C ATOM 1716 C LEU A 251 26.156 92.848-396.833 1.00 67.29 C ANISOU 1716 C LEU A 251 7572 7741 10255 426 -669 -190 C ATOM 1717 O LEU A 251 26.980 93.756-396.759 1.00 69.98 O ANISOU 1717 O LEU A 251 7982 8129 10479 668 -747 -333 O ATOM 1718 CB LEU A 251 24.880 94.274-398.442 1.00 67.99 C ANISOU 1718 CB LEU A 251 7274 7839 10721 460 -984 -557 C ATOM 1719 CG LEU A 251 23.804 94.321-399.522 1.00 70.17 C ANISOU 1719 CG LEU A 251 7281 8032 11347 266 -1130 -646 C ATOM 1720 CD1 LEU A 251 23.968 95.560-400.383 1.00 70.84 C ANISOU 1720 CD1 LEU A 251 7246 8108 11563 480 -1409 -991 C ATOM 1721 CD2 LEU A 251 23.871 93.061-400.369 1.00 72.41 C ANISOU 1721 CD2 LEU A 251 7574 8039 11898 -53 -1162 -446 C ATOM 1722 N LEU A 252 26.390 91.619-396.382 1.00 63.09 N ANISOU 1722 N LEU A 252 7161 7146 9664 269 -528 35 N ATOM 1723 CA LEU A 252 27.654 91.250-395.750 1.00 59.82 C ANISOU 1723 CA LEU A 252 6965 6702 9063 347 -466 109 C ATOM 1724 C LEU A 252 28.857 91.652-396.602 1.00 60.14 C ANISOU 1724 C LEU A 252 7062 6636 9153 458 -653 -11 C ATOM 1725 O LEU A 252 28.861 91.430-397.811 1.00 60.77 O ANISOU 1725 O LEU A 252 7076 6560 9452 366 -822 -61 O ATOM 1726 CB LEU A 252 27.684 89.747-395.479 1.00 62.09 C ANISOU 1726 CB LEU A 252 7337 6916 9340 153 -341 333 C ATOM 1727 CG LEU A 252 26.506 89.202-394.677 1.00 61.30 C ANISOU 1727 CG LEU A 252 7176 6948 9168 72 -167 465 C ATOM 1728 CD1 LEU A 252 26.719 87.733-394.380 1.00 60.11 C ANISOU 1728 CD1 LEU A 252 7124 6749 8966 -49 -56 668 C ATOM 1729 CD2 LEU A 252 26.325 89.984-393.392 1.00 58.72 C ANISOU 1729 CD2 LEU A 252 6904 6797 8611 262 -69 397 C ATOM 1730 N PRO A 253 29.878 92.255-395.971 1.00 68.03 N ANISOU 1730 N PRO A 253 8177 7722 9948 666 -627 -50 N ATOM 1731 CA PRO A 253 31.112 92.662-396.635 1.00 65.47 C ANISOU 1731 CA PRO A 253 7905 7366 9606 823 -785 -147 C ATOM 1732 C PRO A 253 32.062 91.491-396.633 1.00 63.97 C ANISOU 1732 C PRO A 253 7851 7074 9379 701 -752 -5 C ATOM 1733 O PRO A 253 31.901 90.604-395.808 1.00 64.84 O ANISOU 1733 O PRO A 253 8033 7180 9423 559 -581 153 O ATOM 1734 CB PRO A 253 31.669 93.745-395.708 1.00 66.87 C ANISOU 1734 CB PRO A 253 8132 7726 9551 1087 -703 -183 C ATOM 1735 CG PRO A 253 30.720 93.828-394.534 1.00 66.21 C ANISOU 1735 CG PRO A 253 8052 7728 9375 1052 -510 -109 C ATOM 1736 CD PRO A 253 29.909 92.586-394.543 1.00 61.66 C ANISOU 1736 CD PRO A 253 7459 7056 8914 773 -441 13 C ATOM 1737 N ILE A 254 33.046 91.489-397.517 1.00 57.89 N ANISOU 1737 N ILE A 254 7118 6244 8634 784 -922 -77 N ATOM 1738 CA ILE A 254 33.975 90.371-397.582 1.00 56.96 C ANISOU 1738 CA ILE A 254 7127 6051 8466 690 -904 37 C ATOM 1739 C ILE A 254 35.395 90.772-397.185 1.00 57.09 C ANISOU 1739 C ILE A 254 7217 6204 8270 886 -901 27 C ATOM 1740 O ILE A 254 36.031 91.589-397.855 1.00 56.48 O ANISOU 1740 O ILE A 254 7108 6193 8159 1106 -1068 -107 O ATOM 1741 CB ILE A 254 33.980 89.739-398.979 1.00 60.17 C ANISOU 1741 CB ILE A 254 7532 6258 9070 598 -1100 -3 C ATOM 1742 CG1 ILE A 254 32.602 89.153-399.287 1.00 61.07 C ANISOU 1742 CG1 ILE A 254 7562 6235 9407 357 -1058 80 C ATOM 1743 CG2 ILE A 254 35.066 88.680-399.079 1.00 57.78 C ANISOU 1743 CG2 ILE A 254 7372 5912 8670 565 -1096 88 C ATOM 1744 CD1 ILE A 254 32.407 88.770-400.736 1.00 63.04 C ANISOU 1744 CD1 ILE A 254 7785 6248 9921 257 -1269 37 C ATOM 1745 N TYR A 255 35.881 90.196-396.086 1.00 55.85 N ANISOU 1745 N TYR A 255 7145 6101 7974 815 -717 168 N ATOM 1746 CA TYR A 255 37.239 90.443-395.615 1.00 60.96 C ANISOU 1746 CA TYR A 255 7840 6880 8441 950 -685 199 C ATOM 1747 C TYR A 255 38.153 89.322-396.086 1.00 57.57 C ANISOU 1747 C TYR A 255 7486 6402 7986 877 -745 233 C ATOM 1748 O TYR A 255 37.762 88.164-396.068 1.00 60.26 O ANISOU 1748 O TYR A 255 7878 6626 8391 689 -695 303 O ATOM 1749 CB TYR A 255 37.277 90.497-394.088 1.00 58.03 C ANISOU 1749 CB TYR A 255 7508 6576 7965 903 -464 321 C ATOM 1750 CG TYR A 255 36.289 91.448-393.457 1.00 57.46 C ANISOU 1750 CG TYR A 255 7393 6545 7893 971 -379 304 C ATOM 1751 CD1 TYR A 255 36.704 92.658-392.921 1.00 54.27 C ANISOU 1751 CD1 TYR A 255 6973 6277 7371 1182 -327 308 C ATOM 1752 CD2 TYR A 255 34.946 91.132-393.386 1.00 58.38 C ANISOU 1752 CD2 TYR A 255 7484 6587 8111 844 -343 297 C ATOM 1753 CE1 TYR A 255 35.802 93.531-392.336 1.00 56.64 C ANISOU 1753 CE1 TYR A 255 7251 6622 7648 1274 -250 286 C ATOM 1754 CE2 TYR A 255 34.039 91.993-392.807 1.00 53.85 C ANISOU 1754 CE2 TYR A 255 6870 6078 7511 927 -272 267 C ATOM 1755 CZ TYR A 255 34.471 93.192-392.283 1.00 53.94 C ANISOU 1755 CZ TYR A 255 6886 6209 7398 1148 -230 251 C ATOM 1756 OH TYR A 255 33.564 94.053-391.704 1.00 61.35 O ANISOU 1756 OH TYR A 255 7803 7219 8290 1261 -160 214 O ATOM 1757 N PRO A 256 39.378 89.657-396.504 1.00 54.42 N ANISOU 1757 N PRO A 256 7089 6121 7468 1055 -849 185 N ATOM 1758 CA PRO A 256 39.926 91.004-396.637 1.00 55.84 C ANISOU 1758 CA PRO A 256 7196 6479 7541 1331 -918 112 C ATOM 1759 C PRO A 256 39.786 91.497-398.066 1.00 58.37 C ANISOU 1759 C PRO A 256 7475 6761 7943 1503 -1187 -75 C ATOM 1760 O PRO A 256 40.052 92.663-398.348 1.00 56.90 O ANISOU 1760 O PRO A 256 7214 6725 7679 1779 -1284 -177 O ATOM 1761 CB PRO A 256 41.417 90.807-396.333 1.00 55.35 C ANISOU 1761 CB PRO A 256 7150 6588 7294 1415 -884 185 C ATOM 1762 CG PRO A 256 41.598 89.333-396.067 1.00 54.30 C ANISOU 1762 CG PRO A 256 7101 6347 7184 1175 -815 261 C ATOM 1763 CD PRO A 256 40.430 88.652-396.675 1.00 54.61 C ANISOU 1763 CD PRO A 256 7183 6164 7404 1016 -873 222 C ATOM 1764 N GLY A 257 39.389 90.604-398.962 1.00 61.13 N ANISOU 1764 N GLY A 257 7872 6904 8450 1358 -1313 -119 N ATOM 1765 CA GLY A 257 39.248 90.957-400.359 1.00 58.43 C ANISOU 1765 CA GLY A 257 7504 6463 8233 1491 -1600 -306 C ATOM 1766 C GLY A 257 38.570 92.299-400.538 1.00 58.89 C ANISOU 1766 C GLY A 257 7439 6583 8354 1669 -1686 -456 C ATOM 1767 O GLY A 257 39.191 93.261-400.982 1.00 62.83 O ANISOU 1767 O GLY A 257 7887 7244 8743 1987 -1846 -599 O ATOM 1768 N GLY A 258 37.294 92.364-400.183 1.00 61.75 N ANISOU 1768 N GLY A 258 7744 6848 8872 1492 -1582 -431 N ATOM 1769 CA GLY A 258 36.511 93.567-400.379 1.00 61.12 C ANISOU 1769 CA GLY A 258 7533 6823 8865 1647 -1668 -595 C ATOM 1770 C GLY A 258 35.146 93.219-400.935 1.00 60.82 C ANISOU 1770 C GLY A 258 7422 6562 9125 1406 -1728 -639 C ATOM 1771 O GLY A 258 34.766 92.053-400.967 1.00 61.62 O ANISOU 1771 O GLY A 258 7579 6489 9346 1118 -1647 -492 O ATOM 1772 N GLY A 259 34.401 94.228-401.369 1.00 76.25 N ANISOU 1772 N GLY A 259 9236 8540 11195 1534 -1866 -836 N ATOM 1773 CA GLY A 259 33.078 94.003-401.920 1.00 81.27 C ANISOU 1773 CA GLY A 259 9757 8986 12137 1300 -1929 -884 C ATOM 1774 C GLY A 259 32.130 93.355-400.931 1.00 75.94 C ANISOU 1774 C GLY A 259 9073 8313 11466 1024 -1640 -666 C ATOM 1775 O GLY A 259 32.525 92.958-399.835 1.00 73.42 O ANISOU 1775 O GLY A 259 8861 8102 10934 996 -1408 -487 O ATOM 1776 N THR A 260 30.866 93.245-401.317 1.00 65.22 N ANISOU 1776 N THR A 260 7575 6846 10359 825 -1664 -686 N ATOM 1777 CA THR A 260 29.869 92.668-400.431 1.00 66.79 C ANISOU 1777 CA THR A 260 7740 7090 10547 599 -1405 -489 C ATOM 1778 C THR A 260 29.084 91.570-401.121 1.00 69.20 C ANISOU 1778 C THR A 260 7988 7173 11132 270 -1410 -346 C ATOM 1779 O THR A 260 29.330 91.253-402.282 1.00 75.14 O ANISOU 1779 O THR A 260 8744 7698 12106 200 -1616 -397 O ATOM 1780 CB THR A 260 28.878 93.716-399.949 1.00 72.04 C ANISOU 1780 CB THR A 260 8248 7940 11185 703 -1358 -612 C ATOM 1781 OG1 THR A 260 28.115 94.187-401.065 1.00 80.07 O ANISOU 1781 OG1 THR A 260 9069 8854 12499 661 -1584 -807 O ATOM 1782 CG2 THR A 260 29.614 94.879-399.301 1.00 74.56 C ANISOU 1782 CG2 THR A 260 8622 8479 11227 1060 -1345 -734 C ATOM 1783 N ARG A 261 28.129 91.001-400.396 1.00 71.72 N ANISOU 1783 N ARG A 261 8253 7563 11433 86 -1184 -159 N ATOM 1784 CA ARG A 261 27.338 89.889-400.897 1.00 66.48 C ANISOU 1784 CA ARG A 261 7525 6738 10997 -217 -1129 44 C ATOM 1785 C ARG A 261 26.149 89.667-399.982 1.00 66.58 C ANISOU 1785 C ARG A 261 7424 6937 10936 -322 -893 192 C ATOM 1786 O ARG A 261 26.306 89.520-398.773 1.00 64.64 O ANISOU 1786 O ARG A 261 7281 6871 10410 -230 -704 272 O ATOM 1787 CB ARG A 261 28.188 88.620-400.956 1.00 67.29 C ANISOU 1787 CB ARG A 261 7825 6710 11032 -297 -1068 238 C ATOM 1788 CG ARG A 261 27.532 87.455-401.677 1.00 67.61 C ANISOU 1788 CG ARG A 261 7821 6552 11317 -574 -1034 463 C ATOM 1789 CD ARG A 261 28.389 86.200-401.577 1.00 70.44 C ANISOU 1789 CD ARG A 261 8390 6833 11541 -596 -948 647 C ATOM 1790 NE ARG A 261 28.192 85.498-400.311 1.00 66.04 N ANISOU 1790 NE ARG A 261 7884 6482 10728 -596 -677 827 N ATOM 1791 CZ ARG A 261 29.063 84.636-399.791 1.00 68.16 C ANISOU 1791 CZ ARG A 261 8333 6784 10782 -534 -585 918 C ATOM 1792 NH1 ARG A 261 30.203 84.379-400.422 1.00 69.05 N ANISOU 1792 NH1 ARG A 261 8593 6760 10883 -466 -725 858 N ATOM 1793 NH2 ARG A 261 28.799 84.039-398.634 1.00 62.86 N ANISOU 1793 NH2 ARG A 261 7690 6295 9900 -520 -369 1048 N ATOM 1794 N ALA A 262 24.957 89.648-400.565 1.00 71.49 N ANISOU 1794 N ALA A 262 7825 7520 11819 -511 -915 225 N ATOM 1795 CA ALA A 262 23.737 89.460-399.794 1.00 71.00 C ANISOU 1795 CA ALA A 262 7618 7674 11684 -597 -705 363 C ATOM 1796 C ALA A 262 23.885 88.320-398.799 1.00 68.83 C ANISOU 1796 C ALA A 262 7496 7497 11159 -618 -462 622 C ATOM 1797 O ALA A 262 24.390 87.253-399.140 1.00 76.31 O ANISOU 1797 O ALA A 262 8561 8288 12147 -722 -436 795 O ATOM 1798 CB ALA A 262 22.572 89.198-400.721 1.00 75.87 C ANISOU 1798 CB ALA A 262 7977 8197 12655 -865 -744 454 C ATOM 1799 N SER A 263 23.442 88.550-397.568 1.00 68.88 N ANISOU 1799 N SER A 263 7507 7764 10902 -493 -300 630 N ATOM 1800 CA SER A 263 23.475 87.521-396.537 1.00 67.26 C ANISOU 1800 CA SER A 263 7428 7672 10455 -480 -94 836 C ATOM 1801 C SER A 263 22.632 86.316-396.938 1.00 69.84 C ANISOU 1801 C SER A 263 7635 7994 10908 -692 22 1117 C ATOM 1802 O SER A 263 21.969 86.332-397.972 1.00 72.21 O ANISOU 1802 O SER A 263 7743 8193 11501 -879 -44 1168 O ATOM 1803 CB SER A 263 22.980 88.090-395.206 1.00 64.71 C ANISOU 1803 CB SER A 263 7113 7618 9857 -296 24 768 C ATOM 1804 OG SER A 263 22.732 87.057-394.266 1.00 65.89 O ANISOU 1804 OG SER A 263 7338 7895 9803 -283 201 956 O ATOM 1805 N THR A 264 22.668 85.264-396.127 1.00 67.52 N ANISOU 1805 N THR A 264 7447 7808 10401 -655 191 1303 N ATOM 1806 CA THR A 264 21.866 84.080-396.395 1.00 68.33 C ANISOU 1806 CA THR A 264 7436 7961 10566 -801 332 1601 C ATOM 1807 C THR A 264 21.316 83.495-395.098 1.00 71.00 C ANISOU 1807 C THR A 264 7791 8598 10587 -655 520 1713 C ATOM 1808 O THR A 264 20.492 82.582-395.120 1.00 74.92 O ANISOU 1808 O THR A 264 8165 9234 11067 -713 662 1966 O ATOM 1809 CB THR A 264 22.680 82.989-397.119 1.00 71.27 C ANISOU 1809 CB THR A 264 7948 8096 11034 -892 315 1758 C ATOM 1810 OG1 THR A 264 23.318 82.152-396.152 1.00 67.29 O ANISOU 1810 OG1 THR A 264 7641 7690 10238 -737 420 1810 O ATOM 1811 CG2 THR A 264 23.735 83.605-398.023 1.00 68.95 C ANISOU 1811 CG2 THR A 264 7760 7518 10921 -914 93 1561 C ATOM 1812 N ALA A 265 21.768 84.038-393.972 1.00 69.30 N ANISOU 1812 N ALA A 265 7725 8483 10124 -449 513 1527 N ATOM 1813 CA ALA A 265 21.450 83.495-392.650 1.00 69.40 C ANISOU 1813 CA ALA A 265 7807 8735 9828 -271 644 1580 C ATOM 1814 C ALA A 265 20.004 83.024-392.472 1.00 68.51 C ANISOU 1814 C ALA A 265 7474 8911 9646 -274 783 1772 C ATOM 1815 O ALA A 265 19.750 81.831-392.313 1.00 81.82 O ANISOU 1815 O ALA A 265 9150 10704 11232 -250 901 1990 O ATOM 1816 CB ALA A 265 21.819 84.504-391.564 1.00 64.75 C ANISOU 1816 CB ALA A 265 7352 8201 9049 -75 597 1339 C ATOM 1817 N LYS A 266 19.069 83.967-392.481 1.00105.31 N ANISOU 1817 N LYS A 266 11948 13727 14337 -274 772 1687 N ATOM 1818 CA LYS A 266 17.657 83.656-392.267 1.00108.64 C ANISOU 1818 CA LYS A 266 12130 14477 14671 -258 902 1855 C ATOM 1819 C LYS A 266 17.123 82.714-393.342 1.00111.06 C ANISOU 1819 C LYS A 266 12237 14757 15205 -489 990 2170 C ATOM 1820 O LYS A 266 16.056 82.116-393.185 1.00121.47 O ANISOU 1820 O LYS A 266 13357 16364 16432 -475 1137 2397 O ATOM 1821 CB LYS A 266 16.822 84.941-392.221 1.00108.66 C ANISOU 1821 CB LYS A 266 11953 14641 14690 -228 853 1674 C ATOM 1822 CG LYS A 266 15.317 84.717-392.179 1.00114.29 C ANISOU 1822 CG LYS A 266 12362 15717 15345 -240 978 1845 C ATOM 1823 CD LYS A 266 14.879 84.038-390.890 1.00112.18 C ANISOU 1823 CD LYS A 266 12168 15774 14681 29 1096 1925 C ATOM 1824 CE LYS A 266 14.733 85.041-389.755 1.00108.83 C ANISOU 1824 CE LYS A 266 11857 15510 13984 301 1038 1648 C ATOM 1825 NZ LYS A 266 13.616 86.001-389.983 1.00112.48 N ANISOU 1825 NZ LYS A 266 12049 16217 14473 295 1031 1560 N ATOM 1826 N ALA A 267 17.877 82.580-394.429 1.00 82.24 N ANISOU 1826 N ALA A 267 8641 10763 11844 -687 902 2197 N ATOM 1827 CA ALA A 267 17.495 81.693-395.525 1.00 88.26 C ANISOU 1827 CA ALA A 267 9250 11422 12863 -920 973 2510 C ATOM 1828 C ALA A 267 18.209 80.340-395.439 1.00 82.99 C ANISOU 1828 C ALA A 267 8779 10675 12077 -857 1058 2707 C ATOM 1829 O ALA A 267 18.326 79.621-396.431 1.00 86.76 O ANISOU 1829 O ALA A 267 9232 10955 12776 -1031 1082 2932 O ATOM 1830 CB ALA A 267 17.765 82.361-396.865 1.00 94.42 C ANISOU 1830 CB ALA A 267 9957 11859 14060 -1169 801 2417 C ATOM 1831 N VAL A 268 18.683 80.004-394.245 1.00 76.20 N ANISOU 1831 N VAL A 268 8116 9963 10872 -597 1093 2612 N ATOM 1832 CA VAL A 268 19.341 78.730-394.001 1.00 76.24 C ANISOU 1832 CA VAL A 268 8299 9950 10718 -483 1165 2751 C ATOM 1833 C VAL A 268 19.000 78.255-392.595 1.00 75.20 C ANISOU 1833 C VAL A 268 8213 10160 10199 -187 1258 2734 C ATOM 1834 O VAL A 268 18.976 77.058-392.318 1.00 75.41 O ANISOU 1834 O VAL A 268 8276 10327 10051 -48 1367 2919 O ATOM 1835 CB VAL A 268 20.869 78.851-394.143 1.00 79.49 C ANISOU 1835 CB VAL A 268 8984 10049 11170 -476 1017 2543 C ATOM 1836 CG1 VAL A 268 21.567 77.601-393.624 1.00 76.91 C ANISOU 1836 CG1 VAL A 268 8843 9763 10617 -302 1080 2617 C ATOM 1837 CG2 VAL A 268 21.252 79.114-395.587 1.00 77.40 C ANISOU 1837 CG2 VAL A 268 8697 9446 11264 -723 907 2572 C ATOM 1838 N PHE A 269 18.720 79.210-391.716 1.00 86.32 N ANISOU 1838 N PHE A 269 9624 11706 11468 -66 1203 2504 N ATOM 1839 CA PHE A 269 18.398 78.908-390.327 1.00 89.81 C ANISOU 1839 CA PHE A 269 10130 12443 11552 234 1247 2436 C ATOM 1840 C PHE A 269 16.916 79.059-389.996 1.00102.99 C ANISOU 1840 C PHE A 269 11549 14500 13083 322 1349 2550 C ATOM 1841 O PHE A 269 16.257 80.009-390.422 1.00107.58 O ANISOU 1841 O PHE A 269 11951 15116 13810 189 1331 2510 O ATOM 1842 CB PHE A 269 19.198 79.813-389.391 1.00 89.55 C ANISOU 1842 CB PHE A 269 10319 12287 11418 355 1109 2096 C ATOM 1843 CG PHE A 269 20.655 79.483-389.321 1.00 81.67 C ANISOU 1843 CG PHE A 269 9568 11011 10451 350 1024 1983 C ATOM 1844 CD1 PHE A 269 21.123 78.550-388.414 1.00 74.34 C ANISOU 1844 CD1 PHE A 269 8793 10152 9302 555 1030 1952 C ATOM 1845 CD2 PHE A 269 21.559 80.114-390.154 1.00 77.27 C ANISOU 1845 CD2 PHE A 269 9079 10146 10135 162 925 1889 C ATOM 1846 CE1 PHE A 269 22.467 78.246-388.341 1.00 77.24 C ANISOU 1846 CE1 PHE A 269 9360 10287 9702 543 951 1836 C ATOM 1847 CE2 PHE A 269 22.904 79.817-390.086 1.00 71.75 C ANISOU 1847 CE2 PHE A 269 8586 9233 9444 168 851 1789 C ATOM 1848 CZ PHE A 269 23.360 78.880-389.179 1.00 75.43 C ANISOU 1848 CZ PHE A 269 9187 9772 9700 345 870 1765 C ATOM 1849 N GLY A 270 16.395 78.115-389.222 1.00 82.79 N ANISOU 1849 N GLY A 270 8968 12261 10228 575 1447 2675 N ATOM 1850 CA GLY A 270 15.099 78.290-388.610 1.00 80.89 C ANISOU 1850 CA GLY A 270 8530 12441 9762 751 1519 2725 C ATOM 1851 C GLY A 270 15.346 78.989-387.293 1.00 82.32 C ANISOU 1851 C GLY A 270 8916 12658 9705 1003 1390 2387 C ATOM 1852 O GLY A 270 15.061 80.175-387.142 1.00 82.04 O ANISOU 1852 O GLY A 270 8853 12617 9700 976 1324 2205 O ATOM 1853 N TYR A 271 15.903 78.243-386.347 1.00171.87 N ANISOU 1853 N TYR A 271 20467 24018 20817 1255 1347 2299 N ATOM 1854 CA TYR A 271 16.293 78.779-385.051 1.00179.43 C ANISOU 1854 CA TYR A 271 21657 24936 21584 1484 1207 1984 C ATOM 1855 C TYR A 271 17.339 79.871-385.245 1.00175.59 C ANISOU 1855 C TYR A 271 21344 24041 21332 1285 1092 1764 C ATOM 1856 O TYR A 271 18.519 79.578-385.432 1.00174.25 O ANISOU 1856 O TYR A 271 21340 23576 21291 1185 1040 1714 O ATOM 1857 CB TYR A 271 16.862 77.651-384.186 1.00186.43 C ANISOU 1857 CB TYR A 271 22724 25850 22262 1742 1161 1930 C ATOM 1858 CG TYR A 271 16.966 77.958-382.705 1.00199.10 C ANISOU 1858 CG TYR A 271 24530 27487 23632 2038 1017 1642 C ATOM 1859 CD1 TYR A 271 15.829 78.187-381.940 1.00202.52 C ANISOU 1859 CD1 TYR A 271 24883 28275 23789 2312 1010 1603 C ATOM 1860 CD2 TYR A 271 18.203 77.990-382.068 1.00198.07 C ANISOU 1860 CD2 TYR A 271 24667 27030 23560 2049 879 1413 C ATOM 1861 CE1 TYR A 271 15.922 78.459-380.583 1.00213.66 C ANISOU 1861 CE1 TYR A 271 26503 29681 24996 2596 855 1332 C ATOM 1862 CE2 TYR A 271 18.305 78.259-380.713 1.00198.60 C ANISOU 1862 CE2 TYR A 271 24925 27079 23456 2300 735 1158 C ATOM 1863 CZ TYR A 271 17.162 78.493-379.976 1.00208.10 C ANISOU 1863 CZ TYR A 271 26071 28604 24392 2578 716 1114 C ATOM 1864 OH TYR A 271 17.263 78.762-378.628 1.00202.07 O ANISOU 1864 OH TYR A 271 25521 27789 23469 2839 550 853 O ATOM 1865 N GLY A 272 16.905 81.128-385.207 1.00101.20 N ANISOU 1865 N GLY A 272 11873 14635 11945 1252 1057 1636 N ATOM 1866 CA GLY A 272 17.804 82.254-385.397 1.00 91.37 C ANISOU 1866 CA GLY A 272 10768 13057 10891 1110 959 1442 C ATOM 1867 C GLY A 272 18.607 82.586-384.154 1.00 91.20 C ANISOU 1867 C GLY A 272 11035 12879 10739 1291 851 1210 C ATOM 1868 O GLY A 272 18.373 82.008-383.092 1.00 95.32 O ANISOU 1868 O GLY A 272 11650 13546 11023 1537 826 1163 O ATOM 1869 N PRO A 273 19.569 83.517-384.278 1.00 65.01 N ANISOU 1869 N PRO A 273 7854 9263 7582 1178 779 1069 N ATOM 1870 CA PRO A 273 20.390 83.954-383.143 1.00 62.35 C ANISOU 1870 CA PRO A 273 7780 8739 7170 1310 688 879 C ATOM 1871 C PRO A 273 19.515 84.577-382.058 1.00 66.31 C ANISOU 1871 C PRO A 273 8332 9428 7434 1571 661 758 C ATOM 1872 O PRO A 273 18.779 85.527-382.329 1.00 74.61 O ANISOU 1872 O PRO A 273 9273 10612 8465 1593 684 726 O ATOM 1873 CB PRO A 273 21.311 85.010-383.758 1.00 64.17 C ANISOU 1873 CB PRO A 273 8062 8702 7617 1140 652 809 C ATOM 1874 CG PRO A 273 21.328 84.708-385.207 1.00 63.29 C ANISOU 1874 CG PRO A 273 7770 8565 7713 909 690 947 C ATOM 1875 CD PRO A 273 19.963 84.185-385.527 1.00 69.41 C ANISOU 1875 CD PRO A 273 8319 9643 8412 931 773 1091 C ATOM 1876 N GLN A 274 19.595 84.038-380.846 1.00 67.99 N ANISOU 1876 N GLN A 274 8713 9652 7468 1785 597 672 N ATOM 1877 CA GLN A 274 18.719 84.466-379.763 1.00 66.23 C ANISOU 1877 CA GLN A 274 8559 9617 6989 2077 549 553 C ATOM 1878 C GLN A 274 19.212 85.721-379.053 1.00 68.48 C ANISOU 1878 C GLN A 274 9059 9668 7292 2139 481 388 C ATOM 1879 O GLN A 274 18.666 86.802-379.256 1.00 68.84 O ANISOU 1879 O GLN A 274 9049 9807 7300 2180 510 348 O ATOM 1880 CB GLN A 274 18.507 83.328-378.767 1.00 67.52 C ANISOU 1880 CB GLN A 274 8807 9904 6943 2321 480 514 C ATOM 1881 CG GLN A 274 17.677 82.195-379.338 1.00 74.51 C ANISOU 1881 CG GLN A 274 9455 11137 7717 2363 570 700 C ATOM 1882 CD GLN A 274 16.303 82.656-379.780 1.00 77.97 C ANISOU 1882 CD GLN A 274 9651 11947 8027 2420 662 796 C ATOM 1883 OE1 GLN A 274 15.505 83.131-378.972 1.00 82.97 O ANISOU 1883 OE1 GLN A 274 10317 12787 8419 2683 613 683 O ATOM 1884 NE2 GLN A 274 16.018 82.513-381.069 1.00 80.29 N ANISOU 1884 NE2 GLN A 274 9695 12324 8486 2175 788 1001 N ATOM 1885 N THR A 275 20.231 85.584-378.214 1.00 76.20 N ANISOU 1885 N THR A 275 10274 10349 8329 2154 395 296 N ATOM 1886 CA THR A 275 20.776 86.744-377.520 1.00 74.21 C ANISOU 1886 CA THR A 275 10233 9848 8117 2202 348 185 C ATOM 1887 C THR A 275 21.560 87.605-378.504 1.00 77.89 C ANISOU 1887 C THR A 275 10645 10145 8805 1969 416 245 C ATOM 1888 O THR A 275 21.856 87.165-379.614 1.00 76.98 O ANISOU 1888 O THR A 275 10369 10042 8837 1758 466 347 O ATOM 1889 CB THR A 275 21.689 86.330-376.359 1.00 78.75 C ANISOU 1889 CB THR A 275 11054 10127 8740 2249 234 89 C ATOM 1890 OG1 THR A 275 22.934 85.845-376.877 1.00 82.78 O ANISOU 1890 OG1 THR A 275 11553 10412 9487 1991 248 150 O ATOM 1891 CG2 THR A 275 21.031 85.243-375.522 1.00 87.77 C ANISOU 1891 CG2 THR A 275 12228 11441 9680 2487 136 11 C ATOM 1892 N ASP A 276 21.894 88.831-378.103 1.00 97.06 N ANISOU 1892 N ASP A 276 13211 12420 11246 2033 413 183 N ATOM 1893 CA ASP A 276 22.637 89.746-378.972 1.00 93.09 C ANISOU 1893 CA ASP A 276 12660 11792 10917 1880 466 226 C ATOM 1894 C ASP A 276 24.094 89.311-379.117 1.00 82.20 C ANISOU 1894 C ASP A 276 11350 10133 9750 1669 454 285 C ATOM 1895 O ASP A 276 24.811 89.769-380.009 1.00 71.81 O ANISOU 1895 O ASP A 276 9962 8741 8581 1526 487 335 O ATOM 1896 CB ASP A 276 22.557 91.181-378.446 1.00 88.99 C ANISOU 1896 CB ASP A 276 12271 11228 10314 2064 478 158 C ATOM 1897 CG ASP A 276 21.128 91.633-378.197 1.00 96.06 C ANISOU 1897 CG ASP A 276 13111 12420 10966 2307 479 74 C ATOM 1898 OD1 ASP A 276 20.624 92.479-378.969 1.00 92.56 O ANISOU 1898 OD1 ASP A 276 12514 12151 10503 2339 521 46 O ATOM 1899 OD2 ASP A 276 20.507 91.134-377.233 1.00 99.75 O ANISOU 1899 OD2 ASP A 276 13679 12964 11258 2482 425 18 O ATOM 1900 N SER A 277 24.519 88.420-378.229 1.00 60.23 N ANISOU 1900 N SER A 277 8696 7215 6973 1672 392 260 N ATOM 1901 CA SER A 277 25.866 87.870-378.267 1.00 58.59 C ANISOU 1901 CA SER A 277 8537 6772 6953 1481 371 297 C ATOM 1902 C SER A 277 25.878 86.453-378.849 1.00 59.55 C ANISOU 1902 C SER A 277 8535 6993 7099 1374 358 332 C ATOM 1903 O SER A 277 26.771 85.656-378.556 1.00 60.57 O ANISOU 1903 O SER A 277 8718 6975 7320 1285 311 316 O ATOM 1904 CB SER A 277 26.497 87.897-376.871 1.00 93.93 C ANISOU 1904 CB SER A 277 13235 10988 11465 1538 297 232 C ATOM 1905 OG SER A 277 25.595 87.424-375.885 1.00 95.31 O ANISOU 1905 OG SER A 277 13500 11239 11473 1750 213 127 O ATOM 1906 N GLN A 278 24.876 86.149-379.670 1.00 61.77 N ANISOU 1906 N GLN A 278 8640 7530 7298 1390 405 386 N ATOM 1907 CA GLN A 278 24.848 84.901-380.425 1.00 60.39 C ANISOU 1907 CA GLN A 278 8334 7460 7152 1289 423 468 C ATOM 1908 C GLN A 278 25.005 85.222-381.903 1.00 61.13 C ANISOU 1908 C GLN A 278 8269 7569 7390 1101 482 568 C ATOM 1909 O GLN A 278 24.515 86.247-382.370 1.00 60.16 O ANISOU 1909 O GLN A 278 8070 7510 7279 1109 509 564 O ATOM 1910 CB GLN A 278 23.542 84.135-380.191 1.00 62.74 C ANISOU 1910 CB GLN A 278 8539 8049 7249 1461 435 489 C ATOM 1911 CG GLN A 278 23.416 83.518-378.804 1.00 65.86 C ANISOU 1911 CG GLN A 278 9084 8447 7492 1681 339 370 C ATOM 1912 CD GLN A 278 22.238 82.575-378.685 1.00 69.14 C ANISOU 1912 CD GLN A 278 9386 9198 7687 1879 350 409 C ATOM 1913 OE1 GLN A 278 21.885 82.143-377.589 1.00 72.68 O ANISOU 1913 OE1 GLN A 278 9934 9715 7965 2123 256 295 O ATOM 1914 NE2 GLN A 278 21.626 82.248-379.815 1.00 70.17 N ANISOU 1914 NE2 GLN A 278 9299 9541 7823 1786 460 578 N ATOM 1915 N TYR A 279 25.689 84.352-382.637 1.00 62.28 N ANISOU 1915 N TYR A 279 8368 7653 7644 951 485 639 N ATOM 1916 CA TYR A 279 25.938 84.594-384.052 1.00 58.87 C ANISOU 1916 CA TYR A 279 7810 7192 7366 778 509 719 C ATOM 1917 C TYR A 279 25.646 83.381-384.921 1.00 59.59 C ANISOU 1917 C TYR A 279 7781 7373 7486 692 544 850 C ATOM 1918 O TYR A 279 25.798 82.237-384.493 1.00 58.27 O ANISOU 1918 O TYR A 279 7658 7241 7240 746 545 872 O ATOM 1919 CB TYR A 279 27.375 85.050-384.265 1.00 56.80 C ANISOU 1919 CB TYR A 279 7636 6711 7236 675 467 681 C ATOM 1920 CG TYR A 279 27.707 86.346-383.573 1.00 55.60 C ANISOU 1920 CG TYR A 279 7583 6469 7072 756 457 602 C ATOM 1921 CD1 TYR A 279 27.788 87.532-384.285 1.00 60.94 C ANISOU 1921 CD1 TYR A 279 8201 7142 7812 752 458 589 C ATOM 1922 CD2 TYR A 279 27.941 86.386-382.207 1.00 57.41 C ANISOU 1922 CD2 TYR A 279 7969 6613 7232 854 440 541 C ATOM 1923 CE1 TYR A 279 28.095 88.725-383.659 1.00 56.42 C ANISOU 1923 CE1 TYR A 279 7722 6509 7207 862 466 541 C ATOM 1924 CE2 TYR A 279 28.248 87.570-381.569 1.00 59.30 C ANISOU 1924 CE2 TYR A 279 8312 6752 7469 932 447 505 C ATOM 1925 CZ TYR A 279 28.323 88.738-382.301 1.00 58.46 C ANISOU 1925 CZ TYR A 279 8144 6671 7399 944 473 517 C ATOM 1926 OH TYR A 279 28.629 89.923-381.676 1.00 61.27 O ANISOU 1926 OH TYR A 279 8603 6949 7729 1056 496 504 O ATOM 1927 N ALA A 280 25.217 83.646-386.147 1.00 65.06 N ANISOU 1927 N ALA A 280 8321 8098 8300 571 567 935 N ATOM 1928 CA ALA A 280 24.990 82.596-387.122 1.00 65.47 C ANISOU 1928 CA ALA A 280 8262 8190 8422 463 608 1094 C ATOM 1929 C ALA A 280 26.281 82.372-387.892 1.00 61.86 C ANISOU 1929 C ALA A 280 7876 7521 8108 333 552 1091 C ATOM 1930 O ALA A 280 26.841 83.308-388.454 1.00 64.50 O ANISOU 1930 O ALA A 280 8214 7728 8566 264 489 1020 O ATOM 1931 CB ALA A 280 23.864 82.983-388.070 1.00 65.87 C ANISOU 1931 CB ALA A 280 8103 8351 8572 376 647 1192 C ATOM 1932 N ILE A 281 26.760 81.133-387.905 1.00 58.89 N ANISOU 1932 N ILE A 281 7552 7134 7691 337 567 1156 N ATOM 1933 CA ILE A 281 27.972 80.786-388.631 1.00 56.35 C ANISOU 1933 CA ILE A 281 7298 6644 7468 241 512 1152 C ATOM 1934 C ILE A 281 27.664 79.786-389.731 1.00 59.81 C ANISOU 1934 C ILE A 281 7662 7092 7972 164 554 1332 C ATOM 1935 O ILE A 281 27.061 78.747-389.479 1.00 61.59 O ANISOU 1935 O ILE A 281 7854 7462 8085 244 636 1451 O ATOM 1936 CB ILE A 281 29.019 80.166-387.700 1.00 57.76 C ANISOU 1936 CB ILE A 281 7618 6784 7543 320 481 1051 C ATOM 1937 CG1 ILE A 281 29.514 81.193-386.681 1.00 54.77 C ANISOU 1937 CG1 ILE A 281 7325 6337 7150 361 437 900 C ATOM 1938 CG2 ILE A 281 30.183 79.629-388.502 1.00 55.46 C ANISOU 1938 CG2 ILE A 281 7377 6376 7318 244 433 1057 C ATOM 1939 CD1 ILE A 281 28.684 81.247-385.424 1.00 57.51 C ANISOU 1939 CD1 ILE A 281 7699 6789 7363 505 460 849 C ATOM 1940 N ILE A 282 28.084 80.091-390.951 1.00 58.81 N ANISOU 1940 N ILE A 282 7513 6809 8022 30 493 1358 N ATOM 1941 CA ILE A 282 27.858 79.187-392.070 1.00 59.00 C ANISOU 1941 CA ILE A 282 7488 6786 8142 -56 521 1542 C ATOM 1942 C ILE A 282 29.156 78.921-392.824 1.00 59.18 C ANISOU 1942 C ILE A 282 7629 6629 8228 -94 424 1494 C ATOM 1943 O ILE A 282 29.634 79.786-393.554 1.00 65.31 O ANISOU 1943 O ILE A 282 8407 7262 9145 -166 311 1405 O ATOM 1944 CB ILE A 282 26.812 79.758-393.037 1.00 62.07 C ANISOU 1944 CB ILE A 282 7705 7145 8732 -197 525 1646 C ATOM 1945 CG1 ILE A 282 25.457 79.853-392.341 1.00 69.46 C ANISOU 1945 CG1 ILE A 282 8501 8314 9576 -143 637 1720 C ATOM 1946 CG2 ILE A 282 26.712 78.904-394.288 1.00 70.26 C ANISOU 1946 CG2 ILE A 282 8711 8061 9924 -315 537 1848 C ATOM 1947 CD1 ILE A 282 24.357 80.406-393.216 1.00 67.28 C ANISOU 1947 CD1 ILE A 282 8016 8045 9503 -292 647 1819 C ATOM 1948 N VAL A 283 29.720 77.726-392.653 1.00 65.21 N ANISOU 1948 N VAL A 283 8486 7424 8867 -15 457 1538 N ATOM 1949 CA VAL A 283 31.006 77.391-393.260 1.00 62.91 C ANISOU 1949 CA VAL A 283 8313 7004 8586 -16 364 1475 C ATOM 1950 C VAL A 283 30.859 76.756-394.633 1.00 64.91 C ANISOU 1950 C VAL A 283 8568 7130 8966 -91 354 1646 C ATOM 1951 O VAL A 283 30.063 75.847-394.812 1.00 66.13 O ANISOU 1951 O VAL A 283 8676 7348 9101 -79 469 1851 O ATOM 1952 CB VAL A 283 31.809 76.448-392.371 1.00 57.79 C ANISOU 1952 CB VAL A 283 7765 6456 7735 124 385 1396 C ATOM 1953 CG1 VAL A 283 32.982 75.873-393.143 1.00 57.78 C ANISOU 1953 CG1 VAL A 283 7868 6364 7721 141 307 1366 C ATOM 1954 CG2 VAL A 283 32.289 77.178-391.134 1.00 60.83 C ANISOU 1954 CG2 VAL A 283 8174 6886 8054 165 353 1206 C ATOM 1955 N ARG A 284 31.640 77.231-395.597 1.00 61.74 N ANISOU 1955 N ARG A 284 8222 6550 8688 -148 213 1569 N ATOM 1956 CA ARG A 284 31.536 76.753-396.970 1.00 62.88 C ANISOU 1956 CA ARG A 284 8388 6513 8989 -225 166 1713 C ATOM 1957 C ARG A 284 32.879 76.317-397.538 1.00 62.64 C ANISOU 1957 C ARG A 284 8519 6390 8892 -145 49 1624 C ATOM 1958 O ARG A 284 33.877 77.009-397.380 1.00 59.47 O ANISOU 1958 O ARG A 284 8165 5993 8439 -95 -67 1422 O ATOM 1959 CB ARG A 284 30.967 77.846-397.875 1.00 67.99 C ANISOU 1959 CB ARG A 284 8929 6996 9907 -373 59 1697 C ATOM 1960 CG ARG A 284 29.477 78.108-397.749 1.00 69.70 C ANISOU 1960 CG ARG A 284 8959 7279 10244 -484 168 1837 C ATOM 1961 CD ARG A 284 29.068 79.213-398.717 1.00 63.88 C ANISOU 1961 CD ARG A 284 8111 6366 9793 -621 22 1767 C ATOM 1962 NE ARG A 284 27.623 79.384-398.800 1.00 69.30 N ANISOU 1962 NE ARG A 284 8591 7107 10631 -755 118 1918 N ATOM 1963 CZ ARG A 284 26.922 80.166-397.989 1.00 69.95 C ANISOU 1963 CZ ARG A 284 8548 7376 10654 -733 175 1839 C ATOM 1964 NH1 ARG A 284 27.536 80.845-397.030 1.00 65.32 N ANISOU 1964 NH1 ARG A 284 8037 6904 9877 -590 149 1628 N ATOM 1965 NH2 ARG A 284 25.610 80.265-398.136 1.00 72.93 N ANISOU 1965 NH2 ARG A 284 8720 7829 11162 -851 260 1981 N ATOM 1966 N ARG A 285 32.899 75.178-398.215 1.00 69.78 N ANISOU 1966 N ARG A 285 9503 7227 9784 -117 84 1788 N ATOM 1967 CA ARG A 285 34.066 74.793-398.990 1.00 72.59 C ANISOU 1967 CA ARG A 285 10017 7472 10093 -35 -47 1713 C ATOM 1968 C ARG A 285 33.602 74.405-400.380 1.00 66.98 C ANISOU 1968 C ARG A 285 9345 6510 9594 -124 -92 1906 C ATOM 1969 O ARG A 285 32.886 73.420-400.537 1.00 73.62 O ANISOU 1969 O ARG A 285 10181 7353 10440 -131 55 2158 O ATOM 1970 CB ARG A 285 34.813 73.628-398.335 1.00 61.92 C ANISOU 1970 CB ARG A 285 8769 6296 8462 146 29 1688 C ATOM 1971 CG ARG A 285 36.066 73.191-399.107 1.00 72.07 C ANISOU 1971 CG ARG A 285 10219 7508 9658 260 -108 1595 C ATOM 1972 CD ARG A 285 36.874 72.101-398.385 1.00 78.67 C ANISOU 1972 CD ARG A 285 11133 8554 10204 454 -47 1520 C ATOM 1973 NE ARG A 285 36.051 70.940-398.057 1.00 87.71 N ANISOU 1973 NE ARG A 285 12268 9800 11258 533 135 1721 N ATOM 1974 CZ ARG A 285 35.667 70.020-398.937 1.00 79.33 C ANISOU 1974 CZ ARG A 285 11287 8641 10213 582 194 1950 C ATOM 1975 NH1 ARG A 285 36.037 70.116-400.209 1.00 77.88 N ANISOU 1975 NH1 ARG A 285 11218 8219 10154 545 67 1989 N ATOM 1976 NH2 ARG A 285 34.909 69.005-398.542 1.00 71.50 N ANISOU 1976 NH2 ARG A 285 10264 7792 9109 688 377 2145 N ATOM 1977 N ASN A 286 33.997 75.182-401.383 1.00 86.65 N ANISOU 1977 N ASN A 286 11871 8785 12268 -178 -300 1795 N ATOM 1978 CA ASN A 286 33.570 74.936-402.760 1.00 95.96 C ANISOU 1978 CA ASN A 286 13090 9662 13707 -284 -387 1953 C ATOM 1979 C ASN A 286 32.087 75.214-402.977 1.00 95.89 C ANISOU 1979 C ASN A 286 12893 9565 13976 -500 -294 2154 C ATOM 1980 O ASN A 286 31.399 74.451-403.656 1.00 91.92 O ANISOU 1980 O ASN A 286 12387 8910 13628 -596 -214 2430 O ATOM 1981 CB ASN A 286 33.886 73.498-403.186 1.00 92.15 C ANISOU 1981 CB ASN A 286 12775 9133 13103 -176 -314 2138 C ATOM 1982 CG ASN A 286 35.345 73.300-403.538 1.00 94.35 C ANISOU 1982 CG ASN A 286 13252 9401 13196 16 -484 1937 C ATOM 1983 OD1 ASN A 286 36.084 74.265-403.741 1.00 92.46 O ANISOU 1983 OD1 ASN A 286 13023 9137 12971 51 -684 1689 O ATOM 1984 ND2 ASN A 286 35.768 72.042-403.621 1.00102.63 N ANISOU 1984 ND2 ASN A 286 14449 10498 14047 170 -405 2044 N ATOM 1985 N ASP A 287 31.602 76.308-402.396 1.00103.09 N ANISOU 1985 N ASP A 287 13641 10584 14945 -570 -299 2025 N ATOM 1986 CA ASP A 287 30.203 76.701-402.534 1.00106.79 C ANISOU 1986 CA ASP A 287 13898 11017 15660 -766 -222 2175 C ATOM 1987 C ASP A 287 29.291 75.787-401.725 1.00101.28 C ANISOU 1987 C ASP A 287 13111 10545 14824 -766 58 2440 C ATOM 1988 O ASP A 287 28.091 76.030-401.617 1.00102.79 O ANISOU 1988 O ASP A 287 13103 10798 15153 -902 163 2581 O ATOM 1989 CB ASP A 287 29.777 76.691-404.003 1.00109.90 C ANISOU 1989 CB ASP A 287 14274 11056 16428 -943 -356 2297 C ATOM 1990 CG ASP A 287 30.756 77.422-404.899 1.00122.43 C ANISOU 1990 CG ASP A 287 15980 12413 18126 -885 -665 2028 C ATOM 1991 OD1 ASP A 287 31.512 78.275-404.386 1.00115.84 O ANISOU 1991 OD1 ASP A 287 15165 11722 17126 -744 -769 1746 O ATOM 1992 OD2 ASP A 287 30.767 77.140-406.117 1.00122.57 O ANISOU 1992 OD2 ASP A 287 16071 12107 18394 -966 -809 2106 O ATOM 1993 N ALA A 288 29.868 74.733-401.158 1.00 81.63 N ANISOU 1993 N ALA A 288 10758 8207 12050 -590 170 2493 N ATOM 1994 CA ALA A 288 29.104 73.783-400.363 1.00 80.28 C ANISOU 1994 CA ALA A 288 10517 8285 11700 -518 417 2721 C ATOM 1995 C ALA A 288 28.934 74.287-398.940 1.00 76.28 C ANISOU 1995 C ALA A 288 9928 8066 10988 -427 482 2554 C ATOM 1996 O ALA A 288 29.897 74.706-398.307 1.00 73.03 O ANISOU 1996 O ALA A 288 9610 7712 10425 -323 390 2291 O ATOM 1997 CB ALA A 288 29.788 72.429-400.361 1.00 78.38 C ANISOU 1997 CB ALA A 288 10453 8095 11232 -327 489 2821 C ATOM 1998 N ILE A 289 27.708 74.242-398.435 1.00 72.21 N ANISOU 1998 N ILE A 289 9236 7733 10467 -462 640 2717 N ATOM 1999 CA ILE A 289 27.446 74.666-397.070 1.00 68.28 C ANISOU 1999 CA ILE A 289 8675 7500 9768 -354 695 2569 C ATOM 2000 C ILE A 289 27.809 73.520-396.148 1.00 69.13 C ANISOU 2000 C ILE A 289 8880 7826 9561 -115 800 2585 C ATOM 2001 O ILE A 289 26.946 72.802-395.662 1.00 69.21 O ANISOU 2001 O ILE A 289 8800 8061 9437 -13 961 2770 O ATOM 2002 CB ILE A 289 25.979 75.066-396.856 1.00 72.98 C ANISOU 2002 CB ILE A 289 9040 8244 10445 -445 808 2714 C ATOM 2003 CG1 ILE A 289 25.493 75.979-397.990 1.00 81.34 C ANISOU 2003 CG1 ILE A 289 9971 9073 11863 -696 708 2739 C ATOM 2004 CG2 ILE A 289 25.803 75.740-395.502 1.00 69.96 C ANISOU 2004 CG2 ILE A 289 8624 8087 9870 -326 816 2507 C ATOM 2005 CD1 ILE A 289 25.110 75.245-399.281 1.00 83.75 C ANISOU 2005 CD1 ILE A 289 10237 9173 12411 -852 746 3044 C ATOM 2006 N VAL A 290 29.106 73.356-395.928 1.00 67.63 N ANISOU 2006 N VAL A 290 8861 7587 9249 -11 698 2378 N ATOM 2007 CA VAL A 290 29.657 72.251-395.154 1.00 64.56 C ANISOU 2007 CA VAL A 290 8571 7377 8581 222 755 2338 C ATOM 2008 C VAL A 290 29.176 72.139-393.699 1.00 68.37 C ANISOU 2008 C VAL A 290 8991 8133 8855 380 828 2254 C ATOM 2009 O VAL A 290 29.062 71.032-393.164 1.00 65.21 O ANISOU 2009 O VAL A 290 8607 7930 8239 594 916 2314 O ATOM 2010 CB VAL A 290 31.185 72.312-395.180 1.00 63.38 C ANISOU 2010 CB VAL A 290 8583 7128 8369 272 608 2092 C ATOM 2011 CG1 VAL A 290 31.747 72.088-393.797 1.00 65.52 C ANISOU 2011 CG1 VAL A 290 8888 7590 8416 439 600 1874 C ATOM 2012 CG2 VAL A 290 31.740 71.322-396.196 1.00 66.27 C ANISOU 2012 CG2 VAL A 290 9073 7390 8717 333 600 2214 C ATOM 2013 N GLN A 291 28.901 73.273-393.061 1.00 65.62 N ANISOU 2013 N GLN A 291 8577 7796 8560 305 780 2104 N ATOM 2014 CA GLN A 291 28.407 73.279-391.685 1.00 65.19 C ANISOU 2014 CA GLN A 291 8479 7965 8324 457 822 2010 C ATOM 2015 C GLN A 291 27.596 74.536-391.386 1.00 66.26 C ANISOU 2015 C GLN A 291 8504 8111 8561 349 813 1968 C ATOM 2016 O GLN A 291 27.831 75.584-391.976 1.00 67.24 O ANISOU 2016 O GLN A 291 8619 8056 8875 177 732 1900 O ATOM 2017 CB GLN A 291 29.563 73.137-390.691 1.00 61.11 C ANISOU 2017 CB GLN A 291 8090 7460 7668 583 725 1737 C ATOM 2018 CG GLN A 291 29.173 73.413-389.248 1.00 63.00 C ANISOU 2018 CG GLN A 291 8309 7848 7779 710 714 1585 C ATOM 2019 CD GLN A 291 30.013 72.642-388.244 1.00 71.19 C ANISOU 2019 CD GLN A 291 9440 8958 8650 897 649 1384 C ATOM 2020 OE1 GLN A 291 30.764 71.738-388.607 1.00 74.05 O ANISOU 2020 OE1 GLN A 291 9864 9321 8949 969 637 1376 O ATOM 2021 NE2 GLN A 291 29.881 72.993-386.968 1.00 67.88 N ANISOU 2021 NE2 GLN A 291 9033 8596 8163 987 594 1208 N ATOM 2022 N SER A 292 26.634 74.424-390.477 1.00 72.44 N ANISOU 2022 N SER A 292 9204 9125 9196 482 888 1996 N ATOM 2023 CA SER A 292 25.767 75.546-390.127 1.00 71.53 C ANISOU 2023 CA SER A 292 8982 9064 9132 422 888 1955 C ATOM 2024 C SER A 292 25.407 75.490-388.651 1.00 71.87 C ANISOU 2024 C SER A 292 9048 9313 8946 644 886 1820 C ATOM 2025 O SER A 292 24.731 74.562-388.209 1.00 75.90 O ANISOU 2025 O SER A 292 9505 10065 9268 837 968 1928 O ATOM 2026 CB SER A 292 24.487 75.503-390.962 1.00 73.77 C ANISOU 2026 CB SER A 292 9069 9442 9520 319 1003 2226 C ATOM 2027 OG SER A 292 23.727 74.341-390.658 1.00 78.93 O ANISOU 2027 OG SER A 292 9646 10364 9981 501 1139 2430 O ATOM 2028 N VAL A 293 25.855 76.478-387.887 1.00 61.23 N ANISOU 2028 N VAL A 293 7783 7871 7610 637 789 1590 N ATOM 2029 CA VAL A 293 25.634 76.471-386.448 1.00 64.55 C ANISOU 2029 CA VAL A 293 8261 8424 7841 845 753 1434 C ATOM 2030 C VAL A 293 25.402 77.869-385.918 1.00 62.37 C ANISOU 2030 C VAL A 293 7999 8087 7610 806 702 1298 C ATOM 2031 O VAL A 293 25.691 78.846-386.594 1.00 62.76 O ANISOU 2031 O VAL A 293 8034 7980 7832 632 679 1282 O ATOM 2032 CB VAL A 293 26.835 75.856-385.694 1.00 62.35 C ANISOU 2032 CB VAL A 293 8138 8055 7496 942 660 1249 C ATOM 2033 CG1 VAL A 293 28.007 76.836-385.656 1.00 62.10 C ANISOU 2033 CG1 VAL A 293 8209 7765 7623 781 566 1087 C ATOM 2034 CG2 VAL A 293 26.433 75.462-384.283 1.00 62.59 C ANISOU 2034 CG2 VAL A 293 8212 8245 7325 1200 612 1113 C ATOM 2035 N VAL A 294 24.876 77.958-384.702 1.00 62.02 N ANISOU 2035 N VAL A 294 7992 8176 7396 1001 675 1190 N ATOM 2036 CA VAL A 294 24.719 79.234-384.020 1.00 64.59 C ANISOU 2036 CA VAL A 294 8371 8438 7731 1013 623 1048 C ATOM 2037 C VAL A 294 25.436 79.185-382.678 1.00 67.04 C ANISOU 2037 C VAL A 294 8861 8639 7973 1141 515 840 C ATOM 2038 O VAL A 294 25.168 78.303-381.865 1.00 73.44 O ANISOU 2038 O VAL A 294 9704 9580 8620 1348 479 785 O ATOM 2039 CB VAL A 294 23.239 79.575-383.797 1.00 71.78 C ANISOU 2039 CB VAL A 294 9157 9610 8508 1136 680 1109 C ATOM 2040 CG1 VAL A 294 23.088 80.542-382.633 1.00 78.22 C ANISOU 2040 CG1 VAL A 294 10090 10396 9235 1269 605 922 C ATOM 2041 CG2 VAL A 294 22.628 80.148-385.067 1.00 72.94 C ANISOU 2041 CG2 VAL A 294 9121 9789 8804 947 758 1262 C ATOM 2042 N LEU A 295 26.349 80.125-382.453 1.00 61.97 N ANISOU 2042 N LEU A 295 8325 7758 7462 1029 458 730 N ATOM 2043 CA LEU A 295 27.153 80.128-381.232 1.00 64.15 C ANISOU 2043 CA LEU A 295 8761 7875 7737 1096 356 554 C ATOM 2044 C LEU A 295 27.095 81.458-380.503 1.00 62.65 C ANISOU 2044 C LEU A 295 8665 7564 7575 1114 326 470 C ATOM 2045 O LEU A 295 26.664 82.461-381.061 1.00 61.50 O ANISOU 2045 O LEU A 295 8463 7445 7460 1061 383 530 O ATOM 2046 CB LEU A 295 28.608 79.777-381.543 1.00 61.44 C ANISOU 2046 CB LEU A 295 8463 7346 7536 943 320 521 C ATOM 2047 CG LEU A 295 28.860 78.386-382.129 1.00 65.09 C ANISOU 2047 CG LEU A 295 8871 7907 7955 960 334 574 C ATOM 2048 CD1 LEU A 295 30.354 78.124-382.253 1.00 60.15 C ANISOU 2048 CD1 LEU A 295 8297 7111 7445 836 279 499 C ATOM 2049 CD2 LEU A 295 28.183 77.314-381.283 1.00 63.07 C ANISOU 2049 CD2 LEU A 295 8620 7836 7509 1211 297 513 C ATOM 2050 N SER A 296 27.541 81.459-379.254 1.00 62.18 N ANISOU 2050 N SER A 296 8751 7362 7512 1198 230 326 N ATOM 2051 CA SER A 296 27.500 82.660-378.438 1.00 64.67 C ANISOU 2051 CA SER A 296 9187 7537 7849 1240 203 262 C ATOM 2052 C SER A 296 28.882 83.016-377.917 1.00 65.77 C ANISOU 2052 C SER A 296 9437 7382 8172 1103 155 208 C ATOM 2053 O SER A 296 29.712 82.134-377.687 1.00 64.23 O ANISOU 2053 O SER A 296 9253 7101 8050 1044 92 146 O ATOM 2054 CB SER A 296 26.537 82.477-377.263 1.00 62.92 C ANISOU 2054 CB SER A 296 9051 7406 7448 1500 123 150 C ATOM 2055 OG SER A 296 26.640 83.556-376.346 1.00 63.10 O ANISOU 2055 OG SER A 296 9233 7239 7503 1551 80 79 O ATOM 2056 N THR A 297 29.120 84.310-377.736 1.00 63.18 N ANISOU 2056 N THR A 297 9175 6918 7911 1066 190 239 N ATOM 2057 CA THR A 297 30.384 84.787-377.204 1.00 58.70 C ANISOU 2057 CA THR A 297 8698 6085 7521 938 170 235 C ATOM 2058 C THR A 297 30.300 84.950-375.693 1.00 63.21 C ANISOU 2058 C THR A 297 9444 6464 8108 1048 73 129 C ATOM 2059 O THR A 297 31.255 85.387-375.056 1.00 61.54 O ANISOU 2059 O THR A 297 9316 6000 8065 943 55 139 O ATOM 2060 CB THR A 297 30.788 86.138-377.825 1.00 58.19 C ANISOU 2060 CB THR A 297 8611 5980 7518 863 269 353 C ATOM 2061 OG1 THR A 297 29.981 87.191-377.276 1.00 59.71 O ANISOU 2061 OG1 THR A 297 8896 6174 7618 1025 293 349 O ATOM 2062 CG2 THR A 297 30.621 86.102-379.336 1.00 56.61 C ANISOU 2062 CG2 THR A 297 8248 5967 7295 796 332 429 C ATOM 2063 N LYS A 298 29.155 84.596-375.119 1.00 65.42 N ANISOU 2063 N LYS A 298 9775 6864 8217 1266 7 33 N ATOM 2064 CA LYS A 298 28.960 84.716-373.678 1.00 73.43 C ANISOU 2064 CA LYS A 298 10975 7693 9231 1413 -119 -95 C ATOM 2065 C LYS A 298 28.881 83.354-373.011 1.00 66.73 C ANISOU 2065 C LYS A 298 10142 6861 8352 1521 -279 -269 C ATOM 2066 O LYS A 298 28.000 82.557-373.321 1.00 64.71 O ANISOU 2066 O LYS A 298 9801 6889 7898 1685 -292 -303 O ATOM 2067 CB LYS A 298 27.695 85.517-373.367 1.00 80.58 C ANISOU 2067 CB LYS A 298 11957 8726 9932 1648 -103 -105 C ATOM 2068 CG LYS A 298 27.503 85.804-371.883 1.00 80.19 C ANISOU 2068 CG LYS A 298 12136 8451 9880 1820 -242 -233 C ATOM 2069 CD LYS A 298 26.442 86.870-371.656 1.00 86.75 C ANISOU 2069 CD LYS A 298 13058 9390 10513 2042 -201 -220 C ATOM 2070 CE LYS A 298 26.447 87.354-370.214 1.00 90.07 C ANISOU 2070 CE LYS A 298 13744 9511 10969 2191 -332 -319 C ATOM 2071 NZ LYS A 298 25.575 88.546-370.022 1.00 79.23 N ANISOU 2071 NZ LYS A 298 12479 8221 9405 2408 -274 -293 N ATOM 2072 N ARG A 299 29.801 83.099-372.085 1.00 76.76 N ANISOU 2072 N ARG A 299 11508 7836 9821 1440 -404 -376 N ATOM 2073 CA ARG A 299 29.862 81.812-371.404 1.00 80.60 C ANISOU 2073 CA ARG A 299 12004 8315 10305 1554 -588 -583 C ATOM 2074 C ARG A 299 28.507 81.439-370.827 1.00 84.74 C ANISOU 2074 C ARG A 299 12593 9041 10564 1907 -697 -713 C ATOM 2075 O ARG A 299 27.701 82.310-370.505 1.00 85.30 O ANISOU 2075 O ARG A 299 12765 9128 10516 2047 -677 -684 O ATOM 2076 CB ARG A 299 30.918 81.838-370.297 1.00 83.23 C ANISOU 2076 CB ARG A 299 12449 8250 10925 1425 -735 -703 C ATOM 2077 CG ARG A 299 32.322 82.138-370.796 1.00 85.35 C ANISOU 2077 CG ARG A 299 12626 8356 11446 1087 -631 -571 C ATOM 2078 CD ARG A 299 33.364 82.040-369.687 1.00 90.70 C ANISOU 2078 CD ARG A 299 13372 8654 12434 936 -779 -684 C ATOM 2079 NE ARG A 299 34.548 82.836-370.000 1.00 90.65 N ANISOU 2079 NE ARG A 299 13309 8479 12656 633 -640 -485 N ATOM 2080 CZ ARG A 299 35.583 82.398-370.710 1.00 87.14 C ANISOU 2080 CZ ARG A 299 12694 8107 12307 427 -580 -438 C ATOM 2081 NH1 ARG A 299 35.594 81.157-371.178 1.00 85.36 N ANISOU 2081 NH1 ARG A 299 12355 8097 11981 487 -645 -579 N ATOM 2082 NH2 ARG A 299 36.611 83.203-370.948 1.00 83.37 N ANISOU 2082 NH2 ARG A 299 12159 7509 12007 188 -452 -243 N ATOM 2083 N GLY A 300 28.257 80.139-370.706 1.00 81.49 N ANISOU 2083 N GLY A 300 12115 8812 10034 2082 -811 -856 N ATOM 2084 CA GLY A 300 27.018 79.663-370.126 1.00 80.72 C ANISOU 2084 CA GLY A 300 12060 8952 9659 2461 -929 -987 C ATOM 2085 C GLY A 300 25.907 79.504-371.143 1.00 82.32 C ANISOU 2085 C GLY A 300 12102 9597 9578 2585 -762 -820 C ATOM 2086 O GLY A 300 25.305 78.438-371.244 1.00 89.34 O ANISOU 2086 O GLY A 300 12894 10794 10258 2819 -801 -864 O ATOM 2087 N GLY A 301 25.634 80.556-371.908 1.00 20.00 N ATOM 2088 CA GLY A 301 24.540 80.565-372.863 1.00 20.00 C ATOM 2089 C GLY A 301 24.412 79.252-373.609 1.00 20.00 C ATOM 2090 O GLY A 301 25.391 78.664-374.053 1.00 80.03 O ANISOU 2090 O GLY A 301 11378 9904 9124 2376 -359 -379 O ATOM 2091 N LYS A 302 23.160 78.807-373.764 1.00 74.94 N ANISOU 2091 N LYS A 302 10666 9762 8044 2812 -336 -336 N ATOM 2092 CA LYS A 302 22.866 77.528-374.390 1.00 76.96 C ANISOU 2092 CA LYS A 302 10752 10327 8164 2915 -276 -241 C ATOM 2093 C LYS A 302 21.776 77.694-375.439 1.00 80.94 C ANISOU 2093 C LYS A 302 11051 11175 8529 2901 -78 13 C ATOM 2094 O LYS A 302 21.081 78.712-375.476 1.00 80.35 O ANISOU 2094 O LYS A 302 10965 11157 8407 2894 -26 56 O ATOM 2095 CB LYS A 302 22.419 76.520-373.328 1.00 80.10 C ANISOU 2095 CB LYS A 302 11197 10905 8331 3324 -462 -438 C ATOM 2096 CG LYS A 302 23.480 76.212-372.277 1.00 81.45 C ANISOU 2096 CG LYS A 302 11546 10731 8669 3343 -690 -719 C ATOM 2097 CD LYS A 302 22.866 75.702-370.974 1.00 91.82 C ANISOU 2097 CD LYS A 302 12963 12156 9768 3783 -934 -977 C ATOM 2098 CE LYS A 302 23.870 74.901-370.141 1.00 93.16 C ANISOU 2098 CE LYS A 302 13230 12078 10088 3843 -1170 -1261 C ATOM 2099 NZ LYS A 302 25.068 75.687-369.724 1.00 79.47 N ANISOU 2099 NZ LYS A 302 11645 9821 8730 3499 -1239 -1353 N ATOM 2100 N ASP A 303 21.643 76.696-376.303 1.00 90.06 N ANISOU 2100 N ASP A 303 12037 12553 9629 2894 34 183 N ATOM 2101 CA ASP A 303 20.531 76.649-377.238 1.00 96.78 C ANISOU 2101 CA ASP A 303 12666 13752 10354 2899 215 443 C ATOM 2102 C ASP A 303 19.317 76.141-376.483 1.00106.52 C ANISOU 2102 C ASP A 303 13842 15392 11239 3320 165 412 C ATOM 2103 O ASP A 303 19.337 76.050-375.257 1.00107.89 O ANISOU 2103 O ASP A 303 14175 15529 11290 3591 -27 164 O ATOM 2104 CB ASP A 303 20.850 75.725-378.415 1.00 99.68 C ANISOU 2104 CB ASP A 303 12888 14187 10798 2749 356 664 C ATOM 2105 CG ASP A 303 21.319 74.350-377.971 1.00 95.24 C ANISOU 2105 CG ASP A 303 12366 13699 10121 2979 271 573 C ATOM 2106 OD1 ASP A 303 21.529 74.156-376.756 1.00 93.94 O ANISOU 2106 OD1 ASP A 303 12345 13482 9867 3217 80 308 O ATOM 2107 OD2 ASP A 303 21.480 73.466-378.841 1.00 90.53 O ANISOU 2107 OD2 ASP A 303 11663 13206 9530 2935 386 758 O ATOM 2108 N ILE A 304 18.263 75.796-377.213 1.00 88.79 N ANISOU 2108 N ILE A 304 11361 13536 8838 3383 330 665 N ATOM 2109 CA ILE A 304 17.046 75.282-376.595 1.00 86.74 C ANISOU 2109 CA ILE A 304 11004 13743 8212 3807 307 677 C ATOM 2110 C ILE A 304 17.203 73.840-376.122 1.00 84.51 C ANISOU 2110 C ILE A 304 10729 13648 7734 4144 226 621 C ATOM 2111 O ILE A 304 16.222 73.122-375.975 1.00 89.03 O ANISOU 2111 O ILE A 304 11150 14686 7992 4493 266 730 O ATOM 2112 CB ILE A 304 15.850 75.370-377.555 1.00 91.31 C ANISOU 2112 CB ILE A 304 11288 14710 8697 3754 529 1002 C ATOM 2113 CG1 ILE A 304 16.315 75.163-378.997 1.00 93.96 C ANISOU 2113 CG1 ILE A 304 11489 14900 9313 3358 715 1272 C ATOM 2114 CG2 ILE A 304 15.155 76.720-377.416 1.00 99.43 C ANISOU 2114 CG2 ILE A 304 12299 15767 9713 3696 530 948 C ATOM 2115 CD1 ILE A 304 15.200 75.166-380.012 1.00 97.32 C ANISOU 2115 CD1 ILE A 304 11605 15660 9713 3257 932 1613 C ATOM 2116 N TYR A 305 18.441 73.421-375.886 1.00111.15 N ANISOU 2116 N TYR A 305 14264 16687 11282 4061 111 448 N ATOM 2117 CA TYR A 305 18.715 72.058-375.444 1.00116.93 C ANISOU 2117 CA TYR A 305 15007 17574 11847 4388 12 348 C ATOM 2118 C TYR A 305 19.738 72.047-374.317 1.00114.33 C ANISOU 2118 C TYR A 305 14922 16885 11635 4454 -262 -42 C ATOM 2119 O TYR A 305 20.255 70.993-373.951 1.00115.30 O ANISOU 2119 O TYR A 305 15074 17039 11697 4667 -379 -191 O ATOM 2120 CB TYR A 305 19.235 71.212-376.607 1.00120.28 C ANISOU 2120 CB TYR A 305 15313 18012 12376 4208 190 590 C ATOM 2121 CG TYR A 305 18.280 71.103-377.774 1.00129.20 C ANISOU 2121 CG TYR A 305 16192 19458 13439 4116 462 1004 C ATOM 2122 CD1 TYR A 305 17.686 69.889-378.100 1.00131.51 C ANISOU 2122 CD1 TYR A 305 16313 20175 13481 4407 584 1231 C ATOM 2123 CD2 TYR A 305 17.978 72.210-378.555 1.00133.02 C ANISOU 2123 CD2 TYR A 305 16600 19819 14124 3745 594 1172 C ATOM 2124 CE1 TYR A 305 16.815 69.784-379.169 1.00136.73 C ANISOU 2124 CE1 TYR A 305 16730 21103 14118 4294 842 1644 C ATOM 2125 CE2 TYR A 305 17.109 72.115-379.622 1.00138.24 C ANISOU 2125 CE2 TYR A 305 17013 20739 14772 3632 826 1541 C ATOM 2126 CZ TYR A 305 16.531 70.903-379.926 1.00139.76 C ANISOU 2126 CZ TYR A 305 17035 21327 14740 3888 955 1791 C ATOM 2127 OH TYR A 305 15.664 70.810-380.992 1.00140.56 O ANISOU 2127 OH TYR A 305 16876 21666 14863 3746 1196 2192 O ATOM 2128 N ASP A 306 20.030 73.225-373.775 1.00139.51 N ANISOU 2128 N ASP A 306 18275 19731 15000 4274 -363 -202 N ATOM 2129 CA ASP A 306 21.055 73.366-372.746 1.00142.81 C ANISOU 2129 CA ASP A 306 18919 19739 15603 4255 -608 -536 C ATOM 2130 C ASP A 306 22.409 72.823-373.203 1.00139.25 C ANISOU 2130 C ASP A 306 18480 19022 15406 3996 -600 -563 C ATOM 2131 O ASP A 306 23.216 72.368-372.390 1.00137.82 O ANISOU 2131 O ASP A 306 18413 18632 15319 4078 -810 -841 O ATOM 2132 CB ASP A 306 20.621 72.703-371.434 1.00150.55 C ANISOU 2132 CB ASP A 306 19988 20879 16336 4759 -875 -829 C ATOM 2133 CG ASP A 306 19.638 73.551-370.646 1.00160.55 C ANISOU 2133 CG ASP A 306 21345 22230 17427 4976 -970 -914 C ATOM 2134 OD1 ASP A 306 19.748 73.587-369.403 1.00162.32 O ANISOU 2134 OD1 ASP A 306 21759 22284 17633 5217 -1249 -1231 O ATOM 2135 OD2 ASP A 306 18.760 74.186-371.270 1.00161.11 O ANISOU 2135 OD2 ASP A 306 21298 22530 17388 4909 -778 -677 O ATOM 2136 N SER A 307 22.647 72.868-374.510 1.00127.06 N ANISOU 2136 N SER A 307 16811 17489 13976 3691 -370 -287 N ATOM 2137 CA SER A 307 23.953 72.536-375.060 1.00119.54 C ANISOU 2137 CA SER A 307 15875 16281 13265 3416 -347 -295 C ATOM 2138 C SER A 307 24.819 73.784-375.033 1.00116.32 C ANISOU 2138 C SER A 307 15586 15439 13171 3031 -362 -344 C ATOM 2139 O SER A 307 24.528 74.762-375.720 1.00116.36 O ANISOU 2139 O SER A 307 15554 15403 13256 2803 -216 -158 O ATOM 2140 CB SER A 307 23.826 72.021-376.495 1.00117.47 C ANISOU 2140 CB SER A 307 15444 16212 12979 3285 -110 23 C ATOM 2141 OG SER A 307 23.098 70.809-376.543 1.00121.59 O ANISOU 2141 OG SER A 307 15848 17144 13207 3652 -73 107 O ATOM 2142 N ASN A 308 25.877 73.752-374.230 1.00129.69 N ANISOU 2142 N ASN A 308 17409 16824 15045 2971 -540 -593 N ATOM 2143 CA ASN A 308 26.777 74.888-374.118 1.00124.39 C ANISOU 2143 CA ASN A 308 16841 15752 14668 2627 -549 -620 C ATOM 2144 C ASN A 308 27.305 75.333-375.478 1.00119.47 C ANISOU 2144 C ASN A 308 16130 15072 14192 2282 -346 -380 C ATOM 2145 O ASN A 308 28.199 74.703-376.041 1.00122.67 O ANISOU 2145 O ASN A 308 16487 15437 14684 2159 -322 -369 O ATOM 2146 CB ASN A 308 27.940 74.551-373.190 1.00125.63 C ANISOU 2146 CB ASN A 308 17098 15614 15021 2589 -753 -892 C ATOM 2147 CG ASN A 308 29.037 75.588-373.241 1.00128.91 C ANISOU 2147 CG ASN A 308 17580 15651 15750 2208 -723 -861 C ATOM 2148 OD1 ASN A 308 28.774 76.789-373.325 1.00125.27 O ANISOU 2148 OD1 ASN A 308 17172 15078 15347 2076 -637 -739 O ATOM 2149 ND2 ASN A 308 30.278 75.129-373.187 1.00124.43 N ANISOU 2149 ND2 ASN A 308 16995 14912 15372 2050 -790 -969 N ATOM 2150 N ILE A 309 26.751 76.426-375.998 1.00 67.24 N ANISOU 2150 N ILE A 309 9495 8460 7594 2150 -217 -210 N ATOM 2151 CA ILE A 309 27.135 76.934-377.308 1.00 66.95 C ANISOU 2151 CA ILE A 309 9372 8374 7692 1856 -52 -2 C ATOM 2152 C ILE A 309 28.067 78.140-377.202 1.00 63.10 C ANISOU 2152 C ILE A 309 8975 7560 7439 1599 -60 -27 C ATOM 2153 O ILE A 309 28.113 78.983-378.105 1.00 61.32 O ANISOU 2153 O ILE A 309 8699 7303 7298 1414 56 121 O ATOM 2154 CB ILE A 309 25.913 77.324-378.154 1.00 64.81 C ANISOU 2154 CB ILE A 309 8975 8348 7302 1872 99 211 C ATOM 2155 CG1 ILE A 309 25.069 78.367-377.420 1.00 71.53 C ANISOU 2155 CG1 ILE A 309 9890 9212 8076 1982 69 157 C ATOM 2156 CG2 ILE A 309 25.080 76.098-378.484 1.00 67.45 C ANISOU 2156 CG2 ILE A 309 9182 9027 7420 2090 154 316 C ATOM 2157 CD1 ILE A 309 23.991 79.000-378.274 1.00 70.46 C ANISOU 2157 CD1 ILE A 309 9613 9287 7872 1947 211 343 C ATOM 2158 N TYR A 310 28.800 78.235-376.095 1.00 63.43 N ANISOU 2158 N TYR A 310 9143 7364 7594 1600 -201 -212 N ATOM 2159 CA TYR A 310 29.845 79.243-375.988 1.00 62.18 C ANISOU 2159 CA TYR A 310 9052 6906 7668 1354 -193 -203 C ATOM 2160 C TYR A 310 30.995 78.835-376.897 1.00 61.29 C ANISOU 2160 C TYR A 310 8853 6756 7679 1142 -141 -143 C ATOM 2161 O TYR A 310 31.552 77.746-376.750 1.00 63.76 O ANISOU 2161 O TYR A 310 9139 7092 7994 1178 -218 -252 O ATOM 2162 CB TYR A 310 30.326 79.377-374.546 1.00 70.06 C ANISOU 2162 CB TYR A 310 10194 7639 8786 1392 -358 -395 C ATOM 2163 CG TYR A 310 31.579 80.214-374.404 1.00 70.57 C ANISOU 2163 CG TYR A 310 10300 7403 9111 1124 -339 -357 C ATOM 2164 CD1 TYR A 310 31.657 81.489-374.946 1.00 68.04 C ANISOU 2164 CD1 TYR A 310 9983 7029 8842 992 -203 -184 C ATOM 2165 CD2 TYR A 310 32.681 79.730-373.716 1.00 65.01 C ANISOU 2165 CD2 TYR A 310 9614 6489 8598 1020 -460 -495 C ATOM 2166 CE1 TYR A 310 32.800 82.253-374.812 1.00 69.19 C ANISOU 2166 CE1 TYR A 310 10150 6940 9199 781 -171 -120 C ATOM 2167 CE2 TYR A 310 33.825 80.485-373.578 1.00 70.83 C ANISOU 2167 CE2 TYR A 310 10360 6979 9572 772 -426 -427 C ATOM 2168 CZ TYR A 310 33.880 81.744-374.126 1.00 68.60 C ANISOU 2168 CZ TYR A 310 10083 6668 9313 662 -274 -225 C ATOM 2169 OH TYR A 310 35.025 82.497-373.985 1.00 63.23 O ANISOU 2169 OH TYR A 310 9398 5781 8846 445 -225 -129 O ATOM 2170 N ILE A 311 31.341 79.709-377.837 1.00 59.36 N ANISOU 2170 N ILE A 311 8563 6472 7520 954 -24 12 N ATOM 2171 CA ILE A 311 32.356 79.411-378.847 1.00 61.10 C ANISOU 2171 CA ILE A 311 8703 6688 7825 780 23 80 C ATOM 2172 C ILE A 311 33.528 78.565-378.350 1.00 59.39 C ANISOU 2172 C ILE A 311 8491 6375 7699 730 -77 -63 C ATOM 2173 O ILE A 311 33.664 77.403-378.723 1.00 61.80 O ANISOU 2173 O ILE A 311 8743 6815 7924 799 -99 -105 O ATOM 2174 CB ILE A 311 32.907 80.701-379.471 1.00 58.94 C ANISOU 2174 CB ILE A 311 8417 6308 7671 604 103 200 C ATOM 2175 CG1 ILE A 311 31.809 81.433-380.242 1.00 57.44 C ANISOU 2175 CG1 ILE A 311 8182 6244 7399 646 193 322 C ATOM 2176 CG2 ILE A 311 34.059 80.388-380.400 1.00 58.31 C ANISOU 2176 CG2 ILE A 311 8266 6226 7664 456 120 241 C ATOM 2177 CD1 ILE A 311 32.207 82.822-380.674 1.00 55.34 C ANISOU 2177 CD1 ILE A 311 7913 5890 7224 547 249 402 C ATOM 2178 N ASP A 312 34.368 79.151-377.507 1.00 60.32 N ANISOU 2178 N ASP A 312 8664 6267 7988 616 -134 -130 N ATOM 2179 CA ASP A 312 35.581 78.484-377.049 1.00 62.44 C ANISOU 2179 CA ASP A 312 8905 6434 8386 524 -229 -265 C ATOM 2180 C ASP A 312 35.382 77.029-376.617 1.00 62.03 C ANISOU 2180 C ASP A 312 8838 6496 8235 709 -352 -459 C ATOM 2181 O ASP A 312 36.250 76.184-376.835 1.00 64.53 O ANISOU 2181 O ASP A 312 9085 6859 8575 674 -396 -548 O ATOM 2182 CB ASP A 312 36.234 79.287-375.925 1.00 62.08 C ANISOU 2182 CB ASP A 312 8924 6108 8556 397 -287 -309 C ATOM 2183 CG ASP A 312 37.133 80.387-376.448 1.00 61.10 C ANISOU 2183 CG ASP A 312 8758 5902 8555 187 -172 -131 C ATOM 2184 OD1 ASP A 312 38.278 80.081-376.861 1.00 60.62 O ANISOU 2184 OD1 ASP A 312 8598 5864 8570 48 -167 -128 O ATOM 2185 OD2 ASP A 312 36.695 81.558-376.443 1.00 62.68 O ANISOU 2185 OD2 ASP A 312 9018 6044 8755 189 -89 0 O ATOM 2186 N ASP A 313 34.244 76.737-376.005 1.00 64.72 N ANISOU 2186 N ASP A 313 9239 6910 8443 938 -411 -532 N ATOM 2187 CA ASP A 313 33.967 75.385-375.540 1.00 68.99 C ANISOU 2187 CA ASP A 313 9763 7593 8856 1180 -537 -724 C ATOM 2188 C ASP A 313 33.485 74.492-376.674 1.00 65.47 C ANISOU 2188 C ASP A 313 9232 7451 8193 1310 -432 -609 C ATOM 2189 O ASP A 313 33.991 73.393-376.868 1.00 63.99 O ANISOU 2189 O ASP A 313 8990 7375 7948 1394 -478 -707 O ATOM 2190 CB ASP A 313 32.931 75.412-374.416 1.00 65.51 C ANISOU 2190 CB ASP A 313 9419 7142 8330 1422 -657 -852 C ATOM 2191 CG ASP A 313 33.486 75.990-373.122 1.00 68.33 C ANISOU 2191 CG ASP A 313 9879 7161 8924 1330 -811 -1014 C ATOM 2192 OD1 ASP A 313 34.725 76.029-372.968 1.00 68.02 O ANISOU 2192 OD1 ASP A 313 9803 6930 9112 1105 -849 -1068 O ATOM 2193 OD2 ASP A 313 32.681 76.398-372.255 1.00 70.76 O ANISOU 2193 OD2 ASP A 313 10300 7394 9190 1485 -897 -1081 O ATOM 2194 N PHE A 314 32.494 74.971-377.415 1.00 62.82 N ANISOU 2194 N PHE A 314 8881 7245 7743 1331 -293 -398 N ATOM 2195 CA PHE A 314 31.957 74.237-378.549 1.00 66.74 C ANISOU 2195 CA PHE A 314 9293 7996 8070 1420 -173 -235 C ATOM 2196 C PHE A 314 33.067 73.573-379.352 1.00 63.86 C ANISOU 2196 C PHE A 314 8881 7636 7747 1316 -154 -230 C ATOM 2197 O PHE A 314 33.035 72.371-379.590 1.00 65.87 O ANISOU 2197 O PHE A 314 9098 8072 7857 1496 -161 -261 O ATOM 2198 CB PHE A 314 31.139 75.174-379.441 1.00 64.97 C ANISOU 2198 CB PHE A 314 9035 7815 7836 1314 -22 6 C ATOM 2199 CG PHE A 314 30.657 74.541-380.716 1.00 63.42 C ANISOU 2199 CG PHE A 314 8745 7819 7534 1338 107 211 C ATOM 2200 CD1 PHE A 314 29.639 73.601-380.699 1.00 66.48 C ANISOU 2200 CD1 PHE A 314 9077 8472 7712 1590 144 275 C ATOM 2201 CD2 PHE A 314 31.207 74.904-381.935 1.00 62.33 C ANISOU 2201 CD2 PHE A 314 8573 7603 7507 1122 188 352 C ATOM 2202 CE1 PHE A 314 29.188 73.023-381.870 1.00 65.70 C ANISOU 2202 CE1 PHE A 314 8888 8535 7540 1597 279 504 C ATOM 2203 CE2 PHE A 314 30.760 74.331-383.111 1.00 63.05 C ANISOU 2203 CE2 PHE A 314 8591 7829 7535 1130 295 549 C ATOM 2204 CZ PHE A 314 29.747 73.387-383.078 1.00 65.44 C ANISOU 2204 CZ PHE A 314 8838 8375 7652 1353 351 640 C ATOM 2205 N PHE A 315 34.054 74.362-379.759 1.00 60.61 N ANISOU 2205 N PHE A 315 8472 7046 7512 1055 -130 -193 N ATOM 2206 CA PHE A 315 35.162 73.852-380.559 1.00 61.93 C ANISOU 2206 CA PHE A 315 8596 7227 7706 959 -119 -192 C ATOM 2207 C PHE A 315 36.131 73.056-379.703 1.00 62.45 C ANISOU 2207 C PHE A 315 8652 7263 7812 1010 -261 -444 C ATOM 2208 O PHE A 315 36.790 72.138-380.186 1.00 64.71 O ANISOU 2208 O PHE A 315 8899 7659 8029 1062 -275 -499 O ATOM 2209 CB PHE A 315 35.899 74.997-381.260 1.00 61.89 C ANISOU 2209 CB PHE A 315 8582 7081 7851 702 -59 -75 C ATOM 2210 CG PHE A 315 35.065 75.715-382.278 1.00 56.88 C ANISOU 2210 CG PHE A 315 7937 6479 7194 653 57 142 C ATOM 2211 CD1 PHE A 315 34.739 75.107-383.479 1.00 58.89 C ANISOU 2211 CD1 PHE A 315 8159 6858 7360 692 127 279 C ATOM 2212 CD2 PHE A 315 34.602 76.993-382.032 1.00 59.53 C ANISOU 2212 CD2 PHE A 315 8294 6716 7609 576 90 203 C ATOM 2213 CE1 PHE A 315 33.966 75.759-384.417 1.00 55.95 C ANISOU 2213 CE1 PHE A 315 7758 6492 7010 627 213 462 C ATOM 2214 CE2 PHE A 315 33.827 77.650-382.968 1.00 58.43 C ANISOU 2214 CE2 PHE A 315 8123 6617 7462 539 177 368 C ATOM 2215 CZ PHE A 315 33.511 77.033-384.162 1.00 56.00 C ANISOU 2215 CZ PHE A 315 7764 6415 7097 550 232 492 C ATOM 2216 N ALA A 316 36.209 73.419-378.428 1.00 63.97 N ANISOU 2216 N ALA A 316 8882 7300 8125 998 -376 -605 N ATOM 2217 CA ALA A 316 37.111 72.763-377.487 1.00 63.48 C ANISOU 2217 CA ALA A 316 8795 7166 8159 1019 -540 -874 C ATOM 2218 C ALA A 316 36.826 71.271-377.410 1.00 64.69 C ANISOU 2218 C ALA A 316 8919 7551 8111 1326 -617 -1031 C ATOM 2219 O ALA A 316 37.660 70.492-376.955 1.00 71.38 O ANISOU 2219 O ALA A 316 9715 8408 8997 1375 -747 -1265 O ATOM 2220 CB ALA A 316 36.986 73.392-376.109 1.00 68.73 C ANISOU 2220 CB ALA A 316 9523 7596 8996 983 -663 -1007 C ATOM 2221 N LYS A 317 35.640 70.883-377.862 1.00 70.30 N ANISOU 2221 N LYS A 317 9645 8465 8600 1544 -531 -896 N ATOM 2222 CA LYS A 317 35.204 69.499-377.790 1.00 71.61 C ANISOU 2222 CA LYS A 317 9782 8894 8532 1894 -579 -1001 C ATOM 2223 C LYS A 317 34.702 69.009-379.143 1.00 69.97 C ANISOU 2223 C LYS A 317 9547 8909 8130 1975 -393 -732 C ATOM 2224 O LYS A 317 33.499 68.912-379.361 1.00 65.57 O ANISOU 2224 O LYS A 317 8985 8511 7416 2134 -301 -563 O ATOM 2225 CB LYS A 317 34.099 69.362-376.745 1.00 69.83 C ANISOU 2225 CB LYS A 317 9595 8736 8203 2165 -680 -1110 C ATOM 2226 CG LYS A 317 34.434 70.007-375.408 1.00 72.47 C ANISOU 2226 CG LYS A 317 9987 8789 8758 2071 -867 -1344 C ATOM 2227 CD LYS A 317 33.188 70.199-374.556 1.00 71.61 C ANISOU 2227 CD LYS A 317 9947 8726 8537 2313 -943 -1389 C ATOM 2228 CE LYS A 317 32.171 71.087-375.264 1.00 72.77 C ANISOU 2228 CE LYS A 317 10110 8941 8598 2238 -742 -1072 C ATOM 2229 NZ LYS A 317 31.009 71.446-374.397 1.00 81.93 N ANISOU 2229 NZ LYS A 317 11338 10141 9650 2455 -818 -1119 N ATOM 2230 N GLY A 318 35.633 68.708-380.044 1.00 69.57 N ANISOU 2230 N GLY A 318 9473 8866 8094 1863 -341 -688 N ATOM 2231 CA GLY A 318 35.314 68.202-381.371 1.00 74.05 C ANISOU 2231 CA GLY A 318 10033 9593 8509 1924 -182 -438 C ATOM 2232 C GLY A 318 34.056 68.780-381.993 1.00 70.21 C ANISOU 2232 C GLY A 318 9546 9137 7992 1883 -28 -135 C ATOM 2233 O GLY A 318 33.326 68.091-382.711 1.00 65.98 O ANISOU 2233 O GLY A 318 8988 8790 7292 2044 91 66 O ATOM 2234 N GLY A 319 33.805 70.056-381.727 1.00 63.12 N ANISOU 2234 N GLY A 319 8665 8061 7257 1668 -25 -95 N ATOM 2235 CA GLY A 319 32.587 70.694-382.180 1.00 61.88 C ANISOU 2235 CA GLY A 319 8487 7941 7082 1630 99 147 C ATOM 2236 C GLY A 319 32.453 70.764-383.687 1.00 64.69 C ANISOU 2236 C GLY A 319 8817 8304 7460 1497 242 418 C ATOM 2237 O GLY A 319 31.344 70.740-384.215 1.00 64.52 O ANISOU 2237 O GLY A 319 8743 8396 7375 1540 358 640 O ATOM 2238 N SER A 320 33.578 70.850-384.387 1.00 84.30 N ANISOU 2238 N SER A 320 11327 10664 10038 1338 224 399 N ATOM 2239 CA SER A 320 33.542 71.048-385.831 1.00 85.02 C ANISOU 2239 CA SER A 320 11414 10704 10185 1198 320 627 C ATOM 2240 C SER A 320 34.737 70.425-386.541 1.00 85.58 C ANISOU 2240 C SER A 320 11528 10754 10235 1192 285 578 C ATOM 2241 O SER A 320 35.877 70.582-386.114 1.00 84.83 O ANISOU 2241 O SER A 320 11451 10592 10188 1132 185 378 O ATOM 2242 CB SER A 320 33.470 72.540-386.151 1.00 83.34 C ANISOU 2242 CB SER A 320 11192 10310 10163 946 326 686 C ATOM 2243 OG SER A 320 33.056 72.753-387.487 1.00 88.08 O ANISOU 2243 OG SER A 320 11768 10869 10828 840 404 907 O ATOM 2244 N GLU A 321 34.461 69.729-387.638 1.00 70.80 N ANISOU 2244 N GLU A 321 9669 8940 8292 1254 371 775 N ATOM 2245 CA GLU A 321 35.494 69.038-388.396 1.00 67.72 C ANISOU 2245 CA GLU A 321 9340 8548 7842 1296 342 744 C ATOM 2246 C GLU A 321 36.360 69.989-389.215 1.00 61.88 C ANISOU 2246 C GLU A 321 8633 7618 7260 1064 284 738 C ATOM 2247 O GLU A 321 37.452 69.618-389.643 1.00 64.81 O ANISOU 2247 O GLU A 321 9052 7991 7580 1090 222 645 O ATOM 2248 CB GLU A 321 34.865 68.006-389.339 1.00 76.11 C ANISOU 2248 CB GLU A 321 10425 9709 8783 1451 460 991 C ATOM 2249 CG GLU A 321 34.620 66.626-388.736 1.00 93.80 C ANISOU 2249 CG GLU A 321 12659 12204 10778 1790 493 947 C ATOM 2250 CD GLU A 321 34.104 65.614-389.762 1.00112.26 C ANISOU 2250 CD GLU A 321 15027 14635 12991 1951 632 1235 C ATOM 2251 OE1 GLU A 321 33.392 66.022-390.707 1.00119.56 O ANISOU 2251 OE1 GLU A 321 15940 15441 14047 1788 729 1520 O ATOM 2252 OE2 GLU A 321 34.407 64.408-389.622 1.00104.78 O ANISOU 2252 OE2 GLU A 321 14112 13877 11822 2246 642 1178 O ATOM 2253 N TYR A 322 35.880 71.209-389.435 1.00 57.60 N ANISOU 2253 N TYR A 322 8059 6940 6886 869 296 824 N ATOM 2254 CA TYR A 322 36.500 72.102-390.418 1.00 59.31 C ANISOU 2254 CA TYR A 322 8300 6998 7237 697 241 851 C ATOM 2255 C TYR A 322 37.258 73.292-389.835 1.00 57.91 C ANISOU 2255 C TYR A 322 8096 6746 7161 564 163 696 C ATOM 2256 O TYR A 322 38.395 73.572-390.228 1.00 58.24 O ANISOU 2256 O TYR A 322 8157 6758 7213 521 86 612 O ATOM 2257 CB TYR A 322 35.447 72.607-391.405 1.00 57.46 C ANISOU 2257 CB TYR A 322 8042 6660 7132 591 300 1076 C ATOM 2258 CG TYR A 322 34.748 71.500-392.151 1.00 58.66 C ANISOU 2258 CG TYR A 322 8212 6857 7218 690 393 1289 C ATOM 2259 CD1 TYR A 322 35.035 71.250-393.487 1.00 59.97 C ANISOU 2259 CD1 TYR A 322 8448 6899 7440 657 370 1408 C ATOM 2260 CD2 TYR A 322 33.809 70.696-391.518 1.00 64.48 C ANISOU 2260 CD2 TYR A 322 8901 7766 7831 840 503 1382 C ATOM 2261 CE1 TYR A 322 34.399 70.228-394.175 1.00 66.68 C ANISOU 2261 CE1 TYR A 322 9322 7769 8245 745 470 1642 C ATOM 2262 CE2 TYR A 322 33.166 69.673-392.194 1.00 65.84 C ANISOU 2262 CE2 TYR A 322 9079 8005 7933 950 613 1621 C ATOM 2263 CZ TYR A 322 33.464 69.442-393.523 1.00 66.93 C ANISOU 2263 CZ TYR A 322 9290 7991 8149 889 606 1763 C ATOM 2264 OH TYR A 322 32.824 68.424-394.199 1.00 64.66 O ANISOU 2264 OH TYR A 322 9015 7747 7807 993 731 2037 O ATOM 2265 N ILE A 323 36.621 74.001-388.912 1.00 61.00 N ANISOU 2265 N ILE A 323 8442 7122 7614 517 188 674 N ATOM 2266 CA ILE A 323 37.177 75.245-388.402 1.00 53.93 C ANISOU 2266 CA ILE A 323 7524 6141 6826 395 141 583 C ATOM 2267 C ILE A 323 37.384 75.204-386.899 1.00 56.74 C ANISOU 2267 C ILE A 323 7870 6517 7173 422 119 432 C ATOM 2268 O ILE A 323 37.090 74.206-386.245 1.00 59.09 O ANISOU 2268 O ILE A 323 8174 6904 7375 553 117 365 O ATOM 2269 CB ILE A 323 36.266 76.425-388.729 1.00 54.14 C ANISOU 2269 CB ILE A 323 7518 6087 6965 305 177 692 C ATOM 2270 CG1 ILE A 323 35.002 76.365-387.876 1.00 55.97 C ANISOU 2270 CG1 ILE A 323 7726 6373 7168 363 243 725 C ATOM 2271 CG2 ILE A 323 35.906 76.424-390.203 1.00 55.37 C ANISOU 2271 CG2 ILE A 323 7672 6192 7173 269 178 832 C ATOM 2272 CD1 ILE A 323 33.998 77.435-388.209 1.00 57.32 C ANISOU 2272 CD1 ILE A 323 7847 6503 7429 295 283 823 C ATOM 2273 N PHE A 324 37.891 76.305-386.361 1.00 63.30 N ANISOU 2273 N PHE A 324 8684 7259 8109 312 94 382 N ATOM 2274 CA PHE A 324 38.156 76.427-384.940 1.00 62.10 C ANISOU 2274 CA PHE A 324 8530 7065 8002 302 61 252 C ATOM 2275 C PHE A 324 38.155 77.913-384.646 1.00 62.22 C ANISOU 2275 C PHE A 324 8539 6966 8135 193 84 304 C ATOM 2276 O PHE A 324 38.763 78.683-385.384 1.00 52.93 O ANISOU 2276 O PHE A 324 7338 5774 6999 121 88 366 O ATOM 2277 CB PHE A 324 39.520 75.826-384.607 1.00 54.60 C ANISOU 2277 CB PHE A 324 7549 6145 7051 281 -11 107 C ATOM 2278 CG PHE A 324 39.722 75.534-383.146 1.00 66.02 C ANISOU 2278 CG PHE A 324 8986 7542 8558 289 -74 -59 C ATOM 2279 CD1 PHE A 324 39.449 74.281-382.631 1.00 68.72 C ANISOU 2279 CD1 PHE A 324 9334 7971 8805 450 -129 -197 C ATOM 2280 CD2 PHE A 324 40.193 76.507-382.291 1.00 63.40 C ANISOU 2280 CD2 PHE A 324 8637 7071 8383 153 -87 -77 C ATOM 2281 CE1 PHE A 324 39.636 74.009-381.290 1.00 67.54 C ANISOU 2281 CE1 PHE A 324 9174 7757 8731 471 -225 -385 C ATOM 2282 CE2 PHE A 324 40.379 76.240-380.950 1.00 67.42 C ANISOU 2282 CE2 PHE A 324 9142 7486 8987 145 -167 -234 C ATOM 2283 CZ PHE A 324 40.100 74.990-380.450 1.00 67.80 C ANISOU 2283 CZ PHE A 324 9197 7609 8955 302 -250 -406 C ATOM 2284 N ALA A 325 37.465 78.326-383.585 1.00 55.14 N ANISOU 2284 N ALA A 325 7673 6004 7275 213 93 277 N ATOM 2285 CA ALA A 325 37.338 79.750-383.282 1.00 55.33 C ANISOU 2285 CA ALA A 325 7709 5926 7387 148 129 340 C ATOM 2286 C ALA A 325 37.493 80.077-381.801 1.00 56.77 C ANISOU 2286 C ALA A 325 7935 5979 7655 129 99 259 C ATOM 2287 O ALA A 325 37.620 79.186-380.960 1.00 60.28 O ANISOU 2287 O ALA A 325 8396 6403 8103 168 28 126 O ATOM 2288 CB ALA A 325 36.020 80.280-383.799 1.00 61.63 C ANISOU 2288 CB ALA A 325 8511 6763 8142 206 185 438 C ATOM 2289 N THR A 326 37.478 81.368-381.492 1.00 57.36 N ANISOU 2289 N THR A 326 8034 5959 7803 86 143 333 N ATOM 2290 CA THR A 326 37.600 81.830-380.117 1.00 57.06 C ANISOU 2290 CA THR A 326 8058 5753 7868 62 121 290 C ATOM 2291 C THR A 326 36.841 83.144-379.925 1.00 57.50 C ANISOU 2291 C THR A 326 8175 5756 7918 116 188 385 C ATOM 2292 O THR A 326 36.945 84.059-380.741 1.00 55.41 O ANISOU 2292 O THR A 326 7871 5547 7637 110 254 495 O ATOM 2293 CB THR A 326 39.075 81.998-379.717 1.00 57.04 C ANISOU 2293 CB THR A 326 8003 5660 8010 -90 107 292 C ATOM 2294 OG1 THR A 326 39.160 82.436-378.357 1.00 60.64 O ANISOU 2294 OG1 THR A 326 8525 5908 8607 -134 82 268 O ATOM 2295 CG2 THR A 326 39.761 83.008-380.620 1.00 57.10 C ANISOU 2295 CG2 THR A 326 7945 5734 8018 -142 188 445 C ATOM 2296 N ALA A 327 36.064 83.224-378.851 1.00 80.65 N ANISOU 2296 N ALA A 327 11204 8594 10846 201 155 324 N ATOM 2297 CA ALA A 327 35.243 84.398-378.587 1.00 82.17 C ANISOU 2297 CA ALA A 327 11468 8753 10999 293 212 391 C ATOM 2298 C ALA A 327 36.103 85.635-378.387 1.00 79.81 C ANISOU 2298 C ALA A 327 11182 8333 10809 217 281 513 C ATOM 2299 O ALA A 327 35.631 86.761-378.511 1.00 84.13 O ANISOU 2299 O ALA A 327 11763 8897 11307 305 350 595 O ATOM 2300 CB ALA A 327 34.362 84.165-377.371 1.00 85.16 C ANISOU 2300 CB ALA A 327 11966 9047 11343 421 140 283 C ATOM 2301 N GLN A 328 37.372 85.414-378.081 1.00 60.35 N ANISOU 2301 N GLN A 328 8676 5770 8485 68 266 528 N ATOM 2302 CA GLN A 328 38.288 86.499-377.769 1.00 61.29 C ANISOU 2302 CA GLN A 328 8788 5783 8718 -8 344 678 C ATOM 2303 C GLN A 328 38.455 87.476-378.926 1.00 58.99 C ANISOU 2303 C GLN A 328 8421 5660 8333 52 439 810 C ATOM 2304 O GLN A 328 38.748 87.080-380.054 1.00 58.27 O ANISOU 2304 O GLN A 328 8228 5734 8177 39 424 795 O ATOM 2305 CB GLN A 328 39.641 85.932-377.362 1.00 61.37 C ANISOU 2305 CB GLN A 328 8716 5707 8894 -196 310 671 C ATOM 2306 CG GLN A 328 40.553 86.934-376.721 1.00 63.48 C ANISOU 2306 CG GLN A 328 8975 5830 9316 -295 394 848 C ATOM 2307 CD GLN A 328 41.102 86.437-375.406 1.00 69.43 C ANISOU 2307 CD GLN A 328 9753 6326 10303 -452 316 787 C ATOM 2308 OE1 GLN A 328 40.402 85.772-374.645 1.00 68.14 O ANISOU 2308 OE1 GLN A 328 9692 6029 10169 -408 197 612 O ATOM 2309 NE2 GLN A 328 42.359 86.761-375.125 1.00 70.57 N ANISOU 2309 NE2 GLN A 328 9789 6405 10619 -627 373 927 N ATOM 2310 N ASN A 329 38.261 88.756-378.629 1.00 64.42 N ANISOU 2310 N ASN A 329 9166 6303 9008 146 524 929 N ATOM 2311 CA ASN A 329 38.385 89.822-379.620 1.00 64.06 C ANISOU 2311 CA ASN A 329 9051 6424 8864 259 600 1035 C ATOM 2312 C ASN A 329 37.433 89.681-380.794 1.00 62.84 C ANISOU 2312 C ASN A 329 8851 6449 8575 364 558 940 C ATOM 2313 O ASN A 329 37.621 90.317-381.831 1.00 63.17 O ANISOU 2313 O ASN A 329 8810 6639 8553 446 573 976 O ATOM 2314 CB ASN A 329 39.823 89.940-380.127 1.00 70.86 C ANISOU 2314 CB ASN A 329 9782 7370 9771 172 633 1144 C ATOM 2315 CG ASN A 329 40.696 90.780-379.217 1.00 74.79 C ANISOU 2315 CG ASN A 329 10288 7750 10377 130 735 1334 C ATOM 2316 OD1 ASN A 329 40.198 91.491-378.345 1.00 75.18 O ANISOU 2316 OD1 ASN A 329 10459 7654 10453 201 791 1399 O ATOM 2317 ND2 ASN A 329 42.008 90.700-379.415 1.00 72.67 N ANISOU 2317 ND2 ASN A 329 9888 7554 10168 22 765 1436 N ATOM 2318 N TRP A 330 36.420 88.841-380.626 1.00 57.14 N ANISOU 2318 N TRP A 330 8175 5717 7819 368 499 820 N ATOM 2319 CA TRP A 330 35.343 88.728-381.597 1.00 54.46 C ANISOU 2319 CA TRP A 330 7786 5528 7377 451 474 756 C ATOM 2320 C TRP A 330 34.627 90.072-381.633 1.00 54.95 C ANISOU 2320 C TRP A 330 7872 5645 7363 622 527 784 C ATOM 2321 O TRP A 330 34.052 90.493-380.629 1.00 59.57 O ANISOU 2321 O TRP A 330 8567 6150 7915 710 555 780 O ATOM 2322 CB TRP A 330 34.375 87.622-381.171 1.00 56.53 C ANISOU 2322 CB TRP A 330 8089 5788 7601 450 423 657 C ATOM 2323 CG TRP A 330 33.309 87.290-382.174 1.00 58.65 C ANISOU 2323 CG TRP A 330 8277 6217 7791 494 409 626 C ATOM 2324 CD1 TRP A 330 32.293 88.095-382.588 1.00 63.51 C ANISOU 2324 CD1 TRP A 330 8858 6935 8339 605 434 624 C ATOM 2325 CD2 TRP A 330 33.142 86.049-382.870 1.00 59.42 C ANISOU 2325 CD2 TRP A 330 8307 6389 7880 427 371 605 C ATOM 2326 NE1 TRP A 330 31.512 87.442-383.506 1.00 60.20 N ANISOU 2326 NE1 TRP A 330 8337 6637 7898 579 414 613 N ATOM 2327 CE2 TRP A 330 32.012 86.180-383.696 1.00 55.33 C ANISOU 2327 CE2 TRP A 330 7710 5999 7314 476 383 617 C ATOM 2328 CE3 TRP A 330 33.848 84.840-382.879 1.00 66.40 C ANISOU 2328 CE3 TRP A 330 9186 7250 8793 340 331 580 C ATOM 2329 CZ2 TRP A 330 31.563 85.155-384.524 1.00 59.70 C ANISOU 2329 CZ2 TRP A 330 8185 6638 7862 426 370 641 C ATOM 2330 CZ3 TRP A 330 33.403 83.820-383.702 1.00 70.03 C ANISOU 2330 CZ3 TRP A 330 9584 7810 9213 326 317 588 C ATOM 2331 CH2 TRP A 330 32.271 83.984-384.513 1.00 68.15 C ANISOU 2331 CH2 TRP A 330 9274 7679 8942 362 343 635 C ATOM 2332 N PRO A 331 34.673 90.765-382.783 1.00 55.38 N ANISOU 2332 N PRO A 331 7827 5833 7382 695 526 795 N ATOM 2333 CA PRO A 331 34.047 92.088-382.873 1.00 54.45 C ANISOU 2333 CA PRO A 331 7713 5796 7180 892 567 795 C ATOM 2334 C PRO A 331 32.574 92.026-382.499 1.00 55.42 C ANISOU 2334 C PRO A 331 7876 5956 7225 973 561 710 C ATOM 2335 O PRO A 331 31.856 91.158-382.994 1.00 58.37 O ANISOU 2335 O PRO A 331 8185 6394 7600 902 513 647 O ATOM 2336 CB PRO A 331 34.201 92.447-384.354 1.00 56.23 C ANISOU 2336 CB PRO A 331 7797 6167 7400 940 509 757 C ATOM 2337 CG PRO A 331 35.373 91.659-384.814 1.00 53.18 C ANISOU 2337 CG PRO A 331 7368 5754 7085 793 470 794 C ATOM 2338 CD PRO A 331 35.305 90.369-384.053 1.00 53.11 C ANISOU 2338 CD PRO A 331 7424 5631 7124 628 468 785 C ATOM 2339 N GLU A 332 32.128 92.923-381.629 1.00 63.31 N ANISOU 2339 N GLU A 332 8979 6930 8146 1133 616 721 N ATOM 2340 CA GLU A 332 30.724 92.950-381.248 1.00 64.71 C ANISOU 2340 CA GLU A 332 9191 7183 8214 1248 607 631 C ATOM 2341 C GLU A 332 29.848 93.242-382.462 1.00 69.35 C ANISOU 2341 C GLU A 332 9612 7977 8759 1307 573 547 C ATOM 2342 O GLU A 332 30.163 94.117-383.271 1.00 70.22 O ANISOU 2342 O GLU A 332 9639 8166 8876 1390 569 537 O ATOM 2343 CB GLU A 332 30.483 93.982-380.149 1.00 67.83 C ANISOU 2343 CB GLU A 332 9742 7513 8516 1444 667 656 C ATOM 2344 CG GLU A 332 30.957 93.539-378.775 1.00 84.69 C ANISOU 2344 CG GLU A 332 12055 9408 10715 1378 671 710 C ATOM 2345 CD GLU A 332 30.673 94.572-377.693 1.00100.67 C ANISOU 2345 CD GLU A 332 14260 11335 12655 1581 724 747 C ATOM 2346 OE1 GLU A 332 30.804 95.786-377.967 1.00 96.64 O ANISOU 2346 OE1 GLU A 332 13743 10900 12075 1747 801 809 O ATOM 2347 OE2 GLU A 332 30.323 94.167-376.564 1.00108.57 O ANISOU 2347 OE2 GLU A 332 15417 12183 13652 1601 681 710 O ATOM 2348 N GLY A 333 28.758 92.489-382.590 1.00 73.46 N ANISOU 2348 N GLY A 333 10074 8593 9245 1270 543 486 N ATOM 2349 CA GLY A 333 27.824 92.662-383.685 1.00 72.28 C ANISOU 2349 CA GLY A 333 9744 8625 9093 1286 510 417 C ATOM 2350 C GLY A 333 28.456 92.507-385.053 1.00 71.57 C ANISOU 2350 C GLY A 333 9519 8528 9146 1157 452 424 C ATOM 2351 O GLY A 333 27.900 92.957-386.054 1.00 75.76 O ANISOU 2351 O GLY A 333 9898 9169 9717 1183 403 353 O ATOM 2352 N PHE A 334 29.623 91.874-385.102 1.00 54.48 N ANISOU 2352 N PHE A 334 7405 6233 7063 1026 442 495 N ATOM 2353 CA PHE A 334 30.295 91.647-386.370 1.00 54.44 C ANISOU 2353 CA PHE A 334 7298 6215 7173 924 371 496 C ATOM 2354 C PHE A 334 29.413 90.813-387.272 1.00 53.85 C ANISOU 2354 C PHE A 334 7095 6191 7175 799 325 483 C ATOM 2355 O PHE A 334 28.805 89.841-386.830 1.00 55.03 O ANISOU 2355 O PHE A 334 7258 6356 7296 726 363 526 O ATOM 2356 CB PHE A 334 31.624 90.919-386.167 1.00 54.20 C ANISOU 2356 CB PHE A 334 7341 6063 7189 805 371 571 C ATOM 2357 CG PHE A 334 32.304 90.523-387.452 1.00 54.50 C ANISOU 2357 CG PHE A 334 7294 6093 7320 716 285 566 C ATOM 2358 CD1 PHE A 334 33.333 91.285-387.969 1.00 57.68 C ANISOU 2358 CD1 PHE A 334 7675 6514 7728 799 243 561 C ATOM 2359 CD2 PHE A 334 31.911 89.392-388.143 1.00 53.31 C ANISOU 2359 CD2 PHE A 334 7090 5927 7238 575 244 576 C ATOM 2360 CE1 PHE A 334 33.955 90.926-389.150 1.00 53.36 C ANISOU 2360 CE1 PHE A 334 7065 5963 7248 750 139 538 C ATOM 2361 CE2 PHE A 334 32.530 89.031-389.324 1.00 52.36 C ANISOU 2361 CE2 PHE A 334 6918 5775 7202 508 153 570 C ATOM 2362 CZ PHE A 334 33.551 89.799-389.827 1.00 52.87 C ANISOU 2362 CZ PHE A 334 6972 5850 7267 599 89 537 C ATOM 2363 N SER A 335 29.345 91.199-388.539 1.00 57.20 N ANISOU 2363 N SER A 335 7389 6643 7701 787 238 427 N ATOM 2364 CA SER A 335 28.711 90.378-389.558 1.00 57.72 C ANISOU 2364 CA SER A 335 7330 6706 7896 631 187 446 C ATOM 2365 C SER A 335 29.496 90.560-390.839 1.00 56.32 C ANISOU 2365 C SER A 335 7098 6449 7851 598 60 401 C ATOM 2366 O SER A 335 29.866 91.679-391.188 1.00 57.28 O ANISOU 2366 O SER A 335 7191 6604 7969 746 -10 299 O ATOM 2367 CB SER A 335 27.252 90.784-389.760 1.00 59.74 C ANISOU 2367 CB SER A 335 7440 7095 8164 659 194 396 C ATOM 2368 OG SER A 335 26.458 90.406-388.648 1.00 59.93 O ANISOU 2368 OG SER A 335 7510 7215 8044 697 298 443 O ATOM 2369 N GLY A 336 29.771 89.462-391.532 1.00 56.13 N ANISOU 2369 N GLY A 336 7069 6330 7927 437 22 472 N ATOM 2370 CA GLY A 336 30.536 89.537-392.759 1.00 54.63 C ANISOU 2370 CA GLY A 336 6851 6049 7856 419 -122 422 C ATOM 2371 C GLY A 336 30.962 88.193-393.308 1.00 54.42 C ANISOU 2371 C GLY A 336 6869 5910 7897 264 -141 521 C ATOM 2372 O GLY A 336 30.570 87.141-392.801 1.00 55.02 O ANISOU 2372 O GLY A 336 6978 5993 7935 167 -37 636 O ATOM 2373 N ILE A 337 31.765 88.236-394.363 1.00 56.47 N ANISOU 2373 N ILE A 337 7135 6082 8240 274 -285 468 N ATOM 2374 CA ILE A 337 32.283 87.034-394.992 1.00 58.29 C ANISOU 2374 CA ILE A 337 7427 6201 8519 163 -322 548 C ATOM 2375 C ILE A 337 33.770 86.960-394.742 1.00 56.20 C ANISOU 2375 C ILE A 337 7272 5958 8122 253 -347 522 C ATOM 2376 O ILE A 337 34.520 87.834-395.170 1.00 54.65 O ANISOU 2376 O ILE A 337 7068 5791 7907 390 -460 419 O ATOM 2377 CB ILE A 337 32.067 87.060-396.508 1.00 56.76 C ANISOU 2377 CB ILE A 337 7165 5867 8536 109 -497 500 C ATOM 2378 CG1 ILE A 337 30.576 87.172-396.834 1.00 57.88 C ANISOU 2378 CG1 ILE A 337 7155 5989 8849 -9 -477 533 C ATOM 2379 CG2 ILE A 337 32.685 85.829-397.152 1.00 56.64 C ANISOU 2379 CG2 ILE A 337 7246 5726 8548 26 -537 590 C ATOM 2380 CD1 ILE A 337 29.725 86.238-396.036 1.00 59.88 C ANISOU 2380 CD1 ILE A 337 7397 6315 9038 -120 -282 709 C ATOM 2381 N LEU A 338 34.199 85.921-394.044 1.00 56.55 N ANISOU 2381 N LEU A 338 7404 6014 8067 194 -247 610 N ATOM 2382 CA LEU A 338 35.619 85.718-393.804 1.00 57.41 C ANISOU 2382 CA LEU A 338 7592 6159 8061 253 -267 589 C ATOM 2383 C LEU A 338 36.244 84.843-394.889 1.00 56.16 C ANISOU 2383 C LEU A 338 7483 5925 7930 230 -378 592 C ATOM 2384 O LEU A 338 35.704 83.799-395.255 1.00 56.99 O ANISOU 2384 O LEU A 338 7611 5952 8091 132 -355 674 O ATOM 2385 CB LEU A 338 35.857 85.122-392.416 1.00 56.03 C ANISOU 2385 CB LEU A 338 7476 6038 7774 217 -125 643 C ATOM 2386 CG LEU A 338 35.565 86.070-391.253 1.00 53.97 C ANISOU 2386 CG LEU A 338 7207 5833 7468 271 -33 634 C ATOM 2387 CD1 LEU A 338 35.894 85.411-389.923 1.00 59.30 C ANISOU 2387 CD1 LEU A 338 7949 6516 8068 229 67 666 C ATOM 2388 CD2 LEU A 338 36.349 87.360-391.420 1.00 52.66 C ANISOU 2388 CD2 LEU A 338 7013 5724 7273 403 -84 584 C ATOM 2389 N THR A 339 37.383 85.286-395.406 1.00 54.30 N ANISOU 2389 N THR A 339 7264 5728 7639 346 -498 512 N ATOM 2390 CA THR A 339 38.066 84.569-396.464 1.00 55.05 C ANISOU 2390 CA THR A 339 7422 5760 7734 368 -630 490 C ATOM 2391 C THR A 339 39.381 84.019-395.957 1.00 56.00 C ANISOU 2391 C THR A 339 7599 6001 7678 417 -600 488 C ATOM 2392 O THR A 339 40.346 84.760-395.779 1.00 55.43 O ANISOU 2392 O THR A 339 7496 6058 7505 536 -635 434 O ATOM 2393 CB THR A 339 38.348 85.472-397.652 1.00 55.24 C ANISOU 2393 CB THR A 339 7416 5750 7823 504 -841 369 C ATOM 2394 OG1 THR A 339 37.134 85.689-398.376 1.00 55.71 O ANISOU 2394 OG1 THR A 339 7419 5656 8094 424 -906 359 O ATOM 2395 CG2 THR A 339 39.368 84.829-398.568 1.00 56.09 C ANISOU 2395 CG2 THR A 339 7611 5832 7867 583 -991 325 C ATOM 2396 N LEU A 340 39.407 82.713-395.715 1.00 54.88 N ANISOU 2396 N LEU A 340 7523 5836 7493 336 -529 549 N ATOM 2397 CA LEU A 340 40.606 82.048-395.232 1.00 53.09 C ANISOU 2397 CA LEU A 340 7333 5730 7108 374 -507 525 C ATOM 2398 C LEU A 340 41.591 81.915-396.374 1.00 53.07 C ANISOU 2398 C LEU A 340 7379 5752 7034 498 -676 454 C ATOM 2399 O LEU A 340 41.213 81.602-397.504 1.00 53.26 O ANISOU 2399 O LEU A 340 7462 5636 7137 512 -789 455 O ATOM 2400 CB LEU A 340 40.270 80.678-394.653 1.00 53.68 C ANISOU 2400 CB LEU A 340 7459 5792 7146 295 -396 583 C ATOM 2401 CG LEU A 340 39.206 80.681-393.559 1.00 52.20 C ANISOU 2401 CG LEU A 340 7236 5589 7010 207 -252 642 C ATOM 2402 CD1 LEU A 340 39.109 79.314-392.911 1.00 53.02 C ANISOU 2402 CD1 LEU A 340 7382 5731 7032 193 -167 665 C ATOM 2403 CD2 LEU A 340 39.521 81.743-392.526 1.00 51.53 C ANISOU 2403 CD2 LEU A 340 7093 5570 6915 208 -202 607 C ATOM 2404 N SER A 341 42.853 82.200-396.073 1.00 59.80 N ANISOU 2404 N SER A 341 8198 6782 7742 592 -700 399 N ATOM 2405 CA SER A 341 43.946 82.106-397.041 1.00 61.32 C ANISOU 2405 CA SER A 341 8425 7062 7811 753 -866 317 C ATOM 2406 C SER A 341 45.287 82.066-396.313 1.00 59.80 C ANISOU 2406 C SER A 341 8166 7114 7442 804 -821 293 C ATOM 2407 O SER A 341 45.335 82.069-395.082 1.00 58.28 O ANISOU 2407 O SER A 341 7908 6976 7260 693 -668 342 O ATOM 2408 CB SER A 341 43.907 83.254-398.064 1.00 62.26 C ANISOU 2408 CB SER A 341 8522 7156 7979 901 -1043 246 C ATOM 2409 OG SER A 341 43.844 84.527-397.438 1.00 66.84 O ANISOU 2409 OG SER A 341 8990 7835 8571 939 -982 256 O ATOM 2410 N GLY A 342 46.373 82.008-397.075 1.00 65.62 N ANISOU 2410 N GLY A 342 8915 7995 8024 975 -963 217 N ATOM 2411 CA GLY A 342 47.692 81.864-396.488 1.00 67.30 C ANISOU 2411 CA GLY A 342 9040 8470 8061 1022 -925 199 C ATOM 2412 C GLY A 342 47.866 80.516-395.812 1.00 63.45 C ANISOU 2412 C GLY A 342 8580 7994 7533 906 -829 188 C ATOM 2413 O GLY A 342 48.928 80.217-395.264 1.00 67.30 O ANISOU 2413 O GLY A 342 8981 8692 7898 914 -797 156 O ATOM 2414 N GLY A 343 46.815 79.703-395.841 1.00 54.70 N ANISOU 2414 N GLY A 343 7576 6680 6527 809 -784 215 N ATOM 2415 CA GLY A 343 46.892 78.358-395.308 1.00 55.39 C ANISOU 2415 CA GLY A 343 7701 6788 6555 757 -712 188 C ATOM 2416 C GLY A 343 48.097 77.663-395.894 1.00 55.31 C ANISOU 2416 C GLY A 343 7719 6964 6333 913 -820 87 C ATOM 2417 O GLY A 343 48.390 77.820-397.076 1.00 54.21 O ANISOU 2417 O GLY A 343 7658 6822 6118 1067 -971 53 O ATOM 2418 N LEU A 344 48.803 76.891-395.079 1.00 53.69 N ANISOU 2418 N LEU A 344 7448 6921 6030 890 -760 18 N ATOM 2419 CA LEU A 344 50.058 76.333-395.536 1.00 54.40 C ANISOU 2419 CA LEU A 344 7530 7246 5895 1049 -858 -95 C ATOM 2420 C LEU A 344 50.529 75.141-394.730 1.00 59.89 C ANISOU 2420 C LEU A 344 8180 8075 6500 1030 -799 -197 C ATOM 2421 O LEU A 344 51.198 75.308-393.721 1.00 57.07 O ANISOU 2421 O LEU A 344 7654 7868 6161 931 -740 -237 O ATOM 2422 CB LEU A 344 51.130 77.418-395.488 1.00 54.97 C ANISOU 2422 CB LEU A 344 7447 7546 5894 1098 -901 -99 C ATOM 2423 CG LEU A 344 52.373 77.202-396.347 1.00 57.53 C ANISOU 2423 CG LEU A 344 7768 8134 5958 1326 -1050 -202 C ATOM 2424 CD1 LEU A 344 53.355 76.264-395.674 1.00 57.39 C ANISOU 2424 CD1 LEU A 344 7643 8365 5797 1321 -1013 -310 C ATOM 2425 CD2 LEU A 344 51.969 76.681-397.713 1.00 61.59 C ANISOU 2425 CD2 LEU A 344 8506 8494 6400 1500 -1201 -242 C ATOM 2426 N SER A 345 50.203 73.937-395.180 1.00 77.01 N ANISOU 2426 N SER A 345 10492 10192 8577 1134 -819 -239 N ATOM 2427 CA SER A 345 50.847 72.762-394.624 1.00 72.47 C ANISOU 2427 CA SER A 345 9876 9805 7856 1199 -803 -382 C ATOM 2428 C SER A 345 52.140 72.616-395.367 1.00 72.22 C ANISOU 2428 C SER A 345 9833 10027 7580 1388 -931 -492 C ATOM 2429 O SER A 345 52.148 72.516-396.589 1.00 80.34 O ANISOU 2429 O SER A 345 11021 11009 8494 1560 -1041 -478 O ATOM 2430 CB SER A 345 50.041 71.502-394.886 1.00 72.68 C ANISOU 2430 CB SER A 345 10066 9719 7831 1300 -770 -374 C ATOM 2431 OG SER A 345 50.578 70.800-395.995 1.00 74.76 O ANISOU 2431 OG SER A 345 10468 10065 7871 1531 -875 -428 O ATOM 2432 N SER A 346 53.248 72.607-394.656 1.00 61.92 N ANISOU 2432 N SER A 346 8504 8830 6192 1553 -1426 1152 N ATOM 2433 CA SER A 346 54.484 72.368-395.349 1.00 65.01 C ANISOU 2433 CA SER A 346 8992 9328 6380 1589 -1369 1056 C ATOM 2434 C SER A 346 54.962 71.020-394.903 1.00 60.92 C ANISOU 2434 C SER A 346 8453 8724 5970 1470 -1138 1107 C ATOM 2435 O SER A 346 55.283 70.833-393.730 1.00 55.01 O ANISOU 2435 O SER A 346 7713 7969 5218 1426 -976 1283 O ATOM 2436 CB SER A 346 55.521 73.454-395.053 1.00 68.61 C ANISOU 2436 CB SER A 346 9563 10008 6497 1727 -1353 1151 C ATOM 2437 OG SER A 346 55.977 73.372-393.716 1.00 69.91 O ANISOU 2437 OG SER A 346 9739 10184 6641 1687 -1159 1387 O ATOM 2438 N ASN A 347 54.924 70.066-395.832 1.00 71.43 N ANISOU 2438 N ASN A 347 9751 9972 7419 1411 -1139 955 N ATOM 2439 CA ASN A 347 55.731 68.854-395.745 1.00 69.46 C ANISOU 2439 CA ASN A 347 9505 9705 7181 1336 -940 968 C ATOM 2440 C ASN A 347 57.036 69.237-396.398 1.00 68.78 C ANISOU 2440 C ASN A 347 9526 9797 6809 1448 -929 904 C ATOM 2441 O ASN A 347 58.080 68.644-396.135 1.00 68.58 O ANISOU 2441 O ASN A 347 9527 9848 6683 1430 -755 967 O ATOM 2442 CB ASN A 347 55.083 67.715-396.523 1.00 58.50 C ANISOU 2442 CB ASN A 347 8029 8160 6040 1246 -952 849 C ATOM 2443 CG ASN A 347 53.584 67.878-396.637 1.00 59.47 C ANISOU 2443 CG ASN A 347 8042 8148 6407 1205 -1096 828 C ATOM 2444 OD1 ASN A 347 52.853 67.677-395.668 1.00 58.50 O ANISOU 2444 OD1 ASN A 347 7847 7956 6424 1152 -1029 950 O ATOM 2445 ND2 ASN A 347 53.114 68.243-397.827 1.00 65.82 N ANISOU 2445 ND2 ASN A 347 8828 8912 7268 1232 -1301 673 N ATOM 2446 N ALA A 348 56.935 70.245-397.264 1.00 86.65 N ANISOU 2446 N ALA A 348 11847 12134 8941 1571 -1128 775 N ATOM 2447 CA ALA A 348 58.074 70.835-397.944 1.00 91.01 C ANISOU 2447 CA ALA A 348 12516 12880 9185 1725 -1149 693 C ATOM 2448 C ALA A 348 59.324 70.480-397.185 1.00 85.56 C ANISOU 2448 C ALA A 348 11850 12327 8331 1724 -908 862 C ATOM 2449 O ALA A 348 60.174 69.738-397.681 1.00 88.20 O ANISOU 2449 O ALA A 348 12202 12704 8607 1736 -801 806 O ATOM 2450 CB ALA A 348 57.915 72.353-398.031 1.00 99.00 C ANISOU 2450 CB ALA A 348 13594 14032 9989 1870 -1331 679 C ATOM 2451 N GLU A 349 59.425 70.995-395.966 1.00 64.27 N ANISOU 2451 N GLU A 349 9147 9695 5578 1704 -826 1079 N ATOM 2452 CA GLU A 349 60.531 70.608-395.107 1.00 74.32 C ANISOU 2452 CA GLU A 349 10420 11072 6747 1662 -602 1269 C ATOM 2453 C GLU A 349 60.107 70.158-393.724 1.00 70.40 C ANISOU 2453 C GLU A 349 9860 10438 6452 1504 -489 1456 C ATOM 2454 O GLU A 349 60.214 70.896-392.744 1.00 70.08 O ANISOU 2454 O GLU A 349 9836 10445 6345 1512 -457 1647 O ATOM 2455 CB GLU A 349 61.637 71.672-395.044 1.00 84.61 C ANISOU 2455 CB GLU A 349 11799 12648 7701 1821 -568 1376 C ATOM 2456 CG GLU A 349 61.279 73.025-395.618 1.00 86.02 C ANISOU 2456 CG GLU A 349 12049 12939 7696 1995 -773 1290 C ATOM 2457 CD GLU A 349 60.634 73.920-394.597 1.00 85.68 C ANISOU 2457 CD GLU A 349 11992 12881 7681 1984 -821 1475 C ATOM 2458 OE1 GLU A 349 59.797 73.404-393.820 1.00 77.61 O ANISOU 2458 OE1 GLU A 349 10900 11651 6937 1835 -794 1547 O ATOM 2459 OE2 GLU A 349 60.977 75.126-394.569 1.00 90.70 O ANISOU 2459 OE2 GLU A 349 12688 13721 8052 2140 -882 1551 O ATOM 2460 N VAL A 350 59.627 68.922-393.674 1.00 51.50 N ANISOU 2460 N VAL A 350 7398 7870 4301 1369 -430 1398 N ATOM 2461 CA VAL A 350 59.461 68.211-392.431 1.00 59.35 C ANISOU 2461 CA VAL A 350 8345 8743 5463 1221 -296 1540 C ATOM 2462 C VAL A 350 60.749 67.442-392.177 1.00 49.89 C ANISOU 2462 C VAL A 350 7140 7645 4171 1160 -116 1617 C ATOM 2463 O VAL A 350 61.031 66.456-392.861 1.00 49.98 O ANISOU 2463 O VAL A 350 7119 7652 4218 1132 -69 1506 O ATOM 2464 CB VAL A 350 58.301 67.229-392.529 1.00 48.49 C ANISOU 2464 CB VAL A 350 6893 7159 4371 1125 -319 1436 C ATOM 2465 CG1 VAL A 350 58.428 66.144-391.473 1.00 48.83 C ANISOU 2465 CG1 VAL A 350 6900 7108 4547 982 -156 1529 C ATOM 2466 CG2 VAL A 350 56.992 67.961-392.393 1.00 58.06 C ANISOU 2466 CG2 VAL A 350 8083 8268 5709 1161 -467 1426 C ATOM 2467 N THR A 351 61.537 67.899-391.210 1.00 20.00 N ATOM 2468 CA THR A 351 62.795 67.252-390.862 1.00 20.00 C ATOM 2469 C THR A 351 62.562 65.840-390.334 1.00 20.00 C ATOM 2470 O THR A 351 61.532 65.546-389.753 1.00 61.96 O ANISOU 2470 O THR A 351 8591 9024 5928 821 197 1880 O ATOM 2471 CB THR A 351 63.561 68.088-389.820 1.00 20.00 C ATOM 2472 OG1 THR A 351 64.727 67.374-389.394 1.00 20.00 O ATOM 2473 CG2 THR A 351 62.747 68.222-388.542 1.00 20.00 C ATOM 2474 N ALA A 352 63.551 64.972-390.551 1.00 55.06 N ANISOU 2474 N ALA A 352 7680 8450 4789 846 345 1909 N ATOM 2475 CA ALA A 352 63.462 63.598-390.061 1.00 55.56 C ANISOU 2475 CA ALA A 352 7684 8400 5026 689 426 1888 C ATOM 2476 C ALA A 352 62.960 63.583-388.627 1.00 57.44 C ANISOU 2476 C ALA A 352 7934 8468 5424 560 440 1997 C ATOM 2477 O ALA A 352 62.024 62.863-388.294 1.00 58.49 O ANISOU 2477 O ALA A 352 8054 8423 5746 493 424 1913 O ATOM 2478 CB ALA A 352 64.813 62.900-390.157 1.00 59.63 C ANISOU 2478 CB ALA A 352 8140 9089 5426 645 553 1954 C ATOM 2479 N GLY A 353 63.587 64.394-387.782 1.00 77.19 N ANISOU 2479 N GLY A 353 10460 11023 7846 536 472 2192 N ATOM 2480 CA GLY A 353 63.209 64.483-386.385 1.00 80.19 C ANISOU 2480 CA GLY A 353 10867 11221 8379 419 480 2310 C ATOM 2481 C GLY A 353 61.743 64.807-386.202 1.00 71.89 C ANISOU 2481 C GLY A 353 9860 9973 7482 471 379 2224 C ATOM 2482 O GLY A 353 61.090 64.252-385.323 1.00 64.83 O ANISOU 2482 O GLY A 353 8977 8883 6773 382 386 2206 O ATOM 2483 N ASP A 354 61.233 65.711-387.034 1.00 92.70 N ANISOU 2483 N ASP A 354 12517 12668 10036 624 279 2167 N ATOM 2484 CA ASP A 354 59.829 66.099-386.985 1.00 90.46 C ANISOU 2484 CA ASP A 354 12250 12230 9891 686 171 2096 C ATOM 2485 C ASP A 354 58.954 64.859-387.105 1.00 91.40 C ANISOU 2485 C ASP A 354 12321 12204 10204 625 183 1938 C ATOM 2486 O ASP A 354 57.812 64.851-386.647 1.00 98.78 O ANISOU 2486 O ASP A 354 13254 12978 11301 637 140 1910 O ATOM 2487 CB ASP A 354 59.492 67.095-388.098 1.00 88.63 C ANISOU 2487 CB ASP A 354 12030 12112 9535 848 43 2023 C ATOM 2488 CG ASP A 354 60.442 68.278-388.134 1.00101.32 C ANISOU 2488 CG ASP A 354 13684 13915 10899 939 39 2167 C ATOM 2489 OD1 ASP A 354 59.966 69.429-388.044 1.00 94.41 O ANISOU 2489 OD1 ASP A 354 12843 13056 9971 1043 -60 2227 O ATOM 2490 OD2 ASP A 354 61.667 68.062-388.254 1.00108.96 O ANISOU 2490 OD2 ASP A 354 14644 15038 11719 916 139 2232 O ATOM 2491 N LEU A 355 59.492 63.813-387.727 1.00 51.06 N ANISOU 2491 N LEU A 355 7165 7166 5069 575 247 1848 N ATOM 2492 CA LEU A 355 58.797 62.533-387.805 1.00 48.50 C ANISOU 2492 CA LEU A 355 6788 6734 4905 515 279 1725 C ATOM 2493 C LEU A 355 58.908 61.779-386.486 1.00 55.09 C ANISOU 2493 C LEU A 355 7637 7454 5839 387 364 1779 C ATOM 2494 O LEU A 355 57.927 61.221-385.987 1.00 54.49 O ANISOU 2494 O LEU A 355 7555 7229 5919 371 366 1718 O ATOM 2495 CB LEU A 355 59.365 61.671-388.933 1.00 47.46 C ANISOU 2495 CB LEU A 355 6603 6722 4708 516 317 1625 C ATOM 2496 CG LEU A 355 58.791 61.847-390.336 1.00 47.67 C ANISOU 2496 CG LEU A 355 6602 6770 4741 621 222 1494 C ATOM 2497 CD1 LEU A 355 59.556 60.992-391.335 1.00 46.71 C ANISOU 2497 CD1 LEU A 355 6442 6755 4549 624 275 1420 C ATOM 2498 CD2 LEU A 355 57.319 61.482-390.336 1.00 51.54 C ANISOU 2498 CD2 LEU A 355 7042 7102 5440 622 172 1423 C ATOM 2499 N MET A 356 60.112 61.762-385.929 1.00 63.58 N ANISOU 2499 N MET A 356 8729 8606 6823 298 432 1893 N ATOM 2500 CA MET A 356 60.371 61.039-384.695 1.00 63.38 C ANISOU 2500 CA MET A 356 8721 8471 6891 155 493 1937 C ATOM 2501 C MET A 356 59.602 61.643-383.524 1.00 66.76 C ANISOU 2501 C MET A 356 9224 8690 7450 155 453 1999 C ATOM 2502 O MET A 356 59.124 60.917-382.658 1.00 67.42 O ANISOU 2502 O MET A 356 9335 8614 7668 90 470 1944 O ATOM 2503 CB MET A 356 61.872 60.984-384.417 1.00 62.67 C ANISOU 2503 CB MET A 356 8610 8519 6684 50 561 2069 C ATOM 2504 CG MET A 356 62.639 60.210-385.482 1.00 60.89 C ANISOU 2504 CG MET A 356 8304 8491 6340 56 614 2005 C ATOM 2505 SD MET A 356 64.404 60.584-385.571 1.00 75.86 S ANISOU 2505 SD MET A 356 10151 10632 8041 15 689 2187 S ATOM 2506 CE MET A 356 64.956 60.100-383.936 1.00 62.70 C ANISOU 2506 CE MET A 356 8481 8849 6495 -212 727 2317 C ATOM 2507 N GLU A 357 59.474 62.966-383.499 1.00 69.88 N ANISOU 2507 N GLU A 357 9660 9093 7800 244 396 2108 N ATOM 2508 CA GLU A 357 58.634 63.618-382.500 1.00 69.19 C ANISOU 2508 CA GLU A 357 9640 8807 7841 278 351 2171 C ATOM 2509 C GLU A 357 57.237 63.037-382.573 1.00 69.30 C ANISOU 2509 C GLU A 357 9637 8691 8002 344 324 2014 C ATOM 2510 O GLU A 357 56.590 62.820-381.552 1.00 70.91 O ANISOU 2510 O GLU A 357 9892 8702 8348 334 330 2005 O ATOM 2511 CB GLU A 357 58.556 65.129-382.734 1.00 82.28 C ANISOU 2511 CB GLU A 357 11324 10531 9406 401 281 2298 C ATOM 2512 CG GLU A 357 59.592 65.957-381.983 1.00 92.85 C ANISOU 2512 CG GLU A 357 12707 11903 10667 348 310 2529 C ATOM 2513 CD GLU A 357 59.262 67.443-381.991 1.00 92.07 C ANISOU 2513 CD GLU A 357 12645 11838 10500 488 235 2664 C ATOM 2514 OE1 GLU A 357 58.057 67.784-382.064 1.00 75.20 O ANISOU 2514 OE1 GLU A 357 10517 9605 8452 597 156 2594 O ATOM 2515 OE2 GLU A 357 60.203 68.265-381.920 1.00 96.15 O ANISOU 2515 OE2 GLU A 357 13172 12493 10868 496 257 2850 O ATOM 2516 N ALA A 358 56.777 62.796-383.795 1.00 56.42 N ANISOU 2516 N ALA A 358 7932 7166 6338 419 295 1896 N ATOM 2517 CA ALA A 358 55.436 62.273-384.024 1.00 54.06 C ANISOU 2517 CA ALA A 358 7585 6781 6176 487 275 1773 C ATOM 2518 C ALA A 358 55.323 60.835-383.543 1.00 49.83 C ANISOU 2518 C ALA A 358 7038 6176 5719 406 360 1676 C ATOM 2519 O ALA A 358 54.514 60.532-382.668 1.00 52.99 O ANISOU 2519 O ALA A 358 7470 6422 6241 429 375 1645 O ATOM 2520 CB ALA A 358 55.069 62.372-385.497 1.00 52.20 C ANISOU 2520 CB ALA A 358 7265 6668 5900 564 214 1689 C ATOM 2521 N TRP A 359 56.134 59.952-384.116 1.00 50.60 N ANISOU 2521 N TRP A 359 7093 6397 5735 328 414 1626 N ATOM 2522 CA TRP A 359 56.118 58.545-383.738 1.00 53.98 C ANISOU 2522 CA TRP A 359 7505 6798 6207 254 487 1534 C ATOM 2523 C TRP A 359 56.086 58.364-382.222 1.00 53.45 C ANISOU 2523 C TRP A 359 7531 6558 6220 190 505 1549 C ATOM 2524 O TRP A 359 55.430 57.461-381.707 1.00 49.61 O ANISOU 2524 O TRP A 359 7054 5986 5810 198 538 1448 O ATOM 2525 CB TRP A 359 57.337 57.829-384.311 1.00 52.70 C ANISOU 2525 CB TRP A 359 7298 6800 5924 161 538 1529 C ATOM 2526 CG TRP A 359 57.179 57.373-385.722 1.00 52.83 C ANISOU 2526 CG TRP A 359 7224 6944 5905 221 543 1458 C ATOM 2527 CD1 TRP A 359 57.935 57.747-386.795 1.00 55.44 C ANISOU 2527 CD1 TRP A 359 7524 7421 6121 246 527 1479 C ATOM 2528 CD2 TRP A 359 56.213 56.442-386.216 1.00 52.77 C ANISOU 2528 CD2 TRP A 359 7145 6923 5982 269 566 1361 C ATOM 2529 NE1 TRP A 359 57.496 57.105-387.930 1.00 57.79 N ANISOU 2529 NE1 TRP A 359 7745 7768 6445 298 529 1393 N ATOM 2530 CE2 TRP A 359 56.440 56.300-387.600 1.00 55.45 C ANISOU 2530 CE2 TRP A 359 7414 7380 6275 306 555 1335 C ATOM 2531 CE3 TRP A 359 55.174 55.721-385.625 1.00 52.84 C ANISOU 2531 CE3 TRP A 359 7143 6835 6099 295 598 1300 C ATOM 2532 CZ2 TRP A 359 55.666 55.466-388.396 1.00 52.96 C ANISOU 2532 CZ2 TRP A 359 7010 7076 6038 349 574 1271 C ATOM 2533 CZ3 TRP A 359 54.408 54.894-386.418 1.00 52.84 C ANISOU 2533 CZ3 TRP A 359 7046 6878 6153 350 628 1242 C ATOM 2534 CH2 TRP A 359 54.658 54.773-387.787 1.00 52.32 C ANISOU 2534 CH2 TRP A 359 6903 6918 6059 367 615 1238 C ATOM 2535 N ASP A 360 56.797 59.234-381.517 1.00 58.71 N ANISOU 2535 N ASP A 360 8269 7171 6867 133 482 1677 N ATOM 2536 CA ASP A 360 56.928 59.134-380.069 1.00 59.48 C ANISOU 2536 CA ASP A 360 8466 7077 7057 49 484 1705 C ATOM 2537 C ASP A 360 55.581 59.039-379.363 1.00 59.96 C ANISOU 2537 C ASP A 360 8582 6942 7258 158 470 1621 C ATOM 2538 O ASP A 360 55.500 58.567-378.233 1.00 64.06 O ANISOU 2538 O ASP A 360 9188 7290 7862 107 475 1571 O ATOM 2539 CB ASP A 360 57.727 60.323-379.517 1.00 62.77 C ANISOU 2539 CB ASP A 360 8939 7456 7453 -3 455 1898 C ATOM 2540 CG ASP A 360 59.224 60.176-379.733 1.00 63.00 C ANISOU 2540 CG ASP A 360 8926 7648 7364 -145 491 1993 C ATOM 2541 OD1 ASP A 360 59.634 59.303-380.528 1.00 62.04 O ANISOU 2541 OD1 ASP A 360 8723 7692 7158 -175 530 1909 O ATOM 2542 OD2 ASP A 360 59.990 60.935-379.103 1.00 66.91 O ANISOU 2542 OD2 ASP A 360 9457 8110 7854 -219 484 2169 O ATOM 2543 N PHE A 361 54.525 59.486-380.030 1.00 55.77 N ANISOU 2543 N PHE A 361 7997 6439 6753 310 447 1602 N ATOM 2544 CA PHE A 361 53.202 59.501-379.426 1.00 60.80 C ANISOU 2544 CA PHE A 361 8665 6920 7518 441 441 1547 C ATOM 2545 C PHE A 361 52.712 58.100-379.049 1.00 66.79 C ANISOU 2545 C PHE A 361 9425 7639 8314 446 503 1385 C ATOM 2546 O PHE A 361 51.687 57.957-378.378 1.00 68.28 O ANISOU 2546 O PHE A 361 9653 7695 8597 561 515 1325 O ATOM 2547 CB PHE A 361 52.202 60.189-380.361 1.00 60.58 C ANISOU 2547 CB PHE A 361 8540 6968 7510 590 399 1568 C ATOM 2548 CG PHE A 361 52.213 61.691-380.266 1.00 68.76 C ANISOU 2548 CG PHE A 361 9608 7973 8543 649 322 1715 C ATOM 2549 CD1 PHE A 361 51.061 62.385-379.924 1.00 63.81 C ANISOU 2549 CD1 PHE A 361 8978 7246 8019 798 280 1750 C ATOM 2550 CD2 PHE A 361 53.375 62.412-380.509 1.00 70.08 C ANISOU 2550 CD2 PHE A 361 9801 8232 8594 568 294 1829 C ATOM 2551 CE1 PHE A 361 51.064 63.770-379.833 1.00 62.68 C ANISOU 2551 CE1 PHE A 361 8861 7092 7864 862 203 1894 C ATOM 2552 CE2 PHE A 361 53.386 63.796-380.418 1.00 64.36 C ANISOU 2552 CE2 PHE A 361 9106 7503 7845 637 225 1974 C ATOM 2553 CZ PHE A 361 52.227 64.474-380.079 1.00 65.20 C ANISOU 2553 CZ PHE A 361 9212 7506 8054 781 174 2006 C ATOM 2554 N PHE A 362 53.449 57.073-379.467 1.00 51.06 N ANISOU 2554 N PHE A 362 7390 5776 6235 336 545 1320 N ATOM 2555 CA PHE A 362 53.046 55.690-379.226 1.00 51.88 C ANISOU 2555 CA PHE A 362 7485 5889 6337 347 603 1170 C ATOM 2556 C PHE A 362 53.930 54.961-378.212 1.00 51.30 C ANISOU 2556 C PHE A 362 7508 5738 6244 199 602 1108 C ATOM 2557 O PHE A 362 53.680 53.799-377.894 1.00 51.93 O ANISOU 2557 O PHE A 362 7599 5829 6303 206 637 970 O ATOM 2558 CB PHE A 362 53.075 54.893-380.531 1.00 47.23 C ANISOU 2558 CB PHE A 362 6757 5520 5668 350 648 1134 C ATOM 2559 CG PHE A 362 52.236 55.474-381.633 1.00 46.90 C ANISOU 2559 CG PHE A 362 6605 5552 5661 468 634 1182 C ATOM 2560 CD1 PHE A 362 50.871 55.255-381.668 1.00 50.14 C ANISOU 2560 CD1 PHE A 362 6959 5935 6158 614 661 1143 C ATOM 2561 CD2 PHE A 362 52.820 56.207-382.658 1.00 45.10 C ANISOU 2561 CD2 PHE A 362 6325 5431 5380 436 589 1263 C ATOM 2562 CE1 PHE A 362 50.101 55.778-382.689 1.00 45.58 C ANISOU 2562 CE1 PHE A 362 6261 5423 5633 700 632 1196 C ATOM 2563 CE2 PHE A 362 52.057 56.730-383.683 1.00 45.67 C ANISOU 2563 CE2 PHE A 362 6300 5557 5495 531 550 1289 C ATOM 2564 CZ PHE A 362 50.697 56.516-383.699 1.00 45.64 C ANISOU 2564 CZ PHE A 362 6228 5515 5599 650 566 1261 C ATOM 2565 N ALA A 363 54.965 55.628-377.710 1.00 49.13 N ANISOU 2565 N ALA A 363 7297 5397 5974 65 557 1215 N ATOM 2566 CA ALA A 363 56.021 54.937-376.969 1.00 57.15 C ANISOU 2566 CA ALA A 363 8365 6380 6970 -119 543 1182 C ATOM 2567 C ALA A 363 55.742 54.666-375.488 1.00 72.59 C ANISOU 2567 C ALA A 363 10471 8073 9036 -143 501 1086 C ATOM 2568 O ALA A 363 56.668 54.660-374.680 1.00 84.63 O ANISOU 2568 O ALA A 363 12062 9493 10600 -316 453 1121 O ATOM 2569 CB ALA A 363 57.342 55.671-377.129 1.00 56.53 C ANISOU 2569 CB ALA A 363 8260 6370 6847 -267 521 1359 C ATOM 2570 N ASP A 364 54.480 54.424-375.139 1.00 65.34 N ANISOU 2570 N ASP A 364 9605 7049 8174 30 519 964 N ATOM 2571 CA ASP A 364 54.113 54.083-373.760 1.00 78.54 C ANISOU 2571 CA ASP A 364 11436 8465 9942 45 480 833 C ATOM 2572 C ASP A 364 52.795 53.321-373.651 1.00 72.33 C ANISOU 2572 C ASP A 364 10664 7674 9143 255 531 656 C ATOM 2573 O ASP A 364 51.724 53.875-373.877 1.00 74.64 O ANISOU 2573 O ASP A 364 10930 7946 9482 446 565 688 O ATOM 2574 CB ASP A 364 54.059 55.331-372.881 1.00 91.32 C ANISOU 2574 CB ASP A 364 13173 9819 11706 53 423 955 C ATOM 2575 CG ASP A 364 53.538 56.540-373.622 1.00103.55 C ANISOU 2575 CG ASP A 364 14646 11434 13265 185 442 1120 C ATOM 2576 OD1 ASP A 364 52.959 56.369-374.714 1.00 93.42 O ANISOU 2576 OD1 ASP A 364 13234 10357 11904 295 493 1103 O ATOM 2577 OD2 ASP A 364 53.714 57.669-373.118 1.00114.03 O ANISOU 2577 OD2 ASP A 364 16040 12607 14681 175 399 1271 O ATOM 2578 N ARG A 365 52.885 52.050-373.279 1.00115.07 N ANISOU 2578 N ARG A 365 16114 13121 14488 224 534 474 N ATOM 2579 CA ARG A 365 51.710 51.194-373.157 1.00119.53 C ANISOU 2579 CA ARG A 365 16690 13720 15006 432 596 303 C ATOM 2580 C ARG A 365 50.660 51.780-372.210 1.00121.94 C ANISOU 2580 C ARG A 365 17126 13772 15433 622 588 254 C ATOM 2581 O ARG A 365 49.481 51.424-372.282 1.00119.29 O ANISOU 2581 O ARG A 365 16765 13486 15072 849 661 173 O ATOM 2582 CB ARG A 365 52.131 49.802-372.681 1.00133.42 C ANISOU 2582 CB ARG A 365 18502 15529 16661 355 574 106 C ATOM 2583 CG ARG A 365 53.236 49.170-373.510 1.00131.81 C ANISOU 2583 CG ARG A 365 18170 15570 16340 168 576 157 C ATOM 2584 CD ARG A 365 54.353 48.674-372.613 1.00133.15 C ANISOU 2584 CD ARG A 365 18437 15643 16512 -55 470 72 C ATOM 2585 NE ARG A 365 53.842 48.206-371.330 1.00132.49 N ANISOU 2585 NE ARG A 365 18538 15335 16466 14 411 -146 N ATOM 2586 CZ ARG A 365 54.596 47.994-370.257 1.00143.78 C ANISOU 2586 CZ ARG A 365 20100 16570 17958 -165 287 -241 C ATOM 2587 NH1 ARG A 365 55.905 48.209-370.311 1.00142.07 N ANISOU 2587 NH1 ARG A 365 19829 16375 17776 -430 221 -113 N ATOM 2588 NH2 ARG A 365 54.042 47.570-369.129 1.00154.69 N ANISOU 2588 NH2 ARG A 365 21666 17735 19375 -76 226 -465 N ATOM 2589 N GLU A 366 51.096 52.673-371.323 1.00103.29 N ANISOU 2589 N GLU A 366 14898 11143 13206 537 505 318 N ATOM 2590 CA GLU A 366 50.201 53.304-370.357 1.00108.87 C ANISOU 2590 CA GLU A 366 15744 11575 14045 716 490 287 C ATOM 2591 C GLU A 366 49.149 53.945-371.236 1.00 92.19 C ANISOU 2591 C GLU A 366 13520 9532 11976 892 543 451 C ATOM 2592 O GLU A 366 47.960 53.924-370.925 1.00 95.56 O ANISOU 2592 O GLU A 366 14031 9755 12523 1038 529 492 O ATOM 2593 CB GLU A 366 51.000 54.023-369.276 1.00115.02 C ANISOU 2593 CB GLU A 366 16686 12042 14973 555 382 348 C ATOM 2594 CG GLU A 366 51.759 53.110-368.333 1.00131.11 C ANISOU 2594 CG GLU A 366 18863 13934 17019 383 296 169 C ATOM 2595 CD GLU A 366 52.737 53.879-367.473 1.00144.89 C ANISOU 2595 CD GLU A 366 20721 15402 18929 166 188 293 C ATOM 2596 OE1 GLU A 366 53.117 53.372-366.396 1.00146.43 O ANISOU 2596 OE1 GLU A 366 21075 15359 19202 56 91 142 O ATOM 2597 OE2 GLU A 366 53.123 54.996-367.880 1.00144.00 O ANISOU 2597 OE2 GLU A 366 20536 15312 18867 106 196 546 O ATOM 2598 N SER A 367 49.585 54.515-372.346 1.00 72.95 N ANISOU 2598 N SER A 367 10891 7380 9447 882 596 545 N ATOM 2599 CA SER A 367 48.708 55.372-373.114 1.00 78.26 C ANISOU 2599 CA SER A 367 11446 8124 10165 991 611 719 C ATOM 2600 C SER A 367 47.968 54.804-374.315 1.00 74.63 C ANISOU 2600 C SER A 367 10789 7942 9626 1093 690 724 C ATOM 2601 O SER A 367 46.746 54.914-374.397 1.00 83.23 O ANISOU 2601 O SER A 367 11803 9056 10766 1293 729 755 O ATOM 2602 CB SER A 367 49.799 56.369-373.474 1.00 85.79 C ANISOU 2602 CB SER A 367 12382 9086 11128 807 546 905 C ATOM 2603 OG SER A 367 50.805 56.335-372.474 1.00 87.31 O ANISOU 2603 OG SER A 367 12723 9085 11364 632 484 891 O ATOM 2604 N VAL A 368 48.702 54.203-375.247 1.00 67.08 N ANISOU 2604 N VAL A 368 9739 7191 8557 957 712 706 N ATOM 2605 CA VAL A 368 48.083 53.681-376.458 1.00 66.94 C ANISOU 2605 CA VAL A 368 9531 7421 8484 1031 780 732 C ATOM 2606 C VAL A 368 48.328 52.209-376.737 1.00 64.34 C ANISOU 2606 C VAL A 368 9160 7255 8031 989 842 612 C ATOM 2607 O VAL A 368 49.467 51.774-376.887 1.00 64.65 O ANISOU 2607 O VAL A 368 9216 7355 7994 807 815 596 O ATOM 2608 CB VAL A 368 48.580 54.499-377.655 1.00 68.31 C ANISOU 2608 CB VAL A 368 9584 7719 8652 936 739 890 C ATOM 2609 CG1 VAL A 368 47.716 55.736-377.855 1.00 66.71 C ANISOU 2609 CG1 VAL A 368 9328 7465 8552 1068 704 1008 C ATOM 2610 CG2 VAL A 368 50.042 54.870-377.474 1.00 65.02 C ANISOU 2610 CG2 VAL A 368 9249 7261 8195 727 676 940 C ATOM 2611 N ASP A 369 47.239 51.456-376.822 1.00 78.94 N ANISOU 2611 N ASP A 369 10941 9196 9856 1168 929 545 N ATOM 2612 CA ASP A 369 47.301 50.038-377.138 1.00 79.37 C ANISOU 2612 CA ASP A 369 10939 9437 9781 1167 1001 449 C ATOM 2613 C ASP A 369 47.395 49.825-378.641 1.00 71.03 C ANISOU 2613 C ASP A 369 9685 8608 8696 1114 1039 570 C ATOM 2614 O ASP A 369 46.381 49.716-379.327 1.00 71.78 O ANISOU 2614 O ASP A 369 9631 8816 8826 1249 1107 637 O ATOM 2615 CB ASP A 369 46.080 49.302-376.572 1.00 85.54 C ANISOU 2615 CB ASP A 369 11731 10241 10531 1403 1091 339 C ATOM 2616 CG ASP A 369 44.791 50.102-376.709 1.00 86.54 C ANISOU 2616 CG ASP A 369 11769 10337 10775 1604 1131 439 C ATOM 2617 OD1 ASP A 369 43.779 49.528-377.167 1.00 87.68 O ANISOU 2617 OD1 ASP A 369 11771 10648 10896 1769 1236 464 O ATOM 2618 OD2 ASP A 369 44.784 51.303-376.353 1.00 75.92 O ANISOU 2618 OD2 ASP A 369 10486 8814 9547 1600 1059 506 O ATOM 2619 N VAL A 370 48.620 49.763-379.150 1.00 54.42 N ANISOU 2619 N VAL A 370 7574 6566 6538 921 993 603 N ATOM 2620 CA VAL A 370 48.838 49.581-380.577 1.00 53.75 C ANISOU 2620 CA VAL A 370 7324 6668 6432 868 1018 707 C ATOM 2621 C VAL A 370 49.684 48.342-380.848 1.00 50.94 C ANISOU 2621 C VAL A 370 6946 6468 5939 767 1050 652 C ATOM 2622 O VAL A 370 50.816 48.250-380.396 1.00 55.75 O ANISOU 2622 O VAL A 370 7646 7047 6490 618 997 610 O ATOM 2623 CB VAL A 370 49.503 50.823-381.195 1.00 52.61 C ANISOU 2623 CB VAL A 370 7166 6479 6344 760 934 824 C ATOM 2624 CG1 VAL A 370 48.569 52.024-381.100 1.00 47.37 C ANISOU 2624 CG1 VAL A 370 6492 5700 5807 874 898 895 C ATOM 2625 CG2 VAL A 370 50.827 51.115-380.500 1.00 53.65 C ANISOU 2625 CG2 VAL A 370 7433 6524 6429 594 868 804 C ATOM 2626 N GLN A 371 49.131 47.394-381.594 1.00 92.12 N ANISOU 2626 N GLN A 371 12030 11862 11111 849 1138 671 N ATOM 2627 CA GLN A 371 49.774 46.097-381.767 1.00 95.27 C ANISOU 2627 CA GLN A 371 12403 12427 11367 791 1178 619 C ATOM 2628 C GLN A 371 50.889 46.075-382.813 1.00 93.48 C ANISOU 2628 C GLN A 371 12103 12304 11110 643 1152 706 C ATOM 2629 O GLN A 371 51.942 45.476-382.597 1.00 93.09 O ANISOU 2629 O GLN A 371 12092 12322 10955 527 1130 659 O ATOM 2630 CB GLN A 371 48.731 45.033-382.106 1.00 94.68 C ANISOU 2630 CB GLN A 371 12215 12516 11243 955 1294 625 C ATOM 2631 CG GLN A 371 47.921 44.536-380.916 1.00104.10 C ANISOU 2631 CG GLN A 371 13503 13674 12377 1111 1336 488 C ATOM 2632 CD GLN A 371 47.006 45.599-380.333 1.00112.44 C ANISOU 2632 CD GLN A 371 14610 14547 13566 1227 1320 491 C ATOM 2633 OE1 GLN A 371 45.800 45.594-380.572 1.00108.89 O ANISOU 2633 OE1 GLN A 371 14054 14151 13167 1400 1401 552 O ATOM 2634 NE2 GLN A 371 47.579 46.519-379.566 1.00115.48 N ANISOU 2634 NE2 GLN A 371 15145 14722 14011 1134 1219 443 N ATOM 2635 N LEU A 372 50.657 46.714-383.950 1.00 58.60 N ANISOU 2635 N LEU A 372 7578 7903 6786 653 1149 828 N ATOM 2636 CA LEU A 372 51.610 46.654-385.052 1.00 53.54 C ANISOU 2636 CA LEU A 372 6866 7360 6116 551 1133 903 C ATOM 2637 C LEU A 372 52.159 48.034-385.350 1.00 51.96 C ANISOU 2637 C LEU A 372 6706 7055 5980 478 1044 957 C ATOM 2638 O LEU A 372 51.555 49.033-384.980 1.00 56.21 O ANISOU 2638 O LEU A 372 7287 7462 6609 526 1000 968 O ATOM 2639 CB LEU A 372 50.946 46.068-386.297 1.00 53.46 C ANISOU 2639 CB LEU A 372 6692 7470 6151 628 1201 995 C ATOM 2640 CG LEU A 372 50.473 44.615-386.165 1.00 57.49 C ANISOU 2640 CG LEU A 372 7140 8133 6572 711 1305 975 C ATOM 2641 CD1 LEU A 372 49.264 44.338-387.056 1.00 63.63 C ANISOU 2641 CD1 LEU A 372 7754 8969 7452 828 1380 1090 C ATOM 2642 CD2 LEU A 372 51.613 43.646-386.461 1.00 55.87 C ANISOU 2642 CD2 LEU A 372 6922 8076 6230 625 1320 968 C ATOM 2643 N PHE A 373 53.304 48.086-386.016 1.00 54.69 N ANISOU 2643 N PHE A 373 7037 7475 6267 380 1019 995 N ATOM 2644 CA PHE A 373 53.957 49.357-386.312 1.00 55.74 C ANISOU 2644 CA PHE A 373 7213 7545 6421 324 941 1046 C ATOM 2645 C PHE A 373 54.339 49.476-387.781 1.00 50.86 C ANISOU 2645 C PHE A 373 6507 7013 5806 327 931 1106 C ATOM 2646 O PHE A 373 55.321 48.874-388.221 1.00 57.50 O ANISOU 2646 O PHE A 373 7322 7971 6555 273 958 1117 O ATOM 2647 CB PHE A 373 55.219 49.505-385.465 1.00 59.15 C ANISOU 2647 CB PHE A 373 7741 7972 6761 198 912 1031 C ATOM 2648 CG PHE A 373 55.023 50.280-384.206 1.00 63.38 C ANISOU 2648 CG PHE A 373 8397 8340 7344 180 865 1010 C ATOM 2649 CD1 PHE A 373 55.554 51.547-384.079 1.00 67.82 C ANISOU 2649 CD1 PHE A 373 9017 8830 7921 137 803 1082 C ATOM 2650 CD2 PHE A 373 54.316 49.746-383.146 1.00 70.35 C ANISOU 2650 CD2 PHE A 373 9339 9137 8252 220 884 921 C ATOM 2651 CE1 PHE A 373 55.383 52.270-382.918 1.00 74.66 C ANISOU 2651 CE1 PHE A 373 9994 9530 8844 123 761 1084 C ATOM 2652 CE2 PHE A 373 54.140 50.466-381.983 1.00 73.98 C ANISOU 2652 CE2 PHE A 373 9921 9414 8773 213 837 901 C ATOM 2653 CZ PHE A 373 54.673 51.727-381.869 1.00 76.58 C ANISOU 2653 CZ PHE A 373 10302 9661 9135 159 775 992 C ATOM 2654 N ILE A 374 53.580 50.250-388.545 1.00 39.53 N ANISOU 2654 N ILE A 374 5026 5516 4479 393 885 1142 N ATOM 2655 CA ILE A 374 53.950 50.476-389.934 1.00 39.24 C ANISOU 2655 CA ILE A 374 4929 5525 4456 398 851 1177 C ATOM 2656 C ILE A 374 55.116 51.446-389.978 1.00 38.62 C ANISOU 2656 C ILE A 374 4935 5456 4284 349 790 1183 C ATOM 2657 O ILE A 374 54.992 52.589-389.558 1.00 37.81 O ANISOU 2657 O ILE A 374 4897 5273 4195 357 723 1192 O ATOM 2658 CB ILE A 374 52.783 51.020-390.752 1.00 40.50 C ANISOU 2658 CB ILE A 374 5009 5607 4771 470 797 1204 C ATOM 2659 CG1 ILE A 374 51.656 49.989-390.796 1.00 38.17 C ANISOU 2659 CG1 ILE A 374 4603 5334 4567 525 878 1232 C ATOM 2660 CG2 ILE A 374 53.245 51.353-392.152 1.00 38.17 C ANISOU 2660 CG2 ILE A 374 4681 5327 4494 469 735 1214 C ATOM 2661 CD1 ILE A 374 50.339 50.533-391.339 1.00 42.25 C ANISOU 2661 CD1 ILE A 374 5020 5772 5261 587 828 1280 C ATOM 2662 N ALA A 375 56.263 50.990-390.455 1.00 50.71 N ANISOU 2662 N ALA A 375 6458 7101 5708 309 820 1192 N ATOM 2663 CA ALA A 375 57.455 51.808-390.357 1.00 49.90 C ANISOU 2663 CA ALA A 375 6424 7044 5492 269 787 1215 C ATOM 2664 C ALA A 375 58.094 52.043-391.710 1.00 50.00 C ANISOU 2664 C ALA A 375 6411 7129 5459 318 763 1219 C ATOM 2665 O ALA A 375 58.618 53.122-391.962 1.00 51.47 O ANISOU 2665 O ALA A 375 6652 7324 5580 344 705 1229 O ATOM 2666 CB ALA A 375 58.461 51.156-389.403 1.00 53.03 C ANISOU 2666 CB ALA A 375 6843 7525 5780 170 845 1230 C ATOM 2667 N GLY A 376 58.034 51.043-392.585 1.00 89.97 N ANISOU 2667 N GLY A 376 11395 12240 10551 346 807 1212 N ATOM 2668 CA GLY A 376 58.638 51.148-393.903 1.00 97.97 C ANISOU 2668 CA GLY A 376 12392 13299 11533 406 786 1205 C ATOM 2669 C GLY A 376 58.142 52.355-394.673 1.00 99.07 C ANISOU 2669 C GLY A 376 12569 13335 11738 473 669 1163 C ATOM 2670 O GLY A 376 58.692 52.714-395.713 1.00 94.57 O ANISOU 2670 O GLY A 376 12020 12787 11127 536 626 1131 O ATOM 2671 N SER A 377 57.100 52.984-394.142 1.00 38.53 N ANISOU 2671 N SER A 377 4912 5559 4168 467 612 1158 N ATOM 2672 CA SER A 377 56.476 54.139-394.768 1.00 40.30 C ANISOU 2672 CA SER A 377 5158 5688 4465 521 483 1120 C ATOM 2673 C SER A 377 57.468 55.258-395.063 1.00 43.00 C ANISOU 2673 C SER A 377 5595 6092 4652 567 417 1094 C ATOM 2674 O SER A 377 57.146 56.209-395.770 1.00 46.82 O ANISOU 2674 O SER A 377 6107 6522 5160 627 294 1041 O ATOM 2675 CB SER A 377 55.378 54.664-393.855 1.00 40.29 C ANISOU 2675 CB SER A 377 5154 5595 4559 510 448 1140 C ATOM 2676 OG SER A 377 55.901 54.881-392.556 1.00 42.22 O ANISOU 2676 OG SER A 377 5470 5874 4699 467 497 1176 O ATOM 2677 N CYS A 378 58.668 55.150-394.517 1.00 65.39 N ANISOU 2677 N CYS A 378 8471 9053 7323 542 496 1136 N ATOM 2678 CA CYS A 378 59.685 56.159-394.753 1.00 68.26 C ANISOU 2678 CA CYS A 378 8910 9513 7513 600 460 1136 C ATOM 2679 C CYS A 378 60.637 55.723-395.846 1.00 70.48 C ANISOU 2679 C CYS A 378 9184 9893 7703 669 491 1100 C ATOM 2680 O CYS A 378 61.618 56.401-396.129 1.00 79.65 O ANISOU 2680 O CYS A 378 10400 11168 8694 740 486 1101 O ATOM 2681 CB CYS A 378 60.469 56.423-393.478 1.00 66.47 C ANISOU 2681 CB CYS A 378 8719 9371 7166 533 528 1234 C ATOM 2682 SG CYS A 378 59.405 56.638-392.058 1.00 82.63 S ANISOU 2682 SG CYS A 378 10779 11277 9338 453 514 1276 S ATOM 2683 N ALA A 379 60.342 54.582-396.456 1.00 51.94 N ANISOU 2683 N ALA A 379 6765 7506 5463 660 531 1079 N ATOM 2684 CA ALA A 379 61.205 54.016-397.481 1.00 56.05 C ANISOU 2684 CA ALA A 379 7273 8105 5918 733 571 1055 C ATOM 2685 C ALA A 379 61.702 55.071-398.463 1.00 62.95 C ANISOU 2685 C ALA A 379 8234 8994 6691 864 478 969 C ATOM 2686 O ALA A 379 62.885 55.095-398.809 1.00 63.26 O ANISOU 2686 O ALA A 379 8298 9176 6563 944 531 974 O ATOM 2687 CB ALA A 379 60.482 52.906-398.216 1.00 61.64 C ANISOU 2687 CB ALA A 379 7902 8714 6803 727 585 1041 C ATOM 2688 N GLY A 380 60.803 55.947-398.899 1.00 53.98 N ANISOU 2688 N GLY A 380 7140 7724 5647 894 335 889 N ATOM 2689 CA GLY A 380 61.125 56.924-399.923 1.00 59.63 C ANISOU 2689 CA GLY A 380 7946 8435 6276 1026 216 774 C ATOM 2690 C GLY A 380 61.979 58.100-399.481 1.00 60.14 C ANISOU 2690 C GLY A 380 8097 8658 6097 1099 208 790 C ATOM 2691 O GLY A 380 62.738 58.648-400.276 1.00 54.89 O ANISOU 2691 O GLY A 380 7507 8073 5275 1240 171 711 O ATOM 2692 N GLU A 381 61.866 58.488-398.216 1.00 52.24 N ANISOU 2692 N GLU A 381 7087 7701 5060 1016 246 897 N ATOM 2693 CA GLU A 381 62.515 59.701-397.728 1.00 52.88 C ANISOU 2693 CA GLU A 381 7241 7919 4932 1077 232 945 C ATOM 2694 C GLU A 381 64.040 59.715-397.899 1.00 53.29 C ANISOU 2694 C GLU A 381 7312 8192 4745 1168 339 993 C ATOM 2695 O GLU A 381 64.647 58.711-398.283 1.00 53.71 O ANISOU 2695 O GLU A 381 7314 8297 4795 1173 434 998 O ATOM 2696 CB GLU A 381 62.142 59.944-396.266 1.00 57.79 C ANISOU 2696 CB GLU A 381 7842 8523 5593 956 269 1077 C ATOM 2697 CG GLU A 381 61.816 61.390-395.962 1.00 61.47 C ANISOU 2697 CG GLU A 381 8379 8995 5982 1012 160 1091 C ATOM 2698 CD GLU A 381 60.589 61.874-396.717 1.00 69.22 C ANISOU 2698 CD GLU A 381 9374 9824 7103 1054 -14 959 C ATOM 2699 OE1 GLU A 381 60.741 62.774-397.577 1.00 63.81 O ANISOU 2699 OE1 GLU A 381 8759 9184 6301 1182 -135 859 O ATOM 2700 OE2 GLU A 381 59.478 61.350-396.459 1.00 61.84 O ANISOU 2700 OE2 GLU A 381 8374 8734 6390 963 -35 957 O ATOM 2701 N SER A 382 64.650 60.869-397.620 1.00 89.95 N ANISOU 2701 N SER A 382 12017 12980 9181 1250 326 1044 N ATOM 2702 CA SER A 382 66.100 61.026-397.721 1.00 95.41 C ANISOU 2702 CA SER A 382 12712 13914 9624 1352 437 1118 C ATOM 2703 C SER A 382 66.747 59.760-397.181 1.00 90.28 C ANISOU 2703 C SER A 382 11953 13330 9018 1235 596 1234 C ATOM 2704 O SER A 382 66.504 59.387-396.039 1.00 87.30 O ANISOU 2704 O SER A 382 11520 12907 8742 1067 645 1348 O ATOM 2705 CB SER A 382 66.581 62.246-396.911 1.00 99.20 C ANISOU 2705 CB SER A 382 13229 14547 9915 1382 450 1255 C ATOM 2706 OG SER A 382 65.626 63.303-396.893 1.00 85.22 O ANISOU 2706 OG SER A 382 11533 12674 8174 1413 297 1194 O ATOM 2707 N LEU A 383 67.545 59.084-397.997 1.00 66.79 N ANISOU 2707 N LEU A 383 8950 10454 5972 1328 666 1198 N ATOM 2708 CA LEU A 383 68.158 57.835-397.557 1.00 65.95 C ANISOU 2708 CA LEU A 383 8728 10427 5903 1224 804 1304 C ATOM 2709 C LEU A 383 68.456 57.901-396.065 1.00 65.76 C ANISOU 2709 C LEU A 383 8644 10473 5869 1053 876 1489 C ATOM 2710 O LEU A 383 68.025 57.044-395.302 1.00 64.62 O ANISOU 2710 O LEU A 383 8439 10235 5879 884 902 1529 O ATOM 2711 CB LEU A 383 69.452 57.543-398.320 1.00 66.98 C ANISOU 2711 CB LEU A 383 8827 10769 5852 1379 902 1320 C ATOM 2712 CG LEU A 383 69.954 56.084-398.311 1.00 66.20 C ANISOU 2712 CG LEU A 383 8607 10731 5816 1313 1014 1382 C ATOM 2713 CD1 LEU A 383 71.468 56.038-398.164 1.00 67.39 C ANISOU 2713 CD1 LEU A 383 8674 11178 5755 1381 1152 1527 C ATOM 2714 CD2 LEU A 383 69.305 55.230-397.229 1.00 64.70 C ANISOU 2714 CD2 LEU A 383 8341 10433 5810 1078 1030 1452 C ATOM 2715 N GLU A 384 69.196 58.929-395.659 1.00101.71 N ANISOU 2715 N GLU A 384 13217 15190 10239 1103 905 1603 N ATOM 2716 CA GLU A 384 69.505 59.139-394.252 1.00 96.03 C ANISOU 2716 CA GLU A 384 12448 14516 9523 940 961 1795 C ATOM 2717 C GLU A 384 68.270 58.874-393.415 1.00 95.59 C ANISOU 2717 C GLU A 384 12412 14211 9695 773 891 1765 C ATOM 2718 O GLU A 384 68.188 57.860-392.727 1.00 94.76 O ANISOU 2718 O GLU A 384 12239 14049 9716 615 936 1800 O ATOM 2719 CB GLU A 384 69.975 60.572-394.011 1.00 96.96 C ANISOU 2719 CB GLU A 384 12620 14770 9452 1033 956 1904 C ATOM 2720 CG GLU A 384 71.259 60.941-394.727 1.00105.43 C ANISOU 2720 CG GLU A 384 13670 16128 10262 1222 1043 1957 C ATOM 2721 CD GLU A 384 71.679 62.367-394.442 1.00117.04 C ANISOU 2721 CD GLU A 384 15189 17753 11528 1324 1044 2082 C ATOM 2722 OE1 GLU A 384 70.787 63.201-394.170 1.00118.06 O ANISOU 2722 OE1 GLU A 384 15409 17745 11705 1317 933 2047 O ATOM 2723 OE2 GLU A 384 72.898 62.650-394.488 1.00107.27 O ANISOU 2723 OE2 GLU A 384 13889 16791 10078 1418 1160 2230 O ATOM 2724 N THR A 385 67.307 59.788-393.494 1.00 59.96 N ANISOU 2724 N THR A 385 7992 9562 5228 823 777 1693 N ATOM 2725 CA THR A 385 66.072 59.677-392.725 1.00 55.06 C ANISOU 2725 CA THR A 385 7392 8714 4814 699 711 1667 C ATOM 2726 C THR A 385 65.372 58.335-392.951 1.00 49.81 C ANISOU 2726 C THR A 385 6677 7918 4332 627 717 1560 C ATOM 2727 O THR A 385 64.753 57.791-392.030 1.00 51.35 O ANISOU 2727 O THR A 385 6852 7986 4673 493 725 1580 O ATOM 2728 CB THR A 385 65.096 60.830-393.019 1.00 54.39 C ANISOU 2728 CB THR A 385 7396 8521 4748 793 576 1591 C ATOM 2729 OG1 THR A 385 63.842 60.568-392.385 1.00 51.35 O ANISOU 2729 OG1 THR A 385 7012 7921 4578 693 523 1558 O ATOM 2730 CG2 THR A 385 64.858 60.971-394.491 1.00 52.56 C ANISOU 2730 CG2 THR A 385 7202 8289 4479 950 493 1418 C ATOM 2731 N ALA A 386 65.476 57.795-394.164 1.00 60.94 N ANISOU 2731 N ALA A 386 8069 9358 5728 725 716 1452 N ATOM 2732 CA ALA A 386 64.903 56.484-394.451 1.00 53.74 C ANISOU 2732 CA ALA A 386 7097 8348 4973 669 736 1382 C ATOM 2733 C ALA A 386 65.354 55.509-393.377 1.00 55.83 C ANISOU 2733 C ALA A 386 7286 8666 5260 515 835 1482 C ATOM 2734 O ALA A 386 64.556 54.740-392.846 1.00 61.04 O ANISOU 2734 O ALA A 386 7920 9207 6065 419 835 1456 O ATOM 2735 CB ALA A 386 65.329 56.005-395.829 1.00 61.20 C ANISOU 2735 CB ALA A 386 8027 9352 5874 797 748 1298 C ATOM 2736 N SER A 387 66.636 55.580-393.040 1.00 58.69 N ANISOU 2736 N SER A 387 7610 9217 5474 496 913 1598 N ATOM 2737 CA SER A 387 67.220 54.697-392.050 1.00 56.63 C ANISOU 2737 CA SER A 387 7266 9024 5226 338 989 1695 C ATOM 2738 C SER A 387 66.993 55.197-390.636 1.00 53.35 C ANISOU 2738 C SER A 387 6885 8514 4870 196 966 1780 C ATOM 2739 O SER A 387 66.429 54.493-389.811 1.00 53.00 O ANISOU 2739 O SER A 387 6834 8352 4952 71 957 1755 O ATOM 2740 CB SER A 387 68.712 54.548-392.302 1.00 59.04 C ANISOU 2740 CB SER A 387 7479 9570 5383 374 1069 1792 C ATOM 2741 OG SER A 387 68.954 54.295-393.674 1.00 65.60 O ANISOU 2741 OG SER A 387 8302 10475 6147 544 1085 1712 O ATOM 2742 N THR A 388 67.429 56.413-390.354 1.00 50.71 N ANISOU 2742 N THR A 388 6594 8232 4443 225 956 1881 N ATOM 2743 CA THR A 388 67.413 56.901-388.980 1.00 51.48 C ANISOU 2743 CA THR A 388 6717 8245 4598 85 944 1998 C ATOM 2744 C THR A 388 66.035 57.031-388.323 1.00 50.91 C ANISOU 2744 C THR A 388 6725 7918 4701 41 865 1919 C ATOM 2745 O THR A 388 65.921 56.965-387.104 1.00 51.40 O ANISOU 2745 O THR A 388 6805 7867 4856 -96 858 1979 O ATOM 2746 CB THR A 388 68.199 58.216-388.826 1.00 53.05 C ANISOU 2746 CB THR A 388 6936 8570 4651 138 960 2158 C ATOM 2747 OG1 THR A 388 67.378 59.172-388.146 1.00 53.44 O ANISOU 2747 OG1 THR A 388 7078 8448 4777 127 888 2184 O ATOM 2748 CG2 THR A 388 68.596 58.771-390.184 1.00 53.34 C ANISOU 2748 CG2 THR A 388 6985 8773 4509 350 967 2110 C ATOM 2749 N VAL A 389 64.990 57.220-389.115 1.00 45.53 N ANISOU 2749 N VAL A 389 6089 7140 4072 159 803 1786 N ATOM 2750 CA VAL A 389 63.647 57.258-388.550 1.00 45.03 C ANISOU 2750 CA VAL A 389 6077 6857 4174 134 740 1717 C ATOM 2751 C VAL A 389 63.254 55.872-388.074 1.00 41.57 C ANISOU 2751 C VAL A 389 5597 6347 3849 34 774 1648 C ATOM 2752 O VAL A 389 63.065 55.646-386.879 1.00 41.92 O ANISOU 2752 O VAL A 389 5669 6283 3975 -78 774 1672 O ATOM 2753 CB VAL A 389 62.594 57.730-389.562 1.00 46.28 C ANISOU 2753 CB VAL A 389 6264 6942 4377 274 659 1603 C ATOM 2754 CG1 VAL A 389 61.202 57.580-388.978 1.00 45.58 C ANISOU 2754 CG1 VAL A 389 6198 6653 4468 251 613 1544 C ATOM 2755 CG2 VAL A 389 62.849 59.166-389.950 1.00 45.72 C ANISOU 2755 CG2 VAL A 389 6250 6935 4186 383 600 1650 C ATOM 2756 N GLN A 390 63.121 54.949-389.024 1.00 65.29 N ANISOU 2756 N GLN A 390 8542 9410 6855 84 799 1560 N ATOM 2757 CA GLN A 390 62.833 53.552-388.721 1.00 62.71 C ANISOU 2757 CA GLN A 390 8165 9065 6598 12 841 1501 C ATOM 2758 C GLN A 390 63.670 53.050-387.556 1.00 66.01 C ANISOU 2758 C GLN A 390 8566 9526 6990 -144 875 1569 C ATOM 2759 O GLN A 390 63.139 52.560-386.559 1.00 69.07 O ANISOU 2759 O GLN A 390 8983 9795 7465 -227 862 1527 O ATOM 2760 CB GLN A 390 63.124 52.684-389.940 1.00 60.35 C ANISOU 2760 CB GLN A 390 7788 8889 6255 81 883 1458 C ATOM 2761 CG GLN A 390 62.139 52.847-391.073 1.00 69.52 C ANISOU 2761 CG GLN A 390 8953 9969 7494 206 839 1376 C ATOM 2762 CD GLN A 390 62.363 51.828-392.171 1.00 83.06 C ANISOU 2762 CD GLN A 390 10592 11770 9198 262 884 1345 C ATOM 2763 OE1 GLN A 390 63.415 51.814-392.812 1.00 84.74 O ANISOU 2763 OE1 GLN A 390 10781 12121 9296 307 916 1375 O ATOM 2764 NE2 GLN A 390 61.375 50.968-392.394 1.00 83.42 N ANISOU 2764 NE2 GLN A 390 10595 11741 9361 272 893 1298 N ATOM 2765 N LYS A 391 64.984 53.163-387.704 1.00 72.16 N ANISOU 2765 N LYS A 391 9293 10478 7647 -177 916 1669 N ATOM 2766 CA LYS A 391 65.924 52.762-386.670 1.00 73.32 C ANISOU 2766 CA LYS A 391 9399 10685 7773 -343 938 1759 C ATOM 2767 C LYS A 391 65.373 53.175-385.313 1.00 80.15 C ANISOU 2767 C LYS A 391 10353 11343 8757 -448 884 1767 C ATOM 2768 O LYS A 391 65.319 52.378-384.379 1.00 84.21 O ANISOU 2768 O LYS A 391 10870 11787 9338 -575 868 1727 O ATOM 2769 CB LYS A 391 67.278 53.422-386.924 1.00 68.46 C ANISOU 2769 CB LYS A 391 8727 10262 7021 -342 982 1914 C ATOM 2770 CG LYS A 391 68.375 52.481-387.390 1.00 61.66 C ANISOU 2770 CG LYS A 391 7744 9587 6098 -459 1033 1995 C ATOM 2771 CD LYS A 391 69.649 53.259-387.710 1.00 66.34 C ANISOU 2771 CD LYS A 391 8266 10397 6544 -420 1093 2163 C ATOM 2772 CE LYS A 391 70.850 52.333-387.897 1.00 85.49 C ANISOU 2772 CE LYS A 391 10547 13002 8935 -568 1132 2283 C ATOM 2773 NZ LYS A 391 72.146 53.077-387.889 1.00 88.85 N ANISOU 2773 NZ LYS A 391 10884 13623 9252 -545 1182 2473 N ATOM 2774 N HIS A 392 64.936 54.425-385.224 1.00 52.39 N ANISOU 2774 N HIS A 392 6917 7723 5264 -383 848 1811 N ATOM 2775 CA HIS A 392 64.364 54.958-383.996 1.00 49.86 C ANISOU 2775 CA HIS A 392 6691 7188 5064 -452 797 1832 C ATOM 2776 C HIS A 392 63.012 54.332-383.653 1.00 52.36 C ANISOU 2776 C HIS A 392 7063 7325 5507 -420 766 1673 C ATOM 2777 O HIS A 392 62.736 54.066-382.487 1.00 53.55 O ANISOU 2777 O HIS A 392 7274 7319 5755 -514 737 1645 O ATOM 2778 CB HIS A 392 64.251 56.480-384.080 1.00 53.51 C ANISOU 2778 CB HIS A 392 7214 7614 5502 -366 768 1935 C ATOM 2779 CG HIS A 392 63.418 57.099-382.998 1.00 63.98 C ANISOU 2779 CG HIS A 392 8644 8702 6964 -387 712 1949 C ATOM 2780 ND1 HIS A 392 62.453 58.033-383.245 1.00 66.23 N ANISOU 2780 ND1 HIS A 392 8989 8892 7282 -252 665 1932 N ATOM 2781 CD2 HIS A 392 63.431 56.889-381.653 1.00 71.18 C ANISOU 2781 CD2 HIS A 392 9610 9443 7993 -526 690 1976 C ATOM 2782 CE1 HIS A 392 61.891 58.393-382.104 1.00 66.54 C ANISOU 2782 CE1 HIS A 392 9114 8721 7449 -291 627 1959 C ATOM 2783 NE2 HIS A 392 62.451 57.725-381.131 1.00 72.27 N ANISOU 2783 NE2 HIS A 392 9846 9382 8231 -453 640 1979 N ATOM 2784 N VAL A 393 62.172 54.101-384.661 1.00 45.39 N ANISOU 2784 N VAL A 393 6158 6464 4626 -284 771 1574 N ATOM 2785 CA VAL A 393 60.863 53.488-384.431 1.00 42.05 C ANISOU 2785 CA VAL A 393 5761 5906 4311 -233 760 1446 C ATOM 2786 C VAL A 393 61.027 52.131-383.779 1.00 43.51 C ANISOU 2786 C VAL A 393 5926 6104 4500 -331 784 1371 C ATOM 2787 O VAL A 393 60.242 51.761-382.916 1.00 43.93 O ANISOU 2787 O VAL A 393 6041 6015 4636 -336 767 1287 O ATOM 2788 CB VAL A 393 60.063 53.309-385.732 1.00 45.04 C ANISOU 2788 CB VAL A 393 6083 6332 4697 -92 768 1380 C ATOM 2789 CG1 VAL A 393 58.703 52.681-385.442 1.00 43.47 C ANISOU 2789 CG1 VAL A 393 5891 6018 4608 -35 772 1279 C ATOM 2790 CG2 VAL A 393 59.902 54.642-386.441 1.00 45.39 C ANISOU 2790 CG2 VAL A 393 6149 6370 4728 6 719 1429 C ATOM 2791 N VAL A 394 62.047 51.391-384.207 1.00 59.07 N ANISOU 2791 N VAL A 394 7812 8259 6374 -393 822 1397 N ATOM 2792 CA VAL A 394 62.382 50.106-383.596 1.00 56.99 C ANISOU 2792 CA VAL A 394 7518 8045 6090 -499 831 1334 C ATOM 2793 C VAL A 394 62.691 50.306-382.121 1.00 64.62 C ANISOU 2793 C VAL A 394 8564 8866 7121 -649 774 1346 C ATOM 2794 O VAL A 394 62.344 49.475-381.279 1.00 71.34 O ANISOU 2794 O VAL A 394 9458 9639 8010 -704 745 1234 O ATOM 2795 CB VAL A 394 63.607 49.449-384.268 1.00 57.90 C ANISOU 2795 CB VAL A 394 7514 8399 6086 -548 873 1396 C ATOM 2796 CG1 VAL A 394 64.059 48.235-383.473 1.00 63.13 C ANISOU 2796 CG1 VAL A 394 8144 9118 6726 -681 857 1343 C ATOM 2797 CG2 VAL A 394 63.283 49.057-385.700 1.00 63.31 C ANISOU 2797 CG2 VAL A 394 8128 9202 6725 -400 925 1370 C ATOM 2798 N SER A 395 63.341 51.424-381.816 1.00 58.36 N ANISOU 2798 N SER A 395 7796 8036 6342 -709 755 1483 N ATOM 2799 CA SER A 395 63.738 51.729-380.453 1.00 56.60 C ANISOU 2799 CA SER A 395 7643 7657 6204 -868 698 1532 C ATOM 2800 C SER A 395 62.577 52.302-379.644 1.00 58.37 C ANISOU 2800 C SER A 395 8007 7611 6559 -807 652 1468 C ATOM 2801 O SER A 395 62.784 52.999-378.650 1.00 65.25 O ANISOU 2801 O SER A 395 8956 8312 7523 -898 605 1547 O ATOM 2802 CB SER A 395 64.906 52.704-380.464 1.00 56.63 C ANISOU 2802 CB SER A 395 7602 7744 6169 -948 709 1741 C ATOM 2803 OG SER A 395 65.750 52.465-379.356 1.00 58.76 O ANISOU 2803 OG SER A 395 7865 7961 6500 -1160 665 1809 O ATOM 2804 N ILE A 396 61.357 52.015-380.090 1.00 45.52 N ANISOU 2804 N ILE A 396 6401 5947 4946 -648 671 1342 N ATOM 2805 CA ILE A 396 60.150 52.380-379.361 1.00 50.80 C ANISOU 2805 CA ILE A 396 7185 6384 5732 -561 639 1265 C ATOM 2806 C ILE A 396 59.414 51.101-379.015 1.00 53.01 C ANISOU 2806 C ILE A 396 7486 6640 6016 -523 646 1080 C ATOM 2807 O ILE A 396 58.889 50.945-377.914 1.00 54.92 O ANISOU 2807 O ILE A 396 7839 6687 6340 -528 605 984 O ATOM 2808 CB ILE A 396 59.228 53.277-380.202 1.00 74.45 C ANISOU 2808 CB ILE A 396 10171 9374 8743 -382 656 1298 C ATOM 2809 CG1 ILE A 396 59.813 54.689-380.305 1.00 74.88 C ANISOU 2809 CG1 ILE A 396 10240 9423 8789 -396 633 1471 C ATOM 2810 CG2 ILE A 396 57.821 53.305-379.609 1.00 74.91 C ANISOU 2810 CG2 ILE A 396 10311 9244 8909 -259 642 1196 C ATOM 2811 CD1 ILE A 396 59.124 55.577-381.325 1.00 73.95 C ANISOU 2811 CD1 ILE A 396 10093 9350 8653 -234 629 1502 C ATOM 2812 N GLY A 397 59.382 50.184-379.975 1.00 64.52 N ANISOU 2812 N GLY A 397 8838 8298 7377 -471 700 1032 N ATOM 2813 CA GLY A 397 58.833 48.866-379.751 1.00 64.67 C ANISOU 2813 CA GLY A 397 8856 8356 7361 -432 718 877 C ATOM 2814 C GLY A 397 59.758 48.098-378.837 1.00 66.04 C ANISOU 2814 C GLY A 397 9055 8536 7502 -609 663 822 C ATOM 2815 O GLY A 397 59.307 47.333-377.993 1.00 67.20 O ANISOU 2815 O GLY A 397 9278 8601 7654 -606 630 670 O ATOM 2816 N ASP A 398 61.059 48.309-379.007 1.00 63.53 N ANISOU 2816 N ASP A 398 8668 8322 7147 -759 647 945 N ATOM 2817 CA ASP A 398 62.048 47.694-378.132 1.00 70.55 C ANISOU 2817 CA ASP A 398 9558 9219 8028 -959 578 923 C ATOM 2818 C ASP A 398 61.766 48.032-376.682 1.00 72.94 C ANISOU 2818 C ASP A 398 10018 9232 8464 -1038 488 851 C ATOM 2819 O ASP A 398 61.529 47.152-375.867 1.00 78.25 O ANISOU 2819 O ASP A 398 10761 9831 9140 -1076 427 683 O ATOM 2820 CB ASP A 398 63.464 48.146-378.496 1.00 90.67 C ANISOU 2820 CB ASP A 398 11999 11913 10540 -1099 584 1113 C ATOM 2821 CG ASP A 398 64.266 47.054-379.183 1.00 90.16 C ANISOU 2821 CG ASP A 398 11786 12127 10342 -1141 614 1118 C ATOM 2822 OD1 ASP A 398 63.681 45.993-379.485 1.00 90.48 O ANISOU 2822 OD1 ASP A 398 11810 12255 10315 -1051 635 986 O ATOM 2823 OD2 ASP A 398 65.480 47.254-379.412 1.00 96.92 O ANISOU 2823 OD2 ASP A 398 12537 13129 11159 -1254 621 1267 O ATOM 2824 N VAL A 399 61.764 49.310-376.366 1.00 20.00 N ATOM 2825 CA VAL A 399 61.650 49.763-374.984 1.00 20.00 C ATOM 2826 C VAL A 399 60.258 49.487-374.427 1.00 20.00 C ATOM 2827 O VAL A 399 60.064 49.624-373.193 1.00 83.79 O ANISOU 2827 O VAL A 399 11889 9676 10271 -1029 291 672 O ATOM 2828 CB VAL A 399 61.955 51.267-374.856 1.00 20.00 C ATOM 2829 CG1 VAL A 399 61.733 51.736-373.427 1.00 20.00 C ATOM 2830 CG2 VAL A 399 63.377 51.563-375.307 1.00 20.00 C ATOM 2831 N ARG A 400 59.296 49.127-375.238 1.00 58.61 N ANISOU 2831 N ARG A 400 8512 6880 6877 -773 453 675 N ATOM 2832 CA ARG A 400 57.935 48.905-374.748 1.00 55.03 C ANISOU 2832 CA ARG A 400 8170 6277 6463 -589 462 511 C ATOM 2833 C ARG A 400 57.512 47.437-374.844 1.00 53.13 C ANISOU 2833 C ARG A 400 7907 6184 6097 -515 486 321 C ATOM 2834 O ARG A 400 56.732 46.948-374.028 1.00 54.96 O ANISOU 2834 O ARG A 400 8256 6286 6339 -419 462 141 O ATOM 2835 CB ARG A 400 56.936 49.821-375.470 1.00 52.03 C ANISOU 2835 CB ARG A 400 7762 5890 6118 -390 534 597 C ATOM 2836 CG ARG A 400 56.406 49.283-376.794 1.00 54.49 C ANISOU 2836 CG ARG A 400 7931 6451 6322 -253 628 596 C ATOM 2837 CD ARG A 400 55.684 50.365-377.609 1.00 52.48 C ANISOU 2837 CD ARG A 400 7625 6195 6120 -113 669 715 C ATOM 2838 NE ARG A 400 54.530 50.953-376.924 1.00 58.24 N ANISOU 2838 NE ARG A 400 8452 6719 6958 34 661 675 N ATOM 2839 CZ ARG A 400 53.267 50.572-377.109 1.00 61.37 C ANISOU 2839 CZ ARG A 400 8821 7137 7358 225 718 597 C ATOM 2840 NH1 ARG A 400 52.981 49.588-377.956 1.00 57.07 N ANISOU 2840 NH1 ARG A 400 8160 6804 6720 284 788 558 N ATOM 2841 NH2 ARG A 400 52.290 51.172-376.441 1.00 56.62 N ANISOU 2841 NH2 ARG A 400 8303 6353 6858 365 712 575 N ATOM 2842 N GLN A 401 58.039 46.748-375.850 1.00 58.73 N ANISOU 2842 N GLN A 401 8465 7171 6677 -544 536 366 N ATOM 2843 CA GLN A 401 57.833 45.311-376.034 1.00 58.67 C ANISOU 2843 CA GLN A 401 8412 7351 6528 -490 560 224 C ATOM 2844 C GLN A 401 56.377 44.851-375.997 1.00 55.00 C ANISOU 2844 C GLN A 401 7992 6875 6032 -250 626 93 C ATOM 2845 O GLN A 401 56.075 43.768-375.505 1.00 57.83 O ANISOU 2845 O GLN A 401 8395 7284 6294 -199 612 -79 O ATOM 2846 CB GLN A 401 58.698 44.508-375.053 1.00 72.48 C ANISOU 2846 CB GLN A 401 10217 9076 8245 -676 446 104 C ATOM 2847 CG GLN A 401 60.192 44.580-375.380 1.00 74.42 C ANISOU 2847 CG GLN A 401 10346 9456 8475 -900 410 253 C ATOM 2848 CD GLN A 401 61.057 43.688-374.501 1.00 81.54 C ANISOU 2848 CD GLN A 401 11268 10370 9345 -1098 286 143 C ATOM 2849 OE1 GLN A 401 60.552 42.967-373.639 1.00 83.60 O ANISOU 2849 OE1 GLN A 401 11646 10534 9583 -1066 216 -72 O ATOM 2850 NE2 GLN A 401 62.370 43.734-374.719 1.00 74.53 N ANISOU 2850 NE2 GLN A 401 10259 9609 8451 -1297 254 287 N ATOM 2851 N ASP A 402 55.485 45.682-376.528 1.00109.54 N ANISOU 2851 N ASP A 402 14876 13732 13014 -99 695 181 N ATOM 2852 CA ASP A 402 54.104 45.292-376.795 1.00109.44 C ANISOU 2852 CA ASP A 402 14842 13769 12972 138 785 118 C ATOM 2853 C ASP A 402 53.769 45.741-378.207 1.00107.33 C ANISOU 2853 C ASP A 402 14416 13642 12724 214 869 287 C ATOM 2854 O ASP A 402 53.065 46.731-378.397 1.00106.99 O ANISOU 2854 O ASP A 402 14372 13491 12789 307 885 363 O ATOM 2855 CB ASP A 402 53.140 45.950-375.801 1.00110.97 C ANISOU 2855 CB ASP A 402 15182 13706 13277 266 766 39 C ATOM 2856 CG ASP A 402 51.703 46.005-376.318 1.00110.56 C ANISOU 2856 CG ASP A 402 15060 13711 13236 515 873 61 C ATOM 2857 OD1 ASP A 402 51.275 45.049-377.003 1.00110.01 O ANISOU 2857 OD1 ASP A 402 14878 13864 13056 612 958 50 O ATOM 2858 OD2 ASP A 402 51.003 47.008-376.044 1.00110.94 O ANISOU 2858 OD2 ASP A 402 15154 13589 13408 612 872 106 O ATOM 2859 N CYS A 403 54.288 45.021-379.198 1.00 58.16 N ANISOU 2859 N CYS A 403 8056 7646 6398 173 912 346 N ATOM 2860 CA CYS A 403 54.165 45.458-380.586 1.00 56.74 C ANISOU 2860 CA CYS A 403 7735 7574 6249 215 969 501 C ATOM 2861 C CYS A 403 54.996 44.634-381.556 1.00 63.31 C ANISOU 2861 C CYS A 403 8443 8635 6976 148 1001 560 C ATOM 2862 O CYS A 403 55.416 43.528-381.245 1.00 69.76 O ANISOU 2862 O CYS A 403 9255 9573 7676 108 1000 484 O ATOM 2863 CB CYS A 403 54.575 46.924-380.706 1.00 59.49 C ANISOU 2863 CB CYS A 403 8114 7785 6706 144 914 611 C ATOM 2864 SG CYS A 403 56.099 47.337-379.829 1.00 72.44 S ANISOU 2864 SG CYS A 403 9847 9339 8338 -85 817 624 S ATOM 2865 N LEU A 404 55.242 45.199-382.732 1.00 41.88 N ANISOU 2865 N LEU A 404 5633 5978 4301 143 1021 693 N ATOM 2866 CA LEU A 404 55.989 44.514-383.773 1.00 41.64 C ANISOU 2866 CA LEU A 404 5485 6147 4189 106 1057 763 C ATOM 2867 C LEU A 404 56.287 45.846-384.459 1.00 41.29 C ANISOU 2867 C LEU A 404 5387 6097 4203 88 1045 885 C ATOM 2868 O LEU A 404 55.401 46.683-384.616 1.00 39.41 O ANISOU 2868 O LEU A 404 5062 5897 4015 179 1085 947 O ATOM 2869 CB LEU A 404 55.115 43.425-384.401 1.00 41.87 C ANISOU 2869 CB LEU A 404 5414 6316 4179 241 1146 766 C ATOM 2870 CG LEU A 404 55.795 42.273-385.151 1.00 40.79 C ANISOU 2870 CG LEU A 404 5170 6403 3927 222 1191 811 C ATOM 2871 CD1 LEU A 404 54.910 41.787-386.299 1.00 40.22 C ANISOU 2871 CD1 LEU A 404 4969 6419 3892 357 1281 904 C ATOM 2872 CD2 LEU A 404 57.179 42.665-385.662 1.00 40.81 C ANISOU 2872 CD2 LEU A 404 5145 6454 3906 97 1151 883 C ATOM 2873 N VAL A 405 57.535 46.046-384.864 1.00 92.21 N ANISOU 2873 N VAL A 405 11889 12499 10647 -28 987 921 N ATOM 2874 CA VAL A 405 57.904 47.295-385.512 1.00 92.36 C ANISOU 2874 CA VAL A 405 11875 12528 10691 -26 972 1022 C ATOM 2875 C VAL A 405 58.268 46.418-386.704 1.00 85.93 C ANISOU 2875 C VAL A 405 10945 11890 9814 1 1021 1074 C ATOM 2876 O VAL A 405 59.087 45.504-386.577 1.00 81.11 O ANISOU 2876 O VAL A 405 10300 11411 9106 -79 1029 1101 O ATOM 2877 CB VAL A 405 59.016 48.181-384.925 1.00 93.53 C ANISOU 2877 CB VAL A 405 12086 12637 10815 -149 918 1073 C ATOM 2878 CG1 VAL A 405 59.564 49.125-385.983 1.00 94.92 C ANISOU 2878 CG1 VAL A 405 12227 12864 10975 -120 911 1168 C ATOM 2879 CG2 VAL A 405 58.488 48.963-383.740 1.00 89.38 C ANISOU 2879 CG2 VAL A 405 11679 11906 10375 -166 867 1043 C ATOM 2880 N LEU A 406 57.656 46.694-387.857 1.00 42.19 N ANISOU 2880 N LEU A 406 5341 6348 4343 113 1050 1097 N ATOM 2881 CA LEU A 406 57.911 45.920-389.077 1.00 39.63 C ANISOU 2881 CA LEU A 406 4914 6154 3990 154 1094 1152 C ATOM 2882 C LEU A 406 58.472 47.083-389.909 1.00 40.69 C ANISOU 2882 C LEU A 406 5044 6262 4153 181 1055 1202 C ATOM 2883 O LEU A 406 58.010 48.220-389.795 1.00 40.00 O ANISOU 2883 O LEU A 406 4972 6056 4171 238 1011 1202 O ATOM 2884 CB LEU A 406 56.764 45.050-389.580 1.00 40.37 C ANISOU 2884 CB LEU A 406 4926 6268 4146 253 1153 1161 C ATOM 2885 CG LEU A 406 55.389 45.693-389.534 1.00 40.23 C ANISOU 2885 CG LEU A 406 4913 6105 4266 327 1136 1155 C ATOM 2886 CD1 LEU A 406 55.141 46.433-390.832 1.00 39.34 C ANISOU 2886 CD1 LEU A 406 4751 5929 4266 370 1097 1212 C ATOM 2887 CD2 LEU A 406 54.311 44.639-389.292 1.00 40.16 C ANISOU 2887 CD2 LEU A 406 4841 6146 4271 408 1214 1151 C ATOM 2888 N CYS A 407 59.460 46.777-390.752 1.00 62.95 N ANISOU 2888 N CYS A 407 7841 9205 6873 150 1067 1240 N ATOM 2889 CA CYS A 407 60.243 47.800-391.439 1.00 68.28 C ANISOU 2889 CA CYS A 407 8536 9875 7531 184 1029 1270 C ATOM 2890 C CYS A 407 60.743 47.328-392.797 1.00 63.70 C ANISOU 2890 C CYS A 407 7890 9333 6981 278 1048 1290 C ATOM 2891 O CYS A 407 61.076 46.161-392.969 1.00 60.79 O ANISOU 2891 O CYS A 407 7453 8965 6680 317 1087 1301 O ATOM 2892 CB CYS A 407 61.669 48.060-390.962 1.00 72.61 C ANISOU 2892 CB CYS A 407 9101 10540 7946 107 1034 1311 C ATOM 2893 SG CYS A 407 61.836 48.239-389.175 1.00 70.05 S ANISOU 2893 SG CYS A 407 8844 10166 7605 -37 1010 1304 S ATOM 2894 N SER A 408 60.797 48.255-393.751 1.00 46.58 N ANISOU 2894 N SER A 408 5744 7195 4758 323 1021 1301 N ATOM 2895 CA SER A 408 61.172 47.957-395.136 1.00 47.52 C ANISOU 2895 CA SER A 408 5828 7311 4915 425 1020 1302 C ATOM 2896 C SER A 408 62.358 48.764-395.702 1.00 48.65 C ANISOU 2896 C SER A 408 6016 7529 4938 482 1000 1301 C ATOM 2897 O SER A 408 62.618 49.878-395.246 1.00 50.82 O ANISOU 2897 O SER A 408 6363 7793 5155 468 954 1291 O ATOM 2898 CB SER A 408 59.854 48.390-395.790 1.00 49.67 C ANISOU 2898 CB SER A 408 6104 7403 5364 473 952 1266 C ATOM 2899 OG SER A 408 59.641 47.757-397.038 1.00 46.49 O ANISOU 2899 OG SER A 408 5642 6969 5053 543 962 1283 O ATOM 2900 N PRO A 409 63.065 48.212-396.708 1.00 51.82 N ANISOU 2900 N PRO A 409 6377 8014 5298 565 1039 1319 N ATOM 2901 CA PRO A 409 64.323 48.764-397.228 1.00 52.46 C ANISOU 2901 CA PRO A 409 6487 8212 5235 646 1048 1325 C ATOM 2902 C PRO A 409 64.111 50.076-397.945 1.00 53.00 C ANISOU 2902 C PRO A 409 6652 8169 5315 739 952 1244 C ATOM 2903 O PRO A 409 62.983 50.379-398.319 1.00 52.88 O ANISOU 2903 O PRO A 409 6664 7977 5452 744 871 1185 O ATOM 2904 CB PRO A 409 64.733 47.716-398.255 1.00 52.67 C ANISOU 2904 CB PRO A 409 6446 8299 5269 735 1106 1351 C ATOM 2905 CG PRO A 409 63.415 47.326-398.830 1.00 52.39 C ANISOU 2905 CG PRO A 409 6397 8077 5432 744 1066 1322 C ATOM 2906 CD PRO A 409 62.601 47.107-397.566 1.00 51.73 C ANISOU 2906 CD PRO A 409 6293 7972 5390 614 1074 1339 C ATOM 2907 N PRO A 410 65.185 50.843-398.151 1.00 49.90 N ANISOU 2907 N PRO A 410 6306 7896 4759 817 956 1245 N ATOM 2908 CA PRO A 410 65.105 52.132-398.848 1.00 51.65 C ANISOU 2908 CA PRO A 410 6632 8046 4948 928 858 1155 C ATOM 2909 C PRO A 410 64.986 51.941-400.354 1.00 49.82 C ANISOU 2909 C PRO A 410 6427 7716 4788 1067 810 1061 C ATOM 2910 O PRO A 410 65.707 51.128-400.925 1.00 51.04 O ANISOU 2910 O PRO A 410 6535 7955 4901 1138 886 1090 O ATOM 2911 CB PRO A 410 66.449 52.799-398.518 1.00 53.50 C ANISOU 2911 CB PRO A 410 6884 8492 4950 980 912 1214 C ATOM 2912 CG PRO A 410 67.078 51.955-397.434 1.00 52.91 C ANISOU 2912 CG PRO A 410 6709 8568 4828 848 1022 1344 C ATOM 2913 CD PRO A 410 66.537 50.578-397.642 1.00 48.66 C ANISOU 2913 CD PRO A 410 6094 7968 4426 802 1054 1341 C ATOM 2914 N ARG A 411 64.088 52.680-400.991 1.00 92.94 N ANISOU 2914 N ARG A 411 11959 12992 10363 1104 677 953 N ATOM 2915 CA ARG A 411 63.920 52.560-402.429 1.00 99.79 C ANISOU 2915 CA ARG A 411 12864 13723 11329 1221 604 852 C ATOM 2916 C ARG A 411 65.273 52.533-403.123 1.00 90.55 C ANISOU 2916 C ARG A 411 11731 12698 9976 1386 664 830 C ATOM 2917 O ARG A 411 65.544 51.650-403.935 1.00 79.10 O ANISOU 2917 O ARG A 411 10249 11219 8585 1457 707 835 O ATOM 2918 CB ARG A 411 63.066 53.705-402.976 1.00 87.07 C ANISOU 2918 CB ARG A 411 11342 11934 9805 1251 425 720 C ATOM 2919 CG ARG A 411 61.563 53.426-402.992 1.00 83.26 C ANISOU 2919 CG ARG A 411 10799 11243 9592 1133 348 725 C ATOM 2920 CD ARG A 411 60.784 54.573-403.629 1.00 90.64 C ANISOU 2920 CD ARG A 411 11809 12012 10618 1162 151 592 C ATOM 2921 NE ARG A 411 61.466 55.057-404.823 1.00 91.08 N ANISOU 2921 NE ARG A 411 11975 12037 10594 1321 65 449 N ATOM 2922 CZ ARG A 411 62.309 56.083-404.832 1.00 89.82 C ANISOU 2922 CZ ARG A 411 11925 12009 10192 1443 32 370 C ATOM 2923 NH1 ARG A 411 62.560 56.745-403.710 1.00 84.57 N ANISOU 2923 NH1 ARG A 411 11266 11506 9361 1407 77 442 N ATOM 2924 NH2 ARG A 411 62.898 56.449-405.960 1.00 85.40 N ANISOU 2924 NH2 ARG A 411 11474 11419 9557 1609 -45 224 N ATOM 2925 N GLU A 412 66.127 53.497-402.795 1.00 59.90 N ANISOU 2925 N GLU A 412 7910 8980 5869 1460 674 822 N ATOM 2926 CA GLU A 412 67.452 53.578-403.412 1.00 61.02 C ANISOU 2926 CA GLU A 412 8082 9294 5808 1644 742 808 C ATOM 2927 C GLU A 412 68.011 52.191-403.696 1.00 66.18 C ANISOU 2927 C GLU A 412 8634 10017 6494 1663 866 895 C ATOM 2928 O GLU A 412 68.430 51.881-404.806 1.00 74.35 O ANISOU 2928 O GLU A 412 9702 11018 7531 1824 869 831 O ATOM 2929 CB GLU A 412 68.433 54.335-402.504 1.00 61.81 C ANISOU 2929 CB GLU A 412 8178 9650 5656 1656 818 901 C ATOM 2930 CG GLU A 412 68.286 55.864-402.502 1.00 73.29 C ANISOU 2930 CG GLU A 412 9752 11103 6990 1729 708 815 C ATOM 2931 CD GLU A 412 69.440 56.547-401.770 1.00 77.88 C ANISOU 2931 CD GLU A 412 10319 11969 7304 1777 808 938 C ATOM 2932 OE1 GLU A 412 69.393 57.789-401.565 1.00 69.07 O ANISOU 2932 OE1 GLU A 412 9285 10895 6062 1828 740 912 O ATOM 2933 OE2 GLU A 412 70.400 55.827-401.402 1.00 77.29 O ANISOU 2933 OE2 GLU A 412 10137 12083 7146 1761 955 1075 O ATOM 2934 N THR A 413 67.968 51.356-402.669 1.00 86.48 N ANISOU 2934 N THR A 413 11086 12677 9097 1499 960 1036 N ATOM 2935 CA THR A 413 68.748 50.128-402.612 1.00 81.77 C ANISOU 2935 CA THR A 413 10371 12239 8460 1504 1092 1153 C ATOM 2936 C THR A 413 68.186 48.957-403.402 1.00 79.49 C ANISOU 2936 C THR A 413 10037 11806 8361 1519 1096 1153 C ATOM 2937 O THR A 413 68.892 47.988-403.666 1.00 85.97 O ANISOU 2937 O THR A 413 10773 12750 9140 1579 1193 1236 O ATOM 2938 CB THR A 413 68.891 49.669-401.160 1.00 77.79 C ANISOU 2938 CB THR A 413 9760 11881 7915 1312 1168 1290 C ATOM 2939 OG1 THR A 413 69.970 48.738-401.060 1.00 77.37 O ANISOU 2939 OG1 THR A 413 9590 12051 7757 1337 1288 1405 O ATOM 2940 CG2 THR A 413 67.597 49.006-400.680 1.00 79.40 C ANISOU 2940 CG2 THR A 413 9930 11918 8321 1152 1133 1294 C ATOM 2941 N VAL A 414 66.925 49.038-403.792 1.00 65.64 N ANISOU 2941 N VAL A 414 8325 9800 6817 1468 992 1080 N ATOM 2942 CA VAL A 414 66.252 47.842-404.269 1.00 64.26 C ANISOU 2942 CA VAL A 414 8076 9503 6838 1437 1013 1133 C ATOM 2943 C VAL A 414 65.459 47.944-405.575 1.00 62.82 C ANISOU 2943 C VAL A 414 7959 9039 6871 1510 901 1038 C ATOM 2944 O VAL A 414 65.351 46.968-406.315 1.00 61.78 O ANISOU 2944 O VAL A 414 7777 8830 6866 1555 936 1094 O ATOM 2945 CB VAL A 414 65.347 47.282-403.156 1.00 66.46 C ANISOU 2945 CB VAL A 414 8266 9781 7203 1244 1040 1218 C ATOM 2946 CG1 VAL A 414 64.096 46.670-403.749 1.00 68.42 C ANISOU 2946 CG1 VAL A 414 8479 9814 7703 1207 997 1232 C ATOM 2947 CG2 VAL A 414 66.128 46.289-402.300 1.00 69.54 C ANISOU 2947 CG2 VAL A 414 8545 10418 7460 1187 1170 1346 C ATOM 2948 N VAL A 415 64.928 49.122-405.875 1.00 47.45 N ANISOU 2948 N VAL A 415 6120 6939 4970 1520 760 902 N ATOM 2949 CA VAL A 415 64.033 49.271-407.022 1.00 54.06 C ANISOU 2949 CA VAL A 415 7009 7484 6047 1547 623 808 C ATOM 2950 C VAL A 415 64.729 49.504-408.365 1.00 48.74 C ANISOU 2950 C VAL A 415 6446 6716 5357 1749 566 684 C ATOM 2951 O VAL A 415 64.376 48.877-409.363 1.00 50.53 O ANISOU 2951 O VAL A 415 6667 6742 5789 1787 531 685 O ATOM 2952 CB VAL A 415 63.020 50.392-406.797 1.00 48.51 C ANISOU 2952 CB VAL A 415 6362 6641 5430 1458 469 710 C ATOM 2953 CG1 VAL A 415 62.184 50.588-408.041 1.00 54.62 C ANISOU 2953 CG1 VAL A 415 7181 7114 6457 1478 307 608 C ATOM 2954 CG2 VAL A 415 62.147 50.071-405.587 1.00 45.71 C ANISOU 2954 CG2 VAL A 415 5899 6331 5139 1275 520 829 C ATOM 2955 N GLY A 416 65.702 50.409-408.397 1.00 47.28 N ANISOU 2955 N GLY A 416 6364 6670 4930 1888 557 582 N ATOM 2956 CA GLY A 416 66.400 50.722-409.633 1.00 53.72 C ANISOU 2956 CA GLY A 416 7305 7410 5697 2112 502 438 C ATOM 2957 C GLY A 416 67.257 49.600-410.212 1.00 62.96 C ANISOU 2957 C GLY A 416 8426 8643 6852 2247 634 525 C ATOM 2958 O GLY A 416 67.031 49.130-411.332 1.00 62.65 O ANISOU 2958 O GLY A 416 8426 8374 7003 2328 579 480 O ATOM 2959 N ILE A 417 68.253 49.171-409.442 1.00 65.13 N ANISOU 2959 N ILE A 417 8608 9227 6910 2269 803 659 N ATOM 2960 CA ILE A 417 69.247 48.202-409.901 1.00 67.18 C ANISOU 2960 CA ILE A 417 8810 9612 7105 2420 937 751 C ATOM 2961 C ILE A 417 68.680 46.796-410.094 1.00 59.72 C ANISOU 2961 C ILE A 417 7745 8561 6386 2333 991 899 C ATOM 2962 O ILE A 417 67.563 46.516-409.667 1.00 50.12 O ANISOU 2962 O ILE A 417 6469 7226 5347 2138 951 955 O ATOM 2963 CB ILE A 417 70.444 48.139-408.919 1.00 74.38 C ANISOU 2963 CB ILE A 417 9624 10908 7728 2439 1096 876 C ATOM 2964 CG1 ILE A 417 69.969 48.352-407.476 1.00 69.26 C ANISOU 2964 CG1 ILE A 417 8897 10372 7047 2194 1109 963 C ATOM 2965 CG2 ILE A 417 71.475 49.192-409.276 1.00 66.87 C ANISOU 2965 CG2 ILE A 417 8782 10097 6527 2660 1096 762 C ATOM 2966 CD1 ILE A 417 68.898 47.376-407.004 1.00 61.55 C ANISOU 2966 CD1 ILE A 417 7816 9286 6286 1987 1113 1066 C ATOM 2967 N PRO A 418 69.456 45.916-410.760 1.00 62.77 N ANISOU 2967 N PRO A 418 8092 9001 6756 2495 1086 972 N ATOM 2968 CA PRO A 418 69.174 44.480-410.877 1.00 53.24 C ANISOU 2968 CA PRO A 418 6752 7773 5704 2445 1169 1154 C ATOM 2969 C PRO A 418 69.513 43.762-409.576 1.00 57.54 C ANISOU 2969 C PRO A 418 7127 8638 6097 2308 1305 1332 C ATOM 2970 O PRO A 418 70.231 44.321-408.747 1.00 58.53 O ANISOU 2970 O PRO A 418 7237 9004 5996 2290 1348 1325 O ATOM 2971 CB PRO A 418 70.147 44.033-411.971 1.00 52.48 C ANISOU 2971 CB PRO A 418 6690 7674 5576 2709 1225 1154 C ATOM 2972 CG PRO A 418 71.265 45.015-411.867 1.00 56.17 C ANISOU 2972 CG PRO A 418 7236 8343 5762 2870 1246 1040 C ATOM 2973 CD PRO A 418 70.554 46.310-411.659 1.00 65.87 C ANISOU 2973 CD PRO A 418 8590 9432 7004 2774 1098 865 C ATOM 2974 N VAL A 419 69.023 42.535-409.412 1.00 57.76 N ANISOU 2974 N VAL A 419 7028 8672 6248 2217 1366 1493 N ATOM 2975 CA VAL A 419 69.182 41.804-408.160 1.00 54.47 C ANISOU 2975 CA VAL A 419 6459 8532 5705 2071 1465 1639 C ATOM 2976 C VAL A 419 70.641 41.571-407.756 1.00 48.88 C ANISOU 2976 C VAL A 419 5671 8163 4740 2163 1576 1712 C ATOM 2977 O VAL A 419 70.964 41.585-406.567 1.00 46.74 O ANISOU 2977 O VAL A 419 5319 8122 4319 2028 1617 1763 O ATOM 2978 CB VAL A 419 68.476 40.461-408.212 1.00 47.82 C ANISOU 2978 CB VAL A 419 5500 7657 5014 2004 1514 1799 C ATOM 2979 CG1 VAL A 419 68.252 39.954-406.802 1.00 50.01 C ANISOU 2979 CG1 VAL A 419 5660 8156 5185 1815 1567 1887 C ATOM 2980 CG2 VAL A 419 67.167 40.604-408.950 1.00 49.39 C ANISOU 2980 CG2 VAL A 419 5761 7509 5497 1961 1416 1760 C ATOM 2981 N THR A 420 71.513 41.348-408.736 1.00 88.71 N ANISOU 2981 N THR A 420 10729 13232 9745 2392 1622 1722 N ATOM 2982 CA THR A 420 72.934 41.171-408.466 1.00 89.38 C ANISOU 2982 CA THR A 420 10722 13648 9591 2506 1731 1802 C ATOM 2983 C THR A 420 73.420 42.228-407.478 1.00 95.87 C ANISOU 2983 C THR A 420 11557 14653 10218 2418 1727 1748 C ATOM 2984 O THR A 420 73.734 41.913-406.330 1.00 93.62 O ANISOU 2984 O THR A 420 11145 14607 9821 2260 1777 1853 O ATOM 2985 CB THR A 420 73.761 41.236-409.765 1.00 94.58 C ANISOU 2985 CB THR A 420 11449 14261 10226 2809 1760 1760 C ATOM 2986 OG1 THR A 420 73.467 40.091-410.575 1.00 82.39 O ANISOU 2986 OG1 THR A 420 9861 12587 8856 2889 1785 1862 O ATOM 2987 CG2 THR A 420 75.261 41.275-409.458 1.00103.31 C ANISOU 2987 CG2 THR A 420 12455 15734 11064 2943 1876 1838 C ATOM 2988 N ARG A 421 73.464 43.481-407.921 1.00129.09 N ANISOU 2988 N ARG A 421 15920 18740 14388 2517 1659 1586 N ATOM 2989 CA ARG A 421 73.802 44.589-407.039 1.00134.22 C ANISOU 2989 CA ARG A 421 16596 19535 14866 2439 1647 1544 C ATOM 2990 C ARG A 421 72.834 44.631-405.864 1.00127.33 C ANISOU 2990 C ARG A 421 15693 18611 14074 2152 1595 1565 C ATOM 2991 O ARG A 421 73.233 44.844-404.719 1.00126.77 O ANISOU 2991 O ARG A 421 15547 18745 13876 2015 1632 1637 O ATOM 2992 CB ARG A 421 73.727 45.922-407.787 1.00141.64 C ANISOU 2992 CB ARG A 421 17729 20312 15777 2592 1555 1348 C ATOM 2993 CG ARG A 421 74.716 46.094-408.922 1.00149.00 C ANISOU 2993 CG ARG A 421 18725 21291 16596 2908 1598 1287 C ATOM 2994 CD ARG A 421 74.614 47.504-409.478 1.00155.51 C ANISOU 2994 CD ARG A 421 19749 21984 17354 3042 1491 1074 C ATOM 2995 NE ARG A 421 75.467 47.722-410.641 1.00154.17 N ANISOU 2995 NE ARG A 421 19674 21824 17078 3372 1516 974 N ATOM 2996 CZ ARG A 421 75.583 48.890-411.264 1.00162.32 C ANISOU 2996 CZ ARG A 421 20889 22779 18007 3552 1430 772 C ATOM 2997 NH1 ARG A 421 74.902 49.942-410.830 1.00174.28 N ANISOU 2997 NH1 ARG A 421 22497 24209 19512 3425 1312 665 N ATOM 2998 NH2 ARG A 421 76.379 49.008-412.317 1.00160.72 N ANISOU 2998 NH2 ARG A 421 20778 22588 17700 3874 1458 672 N ATOM 2999 N ALA A 422 71.556 44.427-406.162 1.00 91.54 N ANISOU 2999 N ALA A 422 11217 13800 9765 2068 1509 1507 N ATOM 3000 CA ALA A 422 70.494 44.599-405.179 1.00 85.46 C ANISOU 3000 CA ALA A 422 10444 12943 9085 1833 1451 1500 C ATOM 3001 C ALA A 422 70.837 44.018-403.814 1.00 82.27 C ANISOU 3001 C ALA A 422 9903 12785 8572 1660 1524 1629 C ATOM 3002 O ALA A 422 70.862 44.735-402.814 1.00 81.47 O ANISOU 3002 O ALA A 422 9815 12750 8391 1533 1504 1616 O ATOM 3003 CB ALA A 422 69.192 44.010-405.692 1.00 82.17 C ANISOU 3003 CB ALA A 422 10038 12261 8921 1778 1392 1490 C ATOM 3004 N VAL A 423 71.092 42.718-403.767 1.00 62.70 N ANISOU 3004 N VAL A 423 7293 10435 6095 1653 1600 1753 N ATOM 3005 CA VAL A 423 71.323 42.061-402.488 1.00 65.68 C ANISOU 3005 CA VAL A 423 7532 10989 6436 1486 1591 1840 C ATOM 3006 C VAL A 423 72.579 42.596-401.800 1.00 64.41 C ANISOU 3006 C VAL A 423 7301 11041 6129 1478 1579 1871 C ATOM 3007 O VAL A 423 72.560 42.892-400.605 1.00 62.05 O ANISOU 3007 O VAL A 423 6964 10776 5836 1307 1510 1866 O ATOM 3008 CB VAL A 423 71.400 40.531-402.633 1.00 63.43 C ANISOU 3008 CB VAL A 423 7109 10797 6196 1507 1621 1954 C ATOM 3009 CG1 VAL A 423 71.544 39.883-401.271 1.00 55.66 C ANISOU 3009 CG1 VAL A 423 5994 9952 5204 1334 1542 1993 C ATOM 3010 CG2 VAL A 423 70.164 40.009-403.340 1.00 55.69 C ANISOU 3010 CG2 VAL A 423 6180 9616 5365 1517 1653 1958 C ATOM 3011 N ASP A 424 73.665 42.725-402.554 1.00 95.14 N ANISOU 3011 N ASP A 424 11174 15084 9890 1668 1660 1914 N ATOM 3012 CA ASP A 424 74.880 43.309-402.008 1.00100.95 C ANISOU 3012 CA ASP A 424 11832 16045 10481 1681 1671 1970 C ATOM 3013 C ASP A 424 74.501 44.512-401.154 1.00100.00 C ANISOU 3013 C ASP A 424 11794 15841 10360 1541 1602 1900 C ATOM 3014 O ASP A 424 74.879 44.605-399.985 1.00 98.69 O ANISOU 3014 O ASP A 424 11529 15783 10184 1379 1560 1960 O ATOM 3015 CB ASP A 424 75.830 43.737-403.132 1.00110.73 C ANISOU 3015 CB ASP A 424 13112 17401 11560 1952 1778 1976 C ATOM 3016 CG ASP A 424 76.533 42.559-403.789 1.00119.39 C ANISOU 3016 CG ASP A 424 14085 18651 12627 2101 1861 2086 C ATOM 3017 OD1 ASP A 424 76.661 41.504-403.136 1.00123.63 O ANISOU 3017 OD1 ASP A 424 14458 19296 13218 1978 1827 2191 O ATOM 3018 OD2 ASP A 424 76.964 42.692-404.956 1.00121.23 O ANISOU 3018 OD2 ASP A 424 14389 18903 12769 2352 1964 2060 O ATOM 3019 N ASN A 425 73.727 45.414-401.748 1.00 87.88 N ANISOU 3019 N ASN A 425 10445 14113 8834 1601 1593 1779 N ATOM 3020 CA ASN A 425 73.285 46.621-401.070 1.00 84.24 C ANISOU 3020 CA ASN A 425 10080 13565 8362 1497 1530 1715 C ATOM 3021 C ASN A 425 72.574 46.305-399.765 1.00 83.83 C ANISOU 3021 C ASN A 425 9971 13433 8449 1246 1449 1729 C ATOM 3022 O ASN A 425 72.969 46.776-398.700 1.00 84.49 O ANISOU 3022 O ASN A 425 10005 13598 8500 1122 1421 1776 O ATOM 3023 CB ASN A 425 72.361 47.428-401.983 1.00 82.22 C ANISOU 3023 CB ASN A 425 10024 13086 8129 1592 1495 1569 C ATOM 3024 CG ASN A 425 73.070 47.962-403.211 1.00 84.29 C ANISOU 3024 CG ASN A 425 10364 13375 8289 1860 1508 1496 C ATOM 3025 OD1 ASN A 425 74.285 48.171-403.200 1.00 88.24 O ANISOU 3025 OD1 ASN A 425 10807 14125 8596 1973 1597 1571 O ATOM 3026 ND2 ASN A 425 72.311 48.193-404.278 1.00 82.67 N ANISOU 3026 ND2 ASN A 425 10286 12910 8215 1968 1416 1347 N ATOM 3027 N LEU A 426 71.523 45.498-399.856 1.00 92.70 N ANISOU 3027 N LEU A 426 11104 14400 9717 1181 1422 1693 N ATOM 3028 CA LEU A 426 70.721 45.151-398.689 1.00 95.57 C ANISOU 3028 CA LEU A 426 11437 14678 10196 976 1353 1681 C ATOM 3029 C LEU A 426 71.560 44.664-397.511 1.00 99.12 C ANISOU 3029 C LEU A 426 11745 15313 10603 841 1334 1763 C ATOM 3030 O LEU A 426 71.351 45.093-396.376 1.00 96.10 O ANISOU 3030 O LEU A 426 11377 14899 10239 680 1288 1753 O ATOM 3031 CB LEU A 426 69.665 44.105-399.054 1.00100.37 C ANISOU 3031 CB LEU A 426 12038 15160 10937 965 1351 1665 C ATOM 3032 CG LEU A 426 68.227 44.608-399.170 1.00105.27 C ANISOU 3032 CG LEU A 426 12779 15547 11670 921 1321 1584 C ATOM 3033 CD1 LEU A 426 67.369 43.624-399.950 1.00100.13 C ANISOU 3033 CD1 LEU A 426 12109 14802 11134 965 1357 1607 C ATOM 3034 CD2 LEU A 426 67.649 44.853-397.784 1.00 99.91 C ANISOU 3034 CD2 LEU A 426 12106 14816 11038 746 1258 1554 C ATOM 3035 N VAL A 427 72.509 43.770-397.782 1.00 72.36 N ANISOU 3035 N VAL A 427 8221 12121 7151 903 1374 1852 N ATOM 3036 CA VAL A 427 73.309 43.162-396.719 1.00 70.38 C ANISOU 3036 CA VAL A 427 7821 12069 6850 760 1354 1939 C ATOM 3037 C VAL A 427 74.300 44.163-396.130 1.00 71.15 C ANISOU 3037 C VAL A 427 7885 12301 6846 712 1371 2010 C ATOM 3038 O VAL A 427 74.499 44.210-394.917 1.00 69.08 O ANISOU 3038 O VAL A 427 7575 12090 6581 517 1335 2050 O ATOM 3039 CB VAL A 427 74.056 41.905-397.199 1.00 65.39 C ANISOU 3039 CB VAL A 427 7040 11639 6168 844 1392 2033 C ATOM 3040 CG1 VAL A 427 74.637 41.158-396.014 1.00 72.96 C ANISOU 3040 CG1 VAL A 427 7852 12789 7080 658 1355 2106 C ATOM 3041 CG2 VAL A 427 73.120 41.004-397.987 1.00 60.09 C ANISOU 3041 CG2 VAL A 427 6405 10839 5587 930 1398 1994 C ATOM 3042 N ASN A 428 74.914 44.963-396.989 1.00 79.49 N ANISOU 3042 N ASN A 428 8974 13420 7809 893 1433 2032 N ATOM 3043 CA ASN A 428 75.752 46.053-396.518 1.00 83.14 C ANISOU 3043 CA ASN A 428 9417 14009 8164 876 1461 2110 C ATOM 3044 C ASN A 428 74.989 46.935-395.543 1.00 82.48 C ANISOU 3044 C ASN A 428 9441 13755 8143 707 1401 2062 C ATOM 3045 O ASN A 428 75.496 47.289-394.480 1.00 85.53 O ANISOU 3045 O ASN A 428 9766 14231 8501 551 1395 2157 O ATOM 3046 CB ASN A 428 76.232 46.903-397.690 1.00 84.31 C ANISOU 3046 CB ASN A 428 9638 14212 8185 1132 1536 2099 C ATOM 3047 CG ASN A 428 77.193 46.165-398.583 1.00 87.51 C ANISOU 3047 CG ASN A 428 9932 14819 8498 1320 1617 2174 C ATOM 3048 OD1 ASN A 428 77.409 44.964-398.419 1.00 86.78 O ANISOU 3048 OD1 ASN A 428 9708 14815 8449 1264 1611 2234 O ATOM 3049 ND2 ASN A 428 77.778 46.878-399.537 1.00 87.47 N ANISOU 3049 ND2 ASN A 428 9986 14901 8346 1561 1697 2169 N ATOM 3050 N TRP A 429 73.764 47.285-395.920 1.00 62.93 N ANISOU 3050 N TRP A 429 7123 11035 5752 738 1362 1928 N ATOM 3051 CA TRP A 429 72.930 48.179-395.122 1.00 62.03 C ANISOU 3051 CA TRP A 429 7125 10748 5695 613 1309 1880 C ATOM 3052 C TRP A 429 72.580 47.568-393.768 1.00 62.20 C ANISOU 3052 C TRP A 429 7104 10724 5805 376 1260 1895 C ATOM 3053 O TRP A 429 72.519 48.272-392.759 1.00 62.11 O ANISOU 3053 O TRP A 429 7132 10670 5798 239 1239 1933 O ATOM 3054 CB TRP A 429 71.654 48.543-395.891 1.00 60.38 C ANISOU 3054 CB TRP A 429 7075 10308 5557 700 1279 1745 C ATOM 3055 CG TRP A 429 70.792 49.576-395.215 1.00 58.26 C ANISOU 3055 CG TRP A 429 6931 9877 5328 610 1229 1703 C ATOM 3056 CD1 TRP A 429 71.138 50.861-394.913 1.00 58.47 C ANISOU 3056 CD1 TRP A 429 7017 9941 5257 623 1230 1749 C ATOM 3057 CD2 TRP A 429 69.436 49.410-394.780 1.00 55.46 C ANISOU 3057 CD2 TRP A 429 6651 9312 5109 511 1176 1625 C ATOM 3058 NE1 TRP A 429 70.085 51.502-394.310 1.00 57.58 N ANISOU 3058 NE1 TRP A 429 7016 9646 5216 535 1175 1705 N ATOM 3059 CE2 TRP A 429 69.028 50.636-394.217 1.00 54.24 C ANISOU 3059 CE2 TRP A 429 6603 9070 4937 467 1144 1627 C ATOM 3060 CE3 TRP A 429 68.526 48.347-394.807 1.00 54.50 C ANISOU 3060 CE3 TRP A 429 6511 9085 5111 469 1161 1568 C ATOM 3061 CZ2 TRP A 429 67.752 50.824-393.686 1.00 51.90 C ANISOU 3061 CZ2 TRP A 429 6394 8580 4746 385 1097 1571 C ATOM 3062 CZ3 TRP A 429 67.259 48.537-394.279 1.00 43.38 C ANISOU 3062 CZ3 TRP A 429 5184 7496 3802 390 1122 1511 C ATOM 3063 CH2 TRP A 429 66.885 49.765-393.726 1.00 41.99 C ANISOU 3063 CH2 TRP A 429 5113 7232 3611 350 1092 1512 C ATOM 3064 N ARG A 430 72.374 46.256-393.750 1.00107.77 N ANISOU 3064 N ARG A 430 12802 16513 11632 336 1245 1872 N ATOM 3065 CA ARG A 430 72.003 45.545-392.530 1.00107.45 C ANISOU 3065 CA ARG A 430 12738 16443 11644 130 1201 1862 C ATOM 3066 C ARG A 430 73.178 45.400-391.565 1.00102.70 C ANISOU 3066 C ARG A 430 12014 16043 10966 -29 1210 1992 C ATOM 3067 O ARG A 430 73.012 44.926-390.441 1.00 96.57 O ANISOU 3067 O ARG A 430 11231 15251 10209 -226 1178 1994 O ATOM 3068 CB ARG A 430 71.424 44.176-392.884 1.00107.05 C ANISOU 3068 CB ARG A 430 12648 16381 11646 160 1189 1803 C ATOM 3069 CG ARG A 430 70.034 44.237-393.507 1.00106.89 C ANISOU 3069 CG ARG A 430 12744 16138 11731 250 1177 1694 C ATOM 3070 CD ARG A 430 68.970 43.727-392.540 1.00115.43 C ANISOU 3070 CD ARG A 430 13875 17104 12879 118 1142 1624 C ATOM 3071 NE ARG A 430 69.296 44.039-391.150 1.00115.03 N ANISOU 3071 NE ARG A 430 13841 17075 12791 -72 1121 1647 N ATOM 3072 CZ ARG A 430 68.836 43.354-390.108 1.00115.09 C ANISOU 3072 CZ ARG A 430 13866 17063 12799 -212 1104 1606 C ATOM 3073 NH1 ARG A 430 68.032 42.315-390.301 1.00106.03 N ANISOU 3073 NH1 ARG A 430 12710 15901 11677 -165 1105 1543 N ATOM 3074 NH2 ARG A 430 69.184 43.705-388.874 1.00120.51 N ANISOU 3074 NH2 ARG A 430 14585 17752 13452 -396 1092 1640 N ATOM 3075 N THR A 431 74.361 45.816-392.013 1.00 81.23 N ANISOU 3075 N THR A 431 9198 13517 8147 57 1262 2109 N ATOM 3076 CA THR A 431 75.563 45.807-391.176 1.00 87.03 C ANISOU 3076 CA THR A 431 9792 14468 8806 -91 1284 2274 C ATOM 3077 C THR A 431 76.295 47.162-391.123 1.00 83.51 C ANISOU 3077 C THR A 431 9346 14099 8284 -54 1335 2397 C ATOM 3078 O THR A 431 76.303 47.842-390.089 1.00 85.71 O ANISOU 3078 O THR A 431 9661 14323 8582 -226 1323 2470 O ATOM 3079 CB THR A 431 76.550 44.692-391.592 1.00 82.20 C ANISOU 3079 CB THR A 431 8991 14121 8121 -45 1313 2361 C ATOM 3080 OG1 THR A 431 77.892 45.115-391.316 1.00 90.61 O ANISOU 3080 OG1 THR A 431 9909 15432 9087 -83 1369 2552 O ATOM 3081 CG2 THR A 431 76.432 44.385-393.074 1.00 77.80 C ANISOU 3081 CG2 THR A 431 8444 13567 7548 226 1349 2299 C ATOM 3082 N ALA A 432 76.907 47.549-392.233 1.00 90.52 N ANISOU 3082 N ALA A 432 10199 15118 9076 178 1400 2430 N ATOM 3083 CA ALA A 432 77.675 48.783-392.283 1.00 91.82 C ANISOU 3083 CA ALA A 432 10352 15407 9129 253 1465 2557 C ATOM 3084 C ALA A 432 78.482 48.727-393.567 1.00 92.68 C ANISOU 3084 C ALA A 432 10392 15715 9109 525 1547 2585 C ATOM 3085 O ALA A 432 78.165 49.385-394.554 1.00 92.34 O ANISOU 3085 O ALA A 432 10474 15601 9011 741 1571 2490 O ATOM 3086 CB ALA A 432 78.582 48.914-391.080 1.00 93.38 C ANISOU 3086 CB ALA A 432 10412 15768 9302 31 1484 2764 C ATOM 3087 N ALA A 433 79.543 47.936-393.532 1.00162.84 N ANISOU 3087 N ALA A 433 19079 24857 17935 513 1591 2721 N ATOM 3088 CA ALA A 433 80.279 47.539-394.727 1.00163.16 C ANISOU 3088 CA ALA A 433 19039 25088 17867 771 1670 2747 C ATOM 3089 C ALA A 433 80.556 48.657-395.729 1.00165.44 C ANISOU 3089 C ALA A 433 19424 25424 18012 1051 1752 2728 C ATOM 3090 O ALA A 433 81.239 49.635-395.422 1.00164.15 O ANISOU 3090 O ALA A 433 19222 25414 17732 1073 1813 2859 O ATOM 3091 CB ALA A 433 79.551 46.390-395.425 1.00160.43 C ANISOU 3091 CB ALA A 433 18737 24607 17613 836 1626 2602 C ATOM 3092 N GLY A 434 80.008 48.494-396.932 1.00109.50 N ANISOU 3092 N GLY A 434 12471 18209 10926 1264 1756 2569 N ATOM 3093 CA GLY A 434 80.399 49.292-398.083 1.00107.24 C ANISOU 3093 CA GLY A 434 12277 18001 10470 1569 1841 2532 C ATOM 3094 C GLY A 434 79.956 50.736-398.077 1.00104.07 C ANISOU 3094 C GLY A 434 12050 17498 9995 1618 1829 2464 C ATOM 3095 O GLY A 434 80.616 51.590-397.491 1.00100.72 O ANISOU 3095 O GLY A 434 11565 17243 9460 1596 1874 2604 O ATOM 3096 N SER A 435 78.842 51.009-398.745 1.00 93.30 N ANISOU 3096 N SER A 435 10895 15871 8682 1687 1768 2263 N ATOM 3097 CA SER A 435 78.387 52.381-398.949 1.00 92.15 C ANISOU 3097 CA SER A 435 10935 15641 8435 1775 1746 2176 C ATOM 3098 C SER A 435 77.555 52.892-397.779 1.00 87.74 C ANISOU 3098 C SER A 435 10422 14911 8005 1522 1657 2184 C ATOM 3099 O SER A 435 77.708 54.036-397.336 1.00 80.60 O ANISOU 3099 O SER A 435 9560 14066 6997 1523 1664 2248 O ATOM 3100 CB SER A 435 77.588 52.472-400.249 1.00 82.30 C ANISOU 3100 CB SER A 435 9899 14204 7167 1964 1715 1957 C ATOM 3101 OG SER A 435 78.260 51.771-401.286 1.00 75.16 O ANISOU 3101 OG SER A 435 8958 13417 6181 2179 1799 1945 O ATOM 3102 N TYR A 436 76.671 52.032-397.286 1.00 92.93 N ANISOU 3102 N TYR A 436 11072 15363 8876 1320 1580 2126 N ATOM 3103 CA TYR A 436 75.826 52.377-396.152 1.00 95.42 C ANISOU 3103 CA TYR A 436 11434 15502 9320 1088 1501 2124 C ATOM 3104 C TYR A 436 76.486 51.955-394.852 1.00 97.68 C ANISOU 3104 C TYR A 436 11549 15908 9656 862 1512 2297 C ATOM 3105 O TYR A 436 75.956 51.117-394.124 1.00 93.01 O ANISOU 3105 O TYR A 436 10925 15196 9217 664 1454 2272 O ATOM 3106 CB TYR A 436 74.458 51.698-396.245 1.00 84.94 C ANISOU 3106 CB TYR A 436 10196 13896 8180 998 1417 1970 C ATOM 3107 CG TYR A 436 74.028 51.324-397.637 1.00 78.85 C ANISOU 3107 CG TYR A 436 9515 13042 7404 1185 1422 1834 C ATOM 3108 CD1 TYR A 436 73.186 52.144-398.368 1.00 72.46 C ANISOU 3108 CD1 TYR A 436 8895 12078 6559 1292 1380 1701 C ATOM 3109 CD2 TYR A 436 74.450 50.139-398.213 1.00 82.31 C ANISOU 3109 CD2 TYR A 436 9852 13555 7867 1249 1465 1848 C ATOM 3110 CE1 TYR A 436 72.789 51.797-399.637 1.00 72.85 C ANISOU 3110 CE1 TYR A 436 9038 12040 6601 1444 1384 1582 C ATOM 3111 CE2 TYR A 436 74.056 49.783-399.479 1.00 79.45 C ANISOU 3111 CE2 TYR A 436 9580 13103 7506 1414 1480 1743 C ATOM 3112 CZ TYR A 436 73.226 50.613-400.187 1.00 74.99 C ANISOU 3112 CZ TYR A 436 9210 12373 6910 1504 1443 1608 C ATOM 3113 OH TYR A 436 72.827 50.260-401.452 1.00 76.85 O ANISOU 3113 OH TYR A 436 9525 12476 7197 1658 1425 1490 O ATOM 3114 N THR A 437 77.649 52.519-394.559 1.00 73.75 N ANISOU 3114 N THR A 437 8410 13126 6484 891 1588 2476 N ATOM 3115 CA THR A 437 78.234 52.300-393.254 1.00 70.55 C ANISOU 3115 CA THR A 437 7858 12821 6125 647 1594 2660 C ATOM 3116 C THR A 437 77.556 53.239-392.284 1.00 67.80 C ANISOU 3116 C THR A 437 7625 12301 5836 491 1544 2683 C ATOM 3117 O THR A 437 77.280 52.881-391.143 1.00 60.90 O ANISOU 3117 O THR A 437 6729 11323 5088 240 1497 2729 O ATOM 3118 CB THR A 437 79.722 52.609-393.232 1.00 77.00 C ANISOU 3118 CB THR A 437 8500 13980 6778 718 1704 2887 C ATOM 3119 OG1 THR A 437 80.144 52.704-391.866 1.00 81.01 O ANISOU 3119 OG1 THR A 437 8897 14543 7339 449 1702 3084 O ATOM 3120 CG2 THR A 437 80.004 53.934-393.939 1.00 75.78 C ANISOU 3120 CG2 THR A 437 8436 13930 6426 969 1773 2903 C ATOM 3121 N ASP A 438 77.274 54.441-392.772 1.00114.92 N ANISOU 3121 N ASP A 438 13728 18238 11697 655 1554 2645 N ATOM 3122 CA ASP A 438 76.780 55.544-391.961 1.00116.32 C ANISOU 3122 CA ASP A 438 14011 18301 11885 559 1522 2705 C ATOM 3123 C ASP A 438 75.290 55.393-391.723 1.00112.05 C ANISOU 3123 C ASP A 438 13628 17436 11511 463 1417 2526 C ATOM 3124 O ASP A 438 74.832 55.247-390.589 1.00107.61 O ANISOU 3124 O ASP A 438 13080 16726 11080 241 1373 2568 O ATOM 3125 CB ASP A 438 77.036 56.859-392.694 1.00124.82 C ANISOU 3125 CB ASP A 438 15175 19501 12749 804 1566 2723 C ATOM 3126 CG ASP A 438 78.028 56.707-393.840 1.00138.36 C ANISOU 3126 CG ASP A 438 16815 21474 14280 1059 1657 2724 C ATOM 3127 OD1 ASP A 438 79.043 57.438-393.850 1.00144.78 O ANISOU 3127 OD1 ASP A 438 17553 22553 14904 1172 1752 2898 O ATOM 3128 OD2 ASP A 438 77.793 55.856-394.733 1.00135.09 O ANISOU 3128 OD2 ASP A 438 16419 21003 13907 1156 1641 2563 O ATOM 3129 N ASN A 439 74.536 55.451-392.812 1.00 95.25 N ANISOU 3129 N ASN A 439 11622 15200 9369 636 1380 2335 N ATOM 3130 CA ASN A 439 73.106 55.215-392.760 1.00 93.31 C ANISOU 3130 CA ASN A 439 11504 14674 9277 570 1290 2172 C ATOM 3131 C ASN A 439 72.827 53.720-392.786 1.00 88.44 C ANISOU 3131 C ASN A 439 10810 13988 8805 481 1275 2090 C ATOM 3132 O ASN A 439 72.188 53.201-393.702 1.00 83.49 O ANISOU 3132 O ASN A 439 10232 13267 8225 579 1253 1947 O ATOM 3133 CB ASN A 439 72.435 55.908-393.932 1.00 88.06 C ANISOU 3133 CB ASN A 439 10993 13936 8529 777 1253 2023 C ATOM 3134 CG ASN A 439 72.947 57.304-394.124 1.00 87.24 C ANISOU 3134 CG ASN A 439 10953 13975 8218 920 1274 2099 C ATOM 3135 OD1 ASN A 439 72.659 58.192-393.327 1.00 88.66 O ANISOU 3135 OD1 ASN A 439 11189 14107 8391 845 1245 2184 O ATOM 3136 ND2 ASN A 439 73.729 57.511-395.178 1.00 90.86 N ANISOU 3136 ND2 ASN A 439 11409 14622 8493 1143 1328 2075 N ATOM 3137 N ASN A 440 73.336 53.026-391.778 1.00 83.21 N ANISOU 3137 N ASN A 440 10029 13385 8203 291 1287 2194 N ATOM 3138 CA ASN A 440 73.075 51.609-391.655 1.00 80.57 C ANISOU 3138 CA ASN A 440 9625 13007 7980 198 1264 2125 C ATOM 3139 C ASN A 440 71.773 51.402-390.918 1.00 76.19 C ANISOU 3139 C ASN A 440 9177 12204 7568 62 1198 2028 C ATOM 3140 O ASN A 440 71.203 52.338-390.364 1.00 79.46 O ANISOU 3140 O ASN A 440 9702 12488 8001 17 1172 2042 O ATOM 3141 CB ASN A 440 74.220 50.905-390.923 1.00 91.00 C ANISOU 3141 CB ASN A 440 10773 14527 9277 53 1297 2273 C ATOM 3142 CG ASN A 440 74.454 51.454-389.523 1.00 91.25 C ANISOU 3142 CG ASN A 440 10804 14536 9329 -166 1291 2416 C ATOM 3143 OD1 ASN A 440 75.560 51.886-389.192 1.00 94.71 O ANISOU 3143 OD1 ASN A 440 11137 15167 9683 -206 1345 2604 O ATOM 3144 ND2 ASN A 440 73.418 51.428-388.691 1.00 87.13 N ANISOU 3144 ND2 ASN A 440 10401 13782 8922 -308 1234 2346 N ATOM 3145 N PHE A 441 71.302 50.168-390.931 1.00 66.09 N ANISOU 3145 N PHE A 441 7863 10873 6376 15 1176 1941 N ATOM 3146 CA PHE A 441 70.140 49.761-390.162 1.00 66.77 C ANISOU 3146 CA PHE A 441 8031 10762 6577 -107 1131 1857 C ATOM 3147 C PHE A 441 70.613 48.663-389.219 1.00 71.88 C ANISOU 3147 C PHE A 441 8584 11493 7235 -288 1129 1899 C ATOM 3148 O PHE A 441 69.854 47.767-388.854 1.00 71.27 O ANISOU 3148 O PHE A 441 8530 11331 7219 -351 1107 1811 O ATOM 3149 CB PHE A 441 69.052 49.248-391.113 1.00 62.67 C ANISOU 3149 CB PHE A 441 7557 10123 6130 19 1115 1717 C ATOM 3150 CG PHE A 441 67.796 48.780-390.424 1.00 68.66 C ANISOU 3150 CG PHE A 441 8387 10706 6994 -70 1085 1635 C ATOM 3151 CD1 PHE A 441 67.095 49.619-389.570 1.00 68.39 C ANISOU 3151 CD1 PHE A 441 8471 10518 6996 -145 1064 1639 C ATOM 3152 CD2 PHE A 441 67.300 47.505-390.653 1.00 71.21 C ANISOU 3152 CD2 PHE A 441 8660 11029 7368 -59 1087 1567 C ATOM 3153 CE1 PHE A 441 65.929 49.184-388.945 1.00 64.04 C ANISOU 3153 CE1 PHE A 441 7988 9817 6527 -203 1053 1569 C ATOM 3154 CE2 PHE A 441 66.136 47.069-390.031 1.00 60.19 C ANISOU 3154 CE2 PHE A 441 7326 9498 6044 -116 1077 1497 C ATOM 3155 CZ PHE A 441 65.453 47.909-389.176 1.00 56.95 C ANISOU 3155 CZ PHE A 441 7035 8937 5667 -184 1064 1493 C ATOM 3156 N ASN A 442 71.881 48.745-388.827 1.00103.18 N ANISOU 3156 N ASN A 442 12438 15643 11123 -371 1157 2044 N ATOM 3157 CA ASN A 442 72.527 47.681-388.063 1.00106.59 C ANISOU 3157 CA ASN A 442 12755 16202 11541 -547 1155 2103 C ATOM 3158 C ASN A 442 72.031 47.548-386.626 1.00102.64 C ANISOU 3158 C ASN A 442 12340 15556 11103 -784 1125 2104 C ATOM 3159 O ASN A 442 72.760 47.832-385.679 1.00108.94 O ANISOU 3159 O ASN A 442 13099 16395 11898 -971 1127 2245 O ATOM 3160 CB ASN A 442 74.045 47.871-388.071 1.00111.49 C ANISOU 3160 CB ASN A 442 13216 17079 12068 -576 1200 2287 C ATOM 3161 CG ASN A 442 74.788 46.632-387.614 1.00111.86 C ANISOU 3161 CG ASN A 442 13108 17308 12086 -723 1196 2348 C ATOM 3162 OD1 ASN A 442 74.178 45.616-387.281 1.00111.39 O ANISOU 3162 OD1 ASN A 442 13072 17189 12061 -801 1160 2242 O ATOM 3163 ND2 ASN A 442 76.115 46.709-387.600 1.00112.48 N ANISOU 3163 ND2 ASN A 442 13019 17632 12086 -757 1240 2528 N ATOM 3164 N ILE A 443 70.790 47.103-386.475 1.00 60.05 N ANISOU 3164 N ILE A 443 7060 9986 5772 -773 1099 1956 N ATOM 3165 CA ILE A 443 70.201 46.854-385.171 1.00 57.50 C ANISOU 3165 CA ILE A 443 6817 9479 5553 -940 1019 1880 C ATOM 3166 C ILE A 443 69.700 45.425-385.176 1.00 55.07 C ANISOU 3166 C ILE A 443 6482 9205 5236 -938 998 1746 C ATOM 3167 O ILE A 443 69.690 44.775-386.223 1.00 52.54 O ANISOU 3167 O ILE A 443 6095 9025 4842 -803 1056 1733 O ATOM 3168 CB ILE A 443 68.998 47.746-384.943 1.00 59.90 C ANISOU 3168 CB ILE A 443 7285 9519 5954 -878 988 1798 C ATOM 3169 CG1 ILE A 443 67.808 47.204-385.740 1.00 61.07 C ANISOU 3169 CG1 ILE A 443 7480 9609 6116 -714 1006 1654 C ATOM 3170 CG2 ILE A 443 69.326 49.199-385.319 1.00 58.94 C ANISOU 3170 CG2 ILE A 443 7195 9392 5806 -805 1019 1920 C ATOM 3171 CD1 ILE A 443 66.576 48.083-385.687 1.00 64.52 C ANISOU 3171 CD1 ILE A 443 8052 9814 6648 -628 980 1584 C ATOM 3172 N SER A 444 69.262 44.932-384.023 1.00 54.78 N ANISOU 3172 N SER A 444 6506 9039 5269 -1074 914 1645 N ATOM 3173 CA SER A 444 68.830 43.536-383.940 1.00 56.15 C ANISOU 3173 CA SER A 444 6654 9276 5404 -1067 891 1518 C ATOM 3174 C SER A 444 67.756 43.254-382.887 1.00 56.91 C ANISOU 3174 C SER A 444 6890 9154 5579 -1113 813 1347 C ATOM 3175 O SER A 444 68.043 42.703-381.824 1.00 56.88 O ANISOU 3175 O SER A 444 6893 9128 5591 -1276 721 1285 O ATOM 3176 CB SER A 444 70.035 42.622-383.713 1.00 60.26 C ANISOU 3176 CB SER A 444 7017 10034 5844 -1200 863 1584 C ATOM 3177 OG SER A 444 69.655 41.263-383.828 1.00 57.98 O ANISOU 3177 OG SER A 444 6692 9852 5484 -1157 849 1475 O ATOM 3178 N SER A 445 66.515 43.607-383.201 1.00 61.74 N ANISOU 3178 N SER A 445 7608 9610 6241 -963 845 1266 N ATOM 3179 CA SER A 445 65.425 43.373-382.272 1.00 60.17 C ANISOU 3179 CA SER A 445 7541 9215 6107 -964 789 1106 C ATOM 3180 C SER A 445 64.574 42.182-382.674 1.00 59.44 C ANISOU 3180 C SER A 445 7431 9211 5943 -831 825 993 C ATOM 3181 O SER A 445 64.369 41.907-383.861 1.00 49.77 O ANISOU 3181 O SER A 445 6129 8110 4671 -691 909 1045 O ATOM 3182 CB SER A 445 64.540 44.609-382.126 1.00 65.94 C ANISOU 3182 CB SER A 445 8398 9704 6953 -890 794 1101 C ATOM 3183 OG SER A 445 63.344 44.276-381.436 1.00 61.92 O ANISOU 3183 OG SER A 445 8002 9032 6491 -832 766 944 O ATOM 3184 N THR A 446 64.089 41.479-381.654 1.00 91.05 N ANISOU 3184 N THR A 446 11510 13146 9938 -874 759 841 N ATOM 3185 CA THR A 446 63.197 40.352-381.835 1.00 91.45 C ANISOU 3185 CA THR A 446 11558 13283 9904 -739 792 729 C ATOM 3186 C THR A 446 61.853 40.936-382.200 1.00 84.42 C ANISOU 3186 C THR A 446 10742 12240 9095 -566 859 707 C ATOM 3187 O THR A 446 60.935 40.217-382.606 1.00 85.49 O ANISOU 3187 O THR A 446 10858 12443 9182 -415 921 661 O ATOM 3188 CB THR A 446 63.036 39.551-380.533 1.00 98.24 C ANISOU 3188 CB THR A 446 12505 14100 10723 -820 690 547 C ATOM 3189 OG1 THR A 446 61.862 39.995-379.845 1.00103.73 O ANISOU 3189 OG1 THR A 446 13356 14557 11500 -736 680 425 O ATOM 3190 CG2 THR A 446 64.248 39.736-379.629 1.00 95.14 C ANISOU 3190 CG2 THR A 446 12108 13674 10366 -1064 569 561 C ATOM 3191 N TYR A 447 61.754 42.254-382.035 1.00 48.46 N ANISOU 3191 N TYR A 447 6261 7491 4662 -589 845 755 N ATOM 3192 CA TYR A 447 60.556 43.006-382.388 1.00 51.35 C ANISOU 3192 CA TYR A 447 6683 7707 5121 -440 893 755 C ATOM 3193 C TYR A 447 60.732 43.661-383.748 1.00 48.11 C ANISOU 3193 C TYR A 447 6187 7360 4733 -370 954 895 C ATOM 3194 O TYR A 447 59.781 44.172-384.339 1.00 46.31 O ANISOU 3194 O TYR A 447 5966 7051 4577 -243 992 911 O ATOM 3195 CB TYR A 447 60.246 44.050-381.314 1.00 51.95 C ANISOU 3195 CB TYR A 447 6901 7525 5314 -491 827 714 C ATOM 3196 CG TYR A 447 59.885 43.426-379.994 1.00 48.85 C ANISOU 3196 CG TYR A 447 6618 7026 4915 -529 761 546 C ATOM 3197 CD1 TYR A 447 60.868 42.937-379.152 1.00 53.95 C ANISOU 3197 CD1 TYR A 447 7280 7693 5526 -710 671 498 C ATOM 3198 CD2 TYR A 447 58.561 43.299-379.600 1.00 53.90 C ANISOU 3198 CD2 TYR A 447 7343 7552 5584 -376 784 430 C ATOM 3199 CE1 TYR A 447 60.546 42.346-377.944 1.00 62.05 C ANISOU 3199 CE1 TYR A 447 8422 8606 6547 -744 589 316 C ATOM 3200 CE2 TYR A 447 58.225 42.712-378.395 1.00 52.66 C ANISOU 3200 CE2 TYR A 447 7305 7297 5408 -384 721 252 C ATOM 3201 CZ TYR A 447 59.222 42.234-377.567 1.00 60.17 C ANISOU 3201 CZ TYR A 447 8289 8249 6323 -570 616 184 C ATOM 3202 OH TYR A 447 58.897 41.643-376.359 1.00 68.14 O ANISOU 3202 OH TYR A 447 9433 9143 7315 -580 531 -20 O ATOM 3203 N ALA A 448 61.961 43.618-384.242 1.00 87.24 N ANISOU 3203 N ALA A 448 11057 12464 9625 -449 957 991 N ATOM 3204 CA ALA A 448 62.283 44.194-385.533 1.00 88.86 C ANISOU 3204 CA ALA A 448 11193 12737 9832 -374 1007 1105 C ATOM 3205 C ALA A 448 62.003 43.180-386.621 1.00 83.91 C ANISOU 3205 C ALA A 448 10465 12262 9155 -258 1077 1120 C ATOM 3206 O ALA A 448 62.591 42.102-386.633 1.00 89.11 O ANISOU 3206 O ALA A 448 11046 13096 9714 -290 1090 1125 O ATOM 3207 CB ALA A 448 63.741 44.606-385.573 1.00 99.47 C ANISOU 3207 CB ALA A 448 12487 14187 11121 -485 992 1209 C ATOM 3208 N ALA A 449 61.107 43.532-387.535 1.00 56.87 N ANISOU 3208 N ALA A 449 7034 8768 5807 -126 1114 1140 N ATOM 3209 CA ALA A 449 60.809 42.676-388.678 1.00 55.96 C ANISOU 3209 CA ALA A 449 6820 8766 5678 -16 1181 1183 C ATOM 3210 C ALA A 449 61.143 43.696-389.781 1.00 52.29 C ANISOU 3210 C ALA A 449 6320 8268 5280 64 1183 1254 C ATOM 3211 O ALA A 449 60.493 44.736-389.890 1.00 49.23 O ANISOU 3211 O ALA A 449 5939 7774 4991 148 1198 1263 O ATOM 3212 CB ALA A 449 59.403 42.112-388.560 1.00 59.83 C ANISOU 3212 CB ALA A 449 7310 9204 6219 78 1217 1136 C ATOM 3213 N ILE A 450 62.154 43.384-390.585 1.00 62.23 N ANISOU 3213 N ILE A 450 7535 9613 6495 45 1151 1294 N ATOM 3214 CA ILE A 450 62.449 44.163-391.781 1.00 58.85 C ANISOU 3214 CA ILE A 450 7088 9160 6111 138 1140 1334 C ATOM 3215 C ILE A 450 61.818 43.534-393.019 1.00 58.64 C ANISOU 3215 C ILE A 450 6998 9121 6162 257 1171 1356 C ATOM 3216 O ILE A 450 61.189 42.479-392.939 1.00 63.34 O ANISOU 3216 O ILE A 450 7522 9798 6746 277 1196 1367 O ATOM 3217 CB ILE A 450 63.967 44.301-392.005 1.00 68.89 C ANISOU 3217 CB ILE A 450 8294 10581 7299 130 1126 1381 C ATOM 3218 CG1 ILE A 450 64.249 44.986-393.344 1.00 71.09 C ANISOU 3218 CG1 ILE A 450 8580 10837 7594 249 1130 1408 C ATOM 3219 CG2 ILE A 450 64.641 42.939-391.946 1.00 75.18 C ANISOU 3219 CG2 ILE A 450 8978 11541 8047 138 1140 1403 C ATOM 3220 CD1 ILE A 450 65.599 44.643-393.933 1.00 67.17 C ANISOU 3220 CD1 ILE A 450 7995 10511 7017 303 1143 1464 C ATOM 3221 N ASP A 451 61.991 44.189-394.162 1.00 94.89 N ANISOU 3221 N ASP A 451 11617 13618 10819 331 1174 1374 N ATOM 3222 CA ASP A 451 60.938 44.262-395.170 1.00102.00 C ANISOU 3222 CA ASP A 451 12461 14484 11810 423 1214 1420 C ATOM 3223 C ASP A 451 61.513 44.586-396.545 1.00 96.99 C ANISOU 3223 C ASP A 451 11774 13943 11135 499 1229 1465 C ATOM 3224 O ASP A 451 62.125 45.635-396.741 1.00 94.03 O ANISOU 3224 O ASP A 451 11389 13680 10659 486 1208 1462 O ATOM 3225 CB ASP A 451 59.892 45.306-394.778 1.00106.15 C ANISOU 3225 CB ASP A 451 13036 14829 12467 458 1178 1403 C ATOM 3226 CG ASP A 451 58.588 45.137-395.532 1.00105.51 C ANISOU 3226 CG ASP A 451 12876 14673 12539 516 1203 1454 C ATOM 3227 OD1 ASP A 451 57.825 44.205-395.202 1.00107.00 O ANISOU 3227 OD1 ASP A 451 12999 14938 12719 511 1272 1497 O ATOM 3228 OD2 ASP A 451 58.326 45.936-396.455 1.00104.32 O ANISOU 3228 OD2 ASP A 451 12729 14390 12519 568 1148 1453 O ATOM 3229 N GLY A 452 61.310 43.678-397.494 1.00 93.40 N ANISOU 3229 N GLY A 452 11279 13444 10766 580 1276 1524 N ATOM 3230 CA GLY A 452 62.406 42.922-398.072 1.00 99.84 C ANISOU 3230 CA GLY A 452 12051 14332 11550 671 1310 1580 C ATOM 3231 C GLY A 452 62.583 43.194-399.552 1.00 90.20 C ANISOU 3231 C GLY A 452 10906 12987 10379 748 1268 1540 C ATOM 3232 O GLY A 452 63.661 42.987-400.107 1.00 89.28 O ANISOU 3232 O GLY A 452 10835 12945 10143 781 1257 1510 O ATOM 3233 N ASN A 453 61.516 43.661-400.194 1.00 66.58 N ANISOU 3233 N ASN A 453 7920 9800 7579 785 1220 1532 N ATOM 3234 CA ASN A 453 61.640 44.590-401.310 1.00 68.52 C ANISOU 3234 CA ASN A 453 8240 9887 7906 868 1134 1463 C ATOM 3235 C ASN A 453 60.670 45.762-401.194 1.00 71.17 C ANISOU 3235 C ASN A 453 8644 10038 8361 828 1018 1375 C ATOM 3236 O ASN A 453 60.359 46.216-400.094 1.00 73.05 O ANISOU 3236 O ASN A 453 8895 10295 8566 744 1008 1356 O ATOM 3237 CB ASN A 453 61.429 43.862-402.639 1.00 69.03 C ANISOU 3237 CB ASN A 453 8256 9858 8113 960 1149 1525 C ATOM 3238 CG ASN A 453 60.234 42.930-402.610 1.00 67.65 C ANISOU 3238 CG ASN A 453 7979 9617 8109 914 1186 1632 C ATOM 3239 OD1 ASN A 453 60.078 42.074-403.480 1.00 64.97 O ANISOU 3239 OD1 ASN A 453 7576 9228 7883 973 1222 1728 O ATOM 3240 ND2 ASN A 453 59.382 43.092-401.604 1.00 67.44 N ANISOU 3240 ND2 ASN A 453 7932 9594 8100 822 1184 1627 N ATOM 3241 N TYR A 454 60.195 46.245-402.338 1.00 20.00 N ATOM 3242 CA TYR A 454 59.335 47.422-402.373 1.00 20.00 C ATOM 3243 C TYR A 454 58.308 47.321-403.497 1.00 20.00 C ATOM 3244 O TYR A 454 58.651 47.012-404.638 1.00 71.50 O ANISOU 3244 O TYR A 454 8651 9488 9026 888 788 1357 O ATOM 3245 CB TYR A 454 60.171 48.692-402.537 1.00 20.00 C ATOM 3246 CG TYR A 454 60.470 49.401-401.235 1.00 20.00 C ATOM 3247 CD1 TYR A 454 61.775 49.712-400.876 1.00 20.00 C ATOM 3248 CD2 TYR A 454 59.448 49.758-400.366 1.00 20.00 C ATOM 3249 CE1 TYR A 454 62.053 50.359-399.687 1.00 20.00 C ATOM 3250 CE2 TYR A 454 59.717 50.406-399.175 1.00 20.00 C ATOM 3251 CZ TYR A 454 61.021 50.704-398.840 1.00 20.00 C ATOM 3252 OH TYR A 454 61.294 51.348-397.656 1.00 20.00 O ATOM 3253 N LYS A 455 57.048 47.583-403.165 1.00 46.90 N ANISOU 3253 N LYS A 455 5558 6298 5965 771 667 1277 N ATOM 3254 CA LYS A 455 55.932 47.152-403.998 1.00 45.82 C ANISOU 3254 CA LYS A 455 5321 5983 6104 736 620 1350 C ATOM 3255 C LYS A 455 55.611 48.190-405.069 1.00 57.64 C ANISOU 3255 C LYS A 455 6880 7259 7761 750 431 1238 C ATOM 3256 O LYS A 455 55.867 49.380-404.891 1.00 51.94 O ANISOU 3256 O LYS A 455 6264 6527 6942 766 323 1103 O ATOM 3257 CB LYS A 455 54.695 46.883-403.139 1.00 47.00 C ANISOU 3257 CB LYS A 455 5370 6153 6333 657 653 1428 C ATOM 3258 CG LYS A 455 53.379 46.985-403.895 1.00 45.52 C ANISOU 3258 CG LYS A 455 5066 5786 6445 613 583 1510 C ATOM 3259 CD LYS A 455 52.265 47.494-402.995 1.00 48.21 C ANISOU 3259 CD LYS A 455 5332 6127 6858 555 565 1541 C ATOM 3260 CE LYS A 455 51.657 46.366-402.178 1.00 50.59 C ANISOU 3260 CE LYS A 455 5519 6581 7122 553 738 1682 C ATOM 3261 NZ LYS A 455 50.223 46.617-401.864 1.00 50.70 N ANISOU 3261 NZ LYS A 455 5409 6545 7311 516 717 1760 N ATOM 3262 N TYR A 456 55.047 47.729-406.181 1.00 44.13 N ANISOU 3262 N TYR A 456 5101 5369 6299 741 384 1299 N ATOM 3263 CA TYR A 456 54.678 48.616-407.275 1.00 49.17 C ANISOU 3263 CA TYR A 456 5791 5766 7127 736 181 1186 C ATOM 3264 C TYR A 456 53.161 48.636-407.451 1.00 47.83 C ANISOU 3264 C TYR A 456 5473 5449 7250 623 107 1285 C ATOM 3265 O TYR A 456 52.603 47.785-408.126 1.00 50.28 O ANISOU 3265 O TYR A 456 5667 5649 7788 588 137 1428 O ATOM 3266 CB TYR A 456 55.368 48.156-408.555 1.00 49.80 C ANISOU 3266 CB TYR A 456 5927 5714 7282 820 156 1159 C ATOM 3267 CG TYR A 456 55.241 49.098-409.731 1.00 48.59 C ANISOU 3267 CG TYR A 456 5872 5304 7287 838 -72 992 C ATOM 3268 CD1 TYR A 456 56.063 50.207-409.854 1.00 51.85 C ANISOU 3268 CD1 TYR A 456 6459 5739 7503 932 -181 778 C ATOM 3269 CD2 TYR A 456 54.321 48.856-410.734 1.00 52.61 C ANISOU 3269 CD2 TYR A 456 6297 5550 8141 764 -182 1052 C ATOM 3270 CE1 TYR A 456 55.953 51.053-410.934 1.00 54.98 C ANISOU 3270 CE1 TYR A 456 6959 5906 8026 962 -404 600 C ATOM 3271 CE2 TYR A 456 54.208 49.697-411.817 1.00 54.09 C ANISOU 3271 CE2 TYR A 456 6581 5484 8486 771 -414 881 C ATOM 3272 CZ TYR A 456 55.021 50.790-411.913 1.00 56.30 C ANISOU 3272 CZ TYR A 456 7050 5794 8549 875 -529 642 C ATOM 3273 OH TYR A 456 54.891 51.618-413.000 1.00 58.71 O ANISOU 3273 OH TYR A 456 7461 5848 8997 892 -775 449 O ATOM 3274 N GLN A 457 52.504 49.617-406.842 1.00 48.97 N ANISOU 3274 N GLN A 457 5613 5601 7392 571 15 1228 N ATOM 3275 CA GLN A 457 51.045 49.696-406.821 1.00 51.04 C ANISOU 3275 CA GLN A 457 5712 5771 7909 470 -42 1336 C ATOM 3276 C GLN A 457 50.515 50.640-407.895 1.00 53.64 C ANISOU 3276 C GLN A 457 6053 5857 8471 419 -293 1232 C ATOM 3277 O GLN A 457 51.286 51.266-408.620 1.00 54.06 O ANISOU 3277 O GLN A 457 6261 5814 8464 477 -426 1053 O ATOM 3278 CB GLN A 457 50.587 50.185-405.447 1.00 46.34 C ANISOU 3278 CB GLN A 457 5093 5335 7178 453 7 1346 C ATOM 3279 CG GLN A 457 49.154 49.859-405.091 1.00 47.40 C ANISOU 3279 CG GLN A 457 5028 5466 7514 382 47 1514 C ATOM 3280 CD GLN A 457 48.915 49.912-403.589 1.00 52.99 C ANISOU 3280 CD GLN A 457 5727 6365 8041 405 169 1542 C ATOM 3281 OE1 GLN A 457 49.860 49.993-402.803 1.00 49.44 O ANISOU 3281 OE1 GLN A 457 5409 6046 7330 455 241 1460 O ATOM 3282 NE2 GLN A 457 47.647 49.863-403.184 1.00 59.64 N ANISOU 3282 NE2 GLN A 457 6409 7218 9032 371 191 1664 N ATOM 3283 N TYR A 458 49.198 50.738-408.007 1.00 51.05 N ANISOU 3283 N TYR A 458 5556 5436 8403 317 -363 1342 N ATOM 3284 CA TYR A 458 48.595 51.748-408.864 1.00 57.54 C ANISOU 3284 CA TYR A 458 6372 6045 9446 248 -628 1237 C ATOM 3285 C TYR A 458 47.879 52.743-407.974 1.00 52.20 C ANISOU 3285 C TYR A 458 5653 5464 8718 219 -699 1211 C ATOM 3286 O TYR A 458 47.241 52.356-406.995 1.00 52.21 O ANISOU 3286 O TYR A 458 5529 5612 8698 207 -550 1362 O ATOM 3287 CB TYR A 458 47.613 51.108-409.839 1.00 54.90 C ANISOU 3287 CB TYR A 458 5851 5507 9502 136 -680 1405 C ATOM 3288 CG TYR A 458 46.519 52.029-410.345 1.00 61.55 C ANISOU 3288 CG TYR A 458 6587 6179 10619 18 -927 1380 C ATOM 3289 CD1 TYR A 458 46.663 52.714-411.537 1.00 59.16 C ANISOU 3289 CD1 TYR A 458 6377 5624 10479 -20 -1191 1206 C ATOM 3290 CD2 TYR A 458 45.334 52.188-409.642 1.00 61.15 C ANISOU 3290 CD2 TYR A 458 6340 6223 10672 -51 -901 1529 C ATOM 3291 CE1 TYR A 458 45.665 53.537-412.009 1.00 60.98 C ANISOU 3291 CE1 TYR A 458 6500 5702 10969 -142 -1437 1179 C ATOM 3292 CE2 TYR A 458 44.334 53.011-410.110 1.00 62.89 C ANISOU 3292 CE2 TYR A 458 6439 6304 11151 -164 -1132 1522 C ATOM 3293 CZ TYR A 458 44.507 53.683-411.292 1.00 66.20 C ANISOU 3293 CZ TYR A 458 6947 6475 11732 -218 -1406 1346 C ATOM 3294 OH TYR A 458 43.518 54.503-411.765 1.00 67.35 O ANISOU 3294 OH TYR A 458 6965 6484 12140 -343 -1658 1332 O ATOM 3295 N ASP A 459 47.985 54.025-408.314 1.00 53.37 N ANISOU 3295 N ASP A 459 5908 5533 8838 224 -930 1017 N ATOM 3296 CA ASP A 459 47.472 55.086-407.459 1.00 56.41 C ANISOU 3296 CA ASP A 459 6279 6022 9133 222 -1007 978 C ATOM 3297 C ASP A 459 46.181 55.663-408.000 1.00 55.24 C ANISOU 3297 C ASP A 459 5965 5729 9295 107 -1219 1015 C ATOM 3298 O ASP A 459 46.204 56.633-408.747 1.00 64.75 O ANISOU 3298 O ASP A 459 7244 6804 10555 89 -1475 844 O ATOM 3299 CB ASP A 459 48.501 56.203-407.325 1.00 54.47 C ANISOU 3299 CB ASP A 459 6262 5840 8594 323 -1114 751 C ATOM 3300 CG ASP A 459 48.064 57.267-406.354 1.00 51.86 C ANISOU 3300 CG ASP A 459 5926 5633 8145 337 -1173 733 C ATOM 3301 OD1 ASP A 459 48.933 58.008-405.849 1.00 60.75 O ANISOU 3301 OD1 ASP A 459 7220 6881 8981 432 -1177 615 O ATOM 3302 OD2 ASP A 459 46.845 57.355-406.085 1.00 52.16 O ANISOU 3302 OD2 ASP A 459 5782 5655 8382 261 -1208 855 O ATOM 3303 N LYS A 460 45.057 55.085-407.597 1.00 57.27 N ANISOU 3303 N LYS A 460 5993 6023 9744 37 -1116 1237 N ATOM 3304 CA LYS A 460 43.761 55.472-408.145 1.00 60.89 C ANISOU 3304 CA LYS A 460 6244 6355 10538 -87 -1298 1323 C ATOM 3305 C LYS A 460 43.516 56.977-408.076 1.00 60.23 C ANISOU 3305 C LYS A 460 6210 6266 10410 -90 -1552 1159 C ATOM 3306 O LYS A 460 42.643 57.497-408.766 1.00 61.79 O ANISOU 3306 O LYS A 460 6271 6327 10878 -199 -1776 1166 O ATOM 3307 CB LYS A 460 42.632 54.712-407.437 1.00 57.92 C ANISOU 3307 CB LYS A 460 5613 6096 10299 -120 -1108 1598 C ATOM 3308 CG LYS A 460 42.158 55.341-406.130 1.00 58.28 C ANISOU 3308 CG LYS A 460 5623 6335 10184 -54 -1051 1621 C ATOM 3309 CD LYS A 460 41.872 54.285-405.067 1.00 62.54 C ANISOU 3309 CD LYS A 460 6070 7061 10631 14 -746 1810 C ATOM 3310 CE LYS A 460 41.191 53.053-405.657 1.00 70.68 C ANISOU 3310 CE LYS A 460 6886 8049 11920 -54 -627 2045 C ATOM 3311 NZ LYS A 460 41.433 51.816-404.838 1.00 61.91 N ANISOU 3311 NZ LYS A 460 5773 7116 10634 38 -324 2167 N ATOM 3312 N TYR A 461 44.289 57.677-407.254 1.00 60.79 N ANISOU 3312 N TYR A 461 6466 6488 10143 27 -1523 1023 N ATOM 3313 CA TYR A 461 44.085 59.106-407.068 1.00 61.13 C ANISOU 3313 CA TYR A 461 6559 6565 10104 48 -1743 890 C ATOM 3314 C TYR A 461 44.796 59.950-408.112 1.00 59.40 C ANISOU 3314 C TYR A 461 6526 6216 9828 65 -2003 631 C ATOM 3315 O TYR A 461 44.149 60.629-408.904 1.00 65.37 O ANISOU 3315 O TYR A 461 7212 6835 10790 -19 -2276 558 O ATOM 3316 CB TYR A 461 44.483 59.524-405.659 1.00 59.59 C ANISOU 3316 CB TYR A 461 6461 6591 9591 165 -1596 894 C ATOM 3317 CG TYR A 461 43.518 59.009-404.633 1.00 56.94 C ANISOU 3317 CG TYR A 461 5934 6366 9336 157 -1412 1115 C ATOM 3318 CD1 TYR A 461 42.301 59.627-404.439 1.00 57.38 C ANISOU 3318 CD1 TYR A 461 5803 6433 9566 116 -1529 1203 C ATOM 3319 CD2 TYR A 461 43.808 57.885-403.877 1.00 56.26 C ANISOU 3319 CD2 TYR A 461 5848 6380 9150 200 -1125 1231 C ATOM 3320 CE1 TYR A 461 41.405 59.158-403.514 1.00 59.74 C ANISOU 3320 CE1 TYR A 461 5928 6840 9932 136 -1353 1402 C ATOM 3321 CE2 TYR A 461 42.913 57.406-402.944 1.00 54.60 C ANISOU 3321 CE2 TYR A 461 5475 6272 8997 216 -959 1414 C ATOM 3322 CZ TYR A 461 41.711 58.051-402.769 1.00 55.56 C ANISOU 3322 CZ TYR A 461 5418 6403 9288 192 -1068 1498 C ATOM 3323 OH TYR A 461 40.803 57.595-401.847 1.00 57.13 O ANISOU 3323 OH TYR A 461 5456 6713 9538 234 -897 1676 O ATOM 3324 N ASN A 462 46.122 59.922-408.118 1.00 59.23 N ANISOU 3324 N ASN A 462 6736 6244 9524 180 -1928 489 N ATOM 3325 CA ASN A 462 46.869 60.631-409.143 1.00 60.96 C ANISOU 3325 CA ASN A 462 7147 6350 9664 230 -2153 234 C ATOM 3326 C ASN A 462 46.741 59.911-410.471 1.00 64.62 C ANISOU 3326 C ASN A 462 7572 6552 10427 143 -2243 214 C ATOM 3327 O ASN A 462 47.067 60.459-411.523 1.00 63.18 O ANISOU 3327 O ASN A 462 7517 6207 10281 156 -2481 -2 O ATOM 3328 CB ASN A 462 48.338 60.748-408.750 1.00 63.08 C ANISOU 3328 CB ASN A 462 7655 6771 9542 395 -2019 116 C ATOM 3329 CG ASN A 462 48.559 61.726-407.615 1.00 68.86 C ANISOU 3329 CG ASN A 462 8457 7727 9980 483 -1994 104 C ATOM 3330 OD1 ASN A 462 48.350 62.929-407.770 1.00 74.67 O ANISOU 3330 OD1 ASN A 462 9239 8479 10652 511 -2221 -22 O ATOM 3331 ND2 ASN A 462 48.989 61.216-406.466 1.00 68.05 N ANISOU 3331 ND2 ASN A 462 8362 7796 9699 528 -1728 238 N ATOM 3332 N ASP A 463 46.256 58.677-410.408 1.00 76.20 N ANISOU 3332 N ASP A 463 8868 7978 12105 61 -2052 441 N ATOM 3333 CA ASP A 463 46.112 57.830-411.582 1.00 77.04 C ANISOU 3333 CA ASP A 463 8918 7838 12516 -26 -2094 483 C ATOM 3334 C ASP A 463 47.468 57.465-412.170 1.00 79.06 C ANISOU 3334 C ASP A 463 9405 8038 12597 98 -2041 328 C ATOM 3335 O ASP A 463 47.689 57.606-413.368 1.00 63.90 O ANISOU 3335 O ASP A 463 7575 5881 10823 86 -2236 174 O ATOM 3336 CB ASP A 463 45.256 58.515-412.639 1.00 82.96 C ANISOU 3336 CB ASP A 463 9585 8345 13592 -161 -2433 396 C ATOM 3337 CG ASP A 463 44.881 57.589-413.764 1.00 67.09 C ANISOU 3337 CG ASP A 463 7467 6058 11965 -284 -2471 500 C ATOM 3338 OD1 ASP A 463 44.943 58.015-414.938 1.00 71.70 O ANISOU 3338 OD1 ASP A 463 8134 6382 12727 -334 -2745 317 O ATOM 3339 OD2 ASP A 463 44.526 56.429-413.471 1.00 65.46 O ANISOU 3339 OD2 ASP A 463 7097 5893 11883 -327 -2229 766 O ATOM 3340 N VAL A 464 48.376 56.994-411.320 1.00 62.20 N ANISOU 3340 N VAL A 464 7360 6118 10155 218 -1781 369 N ATOM 3341 CA VAL A 464 49.710 56.635-411.770 1.00 61.77 C ANISOU 3341 CA VAL A 464 7506 6056 9908 353 -1705 245 C ATOM 3342 C VAL A 464 50.223 55.407-411.050 1.00 61.03 C ANISOU 3342 C VAL A 464 7371 6129 9689 397 -1380 431 C ATOM 3343 O VAL A 464 49.850 55.153-409.907 1.00 62.03 O ANISOU 3343 O VAL A 464 7391 6443 9733 371 -1213 586 O ATOM 3344 CB VAL A 464 50.714 57.761-411.501 1.00 74.88 C ANISOU 3344 CB VAL A 464 9392 7862 11198 506 -1779 12 C ATOM 3345 CG1 VAL A 464 51.863 57.688-412.504 1.00 85.71 C ANISOU 3345 CG1 VAL A 464 10968 9129 12467 641 -1827 -180 C ATOM 3346 CG2 VAL A 464 50.030 59.112-411.555 1.00 74.57 C ANISOU 3346 CG2 VAL A 464 9353 7795 11184 466 -2051 -119 C ATOM 3347 N ASN A 465 51.094 54.657-411.720 1.00 64.35 N ANISOU 3347 N ASN A 465 7883 6479 10088 473 -1301 407 N ATOM 3348 CA ASN A 465 51.761 53.523-411.099 1.00 62.55 C ANISOU 3348 CA ASN A 465 7636 6428 9703 533 -1011 557 C ATOM 3349 C ASN A 465 52.944 54.008-410.279 1.00 63.09 C ANISOU 3349 C ASN A 465 7864 6743 9363 670 -913 448 C ATOM 3350 O ASN A 465 53.698 54.873-410.718 1.00 69.04 O ANISOU 3350 O ASN A 465 8794 7484 9954 776 -1041 238 O ATOM 3351 CB ASN A 465 52.211 52.522-412.156 1.00 67.07 C ANISOU 3351 CB ASN A 465 8227 6834 10423 569 -968 596 C ATOM 3352 CG ASN A 465 51.043 51.843-412.847 1.00 76.21 C ANISOU 3352 CG ASN A 465 9194 7767 11997 421 -1016 774 C ATOM 3353 OD1 ASN A 465 49.990 51.621-412.243 1.00 72.91 O ANISOU 3353 OD1 ASN A 465 8583 7411 11707 308 -959 956 O ATOM 3354 ND2 ASN A 465 51.224 51.509-414.120 1.00 82.10 N ANISOU 3354 ND2 ASN A 465 9987 8248 12960 430 -1118 733 N ATOM 3355 N ARG A 466 53.112 53.444-409.091 1.00 55.46 N ANISOU 3355 N ARG A 466 6837 6005 8232 668 -689 593 N ATOM 3356 CA ARG A 466 53.983 54.043-408.098 1.00 54.16 C ANISOU 3356 CA ARG A 466 6784 6073 7720 752 -612 527 C ATOM 3357 C ARG A 466 54.623 52.972-407.206 1.00 53.02 C ANISOU 3357 C ARG A 466 6602 6134 7410 773 -349 671 C ATOM 3358 O ARG A 466 54.002 51.965-406.895 1.00 52.11 O ANISOU 3358 O ARG A 466 6343 6029 7428 700 -225 841 O ATOM 3359 CB ARG A 466 53.146 55.042-407.283 1.00 54.76 C ANISOU 3359 CB ARG A 466 6819 6199 7787 690 -704 522 C ATOM 3360 CG ARG A 466 53.808 55.644-406.057 1.00 50.52 C ANISOU 3360 CG ARG A 466 6367 5892 6936 747 -614 507 C ATOM 3361 CD ARG A 466 52.782 56.374-405.180 1.00 53.76 C ANISOU 3361 CD ARG A 466 6700 6334 7393 678 -673 557 C ATOM 3362 NE ARG A 466 52.861 57.834-405.274 1.00 58.46 N ANISOU 3362 NE ARG A 466 7402 6936 7873 730 -867 410 N ATOM 3363 CZ ARG A 466 52.161 58.578-406.125 1.00 56.42 C ANISOU 3363 CZ ARG A 466 7132 6526 7780 703 -1105 307 C ATOM 3364 NH1 ARG A 466 51.331 57.994-406.980 1.00 51.28 N ANISOU 3364 NH1 ARG A 466 6360 5682 7443 611 -1178 346 N ATOM 3365 NH2 ARG A 466 52.295 59.902-406.130 1.00 60.79 N ANISOU 3365 NH2 ARG A 466 7788 7122 8186 765 -1277 173 N ATOM 3366 N TRP A 467 55.873 53.178-406.808 1.00 47.92 N ANISOU 3366 N TRP A 467 6076 5661 6470 875 -267 607 N ATOM 3367 CA TRP A 467 56.516 52.278-405.853 1.00 47.47 C ANISOU 3367 CA TRP A 467 5981 5812 6243 879 -43 732 C ATOM 3368 C TRP A 467 56.195 52.691-404.416 1.00 48.62 C ANISOU 3368 C TRP A 467 6100 6101 6272 816 14 786 C ATOM 3369 O TRP A 467 56.363 53.853-404.041 1.00 56.48 O ANISOU 3369 O TRP A 467 7183 7140 7138 842 -74 699 O ATOM 3370 CB TRP A 467 58.032 52.274-406.046 1.00 45.99 C ANISOU 3370 CB TRP A 467 5911 5759 5806 1009 26 665 C ATOM 3371 CG TRP A 467 58.493 51.587-407.274 1.00 52.97 C ANISOU 3371 CG TRP A 467 6815 6534 6779 1092 26 643 C ATOM 3372 CD1 TRP A 467 58.936 52.171-408.425 1.00 53.17 C ANISOU 3372 CD1 TRP A 467 6964 6428 6809 1206 -110 479 C ATOM 3373 CD2 TRP A 467 58.591 50.177-407.492 1.00 47.41 C ANISOU 3373 CD2 TRP A 467 6013 5837 6164 1085 169 786 C ATOM 3374 NE1 TRP A 467 59.289 51.216-409.339 1.00 53.50 N ANISOU 3374 NE1 TRP A 467 6995 6376 6958 1270 -60 515 N ATOM 3375 CE2 TRP A 467 59.083 49.978-408.781 1.00 49.22 C ANISOU 3375 CE2 TRP A 467 6309 5925 6468 1194 114 716 C ATOM 3376 CE3 TRP A 467 58.292 49.065-406.691 1.00 47.41 C ANISOU 3376 CE3 TRP A 467 5878 5957 6177 1006 334 966 C ATOM 3377 CZ2 TRP A 467 59.296 48.706-409.318 1.00 49.40 C ANISOU 3377 CZ2 TRP A 467 6262 5918 6590 1226 224 840 C ATOM 3378 CZ3 TRP A 467 58.499 47.806-407.222 1.00 50.16 C ANISOU 3378 CZ3 TRP A 467 6155 6299 6606 1038 439 1083 C ATOM 3379 CH2 TRP A 467 58.998 47.634-408.521 1.00 49.69 C ANISOU 3379 CH2 TRP A 467 6156 6094 6630 1145 387 1031 C ATOM 3380 N VAL A 468 55.748 51.739-403.607 1.00 42.13 N ANISOU 3380 N VAL A 468 5165 5353 5491 746 159 930 N ATOM 3381 CA VAL A 468 55.467 52.021-402.206 1.00 40.87 C ANISOU 3381 CA VAL A 468 4991 5308 5229 696 219 975 C ATOM 3382 C VAL A 468 56.104 50.997-401.273 1.00 40.40 C ANISOU 3382 C VAL A 468 4905 5424 5020 682 408 1064 C ATOM 3383 O VAL A 468 56.269 49.837-401.630 1.00 40.09 O ANISOU 3383 O VAL A 468 4800 5412 5020 688 506 1137 O ATOM 3384 CB VAL A 468 53.956 52.073-401.948 1.00 42.30 C ANISOU 3384 CB VAL A 468 5055 5392 5625 623 176 1041 C ATOM 3385 CG1 VAL A 468 53.324 53.165-402.787 1.00 42.77 C ANISOU 3385 CG1 VAL A 468 5130 5290 5832 621 -35 950 C ATOM 3386 CG2 VAL A 468 53.321 50.733-402.259 1.00 41.65 C ANISOU 3386 CG2 VAL A 468 4831 5281 5715 589 279 1174 C ATOM 3387 N PRO A 469 56.470 51.427-400.065 1.00 69.59 N ANISOU 3387 N PRO A 469 8653 9238 8550 661 452 1063 N ATOM 3388 CA PRO A 469 57.051 50.525-399.071 1.00 72.04 C ANISOU 3388 CA PRO A 469 8942 9704 8725 627 604 1132 C ATOM 3389 C PRO A 469 56.112 49.363-398.812 1.00 73.90 C ANISOU 3389 C PRO A 469 9058 9933 9088 588 691 1224 C ATOM 3390 O PRO A 469 54.924 49.585-398.574 1.00 72.48 O ANISOU 3390 O PRO A 469 8824 9666 9048 563 656 1245 O ATOM 3391 CB PRO A 469 57.129 51.404-397.820 1.00 77.95 C ANISOU 3391 CB PRO A 469 9758 10499 9361 591 590 1116 C ATOM 3392 CG PRO A 469 56.136 52.511-398.079 1.00 76.20 C ANISOU 3392 CG PRO A 469 9549 10138 9265 601 450 1071 C ATOM 3393 CD PRO A 469 56.338 52.787-399.529 1.00 75.79 C ANISOU 3393 CD PRO A 469 9517 10008 9272 662 351 1003 C ATOM 3394 N LEU A 470 56.641 48.145-398.847 1.00 62.44 N ANISOU 3394 N LEU A 470 7557 8590 7576 593 807 1285 N ATOM 3395 CA LEU A 470 55.808 46.959-398.717 1.00 57.86 C ANISOU 3395 CA LEU A 470 6860 8031 7092 579 898 1382 C ATOM 3396 C LEU A 470 55.390 46.706-397.271 1.00 55.66 C ANISOU 3396 C LEU A 470 6577 7835 6738 537 965 1391 C ATOM 3397 O LEU A 470 54.322 46.149-397.018 1.00 53.09 O ANISOU 3397 O LEU A 470 6165 7499 6508 540 1013 1451 O ATOM 3398 CB LEU A 470 56.517 45.737-399.308 1.00 58.51 C ANISOU 3398 CB LEU A 470 6891 8214 7128 615 991 1451 C ATOM 3399 CG LEU A 470 55.659 44.491-399.546 1.00 58.51 C ANISOU 3399 CG LEU A 470 6758 8232 7241 625 1080 1577 C ATOM 3400 CD1 LEU A 470 54.222 44.858-399.939 1.00 60.51 C ANISOU 3400 CD1 LEU A 470 6937 8325 7728 611 1023 1619 C ATOM 3401 CD2 LEU A 470 56.302 43.583-400.593 1.00 54.73 C ANISOU 3401 CD2 LEU A 470 6234 7785 6775 681 1130 1652 C ATOM 3402 N ALA A 471 56.226 47.132-396.330 1.00 81.08 N ANISOU 3402 N ALA A 471 9887 11130 9791 503 967 1335 N ATOM 3403 CA ALA A 471 55.946 46.938-394.909 1.00 81.63 C ANISOU 3403 CA ALA A 471 9977 11247 9790 460 1013 1323 C ATOM 3404 C ALA A 471 54.521 47.334-394.537 1.00 70.41 C ANISOU 3404 C ALA A 471 8527 9717 8509 476 986 1327 C ATOM 3405 O ALA A 471 53.797 46.567-393.905 1.00 70.46 O ANISOU 3405 O ALA A 471 8483 9763 8525 490 1060 1352 O ATOM 3406 CB ALA A 471 56.939 47.712-394.070 1.00 83.88 C ANISOU 3406 CB ALA A 471 10370 11568 9932 409 981 1272 C ATOM 3407 N ALA A 472 54.135 48.545-394.919 1.00 50.79 N ANISOU 3407 N ALA A 472 6072 7109 6117 486 879 1299 N ATOM 3408 CA ALA A 472 52.786 49.043-394.674 1.00 54.04 C ANISOU 3408 CA ALA A 472 6438 7421 6675 507 840 1315 C ATOM 3409 C ALA A 472 51.742 47.960-394.927 1.00 53.64 C ANISOU 3409 C ALA A 472 6248 7394 6740 540 925 1402 C ATOM 3410 O ALA A 472 50.739 47.857-394.220 1.00 48.51 O ANISOU 3410 O ALA A 472 5552 6738 6140 572 964 1426 O ATOM 3411 CB ALA A 472 52.512 50.240-395.564 1.00 56.05 C ANISOU 3411 CB ALA A 472 6700 7556 7041 517 698 1290 C ATOM 3412 N ASP A 473 51.993 47.155-395.948 1.00 55.91 N ANISOU 3412 N ASP A 473 6465 7712 7067 545 960 1459 N ATOM 3413 CA ASP A 473 51.046 46.143-396.364 1.00 52.71 C ANISOU 3413 CA ASP A 473 5912 7334 6782 578 1043 1576 C ATOM 3414 C ASP A 473 51.072 44.909-395.459 1.00 53.69 C ANISOU 3414 C ASP A 473 6016 7622 6762 609 1185 1603 C ATOM 3415 O ASP A 473 50.056 44.548-394.869 1.00 54.96 O ANISOU 3415 O ASP A 473 6110 7819 6953 656 1251 1645 O ATOM 3416 CB ASP A 473 51.313 45.764-397.818 1.00 52.49 C ANISOU 3416 CB ASP A 473 5822 7257 6865 575 1021 1640 C ATOM 3417 CG ASP A 473 50.129 45.100-398.457 1.00 59.57 C ANISOU 3417 CG ASP A 473 6548 8125 7962 593 1068 1790 C ATOM 3418 OD1 ASP A 473 49.718 45.532-399.553 1.00 61.69 O ANISOU 3418 OD1 ASP A 473 6757 8247 8436 568 972 1829 O ATOM 3419 OD2 ASP A 473 49.596 44.152-397.846 1.00 61.88 O ANISOU 3419 OD2 ASP A 473 6762 8544 8204 635 1196 1871 O ATOM 3420 N ILE A 474 52.231 44.267-395.353 1.00 51.17 N ANISOU 3420 N ILE A 474 5751 7413 6278 591 1228 1575 N ATOM 3421 CA ILE A 474 52.373 43.055-394.547 1.00 56.41 C ANISOU 3421 CA ILE A 474 6400 8247 6786 615 1341 1584 C ATOM 3422 C ILE A 474 51.809 43.234-393.139 1.00 54.99 C ANISOU 3422 C ILE A 474 6279 8075 6539 630 1357 1507 C ATOM 3423 O ILE A 474 51.338 42.277-392.525 1.00 64.67 O ANISOU 3423 O ILE A 474 7468 9417 7687 686 1449 1519 O ATOM 3424 CB ILE A 474 53.848 42.586-394.455 1.00 68.42 C ANISOU 3424 CB ILE A 474 7983 9884 8129 575 1351 1543 C ATOM 3425 CG1 ILE A 474 54.635 43.456-393.473 1.00 70.52 C ANISOU 3425 CG1 ILE A 474 8386 10124 8286 506 1285 1424 C ATOM 3426 CG2 ILE A 474 54.502 42.582-395.833 1.00 60.97 C ANISOU 3426 CG2 ILE A 474 7007 8912 7248 581 1326 1602 C ATOM 3427 CD1 ILE A 474 56.122 43.129-393.413 1.00 77.66 C ANISOU 3427 CD1 ILE A 474 9329 11148 9031 455 1288 1403 C ATOM 3428 N ALA A 475 51.857 44.464-392.633 1.00 64.92 N ANISOU 3428 N ALA A 475 7634 9211 7823 594 1267 1425 N ATOM 3429 CA ALA A 475 51.354 44.767-391.296 1.00 66.32 C ANISOU 3429 CA ALA A 475 7885 9357 7958 614 1271 1349 C ATOM 3430 C ALA A 475 49.861 44.481-391.190 1.00 65.36 C ANISOU 3430 C ALA A 475 7659 9235 7938 715 1334 1410 C ATOM 3431 O ALA A 475 49.395 43.922-390.198 1.00 67.89 O ANISOU 3431 O ALA A 475 8003 9618 8176 779 1402 1367 O ATOM 3432 CB ALA A 475 51.646 46.214-390.931 1.00 84.94 C ANISOU 3432 CB ALA A 475 10352 11576 10347 566 1161 1286 C ATOM 3433 N GLY A 476 49.108 44.866-392.212 1.00 88.92 N ANISOU 3433 N GLY A 476 10527 12153 11105 733 1308 1510 N ATOM 3434 CA GLY A 476 47.694 44.553-392.256 1.00 89.62 C ANISOU 3434 CA GLY A 476 10477 12265 11308 826 1378 1608 C ATOM 3435 C GLY A 476 47.533 43.066-392.466 1.00 92.56 C ANISOU 3435 C GLY A 476 10751 12810 11608 884 1513 1697 C ATOM 3436 O GLY A 476 46.593 42.447-391.973 1.00 98.48 O ANISOU 3436 O GLY A 476 11426 13656 12335 990 1616 1745 O ATOM 3437 N LEU A 477 48.478 42.496-393.204 1.00 45.61 N ANISOU 3437 N LEU A 477 4803 6915 5613 829 1516 1725 N ATOM 3438 CA LEU A 477 48.487 41.072-393.474 1.00 47.38 C ANISOU 3438 CA LEU A 477 4936 7314 5752 883 1636 1822 C ATOM 3439 C LEU A 477 48.709 40.293-392.187 1.00 50.06 C ANISOU 3439 C LEU A 477 5360 7804 5856 936 1705 1717 C ATOM 3440 O LEU A 477 48.556 39.075-392.157 1.00 46.87 O ANISOU 3440 O LEU A 477 4887 7580 5341 1009 1811 1782 O ATOM 3441 CB LEU A 477 49.583 40.742-394.482 1.00 45.28 C ANISOU 3441 CB LEU A 477 4670 7056 5478 818 1610 1861 C ATOM 3442 CG LEU A 477 49.439 39.453-395.285 1.00 46.08 C ANISOU 3442 CG LEU A 477 4633 7290 5586 871 1717 2031 C ATOM 3443 CD1 LEU A 477 48.143 39.467-396.078 1.00 48.73 C ANISOU 3443 CD1 LEU A 477 4799 7564 6154 909 1752 2209 C ATOM 3444 CD2 LEU A 477 50.639 39.265-396.207 1.00 50.07 C ANISOU 3444 CD2 LEU A 477 5164 7781 6080 818 1678 2048 C ATOM 3445 N CYS A 478 49.073 41.002-391.120 1.00 57.29 N ANISOU 3445 N CYS A 478 6427 8643 6696 900 1636 1554 N ATOM 3446 CA CYS A 478 49.219 40.386-389.802 1.00 61.72 C ANISOU 3446 CA CYS A 478 7088 9302 7059 941 1673 1425 C ATOM 3447 C CYS A 478 47.945 40.510-388.977 1.00 66.00 C ANISOU 3447 C CYS A 478 7626 9829 7622 1069 1724 1397 C ATOM 3448 O CYS A 478 47.511 39.543-388.351 1.00 71.20 O ANISOU 3448 O CYS A 478 8278 10636 8140 1180 1815 1367 O ATOM 3449 CB CYS A 478 50.370 41.024-389.036 1.00 59.52 C ANISOU 3449 CB CYS A 478 6979 8936 6699 824 1568 1273 C ATOM 3450 SG CYS A 478 51.972 40.618-389.706 1.00 70.35 S ANISOU 3450 SG CYS A 478 8357 10394 7980 705 1532 1291 S ATOM 3451 N ALA A 479 47.359 41.707-388.972 1.00 90.11 N ANISOU 3451 N ALA A 479 10685 12716 10838 1066 1665 1403 N ATOM 3452 CA ALA A 479 46.105 41.950-388.267 1.00 92.20 C ANISOU 3452 CA ALA A 479 10927 12958 11146 1202 1714 1395 C ATOM 3453 C ALA A 479 45.151 40.852-388.666 1.00 90.57 C ANISOU 3453 C ALA A 479 10551 12940 10923 1337 1859 1534 C ATOM 3454 O ALA A 479 44.237 40.479-387.923 1.00 95.81 O ANISOU 3454 O ALA A 479 11197 13684 11521 1493 1949 1514 O ATOM 3455 CB ALA A 479 45.545 43.300-388.629 1.00 81.73 C ANISOU 3455 CB ALA A 479 9564 11462 10029 1179 1632 1447 C ATOM 3456 N ARG A 480 45.378 40.369-389.880 1.00 79.70 N ANISOU 3456 N ARG A 480 9045 11628 9610 1283 1883 1684 N ATOM 3457 CA ARG A 480 44.676 39.232-390.421 1.00 82.17 C ANISOU 3457 CA ARG A 480 9184 12132 9906 1388 2024 1856 C ATOM 3458 C ARG A 480 45.203 37.978-389.759 1.00 89.64 C ANISOU 3458 C ARG A 480 10202 13278 10581 1451 2096 1772 C ATOM 3459 O ARG A 480 44.957 37.733-388.582 1.00 91.19 O ANISOU 3459 O ARG A 480 10500 13531 10618 1551 2126 1628 O ATOM 3460 CB ARG A 480 44.923 39.141-391.927 1.00 80.57 C ANISOU 3460 CB ARG A 480 8846 11898 9868 1293 2006 2036 C ATOM 3461 CG ARG A 480 43.992 39.990-392.766 1.00 77.59 C ANISOU 3461 CG ARG A 480 8322 11386 9774 1269 1968 2181 C ATOM 3462 CD ARG A 480 42.624 39.349-392.838 1.00 79.49 C ANISOU 3462 CD ARG A 480 8361 11772 10068 1410 2115 2370 C ATOM 3463 NE ARG A 480 41.616 40.209-393.444 1.00 82.10 N ANISOU 3463 NE ARG A 480 8535 11984 10674 1388 2071 2505 N ATOM 3464 CZ ARG A 480 41.317 40.197-394.738 1.00 85.93 C ANISOU 3464 CZ ARG A 480 8849 12409 11393 1309 2050 2703 C ATOM 3465 NH1 ARG A 480 41.962 39.369-395.553 1.00 85.99 N ANISOU 3465 NH1 ARG A 480 8830 12457 11386 1259 2080 2793 N ATOM 3466 NH2 ARG A 480 40.380 41.010-395.218 1.00 81.37 N ANISOU 3466 NH2 ARG A 480 8123 11722 11070 1277 1991 2815 N ATOM 3467 N THR A 481 45.959 37.211-390.539 1.00129.64 N ANISOU 3467 N THR A 481 15219 18441 15597 1392 2112 1855 N ATOM 3468 CA THR A 481 46.433 35.884-390.160 1.00141.62 C ANISOU 3468 CA THR A 481 16759 20188 16862 1454 2183 1823 C ATOM 3469 C THR A 481 46.859 35.777-388.699 1.00143.99 C ANISOU 3469 C THR A 481 17251 20511 16946 1474 2136 1568 C ATOM 3470 O THR A 481 47.663 36.574-388.211 1.00145.62 O ANISOU 3470 O THR A 481 17606 20555 17168 1348 2011 1413 O ATOM 3471 CB THR A 481 47.578 35.407-391.082 1.00140.15 C ANISOU 3471 CB THR A 481 16546 20043 16660 1347 2152 1896 C ATOM 3472 OG1 THR A 481 47.195 35.563-392.455 1.00131.80 O ANISOU 3472 OG1 THR A 481 15329 18918 15832 1322 2177 2119 O ATOM 3473 CG2 THR A 481 47.892 33.942-390.828 1.00148.81 C ANISOU 3473 CG2 THR A 481 17622 21414 17505 1433 2233 1910 C ATOM 3474 N ASP A 482 46.303 34.771-388.024 1.00198.18 N ANISOU 3474 N ASP A 482 24109 27581 23609 1637 2235 1533 N ATOM 3475 CA ASP A 482 46.497 34.566-386.590 1.00205.51 C ANISOU 3475 CA ASP A 482 25221 28530 24333 1686 2191 1279 C ATOM 3476 C ASP A 482 46.429 35.885-385.838 1.00220.77 C ANISOU 3476 C ASP A 482 27295 30193 26394 1626 2088 1129 C ATOM 3477 O ASP A 482 45.785 36.836-386.286 1.00221.23 O ANISOU 3477 O ASP A 482 27285 30107 26666 1623 2090 1230 O ATOM 3478 CB ASP A 482 47.824 33.855-386.311 1.00200.62 C ANISOU 3478 CB ASP A 482 24695 28009 23524 1580 2112 1160 C ATOM 3479 CG ASP A 482 47.772 32.372-386.626 1.00199.36 C ANISOU 3479 CG ASP A 482 24430 28161 23156 1696 2216 1256 C ATOM 3480 OD1 ASP A 482 46.665 31.854-386.882 1.00198.08 O ANISOU 3480 OD1 ASP A 482 24144 28149 22970 1877 2359 1396 O ATOM 3481 OD2 ASP A 482 48.839 31.728-386.614 1.00193.56 O ANISOU 3481 OD2 ASP A 482 23728 27537 22279 1612 2157 1206 O ATOM 3482 N ASN A 483 47.089 35.946-384.689 1.00224.72 N ANISOU 3482 N ASN A 483 27990 30624 26771 1574 1990 894 N ATOM 3483 CA ASN A 483 47.136 37.205-383.967 1.00228.62 C ANISOU 3483 CA ASN A 483 28624 30848 27392 1506 1887 770 C ATOM 3484 C ASN A 483 48.476 37.933-383.985 1.00239.54 C ANISOU 3484 C ASN A 483 30103 32072 28839 1273 1744 716 C ATOM 3485 O ASN A 483 49.521 37.374-384.326 1.00242.12 O ANISOU 3485 O ASN A 483 30417 32500 29078 1160 1709 725 O ATOM 3486 CB ASN A 483 46.532 37.102-382.562 1.00223.68 C ANISOU 3486 CB ASN A 483 28150 30181 26657 1650 1888 565 C ATOM 3487 CG ASN A 483 46.734 35.752-381.921 1.00220.26 C ANISOU 3487 CG ASN A 483 27779 29959 25952 1736 1911 425 C ATOM 3488 OD1 ASN A 483 47.699 35.048-382.212 1.00217.22 O ANISOU 3488 OD1 ASN A 483 27379 29700 25455 1625 1871 425 O ATOM 3489 ND2 ASN A 483 45.824 35.387-381.023 1.00223.58 N ANISOU 3489 ND2 ASN A 483 28272 30426 26254 1949 1970 297 N ATOM 3490 N VAL A 484 48.413 39.195-383.596 1.00134.50 N ANISOU 3490 N VAL A 484 16887 18531 15684 1218 1668 673 N ATOM 3491 CA VAL A 484 49.414 40.170-383.976 1.00132.90 C ANISOU 3491 CA VAL A 484 16719 18182 15595 1027 1561 705 C ATOM 3492 C VAL A 484 50.271 40.630-382.796 1.00133.27 C ANISOU 3492 C VAL A 484 16956 18075 15606 906 1443 537 C ATOM 3493 O VAL A 484 51.318 40.030-382.513 1.00133.38 O ANISOU 3493 O VAL A 484 17016 18162 15500 792 1391 466 O ATOM 3494 CB VAL A 484 48.707 41.357-384.619 1.00132.14 C ANISOU 3494 CB VAL A 484 16553 17946 15709 1050 1559 826 C ATOM 3495 CG1 VAL A 484 47.677 40.838-385.607 1.00132.35 C ANISOU 3495 CG1 VAL A 484 16387 18109 15792 1175 1675 991 C ATOM 3496 CG2 VAL A 484 47.994 42.174-383.561 1.00133.12 C ANISOU 3496 CG2 VAL A 484 16789 17894 15897 1128 1529 731 C ATOM 3497 N ARG A 496 53.313 35.741-396.786 1.00134.19 N ANISOU 3497 N ARG A 496 19427 16314 15245 4926 -3462 -1180 N ATOM 3498 CA ARG A 496 52.513 35.067-395.767 1.00138.49 C ANISOU 3498 CA ARG A 496 20561 16947 15110 5684 -3815 -1428 C ATOM 3499 C ARG A 496 51.088 34.807-396.250 1.00139.31 C ANISOU 3499 C ARG A 496 20707 17596 14627 6215 -3222 -1191 C ATOM 3500 O ARG A 496 50.162 34.653-395.453 1.00141.95 O ANISOU 3500 O ARG A 496 21503 18078 14352 6832 -3321 -1383 O ATOM 3501 CB ARG A 496 52.480 35.900-394.487 1.00138.26 C ANISOU 3501 CB ARG A 496 20905 16614 15012 5662 -4252 -1885 C ATOM 3502 CG ARG A 496 53.838 36.417-394.059 1.00137.16 C ANISOU 3502 CG ARG A 496 20608 15939 15568 5070 -4725 -2003 C ATOM 3503 CD ARG A 496 53.849 36.741-392.574 1.00139.43 C ANISOU 3503 CD ARG A 496 21348 15837 15792 5274 -5354 -2413 C ATOM 3504 NE ARG A 496 55.180 37.128-392.115 1.00139.39 N ANISOU 3504 NE ARG A 496 21133 15292 16535 4753 -5856 -2435 N ATOM 3505 CZ ARG A 496 55.541 37.199-390.837 1.00142.42 C ANISOU 3505 CZ ARG A 496 21796 15194 17125 4860 -6589 -2720 C ATOM 3506 NH1 ARG A 496 54.672 36.902-389.878 1.00145.69 N ANISOU 3506 NH1 ARG A 496 22774 15585 16997 5495 -6919 -3060 N ATOM 3507 NH2 ARG A 496 56.776 37.562-390.517 1.00142.65 N ANISOU 3507 NH2 ARG A 496 21500 14746 17955 4360 -6998 -2629 N ATOM 3508 N GLY A 497 50.930 34.743-397.566 1.00139.31 N ANISOU 3508 N GLY A 497 20196 17850 14887 5998 -2597 -724 N ATOM 3509 CA GLY A 497 49.623 34.720-398.194 1.00139.71 C ANISOU 3509 CA GLY A 497 20116 18350 14619 6345 -1959 -372 C ATOM 3510 C GLY A 497 49.572 35.935-399.093 1.00134.89 C ANISOU 3510 C GLY A 497 18993 17734 14525 5651 -1548 -269 C ATOM 3511 O GLY A 497 49.711 37.058-398.616 1.00131.89 O ANISOU 3511 O GLY A 497 18689 17235 14188 5294 -1740 -632 O ATOM 3512 N GLN A 498 49.398 35.719-400.392 1.00 84.20 N ANISOU 3512 N GLN A 498 12046 11401 8547 5501 -993 220 N ATOM 3513 CA GLN A 498 49.641 36.781-401.360 1.00 80.49 C ANISOU 3513 CA GLN A 498 11055 10777 8749 4812 -715 248 C ATOM 3514 C GLN A 498 49.036 38.122-400.965 1.00 77.86 C ANISOU 3514 C GLN A 498 10815 10554 8216 4631 -803 -82 C ATOM 3515 O GLN A 498 48.029 38.184-400.262 1.00 79.06 O ANISOU 3515 O GLN A 498 11299 10967 7773 5068 -827 -146 O ATOM 3516 CB GLN A 498 49.206 36.368-402.769 1.00 81.98 C ANISOU 3516 CB GLN A 498 10677 10964 9509 4781 -52 791 C ATOM 3517 CG GLN A 498 49.923 37.133-403.881 1.00 79.37 C ANISOU 3517 CG GLN A 498 9805 10289 10064 4064 165 740 C ATOM 3518 CD GLN A 498 51.444 36.992-403.832 1.00 77.78 C ANISOU 3518 CD GLN A 498 9593 9802 10159 3698 -100 608 C ATOM 3519 OE1 GLN A 498 52.015 36.554-402.832 1.00 78.20 O ANISOU 3519 OE1 GLN A 498 10044 9858 9810 3876 -577 446 O ATOM 3520 NE2 GLN A 498 52.105 37.367-404.922 1.00 76.56 N ANISOU 3520 NE2 GLN A 498 8972 9342 10776 3193 205 662 N ATOM 3521 N ILE A 499 49.678 39.189-401.423 1.00 81.00 N ANISOU 3521 N ILE A 499 10919 10763 9095 4037 -830 -283 N ATOM 3522 CA ILE A 499 49.232 40.541-401.145 1.00 78.74 C ANISOU 3522 CA ILE A 499 10667 10606 8643 3865 -927 -592 C ATOM 3523 C ILE A 499 48.294 40.993-402.237 1.00 79.36 C ANISOU 3523 C ILE A 499 10274 10769 9109 3769 -517 -421 C ATOM 3524 O ILE A 499 48.363 40.520-403.371 1.00 80.81 O ANISOU 3524 O ILE A 499 10013 10757 9936 3626 -139 -152 O ATOM 3525 CB ILE A 499 50.398 41.522-401.076 1.00 75.96 C ANISOU 3525 CB ILE A 499 10238 10043 8581 3380 -1159 -894 C ATOM 3526 CG1 ILE A 499 51.374 41.260-402.224 1.00 75.81 C ANISOU 3526 CG1 ILE A 499 9764 9719 9322 2992 -924 -718 C ATOM 3527 CG2 ILE A 499 51.103 41.403-399.737 1.00 75.85 C ANISOU 3527 CG2 ILE A 499 10699 9884 8236 3482 -1598 -1142 C ATOM 3528 CD1 ILE A 499 52.389 40.162-401.952 1.00 76.82 C ANISOU 3528 CD1 ILE A 499 10000 9609 9579 3015 -1077 -551 C ATOM 3529 N LEU A 500 47.443 41.946-401.893 1.00 93.80 N ANISOU 3529 N LEU A 500 12173 12833 10632 3833 -592 -611 N ATOM 3530 CA LEU A 500 46.287 42.268-402.708 1.00 95.61 C ANISOU 3530 CA LEU A 500 11995 13138 11194 3864 -251 -466 C ATOM 3531 C LEU A 500 46.588 42.970-404.030 1.00 95.78 C ANISOU 3531 C LEU A 500 11404 12882 12107 3364 -52 -681 C ATOM 3532 O LEU A 500 46.387 42.400-405.105 1.00 98.31 O ANISOU 3532 O LEU A 500 11279 12946 13127 3286 360 -431 O ATOM 3533 CB LEU A 500 45.299 43.092-401.886 1.00 95.11 C ANISOU 3533 CB LEU A 500 12189 13422 10528 4100 -422 -621 C ATOM 3534 CG LEU A 500 44.982 42.501-400.513 1.00 95.39 C ANISOU 3534 CG LEU A 500 12893 13694 9658 4618 -586 -562 C ATOM 3535 CD1 LEU A 500 43.974 43.364-399.779 1.00 94.99 C ANISOU 3535 CD1 LEU A 500 13064 13968 9061 4838 -659 -694 C ATOM 3536 CD2 LEU A 500 44.475 41.073-400.639 1.00 98.94 C ANISOU 3536 CD2 LEU A 500 13409 14175 10008 5108 -267 -81 C ATOM 3537 N ASN A 501 47.064 44.206-403.951 1.00 43.69 N ANISOU 3537 N ASN A 501 4782 6330 5488 3073 -320 -1157 N ATOM 3538 CA ASN A 501 47.015 45.089-405.100 1.00 44.87 C ANISOU 3538 CA ASN A 501 4398 6326 6326 2732 -174 -1530 C ATOM 3539 C ASN A 501 48.349 45.303-405.771 1.00 44.04 C ANISOU 3539 C ASN A 501 4120 5928 6685 2350 -157 -1751 C ATOM 3540 O ASN A 501 48.495 46.205-406.592 1.00 45.06 O ANISOU 3540 O ASN A 501 3897 5976 7246 2110 -121 -2199 O ATOM 3541 CB ASN A 501 46.423 46.426-404.680 1.00 44.40 C ANISOU 3541 CB ASN A 501 4365 6614 5891 2783 -441 -1940 C ATOM 3542 CG ASN A 501 45.670 46.332-403.368 1.00 43.38 C ANISOU 3542 CG ASN A 501 4721 6848 4913 3189 -640 -1705 C ATOM 3543 OD1 ASN A 501 46.172 45.752-402.402 1.00 41.69 O ANISOU 3543 OD1 ASN A 501 4989 6675 4176 3359 -819 -1498 O ATOM 3544 ND2 ASN A 501 44.459 46.893-403.321 1.00 44.81 N ANISOU 3544 ND2 ASN A 501 4771 7270 4983 3361 -606 -1772 N ATOM 3545 N VAL A 502 49.322 44.472-405.428 1.00 54.67 N ANISOU 3545 N VAL A 502 5707 7124 7943 2334 -182 -1459 N ATOM 3546 CA VAL A 502 50.609 44.515-406.109 1.00 54.19 C ANISOU 3546 CA VAL A 502 5467 6744 8377 1996 -82 -1541 C ATOM 3547 C VAL A 502 50.401 44.324-407.601 1.00 56.95 C ANISOU 3547 C VAL A 502 5273 6748 9618 1771 347 -1598 C ATOM 3548 O VAL A 502 49.385 43.786-408.029 1.00 59.37 O ANISOU 3548 O VAL A 502 5345 6996 10218 1901 607 -1392 O ATOM 3549 CB VAL A 502 51.572 43.421-405.588 1.00 53.04 C ANISOU 3549 CB VAL A 502 5581 6448 8122 2036 -130 -1145 C ATOM 3550 CG1 VAL A 502 52.835 43.337-406.463 1.00 52.99 C ANISOU 3550 CG1 VAL A 502 5318 6068 8749 1689 85 -1120 C ATOM 3551 CG2 VAL A 502 51.941 43.682-404.135 1.00 50.98 C ANISOU 3551 CG2 VAL A 502 5816 6401 7152 2209 -578 -1193 C ATOM 3552 N ILE A 503 51.361 44.771-408.397 1.00 45.32 N ANISOU 3552 N ILE A 503 3584 5018 8619 1468 451 -1854 N ATOM 3553 CA ILE A 503 51.284 44.576-409.831 1.00 48.32 C ANISOU 3553 CA ILE A 503 3452 4985 9923 1246 858 -1960 C ATOM 3554 C ILE A 503 52.688 44.333-410.343 1.00 47.67 C ANISOU 3554 C ILE A 503 3344 4576 10192 1001 1022 -1867 C ATOM 3555 O ILE A 503 52.929 44.286-411.546 1.00 50.01 O ANISOU 3555 O ILE A 503 3259 4482 11260 788 1352 -2009 O ATOM 3556 CB ILE A 503 50.659 45.794-410.533 1.00 50.69 C ANISOU 3556 CB ILE A 503 3384 5334 10542 1169 805 -2653 C ATOM 3557 CG1 ILE A 503 51.717 46.865-410.820 1.00 50.29 C ANISOU 3557 CG1 ILE A 503 3338 5328 10443 1027 660 -3153 C ATOM 3558 CG2 ILE A 503 49.514 46.361-409.692 1.00 50.37 C ANISOU 3558 CG2 ILE A 503 3488 5741 9908 1431 515 -2784 C ATOM 3559 CD1 ILE A 503 51.156 48.144-411.410 1.00 53.08 C ANISOU 3559 CD1 ILE A 503 3349 5852 10966 1059 508 -3934 C ATOM 3560 N LYS A 504 53.607 44.156-409.407 1.00 68.94 N ANISOU 3560 N LYS A 504 6427 7396 12372 1048 801 -1611 N ATOM 3561 CA LYS A 504 55.018 44.078-409.721 1.00 68.20 C ANISOU 3561 CA LYS A 504 6332 7034 12547 846 925 -1487 C ATOM 3562 C LYS A 504 55.754 44.230-408.407 1.00 65.52 C ANISOU 3562 C LYS A 504 6402 6917 11577 965 565 -1313 C ATOM 3563 O LYS A 504 55.383 45.059-407.579 1.00 64.60 O ANISOU 3563 O LYS A 504 6511 7139 10896 1130 242 -1546 O ATOM 3564 CB LYS A 504 55.395 45.231-410.655 1.00 69.83 C ANISOU 3564 CB LYS A 504 6293 7145 13093 685 1032 -2028 C ATOM 3565 CG LYS A 504 56.767 45.154-411.325 1.00 70.10 C ANISOU 3565 CG LYS A 504 6245 6830 13559 490 1307 -1896 C ATOM 3566 CD LYS A 504 57.191 46.552-411.794 1.00 71.66 C ANISOU 3566 CD LYS A 504 6369 7152 13708 517 1268 -2459 C ATOM 3567 CE LYS A 504 58.026 46.541-413.074 1.00 73.96 C ANISOU 3567 CE LYS A 504 6388 7030 14683 336 1674 -2558 C ATOM 3568 NZ LYS A 504 58.103 47.909-413.688 1.00 76.88 N ANISOU 3568 NZ LYS A 504 6635 7583 14994 471 1609 -3265 N ATOM 3569 N LEU A 505 56.791 43.428-408.205 1.00 40.92 N ANISOU 3569 N LEU A 505 3344 3587 8616 891 622 -894 N ATOM 3570 CA LEU A 505 57.671 43.628-407.060 1.00 39.28 C ANISOU 3570 CA LEU A 505 3420 3464 8040 957 306 -755 C ATOM 3571 C LEU A 505 59.128 43.881-407.492 1.00 39.42 C ANISOU 3571 C LEU A 505 3300 3196 8483 759 524 -587 C ATOM 3572 O LEU A 505 59.571 43.431-408.552 1.00 40.41 O ANISOU 3572 O LEU A 505 3157 3023 9173 571 905 -438 O ATOM 3573 CB LEU A 505 57.566 42.457-406.085 1.00 38.93 C ANISOU 3573 CB LEU A 505 3588 3477 7727 1124 33 -441 C ATOM 3574 CG LEU A 505 56.156 42.152-405.561 1.00 39.21 C ANISOU 3574 CG LEU A 505 3828 3816 7254 1420 -147 -538 C ATOM 3575 CD1 LEU A 505 56.167 40.851-404.765 1.00 40.00 C ANISOU 3575 CD1 LEU A 505 4152 3939 7106 1655 -385 -255 C ATOM 3576 CD2 LEU A 505 55.599 43.292-404.719 1.00 38.16 C ANISOU 3576 CD2 LEU A 505 3957 3988 6553 1564 -453 -884 C ATOM 3577 N ALA A 506 59.866 44.622-406.679 1.00 90.10 N ANISOU 3577 N ALA A 506 9897 9679 14657 831 334 -567 N ATOM 3578 CA ALA A 506 61.212 44.999-407.063 1.00 90.79 C ANISOU 3578 CA ALA A 506 9858 9520 15117 724 599 -357 C ATOM 3579 C ALA A 506 62.036 43.768-407.413 1.00 91.12 C ANISOU 3579 C ALA A 506 9644 9269 15709 527 789 111 C ATOM 3580 O ALA A 506 62.841 43.801-408.344 1.00 92.02 O ANISOU 3580 O ALA A 506 9530 9144 16291 387 1197 269 O ATOM 3581 CB ALA A 506 61.875 45.784-405.960 1.00 90.73 C ANISOU 3581 CB ALA A 506 10059 9583 14832 879 395 -259 C ATOM 3582 N ILE A 507 61.832 42.688-406.667 1.00111.29 N ANISOU 3582 N ILE A 507 12244 11867 18174 560 480 311 N ATOM 3583 CA ILE A 507 62.486 41.418-406.960 1.00112.20 C ANISOU 3583 CA ILE A 507 12096 11791 18744 441 556 746 C ATOM 3584 C ILE A 507 61.511 40.253-406.832 1.00112.62 C ANISOU 3584 C ILE A 507 12180 11902 18708 541 497 830 C ATOM 3585 O ILE A 507 60.613 40.274-405.990 1.00112.56 O ANISOU 3585 O ILE A 507 12479 12095 18192 767 108 669 O ATOM 3586 CB ILE A 507 63.688 41.174-406.028 1.00113.20 C ANISOU 3586 CB ILE A 507 12212 11832 18966 441 156 992 C ATOM 3587 CG1 ILE A 507 63.208 40.863-404.609 1.00113.18 C ANISOU 3587 CG1 ILE A 507 12606 11953 18443 620 -463 769 C ATOM 3588 CG2 ILE A 507 64.616 42.379-406.028 1.00113.67 C ANISOU 3588 CG2 ILE A 507 12159 11798 19234 404 376 1087 C ATOM 3589 CD1 ILE A 507 64.228 41.173-403.536 1.00115.00 C ANISOU 3589 CD1 ILE A 507 12828 11974 18891 583 -920 939 C ATOM 3590 N GLU A 508 61.695 39.239-407.670 1.00118.20 N ANISOU 3590 N GLU A 508 12578 12434 19897 426 936 1117 N ATOM 3591 CA GLU A 508 60.802 38.086-407.686 1.00119.37 C ANISOU 3591 CA GLU A 508 12722 12624 20011 593 1007 1328 C ATOM 3592 C GLU A 508 61.485 36.867-408.297 1.00120.65 C ANISOU 3592 C GLU A 508 12501 12547 20794 451 1476 1790 C ATOM 3593 O GLU A 508 62.064 36.946-409.379 1.00121.95 O ANISOU 3593 O GLU A 508 12576 12625 21135 536 1842 2008 O ATOM 3594 CB GLU A 508 59.520 38.412-408.456 1.00119.53 C ANISOU 3594 CB GLU A 508 12818 12727 19870 708 1215 1085 C ATOM 3595 CG GLU A 508 58.324 38.718-407.570 1.00119.24 C ANISOU 3595 CG GLU A 508 13140 13056 19110 1034 765 836 C ATOM 3596 CD GLU A 508 57.099 39.128-408.364 1.00119.73 C ANISOU 3596 CD GLU A 508 13165 13221 19105 1117 983 597 C ATOM 3597 OE1 GLU A 508 57.195 40.092-409.151 1.00119.48 O ANISOU 3597 OE1 GLU A 508 12986 13040 19370 888 1176 285 O ATOM 3598 OE2 GLU A 508 56.041 38.485-408.201 1.00120.99 O ANISOU 3598 OE2 GLU A 508 13430 13615 18924 1450 946 709 O ATOM 3599 N THR A 509 61.412 35.742-407.594 1.00196.26 N ANISOU 3599 N THR A 509 22600 22663 29306 1367 750 2056 N ATOM 3600 CA THR A 509 61.141 35.748-406.163 1.00195.48 C ANISOU 3600 CA THR A 509 22852 22609 28814 1373 48 1700 C ATOM 3601 C THR A 509 62.229 35.009-405.391 1.00196.92 C ANISOU 3601 C THR A 509 23005 22573 29244 1262 -423 1854 C ATOM 3602 O THR A 509 62.656 35.451-404.325 1.00196.49 O ANISOU 3602 O THR A 509 23101 22400 29157 1128 -891 1631 O ATOM 3603 CB THR A 509 59.776 35.109-405.844 1.00196.38 C ANISOU 3603 CB THR A 509 23431 23034 28149 1828 -367 1429 C ATOM 3604 OG1 THR A 509 59.901 33.682-405.843 1.00199.72 O ANISOU 3604 OG1 THR A 509 24005 23581 28298 2267 -596 1646 O ATOM 3605 CG2 THR A 509 58.740 35.522-406.879 1.00195.56 C ANISOU 3605 CG2 THR A 509 23280 23132 27891 1933 88 1345 C ATOM 3606 N PRO A 510 62.674 33.883-405.937 1.00 20.00 N ATOM 3607 CA PRO A 510 61.878 33.136-406.917 1.00 20.00 C ATOM 3608 C PRO A 510 61.271 31.874-406.314 1.00 20.00 C ATOM 3609 O PRO A 510 62.017 30.947-405.995 1.00192.29 O ANISOU 3609 O PRO A 510 22362 22209 28489 2287 -626 2854 O ATOM 3610 CB PRO A 510 62.904 32.766-407.992 1.00 20.00 C ATOM 3611 CG PRO A 510 64.206 32.717-407.272 1.00 20.00 C ATOM 3612 CD PRO A 510 64.125 33.788-406.230 1.00 20.00 C ATOM 3613 OXT PRO A 510 60.056 31.779-406.146 1.00 30.00 O TER 3614 PRO A 510 ATOM 3615 N ASN B 21 -13.596 51.841-381.169 1.00197.86 N ANISOU 3615 N ASN B 21 24661 26429 24087 2495 2157 811 N ATOM 3616 CA ASN B 21 -13.962 51.287-382.465 1.00197.34 C ANISOU 3616 CA ASN B 21 24318 26496 24167 2489 2234 1084 C ATOM 3617 C ASN B 21 -13.035 51.378-383.677 1.00195.79 C ANISOU 3617 C ASN B 21 24054 26410 23928 2308 2221 1166 C ATOM 3618 O ASN B 21 -13.461 51.786-384.765 1.00193.89 O ANISOU 3618 O ASN B 21 23800 26047 23823 2096 2111 1224 O ATOM 3619 CB ASN B 21 -15.344 51.830-382.860 1.00196.39 C ANISOU 3619 CB ASN B 21 24139 26174 24305 2396 2133 1184 C ATOM 3620 CG ASN B 21 -15.929 51.136-384.062 1.00196.45 C ANISOU 3620 CG ASN B 21 23856 26290 24496 2408 2196 1454 C ATOM 3621 OD1 ASN B 21 -15.337 50.200-384.594 1.00197.29 O ANISOU 3621 OD1 ASN B 21 23792 26618 24550 2493 2331 1592 O ATOM 3622 ND2 ASN B 21 -17.101 51.590-384.499 1.00195.76 N ANISOU 3622 ND2 ASN B 21 23705 26048 24628 2319 2091 1540 N ATOM 3623 N ASN B 22 -11.776 51.058-383.432 1.00 20.00 N ATOM 3624 CA ASN B 22 -10.487 51.573-383.879 1.00 20.00 C ATOM 3625 C ASN B 22 -10.104 52.865-383.163 1.00 20.00 C ATOM 3626 O ASN B 22 -9.334 53.688-383.821 1.00254.18 O ANISOU 3626 O ASN B 22 31650 33792 31136 1860 2028 1018 O ATOM 3627 CB ASN B 22 -10.494 51.793-385.393 1.00 20.00 C ATOM 3628 CG ASN B 22 -10.509 50.492-386.171 1.00 20.00 C ATOM 3629 OD1 ASN B 22 -10.098 49.448-385.664 1.00 20.00 O ATOM 3630 ND2 ASN B 22 -10.984 50.548-387.409 1.00 20.00 N ATOM 3631 N SER B 23 -10.494 53.048-382.010 1.00 20.00 N ATOM 3632 CA SER B 23 -10.432 54.283-381.236 1.00 20.00 C ATOM 3633 C SER B 23 -11.591 55.211-381.584 1.00 20.00 C ATOM 3634 O SER B 23 -11.332 56.496-381.417 1.00208.55 O ANISOU 3634 O SER B 23 26321 27532 25386 1610 1732 647 O ATOM 3635 CB SER B 23 -9.098 54.995-381.470 1.00 20.00 C ATOM 3636 OG SER B 23 -8.984 55.431-382.813 1.00 20.00 O ATOM 3637 N THR B 24 -12.717 54.755-381.833 1.00174.40 N ANISOU 3637 N THR B 24 21903 23194 21167 1942 1862 707 N ATOM 3638 CA THR B 24 -13.969 55.505-381.826 1.00173.40 C ANISOU 3638 CA THR B 24 21796 22849 21241 1843 1757 759 C ATOM 3639 C THR B 24 -13.948 56.750-382.715 1.00171.27 C ANISOU 3639 C THR B 24 21516 22530 21027 1598 1654 820 C ATOM 3640 O THR B 24 -14.102 57.868-382.238 1.00276.83 O ANISOU 3640 O THR B 24 35042 35792 34348 1455 1557 709 O ATOM 3641 CB THR B 24 -14.520 55.883-380.422 1.00174.52 C ANISOU 3641 CB THR B 24 22160 22769 21382 1888 1683 581 C ATOM 3642 OG1 THR B 24 -15.631 56.781-380.533 1.00173.61 O ANISOU 3642 OG1 THR B 24 22071 22452 21439 1784 1575 641 O ATOM 3643 CG2 THR B 24 -13.427 56.514-379.556 1.00174.83 C ANISOU 3643 CG2 THR B 24 22401 22766 21262 1787 1616 379 C ATOM 3644 N GLY B 25 -13.710 56.548-384.009 1.00 91.93 N ANISOU 3644 N GLY B 25 11277 12568 11084 1555 1679 1001 N ATOM 3645 CA GLY B 25 -13.615 57.657-384.939 1.00 83.53 C ANISOU 3645 CA GLY B 25 10198 11473 10065 1357 1593 1056 C ATOM 3646 C GLY B 25 -14.952 58.370-385.004 1.00 73.33 C ANISOU 3646 C GLY B 25 8951 9991 8921 1266 1469 1077 C ATOM 3647 O GLY B 25 -15.748 58.129-385.913 1.00 65.50 O ANISOU 3647 O GLY B 25 7850 8986 8050 1195 1423 1192 O ATOM 3648 N THR B 26 -15.204 59.249-384.038 1.00 73.25 N ANISOU 3648 N THR B 26 9104 9827 8900 1274 1409 966 N ATOM 3649 CA THR B 26 -16.472 59.967-383.987 1.00 65.31 C ANISOU 3649 CA THR B 26 8148 8653 8014 1208 1294 995 C ATOM 3650 C THR B 26 -16.112 61.278-384.651 1.00 62.16 C ANISOU 3650 C THR B 26 7785 8241 7593 1022 1209 1011 C ATOM 3651 O THR B 26 -15.272 62.022-384.144 1.00 69.73 O ANISOU 3651 O THR B 26 8861 9196 8436 923 1188 927 O ATOM 3652 CB THR B 26 -17.000 60.295-382.578 1.00 65.78 C ANISOU 3652 CB THR B 26 8390 8538 8064 1249 1249 886 C ATOM 3653 OG1 THR B 26 -17.342 59.090-381.882 1.00 72.50 O ANISOU 3653 OG1 THR B 26 9226 9395 8925 1452 1333 853 O ATOM 3654 CG2 THR B 26 -18.230 61.174-382.682 1.00 60.36 C ANISOU 3654 CG2 THR B 26 7735 7704 7495 1196 1138 949 C ATOM 3655 N ALA B 27 -16.738 61.566-385.787 1.00 71.87 N ANISOU 3655 N ALA B 27 8910 9469 8930 978 1153 1116 N ATOM 3656 CA ALA B 27 -16.521 62.847-386.449 1.00 70.71 C ANISOU 3656 CA ALA B 27 8803 9311 8753 833 1072 1126 C ATOM 3657 C ALA B 27 -17.484 63.869-385.878 1.00 73.47 C ANISOU 3657 C ALA B 27 9274 9517 9123 793 969 1108 C ATOM 3658 O ALA B 27 -18.317 63.543-385.034 1.00 78.59 O ANISOU 3658 O ALA B 27 9971 10065 9826 876 957 1096 O ATOM 3659 CB ALA B 27 -16.701 62.725-387.952 1.00 66.58 C ANISOU 3659 CB ALA B 27 8131 8839 8326 812 1047 1224 C ATOM 3660 N ALA B 28 -17.358 65.105-386.337 1.00 69.64 N ANISOU 3660 N ALA B 28 8838 9033 8588 681 900 1119 N ATOM 3661 CA ALA B 28 -18.247 66.172-385.915 1.00 69.74 C ANISOU 3661 CA ALA B 28 8955 8939 8603 643 807 1131 C ATOM 3662 C ALA B 28 -18.308 67.191-387.032 1.00 68.44 C ANISOU 3662 C ALA B 28 8768 8829 8406 572 739 1171 C ATOM 3663 O ALA B 28 -17.275 67.634-387.538 1.00 68.77 O ANISOU 3663 O ALA B 28 8799 8967 8362 503 770 1160 O ATOM 3664 CB ALA B 28 -17.751 66.817-384.630 1.00 73.97 C ANISOU 3664 CB ALA B 28 9641 9412 9054 576 815 1076 C ATOM 3665 N LEU B 29 -19.525 67.552-387.419 1.00 46.03 N ANISOU 3665 N LEU B 29 5924 5936 5629 604 643 1213 N ATOM 3666 CA LEU B 29 -19.737 68.441-388.547 1.00 46.41 C ANISOU 3666 CA LEU B 29 5957 6033 5642 569 564 1231 C ATOM 3667 C LEU B 29 -20.893 69.374-388.273 1.00 44.18 C ANISOU 3667 C LEU B 29 5756 5696 5336 583 463 1264 C ATOM 3668 O LEU B 29 -21.923 68.971-387.742 1.00 44.45 O ANISOU 3668 O LEU B 29 5791 5647 5450 650 421 1292 O ATOM 3669 CB LEU B 29 -20.037 67.630-389.806 1.00 46.36 C ANISOU 3669 CB LEU B 29 5811 6045 5758 611 529 1245 C ATOM 3670 CG LEU B 29 -20.572 68.415-390.998 1.00 43.23 C ANISOU 3670 CG LEU B 29 5409 5660 5357 600 410 1239 C ATOM 3671 CD1 LEU B 29 -19.418 68.868-391.882 1.00 44.10 C ANISOU 3671 CD1 LEU B 29 5513 5852 5392 553 448 1212 C ATOM 3672 CD2 LEU B 29 -21.560 67.552-391.778 1.00 45.71 C ANISOU 3672 CD2 LEU B 29 5599 5924 5846 648 320 1262 C ATOM 3673 N ALA B 30 -20.721 70.631-388.641 1.00 57.04 N ANISOU 3673 N ALA B 30 7445 7386 6841 535 427 1272 N ATOM 3674 CA ALA B 30 -21.796 71.590-388.509 1.00 59.36 C ANISOU 3674 CA ALA B 30 7809 7662 7082 561 333 1318 C ATOM 3675 C ALA B 30 -21.813 72.471-389.739 1.00 60.56 C ANISOU 3675 C ALA B 30 7958 7913 7139 567 267 1297 C ATOM 3676 O ALA B 30 -20.767 72.929-390.203 1.00 57.12 O ANISOU 3676 O ALA B 30 7522 7565 6617 523 323 1274 O ATOM 3677 CB ALA B 30 -21.625 72.419-387.250 1.00 59.38 C ANISOU 3677 CB ALA B 30 7925 7634 7003 507 373 1372 C ATOM 3678 N GLY B 31 -23.007 72.697-390.274 1.00 54.02 N ANISOU 3678 N GLY B 31 7129 7076 6322 634 141 1299 N ATOM 3679 CA GLY B 31 -23.155 73.515-391.460 1.00 51.43 C ANISOU 3679 CA GLY B 31 6814 6832 5894 665 56 1254 C ATOM 3680 C GLY B 31 -24.585 73.591-391.947 1.00 54.65 C ANISOU 3680 C GLY B 31 7218 7222 6326 743 -107 1241 C ATOM 3681 O GLY B 31 -25.502 73.060-391.320 1.00 53.26 O ANISOU 3681 O GLY B 31 7020 6976 6241 774 -150 1289 O ATOM 3682 N LYS B 32 -24.761 74.244-393.089 1.00 66.31 N ANISOU 3682 N LYS B 32 8716 8765 7715 783 -204 1169 N ATOM 3683 CA LYS B 32 -26.081 74.520-393.638 1.00 65.53 C ANISOU 3683 CA LYS B 32 8628 8675 7594 861 -383 1136 C ATOM 3684 C LYS B 32 -26.616 73.330-394.427 1.00 60.63 C ANISOU 3684 C LYS B 32 7888 7958 7192 857 -498 1077 C ATOM 3685 O LYS B 32 -25.904 72.741-395.235 1.00 60.40 O ANISOU 3685 O LYS B 32 7792 7886 7270 814 -479 1019 O ATOM 3686 CB LYS B 32 -26.004 75.760-394.529 1.00 66.68 C ANISOU 3686 CB LYS B 32 8862 8938 7534 922 -444 1063 C ATOM 3687 CG LYS B 32 -24.828 76.667-394.173 1.00 64.40 C ANISOU 3687 CG LYS B 32 8635 8752 7081 896 -284 1107 C ATOM 3688 CD LYS B 32 -24.995 78.082-394.700 1.00 69.81 C ANISOU 3688 CD LYS B 32 9416 9594 7515 991 -325 1082 C ATOM 3689 CE LYS B 32 -24.825 78.149-396.205 1.00 76.20 C ANISOU 3689 CE LYS B 32 10234 10409 8310 1054 -422 919 C ATOM 3690 NZ LYS B 32 -25.110 79.519-396.708 1.00 74.78 N ANISOU 3690 NZ LYS B 32 10158 10394 7861 1182 -470 879 N ATOM 3691 N PHE B 33 -27.877 72.982-394.188 1.00 57.78 N ANISOU 3691 N PHE B 33 7486 7564 6902 899 -620 1109 N ATOM 3692 CA PHE B 33 -28.499 71.860-394.890 1.00 62.37 C ANISOU 3692 CA PHE B 33 7927 8065 7704 887 -742 1077 C ATOM 3693 C PHE B 33 -29.898 72.169-395.418 1.00 59.43 C ANISOU 3693 C PHE B 33 7551 7717 7312 949 -971 1035 C ATOM 3694 O PHE B 33 -30.529 73.143-395.011 1.00 60.60 O ANISOU 3694 O PHE B 33 7802 7950 7273 1021 -1022 1057 O ATOM 3695 CB PHE B 33 -28.544 70.619-394.000 1.00 56.76 C ANISOU 3695 CB PHE B 33 7105 7285 7177 870 -643 1177 C ATOM 3696 CG PHE B 33 -27.194 70.122-393.601 1.00 50.53 C ANISOU 3696 CG PHE B 33 6303 6476 6419 813 -442 1199 C ATOM 3697 CD1 PHE B 33 -26.846 70.028-392.267 1.00 51.47 C ANISOU 3697 CD1 PHE B 33 6470 6586 6500 820 -296 1270 C ATOM 3698 CD2 PHE B 33 -26.267 69.755-394.564 1.00 50.51 C ANISOU 3698 CD2 PHE B 33 6246 6462 6484 758 -409 1146 C ATOM 3699 CE1 PHE B 33 -25.599 69.571-391.897 1.00 53.30 C ANISOU 3699 CE1 PHE B 33 6694 6813 6744 771 -130 1274 C ATOM 3700 CE2 PHE B 33 -25.013 69.296-394.203 1.00 51.62 C ANISOU 3700 CE2 PHE B 33 6369 6607 6636 716 -230 1171 C ATOM 3701 CZ PHE B 33 -24.678 69.204-392.868 1.00 51.16 C ANISOU 3701 CZ PHE B 33 6360 6558 6522 723 -95 1228 C ATOM 3702 N GLN B 34 -30.367 71.319-396.325 1.00 53.51 N ANISOU 3702 N GLN B 34 6672 6899 6761 918 -1114 984 N ATOM 3703 CA GLN B 34 -31.656 71.507-396.977 1.00 53.84 C ANISOU 3703 CA GLN B 34 6691 6958 6808 960 -1364 921 C ATOM 3704 C GLN B 34 -32.787 71.137-396.032 1.00 55.25 C ANISOU 3704 C GLN B 34 6802 7159 7030 1014 -1406 1042 C ATOM 3705 O GLN B 34 -33.946 71.477-396.271 1.00 58.79 O ANISOU 3705 O GLN B 34 7250 7661 7428 1072 -1604 1018 O ATOM 3706 CB GLN B 34 -31.730 70.639-398.234 1.00 54.02 C ANISOU 3706 CB GLN B 34 6577 6878 7070 882 -1509 840 C ATOM 3707 CG GLN B 34 -32.807 71.043-399.229 1.00 57.38 C ANISOU 3707 CG GLN B 34 7012 7311 7478 908 -1801 710 C ATOM 3708 CD GLN B 34 -32.896 70.087-400.406 1.00 61.91 C ANISOU 3708 CD GLN B 34 7433 7751 8340 804 -1953 649 C ATOM 3709 OE1 GLN B 34 -33.200 68.904-400.239 1.00 63.70 O ANISOU 3709 OE1 GLN B 34 7463 7923 8816 742 -1950 763 O ATOM 3710 NE2 GLN B 34 -32.639 70.598-401.605 1.00 61.92 N ANISOU 3710 NE2 GLN B 34 7520 7695 8313 790 -2088 476 N ATOM 3711 N TRP B 35 -32.440 70.453-394.947 1.00 57.48 N ANISOU 3711 N TRP B 35 7035 7405 7398 1008 -1222 1167 N ATOM 3712 CA TRP B 35 -33.445 69.851-394.078 1.00 59.25 C ANISOU 3712 CA TRP B 35 7171 7626 7716 1070 -1246 1287 C ATOM 3713 C TRP B 35 -32.940 69.716-392.637 1.00 57.78 C ANISOU 3713 C TRP B 35 7042 7411 7500 1100 -1023 1398 C ATOM 3714 O TRP B 35 -31.822 69.263-392.405 1.00 56.79 O ANISOU 3714 O TRP B 35 6914 7241 7422 1046 -850 1396 O ATOM 3715 CB TRP B 35 -33.836 68.484-394.654 1.00 54.85 C ANISOU 3715 CB TRP B 35 6389 7013 7439 1026 -1325 1310 C ATOM 3716 CG TRP B 35 -35.124 67.899-394.144 1.00 56.15 C ANISOU 3716 CG TRP B 35 6426 7199 7711 1101 -1422 1415 C ATOM 3717 CD1 TRP B 35 -35.293 66.670-393.592 1.00 61.54 C ANISOU 3717 CD1 TRP B 35 6940 7851 8591 1125 -1334 1532 C ATOM 3718 CD2 TRP B 35 -36.419 68.514-394.162 1.00 60.50 C ANISOU 3718 CD2 TRP B 35 6996 7823 8167 1177 -1627 1420 C ATOM 3719 NE1 TRP B 35 -36.611 66.476-393.256 1.00 64.01 N ANISOU 3719 NE1 TRP B 35 7161 8208 8951 1211 -1467 1614 N ATOM 3720 CE2 TRP B 35 -37.323 67.590-393.591 1.00 60.63 C ANISOU 3720 CE2 TRP B 35 6845 7844 8346 1240 -1653 1549 C ATOM 3721 CE3 TRP B 35 -36.903 69.748-394.591 1.00 67.17 C ANISOU 3721 CE3 TRP B 35 7981 8748 8791 1215 -1786 1333 C ATOM 3722 CZ2 TRP B 35 -38.675 67.865-393.443 1.00 66.09 C ANISOU 3722 CZ2 TRP B 35 7503 8613 8997 1329 -1839 1599 C ATOM 3723 CZ3 TRP B 35 -38.248 70.022-394.443 1.00 70.10 C ANISOU 3723 CZ3 TRP B 35 8326 9204 9106 1305 -1972 1377 C ATOM 3724 CH2 TRP B 35 -39.120 69.082-393.872 1.00 72.69 C ANISOU 3724 CH2 TRP B 35 8480 9528 9610 1357 -2001 1511 C ATOM 3725 N GLY B 36 -33.766 70.124-391.675 1.00 55.52 N ANISOU 3725 N GLY B 36 6815 7145 7134 1190 -1039 1492 N ATOM 3726 CA GLY B 36 -33.419 70.054-390.264 1.00 60.23 C ANISOU 3726 CA GLY B 36 7485 7685 7716 1224 -857 1590 C ATOM 3727 C GLY B 36 -33.350 68.607-389.832 1.00 52.43 C ANISOU 3727 C GLY B 36 6352 6623 6945 1243 -765 1638 C ATOM 3728 O GLY B 36 -33.586 67.726-390.650 1.00 62.08 O ANISOU 3728 O GLY B 36 7406 7855 8327 1221 -839 1618 O ATOM 3729 N PRO B 37 -33.099 68.340-388.539 1.00 52.91 N ANISOU 3729 N PRO B 37 6472 6610 7020 1293 -612 1707 N ATOM 3730 CA PRO B 37 -33.184 69.182-387.345 1.00 53.13 C ANISOU 3730 CA PRO B 37 6669 6591 6926 1336 -550 1775 C ATOM 3731 C PRO B 37 -32.251 70.365-387.344 1.00 52.20 C ANISOU 3731 C PRO B 37 6709 6498 6625 1246 -488 1735 C ATOM 3732 O PRO B 37 -31.099 70.255-387.762 1.00 48.68 O ANISOU 3732 O PRO B 37 6264 6062 6169 1155 -401 1653 O ATOM 3733 CB PRO B 37 -32.732 68.221-386.246 1.00 53.01 C ANISOU 3733 CB PRO B 37 6649 6466 7026 1380 -385 1802 C ATOM 3734 CG PRO B 37 -31.666 67.460-386.931 1.00 52.36 C ANISOU 3734 CG PRO B 37 6479 6408 7008 1300 -302 1714 C ATOM 3735 CD PRO B 37 -32.394 67.090-388.207 1.00 50.70 C ANISOU 3735 CD PRO B 37 6100 6278 6886 1293 -460 1705 C ATOM 3736 N ALA B 38 -32.760 71.484-386.842 1.00 54.32 N ANISOU 3736 N ALA B 38 7099 6787 6753 1279 -528 1814 N ATOM 3737 CA ALA B 38 -31.964 72.681-386.646 1.00 54.02 C ANISOU 3737 CA ALA B 38 7201 6783 6541 1204 -457 1820 C ATOM 3738 C ALA B 38 -31.406 72.697-385.230 1.00 51.97 C ANISOU 3738 C ALA B 38 7040 6390 6315 1178 -310 1889 C ATOM 3739 O ALA B 38 -32.122 72.439-384.267 1.00 54.80 O ANISOU 3739 O ALA B 38 7424 6647 6751 1259 -310 1982 O ATOM 3740 CB ALA B 38 -32.806 73.928-386.903 1.00 58.48 C ANISOU 3740 CB ALA B 38 7834 7463 6922 1257 -575 1888 C ATOM 3741 N PHE B 39 -30.121 72.993-385.116 1.00 49.61 N ANISOU 3741 N PHE B 39 6797 6087 5965 1067 -195 1839 N ATOM 3742 CA PHE B 39 -29.472 73.076-383.820 1.00 50.26 C ANISOU 3742 CA PHE B 39 6979 6038 6079 1016 -75 1882 C ATOM 3743 C PHE B 39 -29.770 71.858-382.959 1.00 51.00 C ANISOU 3743 C PHE B 39 7051 5979 6349 1096 -35 1874 C ATOM 3744 O PHE B 39 -30.226 71.980-381.826 1.00 51.85 O ANISOU 3744 O PHE B 39 7244 5951 6504 1143 -20 1962 O ATOM 3745 CB PHE B 39 -29.874 74.364-383.108 1.00 53.05 C ANISOU 3745 CB PHE B 39 7449 6382 6325 1007 -88 2030 C ATOM 3746 CG PHE B 39 -29.422 75.602-383.820 1.00 50.78 C ANISOU 3746 CG PHE B 39 7188 6262 5845 939 -94 2046 C ATOM 3747 CD1 PHE B 39 -30.290 76.317-384.621 1.00 52.46 C ANISOU 3747 CD1 PHE B 39 7387 6624 5921 1016 -205 2085 C ATOM 3748 CD2 PHE B 39 -28.117 76.036-383.712 1.00 49.89 C ANISOU 3748 CD2 PHE B 39 7106 6171 5678 811 9 2016 C ATOM 3749 CE1 PHE B 39 -29.864 77.454-385.283 1.00 52.63 C ANISOU 3749 CE1 PHE B 39 7437 6814 5746 983 -200 2092 C ATOM 3750 CE2 PHE B 39 -27.689 77.173-384.373 1.00 53.24 C ANISOU 3750 CE2 PHE B 39 7541 6767 5920 768 16 2040 C ATOM 3751 CZ PHE B 39 -28.564 77.881-385.159 1.00 55.35 C ANISOU 3751 CZ PHE B 39 7805 7182 6045 863 -82 2076 C ATOM 3752 N GLN B 40 -29.491 70.684-383.508 1.00 71.60 N ANISOU 3752 N GLN B 40 9542 8609 9053 1119 -11 1777 N ATOM 3753 CA GLN B 40 -29.603 69.441-382.763 1.00 78.26 C ANISOU 3753 CA GLN B 40 10352 9340 10044 1210 53 1757 C ATOM 3754 C GLN B 40 -28.465 68.516-383.147 1.00 75.17 C ANISOU 3754 C GLN B 40 9888 8986 9687 1164 151 1643 C ATOM 3755 O GLN B 40 -28.116 68.419-384.320 1.00 70.35 O ANISOU 3755 O GLN B 40 9179 8496 9055 1110 128 1598 O ATOM 3756 CB GLN B 40 -30.941 68.762-383.046 1.00 83.16 C ANISOU 3756 CB GLN B 40 10851 9980 10767 1350 -41 1816 C ATOM 3757 CG GLN B 40 -32.131 69.450-382.407 1.00 91.06 C ANISOU 3757 CG GLN B 40 11921 10926 11750 1436 -125 1946 C ATOM 3758 CD GLN B 40 -33.415 68.674-382.604 1.00101.26 C ANISOU 3758 CD GLN B 40 13077 12245 13153 1583 -216 2007 C ATOM 3759 OE1 GLN B 40 -33.397 67.536-383.078 1.00101.13 O ANISOU 3759 OE1 GLN B 40 12908 12269 13246 1623 -200 1960 O ATOM 3760 NE2 GLN B 40 -34.541 69.284-382.241 1.00 99.37 N ANISOU 3760 NE2 GLN B 40 12876 11994 12885 1668 -312 2130 N ATOM 3761 N ILE B 41 -27.886 67.843-382.157 1.00 90.15 N ANISOU 3761 N ILE B 41 11840 10779 11635 1193 258 1594 N ATOM 3762 CA ILE B 41 -26.796 66.913-382.416 1.00 93.60 C ANISOU 3762 CA ILE B 41 12211 11268 12085 1171 360 1494 C ATOM 3763 C ILE B 41 -27.343 65.573-382.892 1.00100.71 C ANISOU 3763 C ILE B 41 12937 12223 13106 1297 372 1506 C ATOM 3764 O ILE B 41 -27.082 64.533-382.287 1.00110.27 O ANISOU 3764 O ILE B 41 14127 13400 14370 1394 469 1468 O ATOM 3765 CB ILE B 41 -25.924 66.672-381.163 1.00101.68 C ANISOU 3765 CB ILE B 41 13365 12172 13095 1165 462 1417 C ATOM 3766 CG1 ILE B 41 -25.575 67.990-380.475 1.00104.79 C ANISOU 3766 CG1 ILE B 41 13924 12480 13411 1040 438 1439 C ATOM 3767 CG2 ILE B 41 -24.638 65.923-381.531 1.00 99.28 C ANISOU 3767 CG2 ILE B 41 13003 11966 12754 1125 560 1314 C ATOM 3768 CD1 ILE B 41 -24.217 68.530-380.868 1.00 96.77 C ANISOU 3768 CD1 ILE B 41 12925 11560 12285 879 478 1377 C ATOM 3769 N LYS B 42 -28.111 65.597-383.973 1.00 52.89 N ANISOU 3769 N LYS B 42 6749 6255 7091 1300 269 1561 N ATOM 3770 CA LYS B 42 -28.583 64.357-384.565 1.00 53.00 C ANISOU 3770 CA LYS B 42 6564 6336 7239 1388 271 1593 C ATOM 3771 C LYS B 42 -27.388 63.579-385.118 1.00 52.19 C ANISOU 3771 C LYS B 42 6375 6315 7139 1339 381 1537 C ATOM 3772 O LYS B 42 -26.504 64.155-385.755 1.00 52.32 O ANISOU 3772 O LYS B 42 6426 6381 7072 1212 384 1488 O ATOM 3773 CB LYS B 42 -29.608 64.644-385.667 1.00 55.23 C ANISOU 3773 CB LYS B 42 6728 6687 7570 1370 107 1652 C ATOM 3774 CG LYS B 42 -30.285 63.403-386.263 1.00 56.31 C ANISOU 3774 CG LYS B 42 6632 6886 7876 1449 81 1715 C ATOM 3775 CD LYS B 42 -30.931 62.518-385.195 1.00 53.19 C ANISOU 3775 CD LYS B 42 6198 6444 7568 1626 150 1777 C ATOM 3776 CE LYS B 42 -31.908 61.530-385.816 1.00 61.77 C ANISOU 3776 CE LYS B 42 7034 7612 8824 1704 84 1877 C ATOM 3777 NZ LYS B 42 -31.360 60.891-387.047 1.00 66.18 N ANISOU 3777 NZ LYS B 42 7415 8266 9465 1606 90 1880 N ATOM 3778 N GLN B 43 -27.352 62.276-384.859 1.00 58.99 N ANISOU 3778 N GLN B 43 7122 7203 8087 1453 479 1555 N ATOM 3779 CA GLN B 43 -26.263 61.445-385.356 1.00 54.94 C ANISOU 3779 CA GLN B 43 6514 6789 7573 1428 594 1529 C ATOM 3780 C GLN B 43 -26.617 60.811-386.692 1.00 59.87 C ANISOU 3780 C GLN B 43 6907 7510 8330 1402 543 1615 C ATOM 3781 O GLN B 43 -27.784 60.533-386.970 1.00 71.56 O ANISOU 3781 O GLN B 43 8265 8992 9932 1456 450 1696 O ATOM 3782 CB GLN B 43 -25.908 60.357-384.346 1.00 59.84 C ANISOU 3782 CB GLN B 43 7137 7408 8190 1579 745 1503 C ATOM 3783 CG GLN B 43 -24.799 59.429-384.811 1.00 61.20 C ANISOU 3783 CG GLN B 43 7203 7711 8340 1578 875 1494 C ATOM 3784 CD GLN B 43 -24.360 58.459-383.735 1.00 62.83 C ANISOU 3784 CD GLN B 43 7447 7932 8495 1743 1024 1440 C ATOM 3785 OE1 GLN B 43 -25.172 57.715-383.181 1.00 61.84 O ANISOU 3785 OE1 GLN B 43 7262 7794 8442 1916 1058 1485 O ATOM 3786 NE2 GLN B 43 -23.067 58.457-383.435 1.00 60.88 N ANISOU 3786 NE2 GLN B 43 7298 7723 8111 1704 1111 1340 N ATOM 3787 N VAL B 44 -25.601 60.572-387.511 1.00 55.39 N ANISOU 3787 N VAL B 44 6276 7019 7749 1315 599 1603 N ATOM 3788 CA VAL B 44 -25.795 60.033-388.850 1.00 55.57 C ANISOU 3788 CA VAL B 44 6090 7107 7916 1261 545 1687 C ATOM 3789 C VAL B 44 -24.795 58.917-389.122 1.00 55.61 C ANISOU 3789 C VAL B 44 5969 7214 7947 1284 702 1734 C ATOM 3790 O VAL B 44 -23.629 59.032-388.757 1.00 64.64 O ANISOU 3790 O VAL B 44 7219 8388 8952 1268 810 1664 O ATOM 3791 CB VAL B 44 -25.601 61.133-389.909 1.00 54.49 C ANISOU 3791 CB VAL B 44 6011 6947 7745 1109 415 1638 C ATOM 3792 CG1 VAL B 44 -25.418 60.517-391.289 1.00 54.69 C ANISOU 3792 CG1 VAL B 44 5845 7014 7920 1038 383 1705 C ATOM 3793 CG2 VAL B 44 -26.765 62.127-389.883 1.00 54.85 C ANISOU 3793 CG2 VAL B 44 6136 6928 7775 1100 241 1618 C ATOM 3794 N THR B 45 -25.242 57.850-389.775 1.00 72.51 N ANISOU 3794 N THR B 45 7871 9417 10261 1320 711 1864 N ATOM 3795 CA THR B 45 -24.371 56.700-390.018 1.00 78.03 C ANISOU 3795 CA THR B 45 8425 10235 10988 1362 875 1947 C ATOM 3796 C THR B 45 -24.256 56.298-391.490 1.00 80.78 C ANISOU 3796 C THR B 45 8570 10613 11510 1249 826 2066 C ATOM 3797 O THR B 45 -23.184 55.899-391.947 1.00 77.30 O ANISOU 3797 O THR B 45 8082 10241 11046 1217 932 2106 O ATOM 3798 CB THR B 45 -24.809 55.488-389.186 1.00 80.17 C ANISOU 3798 CB THR B 45 8577 10587 11297 1556 1003 2029 C ATOM 3799 OG1 THR B 45 -24.653 55.793-387.794 1.00 70.27 O ANISOU 3799 OG1 THR B 45 7536 9287 9875 1665 1066 1900 O ATOM 3800 CG2 THR B 45 -23.968 54.269-389.531 1.00 81.13 C ANISOU 3800 CG2 THR B 45 8523 10863 11441 1611 1176 2144 C ATOM 3801 N ASN B 46 -25.355 56.403-392.229 1.00117.11 N ANISOU 3801 N ASN B 46 13052 15155 16290 1187 656 2123 N ATOM 3802 CA ASN B 46 -25.346 56.070-393.651 1.00117.67 C ANISOU 3802 CA ASN B 46 12937 15212 16559 1062 575 2226 C ATOM 3803 C ASN B 46 -25.357 57.315-394.521 1.00116.68 C ANISOU 3803 C ASN B 46 12946 14968 16419 915 389 2107 C ATOM 3804 O ASN B 46 -25.527 58.427-394.025 1.00170.68 O ANISOU 3804 O ASN B 46 19997 21757 23098 915 320 1967 O ATOM 3805 CB ASN B 46 -26.555 55.210-394.013 1.00119.71 C ANISOU 3805 CB ASN B 46 12934 15490 17059 1083 493 2380 C ATOM 3806 CG ASN B 46 -26.870 54.172-392.960 1.00120.91 C ANISOU 3806 CG ASN B 46 12979 15762 17201 1272 654 2478 C ATOM 3807 OD1 ASN B 46 -26.024 53.826-392.134 1.00120.47 O ANISOU 3807 OD1 ASN B 46 13007 15785 16982 1385 847 2450 O ATOM 3808 ND2 ASN B 46 -28.097 53.665-392.983 1.00122.65 N ANISOU 3808 ND2 ASN B 46 13010 16002 17590 1318 569 2587 N ATOM 3809 N GLU B 47 -25.171 57.126-395.823 1.00105.86 N ANISOU 3809 N GLU B 47 11452 13552 15218 797 311 2168 N ATOM 3810 CA GLU B 47 -25.365 58.212-396.770 1.00103.53 C ANISOU 3810 CA GLU B 47 11263 13136 14937 676 110 2051 C ATOM 3811 C GLU B 47 -26.859 58.346-396.994 1.00100.50 C ANISOU 3811 C GLU B 47 10803 12698 14683 659 -105 2047 C ATOM 3812 O GLU B 47 -27.433 59.411-396.790 1.00 97.14 O ANISOU 3812 O GLU B 47 10543 12231 14133 663 -238 1915 O ATOM 3813 CB GLU B 47 -24.665 57.915-398.096 1.00113.43 C ANISOU 3813 CB GLU B 47 12418 14332 16350 564 91 2113 C ATOM 3814 CG GLU B 47 -24.694 59.070-399.086 1.00105.59 C ANISOU 3814 CG GLU B 47 11566 13207 15345 464 -102 1964 C ATOM 3815 CD GLU B 47 -24.522 58.609-400.523 1.00112.68 C ANISOU 3815 CD GLU B 47 12316 13994 16503 346 -196 2041 C ATOM 3816 OE1 GLU B 47 -23.439 58.843-401.101 1.00113.80 O ANISOU 3816 OE1 GLU B 47 12525 14099 16613 313 -133 2025 O ATOM 3817 OE2 GLU B 47 -25.467 58.002-401.075 1.00110.50 O ANISOU 3817 OE2 GLU B 47 11850 13660 16474 285 -337 2127 O ATOM 3818 N VAL B 48 -27.480 57.240-397.399 1.00 85.60 N ANISOU 3818 N VAL B 48 8651 10831 13044 644 -135 2209 N ATOM 3819 CA VAL B 48 -28.922 57.183-397.638 1.00 88.24 C ANISOU 3819 CA VAL B 48 8861 11136 13532 624 -345 2233 C ATOM 3820 C VAL B 48 -29.694 57.535-396.375 1.00 78.87 C ANISOU 3820 C VAL B 48 7775 10006 12186 762 -334 2188 C ATOM 3821 O VAL B 48 -30.916 57.693-396.403 1.00 78.56 O ANISOU 3821 O VAL B 48 7675 9957 12217 770 -513 2189 O ATOM 3822 CB VAL B 48 -29.356 55.788-398.124 1.00 89.16 C ANISOU 3822 CB VAL B 48 8637 11293 13946 594 -338 2456 C ATOM 3823 CG1 VAL B 48 -30.825 55.775-398.504 1.00 95.54 C ANISOU 3823 CG1 VAL B 48 9300 12070 14930 549 -589 2477 C ATOM 3824 CG2 VAL B 48 -28.498 55.348-399.300 1.00 98.52 C ANISOU 3824 CG2 VAL B 48 9715 12413 15305 462 -319 2537 C ATOM 3825 N ASP B 49 -28.972 57.657-395.267 1.00 62.79 N ANISOU 3825 N ASP B 49 5894 8023 9940 870 -133 2150 N ATOM 3826 CA ASP B 49 -29.580 58.003-393.991 1.00 58.50 C ANISOU 3826 CA ASP B 49 5472 7505 9251 1004 -106 2108 C ATOM 3827 C ASP B 49 -29.388 59.473-393.648 1.00 54.77 C ANISOU 3827 C ASP B 49 5291 6973 8547 984 -166 1939 C ATOM 3828 O ASP B 49 -30.097 60.012-392.807 1.00 56.74 O ANISOU 3828 O ASP B 49 5649 7213 8696 1064 -208 1906 O ATOM 3829 CB ASP B 49 -29.019 57.126-392.874 1.00 62.78 C ANISOU 3829 CB ASP B 49 5994 8132 9726 1149 143 2174 C ATOM 3830 CG ASP B 49 -29.911 57.106-391.650 1.00 68.25 C ANISOU 3830 CG ASP B 49 6733 8837 10360 1308 158 2180 C ATOM 3831 OD1 ASP B 49 -31.128 57.365-391.805 1.00 65.95 O ANISOU 3831 OD1 ASP B 49 6383 8525 10151 1311 -19 2204 O ATOM 3832 OD2 ASP B 49 -29.398 56.824-390.541 1.00 75.35 O ANISOU 3832 OD2 ASP B 49 7730 9763 11135 1434 337 2158 O ATOM 3833 N LEU B 50 -28.418 60.118-394.277 1.00 50.05 N ANISOU 3833 N LEU B 50 4810 6340 7865 886 -159 1849 N ATOM 3834 CA LEU B 50 -28.278 61.552-394.097 1.00 55.98 C ANISOU 3834 CA LEU B 50 5809 7054 8406 863 -225 1708 C ATOM 3835 C LEU B 50 -29.137 62.275-395.123 1.00 50.60 C ANISOU 3835 C LEU B 50 5130 6323 7771 793 -474 1643 C ATOM 3836 O LEU B 50 -29.708 63.323-394.829 1.00 52.51 O ANISOU 3836 O LEU B 50 5523 6563 7866 821 -577 1567 O ATOM 3837 CB LEU B 50 -26.815 62.012-394.142 1.00 54.72 C ANISOU 3837 CB LEU B 50 5787 6902 8101 816 -90 1639 C ATOM 3838 CG LEU B 50 -26.077 62.277-395.452 1.00 53.52 C ANISOU 3838 CG LEU B 50 5627 6717 7990 709 -139 1596 C ATOM 3839 CD1 LEU B 50 -26.637 63.477-396.168 1.00 53.87 C ANISOU 3839 CD1 LEU B 50 5787 6710 7970 665 -342 1480 C ATOM 3840 CD2 LEU B 50 -24.607 62.512-395.153 1.00 54.63 C ANISOU 3840 CD2 LEU B 50 5879 6900 7978 700 38 1563 C ATOM 3841 N VAL B 51 -29.238 61.716-396.326 1.00 54.03 N ANISOU 3841 N VAL B 51 5399 6719 8410 705 -578 1675 N ATOM 3842 CA VAL B 51 -30.152 62.258-397.326 1.00 52.42 C ANISOU 3842 CA VAL B 51 5182 6458 8276 640 -844 1600 C ATOM 3843 C VAL B 51 -31.561 62.236-396.761 1.00 57.73 C ANISOU 3843 C VAL B 51 5797 7171 8965 714 -970 1640 C ATOM 3844 O VAL B 51 -32.267 63.235-396.767 1.00 60.09 O ANISOU 3844 O VAL B 51 6225 7476 9131 738 -1128 1546 O ATOM 3845 CB VAL B 51 -30.122 61.458-398.627 1.00 58.23 C ANISOU 3845 CB VAL B 51 5717 7122 9286 524 -944 1651 C ATOM 3846 CG1 VAL B 51 -31.075 62.064-399.624 1.00 61.70 C ANISOU 3846 CG1 VAL B 51 6165 7489 9788 458 -1245 1540 C ATOM 3847 CG2 VAL B 51 -28.727 61.445-399.191 1.00 59.82 C ANISOU 3847 CG2 VAL B 51 5969 7281 9478 465 -815 1633 C ATOM 3848 N ASN B 52 -31.964 61.082-396.256 1.00 83.30 N ANISOU 3848 N ASN B 52 8837 10456 12359 766 -892 1790 N ATOM 3849 CA ASN B 52 -33.232 60.969-395.562 1.00 91.48 C ANISOU 3849 CA ASN B 52 9808 11542 13408 865 -976 1852 C ATOM 3850 C ASN B 52 -33.458 62.158-394.625 1.00 82.53 C ANISOU 3850 C ASN B 52 8927 10421 12010 955 -973 1768 C ATOM 3851 O ASN B 52 -34.579 62.647-394.492 1.00 86.01 O ANISOU 3851 O ASN B 52 9384 10886 12411 1003 -1140 1761 O ATOM 3852 CB ASN B 52 -33.270 59.648-394.781 1.00 97.06 C ANISOU 3852 CB ASN B 52 10325 12313 14240 961 -794 2021 C ATOM 3853 CG ASN B 52 -34.535 59.480-393.956 1.00109.84 C ANISOU 3853 CG ASN B 52 11877 13986 15873 1093 -855 2098 C ATOM 3854 OD1 ASN B 52 -35.601 59.979-394.320 1.00119.71 O ANISOU 3854 OD1 ASN B 52 13107 15239 17140 1076 -1084 2072 O ATOM 3855 ND2 ASN B 52 -34.423 58.761-392.840 1.00105.47 N ANISOU 3855 ND2 ASN B 52 11288 13479 15307 1237 -653 2191 N ATOM 3856 N THR B 53 -32.383 62.637-394.004 1.00 53.80 N ANISOU 3856 N THR B 53 5477 6770 8195 971 -789 1715 N ATOM 3857 CA THR B 53 -32.502 63.562-392.882 1.00 53.31 C ANISOU 3857 CA THR B 53 5626 6714 7916 1058 -738 1684 C ATOM 3858 C THR B 53 -32.068 64.994-393.189 1.00 51.24 C ANISOU 3858 C THR B 53 5584 6444 7439 1006 -791 1559 C ATOM 3859 O THR B 53 -32.628 65.935-392.643 1.00 54.57 O ANISOU 3859 O THR B 53 6145 6885 7705 1062 -849 1547 O ATOM 3860 CB THR B 53 -31.721 63.057-391.648 1.00 52.15 C ANISOU 3860 CB THR B 53 5533 6560 7723 1133 -489 1729 C ATOM 3861 OG1 THR B 53 -32.127 61.721-391.329 1.00 53.15 O ANISOU 3861 OG1 THR B 53 5454 6715 8025 1215 -422 1847 O ATOM 3862 CG2 THR B 53 -31.986 63.940-390.444 1.00 51.51 C ANISOU 3862 CG2 THR B 53 5652 6453 7465 1215 -457 1718 C ATOM 3863 N PHE B 54 -31.073 65.172-394.043 1.00 54.08 N ANISOU 3863 N PHE B 54 5974 6787 7788 911 -764 1483 N ATOM 3864 CA PHE B 54 -30.627 66.511-394.399 1.00 51.66 C ANISOU 3864 CA PHE B 54 5861 6491 7275 879 -804 1369 C ATOM 3865 C PHE B 54 -30.324 66.507-395.884 1.00 52.87 C ANISOU 3865 C PHE B 54 5967 6613 7508 796 -950 1278 C ATOM 3866 O PHE B 54 -29.408 67.181-396.361 1.00 53.48 O ANISOU 3866 O PHE B 54 6179 6694 7446 770 -961 1175 O ATOM 3867 CB PHE B 54 -29.273 66.791-393.763 1.00 49.68 C ANISOU 3867 CB PHE B 54 5733 6247 6895 863 -588 1358 C ATOM 3868 CG PHE B 54 -29.219 66.509-392.292 1.00 51.87 C ANISOU 3868 CG PHE B 54 6052 6521 7135 931 -437 1434 C ATOM 3869 CD1 PHE B 54 -29.360 67.537-391.366 1.00 52.46 C ANISOU 3869 CD1 PHE B 54 6299 6603 7032 969 -415 1437 C ATOM 3870 CD2 PHE B 54 -29.006 65.230-391.830 1.00 52.42 C ANISOU 3870 CD2 PHE B 54 5994 6577 7348 964 -315 1506 C ATOM 3871 CE1 PHE B 54 -29.299 67.285-390.002 1.00 48.79 C ANISOU 3871 CE1 PHE B 54 5888 6098 6553 1026 -289 1497 C ATOM 3872 CE2 PHE B 54 -28.942 64.972-390.475 1.00 52.36 C ANISOU 3872 CE2 PHE B 54 6045 6549 7302 1042 -184 1549 C ATOM 3873 CZ PHE B 54 -29.092 65.999-389.560 1.00 51.74 C ANISOU 3873 CZ PHE B 54 6148 6444 7065 1068 -178 1538 C ATOM 3874 N GLY B 55 -31.132 65.751-396.609 1.00 51.98 N ANISOU 3874 N GLY B 55 5656 6463 7630 759 -1066 1321 N ATOM 3875 CA GLY B 55 -30.778 65.255-397.925 1.00 51.65 C ANISOU 3875 CA GLY B 55 5521 6349 7756 657 -1160 1272 C ATOM 3876 C GLY B 55 -30.158 65.254-399.297 1.00 51.61 C ANISOU 3876 C GLY B 55 5654 6304 7653 622 -1313 1107 C ATOM 3877 O GLY B 55 -29.479 64.319-399.695 1.00 55.34 O ANISOU 3877 O GLY B 55 6287 6829 7911 683 -1405 1014 O ATOM 3878 N GLN B 56 -30.427 66.340-400.016 1.00 64.09 N ANISOU 3878 N GLN B 56 7167 7792 9393 534 -1332 1080 N ATOM 3879 CA GLN B 56 -29.821 66.627-401.303 1.00 54.87 C ANISOU 3879 CA GLN B 56 6106 6549 8193 502 -1496 915 C ATOM 3880 C GLN B 56 -28.981 67.873-401.086 1.00 54.43 C ANISOU 3880 C GLN B 56 6281 6558 7842 570 -1386 818 C ATOM 3881 O GLN B 56 -29.238 68.645-400.165 1.00 54.88 O ANISOU 3881 O GLN B 56 6457 6724 7670 650 -1334 819 O ATOM 3882 CB GLN B 56 -31.191 67.000-401.871 1.00 64.39 C ANISOU 3882 CB GLN B 56 7308 7739 9419 506 -1797 812 C ATOM 3883 CG GLN B 56 -32.146 65.826-402.076 1.00 61.98 C ANISOU 3883 CG GLN B 56 6752 7389 9410 434 -1934 916 C ATOM 3884 CD GLN B 56 -31.766 64.949-403.255 1.00 61.12 C ANISOU 3884 CD GLN B 56 6485 7123 9613 299 -2004 936 C ATOM 3885 OE1 GLN B 56 -31.492 65.441-404.352 1.00 62.71 O ANISOU 3885 OE1 GLN B 56 6782 7211 9835 256 -2142 785 O ATOM 3886 NE2 GLN B 56 -31.753 63.639-403.033 1.00 71.96 N ANISOU 3886 NE2 GLN B 56 7616 8490 11235 240 -1908 1132 N ATOM 3887 N PRO B 57 -27.959 68.065-401.931 1.00 50.84 N ANISOU 3887 N PRO B 57 5881 6036 7401 539 -1345 750 N ATOM 3888 CA PRO B 57 -27.074 69.221-401.813 1.00 56.25 C ANISOU 3888 CA PRO B 57 6760 6795 7816 607 -1232 671 C ATOM 3889 C PRO B 57 -27.541 70.373-402.695 1.00 52.45 C ANISOU 3889 C PRO B 57 6435 6308 7186 670 -1433 480 C ATOM 3890 O PRO B 57 -27.462 70.260-403.914 1.00 52.95 O ANISOU 3890 O PRO B 57 6493 6241 7385 637 -1572 375 O ATOM 3891 CB PRO B 57 -25.737 68.688-402.359 1.00 49.04 C ANISOU 3891 CB PRO B 57 5799 5811 7023 553 -1089 711 C ATOM 3892 CG PRO B 57 -25.986 67.231-402.751 1.00 49.88 C ANISOU 3892 CG PRO B 57 5682 5805 7465 455 -1127 824 C ATOM 3893 CD PRO B 57 -27.457 67.122-402.939 1.00 51.71 C ANISOU 3893 CD PRO B 57 5853 6005 7790 442 -1365 784 C ATOM 3894 N THR B 58 -28.015 71.464-402.100 1.00 60.08 N ANISOU 3894 N THR B 58 7540 7410 7877 767 -1448 438 N ATOM 3895 CA THR B 58 -28.375 72.634-402.888 1.00 64.00 C ANISOU 3895 CA THR B 58 8198 7941 8178 860 -1613 255 C ATOM 3896 C THR B 58 -27.088 73.396-403.122 1.00 62.50 C ANISOU 3896 C THR B 58 8129 7795 7824 912 -1451 214 C ATOM 3897 O THR B 58 -26.092 73.123-402.461 1.00 56.90 O ANISOU 3897 O THR B 58 7381 7119 7118 875 -1224 337 O ATOM 3898 CB THR B 58 -29.394 73.544-402.166 1.00 68.63 C ANISOU 3898 CB THR B 58 8879 8686 8511 961 -1683 252 C ATOM 3899 OG1 THR B 58 -28.720 74.641-401.538 1.00 66.68 O ANISOU 3899 OG1 THR B 58 8769 8589 7976 1045 -1504 284 O ATOM 3900 CG2 THR B 58 -30.170 72.756-401.122 1.00 67.22 C ANISOU 3900 CG2 THR B 58 8570 8523 8448 919 -1664 411 C ATOM 3901 N ALA B 59 -27.108 74.346-404.055 1.00 57.47 N ANISOU 3901 N ALA B 59 7634 7167 7036 1008 -1571 36 N ATOM 3902 CA ALA B 59 -25.912 75.129-404.388 1.00 53.16 C ANISOU 3902 CA ALA B 59 7198 6674 6328 1083 -1426 -9 C ATOM 3903 C ALA B 59 -25.480 76.023-403.232 1.00 52.83 C ANISOU 3903 C ALA B 59 7222 6847 6005 1145 -1218 104 C ATOM 3904 O ALA B 59 -24.474 76.718-403.313 1.00 51.56 O ANISOU 3904 O ALA B 59 7130 6770 5691 1205 -1075 102 O ATOM 3905 CB ALA B 59 -26.148 75.960-405.640 1.00 54.07 C ANISOU 3905 CB ALA B 59 7459 6754 6331 1202 -1613 -239 C ATOM 3906 N GLU B 60 -26.258 75.984-402.159 1.00 53.54 N ANISOU 3906 N GLU B 60 7281 7018 6045 1127 -1209 213 N ATOM 3907 CA GLU B 60 -25.980 76.745-400.959 1.00 53.44 C ANISOU 3907 CA GLU B 60 7318 7178 5810 1160 -1031 344 C ATOM 3908 C GLU B 60 -25.655 75.763-399.842 1.00 51.89 C ANISOU 3908 C GLU B 60 7001 6935 5779 1040 -880 513 C ATOM 3909 O GLU B 60 -25.229 76.149-398.755 1.00 50.22 O ANISOU 3909 O GLU B 60 6811 6820 5451 1028 -716 634 O ATOM 3910 CB GLU B 60 -27.209 77.579-400.592 1.00 51.13 C ANISOU 3910 CB GLU B 60 7105 7011 5310 1257 -1151 337 C ATOM 3911 CG GLU B 60 -27.034 78.512-399.401 1.00 55.92 C ANISOU 3911 CG GLU B 60 7770 7795 5682 1296 -984 488 C ATOM 3912 CD GLU B 60 -26.269 79.776-399.754 1.00 51.94 C ANISOU 3912 CD GLU B 60 7372 7449 4912 1402 -890 452 C ATOM 3913 OE1 GLU B 60 -26.926 80.802-400.036 1.00 53.11 O ANISOU 3913 OE1 GLU B 60 7623 7741 4817 1542 -979 395 O ATOM 3914 OE2 GLU B 60 -25.017 79.742-399.765 1.00 49.73 O ANISOU 3914 OE2 GLU B 60 7068 7169 4659 1359 -726 484 O ATOM 3915 N THR B 61 -25.861 74.483-400.127 1.00 52.32 N ANISOU 3915 N THR B 61 6929 6840 6112 955 -940 521 N ATOM 3916 CA THR B 61 -25.656 73.422-399.150 1.00 52.14 C ANISOU 3916 CA THR B 61 6786 6773 6251 866 -811 665 C ATOM 3917 C THR B 61 -24.474 72.537-399.534 1.00 46.27 C ANISOU 3917 C THR B 61 5951 5950 5678 792 -689 693 C ATOM 3918 O THR B 61 -23.740 72.054-398.674 1.00 49.53 O ANISOU 3918 O THR B 61 6316 6387 6115 746 -513 798 O ATOM 3919 CB THR B 61 -26.914 72.548-399.034 1.00 52.00 C ANISOU 3919 CB THR B 61 6662 6681 6415 843 -958 694 C ATOM 3920 OG1 THR B 61 -27.984 73.337-398.508 1.00 53.00 O ANISOU 3920 OG1 THR B 61 6867 6898 6371 919 -1052 699 O ATOM 3921 CG2 THR B 61 -26.668 71.362-398.120 1.00 46.56 C ANISOU 3921 CG2 THR B 61 5843 5948 5898 778 -817 833 C ATOM 3922 N ALA B 62 -24.296 72.352-400.836 1.00 74.24 N ANISOU 3922 N ALA B 62 9477 9396 9334 787 -793 595 N ATOM 3923 CA ALA B 62 -23.300 71.437-401.391 1.00 75.77 C ANISOU 3923 CA ALA B 62 9571 9496 9722 721 -706 634 C ATOM 3924 C ALA B 62 -22.158 71.044-400.457 1.00 71.40 C ANISOU 3924 C ALA B 62 8973 9017 9138 685 -465 762 C ATOM 3925 O ALA B 62 -22.081 69.905-400.003 1.00 73.77 O ANISOU 3925 O ALA B 62 9146 9284 9601 628 -392 866 O ATOM 3926 CB ALA B 62 -22.744 72.002-402.686 1.00 79.21 C ANISOU 3926 CB ALA B 62 10085 9876 10137 765 -770 509 C ATOM 3927 N ASP B 63 -21.272 71.985-400.175 1.00 57.07 N ANISOU 3927 N ASP B 63 7257 7316 7110 724 -345 753 N ATOM 3928 CA ASP B 63 -20.033 71.652-399.488 1.00 44.95 C ANISOU 3928 CA ASP B 63 5681 5850 5548 684 -139 850 C ATOM 3929 C ASP B 63 -20.222 71.001-398.125 1.00 43.74 C ANISOU 3929 C ASP B 63 5476 5726 5419 640 -46 951 C ATOM 3930 O ASP B 63 -19.263 70.505-397.549 1.00 46.34 O ANISOU 3930 O ASP B 63 5759 6099 5748 605 105 1019 O ATOM 3931 CB ASP B 63 -19.125 72.880-399.373 1.00 49.44 C ANISOU 3931 CB ASP B 63 6354 6555 5877 730 -42 830 C ATOM 3932 CG ASP B 63 -18.425 73.213-400.684 1.00 56.51 C ANISOU 3932 CG ASP B 63 7274 7422 6776 784 -64 756 C ATOM 3933 OD1 ASP B 63 -18.632 72.468-401.673 1.00 50.89 O ANISOU 3933 OD1 ASP B 63 6505 6562 6270 770 -160 721 O ATOM 3934 OD2 ASP B 63 -17.669 74.212-400.727 1.00 60.79 O ANISOU 3934 OD2 ASP B 63 7886 8086 7127 840 15 743 O ATOM 3935 N TYR B 64 -21.446 70.999-397.606 1.00 54.03 N ANISOU 3935 N TYR B 64 6790 7005 6734 653 -141 954 N ATOM 3936 CA TYR B 64 -21.704 70.375-396.310 1.00 53.81 C ANISOU 3936 CA TYR B 64 6723 6983 6738 633 -61 1041 C ATOM 3937 C TYR B 64 -22.291 68.990-396.485 1.00 53.60 C ANISOU 3937 C TYR B 64 6549 6868 6950 617 -102 1088 C ATOM 3938 O TYR B 64 -22.003 68.084-395.718 1.00 53.60 O ANISOU 3938 O TYR B 64 6477 6872 7017 608 13 1163 O ATOM 3939 CB TYR B 64 -22.635 71.223-395.450 1.00 57.72 C ANISOU 3939 CB TYR B 64 7317 7515 7098 669 -115 1048 C ATOM 3940 CG TYR B 64 -22.137 72.622-395.206 1.00 53.90 C ANISOU 3940 CG TYR B 64 6962 7139 6379 684 -67 1034 C ATOM 3941 CD1 TYR B 64 -22.404 73.634-396.116 1.00 48.75 C ANISOU 3941 CD1 TYR B 64 6383 6536 5604 742 -167 957 C ATOM 3942 CD2 TYR B 64 -21.406 72.935-394.070 1.00 53.67 C ANISOU 3942 CD2 TYR B 64 6976 7167 6251 644 75 1099 C ATOM 3943 CE1 TYR B 64 -21.957 74.920-395.907 1.00 52.52 C ANISOU 3943 CE1 TYR B 64 6959 7138 5857 772 -109 966 C ATOM 3944 CE2 TYR B 64 -20.951 74.222-393.849 1.00 46.75 C ANISOU 3944 CE2 TYR B 64 6189 6400 5173 647 121 1114 C ATOM 3945 CZ TYR B 64 -21.230 75.212-394.773 1.00 53.59 C ANISOU 3945 CZ TYR B 64 7113 7337 5912 717 38 1058 C ATOM 3946 OH TYR B 64 -20.788 76.504-394.575 1.00 57.05 O ANISOU 3946 OH TYR B 64 7625 7913 6140 737 98 1091 O ATOM 3947 N PHE B 65 -23.134 68.829-397.491 1.00 44.66 N ANISOU 3947 N PHE B 65 5365 5660 5943 619 -272 1045 N ATOM 3948 CA PHE B 65 -23.621 67.505-397.816 1.00 49.58 C ANISOU 3948 CA PHE B 65 5815 6205 6817 590 -314 1111 C ATOM 3949 C PHE B 65 -22.412 66.654-398.163 1.00 49.99 C ANISOU 3949 C PHE B 65 5772 6251 6970 552 -172 1176 C ATOM 3950 O PHE B 65 -22.142 65.655-397.500 1.00 48.97 O ANISOU 3950 O PHE B 65 5543 6152 6912 554 -44 1275 O ATOM 3951 CB PHE B 65 -24.584 67.538-398.995 1.00 50.79 C ANISOU 3951 CB PHE B 65 5926 6268 7104 575 -542 1044 C ATOM 3952 CG PHE B 65 -25.255 66.231-399.249 1.00 47.75 C ANISOU 3952 CG PHE B 65 5341 5814 6989 534 -604 1134 C ATOM 3953 CD1 PHE B 65 -26.540 66.004-398.798 1.00 48.39 C ANISOU 3953 CD1 PHE B 65 5363 5900 7122 560 -715 1162 C ATOM 3954 CD2 PHE B 65 -24.597 65.222-399.921 1.00 52.95 C ANISOU 3954 CD2 PHE B 65 5855 6414 7850 476 -544 1212 C ATOM 3955 CE1 PHE B 65 -27.160 64.799-399.023 1.00 48.33 C ANISOU 3955 CE1 PHE B 65 5147 5849 7367 525 -768 1263 C ATOM 3956 CE2 PHE B 65 -25.210 64.012-400.146 1.00 55.45 C ANISOU 3956 CE2 PHE B 65 5963 6684 8422 436 -590 1324 C ATOM 3957 CZ PHE B 65 -26.490 63.800-399.697 1.00 48.52 C ANISOU 3957 CZ PHE B 65 5018 5820 7596 459 -702 1348 C ATOM 3958 N MET B 66 -21.681 67.057-399.199 1.00 46.43 N ANISOU 3958 N MET B 66 5356 5770 6515 534 -190 1123 N ATOM 3959 CA MET B 66 -20.446 66.382-399.569 1.00 48.21 C ANISOU 3959 CA MET B 66 5503 6001 6812 508 -52 1196 C ATOM 3960 C MET B 66 -19.589 66.116-398.347 1.00 47.71 C ANISOU 3960 C MET B 66 5448 6060 6620 524 151 1261 C ATOM 3961 O MET B 66 -19.207 64.977-398.079 1.00 53.67 O ANISOU 3961 O MET B 66 6078 6838 7475 520 261 1366 O ATOM 3962 CB MET B 66 -19.655 67.228-400.559 1.00 52.74 C ANISOU 3962 CB MET B 66 6169 6554 7315 518 -73 1116 C ATOM 3963 CG MET B 66 -19.693 66.737-401.994 1.00 60.16 C ANISOU 3963 CG MET B 66 7027 7343 8487 482 -185 1114 C ATOM 3964 SD MET B 66 -21.349 66.653-402.681 1.00 87.55 S ANISOU 3964 SD MET B 66 10461 10669 12134 451 -458 1037 S ATOM 3965 CE MET B 66 -21.802 64.971-402.266 1.00 62.38 C ANISOU 3965 CE MET B 66 7030 7467 9206 389 -407 1225 C ATOM 3966 N SER B 67 -19.289 67.180-397.612 1.00 46.60 N ANISOU 3966 N SER B 67 5453 6000 6253 544 194 1201 N ATOM 3967 CA SER B 67 -18.443 67.091-396.428 1.00 46.55 C ANISOU 3967 CA SER B 67 5477 6097 6114 545 358 1238 C ATOM 3968 C SER B 67 -18.766 65.819-395.659 1.00 47.32 C ANISOU 3968 C SER B 67 5468 6189 6321 561 426 1315 C ATOM 3969 O SER B 67 -17.882 65.014-395.374 1.00 44.29 O ANISOU 3969 O SER B 67 5017 5867 5943 568 561 1374 O ATOM 3970 CB SER B 67 -18.656 68.316-395.534 1.00 43.21 C ANISOU 3970 CB SER B 67 5204 5724 5488 551 348 1183 C ATOM 3971 OG SER B 67 -17.429 68.831-395.048 1.00 43.70 O ANISOU 3971 OG SER B 67 5323 5888 5392 528 469 1183 O ATOM 3972 N ALA B 68 -20.042 65.640-395.339 1.00 42.16 N ANISOU 3972 N ALA B 68 4797 5478 5745 584 332 1318 N ATOM 3973 CA ALA B 68 -20.502 64.417-394.701 1.00 42.78 C ANISOU 3973 CA ALA B 68 4761 5554 5941 624 387 1397 C ATOM 3974 C ALA B 68 -20.366 63.241-395.656 1.00 43.50 C ANISOU 3974 C ALA B 68 4662 5627 6238 612 401 1493 C ATOM 3975 O ALA B 68 -19.537 62.365-395.443 1.00 44.39 O ANISOU 3975 O ALA B 68 4695 5810 6363 633 548 1567 O ATOM 3976 CB ALA B 68 -21.928 64.559-394.238 1.00 50.03 C ANISOU 3976 CB ALA B 68 5692 6418 6899 660 271 1390 C ATOM 3977 N MET B 69 -21.173 63.225-396.713 1.00 47.23 N ANISOU 3977 N MET B 69 5062 6010 6874 576 245 1497 N ATOM 3978 CA MET B 69 -21.201 62.084-397.626 1.00 50.85 C ANISOU 3978 CA MET B 69 5319 6429 7573 545 238 1613 C ATOM 3979 C MET B 69 -19.830 61.456-397.837 1.00 51.13 C ANISOU 3979 C MET B 69 5292 6531 7603 544 409 1698 C ATOM 3980 O MET B 69 -19.601 60.313-397.440 1.00 58.31 O ANISOU 3980 O MET B 69 6066 7514 8574 585 539 1820 O ATOM 3981 CB MET B 69 -21.793 62.452-398.985 1.00 51.98 C ANISOU 3981 CB MET B 69 5437 6443 7869 476 35 1569 C ATOM 3982 CG MET B 69 -22.078 61.232-399.855 1.00 57.44 C ANISOU 3982 CG MET B 69 5898 7069 8858 423 -3 1709 C ATOM 3983 SD MET B 69 -22.075 61.538-401.641 1.00 72.42 S ANISOU 3983 SD MET B 69 7777 8785 10955 323 -196 1664 S ATOM 3984 CE MET B 69 -20.324 61.496-402.020 1.00 63.26 C ANISOU 3984 CE MET B 69 6652 7658 9727 329 -8 1716 C ATOM 3985 N ASN B 70 -18.916 62.196-398.458 1.00 57.21 N ANISOU 3985 N ASN B 70 6157 7292 8289 513 414 1641 N ATOM 3986 CA ASN B 70 -17.622 61.618-398.805 1.00 59.56 C ANISOU 3986 CA ASN B 70 6386 7652 8593 515 560 1736 C ATOM 3987 C ASN B 70 -16.716 61.422-397.591 1.00 59.23 C ANISOU 3987 C ASN B 70 6391 7769 8344 574 743 1742 C ATOM 3988 O ASN B 70 -15.514 61.200-397.726 1.00 62.48 O ANISOU 3988 O ASN B 70 6784 8267 8687 585 862 1794 O ATOM 3989 CB ASN B 70 -16.927 62.402-399.924 1.00 58.94 C ANISOU 3989 CB ASN B 70 6378 7507 8508 480 506 1686 C ATOM 3990 CG ASN B 70 -16.235 63.640-399.425 1.00 55.94 C ANISOU 3990 CG ASN B 70 6183 7209 7864 503 543 1565 C ATOM 3991 OD1 ASN B 70 -16.466 64.084-398.302 1.00 56.26 O ANISOU 3991 OD1 ASN B 70 6315 7319 7742 523 569 1503 O ATOM 3992 ND2 ASN B 70 -15.377 64.212-400.260 1.00 54.90 N ANISOU 3992 ND2 ASN B 70 6099 7063 7697 502 546 1544 N ATOM 3993 N PHE B 71 -17.305 61.509-396.404 1.00 41.69 N ANISOU 3993 N PHE B 71 4235 5580 6026 613 753 1687 N ATOM 3994 CA PHE B 71 -16.623 61.101-395.182 1.00 41.94 C ANISOU 3994 CA PHE B 71 4299 5737 5898 674 907 1685 C ATOM 3995 C PHE B 71 -17.152 59.750-394.744 1.00 42.00 C ANISOU 3995 C PHE B 71 4158 5783 6017 750 980 1789 C ATOM 3996 O PHE B 71 -16.389 58.887-394.349 1.00 44.31 O ANISOU 3996 O PHE B 71 4386 6195 6253 814 1129 1854 O ATOM 3997 CB PHE B 71 -16.830 62.113-394.052 1.00 40.90 C ANISOU 3997 CB PHE B 71 4354 5601 5586 675 879 1553 C ATOM 3998 CG PHE B 71 -16.691 61.517-392.669 1.00 41.92 C ANISOU 3998 CG PHE B 71 4513 5796 5619 748 988 1536 C ATOM 3999 CD1 PHE B 71 -15.555 61.739-391.914 1.00 42.17 C ANISOU 3999 CD1 PHE B 71 4638 5920 5465 748 1082 1477 C ATOM 4000 CD2 PHE B 71 -17.700 60.736-392.125 1.00 42.22 C ANISOU 4000 CD2 PHE B 71 4486 5802 5753 824 987 1572 C ATOM 4001 CE1 PHE B 71 -15.423 61.191-390.650 1.00 40.73 C ANISOU 4001 CE1 PHE B 71 4501 5779 5195 820 1164 1434 C ATOM 4002 CE2 PHE B 71 -17.567 60.187-390.864 1.00 43.33 C ANISOU 4002 CE2 PHE B 71 4671 5991 5803 914 1086 1539 C ATOM 4003 CZ PHE B 71 -16.427 60.414-390.130 1.00 42.29 C ANISOU 4003 CZ PHE B 71 4649 5933 5486 911 1170 1460 C ATOM 4004 N LEU B 72 -18.469 59.583-394.797 1.00 44.09 N ANISOU 4004 N LEU B 72 4364 5963 6426 756 874 1807 N ATOM 4005 CA LEU B 72 -19.081 58.319-394.428 1.00 44.42 C ANISOU 4005 CA LEU B 72 4241 6049 6586 839 939 1921 C ATOM 4006 C LEU B 72 -18.478 57.178-395.242 1.00 45.61 C ANISOU 4006 C LEU B 72 4187 6273 6871 844 1041 2096 C ATOM 4007 O LEU B 72 -18.804 56.011-395.023 1.00 49.11 O ANISOU 4007 O LEU B 72 4460 6791 7407 923 1128 2227 O ATOM 4008 CB LEU B 72 -20.595 58.360-394.639 1.00 46.75 C ANISOU 4008 CB LEU B 72 4471 6243 7047 827 782 1935 C ATOM 4009 CG LEU B 72 -21.462 59.117-393.636 1.00 46.73 C ANISOU 4009 CG LEU B 72 4621 6191 6942 866 706 1821 C ATOM 4010 CD1 LEU B 72 -20.974 58.847-392.233 1.00 44.92 C ANISOU 4010 CD1 LEU B 72 4487 6037 6544 971 857 1776 C ATOM 4011 CD2 LEU B 72 -21.458 60.602-393.921 1.00 44.48 C ANISOU 4011 CD2 LEU B 72 4520 5830 6550 783 578 1690 C ATOM 4012 N GLN B 73 -17.607 57.522-396.186 1.00 83.03 N ANISOU 4012 N GLN B 73 8934 10993 11619 768 1035 2113 N ATOM 4013 CA GLN B 73 -16.869 56.532-396.964 1.00 84.97 C ANISOU 4013 CA GLN B 73 9001 11305 11978 770 1141 2296 C ATOM 4014 C GLN B 73 -15.808 55.831-396.106 1.00 88.28 C ANISOU 4014 C GLN B 73 9416 11924 12204 882 1350 2337 C ATOM 4015 O GLN B 73 -15.506 54.653-396.315 1.00 94.18 O ANISOU 4015 O GLN B 73 9980 12781 13024 942 1476 2519 O ATOM 4016 CB GLN B 73 -16.219 57.200-398.177 1.00 84.15 C ANISOU 4016 CB GLN B 73 8935 11108 11930 672 1069 2291 C ATOM 4017 CG GLN B 73 -17.199 57.931-399.081 1.00 85.39 C ANISOU 4017 CG GLN B 73 9119 11068 12257 573 849 2220 C ATOM 4018 CD GLN B 73 -18.050 56.985-399.903 1.00 91.59 C ANISOU 4018 CD GLN B 73 9679 11768 13354 523 775 2380 C ATOM 4019 OE1 GLN B 73 -17.618 55.884-400.251 1.00 95.10 O ANISOU 4019 OE1 GLN B 73 9934 12274 13924 534 890 2581 O ATOM 4020 NE2 GLN B 73 -19.265 57.413-400.224 1.00 88.80 N ANISOU 4020 NE2 GLN B 73 9333 11281 13125 464 576 2303 N ATOM 4021 N TYR B 74 -15.242 56.569-395.149 1.00 55.03 N ANISOU 4021 N TYR B 74 5404 7762 7744 909 1379 2171 N ATOM 4022 CA TYR B 74 -14.337 56.015-394.141 1.00 54.01 C ANISOU 4022 CA TYR B 74 5307 7811 7402 1020 1543 2154 C ATOM 4023 C TYR B 74 -15.005 56.100-392.775 1.00 51.61 C ANISOU 4023 C TYR B 74 5119 7497 6994 1096 1538 2020 C ATOM 4024 O TYR B 74 -14.367 55.885-391.748 1.00 54.21 O ANISOU 4024 O TYR B 74 5536 7934 7128 1182 1635 1939 O ATOM 4025 CB TYR B 74 -13.039 56.819-394.075 1.00 51.22 C ANISOU 4025 CB TYR B 74 5094 7520 6848 978 1566 2061 C ATOM 4026 CG TYR B 74 -12.643 57.509-395.357 1.00 50.97 C ANISOU 4026 CG TYR B 74 5053 7407 6906 873 1490 2100 C ATOM 4027 CD1 TYR B 74 -11.601 57.023-396.134 1.00 52.54 C ANISOU 4027 CD1 TYR B 74 5148 7697 7118 883 1580 2240 C ATOM 4028 CD2 TYR B 74 -13.300 58.657-395.786 1.00 50.96 C ANISOU 4028 CD2 TYR B 74 5153 7242 6966 780 1330 1998 C ATOM 4029 CE1 TYR B 74 -11.226 57.655-397.309 1.00 55.26 C ANISOU 4029 CE1 TYR B 74 5495 7948 7553 803 1511 2271 C ATOM 4030 CE2 TYR B 74 -12.938 59.297-396.963 1.00 50.89 C ANISOU 4030 CE2 TYR B 74 5152 7154 7030 709 1259 2014 C ATOM 4031 CZ TYR B 74 -11.898 58.792-397.722 1.00 52.71 C ANISOU 4031 CZ TYR B 74 5283 7454 7290 721 1349 2148 C ATOM 4032 OH TYR B 74 -11.525 59.413-398.899 1.00 54.01 O ANISOU 4032 OH TYR B 74 5463 7523 7536 667 1281 2163 O ATOM 4033 N GLY B 75 -16.295 56.419-392.768 1.00 91.21 N ANISOU 4033 N GLY B 75 10139 12375 12142 1069 1415 1994 N ATOM 4034 CA GLY B 75 -16.960 56.837-391.550 1.00 94.95 C ANISOU 4034 CA GLY B 75 10760 12792 12524 1120 1378 1856 C ATOM 4035 C GLY B 75 -17.879 55.832-390.891 1.00101.27 C ANISOU 4035 C GLY B 75 11461 13618 13398 1258 1430 1914 C ATOM 4036 O GLY B 75 -18.636 55.120-391.550 1.00101.30 O ANISOU 4036 O GLY B 75 11268 13621 13600 1272 1414 2061 O ATOM 4037 N ASN B 76 -17.795 55.784-389.568 1.00127.26 N ANISOU 4037 N ASN B 76 14889 16929 16535 1363 1489 1796 N ATOM 4038 CA ASN B 76 -18.710 54.998-388.765 1.00129.13 C ANISOU 4038 CA ASN B 76 15076 17171 16818 1519 1533 1817 C ATOM 4039 C ASN B 76 -19.851 55.906-388.331 1.00121.13 C ANISOU 4039 C ASN B 76 14181 15984 15858 1483 1384 1735 C ATOM 4040 O ASN B 76 -20.979 55.776-388.802 1.00122.85 O ANISOU 4040 O ASN B 76 14277 16149 16251 1479 1299 1826 O ATOM 4041 CB ASN B 76 -17.996 54.438-387.529 1.00135.66 C ANISOU 4041 CB ASN B 76 16006 18094 17443 1675 1672 1715 C ATOM 4042 CG ASN B 76 -16.533 54.102-387.789 1.00142.71 C ANISOU 4042 CG ASN B 76 16885 19150 18187 1669 1784 1724 C ATOM 4043 OD1 ASN B 76 -16.184 53.567-388.842 1.00148.40 O ANISOU 4043 OD1 ASN B 76 17424 19972 18991 1641 1835 1888 O ATOM 4044 ND2 ASN B 76 -15.671 54.412-386.823 1.00136.66 N ANISOU 4044 ND2 ASN B 76 16309 18408 17208 1695 1813 1553 N ATOM 4045 N ASP B 77 -19.538 56.843-387.441 1.00 69.26 N ANISOU 4045 N ASP B 77 7844 9332 9140 1449 1347 1574 N ATOM 4046 CA ASP B 77 -20.538 57.766-386.921 1.00 67.25 C ANISOU 4046 CA ASP B 77 7719 8918 8915 1421 1218 1509 C ATOM 4047 C ASP B 77 -20.163 59.232-387.156 1.00 65.91 C ANISOU 4047 C ASP B 77 7704 8671 8666 1252 1111 1427 C ATOM 4048 O ASP B 77 -18.999 59.617-387.058 1.00 68.52 O ANISOU 4048 O ASP B 77 8123 9048 8862 1185 1155 1358 O ATOM 4049 CB ASP B 77 -20.823 57.497-385.432 1.00 68.85 C ANISOU 4049 CB ASP B 77 8052 9062 9046 1568 1269 1417 C ATOM 4050 CG ASP B 77 -19.946 58.320-384.496 1.00 71.70 C ANISOU 4050 CG ASP B 77 8649 9359 9236 1507 1267 1256 C ATOM 4051 OD1 ASP B 77 -18.816 58.682-384.883 1.00 74.07 O ANISOU 4051 OD1 ASP B 77 8977 9731 9435 1399 1287 1221 O ATOM 4052 OD2 ASP B 77 -20.390 58.597-383.359 1.00 70.21 O ANISOU 4052 OD2 ASP B 77 8612 9042 9024 1568 1241 1173 O ATOM 4053 N LEU B 78 -21.170 60.037-387.478 1.00 46.51 N ANISOU 4053 N LEU B 78 5270 6115 6286 1193 971 1444 N ATOM 4054 CA LEU B 78 -20.994 61.457-387.701 1.00 46.23 C ANISOU 4054 CA LEU B 78 5373 6022 6171 1059 872 1383 C ATOM 4055 C LEU B 78 -22.055 62.185-386.904 1.00 45.37 C ANISOU 4055 C LEU B 78 5384 5793 6063 1082 779 1361 C ATOM 4056 O LEU B 78 -23.230 61.843-386.966 1.00 53.45 O ANISOU 4056 O LEU B 78 6328 6779 7202 1154 717 1423 O ATOM 4057 CB LEU B 78 -21.155 61.777-389.187 1.00 47.08 C ANISOU 4057 CB LEU B 78 5375 6149 6364 968 780 1439 C ATOM 4058 CG LEU B 78 -21.020 63.246-389.595 1.00 47.91 C ANISOU 4058 CG LEU B 78 5607 6221 6376 856 679 1382 C ATOM 4059 CD1 LEU B 78 -19.559 63.605-389.802 1.00 48.51 C ANISOU 4059 CD1 LEU B 78 5731 6373 6327 784 758 1340 C ATOM 4060 CD2 LEU B 78 -21.810 63.532-390.862 1.00 46.99 C ANISOU 4060 CD2 LEU B 78 5406 6077 6371 815 539 1417 C ATOM 4061 N ARG B 79 -21.651 63.178-386.137 1.00 49.43 N ANISOU 4061 N ARG B 79 6078 6249 6454 1020 768 1288 N ATOM 4062 CA ARG B 79 -22.621 63.967-385.413 1.00 51.80 C ANISOU 4062 CA ARG B 79 6495 6433 6755 1033 682 1292 C ATOM 4063 C ARG B 79 -22.706 65.316-386.102 1.00 43.46 C ANISOU 4063 C ARG B 79 5492 5386 5634 915 579 1303 C ATOM 4064 O ARG B 79 -21.680 65.980-386.278 1.00 45.37 O ANISOU 4064 O ARG B 79 5792 5678 5768 815 608 1263 O ATOM 4065 CB ARG B 79 -22.175 64.147-383.970 1.00 46.96 C ANISOU 4065 CB ARG B 79 6049 5728 6067 1047 738 1220 C ATOM 4066 CG ARG B 79 -21.580 62.894-383.346 1.00 48.92 C ANISOU 4066 CG ARG B 79 6273 6002 6312 1155 860 1162 C ATOM 4067 CD ARG B 79 -22.654 61.964-382.812 1.00 49.57 C ANISOU 4067 CD ARG B 79 6304 6027 6503 1334 876 1199 C ATOM 4068 NE ARG B 79 -22.088 60.873-382.022 1.00 51.37 N ANISOU 4068 NE ARG B 79 6546 6275 6696 1464 999 1125 N ATOM 4069 CZ ARG B 79 -21.683 60.994-380.762 1.00 54.39 C ANISOU 4069 CZ ARG B 79 7110 6546 7011 1494 1024 1010 C ATOM 4070 NH1 ARG B 79 -21.772 62.164-380.142 1.00 58.50 N ANISOU 4070 NH1 ARG B 79 7798 6919 7511 1385 940 981 N ATOM 4071 NH2 ARG B 79 -21.183 59.946-380.122 1.00 55.96 N ANISOU 4071 NH2 ARG B 79 7322 6780 7162 1636 1129 926 N ATOM 4072 N VAL B 80 -23.915 65.724-386.501 1.00 44.92 N ANISOU 4072 N VAL B 80 5652 5543 5873 939 460 1357 N ATOM 4073 CA VAL B 80 -24.097 66.993-387.212 1.00 43.11 C ANISOU 4073 CA VAL B 80 5474 5343 5561 859 358 1362 C ATOM 4074 C VAL B 80 -25.011 67.958-386.476 1.00 47.41 C ANISOU 4074 C VAL B 80 6138 5820 6055 878 282 1405 C ATOM 4075 O VAL B 80 -25.742 67.573-385.573 1.00 47.58 O ANISOU 4075 O VAL B 80 6183 5756 6141 963 282 1442 O ATOM 4076 CB VAL B 80 -24.648 66.781-388.628 1.00 46.90 C ANISOU 4076 CB VAL B 80 5821 5875 6124 859 255 1376 C ATOM 4077 CG1 VAL B 80 -24.135 65.470-389.200 1.00 49.26 C ANISOU 4077 CG1 VAL B 80 5961 6212 6542 873 328 1385 C ATOM 4078 CG2 VAL B 80 -26.158 66.789-388.608 1.00 48.27 C ANISOU 4078 CG2 VAL B 80 5960 6010 6372 933 127 1429 C ATOM 4079 N VAL B 81 -24.952 69.220-386.873 1.00 54.37 N ANISOU 4079 N VAL B 81 7093 6750 6816 812 224 1411 N ATOM 4080 CA VAL B 81 -25.830 70.247-386.333 1.00 53.65 C ANISOU 4080 CA VAL B 81 7103 6626 6655 832 150 1479 C ATOM 4081 C VAL B 81 -26.169 71.226-387.449 1.00 52.51 C ANISOU 4081 C VAL B 81 6957 6588 6406 816 45 1478 C ATOM 4082 O VAL B 81 -25.289 71.916-387.967 1.00 52.60 O ANISOU 4082 O VAL B 81 6998 6680 6308 747 77 1442 O ATOM 4083 CB VAL B 81 -25.156 71.011-385.183 1.00 54.44 C ANISOU 4083 CB VAL B 81 7341 6672 6671 762 228 1504 C ATOM 4084 CG1 VAL B 81 -25.995 72.205-384.770 1.00 54.87 C ANISOU 4084 CG1 VAL B 81 7488 6715 6644 772 159 1608 C ATOM 4085 CG2 VAL B 81 -24.925 70.097-384.004 1.00 56.56 C ANISOU 4085 CG2 VAL B 81 7641 6813 7037 794 309 1482 C ATOM 4086 N ARG B 82 -27.439 71.287-387.831 1.00 59.49 N ANISOU 4086 N ARG B 82 7806 7481 7316 893 -86 1510 N ATOM 4087 CA ARG B 82 -27.829 72.156-388.933 1.00 61.14 C ANISOU 4087 CA ARG B 82 8022 7793 7415 899 -206 1481 C ATOM 4088 C ARG B 82 -27.877 73.616-388.513 1.00 61.29 C ANISOU 4088 C ARG B 82 8172 7875 7240 893 -204 1545 C ATOM 4089 O ARG B 82 -28.522 73.963-387.527 1.00 65.20 O ANISOU 4089 O ARG B 82 8730 8325 7718 930 -206 1649 O ATOM 4090 CB ARG B 82 -29.187 71.750-389.498 1.00 67.78 C ANISOU 4090 CB ARG B 82 8778 8637 8337 980 -370 1486 C ATOM 4091 CG ARG B 82 -29.597 72.566-390.722 1.00 66.50 C ANISOU 4091 CG ARG B 82 8630 8577 8061 995 -519 1420 C ATOM 4092 CD ARG B 82 -31.097 72.551-390.928 1.00 68.18 C ANISOU 4092 CD ARG B 82 8802 8811 8294 1082 -700 1447 C ATOM 4093 NE ARG B 82 -31.464 72.758-392.323 1.00 66.77 N ANISOU 4093 NE ARG B 82 8587 8693 8090 1088 -871 1335 N ATOM 4094 CZ ARG B 82 -32.696 73.044-392.726 1.00 67.68 C ANISOU 4094 CZ ARG B 82 8689 8863 8163 1160 -1064 1326 C ATOM 4095 NH1 ARG B 82 -33.668 73.170-391.834 1.00 65.98 N ANISOU 4095 NH1 ARG B 82 8486 8660 7922 1238 -1097 1443 N ATOM 4096 NH2 ARG B 82 -32.952 73.211-394.014 1.00 71.97 N ANISOU 4096 NH2 ARG B 82 9212 9444 8690 1158 -1232 1196 N ATOM 4097 N ALA B 83 -27.200 74.472-389.269 1.00103.40 N ANISOU 4097 N ALA B 83 13540 13318 12431 856 -195 1498 N ATOM 4098 CA ALA B 83 -27.264 75.904-389.023 1.00108.34 C ANISOU 4098 CA ALA B 83 14267 14043 12855 865 -189 1574 C ATOM 4099 C ALA B 83 -28.435 76.518-389.779 1.00107.03 C ANISOU 4099 C ALA B 83 14117 13974 12576 970 -348 1566 C ATOM 4100 O ALA B 83 -28.491 76.475-391.006 1.00108.14 O ANISOU 4100 O ALA B 83 14224 14171 12694 1000 -441 1447 O ATOM 4101 CB ALA B 83 -25.963 76.574-389.418 1.00101.87 C ANISOU 4101 CB ALA B 83 13470 13319 11917 797 -90 1539 C ATOM 4102 N VAL B 84 -29.373 77.078-389.027 1.00 53.58 N ANISOU 4102 N VAL B 84 7402 7216 5740 1030 -387 1692 N ATOM 4103 CA VAL B 84 -30.520 77.769-389.586 1.00 54.72 C ANISOU 4103 CA VAL B 84 7573 7479 5739 1143 -538 1702 C ATOM 4104 C VAL B 84 -30.405 79.232-389.201 1.00 53.28 C ANISOU 4104 C VAL B 84 7488 7433 5322 1166 -477 1826 C ATOM 4105 O VAL B 84 -29.731 79.547-388.228 1.00 58.04 O ANISOU 4105 O VAL B 84 8126 7992 5935 1086 -337 1941 O ATOM 4106 CB VAL B 84 -31.821 77.198-389.006 1.00 51.24 C ANISOU 4106 CB VAL B 84 7100 6963 5406 1216 -637 1782 C ATOM 4107 CG1 VAL B 84 -32.716 78.311-388.473 1.00 57.63 C ANISOU 4107 CG1 VAL B 84 7991 7871 6033 1307 -679 1938 C ATOM 4108 CG2 VAL B 84 -32.534 76.335-390.038 1.00 59.08 C ANISOU 4108 CG2 VAL B 84 7990 7951 6508 1259 -805 1655 C ATOM 4109 N ASP B 85 -31.036 80.132-389.945 1.00 52.65 N ANISOU 4109 N ASP B 85 7449 7524 5030 1274 -582 1809 N ATOM 4110 CA ASP B 85 -31.047 81.524-389.509 1.00 53.41 C ANISOU 4110 CA ASP B 85 7624 7777 4893 1317 -515 1966 C ATOM 4111 C ASP B 85 -32.234 81.322-388.597 1.00 58.25 C ANISOU 4111 C ASP B 85 8268 8386 5479 1390 -564 2152 C ATOM 4112 O ASP B 85 -33.226 80.737-389.005 1.00 56.65 O ANISOU 4112 O ASP B 85 8089 8322 5115 1523 -696 2159 O ATOM 4113 CB ASP B 85 -31.088 82.505-390.675 1.00 54.29 C ANISOU 4113 CB ASP B 85 7779 8110 4740 1428 -579 1873 C ATOM 4114 CG ASP B 85 -31.221 83.947-390.205 1.00 56.28 C ANISOU 4114 CG ASP B 85 8095 8557 4730 1498 -503 2067 C ATOM 4115 OD1 ASP B 85 -30.198 84.564-389.815 1.00 57.00 O ANISOU 4115 OD1 ASP B 85 8190 8700 4769 1422 -338 2162 O ATOM 4116 OD2 ASP B 85 -32.358 84.459-390.226 1.00 57.84 O ANISOU 4116 OD2 ASP B 85 8330 8872 4774 1629 -610 2136 O ATOM 4117 N ARG B 86 -32.133 81.819-387.370 1.00 63.87 N ANISOU 4117 N ARG B 86 8984 8937 6346 1309 -463 2298 N ATOM 4118 CA ARG B 86 -33.162 81.624-386.344 1.00 61.53 C ANISOU 4118 CA ARG B 86 8717 8587 6074 1375 -500 2491 C ATOM 4119 C ARG B 86 -34.188 82.726-386.619 1.00 62.68 C ANISOU 4119 C ARG B 86 8906 8950 5959 1524 -591 2608 C ATOM 4120 O ARG B 86 -35.348 82.615-386.225 1.00 76.07 O ANISOU 4120 O ARG B 86 10604 10632 7666 1623 -687 2712 O ATOM 4121 CB ARG B 86 -32.575 81.825-384.945 1.00 71.50 C ANISOU 4121 CB ARG B 86 10022 9701 7445 1262 -346 2671 C ATOM 4122 CG ARG B 86 -32.472 80.564-384.119 1.00 60.80 C ANISOU 4122 CG ARG B 86 8648 8082 6372 1202 -318 2634 C ATOM 4123 CD ARG B 86 -31.389 80.695-383.057 1.00 61.33 C ANISOU 4123 CD ARG B 86 8758 8002 6542 1049 -166 2710 C ATOM 4124 NE ARG B 86 -31.864 80.211-381.763 1.00 63.65 N ANISOU 4124 NE ARG B 86 9097 8062 7024 1052 -152 2824 N ATOM 4125 CZ ARG B 86 -31.934 78.929-381.417 1.00 61.68 C ANISOU 4125 CZ ARG B 86 8826 7628 6980 1067 -161 2715 C ATOM 4126 NH1 ARG B 86 -31.555 77.984-382.267 1.00 67.67 N ANISOU 4126 NH1 ARG B 86 9506 8415 7790 1066 -181 2510 N ATOM 4127 NH2 ARG B 86 -32.388 78.592-380.215 1.00 65.79 N ANISOU 4127 NH2 ARG B 86 9404 7935 7657 1093 -146 2822 N ATOM 4128 N ASP B 87 -33.753 83.790-387.281 1.00 62.35 N ANISOU 4128 N ASP B 87 8896 9123 5672 1557 -557 2596 N ATOM 4129 CA ASP B 87 -34.593 84.960-387.484 1.00 68.03 C ANISOU 4129 CA ASP B 87 9664 10084 6101 1711 -615 2723 C ATOM 4130 C ASP B 87 -35.520 84.822-388.688 1.00 68.01 C ANISOU 4130 C ASP B 87 9658 10218 5965 1861 -827 2535 C ATOM 4131 O ASP B 87 -36.526 85.523-388.781 1.00 68.81 O ANISOU 4131 O ASP B 87 9795 10499 5849 2013 -922 2629 O ATOM 4132 CB ASP B 87 -33.728 86.217-387.641 1.00 68.54 C ANISOU 4132 CB ASP B 87 9758 10346 5937 1703 -474 2807 C ATOM 4133 CG ASP B 87 -32.947 86.555-386.382 1.00 77.06 C ANISOU 4133 CG ASP B 87 10834 11318 7129 1551 -286 3036 C ATOM 4134 OD1 ASP B 87 -33.577 86.681-385.310 1.00 72.35 O ANISOU 4134 OD1 ASP B 87 10256 10631 6601 1547 -271 3263 O ATOM 4135 OD2 ASP B 87 -31.702 86.703-386.472 1.00 87.65 O ANISOU 4135 OD2 ASP B 87 12150 12659 8493 1434 -163 2992 O ATOM 4136 N THR B 88 -35.188 83.937-389.619 1.00 62.19 N ANISOU 4136 N THR B 88 7107 9691 6833 437 -580 -412 N ATOM 4137 CA THR B 88 -35.970 83.854-390.843 1.00 60.24 C ANISOU 4137 CA THR B 88 7038 9402 6449 635 -630 -313 C ATOM 4138 C THR B 88 -36.180 82.445-391.368 1.00 63.59 C ANISOU 4138 C THR B 88 7738 9527 6897 706 -663 -351 C ATOM 4139 O THR B 88 -36.617 82.264-392.498 1.00 57.93 O ANISOU 4139 O THR B 88 7179 8760 6072 877 -738 -312 O ATOM 4140 CB THR B 88 -35.348 84.691-391.962 1.00 61.50 C ANISOU 4140 CB THR B 88 7172 9909 6287 898 -752 -381 C ATOM 4141 OG1 THR B 88 -34.055 84.169-392.280 1.00 62.53 O ANISOU 4141 OG1 THR B 88 7386 10124 6247 1024 -840 -595 O ATOM 4142 CG2 THR B 88 -35.226 86.143-391.535 1.00 64.43 C ANISOU 4142 CG2 THR B 88 7241 10632 6608 851 -708 -304 C ATOM 4143 N ALA B 89 -35.866 81.441-390.567 1.00 61.28 N ANISOU 4143 N ALA B 89 7494 9042 6747 587 -616 -426 N ATOM 4144 CA ALA B 89 -36.144 80.086-390.987 1.00 59.73 C ANISOU 4144 CA ALA B 89 7529 8586 6581 646 -619 -416 C ATOM 4145 C ALA B 89 -37.592 79.842-390.649 1.00 62.17 C ANISOU 4145 C ALA B 89 7865 8653 7102 509 -535 -243 C ATOM 4146 O ALA B 89 -38.118 80.456-389.724 1.00 62.52 O ANISOU 4146 O ALA B 89 7764 8690 7299 345 -459 -167 O ATOM 4147 CB ALA B 89 -35.275 79.123-390.259 1.00 63.03 C ANISOU 4147 CB ALA B 89 7973 8941 7033 623 -604 -560 C ATOM 4148 N LYS B 90 -38.234 78.948-391.398 1.00 60.23 N ANISOU 4148 N LYS B 90 7801 8213 6872 578 -547 -174 N ATOM 4149 CA LYS B 90 -39.644 78.639-391.195 1.00 57.96 C ANISOU 4149 CA LYS B 90 7545 7716 6763 480 -479 -29 C ATOM 4150 C LYS B 90 -39.967 77.161-391.434 1.00 59.50 C ANISOU 4150 C LYS B 90 7904 7676 7028 484 -457 1 C ATOM 4151 O LYS B 90 -39.498 76.562-392.400 1.00 62.42 O ANISOU 4151 O LYS B 90 8401 8020 7296 610 -519 -20 O ATOM 4152 CB LYS B 90 -40.515 79.529-392.089 1.00 59.29 C ANISOU 4152 CB LYS B 90 7696 7956 6877 580 -533 61 C ATOM 4153 CG LYS B 90 -40.470 81.010-391.719 1.00 61.55 C ANISOU 4153 CG LYS B 90 7786 8495 7105 575 -517 95 C ATOM 4154 CD LYS B 90 -40.912 81.216-390.283 1.00 59.77 C ANISOU 4154 CD LYS B 90 7435 8195 7079 358 -379 178 C ATOM 4155 CE LYS B 90 -40.577 82.604-389.788 1.00 62.31 C ANISOU 4155 CE LYS B 90 7534 8775 7366 313 -343 226 C ATOM 4156 NZ LYS B 90 -40.911 82.744-388.344 1.00 64.60 N ANISOU 4156 NZ LYS B 90 7714 8938 7892 76 -215 312 N ATOM 4157 N ASN B 91 -40.756 76.582-390.530 1.00 55.06 N ANISOU 4157 N ASN B 91 7334 6949 6637 352 -365 63 N ATOM 4158 CA ASN B 91 -41.322 75.253-390.706 1.00 54.15 C ANISOU 4158 CA ASN B 91 7337 6642 6596 349 -327 127 C ATOM 4159 C ASN B 91 -42.644 75.392-391.423 1.00 52.80 C ANISOU 4159 C ASN B 91 7191 6376 6494 355 -338 239 C ATOM 4160 O ASN B 91 -43.492 76.158-390.985 1.00 52.51 O ANISOU 4160 O ASN B 91 7074 6352 6525 303 -305 289 O ATOM 4161 CB ASN B 91 -41.613 74.625-389.351 1.00 55.44 C ANISOU 4161 CB ASN B 91 7473 6702 6888 236 -241 121 C ATOM 4162 CG ASN B 91 -40.371 74.205-388.624 1.00 54.64 C ANISOU 4162 CG ASN B 91 7356 6669 6736 260 -251 -20 C ATOM 4163 OD1 ASN B 91 -39.846 74.946-387.800 1.00 57.06 O ANISOU 4163 OD1 ASN B 91 7553 7053 7074 192 -265 -116 O ATOM 4164 ND2 ASN B 91 -39.888 73.006-388.919 1.00 55.63 N ANISOU 4164 ND2 ASN B 91 7576 6773 6786 366 -245 -33 N ATOM 4165 N SER B 92 -42.841 74.666-392.514 1.00 55.54 N ANISOU 4165 N SER B 92 7641 6625 6835 423 -386 281 N ATOM 4166 CA SER B 92 -44.120 74.730-393.201 1.00 52.02 C ANISOU 4166 CA SER B 92 7204 6081 6482 431 -421 353 C ATOM 4167 C SER B 92 -45.247 74.560-392.186 1.00 55.80 C ANISOU 4167 C SER B 92 7624 6489 7088 327 -315 411 C ATOM 4168 O SER B 92 -45.093 73.836-391.207 1.00 58.19 O ANISOU 4168 O SER B 92 7930 6746 7433 249 -226 415 O ATOM 4169 CB SER B 92 -44.197 73.647-394.264 1.00 54.79 C ANISOU 4169 CB SER B 92 7660 6279 6879 459 -465 403 C ATOM 4170 OG SER B 92 -42.940 73.475-394.877 1.00 53.45 O ANISOU 4170 OG SER B 92 7575 6148 6587 548 -521 365 O ATOM 4171 N SER B 93 -46.376 75.229-392.415 1.00 70.41 N ANISOU 4171 N SER B 93 9427 8343 8984 358 -336 445 N ATOM 4172 CA SER B 93 -47.497 75.180-391.472 1.00 68.90 C ANISOU 4172 CA SER B 93 9192 8098 8890 293 -236 502 C ATOM 4173 C SER B 93 -48.854 75.387-392.149 1.00 66.85 C ANISOU 4173 C SER B 93 8912 7809 8680 374 -280 528 C ATOM 4174 O SER B 93 -48.923 75.739-393.324 1.00 66.35 O ANISOU 4174 O SER B 93 8856 7771 8584 484 -408 489 O ATOM 4175 CB SER B 93 -47.302 76.216-390.363 1.00 66.74 C ANISOU 4175 CB SER B 93 8836 7920 8601 247 -167 517 C ATOM 4176 OG SER B 93 -47.651 77.509-390.819 1.00 67.46 O ANISOU 4176 OG SER B 93 8851 8154 8625 350 -208 545 O ATOM 4177 N PRO B 94 -49.948 75.168-391.402 1.00 52.46 N ANISOU 4177 N PRO B 94 7068 5934 6932 344 -192 575 N ATOM 4178 CA PRO B 94 -51.286 75.282-391.980 1.00 51.92 C ANISOU 4178 CA PRO B 94 6970 5853 6904 444 -234 574 C ATOM 4179 C PRO B 94 -51.768 76.719-391.955 1.00 52.92 C ANISOU 4179 C PRO B 94 7025 6129 6954 582 -246 593 C ATOM 4180 O PRO B 94 -52.773 77.036-392.584 1.00 52.40 O ANISOU 4180 O PRO B 94 6923 6101 6886 728 -313 564 O ATOM 4181 CB PRO B 94 -52.159 74.440-391.034 1.00 50.83 C ANISOU 4181 CB PRO B 94 6843 5629 6840 377 -118 614 C ATOM 4182 CG PRO B 94 -51.234 73.861-390.007 1.00 51.17 C ANISOU 4182 CG PRO B 94 6931 5628 6883 252 -35 630 C ATOM 4183 CD PRO B 94 -50.007 74.715-390.007 1.00 51.20 C ANISOU 4183 CD PRO B 94 6920 5715 6817 239 -66 608 C ATOM 4184 N ILE B 95 -51.076 77.576-391.215 1.00 51.80 N ANISOU 4184 N ILE B 95 6845 6086 6750 548 -181 643 N ATOM 4185 CA ILE B 95 -51.427 78.989-391.184 1.00 52.73 C ANISOU 4185 CA ILE B 95 6870 6386 6778 686 -171 704 C ATOM 4186 C ILE B 95 -51.114 79.651-392.517 1.00 54.93 C ANISOU 4186 C ILE B 95 7121 6812 6939 867 -338 627 C ATOM 4187 O ILE B 95 -51.847 80.519-392.979 1.00 53.95 O ANISOU 4187 O ILE B 95 6931 6835 6734 1076 -390 635 O ATOM 4188 CB ILE B 95 -50.660 79.742-390.076 1.00 54.94 C ANISOU 4188 CB ILE B 95 7088 6739 7047 571 -58 794 C ATOM 4189 CG1 ILE B 95 -51.457 79.748-388.772 1.00 55.86 C ANISOU 4189 CG1 ILE B 95 7206 6758 7262 493 96 907 C ATOM 4190 CG2 ILE B 95 -50.390 81.175-390.497 1.00 54.15 C ANISOU 4190 CG2 ILE B 95 6871 6895 6807 716 -92 843 C ATOM 4191 CD1 ILE B 95 -51.024 78.706-387.789 1.00 53.40 C ANISOU 4191 CD1 ILE B 95 6972 6251 7068 297 151 874 C ATOM 4192 N ALA B 96 -50.033 79.204-393.142 1.00 58.84 N ANISOU 4192 N ALA B 96 7675 7269 7413 819 -432 546 N ATOM 4193 CA ALA B 96 -49.371 79.978-394.181 1.00 59.69 C ANISOU 4193 CA ALA B 96 7766 7535 7377 982 -586 475 C ATOM 4194 C ALA B 96 -50.041 79.949-395.549 1.00 55.93 C ANISOU 4194 C ALA B 96 7323 7029 6897 1178 -782 372 C ATOM 4195 O ALA B 96 -49.376 80.135-396.566 1.00 58.08 O ANISOU 4195 O ALA B 96 7642 7336 7088 1290 -948 280 O ATOM 4196 CB ALA B 96 -47.915 79.554-394.300 1.00 61.19 C ANISOU 4196 CB ALA B 96 8021 7702 7527 884 -614 423 C ATOM 4197 N GLY B 97 -51.347 79.740-395.588 1.00 53.70 N ANISOU 4197 N GLY B 97 7018 6683 6702 1238 -779 370 N ATOM 4198 CA GLY B 97 -52.073 79.909-396.837 1.00 54.90 C ANISOU 4198 CA GLY B 97 7168 6834 6858 1457 -989 244 C ATOM 4199 C GLY B 97 -53.228 80.888-396.700 1.00 54.61 C ANISOU 4199 C GLY B 97 7023 6993 6735 1699 -985 256 C ATOM 4200 O GLY B 97 -53.633 81.554-397.655 1.00 57.14 O ANISOU 4200 O GLY B 97 7306 7435 6969 1977 -1175 143 O ATOM 4201 N ASN B 98 -53.755 80.959-395.487 1.00 56.66 N ANISOU 4201 N ASN B 98 8891 5857 6782 -352 554 577 N ATOM 4202 CA ASN B 98 -54.901 81.781-395.186 1.00 55.19 C ANISOU 4202 CA ASN B 98 8581 5843 6547 -303 568 641 C ATOM 4203 C ASN B 98 -54.728 83.201-395.659 1.00 57.15 C ANISOU 4203 C ASN B 98 8689 6149 6875 -442 516 646 C ATOM 4204 O ASN B 98 -53.759 83.520-396.338 1.00 57.67 O ANISOU 4204 O ASN B 98 8737 6143 7033 -579 484 602 O ATOM 4205 CB ASN B 98 -55.156 81.757-393.691 1.00 58.67 C ANISOU 4205 CB ASN B 98 9232 6153 6908 -171 528 750 C ATOM 4206 CG ASN B 98 -55.757 80.465-393.249 1.00 60.15 C ANISOU 4206 CG ASN B 98 9520 6357 6977 18 622 778 C ATOM 4207 OD1 ASN B 98 -56.727 80.002-393.842 1.00 57.09 O ANISOU 4207 OD1 ASN B 98 8949 6194 6549 77 728 774 O ATOM 4208 ND2 ASN B 98 -55.189 79.859-392.216 1.00 58.13 N ANISOU 4208 ND2 ASN B 98 9571 5855 6659 122 579 827 N ATOM 4209 N ILE B 99 -55.676 84.049-395.279 1.00 55.29 N ANISOU 4209 N ILE B 99 8357 6045 6605 -393 518 712 N ATOM 4210 CA ILE B 99 -55.720 85.434-395.725 1.00 56.11 C ANISOU 4210 CA ILE B 99 8315 6238 6768 -477 488 739 C ATOM 4211 C ILE B 99 -56.058 86.361-394.565 1.00 54.49 C ANISOU 4211 C ILE B 99 8144 5999 6561 -418 420 872 C ATOM 4212 O ILE B 99 -57.064 86.170-393.891 1.00 55.22 O ANISOU 4212 O ILE B 99 8226 6181 6574 -304 451 902 O ATOM 4213 CB ILE B 99 -56.778 85.611-396.817 1.00 54.88 C ANISOU 4213 CB ILE B 99 7939 6346 6568 -476 569 670 C ATOM 4214 CG1 ILE B 99 -57.096 87.095-397.013 1.00 53.70 C ANISOU 4214 CG1 ILE B 99 7667 6293 6442 -499 550 725 C ATOM 4215 CG2 ILE B 99 -58.032 84.829-396.460 1.00 54.54 C ANISOU 4215 CG2 ILE B 99 7857 6438 6426 -353 635 683 C ATOM 4216 CD1 ILE B 99 -57.948 87.404-398.237 1.00 53.77 C ANISOU 4216 CD1 ILE B 99 7505 6521 6404 -515 605 653 C ATOM 4217 N GLU B 100 -55.209 87.354-394.326 1.00 80.54 N ANISOU 4217 N GLU B 100 11474 9172 9956 -496 325 969 N ATOM 4218 CA GLU B 100 -55.479 88.361-393.312 1.00 81.00 C ANISOU 4218 CA GLU B 100 11530 9211 10035 -448 238 1120 C ATOM 4219 C GLU B 100 -56.956 88.716-393.335 1.00 81.29 C ANISOU 4219 C GLU B 100 11387 9502 9997 -347 319 1100 C ATOM 4220 O GLU B 100 -57.555 88.812-394.402 1.00100.05 O ANISOU 4220 O GLU B 100 13601 12068 12346 -359 414 1011 O ATOM 4221 CB GLU B 100 -54.681 89.629-393.610 1.00 80.70 C ANISOU 4221 CB GLU B 100 11420 9123 10118 -542 170 1243 C ATOM 4222 CG GLU B 100 -53.181 89.449-393.724 1.00 80.33 C ANISOU 4222 CG GLU B 100 11518 8834 10169 -674 92 1290 C ATOM 4223 CD GLU B 100 -52.486 89.605-392.399 1.00 80.85 C ANISOU 4223 CD GLU B 100 11785 8644 10289 -689 -87 1465 C ATOM 4224 OE1 GLU B 100 -52.793 88.813-391.480 1.00 81.38 O ANISOU 4224 OE1 GLU B 100 12026 8621 10272 -607 -130 1438 O ATOM 4225 OE2 GLU B 100 -51.639 90.519-392.281 1.00 80.82 O ANISOU 4225 OE2 GLU B 100 11776 8525 10408 -778 -191 1649 O ATOM 4226 N TYR B 101 -57.545 88.910-392.165 1.00 60.38 N ANISOU 4226 N TYR B 101 8777 6850 7313 -254 272 1187 N ATOM 4227 CA TYR B 101 -58.907 89.422-392.097 1.00 60.76 C ANISOU 4227 CA TYR B 101 8641 7134 7311 -172 340 1190 C ATOM 4228 C TYR B 101 -59.258 89.818-390.680 1.00 60.76 C ANISOU 4228 C TYR B 101 8696 7089 7302 -89 253 1311 C ATOM 4229 O TYR B 101 -58.863 89.154-389.726 1.00 57.26 O ANISOU 4229 O TYR B 101 8470 6464 6821 -54 182 1349 O ATOM 4230 CB TYR B 101 -59.914 88.400-392.618 1.00 60.43 C ANISOU 4230 CB TYR B 101 8540 7256 7166 -124 476 1074 C ATOM 4231 CG TYR B 101 -60.334 87.355-391.606 1.00 56.68 C ANISOU 4231 CG TYR B 101 8210 6728 6599 -18 502 1096 C ATOM 4232 CD1 TYR B 101 -59.787 86.080-391.629 1.00 56.91 C ANISOU 4232 CD1 TYR B 101 8414 6624 6584 2 528 1053 C ATOM 4233 CD2 TYR B 101 -61.283 87.639-390.636 1.00 57.17 C ANISOU 4233 CD2 TYR B 101 8237 6875 6610 77 510 1167 C ATOM 4234 CE1 TYR B 101 -60.169 85.120-390.715 1.00 56.97 C ANISOU 4234 CE1 TYR B 101 8579 6578 6488 132 568 1093 C ATOM 4235 CE2 TYR B 101 -61.666 86.686-389.716 1.00 58.94 C ANISOU 4235 CE2 TYR B 101 8614 7049 6732 191 550 1201 C ATOM 4236 CZ TYR B 101 -61.106 85.429-389.761 1.00 58.14 C ANISOU 4236 CZ TYR B 101 8706 6809 6576 228 582 1170 C ATOM 4237 OH TYR B 101 -61.484 84.475-388.849 1.00 58.07 O ANISOU 4237 OH TYR B 101 8873 6744 6447 374 637 1224 O ATOM 4238 N THR B 102 -60.012 90.897-390.544 1.00 61.87 N ANISOU 4238 N THR B 102 8649 7392 7468 -50 253 1374 N ATOM 4239 CA THR B 102 -60.348 91.414-389.228 1.00 65.30 C ANISOU 4239 CA THR B 102 9100 7802 7909 22 156 1498 C ATOM 4240 C THR B 102 -61.810 91.830-389.195 1.00 65.85 C ANISOU 4240 C THR B 102 8954 8134 7932 100 256 1473 C ATOM 4241 O THR B 102 -62.229 92.708-389.946 1.00 66.16 O ANISOU 4241 O THR B 102 8793 8334 8010 93 304 1466 O ATOM 4242 CB THR B 102 -59.470 92.626-388.881 1.00 62.58 C ANISOU 4242 CB THR B 102 8736 7344 7699 -20 -6 1675 C ATOM 4243 OG1 THR B 102 -58.246 92.559-389.625 1.00 57.58 O ANISOU 4243 OG1 THR B 102 8183 6561 7135 -128 -35 1680 O ATOM 4244 CG2 THR B 102 -59.168 92.660-387.386 1.00 64.51 C ANISOU 4244 CG2 THR B 102 9148 7409 7952 14 -186 1817 C ATOM 4245 N ILE B 103 -62.591 91.193-388.332 1.00 60.93 N ANISOU 4245 N ILE B 103 8386 7546 7218 180 291 1467 N ATOM 4246 CA ILE B 103 -64.005 91.516-388.213 1.00 59.57 C ANISOU 4246 CA ILE B 103 8011 7616 7005 243 390 1453 C ATOM 4247 C ILE B 103 -64.187 92.905-387.608 1.00 58.29 C ANISOU 4247 C ILE B 103 7699 7517 6932 273 291 1569 C ATOM 4248 O ILE B 103 -64.435 93.047-386.409 1.00 59.73 O ANISOU 4248 O ILE B 103 7917 7672 7106 333 214 1651 O ATOM 4249 CB ILE B 103 -64.745 90.455-387.382 1.00 59.35 C ANISOU 4249 CB ILE B 103 8088 7606 6857 327 466 1445 C ATOM 4250 CG1 ILE B 103 -64.652 89.093-388.075 1.00 57.76 C ANISOU 4250 CG1 ILE B 103 7997 7373 6576 319 579 1361 C ATOM 4251 CG2 ILE B 103 -66.200 90.842-387.179 1.00 60.00 C ANISOU 4251 CG2 ILE B 103 7951 7937 6911 376 565 1451 C ATOM 4252 CD1 ILE B 103 -65.405 88.002-387.363 1.00 57.95 C ANISOU 4252 CD1 ILE B 103 8119 7427 6474 427 684 1388 C ATOM 4253 N SER B 104 -64.058 93.923-388.452 1.00 56.17 N ANISOU 4253 N SER B 104 7265 7331 6745 244 292 1585 N ATOM 4254 CA SER B 104 -64.115 95.317-388.020 1.00 56.68 C ANISOU 4254 CA SER B 104 7169 7455 6910 290 201 1724 C ATOM 4255 C SER B 104 -65.375 95.634-387.231 1.00 55.75 C ANISOU 4255 C SER B 104 6897 7517 6767 370 234 1738 C ATOM 4256 O SER B 104 -65.336 96.385-386.259 1.00 56.45 O ANISOU 4256 O SER B 104 6928 7595 6926 419 111 1874 O ATOM 4257 CB SER B 104 -64.001 96.254-389.223 1.00 56.84 C ANISOU 4257 CB SER B 104 7041 7572 6985 282 252 1728 C ATOM 4258 OG SER B 104 -62.664 96.303-389.700 1.00 56.06 O ANISOU 4258 OG SER B 104 7060 7293 6947 214 186 1783 O ATOM 4259 N THR B 105 -66.496 95.062-387.651 1.00 58.46 N ANISOU 4259 N THR B 105 7166 8028 7018 377 392 1614 N ATOM 4260 CA THR B 105 -67.745 95.252-386.934 1.00 57.84 C ANISOU 4260 CA THR B 105 6939 8125 6911 438 446 1622 C ATOM 4261 C THR B 105 -68.570 93.985-386.918 1.00 57.43 C ANISOU 4261 C THR B 105 6948 8136 6737 432 586 1535 C ATOM 4262 O THR B 105 -69.147 93.604-387.931 1.00 56.75 O ANISOU 4262 O THR B 105 6798 8158 6606 391 706 1450 O ATOM 4263 CB THR B 105 -68.573 96.364-387.550 1.00 56.30 C ANISOU 4263 CB THR B 105 6489 8141 6763 466 505 1617 C ATOM 4264 OG1 THR B 105 -67.838 97.593-387.481 1.00 56.74 O ANISOU 4264 OG1 THR B 105 6473 8150 6935 505 385 1743 O ATOM 4265 CG2 THR B 105 -69.881 96.515-386.795 1.00 58.08 C ANISOU 4265 CG2 THR B 105 6551 8550 6966 515 567 1621 C ATOM 4266 N PRO B 106 -68.625 93.323-385.757 1.00 66.94 N ANISOU 4266 N PRO B 106 8288 9265 7883 481 564 1578 N ATOM 4267 CA PRO B 106 -69.424 92.107-385.634 1.00 70.53 C ANISOU 4267 CA PRO B 106 8801 9782 8215 505 714 1541 C ATOM 4268 C PRO B 106 -70.850 92.481-385.948 1.00 74.32 C ANISOU 4268 C PRO B 106 9021 10524 8695 497 843 1521 C ATOM 4269 O PRO B 106 -71.348 93.471-385.415 1.00 77.76 O ANISOU 4269 O PRO B 106 9288 11069 9190 525 805 1559 O ATOM 4270 CB PRO B 106 -69.315 91.756-384.146 1.00 76.81 C ANISOU 4270 CB PRO B 106 9767 10467 8952 590 649 1619 C ATOM 4271 CG PRO B 106 -68.136 92.502-383.644 1.00 79.46 C ANISOU 4271 CG PRO B 106 10206 10612 9375 581 430 1687 C ATOM 4272 CD PRO B 106 -68.050 93.746-384.471 1.00 74.77 C ANISOU 4272 CD PRO B 106 9376 10121 8912 528 393 1689 C ATOM 4273 N GLY B 107 -71.505 91.723-386.812 1.00 87.87 N ANISOU 4273 N GLY B 107 10697 12336 10352 455 980 1478 N ATOM 4274 CA GLY B 107 -72.887 92.023-387.118 1.00 86.27 C ANISOU 4274 CA GLY B 107 10265 12364 10149 429 1090 1478 C ATOM 4275 C GLY B 107 -73.756 91.648-385.939 1.00 87.35 C ANISOU 4275 C GLY B 107 10371 12588 10231 492 1173 1552 C ATOM 4276 O GLY B 107 -73.295 91.583-384.801 1.00 89.26 O ANISOU 4276 O GLY B 107 10741 12723 10451 567 1108 1596 O ATOM 4277 N SER B 108 -75.026 91.408-386.216 1.00 61.22 N ANISOU 4277 N SER B 108 6901 9466 6895 457 1310 1579 N ATOM 4278 CA SER B 108 -75.914 90.805-385.243 1.00 62.03 C ANISOU 4278 CA SER B 108 6982 9659 6929 510 1432 1669 C ATOM 4279 C SER B 108 -76.818 89.882-386.041 1.00 66.11 C ANISOU 4279 C SER B 108 7433 10288 7397 450 1582 1730 C ATOM 4280 O SER B 108 -76.899 90.004-387.261 1.00 68.87 O ANISOU 4280 O SER B 108 7718 10668 7783 357 1561 1687 O ATOM 4281 CB SER B 108 -76.723 91.882-384.526 1.00 64.37 C ANISOU 4281 CB SER B 108 7060 10112 7284 520 1427 1677 C ATOM 4282 OG SER B 108 -77.775 92.351-385.355 1.00 68.76 O ANISOU 4282 OG SER B 108 7386 10853 7887 431 1497 1661 O ATOM 4283 N ASN B 109 -77.477 88.946-385.371 1.00 99.91 N ANISOU 4283 N ASN B 109 11744 14623 11594 507 1726 1853 N ATOM 4284 CA ASN B 109 -78.436 88.075-386.044 1.00104.70 C ANISOU 4284 CA ASN B 109 12261 15352 12170 450 1869 1971 C ATOM 4285 C ASN B 109 -77.899 87.325-387.265 1.00106.29 C ANISOU 4285 C ASN B 109 12552 15469 12366 399 1838 1969 C ATOM 4286 O ASN B 109 -78.677 86.894-388.116 1.00112.05 O ANISOU 4286 O ASN B 109 13165 16302 13105 311 1894 2059 O ATOM 4287 CB ASN B 109 -79.691 88.863-386.431 1.00104.73 C ANISOU 4287 CB ASN B 109 11988 15560 12243 335 1905 1981 C ATOM 4288 CG ASN B 109 -80.485 89.321-385.223 1.00110.52 C ANISOU 4288 CG ASN B 109 12597 16419 12976 379 1983 2024 C ATOM 4289 OD1 ASN B 109 -80.778 88.529-384.327 1.00114.55 O ANISOU 4289 OD1 ASN B 109 13177 16944 13403 467 2109 2146 O ATOM 4290 ND2 ASN B 109 -80.842 90.603-385.194 1.00110.07 N ANISOU 4290 ND2 ASN B 109 12357 16457 13007 332 1915 1933 N ATOM 4291 N TYR B 110 -76.580 87.178-387.357 1.00 59.62 N ANISOU 4291 N TYR B 110 6841 9365 6446 446 1735 1879 N ATOM 4292 CA TYR B 110 -75.988 86.297-388.360 1.00 60.84 C ANISOU 4292 CA TYR B 110 7097 9431 6588 420 1718 1884 C ATOM 4293 C TYR B 110 -76.037 84.872-387.827 1.00 60.15 C ANISOU 4293 C TYR B 110 7149 9305 6400 544 1852 2045 C ATOM 4294 O TYR B 110 -76.408 84.654-386.678 1.00 61.51 O ANISOU 4294 O TYR B 110 7373 9496 6503 655 1948 2132 O ATOM 4295 CB TYR B 110 -74.542 86.686-388.657 1.00 58.49 C ANISOU 4295 CB TYR B 110 6954 8945 6326 417 1567 1732 C ATOM 4296 CG TYR B 110 -74.394 87.936-389.498 1.00 59.49 C ANISOU 4296 CG TYR B 110 6961 9102 6542 309 1449 1604 C ATOM 4297 CD1 TYR B 110 -74.264 89.180-388.907 1.00 59.26 C ANISOU 4297 CD1 TYR B 110 6873 9078 6565 325 1375 1543 C ATOM 4298 CD2 TYR B 110 -74.373 87.868-390.885 1.00 62.16 C ANISOU 4298 CD2 TYR B 110 7255 9459 6904 206 1406 1562 C ATOM 4299 CE1 TYR B 110 -74.125 90.319-389.669 1.00 59.21 C ANISOU 4299 CE1 TYR B 110 6769 9098 6629 262 1285 1454 C ATOM 4300 CE2 TYR B 110 -74.234 89.007-391.655 1.00 57.85 C ANISOU 4300 CE2 TYR B 110 6637 8929 6414 135 1309 1454 C ATOM 4301 CZ TYR B 110 -74.111 90.226-391.041 1.00 57.30 C ANISOU 4301 CZ TYR B 110 6512 8867 6391 173 1261 1406 C ATOM 4302 OH TYR B 110 -73.971 91.365-391.802 1.00 58.89 O ANISOU 4302 OH TYR B 110 6651 9085 6638 136 1182 1326 O ATOM 4303 N ALA B 111 -75.660 83.901-388.649 1.00 65.90 N ANISOU 4303 N ALA B 111 7944 9980 7116 542 1862 2095 N ATOM 4304 CA ALA B 111 -75.639 82.504-388.213 1.00 66.15 C ANISOU 4304 CA ALA B 111 8115 9968 7050 692 1997 2270 C ATOM 4305 C ALA B 111 -74.362 81.858-388.741 1.00 64.48 C ANISOU 4305 C ALA B 111 8038 9619 6841 710 1942 2241 C ATOM 4306 O ALA B 111 -73.505 82.544-389.283 1.00 65.42 O ANISOU 4306 O ALA B 111 8070 9745 7041 573 1831 2145 O ATOM 4307 CB ALA B 111 -77.013 81.897-388.331 1.00 93.67 C ANISOU 4307 CB ALA B 111 11423 13649 10520 682 2153 2507 C ATOM 4308 N VAL B 112 -74.243 80.542-388.593 1.00 66.29 N ANISOU 4308 N VAL B 112 8489 9722 6977 888 2020 2327 N ATOM 4309 CA VAL B 112 -73.048 79.820-389.031 1.00 64.53 C ANISOU 4309 CA VAL B 112 8401 9361 6755 926 1976 2302 C ATOM 4310 C VAL B 112 -72.487 79.293-390.356 1.00 65.37 C ANISOU 4310 C VAL B 112 8297 9598 6944 797 1956 2373 C ATOM 4311 O VAL B 112 -71.292 79.033-390.463 1.00 70.71 O ANISOU 4311 O VAL B 112 8760 10458 7648 715 2003 2502 O ATOM 4312 CB VAL B 112 -72.761 78.553-388.190 1.00 69.63 C ANISOU 4312 CB VAL B 112 9290 9896 7269 1170 2113 2460 C ATOM 4313 CG1 VAL B 112 -71.622 77.763-388.775 1.00 67.18 C ANISOU 4313 CG1 VAL B 112 9130 9428 6966 1217 2061 2412 C ATOM 4314 CG2 VAL B 112 -72.436 78.936-386.754 1.00 65.18 C ANISOU 4314 CG2 VAL B 112 8961 9198 6607 1294 2111 2406 C ATOM 4315 N GLY B 113 -73.341 79.111-391.357 1.00 88.16 N ANISOU 4315 N GLY B 113 11242 12384 9870 767 1869 2294 N ATOM 4316 CA GLY B 113 -72.893 78.632-392.657 1.00 86.81 C ANISOU 4316 CA GLY B 113 10890 12320 9772 646 1817 2364 C ATOM 4317 C GLY B 113 -73.448 79.706-393.587 1.00 88.91 C ANISOU 4317 C GLY B 113 10982 12676 10125 423 1677 2234 C ATOM 4318 O GLY B 113 -73.886 79.394-394.697 1.00 90.39 O ANISOU 4318 O GLY B 113 11075 12902 10367 311 1583 2242 O ATOM 4319 N ASP B 114 -73.461 80.962-393.148 1.00 65.81 N ANISOU 4319 N ASP B 114 8018 9783 7204 370 1657 2128 N ATOM 4320 CA ASP B 114 -73.867 82.045-394.036 1.00 63.00 C ANISOU 4320 CA ASP B 114 7538 9487 6912 193 1528 1993 C ATOM 4321 C ASP B 114 -72.629 82.245-394.881 1.00 60.76 C ANISOU 4321 C ASP B 114 7346 9071 6668 132 1397 1807 C ATOM 4322 O ASP B 114 -71.533 82.355-394.349 1.00 60.23 O ANISOU 4322 O ASP B 114 7437 8852 6595 199 1382 1692 O ATOM 4323 CB ASP B 114 -74.176 83.312-393.247 1.00 62.10 C ANISOU 4323 CB ASP B 114 7394 9402 6801 186 1529 1895 C ATOM 4324 CG ASP B 114 -75.511 83.238-392.544 1.00 70.46 C ANISOU 4324 CG ASP B 114 8325 10614 7832 213 1654 2068 C ATOM 4325 OD1 ASP B 114 -76.346 82.403-392.956 1.00 69.77 O ANISOU 4325 OD1 ASP B 114 8137 10632 7739 190 1716 2269 O ATOM 4326 OD2 ASP B 114 -75.730 84.009-391.584 1.00 73.98 O ANISOU 4326 OD2 ASP B 114 8762 11080 8268 254 1687 2019 O ATOM 4327 N LYS B 115 -72.804 82.274-396.196 1.00 63.38 N ANISOU 4327 N LYS B 115 7590 9454 7037 0 1294 1791 N ATOM 4328 CA LYS B 115 -71.670 82.277-397.111 1.00 62.20 C ANISOU 4328 CA LYS B 115 7520 9194 6920 -59 1181 1639 C ATOM 4329 C LYS B 115 -71.084 83.667-397.325 1.00 61.09 C ANISOU 4329 C LYS B 115 7421 8990 6801 -125 1093 1431 C ATOM 4330 O LYS B 115 -71.783 84.669-397.247 1.00 60.53 O ANISOU 4330 O LYS B 115 7276 8995 6726 -162 1080 1410 O ATOM 4331 CB LYS B 115 -72.044 81.618-398.444 1.00 68.59 C ANISOU 4331 CB LYS B 115 8235 10074 7751 -162 1093 1726 C ATOM 4332 CG LYS B 115 -72.505 80.176-398.285 1.00 65.16 C ANISOU 4332 CG LYS B 115 7746 9699 7311 -79 1178 1976 C ATOM 4333 CD LYS B 115 -72.155 79.321-399.488 1.00 65.45 C ANISOU 4333 CD LYS B 115 7746 9734 7389 -141 1073 2024 C ATOM 4334 CE LYS B 115 -72.352 77.849-399.159 1.00 70.52 C ANISOU 4334 CE LYS B 115 8351 10413 8030 -5 1179 2284 C ATOM 4335 NZ LYS B 115 -71.942 76.948-400.274 1.00 69.77 N ANISOU 4335 NZ LYS B 115 8201 10319 7988 -46 1072 2348 N ATOM 4336 N ILE B 116 -69.783 83.702-397.588 1.00 70.10 N ANISOU 4336 N ILE B 116 8678 9989 7966 -129 1039 1296 N ATOM 4337 CA ILE B 116 -69.059 84.947-397.776 1.00 66.42 C ANISOU 4337 CA ILE B 116 8261 9448 7526 -174 968 1137 C ATOM 4338 C ILE B 116 -68.488 84.982-399.184 1.00 63.43 C ANISOU 4338 C ILE B 116 7897 9041 7164 -280 867 1038 C ATOM 4339 O ILE B 116 -68.159 83.943-399.758 1.00 66.44 O ANISOU 4339 O ILE B 116 8289 9402 7554 -302 848 1059 O ATOM 4340 CB ILE B 116 -67.917 85.077-396.756 1.00 68.19 C ANISOU 4340 CB ILE B 116 8627 9509 7772 -96 986 1084 C ATOM 4341 CG1 ILE B 116 -68.452 84.904-395.335 1.00 73.72 C ANISOU 4341 CG1 ILE B 116 9348 10224 8439 20 1074 1187 C ATOM 4342 CG2 ILE B 116 -67.221 86.416-396.898 1.00 67.99 C ANISOU 4342 CG2 ILE B 116 8629 9418 7787 -136 916 976 C ATOM 4343 CD1 ILE B 116 -67.376 84.946-394.268 1.00 72.46 C ANISOU 4343 CD1 ILE B 116 9365 9880 8287 98 1060 1160 C ATOM 4344 N THR B 117 -68.373 86.180-399.741 1.00 58.27 N ANISOU 4344 N THR B 117 7245 8387 6509 -332 805 941 N ATOM 4345 CA THR B 117 -67.931 86.332-401.117 1.00 59.27 C ANISOU 4345 CA THR B 117 7402 8491 6627 -426 710 849 C ATOM 4346 C THR B 117 -66.845 87.383-401.239 1.00 58.08 C ANISOU 4346 C THR B 117 7335 8235 6498 -424 690 735 C ATOM 4347 O THR B 117 -67.019 88.520-400.808 1.00 58.43 O ANISOU 4347 O THR B 117 7369 8292 6540 -378 707 735 O ATOM 4348 CB THR B 117 -69.102 86.718-402.026 1.00 61.53 C ANISOU 4348 CB THR B 117 7626 8894 6857 -494 638 881 C ATOM 4349 OG1 THR B 117 -70.073 85.664-402.027 1.00 65.65 O ANISOU 4349 OG1 THR B 117 8059 9511 7375 -516 641 1028 O ATOM 4350 CG2 THR B 117 -68.621 86.961-403.446 1.00 58.36 C ANISOU 4350 CG2 THR B 117 7295 8453 6425 -579 525 781 C ATOM 4351 N VAL B 118 -65.722 86.994-401.832 1.00 59.98 N ANISOU 4351 N VAL B 118 7647 8376 6766 -472 658 658 N ATOM 4352 CA VAL B 118 -64.602 87.900-402.019 1.00 56.69 C ANISOU 4352 CA VAL B 118 7308 7853 6378 -482 648 580 C ATOM 4353 C VAL B 118 -64.583 88.366-403.459 1.00 59.76 C ANISOU 4353 C VAL B 118 7724 8270 6713 -550 579 506 C ATOM 4354 O VAL B 118 -64.479 87.562-404.379 1.00 57.66 O ANISOU 4354 O VAL B 118 7463 8013 6432 -625 522 465 O ATOM 4355 CB VAL B 118 -63.256 87.222-401.716 1.00 59.24 C ANISOU 4355 CB VAL B 118 7709 8029 6772 -500 661 545 C ATOM 4356 CG1 VAL B 118 -62.145 88.254-401.705 1.00 55.74 C ANISOU 4356 CG1 VAL B 118 7332 7473 6373 -511 657 516 C ATOM 4357 CG2 VAL B 118 -63.307 86.481-400.388 1.00 56.96 C ANISOU 4357 CG2 VAL B 118 7441 7693 6507 -423 713 620 C ATOM 4358 N LYS B 119 -64.681 89.670-403.653 1.00 58.84 N ANISOU 4358 N LYS B 119 7632 8164 6560 -510 581 500 N ATOM 4359 CA LYS B 119 -64.743 90.225-404.992 1.00 70.55 C ANISOU 4359 CA LYS B 119 9182 9663 7959 -544 520 439 C ATOM 4360 C LYS B 119 -63.461 90.974-405.333 1.00 72.32 C ANISOU 4360 C LYS B 119 9491 9784 8204 -534 549 400 C ATOM 4361 O LYS B 119 -62.803 91.544-404.459 1.00 72.88 O ANISOU 4361 O LYS B 119 9553 9791 8348 -478 609 457 O ATOM 4362 CB LYS B 119 -65.960 91.153-405.131 1.00 80.60 C ANISOU 4362 CB LYS B 119 10447 11029 9147 -485 504 477 C ATOM 4363 CG LYS B 119 -67.291 90.496-404.754 1.00 78.01 C ANISOU 4363 CG LYS B 119 10024 10807 8808 -507 484 544 C ATOM 4364 CD LYS B 119 -68.447 91.499-404.695 1.00 80.98 C ANISOU 4364 CD LYS B 119 10384 11265 9118 -447 480 586 C ATOM 4365 CE LYS B 119 -69.132 91.670-406.049 1.00 90.01 C ANISOU 4365 CE LYS B 119 11628 12427 10143 -502 361 558 C ATOM 4366 NZ LYS B 119 -70.406 92.447-405.955 1.00 88.13 N ANISOU 4366 NZ LYS B 119 11378 12264 9843 -458 347 609 N ATOM 4367 N TYR B 120 -63.102 90.954-406.611 1.00 75.72 N ANISOU 4367 N TYR B 120 10004 10196 8571 -592 497 324 N ATOM 4368 CA TYR B 120 -62.008 91.773-407.105 1.00 79.46 C ANISOU 4368 CA TYR B 120 10564 10586 9040 -575 536 306 C ATOM 4369 C TYR B 120 -62.582 92.882-407.971 1.00 86.87 C ANISOU 4369 C TYR B 120 11604 11565 9839 -496 518 310 C ATOM 4370 O TYR B 120 -62.930 92.661-409.130 1.00 87.78 O ANISOU 4370 O TYR B 120 11809 11698 9845 -544 432 239 O ATOM 4371 CB TYR B 120 -61.019 90.925-407.900 1.00 77.68 C ANISOU 4371 CB TYR B 120 10375 10298 8842 -692 505 214 C ATOM 4372 CG TYR B 120 -59.807 91.682-408.397 1.00 75.81 C ANISOU 4372 CG TYR B 120 10220 9974 8611 -689 562 211 C ATOM 4373 CD1 TYR B 120 -59.347 92.811-407.733 1.00 74.74 C ANISOU 4373 CD1 TYR B 120 10090 9791 8516 -594 648 327 C ATOM 4374 CD2 TYR B 120 -59.107 91.249-409.517 1.00 72.84 C ANISOU 4374 CD2 TYR B 120 9904 9565 8208 -783 528 115 C ATOM 4375 CE1 TYR B 120 -58.235 93.497-408.183 1.00 74.67 C ANISOU 4375 CE1 TYR B 120 10147 9705 8519 -588 710 369 C ATOM 4376 CE2 TYR B 120 -57.996 91.930-409.970 1.00 70.33 C ANISOU 4376 CE2 TYR B 120 9657 9171 7895 -784 597 129 C ATOM 4377 CZ TYR B 120 -57.564 93.050-409.301 1.00 70.81 C ANISOU 4377 CZ TYR B 120 9724 9185 7995 -685 694 267 C ATOM 4378 OH TYR B 120 -56.455 93.724-409.755 1.00 70.36 O ANISOU 4378 OH TYR B 120 9730 9055 7949 -682 772 323 O ATOM 4379 N VAL B 121 -62.690 94.073-407.395 1.00 79.91 N ANISOU 4379 N VAL B 121 10717 10690 8957 -366 590 405 N ATOM 4380 CA VAL B 121 -63.314 95.193-408.082 1.00 80.89 C ANISOU 4380 CA VAL B 121 10947 10847 8939 -249 588 427 C ATOM 4381 C VAL B 121 -64.705 94.807-408.572 1.00 84.17 C ANISOU 4381 C VAL B 121 11391 11341 9249 -284 482 376 C ATOM 4382 O VAL B 121 -64.916 94.591-409.767 1.00 82.62 O ANISOU 4382 O VAL B 121 11328 11130 8933 -335 387 305 O ATOM 4383 CB VAL B 121 -62.474 95.658-409.279 1.00 76.04 C ANISOU 4383 CB VAL B 121 10495 10165 8232 -233 601 395 C ATOM 4384 CG1 VAL B 121 -62.959 97.009-409.764 1.00 78.34 C ANISOU 4384 CG1 VAL B 121 10917 10471 8378 -55 635 459 C ATOM 4385 CG2 VAL B 121 -61.011 95.731-408.895 1.00 77.85 C ANISOU 4385 CG2 VAL B 121 10684 10309 8587 -256 690 450 C ATOM 4386 N SER B 122 -65.646 94.712-407.637 1.00 95.00 N ANISOU 4386 N SER B 122 12640 12788 10668 -265 489 427 N ATOM 4387 CA SER B 122 -67.036 94.384-407.950 1.00 96.80 C ANISOU 4387 CA SER B 122 12872 13091 10818 -306 394 420 C ATOM 4388 C SER B 122 -67.149 93.197-408.906 1.00100.06 C ANISOU 4388 C SER B 122 13331 13493 11193 -460 263 357 C ATOM 4389 O SER B 122 -68.032 93.160-409.766 1.00101.79 O ANISOU 4389 O SER B 122 13648 13728 11298 -500 139 350 O ATOM 4390 CB SER B 122 -67.760 95.604-408.527 1.00 92.93 C ANISOU 4390 CB SER B 122 12515 12611 10183 -185 377 437 C ATOM 4391 OG SER B 122 -67.748 96.685-407.611 1.00 85.02 O ANISOU 4391 OG SER B 122 11438 11637 9228 -31 492 519 O ATOM 4392 N ASP B 123 -66.253 92.228-408.747 1.00 91.77 N ANISOU 4392 N ASP B 123 12215 12410 10243 -544 278 326 N ATOM 4393 CA ASP B 123 -66.249 91.041-409.592 1.00 91.38 C ANISOU 4393 CA ASP B 123 12176 12361 10185 -680 156 284 C ATOM 4394 C ASP B 123 -65.958 89.807-408.747 1.00 83.10 C ANISOU 4394 C ASP B 123 10969 11329 9276 -736 198 315 C ATOM 4395 O ASP B 123 -64.957 89.760-408.036 1.00 81.41 O ANISOU 4395 O ASP B 123 10718 11059 9155 -708 300 300 O ATOM 4396 CB ASP B 123 -65.210 91.184-410.706 1.00 92.78 C ANISOU 4396 CB ASP B 123 12489 12458 10306 -711 121 190 C ATOM 4397 CG ASP B 123 -65.628 90.492-411.988 1.00 99.80 C ANISOU 4397 CG ASP B 123 13459 13352 11107 -824 -65 154 C ATOM 4398 OD1 ASP B 123 -66.269 89.420-411.904 1.00100.68 O ANISOU 4398 OD1 ASP B 123 13462 13522 11271 -913 -154 210 O ATOM 4399 OD2 ASP B 123 -65.318 91.022-413.080 1.00 97.33 O ANISOU 4399 OD2 ASP B 123 13326 12985 10670 -818 -128 89 O ATOM 4400 N ASP B 124 -66.830 88.809-408.833 1.00 87.73 N ANISOU 4400 N ASP B 124 11478 11984 9873 -807 115 381 N ATOM 4401 CA ASP B 124 -66.736 87.633-407.971 1.00 88.23 C ANISOU 4401 CA ASP B 124 11402 12072 10048 -821 171 446 C ATOM 4402 C ASP B 124 -65.539 86.730-408.271 1.00 87.01 C ANISOU 4402 C ASP B 124 11240 11855 9964 -873 169 382 C ATOM 4403 O ASP B 124 -65.347 86.299-409.407 1.00 92.96 O ANISOU 4403 O ASP B 124 12029 12604 10688 -958 52 339 O ATOM 4404 CB ASP B 124 -68.025 86.814-408.054 1.00 97.26 C ANISOU 4404 CB ASP B 124 12456 13314 11184 -872 88 581 C ATOM 4405 CG ASP B 124 -69.218 87.548-407.480 1.00102.32 C ANISOU 4405 CG ASP B 124 13071 14022 11785 -825 118 659 C ATOM 4406 OD1 ASP B 124 -69.123 88.778-407.292 1.00104.50 O ANISOU 4406 OD1 ASP B 124 13415 14272 12017 -752 171 596 O ATOM 4407 OD2 ASP B 124 -70.248 86.890-407.216 1.00102.69 O ANISOU 4407 OD2 ASP B 124 13018 14151 11849 -857 95 800 O ATOM 4408 N ILE B 125 -64.746 86.435-407.241 1.00 61.44 N ANISOU 4408 N ILE B 125 7965 8561 6819 -823 288 378 N ATOM 4409 CA ILE B 125 -63.615 85.518-407.367 1.00 58.31 C ANISOU 4409 CA ILE B 125 7561 8095 6500 -864 299 324 C ATOM 4410 C ILE B 125 -63.873 84.255-406.553 1.00 60.90 C ANISOU 4410 C ILE B 125 7798 8449 6893 -825 342 424 C ATOM 4411 O ILE B 125 -63.826 83.137-407.072 1.00 57.91 O ANISOU 4411 O ILE B 125 7360 8098 6544 -865 286 454 O ATOM 4412 CB ILE B 125 -62.311 86.147-406.851 1.00 55.78 C ANISOU 4412 CB ILE B 125 7310 7650 6234 -839 391 252 C ATOM 4413 CG1 ILE B 125 -62.114 87.544-407.434 1.00 61.62 C ANISOU 4413 CG1 ILE B 125 8138 8370 6906 -831 388 204 C ATOM 4414 CG2 ILE B 125 -61.131 85.259-407.189 1.00 56.94 C ANISOU 4414 CG2 ILE B 125 7460 7718 6455 -904 388 181 C ATOM 4415 CD1 ILE B 125 -61.645 87.544-408.870 1.00 59.96 C ANISOU 4415 CD1 ILE B 125 7994 8147 6642 -915 307 110 C ATOM 4416 N GLU B 126 -64.142 84.448-405.267 1.00 65.44 N ANISOU 4416 N GLU B 126 8365 9015 7485 -732 444 491 N ATOM 4417 CA GLU B 126 -64.391 83.341-404.356 1.00 65.28 C ANISOU 4417 CA GLU B 126 8294 9007 7502 -659 511 601 C ATOM 4418 C GLU B 126 -65.763 83.505-403.722 1.00 65.73 C ANISOU 4418 C GLU B 126 8285 9173 7517 -603 545 733 C ATOM 4419 O GLU B 126 -66.151 84.607-403.340 1.00 62.80 O ANISOU 4419 O GLU B 126 7928 8817 7115 -582 566 717 O ATOM 4420 CB GLU B 126 -63.307 83.290-403.279 1.00 66.49 C ANISOU 4420 CB GLU B 126 8536 9018 7708 -592 601 564 C ATOM 4421 CG GLU B 126 -63.498 82.203-402.234 1.00 67.40 C ANISOU 4421 CG GLU B 126 8656 9118 7835 -481 682 676 C ATOM 4422 CD GLU B 126 -63.441 80.805-402.819 1.00 69.53 C ANISOU 4422 CD GLU B 126 8868 9422 8128 -479 663 731 C ATOM 4423 OE1 GLU B 126 -62.390 80.140-402.673 1.00 67.20 O ANISOU 4423 OE1 GLU B 126 8641 9012 7879 -455 686 682 O ATOM 4424 OE2 GLU B 126 -64.444 80.374-403.427 1.00 69.82 O ANISOU 4424 OE2 GLU B 126 8789 9596 8144 -502 616 838 O ATOM 4425 N THR B 127 -66.499 82.407-403.614 1.00 60.63 N ANISOU 4425 N THR B 127 7554 8609 6875 -576 555 882 N ATOM 4426 CA THR B 127 -67.867 82.463-403.120 1.00 62.54 C ANISOU 4426 CA THR B 127 7714 8966 7082 -543 588 1034 C ATOM 4427 C THR B 127 -68.170 81.309-402.178 1.00 63.03 C ANISOU 4427 C THR B 127 7736 9054 7160 -428 699 1203 C ATOM 4428 O THR B 127 -69.328 80.944-401.981 1.00 63.12 O ANISOU 4428 O THR B 127 7651 9180 7153 -411 725 1384 O ATOM 4429 CB THR B 127 -68.877 82.408-404.279 1.00 66.53 C ANISOU 4429 CB THR B 127 8141 9578 7558 -652 453 1116 C ATOM 4430 OG1 THR B 127 -68.883 81.092-404.849 1.00 67.40 O ANISOU 4430 OG1 THR B 127 8179 9724 7706 -673 397 1238 O ATOM 4431 CG2 THR B 127 -68.513 83.424-405.352 1.00 68.27 C ANISOU 4431 CG2 THR B 127 8445 9758 7738 -746 336 952 C ATOM 4432 N GLU B 128 -67.126 80.731-401.600 1.00 90.22 N ANISOU 4432 N GLU B 128 11267 12384 10630 -345 767 1159 N ATOM 4433 CA GLU B 128 -67.306 79.577-400.732 1.00 96.03 C ANISOU 4433 CA GLU B 128 12007 13121 11358 -202 881 1323 C ATOM 4434 C GLU B 128 -66.889 79.860-399.300 1.00 94.17 C ANISOU 4434 C GLU B 128 11910 12775 11094 -80 989 1292 C ATOM 4435 O GLU B 128 -66.874 78.966-398.455 1.00 96.30 O ANISOU 4435 O GLU B 128 12246 13009 11335 66 1091 1408 O ATOM 4436 CB GLU B 128 -66.573 78.360-401.296 1.00100.25 C ANISOU 4436 CB GLU B 128 12539 13615 11935 -178 861 1349 C ATOM 4437 CG GLU B 128 -67.257 77.804-402.523 1.00103.77 C ANISOU 4437 CG GLU B 128 12825 14193 12408 -269 750 1470 C ATOM 4438 CD GLU B 128 -68.767 77.849-402.388 1.00108.66 C ANISOU 4438 CD GLU B 128 13328 14960 12996 -275 761 1681 C ATOM 4439 OE1 GLU B 128 -69.298 77.225-401.444 1.00108.03 O ANISOU 4439 OE1 GLU B 128 13234 14918 12894 -137 896 1868 O ATOM 4440 OE2 GLU B 128 -69.423 78.515-403.219 1.00109.98 O ANISOU 4440 OE2 GLU B 128 13433 15197 13156 -416 636 1667 O ATOM 4441 N GLY B 129 -66.557 81.116-399.032 1.00 59.30 N ANISOU 4441 N GLY B 129 7549 8301 6680 -130 957 1153 N ATOM 4442 CA GLY B 129 -66.282 81.542-397.675 1.00 59.87 C ANISOU 4442 CA GLY B 129 7741 8277 6731 -32 1021 1144 C ATOM 4443 C GLY B 129 -67.551 81.369-396.875 1.00 64.54 C ANISOU 4443 C GLY B 129 8266 8989 7267 55 1115 1306 C ATOM 4444 O GLY B 129 -68.624 81.190-397.444 1.00 65.19 O ANISOU 4444 O GLY B 129 8199 9228 7343 10 1117 1411 O ATOM 4445 N LYS B 130 -67.437 81.413-395.555 1.00 63.33 N ANISOU 4445 N LYS B 130 8231 8756 7074 174 1183 1339 N ATOM 4446 CA LYS B 130 -68.607 81.223-394.714 1.00 60.07 C ANISOU 4446 CA LYS B 130 7764 8456 6602 267 1289 1496 C ATOM 4447 C LYS B 130 -68.323 81.502-393.248 1.00 60.62 C ANISOU 4447 C LYS B 130 7996 8413 6622 386 1330 1497 C ATOM 4448 O LYS B 130 -67.359 80.986-392.689 1.00 63.06 O ANISOU 4448 O LYS B 130 8511 8544 6906 475 1328 1475 O ATOM 4449 CB LYS B 130 -69.152 79.803-394.879 1.00 62.41 C ANISOU 4449 CB LYS B 130 8021 8828 6864 357 1385 1691 C ATOM 4450 CG LYS B 130 -68.075 78.747-395.032 1.00 62.59 C ANISOU 4450 CG LYS B 130 8184 8711 6887 437 1390 1680 C ATOM 4451 CD LYS B 130 -68.670 77.349-395.103 1.00 76.65 C ANISOU 4451 CD LYS B 130 9914 10577 8633 565 1499 1919 C ATOM 4452 CE LYS B 130 -69.183 76.898-393.743 1.00 83.31 C ANISOU 4452 CE LYS B 130 10872 11411 9372 766 1656 2084 C ATOM 4453 NZ LYS B 130 -69.454 75.430-393.704 1.00 87.76 N ANISOU 4453 NZ LYS B 130 11444 12011 9890 946 1784 2333 N ATOM 4454 N ILE B 131 -69.167 82.330-392.637 1.00 59.95 N ANISOU 4454 N ILE B 131 7826 8426 6525 383 1352 1525 N ATOM 4455 CA ILE B 131 -69.129 82.549-391.201 1.00 60.42 C ANISOU 4455 CA ILE B 131 8019 8408 6529 500 1385 1557 C ATOM 4456 C ILE B 131 -69.092 81.193-390.524 1.00 60.64 C ANISOU 4456 C ILE B 131 8214 8367 6460 674 1500 1693 C ATOM 4457 O ILE B 131 -69.740 80.257-390.984 1.00 65.58 O ANISOU 4457 O ILE B 131 8753 9105 7061 713 1600 1829 O ATOM 4458 CB ILE B 131 -70.371 83.305-390.726 1.00 60.97 C ANISOU 4458 CB ILE B 131 7922 8651 6592 487 1433 1615 C ATOM 4459 CG1 ILE B 131 -70.393 84.717-391.318 1.00 60.65 C ANISOU 4459 CG1 ILE B 131 7738 8669 6639 350 1325 1490 C ATOM 4460 CG2 ILE B 131 -70.407 83.363-389.211 1.00 65.95 C ANISOU 4460 CG2 ILE B 131 8694 9212 7153 620 1471 1669 C ATOM 4461 CD1 ILE B 131 -71.673 85.483-391.028 1.00 64.34 C ANISOU 4461 CD1 ILE B 131 8014 9321 7110 325 1369 1539 C ATOM 4462 N THR B 132 -68.329 81.073-389.444 1.00 64.05 N ANISOU 4462 N THR B 132 8900 8605 6831 789 1478 1677 N ATOM 4463 CA THR B 132 -68.154 79.773-388.811 1.00 65.97 C ANISOU 4463 CA THR B 132 9360 8745 6959 985 1585 1800 C ATOM 4464 C THR B 132 -68.317 79.802-387.299 1.00 65.28 C ANISOU 4464 C THR B 132 9483 8568 6754 1141 1621 1870 C ATOM 4465 O THR B 132 -68.354 78.757-386.663 1.00 73.47 O ANISOU 4465 O THR B 132 10720 9532 7665 1338 1733 1999 O ATOM 4466 CB THR B 132 -66.792 79.146-389.160 1.00 66.55 C ANISOU 4466 CB THR B 132 9635 8605 7046 1005 1517 1720 C ATOM 4467 OG1 THR B 132 -65.750 80.098-388.921 1.00 65.19 O ANISOU 4467 OG1 THR B 132 9579 8257 6934 905 1349 1567 O ATOM 4468 CG2 THR B 132 -66.763 78.725-390.619 1.00 64.73 C ANISOU 4468 CG2 THR B 132 9210 8481 6902 899 1517 1698 C ATOM 4469 N GLU B 133 -68.412 80.989-386.720 1.00 62.97 N ANISOU 4469 N GLU B 133 9153 8278 6496 1069 1524 1800 N ATOM 4470 CA GLU B 133 -68.663 81.081-385.291 1.00 65.07 C ANISOU 4470 CA GLU B 133 9597 8475 6651 1205 1540 1870 C ATOM 4471 C GLU B 133 -69.333 82.386-384.925 1.00 71.83 C ANISOU 4471 C GLU B 133 10252 9468 7572 1106 1481 1834 C ATOM 4472 O GLU B 133 -68.769 83.463-385.121 1.00 67.38 O ANISOU 4472 O GLU B 133 9626 8858 7118 977 1320 1722 O ATOM 4473 CB GLU B 133 -67.370 80.925-384.492 1.00 71.78 C ANISOU 4473 CB GLU B 133 10821 9011 7441 1285 1404 1824 C ATOM 4474 CG GLU B 133 -67.586 80.937-382.982 1.00 80.40 C ANISOU 4474 CG GLU B 133 12154 10002 8394 1440 1395 1906 C ATOM 4475 CD GLU B 133 -66.288 81.031-382.191 1.00 84.20 C ANISOU 4475 CD GLU B 133 13012 10149 8833 1477 1194 1861 C ATOM 4476 OE1 GLU B 133 -65.343 80.256-382.480 1.00 80.09 O ANISOU 4476 OE1 GLU B 133 12714 9433 8284 1523 1171 1838 O ATOM 4477 OE2 GLU B 133 -66.224 81.879-381.270 1.00 82.72 O ANISOU 4477 OE2 GLU B 133 12896 9889 8643 1458 1048 1861 O ATOM 4478 N VAL B 134 -70.544 82.279-384.395 1.00 68.72 N ANISOU 4478 N VAL B 134 9748 9248 7113 1174 1621 1949 N ATOM 4479 CA VAL B 134 -71.259 83.431-383.875 1.00 64.44 C ANISOU 4479 CA VAL B 134 9023 8840 6620 1108 1582 1929 C ATOM 4480 C VAL B 134 -71.534 83.192-382.399 1.00 67.19 C ANISOU 4480 C VAL B 134 9574 9125 6830 1274 1623 2024 C ATOM 4481 O VAL B 134 -71.321 82.087-381.895 1.00 67.45 O ANISOU 4481 O VAL B 134 9877 9034 6718 1447 1711 2119 O ATOM 4482 CB VAL B 134 -72.585 83.639-384.610 1.00 61.38 C ANISOU 4482 CB VAL B 134 8289 8740 6293 1012 1709 1978 C ATOM 4483 CG1 VAL B 134 -72.335 84.177-386.006 1.00 60.69 C ANISOU 4483 CG1 VAL B 134 8016 8706 6338 838 1624 1865 C ATOM 4484 CG2 VAL B 134 -73.360 82.333-384.675 1.00 65.20 C ANISOU 4484 CG2 VAL B 134 8778 9317 6677 1122 1920 2162 C ATOM 4485 N ASP B 135 -71.993 84.222-381.701 1.00 73.58 N ANISOU 4485 N ASP B 135 10266 10015 7676 1235 1556 2004 N ATOM 4486 CA ASP B 135 -72.387 84.059-380.309 1.00 72.31 C ANISOU 4486 CA ASP B 135 10272 9822 7381 1382 1593 2095 C ATOM 4487 C ASP B 135 -73.900 83.926-380.201 1.00 72.83 C ANISOU 4487 C ASP B 135 10090 10164 7419 1397 1809 2205 C ATOM 4488 O ASP B 135 -74.558 83.445-381.121 1.00 78.03 O ANISOU 4488 O ASP B 135 10554 10984 8109 1349 1961 2264 O ATOM 4489 CB ASP B 135 -71.887 85.223-379.451 1.00 77.09 C ANISOU 4489 CB ASP B 135 10926 10325 8041 1343 1360 2029 C ATOM 4490 CG ASP B 135 -72.388 86.569-379.933 1.00 76.45 C ANISOU 4490 CG ASP B 135 10461 10447 8138 1178 1297 1957 C ATOM 4491 OD1 ASP B 135 -73.088 86.610-380.964 1.00 73.99 O ANISOU 4491 OD1 ASP B 135 9878 10336 7899 1085 1422 1939 O ATOM 4492 OD2 ASP B 135 -72.074 87.586-379.280 1.00 73.42 O ANISOU 4492 OD2 ASP B 135 10060 10015 7820 1149 1112 1933 O ATOM 4493 N ALA B 136 -74.453 84.359-379.077 1.00 66.73 N ANISOU 4493 N ALA B 136 9318 9443 6592 1455 1812 2245 N ATOM 4494 CA ALA B 136 -75.882 84.226-378.855 1.00 69.91 C ANISOU 4494 CA ALA B 136 9496 10102 6965 1469 2026 2362 C ATOM 4495 C ALA B 136 -76.682 85.261-379.637 1.00 73.94 C ANISOU 4495 C ALA B 136 9582 10856 7655 1269 2021 2294 C ATOM 4496 O ALA B 136 -77.860 85.056-379.926 1.00 73.80 O ANISOU 4496 O ALA B 136 9333 11059 7649 1228 2203 2394 O ATOM 4497 CB ALA B 136 -76.192 84.325-377.376 1.00 63.49 C ANISOU 4497 CB ALA B 136 8836 9262 6027 1600 2032 2423 C ATOM 4498 N ASP B 137 -76.039 86.370-379.983 1.00 85.38 N ANISOU 4498 N ASP B 137 10943 12257 9241 1153 1812 2144 N ATOM 4499 CA ASP B 137 -76.732 87.479-380.634 1.00 83.23 C ANISOU 4499 CA ASP B 137 10306 12193 9125 995 1790 2074 C ATOM 4500 C ASP B 137 -76.507 87.490-382.139 1.00 82.26 C ANISOU 4500 C ASP B 137 10072 12090 9094 871 1774 2010 C ATOM 4501 O ASP B 137 -77.056 88.334-382.847 1.00 83.43 O ANISOU 4501 O ASP B 137 9957 12389 9354 748 1757 1954 O ATOM 4502 CB ASP B 137 -76.274 88.816-380.049 1.00 81.50 C ANISOU 4502 CB ASP B 137 10029 11935 9002 966 1579 1983 C ATOM 4503 CG ASP B 137 -76.261 88.819-378.531 1.00 86.02 C ANISOU 4503 CG ASP B 137 10765 12438 9480 1088 1532 2040 C ATOM 4504 OD1 ASP B 137 -76.956 87.975-377.922 1.00 84.49 O ANISOU 4504 OD1 ASP B 137 10652 12299 9152 1185 1708 2145 O ATOM 4505 OD2 ASP B 137 -75.554 89.671-377.947 1.00 90.56 O ANISOU 4505 OD2 ASP B 137 11393 12901 10114 1089 1312 2000 O ATOM 4506 N GLY B 138 -75.693 86.561-382.624 1.00 88.16 N ANISOU 4506 N GLY B 138 11033 12677 9787 911 1772 2017 N ATOM 4507 CA GLY B 138 -75.376 86.503-384.037 1.00 90.83 C ANISOU 4507 CA GLY B 138 11293 13016 10203 798 1739 1954 C ATOM 4508 C GLY B 138 -74.179 87.363-384.388 1.00 89.34 C ANISOU 4508 C GLY B 138 11164 12677 10104 739 1534 1811 C ATOM 4509 O GLY B 138 -73.838 87.517-385.560 1.00 90.89 O ANISOU 4509 O GLY B 138 11296 12870 10368 642 1488 1739 O ATOM 4510 N LYS B 139 -73.546 87.933-383.368 1.00 83.11 N ANISOU 4510 N LYS B 139 10500 11763 9316 797 1404 1789 N ATOM 4511 CA LYS B 139 -72.332 88.711-383.561 1.00 81.48 C ANISOU 4511 CA LYS B 139 10368 11393 9198 749 1203 1704 C ATOM 4512 C LYS B 139 -71.282 87.809-384.182 1.00 84.49 C ANISOU 4512 C LYS B 139 10972 11584 9546 751 1182 1675 C ATOM 4513 O LYS B 139 -70.991 86.738-383.646 1.00 89.40 O ANISOU 4513 O LYS B 139 11839 12076 10052 858 1230 1730 O ATOM 4514 CB LYS B 139 -71.835 89.256-382.221 1.00 86.57 C ANISOU 4514 CB LYS B 139 11148 11908 9836 819 1050 1739 C ATOM 4515 CG LYS B 139 -72.729 90.328-381.608 1.00 85.59 C ANISOU 4515 CG LYS B 139 10776 11970 9775 812 1034 1760 C ATOM 4516 CD LYS B 139 -72.417 90.548-380.134 1.00 87.35 C ANISOU 4516 CD LYS B 139 11163 12072 9955 902 898 1826 C ATOM 4517 CE LYS B 139 -70.954 90.913-379.921 1.00 91.07 C ANISOU 4517 CE LYS B 139 11846 12277 10478 889 652 1834 C ATOM 4518 NZ LYS B 139 -70.539 90.799-378.490 1.00 97.92 N ANISOU 4518 NZ LYS B 139 12978 12963 11266 981 497 1916 N ATOM 4519 N ILE B 140 -70.719 88.230-385.312 1.00 62.08 N ANISOU 4519 N ILE B 140 8058 8730 6801 645 1116 1591 N ATOM 4520 CA ILE B 140 -69.735 87.404-386.018 1.00 61.60 C ANISOU 4520 CA ILE B 140 8173 8507 6724 629 1099 1552 C ATOM 4521 C ILE B 140 -68.407 87.298-385.267 1.00 61.91 C ANISOU 4521 C ILE B 140 8504 8269 6750 675 950 1554 C ATOM 4522 O ILE B 140 -67.710 88.296-385.065 1.00 58.33 O ANISOU 4522 O ILE B 140 8049 7726 6387 624 789 1541 O ATOM 4523 CB ILE B 140 -69.470 87.916-387.445 1.00 60.42 C ANISOU 4523 CB ILE B 140 7874 8411 6671 500 1064 1462 C ATOM 4524 CG1 ILE B 140 -70.788 88.247-388.150 1.00 59.10 C ANISOU 4524 CG1 ILE B 140 7439 8496 6522 442 1164 1464 C ATOM 4525 CG2 ILE B 140 -68.692 86.881-388.234 1.00 58.55 C ANISOU 4525 CG2 ILE B 140 7780 8055 6411 482 1080 1426 C ATOM 4526 CD1 ILE B 140 -70.635 88.530-389.633 1.00 58.10 C ANISOU 4526 CD1 ILE B 140 7213 8413 6449 330 1137 1383 C ATOM 4527 N LYS B 141 -68.057 86.081-384.862 1.00 71.94 N ANISOU 4527 N LYS B 141 10031 9396 7907 777 1001 1593 N ATOM 4528 CA LYS B 141 -66.826 85.863-384.114 1.00 73.91 C ANISOU 4528 CA LYS B 141 10606 9353 8124 826 853 1604 C ATOM 4529 C LYS B 141 -65.715 85.247-384.968 1.00 71.09 C ANISOU 4529 C LYS B 141 10382 8834 7794 776 822 1540 C ATOM 4530 O LYS B 141 -64.542 85.547-384.765 1.00 67.58 O ANISOU 4530 O LYS B 141 10111 8166 7399 730 656 1525 O ATOM 4531 CB LYS B 141 -67.086 85.003-382.873 1.00 76.62 C ANISOU 4531 CB LYS B 141 11215 9599 8300 1003 906 1696 C ATOM 4532 CG LYS B 141 -68.009 85.642-381.840 1.00 78.79 C ANISOU 4532 CG LYS B 141 11400 9995 8543 1052 905 1760 C ATOM 4533 CD LYS B 141 -67.411 86.909-381.237 1.00 82.07 C ANISOU 4533 CD LYS B 141 11812 10310 9060 981 663 1760 C ATOM 4534 CE LYS B 141 -68.277 87.444-380.098 1.00 87.94 C ANISOU 4534 CE LYS B 141 12491 11158 9763 1046 648 1828 C ATOM 4535 NZ LYS B 141 -67.817 88.770-379.584 1.00 93.58 N ANISOU 4535 NZ LYS B 141 13132 11819 10604 974 406 1857 N ATOM 4536 N LYS B 142 -66.079 84.396-385.921 1.00 65.16 N ANISOU 4536 N LYS B 142 9541 8194 7021 777 972 1518 N ATOM 4537 CA LYS B 142 -65.074 83.740-386.758 1.00 63.13 C ANISOU 4537 CA LYS B 142 9390 7803 6793 735 952 1455 C ATOM 4538 C LYS B 142 -65.601 83.328-388.133 1.00 62.06 C ANISOU 4538 C LYS B 142 9023 7862 6696 667 1069 1420 C ATOM 4539 O LYS B 142 -66.730 82.864-388.260 1.00 60.72 O ANISOU 4539 O LYS B 142 8717 7880 6475 719 1208 1494 O ATOM 4540 CB LYS B 142 -64.501 82.522-386.028 1.00 64.12 C ANISOU 4540 CB LYS B 142 9861 7709 6791 892 975 1508 C ATOM 4541 CG LYS B 142 -63.523 81.691-386.843 1.00 64.03 C ANISOU 4541 CG LYS B 142 9958 7566 6803 869 974 1449 C ATOM 4542 CD LYS B 142 -63.289 80.335-386.190 1.00 67.82 C ANISOU 4542 CD LYS B 142 10750 7885 7133 1073 1054 1527 C ATOM 4543 CE LYS B 142 -62.989 80.482-384.701 1.00 73.07 C ANISOU 4543 CE LYS B 142 11742 8332 7689 1187 952 1586 C ATOM 4544 NZ LYS B 142 -62.911 79.170-383.989 1.00 70.50 N ANISOU 4544 NZ LYS B 142 11754 7852 7179 1428 1049 1679 N ATOM 4545 N ILE B 143 -64.769 83.495-389.156 1.00 67.55 N ANISOU 4545 N ILE B 143 9680 8504 7483 545 1000 1323 N ATOM 4546 CA ILE B 143 -65.116 83.086-390.512 1.00 68.18 C ANISOU 4546 CA ILE B 143 9572 8736 7597 472 1070 1286 C ATOM 4547 C ILE B 143 -64.000 82.245-391.116 1.00 58.81 C ANISOU 4547 C ILE B 143 8519 7395 6430 455 1046 1229 C ATOM 4548 O ILE B 143 -62.937 82.088-390.513 1.00 59.56 O ANISOU 4548 O ILE B 143 8851 7260 6520 486 972 1210 O ATOM 4549 CB ILE B 143 -65.339 84.291-391.421 1.00 67.13 C ANISOU 4549 CB ILE B 143 9213 8735 7559 322 1012 1209 C ATOM 4550 CG1 ILE B 143 -64.002 84.899-391.838 1.00 68.91 C ANISOU 4550 CG1 ILE B 143 9512 8798 7872 221 888 1117 C ATOM 4551 CG2 ILE B 143 -66.180 85.330-390.716 1.00 71.31 C ANISOU 4551 CG2 ILE B 143 9628 9375 8090 337 1006 1251 C ATOM 4552 CD1 ILE B 143 -64.134 86.199-392.603 1.00 66.49 C ANISOU 4552 CD1 ILE B 143 9023 8599 7643 112 837 1065 C ATOM 4553 N ASN B 144 -64.235 81.698-392.304 1.00 81.80 N ANISOU 4553 N ASN B 144 11285 10428 9369 401 1095 1209 N ATOM 4554 CA ASN B 144 -63.196 80.952-393.011 1.00 78.48 C ANISOU 4554 CA ASN B 144 10946 9887 8984 370 1069 1143 C ATOM 4555 C ASN B 144 -63.291 81.116-394.521 1.00 75.68 C ANISOU 4555 C ASN B 144 10381 9670 8703 225 1042 1068 C ATOM 4556 O ASN B 144 -64.195 80.581-395.157 1.00 78.60 O ANISOU 4556 O ASN B 144 10596 10213 9056 230 1099 1136 O ATOM 4557 CB ASN B 144 -63.218 79.471-392.632 1.00 83.47 C ANISOU 4557 CB ASN B 144 11716 10466 9533 542 1170 1244 C ATOM 4558 CG ASN B 144 -61.982 78.730-393.114 1.00 85.27 C ANISOU 4558 CG ASN B 144 12071 10528 9799 531 1134 1171 C ATOM 4559 OD1 ASN B 144 -61.834 78.444-394.304 1.00 81.95 O ANISOU 4559 OD1 ASN B 144 11499 10193 9446 438 1124 1119 O ATOM 4560 ND2 ASN B 144 -61.088 78.408-392.185 1.00 78.50 N ANISOU 4560 ND2 ASN B 144 11503 9426 8896 623 1104 1168 N ATOM 4561 N ILE B 145 -62.344 81.864-395.079 1.00 57.11 N ANISOU 4561 N ILE B 145 8036 7232 6430 95 947 947 N ATOM 4562 CA ILE B 145 -62.282 82.114-396.513 1.00 57.16 C ANISOU 4562 CA ILE B 145 7886 7339 6493 -42 908 861 C ATOM 4563 C ILE B 145 -61.201 81.271-397.191 1.00 58.19 C ANISOU 4563 C ILE B 145 8080 7361 6668 -83 887 789 C ATOM 4564 O ILE B 145 -60.015 81.398-396.877 1.00 55.66 O ANISOU 4564 O ILE B 145 7909 6849 6391 -111 843 731 O ATOM 4565 CB ILE B 145 -61.988 83.593-396.800 1.00 56.28 C ANISOU 4565 CB ILE B 145 7726 7224 6432 -150 834 789 C ATOM 4566 CG1 ILE B 145 -62.928 84.492-395.993 1.00 62.17 C ANISOU 4566 CG1 ILE B 145 8416 8059 7148 -98 848 859 C ATOM 4567 CG2 ILE B 145 -62.091 83.878-398.288 1.00 59.24 C ANISOU 4567 CG2 ILE B 145 7966 7711 6831 -268 801 710 C ATOM 4568 CD1 ILE B 145 -62.645 85.977-396.144 1.00 56.24 C ANISOU 4568 CD1 ILE B 145 7617 7303 6448 -164 784 825 C ATOM 4569 N PRO B 146 -61.609 80.401-398.127 1.00 56.56 N ANISOU 4569 N PRO B 146 7755 7276 6461 -92 908 807 N ATOM 4570 CA PRO B 146 -60.651 79.608-398.900 1.00 57.14 C ANISOU 4570 CA PRO B 146 7846 7277 6587 -138 883 735 C ATOM 4571 C PRO B 146 -59.863 80.513-399.842 1.00 55.24 C ANISOU 4571 C PRO B 146 7569 7006 6414 -308 800 590 C ATOM 4572 O PRO B 146 -60.454 81.418-400.425 1.00 56.15 O ANISOU 4572 O PRO B 146 7576 7239 6518 -383 765 569 O ATOM 4573 CB PRO B 146 -61.552 78.673-399.716 1.00 56.70 C ANISOU 4573 CB PRO B 146 7622 7403 6517 -114 901 829 C ATOM 4574 CG PRO B 146 -62.872 78.691-399.026 1.00 57.93 C ANISOU 4574 CG PRO B 146 7727 7680 6602 -16 968 983 C ATOM 4575 CD PRO B 146 -62.998 80.070-398.474 1.00 59.19 C ANISOU 4575 CD PRO B 146 7922 7817 6750 -63 946 922 C ATOM 4576 N THR B 147 -58.562 80.275-400.002 1.00 54.85 N ANISOU 4576 N THR B 147 7617 6798 6427 -363 775 502 N ATOM 4577 CA THR B 147 -57.731 81.173-400.798 1.00 54.92 C ANISOU 4577 CA THR B 147 7604 6764 6498 -518 717 388 C ATOM 4578 C THR B 147 -57.241 80.579-402.111 1.00 52.90 C ANISOU 4578 C THR B 147 7259 6553 6288 -615 687 295 C ATOM 4579 O THR B 147 -56.469 81.211-402.828 1.00 53.42 O ANISOU 4579 O THR B 147 7317 6579 6401 -740 651 201 O ATOM 4580 CB THR B 147 -56.512 81.656-400.006 1.00 56.49 C ANISOU 4580 CB THR B 147 7975 6736 6752 -548 695 373 C ATOM 4581 OG1 THR B 147 -55.756 80.523-399.574 1.00 52.67 O ANISOU 4581 OG1 THR B 147 7625 6099 6288 -496 710 367 O ATOM 4582 CG2 THR B 147 -56.955 82.447-398.797 1.00 53.85 C ANISOU 4582 CG2 THR B 147 7717 6363 6382 -473 691 468 C ATOM 4583 N ALA B 148 -57.683 79.372-402.429 1.00 53.24 N ANISOU 4583 N ALA B 148 7227 6681 6320 -552 701 339 N ATOM 4584 CA ALA B 148 -57.260 78.738-403.669 1.00 52.66 C ANISOU 4584 CA ALA B 148 7049 6661 6297 -640 654 263 C ATOM 4585 C ALA B 148 -57.473 79.674-404.848 1.00 52.39 C ANISOU 4585 C ALA B 148 6922 6732 6252 -780 579 184 C ATOM 4586 O ALA B 148 -56.540 79.985-405.590 1.00 63.07 O ANISOU 4586 O ALA B 148 8280 8031 7651 -897 549 67 O ATOM 4587 CB ALA B 148 -58.023 77.445-403.886 1.00 53.34 C ANISOU 4587 CB ALA B 148 7027 6871 6370 -539 663 380 C ATOM 4588 N LYS B 149 -58.711 80.127-405.006 1.00 70.36 N ANISOU 4588 N LYS B 149 9127 9149 8457 -761 554 257 N ATOM 4589 CA LYS B 149 -59.096 80.943-406.148 1.00 71.41 C ANISOU 4589 CA LYS B 149 9203 9380 8549 -867 471 200 C ATOM 4590 C LYS B 149 -58.440 82.315-406.111 1.00 70.10 C ANISOU 4590 C LYS B 149 9129 9127 8378 -920 491 118 C ATOM 4591 O LYS B 149 -57.969 82.812-407.131 1.00 69.20 O ANISOU 4591 O LYS B 149 9019 9015 8257 -1016 447 28 O ATOM 4592 CB LYS B 149 -60.620 81.094-406.209 1.00 74.23 C ANISOU 4592 CB LYS B 149 9487 9888 8830 -828 435 315 C ATOM 4593 CG LYS B 149 -61.388 79.782-406.367 1.00 82.72 C ANISOU 4593 CG LYS B 149 10447 11069 9914 -781 405 453 C ATOM 4594 CD LYS B 149 -62.899 80.017-406.283 1.00 86.31 C ANISOU 4594 CD LYS B 149 10835 11656 10302 -756 377 596 C ATOM 4595 CE LYS B 149 -63.694 78.709-406.248 1.00 79.88 C ANISOU 4595 CE LYS B 149 9899 10944 9506 -692 368 798 C ATOM 4596 NZ LYS B 149 -63.942 78.146-407.609 1.00 71.96 N ANISOU 4596 NZ LYS B 149 8789 10029 8523 -794 207 840 N ATOM 4597 N ILE B 150 -58.404 82.928-404.935 1.00 60.27 N ANISOU 4597 N ILE B 150 7959 7806 7136 -849 554 172 N ATOM 4598 CA ILE B 150 -57.943 84.308-404.849 1.00 60.02 C ANISOU 4598 CA ILE B 150 7989 7712 7103 -878 568 152 C ATOM 4599 C ILE B 150 -56.442 84.473-405.061 1.00 59.01 C ANISOU 4599 C ILE B 150 7929 7437 7057 -966 581 85 C ATOM 4600 O ILE B 150 -56.027 85.356-405.809 1.00101.50 O ANISOU 4600 O ILE B 150 13319 12817 12428 -1029 576 48 O ATOM 4601 CB ILE B 150 -58.425 85.042-403.568 1.00 60.51 C ANISOU 4601 CB ILE B 150 8088 7752 7152 -781 608 253 C ATOM 4602 CG1 ILE B 150 -58.830 84.046-402.485 1.00 60.91 C ANISOU 4602 CG1 ILE B 150 8156 7783 7203 -685 641 326 C ATOM 4603 CG2 ILE B 150 -59.625 85.939-403.880 1.00 61.23 C ANISOU 4603 CG2 ILE B 150 8118 7986 7159 -747 593 287 C ATOM 4604 CD1 ILE B 150 -59.712 84.666-401.398 1.00 61.55 C ANISOU 4604 CD1 ILE B 150 8239 7902 7244 -587 669 425 C ATOM 4605 N ILE B 151 -55.624 83.635-404.429 1.00 50.87 N ANISOU 4605 N ILE B 151 6954 6274 6100 -966 600 81 N ATOM 4606 CA ILE B 151 -54.178 83.757-404.632 1.00 49.88 C ANISOU 4606 CA ILE B 151 6891 5998 6063 -1071 607 28 C ATOM 4607 C ILE B 151 -53.869 83.538-406.113 1.00 49.27 C ANISOU 4607 C ILE B 151 6736 5999 5986 -1177 583 -86 C ATOM 4608 O ILE B 151 -52.916 84.102-406.656 1.00 51.15 O ANISOU 4608 O ILE B 151 6996 6171 6266 -1276 598 -127 O ATOM 4609 CB ILE B 151 -53.329 82.793-403.753 1.00 49.51 C ANISOU 4609 CB ILE B 151 6946 5775 6091 -1057 618 36 C ATOM 4610 CG1 ILE B 151 -53.279 81.407-404.386 1.00 49.19 C ANISOU 4610 CG1 ILE B 151 6840 5785 6065 -1059 615 -42 C ATOM 4611 CG2 ILE B 151 -53.837 82.749-402.312 1.00 50.33 C ANISOU 4611 CG2 ILE B 151 7146 5814 6162 -927 626 147 C ATOM 4612 CD1 ILE B 151 -52.005 80.649-404.083 1.00 48.39 C ANISOU 4612 CD1 ILE B 151 6833 5497 6056 -1101 625 -84 C ATOM 4613 N ALA B 152 -54.694 82.730-406.768 1.00 50.80 N ANISOU 4613 N ALA B 152 6835 6334 6132 -1157 540 -118 N ATOM 4614 CA ALA B 152 -54.566 82.531-408.201 1.00 49.39 C ANISOU 4614 CA ALA B 152 6584 6244 5939 -1254 484 -215 C ATOM 4615 C ALA B 152 -54.760 83.864-408.914 1.00 50.62 C ANISOU 4615 C ALA B 152 6775 6446 6014 -1286 473 -229 C ATOM 4616 O ALA B 152 -53.819 84.418-409.480 1.00 49.79 O ANISOU 4616 O ALA B 152 6708 6280 5930 -1368 499 -282 O ATOM 4617 CB ALA B 152 -55.584 81.525-408.681 1.00 50.48 C ANISOU 4617 CB ALA B 152 6614 6527 6039 -1218 410 -192 C ATOM 4618 N LYS B 153 -55.985 84.375-408.871 1.00 52.03 N ANISOU 4618 N LYS B 153 6947 6727 6094 -1212 444 -167 N ATOM 4619 CA LYS B 153 -56.301 85.667-409.458 1.00 55.71 C ANISOU 4619 CA LYS B 153 7473 7233 6463 -1203 439 -163 C ATOM 4620 C LYS B 153 -55.274 86.725-409.047 1.00 54.98 C ANISOU 4620 C LYS B 153 7454 7021 6416 -1204 531 -127 C ATOM 4621 O LYS B 153 -54.881 87.562-409.856 1.00 56.58 O ANISOU 4621 O LYS B 153 7710 7219 6567 -1228 549 -146 O ATOM 4622 CB LYS B 153 -57.706 86.102-409.035 1.00 56.83 C ANISOU 4622 CB LYS B 153 7605 7468 6518 -1104 416 -78 C ATOM 4623 CG LYS B 153 -58.164 87.433-409.611 1.00 53.17 C ANISOU 4623 CG LYS B 153 7220 7045 5939 -1063 410 -66 C ATOM 4624 CD LYS B 153 -58.464 87.297-411.087 1.00 59.67 C ANISOU 4624 CD LYS B 153 8081 7931 6660 -1127 300 -144 C ATOM 4625 CE LYS B 153 -59.242 88.488-411.608 1.00 65.82 C ANISOU 4625 CE LYS B 153 8969 8749 7289 -1055 274 -118 C ATOM 4626 NZ LYS B 153 -59.939 88.168-412.891 1.00 70.92 N ANISOU 4626 NZ LYS B 153 9671 9457 7818 -1110 116 -168 N ATOM 4627 N ALA B 154 -54.842 86.681-407.791 1.00 55.27 N ANISOU 4627 N ALA B 154 7503 6953 6544 -1173 582 -53 N ATOM 4628 CA ALA B 154 -53.922 87.684-407.261 1.00 57.18 C ANISOU 4628 CA ALA B 154 7805 7073 6848 -1177 644 36 C ATOM 4629 C ALA B 154 -52.546 87.575-407.905 1.00 58.92 C ANISOU 4629 C ALA B 154 8047 7196 7143 -1303 673 -15 C ATOM 4630 O ALA B 154 -51.960 88.576-408.324 1.00 55.94 O ANISOU 4630 O ALA B 154 7705 6787 6761 -1321 723 42 O ATOM 4631 CB ALA B 154 -53.816 87.566-405.752 1.00 56.43 C ANISOU 4631 CB ALA B 154 7737 6874 6830 -1126 652 138 C ATOM 4632 N LYS B 155 -52.023 86.357-407.972 1.00 71.99 N ANISOU 4632 N LYS B 155 9677 8806 8870 -1381 651 -107 N ATOM 4633 CA LYS B 155 -50.766 86.126-408.665 1.00 71.58 C ANISOU 4633 CA LYS B 155 9626 8678 8895 -1515 677 -175 C ATOM 4634 C LYS B 155 -50.911 86.626-410.090 1.00 65.13 C ANISOU 4634 C LYS B 155 8797 7972 7979 -1548 675 -246 C ATOM 4635 O LYS B 155 -50.016 87.255-410.646 1.00 66.36 O ANISOU 4635 O LYS B 155 8983 8077 8152 -1617 733 -233 O ATOM 4636 CB LYS B 155 -50.403 84.635-408.658 1.00 69.86 C ANISOU 4636 CB LYS B 155 9364 8428 8752 -1571 644 -280 C ATOM 4637 CG LYS B 155 -49.637 84.178-407.421 1.00 63.72 C ANISOU 4637 CG LYS B 155 8659 7465 8088 -1578 660 -221 C ATOM 4638 CD LYS B 155 -49.366 82.683-407.446 1.00 65.24 C ANISOU 4638 CD LYS B 155 8820 7633 8336 -1593 638 -318 C ATOM 4639 CE LYS B 155 -48.613 82.239-406.196 1.00 70.68 C ANISOU 4639 CE LYS B 155 9634 8108 9112 -1582 644 -258 C ATOM 4640 NZ LYS B 155 -48.503 80.751-406.080 1.00 67.43 N ANISOU 4640 NZ LYS B 155 9215 7673 8733 -1540 634 -330 N ATOM 4641 N GLU B 156 -52.070 86.352-410.664 1.00 65.51 N ANISOU 4641 N GLU B 156 8814 8163 7914 -1494 602 -303 N ATOM 4642 CA GLU B 156 -52.343 86.658-412.057 1.00 68.62 C ANISOU 4642 CA GLU B 156 9229 8654 8190 -1520 558 -381 C ATOM 4643 C GLU B 156 -52.344 88.153-412.371 1.00 71.12 C ANISOU 4643 C GLU B 156 9649 8966 8407 -1452 623 -299 C ATOM 4644 O GLU B 156 -52.248 88.544-413.533 1.00 70.60 O ANISOU 4644 O GLU B 156 9647 8939 8237 -1472 613 -354 O ATOM 4645 CB GLU B 156 -53.676 86.024-412.457 1.00 68.37 C ANISOU 4645 CB GLU B 156 9155 8755 8067 -1479 435 -418 C ATOM 4646 CG GLU B 156 -54.378 86.679-413.620 1.00 67.98 C ANISOU 4646 CG GLU B 156 9188 8792 7850 -1458 360 -447 C ATOM 4647 CD GLU B 156 -55.772 86.125-413.817 1.00 88.97 C ANISOU 4647 CD GLU B 156 11811 11560 10433 -1424 222 -433 C ATOM 4648 OE1 GLU B 156 -55.986 84.943-413.458 1.00 84.05 O ANISOU 4648 OE1 GLU B 156 11070 10969 9897 -1449 175 -429 O ATOM 4649 OE2 GLU B 156 -56.646 86.871-414.320 1.00 93.92 O ANISOU 4649 OE2 GLU B 156 12537 12235 10914 -1367 163 -409 O ATOM 4650 N VAL B 157 -52.445 88.991-411.343 1.00 49.67 N ANISOU 4650 N VAL B 157 6957 6200 5715 -1360 689 -157 N ATOM 4651 CA VAL B 157 -52.521 90.437-411.559 1.00 49.68 C ANISOU 4651 CA VAL B 157 7044 6207 5625 -1259 758 -42 C ATOM 4652 C VAL B 157 -51.566 91.245-410.668 1.00 49.62 C ANISOU 4652 C VAL B 157 7039 6080 5736 -1245 860 138 C ATOM 4653 O VAL B 157 -51.873 92.367-410.271 1.00 52.32 O ANISOU 4653 O VAL B 157 7410 6429 6039 -1119 907 292 O ATOM 4654 CB VAL B 157 -53.969 90.960-411.400 1.00 51.06 C ANISOU 4654 CB VAL B 157 7248 6482 5671 -1116 713 -6 C ATOM 4655 CG1 VAL B 157 -54.877 90.348-412.455 1.00 51.39 C ANISOU 4655 CG1 VAL B 157 7315 6626 5585 -1140 593 -141 C ATOM 4656 CG2 VAL B 157 -54.496 90.655-410.010 1.00 51.49 C ANISOU 4656 CG2 VAL B 157 7223 6529 5812 -1072 698 61 C ATOM 4657 N GLY B 158 -50.410 90.670-410.359 1.00127.12 N ANISOU 4657 N GLY B 158 16820 15780 15698 -1377 881 136 N ATOM 4658 CA GLY B 158 -49.366 91.386-409.647 1.00131.58 C ANISOU 4658 CA GLY B 158 17396 16211 16389 -1401 953 330 C ATOM 4659 C GLY B 158 -49.661 91.702-408.193 1.00137.78 C ANISOU 4659 C GLY B 158 18168 16934 17248 -1326 921 486 C ATOM 4660 O GLY B 158 -48.764 92.099-407.444 1.00140.62 O ANISOU 4660 O GLY B 158 18536 17156 17737 -1371 936 662 O ATOM 4661 N GLU B 159 -50.917 91.525-407.789 1.00 80.20 N ANISOU 4661 N GLU B 159 10857 9739 9878 -1220 865 436 N ATOM 4662 CA GLU B 159 -51.323 91.825-406.418 1.00 81.62 C ANISOU 4662 CA GLU B 159 11022 9879 10111 -1139 830 571 C ATOM 4663 C GLU B 159 -51.179 90.622-405.482 1.00 76.75 C ANISOU 4663 C GLU B 159 10412 9169 9581 -1202 763 509 C ATOM 4664 O GLU B 159 -52.119 90.257-404.780 1.00 76.90 O ANISOU 4664 O GLU B 159 10416 9239 9563 -1122 721 489 O ATOM 4665 CB GLU B 159 -52.763 92.351-406.378 1.00 79.98 C ANISOU 4665 CB GLU B 159 10792 9822 9776 -984 819 571 C ATOM 4666 CG GLU B 159 -53.001 93.606-407.202 1.00 77.68 C ANISOU 4666 CG GLU B 159 10528 9609 9377 -879 885 649 C ATOM 4667 CD GLU B 159 -54.345 94.250-406.915 1.00 77.68 C ANISOU 4667 CD GLU B 159 10509 9728 9276 -719 871 685 C ATOM 4668 OE1 GLU B 159 -54.722 94.360-405.729 1.00 79.46 O ANISOU 4668 OE1 GLU B 159 10680 9944 9567 -668 841 775 O ATOM 4669 OE2 GLU B 159 -55.021 94.659-407.876 1.00 75.08 O ANISOU 4669 OE2 GLU B 159 10232 9497 8799 -646 884 625 O ATOM 4670 N TYR B 160 -49.999 90.015-405.468 1.00 58.66 N ANISOU 4670 N TYR B 160 8154 6736 7398 -1336 760 489 N ATOM 4671 CA TYR B 160 -49.737 88.902-404.569 1.00 58.46 C ANISOU 4671 CA TYR B 160 8175 6591 7446 -1378 700 445 C ATOM 4672 C TYR B 160 -48.410 89.094-403.840 1.00 63.55 C ANISOU 4672 C TYR B 160 8900 7009 8236 -1481 673 593 C ATOM 4673 O TYR B 160 -47.385 89.332-404.473 1.00 67.42 O ANISOU 4673 O TYR B 160 9387 7434 8796 -1599 714 621 O ATOM 4674 CB TYR B 160 -49.725 87.580-405.339 1.00 58.41 C ANISOU 4674 CB TYR B 160 8140 6633 7419 -1440 699 236 C ATOM 4675 CG TYR B 160 -49.314 86.395-404.491 1.00 57.89 C ANISOU 4675 CG TYR B 160 8144 6428 7425 -1464 656 200 C ATOM 4676 CD1 TYR B 160 -50.263 85.558-403.927 1.00 55.96 C ANISOU 4676 CD1 TYR B 160 7903 6240 7118 -1353 629 156 C ATOM 4677 CD2 TYR B 160 -47.975 86.120-404.246 1.00 57.19 C ANISOU 4677 CD2 TYR B 160 8130 6141 7458 -1588 646 227 C ATOM 4678 CE1 TYR B 160 -49.888 84.474-403.148 1.00 56.01 C ANISOU 4678 CE1 TYR B 160 8004 6110 7168 -1339 602 138 C ATOM 4679 CE2 TYR B 160 -47.591 85.046-403.471 1.00 57.20 C ANISOU 4679 CE2 TYR B 160 8233 5994 7508 -1590 603 195 C ATOM 4680 CZ TYR B 160 -48.549 84.223-402.924 1.00 56.41 C ANISOU 4680 CZ TYR B 160 8152 5953 7329 -1453 585 150 C ATOM 4681 OH TYR B 160 -48.166 83.148-402.148 1.00 51.17 O ANISOU 4681 OH TYR B 160 7618 5133 6692 -1422 554 132 O ATOM 4682 N PRO B 161 -48.425 89.002-402.501 1.00 57.89 N ANISOU 4682 N PRO B 161 8266 6163 7566 -1442 594 703 N ATOM 4683 CA PRO B 161 -49.614 88.829-401.664 1.00 55.16 C ANISOU 4683 CA PRO B 161 7926 5891 7140 -1298 555 697 C ATOM 4684 C PRO B 161 -50.119 90.173-401.135 1.00 59.78 C ANISOU 4684 C PRO B 161 8469 6528 7717 -1202 540 887 C ATOM 4685 O PRO B 161 -50.976 90.210-400.251 1.00 62.41 O ANISOU 4685 O PRO B 161 8808 6898 8007 -1094 499 923 O ATOM 4686 CB PRO B 161 -49.100 87.970-400.496 1.00 48.98 C ANISOU 4686 CB PRO B 161 7296 4898 6416 -1319 470 724 C ATOM 4687 CG PRO B 161 -47.617 87.743-400.761 1.00 48.65 C ANISOU 4687 CG PRO B 161 7325 4665 6495 -1488 456 744 C ATOM 4688 CD PRO B 161 -47.198 88.801-401.721 1.00 52.01 C ANISOU 4688 CD PRO B 161 7643 5164 6955 -1556 523 818 C ATOM 4689 N THR B 162 -49.580 91.262-401.665 1.00 91.52 N ANISOU 4689 N THR B 162 12442 10553 11778 -1232 581 1020 N ATOM 4690 CA THR B 162 -50.025 92.592-401.285 1.00 88.66 C ANISOU 4690 CA THR B 162 12019 10254 11412 -1120 580 1222 C ATOM 4691 C THR B 162 -51.543 92.651-401.037 1.00 90.40 C ANISOU 4691 C THR B 162 12179 10654 11513 -967 584 1143 C ATOM 4692 O THR B 162 -51.980 92.784-399.883 1.00 91.53 O ANISOU 4692 O THR B 162 12333 10768 11675 -899 512 1236 O ATOM 4693 CB THR B 162 -49.578 93.634-402.320 1.00 92.61 C ANISOU 4693 CB THR B 162 12463 10815 11911 -1119 676 1325 C ATOM 4694 OG1 THR B 162 -49.277 92.980-403.560 1.00 93.36 O ANISOU 4694 OG1 THR B 162 12564 10953 11955 -1206 747 1125 O ATOM 4695 CG2 THR B 162 -48.326 94.345-401.842 1.00 96.64 C ANISOU 4695 CG2 THR B 162 12996 11146 12576 -1199 641 1609 C ATOM 4696 N LEU B 163 -52.336 92.543-402.104 1.00 51.69 N ANISOU 4696 N LEU B 163 7221 5928 6489 -923 657 982 N ATOM 4697 CA LEU B 163 -53.796 92.565-401.985 1.00 51.90 C ANISOU 4697 CA LEU B 163 7190 6124 6405 -801 661 911 C ATOM 4698 C LEU B 163 -54.362 93.885-401.442 1.00 52.86 C ANISOU 4698 C LEU B 163 7250 6313 6523 -666 662 1091 C ATOM 4699 O LEU B 163 -53.797 94.959-401.653 1.00 53.04 O ANISOU 4699 O LEU B 163 7255 6310 6587 -637 692 1259 O ATOM 4700 CB LEU B 163 -54.278 91.443-401.071 1.00 56.80 C ANISOU 4700 CB LEU B 163 7842 6716 7023 -796 608 834 C ATOM 4701 CG LEU B 163 -54.347 90.016-401.572 1.00 51.96 C ANISOU 4701 CG LEU B 163 7253 6115 6373 -859 615 646 C ATOM 4702 CD1 LEU B 163 -55.268 89.216-400.655 1.00 52.66 C ANISOU 4702 CD1 LEU B 163 7350 6239 6419 -780 593 623 C ATOM 4703 CD2 LEU B 163 -54.863 90.012-402.979 1.00 52.57 C ANISOU 4703 CD2 LEU B 163 7269 6347 6357 -870 657 522 C ATOM 4704 N GLY B 164 -55.512 93.788-400.775 1.00112.65 N ANISOU 4704 N GLY B 164 14776 13981 14044 -576 638 1066 N ATOM 4705 CA GLY B 164 -56.052 94.873-399.974 1.00120.23 C ANISOU 4705 CA GLY B 164 15664 14993 15024 -452 619 1234 C ATOM 4706 C GLY B 164 -56.903 95.923-400.670 1.00120.15 C ANISOU 4706 C GLY B 164 15581 15148 14922 -325 686 1257 C ATOM 4707 O GLY B 164 -58.042 96.177-400.263 1.00107.93 O ANISOU 4707 O GLY B 164 13964 13721 13324 -229 684 1248 O ATOM 4708 N SER B 165 -56.357 96.541-401.713 1.00 98.43 N ANISOU 4708 N SER B 165 12858 12398 12143 -317 749 1292 N ATOM 4709 CA SER B 165 -56.932 97.777-402.240 1.00 90.77 C ANISOU 4709 CA SER B 165 11853 11542 11092 -159 813 1381 C ATOM 4710 C SER B 165 -58.254 97.547-402.975 1.00 87.88 C ANISOU 4710 C SER B 165 11499 11325 10566 -109 831 1194 C ATOM 4711 O SER B 165 -59.263 98.181-402.665 1.00 93.17 O ANISOU 4711 O SER B 165 12108 12101 11190 16 837 1234 O ATOM 4712 CB SER B 165 -55.916 98.508-403.129 1.00 89.47 C ANISOU 4712 CB SER B 165 11742 11322 10929 -144 888 1500 C ATOM 4713 OG SER B 165 -56.159 99.904-403.138 1.00 92.05 O ANISOU 4713 OG SER B 165 12026 11715 11235 44 944 1707 O ATOM 4714 N ASN B 166 -58.241 96.632-403.940 1.00 67.74 N ANISOU 4714 N ASN B 166 9024 8776 7939 -214 827 1003 N ATOM 4715 CA ASN B 166 -59.412 96.360-404.761 1.00 69.19 C ANISOU 4715 CA ASN B 166 9239 9077 7974 -194 813 850 C ATOM 4716 C ASN B 166 -60.059 95.063-404.309 1.00 71.28 C ANISOU 4716 C ASN B 166 9457 9373 8253 -288 752 726 C ATOM 4717 O ASN B 166 -61.026 94.579-404.903 1.00 68.25 O ANISOU 4717 O ASN B 166 9085 9076 7770 -308 717 617 O ATOM 4718 CB ASN B 166 -59.006 96.244-406.228 1.00 69.00 C ANISOU 4718 CB ASN B 166 9335 9037 7846 -240 826 749 C ATOM 4719 CG ASN B 166 -57.854 97.155-406.587 1.00 70.29 C ANISOU 4719 CG ASN B 166 9550 9122 8034 -193 906 887 C ATOM 4720 OD1 ASN B 166 -57.854 98.336-406.248 1.00 71.62 O ANISOU 4720 OD1 ASN B 166 9697 9303 8211 -44 961 1068 O ATOM 4721 ND2 ASN B 166 -56.861 96.609-407.276 1.00 74.70 N ANISOU 4721 ND2 ASN B 166 10166 9606 8612 -315 917 820 N ATOM 4722 N TRP B 167 -59.502 94.491-403.253 1.00 78.59 N ANISOU 4722 N TRP B 167 10346 10216 9300 -343 735 767 N ATOM 4723 CA TRP B 167 -60.003 93.233-402.736 1.00 77.55 C ANISOU 4723 CA TRP B 167 10186 10101 9180 -404 699 681 C ATOM 4724 C TRP B 167 -60.996 93.486-401.613 1.00 73.65 C ANISOU 4724 C TRP B 167 9611 9680 8694 -316 695 753 C ATOM 4725 O TRP B 167 -60.694 94.187-400.644 1.00 78.18 O ANISOU 4725 O TRP B 167 10154 10209 9343 -255 692 883 O ATOM 4726 CB TRP B 167 -58.841 92.360-402.274 1.00 77.79 C ANISOU 4726 CB TRP B 167 10262 9981 9312 -500 682 673 C ATOM 4727 CG TRP B 167 -57.939 91.985-403.410 1.00 72.50 C ANISOU 4727 CG TRP B 167 9651 9257 8639 -601 688 583 C ATOM 4728 CD1 TRP B 167 -56.844 92.668-403.851 1.00 71.70 C ANISOU 4728 CD1 TRP B 167 9593 9070 8581 -630 718 642 C ATOM 4729 CD2 TRP B 167 -58.073 90.845-404.266 1.00 70.68 C ANISOU 4729 CD2 TRP B 167 9430 9061 8364 -686 665 436 C ATOM 4730 NE1 TRP B 167 -56.282 92.019-404.923 1.00 66.93 N ANISOU 4730 NE1 TRP B 167 9029 8446 7956 -734 720 519 N ATOM 4731 CE2 TRP B 167 -57.018 90.897-405.198 1.00 68.67 C ANISOU 4731 CE2 TRP B 167 9226 8741 8126 -768 679 389 C ATOM 4732 CE3 TRP B 167 -58.981 89.784-404.333 1.00 72.36 C ANISOU 4732 CE3 TRP B 167 9602 9359 8532 -697 633 365 C ATOM 4733 CZ2 TRP B 167 -56.843 89.928-406.181 1.00 71.40 C ANISOU 4733 CZ2 TRP B 167 9578 9106 8446 -863 648 253 C ATOM 4734 CZ3 TRP B 167 -58.808 88.822-405.312 1.00 69.45 C ANISOU 4734 CZ3 TRP B 167 9237 9008 8144 -785 598 257 C ATOM 4735 CH2 TRP B 167 -57.747 88.902-406.222 1.00 71.84 C ANISOU 4735 CH2 TRP B 167 9586 9246 8465 -868 600 192 C ATOM 4736 N THR B 168 -62.190 92.923-401.756 1.00 61.38 N ANISOU 4736 N THR B 168 8014 8241 7065 -315 689 686 N ATOM 4737 CA THR B 168 -63.279 93.216-400.836 1.00 62.94 C ANISOU 4737 CA THR B 168 8123 8535 7256 -236 699 747 C ATOM 4738 C THR B 168 -64.054 91.961-400.456 1.00 62.94 C ANISOU 4738 C THR B 168 8091 8588 7237 -274 699 710 C ATOM 4739 O THR B 168 -64.024 90.965-401.174 1.00 56.50 O ANISOU 4739 O THR B 168 7306 7772 6391 -351 682 637 O ATOM 4740 CB THR B 168 -64.238 94.235-401.452 1.00 59.02 C ANISOU 4740 CB THR B 168 7593 8157 6675 -161 710 755 C ATOM 4741 OG1 THR B 168 -64.682 93.764-402.732 1.00 57.24 O ANISOU 4741 OG1 THR B 168 7426 7975 6349 -226 679 653 O ATOM 4742 CG2 THR B 168 -63.528 95.567-401.635 1.00 67.49 C ANISOU 4742 CG2 THR B 168 8690 9185 7767 -73 733 842 C ATOM 4743 N ALA B 169 -64.746 92.010-399.325 1.00 56.46 N ANISOU 4743 N ALA B 169 7201 7817 6433 -212 719 778 N ATOM 4744 CA ALA B 169 -65.486 90.848-398.854 1.00 59.33 C ANISOU 4744 CA ALA B 169 7536 8232 6773 -225 742 781 C ATOM 4745 C ALA B 169 -66.863 91.239-398.373 1.00 59.98 C ANISOU 4745 C ALA B 169 7506 8461 6822 -172 772 834 C ATOM 4746 O ALA B 169 -66.993 92.096-397.505 1.00 58.38 O ANISOU 4746 O ALA B 169 7254 8274 6655 -98 781 894 O ATOM 4747 CB ALA B 169 -64.732 90.157-397.740 1.00 56.49 C ANISOU 4747 CB ALA B 169 7249 7746 6467 -205 747 819 C ATOM 4748 N GLU B 170 -67.885 90.599-398.931 1.00 78.76 N ANISOU 4748 N GLU B 170 9837 10947 9142 -216 780 830 N ATOM 4749 CA GLU B 170 -69.265 90.838-398.523 1.00 86.65 C ANISOU 4749 CA GLU B 170 10723 12087 10112 -188 814 891 C ATOM 4750 C GLU B 170 -69.917 89.532-398.071 1.00 86.42 C ANISOU 4750 C GLU B 170 10657 12109 10070 -204 862 964 C ATOM 4751 O GLU B 170 -69.389 88.449-398.318 1.00 86.48 O ANISOU 4751 O GLU B 170 10725 12054 10079 -233 859 962 O ATOM 4752 CB GLU B 170 -70.070 91.460-399.669 1.00 92.01 C ANISOU 4752 CB GLU B 170 11382 12849 10727 -228 768 862 C ATOM 4753 CG GLU B 170 -70.293 90.523-400.852 1.00101.87 C ANISOU 4753 CG GLU B 170 12673 14106 11927 -333 706 843 C ATOM 4754 CD GLU B 170 -71.153 91.137-401.945 1.00114.36 C ANISOU 4754 CD GLU B 170 14276 15747 13429 -375 630 826 C ATOM 4755 OE1 GLU B 170 -71.025 92.355-402.196 1.00120.02 O ANISOU 4755 OE1 GLU B 170 15038 16448 14115 -312 623 782 O ATOM 4756 OE2 GLU B 170 -71.953 90.400-402.561 1.00113.59 O ANISOU 4756 OE2 GLU B 170 14162 15700 13296 -464 569 877 O ATOM 4757 N ILE B 171 -71.066 89.643-397.413 1.00 58.94 N ANISOU 4757 N ILE B 171 7070 8746 6577 -176 916 1043 N ATOM 4758 CA ILE B 171 -71.790 88.479-396.915 1.00 60.15 C ANISOU 4758 CA ILE B 171 7177 8964 6713 -172 986 1153 C ATOM 4759 C ILE B 171 -72.802 87.963-397.943 1.00 59.32 C ANISOU 4759 C ILE B 171 7004 8960 6573 -268 955 1220 C ATOM 4760 O ILE B 171 -72.937 88.517-399.032 1.00 59.77 O ANISOU 4760 O ILE B 171 7075 9026 6609 -339 864 1160 O ATOM 4761 CB ILE B 171 -72.525 88.811-395.602 1.00 60.34 C ANISOU 4761 CB ILE B 171 7118 9066 6744 -97 1069 1228 C ATOM 4762 CG1 ILE B 171 -71.600 89.557-394.646 1.00 59.60 C ANISOU 4762 CG1 ILE B 171 7085 8870 6689 -15 1052 1180 C ATOM 4763 CG2 ILE B 171 -73.011 87.545-394.921 1.00 58.42 C ANISOU 4763 CG2 ILE B 171 6867 8859 6472 -57 1166 1359 C ATOM 4764 CD1 ILE B 171 -70.713 88.628-393.831 1.00 63.35 C ANISOU 4764 CD1 ILE B 171 7702 9209 7161 46 1073 1205 C ATOM 4765 N SER B 172 -73.504 86.891-397.591 1.00 70.11 N ANISOU 4765 N SER B 172 8311 10395 7931 -265 1022 1366 N ATOM 4766 CA SER B 172 -74.557 86.353-398.430 1.00 73.60 C ANISOU 4766 CA SER B 172 8671 10937 8356 -363 982 1489 C ATOM 4767 C SER B 172 -75.560 87.466-398.648 1.00 78.72 C ANISOU 4767 C SER B 172 9246 11673 8992 -416 947 1476 C ATOM 4768 O SER B 172 -75.636 88.393-397.842 1.00 80.91 O ANISOU 4768 O SER B 172 9492 11971 9280 -351 1001 1418 O ATOM 4769 CB SER B 172 -75.227 85.178-397.720 1.00 77.50 C ANISOU 4769 CB SER B 172 9091 11505 8849 -319 1097 1697 C ATOM 4770 OG SER B 172 -75.899 84.333-398.637 1.00 88.09 O ANISOU 4770 OG SER B 172 10368 12909 10194 -412 1037 1858 O ATOM 4771 N SER B 173 -76.325 87.392-399.735 1.00158.77 N ANISOU 4771 N SER B 173 19364 21855 19107 -534 843 1536 N ATOM 4772 CA SER B 173 -77.383 88.369-399.978 1.00160.58 C ANISOU 4772 CA SER B 173 19543 22156 19314 -587 802 1539 C ATOM 4773 C SER B 173 -78.760 87.706-399.960 1.00161.24 C ANISOU 4773 C SER B 173 19504 22352 19409 -679 815 1762 C ATOM 4774 O SER B 173 -79.386 87.515-401.001 1.00162.15 O ANISOU 4774 O SER B 173 19636 22471 19503 -804 680 1846 O ATOM 4775 CB SER B 173 -77.156 89.121-401.293 1.00154.77 C ANISOU 4775 CB SER B 173 18934 21348 18524 -646 644 1417 C ATOM 4776 OG SER B 173 -77.421 88.296-402.413 1.00157.55 O ANISOU 4776 OG SER B 173 19327 21682 18854 -768 508 1508 O ATOM 4777 N SER B 174 -79.216 87.346-398.765 1.00107.64 N ANISOU 4777 N SER B 174 12601 15647 12650 -618 972 1874 N ATOM 4778 CA SER B 174 -78.416 87.549-397.562 1.00106.78 C ANISOU 4778 CA SER B 174 12509 15507 12554 -473 1095 1778 C ATOM 4779 C SER B 174 -78.641 86.492-396.484 1.00106.88 C ANISOU 4779 C SER B 174 12464 15571 12574 -396 1250 1947 C ATOM 4780 O SER B 174 -79.556 85.669-396.567 1.00107.57 O ANISOU 4780 O SER B 174 12461 15746 12666 -449 1293 2164 O ATOM 4781 CB SER B 174 -78.616 88.964-396.988 1.00106.08 C ANISOU 4781 CB SER B 174 12379 15452 12474 -424 1119 1655 C ATOM 4782 OG SER B 174 -79.987 89.316-396.900 1.00106.28 O ANISOU 4782 OG SER B 174 12274 15602 12506 -493 1143 1754 O ATOM 4783 N SER B 175 -77.771 86.511-395.483 1.00 90.81 N ANISOU 4783 N SER B 175 10501 13469 10535 -265 1327 1865 N ATOM 4784 CA SER B 175 -77.976 85.728-394.283 1.00 79.24 C ANISOU 4784 CA SER B 175 9021 12036 9049 -158 1482 2002 C ATOM 4785 C SER B 175 -79.183 86.309-393.571 1.00 79.93 C ANISOU 4785 C SER B 175 8959 12266 9146 -173 1567 2075 C ATOM 4786 O SER B 175 -79.682 87.365-393.954 1.00 83.64 O ANISOU 4786 O SER B 175 9349 12788 9641 -252 1500 1993 O ATOM 4787 CB SER B 175 -76.761 85.860-393.379 1.00 73.59 C ANISOU 4787 CB SER B 175 8452 11190 8320 -25 1501 1875 C ATOM 4788 OG SER B 175 -76.763 87.120-392.730 1.00 63.78 O ANISOU 4788 OG SER B 175 7172 9960 7100 -2 1483 1758 O ATOM 4789 N SER B 176 -79.643 85.637-392.525 1.00110.41 N ANISOU 4789 N SER B 176 12787 16186 12978 -87 1721 2231 N ATOM 4790 CA SER B 176 -80.738 86.164-391.725 1.00107.67 C ANISOU 4790 CA SER B 176 12291 15978 12640 -97 1819 2298 C ATOM 4791 C SER B 176 -80.417 87.574-391.232 1.00102.73 C ANISOU 4791 C SER B 176 11650 15339 12044 -70 1760 2088 C ATOM 4792 O SER B 176 -81.246 88.479-391.331 1.00 94.49 O ANISOU 4792 O SER B 176 10464 14399 11039 -143 1745 2061 O ATOM 4793 CB SER B 176 -81.007 85.251-390.534 1.00101.63 C ANISOU 4793 CB SER B 176 11545 15251 11820 33 2001 2474 C ATOM 4794 OG SER B 176 -81.053 83.898-390.941 1.00 99.60 O ANISOU 4794 OG SER B 176 11326 14984 11532 56 2060 2682 O ATOM 4795 N GLY B 177 -79.204 87.758-390.720 1.00 61.86 N ANISOU 4795 N GLY B 177 6621 10027 6856 37 1717 1958 N ATOM 4796 CA GLY B 177 -78.840 88.979-390.026 1.00 57.85 C ANISOU 4796 CA GLY B 177 6095 9504 6383 89 1664 1819 C ATOM 4797 C GLY B 177 -77.892 89.956-390.684 1.00 58.35 C ANISOU 4797 C GLY B 177 6172 9505 6495 50 1520 1657 C ATOM 4798 O GLY B 177 -77.223 89.631-391.665 1.00 60.79 O ANISOU 4798 O GLY B 177 6495 9799 6804 -38 1454 1629 O ATOM 4799 N LEU B 178 -77.827 91.158-390.110 1.00110.63 N ANISOU 4799 N LEU B 178 12796 16083 13154 125 1466 1571 N ATOM 4800 CA LEU B 178 -77.154 92.303-390.728 1.00115.93 C ANISOU 4800 CA LEU B 178 13445 16725 13877 121 1354 1458 C ATOM 4801 C LEU B 178 -75.907 92.920-390.076 1.00106.82 C ANISOU 4801 C LEU B 178 12342 15474 12772 220 1277 1416 C ATOM 4802 O LEU B 178 -75.271 92.302-389.225 1.00101.22 O ANISOU 4802 O LEU B 178 11664 14738 12056 287 1297 1465 O ATOM 4803 CB LEU B 178 -78.352 93.226-390.955 1.00113.55 C ANISOU 4803 CB LEU B 178 12953 16585 13604 81 1375 1458 C ATOM 4804 CG LEU B 178 -78.917 93.884-389.689 1.00114.16 C ANISOU 4804 CG LEU B 178 12875 16773 13726 147 1423 1489 C ATOM 4805 CD1 LEU B 178 -80.180 94.658-390.019 1.00113.38 C ANISOU 4805 CD1 LEU B 178 12589 16837 13655 95 1455 1492 C ATOM 4806 CD2 LEU B 178 -79.187 92.864-388.591 1.00109.68 C ANISOU 4806 CD2 LEU B 178 12327 16228 13119 176 1527 1587 C ATOM 4807 N ALA B 179 -75.576 94.142-390.500 1.00 73.69 N ANISOU 4807 N ALA B 179 8163 11218 8619 231 1181 1349 N ATOM 4808 CA ALA B 179 -74.588 95.005-389.834 1.00 80.14 C ANISOU 4808 CA ALA B 179 8975 11968 9507 318 1091 1353 C ATOM 4809 C ALA B 179 -73.067 94.811-389.885 1.00 68.36 C ANISOU 4809 C ALA B 179 7669 10272 8032 333 998 1344 C ATOM 4810 O ALA B 179 -72.319 95.675-389.416 1.00 66.37 O ANISOU 4810 O ALA B 179 7413 9953 7851 392 904 1384 O ATOM 4811 CB ALA B 179 -75.046 95.211-388.386 1.00 83.48 C ANISOU 4811 CB ALA B 179 9299 12462 9959 382 1107 1419 C ATOM 4812 N ALA B 180 -72.613 93.707-390.473 1.00 73.78 N ANISOU 4812 N ALA B 180 8508 10863 8663 276 1017 1310 N ATOM 4813 CA ALA B 180 -71.223 93.282-390.327 1.00 68.19 C ANISOU 4813 CA ALA B 180 7989 9953 7966 282 943 1306 C ATOM 4814 C ALA B 180 -70.220 93.951-391.261 1.00 67.23 C ANISOU 4814 C ALA B 180 7917 9738 7891 259 866 1267 C ATOM 4815 O ALA B 180 -70.590 94.504-392.295 1.00 71.11 O ANISOU 4815 O ALA B 180 8336 10309 8373 236 882 1224 O ATOM 4816 CB ALA B 180 -71.131 91.778-390.475 1.00 66.67 C ANISOU 4816 CB ALA B 180 7934 9698 7700 252 1004 1297 C ATOM 4817 N VAL B 181 -68.928 93.856-390.878 1.00 20.00 N ATOM 4818 CA VAL B 181 -67.843 94.467-391.637 1.00 20.00 C ATOM 4819 C VAL B 181 -66.573 93.626-391.557 1.00 20.00 C ATOM 4820 O VAL B 181 -65.802 93.753-390.609 1.00 64.47 O ANISOU 4820 O VAL B 181 8055 8748 7692 217 564 1367 O ATOM 4821 CB VAL B 181 -67.538 95.892-391.139 1.00 20.00 C ATOM 4822 CG1 VAL B 181 -66.341 96.468-391.877 1.00 20.00 C ATOM 4823 CG2 VAL B 181 -68.756 96.786-391.304 1.00 20.00 C ATOM 4824 N ILE B 182 -66.300 92.825-392.583 1.00 58.74 N ANISOU 4824 N ILE B 182 7316 8130 6872 126 701 1192 N ATOM 4825 CA ILE B 182 -65.052 92.069-392.624 1.00 58.81 C ANISOU 4825 CA ILE B 182 7506 7942 6896 79 655 1175 C ATOM 4826 C ILE B 182 -64.045 92.810-393.485 1.00 55.61 C ANISOU 4826 C ILE B 182 7115 7461 6554 30 607 1175 C ATOM 4827 O ILE B 182 -64.385 93.274-394.570 1.00 58.34 O ANISOU 4827 O ILE B 182 7380 7910 6876 14 649 1124 O ATOM 4828 CB ILE B 182 -65.249 90.683-393.227 1.00 57.70 C ANISOU 4828 CB ILE B 182 7433 7809 6683 38 727 1091 C ATOM 4829 CG1 ILE B 182 -66.440 89.976-392.572 1.00 64.28 C ANISOU 4829 CG1 ILE B 182 8221 8757 7444 96 808 1122 C ATOM 4830 CG2 ILE B 182 -63.980 89.872-393.068 1.00 57.37 C ANISOU 4830 CG2 ILE B 182 7584 7555 6659 9 681 1078 C ATOM 4831 CD1 ILE B 182 -66.927 88.755-393.340 1.00 64.42 C ANISOU 4831 CD1 ILE B 182 8239 8839 7398 66 888 1086 C ATOM 4832 N THR B 183 -62.806 92.916-393.013 1.00 56.76 N ANISOU 4832 N THR B 183 7379 7416 6772 6 517 1246 N ATOM 4833 CA THR B 183 -61.785 93.694-393.721 1.00 57.16 C ANISOU 4833 CA THR B 183 7436 7389 6895 -38 479 1291 C ATOM 4834 C THR B 183 -60.563 92.861-394.126 1.00 56.87 C ANISOU 4834 C THR B 183 7560 7169 6880 -136 455 1242 C ATOM 4835 O THR B 183 -59.897 92.257-393.279 1.00 59.89 O ANISOU 4835 O THR B 183 8089 7379 7287 -156 383 1281 O ATOM 4836 CB THR B 183 -61.308 94.881-392.880 1.00 55.56 C ANISOU 4836 CB THR B 183 7190 7124 6795 9 377 1481 C ATOM 4837 OG1 THR B 183 -62.348 95.860-392.803 1.00 57.42 O ANISOU 4837 OG1 THR B 183 7245 7549 7024 106 412 1524 O ATOM 4838 CG2 THR B 183 -60.081 95.496-393.508 1.00 55.97 C ANISOU 4838 CG2 THR B 183 7275 7062 6930 -42 341 1571 C ATOM 4839 N LEU B 184 -60.250 92.860-395.419 1.00 54.86 N ANISOU 4839 N LEU B 184 7291 6944 6611 -195 507 1160 N ATOM 4840 CA LEU B 184 -59.246 91.946-395.963 1.00 54.55 C ANISOU 4840 CA LEU B 184 7375 6767 6584 -294 504 1081 C ATOM 4841 C LEU B 184 -57.834 92.519-396.026 1.00 56.38 C ANISOU 4841 C LEU B 184 7673 6827 6922 -363 442 1186 C ATOM 4842 O LEU B 184 -57.620 93.603-396.562 1.00 55.03 O ANISOU 4842 O LEU B 184 7425 6700 6785 -350 456 1267 O ATOM 4843 CB LEU B 184 -59.670 91.484-397.358 1.00 56.44 C ANISOU 4843 CB LEU B 184 7566 7128 6750 -335 582 933 C ATOM 4844 CG LEU B 184 -60.934 90.629-397.455 1.00 54.71 C ANISOU 4844 CG LEU B 184 7295 7055 6438 -302 633 849 C ATOM 4845 CD1 LEU B 184 -61.166 90.219-398.895 1.00 57.44 C ANISOU 4845 CD1 LEU B 184 7609 7489 6727 -365 663 734 C ATOM 4846 CD2 LEU B 184 -60.845 89.401-396.560 1.00 55.39 C ANISOU 4846 CD2 LEU B 184 7481 7051 6515 -284 630 848 C ATOM 4847 N GLY B 185 -56.869 91.777-395.495 1.00 56.62 N ANISOU 4847 N GLY B 185 7856 6656 7000 -430 377 1200 N ATOM 4848 CA GLY B 185 -55.472 92.156-395.602 1.00 61.35 C ANISOU 4848 CA GLY B 185 8529 7073 7708 -525 314 1305 C ATOM 4849 C GLY B 185 -54.759 91.353-396.677 1.00 53.07 C ANISOU 4849 C GLY B 185 7531 5977 6655 -632 371 1164 C ATOM 4850 O GLY B 185 -55.324 91.108-397.741 1.00 56.89 O ANISOU 4850 O GLY B 185 7933 6616 7065 -629 461 1023 O ATOM 4851 N LYS B 186 -53.527 90.928-396.398 1.00 73.60 N ANISOU 4851 N LYS B 186 10271 8357 9337 -733 303 1206 N ATOM 4852 CA LYS B 186 -52.716 90.212-397.383 1.00 69.10 C ANISOU 4852 CA LYS B 186 9739 7730 8784 -846 352 1082 C ATOM 4853 C LYS B 186 -52.763 88.702-397.192 1.00 67.50 C ANISOU 4853 C LYS B 186 9648 7467 8531 -844 359 933 C ATOM 4854 O LYS B 186 -53.274 88.211-396.192 1.00 68.23 O ANISOU 4854 O LYS B 186 9827 7523 8574 -755 323 949 O ATOM 4855 CB LYS B 186 -51.255 90.656-397.308 1.00 75.72 C ANISOU 4855 CB LYS B 186 10655 8360 9756 -972 285 1229 C ATOM 4856 CG LYS B 186 -50.998 91.962-396.575 1.00 82.84 C ANISOU 4856 CG LYS B 186 11530 9201 10745 -951 197 1496 C ATOM 4857 CD LYS B 186 -49.516 92.317-396.664 1.00 90.18 C ANISOU 4857 CD LYS B 186 12525 9925 11815 -1098 138 1665 C ATOM 4858 CE LYS B 186 -49.033 93.117-395.463 1.00 79.95 C ANISOU 4858 CE LYS B 186 11287 8461 10631 -1107 -29 1966 C ATOM 4859 NZ LYS B 186 -47.549 93.279-395.499 1.00 64.62 N ANISOU 4859 NZ LYS B 186 9430 6288 8834 -1276 -105 2147 N ATOM 4860 N ILE B 187 -52.215 87.968-398.154 1.00 59.24 N ANISOU 4860 N ILE B 187 8602 6412 7496 -929 410 800 N ATOM 4861 CA ILE B 187 -52.107 86.522-398.043 1.00 60.38 C ANISOU 4861 CA ILE B 187 8846 6489 7607 -918 421 681 C ATOM 4862 C ILE B 187 -50.946 86.198-397.117 1.00 59.73 C ANISOU 4862 C ILE B 187 8977 6117 7599 -973 324 763 C ATOM 4863 O ILE B 187 -49.808 86.540-397.425 1.00 58.59 O ANISOU 4863 O ILE B 187 8865 5840 7558 -1108 291 809 O ATOM 4864 CB ILE B 187 -51.838 85.885-399.405 1.00 55.50 C ANISOU 4864 CB ILE B 187 8140 5956 6991 -997 491 524 C ATOM 4865 CG1 ILE B 187 -52.919 86.282-400.397 1.00 56.68 C ANISOU 4865 CG1 ILE B 187 8110 6362 7062 -961 552 459 C ATOM 4866 CG2 ILE B 187 -51.813 84.386-399.285 1.00 56.09 C ANISOU 4866 CG2 ILE B 187 8291 5983 7036 -955 507 427 C ATOM 4867 CD1 ILE B 187 -54.282 85.755-400.033 1.00 58.96 C ANISOU 4867 CD1 ILE B 187 8355 6795 7251 -831 575 443 C ATOM 4868 N ILE B 188 -51.218 85.550-395.984 1.00 55.54 N ANISOU 4868 N ILE B 188 8613 5480 7011 -870 276 793 N ATOM 4869 CA ILE B 188 -50.173 85.301-394.988 1.00 55.81 C ANISOU 4869 CA ILE B 188 8903 5208 7096 -911 151 889 C ATOM 4870 C ILE B 188 -49.146 84.347-395.551 1.00 52.05 C ANISOU 4870 C ILE B 188 8514 4595 6668 -1004 170 783 C ATOM 4871 O ILE B 188 -49.481 83.226-395.924 1.00 52.80 O ANISOU 4871 O ILE B 188 8602 4762 6697 -929 255 648 O ATOM 4872 CB ILE B 188 -50.702 84.675-393.684 1.00 57.56 C ANISOU 4872 CB ILE B 188 9330 5329 7211 -755 99 930 C ATOM 4873 CG1 ILE B 188 -52.225 84.755-393.610 1.00 53.66 C ANISOU 4873 CG1 ILE B 188 8683 5097 6610 -608 190 904 C ATOM 4874 CG2 ILE B 188 -50.040 85.328-392.469 1.00 59.63 C ANISOU 4874 CG2 ILE B 188 9799 5334 7524 -793 -88 1120 C ATOM 4875 CD1 ILE B 188 -52.818 84.023-392.418 1.00 54.77 C ANISOU 4875 CD1 ILE B 188 9018 5165 6627 -438 176 940 C ATOM 4876 N THR B 189 -47.896 84.792-395.606 1.00 56.62 N ANISOU 4876 N THR B 189 7006 8266 6240 1726 -847 482 N ATOM 4877 CA THR B 189 -46.811 83.963-396.106 1.00 57.50 C ANISOU 4877 CA THR B 189 7254 8227 6365 1628 -947 351 C ATOM 4878 C THR B 189 -45.885 83.532-394.971 1.00 55.62 C ANISOU 4878 C THR B 189 6999 7923 6210 1338 -778 402 C ATOM 4879 O THR B 189 -44.988 82.717-395.167 1.00 58.65 O ANISOU 4879 O THR B 189 7494 8177 6614 1246 -818 312 O ATOM 4880 CB THR B 189 -46.022 84.692-397.202 1.00 58.62 C ANISOU 4880 CB THR B 189 7403 8603 6267 1888 -1152 233 C ATOM 4881 OG1 THR B 189 -46.105 86.101-396.977 1.00 58.94 O ANISOU 4881 OG1 THR B 189 7254 9028 6114 2068 -1118 321 O ATOM 4882 CG2 THR B 189 -46.612 84.391-398.568 1.00 58.60 C ANISOU 4882 CG2 THR B 189 7526 8470 6268 2110 -1396 91 C ATOM 4883 N ASP B 190 -46.116 84.070-393.780 1.00 66.87 N ANISOU 4883 N ASP B 190 8286 9429 7691 1210 -595 546 N ATOM 4884 CA ASP B 190 -45.327 83.690-392.614 1.00 66.62 C ANISOU 4884 CA ASP B 190 8225 9311 7775 937 -457 572 C ATOM 4885 C ASP B 190 -45.989 82.508-391.919 1.00 61.43 C ANISOU 4885 C ASP B 190 7673 8329 7338 753 -362 597 C ATOM 4886 O ASP B 190 -47.023 82.660-391.272 1.00 60.27 O ANISOU 4886 O ASP B 190 7490 8120 7290 717 -253 716 O ATOM 4887 CB ASP B 190 -45.191 84.873-391.646 1.00 71.32 C ANISOU 4887 CB ASP B 190 8612 10129 8359 867 -320 720 C ATOM 4888 CG ASP B 190 -44.238 84.586-390.496 1.00 73.26 C ANISOU 4888 CG ASP B 190 8805 10294 8736 593 -224 704 C ATOM 4889 OD1 ASP B 190 -43.928 83.401-390.264 1.00 80.12 O ANISOU 4889 OD1 ASP B 190 9809 10918 9715 470 -236 598 O ATOM 4890 OD2 ASP B 190 -43.801 85.545-389.821 1.00 73.24 O ANISOU 4890 OD2 ASP B 190 8613 10483 8732 510 -142 795 O ATOM 4891 N SER B 191 -45.397 81.328-392.064 1.00 54.73 N ANISOU 4891 N SER B 191 6955 7296 6545 663 -401 492 N ATOM 4892 CA SER B 191 -45.925 80.132-391.430 1.00 54.72 C ANISOU 4892 CA SER B 191 7044 7028 6719 513 -319 509 C ATOM 4893 C SER B 191 -46.118 80.385-389.949 1.00 60.09 C ANISOU 4893 C SER B 191 7641 7666 7523 344 -168 599 C ATOM 4894 O SER B 191 -46.989 79.797-389.320 1.00 58.67 O ANISOU 4894 O SER B 191 7510 7312 7470 272 -89 652 O ATOM 4895 CB SER B 191 -44.968 78.966-391.621 1.00 59.40 C ANISOU 4895 CB SER B 191 7749 7502 7318 454 -358 407 C ATOM 4896 OG SER B 191 -43.858 79.090-390.754 1.00 54.64 O ANISOU 4896 OG SER B 191 7088 6968 6706 349 -313 356 O ATOM 4897 N GLY B 192 -45.287 81.260-389.395 1.00 54.86 N ANISOU 4897 N GLY B 192 6852 7162 6829 279 -136 611 N ATOM 4898 CA GLY B 192 -45.433 81.691-388.018 1.00 56.15 C ANISOU 4898 CA GLY B 192 6917 7276 7141 105 -7 712 C ATOM 4899 C GLY B 192 -44.923 80.699-386.997 1.00 55.96 C ANISOU 4899 C GLY B 192 6954 7040 7269 -74 18 623 C ATOM 4900 O GLY B 192 -45.418 80.651-385.873 1.00 60.49 O ANISOU 4900 O GLY B 192 7518 7456 8008 -205 106 695 O ATOM 4901 N ILE B 193 -43.925 79.911-387.379 1.00 60.15 N ANISOU 4901 N ILE B 193 7552 7569 7733 -54 -66 464 N ATOM 4902 CA ILE B 193 -43.373 78.911-386.474 1.00 58.48 C ANISOU 4902 CA ILE B 193 7394 7196 7628 -163 -62 354 C ATOM 4903 C ILE B 193 -42.027 78.381-386.943 1.00 56.49 C ANISOU 4903 C ILE B 193 7173 7039 7252 -94 -152 184 C ATOM 4904 O ILE B 193 -41.841 78.096-388.125 1.00 61.67 O ANISOU 4904 O ILE B 193 7909 7762 7760 48 -212 164 O ATOM 4905 CB ILE B 193 -44.341 77.729-386.306 1.00 56.33 C ANISOU 4905 CB ILE B 193 7264 6710 7430 -152 -29 384 C ATOM 4906 CG1 ILE B 193 -43.860 76.798-385.196 1.00 57.07 C ANISOU 4906 CG1 ILE B 193 7398 6661 7626 -234 -30 274 C ATOM 4907 CG2 ILE B 193 -44.503 76.979-387.617 1.00 55.01 C ANISOU 4907 CG2 ILE B 193 7204 6554 7144 -12 -84 371 C ATOM 4908 CD1 ILE B 193 -43.695 77.489-383.868 1.00 59.05 C ANISOU 4908 CD1 ILE B 193 7548 6843 8045 -394 -2 271 C ATOM 4909 N LEU B 194 -41.088 78.259-386.007 1.00 57.44 N ANISOU 4909 N LEU B 194 7230 7156 7438 -183 -168 56 N ATOM 4910 CA LEU B 194 -39.778 77.661-386.274 1.00 58.22 C ANISOU 4910 CA LEU B 194 7358 7351 7413 -89 -247 -126 C ATOM 4911 C LEU B 194 -39.384 76.730-385.137 1.00 57.80 C ANISOU 4911 C LEU B 194 7328 7161 7474 -138 -260 -259 C ATOM 4912 O LEU B 194 -39.266 77.158-383.993 1.00 60.48 O ANISOU 4912 O LEU B 194 7559 7436 7983 -285 -262 -310 O ATOM 4913 CB LEU B 194 -38.704 78.736-386.438 1.00 59.39 C ANISOU 4913 CB LEU B 194 7353 7750 7461 -81 -299 -215 C ATOM 4914 CG LEU B 194 -37.365 78.331-387.059 1.00 59.74 C ANISOU 4914 CG LEU B 194 7436 7959 7302 84 -387 -395 C ATOM 4915 CD1 LEU B 194 -36.411 79.506-387.032 1.00 60.33 C ANISOU 4915 CD1 LEU B 194 7325 8304 7294 74 -433 -489 C ATOM 4916 CD2 LEU B 194 -36.738 77.146-386.356 1.00 61.13 C ANISOU 4916 CD2 LEU B 194 7673 8037 7515 116 -410 -553 C ATOM 4917 N LEU B 195 -39.164 75.459-385.457 1.00 57.95 N ANISOU 4917 N LEU B 195 7479 7138 7401 -3 -277 -312 N ATOM 4918 CA LEU B 195 -38.748 74.481-384.462 1.00 61.14 C ANISOU 4918 CA LEU B 195 7909 7457 7863 23 -307 -454 C ATOM 4919 C LEU B 195 -37.247 74.194-384.558 1.00 59.29 C ANISOU 4919 C LEU B 195 7647 7397 7482 168 -388 -663 C ATOM 4920 O LEU B 195 -36.741 73.786-385.608 1.00 59.35 O ANISOU 4920 O LEU B 195 7736 7523 7292 336 -392 -651 O ATOM 4921 CB LEU B 195 -39.543 73.190-384.628 1.00 63.15 C ANISOU 4921 CB LEU B 195 8307 7589 8099 108 -258 -360 C ATOM 4922 CG LEU B 195 -41.040 73.369-384.862 1.00 60.73 C ANISOU 4922 CG LEU B 195 8041 7153 7881 21 -182 -160 C ATOM 4923 CD1 LEU B 195 -41.729 72.018-384.914 1.00 56.07 C ANISOU 4923 CD1 LEU B 195 7560 6473 7271 103 -139 -93 C ATOM 4924 CD2 LEU B 195 -41.639 74.238-383.775 1.00 61.90 C ANISOU 4924 CD2 LEU B 195 8111 7188 8221 -149 -162 -137 C ATOM 4925 N ALA B 196 -36.536 74.412-383.457 1.00 62.95 N ANISOU 4925 N ALA B 196 7998 7870 8051 113 -461 -860 N ATOM 4926 CA ALA B 196 -35.102 74.175-383.423 1.00 61.73 C ANISOU 4926 CA ALA B 196 7796 7901 7759 272 -552 -1099 C ATOM 4927 C ALA B 196 -34.812 73.083-382.419 1.00 66.63 C ANISOU 4927 C ALA B 196 8447 8442 8426 380 -618 -1274 C ATOM 4928 O ALA B 196 -34.984 71.907-382.715 1.00 61.79 O ANISOU 4928 O ALA B 196 7968 7821 7689 561 -583 -1221 O ATOM 4929 CB ALA B 196 -34.360 75.446-383.051 1.00 62.84 C ANISOU 4929 CB ALA B 196 7734 8171 7971 141 -613 -1231 C ATOM 4930 N GLU B 197 -34.386 73.474-381.223 1.00 65.31 N ANISOU 4930 N GLU B 197 8147 8222 8447 275 -720 -1480 N ATOM 4931 CA GLU B 197 -34.104 72.508-380.174 1.00 70.67 C ANISOU 4931 CA GLU B 197 8847 8821 9183 401 -824 -1690 C ATOM 4932 C GLU B 197 -35.414 71.925-379.687 1.00 67.66 C ANISOU 4932 C GLU B 197 8583 8199 8926 338 -772 -1530 C ATOM 4933 O GLU B 197 -36.480 72.329-380.149 1.00 66.73 O ANISOU 4933 O GLU B 197 8514 7983 8857 190 -654 -1273 O ATOM 4934 CB GLU B 197 -33.379 73.175-379.012 1.00 71.47 C ANISOU 4934 CB GLU B 197 8765 8883 9507 274 -975 -1966 C ATOM 4935 CG GLU B 197 -32.190 74.031-379.406 1.00 70.34 C ANISOU 4935 CG GLU B 197 8457 8989 9281 275 -1024 -2121 C ATOM 4936 CD GLU B 197 -32.605 75.377-379.965 1.00 71.35 C ANISOU 4936 CD GLU B 197 8489 9152 9469 27 -922 -1901 C ATOM 4937 OE1 GLU B 197 -31.735 76.080-380.516 1.00 71.51 O ANISOU 4937 OE1 GLU B 197 8389 9421 9359 56 -941 -1982 O ATOM 4938 OE2 GLU B 197 -33.800 75.727-379.855 1.00 68.95 O ANISOU 4938 OE2 GLU B 197 8227 8651 9319 -167 -825 -1652 O ATOM 4939 N ILE B 198 -35.340 70.980-378.754 1.00 71.16 N ANISOU 4939 N ILE B 198 9068 8566 9402 481 -870 -1698 N ATOM 4940 CA ILE B 198 -36.555 70.412-378.177 1.00 78.96 C ANISOU 4940 CA ILE B 198 10166 9341 10493 448 -842 -1578 C ATOM 4941 C ILE B 198 -36.827 70.995-376.791 1.00 77.96 C ANISOU 4941 C ILE B 198 9980 8954 10688 249 -958 -1706 C ATOM 4942 O ILE B 198 -37.945 70.916-376.280 1.00 75.83 O ANISOU 4942 O ILE B 198 9795 8468 10549 154 -925 -1578 O ATOM 4943 CB ILE B 198 -36.524 68.864-378.149 1.00 81.23 C ANISOU 4943 CB ILE B 198 10566 9727 10572 772 -858 -1622 C ATOM 4944 CG1 ILE B 198 -36.430 68.310-379.573 1.00 81.04 C ANISOU 4944 CG1 ILE B 198 10608 9908 10277 921 -714 -1419 C ATOM 4945 CG2 ILE B 198 -37.772 68.306-377.478 1.00 74.09 C ANISOU 4945 CG2 ILE B 198 9763 8629 9760 753 -845 -1524 C ATOM 4946 CD1 ILE B 198 -37.629 68.645-380.456 1.00 66.69 C ANISOU 4946 CD1 ILE B 198 8851 7999 8489 738 -555 -1099 C ATOM 4947 N GLU B 199 -35.810 71.602-376.192 1.00120.33 N ANISOU 4947 N GLU B 199 15195 14333 16191 182 -1096 -1957 N ATOM 4948 CA GLU B 199 -36.022 72.330-374.949 1.00126.94 C ANISOU 4948 CA GLU B 199 15952 14892 17389 -67 -1203 -2050 C ATOM 4949 C GLU B 199 -37.091 73.392-375.187 1.00118.83 C ANISOU 4949 C GLU B 199 14918 13719 16514 -368 -1038 -1720 C ATOM 4950 O GLU B 199 -37.850 73.749-374.284 1.00121.62 O ANISOU 4950 O GLU B 199 15294 13785 17131 -550 -1054 -1652 O ATOM 4951 CB GLU B 199 -34.725 72.973-374.445 1.00138.95 C ANISOU 4951 CB GLU B 199 17265 16477 19053 -137 -1364 -2350 C ATOM 4952 CG GLU B 199 -33.963 73.792-375.475 1.00134.59 C ANISOU 4952 CG GLU B 199 16575 16209 18353 -185 -1278 -2303 C ATOM 4953 CD GLU B 199 -32.765 73.054-376.047 1.00137.04 C ANISOU 4953 CD GLU B 199 16882 16834 18354 153 -1346 -2533 C ATOM 4954 OE1 GLU B 199 -31.719 73.701-376.277 1.00132.77 O ANISOU 4954 OE1 GLU B 199 16175 16495 17777 140 -1398 -2694 O ATOM 4955 OE2 GLU B 199 -32.869 71.828-376.266 1.00135.02 O ANISOU 4955 OE2 GLU B 199 16782 16640 17878 447 -1341 -2542 O ATOM 4956 N ASN B 200 -37.146 73.884-376.418 1.00110.63 N ANISOU 4956 N ASN B 200 13855 12884 15294 -389 -886 -1516 N ATOM 4957 CA ASN B 200 -38.147 74.859-376.809 1.00110.96 C ANISOU 4957 CA ASN B 200 13887 12857 15416 -601 -727 -1203 C ATOM 4958 C ASN B 200 -39.305 74.221-377.564 1.00105.28 C ANISOU 4958 C ASN B 200 13344 12132 14524 -487 -595 -971 C ATOM 4959 O ASN B 200 -40.310 74.869-377.821 1.00104.06 O ANISOU 4959 O ASN B 200 13206 11908 14424 -611 -473 -725 O ATOM 4960 CB ASN B 200 -37.508 75.954-377.664 1.00107.87 C ANISOU 4960 CB ASN B 200 13335 12707 14945 -687 -668 -1142 C ATOM 4961 CG ASN B 200 -36.405 76.690-376.942 1.00112.93 C ANISOU 4961 CG ASN B 200 13760 13381 15769 -828 -788 -1359 C ATOM 4962 OD1 ASN B 200 -36.184 76.477-375.757 1.00111.69 O ANISOU 4962 OD1 ASN B 200 13569 13019 15849 -897 -922 -1549 O ATOM 4963 ND2 ASN B 200 -35.701 77.566-377.661 1.00116.71 N ANISOU 4963 ND2 ASN B 200 14083 14123 16140 -864 -756 -1347 N ATOM 4964 N ALA B 201 -39.146 72.946-377.903 1.00 91.29 N ANISOU 4964 N ALA B 201 11688 10452 12547 -239 -621 -1051 N ATOM 4965 CA ALA B 201 -40.132 72.177-378.667 1.00 91.35 C ANISOU 4965 CA ALA B 201 11838 10481 12391 -122 -507 -853 C ATOM 4966 C ALA B 201 -41.530 72.798-378.773 1.00 82.57 C ANISOU 4966 C ALA B 201 10766 9228 11379 -274 -387 -598 C ATOM 4967 O ALA B 201 -41.761 73.706-379.567 1.00 77.73 O ANISOU 4967 O ALA B 201 10096 8694 10742 -366 -300 -440 O ATOM 4968 CB ALA B 201 -40.231 70.754-378.118 1.00 98.93 C ANISOU 4968 CB ALA B 201 12907 11411 13270 93 -573 -966 C ATOM 4969 N GLU B 202 -42.461 72.291-377.972 1.00123.51 N ANISOU 4969 N GLU B 202 16052 14226 16651 -263 -390 -570 N ATOM 4970 CA GLU B 202 -43.850 72.739-378.027 1.00123.92 C ANISOU 4970 CA GLU B 202 16160 14157 16767 -352 -275 -342 C ATOM 4971 C GLU B 202 -44.043 74.125-377.411 1.00119.42 C ANISOU 4971 C GLU B 202 15502 13443 16428 -580 -247 -252 C ATOM 4972 O GLU B 202 -45.153 74.652-377.380 1.00119.07 O ANISOU 4972 O GLU B 202 15495 13306 16441 -642 -144 -52 O ATOM 4973 CB GLU B 202 -44.778 71.713-377.359 1.00126.31 C ANISOU 4973 CB GLU B 202 16606 14328 17059 -234 -290 -349 C ATOM 4974 CG GLU B 202 -44.276 71.204-376.017 1.00131.74 C ANISOU 4974 CG GLU B 202 17328 14865 17864 -186 -451 -580 C ATOM 4975 CD GLU B 202 -44.202 72.300-374.971 1.00140.60 C ANISOU 4975 CD GLU B 202 18398 15741 19283 -408 -504 -603 C ATOM 4976 OE1 GLU B 202 -45.251 72.631-374.378 1.00139.19 O ANISOU 4976 OE1 GLU B 202 18301 15353 19232 -482 -457 -472 O ATOM 4977 OE2 GLU B 202 -43.094 72.826-374.739 1.00136.81 O ANISOU 4977 OE2 GLU B 202 17789 15279 18913 -505 -590 -747 O ATOM 4978 N ALA B 203 -42.959 74.713-376.924 1.00 67.15 N ANISOU 4978 N ALA B 203 8754 6822 9939 -695 -333 -393 N ATOM 4979 CA ALA B 203 -43.017 76.055-376.366 1.00 66.56 C ANISOU 4979 CA ALA B 203 8555 6635 10100 -934 -296 -283 C ATOM 4980 C ALA B 203 -43.140 77.080-377.481 1.00 66.39 C ANISOU 4980 C ALA B 203 8428 6835 9964 -976 -167 -79 C ATOM 4981 O ALA B 203 -43.600 78.195-377.263 1.00 67.46 O ANISOU 4981 O ALA B 203 8475 6926 10230 -1127 -76 116 O ATOM 4982 CB ALA B 203 -41.790 76.336-375.525 1.00 69.08 C ANISOU 4982 CB ALA B 203 8737 6900 10609 -1052 -442 -515 C ATOM 4983 N ALA B 204 -42.714 76.701-378.678 1.00 66.23 N ANISOU 4983 N ALA B 204 8415 7057 9693 -824 -166 -119 N ATOM 4984 CA ALA B 204 -42.907 77.540-379.845 1.00 64.14 C ANISOU 4984 CA ALA B 204 8082 7004 9285 -804 -75 49 C ATOM 4985 C ALA B 204 -44.262 77.199-380.429 1.00 62.57 C ANISOU 4985 C ALA B 204 8014 6769 8992 -698 16 222 C ATOM 4986 O ALA B 204 -44.915 78.035-381.042 1.00 65.64 O ANISOU 4986 O ALA B 204 8359 7250 9331 -690 100 403 O ATOM 4987 CB ALA B 204 -41.821 77.292-380.859 1.00 66.73 C ANISOU 4987 CB ALA B 204 8378 7576 9402 -679 -136 -85 C ATOM 4988 N MET B 205 -44.675 75.954-380.224 1.00 65.36 N ANISOU 4988 N MET B 205 8511 7011 9311 -596 -11 155 N ATOM 4989 CA MET B 205 -45.980 75.482-380.663 1.00 61.71 C ANISOU 4989 CA MET B 205 8161 6511 8774 -497 63 287 C ATOM 4990 C MET B 205 -47.063 76.090-379.789 1.00 63.82 C ANISOU 4990 C MET B 205 8453 6602 9193 -576 138 432 C ATOM 4991 O MET B 205 -48.248 75.955-380.073 1.00 58.66 O ANISOU 4991 O MET B 205 7873 5930 8486 -492 209 552 O ATOM 4992 CB MET B 205 -46.050 73.958-380.570 1.00 61.44 C ANISOU 4992 CB MET B 205 8248 6437 8660 -367 16 177 C ATOM 4993 CG MET B 205 -45.085 73.232-381.480 1.00 59.50 C ANISOU 4993 CG MET B 205 7997 6360 8249 -258 -32 78 C ATOM 4994 SD MET B 205 -45.625 73.330-383.185 1.00 56.04 S ANISOU 4994 SD MET B 205 7565 6064 7663 -184 25 224 S ATOM 4995 CE MET B 205 -47.205 72.505-383.058 1.00 57.47 C ANISOU 4995 CE MET B 205 7840 6141 7854 -124 89 325 C ATOM 4996 N THR B 206 -46.649 76.753-378.719 1.00 65.73 N ANISOU 4996 N THR B 206 8630 6710 9635 -735 119 420 N ATOM 4997 CA THR B 206 -47.582 77.333-377.768 1.00 63.39 C ANISOU 4997 CA THR B 206 8368 6204 9512 -821 192 576 C ATOM 4998 C THR B 206 -47.207 78.778-377.490 1.00 65.36 C ANISOU 4998 C THR B 206 8446 6475 9913 -1003 251 716 C ATOM 4999 O THR B 206 -47.076 79.200-376.341 1.00 73.85 O ANISOU 4999 O THR B 206 9491 7333 11235 -1171 239 740 O ATOM 5000 CB THR B 206 -47.610 76.527-376.461 1.00 70.10 C ANISOU 5000 CB THR B 206 9338 6782 10515 -841 97 437 C ATOM 5001 OG1 THR B 206 -47.946 75.164-376.754 1.00 67.71 O ANISOU 5001 OG1 THR B 206 9169 6518 10038 -649 52 324 O ATOM 5002 CG2 THR B 206 -48.636 77.098-375.489 1.00 75.64 C ANISOU 5002 CG2 THR B 206 10110 7233 11395 -915 172 614 C ATOM 5003 N ALA B 207 -47.015 79.534-378.560 1.00 64.83 N ANISOU 5003 N ALA B 207 8258 6675 9700 -964 306 809 N ATOM 5004 CA ALA B 207 -46.740 80.950-378.443 1.00 66.69 C ANISOU 5004 CA ALA B 207 8303 7009 10028 -1100 384 979 C ATOM 5005 C ALA B 207 -48.022 81.697-378.731 1.00 68.51 C ANISOU 5005 C ALA B 207 8542 7293 10196 -1006 535 1259 C ATOM 5006 O ALA B 207 -48.709 81.392-379.700 1.00 66.41 O ANISOU 5006 O ALA B 207 8351 7160 9723 -803 552 1274 O ATOM 5007 CB ALA B 207 -45.670 81.359-379.422 1.00 64.96 C ANISOU 5007 CB ALA B 207 7936 7095 9651 -1071 335 893 C ATOM 5008 N VAL B 208 -48.347 82.671-377.891 1.00 80.81 N ANISOU 5008 N VAL B 208 10016 8746 11942 -1143 644 1481 N ATOM 5009 CA VAL B 208 -49.575 83.433-378.057 1.00 82.86 C ANISOU 5009 CA VAL B 208 10281 9067 12136 -1022 804 1770 C ATOM 5010 C VAL B 208 -49.818 83.776-379.522 1.00 75.60 C ANISOU 5010 C VAL B 208 9302 8506 10918 -786 820 1799 C ATOM 5011 O VAL B 208 -50.899 83.535-380.048 1.00 70.45 O ANISOU 5011 O VAL B 208 8755 7895 10117 -571 857 1847 O ATOM 5012 CB VAL B 208 -49.563 84.719-377.214 1.00 94.14 C ANISOU 5012 CB VAL B 208 11547 10444 13777 -1207 939 2053 C ATOM 5013 CG1 VAL B 208 -49.610 84.378-375.734 1.00 93.46 C ANISOU 5013 CG1 VAL B 208 11561 9933 14017 -1417 916 2047 C ATOM 5014 CG2 VAL B 208 -48.330 85.555-377.534 1.00 73.00 C ANISOU 5014 CG2 VAL B 208 8610 8019 11109 -1341 917 2044 C ATOM 5015 N ASP B 209 -48.803 84.318-380.183 1.00 86.29 N ANISOU 5015 N ASP B 209 10487 10117 12182 -810 771 1745 N ATOM 5016 CA ASP B 209 -48.934 84.735-381.574 1.00 82.99 C ANISOU 5016 CA ASP B 209 10010 10037 11485 -573 754 1757 C ATOM 5017 C ASP B 209 -49.309 83.575-382.500 1.00 74.95 C ANISOU 5017 C ASP B 209 9170 9000 10309 -391 645 1559 C ATOM 5018 O ASP B 209 -50.232 83.689-383.302 1.00 73.06 O ANISOU 5018 O ASP B 209 8967 8880 9912 -167 659 1614 O ATOM 5019 CB ASP B 209 -47.654 85.433-382.043 1.00 93.00 C ANISOU 5019 CB ASP B 209 11080 11575 12680 -629 698 1700 C ATOM 5020 CG ASP B 209 -47.480 86.809-381.416 1.00105.45 C ANISOU 5020 CG ASP B 209 12425 13278 14364 -760 830 1961 C ATOM 5021 OD1 ASP B 209 -48.156 87.761-381.860 1.00107.29 O ANISOU 5021 OD1 ASP B 209 12562 13748 14454 -585 935 2191 O ATOM 5022 OD2 ASP B 209 -46.663 86.940-380.478 1.00104.93 O ANISOU 5022 OD2 ASP B 209 12257 13083 14529 -1029 827 1936 O ATOM 5023 N PHE B 210 -48.602 82.458-382.385 1.00 68.11 N ANISOU 5023 N PHE B 210 8399 7990 9488 -477 536 1331 N ATOM 5024 CA PHE B 210 -48.917 81.280-383.191 1.00 63.05 C ANISOU 5024 CA PHE B 210 7911 7318 8729 -336 450 1175 C ATOM 5025 C PHE B 210 -50.297 80.742-382.846 1.00 63.17 C ANISOU 5025 C PHE B 210 8059 7167 8774 -254 512 1243 C ATOM 5026 O PHE B 210 -51.190 80.718-383.689 1.00 63.85 O ANISOU 5026 O PHE B 210 8176 7351 8733 -66 513 1272 O ATOM 5027 CB PHE B 210 -47.867 80.192-382.980 1.00 61.91 C ANISOU 5027 CB PHE B 210 7829 7068 8625 -431 346 955 C ATOM 5028 CG PHE B 210 -48.076 78.966-383.823 1.00 58.06 C ANISOU 5028 CG PHE B 210 7473 6564 8023 -304 274 832 C ATOM 5029 CD1 PHE B 210 -48.031 79.042-385.203 1.00 56.56 C ANISOU 5029 CD1 PHE B 210 7274 6546 7669 -160 215 807 C ATOM 5030 CD2 PHE B 210 -48.281 77.730-383.233 1.00 59.67 C ANISOU 5030 CD2 PHE B 210 7801 6582 8290 -324 258 745 C ATOM 5031 CE1 PHE B 210 -48.205 77.909-385.979 1.00 58.78 C ANISOU 5031 CE1 PHE B 210 7661 6785 7887 -75 154 719 C ATOM 5032 CE2 PHE B 210 -48.453 76.593-384.004 1.00 59.22 C ANISOU 5032 CE2 PHE B 210 7834 6531 8136 -221 211 666 C ATOM 5033 CZ PHE B 210 -48.415 76.683-385.378 1.00 58.56 C ANISOU 5033 CZ PHE B 210 7734 6591 7926 -115 165 664 C ATOM 5034 N GLN B 211 -50.463 80.315-381.597 1.00 61.15 N ANISOU 5034 N GLN B 211 7882 6666 8688 -379 546 1248 N ATOM 5035 CA GLN B 211 -51.724 79.760-381.119 1.00 60.90 C ANISOU 5035 CA GLN B 211 7990 6472 8677 -294 601 1298 C ATOM 5036 C GLN B 211 -52.901 80.667-381.443 1.00 61.43 C ANISOU 5036 C GLN B 211 8025 6655 8660 -129 711 1499 C ATOM 5037 O GLN B 211 -54.035 80.209-381.533 1.00 61.41 O ANISOU 5037 O GLN B 211 8122 6617 8593 24 739 1509 O ATOM 5038 CB GLN B 211 -51.657 79.503-379.612 1.00 61.19 C ANISOU 5038 CB GLN B 211 8103 6224 8921 -449 615 1300 C ATOM 5039 CG GLN B 211 -50.938 78.222-379.235 1.00 62.74 C ANISOU 5039 CG GLN B 211 8388 6295 9156 -503 490 1065 C ATOM 5040 CD GLN B 211 -51.804 76.997-379.428 1.00 59.78 C ANISOU 5040 CD GLN B 211 8158 5884 8670 -346 470 987 C ATOM 5041 OE1 GLN B 211 -53.008 77.044-379.200 1.00 60.05 O ANISOU 5041 OE1 GLN B 211 8272 5864 8682 -243 543 1091 O ATOM 5042 NE2 GLN B 211 -51.197 75.895-379.845 1.00 59.43 N ANISOU 5042 NE2 GLN B 211 8143 5892 8547 -312 376 813 N ATOM 5043 N ALA B 212 -52.624 81.953-381.618 1.00 62.38 N ANISOU 5043 N ALA B 212 7992 6946 8765 -137 774 1657 N ATOM 5044 CA ALA B 212 -53.667 82.911-381.944 1.00 66.52 C ANISOU 5044 CA ALA B 212 8463 7633 9179 65 883 1863 C ATOM 5045 C ALA B 212 -54.343 82.545-383.252 1.00 65.15 C ANISOU 5045 C ALA B 212 8318 7634 8803 324 804 1749 C ATOM 5046 O ALA B 212 -55.560 82.399-383.309 1.00 60.57 O ANISOU 5046 O ALA B 212 7808 7048 8158 509 848 1788 O ATOM 5047 CB ALA B 212 -53.092 84.301-382.034 1.00 65.11 C ANISOU 5047 CB ALA B 212 8083 7670 8985 33 951 2043 C ATOM 5048 N ASN B 213 -53.546 82.398-384.303 1.00 65.00 N ANISOU 5048 N ASN B 213 8244 7762 8692 341 676 1599 N ATOM 5049 CA ASN B 213 -54.080 82.124-385.626 1.00 57.45 C ANISOU 5049 CA ASN B 213 7301 6948 7579 568 570 1482 C ATOM 5050 C ASN B 213 -54.668 80.731-385.746 1.00 62.23 C ANISOU 5050 C ASN B 213 8045 7383 8218 575 514 1331 C ATOM 5051 O ASN B 213 -55.552 80.495-386.563 1.00 56.18 O ANISOU 5051 O ASN B 213 7291 6687 7369 766 459 1266 O ATOM 5052 CB ASN B 213 -53.015 82.346-386.689 1.00 62.96 C ANISOU 5052 CB ASN B 213 7923 7817 8182 582 438 1369 C ATOM 5053 CG ASN B 213 -52.614 83.789-386.799 1.00 64.18 C ANISOU 5053 CG ASN B 213 7913 8229 8244 652 480 1514 C ATOM 5054 OD1 ASN B 213 -52.389 84.300-387.892 1.00 65.74 O ANISOU 5054 OD1 ASN B 213 8042 8655 8281 831 375 1458 O ATOM 5055 ND2 ASN B 213 -52.534 84.468-385.664 1.00 67.70 N ANISOU 5055 ND2 ASN B 213 8289 8641 8792 517 631 1709 N ATOM 5056 N LEU B 214 -54.184 79.805-384.929 1.00 59.82 N ANISOU 5056 N LEU B 214 7826 6870 8033 379 521 1269 N ATOM 5057 CA LEU B 214 -54.755 78.469-384.919 1.00 60.54 C ANISOU 5057 CA LEU B 214 8030 6830 8141 393 487 1153 C ATOM 5058 C LEU B 214 -56.226 78.555-384.523 1.00 55.29 C ANISOU 5058 C LEU B 214 7415 6145 7449 552 571 1232 C ATOM 5059 O LEU B 214 -57.028 77.691-384.882 1.00 55.26 O ANISOU 5059 O LEU B 214 7459 6129 7407 649 537 1140 O ATOM 5060 CB LEU B 214 -53.987 77.558-383.966 1.00 58.64 C ANISOU 5060 CB LEU B 214 7868 6404 8009 204 481 1083 C ATOM 5061 CG LEU B 214 -52.544 77.253-384.359 1.00 58.66 C ANISOU 5061 CG LEU B 214 7834 6437 8016 85 392 974 C ATOM 5062 CD1 LEU B 214 -51.902 76.332-383.336 1.00 54.64 C ANISOU 5062 CD1 LEU B 214 7399 5763 7597 -44 377 886 C ATOM 5063 CD2 LEU B 214 -52.490 76.635-385.744 1.00 57.56 C ANISOU 5063 CD2 LEU B 214 7692 6393 7786 173 298 880 C ATOM 5064 N LYS B 215 -56.567 79.604-383.779 1.00 57.05 N ANISOU 5064 N LYS B 215 7615 6372 7688 582 689 1412 N ATOM 5065 CA LYS B 215 -57.947 79.874-383.406 1.00 57.75 C ANISOU 5065 CA LYS B 215 7753 6467 7724 776 786 1515 C ATOM 5066 C LYS B 215 -58.624 80.597-384.554 1.00 66.45 C ANISOU 5066 C LYS B 215 8754 7825 8669 1045 757 1523 C ATOM 5067 O LYS B 215 -59.677 80.181-385.031 1.00 65.22 O ANISOU 5067 O LYS B 215 8622 7727 8432 1244 724 1434 O ATOM 5068 CB LYS B 215 -57.999 80.751-382.152 1.00 61.37 C ANISOU 5068 CB LYS B 215 8228 6815 8274 706 934 1742 C ATOM 5069 CG LYS B 215 -57.744 80.028-380.836 1.00 62.26 C ANISOU 5069 CG LYS B 215 8477 6631 8549 511 950 1723 C ATOM 5070 CD LYS B 215 -57.320 81.010-379.738 1.00 65.85 C ANISOU 5070 CD LYS B 215 8904 6949 9166 349 1057 1937 C ATOM 5071 CE LYS B 215 -57.291 80.360-378.352 1.00 66.73 C ANISOU 5071 CE LYS B 215 9174 6727 9452 203 1054 1913 C ATOM 5072 NZ LYS B 215 -56.431 81.093-377.368 1.00 71.04 N ANISOU 5072 NZ LYS B 215 9667 7093 10232 -51 1091 2044 N ATOM 5073 N LYS B 216 -57.993 81.679-384.996 1.00 58.68 N ANISOU 5073 N LYS B 216 7645 7013 7639 1065 755 1611 N ATOM 5074 CA LYS B 216 -58.550 82.567-386.011 1.00 59.30 C ANISOU 5074 CA LYS B 216 7614 7368 7550 1361 717 1630 C ATOM 5075 C LYS B 216 -59.008 81.832-387.257 1.00 61.35 C ANISOU 5075 C LYS B 216 7879 7687 7746 1512 543 1392 C ATOM 5076 O LYS B 216 -60.063 82.130-387.805 1.00 57.65 O ANISOU 5076 O LYS B 216 7375 7367 7164 1804 513 1356 O ATOM 5077 CB LYS B 216 -57.518 83.619-386.397 1.00 59.03 C ANISOU 5077 CB LYS B 216 7441 7521 7465 1332 699 1713 C ATOM 5078 CG LYS B 216 -58.069 84.761-387.221 1.00 63.63 C ANISOU 5078 CG LYS B 216 7897 8429 7849 1678 681 1781 C ATOM 5079 CD LYS B 216 -56.978 85.779-387.514 1.00 64.26 C ANISOU 5079 CD LYS B 216 7832 8722 7863 1646 667 1871 C ATOM 5080 CE LYS B 216 -57.549 87.165-387.784 1.00 66.66 C ANISOU 5080 CE LYS B 216 7988 9371 7967 1983 739 2062 C ATOM 5081 NZ LYS B 216 -56.474 88.166-388.043 1.00 72.36 N ANISOU 5081 NZ LYS B 216 8545 10344 8603 1960 731 2159 N ATOM 5082 N TYR B 217 -58.211 80.877-387.711 1.00 60.51 N ANISOU 5082 N TYR B 217 7807 7463 7720 1321 424 1230 N ATOM 5083 CA TYR B 217 -58.535 80.155-388.928 1.00 55.01 C ANISOU 5083 CA TYR B 217 7104 6786 7011 1415 254 1025 C ATOM 5084 C TYR B 217 -58.954 78.727-388.624 1.00 54.27 C ANISOU 5084 C TYR B 217 7098 6506 7015 1293 257 928 C ATOM 5085 O TYR B 217 -58.861 77.848-389.477 1.00 54.20 O ANISOU 5085 O TYR B 217 7085 6449 7058 1247 133 782 O ATOM 5086 CB TYR B 217 -57.354 80.186-389.892 1.00 54.37 C ANISOU 5086 CB TYR B 217 6987 6740 6932 1334 109 933 C ATOM 5087 CG TYR B 217 -56.896 81.588-390.199 1.00 60.86 C ANISOU 5087 CG TYR B 217 7708 7788 7627 1474 97 1020 C ATOM 5088 CD1 TYR B 217 -57.575 82.374-391.116 1.00 61.54 C ANISOU 5088 CD1 TYR B 217 7714 8092 7577 1798 -5 973 C ATOM 5089 CD2 TYR B 217 -55.791 82.129-389.565 1.00 56.97 C ANISOU 5089 CD2 TYR B 217 7185 7317 7143 1302 179 1140 C ATOM 5090 CE1 TYR B 217 -57.164 83.659-391.396 1.00 57.06 C ANISOU 5090 CE1 TYR B 217 7040 7780 6859 1963 -16 1062 C ATOM 5091 CE2 TYR B 217 -55.369 83.415-389.837 1.00 57.55 C ANISOU 5091 CE2 TYR B 217 7140 7641 7087 1433 177 1233 C ATOM 5092 CZ TYR B 217 -56.059 84.179-390.754 1.00 60.45 C ANISOU 5092 CZ TYR B 217 7431 8245 7294 1773 84 1204 C ATOM 5093 OH TYR B 217 -55.639 85.466-391.029 1.00 59.54 O ANISOU 5093 OH TYR B 217 7182 8425 7014 1940 81 1306 O ATOM 5094 N GLY B 218 -59.416 78.508-387.397 1.00 55.54 N ANISOU 5094 N GLY B 218 7337 6566 7200 1248 400 1023 N ATOM 5095 CA GLY B 218 -59.982 77.235-386.982 1.00 55.38 C ANISOU 5095 CA GLY B 218 7394 6419 7227 1193 414 943 C ATOM 5096 C GLY B 218 -59.310 75.968-387.489 1.00 56.22 C ANISOU 5096 C GLY B 218 7510 6437 7415 1012 319 819 C ATOM 5097 O GLY B 218 -59.960 75.117-388.098 1.00 57.80 O ANISOU 5097 O GLY B 218 7682 6650 7629 1059 254 708 O ATOM 5098 N ILE B 219 -58.012 75.840-387.229 1.00 53.35 N ANISOU 5098 N ILE B 219 7171 5994 7105 813 318 846 N ATOM 5099 CA ILE B 219 -57.263 74.636-387.576 1.00 53.34 C ANISOU 5099 CA ILE B 219 7187 5918 7162 659 256 765 C ATOM 5100 C ILE B 219 -56.400 74.193-386.401 1.00 52.60 C ANISOU 5100 C ILE B 219 7170 5708 7107 499 321 799 C ATOM 5101 O ILE B 219 -56.206 74.959-385.455 1.00 53.39 O ANISOU 5101 O ILE B 219 7298 5765 7222 469 390 878 O ATOM 5102 CB ILE B 219 -56.367 74.844-388.815 1.00 52.72 C ANISOU 5102 CB ILE B 219 7054 5886 7092 627 136 715 C ATOM 5103 CG1 ILE B 219 -55.600 76.162-388.709 1.00 52.24 C ANISOU 5103 CG1 ILE B 219 6963 5901 6983 636 143 780 C ATOM 5104 CG2 ILE B 219 -57.196 74.804-390.084 1.00 54.63 C ANISOU 5104 CG2 ILE B 219 7228 6189 7339 766 21 627 C ATOM 5105 CD1 ILE B 219 -54.783 76.490-389.938 1.00 52.81 C ANISOU 5105 CD1 ILE B 219 6995 6045 7026 657 11 719 C ATOM 5106 N PRO B 220 -55.890 72.949-386.451 1.00 52.56 N ANISOU 5106 N PRO B 220 7191 5656 7125 408 293 741 N ATOM 5107 CA PRO B 220 -55.077 72.377-385.374 1.00 52.32 C ANISOU 5107 CA PRO B 220 7229 5536 7115 304 324 733 C ATOM 5108 C PRO B 220 -53.634 72.828-385.479 1.00 52.09 C ANISOU 5108 C PRO B 220 7180 5507 7105 200 286 721 C ATOM 5109 O PRO B 220 -53.239 73.362-386.515 1.00 55.09 O ANISOU 5109 O PRO B 220 7504 5963 7466 209 232 720 O ATOM 5110 CB PRO B 220 -55.144 70.868-385.641 1.00 53.04 C ANISOU 5110 CB PRO B 220 7322 5645 7186 302 307 687 C ATOM 5111 CG PRO B 220 -56.131 70.679-386.750 1.00 51.94 C ANISOU 5111 CG PRO B 220 7110 5576 7049 374 278 679 C ATOM 5112 CD PRO B 220 -56.144 71.959-387.508 1.00 52.07 C ANISOU 5112 CD PRO B 220 7082 5628 7075 416 231 687 C ATOM 5113 N GLY B 221 -52.853 72.606-384.429 1.00 56.34 N ANISOU 5113 N GLY B 221 7764 5968 7675 122 295 691 N ATOM 5114 CA GLY B 221 -51.455 72.994-384.444 1.00 56.69 C ANISOU 5114 CA GLY B 221 7777 6030 7733 34 253 651 C ATOM 5115 C GLY B 221 -50.553 71.916-385.008 1.00 55.54 C ANISOU 5115 C GLY B 221 7639 5930 7534 37 203 582 C ATOM 5116 O GLY B 221 -49.810 71.276-384.267 1.00 59.79 O ANISOU 5116 O GLY B 221 8209 6438 8069 22 186 510 O ATOM 5117 N VAL B 222 -50.611 71.717-386.320 1.00 52.49 N ANISOU 5117 N VAL B 222 7223 5612 7107 73 172 604 N ATOM 5118 CA VAL B 222 -49.800 70.694-386.970 1.00 51.76 C ANISOU 5118 CA VAL B 222 7143 5556 6969 82 142 584 C ATOM 5119 C VAL B 222 -48.829 71.314-387.975 1.00 51.91 C ANISOU 5119 C VAL B 222 7142 5632 6948 81 77 568 C ATOM 5120 O VAL B 222 -49.245 71.911-388.959 1.00 52.00 O ANISOU 5120 O VAL B 222 7129 5664 6966 109 31 593 O ATOM 5121 CB VAL B 222 -50.680 69.660-387.694 1.00 59.36 C ANISOU 5121 CB VAL B 222 8093 6519 7941 115 158 640 C ATOM 5122 CG1 VAL B 222 -49.840 68.507-388.195 1.00 51.74 C ANISOU 5122 CG1 VAL B 222 7136 5587 6934 123 159 667 C ATOM 5123 CG2 VAL B 222 -51.771 69.155-386.768 1.00 53.31 C ANISOU 5123 CG2 VAL B 222 7341 5732 7183 147 216 646 C ATOM 5124 N VAL B 223 -47.532 71.166-387.731 1.00 54.25 N ANISOU 5124 N VAL B 223 7453 5968 7193 77 56 506 N ATOM 5125 CA VAL B 223 -46.529 71.773-388.597 1.00 54.05 C ANISOU 5125 CA VAL B 223 7419 6018 7100 101 -10 475 C ATOM 5126 C VAL B 223 -45.480 70.760-389.024 1.00 52.28 C ANISOU 5126 C VAL B 223 7242 5825 6796 158 -21 459 C ATOM 5127 O VAL B 223 -45.315 69.727-388.380 1.00 54.41 O ANISOU 5127 O VAL B 223 7533 6091 7051 184 25 454 O ATOM 5128 CB VAL B 223 -45.811 72.927-387.884 1.00 54.67 C ANISOU 5128 CB VAL B 223 7444 6160 7169 61 -26 403 C ATOM 5129 CG1 VAL B 223 -46.824 73.938-387.359 1.00 54.22 C ANISOU 5129 CG1 VAL B 223 7335 6077 7190 12 13 462 C ATOM 5130 CG2 VAL B 223 -44.953 72.387-386.750 1.00 54.08 C ANISOU 5130 CG2 VAL B 223 7375 6076 7098 41 -18 304 C ATOM 5131 N ALA B 224 -44.775 71.056-390.111 1.00 54.78 N ANISOU 5131 N ALA B 224 7583 6186 7045 208 -84 455 N ATOM 5132 CA ALA B 224 -43.653 70.227-390.537 1.00 55.65 C ANISOU 5132 CA ALA B 224 7749 6336 7058 290 -87 452 C ATOM 5133 C ALA B 224 -42.579 70.256-389.457 1.00 53.72 C ANISOU 5133 C ALA B 224 7486 6188 6737 328 -82 323 C ATOM 5134 O ALA B 224 -42.379 71.277-388.803 1.00 53.33 O ANISOU 5134 O ALA B 224 7375 6181 6706 276 -111 228 O ATOM 5135 CB ALA B 224 -43.092 70.723-391.859 1.00 56.47 C ANISOU 5135 CB ALA B 224 7901 6458 7097 353 -174 456 C ATOM 5136 N LEU B 225 -41.888 69.142-389.268 1.00 56.23 N ANISOU 5136 N LEU B 225 7840 6550 6974 427 -48 320 N ATOM 5137 CA LEU B 225 -40.950 69.017-388.163 1.00 57.12 C ANISOU 5137 CA LEU B 225 7925 6754 7024 495 -64 164 C ATOM 5138 C LEU B 225 -39.666 69.818-388.365 1.00 55.74 C ANISOU 5138 C LEU B 225 7734 6703 6743 557 -136 25 C ATOM 5139 O LEU B 225 -39.048 70.255-387.401 1.00 57.02 O ANISOU 5139 O LEU B 225 7828 6926 6910 551 -180 -142 O ATOM 5140 CB LEU B 225 -40.622 67.545-387.931 1.00 57.93 C ANISOU 5140 CB LEU B 225 8063 6910 7038 642 -10 201 C ATOM 5141 CG LEU B 225 -39.571 67.223-386.868 1.00 56.85 C ANISOU 5141 CG LEU B 225 7901 6890 6808 783 -51 11 C ATOM 5142 CD1 LEU B 225 -40.158 67.424-385.484 1.00 58.09 C ANISOU 5142 CD1 LEU B 225 8011 6969 7091 700 -85 -101 C ATOM 5143 CD2 LEU B 225 -39.038 65.803-387.030 1.00 58.86 C ANISOU 5143 CD2 LEU B 225 8195 7263 6908 1004 7 80 C ATOM 5144 N TYR B 226 -39.265 70.010-389.616 1.00 54.75 N ANISOU 5144 N TYR B 226 7666 6610 6527 620 -161 83 N ATOM 5145 CA TYR B 226 -37.983 70.633-389.909 1.00 55.69 C ANISOU 5145 CA TYR B 226 7783 6880 6498 726 -230 -51 C ATOM 5146 C TYR B 226 -38.136 71.878-390.754 1.00 55.37 C ANISOU 5146 C TYR B 226 7730 6862 6446 681 -298 -42 C ATOM 5147 O TYR B 226 -38.889 71.883-391.724 1.00 58.46 O ANISOU 5147 O TYR B 226 8182 7149 6883 660 -308 88 O ATOM 5148 CB TYR B 226 -37.076 69.644-390.634 1.00 55.84 C ANISOU 5148 CB TYR B 226 7907 6958 6353 926 -210 -9 C ATOM 5149 CG TYR B 226 -36.711 68.449-389.798 1.00 62.04 C ANISOU 5149 CG TYR B 226 8688 7796 7088 1044 -150 -35 C ATOM 5150 CD1 TYR B 226 -36.259 68.605-388.501 1.00 57.61 C ANISOU 5150 CD1 TYR B 226 8038 7320 6533 1063 -191 -242 C ATOM 5151 CD2 TYR B 226 -36.815 67.166-390.306 1.00 59.31 C ANISOU 5151 CD2 TYR B 226 8417 7423 6694 1149 -62 148 C ATOM 5152 CE1 TYR B 226 -35.925 67.521-387.730 1.00 59.39 C ANISOU 5152 CE1 TYR B 226 8258 7611 6695 1218 -167 -295 C ATOM 5153 CE2 TYR B 226 -36.481 66.073-389.540 1.00 59.10 C ANISOU 5153 CE2 TYR B 226 8374 7494 6587 1304 -8 131 C ATOM 5154 CZ TYR B 226 -36.035 66.260-388.252 1.00 59.34 C ANISOU 5154 CZ TYR B 226 8326 7620 6602 1356 -72 -107 C ATOM 5155 OH TYR B 226 -35.695 65.181-387.471 1.00 61.26 O ANISOU 5155 OH TYR B 226 8551 7976 6748 1556 -48 -156 O ATOM 5156 N PRO B 227 -37.412 72.943-390.395 1.00 57.63 N ANISOU 5156 N PRO B 227 7926 7301 6670 681 -358 -192 N ATOM 5157 CA PRO B 227 -37.478 74.171-391.189 1.00 55.37 C ANISOU 5157 CA PRO B 227 7611 7098 6328 684 -429 -187 C ATOM 5158 C PRO B 227 -37.144 73.810-392.621 1.00 55.88 C ANISOU 5158 C PRO B 227 7826 7145 6262 843 -483 -130 C ATOM 5159 O PRO B 227 -36.313 72.929-392.822 1.00 58.09 O ANISOU 5159 O PRO B 227 8196 7440 6435 973 -467 -148 O ATOM 5160 CB PRO B 227 -36.363 75.033-390.596 1.00 58.12 C ANISOU 5160 CB PRO B 227 7836 7667 6581 707 -476 -371 C ATOM 5161 CG PRO B 227 -36.141 74.489-389.221 1.00 57.94 C ANISOU 5161 CG PRO B 227 7742 7608 6665 633 -434 -467 C ATOM 5162 CD PRO B 227 -36.427 73.024-389.306 1.00 62.45 C ANISOU 5162 CD PRO B 227 8443 8037 7247 704 -376 -383 C ATOM 5163 N GLY B 228 -37.786 74.437-393.596 1.00 54.74 N ANISOU 5163 N GLY B 228 7714 6958 6127 852 -552 -61 N ATOM 5164 CA GLY B 228 -37.473 74.132-394.979 1.00 56.24 C ANISOU 5164 CA GLY B 228 8061 7087 6221 999 -634 -17 C ATOM 5165 C GLY B 228 -38.649 74.074-395.921 1.00 56.85 C ANISOU 5165 C GLY B 228 8197 6968 6434 960 -687 105 C ATOM 5166 O GLY B 228 -39.715 73.586-395.567 1.00 54.73 O ANISOU 5166 O GLY B 228 7891 6558 6346 824 -616 201 O ATOM 5167 N GLU B 229 -38.437 74.564-397.135 1.00 55.35 N ANISOU 5167 N GLU B 229 8101 6776 6152 1099 -830 80 N ATOM 5168 CA GLU B 229 -39.461 74.548-398.166 1.00 58.14 C ANISOU 5168 CA GLU B 229 8514 6934 6641 1093 -930 154 C ATOM 5169 C GLU B 229 -39.791 73.112-398.529 1.00 59.03 C ANISOU 5169 C GLU B 229 8721 6787 6921 1008 -861 307 C ATOM 5170 O GLU B 229 -40.786 72.838-399.182 1.00 60.39 O ANISOU 5170 O GLU B 229 8909 6763 7275 943 -915 380 O ATOM 5171 CB GLU B 229 -38.985 75.295-399.412 1.00 60.32 C ANISOU 5171 CB GLU B 229 8897 7252 6769 1297 -1130 70 C ATOM 5172 CG GLU B 229 -38.299 76.628-399.134 1.00 57.26 C ANISOU 5172 CG GLU B 229 8418 7190 6147 1428 -1191 -77 C ATOM 5173 CD GLU B 229 -36.830 76.473-398.776 1.00 58.30 C ANISOU 5173 CD GLU B 229 8580 7496 6075 1518 -1145 -159 C ATOM 5174 OE1 GLU B 229 -36.350 75.319-398.680 1.00 61.89 O ANISOU 5174 OE1 GLU B 229 9132 7825 6560 1499 -1055 -96 O ATOM 5175 OE2 GLU B 229 -36.153 77.505-398.590 1.00 57.61 O ANISOU 5175 OE2 GLU B 229 8406 7695 5787 1626 -1198 -286 O ATOM 5176 N LEU B 230 -38.943 72.190-398.105 1.00 61.71 N ANISOU 5176 N LEU B 230 9104 7146 7196 1023 -744 355 N ATOM 5177 CA LEU B 230 -39.191 70.786-398.369 1.00 62.07 C ANISOU 5177 CA LEU B 230 9212 6994 7379 955 -648 538 C ATOM 5178 C LEU B 230 -40.404 70.317-397.598 1.00 60.99 C ANISOU 5178 C LEU B 230 8950 6793 7430 773 -543 611 C ATOM 5179 O LEU B 230 -40.982 69.286-397.919 1.00 56.61 O ANISOU 5179 O LEU B 230 8405 6075 7031 686 -482 770 O ATOM 5180 CB LEU B 230 -37.980 69.945-397.980 1.00 62.95 C ANISOU 5180 CB LEU B 230 9382 7204 7333 1067 -535 571 C ATOM 5181 CG LEU B 230 -37.027 69.589-399.117 1.00 64.83 C ANISOU 5181 CG LEU B 230 9803 7369 7462 1237 -589 638 C ATOM 5182 CD1 LEU B 230 -35.767 68.936-398.574 1.00 59.94 C ANISOU 5182 CD1 LEU B 230 9221 6922 6632 1404 -475 631 C ATOM 5183 CD2 LEU B 230 -37.744 68.678-400.096 1.00 62.09 C ANISOU 5183 CD2 LEU B 230 9528 6724 7341 1137 -582 864 C ATOM 5184 N GLY B 231 -40.782 71.076-396.575 1.00 60.15 N ANISOU 5184 N GLY B 231 8722 6821 7310 717 -519 505 N ATOM 5185 CA GLY B 231 -41.919 70.728-395.743 1.00 59.39 C ANISOU 5185 CA GLY B 231 8522 6680 7364 573 -425 556 C ATOM 5186 C GLY B 231 -43.243 71.006-396.424 1.00 54.11 C ANISOU 5186 C GLY B 231 7823 5874 6862 506 -501 591 C ATOM 5187 O GLY B 231 -44.275 70.469-396.042 1.00 59.30 O ANISOU 5187 O GLY B 231 8414 6460 7656 401 -431 657 O ATOM 5188 N ASP B 232 -43.207 71.850-397.441 1.00 55.10 N ANISOU 5188 N ASP B 232 7994 5980 6961 594 -661 526 N ATOM 5189 CA ASP B 232 -44.406 72.202-398.173 1.00 54.61 C ANISOU 5189 CA ASP B 232 7901 5804 7046 580 -774 516 C ATOM 5190 C ASP B 232 -45.017 70.992-398.856 1.00 56.09 C ANISOU 5190 C ASP B 232 8111 5759 7443 478 -766 642 C ATOM 5191 O ASP B 232 -46.176 71.031-399.270 1.00 57.65 O ANISOU 5191 O ASP B 232 8248 5853 7804 433 -837 630 O ATOM 5192 CB ASP B 232 -44.097 73.278-399.210 1.00 55.79 C ANISOU 5192 CB ASP B 232 8110 5987 7102 745 -980 403 C ATOM 5193 CG ASP B 232 -43.750 74.609-398.577 1.00 55.08 C ANISOU 5193 CG ASP B 232 7944 6163 6820 841 -989 296 C ATOM 5194 OD1 ASP B 232 -43.852 74.714-397.335 1.00 53.50 O ANISOU 5194 OD1 ASP B 232 7646 6076 6605 750 -842 312 O ATOM 5195 OD2 ASP B 232 -43.383 75.546-399.317 1.00 55.33 O ANISOU 5195 OD2 ASP B 232 8010 6293 6721 1010 -1149 200 O ATOM 5196 N LYS B 233 -44.245 69.920-398.979 1.00 61.97 N ANISOU 5196 N LYS B 233 8926 6436 8182 450 -677 767 N ATOM 5197 CA LYS B 233 -44.719 68.723-399.663 1.00 65.44 C ANISOU 5197 CA LYS B 233 9371 6665 8830 339 -648 932 C ATOM 5198 C LYS B 233 -45.561 67.818-398.758 1.00 64.15 C ANISOU 5198 C LYS B 233 9079 6536 8758 208 -479 1029 C ATOM 5199 O LYS B 233 -46.184 66.870-399.227 1.00 67.72 O ANISOU 5199 O LYS B 233 9482 6850 9398 95 -446 1166 O ATOM 5200 CB LYS B 233 -43.544 67.956-400.274 1.00 65.37 C ANISOU 5200 CB LYS B 233 9493 6577 8769 392 -614 1067 C ATOM 5201 CG LYS B 233 -42.941 68.634-401.498 1.00 66.71 C ANISOU 5201 CG LYS B 233 9810 6630 8907 515 -815 996 C ATOM 5202 CD LYS B 233 -41.561 68.081-401.836 1.00 70.94 C ANISOU 5202 CD LYS B 233 10497 7158 9300 628 -759 1103 C ATOM 5203 CE LYS B 233 -41.616 66.623-402.278 1.00 71.16 C ANISOU 5203 CE LYS B 233 10539 6995 9503 519 -634 1379 C ATOM 5204 NZ LYS B 233 -40.261 65.989-402.369 1.00 72.61 N ANISOU 5204 NZ LYS B 233 10855 7228 9504 664 -525 1513 N ATOM 5205 N ILE B 234 -45.589 68.125-397.465 1.00 63.16 N ANISOU 5205 N ILE B 234 8896 6596 8507 224 -382 957 N ATOM 5206 CA ILE B 234 -46.386 67.364-396.511 1.00 60.95 C ANISOU 5206 CA ILE B 234 8512 6368 8278 139 -242 1018 C ATOM 5207 C ILE B 234 -47.855 67.796-396.505 1.00 60.85 C ANISOU 5207 C ILE B 234 8404 6317 8400 80 -296 953 C ATOM 5208 O ILE B 234 -48.169 68.974-396.644 1.00 61.56 O ANISOU 5208 O ILE B 234 8492 6430 8469 139 -406 823 O ATOM 5209 CB ILE B 234 -45.833 67.499-395.087 1.00 59.62 C ANISOU 5209 CB ILE B 234 8334 6378 7939 192 -141 950 C ATOM 5210 CG1 ILE B 234 -44.404 66.968-395.011 1.00 62.49 C ANISOU 5210 CG1 ILE B 234 8776 6814 8154 288 -87 991 C ATOM 5211 CG2 ILE B 234 -46.703 66.745-394.109 1.00 55.09 C ANISOU 5211 CG2 ILE B 234 7674 5851 7405 136 -24 995 C ATOM 5212 CD1 ILE B 234 -43.854 66.917-393.595 1.00 62.69 C ANISOU 5212 CD1 ILE B 234 8778 7003 8039 348 -8 903 C ATOM 5213 N GLU B 235 -48.749 66.827-396.332 1.00 56.07 N ANISOU 5213 N GLU B 235 7707 5685 7911 -10 -214 1045 N ATOM 5214 CA GLU B 235 -50.187 67.084-396.310 1.00 55.74 C ANISOU 5214 CA GLU B 235 7565 5626 7986 -45 -256 977 C ATOM 5215 C GLU B 235 -50.881 66.186-395.298 1.00 59.28 C ANISOU 5215 C GLU B 235 7928 6172 8424 -87 -107 1039 C ATOM 5216 O GLU B 235 -51.100 65.006-395.555 1.00 58.55 O ANISOU 5216 O GLU B 235 7768 6060 8418 -164 -36 1175 O ATOM 5217 CB GLU B 235 -50.800 66.839-397.692 1.00 59.66 C ANISOU 5217 CB GLU B 235 8018 5944 8707 -111 -387 996 C ATOM 5218 CG GLU B 235 -52.262 67.265-397.813 1.00 58.98 C ANISOU 5218 CG GLU B 235 7823 5854 8733 -102 -472 873 C ATOM 5219 CD GLU B 235 -53.085 66.319-398.670 1.00 71.22 C ANISOU 5219 CD GLU B 235 9255 7270 10535 -229 -514 935 C ATOM 5220 OE1 GLU B 235 -53.253 65.142-398.271 1.00 71.28 O ANISOU 5220 OE1 GLU B 235 9183 7323 10576 -332 -363 1083 O ATOM 5221 OE2 GLU B 235 -53.581 66.757-399.730 1.00 73.77 O ANISOU 5221 OE2 GLU B 235 9552 7453 11024 -218 -708 827 O ATOM 5222 N ILE B 236 -51.237 66.752-394.155 1.00 58.61 N ANISOU 5222 N ILE B 236 7843 6195 8232 -30 -61 948 N ATOM 5223 CA ILE B 236 -51.899 65.986-393.111 1.00 60.82 C ANISOU 5223 CA ILE B 236 8067 6570 8473 -33 58 979 C ATOM 5224 C ILE B 236 -53.384 65.777-393.403 1.00 62.11 C ANISOU 5224 C ILE B 236 8119 6724 8755 -59 36 956 C ATOM 5225 O ILE B 236 -54.069 66.694-393.853 1.00 65.45 O ANISOU 5225 O ILE B 236 8524 7106 9237 -22 -67 851 O ATOM 5226 CB ILE B 236 -51.763 66.679-391.745 1.00 62.85 C ANISOU 5226 CB ILE B 236 8379 6905 8595 37 101 889 C ATOM 5227 CG1 ILE B 236 -50.291 66.908-391.400 1.00 67.57 C ANISOU 5227 CG1 ILE B 236 9060 7529 9085 66 108 875 C ATOM 5228 CG2 ILE B 236 -52.433 65.857-390.664 1.00 58.03 C ANISOU 5228 CG2 ILE B 236 7736 6378 7934 64 200 907 C ATOM 5229 CD1 ILE B 236 -49.689 68.131-392.058 1.00 61.98 C ANISOU 5229 CD1 ILE B 236 8395 6788 8368 82 5 808 C ATOM 5230 N GLU B 237 -53.875 64.569-393.149 1.00 56.34 N ANISOU 5230 N GLU B 237 7302 6061 8044 -97 129 1048 N ATOM 5231 CA GLU B 237 -55.305 64.296-393.214 1.00 56.34 C ANISOU 5231 CA GLU B 237 7181 6100 8125 -104 122 1006 C ATOM 5232 C GLU B 237 -55.795 63.962-391.812 1.00 56.60 C ANISOU 5232 C GLU B 237 7222 6281 8002 -14 228 982 C ATOM 5233 O GLU B 237 -55.286 63.039-391.182 1.00 60.67 O ANISOU 5233 O GLU B 237 7744 6891 8417 3 325 1074 O ATOM 5234 CB GLU B 237 -55.595 63.138-394.171 1.00 62.24 C ANISOU 5234 CB GLU B 237 7788 6818 9042 -229 133 1134 C ATOM 5235 CG GLU B 237 -57.083 62.837-394.352 1.00 59.98 C ANISOU 5235 CG GLU B 237 7342 6586 8860 -244 107 1067 C ATOM 5236 CD GLU B 237 -57.355 61.787-395.426 1.00 63.12 C ANISOU 5236 CD GLU B 237 7570 6930 9483 -408 99 1195 C ATOM 5237 OE1 GLU B 237 -57.836 62.154-396.520 1.00 67.76 O ANISOU 5237 OE1 GLU B 237 8091 7367 10289 -477 -51 1113 O ATOM 5238 OE2 GLU B 237 -57.086 60.592-395.177 1.00 68.25 O ANISOU 5238 OE2 GLU B 237 8144 7690 10099 -462 237 1382 O ATOM 5239 N ILE B 238 -56.771 64.720-391.319 1.00 55.16 N ANISOU 5239 N ILE B 238 7050 6124 7786 74 201 859 N ATOM 5240 CA ILE B 238 -57.297 64.505-389.973 1.00 55.50 C ANISOU 5240 CA ILE B 238 7131 6274 7682 178 283 826 C ATOM 5241 C ILE B 238 -58.767 64.106-389.971 1.00 55.84 C ANISOU 5241 C ILE B 238 7063 6415 7737 235 291 773 C ATOM 5242 O ILE B 238 -59.601 64.771-390.580 1.00 55.75 O ANISOU 5242 O ILE B 238 7000 6376 7806 266 214 681 O ATOM 5243 CB ILE B 238 -57.138 65.749-389.094 1.00 56.02 C ANISOU 5243 CB ILE B 238 7329 6289 7667 258 274 746 C ATOM 5244 CG1 ILE B 238 -55.683 66.200-389.068 1.00 53.57 C ANISOU 5244 CG1 ILE B 238 7105 5907 7342 204 258 773 C ATOM 5245 CG2 ILE B 238 -57.610 65.466-387.679 1.00 56.13 C ANISOU 5245 CG2 ILE B 238 7408 6367 7552 362 344 718 C ATOM 5246 CD1 ILE B 238 -55.454 67.460-388.261 1.00 52.89 C ANISOU 5246 CD1 ILE B 238 7114 5772 7209 247 252 716 C ATOM 5247 N VAL B 239 -59.077 63.018-389.276 1.00 58.02 N ANISOU 5247 N VAL B 239 7298 6833 7913 278 374 816 N ATOM 5248 CA VAL B 239 -60.453 62.567-389.132 1.00 58.30 C ANISOU 5248 CA VAL B 239 7227 7005 7919 358 389 755 C ATOM 5249 C VAL B 239 -60.725 62.185-387.678 1.00 56.90 C ANISOU 5249 C VAL B 239 7142 6946 7531 516 458 728 C ATOM 5250 O VAL B 239 -59.908 61.512-387.048 1.00 56.92 O ANISOU 5250 O VAL B 239 7195 6999 7434 533 506 799 O ATOM 5251 CB VAL B 239 -60.754 61.374-390.061 1.00 61.80 C ANISOU 5251 CB VAL B 239 7458 7545 8480 242 405 847 C ATOM 5252 CG1 VAL B 239 -62.121 60.787-389.755 1.00 65.08 C ANISOU 5252 CG1 VAL B 239 7745 8154 8829 339 429 775 C ATOM 5253 CG2 VAL B 239 -60.678 61.803-391.515 1.00 60.31 C ANISOU 5253 CG2 VAL B 239 7185 7196 8534 96 300 841 C ATOM 5254 N SER B 240 -61.869 62.626-387.153 1.00 58.60 N ANISOU 5254 N SER B 240 7388 7207 7669 659 451 616 N ATOM 5255 CA SER B 240 -62.233 62.391-385.755 1.00 60.44 C ANISOU 5255 CA SER B 240 7743 7517 7706 834 494 572 C ATOM 5256 C SER B 240 -63.092 61.149-385.606 1.00 60.64 C ANISOU 5256 C SER B 240 7634 7787 7618 926 533 565 C ATOM 5257 O SER B 240 -63.563 60.596-386.597 1.00 61.39 O ANISOU 5257 O SER B 240 7525 7987 7813 840 530 588 O ATOM 5258 CB SER B 240 -62.999 63.586-385.197 1.00 57.61 C ANISOU 5258 CB SER B 240 7513 7070 7305 968 479 476 C ATOM 5259 OG SER B 240 -64.156 63.843-385.971 1.00 56.33 O ANISOU 5259 OG SER B 240 7227 6985 7189 1024 450 398 O ATOM 5260 N LYS B 241 -63.308 60.717-384.367 1.00 58.78 N ANISOU 5260 N LYS B 241 7507 7644 7181 1105 557 527 N ATOM 5261 CA LYS B 241 -64.157 59.560-384.125 1.00 60.17 C ANISOU 5261 CA LYS B 241 7560 8098 7202 1235 590 510 C ATOM 5262 C LYS B 241 -65.513 59.797-384.764 1.00 66.81 C ANISOU 5262 C LYS B 241 8268 9029 8087 1272 575 414 C ATOM 5263 O LYS B 241 -66.261 58.856-385.043 1.00 65.72 O ANISOU 5263 O LYS B 241 7938 9140 7894 1310 597 404 O ATOM 5264 CB LYS B 241 -64.322 59.297-382.626 1.00 66.63 C ANISOU 5264 CB LYS B 241 8562 8975 7781 1475 583 439 C ATOM 5265 CG LYS B 241 -65.116 58.022-382.311 1.00 73.40 C ANISOU 5265 CG LYS B 241 9292 10171 8427 1650 610 420 C ATOM 5266 CD LYS B 241 -65.635 58.018-380.872 1.00 62.28 C ANISOU 5266 CD LYS B 241 8097 8790 6776 1937 572 298 C ATOM 5267 CE LYS B 241 -66.571 56.841-380.598 1.00 70.01 C ANISOU 5267 CE LYS B 241 8944 10144 7513 2149 590 255 C ATOM 5268 NZ LYS B 241 -67.827 56.929-381.385 1.00 66.45 N ANISOU 5268 NZ LYS B 241 8312 9836 7100 2140 616 195 N ATOM 5269 N ALA B 242 -65.822 61.068-384.993 1.00 84.82 N ANISOU 5269 N ALA B 242 10637 11132 10460 1277 534 339 N ATOM 5270 CA ALA B 242 -67.092 61.463-385.587 1.00 84.49 C ANISOU 5270 CA ALA B 242 10482 11169 10450 1361 500 215 C ATOM 5271 C ALA B 242 -67.176 61.055-387.054 1.00 81.44 C ANISOU 5271 C ALA B 242 9831 10828 10285 1167 455 228 C ATOM 5272 O ALA B 242 -67.910 60.135-387.409 1.00 81.92 O ANISOU 5272 O ALA B 242 9681 11103 10340 1170 461 197 O ATOM 5273 CB ALA B 242 -67.289 62.976-385.445 1.00 86.77 C ANISOU 5273 CB ALA B 242 10935 11272 10763 1451 472 156 C ATOM 5274 N ASP B 243 -66.411 61.740-387.899 1.00 94.75 N ANISOU 5274 N ASP B 243 11523 12306 12172 998 403 273 N ATOM 5275 CA ASP B 243 -66.452 61.505-389.338 1.00 96.55 C ANISOU 5275 CA ASP B 243 11531 12504 12648 812 329 274 C ATOM 5276 C ASP B 243 -65.687 60.241-389.725 1.00 95.61 C ANISOU 5276 C ASP B 243 11277 12437 12614 607 386 456 C ATOM 5277 O ASP B 243 -65.409 60.018-390.903 1.00 94.03 O ANISOU 5277 O ASP B 243 10927 12146 12654 407 333 513 O ATOM 5278 CB ASP B 243 -65.889 62.710-390.107 1.00 95.96 C ANISOU 5278 CB ASP B 243 11531 12193 12736 740 234 251 C ATOM 5279 CG ASP B 243 -66.631 64.009-389.805 1.00 99.76 C ANISOU 5279 CG ASP B 243 12123 12654 13128 965 190 104 C ATOM 5280 OD1 ASP B 243 -67.169 64.629-390.751 1.00102.92 O ANISOU 5280 OD1 ASP B 243 12425 13027 13653 1006 72 -22 O ATOM 5281 OD2 ASP B 243 -66.669 64.420-388.625 1.00 95.72 O ANISOU 5281 OD2 ASP B 243 11795 12150 12424 1116 267 120 O ATOM 5282 N TYR B 244 -65.346 59.415-388.739 1.00 61.95 N ANISOU 5282 N TYR B 244 7067 8319 8152 676 487 551 N ATOM 5283 CA TYR B 244 -64.592 58.196-389.016 1.00 64.66 C ANISOU 5283 CA TYR B 244 7280 8757 8529 534 563 752 C ATOM 5284 C TYR B 244 -65.482 57.049-389.472 1.00 65.51 C ANISOU 5284 C TYR B 244 7095 9122 8672 491 598 785 C ATOM 5285 O TYR B 244 -65.087 56.255-390.324 1.00 67.94 O ANISOU 5285 O TYR B 244 7212 9449 9152 290 634 958 O ATOM 5286 CB TYR B 244 -63.792 57.764-387.793 1.00 68.73 C ANISOU 5286 CB TYR B 244 7960 9351 8803 664 639 831 C ATOM 5287 CG TYR B 244 -63.073 56.440-387.967 1.00 69.16 C ANISOU 5287 CG TYR B 244 7872 9575 8830 592 732 1046 C ATOM 5288 CD1 TYR B 244 -61.927 56.344-388.743 1.00 70.31 C ANISOU 5288 CD1 TYR B 244 8003 9577 9135 410 752 1214 C ATOM 5289 CD2 TYR B 244 -63.535 55.289-387.344 1.00 69.64 C ANISOU 5289 CD2 TYR B 244 7815 9963 8681 738 805 1092 C ATOM 5290 CE1 TYR B 244 -61.266 55.137-388.898 1.00 71.63 C ANISOU 5290 CE1 TYR B 244 8041 9914 9260 375 856 1441 C ATOM 5291 CE2 TYR B 244 -62.880 54.086-387.493 1.00 74.09 C ANISOU 5291 CE2 TYR B 244 8233 10722 9194 706 904 1316 C ATOM 5292 CZ TYR B 244 -61.747 54.015-388.271 1.00 72.66 C ANISOU 5292 CZ TYR B 244 8039 10387 9181 525 937 1500 C ATOM 5293 OH TYR B 244 -61.094 52.815-388.424 1.00 75.23 O ANISOU 5293 OH TYR B 244 8219 10923 9443 521 1055 1752 O ATOM 5294 N ALA B 245 -66.670 56.951-388.885 1.00 72.93 N ANISOU 5294 N ALA B 245 7997 10267 9447 685 594 631 N ATOM 5295 CA ALA B 245 -67.642 55.945-389.298 1.00 75.78 C ANISOU 5295 CA ALA B 245 8054 10906 9832 660 616 626 C ATOM 5296 C ALA B 245 -68.112 56.249-390.714 1.00 74.14 C ANISOU 5296 C ALA B 245 7639 10562 9970 453 513 557 C ATOM 5297 O ALA B 245 -68.179 55.371-391.572 1.00 71.58 O ANISOU 5297 O ALA B 245 7038 10312 9849 244 531 678 O ATOM 5298 CB ALA B 245 -68.818 55.918-388.339 1.00 78.31 C ANISOU 5298 CB ALA B 245 8409 11470 9874 953 617 439 C ATOM 5299 N LYS B 246 -68.435 57.510-390.952 1.00116.78 N ANISOU 5299 N LYS B 246 13168 15760 15442 523 396 365 N ATOM 5300 CA LYS B 246 -68.723 57.973-392.294 1.00119.07 C ANISOU 5300 CA LYS B 246 13308 15873 16061 362 255 268 C ATOM 5301 C LYS B 246 -67.418 58.064-393.068 1.00117.50 C ANISOU 5301 C LYS B 246 13162 15396 16087 115 240 456 C ATOM 5302 O LYS B 246 -67.373 58.636-394.150 1.00113.22 O ANISOU 5302 O LYS B 246 12574 14632 15813 -6 100 383 O ATOM 5303 CB LYS B 246 -69.401 59.339-392.248 1.00114.40 C ANISOU 5303 CB LYS B 246 12853 15189 15426 576 136 13 C ATOM 5304 CG LYS B 246 -70.898 59.274-392.007 1.00120.30 C ANISOU 5304 CG LYS B 246 13467 16190 16051 800 101 -217 C ATOM 5305 CD LYS B 246 -71.515 60.662-392.052 1.00129.58 C ANISOU 5305 CD LYS B 246 14773 17280 17181 1041 -11 -447 C ATOM 5306 CE LYS B 246 -72.957 60.620-392.533 1.00133.02 C ANISOU 5306 CE LYS B 246 14975 17910 17655 1193 -121 -717 C ATOM 5307 NZ LYS B 246 -73.796 59.681-391.742 1.00127.27 N ANISOU 5307 NZ LYS B 246 14144 17518 16694 1332 -21 -751 N ATOM 5308 N GLY B 247 -66.362 57.491-392.498 1.00143.01 N ANISOU 5308 N GLY B 247 16497 18650 19192 72 372 682 N ATOM 5309 CA GLY B 247 -65.024 57.568-393.057 1.00140.56 C ANISOU 5309 CA GLY B 247 16276 18105 19027 -110 379 867 C ATOM 5310 C GLY B 247 -64.957 57.477-394.566 1.00139.27 C ANISOU 5310 C GLY B 247 15938 17737 19242 -365 274 910 C ATOM 5311 O GLY B 247 -64.049 58.030-395.188 1.00138.48 O ANISOU 5311 O GLY B 247 15961 17374 19281 -466 209 963 O ATOM 5312 N ALA B 248 -65.911 56.777-395.163 1.00 76.64 N ANISOU 5312 N ALA B 248 7714 9920 11486 -469 245 879 N ATOM 5313 CA ALA B 248 -65.928 56.639-396.611 1.00 77.34 C ANISOU 5313 CA ALA B 248 7618 9784 11985 -731 120 907 C ATOM 5314 C ALA B 248 -66.623 57.825-397.278 1.00 74.59 C ANISOU 5314 C ALA B 248 7293 9253 11795 -655 -116 587 C ATOM 5315 O ALA B 248 -66.118 58.394-398.250 1.00 76.27 O ANISOU 5315 O ALA B 248 7564 9165 12251 -766 -264 563 O ATOM 5316 CB ALA B 248 -66.616 55.332-397.002 1.00 78.94 C ANISOU 5316 CB ALA B 248 7460 10185 12349 -905 185 1023 C ATOM 5317 N SER B 249 -67.779 58.198-396.737 1.00 90.42 N ANISOU 5317 N SER B 249 9261 11459 13637 -428 -156 336 N ATOM 5318 CA SER B 249 -68.592 59.263-397.310 1.00 92.57 C ANISOU 5318 CA SER B 249 9523 11633 14018 -289 -376 15 C ATOM 5319 C SER B 249 -68.078 60.638-396.906 1.00 91.60 C ANISOU 5319 C SER B 249 9714 11382 13706 -78 -418 -68 C ATOM 5320 O SER B 249 -67.992 61.540-397.736 1.00 92.63 O ANISOU 5320 O SER B 249 9890 11308 13997 -52 -607 -211 O ATOM 5321 CB SER B 249 -70.045 59.103-396.868 1.00 94.79 C ANISOU 5321 CB SER B 249 9636 12213 14167 -89 -387 -215 C ATOM 5322 OG SER B 249 -70.451 57.745-396.943 1.00109.02 O ANISOU 5322 OG SER B 249 11149 14216 16056 -261 -295 -99 O ATOM 5323 N ALA B 250 -67.742 60.788-395.628 1.00104.88 N ANISOU 5323 N ALA B 250 11602 13193 15053 77 -251 20 N ATOM 5324 CA ALA B 250 -67.277 62.064-395.085 1.00101.72 C ANISOU 5324 CA ALA B 250 11482 12702 14466 266 -261 -28 C ATOM 5325 C ALA B 250 -66.380 62.810-396.062 1.00 95.06 C ANISOU 5325 C ALA B 250 10723 11579 13815 162 -398 -16 C ATOM 5326 O ALA B 250 -65.290 62.348-396.400 1.00 93.90 O ANISOU 5326 O ALA B 250 10614 11290 13774 -46 -357 184 O ATOM 5327 CB ALA B 250 -66.552 61.849-393.764 1.00104.78 C ANISOU 5327 CB ALA B 250 12067 13168 14575 315 -67 148 C ATOM 5328 N LEU B 251 -66.848 63.971-396.507 1.00 66.41 N ANISOU 5328 N LEU B 251 7129 7896 10206 344 -564 -231 N ATOM 5329 CA LEU B 251 -66.121 64.761-397.490 1.00 68.05 C ANISOU 5329 CA LEU B 251 7412 7870 10575 303 -732 -263 C ATOM 5330 C LEU B 251 -65.224 65.814-396.845 1.00 67.29 C ANISOU 5330 C LEU B 251 7572 7741 10255 426 -669 -190 C ATOM 5331 O LEU B 251 -65.593 66.984-396.771 1.00 69.98 O ANISOU 5331 O LEU B 251 7982 8129 10479 668 -747 -333 O ATOM 5332 CB LEU B 251 -67.099 65.430-398.454 1.00 67.99 C ANISOU 5332 CB LEU B 251 7274 7839 10721 460 -984 -557 C ATOM 5333 CG LEU B 251 -67.682 64.525-399.533 1.00 70.17 C ANISOU 5333 CG LEU B 251 7281 8032 11347 266 -1130 -646 C ATOM 5334 CD1 LEU B 251 -68.669 65.291-400.396 1.00 70.84 C ANISOU 5334 CD1 LEU B 251 7246 8108 11563 480 -1409 -991 C ATOM 5335 CD2 LEU B 251 -66.559 63.947-400.381 1.00 72.41 C ANISOU 5335 CD2 LEU B 251 7574 8039 11898 -53 -1162 -446 C ATOM 5336 N LEU B 252 -64.044 65.397-396.393 1.00 63.09 N ANISOU 5336 N LEU B 252 7161 7146 9664 269 -528 35 N ATOM 5337 CA LEU B 252 -63.089 66.302-395.762 1.00 59.82 C ANISOU 5337 CA LEU B 252 6965 6702 9063 347 -466 109 C ATOM 5338 C LEU B 252 -62.830 67.544-396.614 1.00 60.14 C ANISOU 5338 C LEU B 252 7062 6636 9153 458 -653 -11 C ATOM 5339 O LEU B 252 -62.635 67.435-397.822 1.00 60.77 O ANISOU 5339 O LEU B 252 7076 6560 9452 366 -822 -61 O ATOM 5340 CB LEU B 252 -61.776 65.570-395.490 1.00 62.09 C ANISOU 5340 CB LEU B 252 7337 6916 9340 153 -341 333 C ATOM 5341 CG LEU B 252 -61.899 64.278-394.688 1.00 61.30 C ANISOU 5341 CG LEU B 252 7176 6948 9168 72 -167 465 C ATOM 5342 CD1 LEU B 252 -60.524 63.722-394.390 1.00 60.11 C ANISOU 5342 CD1 LEU B 252 7124 6749 8966 -49 -56 668 C ATOM 5343 CD2 LEU B 252 -62.666 64.517-393.402 1.00 58.72 C ANISOU 5343 CD2 LEU B 252 6904 6797 8611 262 -69 397 C ATOM 5344 N PRO B 253 -62.836 68.729-395.982 1.00 68.03 N ANISOU 5344 N PRO B 253 8177 7722 9948 666 -627 -50 N ATOM 5345 CA PRO B 253 -62.565 70.000-396.647 1.00 65.47 C ANISOU 5345 CA PRO B 253 7905 7366 9606 823 -785 -147 C ATOM 5346 C PRO B 253 -61.075 70.230-396.644 1.00 63.97 C ANISOU 5346 C PRO B 253 7851 7074 9379 701 -752 -5 C ATOM 5347 O PRO B 253 -60.390 69.644-395.819 1.00 64.84 O ANISOU 5347 O PRO B 253 8033 7180 9423 559 -581 153 O ATOM 5348 CB PRO B 253 -63.220 71.027-395.720 1.00 66.87 C ANISOU 5348 CB PRO B 253 8132 7726 9551 1087 -703 -183 C ATOM 5349 CG PRO B 253 -63.771 70.250-394.546 1.00 66.21 C ANISOU 5349 CG PRO B 253 8052 7728 9375 1052 -510 -109 C ATOM 5350 CD PRO B 253 -63.107 68.924-394.555 1.00 61.66 C ANISOU 5350 CD PRO B 253 7459 7056 8914 773 -441 13 C ATOM 5351 N ILE B 254 -60.577 71.079-397.528 1.00 57.89 N ANISOU 5351 N ILE B 254 7118 6244 8634 784 -922 -77 N ATOM 5352 CA ILE B 254 -59.143 71.318-397.593 1.00 56.96 C ANISOU 5352 CA ILE B 254 7127 6051 8466 690 -904 37 C ATOM 5353 C ILE B 254 -58.773 72.746-397.196 1.00 57.09 C ANISOU 5353 C ILE B 254 7217 6204 8270 886 -901 27 C ATOM 5354 O ILE B 254 -59.158 73.707-397.867 1.00 56.48 O ANISOU 5354 O ILE B 254 7108 6193 8159 1106 -1068 -107 O ATOM 5355 CB ILE B 254 -58.595 71.003-398.989 1.00 60.17 C ANISOU 5355 CB ILE B 254 7532 6258 9070 598 -1100 -3 C ATOM 5356 CG1 ILE B 254 -58.782 69.518-399.298 1.00 61.07 C ANISOU 5356 CG1 ILE B 254 7562 6235 9407 357 -1058 80 C ATOM 5357 CG2 ILE B 254 -57.132 71.407-399.089 1.00 57.78 C ANISOU 5357 CG2 ILE B 254 7372 5912 8670 565 -1096 88 C ATOM 5358 CD1 ILE B 254 -58.550 69.156-400.747 1.00 63.04 C ANISOU 5358 CD1 ILE B 254 7785 6248 9921 257 -1269 37 C ATOM 5359 N TYR B 255 -58.032 72.876-396.097 1.00 55.85 N ANISOU 5359 N TYR B 255 7145 6101 7974 815 -717 168 N ATOM 5360 CA TYR B 255 -57.560 74.173-395.627 1.00 60.96 C ANISOU 5360 CA TYR B 255 7840 6880 8441 950 -685 199 C ATOM 5361 C TYR B 255 -56.132 74.397-396.097 1.00 57.57 C ANISOU 5361 C TYR B 255 7486 6402 7986 877 -745 233 C ATOM 5362 O TYR B 255 -55.328 73.476-396.079 1.00 60.26 O ANISOU 5362 O TYR B 255 7878 6626 8391 689 -695 303 O ATOM 5363 CB TYR B 255 -57.588 74.234-394.100 1.00 58.03 C ANISOU 5363 CB TYR B 255 7508 6576 7965 903 -464 321 C ATOM 5364 CG TYR B 255 -58.908 73.860-393.469 1.00 57.46 C ANISOU 5364 CG TYR B 255 7393 6545 7893 971 -379 304 C ATOM 5365 CD1 TYR B 255 -59.744 74.828-392.933 1.00 54.27 C ANISOU 5365 CD1 TYR B 255 6973 6277 7371 1182 -327 308 C ATOM 5366 CD2 TYR B 255 -59.311 72.541-393.398 1.00 58.38 C ANISOU 5366 CD2 TYR B 255 7484 6587 8111 844 -343 297 C ATOM 5367 CE1 TYR B 255 -60.952 74.490-392.348 1.00 56.64 C ANISOU 5367 CE1 TYR B 255 7251 6622 7648 1274 -250 286 C ATOM 5368 CE2 TYR B 255 -60.512 72.192-392.818 1.00 53.85 C ANISOU 5368 CE2 TYR B 255 6870 6078 7511 927 -272 267 C ATOM 5369 CZ TYR B 255 -61.331 73.169-392.295 1.00 53.94 C ANISOU 5369 CZ TYR B 255 6886 6209 7398 1148 -230 251 C ATOM 5370 OH TYR B 255 -62.532 72.820-391.716 1.00 61.35 O ANISOU 5370 OH TYR B 255 7803 7219 8290 1261 -160 214 O ATOM 5371 N PRO B 256 -55.803 75.624-396.515 1.00 54.42 N ANISOU 5371 N PRO B 256 7089 6121 7468 1055 -849 185 N ATOM 5372 CA PRO B 256 -56.690 76.776-396.649 1.00 55.84 C ANISOU 5372 CA PRO B 256 7196 6479 7541 1331 -918 112 C ATOM 5373 C PRO B 256 -57.186 76.904-398.078 1.00 58.37 C ANISOU 5373 C PRO B 256 7475 6761 7943 1503 -1187 -75 C ATOM 5374 O PRO B 256 -58.059 77.721-398.360 1.00 56.90 O ANISOU 5374 O PRO B 256 7214 6725 7679 1779 -1284 -177 O ATOM 5375 CB PRO B 256 -55.768 77.965-396.344 1.00 55.35 C ANISOU 5375 CB PRO B 256 7150 6588 7294 1415 -884 185 C ATOM 5376 CG PRO B 256 -54.404 77.378-396.078 1.00 54.30 C ANISOU 5376 CG PRO B 256 7101 6347 7184 1175 -815 261 C ATOM 5377 CD PRO B 256 -54.405 76.026-396.685 1.00 54.61 C ANISOU 5377 CD PRO B 256 7183 6164 7404 1016 -873 222 C ATOM 5378 N GLY B 257 -56.615 76.111-398.973 1.00 61.13 N ANISOU 5378 N GLY B 257 7872 6904 8450 1358 -1313 -119 N ATOM 5379 CA GLY B 257 -56.990 76.166-400.371 1.00 58.43 C ANISOU 5379 CA GLY B 257 7504 6463 8233 1491 -1600 -306 C ATOM 5380 C GLY B 257 -58.491 76.258-400.550 1.00 58.89 C ANISOU 5380 C GLY B 257 7439 6583 8354 1669 -1686 -456 C ATOM 5381 O GLY B 257 -59.009 77.278-400.994 1.00 62.83 O ANISOU 5381 O GLY B 257 7887 7244 8743 1987 -1846 -599 O ATOM 5382 N GLY B 258 -59.190 75.188-400.195 1.00 61.75 N ANISOU 5382 N GLY B 258 7744 6848 8872 1492 -1582 -431 N ATOM 5383 CA GLY B 258 -60.624 75.119-400.392 1.00 61.12 C ANISOU 5383 CA GLY B 258 7533 6823 8865 1647 -1668 -595 C ATOM 5384 C GLY B 258 -61.012 73.764-400.947 1.00 60.82 C ANISOU 5384 C GLY B 258 7422 6562 9125 1406 -1728 -639 C ATOM 5385 O GLY B 258 -60.196 72.848-400.979 1.00 61.62 O ANISOU 5385 O GLY B 258 7579 6489 9346 1118 -1647 -492 O ATOM 5386 N GLY B 259 -62.258 73.629-401.381 1.00 76.25 N ANISOU 5386 N GLY B 259 9236 8540 11195 1534 -1866 -836 N ATOM 5387 CA GLY B 259 -62.731 72.373-401.932 1.00 81.27 C ANISOU 5387 CA GLY B 259 9757 8986 12137 1300 -1929 -884 C ATOM 5388 C GLY B 259 -62.650 71.228-400.943 1.00 75.94 C ANISOU 5388 C GLY B 259 9073 8313 11466 1024 -1640 -666 C ATOM 5389 O GLY B 259 -62.108 71.370-399.847 1.00 73.42 O ANISOU 5389 O GLY B 259 8861 8102 10934 996 -1408 -487 O ATOM 5390 N THR B 260 -63.191 70.081-401.329 1.00 65.22 N ANISOU 5390 N THR B 260 7575 6846 10359 825 -1664 -686 N ATOM 5391 CA THR B 260 -63.196 68.929-400.443 1.00 66.79 C ANISOU 5391 CA THR B 260 7740 7090 10547 599 -1405 -489 C ATOM 5392 C THR B 260 -62.643 67.697-401.132 1.00 69.20 C ANISOU 5392 C THR B 260 7988 7173 11132 270 -1410 -346 C ATOM 5393 O THR B 260 -62.245 67.750-402.293 1.00 75.14 O ANISOU 5393 O THR B 260 8744 7698 12106 200 -1616 -397 O ATOM 5394 CB THR B 260 -64.601 68.602-399.961 1.00 72.04 C ANISOU 5394 CB THR B 260 8248 7940 11185 703 -1358 -612 C ATOM 5395 OG1 THR B 260 -65.392 68.180-401.077 1.00 80.07 O ANISOU 5395 OG1 THR B 260 9069 8854 12499 661 -1584 -807 O ATOM 5396 CG2 THR B 260 -65.234 69.824-399.313 1.00 74.56 C ANISOU 5396 CG2 THR B 260 8622 8479 11227 1060 -1345 -734 C ATOM 5397 N ARG B 261 -62.634 66.586-400.407 1.00 71.72 N ANISOU 5397 N ARG B 261 8253 7563 11433 86 -1184 -159 N ATOM 5398 CA ARG B 261 -62.072 65.343-400.907 1.00 66.48 C ANISOU 5398 CA ARG B 261 7525 6738 10997 -217 -1129 44 C ATOM 5399 C ARG B 261 -62.480 64.204-399.993 1.00 66.58 C ANISOU 5399 C ARG B 261 7424 6937 10936 -322 -893 192 C ATOM 5400 O ARG B 261 -62.274 64.265-398.783 1.00 64.64 O ANISOU 5400 O ARG B 261 7281 6871 10410 -230 -704 272 O ATOM 5401 CB ARG B 261 -60.548 65.436-400.966 1.00 67.29 C ANISOU 5401 CB ARG B 261 7825 6710 11032 -297 -1068 238 C ATOM 5402 CG ARG B 261 -59.871 64.282-401.687 1.00 67.61 C ANISOU 5402 CG ARG B 261 7821 6552 11317 -574 -1034 463 C ATOM 5403 CD ARG B 261 -58.356 64.390-401.587 1.00 70.44 C ANISOU 5403 CD ARG B 261 8390 6833 11541 -596 -948 647 C ATOM 5404 NE ARG B 261 -57.849 63.866-400.321 1.00 66.04 N ANISOU 5404 NE ARG B 261 7884 6482 10728 -596 -677 827 N ATOM 5405 CZ ARG B 261 -56.666 64.184-399.800 1.00 68.16 C ANISOU 5405 CZ ARG B 261 8333 6784 10782 -534 -585 918 C ATOM 5406 NH1 ARG B 261 -55.869 65.039-400.431 1.00 69.05 N ANISOU 5406 NH1 ARG B 261 8593 6760 10883 -466 -725 858 N ATOM 5407 NH2 ARG B 261 -56.284 63.655-398.643 1.00 62.86 N ANISOU 5407 NH2 ARG B 261 7690 6295 9900 -520 -369 1048 N ATOM 5408 N ALA B 262 -63.064 63.164-400.576 1.00 71.49 N ANISOU 5408 N ALA B 262 7825 7520 11819 -511 -915 225 N ATOM 5409 CA ALA B 262 -63.517 62.016-399.805 1.00 71.00 C ANISOU 5409 CA ALA B 262 7618 7674 11684 -597 -705 363 C ATOM 5410 C ALA B 262 -62.458 61.569-398.809 1.00 68.83 C ANISOU 5410 C ALA B 262 7496 7497 11159 -618 -462 622 C ATOM 5411 O ALA B 262 -61.282 61.468-399.150 1.00 76.31 O ANISOU 5411 O ALA B 262 8561 8288 12147 -722 -436 795 O ATOM 5412 CB ALA B 262 -63.878 60.878-400.732 1.00 75.87 C ANISOU 5412 CB ALA B 262 7977 8197 12655 -865 -744 454 C ATOM 5413 N SER B 263 -62.881 61.303-397.578 1.00 68.88 N ANISOU 5413 N SER B 263 7507 7764 10902 -493 -300 630 N ATOM 5414 CA SER B 263 -61.976 60.813-396.547 1.00 67.26 C ANISOU 5414 CA SER B 263 7428 7672 10455 -480 -94 836 C ATOM 5415 C SER B 263 -61.359 59.477-396.947 1.00 69.84 C ANISOU 5415 C SER B 263 7635 7994 10908 -692 22 1117 C ATOM 5416 O SER B 263 -61.707 58.913-397.981 1.00 72.21 O ANISOU 5416 O SER B 263 7743 8193 11501 -879 -44 1168 O ATOM 5417 CB SER B 263 -62.716 60.673-395.216 1.00 64.71 C ANISOU 5417 CB SER B 263 7113 7618 9857 -296 24 768 C ATOM 5418 OG SER B 263 -61.950 59.938-394.276 1.00 65.89 O ANISOU 5418 OG SER B 263 7338 7895 9803 -283 201 956 O ATOM 5419 N THR B 264 -60.433 58.978-396.136 1.00 67.52 N ANISOU 5419 N THR B 264 7447 7808 10401 -655 191 1303 N ATOM 5420 CA THR B 264 -59.816 57.689-396.404 1.00 68.33 C ANISOU 5420 CA THR B 264 7436 7961 10566 -801 332 1601 C ATOM 5421 C THR B 264 -59.588 56.919-395.106 1.00 71.00 C ANISOU 5421 C THR B 264 7791 8598 10587 -655 520 1713 C ATOM 5422 O THR B 264 -59.214 55.747-395.128 1.00 74.92 O ANISOU 5422 O THR B 264 8165 9234 11067 -713 662 1966 O ATOM 5423 CB THR B 264 -58.463 57.842-397.127 1.00 71.27 C ANISOU 5423 CB THR B 264 7948 8096 11034 -892 315 1758 C ATOM 5424 OG1 THR B 264 -57.418 57.971-396.160 1.00 67.29 O ANISOU 5424 OG1 THR B 264 7641 7690 10238 -737 420 1810 O ATOM 5425 CG2 THR B 264 -58.462 59.063-398.032 1.00 68.95 C ANISOU 5425 CG2 THR B 264 7760 7518 10921 -914 93 1561 C ATOM 5426 N ALA B 265 -59.829 57.583-393.980 1.00 69.30 N ANISOU 5426 N ALA B 265 7725 8483 10124 -449 513 1527 N ATOM 5427 CA ALA B 265 -59.520 57.036-392.658 1.00 69.40 C ANISOU 5427 CA ALA B 265 7807 8735 9828 -271 644 1580 C ATOM 5428 C ALA B 265 -59.842 55.549-392.480 1.00 68.51 C ANISOU 5428 C ALA B 265 7474 8911 9646 -274 783 1772 C ATOM 5429 O ALA B 265 -58.941 54.728-392.321 1.00 81.82 O ANISOU 5429 O ALA B 265 9150 10704 11232 -250 901 1990 O ATOM 5430 CB ALA B 265 -60.206 57.863-391.573 1.00 64.75 C ANISOU 5430 CB ALA B 265 7352 8201 9049 -75 597 1339 C ATOM 5431 N LYS B 266 -61.128 55.216-392.490 1.00105.31 N ANISOU 5431 N LYS B 266 11948 13727 14337 -274 772 1687 N ATOM 5432 CA LYS B 266 -61.571 53.841-392.276 1.00108.64 C ANISOU 5432 CA LYS B 266 12130 14477 14671 -258 902 1855 C ATOM 5433 C LYS B 266 -61.027 52.905-393.350 1.00111.06 C ANISOU 5433 C LYS B 266 12237 14757 15205 -489 990 2170 C ATOM 5434 O LYS B 266 -61.048 51.682-393.193 1.00121.47 O ANISOU 5434 O LYS B 266 13357 16364 16432 -475 1137 2397 O ATOM 5435 CB LYS B 266 -63.102 53.767-392.230 1.00108.66 C ANISOU 5435 CB LYS B 266 11953 14641 14690 -228 853 1674 C ATOM 5436 CG LYS B 266 -63.667 52.355-392.187 1.00114.29 C ANISOU 5436 CG LYS B 266 12362 15717 15345 -240 978 1845 C ATOM 5437 CD LYS B 266 -63.303 51.635-390.899 1.00112.18 C ANISOU 5437 CD LYS B 266 12168 15774 14681 29 1096 1925 C ATOM 5438 CE LYS B 266 -64.243 52.014-389.764 1.00108.83 C ANISOU 5438 CE LYS B 266 11857 15510 13984 301 1038 1648 C ATOM 5439 NZ LYS B 266 -65.634 51.534-389.992 1.00112.48 N ANISOU 5439 NZ LYS B 266 12049 16217 14473 295 1031 1560 N ATOM 5440 N ALA B 267 -60.532 53.488-394.437 1.00 82.24 N ANISOU 5440 N ALA B 267 8641 10763 11844 -687 902 2197 N ATOM 5441 CA ALA B 267 -59.957 52.710-395.532 1.00 88.26 C ANISOU 5441 CA ALA B 267 9250 11422 12863 -920 973 2510 C ATOM 5442 C ALA B 267 -58.429 52.646-395.446 1.00 82.99 C ANISOU 5442 C ALA B 267 8779 10675 12077 -857 1058 2707 C ATOM 5443 O ALA B 267 -57.748 52.384-396.438 1.00 86.76 O ANISOU 5443 O ALA B 267 9232 10955 12776 -1031 1082 2932 O ATOM 5444 CB ALA B 267 -60.397 53.281-396.873 1.00 94.42 C ANISOU 5444 CB ALA B 267 9957 11859 14060 -1169 801 2417 C ATOM 5445 N VAL B 268 -57.900 52.886-394.252 1.00 76.20 N ANISOU 5445 N VAL B 268 8116 9963 10872 -597 1093 2612 N ATOM 5446 CA VAL B 268 -56.468 52.811-394.008 1.00 76.24 C ANISOU 5446 CA VAL B 268 8299 9950 10718 -483 1165 2751 C ATOM 5447 C VAL B 268 -56.230 52.278-392.602 1.00 75.20 C ANISOU 5447 C VAL B 268 8213 10160 10199 -187 1258 2734 C ATOM 5448 O VAL B 268 -55.208 51.653-392.325 1.00 75.41 O ANISOU 5448 O VAL B 268 8276 10327 10051 -48 1367 2919 O ATOM 5449 CB VAL B 268 -55.802 54.192-394.150 1.00 79.49 C ANISOU 5449 CB VAL B 268 8984 10049 11170 -476 1017 2543 C ATOM 5450 CG1 VAL B 268 -54.371 54.165-393.631 1.00 76.91 C ANISOU 5450 CG1 VAL B 268 8843 9763 10617 -302 1080 2617 C ATOM 5451 CG2 VAL B 268 -55.836 54.655-395.594 1.00 77.40 C ANISOU 5451 CG2 VAL B 268 8697 9446 11264 -723 907 2572 C ATOM 5452 N PHE B 269 -57.197 52.517-391.723 1.00 86.32 N ANISOU 5452 N PHE B 269 9624 11706 11468 -66 1203 2504 N ATOM 5453 CA PHE B 269 -57.098 52.088-390.334 1.00 89.81 C ANISOU 5453 CA PHE B 269 10130 12443 11552 234 1247 2436 C ATOM 5454 C PHE B 269 -57.976 50.883-390.002 1.00102.99 C ANISOU 5454 C PHE B 269 11549 14500 13083 322 1349 2550 C ATOM 5455 O PHE B 269 -59.129 50.794-390.429 1.00107.58 O ANISOU 5455 O PHE B 269 11951 15116 13810 189 1331 2510 O ATOM 5456 CB PHE B 269 -57.477 53.235-389.398 1.00 89.55 C ANISOU 5456 CB PHE B 269 10319 12287 11418 355 1109 2096 C ATOM 5457 CG PHE B 269 -56.457 54.326-389.328 1.00 81.67 C ANISOU 5457 CG PHE B 269 9568 11011 10451 350 1024 1983 C ATOM 5458 CD1 PHE B 269 -55.415 54.261-388.421 1.00 74.34 C ANISOU 5458 CD1 PHE B 269 8793 10152 9302 555 1030 1952 C ATOM 5459 CD2 PHE B 269 -56.546 55.425-390.161 1.00 77.27 C ANISOU 5459 CD2 PHE B 269 9079 10146 10135 162 925 1889 C ATOM 5460 CE1 PHE B 269 -54.476 55.269-388.348 1.00 77.24 C ANISOU 5460 CE1 PHE B 269 9360 10287 9702 543 951 1836 C ATOM 5461 CE2 PHE B 269 -55.611 56.437-390.093 1.00 71.75 C ANISOU 5461 CE2 PHE B 269 8586 9233 9444 168 851 1789 C ATOM 5462 CZ PHE B 269 -54.573 56.358-389.186 1.00 75.43 C ANISOU 5462 CZ PHE B 269 9187 9772 9700 345 870 1765 C ATOM 5463 N GLY B 270 -57.423 49.958-389.229 1.00 82.79 N ANISOU 5463 N GLY B 270 8968 12261 10228 575 1447 2675 N ATOM 5464 CA GLY B 270 -58.228 48.927-388.617 1.00 80.89 C ANISOU 5464 CA GLY B 270 8530 12441 9762 751 1519 2725 C ATOM 5465 C GLY B 270 -58.707 49.493-387.300 1.00 82.32 C ANISOU 5465 C GLY B 270 8916 12658 9705 1003 1390 2387 C ATOM 5466 O GLY B 270 -59.875 49.845-387.149 1.00 82.04 O ANISOU 5466 O GLY B 270 8853 12617 9700 976 1324 2205 O ATOM 5467 N TYR B 271 -57.782 49.598-386.353 1.00171.87 N ANISOU 5467 N TYR B 271 20467 24018 20817 1255 1347 2299 N ATOM 5468 CA TYR B 271 -58.049 50.205-385.058 1.00179.43 C ANISOU 5468 CA TYR B 271 21657 24936 21584 1484 1207 1984 C ATOM 5469 C TYR B 271 -58.464 51.660-385.252 1.00175.59 C ANISOU 5469 C TYR B 271 21344 24041 21332 1285 1092 1764 C ATOM 5470 O TYR B 271 -57.616 52.531-385.439 1.00174.25 O ANISOU 5470 O TYR B 271 21340 23576 21291 1185 1040 1714 O ATOM 5471 CB TYR B 271 -56.788 50.128-384.192 1.00186.43 C ANISOU 5471 CB TYR B 271 22724 25850 22262 1742 1161 1930 C ATOM 5472 CG TYR B 271 -57.001 50.374-382.712 1.00199.10 C ANISOU 5472 CG TYR B 271 24530 27487 23632 2038 1017 1642 C ATOM 5473 CD1 TYR B 271 -57.773 49.507-381.946 1.00202.52 C ANISOU 5473 CD1 TYR B 271 24883 28275 23789 2312 1010 1603 C ATOM 5474 CD2 TYR B 271 -56.406 51.458-382.075 1.00198.07 C ANISOU 5474 CD2 TYR B 271 24667 27030 23560 2049 879 1413 C ATOM 5475 CE1 TYR B 271 -57.961 49.725-380.589 1.00213.66 C ANISOU 5475 CE1 TYR B 271 26503 29681 24996 2596 855 1332 C ATOM 5476 CE2 TYR B 271 -56.587 51.682-380.720 1.00198.60 C ANISOU 5476 CE2 TYR B 271 24925 27079 23456 2300 735 1158 C ATOM 5477 CZ TYR B 271 -57.365 50.813-379.983 1.00208.10 C ANISOU 5477 CZ TYR B 271 26071 28604 24392 2578 716 1114 C ATOM 5478 OH TYR B 271 -57.547 51.036-378.635 1.00202.07 O ANISOU 5478 OH TYR B 271 25521 27789 23469 2839 550 853 O ATOM 5479 N GLY B 272 -59.769 51.919-385.215 1.00101.20 N ANISOU 5479 N GLY B 272 11873 14635 11945 1252 1057 1636 N ATOM 5480 CA GLY B 272 -60.289 53.262-385.405 1.00 91.37 C ANISOU 5480 CA GLY B 272 10768 13057 10891 1110 959 1442 C ATOM 5481 C GLY B 272 -60.171 54.123-384.162 1.00 91.20 C ANISOU 5481 C GLY B 272 11035 12879 10739 1291 851 1210 C ATOM 5482 O GLY B 272 -59.790 53.630-383.100 1.00 95.32 O ANISOU 5482 O GLY B 272 11650 13546 11023 1537 826 1163 O ATOM 5483 N PRO B 273 -60.489 55.423-384.287 1.00 65.01 N ANISOU 5483 N PRO B 273 7854 9263 7582 1178 779 1069 N ATOM 5484 CA PRO B 273 -60.453 56.353-383.151 1.00 62.35 C ANISOU 5484 CA PRO B 273 7780 8739 7170 1310 688 879 C ATOM 5485 C PRO B 273 -61.433 55.912-382.067 1.00 66.31 C ANISOU 5485 C PRO B 273 8332 9428 7434 1571 661 758 C ATOM 5486 O PRO B 273 -62.625 55.755-382.338 1.00 74.61 O ANISOU 5486 O PRO B 273 9273 10612 8465 1593 684 726 O ATOM 5487 CB PRO B 273 -60.901 57.681-383.766 1.00 64.17 C ANISOU 5487 CB PRO B 273 8062 8702 7617 1140 652 809 C ATOM 5488 CG PRO B 273 -60.631 57.542-385.216 1.00 63.29 C ANISOU 5488 CG PRO B 273 7770 8565 7713 909 690 947 C ATOM 5489 CD PRO B 273 -60.868 56.100-385.535 1.00 69.41 C ANISOU 5489 CD PRO B 273 8319 9643 8412 931 773 1091 C ATOM 5490 N GLN B 274 -60.928 55.710-380.855 1.00 67.99 N ANISOU 5490 N GLN B 274 8713 9652 7468 1785 597 672 N ATOM 5491 CA GLN B 274 -61.739 55.169-379.771 1.00 66.23 C ANISOU 5491 CA GLN B 274 8559 9617 6989 2077 549 553 C ATOM 5492 C GLN B 274 -62.575 56.227-379.062 1.00 68.48 C ANISOU 5492 C GLN B 274 9059 9668 7292 2139 481 388 C ATOM 5493 O GLN B 274 -63.783 56.301-379.265 1.00 68.84 O ANISOU 5493 O GLN B 274 9049 9807 7300 2180 510 348 O ATOM 5494 CB GLN B 274 -60.863 54.412-378.776 1.00 67.52 C ANISOU 5494 CB GLN B 274 8807 9904 6943 2321 480 514 C ATOM 5495 CG GLN B 274 -60.303 53.125-379.346 1.00 74.51 C ANISOU 5495 CG GLN B 274 9455 11137 7717 2363 570 700 C ATOM 5496 CD GLN B 274 -61.394 52.170-379.788 1.00 77.97 C ANISOU 5496 CD GLN B 274 9651 11947 8027 2420 662 796 C ATOM 5497 OE1 GLN B 274 -62.206 51.720-378.980 1.00 82.97 O ANISOU 5497 OE1 GLN B 274 10317 12787 8419 2683 613 683 O ATOM 5498 NE2 GLN B 274 -61.414 51.851-381.077 1.00 80.29 N ANISOU 5498 NE2 GLN B 274 9695 12324 8486 2175 788 1001 N ATOM 5499 N THR B 275 -61.943 57.038-378.223 1.00 76.20 N ANISOU 5499 N THR B 275 10274 10349 8329 2154 395 296 N ATOM 5500 CA THR B 275 -62.670 58.094-377.530 1.00 74.21 C ANISOU 5500 CA THR B 275 10233 9848 8117 2202 348 185 C ATOM 5501 C THR B 275 -63.018 59.205-378.514 1.00 77.89 C ANISOU 5501 C THR B 275 10645 10145 8805 1969 416 245 C ATOM 5502 O THR B 275 -62.489 59.239-379.624 1.00 76.98 O ANISOU 5502 O THR B 275 10369 10042 8837 1758 466 347 O ATOM 5503 CB THR B 275 -61.852 58.674-376.368 1.00 78.75 C ANISOU 5503 CB THR B 275 11054 10127 8740 2249 234 89 C ATOM 5504 OG1 THR B 275 -60.806 59.505-376.886 1.00 82.78 O ANISOU 5504 OG1 THR B 275 11553 10412 9487 1991 248 150 O ATOM 5505 CG2 THR B 275 -61.246 57.558-375.531 1.00 87.77 C ANISOU 5505 CG2 THR B 275 12228 11441 9680 2487 136 11 C ATOM 5506 N ASP B 276 -63.908 60.112-378.113 1.00 97.06 N ANISOU 5506 N ASP B 276 13211 12420 11246 2033 413 183 N ATOM 5507 CA ASP B 276 -64.324 61.214-378.982 1.00 93.09 C ANISOU 5507 CA ASP B 276 12660 11792 10917 1880 466 226 C ATOM 5508 C ASP B 276 -63.213 62.254-379.128 1.00 82.20 C ANISOU 5508 C ASP B 276 11350 10133 9750 1669 454 285 C ATOM 5509 O ASP B 276 -63.247 63.104-380.020 1.00 71.81 O ANISOU 5509 O ASP B 276 9962 8741 8581 1526 487 335 O ATOM 5510 CB ASP B 276 -65.604 61.869-378.457 1.00 88.99 C ANISOU 5510 CB ASP B 276 12271 11228 10314 2064 478 158 C ATOM 5511 CG ASP B 276 -66.714 60.863-378.208 1.00 96.06 C ANISOU 5511 CG ASP B 276 13111 12420 10966 2307 479 74 C ATOM 5512 OD1 ASP B 276 -67.699 60.854-378.980 1.00 92.56 O ANISOU 5512 OD1 ASP B 276 12514 12151 10503 2339 521 46 O ATOM 5513 OD2 ASP B 276 -66.597 60.075-377.244 1.00 99.75 O ANISOU 5513 OD2 ASP B 276 13679 12964 11258 2482 425 18 O ATOM 5514 N SER B 277 -62.230 62.172-378.239 1.00 60.23 N ANISOU 5514 N SER B 277 8696 7215 6973 1672 392 260 N ATOM 5515 CA SER B 277 -61.076 63.057-378.277 1.00 58.59 C ANISOU 5515 CA SER B 277 8537 6772 6953 1481 371 297 C ATOM 5516 C SER B 277 -59.846 62.353-378.858 1.00 59.55 C ANISOU 5516 C SER B 277 8535 6993 7099 1374 358 332 C ATOM 5517 O SER B 277 -58.708 62.723-378.565 1.00 60.57 O ANISOU 5517 O SER B 277 8718 6975 7320 1285 311 316 O ATOM 5518 CB SER B 277 -60.782 63.617-376.881 1.00 93.93 C ANISOU 5518 CB SER B 277 13235 10988 11465 1538 297 232 C ATOM 5519 OG SER B 277 -60.828 62.599-375.895 1.00 95.31 O ANISOU 5519 OG SER B 277 13500 11239 11473 1750 213 127 O ATOM 5520 N GLN B 278 -60.088 61.335-379.679 1.00 61.77 N ANISOU 5520 N GLN B 278 8640 7530 7298 1390 405 386 N ATOM 5521 CA GLN B 278 -59.024 60.681-380.434 1.00 60.39 C ANISOU 5521 CA GLN B 278 8334 7460 7152 1289 423 468 C ATOM 5522 C GLN B 278 -59.223 60.979-381.912 1.00 61.13 C ANISOU 5522 C GLN B 278 8269 7569 7390 1101 482 568 C ATOM 5523 O GLN B 278 -60.355 61.071-382.379 1.00 60.16 O ANISOU 5523 O GLN B 278 8070 7510 7279 1109 509 564 O ATOM 5524 CB GLN B 278 -59.021 59.167-380.200 1.00 62.74 C ANISOU 5524 CB GLN B 278 8539 8049 7249 1461 435 489 C ATOM 5525 CG GLN B 278 -58.552 58.748-378.812 1.00 65.86 C ANISOU 5525 CG GLN B 278 9084 8447 7492 1681 339 370 C ATOM 5526 CD GLN B 278 -58.332 57.255-378.693 1.00 69.14 C ANISOU 5526 CD GLN B 278 9386 9198 7687 1879 350 409 C ATOM 5527 OE1 GLN B 278 -58.138 56.732-377.597 1.00 72.68 O ANISOU 5527 OE1 GLN B 278 9934 9715 7965 2123 256 295 O ATOM 5528 NE2 GLN B 278 -58.358 56.561-379.823 1.00 70.17 N ANISOU 5528 NE2 GLN B 278 9299 9541 7823 1786 460 578 N ATOM 5529 N TYR B 279 -58.126 61.130-382.645 1.00 62.28 N ANISOU 5529 N TYR B 279 8368 7653 7644 951 485 639 N ATOM 5530 CA TYR B 279 -58.209 61.467-384.061 1.00 58.87 C ANISOU 5530 CA TYR B 279 7810 7192 7366 778 509 719 C ATOM 5531 C TYR B 279 -57.308 60.603-384.929 1.00 59.59 C ANISOU 5531 C TYR B 279 7781 7373 7486 692 544 850 C ATOM 5532 O TYR B 279 -56.244 60.158-384.501 1.00 58.27 O ANISOU 5532 O TYR B 279 7658 7241 7240 746 545 872 O ATOM 5533 CB TYR B 279 -57.879 62.938-384.274 1.00 56.80 C ANISOU 5533 CB TYR B 279 7636 6711 7236 675 467 681 C ATOM 5534 CG TYR B 279 -58.830 63.878-383.582 1.00 55.60 C ANISOU 5534 CG TYR B 279 7583 6469 7072 756 457 602 C ATOM 5535 CD1 TYR B 279 -59.814 64.546-384.295 1.00 60.94 C ANISOU 5535 CD1 TYR B 279 8201 7142 7812 752 458 589 C ATOM 5536 CD2 TYR B 279 -58.747 64.100-382.216 1.00 57.41 C ANISOU 5536 CD2 TYR B 279 7969 6613 7232 854 440 541 C ATOM 5537 CE1 TYR B 279 -60.690 65.413-383.669 1.00 56.42 C ANISOU 5537 CE1 TYR B 279 7722 6509 7207 862 466 541 C ATOM 5538 CE2 TYR B 279 -59.615 64.963-381.579 1.00 59.30 C ANISOU 5538 CE2 TYR B 279 8312 6752 7469 932 447 505 C ATOM 5539 CZ TYR B 279 -60.586 65.616-382.311 1.00 58.46 C ANISOU 5539 CZ TYR B 279 8144 6671 7399 944 473 517 C ATOM 5540 OH TYR B 279 -61.455 66.478-381.687 1.00 61.27 O ANISOU 5540 OH TYR B 279 8603 6949 7729 1056 496 504 O ATOM 5541 N ALA B 280 -57.754 60.366-386.155 1.00 65.06 N ANISOU 5541 N ALA B 280 8321 8098 8300 571 567 935 N ATOM 5542 CA ALA B 280 -56.961 59.641-387.131 1.00 65.47 C ANISOU 5542 CA ALA B 280 8262 8190 8422 463 608 1094 C ATOM 5543 C ALA B 280 -56.116 60.642-387.900 1.00 61.86 C ANISOU 5543 C ALA B 280 7876 7521 8108 333 552 1091 C ATOM 5544 O ALA B 280 -56.642 61.598-388.463 1.00 64.50 O ANISOU 5544 O ALA B 280 8214 7728 8566 264 489 1020 O ATOM 5545 CB ALA B 280 -57.863 58.863-388.078 1.00 65.87 C ANISOU 5545 CB ALA B 280 8103 8351 8572 376 647 1192 C ATOM 5546 N ILE B 281 -54.805 60.431-387.913 1.00 58.89 N ANISOU 5546 N ILE B 281 7552 7134 7691 337 567 1156 N ATOM 5547 CA ILE B 281 -53.894 61.303-388.639 1.00 56.35 C ANISOU 5547 CA ILE B 281 7298 6644 7468 241 512 1152 C ATOM 5548 C ILE B 281 -53.185 60.533-389.739 1.00 59.81 C ANISOU 5548 C ILE B 281 7662 7092 7972 164 554 1332 C ATOM 5549 O ILE B 281 -52.592 59.488-389.486 1.00 61.59 O ANISOU 5549 O ILE B 281 7854 7462 8085 244 636 1451 O ATOM 5550 CB ILE B 281 -52.830 61.895-387.708 1.00 57.76 C ANISOU 5550 CB ILE B 281 7618 6784 7543 320 481 1051 C ATOM 5551 CG1 ILE B 281 -53.468 62.840-386.689 1.00 54.77 C ANISOU 5551 CG1 ILE B 281 7325 6337 7150 361 437 900 C ATOM 5552 CG2 ILE B 281 -51.780 62.629-388.509 1.00 55.46 C ANISOU 5552 CG2 ILE B 281 7377 6376 7318 244 433 1057 C ATOM 5553 CD1 ILE B 281 -53.934 62.151-385.432 1.00 57.51 C ANISOU 5553 CD1 ILE B 281 7699 6789 7363 505 460 849 C ATOM 5554 N ILE B 282 -53.236 61.049-390.958 1.00 58.81 N ANISOU 5554 N ILE B 282 7513 6809 8022 30 493 1358 N ATOM 5555 CA ILE B 282 -52.569 60.397-392.077 1.00 59.00 C ANISOU 5555 CA ILE B 282 7488 6786 8142 -56 521 1542 C ATOM 5556 C ILE B 282 -51.685 61.384-392.831 1.00 59.18 C ANISOU 5556 C ILE B 282 7629 6629 8228 -94 424 1494 C ATOM 5557 O ILE B 282 -52.191 62.233-393.562 1.00 65.31 O ANISOU 5557 O ILE B 282 8407 7262 9145 -166 311 1405 O ATOM 5558 CB ILE B 282 -53.590 59.782-393.044 1.00 62.07 C ANISOU 5558 CB ILE B 282 7705 7145 8732 -197 525 1646 C ATOM 5559 CG1 ILE B 282 -54.355 58.659-392.349 1.00 69.46 C ANISOU 5559 CG1 ILE B 282 8501 8314 9576 -143 637 1720 C ATOM 5560 CG2 ILE B 282 -52.902 59.265-394.295 1.00 70.26 C ANISOU 5560 CG2 ILE B 282 8711 8061 9924 -315 537 1848 C ATOM 5561 CD1 ILE B 282 -55.387 57.988-393.223 1.00 67.28 C ANISOU 5561 CD1 ILE B 282 8016 8045 9503 -292 647 1819 C ATOM 5562 N VAL B 283 -50.369 61.269-392.660 1.00 65.21 N ANISOU 5562 N VAL B 283 8486 7424 8867 -15 457 1538 N ATOM 5563 CA VAL B 283 -49.431 62.211-393.267 1.00 62.91 C ANISOU 5563 CA VAL B 283 8313 7004 8586 -16 364 1475 C ATOM 5564 C VAL B 283 -48.957 61.764-394.639 1.00 64.91 C ANISOU 5564 C VAL B 283 8568 7130 8966 -91 354 1646 C ATOM 5565 O VAL B 283 -48.573 60.618-394.818 1.00 66.13 O ANISOU 5565 O VAL B 283 8676 7348 9101 -79 469 1851 O ATOM 5566 CB VAL B 283 -48.212 62.429-392.378 1.00 57.79 C ANISOU 5566 CB VAL B 283 7765 6456 7735 124 385 1396 C ATOM 5567 CG1 VAL B 283 -47.124 63.152-393.150 1.00 57.78 C ANISOU 5567 CG1 VAL B 283 7868 6364 7721 141 307 1366 C ATOM 5568 CG2 VAL B 283 -48.601 63.212-391.141 1.00 60.83 C ANISOU 5568 CG2 VAL B 283 8174 6886 8054 165 353 1206 C ATOM 5569 N ARG B 284 -48.973 62.677-395.604 1.00 61.74 N ANISOU 5569 N ARG B 284 8222 6550 8688 -148 213 1569 N ATOM 5570 CA ARG B 284 -48.611 62.346-396.977 1.00 62.88 C ANISOU 5570 CA ARG B 284 8388 6513 8989 -225 166 1713 C ATOM 5571 C ARG B 284 -47.559 63.286-397.544 1.00 62.64 C ANISOU 5571 C ARG B 284 8519 6390 8892 -145 49 1624 C ATOM 5572 O ARG B 284 -47.652 64.497-397.387 1.00 59.47 O ANISOU 5572 O ARG B 284 8165 5993 8439 -95 -67 1422 O ATOM 5573 CB ARG B 284 -49.843 62.406-397.882 1.00 67.99 C ANISOU 5573 CB ARG B 284 8929 6996 9907 -373 59 1697 C ATOM 5574 CG ARG B 284 -50.820 61.251-397.756 1.00 69.70 C ANISOU 5574 CG ARG B 284 8959 7279 10244 -484 168 1837 C ATOM 5575 CD ARG B 284 -51.980 61.455-398.724 1.00 63.88 C ANISOU 5575 CD ARG B 284 8111 6366 9793 -621 22 1767 C ATOM 5576 NE ARG B 284 -52.856 60.293-398.808 1.00 69.30 N ANISOU 5576 NE ARG B 284 8591 7107 10631 -755 118 1918 N ATOM 5577 CZ ARG B 284 -53.885 60.082-397.997 1.00 69.95 C ANISOU 5577 CZ ARG B 284 8548 7376 10654 -733 175 1839 C ATOM 5578 NH1 ARG B 284 -54.163 60.954-397.038 1.00 65.32 N ANISOU 5578 NH1 ARG B 284 8037 6904 9877 -590 149 1628 N ATOM 5579 NH2 ARG B 284 -54.633 58.998-398.143 1.00 72.93 N ANISOU 5579 NH2 ARG B 284 8720 7829 11162 -851 260 1981 N ATOM 5580 N ARG B 285 -46.565 62.729-398.221 1.00 69.78 N ANISOU 5580 N ARG B 285 9503 7227 9784 -117 84 1788 N ATOM 5581 CA ARG B 285 -45.643 63.543-398.996 1.00 72.59 C ANISOU 5581 CA ARG B 285 10017 7472 10093 -35 -47 1713 C ATOM 5582 C ARG B 285 -45.541 62.946-400.386 1.00 66.98 C ANISOU 5582 C ARG B 285 9345 6510 9594 -124 -92 1906 C ATOM 5583 O ARG B 285 -45.052 61.831-400.543 1.00 73.62 O ANISOU 5583 O ARG B 285 10181 7353 10440 -131 55 2158 O ATOM 5584 CB ARG B 285 -44.260 63.600-398.341 1.00 61.92 C ANISOU 5584 CB ARG B 285 8769 6296 8462 146 29 1688 C ATOM 5585 CG ARG B 285 -43.251 64.462-399.113 1.00 72.07 C ANISOU 5585 CG ARG B 285 10219 7508 9658 260 -108 1595 C ATOM 5586 CD ARG B 285 -41.903 64.611-398.390 1.00 78.67 C ANISOU 5586 CD ARG B 285 11133 8554 10204 454 -47 1520 C ATOM 5587 NE ARG B 285 -41.316 63.315-398.062 1.00 87.71 N ANISOU 5587 NE ARG B 285 12268 9800 11258 533 135 1721 N ATOM 5588 CZ ARG B 285 -40.714 62.519-398.941 1.00 79.33 C ANISOU 5588 CZ ARG B 285 11287 8641 10213 582 194 1950 C ATOM 5589 NH1 ARG B 285 -40.610 62.887-400.214 1.00 77.88 N ANISOU 5589 NH1 ARG B 285 11218 8219 10154 545 67 1989 N ATOM 5590 NH2 ARG B 285 -40.220 61.353-398.546 1.00 71.50 N ANISOU 5590 NH2 ARG B 285 10264 7792 9109 688 377 2145 N ATOM 5591 N ASN B 286 -46.014 63.679-401.389 1.00 86.65 N ANISOU 5591 N ASN B 286 11871 8785 12268 -178 -300 1795 N ATOM 5592 CA ASN B 286 -46.016 63.186-402.766 1.00 95.96 C ANISOU 5592 CA ASN B 286 13090 9662 13707 -284 -387 1953 C ATOM 5593 C ASN B 286 -47.003 62.045-402.983 1.00 95.89 C ANISOU 5593 C ASN B 286 12893 9565 13976 -500 -294 2154 C ATOM 5594 O ASN B 286 -46.691 61.066-403.662 1.00 91.92 O ANISOU 5594 O ASN B 286 12387 8910 13628 -596 -214 2430 O ATOM 5595 CB ASN B 286 -44.615 62.733-403.192 1.00 92.15 C ANISOU 5595 CB ASN B 286 12775 9133 13103 -176 -314 2138 C ATOM 5596 CG ASN B 286 -43.708 63.893-403.544 1.00 94.35 C ANISOU 5596 CG ASN B 286 13252 9401 13196 16 -484 1937 C ATOM 5597 OD1 ASN B 286 -44.169 65.018-403.747 1.00 92.46 O ANISOU 5597 OD1 ASN B 286 13023 9137 12971 51 -684 1689 O ATOM 5598 ND2 ASN B 286 -42.408 63.625-403.626 1.00102.63 N ANISOU 5598 ND2 ASN B 286 14449 10498 14047 170 -405 2044 N ATOM 5599 N ASP B 287 -48.193 62.177-402.403 1.00103.09 N ANISOU 5599 N ASP B 287 13641 10584 14945 -570 -299 2025 N ATOM 5600 CA ASP B 287 -49.238 61.167-402.540 1.00106.79 C ANISOU 5600 CA ASP B 287 13898 11017 15660 -766 -222 2175 C ATOM 5601 C ASP B 287 -48.908 59.919-401.731 1.00101.28 C ANISOU 5601 C ASP B 287 13111 10545 14824 -766 58 2440 C ATOM 5602 O ASP B 287 -49.723 59.005-401.624 1.00102.79 O ANISOU 5602 O ASP B 287 13103 10798 15153 -902 163 2581 O ATOM 5603 CB ASP B 287 -49.444 60.795-404.010 1.00109.90 C ANISOU 5603 CB ASP B 287 14274 11056 16428 -943 -356 2297 C ATOM 5604 CG ASP B 287 -49.581 62.008-404.906 1.00122.43 C ANISOU 5604 CG ASP B 287 15980 12413 18126 -885 -665 2028 C ATOM 5605 OD1 ASP B 287 -49.936 63.091-404.393 1.00115.84 O ANISOU 5605 OD1 ASP B 287 15165 11722 17126 -744 -769 1746 O ATOM 5606 OD2 ASP B 287 -49.331 61.876-406.124 1.00122.57 O ANISOU 5606 OD2 ASP B 287 16071 12107 18394 -966 -809 2106 O ATOM 5607 N ALA B 288 -47.707 59.887-401.164 1.00 81.63 N ANISOU 5607 N ALA B 288 10758 8207 12050 -590 170 2493 N ATOM 5608 CA ALA B 288 -47.272 58.748-400.369 1.00 80.28 C ANISOU 5608 CA ALA B 288 10517 8285 11700 -518 417 2721 C ATOM 5609 C ALA B 288 -47.794 58.855-398.946 1.00 76.28 C ANISOU 5609 C ALA B 288 9928 8066 10988 -427 482 2554 C ATOM 5610 O ALA B 288 -47.670 59.898-398.313 1.00 73.03 O ANISOU 5610 O ALA B 288 9610 7712 10425 -323 390 2291 O ATOM 5611 CB ALA B 288 -45.758 58.656-400.366 1.00 78.38 C ANISOU 5611 CB ALA B 288 10453 8095 11232 -327 489 2821 C ATOM 5612 N ILE B 289 -48.373 57.774-398.441 1.00 72.21 N ANISOU 5612 N ILE B 289 9236 7733 10467 -462 640 2717 N ATOM 5613 CA ILE B 289 -48.872 57.761-397.075 1.00 68.28 C ANISOU 5613 CA ILE B 289 8675 7500 9768 -354 695 2569 C ATOM 5614 C ILE B 289 -47.699 57.497-396.153 1.00 69.13 C ANISOU 5614 C ILE B 289 8880 7826 9561 -115 800 2585 C ATOM 5615 O ILE B 289 -47.514 56.391-395.667 1.00 69.21 O ANISOU 5615 O ILE B 289 8800 8061 9437 -13 961 2770 O ATOM 5616 CB ILE B 289 -49.956 56.697-396.862 1.00 72.98 C ANISOU 5616 CB ILE B 289 9040 8244 10445 -445 808 2714 C ATOM 5617 CG1 ILE B 289 -50.990 56.737-397.996 1.00 81.34 C ANISOU 5617 CG1 ILE B 289 9971 9073 11863 -696 708 2739 C ATOM 5618 CG2 ILE B 289 -50.628 56.885-395.508 1.00 69.96 C ANISOU 5618 CG2 ILE B 289 8624 8087 9870 -326 816 2507 C ATOM 5619 CD1 ILE B 289 -50.548 56.036-399.287 1.00 83.75 C ANISOU 5619 CD1 ILE B 289 10237 9173 12411 -852 746 3044 C ATOM 5620 N VAL B 290 -46.904 58.535-395.933 1.00 67.63 N ANISOU 5620 N VAL B 290 8861 7587 9249 -11 698 2378 N ATOM 5621 CA VAL B 290 -45.671 58.454-395.159 1.00 64.56 C ANISOU 5621 CA VAL B 290 8571 7377 8581 222 755 2338 C ATOM 5622 C VAL B 290 -45.818 57.982-393.704 1.00 68.37 C ANISOU 5622 C VAL B 290 8991 8133 8855 380 828 2254 C ATOM 5623 O VAL B 290 -44.919 57.326-393.169 1.00 65.21 O ANISOU 5623 O VAL B 290 8607 7930 8239 594 916 2314 O ATOM 5624 CB VAL B 290 -44.954 59.804-395.185 1.00 63.38 C ANISOU 5624 CB VAL B 290 8583 7128 8369 272 608 2092 C ATOM 5625 CG1 VAL B 290 -44.478 60.177-393.802 1.00 65.52 C ANISOU 5625 CG1 VAL B 290 8888 7590 8416 439 600 1874 C ATOM 5626 CG2 VAL B 290 -43.819 59.784-396.201 1.00 66.27 C ANISOU 5626 CG2 VAL B 290 9073 7390 8717 333 600 2214 C ATOM 5627 N GLN B 291 -46.935 58.317-393.066 1.00 65.62 N ANISOU 5627 N GLN B 291 8577 7796 8560 305 780 2104 N ATOM 5628 CA GLN B 291 -47.191 57.893-391.690 1.00 65.19 C ANISOU 5628 CA GLN B 291 8479 7965 8324 457 822 2010 C ATOM 5629 C GLN B 291 -48.685 57.827-391.392 1.00 66.26 C ANISOU 5629 C GLN B 291 8504 8111 8561 349 813 1968 C ATOM 5630 O GLN B 291 -49.471 58.558-391.982 1.00 67.24 O ANISOU 5630 O GLN B 291 8619 8056 8875 177 732 1900 O ATOM 5631 CB GLN B 291 -46.485 58.820-390.696 1.00 61.11 C ANISOU 5631 CB GLN B 291 8090 7460 7668 583 725 1737 C ATOM 5632 CG GLN B 291 -46.921 58.623-389.253 1.00 63.00 C ANISOU 5632 CG GLN B 291 8309 7848 7779 710 714 1585 C ATOM 5633 CD GLN B 291 -45.832 58.960-388.249 1.00 71.19 C ANISOU 5633 CD GLN B 291 9440 8958 8650 897 649 1384 C ATOM 5634 OE1 GLN B 291 -44.672 59.152-388.612 1.00 74.05 O ANISOU 5634 OE1 GLN B 291 9864 9321 8949 969 637 1376 O ATOM 5635 NE2 GLN B 291 -46.201 59.023-386.973 1.00 67.88 N ANISOU 5635 NE2 GLN B 291 9033 8596 8163 987 594 1208 N ATOM 5636 N SER B 292 -49.073 56.939-390.483 1.00 72.44 N ANISOU 5636 N SER B 292 9204 9125 9196 482 888 1996 N ATOM 5637 CA SER B 292 -50.480 56.756-390.133 1.00 71.53 C ANISOU 5637 CA SER B 292 8982 9064 9132 422 888 1955 C ATOM 5638 C SER B 292 -50.613 56.418-388.657 1.00 71.87 C ANISOU 5638 C SER B 292 9048 9313 8946 644 886 1820 C ATOM 5639 O SER B 292 -50.153 55.366-388.215 1.00 75.90 O ANISOU 5639 O SER B 292 9505 10065 9268 837 968 1928 O ATOM 5640 CB SER B 292 -51.088 55.629-390.968 1.00 73.77 C ANISOU 5640 CB SER B 292 9069 9442 9520 319 1003 2226 C ATOM 5641 OG SER B 292 -50.468 54.387-390.664 1.00 78.93 O ANISOU 5641 OG SER B 292 9646 10364 9981 501 1139 2430 O ATOM 5642 N VAL B 293 -51.241 57.303-387.893 1.00 61.23 N ANISOU 5642 N VAL B 293 7783 7871 7610 637 789 1590 N ATOM 5643 CA VAL B 293 -51.346 57.109-386.454 1.00 64.55 C ANISOU 5643 CA VAL B 293 8261 8424 7841 845 753 1434 C ATOM 5644 C VAL B 293 -52.671 57.613-385.924 1.00 62.37 C ANISOU 5644 C VAL B 293 7999 8087 7610 806 702 1298 C ATOM 5645 O VAL B 293 -53.368 58.356-386.601 1.00 62.76 O ANISOU 5645 O VAL B 293 8034 7980 7832 632 679 1282 O ATOM 5646 CB VAL B 293 -50.210 57.836-385.700 1.00 62.35 C ANISOU 5646 CB VAL B 293 8138 8055 7496 942 660 1249 C ATOM 5647 CG1 VAL B 293 -50.465 59.342-385.663 1.00 62.10 C ANISOU 5647 CG1 VAL B 293 8209 7765 7623 781 566 1087 C ATOM 5648 CG2 VAL B 293 -50.073 57.290-384.290 1.00 62.59 C ANISOU 5648 CG2 VAL B 293 8212 8245 7325 1200 612 1113 C ATOM 5649 N VAL B 294 -53.013 57.204-384.709 1.00 62.02 N ANISOU 5649 N VAL B 294 7992 8176 7396 1001 675 1190 N ATOM 5650 CA VAL B 294 -54.194 57.712-384.027 1.00 64.59 C ANISOU 5650 CA VAL B 294 8371 8438 7731 1013 623 1048 C ATOM 5651 C VAL B 294 -53.791 58.306-382.685 1.00 67.04 C ANISOU 5651 C VAL B 294 8861 8639 7973 1141 515 840 C ATOM 5652 O VAL B 294 -53.165 57.630-381.872 1.00 73.44 O ANISOU 5652 O VAL B 294 9704 9580 8620 1348 479 785 O ATOM 5653 CB VAL B 294 -55.235 56.606-383.804 1.00 71.78 C ANISOU 5653 CB VAL B 294 9157 9610 8508 1136 680 1109 C ATOM 5654 CG1 VAL B 294 -56.147 56.964-382.641 1.00 78.22 C ANISOU 5654 CG1 VAL B 294 10090 10396 9235 1269 605 922 C ATOM 5655 CG2 VAL B 294 -56.038 56.367-385.075 1.00 72.94 C ANISOU 5655 CG2 VAL B 294 9121 9789 8804 947 758 1262 C ATOM 5656 N LEU B 295 -54.143 59.569-382.460 1.00 61.97 N ANISOU 5656 N LEU B 295 8325 7758 7462 1029 458 730 N ATOM 5657 CA LEU B 295 -53.740 60.265-381.240 1.00 64.15 C ANISOU 5657 CA LEU B 295 8761 7875 7737 1096 356 554 C ATOM 5658 C LEU B 295 -54.919 60.886-380.511 1.00 62.65 C ANISOU 5658 C LEU B 295 8665 7564 7575 1114 326 470 C ATOM 5659 O LEU B 295 -56.002 61.020-381.069 1.00 61.50 O ANISOU 5659 O LEU B 295 8463 7445 7460 1061 383 530 O ATOM 5660 CB LEU B 295 -52.703 61.345-381.551 1.00 61.44 C ANISOU 5660 CB LEU B 295 8463 7346 7536 943 320 521 C ATOM 5661 CG LEU B 295 -51.375 60.861-382.136 1.00 65.09 C ANISOU 5661 CG LEU B 295 8871 7907 7955 960 334 574 C ATOM 5662 CD1 LEU B 295 -50.396 62.019-382.260 1.00 60.15 C ANISOU 5662 CD1 LEU B 295 8297 7111 7445 836 279 499 C ATOM 5663 CD2 LEU B 295 -50.791 59.736-381.290 1.00 63.07 C ANISOU 5663 CD2 LEU B 295 8620 7836 7509 1211 297 513 C ATOM 5664 N SER B 296 -54.695 61.272-379.262 1.00 62.18 N ANISOU 5664 N SER B 296 8751 7362 7512 1198 230 326 N ATOM 5665 CA SER B 296 -55.753 61.843-378.446 1.00 64.67 C ANISOU 5665 CA SER B 296 9187 7537 7849 1240 203 262 C ATOM 5666 C SER B 296 -55.363 63.215-377.926 1.00 65.77 C ANISOU 5666 C SER B 296 9437 7382 8172 1103 155 208 C ATOM 5667 O SER B 296 -54.184 63.488-377.696 1.00 64.23 O ANISOU 5667 O SER B 296 9253 7101 8050 1044 92 146 O ATOM 5668 CB SER B 296 -56.081 60.919-377.272 1.00 62.92 C ANISOU 5668 CB SER B 296 9051 7406 7448 1500 123 150 C ATOM 5669 OG SER B 296 -56.961 61.551-376.354 1.00 63.10 O ANISOU 5669 OG SER B 296 9233 7239 7503 1551 80 79 O ATOM 5670 N THR B 297 -56.361 64.074-377.745 1.00 63.18 N ANISOU 5670 N THR B 297 9175 6918 7911 1066 190 239 N ATOM 5671 CA THR B 297 -56.136 65.405-377.213 1.00 58.70 C ANISOU 5671 CA THR B 297 8698 6085 7521 938 170 235 C ATOM 5672 C THR B 297 -56.319 65.415-375.702 1.00 63.21 C ANISOU 5672 C THR B 297 9444 6464 8108 1048 73 129 C ATOM 5673 O THR B 297 -56.216 66.460-375.066 1.00 61.54 O ANISOU 5673 O THR B 297 9316 6000 8065 943 55 139 O ATOM 5674 CB THR B 297 -57.099 66.435-377.835 1.00 58.19 C ANISOU 5674 CB THR B 297 8611 5980 7518 863 269 353 C ATOM 5675 OG1 THR B 297 -58.415 66.269-377.286 1.00 59.71 O ANISOU 5675 OG1 THR B 297 8896 6174 7618 1025 293 349 O ATOM 5676 CG2 THR B 297 -57.151 66.273-379.346 1.00 56.61 C ANISOU 5676 CG2 THR B 297 8248 5967 7295 796 332 429 C ATOM 5677 N LYS B 298 -56.591 64.248-375.128 1.00 65.42 N ANISOU 5677 N LYS B 298 9775 6864 8217 1266 7 33 N ATOM 5678 CA LYS B 298 -56.794 64.140-373.687 1.00 73.43 C ANISOU 5678 CA LYS B 298 10975 7693 9231 1413 -119 -95 C ATOM 5679 C LYS B 298 -55.657 63.386-373.019 1.00 66.73 C ANISOU 5679 C LYS B 298 10142 6861 8352 1521 -279 -269 C ATOM 5680 O LYS B 298 -55.413 62.223-373.329 1.00 64.71 O ANISOU 5680 O LYS B 298 9801 6889 7898 1685 -292 -303 O ATOM 5681 CB LYS B 298 -58.123 63.451-373.376 1.00 80.58 C ANISOU 5681 CB LYS B 298 11957 8726 9932 1648 -103 -105 C ATOM 5682 CG LYS B 298 -58.468 63.431-371.892 1.00 80.19 C ANISOU 5682 CG LYS B 298 12136 8451 9880 1820 -242 -233 C ATOM 5683 CD LYS B 298 -59.924 63.052-371.666 1.00 86.75 C ANISOU 5683 CD LYS B 298 13058 9390 10513 2042 -201 -220 C ATOM 5684 CE LYS B 298 -60.340 63.301-370.224 1.00 90.07 C ANISOU 5684 CE LYS B 298 13744 9511 10969 2191 -332 -319 C ATOM 5685 NZ LYS B 298 -61.808 63.149-370.032 1.00 79.23 N ANISOU 5685 NZ LYS B 298 12479 8221 9405 2408 -274 -293 N ATOM 5686 N ARG B 299 -54.973 64.052-372.094 1.00 76.76 N ANISOU 5686 N ARG B 299 11508 7836 9821 1440 -404 -376 N ATOM 5687 CA ARG B 299 -53.831 63.456-371.412 1.00 80.60 C ANISOU 5687 CA ARG B 299 12004 8315 10305 1554 -588 -583 C ATOM 5688 C ARG B 299 -54.193 62.098-370.835 1.00 84.74 C ANISOU 5688 C ARG B 299 12593 9041 10564 1907 -697 -713 C ATOM 5689 O ARG B 299 -55.351 61.841-370.514 1.00 85.30 O ANISOU 5689 O ARG B 299 12765 9128 10516 2047 -677 -684 O ATOM 5690 CB ARG B 299 -53.322 64.381-370.306 1.00 83.23 C ANISOU 5690 CB ARG B 299 12449 8250 10925 1425 -735 -703 C ATOM 5691 CG ARG B 299 -52.873 65.745-370.804 1.00 85.35 C ANISOU 5691 CG ARG B 299 12626 8356 11446 1087 -631 -571 C ATOM 5692 CD ARG B 299 -52.264 66.595-369.696 1.00 90.70 C ANISOU 5692 CD ARG B 299 13372 8654 12434 936 -779 -684 C ATOM 5693 NE ARG B 299 -52.354 68.019-370.009 1.00 90.65 N ANISOU 5693 NE ARG B 299 13309 8479 12656 633 -640 -485 N ATOM 5694 CZ ARG B 299 -51.453 68.692-370.718 1.00 87.14 C ANISOU 5694 CZ ARG B 299 12694 8107 12307 427 -580 -438 C ATOM 5695 NH1 ARG B 299 -50.376 68.076-371.186 1.00 85.36 N ANISOU 5695 NH1 ARG B 299 12355 8097 11981 487 -645 -579 N ATOM 5696 NH2 ARG B 299 -51.630 69.986-370.957 1.00 83.37 N ANISOU 5696 NH2 ARG B 299 12159 7509 12007 188 -452 -243 N ATOM 5697 N GLY B 300 -53.196 61.227-370.714 1.00 81.49 N ANISOU 5697 N GLY B 300 12115 8812 10034 2082 -811 -856 N ATOM 5698 CA GLY B 300 -53.410 59.917-370.134 1.00 80.72 C ANISOU 5698 CA GLY B 300 12060 8952 9659 2461 -929 -987 C ATOM 5699 C GLY B 300 -53.832 58.877-371.151 1.00 82.32 C ANISOU 5699 C GLY B 300 12102 9597 9578 2585 -762 -820 C ATOM 5700 O GLY B 300 -53.215 57.820-371.251 1.00 89.34 O ANISOU 5700 O GLY B 300 12894 10794 10258 2819 -801 -864 O ATOM 5701 N GLY B 301 -54.878 59.171-371.916 1.00 20.00 N ATOM 5702 CA GLY B 301 -55.438 58.231-372.871 1.00 20.00 C ATOM 5703 C GLY B 301 -54.368 57.458-373.616 1.00 20.00 C ATOM 5704 O GLY B 301 -53.365 58.007-374.061 1.00 80.03 O ANISOU 5704 O GLY B 301 11378 9904 9124 2376 -359 -379 O ATOM 5705 N LYS B 302 -54.614 56.152-373.771 1.00 74.94 N ANISOU 5705 N LYS B 302 10666 9762 8044 2812 -336 -336 N ATOM 5706 CA LYS B 302 -53.658 55.253-374.396 1.00 76.96 C ANISOU 5706 CA LYS B 302 10752 10327 8164 2915 -276 -241 C ATOM 5707 C LYS B 302 -54.351 54.395-375.446 1.00 80.94 C ANISOU 5707 C LYS B 302 11051 11175 8529 2901 -78 13 C ATOM 5708 O LYS B 302 -55.580 54.308-375.483 1.00 80.35 O ANISOU 5708 O LYS B 302 10965 11157 8407 2894 -26 56 O ATOM 5709 CB LYS B 302 -53.013 54.359-373.334 1.00 80.10 C ANISOU 5709 CB LYS B 302 11197 10905 8331 3324 -462 -438 C ATOM 5710 CG LYS B 302 -52.212 55.121-372.283 1.00 81.45 C ANISOU 5710 CG LYS B 302 11546 10731 8669 3343 -690 -719 C ATOM 5711 CD LYS B 302 -52.082 54.334-370.980 1.00 91.82 C ANISOU 5711 CD LYS B 302 12963 12156 9768 3783 -934 -977 C ATOM 5712 CE LYS B 302 -50.884 54.797-370.147 1.00 93.16 C ANISOU 5712 CE LYS B 302 13230 12078 10088 3843 -1170 -1261 C ATOM 5713 NZ LYS B 302 -50.959 56.228-369.730 1.00 79.47 N ANISOU 5713 NZ LYS B 302 11645 9821 8730 3499 -1239 -1353 N ATOM 5714 N ASP B 303 -53.555 53.777-376.309 1.00 90.06 N ANISOU 5714 N ASP B 303 12037 12553 9629 2894 34 183 N ATOM 5715 CA ASP B 303 -54.075 52.794-377.244 1.00 96.78 C ANISOU 5715 CA ASP B 303 12666 13752 10354 2899 215 443 C ATOM 5716 C ASP B 303 -54.248 51.489-376.489 1.00106.52 C ANISOU 5716 C ASP B 303 13842 15392 11239 3320 165 412 C ATOM 5717 O ASP B 303 -54.160 51.461-375.263 1.00107.89 O ANISOU 5717 O ASP B 303 14175 15529 11290 3591 -27 164 O ATOM 5718 CB ASP B 303 -53.116 52.602-378.421 1.00 99.68 C ANISOU 5718 CB ASP B 303 12888 14187 10798 2749 356 664 C ATOM 5719 CG ASP B 303 -51.693 52.314-377.977 1.00 95.24 C ANISOU 5719 CG ASP B 303 12366 13699 10121 2979 271 573 C ATOM 5720 OD1 ASP B 303 -51.419 52.399-376.761 1.00 93.94 O ANISOU 5720 OD1 ASP B 303 12345 13482 9867 3217 80 308 O ATOM 5721 OD2 ASP B 303 -50.847 52.008-378.846 1.00 90.53 O ANISOU 5721 OD2 ASP B 303 11663 13206 9530 2935 386 758 O ATOM 5722 N ILE B 304 -54.482 50.405-377.219 1.00 88.79 N ANISOU 5722 N ILE B 304 11361 13536 8838 3383 330 665 N ATOM 5723 CA ILE B 304 -54.651 49.095-376.601 1.00 86.74 C ANISOU 5723 CA ILE B 304 11004 13743 8212 3807 307 677 C ATOM 5724 C ILE B 304 -53.327 48.504-376.127 1.00 84.51 C ANISOU 5724 C ILE B 304 10729 13648 7734 4144 226 621 C ATOM 5725 O ILE B 304 -53.202 47.293-375.980 1.00 89.03 O ANISOU 5725 O ILE B 304 11150 14686 7992 4493 266 730 O ATOM 5726 CB ILE B 304 -55.330 48.105-377.561 1.00 91.31 C ANISOU 5726 CB ILE B 304 11288 14710 8697 3754 529 1002 C ATOM 5727 CG1 ILE B 304 -54.917 48.403-379.002 1.00 93.96 C ANISOU 5727 CG1 ILE B 304 11489 14900 9313 3358 715 1272 C ATOM 5728 CG2 ILE B 304 -56.846 48.186-377.422 1.00 99.43 C ANISOU 5728 CG2 ILE B 304 12299 15767 9713 3696 530 948 C ATOM 5729 CD1 ILE B 304 -55.481 47.442-380.018 1.00 97.32 C ANISOU 5729 CD1 ILE B 304 11605 15660 9713 3257 932 1613 C ATOM 5730 N TYR B 305 -52.341 49.361-375.891 1.00111.15 N ANISOU 5730 N TYR B 305 14264 16687 11282 4061 111 448 N ATOM 5731 CA TYR B 305 -51.026 48.911-375.448 1.00116.93 C ANISOU 5731 CA TYR B 305 15007 17574 11847 4388 12 348 C ATOM 5732 C TYR B 305 -50.501 49.789-374.322 1.00114.33 C ANISOU 5732 C TYR B 305 14922 16885 11635 4454 -262 -42 C ATOM 5733 O TYR B 305 -49.331 49.704-373.956 1.00115.30 O ANISOU 5733 O TYR B 305 15074 17039 11697 4667 -379 -191 O ATOM 5734 CB TYR B 305 -50.033 48.933-376.611 1.00120.28 C ANISOU 5734 CB TYR B 305 15313 18012 12376 4208 190 590 C ATOM 5735 CG TYR B 305 -50.420 48.053-377.779 1.00129.20 C ANISOU 5735 CG TYR B 305 16192 19458 13439 4116 462 1004 C ATOM 5736 CD1 TYR B 305 -49.671 46.928-378.104 1.00131.51 C ANISOU 5736 CD1 TYR B 305 16313 20175 13481 4407 584 1231 C ATOM 5737 CD2 TYR B 305 -51.529 48.350-378.560 1.00133.02 C ANISOU 5737 CD2 TYR B 305 16600 19819 14124 3745 594 1172 C ATOM 5738 CE1 TYR B 305 -50.019 46.123-379.173 1.00136.73 C ANISOU 5738 CE1 TYR B 305 16730 21103 14118 4294 842 1644 C ATOM 5739 CE2 TYR B 305 -51.884 47.552-379.627 1.00138.24 C ANISOU 5739 CE2 TYR B 305 17013 20739 14772 3632 826 1541 C ATOM 5740 CZ TYR B 305 -51.129 46.441-379.930 1.00139.76 C ANISOU 5740 CZ TYR B 305 17035 21327 14740 3888 955 1791 C ATOM 5741 OH TYR B 305 -51.485 45.645-380.996 1.00140.56 O ANISOU 5741 OH TYR B 305 16876 21666 14863 3746 1196 2192 O ATOM 5742 N ASP B 306 -51.372 50.635-373.781 1.00139.51 N ANISOU 5742 N ASP B 306 18275 19731 15000 4274 -363 -202 N ATOM 5743 CA ASP B 306 -50.976 51.592-372.751 1.00142.81 C ANISOU 5743 CA ASP B 306 18919 19739 15603 4255 -608 -536 C ATOM 5744 C ASP B 306 -49.825 52.487-373.208 1.00139.25 C ANISOU 5744 C ASP B 306 18480 19022 15406 3996 -600 -563 C ATOM 5745 O ASP B 306 -49.026 52.955-372.395 1.00137.82 O ANISOU 5745 O ASP B 306 18413 18632 15319 4078 -810 -841 O ATOM 5746 CB ASP B 306 -50.623 50.883-371.439 1.00150.55 C ANISOU 5746 CB ASP B 306 19988 20879 16336 4759 -875 -829 C ATOM 5747 CG ASP B 306 -51.851 50.462-370.652 1.00160.55 C ANISOU 5747 CG ASP B 306 21345 22230 17427 4976 -970 -914 C ATOM 5748 OD1 ASP B 306 -51.828 50.576-369.408 1.00162.32 O ANISOU 5748 OD1 ASP B 306 21759 22284 17633 5217 -1249 -1231 O ATOM 5749 OD2 ASP B 306 -52.842 50.023-371.275 1.00161.11 O ANISOU 5749 OD2 ASP B 306 21298 22530 17388 4909 -778 -677 O ATOM 5750 N SER B 307 -49.744 52.716-374.515 1.00127.06 N ANISOU 5750 N SER B 307 16811 17489 13976 3691 -370 -287 N ATOM 5751 CA SER B 307 -48.798 53.676-375.066 1.00119.54 C ANISOU 5751 CA SER B 307 15875 16281 13265 3416 -347 -295 C ATOM 5752 C SER B 307 -49.440 55.053-375.038 1.00116.32 C ANISOU 5752 C SER B 307 15586 15439 13171 3031 -362 -344 C ATOM 5753 O SER B 307 -50.431 55.294-375.726 1.00116.36 O ANISOU 5753 O SER B 307 15554 15403 13256 2803 -216 -158 O ATOM 5754 CB SER B 307 -48.417 53.306-376.500 1.00117.47 C ANISOU 5754 CB SER B 307 15444 16212 12979 3285 -110 23 C ATOM 5755 OG SER B 307 -47.738 52.066-376.548 1.00121.59 O ANISOU 5755 OG SER B 307 15848 17144 13207 3652 -73 107 O ATOM 5756 N ASN B 308 -48.879 55.950-374.236 1.00129.69 N ANISOU 5756 N ASN B 308 17409 16824 15045 2971 -540 -593 N ATOM 5757 CA ASN B 308 -49.407 57.300-374.124 1.00124.39 C ANISOU 5757 CA ASN B 308 16841 15752 14668 2627 -549 -620 C ATOM 5758 C ASN B 308 -49.524 57.980-375.484 1.00119.47 C ANISOU 5758 C ASN B 308 16130 15072 14192 2282 -346 -380 C ATOM 5759 O ASN B 308 -48.529 58.435-376.047 1.00122.67 O ANISOU 5759 O ASN B 308 16487 15437 14684 2159 -322 -369 O ATOM 5760 CB ASN B 308 -48.530 58.135-373.196 1.00125.63 C ANISOU 5760 CB ASN B 308 17098 15614 15021 2589 -753 -892 C ATOM 5761 CG ASN B 308 -48.871 59.605-373.248 1.00128.91 C ANISOU 5761 CG ASN B 308 17580 15651 15750 2208 -723 -861 C ATOM 5762 OD1 ASN B 308 -50.042 59.983-373.332 1.00125.27 O ANISOU 5762 OD1 ASN B 308 17172 15078 15347 2076 -637 -739 O ATOM 5763 ND2 ASN B 308 -47.849 60.446-373.193 1.00124.43 N ANISOU 5763 ND2 ASN B 308 16995 14912 15372 2050 -790 -969 N ATOM 5764 N ILE B 309 -50.747 58.053-376.004 1.00 67.24 N ANISOU 5764 N ILE B 309 9495 8460 7594 2150 -217 -210 N ATOM 5765 CA ILE B 309 -50.992 58.640-377.315 1.00 66.95 C ANISOU 5765 CA ILE B 309 9372 8374 7692 1856 -52 -2 C ATOM 5766 C ILE B 309 -51.563 60.053-377.209 1.00 63.10 C ANISOU 5766 C ILE B 309 8975 7560 7439 1599 -60 -27 C ATOM 5767 O ILE B 309 -52.268 60.518-378.112 1.00 61.32 O ANISOU 5767 O ILE B 309 8699 7303 7298 1414 56 121 O ATOM 5768 CB ILE B 309 -51.945 57.782-378.161 1.00 64.81 C ANISOU 5768 CB ILE B 309 8975 8348 7302 1872 99 211 C ATOM 5769 CG1 ILE B 309 -53.271 57.579-377.427 1.00 71.53 C ANISOU 5769 CG1 ILE B 309 9890 9212 8076 1982 69 157 C ATOM 5770 CG2 ILE B 309 -51.306 56.444-378.491 1.00 67.45 C ANISOU 5770 CG2 ILE B 309 9182 9027 7420 2090 154 316 C ATOM 5771 CD1 ILE B 309 -54.361 56.967-378.281 1.00 70.46 C ANISOU 5771 CD1 ILE B 309 9613 9287 7872 1947 211 343 C ATOM 5772 N TYR B 310 -51.276 60.734-376.102 1.00 63.43 N ANISOU 5772 N TYR B 310 9143 7364 7594 1600 -201 -212 N ATOM 5773 CA TYR B 310 -51.620 62.145-375.995 1.00 62.18 C ANISOU 5773 CA TYR B 310 9052 6906 7668 1354 -193 -203 C ATOM 5774 C TYR B 310 -50.688 62.933-376.904 1.00 61.29 C ANISOU 5774 C TYR B 310 8853 6756 7679 1142 -141 -143 C ATOM 5775 O TYR B 310 -49.467 62.864-376.757 1.00 63.76 O ANISOU 5775 O TYR B 310 9139 7092 7994 1178 -218 -252 O ATOM 5776 CB TYR B 310 -51.494 62.628-374.554 1.00 70.06 C ANISOU 5776 CB TYR B 310 10194 7639 8786 1392 -358 -395 C ATOM 5777 CG TYR B 310 -51.585 64.132-374.411 1.00 70.57 C ANISOU 5777 CG TYR B 310 10300 7403 9111 1124 -339 -357 C ATOM 5778 CD1 TYR B 310 -52.647 64.842-374.954 1.00 68.04 C ANISOU 5778 CD1 TYR B 310 9983 7029 8842 992 -203 -184 C ATOM 5779 CD2 TYR B 310 -50.611 64.840-373.724 1.00 65.01 C ANISOU 5779 CD2 TYR B 310 9614 6489 8598 1020 -460 -495 C ATOM 5780 CE1 TYR B 310 -52.730 66.214-374.820 1.00 69.19 C ANISOU 5780 CE1 TYR B 310 10150 6940 9199 781 -171 -120 C ATOM 5781 CE2 TYR B 310 -50.687 66.209-373.586 1.00 70.83 C ANISOU 5781 CE2 TYR B 310 10360 6979 9572 772 -426 -427 C ATOM 5782 CZ TYR B 310 -51.747 66.891-374.134 1.00 68.60 C ANISOU 5782 CZ TYR B 310 10083 6668 9313 662 -274 -225 C ATOM 5783 OH TYR B 310 -51.820 68.259-373.994 1.00 63.23 O ANISOU 5783 OH TYR B 310 9398 5781 8846 445 -225 -129 O ATOM 5784 N ILE B 311 -51.268 63.672-377.844 1.00 59.36 N ANISOU 5784 N ILE B 311 8563 6472 7520 954 -24 12 N ATOM 5785 CA ILE B 311 -50.498 64.397-378.854 1.00 61.10 C ANISOU 5785 CA ILE B 311 8703 6688 7825 780 23 80 C ATOM 5786 C ILE B 311 -49.178 64.983-378.357 1.00 59.39 C ANISOU 5786 C ILE B 311 8491 6375 7699 730 -77 -63 C ATOM 5787 O ILE B 311 -48.105 64.515-378.730 1.00 61.80 O ANISOU 5787 O ILE B 311 8743 6815 7924 799 -99 -105 O ATOM 5788 CB ILE B 311 -51.335 65.524-379.480 1.00 58.94 C ANISOU 5788 CB ILE B 311 8417 6308 7671 604 103 200 C ATOM 5789 CG1 ILE B 311 -52.520 64.945-380.250 1.00 57.44 C ANISOU 5789 CG1 ILE B 311 8182 6244 7399 646 193 322 C ATOM 5790 CG2 ILE B 311 -50.483 66.361-380.408 1.00 58.31 C ANISOU 5790 CG2 ILE B 311 8266 6226 7664 456 120 241 C ATOM 5791 CD1 ILE B 311 -53.519 65.988-380.683 1.00 55.34 C ANISOU 5791 CD1 ILE B 311 7913 5890 7224 547 249 402 C ATOM 5792 N ASP B 312 -49.260 66.005-377.515 1.00 60.32 N ANISOU 5792 N ASP B 312 8664 6267 7988 616 -134 -130 N ATOM 5793 CA ASP B 312 -48.073 66.716-377.056 1.00 62.44 C ANISOU 5793 CA ASP B 312 8905 6434 8386 524 -229 -265 C ATOM 5794 C ASP B 312 -46.917 65.810-376.624 1.00 62.03 C ANISOU 5794 C ASP B 312 8838 6496 8235 709 -352 -459 C ATOM 5795 O ASP B 312 -45.749 66.134-376.842 1.00 64.53 O ANISOU 5795 O ASP B 312 9085 6859 8575 674 -396 -548 O ATOM 5796 CB ASP B 312 -48.437 67.685-375.932 1.00 62.08 C ANISOU 5796 CB ASP B 312 8924 6108 8556 397 -287 -309 C ATOM 5797 CG ASP B 312 -48.934 69.016-376.456 1.00 61.10 C ANISOU 5797 CG ASP B 312 8758 5902 8555 187 -172 -131 C ATOM 5798 OD1 ASP B 312 -48.092 69.850-376.869 1.00 60.62 O ANISOU 5798 OD1 ASP B 312 8598 5864 8570 48 -167 -128 O ATOM 5799 OD2 ASP B 312 -50.166 69.227-376.451 1.00 62.68 O ANISOU 5799 OD2 ASP B 312 9018 6044 8755 189 -89 0 O ATOM 5800 N ASP B 313 -47.238 64.680-376.012 1.00 64.72 N ANISOU 5800 N ASP B 313 9239 6910 8443 938 -411 -532 N ATOM 5801 CA ASP B 313 -46.210 63.761-375.547 1.00 68.99 C ANISOU 5801 CA ASP B 313 9763 7593 8856 1180 -537 -724 C ATOM 5802 C ASP B 313 -45.682 62.893-376.680 1.00 65.47 C ANISOU 5802 C ASP B 313 9232 7451 8193 1310 -432 -609 C ATOM 5803 O ASP B 313 -44.477 62.776-376.874 1.00 63.99 O ANISOU 5803 O ASP B 313 8990 7375 7948 1394 -478 -707 O ATOM 5804 CB ASP B 313 -46.756 62.879-374.422 1.00 65.51 C ANISOU 5804 CB ASP B 313 9419 7142 8330 1422 -657 -852 C ATOM 5805 CG ASP B 313 -46.976 63.650-373.128 1.00 68.33 C ANISOU 5805 CG ASP B 313 9879 7161 8924 1330 -811 -1014 C ATOM 5806 OD1 ASP B 313 -46.385 64.740-372.975 1.00 68.02 O ANISOU 5806 OD1 ASP B 313 9803 6930 9112 1105 -849 -1068 O ATOM 5807 OD2 ASP B 313 -47.734 63.160-372.262 1.00 70.76 O ANISOU 5807 OD2 ASP B 313 10300 7394 9190 1485 -897 -1081 O ATOM 5808 N PHE B 314 -46.595 62.279-377.421 1.00 62.82 N ANISOU 5808 N PHE B 314 8881 7245 7743 1331 -293 -398 N ATOM 5809 CA PHE B 314 -46.231 61.444-378.555 1.00 66.74 C ANISOU 5809 CA PHE B 314 9293 7996 8070 1420 -173 -235 C ATOM 5810 C PHE B 314 -45.099 62.068-379.358 1.00 63.86 C ANISOU 5810 C PHE B 314 8881 7636 7747 1316 -154 -230 C ATOM 5811 O PHE B 314 -44.076 61.434-379.595 1.00 65.87 O ANISOU 5811 O PHE B 314 9098 8072 7857 1496 -161 -261 O ATOM 5812 CB PHE B 314 -47.453 61.211-379.447 1.00 64.97 C ANISOU 5812 CB PHE B 314 9035 7815 7836 1314 -22 6 C ATOM 5813 CG PHE B 314 -47.149 60.475-380.722 1.00 63.42 C ANISOU 5813 CG PHE B 314 8745 7819 7534 1338 107 211 C ATOM 5814 CD1 PHE B 314 -46.850 59.122-380.704 1.00 66.48 C ANISOU 5814 CD1 PHE B 314 9077 8472 7712 1590 144 275 C ATOM 5815 CD2 PHE B 314 -47.185 61.132-381.941 1.00 62.33 C ANISOU 5815 CD2 PHE B 314 8573 7603 7507 1122 188 352 C ATOM 5816 CE1 PHE B 314 -46.578 58.440-381.875 1.00 65.70 C ANISOU 5816 CE1 PHE B 314 8888 8535 7540 1597 279 504 C ATOM 5817 CE2 PHE B 314 -46.915 60.458-383.117 1.00 63.05 C ANISOU 5817 CE2 PHE B 314 8591 7829 7535 1130 295 549 C ATOM 5818 CZ PHE B 314 -46.610 59.107-383.084 1.00 65.44 C ANISOU 5818 CZ PHE B 314 8838 8375 7652 1353 351 640 C ATOM 5819 N PHE B 315 -45.282 63.318-379.765 1.00 60.61 N ANISOU 5819 N PHE B 315 8472 7046 7512 1055 -130 -193 N ATOM 5820 CA PHE B 315 -44.282 64.018-380.565 1.00 61.93 C ANISOU 5820 CA PHE B 315 8596 7227 7706 959 -119 -192 C ATOM 5821 C PHE B 315 -43.107 64.454-379.709 1.00 62.45 C ANISOU 5821 C PHE B 315 8652 7263 7812 1010 -261 -444 C ATOM 5822 O PHE B 315 -41.982 64.560-380.191 1.00 64.71 O ANISOU 5822 O PHE B 315 8899 7659 8029 1062 -275 -499 O ATOM 5823 CB PHE B 315 -44.900 65.232-381.266 1.00 61.89 C ANISOU 5823 CB PHE B 315 8582 7081 7851 702 -59 -75 C ATOM 5824 CG PHE B 315 -45.940 64.874-382.284 1.00 56.88 C ANISOU 5824 CG PHE B 315 7937 6479 7194 653 57 142 C ATOM 5825 CD1 PHE B 315 -45.579 64.285-383.485 1.00 58.89 C ANISOU 5825 CD1 PHE B 315 8159 6858 7360 692 127 279 C ATOM 5826 CD2 PHE B 315 -47.277 65.118-382.039 1.00 59.53 C ANISOU 5826 CD2 PHE B 315 8294 6716 7609 576 90 203 C ATOM 5827 CE1 PHE B 315 -46.531 63.945-384.424 1.00 55.95 C ANISOU 5827 CE1 PHE B 315 7758 6492 7010 627 213 462 C ATOM 5828 CE2 PHE B 315 -48.235 64.779-382.975 1.00 58.43 C ANISOU 5828 CE2 PHE B 315 8123 6617 7462 539 177 368 C ATOM 5829 CZ PHE B 315 -47.861 64.195-384.169 1.00 56.00 C ANISOU 5829 CZ PHE B 315 7764 6415 7097 550 232 492 C ATOM 5830 N ALA B 316 -43.382 64.705-378.434 1.00 63.97 N ANISOU 5830 N ALA B 316 8882 7300 8125 998 -376 -605 N ATOM 5831 CA ALA B 316 -42.361 65.153-377.493 1.00 63.48 C ANISOU 5831 CA ALA B 316 8795 7166 8159 1019 -540 -874 C ATOM 5832 C ALA B 316 -41.216 64.155-377.415 1.00 64.69 C ANISOU 5832 C ALA B 316 8919 7551 8111 1326 -617 -1031 C ATOM 5833 O ALA B 316 -40.122 64.483-376.960 1.00 71.38 O ANISOU 5833 O ALA B 316 9715 8408 8997 1375 -747 -1265 O ATOM 5834 CB ALA B 316 -42.967 65.363-376.115 1.00 68.73 C ANISOU 5834 CB ALA B 316 9523 7596 8996 983 -663 -1007 C ATOM 5835 N LYS B 317 -41.478 62.935-377.867 1.00 70.30 N ANISOU 5835 N LYS B 317 9645 8465 8600 1544 -531 -896 N ATOM 5836 CA LYS B 317 -40.503 61.861-377.795 1.00 71.61 C ANISOU 5836 CA LYS B 317 9782 8894 8532 1894 -579 -1001 C ATOM 5837 C LYS B 317 -40.333 61.180-379.147 1.00 69.97 C ANISOU 5837 C LYS B 317 9547 8909 8130 1975 -393 -732 C ATOM 5838 O LYS B 317 -40.855 60.091-379.365 1.00 65.57 O ANISOU 5838 O LYS B 317 8985 8511 7416 2134 -301 -563 O ATOM 5839 CB LYS B 317 -40.942 60.838-376.750 1.00 69.83 C ANISOU 5839 CB LYS B 317 9595 8736 8203 2165 -680 -1110 C ATOM 5840 CG LYS B 317 -41.330 61.452-375.413 1.00 72.47 C ANISOU 5840 CG LYS B 317 9987 8789 8758 2071 -867 -1344 C ATOM 5841 CD LYS B 317 -42.124 60.473-374.561 1.00 71.61 C ANISOU 5841 CD LYS B 317 9947 8726 8537 2313 -943 -1389 C ATOM 5842 CE LYS B 317 -43.404 60.042-375.269 1.00 72.77 C ANISOU 5842 CE LYS B 317 10110 8941 8598 2238 -742 -1072 C ATOM 5843 NZ LYS B 317 -44.300 59.220-374.402 1.00 81.93 N ANISOU 5843 NZ LYS B 317 11338 10141 9650 2455 -818 -1119 N ATOM 5844 N GLY B 318 -39.602 61.832-380.048 1.00 69.57 N ANISOU 5844 N GLY B 318 9473 8866 8094 1863 -341 -688 N ATOM 5845 CA GLY B 318 -39.326 61.301-381.375 1.00 74.05 C ANISOU 5845 CA GLY B 318 10033 9593 8509 1924 -182 -438 C ATOM 5846 C GLY B 318 -40.460 60.506-381.997 1.00 70.21 C ANISOU 5846 C GLY B 318 9546 9137 7992 1883 -28 -135 C ATOM 5847 O GLY B 318 -40.233 59.528-382.715 1.00 65.98 O ANISOU 5847 O GLY B 318 8988 8790 7292 2044 91 66 O ATOM 5848 N GLY B 319 -41.688 60.932-381.732 1.00 63.12 N ANISOU 5848 N GLY B 319 8665 8061 7257 1668 -25 -95 N ATOM 5849 CA GLY B 319 -42.853 60.202-382.185 1.00 61.88 C ANISOU 5849 CA GLY B 319 8487 7941 7082 1630 99 147 C ATOM 5850 C GLY B 319 -42.981 60.121-383.692 1.00 64.69 C ANISOU 5850 C GLY B 319 8817 8304 7460 1497 242 418 C ATOM 5851 O GLY B 319 -43.519 59.152-384.219 1.00 64.52 O ANISOU 5851 O GLY B 319 8743 8396 7375 1540 358 640 O ATOM 5852 N SER B 320 -42.487 61.136-384.392 1.00 84.30 N ANISOU 5852 N SER B 320 11327 10664 10038 1338 224 399 N ATOM 5853 CA SER B 320 -42.677 61.205-385.836 1.00 85.02 C ANISOU 5853 CA SER B 320 11414 10704 10185 1198 320 627 C ATOM 5854 C SER B 320 -41.536 61.922-386.546 1.00 85.58 C ANISOU 5854 C SER B 320 11528 10754 10235 1192 285 578 C ATOM 5855 O SER B 320 -41.096 62.986-386.119 1.00 84.83 O ANISOU 5855 O SER B 320 11451 10592 10188 1132 185 378 O ATOM 5856 CB SER B 320 -44.001 61.894-386.156 1.00 83.34 C ANISOU 5856 CB SER B 320 11192 10310 10163 946 326 686 C ATOM 5857 OG SER B 320 -44.394 61.644-387.492 1.00 88.08 O ANISOU 5857 OG SER B 320 11768 10869 10828 840 404 907 O ATOM 5858 N GLU B 321 -41.074 61.333-387.643 1.00 70.80 N ANISOU 5858 N GLU B 321 9669 8940 8292 1254 371 775 N ATOM 5859 CA GLU B 321 -39.956 61.877-388.400 1.00 67.72 C ANISOU 5859 CA GLU B 321 9340 8548 7842 1296 342 744 C ATOM 5860 C GLU B 321 -40.340 63.104-389.220 1.00 61.88 C ANISOU 5860 C GLU B 321 8633 7618 7260 1064 284 738 C ATOM 5861 O GLU B 321 -39.470 63.860-389.648 1.00 64.81 O ANISOU 5861 O GLU B 321 9052 7991 7580 1090 222 645 O ATOM 5862 CB GLU B 321 -39.381 60.813-389.343 1.00 76.11 C ANISOU 5862 CB GLU B 321 10425 9709 8783 1451 460 991 C ATOM 5863 CG GLU B 321 -38.313 59.906-388.739 1.00 93.80 C ANISOU 5863 CG GLU B 321 12659 12204 10778 1790 493 947 C ATOM 5864 CD GLU B 321 -37.699 58.949-389.765 1.00112.26 C ANISOU 5864 CD GLU B 321 15027 14635 12991 1951 632 1235 C ATOM 5865 OE1 GLU B 321 -38.410 58.541-390.711 1.00119.56 O ANISOU 5865 OE1 GLU B 321 15940 15441 14047 1788 729 1520 O ATOM 5866 OE2 GLU B 321 -36.505 58.603-389.625 1.00104.78 O ANISOU 5866 OE2 GLU B 321 14112 13877 11822 2246 642 1178 O ATOM 5867 N TYR B 322 -41.636 63.305-389.440 1.00 57.60 N ANISOU 5867 N TYR B 322 8059 6940 6886 869 296 824 N ATOM 5868 CA TYR B 322 -42.094 64.290-390.423 1.00 59.31 C ANISOU 5868 CA TYR B 322 8300 6998 7237 697 241 851 C ATOM 5869 C TYR B 322 -42.740 65.545-389.841 1.00 57.91 C ANISOU 5869 C TYR B 322 8096 6746 7161 564 163 696 C ATOM 5870 O TYR B 322 -42.408 66.668-390.234 1.00 58.24 O ANISOU 5870 O TYR B 322 8157 6758 7213 521 86 612 O ATOM 5871 CB TYR B 322 -43.061 63.635-391.411 1.00 57.46 C ANISOU 5871 CB TYR B 322 8042 6660 7132 591 300 1076 C ATOM 5872 CG TYR B 322 -42.457 62.473-392.157 1.00 58.66 C ANISOU 5872 CG TYR B 322 8212 6857 7218 690 393 1289 C ATOM 5873 CD1 TYR B 322 -42.096 62.594-393.492 1.00 59.97 C ANISOU 5873 CD1 TYR B 322 8448 6899 7440 657 370 1408 C ATOM 5874 CD2 TYR B 322 -42.236 61.256-391.523 1.00 64.48 C ANISOU 5874 CD2 TYR B 322 8901 7766 7831 840 503 1382 C ATOM 5875 CE1 TYR B 322 -41.534 61.530-394.179 1.00 66.68 C ANISOU 5875 CE1 TYR B 322 9322 7769 8245 745 470 1642 C ATOM 5876 CE2 TYR B 322 -41.677 60.186-392.199 1.00 65.84 C ANISOU 5876 CE2 TYR B 322 9079 8005 7933 950 613 1621 C ATOM 5877 CZ TYR B 322 -41.327 60.326-393.527 1.00 66.93 C ANISOU 5877 CZ TYR B 322 9290 7991 8149 889 606 1763 C ATOM 5878 OH TYR B 322 -40.770 59.260-394.203 1.00 64.66 O ANISOU 5878 OH TYR B 322 9015 7747 7807 993 731 2037 O ATOM 5879 N ILE B 323 -43.674 65.351-388.918 1.00 61.00 N ANISOU 5879 N ILE B 323 8442 7122 7614 517 188 674 N ATOM 5880 CA ILE B 323 -44.468 66.459-388.409 1.00 53.93 C ANISOU 5880 CA ILE B 323 7524 6141 6826 395 141 583 C ATOM 5881 C ILE B 323 -44.329 66.618-386.905 1.00 56.74 C ANISOU 5881 C ILE B 323 7870 6517 7173 422 119 432 C ATOM 5882 O ILE B 323 -43.616 65.860-386.251 1.00 59.09 O ANISOU 5882 O ILE B 323 8174 6904 7375 553 117 365 O ATOM 5883 CB ILE B 323 -45.946 66.267-388.736 1.00 54.14 C ANISOU 5883 CB ILE B 323 7518 6087 6965 305 177 692 C ATOM 5884 CG1 ILE B 323 -46.532 65.145-387.883 1.00 55.97 C ANISOU 5884 CG1 ILE B 323 7726 6373 7168 363 243 725 C ATOM 5885 CG2 ILE B 323 -46.126 65.956-390.210 1.00 55.37 C ANISOU 5885 CG2 ILE B 323 7672 6192 7173 269 178 832 C ATOM 5886 CD1 ILE B 323 -47.962 64.817-388.216 1.00 57.32 C ANISOU 5886 CD1 ILE B 323 7847 6503 7429 295 283 823 C ATOM 5887 N PHE B 324 -45.024 67.611-386.368 1.00 63.30 N ANISOU 5887 N PHE B 324 8684 7259 8109 312 94 382