HEADER    OXIDOREDUCTASE                          29-JUN-18   6A6R              
TITLE     CRYSTAL STRUCTURE OF THE MODIFIED FRUCTOSYL PEPTIDE OXIDASE FROM      
TITLE    2 ASPERGILLUS NIDULANS, SELENO-METHIONINE DERIVATIVE                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FRUCTOSYL AMINE: OXYGEN OXIDOREDUCTASE;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIDULANS;                           
SOURCE   3 ORGANISM_TAXID: 162425;                                              
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    FRUCTOSYL PEPTIDE, OXIDOREDUCTASE, ASPERGILLUS NIDULANS, FAD-BINDING  
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.OGAWA,Y.MARUYAMA,T.ITOH,W.HASHIMOTO,K.MURATA                        
REVDAT   1   15-MAY-19 6A6R    0                                                
JRNL        AUTH   N.OGAWA,T.KIMURA,F.UMEHARA,Y.KATAYAMA,G.NAGAI,K.SUZUKI,      
JRNL        AUTH 2 K.AISAKA,Y.MARUYAMA,T.ITOH,W.HASHIMOTO,K.MURATA,M.ICHIMURA   
JRNL        TITL   CREATION OF HAEMOGLOBIN A1C DIRECT OXIDASE FROM FRUCTOSYL    
JRNL        TITL 2 PEPTIDE OXIDASE BY COMBINED STRUCTURE-BASED SITE SPECIFIC    
JRNL        TITL 3 MUTAGENESIS AND RANDOM MUTAGENESIS.                          
JRNL        REF    SCI REP                       V.   9   942 2019              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   30700768                                                     
JRNL        DOI    10.1038/S41598-018-37806-X                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.15                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 15887                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.820                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 766                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 41.1573 -  4.4595    1.00     3177   182  0.1979 0.2442        
REMARK   3     2  4.4595 -  3.5403    1.00     3042   155  0.1808 0.2245        
REMARK   3     3  3.5403 -  3.0929    1.00     3023   136  0.2209 0.2593        
REMARK   3     4  3.0929 -  2.8102    1.00     2971   146  0.2509 0.3133        
REMARK   3     5  2.8102 -  2.6088    0.97     2908   147  0.2482 0.3286        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.410           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           3555                                  
REMARK   3   ANGLE     :  1.119           4823                                  
REMARK   3   CHIRALITY :  0.035            513                                  
REMARK   3   PLANARITY :  0.004            609                                  
REMARK   3   DIHEDRAL  : 11.997           1295                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 80 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  15.7715 -28.9545  30.1891              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2143 T22:   0.2572                                     
REMARK   3      T33:   0.2175 T12:  -0.0462                                     
REMARK   3      T13:  -0.0171 T23:  -0.0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8292 L22:   1.1326                                     
REMARK   3      L33:   1.4241 L12:  -0.6824                                     
REMARK   3      L13:   0.0592 L23:   0.5700                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1018 S12:   0.0191 S13:  -0.0118                       
REMARK   3      S21:  -0.0351 S22:   0.0881 S23:  -0.1397                       
REMARK   3      S31:  -0.1418 S32:   0.1058 S33:  -0.1744                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 81 THROUGH 220 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  15.6387 -27.9930  19.1268              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1654 T22:   0.2330                                     
REMARK   3      T33:   0.2643 T12:   0.0028                                     
REMARK   3      T13:  -0.0271 T23:   0.0259                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1156 L22:   1.0896                                     
REMARK   3      L33:   2.2692 L12:  -0.2125                                     
REMARK   3      L13:  -0.6799 L23:   0.0437                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0074 S12:   0.0499 S13:   0.0508                       
REMARK   3      S21:  -0.0978 S22:   0.0256 S23:  -0.1282                       
REMARK   3      S31:  -0.0033 S32:   0.0769 S33:  -0.0381                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 221 THROUGH 433 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.1812 -20.2503  18.6668              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3414 T22:   0.2143                                     
REMARK   3      T33:   0.3181 T12:  -0.0361                                     
REMARK   3      T13:   0.0457 T23:  -0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0748 L22:   0.9005                                     
REMARK   3      L33:   2.7995 L12:  -0.0361                                     
REMARK   3      L13:   0.5932 L23:   0.5877                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0109 S12:  -0.0351 S13:   0.1609                       
REMARK   3      S21:  -0.0189 S22:  -0.0974 S23:   0.0962                       
REMARK   3      S31:  -0.5101 S32:  -0.0393 S33:   0.1117                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE ENTRY CONTAINS FRIEDEL PAIRS IN       
REMARK   3  F_PLUS/MINUS COLUMNS AND I_PLUS/MINUS COLUMNS                       
REMARK   4                                                                      
REMARK   4 6A6R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUL-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300007022.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-MAY-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 10.4                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL38B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97980                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15887                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 20.00                              
REMARK 200  R MERGE                    (I) : 0.09500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 44.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THE ENTRY CONTAINS FRIEDEL PAIRS IN F_PLUS/MINUS COLUMNS     
REMARK 200  AND I_PLUS/MINUS COLUMNS                                            
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.75 M AMMONIUM SULFATE, 0.2 M LITHIUM   
REMARK 280  SULFATE, 0.08 M CAPS (N-CYCLOHEXYL-3-AMINOPROPANESULFONIC ACID)     
REMARK 280  BUFFER (PH 10.4), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      108.20333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       54.10167            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       54.10167            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      108.20333            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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     MSE A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ASN A   434                                                      
REMARK 465     GLU A   435                                                      
REMARK 465     ALA A   436                                                      
REMARK 465     LYS A   437                                                      
REMARK 465     MSE A   438                                                      
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    MSE A 291   CG  - SE   -  CE  ANGL. DEV. = -14.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A 160       86.74    -68.61                                   
REMARK 500    ALA A 219       62.70   -119.09                                   
REMARK 500    TYR A 265      -45.80   -143.21                                   
REMARK 500    ASP A 272     -159.75    -82.10                                   
REMARK 500    ASP A 281     -159.95   -106.26                                   
REMARK 500    PRO A 300      108.02    -57.46                                   
REMARK 500    THR A 316     -106.26   -126.53                                   
REMARK 500    HIS A 377       31.13   -153.05                                   
REMARK 500    SER A 417     -140.86     55.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue D1D A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue D1D A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 504                 
DBREF  6A6R A    1   438  PDB    6A6R     6A6R             1    438             
SEQRES   1 A  438  MSE ALA PRO ARG ALA ASN THR LYS ILE ILE VAL VAL GLY          
SEQRES   2 A  438  GLY GLY GLY THR MSE GLY SER SER THR ALA LEU HIS LEU          
SEQRES   3 A  438  LEU ARG ALA GLY TYR THR PRO SER ASN ILE THR VAL LEU          
SEQRES   4 A  438  ASP THR TYR PRO ILE PRO SER ALA GLN SER ALA GLY TYR          
SEQRES   5 A  438  ASP LEU ASN LYS ILE PHE GLY ILE ARG LEU ARG ASN LYS          
SEQRES   6 A  438  PRO ASP LEU GLN LEU TYR LEU GLU ALA LEU ASP MSE TRP          
SEQRES   7 A  438  LYS ASN ASP PRO LEU PHE LYS PRO PHE PHE HIS ASN VAL          
SEQRES   8 A  438  GLY GLN MSE ASP VAL SER SER THR GLU GLU GLY ILE LYS          
SEQRES   9 A  438  LYS LEU ARG MSE ARG TYR GLN SER LEU LEU ASP ALA GLY          
SEQRES  10 A  438  ILE GLY LEU GLU LYS THR ASN PHE LEU LEU GLU SER GLU          
SEQRES  11 A  438  ASP GLU ILE LEU ALA LYS ALA PRO HIS PHE THR ARG GLU          
SEQRES  12 A  438  GLN ILE LYS GLY TRP LYS GLY LEU PHE CSO GLY ASP GLY          
SEQRES  13 A  438  GLY TRP LEU ALA ALA ALA LYS ALA ILE ASN ALA ILE GLY          
SEQRES  14 A  438  GLN PHE LEU LYS GLU GLN GLY VAL LYS PHE GLY PHE GLY          
SEQRES  15 A  438  GLU ALA GLY THR PHE LYS LYS PRO LEU PHE ALA ASP ALA          
SEQRES  16 A  438  ASP GLU LYS THR CYS ILE GLY VAL GLU THR VAL ASP GLY          
SEQRES  17 A  438  THR LYS TYR TYR ALA ASP LYS VAL VAL LEU ALA ALA GLY          
SEQRES  18 A  438  ALA TRP SER SER THR LEU VAL ASP LEU GLU GLU GLN CYS          
SEQRES  19 A  438  VAL SER LYS ALA TRP VAL PHE ALA HIS ILE GLN LEU THR          
SEQRES  20 A  438  PRO ALA GLU ALA ALA ALA TYR LYS ASN THR PRO VAL ILE          
SEQRES  21 A  438  TYR ASP GLY ASP TYR GLY PHE PHE ILE GLU PRO ASP GLU          
SEQRES  22 A  438  ASN GLY ILE ILE LYS VAL CYS ASP GLU PHE PRO GLY PHE          
SEQRES  23 A  438  THR HIS PHE LYS MSE HIS GLN PRO TYR GLY SER PRO VAL          
SEQRES  24 A  438  PRO LYS LEU ILE SER VAL PRO ARG SER HIS ALA LYS HIS          
SEQRES  25 A  438  PRO THR ASP THR TYR PRO HIS ALA SER GLU VAL THR ILE          
SEQRES  26 A  438  LYS LYS ALA ILE ASN ARG PHE LEU PRO ARG PHE ASN ASP          
SEQRES  27 A  438  LYS GLU LEU PHE ASN ARG ALA MSE CYS TRP CYS THR ASP          
SEQRES  28 A  438  THR ALA ASP ALA ASN LEU LEU VAL CYS GLU HIS PRO ARG          
SEQRES  29 A  438  TRP LYS GLY PHE TYR LEU ALA THR GLY ASP SER GLY HIS          
SEQRES  30 A  438  SER PHE LYS LEU LEU PRO ASN ILE GLY LYS HIS VAL VAL          
SEQRES  31 A  438  GLU LEU LEU GLU GLY ARG LEU GLU SER VAL PHE LYS ASP          
SEQRES  32 A  438  ALA TRP ARG TRP ARG PRO GLY SER GLY ASP ALA LEU LYS          
SEQRES  33 A  438  SER ARG ARG ALA ALA PRO ALA LYS ASP LEU ALA ASP MSE          
SEQRES  34 A  438  PRO GLY TRP ARG ASN GLU ALA LYS MSE                          
HET    MSE  A  18       8                                                       
HET    MSE  A  77       8                                                       
HET    MSE  A  94       8                                                       
HET    MSE  A 108       8                                                       
HET    CSO  A 153       7                                                       
HET    MSE  A 291       8                                                       
HET    MSE  A 346       8                                                       
HET    MSE  A 429       8                                                       
HET    FAD  A 501      53                                                       
HET    D1D  A 502       8                                                       
HET    D1D  A 503       8                                                       
HET    SO4  A 504       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     CSO S-HYDROXYCYSTEINE                                                
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     D1D (4S,5S)-1,2-DITHIANE-4,5-DIOL                                    
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    7(C5 H11 N O2 SE)                                            
FORMUL   1  CSO    C3 H7 N O3 S                                                 
FORMUL   2  FAD    C27 H33 N9 O15 P2                                            
FORMUL   3  D1D    2(C4 H8 O2 S2)                                               
FORMUL   5  SO4    O4 S 2-                                                      
FORMUL   6  HOH   *46(H2 O)                                                     
HELIX    1 AA1 GLY A   16  GLY A   30  1                                  15    
HELIX    2 AA2 THR A   32  SER A   34  5                                   3    
HELIX    3 AA3 PRO A   66  ASP A   81  1                                  16    
HELIX    4 AA4 PHE A   84  PRO A   86  5                                   3    
HELIX    5 AA5 THR A   99  ASP A  115  1                                  17    
HELIX    6 AA6 GLY A  119  LYS A  122  5                                   4    
HELIX    7 AA7 SER A  129  ALA A  137  1                                   9    
HELIX    8 AA8 ALA A  160  GLY A  176  1                                  17    
HELIX    9 AA9 PHE A  181  GLY A  185  5                                   5    
HELIX   10 AB1 ALA A  220  ALA A  222  5                                   3    
HELIX   11 AB2 TRP A  223  VAL A  228  1                                   6    
HELIX   12 AB3 THR A  247  ALA A  252  1                                   6    
HELIX   13 AB4 ALA A  253  LYS A  255  5                                   3    
HELIX   14 AB5 PRO A  318  LEU A  333  1                                  16    
HELIX   15 AB6 PRO A  334  ASN A  337  5                                   4    
HELIX   16 AB7 SER A  378  LEU A  382  5                                   5    
HELIX   17 AB8 ASN A  384  GLU A  394  1                                  11    
HELIX   18 AB9 GLU A  398  ASP A  403  1                                   6    
HELIX   19 AC1 ALA A  427  MSE A  429  5                                   3    
SHEET    1 AA1 6 LYS A 178  GLY A 180  0                                        
SHEET    2 AA1 6 ILE A  36  LEU A  39  1  N  VAL A  38   O  LYS A 178           
SHEET    3 AA1 6 ILE A   9  VAL A  12  1  N  VAL A  11   O  THR A  37           
SHEET    4 AA1 6 LYS A 215  LEU A 218  1  O  VAL A 217   N  ILE A  10           
SHEET    5 AA1 6 PHE A 368  THR A 372  1  O  TYR A 369   N  VAL A 216           
SHEET    6 AA1 6 LEU A 358  GLU A 361 -1  N  CYS A 360   O  LEU A 370           
SHEET    1 AA2 3 LYS A  56  PHE A  58  0                                        
SHEET    2 AA2 3 GLY A 157  LEU A 159 -1  O  GLY A 157   N  PHE A  58           
SHEET    3 AA2 3 PHE A  88  HIS A  89 -1  N  HIS A  89   O  TRP A 158           
SHEET    1 AA3 8 ASN A 124  LEU A 127  0                                        
SHEET    2 AA3 8 LYS A 149  CSO A 153 -1  O  GLY A 150   N  LEU A 127           
SHEET    3 AA3 8 GLN A  93  SER A  97 -1  N  GLN A  93   O  CSO A 153           
SHEET    4 AA3 8 VAL A 259  ASP A 262  1  O  VAL A 259   N  MSE A  94           
SHEET    5 AA3 8 GLY A 266  PHE A 268 -1  O  GLY A 266   N  ASP A 262           
SHEET    6 AA3 8 ILE A 276  CYS A 280 -1  O  CYS A 280   N  PHE A 267           
SHEET    7 AA3 8 VAL A 235  GLN A 245 -1  N  ILE A 244   O  ILE A 277           
SHEET    8 AA3 8 PHE A 342  ASP A 351 -1  O  CYS A 347   N  TRP A 239           
SHEET    1 AA4 3 PHE A 187  PHE A 192  0                                        
SHEET    2 AA4 3 CYS A 200  THR A 205 -1  O  GLY A 202   N  LEU A 191           
SHEET    3 AA4 3 LYS A 210  TYR A 212 -1  O  TYR A 211   N  VAL A 203           
SHEET    1 AA5 2 PHE A 286  THR A 287  0                                        
SHEET    2 AA5 2 LYS A 424  ASP A 425  1  O  LYS A 424   N  THR A 287           
SHEET    1 AA6 2 PHE A 289  HIS A 292  0                                        
SHEET    2 AA6 2 LYS A 301  SER A 304 -1  O  ILE A 303   N  LYS A 290           
LINK         C   THR A  17                 N   MSE A  18     1555   1555  1.33  
LINK         C   MSE A  18                 N   GLY A  19     1555   1555  1.33  
LINK         C   ASP A  76                 N   MSE A  77     1555   1555  1.33  
LINK         C   MSE A  77                 N   TRP A  78     1555   1555  1.33  
LINK         C   GLN A  93                 N   MSE A  94     1555   1555  1.33  
LINK         C   MSE A  94                 N   ASP A  95     1555   1555  1.33  
LINK         C   ARG A 107                 N   MSE A 108     1555   1555  1.33  
LINK         C   MSE A 108                 N   ARG A 109     1555   1555  1.33  
LINK         C   PHE A 152                 N   CSO A 153     1555   1555  1.33  
LINK         C   CSO A 153                 N   GLY A 154     1555   1555  1.33  
LINK         C   LYS A 290                 N   MSE A 291     1555   1555  1.32  
LINK         C   MSE A 291                 N   HIS A 292     1555   1555  1.32  
LINK         C   ALA A 345                 N   MSE A 346     1555   1555  1.33  
LINK         C   MSE A 346                 N   CYS A 347     1555   1555  1.33  
LINK         SG  CYS A 347                 C8M FAD A 501     1555   1555  1.70  
LINK         C   ASP A 428                 N   MSE A 429     1555   1555  1.33  
LINK         C   MSE A 429                 N   PRO A 430     1555   1555  1.34  
CISPEP   1 ILE A   44    PRO A   45          0        -1.66                     
SITE     1 AC1 35 VAL A  12  GLY A  13  GLY A  16  THR A  17                    
SITE     2 AC1 35 MSE A  18  LEU A  39  ASP A  40  THR A  41                    
SITE     3 AC1 35 SER A  46  GLN A  48  SER A  49  ALA A  50                    
SITE     4 AC1 35 LYS A  56  ILE A  57  GLY A 185  THR A 186                    
SITE     5 AC1 35 PHE A 187  ALA A 219  ALA A 220  GLY A 221                    
SITE     6 AC1 35 TRP A 223  LEU A 227  CYS A 347  CYS A 349                    
SITE     7 AC1 35 ASP A 374  GLY A 376  HIS A 377  SER A 378                    
SITE     8 AC1 35 PHE A 379  LYS A 380  HOH A 607  HOH A 612                    
SITE     9 AC1 35 HOH A 621  HOH A 626  HOH A 639                               
SITE     1 AC2  5 THR A  41  PRO A  43  LEU A  72  ASP A  76                    
SITE     2 AC2  5 PHE A 181                                                     
SITE     1 AC3  3 TYR A  42  LEU A  72  ASP A  76                               
SITE     1 AC4  6 ARG A   4  ALA A  29  PHE A 342  ASN A 343                    
SITE     2 AC4  6 ARG A 344  HOH A 613                                          
CRYST1   73.199   73.199  162.305  90.00  90.00 120.00 P 32 2 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      0.013661  0.007887  0.000000        0.00000                         
SCALE2      0.000000  0.015775  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006161        0.00000                         
ATOM      1  N   PRO A   3      24.202 -26.226  50.964  1.00 39.57           N  
ATOM      2  CA  PRO A   3      24.370 -27.556  50.369  1.00 39.45           C  
ATOM      3  C   PRO A   3      23.181 -27.929  49.486  1.00 39.98           C  
ATOM      4  O   PRO A   3      22.067 -27.465  49.737  1.00 40.58           O  
ATOM      5  CB  PRO A   3      24.461 -28.485  51.587  1.00 40.00           C  
ATOM      6  CG  PRO A   3      24.792 -27.591  52.741  1.00 40.94           C  
ATOM      7  CD  PRO A   3      24.134 -26.284  52.433  1.00 40.74           C  
ATOM      8  N   ARG A   4      23.417 -28.757  48.470  1.00 38.99           N  
ATOM      9  CA  ARG A   4      22.369 -29.151  47.532  1.00 37.16           C  
ATOM     10  C   ARG A   4      21.221 -29.881  48.220  1.00 39.18           C  
ATOM     11  O   ARG A   4      20.054 -29.686  47.875  1.00 40.09           O  
ATOM     12  CB  ARG A   4      22.943 -30.041  46.427  1.00 35.32           C  
ATOM     13  CG  ARG A   4      23.954 -29.356  45.528  1.00 34.68           C  
ATOM     14  CD  ARG A   4      24.429 -30.282  44.417  1.00 34.05           C  
ATOM     15  NE  ARG A   4      25.309 -29.589  43.480  1.00 32.25           N  
ATOM     16  CZ  ARG A   4      26.162 -30.194  42.663  1.00 29.69           C  
ATOM     17  NH1 ARG A   4      26.260 -31.516  42.663  1.00 26.87           N  
ATOM     18  NH2 ARG A   4      26.922 -29.472  41.851  1.00 28.22           N  
ATOM     19  N   ALA A   5      21.561 -30.723  49.190  1.00 40.05           N  
ATOM     20  CA  ALA A   5      20.570 -31.541  49.877  1.00 40.03           C  
ATOM     21  C   ALA A   5      19.626 -30.700  50.731  1.00 40.62           C  
ATOM     22  O   ALA A   5      18.467 -31.063  50.925  1.00 38.97           O  
ATOM     23  CB  ALA A   5      21.260 -32.588  50.730  1.00 42.15           C  
ATOM     24  N   ASN A   6      20.119 -29.576  51.238  1.00 43.16           N  
ATOM     25  CA  ASN A   6      19.318 -28.736  52.121  1.00 46.08           C  
ATOM     26  C   ASN A   6      18.757 -27.495  51.434  1.00 45.09           C  
ATOM     27  O   ASN A   6      18.137 -26.648  52.081  1.00 47.61           O  
ATOM     28  CB  ASN A   6      20.142 -28.316  53.340  1.00 49.10           C  
ATOM     29  CG  ASN A   6      20.433 -29.476  54.270  1.00 52.25           C  
ATOM     30  OD1 ASN A   6      21.590 -29.831  54.495  1.00 53.84           O  
ATOM     31  ND2 ASN A   6      19.381 -30.075  54.814  1.00 52.93           N  
ATOM     32  N   THR A   7      18.971 -27.387  50.127  1.00 40.83           N  
ATOM     33  CA  THR A   7      18.525 -26.213  49.389  1.00 38.51           C  
ATOM     34  C   THR A   7      17.189 -26.466  48.696  1.00 38.52           C  
ATOM     35  O   THR A   7      16.997 -27.494  48.045  1.00 37.70           O  
ATOM     36  CB  THR A   7      19.575 -25.776  48.349  1.00 36.40           C  
ATOM     37  OG1 THR A   7      20.818 -25.513  49.009  1.00 36.74           O  
ATOM     38  CG2 THR A   7      19.125 -24.520  47.622  1.00 35.54           C  
ATOM     39  N   LYS A   8      16.262 -25.528  48.855  1.00 39.21           N  
ATOM     40  CA  LYS A   8      14.959 -25.624  48.212  1.00 38.59           C  
ATOM     41  C   LYS A   8      14.913 -24.759  46.960  1.00 37.00           C  
ATOM     42  O   LYS A   8      15.365 -23.614  46.967  1.00 35.82           O  
ATOM     43  CB  LYS A   8      13.848 -25.219  49.181  1.00 39.57           C  
ATOM     44  CG  LYS A   8      13.720 -26.131  50.387  1.00 40.89           C  
ATOM     45  CD  LYS A   8      12.635 -25.642  51.326  1.00 43.37           C  
ATOM     46  CE  LYS A   8      11.304 -25.535  50.605  1.00 44.72           C  
ATOM     47  NZ  LYS A   8      10.242 -24.964  51.476  1.00 47.70           N  
ATOM     48  N   ILE A   9      14.372 -25.321  45.885  1.00 36.54           N  
ATOM     49  CA  ILE A   9      14.287 -24.630  44.605  1.00 35.54           C  
ATOM     50  C   ILE A   9      12.859 -24.664  44.072  1.00 35.80           C  
ATOM     51  O   ILE A   9      12.172 -25.680  44.187  1.00 35.50           O  
ATOM     52  CB  ILE A   9      15.230 -25.262  43.551  1.00 34.95           C  
ATOM     53  CG1 ILE A   9      16.649 -25.421  44.104  1.00 35.14           C  
ATOM     54  CG2 ILE A   9      15.241 -24.441  42.269  1.00 34.14           C  
ATOM     55  CD1 ILE A   9      17.367 -24.115  44.327  1.00 35.47           C  
ATOM     56  N   ILE A  10      12.414 -23.553  43.494  1.00 36.52           N  
ATOM     57  CA  ILE A  10      11.131 -23.510  42.799  1.00 35.18           C  
ATOM     58  C   ILE A  10      11.344 -23.319  41.301  1.00 34.96           C  
ATOM     59  O   ILE A  10      12.033 -22.390  40.883  1.00 37.58           O  
ATOM     60  CB  ILE A  10      10.234 -22.381  43.327  1.00 34.80           C  
ATOM     61  CG1 ILE A  10       9.873 -22.631  44.793  1.00 34.29           C  
ATOM     62  CG2 ILE A  10       8.975 -22.260  42.477  1.00 33.39           C  
ATOM     63  CD1 ILE A  10       9.237 -21.440  45.479  1.00 34.03           C  
ATOM     64  N   VAL A  11      10.756 -24.198  40.495  1.00 31.91           N  
ATOM     65  CA  VAL A  11      10.871 -24.088  39.046  1.00 30.25           C  
ATOM     66  C   VAL A  11       9.539 -23.719  38.392  1.00 30.42           C  
ATOM     67  O   VAL A  11       8.666 -24.568  38.207  1.00 30.21           O  
ATOM     68  CB  VAL A  11      11.385 -25.395  38.421  1.00 29.52           C  
ATOM     69  CG1 VAL A  11      11.573 -25.222  36.915  1.00 28.86           C  
ATOM     70  CG2 VAL A  11      12.686 -25.819  39.080  1.00 29.50           C  
ATOM     71  N   VAL A  12       9.391 -22.445  38.046  1.00 30.68           N  
ATOM     72  CA  VAL A  12       8.204 -21.976  37.344  1.00 30.28           C  
ATOM     73  C   VAL A  12       8.279 -22.354  35.870  1.00 34.56           C  
ATOM     74  O   VAL A  12       9.239 -22.009  35.178  1.00 33.30           O  
ATOM     75  CB  VAL A  12       8.038 -20.452  37.469  1.00 28.52           C  
ATOM     76  CG1 VAL A  12       6.796 -19.994  36.722  1.00 26.57           C  
ATOM     77  CG2 VAL A  12       7.979 -20.041  38.938  1.00 29.20           C  
ATOM     78  N   GLY A  13       7.265 -23.069  35.394  1.00 36.79           N  
ATOM     79  CA  GLY A  13       7.243 -23.522  34.017  1.00 36.99           C  
ATOM     80  C   GLY A  13       7.993 -24.829  33.850  1.00 37.43           C  
ATOM     81  O   GLY A  13       8.500 -25.137  32.768  1.00 38.11           O  
ATOM     82  N   GLY A  14       8.054 -25.606  34.928  1.00 35.04           N  
ATOM     83  CA  GLY A  14       8.777 -26.864  34.930  1.00 32.55           C  
ATOM     84  C   GLY A  14       8.108 -27.963  34.124  1.00 31.77           C  
ATOM     85  O   GLY A  14       8.603 -29.089  34.070  1.00 31.10           O  
ATOM     86  N   GLY A  15       6.980 -27.641  33.500  1.00 31.77           N  
ATOM     87  CA  GLY A  15       6.292 -28.586  32.641  1.00 31.53           C  
ATOM     88  C   GLY A  15       6.690 -28.392  31.192  1.00 31.55           C  
ATOM     89  O   GLY A  15       6.229 -29.114  30.308  1.00 32.50           O  
ATOM     90  N   GLY A  16       7.553 -27.410  30.951  1.00 29.78           N  
ATOM     91  CA  GLY A  16       8.005 -27.097  29.611  1.00 28.67           C  
ATOM     92  C   GLY A  16       9.409 -27.595  29.331  1.00 29.36           C  
ATOM     93  O   GLY A  16       9.952 -28.414  30.074  1.00 28.34           O  
ATOM     94  N   THR A  17       9.999 -27.085  28.255  1.00 29.63           N  
ATOM     95  CA  THR A  17      11.300 -27.543  27.781  1.00 28.77           C  
ATOM     96  C   THR A  17      12.431 -27.233  28.757  1.00 30.15           C  
ATOM     97  O   THR A  17      13.044 -28.140  29.323  1.00 31.97           O  
ATOM     98  CB  THR A  17      11.640 -26.908  26.427  1.00 28.78           C  
ATOM     99  OG1 THR A  17      10.521 -27.041  25.543  1.00 29.39           O  
ATOM    100  CG2 THR A  17      12.860 -27.572  25.813  1.00 28.80           C  
HETATM  101  N   MSE A  18      12.705 -25.946  28.944  1.00 27.94           N  
HETATM  102  CA  MSE A  18      13.803 -25.511  29.799  1.00 28.07           C  
HETATM  103  C   MSE A  18      13.498 -25.756  31.282  1.00 28.81           C  
HETATM  104  O   MSE A  18      14.409 -25.947  32.092  1.00 28.10           O  
HETATM  105  CB  MSE A  18      14.109 -24.032  29.548  1.00 28.86           C  
HETATM  106  CG  MSE A  18      14.522 -23.729  28.106  1.00 29.90           C  
HETATM  107 SE   MSE A  18      14.904 -21.846  27.721  1.00 50.34          SE  
HETATM  108  CE  MSE A  18      16.446 -21.590  28.890  1.00 22.61           C  
ATOM    109  N   GLY A  19      12.215 -25.763  31.630  1.00 28.96           N  
ATOM    110  CA  GLY A  19      11.803 -26.006  33.001  1.00 29.07           C  
ATOM    111  C   GLY A  19      12.040 -27.434  33.460  1.00 28.01           C  
ATOM    112  O   GLY A  19      12.617 -27.665  34.527  1.00 27.66           O  
ATOM    113  N   SER A  20      11.593 -28.396  32.659  1.00 26.56           N  
ATOM    114  CA  SER A  20      11.740 -29.803  33.015  1.00 24.37           C  
ATOM    115  C   SER A  20      13.206 -30.219  32.978  1.00 24.48           C  
ATOM    116  O   SER A  20      13.657 -31.014  33.806  1.00 26.49           O  
ATOM    117  CB  SER A  20      10.911 -30.692  32.083  1.00 24.00           C  
ATOM    118  OG  SER A  20      11.319 -30.559  30.729  1.00 23.05           O  
ATOM    119  N   SER A  21      13.946 -29.667  32.021  1.00 23.13           N  
ATOM    120  CA  SER A  21      15.374 -29.931  31.906  1.00 23.45           C  
ATOM    121  C   SER A  21      16.100 -29.505  33.175  1.00 23.92           C  
ATOM    122  O   SER A  21      16.949 -30.233  33.686  1.00 25.07           O  
ATOM    123  CB  SER A  21      15.962 -29.207  30.696  1.00 25.25           C  
ATOM    124  OG  SER A  21      17.333 -29.520  30.537  1.00 27.08           O  
ATOM    125  N   THR A  22      15.755 -28.324  33.678  1.00 24.71           N  
ATOM    126  CA  THR A  22      16.313 -27.829  34.931  1.00 25.47           C  
ATOM    127  C   THR A  22      15.953 -28.764  36.084  1.00 25.85           C  
ATOM    128  O   THR A  22      16.808 -29.126  36.893  1.00 25.68           O  
ATOM    129  CB  THR A  22      15.816 -26.402  35.243  1.00 24.58           C  
ATOM    130  OG1 THR A  22      16.345 -25.486  34.276  1.00 25.28           O  
ATOM    131  CG2 THR A  22      16.258 -25.969  36.630  1.00 24.14           C  
ATOM    132  N   ALA A  23      14.685 -29.161  36.141  1.00 25.67           N  
ATOM    133  CA  ALA A  23      14.204 -30.045  37.195  1.00 27.95           C  
ATOM    134  C   ALA A  23      14.939 -31.378  37.175  1.00 29.93           C  
ATOM    135  O   ALA A  23      15.265 -31.933  38.221  1.00 31.21           O  
ATOM    136  CB  ALA A  23      12.709 -30.267  37.057  1.00 28.75           C  
ATOM    137  N   LEU A  24      15.200 -31.884  35.975  1.00 31.42           N  
ATOM    138  CA  LEU A  24      15.938 -33.132  35.813  1.00 30.34           C  
ATOM    139  C   LEU A  24      17.346 -33.038  36.395  1.00 29.17           C  
ATOM    140  O   LEU A  24      17.761 -33.892  37.177  1.00 29.92           O  
ATOM    141  CB  LEU A  24      16.016 -33.517  34.338  1.00 29.97           C  
ATOM    142  CG  LEU A  24      17.013 -34.627  34.004  1.00 30.30           C  
ATOM    143  CD1 LEU A  24      16.604 -35.943  34.653  1.00 30.58           C  
ATOM    144  CD2 LEU A  24      17.136 -34.784  32.502  1.00 29.42           C  
ATOM    145  N   HIS A  25      18.074 -31.993  36.017  1.00 28.45           N  
ATOM    146  CA  HIS A  25      19.468 -31.858  36.421  1.00 30.55           C  
ATOM    147  C   HIS A  25      19.641 -31.471  37.888  1.00 31.69           C  
ATOM    148  O   HIS A  25      20.718 -31.653  38.454  1.00 32.31           O  
ATOM    149  CB  HIS A  25      20.176 -30.845  35.525  1.00 32.28           C  
ATOM    150  CG  HIS A  25      20.552 -31.397  34.185  1.00 34.46           C  
ATOM    151  ND1 HIS A  25      21.658 -32.196  33.993  1.00 35.59           N  
ATOM    152  CD2 HIS A  25      19.961 -31.274  32.973  1.00 34.77           C  
ATOM    153  CE1 HIS A  25      21.736 -32.537  32.719  1.00 36.10           C  
ATOM    154  NE2 HIS A  25      20.720 -31.990  32.079  1.00 35.37           N  
ATOM    155  N   LEU A  26      18.590 -30.940  38.504  1.00 31.95           N  
ATOM    156  CA  LEU A  26      18.607 -30.714  39.944  1.00 30.50           C  
ATOM    157  C   LEU A  26      18.674 -32.059  40.657  1.00 32.61           C  
ATOM    158  O   LEU A  26      19.474 -32.247  41.573  1.00 35.26           O  
ATOM    159  CB  LEU A  26      17.378 -29.925  40.400  1.00 27.76           C  
ATOM    160  CG  LEU A  26      17.377 -28.418  40.135  1.00 25.45           C  
ATOM    161  CD1 LEU A  26      16.026 -27.807  40.477  1.00 24.80           C  
ATOM    162  CD2 LEU A  26      18.487 -27.735  40.916  1.00 24.96           C  
ATOM    163  N   LEU A  27      17.837 -32.996  40.220  1.00 31.90           N  
ATOM    164  CA  LEU A  27      17.816 -34.333  40.806  1.00 32.65           C  
ATOM    165  C   LEU A  27      19.138 -35.062  40.576  1.00 33.24           C  
ATOM    166  O   LEU A  27      19.651 -35.726  41.476  1.00 33.41           O  
ATOM    167  CB  LEU A  27      16.655 -35.157  40.239  1.00 32.55           C  
ATOM    168  CG  LEU A  27      15.245 -34.787  40.713  1.00 34.40           C  
ATOM    169  CD1 LEU A  27      14.204 -35.734  40.134  1.00 35.36           C  
ATOM    170  CD2 LEU A  27      15.170 -34.782  42.230  1.00 35.84           C  
ATOM    171  N   ARG A  28      19.688 -34.927  39.373  1.00 33.41           N  
ATOM    172  CA  ARG A  28      20.945 -35.586  39.029  1.00 33.85           C  
ATOM    173  C   ARG A  28      22.115 -35.025  39.834  1.00 33.69           C  
ATOM    174  O   ARG A  28      23.091 -35.726  40.093  1.00 34.13           O  
ATOM    175  CB  ARG A  28      21.231 -35.454  37.530  1.00 33.36           C  
ATOM    176  CG  ARG A  28      20.270 -36.232  36.643  1.00 33.84           C  
ATOM    177  CD  ARG A  28      20.766 -36.301  35.202  1.00 33.90           C  
ATOM    178  NE  ARG A  28      19.933 -37.172  34.376  1.00 34.17           N  
ATOM    179  CZ  ARG A  28      20.242 -37.549  33.138  1.00 34.80           C  
ATOM    180  NH1 ARG A  28      21.372 -37.134  32.581  1.00 36.11           N  
ATOM    181  NH2 ARG A  28      19.427 -38.344  32.458  1.00 33.53           N  
ATOM    182  N   ALA A  29      22.006 -33.763  40.235  1.00 33.16           N  
ATOM    183  CA  ALA A  29      23.077 -33.100  40.974  1.00 33.31           C  
ATOM    184  C   ALA A  29      23.082 -33.502  42.444  1.00 33.83           C  
ATOM    185  O   ALA A  29      24.050 -33.249  43.159  1.00 33.76           O  
ATOM    186  CB  ALA A  29      22.956 -31.589  40.842  1.00 33.18           C  
ATOM    187  N   GLY A  30      21.996 -34.121  42.894  1.00 33.87           N  
ATOM    188  CA  GLY A  30      21.909 -34.592  44.263  1.00 34.62           C  
ATOM    189  C   GLY A  30      20.995 -33.755  45.137  1.00 35.20           C  
ATOM    190  O   GLY A  30      21.014 -33.884  46.362  1.00 36.01           O  
ATOM    191  N   TYR A  31      20.202 -32.887  44.512  1.00 34.06           N  
ATOM    192  CA  TYR A  31      19.205 -32.111  45.241  1.00 33.84           C  
ATOM    193  C   TYR A  31      18.105 -33.033  45.749  1.00 34.53           C  
ATOM    194  O   TYR A  31      17.730 -33.989  45.072  1.00 34.41           O  
ATOM    195  CB  TYR A  31      18.610 -31.007  44.358  1.00 31.78           C  
ATOM    196  CG  TYR A  31      19.502 -29.795  44.201  1.00 31.71           C  
ATOM    197  CD1 TYR A  31      20.573 -29.804  43.316  1.00 32.45           C  
ATOM    198  CD2 TYR A  31      19.272 -28.639  44.937  1.00 31.43           C  
ATOM    199  CE1 TYR A  31      21.391 -28.697  43.171  1.00 32.11           C  
ATOM    200  CE2 TYR A  31      20.083 -27.529  44.799  1.00 30.78           C  
ATOM    201  CZ  TYR A  31      21.139 -27.564  43.916  1.00 31.49           C  
ATOM    202  OH  TYR A  31      21.948 -26.459  43.778  1.00 32.04           O  
ATOM    203  N   THR A  32      17.598 -32.750  46.944  1.00 35.79           N  
ATOM    204  CA  THR A  32      16.522 -33.549  47.518  1.00 37.16           C  
ATOM    205  C   THR A  32      15.224 -33.308  46.752  1.00 36.32           C  
ATOM    206  O   THR A  32      14.788 -32.163  46.616  1.00 35.77           O  
ATOM    207  CB  THR A  32      16.309 -33.227  49.009  1.00 39.87           C  
ATOM    208  OG1 THR A  32      17.560 -33.316  49.702  1.00 41.82           O  
ATOM    209  CG2 THR A  32      15.315 -34.196  49.633  1.00 40.75           C  
ATOM    210  N   PRO A  33      14.611 -34.389  46.238  1.00 35.62           N  
ATOM    211  CA  PRO A  33      13.372 -34.325  45.451  1.00 33.92           C  
ATOM    212  C   PRO A  33      12.260 -33.535  46.137  1.00 34.87           C  
ATOM    213  O   PRO A  33      11.611 -32.712  45.491  1.00 35.25           O  
ATOM    214  CB  PRO A  33      12.981 -35.797  45.300  1.00 33.41           C  
ATOM    215  CG  PRO A  33      14.276 -36.523  45.344  1.00 33.94           C  
ATOM    216  CD  PRO A  33      15.137 -35.764  46.321  1.00 35.04           C  
ATOM    217  N   SER A  34      12.056 -33.773  47.428  1.00 36.68           N  
ATOM    218  CA  SER A  34      11.002 -33.093  48.173  1.00 36.67           C  
ATOM    219  C   SER A  34      11.299 -31.606  48.372  1.00 36.73           C  
ATOM    220  O   SER A  34      10.406 -30.829  48.710  1.00 37.07           O  
ATOM    221  CB  SER A  34      10.790 -33.769  49.529  1.00 37.26           C  
ATOM    222  OG  SER A  34      12.003 -33.839  50.254  1.00 38.63           O  
ATOM    223  N   ASN A  35      12.553 -31.215  48.163  1.00 35.88           N  
ATOM    224  CA  ASN A  35      12.932 -29.809  48.245  1.00 36.13           C  
ATOM    225  C   ASN A  35      12.732 -29.074  46.926  1.00 34.07           C  
ATOM    226  O   ASN A  35      12.973 -27.871  46.833  1.00 33.08           O  
ATOM    227  CB  ASN A  35      14.387 -29.671  48.689  1.00 37.94           C  
ATOM    228  CG  ASN A  35      14.566 -29.912  50.168  1.00 41.49           C  
ATOM    229  OD1 ASN A  35      13.617 -29.803  50.945  1.00 42.84           O  
ATOM    230  ND2 ASN A  35      15.791 -30.233  50.572  1.00 42.85           N  
ATOM    231  N   ILE A  36      12.292 -29.805  45.907  1.00 33.51           N  
ATOM    232  CA  ILE A  36      12.066 -29.224  44.589  1.00 32.76           C  
ATOM    233  C   ILE A  36      10.574 -29.132  44.284  1.00 32.73           C  
ATOM    234  O   ILE A  36       9.848 -30.121  44.388  1.00 32.82           O  
ATOM    235  CB  ILE A  36      12.761 -30.045  43.489  1.00 32.16           C  
ATOM    236  CG1 ILE A  36      14.248 -30.207  43.806  1.00 33.21           C  
ATOM    237  CG2 ILE A  36      12.569 -29.392  42.129  1.00 30.43           C  
ATOM    238  CD1 ILE A  36      14.963 -31.156  42.871  1.00 34.20           C  
ATOM    239  N   THR A  37      10.121 -27.940  43.909  1.00 32.45           N  
ATOM    240  CA  THR A  37       8.711 -27.719  43.611  1.00 31.73           C  
ATOM    241  C   THR A  37       8.525 -27.185  42.192  1.00 31.46           C  
ATOM    242  O   THR A  37       9.004 -26.101  41.863  1.00 33.83           O  
ATOM    243  CB  THR A  37       8.072 -26.735  44.612  1.00 31.92           C  
ATOM    244  OG1 THR A  37       8.301 -27.195  45.947  1.00 32.77           O  
ATOM    245  CG2 THR A  37       6.576 -26.628  44.375  1.00 31.73           C  
ATOM    246  N   VAL A  38       7.834 -27.954  41.354  1.00 29.21           N  
ATOM    247  CA  VAL A  38       7.558 -27.544  39.979  1.00 28.37           C  
ATOM    248  C   VAL A  38       6.189 -26.878  39.876  1.00 29.93           C  
ATOM    249  O   VAL A  38       5.185 -27.436  40.316  1.00 30.49           O  
ATOM    250  CB  VAL A  38       7.618 -28.745  39.006  1.00 27.50           C  
ATOM    251  CG1 VAL A  38       6.962 -28.396  37.680  1.00 27.22           C  
ATOM    252  CG2 VAL A  38       9.055 -29.191  38.797  1.00 26.67           C  
ATOM    253  N   LEU A  39       6.151 -25.682  39.299  1.00 30.94           N  
ATOM    254  CA  LEU A  39       4.899 -24.950  39.154  1.00 33.28           C  
ATOM    255  C   LEU A  39       4.606 -24.639  37.696  1.00 36.47           C  
ATOM    256  O   LEU A  39       5.321 -23.868  37.054  1.00 39.87           O  
ATOM    257  CB  LEU A  39       4.933 -23.655  39.967  1.00 31.31           C  
ATOM    258  CG  LEU A  39       5.075 -23.815  41.486  1.00 30.15           C  
ATOM    259  CD1 LEU A  39       5.187 -22.463  42.167  1.00 28.72           C  
ATOM    260  CD2 LEU A  39       3.908 -24.597  42.062  1.00 30.10           C  
ATOM    261  N   ASP A  40       3.545 -25.243  37.175  1.00 37.66           N  
ATOM    262  CA  ASP A  40       3.128 -24.996  35.799  1.00 36.79           C  
ATOM    263  C   ASP A  40       1.608 -24.985  35.728  1.00 36.35           C  
ATOM    264  O   ASP A  40       0.947 -25.718  36.453  1.00 34.26           O  
ATOM    265  CB  ASP A  40       3.710 -26.052  34.847  1.00 41.57           C  
ATOM    266  CG  ASP A  40       3.664 -25.623  33.395  1.00 47.01           C  
ATOM    267  OD1 ASP A  40       2.612 -25.138  32.933  1.00 46.43           O  
ATOM    268  OD2 ASP A  40       4.689 -25.787  32.705  1.00 54.82           O  
ATOM    269  N   THR A  41       1.062 -24.154  34.846  1.00 36.20           N  
ATOM    270  CA  THR A  41      -0.378 -24.110  34.613  1.00 36.30           C  
ATOM    271  C   THR A  41      -0.928 -25.488  34.238  1.00 32.69           C  
ATOM    272  O   THR A  41      -1.978 -25.899  34.724  1.00 33.56           O  
ATOM    273  CB  THR A  41      -0.735 -23.108  33.496  1.00 34.74           C  
ATOM    274  OG1 THR A  41      -0.149 -21.834  33.790  1.00 36.62           O  
ATOM    275  CG2 THR A  41      -2.243 -22.959  33.372  1.00 34.39           C  
ATOM    276  N   TYR A  42      -0.211 -26.196  33.373  1.00 30.92           N  
ATOM    277  CA  TYR A  42      -0.611 -27.539  32.970  1.00 30.36           C  
ATOM    278  C   TYR A  42       0.352 -28.600  33.499  1.00 30.68           C  
ATOM    279  O   TYR A  42       1.545 -28.343  33.651  1.00 31.05           O  
ATOM    280  CB  TYR A  42      -0.702 -27.635  31.446  1.00 28.46           C  
ATOM    281  CG  TYR A  42      -1.843 -26.851  30.847  1.00 28.39           C  
ATOM    282  CD1 TYR A  42      -3.084 -27.439  30.646  1.00 28.19           C  
ATOM    283  CD2 TYR A  42      -1.679 -25.522  30.474  1.00 28.97           C  
ATOM    284  CE1 TYR A  42      -4.131 -26.727  30.093  1.00 28.96           C  
ATOM    285  CE2 TYR A  42      -2.722 -24.802  29.919  1.00 29.44           C  
ATOM    286  CZ  TYR A  42      -3.946 -25.410  29.731  1.00 30.22           C  
ATOM    287  OH  TYR A  42      -4.990 -24.701  29.181  1.00 31.68           O  
ATOM    288  N   PRO A  43      -0.171 -29.799  33.791  1.00 30.38           N  
ATOM    289  CA  PRO A  43       0.682 -30.909  34.228  1.00 30.46           C  
ATOM    290  C   PRO A  43       1.696 -31.305  33.158  1.00 30.72           C  
ATOM    291  O   PRO A  43       1.407 -31.182  31.970  1.00 30.54           O  
ATOM    292  CB  PRO A  43      -0.317 -32.040  34.480  1.00 31.23           C  
ATOM    293  CG  PRO A  43      -1.606 -31.349  34.761  1.00 32.07           C  
ATOM    294  CD  PRO A  43      -1.601 -30.138  33.875  1.00 31.58           C  
ATOM    295  N   ILE A  44       2.867 -31.770  33.583  1.00 31.10           N  
ATOM    296  CA  ILE A  44       3.924 -32.169  32.662  1.00 31.55           C  
ATOM    297  C   ILE A  44       3.566 -33.487  31.970  1.00 32.86           C  
ATOM    298  O   ILE A  44       3.137 -34.438  32.625  1.00 33.33           O  
ATOM    299  CB  ILE A  44       5.288 -32.295  33.398  1.00 25.07           C  
ATOM    300  CG1 ILE A  44       6.407 -32.691  32.431  1.00 25.08           C  
ATOM    301  CG2 ILE A  44       5.207 -33.283  34.553  1.00 25.70           C  
ATOM    302  CD1 ILE A  44       7.794 -32.500  33.005  1.00 24.11           C  
ATOM    303  N   PRO A  45       3.711 -33.542  30.633  1.00 32.92           N  
ATOM    304  CA  PRO A  45       4.147 -32.465  29.732  1.00 32.61           C  
ATOM    305  C   PRO A  45       3.061 -31.419  29.467  1.00 31.40           C  
ATOM    306  O   PRO A  45       1.942 -31.775  29.094  1.00 30.18           O  
ATOM    307  CB  PRO A  45       4.503 -33.215  28.445  1.00 32.45           C  
ATOM    308  CG  PRO A  45       3.629 -34.410  28.464  1.00 32.41           C  
ATOM    309  CD  PRO A  45       3.511 -34.811  29.907  1.00 32.49           C  
ATOM    310  N   SER A  46       3.405 -30.147  29.659  1.00 30.95           N  
ATOM    311  CA  SER A  46       2.456 -29.046  29.524  1.00 31.36           C  
ATOM    312  C   SER A  46       1.807 -29.008  28.144  1.00 33.42           C  
ATOM    313  O   SER A  46       2.491 -28.935  27.125  1.00 35.23           O  
ATOM    314  CB  SER A  46       3.148 -27.711  29.806  1.00 30.92           C  
ATOM    315  OG  SER A  46       2.231 -26.633  29.716  1.00 30.82           O  
ATOM    316  N   ALA A  47       0.480 -29.049  28.124  1.00 33.05           N  
ATOM    317  CA  ALA A  47      -0.272 -29.105  26.878  1.00 32.27           C  
ATOM    318  C   ALA A  47      -0.172 -27.816  26.061  1.00 34.54           C  
ATOM    319  O   ALA A  47      -0.525 -27.803  24.881  1.00 36.63           O  
ATOM    320  CB  ALA A  47      -1.730 -29.426  27.165  1.00 30.79           C  
ATOM    321  N   GLN A  48       0.300 -26.735  26.676  1.00 34.60           N  
ATOM    322  CA  GLN A  48       0.437 -25.474  25.949  1.00 35.53           C  
ATOM    323  C   GLN A  48       1.904 -25.117  25.697  1.00 34.38           C  
ATOM    324  O   GLN A  48       2.205 -24.070  25.126  1.00 33.53           O  
ATOM    325  CB  GLN A  48      -0.260 -24.335  26.699  1.00 36.48           C  
ATOM    326  CG  GLN A  48       0.454 -23.876  27.958  1.00 37.01           C  
ATOM    327  CD  GLN A  48      -0.196 -22.654  28.583  1.00 38.62           C  
ATOM    328  OE1 GLN A  48      -1.178 -22.122  28.061  1.00 40.18           O  
ATOM    329  NE2 GLN A  48       0.349 -22.204  29.710  1.00 37.66           N  
ATOM    330  N   SER A  49       2.808 -25.992  26.127  1.00 33.81           N  
ATOM    331  CA  SER A  49       4.239 -25.801  25.897  1.00 33.65           C  
ATOM    332  C   SER A  49       4.574 -25.909  24.415  1.00 34.23           C  
ATOM    333  O   SER A  49       3.924 -26.651  23.680  1.00 34.45           O  
ATOM    334  CB  SER A  49       5.049 -26.829  26.690  1.00 32.49           C  
ATOM    335  OG  SER A  49       6.401 -26.855  26.267  1.00 31.98           O  
ATOM    336  N   ALA A  50       5.593 -25.173  23.977  1.00 34.56           N  
ATOM    337  CA  ALA A  50       6.014 -25.218  22.579  1.00 34.38           C  
ATOM    338  C   ALA A  50       6.629 -26.576  22.245  1.00 34.68           C  
ATOM    339  O   ALA A  50       6.680 -26.980  21.082  1.00 35.44           O  
ATOM    340  CB  ALA A  50       6.997 -24.096  22.279  1.00 33.14           C  
ATOM    341  N   GLY A  51       7.090 -27.279  23.276  1.00 33.40           N  
ATOM    342  CA  GLY A  51       7.661 -28.602  23.108  1.00 34.10           C  
ATOM    343  C   GLY A  51       6.613 -29.700  23.105  1.00 34.79           C  
ATOM    344  O   GLY A  51       6.944 -30.882  23.008  1.00 33.63           O  
ATOM    345  N   TYR A  52       5.347 -29.309  23.218  1.00 35.91           N  
ATOM    346  CA  TYR A  52       4.237 -30.256  23.171  1.00 36.62           C  
ATOM    347  C   TYR A  52       3.863 -30.539  21.718  1.00 35.54           C  
ATOM    348  O   TYR A  52       2.792 -30.151  21.254  1.00 33.99           O  
ATOM    349  CB  TYR A  52       3.033 -29.712  23.949  1.00 38.00           C  
ATOM    350  CG  TYR A  52       1.963 -30.741  24.239  1.00 39.38           C  
ATOM    351  CD1 TYR A  52       2.195 -31.776  25.136  1.00 39.56           C  
ATOM    352  CD2 TYR A  52       0.717 -30.670  23.630  1.00 39.76           C  
ATOM    353  CE1 TYR A  52       1.223 -32.718  25.408  1.00 39.52           C  
ATOM    354  CE2 TYR A  52      -0.263 -31.608  23.898  1.00 39.77           C  
ATOM    355  CZ  TYR A  52      -0.003 -32.629  24.789  1.00 40.84           C  
ATOM    356  OH  TYR A  52      -0.970 -33.568  25.063  1.00 43.32           O  
ATOM    357  N   ASP A  53       4.758 -31.223  21.012  1.00 35.46           N  
ATOM    358  CA  ASP A  53       4.639 -31.430  19.573  1.00 36.91           C  
ATOM    359  C   ASP A  53       4.940 -32.884  19.202  1.00 37.77           C  
ATOM    360  O   ASP A  53       5.603 -33.595  19.958  1.00 36.85           O  
ATOM    361  CB  ASP A  53       5.596 -30.485  18.840  1.00 38.97           C  
ATOM    362  CG  ASP A  53       5.238 -30.291  17.376  1.00 41.96           C  
ATOM    363  OD1 ASP A  53       4.547 -31.153  16.794  1.00 44.33           O  
ATOM    364  OD2 ASP A  53       5.663 -29.266  16.804  1.00 42.69           O  
ATOM    365  N   LEU A  54       4.453 -33.319  18.041  1.00 39.05           N  
ATOM    366  CA  LEU A  54       4.804 -34.632  17.504  1.00 37.83           C  
ATOM    367  C   LEU A  54       6.309 -34.753  17.314  1.00 36.20           C  
ATOM    368  O   LEU A  54       6.907 -35.781  17.624  1.00 36.70           O  
ATOM    369  CB  LEU A  54       4.099 -34.888  16.170  1.00 40.02           C  
ATOM    370  CG  LEU A  54       2.619 -35.269  16.199  1.00 41.77           C  
ATOM    371  CD1 LEU A  54       2.138 -35.597  14.796  1.00 42.80           C  
ATOM    372  CD2 LEU A  54       2.375 -36.439  17.140  1.00 41.53           C  
ATOM    373  N   ASN A  55       6.919 -33.693  16.803  1.00 35.46           N  
ATOM    374  CA  ASN A  55       8.338 -33.724  16.501  1.00 34.88           C  
ATOM    375  C   ASN A  55       8.954 -32.335  16.384  1.00 33.57           C  
ATOM    376  O   ASN A  55       8.257 -31.350  16.149  1.00 33.40           O  
ATOM    377  CB  ASN A  55       8.580 -34.518  15.210  1.00 36.62           C  
ATOM    378  CG  ASN A  55       7.586 -34.173  14.114  1.00 38.83           C  
ATOM    379  OD1 ASN A  55       7.195 -33.016  13.952  1.00 39.56           O  
ATOM    380  ND2 ASN A  55       7.167 -35.182  13.356  1.00 40.62           N  
ATOM    381  N   LYS A  56      10.266 -32.270  16.582  1.00 32.63           N  
ATOM    382  CA  LYS A  56      11.045 -31.072  16.306  1.00 32.83           C  
ATOM    383  C   LYS A  56      12.214 -31.493  15.439  1.00 35.39           C  
ATOM    384  O   LYS A  56      12.433 -32.683  15.241  1.00 36.87           O  
ATOM    385  CB  LYS A  56      11.541 -30.409  17.594  1.00 31.21           C  
ATOM    386  CG  LYS A  56      10.447 -29.932  18.528  1.00 31.07           C  
ATOM    387  CD  LYS A  56       9.664 -28.775  17.937  1.00 31.89           C  
ATOM    388  CE  LYS A  56       8.684 -28.221  18.953  1.00 31.19           C  
ATOM    389  NZ  LYS A  56       7.680 -27.314  18.332  1.00 32.34           N  
ATOM    390  N   ILE A  57      12.974 -30.530  14.933  1.00 36.67           N  
ATOM    391  CA  ILE A  57      14.157 -30.850  14.145  1.00 37.03           C  
ATOM    392  C   ILE A  57      15.427 -30.698  14.976  1.00 38.30           C  
ATOM    393  O   ILE A  57      15.587 -29.712  15.694  1.00 37.78           O  
ATOM    394  CB  ILE A  57      14.266 -29.954  12.904  1.00 36.93           C  
ATOM    395  CG1 ILE A  57      13.004 -30.064  12.049  1.00 36.31           C  
ATOM    396  CG2 ILE A  57      15.496 -30.315  12.097  1.00 38.73           C  
ATOM    397  CD1 ILE A  57      12.996 -29.124  10.864  1.00 36.68           C  
ATOM    398  N   PHE A  58      16.322 -31.679  14.886  1.00 39.72           N  
ATOM    399  CA  PHE A  58      17.650 -31.545  15.476  1.00 40.54           C  
ATOM    400  C   PHE A  58      18.677 -31.328  14.376  1.00 43.24           C  
ATOM    401  O   PHE A  58      18.825 -32.157  13.478  1.00 44.41           O  
ATOM    402  CB  PHE A  58      18.026 -32.773  16.308  1.00 40.47           C  
ATOM    403  CG  PHE A  58      19.334 -32.628  17.038  1.00 41.48           C  
ATOM    404  CD1 PHE A  58      19.438 -31.786  18.130  1.00 41.63           C  
ATOM    405  CD2 PHE A  58      20.457 -33.329  16.634  1.00 43.09           C  
ATOM    406  CE1 PHE A  58      20.634 -31.641  18.806  1.00 41.73           C  
ATOM    407  CE2 PHE A  58      21.656 -33.189  17.307  1.00 43.59           C  
ATOM    408  CZ  PHE A  58      21.745 -32.345  18.396  1.00 42.74           C  
ATOM    409  N   GLY A  59      19.380 -30.205  14.441  1.00 44.95           N  
ATOM    410  CA  GLY A  59      20.364 -29.882  13.428  1.00 46.94           C  
ATOM    411  C   GLY A  59      21.357 -28.863  13.930  1.00 47.71           C  
ATOM    412  O   GLY A  59      21.064 -28.098  14.846  1.00 46.87           O  
ATOM    413  N   ILE A  60      22.539 -28.852  13.328  1.00 50.43           N  
ATOM    414  CA  ILE A  60      23.576 -27.918  13.729  1.00 54.20           C  
ATOM    415  C   ILE A  60      23.272 -26.517  13.199  1.00 61.34           C  
ATOM    416  O   ILE A  60      22.789 -26.353  12.077  1.00 62.42           O  
ATOM    417  CB  ILE A  60      24.972 -28.387  13.247  1.00 54.11           C  
ATOM    418  CG1 ILE A  60      26.070 -27.472  13.798  1.00 54.08           C  
ATOM    419  CG2 ILE A  60      25.029 -28.481  11.723  1.00 55.48           C  
ATOM    420  CD1 ILE A  60      27.470 -27.908  13.434  1.00 54.88           C  
ATOM    421  N   ARG A  61      23.530 -25.513  14.030  1.00 65.24           N  
ATOM    422  CA  ARG A  61      23.372 -24.119  13.638  1.00 68.31           C  
ATOM    423  C   ARG A  61      24.371 -23.251  14.389  1.00 65.55           C  
ATOM    424  O   ARG A  61      24.394 -23.236  15.618  1.00 64.39           O  
ATOM    425  CB  ARG A  61      21.941 -23.639  13.892  1.00 72.38           C  
ATOM    426  CG  ARG A  61      21.025 -23.814  12.691  1.00 78.38           C  
ATOM    427  CD  ARG A  61      19.576 -23.496  13.015  1.00 82.04           C  
ATOM    428  NE  ARG A  61      18.748 -23.504  11.811  1.00 87.51           N  
ATOM    429  CZ  ARG A  61      18.187 -24.591  11.290  1.00 89.11           C  
ATOM    430  NH1 ARG A  61      18.359 -25.773  11.868  1.00 88.28           N  
ATOM    431  NH2 ARG A  61      17.452 -24.497  10.189  1.00 90.06           N  
ATOM    432  N   LEU A  62      25.200 -22.533  13.641  1.00 64.95           N  
ATOM    433  CA  LEU A  62      26.252 -21.714  14.227  1.00 63.45           C  
ATOM    434  C   LEU A  62      26.016 -20.236  13.947  1.00 65.59           C  
ATOM    435  O   LEU A  62      26.606 -19.670  13.025  1.00 70.04           O  
ATOM    436  CB  LEU A  62      27.619 -22.141  13.689  1.00 63.11           C  
ATOM    437  CG  LEU A  62      27.936 -23.636  13.765  1.00 62.19           C  
ATOM    438  CD1 LEU A  62      29.314 -23.929  13.191  1.00 64.08           C  
ATOM    439  CD2 LEU A  62      27.828 -24.144  15.196  1.00 60.13           C  
ATOM    440  N   ARG A  63      25.149 -19.615  14.740  1.00 63.27           N  
ATOM    441  CA  ARG A  63      24.851 -18.196  14.586  1.00 63.79           C  
ATOM    442  C   ARG A  63      25.398 -17.393  15.764  1.00 61.97           C  
ATOM    443  O   ARG A  63      25.595 -16.182  15.663  1.00 64.93           O  
ATOM    444  CB  ARG A  63      23.342 -17.970  14.445  1.00 64.32           C  
ATOM    445  CG  ARG A  63      22.742 -18.516  13.152  1.00 66.79           C  
ATOM    446  CD  ARG A  63      23.257 -17.766  11.925  1.00 71.30           C  
ATOM    447  NE  ARG A  63      22.792 -16.381  11.878  1.00 74.52           N  
ATOM    448  CZ  ARG A  63      23.157 -15.498  10.951  1.00 78.76           C  
ATOM    449  NH1 ARG A  63      24.000 -15.851   9.989  1.00 80.26           N  
ATOM    450  NH2 ARG A  63      22.683 -14.260  10.986  1.00 80.51           N  
ATOM    451  N   ASN A  64      25.642 -18.077  16.880  1.00 57.65           N  
ATOM    452  CA  ASN A  64      26.207 -17.444  18.068  1.00 55.47           C  
ATOM    453  C   ASN A  64      27.385 -18.230  18.630  1.00 53.20           C  
ATOM    454  O   ASN A  64      27.594 -19.389  18.274  1.00 50.47           O  
ATOM    455  CB  ASN A  64      25.135 -17.274  19.143  1.00 54.74           C  
ATOM    456  CG  ASN A  64      24.185 -16.135  18.841  1.00 56.73           C  
ATOM    457  OD1 ASN A  64      24.585 -15.105  18.297  1.00 58.65           O  
ATOM    458  ND2 ASN A  64      22.918 -16.313  19.193  1.00 55.85           N  
ATOM    459  N   LYS A  65      28.148 -17.596  19.516  1.00 55.13           N  
ATOM    460  CA  LYS A  65      29.362 -18.208  20.049  1.00 55.20           C  
ATOM    461  C   LYS A  65      29.149 -19.469  20.915  1.00 50.88           C  
ATOM    462  O   LYS A  65      29.998 -20.359  20.895  1.00 49.67           O  
ATOM    463  CB  LYS A  65      30.179 -17.171  20.840  1.00 58.27           C  
ATOM    464  CG  LYS A  65      29.434 -16.452  21.952  1.00 60.23           C  
ATOM    465  CD  LYS A  65      30.391 -15.776  22.931  1.00 62.72           C  
ATOM    466  CE  LYS A  65      29.661 -15.330  24.194  1.00 61.76           C  
ATOM    467  NZ  LYS A  65      30.571 -14.701  25.190  1.00 64.04           N  
ATOM    468  N   PRO A  66      28.032 -19.574  21.668  1.00 48.15           N  
ATOM    469  CA  PRO A  66      27.984 -20.825  22.435  1.00 44.92           C  
ATOM    470  C   PRO A  66      27.329 -21.989  21.683  1.00 41.48           C  
ATOM    471  O   PRO A  66      27.320 -23.110  22.191  1.00 40.56           O  
ATOM    472  CB  PRO A  66      27.149 -20.437  23.653  1.00 44.18           C  
ATOM    473  CG  PRO A  66      26.175 -19.456  23.110  1.00 44.75           C  
ATOM    474  CD  PRO A  66      26.906 -18.686  22.026  1.00 47.51           C  
ATOM    475  N   ASP A  67      26.802 -21.719  20.492  1.00 40.29           N  
ATOM    476  CA  ASP A  67      26.027 -22.700  19.729  1.00 38.56           C  
ATOM    477  C   ASP A  67      26.757 -24.014  19.448  1.00 38.11           C  
ATOM    478  O   ASP A  67      26.148 -25.086  19.467  1.00 35.16           O  
ATOM    479  CB  ASP A  67      25.579 -22.087  18.401  1.00 39.10           C  
ATOM    480  CG  ASP A  67      24.517 -21.020  18.579  1.00 38.59           C  
ATOM    481  OD1 ASP A  67      23.909 -20.958  19.669  1.00 38.71           O  
ATOM    482  OD2 ASP A  67      24.282 -20.253  17.622  1.00 37.43           O  
ATOM    483  N   LEU A  68      28.057 -23.931  19.182  1.00 40.72           N  
ATOM    484  CA  LEU A  68      28.830 -25.117  18.832  1.00 41.84           C  
ATOM    485  C   LEU A  68      28.913 -26.106  19.994  1.00 41.34           C  
ATOM    486  O   LEU A  68      28.680 -27.302  19.813  1.00 41.60           O  
ATOM    487  CB  LEU A  68      30.235 -24.728  18.373  1.00 43.76           C  
ATOM    488  CG  LEU A  68      31.128 -25.880  17.909  1.00 43.60           C  
ATOM    489  CD1 LEU A  68      30.414 -26.744  16.879  1.00 43.80           C  
ATOM    490  CD2 LEU A  68      32.426 -25.346  17.338  1.00 45.48           C  
ATOM    491  N   GLN A  69      29.233 -25.612  21.185  1.00 39.64           N  
ATOM    492  CA  GLN A  69      29.353 -26.490  22.343  1.00 39.36           C  
ATOM    493  C   GLN A  69      27.993 -27.010  22.812  1.00 38.02           C  
ATOM    494  O   GLN A  69      27.884 -28.146  23.273  1.00 37.54           O  
ATOM    495  CB  GLN A  69      30.057 -25.776  23.493  1.00 40.81           C  
ATOM    496  CG  GLN A  69      30.313 -26.678  24.688  1.00 42.36           C  
ATOM    497  CD  GLN A  69      30.939 -25.947  25.850  1.00 44.84           C  
ATOM    498  OE1 GLN A  69      31.681 -24.982  25.664  1.00 47.67           O  
ATOM    499  NE2 GLN A  69      30.639 -26.399  27.062  1.00 44.15           N  
ATOM    500  N   LEU A  70      26.962 -26.178  22.696  1.00 36.09           N  
ATOM    501  CA  LEU A  70      25.608 -26.584  23.057  1.00 32.56           C  
ATOM    502  C   LEU A  70      25.102 -27.694  22.140  1.00 34.20           C  
ATOM    503  O   LEU A  70      24.463 -28.644  22.594  1.00 34.18           O  
ATOM    504  CB  LEU A  70      24.659 -25.386  23.008  1.00 30.54           C  
ATOM    505  CG  LEU A  70      24.826 -24.341  24.113  1.00 29.28           C  
ATOM    506  CD1 LEU A  70      23.924 -23.141  23.867  1.00 29.45           C  
ATOM    507  CD2 LEU A  70      24.537 -24.958  25.471  1.00 26.41           C  
ATOM    508  N   TYR A  71      25.392 -27.566  20.848  1.00 35.26           N  
ATOM    509  CA  TYR A  71      25.006 -28.575  19.867  1.00 34.90           C  
ATOM    510  C   TYR A  71      25.716 -29.900  20.117  1.00 36.11           C  
ATOM    511  O   TYR A  71      25.074 -30.945  20.203  1.00 36.26           O  
ATOM    512  CB  TYR A  71      25.300 -28.082  18.449  1.00 35.72           C  
ATOM    513  CG  TYR A  71      25.268 -29.166  17.391  1.00 35.53           C  
ATOM    514  CD1 TYR A  71      24.062 -29.642  16.890  1.00 35.62           C  
ATOM    515  CD2 TYR A  71      26.445 -29.705  16.885  1.00 36.53           C  
ATOM    516  CE1 TYR A  71      24.031 -30.632  15.920  1.00 36.58           C  
ATOM    517  CE2 TYR A  71      26.424 -30.694  15.915  1.00 37.22           C  
ATOM    518  CZ  TYR A  71      25.215 -31.152  15.435  1.00 37.25           C  
ATOM    519  OH  TYR A  71      25.193 -32.136  14.470  1.00 37.84           O  
ATOM    520  N   LEU A  72      27.041 -29.851  20.228  1.00 37.48           N  
ATOM    521  CA  LEU A  72      27.836 -31.050  20.473  1.00 37.97           C  
ATOM    522  C   LEU A  72      27.416 -31.739  21.769  1.00 39.09           C  
ATOM    523  O   LEU A  72      27.374 -32.967  21.847  1.00 38.86           O  
ATOM    524  CB  LEU A  72      29.327 -30.708  20.522  1.00 36.86           C  
ATOM    525  CG  LEU A  72      29.992 -30.202  19.239  1.00 38.02           C  
ATOM    526  CD1 LEU A  72      31.480 -29.970  19.465  1.00 38.52           C  
ATOM    527  CD2 LEU A  72      29.763 -31.164  18.082  1.00 37.29           C  
ATOM    528  N   GLU A  73      27.097 -30.939  22.781  1.00 39.49           N  
ATOM    529  CA  GLU A  73      26.658 -31.463  24.069  1.00 40.18           C  
ATOM    530  C   GLU A  73      25.332 -32.208  23.932  1.00 38.38           C  
ATOM    531  O   GLU A  73      25.182 -33.332  24.413  1.00 37.69           O  
ATOM    532  CB  GLU A  73      26.525 -30.325  25.081  1.00 43.26           C  
ATOM    533  CG  GLU A  73      26.516 -30.758  26.532  1.00 46.69           C  
ATOM    534  CD  GLU A  73      26.720 -29.588  27.478  1.00 50.45           C  
ATOM    535  OE1 GLU A  73      27.005 -29.829  28.672  1.00 52.15           O  
ATOM    536  OE2 GLU A  73      26.602 -28.428  27.025  1.00 50.59           O  
ATOM    537  N   ALA A  74      24.375 -31.576  23.263  1.00 37.54           N  
ATOM    538  CA  ALA A  74      23.051 -32.157  23.080  1.00 35.92           C  
ATOM    539  C   ALA A  74      23.091 -33.391  22.186  1.00 35.70           C  
ATOM    540  O   ALA A  74      22.366 -34.360  22.418  1.00 35.93           O  
ATOM    541  CB  ALA A  74      22.101 -31.120  22.500  1.00 35.50           C  
ATOM    542  N   LEU A  75      23.930 -33.342  21.157  1.00 34.88           N  
ATOM    543  CA  LEU A  75      24.088 -34.470  20.250  1.00 33.17           C  
ATOM    544  C   LEU A  75      24.564 -35.693  21.021  1.00 32.61           C  
ATOM    545  O   LEU A  75      24.006 -36.779  20.878  1.00 33.63           O  
ATOM    546  CB  LEU A  75      25.069 -34.132  19.124  1.00 33.48           C  
ATOM    547  CG  LEU A  75      25.345 -35.220  18.083  1.00 33.48           C  
ATOM    548  CD1 LEU A  75      24.056 -35.669  17.413  1.00 33.31           C  
ATOM    549  CD2 LEU A  75      26.340 -34.724  17.049  1.00 33.97           C  
ATOM    550  N   ASP A  76      25.582 -35.496  21.852  1.00 31.98           N  
ATOM    551  CA  ASP A  76      26.159 -36.577  22.641  1.00 32.11           C  
ATOM    552  C   ASP A  76      25.109 -37.236  23.531  1.00 31.47           C  
ATOM    553  O   ASP A  76      25.084 -38.460  23.670  1.00 31.09           O  
ATOM    554  CB  ASP A  76      27.319 -36.050  23.489  1.00 32.66           C  
ATOM    555  CG  ASP A  76      28.302 -37.140  23.876  1.00 33.71           C  
ATOM    556  OD1 ASP A  76      28.264 -38.225  23.258  1.00 33.04           O  
ATOM    557  OD2 ASP A  76      29.123 -36.911  24.790  1.00 34.84           O  
HETATM  558  N   MSE A  77      24.229 -36.423  24.108  1.00 31.20           N  
HETATM  559  CA  MSE A  77      23.182 -36.936  24.983  1.00 31.19           C  
HETATM  560  C   MSE A  77      21.989 -37.494  24.207  1.00 32.65           C  
HETATM  561  O   MSE A  77      21.391 -38.487  24.624  1.00 33.68           O  
HETATM  562  CB  MSE A  77      22.716 -35.848  25.944  1.00 30.43           C  
HETATM  563  CG  MSE A  77      23.826 -35.361  26.864  1.00 30.62           C  
HETATM  564 SE   MSE A  77      23.249 -33.998  28.143  1.00 50.36          SE  
HETATM  565  CE  MSE A  77      22.286 -35.133  29.406  1.00 44.77           C  
ATOM    566  N   TRP A  78      21.638 -36.868  23.086  1.00 32.59           N  
ATOM    567  CA  TRP A  78      20.547 -37.377  22.257  1.00 32.45           C  
ATOM    568  C   TRP A  78      20.863 -38.771  21.716  1.00 34.29           C  
ATOM    569  O   TRP A  78      19.957 -39.543  21.411  1.00 35.81           O  
ATOM    570  CB  TRP A  78      20.249 -36.430  21.091  1.00 31.77           C  
ATOM    571  CG  TRP A  78      19.298 -35.306  21.409  1.00 31.01           C  
ATOM    572  CD1 TRP A  78      19.542 -33.968  21.279  1.00 31.18           C  
ATOM    573  CD2 TRP A  78      17.956 -35.420  21.897  1.00 30.55           C  
ATOM    574  NE1 TRP A  78      18.439 -33.244  21.654  1.00 29.74           N  
ATOM    575  CE2 TRP A  78      17.448 -34.111  22.041  1.00 29.49           C  
ATOM    576  CE3 TRP A  78      17.129 -36.501  22.229  1.00 31.77           C  
ATOM    577  CZ2 TRP A  78      16.159 -33.852  22.504  1.00 28.67           C  
ATOM    578  CZ3 TRP A  78      15.848 -36.243  22.688  1.00 31.68           C  
ATOM    579  CH2 TRP A  78      15.376 -34.929  22.820  1.00 29.95           C  
ATOM    580  N   LYS A  79      22.149 -39.088  21.602  1.00 34.66           N  
ATOM    581  CA  LYS A  79      22.576 -40.369  21.051  1.00 36.56           C  
ATOM    582  C   LYS A  79      22.877 -41.416  22.121  1.00 37.12           C  
ATOM    583  O   LYS A  79      22.728 -42.613  21.880  1.00 38.39           O  
ATOM    584  CB  LYS A  79      23.817 -40.183  20.170  1.00 39.01           C  
ATOM    585  CG  LYS A  79      23.571 -39.442  18.871  1.00 41.05           C  
ATOM    586  CD  LYS A  79      24.885 -39.064  18.197  1.00 43.15           C  
ATOM    587  CE  LYS A  79      25.721 -40.286  17.840  1.00 44.59           C  
ATOM    588  NZ  LYS A  79      25.112 -41.096  16.750  1.00 44.04           N  
ATOM    589  N   ASN A  80      23.306 -40.971  23.298  1.00 36.60           N  
ATOM    590  CA  ASN A  80      23.835 -41.900  24.291  1.00 37.41           C  
ATOM    591  C   ASN A  80      23.105 -41.929  25.629  1.00 37.53           C  
ATOM    592  O   ASN A  80      23.139 -42.941  26.324  1.00 39.40           O  
ATOM    593  CB  ASN A  80      25.315 -41.597  24.541  1.00 38.18           C  
ATOM    594  CG  ASN A  80      26.145 -41.694  23.281  1.00 39.22           C  
ATOM    595  OD1 ASN A  80      26.465 -42.790  22.821  1.00 39.81           O  
ATOM    596  ND2 ASN A  80      26.498 -40.546  22.712  1.00 39.15           N  
ATOM    597  N   ASP A  81      22.462 -40.827  26.001  1.00 36.71           N  
ATOM    598  CA  ASP A  81      21.748 -40.779  27.272  1.00 35.95           C  
ATOM    599  C   ASP A  81      20.540 -41.708  27.223  1.00 36.37           C  
ATOM    600  O   ASP A  81      19.698 -41.582  26.338  1.00 35.61           O  
ATOM    601  CB  ASP A  81      21.310 -39.350  27.608  1.00 34.61           C  
ATOM    602  CG  ASP A  81      20.847 -39.202  29.049  1.00 34.49           C  
ATOM    603  OD1 ASP A  81      19.758 -39.713  29.379  1.00 34.65           O  
ATOM    604  OD2 ASP A  81      21.568 -38.569  29.848  1.00 33.72           O  
ATOM    605  N   PRO A  82      20.455 -42.649  28.175  1.00 37.75           N  
ATOM    606  CA  PRO A  82      19.374 -43.642  28.205  1.00 37.16           C  
ATOM    607  C   PRO A  82      17.984 -43.027  28.350  1.00 35.96           C  
ATOM    608  O   PRO A  82      16.995 -43.680  28.022  1.00 36.44           O  
ATOM    609  CB  PRO A  82      19.719 -44.504  29.427  1.00 38.03           C  
ATOM    610  CG  PRO A  82      20.607 -43.651  30.262  1.00 39.36           C  
ATOM    611  CD  PRO A  82      21.397 -42.830  29.292  1.00 39.65           C  
ATOM    612  N   LEU A  83      17.910 -41.788  28.823  1.00 35.15           N  
ATOM    613  CA  LEU A  83      16.626 -41.114  28.977  1.00 34.92           C  
ATOM    614  C   LEU A  83      16.156 -40.482  27.667  1.00 35.60           C  
ATOM    615  O   LEU A  83      14.964 -40.488  27.362  1.00 36.97           O  
ATOM    616  CB  LEU A  83      16.707 -40.046  30.072  1.00 34.77           C  
ATOM    617  CG  LEU A  83      15.399 -39.379  30.505  1.00 35.06           C  
ATOM    618  CD1 LEU A  83      14.415 -40.409  31.038  1.00 35.78           C  
ATOM    619  CD2 LEU A  83      15.660 -38.302  31.551  1.00 34.79           C  
ATOM    620  N   PHE A  84      17.094 -39.945  26.893  1.00 34.80           N  
ATOM    621  CA  PHE A  84      16.741 -39.177  25.701  1.00 34.70           C  
ATOM    622  C   PHE A  84      16.922 -39.953  24.393  1.00 36.42           C  
ATOM    623  O   PHE A  84      16.283 -39.641  23.389  1.00 36.44           O  
ATOM    624  CB  PHE A  84      17.563 -37.884  25.656  1.00 33.07           C  
ATOM    625  CG  PHE A  84      17.309 -36.962  26.821  1.00 31.69           C  
ATOM    626  CD1 PHE A  84      16.214 -36.110  26.824  1.00 30.43           C  
ATOM    627  CD2 PHE A  84      18.165 -36.944  27.909  1.00 31.61           C  
ATOM    628  CE1 PHE A  84      15.977 -35.261  27.891  1.00 29.40           C  
ATOM    629  CE2 PHE A  84      17.934 -36.098  28.979  1.00 30.98           C  
ATOM    630  CZ  PHE A  84      16.838 -35.256  28.969  1.00 29.50           C  
ATOM    631  N   LYS A  85      17.780 -40.968  24.413  1.00 38.29           N  
ATOM    632  CA  LYS A  85      18.096 -41.749  23.213  1.00 39.33           C  
ATOM    633  C   LYS A  85      16.896 -42.322  22.428  1.00 38.92           C  
ATOM    634  O   LYS A  85      16.901 -42.272  21.199  1.00 39.29           O  
ATOM    635  CB  LYS A  85      19.039 -42.899  23.576  1.00 41.89           C  
ATOM    636  CG  LYS A  85      19.501 -43.705  22.377  1.00 45.30           C  
ATOM    637  CD  LYS A  85      20.484 -44.787  22.780  1.00 48.36           C  
ATOM    638  CE  LYS A  85      21.007 -45.521  21.558  1.00 49.61           C  
ATOM    639  NZ  LYS A  85      22.028 -46.536  21.925  1.00 52.09           N  
ATOM    640  N   PRO A  86      15.870 -42.867  23.117  1.00 37.95           N  
ATOM    641  CA  PRO A  86      14.797 -43.489  22.326  1.00 36.82           C  
ATOM    642  C   PRO A  86      13.971 -42.519  21.480  1.00 36.49           C  
ATOM    643  O   PRO A  86      13.159 -42.966  20.668  1.00 38.59           O  
ATOM    644  CB  PRO A  86      13.904 -44.133  23.394  1.00 36.46           C  
ATOM    645  CG  PRO A  86      14.770 -44.274  24.593  1.00 36.54           C  
ATOM    646  CD  PRO A  86      15.664 -43.084  24.560  1.00 36.58           C  
ATOM    647  N   PHE A  87      14.171 -41.219  21.657  1.00 34.55           N  
ATOM    648  CA  PHE A  87      13.318 -40.238  20.996  1.00 32.88           C  
ATOM    649  C   PHE A  87      14.043 -39.456  19.897  1.00 32.24           C  
ATOM    650  O   PHE A  87      13.479 -38.528  19.311  1.00 31.45           O  
ATOM    651  CB  PHE A  87      12.736 -39.282  22.039  1.00 30.63           C  
ATOM    652  CG  PHE A  87      12.169 -39.982  23.244  1.00 29.61           C  
ATOM    653  CD1 PHE A  87      11.009 -40.734  23.143  1.00 29.27           C  
ATOM    654  CD2 PHE A  87      12.802 -39.897  24.476  1.00 29.71           C  
ATOM    655  CE1 PHE A  87      10.486 -41.383  24.249  1.00 30.27           C  
ATOM    656  CE2 PHE A  87      12.285 -40.544  25.587  1.00 29.60           C  
ATOM    657  CZ  PHE A  87      11.126 -41.288  25.474  1.00 30.22           C  
ATOM    658  N   PHE A  88      15.286 -39.837  19.612  1.00 30.89           N  
ATOM    659  CA  PHE A  88      16.050 -39.211  18.535  1.00 30.27           C  
ATOM    660  C   PHE A  88      16.140 -40.127  17.318  1.00 30.55           C  
ATOM    661  O   PHE A  88      16.594 -41.267  17.416  1.00 30.07           O  
ATOM    662  CB  PHE A  88      17.452 -38.835  19.016  1.00 30.36           C  
ATOM    663  CG  PHE A  88      18.357 -38.342  17.922  1.00 29.34           C  
ATOM    664  CD1 PHE A  88      17.954 -37.318  17.081  1.00 28.95           C  
ATOM    665  CD2 PHE A  88      19.614 -38.895  17.742  1.00 29.22           C  
ATOM    666  CE1 PHE A  88      18.784 -36.860  16.074  1.00 28.60           C  
ATOM    667  CE2 PHE A  88      20.449 -38.441  16.739  1.00 29.63           C  
ATOM    668  CZ  PHE A  88      20.033 -37.422  15.903  1.00 28.75           C  
ATOM    669  N   HIS A  89      15.696 -39.618  16.173  1.00 31.71           N  
ATOM    670  CA  HIS A  89      15.714 -40.377  14.925  1.00 32.26           C  
ATOM    671  C   HIS A  89      16.726 -39.769  13.960  1.00 30.00           C  
ATOM    672  O   HIS A  89      16.468 -38.733  13.348  1.00 28.36           O  
ATOM    673  CB  HIS A  89      14.321 -40.409  14.292  1.00 33.36           C  
ATOM    674  CG  HIS A  89      13.265 -40.982  15.186  1.00 36.11           C  
ATOM    675  ND1 HIS A  89      12.667 -42.201  14.945  1.00 38.37           N  
ATOM    676  CD2 HIS A  89      12.696 -40.502  16.317  1.00 37.03           C  
ATOM    677  CE1 HIS A  89      11.778 -42.448  15.890  1.00 39.09           C  
ATOM    678  NE2 HIS A  89      11.776 -41.433  16.735  1.00 39.12           N  
ATOM    679  N   ASN A  90      17.879 -40.415  13.833  1.00 29.72           N  
ATOM    680  CA  ASN A  90      18.970 -39.872  13.034  1.00 29.89           C  
ATOM    681  C   ASN A  90      18.826 -40.223  11.560  1.00 29.81           C  
ATOM    682  O   ASN A  90      19.473 -41.140  11.060  1.00 31.59           O  
ATOM    683  CB  ASN A  90      20.317 -40.365  13.568  1.00 31.58           C  
ATOM    684  CG  ASN A  90      21.492 -39.740  12.848  1.00 34.72           C  
ATOM    685  OD1 ASN A  90      22.447 -40.426  12.493  1.00 37.28           O  
ATOM    686  ND2 ASN A  90      21.422 -38.433  12.617  1.00 35.36           N  
ATOM    687  N   VAL A  91      17.966 -39.481  10.873  1.00 28.66           N  
ATOM    688  CA  VAL A  91      17.711 -39.703   9.457  1.00 31.79           C  
ATOM    689  C   VAL A  91      18.407 -38.648   8.602  1.00 30.64           C  
ATOM    690  O   VAL A  91      18.409 -38.731   7.375  1.00 30.53           O  
ATOM    691  CB  VAL A  91      16.205 -39.685   9.157  1.00 30.29           C  
ATOM    692  CG1 VAL A  91      15.519 -40.855   9.836  1.00 23.99           C  
ATOM    693  CG2 VAL A  91      15.599 -38.370   9.615  1.00 29.93           C  
ATOM    694  N   GLY A  92      18.994 -37.656   9.262  1.00 31.92           N  
ATOM    695  CA  GLY A  92      19.682 -36.582   8.572  1.00 31.96           C  
ATOM    696  C   GLY A  92      18.747 -35.451   8.187  1.00 32.37           C  
ATOM    697  O   GLY A  92      17.535 -35.530   8.385  1.00 30.43           O  
ATOM    698  N   GLN A  93      19.320 -34.390   7.633  1.00 34.36           N  
ATOM    699  CA  GLN A  93      18.541 -33.253   7.172  1.00 36.27           C  
ATOM    700  C   GLN A  93      19.111 -32.746   5.858  1.00 36.94           C  
ATOM    701  O   GLN A  93      20.326 -32.729   5.668  1.00 38.47           O  
ATOM    702  CB  GLN A  93      18.535 -32.142   8.222  1.00 38.88           C  
ATOM    703  CG  GLN A  93      17.784 -30.890   7.812  1.00 41.39           C  
ATOM    704  CD  GLN A  93      17.665 -29.898   8.947  1.00 44.15           C  
ATOM    705  OE1 GLN A  93      18.064 -30.184  10.076  1.00 45.54           O  
ATOM    706  NE2 GLN A  93      17.115 -28.724   8.656  1.00 44.83           N  
HETATM  707  N   MSE A  94      18.234 -32.346   4.947  1.00 37.41           N  
HETATM  708  CA  MSE A  94      18.679 -31.802   3.674  1.00 38.78           C  
HETATM  709  C   MSE A  94      18.043 -30.451   3.378  1.00 39.23           C  
HETATM  710  O   MSE A  94      16.819 -30.312   3.392  1.00 37.39           O  
HETATM  711  CB  MSE A  94      18.374 -32.771   2.537  1.00 39.85           C  
HETATM  712  CG  MSE A  94      18.713 -32.204   1.173  1.00 43.21           C  
HETATM  713 SE   MSE A  94      18.231 -33.394  -0.283  1.00 80.49          SE  
HETATM  714  CE  MSE A  94      19.390 -34.885   0.156  1.00 40.67           C  
ATOM    715  N   ASP A  95      18.887 -29.458   3.115  1.00 41.68           N  
ATOM    716  CA  ASP A  95      18.421 -28.144   2.700  1.00 42.34           C  
ATOM    717  C   ASP A  95      18.515 -28.028   1.186  1.00 40.97           C  
ATOM    718  O   ASP A  95      19.563 -28.303   0.601  1.00 40.88           O  
ATOM    719  CB  ASP A  95      19.237 -27.040   3.373  1.00 45.81           C  
ATOM    720  CG  ASP A  95      19.307 -27.201   4.877  1.00 49.90           C  
ATOM    721  OD1 ASP A  95      18.330 -27.703   5.470  1.00 50.76           O  
ATOM    722  OD2 ASP A  95      20.343 -26.830   5.466  1.00 52.19           O  
ATOM    723  N   VAL A  96      17.415 -27.633   0.553  1.00 39.69           N  
ATOM    724  CA  VAL A  96      17.380 -27.506  -0.901  1.00 39.63           C  
ATOM    725  C   VAL A  96      17.022 -26.089  -1.342  1.00 40.12           C  
ATOM    726  O   VAL A  96      16.498 -25.297  -0.560  1.00 40.09           O  
ATOM    727  CB  VAL A  96      16.376 -28.495  -1.532  1.00 38.92           C  
ATOM    728  CG1 VAL A  96      16.791 -29.927  -1.244  1.00 38.97           C  
ATOM    729  CG2 VAL A  96      14.970 -28.231  -1.018  1.00 37.90           C  
ATOM    730  N   SER A  97      17.318 -25.785  -2.603  1.00 40.64           N  
ATOM    731  CA  SER A  97      17.009 -24.491  -3.203  1.00 41.67           C  
ATOM    732  C   SER A  97      17.183 -24.539  -4.717  1.00 42.96           C  
ATOM    733  O   SER A  97      17.960 -25.343  -5.231  1.00 42.05           O  
ATOM    734  CB  SER A  97      17.895 -23.391  -2.618  1.00 42.25           C  
ATOM    735  OG  SER A  97      17.732 -22.182  -3.339  1.00 43.99           O  
ATOM    736  N   SER A  98      16.463 -23.674  -5.427  1.00 45.08           N  
ATOM    737  CA  SER A  98      16.588 -23.584  -6.882  1.00 47.71           C  
ATOM    738  C   SER A  98      16.837 -22.146  -7.337  1.00 49.05           C  
ATOM    739  O   SER A  98      17.138 -21.901  -8.505  1.00 51.33           O  
ATOM    740  CB  SER A  98      15.339 -24.138  -7.571  1.00 49.55           C  
ATOM    741  OG  SER A  98      14.200 -23.349  -7.273  1.00 51.26           O  
ATOM    742  N   THR A  99      16.703 -21.199  -6.415  1.00 48.95           N  
ATOM    743  CA  THR A  99      17.032 -19.808  -6.701  1.00 51.63           C  
ATOM    744  C   THR A  99      18.543 -19.626  -6.625  1.00 55.64           C  
ATOM    745  O   THR A  99      19.231 -20.408  -5.971  1.00 55.67           O  
ATOM    746  CB  THR A  99      16.345 -18.844  -5.719  1.00 51.08           C  
ATOM    747  OG1 THR A  99      16.931 -18.979  -4.418  1.00 50.18           O  
ATOM    748  CG2 THR A  99      14.858 -19.146  -5.629  1.00 51.42           C  
ATOM    749  N   GLU A 100      19.065 -18.600  -7.289  1.00 60.49           N  
ATOM    750  CA  GLU A 100      20.504 -18.357  -7.268  1.00 63.78           C  
ATOM    751  C   GLU A 100      20.968 -17.801  -5.927  1.00 63.20           C  
ATOM    752  O   GLU A 100      22.109 -18.019  -5.523  1.00 62.14           O  
ATOM    753  CB  GLU A 100      20.911 -17.412  -8.398  1.00 68.43           C  
ATOM    754  CG  GLU A 100      21.257 -18.137  -9.688  1.00 73.51           C  
ATOM    755  CD  GLU A 100      22.345 -19.183  -9.493  1.00 77.70           C  
ATOM    756  OE1 GLU A 100      23.311 -18.907  -8.750  1.00 79.52           O  
ATOM    757  OE2 GLU A 100      22.232 -20.284 -10.074  1.00 78.69           O  
ATOM    758  N   GLU A 101      20.084 -17.090  -5.235  1.00 64.23           N  
ATOM    759  CA  GLU A 101      20.412 -16.562  -3.916  1.00 63.97           C  
ATOM    760  C   GLU A 101      20.333 -17.662  -2.861  1.00 59.75           C  
ATOM    761  O   GLU A 101      21.132 -17.698  -1.926  1.00 60.18           O  
ATOM    762  CB  GLU A 101      19.481 -15.409  -3.542  1.00 68.30           C  
ATOM    763  CG  GLU A 101      19.901 -14.672  -2.279  1.00 72.49           C  
ATOM    764  CD  GLU A 101      18.840 -13.712  -1.777  1.00 76.98           C  
ATOM    765  OE1 GLU A 101      17.747 -13.663  -2.379  1.00 78.79           O  
ATOM    766  OE2 GLU A 101      19.100 -13.008  -0.777  1.00 78.22           O  
ATOM    767  N   GLY A 102      19.363 -18.557  -3.017  1.00 54.53           N  
ATOM    768  CA  GLY A 102      19.195 -19.661  -2.092  1.00 49.23           C  
ATOM    769  C   GLY A 102      20.346 -20.643  -2.181  1.00 47.15           C  
ATOM    770  O   GLY A 102      20.861 -21.102  -1.162  1.00 44.86           O  
ATOM    771  N   ILE A 103      20.745 -20.966  -3.407  1.00 46.69           N  
ATOM    772  CA  ILE A 103      21.887 -21.843  -3.643  1.00 44.01           C  
ATOM    773  C   ILE A 103      23.154 -21.210  -3.075  1.00 43.65           C  
ATOM    774  O   ILE A 103      23.947 -21.872  -2.401  1.00 40.89           O  
ATOM    775  CB  ILE A 103      22.066 -22.133  -5.147  1.00 42.27           C  
ATOM    776  CG1 ILE A 103      20.934 -23.033  -5.646  1.00 40.00           C  
ATOM    777  CG2 ILE A 103      23.409 -22.788  -5.416  1.00 41.42           C  
ATOM    778  CD1 ILE A 103      20.869 -23.164  -7.152  1.00 39.70           C  
ATOM    779  N   LYS A 104      23.320 -19.919  -3.346  1.00 45.63           N  
ATOM    780  CA  LYS A 104      24.407 -19.125  -2.787  1.00 47.40           C  
ATOM    781  C   LYS A 104      24.453 -19.250  -1.266  1.00 48.38           C  
ATOM    782  O   LYS A 104      25.523 -19.391  -0.673  1.00 47.79           O  
ATOM    783  CB  LYS A 104      24.244 -17.659  -3.201  1.00 48.57           C  
ATOM    784  CG  LYS A 104      25.109 -16.660  -2.450  1.00 50.23           C  
ATOM    785  CD  LYS A 104      24.685 -15.235  -2.791  1.00 52.52           C  
ATOM    786  CE  LYS A 104      25.406 -14.199  -1.941  1.00 53.71           C  
ATOM    787  NZ  LYS A 104      26.843 -14.067  -2.307  1.00 55.28           N  
ATOM    788  N   LYS A 105      23.278 -19.218  -0.646  1.00 50.19           N  
ATOM    789  CA  LYS A 105      23.169 -19.288   0.806  1.00 51.56           C  
ATOM    790  C   LYS A 105      23.505 -20.684   1.335  1.00 48.60           C  
ATOM    791  O   LYS A 105      24.057 -20.825   2.426  1.00 47.95           O  
ATOM    792  CB  LYS A 105      21.764 -18.877   1.248  1.00 56.02           C  
ATOM    793  CG  LYS A 105      21.738 -17.873   2.389  1.00 60.58           C  
ATOM    794  CD  LYS A 105      20.319 -17.411   2.678  1.00 63.78           C  
ATOM    795  CE  LYS A 105      20.296 -16.275   3.688  1.00 66.22           C  
ATOM    796  NZ  LYS A 105      18.914 -15.770   3.913  1.00 67.06           N  
ATOM    797  N   LEU A 106      23.163 -21.709   0.560  1.00 46.32           N  
ATOM    798  CA  LEU A 106      23.515 -23.082   0.908  1.00 44.07           C  
ATOM    799  C   LEU A 106      25.027 -23.260   0.956  1.00 44.33           C  
ATOM    800  O   LEU A 106      25.567 -23.781   1.931  1.00 43.82           O  
ATOM    801  CB  LEU A 106      22.914 -24.072  -0.092  1.00 44.59           C  
ATOM    802  CG  LEU A 106      21.394 -24.212  -0.131  1.00 45.29           C  
ATOM    803  CD1 LEU A 106      20.988 -25.205  -1.206  1.00 45.28           C  
ATOM    804  CD2 LEU A 106      20.863 -24.636   1.228  1.00 44.58           C  
ATOM    805  N   ARG A 107      25.700 -22.820  -0.105  1.00 45.05           N  
ATOM    806  CA  ARG A 107      27.148 -22.959  -0.217  1.00 45.84           C  
ATOM    807  C   ARG A 107      27.880 -22.224   0.902  1.00 47.69           C  
ATOM    808  O   ARG A 107      28.923 -22.678   1.371  1.00 49.11           O  
ATOM    809  CB  ARG A 107      27.633 -22.455  -1.578  1.00 45.15           C  
ATOM    810  CG  ARG A 107      27.061 -23.225  -2.761  1.00 44.58           C  
ATOM    811  CD  ARG A 107      27.950 -23.111  -3.986  1.00 45.98           C  
ATOM    812  NE  ARG A 107      27.447 -23.905  -5.104  1.00 45.88           N  
ATOM    813  CZ  ARG A 107      26.799 -23.398  -6.147  1.00 44.76           C  
ATOM    814  NH1 ARG A 107      26.582 -22.091  -6.221  1.00 44.53           N  
ATOM    815  NH2 ARG A 107      26.373 -24.195  -7.116  1.00 43.88           N  
HETATM  816  N   MSE A 108      27.334 -21.092   1.332  1.00 47.40           N  
HETATM  817  CA  MSE A 108      27.949 -20.327   2.411  1.00 47.05           C  
HETATM  818  C   MSE A 108      27.739 -21.006   3.763  1.00 46.39           C  
HETATM  819  O   MSE A 108      28.625 -20.984   4.615  1.00 46.60           O  
HETATM  820  CB  MSE A 108      27.399 -18.899   2.442  1.00 46.15           C  
HETATM  821  CG  MSE A 108      27.865 -18.030   1.284  1.00 47.42           C  
HETATM  822 SE   MSE A 108      27.309 -16.165   1.438  1.00 75.27          SE  
HETATM  823  CE  MSE A 108      25.388 -16.387   1.184  1.00 85.16           C  
ATOM    824  N   ARG A 109      26.568 -21.606   3.954  1.00 46.13           N  
ATOM    825  CA  ARG A 109      26.285 -22.339   5.183  1.00 46.73           C  
ATOM    826  C   ARG A 109      27.196 -23.557   5.306  1.00 44.06           C  
ATOM    827  O   ARG A 109      27.699 -23.860   6.389  1.00 43.86           O  
ATOM    828  CB  ARG A 109      24.815 -22.764   5.241  1.00 50.71           C  
ATOM    829  CG  ARG A 109      23.877 -21.669   5.732  1.00 56.23           C  
ATOM    830  CD  ARG A 109      22.521 -22.228   6.143  1.00 60.71           C  
ATOM    831  NE  ARG A 109      21.621 -22.408   5.006  1.00 65.45           N  
ATOM    832  CZ  ARG A 109      20.769 -21.481   4.577  1.00 68.94           C  
ATOM    833  NH1 ARG A 109      20.703 -20.307   5.191  1.00 71.15           N  
ATOM    834  NH2 ARG A 109      19.984 -21.727   3.536  1.00 68.99           N  
ATOM    835  N   TYR A 110      27.408 -24.248   4.191  1.00 42.25           N  
ATOM    836  CA  TYR A 110      28.344 -25.366   4.150  1.00 42.19           C  
ATOM    837  C   TYR A 110      29.758 -24.916   4.509  1.00 43.36           C  
ATOM    838  O   TYR A 110      30.419 -25.529   5.349  1.00 43.73           O  
ATOM    839  CB  TYR A 110      28.344 -26.021   2.767  1.00 42.81           C  
ATOM    840  CG  TYR A 110      29.422 -27.067   2.591  1.00 42.83           C  
ATOM    841  CD1 TYR A 110      29.252 -28.354   3.084  1.00 41.75           C  
ATOM    842  CD2 TYR A 110      30.610 -26.769   1.932  1.00 43.69           C  
ATOM    843  CE1 TYR A 110      30.233 -29.314   2.929  1.00 42.11           C  
ATOM    844  CE2 TYR A 110      31.599 -27.722   1.773  1.00 43.85           C  
ATOM    845  CZ  TYR A 110      31.403 -28.993   2.273  1.00 43.41           C  
ATOM    846  OH  TYR A 110      32.381 -29.948   2.119  1.00 44.49           O  
ATOM    847  N   GLN A 111      30.214 -23.843   3.869  1.00 43.39           N  
ATOM    848  CA  GLN A 111      31.555 -23.319   4.106  1.00 44.14           C  
ATOM    849  C   GLN A 111      31.694 -22.818   5.541  1.00 45.16           C  
ATOM    850  O   GLN A 111      32.787 -22.811   6.111  1.00 44.42           O  
ATOM    851  CB  GLN A 111      31.875 -22.196   3.116  1.00 43.10           C  
ATOM    852  CG  GLN A 111      33.313 -21.710   3.177  1.00 43.52           C  
ATOM    853  CD  GLN A 111      34.308 -22.782   2.773  1.00 44.72           C  
ATOM    854  OE1 GLN A 111      34.124 -23.468   1.766  1.00 45.27           O  
ATOM    855  NE2 GLN A 111      35.367 -22.936   3.560  1.00 44.81           N  
ATOM    856  N   SER A 112      30.573 -22.406   6.119  1.00 47.02           N  
ATOM    857  CA  SER A 112      30.548 -21.934   7.496  1.00 48.88           C  
ATOM    858  C   SER A 112      30.910 -23.057   8.465  1.00 46.22           C  
ATOM    859  O   SER A 112      31.668 -22.853   9.413  1.00 46.27           O  
ATOM    860  CB  SER A 112      29.172 -21.362   7.834  1.00 52.03           C  
ATOM    861  OG  SER A 112      29.122 -20.918   9.175  1.00 55.94           O  
ATOM    862  N   LEU A 113      30.364 -24.243   8.215  1.00 43.35           N  
ATOM    863  CA  LEU A 113      30.646 -25.410   9.043  1.00 41.24           C  
ATOM    864  C   LEU A 113      32.121 -25.795   8.965  1.00 42.27           C  
ATOM    865  O   LEU A 113      32.743 -26.121   9.976  1.00 43.70           O  
ATOM    866  CB  LEU A 113      29.774 -26.592   8.618  1.00 39.55           C  
ATOM    867  CG  LEU A 113      28.260 -26.372   8.613  1.00 37.94           C  
ATOM    868  CD1 LEU A 113      27.552 -27.559   7.979  1.00 38.13           C  
ATOM    869  CD2 LEU A 113      27.746 -26.132  10.025  1.00 37.03           C  
ATOM    870  N   LEU A 114      32.673 -25.754   7.757  1.00 41.70           N  
ATOM    871  CA  LEU A 114      34.074 -26.095   7.541  1.00 42.66           C  
ATOM    872  C   LEU A 114      35.001 -25.187   8.339  1.00 45.42           C  
ATOM    873  O   LEU A 114      35.996 -25.645   8.904  1.00 45.91           O  
ATOM    874  CB  LEU A 114      34.424 -26.013   6.052  1.00 40.95           C  
ATOM    875  CG  LEU A 114      34.230 -27.265   5.195  1.00 39.62           C  
ATOM    876  CD1 LEU A 114      32.803 -27.789   5.272  1.00 38.14           C  
ATOM    877  CD2 LEU A 114      34.605 -26.961   3.760  1.00 40.38           C  
ATOM    878  N   ASP A 115      34.661 -23.903   8.396  1.00 46.97           N  
ATOM    879  CA  ASP A 115      35.523 -22.905   9.024  1.00 48.44           C  
ATOM    880  C   ASP A 115      35.613 -23.058  10.544  1.00 48.05           C  
ATOM    881  O   ASP A 115      36.393 -22.361  11.195  1.00 49.68           O  
ATOM    882  CB  ASP A 115      35.041 -21.497   8.667  1.00 48.85           C  
ATOM    883  CG  ASP A 115      35.246 -21.167   7.198  1.00 49.78           C  
ATOM    884  OD1 ASP A 115      36.181 -21.725   6.584  1.00 49.21           O  
ATOM    885  OD2 ASP A 115      34.476 -20.348   6.654  1.00 50.62           O  
ATOM    886  N   ALA A 116      34.822 -23.968  11.106  1.00 45.54           N  
ATOM    887  CA  ALA A 116      34.905 -24.273  12.530  1.00 46.32           C  
ATOM    888  C   ALA A 116      36.186 -25.044  12.837  1.00 47.94           C  
ATOM    889  O   ALA A 116      36.741 -24.941  13.932  1.00 48.78           O  
ATOM    890  CB  ALA A 116      33.685 -25.062  12.979  1.00 45.53           C  
ATOM    891  N   GLY A 117      36.642 -25.826  11.862  1.00 48.17           N  
ATOM    892  CA  GLY A 117      37.910 -26.527  11.960  1.00 48.30           C  
ATOM    893  C   GLY A 117      37.903 -27.807  12.777  1.00 47.79           C  
ATOM    894  O   GLY A 117      38.964 -28.330  13.115  1.00 50.75           O  
ATOM    895  N   ILE A 118      36.722 -28.323  13.095  1.00 44.76           N  
ATOM    896  CA  ILE A 118      36.634 -29.542  13.891  1.00 45.15           C  
ATOM    897  C   ILE A 118      36.374 -30.776  13.030  1.00 45.06           C  
ATOM    898  O   ILE A 118      36.239 -31.886  13.548  1.00 45.07           O  
ATOM    899  CB  ILE A 118      35.533 -29.436  14.961  1.00 44.09           C  
ATOM    900  CG1 ILE A 118      34.203 -29.051  14.317  1.00 42.90           C  
ATOM    901  CG2 ILE A 118      35.927 -28.425  16.025  1.00 44.68           C  
ATOM    902  CD1 ILE A 118      33.053 -28.979  15.292  1.00 42.44           C  
ATOM    903  N   GLY A 119      36.304 -30.577  11.717  1.00 44.81           N  
ATOM    904  CA  GLY A 119      36.125 -31.676  10.783  1.00 43.61           C  
ATOM    905  C   GLY A 119      34.678 -31.985  10.446  1.00 41.70           C  
ATOM    906  O   GLY A 119      34.316 -33.147  10.256  1.00 41.74           O  
ATOM    907  N   LEU A 120      33.850 -30.947  10.358  1.00 39.77           N  
ATOM    908  CA  LEU A 120      32.428 -31.122  10.067  1.00 37.44           C  
ATOM    909  C   LEU A 120      32.170 -31.534   8.617  1.00 36.98           C  
ATOM    910  O   LEU A 120      31.063 -31.949   8.273  1.00 35.81           O  
ATOM    911  CB  LEU A 120      31.657 -29.838  10.385  1.00 36.18           C  
ATOM    912  CG  LEU A 120      31.569 -29.451  11.865  1.00 35.74           C  
ATOM    913  CD1 LEU A 120      30.948 -28.072  12.036  1.00 35.12           C  
ATOM    914  CD2 LEU A 120      30.783 -30.491  12.646  1.00 34.45           C  
ATOM    915  N   GLU A 121      33.190 -31.429   7.769  1.00 37.68           N  
ATOM    916  CA  GLU A 121      33.042 -31.809   6.367  1.00 37.83           C  
ATOM    917  C   GLU A 121      32.902 -33.321   6.221  1.00 38.50           C  
ATOM    918  O   GLU A 121      32.541 -33.821   5.157  1.00 38.61           O  
ATOM    919  CB  GLU A 121      34.228 -31.310   5.535  1.00 38.26           C  
ATOM    920  CG  GLU A 121      35.532 -32.061   5.764  1.00 38.93           C  
ATOM    921  CD  GLU A 121      36.324 -31.524   6.944  1.00 39.53           C  
ATOM    922  OE1 GLU A 121      37.454 -32.008   7.173  1.00 39.92           O  
ATOM    923  OE2 GLU A 121      35.822 -30.617   7.640  1.00 39.32           O  
ATOM    924  N   LYS A 122      33.189 -34.044   7.299  1.00 39.39           N  
ATOM    925  CA  LYS A 122      33.096 -35.498   7.296  1.00 39.38           C  
ATOM    926  C   LYS A 122      31.646 -35.980   7.309  1.00 38.16           C  
ATOM    927  O   LYS A 122      31.348 -37.069   6.824  1.00 39.19           O  
ATOM    928  CB  LYS A 122      33.847 -36.084   8.495  1.00 40.75           C  
ATOM    929  CG  LYS A 122      35.302 -36.454   8.220  1.00 43.21           C  
ATOM    930  CD  LYS A 122      36.187 -35.231   8.052  1.00 44.23           C  
ATOM    931  CE  LYS A 122      37.643 -35.638   7.869  1.00 46.41           C  
ATOM    932  NZ  LYS A 122      38.557 -34.465   7.772  1.00 47.16           N  
ATOM    933  N   THR A 123      30.747 -35.171   7.863  1.00 36.44           N  
ATOM    934  CA  THR A 123      29.347 -35.567   7.983  1.00 36.26           C  
ATOM    935  C   THR A 123      28.405 -34.512   7.401  1.00 37.13           C  
ATOM    936  O   THR A 123      27.210 -34.497   7.701  1.00 36.29           O  
ATOM    937  CB  THR A 123      28.961 -35.838   9.453  1.00 35.60           C  
ATOM    938  OG1 THR A 123      29.160 -34.653  10.234  1.00 36.15           O  
ATOM    939  CG2 THR A 123      29.807 -36.966  10.029  1.00 35.33           C  
ATOM    940  N   ASN A 124      28.955 -33.637   6.565  1.00 38.25           N  
ATOM    941  CA  ASN A 124      28.167 -32.627   5.865  1.00 36.99           C  
ATOM    942  C   ASN A 124      28.640 -32.486   4.423  1.00 37.05           C  
ATOM    943  O   ASN A 124      29.830 -32.307   4.169  1.00 37.97           O  
ATOM    944  CB  ASN A 124      28.247 -31.282   6.588  1.00 36.82           C  
ATOM    945  CG  ASN A 124      27.704 -31.350   8.003  1.00 35.96           C  
ATOM    946  OD1 ASN A 124      26.523 -31.099   8.239  1.00 35.78           O  
ATOM    947  ND2 ASN A 124      28.567 -31.697   8.953  1.00 34.96           N  
ATOM    948  N   PHE A 125      27.708 -32.568   3.480  1.00 37.50           N  
ATOM    949  CA  PHE A 125      28.066 -32.594   2.065  1.00 38.21           C  
ATOM    950  C   PHE A 125      27.209 -31.660   1.218  1.00 39.31           C  
ATOM    951  O   PHE A 125      26.000 -31.550   1.427  1.00 39.66           O  
ATOM    952  CB  PHE A 125      27.948 -34.020   1.516  1.00 37.25           C  
ATOM    953  CG  PHE A 125      28.479 -35.075   2.444  1.00 37.37           C  
ATOM    954  CD1 PHE A 125      29.821 -35.417   2.430  1.00 38.92           C  
ATOM    955  CD2 PHE A 125      27.633 -35.727   3.330  1.00 37.03           C  
ATOM    956  CE1 PHE A 125      30.313 -36.390   3.286  1.00 39.69           C  
ATOM    957  CE2 PHE A 125      28.118 -36.698   4.187  1.00 37.66           C  
ATOM    958  CZ  PHE A 125      29.460 -37.031   4.164  1.00 38.61           C  
ATOM    959  N   LEU A 126      27.847 -30.989   0.263  1.00 39.99           N  
ATOM    960  CA  LEU A 126      27.129 -30.249  -0.769  1.00 40.52           C  
ATOM    961  C   LEU A 126      26.694 -31.209  -1.864  1.00 42.07           C  
ATOM    962  O   LEU A 126      27.464 -32.076  -2.273  1.00 42.41           O  
ATOM    963  CB  LEU A 126      27.999 -29.140  -1.368  1.00 41.68           C  
ATOM    964  CG  LEU A 126      28.120 -27.804  -0.638  1.00 41.06           C  
ATOM    965  CD1 LEU A 126      29.070 -26.888  -1.389  1.00 41.23           C  
ATOM    966  CD2 LEU A 126      26.756 -27.153  -0.491  1.00 40.37           C  
ATOM    967  N   LEU A 127      25.464 -31.053  -2.341  1.00 43.61           N  
ATOM    968  CA  LEU A 127      24.963 -31.888  -3.427  1.00 46.07           C  
ATOM    969  C   LEU A 127      24.724 -31.053  -4.684  1.00 49.17           C  
ATOM    970  O   LEU A 127      23.723 -30.342  -4.790  1.00 49.60           O  
ATOM    971  CB  LEU A 127      23.680 -32.601  -3.004  1.00 44.63           C  
ATOM    972  CG  LEU A 127      23.781 -33.372  -1.685  1.00 43.58           C  
ATOM    973  CD1 LEU A 127      22.507 -34.152  -1.424  1.00 42.60           C  
ATOM    974  CD2 LEU A 127      24.990 -34.296  -1.685  1.00 44.10           C  
ATOM    975  N   GLU A 128      25.653 -31.149  -5.632  1.00 51.11           N  
ATOM    976  CA  GLU A 128      25.626 -30.325  -6.838  1.00 54.34           C  
ATOM    977  C   GLU A 128      24.910 -31.011  -8.000  1.00 56.29           C  
ATOM    978  O   GLU A 128      24.684 -30.403  -9.047  1.00 57.31           O  
ATOM    979  CB  GLU A 128      27.053 -29.959  -7.256  1.00 55.58           C  
ATOM    980  CG  GLU A 128      27.876 -29.277  -6.171  1.00 55.84           C  
ATOM    981  CD  GLU A 128      27.535 -27.806  -6.007  1.00 57.06           C  
ATOM    982  OE1 GLU A 128      26.789 -27.264  -6.849  1.00 58.18           O  
ATOM    983  OE2 GLU A 128      28.019 -27.189  -5.034  1.00 56.56           O  
ATOM    984  N   SER A 129      24.557 -32.277  -7.810  1.00 56.49           N  
ATOM    985  CA  SER A 129      23.899 -33.055  -8.852  1.00 56.24           C  
ATOM    986  C   SER A 129      22.485 -33.452  -8.445  1.00 56.25           C  
ATOM    987  O   SER A 129      22.104 -33.320  -7.284  1.00 57.00           O  
ATOM    988  CB  SER A 129      24.716 -34.304  -9.177  1.00 56.26           C  
ATOM    989  OG  SER A 129      23.956 -35.225  -9.936  1.00 57.25           O  
ATOM    990  N   GLU A 130      21.714 -33.943  -9.409  1.00 56.99           N  
ATOM    991  CA  GLU A 130      20.355 -34.399  -9.147  1.00 57.46           C  
ATOM    992  C   GLU A 130      20.347 -35.844  -8.666  1.00 55.59           C  
ATOM    993  O   GLU A 130      19.441 -36.261  -7.948  1.00 55.71           O  
ATOM    994  CB  GLU A 130      19.486 -34.259 -10.399  1.00 62.33           C  
ATOM    995  CG  GLU A 130      19.233 -32.820 -10.823  1.00 65.84           C  
ATOM    996  CD  GLU A 130      18.433 -32.717 -12.109  1.00 70.15           C  
ATOM    997  OE1 GLU A 130      18.020 -33.769 -12.644  1.00 72.09           O  
ATOM    998  OE2 GLU A 130      18.219 -31.581 -12.586  1.00 71.00           O  
ATOM    999  N   ASP A 131      21.360 -36.603  -9.069  1.00 54.53           N  
ATOM   1000  CA  ASP A 131      21.484 -37.995  -8.657  1.00 55.13           C  
ATOM   1001  C   ASP A 131      21.855 -38.084  -7.187  1.00 53.78           C  
ATOM   1002  O   ASP A 131      21.425 -38.994  -6.480  1.00 53.58           O  
ATOM   1003  CB  ASP A 131      22.529 -38.719  -9.504  1.00 58.70           C  
ATOM   1004  CG  ASP A 131      22.285 -38.561 -10.988  1.00 62.09           C  
ATOM   1005  OD1 ASP A 131      21.141 -38.236 -11.368  1.00 63.11           O  
ATOM   1006  OD2 ASP A 131      23.236 -38.762 -11.772  1.00 63.57           O  
ATOM   1007  N   GLU A 132      22.661 -37.129  -6.736  1.00 53.12           N  
ATOM   1008  CA  GLU A 132      23.066 -37.052  -5.340  1.00 50.19           C  
ATOM   1009  C   GLU A 132      21.876 -36.735  -4.438  1.00 45.63           C  
ATOM   1010  O   GLU A 132      21.782 -37.245  -3.323  1.00 43.72           O  
ATOM   1011  CB  GLU A 132      24.167 -36.003  -5.164  1.00 51.92           C  
ATOM   1012  CG  GLU A 132      25.481 -36.381  -5.837  1.00 55.38           C  
ATOM   1013  CD  GLU A 132      26.511 -35.266  -5.797  1.00 57.77           C  
ATOM   1014  OE1 GLU A 132      26.117 -34.082  -5.868  1.00 59.06           O  
ATOM   1015  OE2 GLU A 132      27.718 -35.574  -5.695  1.00 58.49           O  
ATOM   1016  N   ILE A 133      20.965 -35.900  -4.930  1.00 44.65           N  
ATOM   1017  CA  ILE A 133      19.766 -35.545  -4.174  1.00 44.03           C  
ATOM   1018  C   ILE A 133      18.812 -36.731  -4.067  1.00 45.36           C  
ATOM   1019  O   ILE A 133      18.301 -37.037  -2.988  1.00 44.44           O  
ATOM   1020  CB  ILE A 133      19.029 -34.353  -4.812  1.00 43.46           C  
ATOM   1021  CG1 ILE A 133      19.839 -33.072  -4.614  1.00 44.09           C  
ATOM   1022  CG2 ILE A 133      17.638 -34.196  -4.214  1.00 41.29           C  
ATOM   1023  CD1 ILE A 133      19.189 -31.838  -5.197  1.00 45.23           C  
ATOM   1024  N   LEU A 134      18.582 -37.399  -5.194  1.00 47.22           N  
ATOM   1025  CA  LEU A 134      17.712 -38.569  -5.231  1.00 48.48           C  
ATOM   1026  C   LEU A 134      18.313 -39.732  -4.452  1.00 50.66           C  
ATOM   1027  O   LEU A 134      17.597 -40.631  -4.014  1.00 49.61           O  
ATOM   1028  CB  LEU A 134      17.444 -38.988  -6.676  1.00 50.16           C  
ATOM   1029  CG  LEU A 134      16.656 -37.988  -7.522  1.00 50.42           C  
ATOM   1030  CD1 LEU A 134      16.749 -38.329  -9.000  1.00 52.13           C  
ATOM   1031  CD2 LEU A 134      15.205 -37.938  -7.070  1.00 49.96           C  
ATOM   1032  N   ALA A 135      19.631 -39.705  -4.282  1.00 53.18           N  
ATOM   1033  CA  ALA A 135      20.336 -40.754  -3.556  1.00 54.48           C  
ATOM   1034  C   ALA A 135      19.977 -40.741  -2.075  1.00 54.55           C  
ATOM   1035  O   ALA A 135      19.953 -41.786  -1.425  1.00 55.92           O  
ATOM   1036  CB  ALA A 135      21.839 -40.604  -3.735  1.00 54.56           C  
ATOM   1037  N   LYS A 136      19.697 -39.554  -1.547  1.00 51.48           N  
ATOM   1038  CA  LYS A 136      19.386 -39.403  -0.130  1.00 47.07           C  
ATOM   1039  C   LYS A 136      17.892 -39.183   0.107  1.00 42.63           C  
ATOM   1040  O   LYS A 136      17.410 -39.337   1.227  1.00 41.78           O  
ATOM   1041  CB  LYS A 136      20.184 -38.245   0.467  1.00 47.97           C  
ATOM   1042  CG  LYS A 136      21.689 -38.455   0.501  1.00 49.94           C  
ATOM   1043  CD  LYS A 136      22.082 -39.390   1.629  1.00 52.74           C  
ATOM   1044  CE  LYS A 136      23.590 -39.423   1.816  1.00 55.29           C  
ATOM   1045  NZ  LYS A 136      24.293 -39.863   0.577  1.00 57.29           N  
ATOM   1046  N   ALA A 137      17.167 -38.817  -0.946  1.00 41.67           N  
ATOM   1047  CA  ALA A 137      15.722 -38.612  -0.854  1.00 39.98           C  
ATOM   1048  C   ALA A 137      15.021 -39.135  -2.104  1.00 42.41           C  
ATOM   1049  O   ALA A 137      14.647 -38.357  -2.982  1.00 44.62           O  
ATOM   1050  CB  ALA A 137      15.405 -37.140  -0.646  1.00 37.77           C  
ATOM   1051  N   PRO A 138      14.834 -40.462  -2.181  1.00 41.83           N  
ATOM   1052  CA  PRO A 138      14.327 -41.135  -3.385  1.00 42.16           C  
ATOM   1053  C   PRO A 138      12.844 -40.899  -3.695  1.00 41.26           C  
ATOM   1054  O   PRO A 138      12.386 -41.337  -4.748  1.00 41.41           O  
ATOM   1055  CB  PRO A 138      14.575 -42.615  -3.079  1.00 42.32           C  
ATOM   1056  CG  PRO A 138      14.534 -42.697  -1.594  1.00 40.94           C  
ATOM   1057  CD  PRO A 138      15.146 -41.418  -1.103  1.00 40.25           C  
ATOM   1058  N   HIS A 139      12.111 -40.225  -2.813  1.00 40.12           N  
ATOM   1059  CA  HIS A 139      10.683 -40.005  -3.046  1.00 41.65           C  
ATOM   1060  C   HIS A 139      10.418 -38.865  -4.032  1.00 42.89           C  
ATOM   1061  O   HIS A 139       9.323 -38.760  -4.586  1.00 43.65           O  
ATOM   1062  CB  HIS A 139       9.961 -39.734  -1.725  1.00 40.85           C  
ATOM   1063  CG  HIS A 139      10.629 -38.703  -0.873  1.00 40.48           C  
ATOM   1064  ND1 HIS A 139      10.617 -37.361  -1.182  1.00 40.86           N  
ATOM   1065  CD2 HIS A 139      11.334 -38.819   0.277  1.00 39.47           C  
ATOM   1066  CE1 HIS A 139      11.285 -36.693  -0.259  1.00 39.59           C  
ATOM   1067  NE2 HIS A 139      11.730 -37.554   0.637  1.00 39.49           N  
ATOM   1068  N   PHE A 140      11.415 -38.010  -4.243  1.00 43.01           N  
ATOM   1069  CA  PHE A 140      11.321 -36.954  -5.249  1.00 43.44           C  
ATOM   1070  C   PHE A 140      11.291 -37.555  -6.649  1.00 44.77           C  
ATOM   1071  O   PHE A 140      11.661 -38.712  -6.835  1.00 46.59           O  
ATOM   1072  CB  PHE A 140      12.499 -35.982  -5.129  1.00 42.99           C  
ATOM   1073  CG  PHE A 140      12.434 -35.087  -3.927  1.00 42.52           C  
ATOM   1074  CD1 PHE A 140      11.260 -34.432  -3.594  1.00 42.87           C  
ATOM   1075  CD2 PHE A 140      13.551 -34.898  -3.128  1.00 42.47           C  
ATOM   1076  CE1 PHE A 140      11.202 -33.604  -2.487  1.00 41.89           C  
ATOM   1077  CE2 PHE A 140      13.498 -34.074  -2.020  1.00 41.65           C  
ATOM   1078  CZ  PHE A 140      12.322 -33.426  -1.700  1.00 41.34           C  
ATOM   1079  N   THR A 141      10.849 -36.775  -7.630  1.00 45.10           N  
ATOM   1080  CA  THR A 141      10.973 -37.180  -9.027  1.00 48.62           C  
ATOM   1081  C   THR A 141      12.045 -36.335  -9.705  1.00 51.65           C  
ATOM   1082  O   THR A 141      12.389 -35.255  -9.224  1.00 51.03           O  
ATOM   1083  CB  THR A 141       9.644 -37.044  -9.801  1.00 49.17           C  
ATOM   1084  OG1 THR A 141       9.367 -35.661 -10.055  1.00 48.40           O  
ATOM   1085  CG2 THR A 141       8.500 -37.661  -9.014  1.00 49.38           C  
ATOM   1086  N   ARG A 142      12.569 -36.827 -10.823  1.00 54.80           N  
ATOM   1087  CA  ARG A 142      13.651 -36.144 -11.523  1.00 56.49           C  
ATOM   1088  C   ARG A 142      13.187 -34.812 -12.101  1.00 57.71           C  
ATOM   1089  O   ARG A 142      13.963 -33.861 -12.198  1.00 57.51           O  
ATOM   1090  CB  ARG A 142      14.215 -37.036 -12.631  1.00 58.90           C  
ATOM   1091  CG  ARG A 142      15.732 -37.109 -12.641  1.00 59.53           C  
ATOM   1092  CD  ARG A 142      16.241 -38.128 -13.646  1.00 62.19           C  
ATOM   1093  NE  ARG A 142      17.692 -38.266 -13.579  1.00 63.83           N  
ATOM   1094  CZ  ARG A 142      18.320 -39.190 -12.860  1.00 65.37           C  
ATOM   1095  NH1 ARG A 142      17.622 -40.066 -12.150  1.00 64.93           N  
ATOM   1096  NH2 ARG A 142      19.646 -39.244 -12.854  1.00 66.82           N  
ATOM   1097  N   GLU A 143      11.915 -34.750 -12.480  1.00 59.59           N  
ATOM   1098  CA  GLU A 143      11.329 -33.525 -13.011  1.00 61.51           C  
ATOM   1099  C   GLU A 143      11.119 -32.495 -11.903  1.00 59.07           C  
ATOM   1100  O   GLU A 143      11.243 -31.291 -12.128  1.00 59.56           O  
ATOM   1101  CB  GLU A 143      10.003 -33.834 -13.711  1.00 66.27           C  
ATOM   1102  CG  GLU A 143       9.288 -32.622 -14.283  1.00 70.68           C  
ATOM   1103  CD  GLU A 143      10.029 -31.994 -15.449  1.00 76.65           C  
ATOM   1104  OE1 GLU A 143      10.820 -32.700 -16.113  1.00 78.95           O  
ATOM   1105  OE2 GLU A 143       9.817 -30.790 -15.704  1.00 78.44           O  
ATOM   1106  N   GLN A 144      10.810 -32.982 -10.705  1.00 56.53           N  
ATOM   1107  CA  GLN A 144      10.522 -32.119  -9.562  1.00 53.35           C  
ATOM   1108  C   GLN A 144      11.739 -31.318  -9.109  1.00 52.40           C  
ATOM   1109  O   GLN A 144      11.623 -30.142  -8.765  1.00 51.69           O  
ATOM   1110  CB  GLN A 144       9.990 -32.956  -8.394  1.00 50.77           C  
ATOM   1111  CG  GLN A 144       9.654 -32.158  -7.141  1.00 48.32           C  
ATOM   1112  CD  GLN A 144       9.176 -33.044  -6.004  1.00 46.46           C  
ATOM   1113  OE1 GLN A 144       9.137 -34.267  -6.133  1.00 47.43           O  
ATOM   1114  NE2 GLN A 144       8.809 -32.429  -4.885  1.00 44.03           N  
ATOM   1115  N   ILE A 145      12.904 -31.955  -9.118  1.00 52.96           N  
ATOM   1116  CA  ILE A 145      14.105 -31.357  -8.542  1.00 52.23           C  
ATOM   1117  C   ILE A 145      15.061 -30.775  -9.582  1.00 53.66           C  
ATOM   1118  O   ILE A 145      16.244 -30.579  -9.301  1.00 53.60           O  
ATOM   1119  CB  ILE A 145      14.880 -32.385  -7.693  1.00 50.13           C  
ATOM   1120  CG1 ILE A 145      15.335 -33.557  -8.563  1.00 50.66           C  
ATOM   1121  CG2 ILE A 145      14.022 -32.876  -6.536  1.00 47.62           C  
ATOM   1122  CD1 ILE A 145      16.363 -34.435  -7.904  1.00 50.16           C  
ATOM   1123  N   LYS A 146      14.553 -30.496 -10.778  1.00 55.30           N  
ATOM   1124  CA  LYS A 146      15.382 -29.915 -11.828  1.00 56.66           C  
ATOM   1125  C   LYS A 146      15.873 -28.526 -11.431  1.00 54.05           C  
ATOM   1126  O   LYS A 146      15.076 -27.609 -11.237  1.00 53.98           O  
ATOM   1127  CB  LYS A 146      14.612 -29.848 -13.148  1.00 61.07           C  
ATOM   1128  CG  LYS A 146      15.346 -29.117 -14.263  1.00 64.13           C  
ATOM   1129  CD  LYS A 146      14.647 -27.811 -14.616  1.00 66.95           C  
ATOM   1130  CE  LYS A 146      15.429 -27.017 -15.652  1.00 70.02           C  
ATOM   1131  NZ  LYS A 146      14.696 -25.794 -16.085  1.00 71.91           N  
ATOM   1132  N   GLY A 147      17.189 -28.380 -11.304  1.00 52.33           N  
ATOM   1133  CA  GLY A 147      17.783 -27.111 -10.926  1.00 51.40           C  
ATOM   1134  C   GLY A 147      17.959 -26.945  -9.427  1.00 50.51           C  
ATOM   1135  O   GLY A 147      18.368 -25.882  -8.958  1.00 50.87           O  
ATOM   1136  N   TRP A 148      17.644 -27.992  -8.670  1.00 48.76           N  
ATOM   1137  CA  TRP A 148      17.827 -27.964  -7.223  1.00 46.61           C  
ATOM   1138  C   TRP A 148      19.286 -28.188  -6.848  1.00 46.70           C  
ATOM   1139  O   TRP A 148      20.008 -28.918  -7.524  1.00 46.61           O  
ATOM   1140  CB  TRP A 148      16.964 -29.026  -6.530  1.00 44.41           C  
ATOM   1141  CG  TRP A 148      15.490 -28.751  -6.514  1.00 42.07           C  
ATOM   1142  CD1 TRP A 148      14.786 -27.981  -7.391  1.00 41.74           C  
ATOM   1143  CD2 TRP A 148      14.539 -29.248  -5.563  1.00 39.62           C  
ATOM   1144  NE1 TRP A 148      13.455 -27.971  -7.049  1.00 40.58           N  
ATOM   1145  CE2 TRP A 148      13.278 -28.741  -5.930  1.00 39.26           C  
ATOM   1146  CE3 TRP A 148      14.633 -30.071  -4.437  1.00 38.10           C  
ATOM   1147  CZ2 TRP A 148      12.120 -29.032  -5.213  1.00 38.25           C  
ATOM   1148  CZ3 TRP A 148      13.484 -30.359  -3.727  1.00 37.12           C  
ATOM   1149  CH2 TRP A 148      12.244 -29.840  -4.117  1.00 37.65           C  
ATOM   1150  N   LYS A 149      19.709 -27.555  -5.760  1.00 46.99           N  
ATOM   1151  CA  LYS A 149      20.996 -27.852  -5.146  1.00 47.10           C  
ATOM   1152  C   LYS A 149      20.764 -28.194  -3.679  1.00 45.49           C  
ATOM   1153  O   LYS A 149      19.858 -27.651  -3.044  1.00 43.53           O  
ATOM   1154  CB  LYS A 149      21.963 -26.674  -5.294  1.00 47.59           C  
ATOM   1155  CG  LYS A 149      22.384 -26.397  -6.731  1.00 49.26           C  
ATOM   1156  CD  LYS A 149      23.062 -27.609  -7.347  1.00 50.66           C  
ATOM   1157  CE  LYS A 149      23.375 -27.393  -8.821  1.00 53.60           C  
ATOM   1158  NZ  LYS A 149      24.434 -26.367  -9.029  1.00 54.98           N  
ATOM   1159  N   GLY A 150      21.572 -29.100  -3.140  1.00 45.65           N  
ATOM   1160  CA  GLY A 150      21.350 -29.576  -1.788  1.00 43.93           C  
ATOM   1161  C   GLY A 150      22.529 -29.485  -0.837  1.00 42.34           C  
ATOM   1162  O   GLY A 150      23.691 -29.495  -1.250  1.00 43.97           O  
ATOM   1163  N   LEU A 151      22.208 -29.386   0.449  1.00 38.96           N  
ATOM   1164  CA  LEU A 151      23.186 -29.493   1.523  1.00 36.55           C  
ATOM   1165  C   LEU A 151      22.718 -30.573   2.491  1.00 36.61           C  
ATOM   1166  O   LEU A 151      21.674 -30.431   3.130  1.00 35.94           O  
ATOM   1167  CB  LEU A 151      23.363 -28.156   2.249  1.00 34.53           C  
ATOM   1168  CG  LEU A 151      24.148 -28.169   3.568  1.00 32.86           C  
ATOM   1169  CD1 LEU A 151      25.605 -28.565   3.352  1.00 31.70           C  
ATOM   1170  CD2 LEU A 151      24.052 -26.820   4.272  1.00 32.82           C  
ATOM   1171  N   PHE A 152      23.478 -31.658   2.589  1.00 36.75           N  
ATOM   1172  CA  PHE A 152      23.069 -32.781   3.423  1.00 35.15           C  
ATOM   1173  C   PHE A 152      23.855 -32.840   4.728  1.00 34.62           C  
ATOM   1174  O   PHE A 152      25.065 -33.065   4.730  1.00 35.28           O  
ATOM   1175  CB  PHE A 152      23.225 -34.099   2.661  1.00 34.90           C  
ATOM   1176  CG  PHE A 152      22.637 -35.283   3.376  1.00 34.66           C  
ATOM   1177  CD1 PHE A 152      21.285 -35.566   3.273  1.00 34.12           C  
ATOM   1178  CD2 PHE A 152      23.432 -36.110   4.155  1.00 33.44           C  
ATOM   1179  CE1 PHE A 152      20.737 -36.650   3.931  1.00 33.08           C  
ATOM   1180  CE2 PHE A 152      22.889 -37.197   4.813  1.00 32.63           C  
ATOM   1181  CZ  PHE A 152      21.540 -37.466   4.701  1.00 32.66           C  
HETATM 1182  N   CSO A 153      23.150 -32.634   5.836  1.00 33.20           N  
HETATM 1183  CA  CSO A 153      23.733 -32.760   7.169  1.00 32.25           C  
HETATM 1184  CB  CSO A 153      23.338 -31.566   8.047  1.00 30.40           C  
HETATM 1185  SG  CSO A 153      23.311 -30.053   7.046  1.00 52.57           S  
HETATM 1186  C   CSO A 153      23.356 -34.096   7.817  1.00 32.10           C  
HETATM 1187  O   CSO A 153      22.199 -34.324   8.172  1.00 31.44           O  
HETATM 1188  OD  CSO A 153      21.678 -29.338   6.933  1.00 25.61           O  
ATOM   1189  N   GLY A 154      24.346 -34.973   7.964  1.00 32.49           N  
ATOM   1190  CA  GLY A 154      24.113 -36.345   8.386  1.00 32.83           C  
ATOM   1191  C   GLY A 154      23.830 -36.580   9.860  1.00 34.36           C  
ATOM   1192  O   GLY A 154      23.270 -37.615  10.224  1.00 35.62           O  
ATOM   1193  N   ASP A 155      24.216 -35.640  10.716  1.00 34.51           N  
ATOM   1194  CA  ASP A 155      23.985 -35.797  12.149  1.00 36.25           C  
ATOM   1195  C   ASP A 155      22.587 -35.319  12.534  1.00 37.34           C  
ATOM   1196  O   ASP A 155      22.181 -35.418  13.690  1.00 34.74           O  
ATOM   1197  CB  ASP A 155      25.046 -35.041  12.951  1.00 38.00           C  
ATOM   1198  CG  ASP A 155      26.430 -35.645  12.799  1.00 41.82           C  
ATOM   1199  OD1 ASP A 155      26.542 -36.889  12.834  1.00 43.11           O  
ATOM   1200  OD2 ASP A 155      27.406 -34.878  12.639  1.00 43.24           O  
ATOM   1201  N   GLY A 156      21.848 -34.812  11.552  1.00 39.83           N  
ATOM   1202  CA  GLY A 156      20.521 -34.279  11.793  1.00 40.03           C  
ATOM   1203  C   GLY A 156      19.456 -35.332  12.046  1.00 39.26           C  
ATOM   1204  O   GLY A 156      19.758 -36.503  12.283  1.00 39.34           O  
ATOM   1205  N   GLY A 157      18.199 -34.903  11.994  1.00 35.88           N  
ATOM   1206  CA  GLY A 157      17.072 -35.791  12.204  1.00 34.05           C  
ATOM   1207  C   GLY A 157      15.955 -35.081  12.941  1.00 32.94           C  
ATOM   1208  O   GLY A 157      15.948 -33.851  13.025  1.00 33.11           O  
ATOM   1209  N   TRP A 158      15.008 -35.847  13.475  1.00 31.35           N  
ATOM   1210  CA  TRP A 158      13.923 -35.260  14.248  1.00 28.51           C  
ATOM   1211  C   TRP A 158      13.839 -35.859  15.650  1.00 27.93           C  
ATOM   1212  O   TRP A 158      14.497 -36.858  15.951  1.00 26.97           O  
ATOM   1213  CB  TRP A 158      12.589 -35.420  13.516  1.00 27.35           C  
ATOM   1214  CG  TRP A 158      12.219 -36.824  13.158  1.00 27.22           C  
ATOM   1215  CD1 TRP A 158      12.641 -37.531  12.071  1.00 28.16           C  
ATOM   1216  CD2 TRP A 158      11.323 -37.683  13.872  1.00 27.00           C  
ATOM   1217  NE1 TRP A 158      12.073 -38.783  12.070  1.00 28.33           N  
ATOM   1218  CE2 TRP A 158      11.260 -38.901  13.165  1.00 27.83           C  
ATOM   1219  CE3 TRP A 158      10.574 -37.544  15.043  1.00 27.02           C  
ATOM   1220  CZ2 TRP A 158      10.477 -39.972  13.592  1.00 28.56           C  
ATOM   1221  CZ3 TRP A 158       9.797 -38.611  15.465  1.00 26.67           C  
ATOM   1222  CH2 TRP A 158       9.755 -39.808  14.741  1.00 27.76           C  
ATOM   1223  N   LEU A 159      13.031 -35.233  16.502  1.00 27.34           N  
ATOM   1224  CA  LEU A 159      12.938 -35.601  17.912  1.00 26.10           C  
ATOM   1225  C   LEU A 159      11.489 -35.810  18.341  1.00 26.04           C  
ATOM   1226  O   LEU A 159      10.645 -34.951  18.100  1.00 25.98           O  
ATOM   1227  CB  LEU A 159      13.573 -34.513  18.783  1.00 24.68           C  
ATOM   1228  CG  LEU A 159      15.021 -34.109  18.494  1.00 24.88           C  
ATOM   1229  CD1 LEU A 159      15.327 -32.741  19.078  1.00 24.13           C  
ATOM   1230  CD2 LEU A 159      15.979 -35.144  19.052  1.00 25.70           C  
ATOM   1231  N   ALA A 160      11.200 -36.942  18.977  1.00 25.59           N  
ATOM   1232  CA  ALA A 160       9.880 -37.155  19.568  1.00 24.81           C  
ATOM   1233  C   ALA A 160       9.715 -36.213  20.753  1.00 24.86           C  
ATOM   1234  O   ALA A 160       9.995 -36.581  21.893  1.00 25.49           O  
ATOM   1235  CB  ALA A 160       9.700 -38.598  20.002  1.00 24.01           C  
ATOM   1236  N   ALA A 161       9.256 -34.998  20.470  1.00 23.92           N  
ATOM   1237  CA  ALA A 161       9.297 -33.902  21.436  1.00 22.17           C  
ATOM   1238  C   ALA A 161       8.506 -34.163  22.720  1.00 23.77           C  
ATOM   1239  O   ALA A 161       9.090 -34.260  23.800  1.00 24.28           O  
ATOM   1240  CB  ALA A 161       8.810 -32.619  20.781  1.00 19.93           C  
ATOM   1241  N   ALA A 162       7.185 -34.260  22.601  1.00 23.57           N  
ATOM   1242  CA  ALA A 162       6.318 -34.451  23.763  1.00 25.14           C  
ATOM   1243  C   ALA A 162       6.670 -35.709  24.553  1.00 26.97           C  
ATOM   1244  O   ALA A 162       6.605 -35.714  25.783  1.00 28.74           O  
ATOM   1245  CB  ALA A 162       4.861 -34.499  23.329  1.00 25.56           C  
ATOM   1246  N   LYS A 163       7.041 -36.772  23.845  1.00 26.45           N  
ATOM   1247  CA  LYS A 163       7.401 -38.026  24.495  1.00 26.80           C  
ATOM   1248  C   LYS A 163       8.662 -37.873  25.342  1.00 27.08           C  
ATOM   1249  O   LYS A 163       8.829 -38.565  26.346  1.00 28.97           O  
ATOM   1250  CB  LYS A 163       7.602 -39.135  23.460  1.00 27.38           C  
ATOM   1251  CG  LYS A 163       6.335 -39.553  22.729  1.00 28.15           C  
ATOM   1252  CD  LYS A 163       6.634 -40.611  21.677  1.00 28.16           C  
ATOM   1253  CE  LYS A 163       5.379 -41.029  20.934  1.00 29.06           C  
ATOM   1254  NZ  LYS A 163       5.671 -42.074  19.913  1.00 31.22           N  
ATOM   1255  N   ALA A 164       9.544 -36.966  24.939  1.00 24.98           N  
ATOM   1256  CA  ALA A 164      10.786 -36.742  25.670  1.00 24.60           C  
ATOM   1257  C   ALA A 164      10.537 -35.980  26.973  1.00 25.98           C  
ATOM   1258  O   ALA A 164      11.091 -36.327  28.019  1.00 25.49           O  
ATOM   1259  CB  ALA A 164      11.784 -36.001  24.802  1.00 23.56           C  
ATOM   1260  N   ILE A 165       9.704 -34.945  26.905  1.00 26.24           N  
ATOM   1261  CA  ILE A 165       9.360 -34.159  28.086  1.00 26.62           C  
ATOM   1262  C   ILE A 165       8.565 -35.011  29.069  1.00 30.03           C  
ATOM   1263  O   ILE A 165       8.763 -34.932  30.285  1.00 30.36           O  
ATOM   1264  CB  ILE A 165       8.557 -32.894  27.712  1.00 23.51           C  
ATOM   1265  CG1 ILE A 165       9.440 -31.923  26.924  1.00 21.12           C  
ATOM   1266  CG2 ILE A 165       8.012 -32.208  28.958  1.00 22.68           C  
ATOM   1267  CD1 ILE A 165       8.777 -30.593  26.626  1.00 20.41           C  
ATOM   1268  N   ASN A 166       7.677 -35.838  28.527  1.00 31.12           N  
ATOM   1269  CA  ASN A 166       6.915 -36.782  29.331  1.00 31.64           C  
ATOM   1270  C   ASN A 166       7.826 -37.785  30.034  1.00 33.81           C  
ATOM   1271  O   ASN A 166       7.543 -38.215  31.154  1.00 36.42           O  
ATOM   1272  CB  ASN A 166       5.895 -37.516  28.457  1.00 31.93           C  
ATOM   1273  CG  ASN A 166       5.128 -38.577  29.219  1.00 33.01           C  
ATOM   1274  OD1 ASN A 166       4.178 -38.275  29.940  1.00 34.47           O  
ATOM   1275  ND2 ASN A 166       5.532 -39.830  29.055  1.00 33.55           N  
ATOM   1276  N   ALA A 167       8.923 -38.151  29.376  1.00 32.97           N  
ATOM   1277  CA  ALA A 167       9.876 -39.094  29.953  1.00 32.36           C  
ATOM   1278  C   ALA A 167      10.562 -38.481  31.169  1.00 32.91           C  
ATOM   1279  O   ALA A 167      10.854 -39.171  32.146  1.00 35.23           O  
ATOM   1280  CB  ALA A 167      10.902 -39.519  28.918  1.00 31.22           C  
ATOM   1281  N   ILE A 168      10.814 -37.179  31.106  1.00 32.01           N  
ATOM   1282  CA  ILE A 168      11.398 -36.465  32.234  1.00 31.76           C  
ATOM   1283  C   ILE A 168      10.385 -36.377  33.370  1.00 31.45           C  
ATOM   1284  O   ILE A 168      10.716 -36.615  34.534  1.00 30.62           O  
ATOM   1285  CB  ILE A 168      11.860 -35.050  31.834  1.00 30.35           C  
ATOM   1286  CG1 ILE A 168      12.941 -35.136  30.753  1.00 29.64           C  
ATOM   1287  CG2 ILE A 168      12.376 -34.289  33.049  1.00 29.67           C  
ATOM   1288  CD1 ILE A 168      13.464 -33.793  30.297  1.00 28.41           C  
ATOM   1289  N   GLY A 169       9.144 -36.055  33.017  1.00 31.73           N  
ATOM   1290  CA  GLY A 169       8.069 -35.935  33.986  1.00 34.29           C  
ATOM   1291  C   GLY A 169       7.805 -37.196  34.787  1.00 36.73           C  
ATOM   1292  O   GLY A 169       7.579 -37.132  35.995  1.00 37.15           O  
ATOM   1293  N   GLN A 170       7.826 -38.344  34.116  1.00 38.53           N  
ATOM   1294  CA  GLN A 170       7.629 -39.624  34.789  1.00 41.73           C  
ATOM   1295  C   GLN A 170       8.718 -39.851  35.832  1.00 40.44           C  
ATOM   1296  O   GLN A 170       8.455 -40.370  36.918  1.00 39.47           O  
ATOM   1297  CB  GLN A 170       7.611 -40.771  33.776  1.00 46.12           C  
ATOM   1298  CG  GLN A 170       6.315 -40.873  32.985  1.00 52.35           C  
ATOM   1299  CD  GLN A 170       6.414 -41.824  31.806  1.00 59.18           C  
ATOM   1300  OE1 GLN A 170       7.486 -42.001  31.226  1.00 62.19           O  
ATOM   1301  NE2 GLN A 170       5.293 -42.442  31.446  1.00 61.81           N  
ATOM   1302  N   PHE A 171       9.939 -39.445  35.497  1.00 39.15           N  
ATOM   1303  CA  PHE A 171      11.067 -39.558  36.413  1.00 38.69           C  
ATOM   1304  C   PHE A 171      10.905 -38.623  37.611  1.00 39.58           C  
ATOM   1305  O   PHE A 171      11.182 -39.011  38.744  1.00 41.55           O  
ATOM   1306  CB  PHE A 171      12.376 -39.264  35.678  1.00 36.89           C  
ATOM   1307  CG  PHE A 171      13.587 -39.261  36.566  1.00 36.45           C  
ATOM   1308  CD1 PHE A 171      13.993 -40.415  37.211  1.00 37.56           C  
ATOM   1309  CD2 PHE A 171      14.330 -38.105  36.743  1.00 36.50           C  
ATOM   1310  CE1 PHE A 171      15.112 -40.415  38.028  1.00 38.19           C  
ATOM   1311  CE2 PHE A 171      15.451 -38.099  37.558  1.00 36.90           C  
ATOM   1312  CZ  PHE A 171      15.841 -39.256  38.200  1.00 37.14           C  
ATOM   1313  N   LEU A 172      10.448 -37.398  37.359  1.00 37.97           N  
ATOM   1314  CA  LEU A 172      10.254 -36.419  38.427  1.00 37.98           C  
ATOM   1315  C   LEU A 172       9.227 -36.904  39.445  1.00 40.78           C  
ATOM   1316  O   LEU A 172       9.479 -36.894  40.652  1.00 41.36           O  
ATOM   1317  CB  LEU A 172       9.818 -35.067  37.854  1.00 35.15           C  
ATOM   1318  CG  LEU A 172      10.759 -34.353  36.879  1.00 33.24           C  
ATOM   1319  CD1 LEU A 172      10.249 -32.950  36.583  1.00 31.38           C  
ATOM   1320  CD2 LEU A 172      12.178 -34.307  37.420  1.00 33.84           C  
ATOM   1321  N   LYS A 173       8.069 -37.329  38.949  1.00 41.88           N  
ATOM   1322  CA  LYS A 173       6.997 -37.816  39.809  1.00 43.53           C  
ATOM   1323  C   LYS A 173       7.427 -39.054  40.588  1.00 45.23           C  
ATOM   1324  O   LYS A 173       7.103 -39.202  41.763  1.00 45.69           O  
ATOM   1325  CB  LYS A 173       5.743 -38.110  38.979  1.00 43.20           C  
ATOM   1326  CG  LYS A 173       5.005 -36.850  38.548  1.00 43.75           C  
ATOM   1327  CD  LYS A 173       4.544 -36.903  37.099  1.00 44.14           C  
ATOM   1328  CE  LYS A 173       3.230 -37.644  36.955  1.00 45.73           C  
ATOM   1329  NZ  LYS A 173       2.726 -37.578  35.557  1.00 46.12           N  
ATOM   1330  N   GLU A 174       8.178 -39.930  39.931  1.00 47.16           N  
ATOM   1331  CA  GLU A 174       8.610 -41.177  40.546  1.00 50.04           C  
ATOM   1332  C   GLU A 174       9.649 -40.926  41.634  1.00 49.59           C  
ATOM   1333  O   GLU A 174       9.836 -41.752  42.524  1.00 50.32           O  
ATOM   1334  CB  GLU A 174       9.169 -42.125  39.483  1.00 53.37           C  
ATOM   1335  CG  GLU A 174       9.246 -43.577  39.911  1.00 58.62           C  
ATOM   1336  CD  GLU A 174       9.484 -44.512  38.740  1.00 63.40           C  
ATOM   1337  OE1 GLU A 174       9.825 -45.691  38.981  1.00 67.30           O  
ATOM   1338  OE2 GLU A 174       9.326 -44.070  37.581  1.00 63.14           O  
ATOM   1339  N   GLN A 175      10.319 -39.781  41.563  1.00 48.15           N  
ATOM   1340  CA  GLN A 175      11.344 -39.437  42.543  1.00 46.43           C  
ATOM   1341  C   GLN A 175      10.763 -38.709  43.750  1.00 45.70           C  
ATOM   1342  O   GLN A 175      11.389 -38.650  44.808  1.00 46.69           O  
ATOM   1343  CB  GLN A 175      12.435 -38.583  41.899  1.00 45.00           C  
ATOM   1344  CG  GLN A 175      13.357 -39.364  40.981  1.00 44.64           C  
ATOM   1345  CD  GLN A 175      14.063 -40.491  41.702  1.00 45.67           C  
ATOM   1346  OE1 GLN A 175      14.490 -40.338  42.846  1.00 45.82           O  
ATOM   1347  NE2 GLN A 175      14.181 -41.637  41.039  1.00 46.63           N  
ATOM   1348  N   GLY A 176       9.567 -38.153  43.588  1.00 44.37           N  
ATOM   1349  CA  GLY A 176       8.905 -37.463  44.679  1.00 43.86           C  
ATOM   1350  C   GLY A 176       9.039 -35.952  44.625  1.00 42.71           C  
ATOM   1351  O   GLY A 176       9.050 -35.286  45.659  1.00 44.09           O  
ATOM   1352  N   VAL A 177       9.151 -35.410  43.418  1.00 40.57           N  
ATOM   1353  CA  VAL A 177       9.136 -33.966  43.225  1.00 39.15           C  
ATOM   1354  C   VAL A 177       7.719 -33.447  43.454  1.00 40.97           C  
ATOM   1355  O   VAL A 177       6.750 -34.055  43.000  1.00 40.74           O  
ATOM   1356  CB  VAL A 177       9.629 -33.580  41.811  1.00 36.35           C  
ATOM   1357  CG1 VAL A 177       9.408 -32.098  41.538  1.00 35.34           C  
ATOM   1358  CG2 VAL A 177      11.094 -33.941  41.647  1.00 36.18           C  
ATOM   1359  N   LYS A 178       7.598 -32.335  44.174  1.00 42.62           N  
ATOM   1360  CA  LYS A 178       6.293 -31.752  44.468  1.00 43.00           C  
ATOM   1361  C   LYS A 178       5.823 -30.870  43.313  1.00 40.63           C  
ATOM   1362  O   LYS A 178       6.624 -30.163  42.704  1.00 40.58           O  
ATOM   1363  CB  LYS A 178       6.354 -30.956  45.774  1.00 45.90           C  
ATOM   1364  CG  LYS A 178       6.832 -31.785  46.960  1.00 48.53           C  
ATOM   1365  CD  LYS A 178       7.043 -30.935  48.206  1.00 51.97           C  
ATOM   1366  CE  LYS A 178       5.736 -30.348  48.715  1.00 54.52           C  
ATOM   1367  NZ  LYS A 178       5.932 -29.570  49.975  1.00 56.50           N  
ATOM   1368  N   PHE A 179       4.527 -30.920  43.013  1.00 39.67           N  
ATOM   1369  CA  PHE A 179       3.975 -30.216  41.854  1.00 38.71           C  
ATOM   1370  C   PHE A 179       2.825 -29.272  42.195  1.00 39.82           C  
ATOM   1371  O   PHE A 179       2.156 -29.422  43.218  1.00 39.87           O  
ATOM   1372  CB  PHE A 179       3.489 -31.218  40.803  1.00 36.68           C  
ATOM   1373  CG  PHE A 179       4.594 -31.903  40.057  1.00 36.20           C  
ATOM   1374  CD1 PHE A 179       5.149 -31.323  38.928  1.00 36.04           C  
ATOM   1375  CD2 PHE A 179       5.070 -33.133  40.475  1.00 35.92           C  
ATOM   1376  CE1 PHE A 179       6.166 -31.955  38.233  1.00 34.89           C  
ATOM   1377  CE2 PHE A 179       6.085 -33.768  39.785  1.00 35.51           C  
ATOM   1378  CZ  PHE A 179       6.632 -33.179  38.664  1.00 34.62           C  
ATOM   1379  N   GLY A 180       2.600 -28.306  41.310  1.00 39.47           N  
ATOM   1380  CA  GLY A 180       1.468 -27.405  41.409  1.00 38.91           C  
ATOM   1381  C   GLY A 180       0.920 -27.090  40.028  1.00 38.71           C  
ATOM   1382  O   GLY A 180       1.643 -26.581  39.170  1.00 38.51           O  
ATOM   1383  N   PHE A 181      -0.353 -27.407  39.803  1.00 38.34           N  
ATOM   1384  CA  PHE A 181      -0.982 -27.162  38.510  1.00 37.88           C  
ATOM   1385  C   PHE A 181      -2.199 -26.256  38.671  1.00 37.99           C  
ATOM   1386  O   PHE A 181      -2.622 -25.968  39.790  1.00 38.68           O  
ATOM   1387  CB  PHE A 181      -1.375 -28.484  37.837  1.00 39.79           C  
ATOM   1388  CG  PHE A 181      -2.721 -29.014  38.262  1.00 42.80           C  
ATOM   1389  CD1 PHE A 181      -2.868 -29.699  39.458  1.00 43.90           C  
ATOM   1390  CD2 PHE A 181      -3.838 -28.836  37.455  1.00 43.24           C  
ATOM   1391  CE1 PHE A 181      -4.104 -30.186  39.848  1.00 44.82           C  
ATOM   1392  CE2 PHE A 181      -5.075 -29.319  37.840  1.00 44.25           C  
ATOM   1393  CZ  PHE A 181      -5.209 -29.996  39.037  1.00 45.16           C  
ATOM   1394  N   GLY A 182      -2.753 -25.806  37.549  1.00 38.00           N  
ATOM   1395  CA  GLY A 182      -3.906 -24.925  37.567  1.00 38.51           C  
ATOM   1396  C   GLY A 182      -3.561 -23.563  38.134  1.00 39.36           C  
ATOM   1397  O   GLY A 182      -2.490 -23.023  37.861  1.00 39.95           O  
ATOM   1398  N   GLU A 183      -4.467 -23.006  38.928  1.00 40.75           N  
ATOM   1399  CA  GLU A 183      -4.214 -21.725  39.572  1.00 42.97           C  
ATOM   1400  C   GLU A 183      -3.174 -21.850  40.687  1.00 43.20           C  
ATOM   1401  O   GLU A 183      -2.568 -20.858  41.092  1.00 44.15           O  
ATOM   1402  CB  GLU A 183      -5.508 -21.140  40.130  1.00 46.05           C  
ATOM   1403  CG  GLU A 183      -6.468 -20.640  39.069  1.00 48.19           C  
ATOM   1404  CD  GLU A 183      -7.569 -19.773  39.645  1.00 52.86           C  
ATOM   1405  OE1 GLU A 183      -7.672 -19.682  40.888  1.00 53.49           O  
ATOM   1406  OE2 GLU A 183      -8.329 -19.177  38.853  1.00 56.02           O  
ATOM   1407  N   ALA A 184      -2.970 -23.068  41.182  1.00 41.04           N  
ATOM   1408  CA  ALA A 184      -1.991 -23.306  42.237  1.00 39.34           C  
ATOM   1409  C   ALA A 184      -0.594 -23.487  41.657  1.00 37.32           C  
ATOM   1410  O   ALA A 184       0.376 -23.669  42.394  1.00 36.94           O  
ATOM   1411  CB  ALA A 184      -2.381 -24.522  43.064  1.00 40.14           C  
ATOM   1412  N   GLY A 185      -0.498 -23.441  40.332  1.00 35.27           N  
ATOM   1413  CA  GLY A 185       0.778 -23.571  39.654  1.00 32.63           C  
ATOM   1414  C   GLY A 185       1.066 -22.415  38.716  1.00 31.40           C  
ATOM   1415  O   GLY A 185       2.114 -22.375  38.071  1.00 29.90           O  
ATOM   1416  N   THR A 186       0.134 -21.469  38.643  1.00 31.98           N  
ATOM   1417  CA  THR A 186       0.283 -20.313  37.769  1.00 32.91           C  
ATOM   1418  C   THR A 186       0.917 -19.135  38.499  1.00 35.55           C  
ATOM   1419  O   THR A 186       0.300 -18.527  39.370  1.00 37.86           O  
ATOM   1420  CB  THR A 186      -1.071 -19.872  37.183  1.00 33.03           C  
ATOM   1421  OG1 THR A 186      -1.632 -20.942  36.412  1.00 32.09           O  
ATOM   1422  CG2 THR A 186      -0.891 -18.656  36.289  1.00 33.36           C  
ATOM   1423  N   PHE A 187       2.152 -18.821  38.125  1.00 37.06           N  
ATOM   1424  CA  PHE A 187       2.924 -17.747  38.745  1.00 38.41           C  
ATOM   1425  C   PHE A 187       2.208 -16.400  38.687  1.00 38.13           C  
ATOM   1426  O   PHE A 187       1.658 -16.024  37.654  1.00 38.77           O  
ATOM   1427  CB  PHE A 187       4.294 -17.644  38.065  1.00 39.43           C  
ATOM   1428  CG  PHE A 187       5.135 -16.497  38.547  1.00 41.52           C  
ATOM   1429  CD1 PHE A 187       5.076 -15.262  37.918  1.00 42.89           C  
ATOM   1430  CD2 PHE A 187       6.001 -16.658  39.616  1.00 42.93           C  
ATOM   1431  CE1 PHE A 187       5.851 -14.207  38.355  1.00 44.75           C  
ATOM   1432  CE2 PHE A 187       6.782 -15.605  40.057  1.00 44.85           C  
ATOM   1433  CZ  PHE A 187       6.708 -14.380  39.424  1.00 45.81           C  
ATOM   1434  N   LYS A 188       2.223 -15.676  39.802  1.00 37.60           N  
ATOM   1435  CA  LYS A 188       1.666 -14.330  39.844  1.00 37.75           C  
ATOM   1436  C   LYS A 188       2.751 -13.295  40.143  1.00 37.88           C  
ATOM   1437  O   LYS A 188       2.893 -12.309  39.421  1.00 37.45           O  
ATOM   1438  CB  LYS A 188       0.551 -14.235  40.886  1.00 38.82           C  
ATOM   1439  CG  LYS A 188      -0.066 -12.852  40.987  1.00 42.05           C  
ATOM   1440  CD  LYS A 188      -1.133 -12.784  42.066  1.00 44.30           C  
ATOM   1441  CE  LYS A 188      -1.771 -11.405  42.108  1.00 46.88           C  
ATOM   1442  NZ  LYS A 188      -2.849 -11.316  43.129  1.00 49.35           N  
ATOM   1443  N   LYS A 189       3.517 -13.528  41.206  1.00 37.74           N  
ATOM   1444  CA  LYS A 189       4.570 -12.599  41.611  1.00 38.97           C  
ATOM   1445  C   LYS A 189       5.571 -13.268  42.544  1.00 38.27           C  
ATOM   1446  O   LYS A 189       5.244 -14.259  43.192  1.00 38.54           O  
ATOM   1447  CB  LYS A 189       3.967 -11.367  42.293  1.00 40.52           C  
ATOM   1448  CG  LYS A 189       3.196 -11.674  43.567  1.00 40.83           C  
ATOM   1449  CD  LYS A 189       2.526 -10.426  44.121  1.00 42.68           C  
ATOM   1450  CE  LYS A 189       1.586 -10.768  45.266  1.00 44.25           C  
ATOM   1451  NZ  LYS A 189       0.835  -9.576  45.747  1.00 46.84           N  
ATOM   1452  N   PRO A 190       6.800 -12.730  42.610  1.00 38.31           N  
ATOM   1453  CA  PRO A 190       7.792 -13.222  43.573  1.00 37.36           C  
ATOM   1454  C   PRO A 190       7.503 -12.726  44.988  1.00 37.50           C  
ATOM   1455  O   PRO A 190       6.844 -11.700  45.146  1.00 36.93           O  
ATOM   1456  CB  PRO A 190       9.115 -12.634  43.059  1.00 37.30           C  
ATOM   1457  CG  PRO A 190       8.821 -12.099  41.689  1.00 37.64           C  
ATOM   1458  CD  PRO A 190       7.377 -11.729  41.701  1.00 38.28           C  
ATOM   1459  N   LEU A 191       7.992 -13.446  45.994  1.00 38.43           N  
ATOM   1460  CA  LEU A 191       7.888 -13.006  47.384  1.00 38.71           C  
ATOM   1461  C   LEU A 191       9.233 -12.473  47.870  1.00 41.38           C  
ATOM   1462  O   LEU A 191      10.277 -13.078  47.616  1.00 42.61           O  
ATOM   1463  CB  LEU A 191       7.416 -14.149  48.284  1.00 36.60           C  
ATOM   1464  CG  LEU A 191       6.010 -14.695  48.023  1.00 35.56           C  
ATOM   1465  CD1 LEU A 191       5.684 -15.813  49.001  1.00 35.72           C  
ATOM   1466  CD2 LEU A 191       4.967 -13.588  48.104  1.00 34.75           C  
ATOM   1467  N   PHE A 192       9.205 -11.342  48.568  1.00 42.48           N  
ATOM   1468  CA  PHE A 192      10.433 -10.690  49.011  1.00 43.68           C  
ATOM   1469  C   PHE A 192      10.515 -10.574  50.530  1.00 45.27           C  
ATOM   1470  O   PHE A 192       9.496 -10.566  51.221  1.00 44.77           O  
ATOM   1471  CB  PHE A 192      10.555  -9.306  48.373  1.00 45.72           C  
ATOM   1472  CG  PHE A 192      10.566  -9.335  46.873  1.00 46.13           C  
ATOM   1473  CD1 PHE A 192      11.746  -9.562  46.182  1.00 46.81           C  
ATOM   1474  CD2 PHE A 192       9.397  -9.141  46.153  1.00 45.90           C  
ATOM   1475  CE1 PHE A 192      11.762  -9.593  44.799  1.00 46.39           C  
ATOM   1476  CE2 PHE A 192       9.406  -9.170  44.769  1.00 46.11           C  
ATOM   1477  CZ  PHE A 192      10.591  -9.397  44.090  1.00 45.82           C  
ATOM   1478  N   ALA A 193      11.739 -10.477  51.038  1.00 47.74           N  
ATOM   1479  CA  ALA A 193      11.979 -10.413  52.474  1.00 50.64           C  
ATOM   1480  C   ALA A 193      11.693  -9.022  53.035  1.00 54.25           C  
ATOM   1481  O   ALA A 193      11.113  -8.887  54.113  1.00 55.62           O  
ATOM   1482  CB  ALA A 193      13.409 -10.823  52.786  1.00 51.17           C  
ATOM   1483  N   ASP A 194      12.105  -7.992  52.304  1.00 56.32           N  
ATOM   1484  CA  ASP A 194      11.860  -6.617  52.726  1.00 60.14           C  
ATOM   1485  C   ASP A 194      11.248  -5.788  51.605  1.00 59.34           C  
ATOM   1486  O   ASP A 194      11.069  -6.273  50.489  1.00 57.78           O  
ATOM   1487  CB  ASP A 194      13.154  -5.968  53.216  1.00 64.93           C  
ATOM   1488  CG  ASP A 194      13.651  -6.573  54.513  1.00 68.59           C  
ATOM   1489  OD1 ASP A 194      13.082  -6.244  55.576  1.00 70.35           O  
ATOM   1490  OD2 ASP A 194      14.609  -7.375  54.470  1.00 69.00           O  
ATOM   1491  N   ALA A 195      10.937  -4.533  51.911  1.00 61.47           N  
ATOM   1492  CA  ALA A 195      10.262  -3.649  50.966  1.00 62.60           C  
ATOM   1493  C   ALA A 195      11.165  -3.260  49.801  1.00 62.36           C  
ATOM   1494  O   ALA A 195      10.682  -2.928  48.717  1.00 61.42           O  
ATOM   1495  CB  ALA A 195       9.758  -2.404  51.680  1.00 65.54           C  
ATOM   1496  N   ASP A 196      12.475  -3.304  50.025  1.00 63.51           N  
ATOM   1497  CA  ASP A 196      13.441  -2.942  48.993  1.00 63.90           C  
ATOM   1498  C   ASP A 196      13.464  -3.960  47.856  1.00 60.61           C  
ATOM   1499  O   ASP A 196      13.994  -3.684  46.781  1.00 60.87           O  
ATOM   1500  CB  ASP A 196      14.845  -2.791  49.592  1.00 67.02           C  
ATOM   1501  CG  ASP A 196      15.284  -4.012  50.388  1.00 68.94           C  
ATOM   1502  OD1 ASP A 196      14.613  -5.063  50.317  1.00 69.38           O  
ATOM   1503  OD2 ASP A 196      16.316  -3.920  51.086  1.00 70.96           O  
ATOM   1504  N   GLU A 197      12.889  -5.133  48.113  1.00 58.44           N  
ATOM   1505  CA  GLU A 197      12.791  -6.208  47.127  1.00 57.05           C  
ATOM   1506  C   GLU A 197      14.140  -6.606  46.535  1.00 56.56           C  
ATOM   1507  O   GLU A 197      14.266  -6.770  45.322  1.00 56.90           O  
ATOM   1508  CB  GLU A 197      11.836  -5.813  45.996  1.00 57.12           C  
ATOM   1509  CG  GLU A 197      10.379  -5.733  46.408  1.00 57.21           C  
ATOM   1510  CD  GLU A 197       9.453  -5.568  45.220  1.00 55.89           C  
ATOM   1511  OE1 GLU A 197       9.943  -5.210  44.128  1.00 55.89           O  
ATOM   1512  OE2 GLU A 197       8.237  -5.802  45.376  1.00 55.29           O  
ATOM   1513  N   LYS A 198      15.143  -6.765  47.391  1.00 56.42           N  
ATOM   1514  CA  LYS A 198      16.463  -7.188  46.938  1.00 56.11           C  
ATOM   1515  C   LYS A 198      16.749  -8.628  47.347  1.00 54.50           C  
ATOM   1516  O   LYS A 198      17.820  -9.162  47.060  1.00 55.09           O  
ATOM   1517  CB  LYS A 198      17.551  -6.264  47.489  1.00 59.03           C  
ATOM   1518  CG  LYS A 198      17.332  -4.791  47.195  1.00 61.92           C  
ATOM   1519  CD  LYS A 198      18.626  -4.000  47.332  1.00 65.22           C  
ATOM   1520  CE  LYS A 198      19.344  -4.313  48.636  1.00 68.09           C  
ATOM   1521  NZ  LYS A 198      18.512  -4.001  49.832  1.00 70.28           N  
ATOM   1522  N   THR A 199      15.788  -9.252  48.020  1.00 52.46           N  
ATOM   1523  CA  THR A 199      15.944 -10.629  48.470  1.00 49.39           C  
ATOM   1524  C   THR A 199      14.667 -11.429  48.242  1.00 45.04           C  
ATOM   1525  O   THR A 199      13.705 -11.317  49.002  1.00 44.40           O  
ATOM   1526  CB  THR A 199      16.323 -10.695  49.960  1.00 51.74           C  
ATOM   1527  OG1 THR A 199      17.482  -9.888  50.197  1.00 54.08           O  
ATOM   1528  CG2 THR A 199      16.615 -12.128  50.372  1.00 51.03           C  
ATOM   1529  N   CYS A 200      14.666 -12.231  47.183  1.00 42.03           N  
ATOM   1530  CA  CYS A 200      13.537 -13.098  46.862  1.00 39.06           C  
ATOM   1531  C   CYS A 200      13.525 -14.324  47.775  1.00 37.87           C  
ATOM   1532  O   CYS A 200      14.567 -14.934  48.014  1.00 37.71           O  
ATOM   1533  CB  CYS A 200      13.601 -13.525  45.391  1.00 37.27           C  
ATOM   1534  SG  CYS A 200      12.263 -14.614  44.851  1.00 38.79           S  
ATOM   1535  N   ILE A 201      12.352 -14.681  48.289  1.00 37.42           N  
ATOM   1536  CA  ILE A 201      12.244 -15.839  49.173  1.00 39.11           C  
ATOM   1537  C   ILE A 201      11.184 -16.831  48.695  1.00 36.32           C  
ATOM   1538  O   ILE A 201      10.937 -17.846  49.347  1.00 34.55           O  
ATOM   1539  CB  ILE A 201      11.923 -15.421  50.629  1.00 42.81           C  
ATOM   1540  CG1 ILE A 201      10.658 -14.558  50.679  1.00 44.32           C  
ATOM   1541  CG2 ILE A 201      13.107 -14.691  51.253  1.00 35.19           C  
ATOM   1542  CD1 ILE A 201      10.236 -14.169  52.085  1.00 35.30           C  
ATOM   1543  N   GLY A 202      10.566 -16.540  47.555  1.00 35.60           N  
ATOM   1544  CA  GLY A 202       9.600 -17.453  46.973  1.00 35.14           C  
ATOM   1545  C   GLY A 202       8.678 -16.821  45.948  1.00 36.31           C  
ATOM   1546  O   GLY A 202       8.938 -15.722  45.457  1.00 37.45           O  
ATOM   1547  N   VAL A 203       7.600 -17.529  45.614  1.00 34.89           N  
ATOM   1548  CA  VAL A 203       6.613 -17.029  44.662  1.00 34.74           C  
ATOM   1549  C   VAL A 203       5.191 -17.216  45.180  1.00 36.17           C  
ATOM   1550  O   VAL A 203       4.927 -18.087  46.012  1.00 36.17           O  
ATOM   1551  CB  VAL A 203       6.725 -17.730  43.285  1.00 32.54           C  
ATOM   1552  CG1 VAL A 203       8.143 -17.656  42.757  1.00 32.95           C  
ATOM   1553  CG2 VAL A 203       6.268 -19.175  43.376  1.00 31.26           C  
ATOM   1554  N   GLU A 204       4.278 -16.391  44.678  1.00 37.18           N  
ATOM   1555  CA  GLU A 204       2.859 -16.555  44.963  1.00 38.77           C  
ATOM   1556  C   GLU A 204       2.108 -16.842  43.670  1.00 38.15           C  
ATOM   1557  O   GLU A 204       2.335 -16.185  42.656  1.00 38.28           O  
ATOM   1558  CB  GLU A 204       2.284 -15.311  45.644  1.00 40.66           C  
ATOM   1559  CG  GLU A 204       0.793 -15.409  45.928  1.00 42.48           C  
ATOM   1560  CD  GLU A 204       0.222 -14.142  46.533  1.00 45.48           C  
ATOM   1561  OE1 GLU A 204      -1.002 -13.924  46.418  1.00 45.36           O  
ATOM   1562  OE2 GLU A 204       0.997 -13.366  47.126  1.00 48.30           O  
ATOM   1563  N   THR A 205       1.225 -17.832  43.702  1.00 37.72           N  
ATOM   1564  CA  THR A 205       0.421 -18.161  42.533  1.00 37.42           C  
ATOM   1565  C   THR A 205      -0.871 -17.341  42.534  1.00 36.73           C  
ATOM   1566  O   THR A 205      -1.160 -16.631  43.497  1.00 35.06           O  
ATOM   1567  CB  THR A 205       0.096 -19.668  42.474  1.00 37.16           C  
ATOM   1568  OG1 THR A 205      -0.542 -20.074  43.690  1.00 39.03           O  
ATOM   1569  CG2 THR A 205       1.370 -20.479  42.286  1.00 34.92           C  
ATOM   1570  N   VAL A 206      -1.641 -17.439  41.453  1.00 37.26           N  
ATOM   1571  CA  VAL A 206      -2.807 -16.577  41.265  1.00 38.66           C  
ATOM   1572  C   VAL A 206      -3.984 -16.961  42.157  1.00 39.97           C  
ATOM   1573  O   VAL A 206      -4.954 -16.213  42.262  1.00 41.98           O  
ATOM   1574  CB  VAL A 206      -3.283 -16.578  39.790  1.00 43.03           C  
ATOM   1575  CG1 VAL A 206      -2.187 -16.049  38.875  1.00 41.59           C  
ATOM   1576  CG2 VAL A 206      -3.726 -17.973  39.362  1.00 42.00           C  
ATOM   1577  N   ASP A 207      -3.906 -18.124  42.796  1.00 40.10           N  
ATOM   1578  CA  ASP A 207      -4.957 -18.545  43.718  1.00 41.38           C  
ATOM   1579  C   ASP A 207      -4.649 -18.084  45.140  1.00 42.04           C  
ATOM   1580  O   ASP A 207      -5.445 -18.289  46.056  1.00 42.99           O  
ATOM   1581  CB  ASP A 207      -5.139 -20.063  43.685  1.00 41.63           C  
ATOM   1582  CG  ASP A 207      -3.982 -20.804  44.322  1.00 43.18           C  
ATOM   1583  OD1 ASP A 207      -2.847 -20.287  44.285  1.00 44.68           O  
ATOM   1584  OD2 ASP A 207      -4.207 -21.910  44.859  1.00 43.14           O  
ATOM   1585  N   GLY A 208      -3.487 -17.465  45.319  1.00 41.24           N  
ATOM   1586  CA  GLY A 208      -3.100 -16.931  46.611  1.00 40.57           C  
ATOM   1587  C   GLY A 208      -2.069 -17.775  47.334  1.00 40.22           C  
ATOM   1588  O   GLY A 208      -1.473 -17.327  48.312  1.00 42.01           O  
ATOM   1589  N   THR A 209      -1.860 -18.997  46.855  1.00 38.73           N  
ATOM   1590  CA  THR A 209      -0.909 -19.917  47.475  1.00 38.18           C  
ATOM   1591  C   THR A 209       0.506 -19.343  47.459  1.00 39.30           C  
ATOM   1592  O   THR A 209       0.929 -18.737  46.473  1.00 39.92           O  
ATOM   1593  CB  THR A 209      -0.906 -21.286  46.765  1.00 35.59           C  
ATOM   1594  OG1 THR A 209      -2.246 -21.781  46.671  1.00 35.86           O  
ATOM   1595  CG2 THR A 209      -0.054 -22.286  47.523  1.00 34.34           C  
ATOM   1596  N   LYS A 210       1.227 -19.531  48.561  1.00 38.42           N  
ATOM   1597  CA  LYS A 210       2.592 -19.038  48.681  1.00 36.80           C  
ATOM   1598  C   LYS A 210       3.582 -20.184  48.846  1.00 36.08           C  
ATOM   1599  O   LYS A 210       3.367 -21.102  49.637  1.00 36.48           O  
ATOM   1600  CB  LYS A 210       2.709 -18.066  49.856  1.00 37.88           C  
ATOM   1601  CG  LYS A 210       1.932 -16.770  49.666  1.00 39.20           C  
ATOM   1602  CD  LYS A 210       2.122 -15.828  50.846  1.00 40.56           C  
ATOM   1603  CE  LYS A 210       1.471 -14.479  50.584  1.00 41.06           C  
ATOM   1604  NZ  LYS A 210       1.688 -13.525  51.708  1.00 42.34           N  
ATOM   1605  N   TYR A 211       4.665 -20.127  48.082  1.00 35.83           N  
ATOM   1606  CA  TYR A 211       5.725 -21.120  48.170  1.00 34.98           C  
ATOM   1607  C   TYR A 211       7.021 -20.432  48.560  1.00 34.55           C  
ATOM   1608  O   TYR A 211       7.372 -19.399  47.996  1.00 34.63           O  
ATOM   1609  CB  TYR A 211       5.897 -21.864  46.844  1.00 34.09           C  
ATOM   1610  CG  TYR A 211       4.661 -22.589  46.363  1.00 34.43           C  
ATOM   1611  CD1 TYR A 211       3.695 -21.932  45.610  1.00 34.33           C  
ATOM   1612  CD2 TYR A 211       4.464 -23.935  46.653  1.00 34.60           C  
ATOM   1613  CE1 TYR A 211       2.566 -22.590  45.164  1.00 34.94           C  
ATOM   1614  CE2 TYR A 211       3.336 -24.603  46.211  1.00 34.98           C  
ATOM   1615  CZ  TYR A 211       2.391 -23.925  45.467  1.00 36.14           C  
ATOM   1616  OH  TYR A 211       1.266 -24.582  45.024  1.00 37.80           O  
ATOM   1617  N   TYR A 212       7.726 -21.004  49.529  1.00 33.65           N  
ATOM   1618  CA  TYR A 212       8.994 -20.445  49.978  1.00 32.35           C  
ATOM   1619  C   TYR A 212      10.145 -21.372  49.618  1.00 31.54           C  
ATOM   1620  O   TYR A 212      10.050 -22.588  49.788  1.00 30.72           O  
ATOM   1621  CB  TYR A 212       8.964 -20.186  51.487  1.00 32.43           C  
ATOM   1622  CG  TYR A 212       7.930 -19.164  51.891  1.00 33.97           C  
ATOM   1623  CD1 TYR A 212       8.236 -17.808  51.913  1.00 34.91           C  
ATOM   1624  CD2 TYR A 212       6.641 -19.552  52.236  1.00 34.83           C  
ATOM   1625  CE1 TYR A 212       7.290 -16.869  52.273  1.00 36.17           C  
ATOM   1626  CE2 TYR A 212       5.688 -18.620  52.597  1.00 36.02           C  
ATOM   1627  CZ  TYR A 212       6.018 -17.281  52.614  1.00 37.10           C  
ATOM   1628  OH  TYR A 212       5.069 -16.352  52.972  1.00 39.08           O  
ATOM   1629  N   ALA A 213      11.227 -20.789  49.110  1.00 31.52           N  
ATOM   1630  CA  ALA A 213      12.426 -21.551  48.777  1.00 31.89           C  
ATOM   1631  C   ALA A 213      13.663 -20.657  48.781  1.00 33.89           C  
ATOM   1632  O   ALA A 213      13.559 -19.432  48.852  1.00 34.10           O  
ATOM   1633  CB  ALA A 213      12.269 -22.225  47.429  1.00 29.78           C  
ATOM   1634  N   ASP A 214      14.833 -21.278  48.698  1.00 34.41           N  
ATOM   1635  CA  ASP A 214      16.082 -20.535  48.684  1.00 36.71           C  
ATOM   1636  C   ASP A 214      16.306 -19.856  47.340  1.00 37.23           C  
ATOM   1637  O   ASP A 214      16.844 -18.750  47.279  1.00 39.14           O  
ATOM   1638  CB  ASP A 214      17.254 -21.459  49.009  1.00 39.12           C  
ATOM   1639  CG  ASP A 214      17.060 -22.201  50.313  1.00 42.97           C  
ATOM   1640  OD1 ASP A 214      17.305 -21.600  51.381  1.00 46.48           O  
ATOM   1641  OD2 ASP A 214      16.660 -23.383  50.269  1.00 42.49           O  
ATOM   1642  N   LYS A 215      15.893 -20.520  46.264  1.00 35.21           N  
ATOM   1643  CA  LYS A 215      16.078 -19.988  44.918  1.00 33.71           C  
ATOM   1644  C   LYS A 215      14.894 -20.316  44.014  1.00 32.04           C  
ATOM   1645  O   LYS A 215      14.257 -21.360  44.159  1.00 31.13           O  
ATOM   1646  CB  LYS A 215      17.374 -20.525  44.304  1.00 33.60           C  
ATOM   1647  CG  LYS A 215      18.637 -19.996  44.964  1.00 34.85           C  
ATOM   1648  CD  LYS A 215      19.878 -20.734  44.501  1.00 35.05           C  
ATOM   1649  CE  LYS A 215      21.125 -20.082  45.076  1.00 37.34           C  
ATOM   1650  NZ  LYS A 215      22.358 -20.864  44.801  1.00 38.99           N  
ATOM   1651  N   VAL A 216      14.609 -19.411  43.083  1.00 31.91           N  
ATOM   1652  CA  VAL A 216      13.489 -19.566  42.164  1.00 31.15           C  
ATOM   1653  C   VAL A 216      13.953 -19.447  40.717  1.00 31.83           C  
ATOM   1654  O   VAL A 216      14.737 -18.558  40.381  1.00 32.45           O  
ATOM   1655  CB  VAL A 216      12.390 -18.517  42.434  1.00 30.56           C  
ATOM   1656  CG1 VAL A 216      11.335 -18.548  41.334  1.00 28.09           C  
ATOM   1657  CG2 VAL A 216      11.756 -18.746  43.800  1.00 30.10           C  
ATOM   1658  N   VAL A 217      13.470 -20.353  39.870  1.00 31.46           N  
ATOM   1659  CA  VAL A 217      13.799 -20.353  38.449  1.00 30.40           C  
ATOM   1660  C   VAL A 217      12.561 -20.062  37.599  1.00 29.52           C  
ATOM   1661  O   VAL A 217      11.547 -20.746  37.721  1.00 28.92           O  
ATOM   1662  CB  VAL A 217      14.407 -21.706  38.014  1.00 28.77           C  
ATOM   1663  CG1 VAL A 217      14.630 -21.733  36.509  1.00 26.51           C  
ATOM   1664  CG2 VAL A 217      15.707 -21.978  38.765  1.00 28.16           C  
ATOM   1665  N   LEU A 218      12.645 -19.044  36.744  1.00 30.16           N  
ATOM   1666  CA  LEU A 218      11.536 -18.696  35.856  1.00 30.33           C  
ATOM   1667  C   LEU A 218      11.772 -19.199  34.437  1.00 30.99           C  
ATOM   1668  O   LEU A 218      12.499 -18.579  33.663  1.00 31.25           O  
ATOM   1669  CB  LEU A 218      11.309 -17.182  35.826  1.00 30.50           C  
ATOM   1670  CG  LEU A 218      10.139 -16.730  34.942  1.00 30.28           C  
ATOM   1671  CD1 LEU A 218       8.805 -17.115  35.565  1.00 29.07           C  
ATOM   1672  CD2 LEU A 218      10.190 -15.238  34.661  1.00 31.44           C  
ATOM   1673  N   ALA A 219      11.152 -20.324  34.101  1.00 31.07           N  
ATOM   1674  CA  ALA A 219      11.243 -20.876  32.753  1.00 29.46           C  
ATOM   1675  C   ALA A 219       9.855 -20.945  32.127  1.00 28.16           C  
ATOM   1676  O   ALA A 219       9.359 -22.027  31.814  1.00 27.64           O  
ATOM   1677  CB  ALA A 219      11.889 -22.252  32.782  1.00 29.04           C  
ATOM   1678  N   ALA A 220       9.235 -19.782  31.952  1.00 28.04           N  
ATOM   1679  CA  ALA A 220       7.849 -19.709  31.500  1.00 28.22           C  
ATOM   1680  C   ALA A 220       7.739 -19.572  29.983  1.00 28.34           C  
ATOM   1681  O   ALA A 220       6.663 -19.282  29.457  1.00 29.02           O  
ATOM   1682  CB  ALA A 220       7.136 -18.552  32.185  1.00 28.14           C  
ATOM   1683  N   GLY A 221       8.852 -19.788  29.287  1.00 33.44           N  
ATOM   1684  CA  GLY A 221       8.879 -19.705  27.838  1.00 33.87           C  
ATOM   1685  C   GLY A 221       8.402 -18.371  27.294  1.00 35.22           C  
ATOM   1686  O   GLY A 221       8.956 -17.319  27.615  1.00 34.84           O  
ATOM   1687  N   ALA A 222       7.356 -18.421  26.475  1.00 35.72           N  
ATOM   1688  CA  ALA A 222       6.832 -17.230  25.817  1.00 35.73           C  
ATOM   1689  C   ALA A 222       5.945 -16.409  26.747  1.00 34.49           C  
ATOM   1690  O   ALA A 222       5.476 -15.331  26.379  1.00 34.49           O  
ATOM   1691  CB  ALA A 222       6.063 -17.620  24.560  1.00 35.47           C  
ATOM   1692  N   TRP A 223       5.717 -16.919  27.952  1.00 33.54           N  
ATOM   1693  CA  TRP A 223       4.893 -16.211  28.927  1.00 34.65           C  
ATOM   1694  C   TRP A 223       5.740 -15.383  29.886  1.00 35.89           C  
ATOM   1695  O   TRP A 223       5.217 -14.542  30.620  1.00 38.50           O  
ATOM   1696  CB  TRP A 223       4.029 -17.196  29.717  1.00 33.43           C  
ATOM   1697  CG  TRP A 223       2.869 -17.763  28.947  1.00 32.46           C  
ATOM   1698  CD1 TRP A 223       1.582 -17.307  28.953  1.00 31.79           C  
ATOM   1699  CD2 TRP A 223       2.887 -18.897  28.071  1.00 31.18           C  
ATOM   1700  NE1 TRP A 223       0.801 -18.082  28.137  1.00 30.60           N  
ATOM   1701  CE2 TRP A 223       1.576 -19.067  27.583  1.00 30.69           C  
ATOM   1702  CE3 TRP A 223       3.884 -19.785  27.652  1.00 30.85           C  
ATOM   1703  CZ2 TRP A 223       1.235 -20.089  26.695  1.00 30.78           C  
ATOM   1704  CZ3 TRP A 223       3.544 -20.799  26.770  1.00 30.03           C  
ATOM   1705  CH2 TRP A 223       2.231 -20.942  26.302  1.00 29.91           C  
ATOM   1706  N   SER A 224       7.048 -15.627  29.869  1.00 34.79           N  
ATOM   1707  CA  SER A 224       7.982 -14.999  30.802  1.00 34.72           C  
ATOM   1708  C   SER A 224       7.907 -13.474  30.799  1.00 36.55           C  
ATOM   1709  O   SER A 224       7.882 -12.846  31.857  1.00 39.18           O  
ATOM   1710  CB  SER A 224       9.413 -15.436  30.484  1.00 32.62           C  
ATOM   1711  OG  SER A 224       9.522 -16.847  30.469  1.00 31.14           O  
ATOM   1712  N   SER A 225       7.864 -12.884  29.609  1.00 36.18           N  
ATOM   1713  CA  SER A 225       7.872 -11.431  29.470  1.00 37.38           C  
ATOM   1714  C   SER A 225       6.547 -10.802  29.893  1.00 37.35           C  
ATOM   1715  O   SER A 225       6.438  -9.580  29.996  1.00 37.77           O  
ATOM   1716  CB  SER A 225       8.201 -11.039  28.028  1.00 37.87           C  
ATOM   1717  OG  SER A 225       7.271 -11.604  27.122  1.00 38.55           O  
ATOM   1718  N   THR A 226       5.544 -11.639  30.138  1.00 36.63           N  
ATOM   1719  CA  THR A 226       4.247 -11.154  30.590  1.00 38.93           C  
ATOM   1720  C   THR A 226       4.123 -11.299  32.104  1.00 40.27           C  
ATOM   1721  O   THR A 226       3.335 -10.601  32.741  1.00 41.48           O  
ATOM   1722  CB  THR A 226       3.086 -11.906  29.912  1.00 39.14           C  
ATOM   1723  OG1 THR A 226       2.889 -13.172  30.556  1.00 39.12           O  
ATOM   1724  CG2 THR A 226       3.384 -12.128  28.435  1.00 38.70           C  
ATOM   1725  N   LEU A 227       4.907 -12.208  32.674  1.00 39.49           N  
ATOM   1726  CA  LEU A 227       4.859 -12.465  34.110  1.00 40.12           C  
ATOM   1727  C   LEU A 227       5.758 -11.499  34.874  1.00 39.05           C  
ATOM   1728  O   LEU A 227       5.368 -10.955  35.909  1.00 39.97           O  
ATOM   1729  CB  LEU A 227       5.260 -13.911  34.407  1.00 39.93           C  
ATOM   1730  CG  LEU A 227       4.376 -14.984  33.770  1.00 39.37           C  
ATOM   1731  CD1 LEU A 227       4.873 -16.373  34.129  1.00 30.52           C  
ATOM   1732  CD2 LEU A 227       2.927 -14.800  34.195  1.00 32.76           C  
ATOM   1733  N   VAL A 228       6.967 -11.298  34.358  1.00 37.64           N  
ATOM   1734  CA  VAL A 228       7.910 -10.347  34.937  1.00 38.20           C  
ATOM   1735  C   VAL A 228       8.409  -9.369  33.868  1.00 39.29           C  
ATOM   1736  O   VAL A 228       8.346  -9.656  32.670  0.61 37.72           O  
ATOM   1737  CB  VAL A 228       9.111 -11.061  35.586  1.00 36.35           C  
ATOM   1738  CG1 VAL A 228       8.631 -12.131  36.565  1.00 35.32           C  
ATOM   1739  CG2 VAL A 228      10.004 -11.674  34.522  1.00 34.96           C  
ATOM   1740  N   ASP A 229       8.896  -8.213  34.308  1.00 41.35           N  
ATOM   1741  CA  ASP A 229       9.338  -7.157  33.401  1.00 42.44           C  
ATOM   1742  C   ASP A 229      10.725  -7.445  32.833  1.00 42.45           C  
ATOM   1743  O   ASP A 229      11.737  -7.230  33.501  1.00 43.33           O  
ATOM   1744  CB  ASP A 229       9.338  -5.806  34.125  1.00 44.80           C  
ATOM   1745  CG  ASP A 229       9.467  -4.627  33.174  1.00 46.45           C  
ATOM   1746  OD1 ASP A 229       9.559  -4.842  31.946  1.00 40.65           O  
ATOM   1747  OD2 ASP A 229       9.482  -3.478  33.663  1.00 48.15           O  
ATOM   1748  N   LEU A 230      10.769  -7.921  31.594  1.00 42.19           N  
ATOM   1749  CA  LEU A 230      12.037  -8.229  30.946  1.00 42.46           C  
ATOM   1750  C   LEU A 230      12.543  -7.041  30.136  1.00 45.75           C  
ATOM   1751  O   LEU A 230      13.568  -7.132  29.461  1.00 45.36           O  
ATOM   1752  CB  LEU A 230      11.898  -9.463  30.053  1.00 39.82           C  
ATOM   1753  CG  LEU A 230      11.559 -10.757  30.798  1.00 38.63           C  
ATOM   1754  CD1 LEU A 230      11.528 -11.948  29.850  1.00 36.30           C  
ATOM   1755  CD2 LEU A 230      12.547 -10.990  31.931  1.00 38.82           C  
ATOM   1756  N   GLU A 231      11.812  -5.932  30.217  1.00 49.18           N  
ATOM   1757  CA  GLU A 231      12.186  -4.678  29.564  1.00 52.32           C  
ATOM   1758  C   GLU A 231      12.454  -4.848  28.071  1.00 51.80           C  
ATOM   1759  O   GLU A 231      13.498  -4.431  27.566  1.00 52.94           O  
ATOM   1760  CB  GLU A 231      13.407  -4.069  30.253  1.00 55.17           C  
ATOM   1761  CG  GLU A 231      13.177  -3.759  31.721  1.00 58.25           C  
ATOM   1762  CD  GLU A 231      14.384  -3.130  32.381  1.00 61.99           C  
ATOM   1763  OE1 GLU A 231      15.335  -2.765  31.660  1.00 63.30           O  
ATOM   1764  OE2 GLU A 231      14.381  -3.002  33.624  1.00 64.01           O  
ATOM   1765  N   GLU A 232      11.502  -5.474  27.385  1.00 49.81           N  
ATOM   1766  CA  GLU A 232      11.526  -5.624  25.931  1.00 49.44           C  
ATOM   1767  C   GLU A 232      12.728  -6.421  25.421  1.00 46.88           C  
ATOM   1768  O   GLU A 232      13.097  -6.316  24.254  1.00 47.62           O  
ATOM   1769  CB  GLU A 232      11.486  -4.248  25.259  1.00 53.63           C  
ATOM   1770  CG  GLU A 232      10.284  -3.404  25.656  1.00 58.06           C  
ATOM   1771  CD  GLU A 232      10.280  -2.036  24.997  1.00 63.58           C  
ATOM   1772  OE1 GLU A 232      10.893  -1.888  23.917  1.00 64.94           O  
ATOM   1773  OE2 GLU A 232       9.665  -1.105  25.561  1.00 66.43           O  
ATOM   1774  N   GLN A 233      13.330  -7.223  26.292  1.00 45.30           N  
ATOM   1775  CA  GLN A 233      14.391  -8.132  25.872  1.00 43.53           C  
ATOM   1776  C   GLN A 233      13.819  -9.322  25.108  1.00 41.94           C  
ATOM   1777  O   GLN A 233      14.503  -9.928  24.287  1.00 42.22           O  
ATOM   1778  CB  GLN A 233      15.191  -8.633  27.073  1.00 42.62           C  
ATOM   1779  CG  GLN A 233      16.138  -7.612  27.667  1.00 44.11           C  
ATOM   1780  CD  GLN A 233      16.932  -8.176  28.830  1.00 44.50           C  
ATOM   1781  OE1 GLN A 233      18.022  -8.718  28.646  1.00 44.41           O  
ATOM   1782  NE2 GLN A 233      16.385  -8.057  30.035  1.00 43.96           N  
ATOM   1783  N   CYS A 234      12.564  -9.658  25.389  1.00 40.82           N  
ATOM   1784  CA  CYS A 234      11.930 -10.816  24.769  1.00 39.69           C  
ATOM   1785  C   CYS A 234      10.579 -10.474  24.151  1.00 40.11           C  
ATOM   1786  O   CYS A 234       9.695  -9.943  24.821  1.00 42.70           O  
ATOM   1787  CB  CYS A 234      11.763 -11.942  25.794  1.00 38.63           C  
ATOM   1788  SG  CYS A 234      13.311 -12.634  26.412  1.00 35.70           S  
ATOM   1789  N   VAL A 235      10.428 -10.780  22.867  1.00 38.38           N  
ATOM   1790  CA  VAL A 235       9.153 -10.604  22.182  1.00 37.41           C  
ATOM   1791  C   VAL A 235       8.608 -11.959  21.743  1.00 35.63           C  
ATOM   1792  O   VAL A 235       9.221 -12.660  20.936  1.00 36.23           O  
ATOM   1793  CB  VAL A 235       9.278  -9.675  20.960  1.00 38.03           C  
ATOM   1794  CG1 VAL A 235       7.939  -9.551  20.250  1.00 38.72           C  
ATOM   1795  CG2 VAL A 235       9.783  -8.306  21.385  1.00 37.89           C  
ATOM   1796  N   SER A 236       7.454 -12.324  22.291  1.00 34.13           N  
ATOM   1797  CA  SER A 236       6.837 -13.610  22.001  1.00 32.14           C  
ATOM   1798  C   SER A 236       6.156 -13.616  20.636  1.00 32.82           C  
ATOM   1799  O   SER A 236       5.437 -12.681  20.284  1.00 34.37           O  
ATOM   1800  CB  SER A 236       5.833 -13.973  23.097  1.00 31.90           C  
ATOM   1801  OG  SER A 236       6.500 -14.272  24.311  1.00 31.79           O  
ATOM   1802  N   LYS A 237       6.392 -14.676  19.868  1.00 31.36           N  
ATOM   1803  CA  LYS A 237       5.835 -14.796  18.524  1.00 31.81           C  
ATOM   1804  C   LYS A 237       5.272 -16.191  18.275  1.00 31.69           C  
ATOM   1805  O   LYS A 237       5.707 -17.163  18.893  1.00 31.74           O  
ATOM   1806  CB  LYS A 237       6.894 -14.476  17.467  1.00 31.34           C  
ATOM   1807  CG  LYS A 237       7.445 -13.068  17.546  1.00 31.61           C  
ATOM   1808  CD  LYS A 237       8.778 -12.958  16.827  1.00 30.08           C  
ATOM   1809  CE  LYS A 237       9.405 -11.599  17.075  1.00 30.91           C  
ATOM   1810  NZ  LYS A 237      10.829 -11.564  16.655  1.00 30.95           N  
ATOM   1811  N   ALA A 238       4.311 -16.285  17.362  1.00 31.45           N  
ATOM   1812  CA  ALA A 238       3.705 -17.569  17.029  1.00 31.12           C  
ATOM   1813  C   ALA A 238       4.049 -18.015  15.611  1.00 31.94           C  
ATOM   1814  O   ALA A 238       3.940 -17.243  14.655  1.00 32.25           O  
ATOM   1815  CB  ALA A 238       2.196 -17.505  17.202  1.00 30.82           C  
ATOM   1816  N   TRP A 239       4.475 -19.267  15.487  1.00 31.24           N  
ATOM   1817  CA  TRP A 239       4.650 -19.889  14.182  1.00 31.38           C  
ATOM   1818  C   TRP A 239       3.556 -20.927  13.982  1.00 33.26           C  
ATOM   1819  O   TRP A 239       2.858 -21.295  14.927  1.00 34.75           O  
ATOM   1820  CB  TRP A 239       6.038 -20.519  14.051  1.00 29.39           C  
ATOM   1821  CG  TRP A 239       7.113 -19.510  13.780  1.00 30.06           C  
ATOM   1822  CD1 TRP A 239       7.643 -19.185  12.566  1.00 30.45           C  
ATOM   1823  CD2 TRP A 239       7.776 -18.681  14.742  1.00 32.00           C  
ATOM   1824  NE1 TRP A 239       8.598 -18.209  12.710  1.00 31.80           N  
ATOM   1825  CE2 TRP A 239       8.700 -17.883  14.035  1.00 33.24           C  
ATOM   1826  CE3 TRP A 239       7.681 -18.538  16.129  1.00 32.90           C  
ATOM   1827  CZ2 TRP A 239       9.522 -16.955  14.671  1.00 34.59           C  
ATOM   1828  CZ3 TRP A 239       8.503 -17.616  16.759  1.00 34.25           C  
ATOM   1829  CH2 TRP A 239       9.411 -16.838  16.030  1.00 34.83           C  
ATOM   1830  N   VAL A 240       3.406 -21.396  12.749  1.00 34.08           N  
ATOM   1831  CA  VAL A 240       2.274 -22.241  12.395  1.00 33.94           C  
ATOM   1832  C   VAL A 240       2.695 -23.579  11.797  1.00 35.05           C  
ATOM   1833  O   VAL A 240       3.767 -23.705  11.201  1.00 35.11           O  
ATOM   1834  CB  VAL A 240       1.353 -21.525  11.394  1.00 32.88           C  
ATOM   1835  CG1 VAL A 240       0.860 -20.219  11.979  1.00 32.69           C  
ATOM   1836  CG2 VAL A 240       2.089 -21.273  10.087  1.00 32.54           C  
ATOM   1837  N   PHE A 241       1.840 -24.580  11.967  1.00 35.73           N  
ATOM   1838  CA  PHE A 241       2.041 -25.866  11.321  1.00 35.65           C  
ATOM   1839  C   PHE A 241       0.703 -26.540  11.050  1.00 33.77           C  
ATOM   1840  O   PHE A 241      -0.317 -26.182  11.637  1.00 34.54           O  
ATOM   1841  CB  PHE A 241       2.944 -26.773  12.168  1.00 37.89           C  
ATOM   1842  CG  PHE A 241       2.418 -27.051  13.551  1.00 39.96           C  
ATOM   1843  CD1 PHE A 241       1.533 -28.093  13.776  1.00 41.14           C  
ATOM   1844  CD2 PHE A 241       2.830 -26.286  14.630  1.00 41.47           C  
ATOM   1845  CE1 PHE A 241       1.054 -28.354  15.047  1.00 41.93           C  
ATOM   1846  CE2 PHE A 241       2.356 -26.545  15.904  1.00 42.10           C  
ATOM   1847  CZ  PHE A 241       1.467 -27.580  16.112  1.00 41.89           C  
ATOM   1848  N   ALA A 242       0.715 -27.510  10.145  1.00 32.55           N  
ATOM   1849  CA  ALA A 242      -0.476 -28.289   9.846  1.00 33.58           C  
ATOM   1850  C   ALA A 242      -0.106 -29.761   9.702  1.00 32.92           C  
ATOM   1851  O   ALA A 242       1.073 -30.110   9.662  1.00 30.37           O  
ATOM   1852  CB  ALA A 242      -1.152 -27.775   8.583  1.00 33.92           C  
ATOM   1853  N   HIS A 243      -1.115 -30.621   9.627  1.00 35.31           N  
ATOM   1854  CA  HIS A 243      -0.876 -32.052   9.506  1.00 36.11           C  
ATOM   1855  C   HIS A 243      -1.614 -32.653   8.317  1.00 35.30           C  
ATOM   1856  O   HIS A 243      -2.709 -32.213   7.963  1.00 35.83           O  
ATOM   1857  CB  HIS A 243      -1.295 -32.774  10.789  1.00 38.81           C  
ATOM   1858  CG  HIS A 243      -0.569 -32.307  12.011  1.00 41.83           C  
ATOM   1859  ND1 HIS A 243       0.409 -33.057  12.627  1.00 43.78           N  
ATOM   1860  CD2 HIS A 243      -0.678 -31.166  12.733  1.00 43.97           C  
ATOM   1861  CE1 HIS A 243       0.872 -32.399  13.675  1.00 44.26           C  
ATOM   1862  NE2 HIS A 243       0.229 -31.249  13.761  1.00 45.25           N  
ATOM   1863  N   ILE A 244      -0.998 -33.656   7.700  1.00 33.38           N  
ATOM   1864  CA  ILE A 244      -1.674 -34.481   6.708  1.00 33.00           C  
ATOM   1865  C   ILE A 244      -1.455 -35.941   7.073  1.00 35.67           C  
ATOM   1866  O   ILE A 244      -0.414 -36.297   7.631  1.00 34.53           O  
ATOM   1867  CB  ILE A 244      -1.174 -34.210   5.276  1.00 29.78           C  
ATOM   1868  CG1 ILE A 244       0.348 -34.332   5.196  1.00 27.96           C  
ATOM   1869  CG2 ILE A 244      -1.613 -32.834   4.810  1.00 28.84           C  
ATOM   1870  CD1 ILE A 244       0.894 -34.173   3.791  1.00 26.99           C  
ATOM   1871  N   GLN A 245      -2.439 -36.782   6.775  1.00 38.81           N  
ATOM   1872  CA  GLN A 245      -2.340 -38.196   7.111  1.00 40.51           C  
ATOM   1873  C   GLN A 245      -2.192 -39.059   5.866  1.00 38.84           C  
ATOM   1874  O   GLN A 245      -2.952 -38.921   4.906  1.00 38.72           O  
ATOM   1875  CB  GLN A 245      -3.558 -38.652   7.917  1.00 43.09           C  
ATOM   1876  CG  GLN A 245      -3.483 -40.110   8.333  1.00 46.57           C  
ATOM   1877  CD  GLN A 245      -4.221 -40.388   9.623  1.00 52.60           C  
ATOM   1878  OE1 GLN A 245      -3.753 -41.155  10.466  1.00 54.11           O  
ATOM   1879  NE2 GLN A 245      -5.383 -39.767   9.786  1.00 55.98           N  
ATOM   1880  N   LEU A 246      -1.204 -39.948   5.893  1.00 36.20           N  
ATOM   1881  CA  LEU A 246      -0.979 -40.873   4.792  1.00 35.19           C  
ATOM   1882  C   LEU A 246      -1.384 -42.286   5.192  1.00 35.50           C  
ATOM   1883  O   LEU A 246      -1.310 -42.652   6.366  1.00 38.24           O  
ATOM   1884  CB  LEU A 246       0.491 -40.857   4.358  1.00 34.32           C  
ATOM   1885  CG  LEU A 246       1.179 -39.510   4.109  1.00 33.64           C  
ATOM   1886  CD1 LEU A 246       2.531 -39.725   3.447  1.00 32.27           C  
ATOM   1887  CD2 LEU A 246       0.311 -38.582   3.276  1.00 35.26           C  
ATOM   1888  N   THR A 247      -1.819 -43.074   4.216  1.00 33.36           N  
ATOM   1889  CA  THR A 247      -2.029 -44.498   4.431  1.00 34.67           C  
ATOM   1890  C   THR A 247      -0.662 -45.161   4.562  1.00 35.62           C  
ATOM   1891  O   THR A 247       0.341 -44.588   4.127  1.00 35.79           O  
ATOM   1892  CB  THR A 247      -2.820 -45.140   3.276  1.00 36.16           C  
ATOM   1893  OG1 THR A 247      -2.051 -45.058   2.069  1.00 38.53           O  
ATOM   1894  CG2 THR A 247      -4.149 -44.432   3.083  1.00 35.04           C  
ATOM   1895  N   PRO A 248      -0.608 -46.355   5.179  1.00 35.72           N  
ATOM   1896  CA  PRO A 248       0.660 -47.087   5.297  1.00 35.54           C  
ATOM   1897  C   PRO A 248       1.361 -47.286   3.952  1.00 37.45           C  
ATOM   1898  O   PRO A 248       2.589 -47.236   3.895  1.00 38.62           O  
ATOM   1899  CB  PRO A 248       0.229 -48.428   5.895  1.00 36.25           C  
ATOM   1900  CG  PRO A 248      -0.981 -48.097   6.694  1.00 35.87           C  
ATOM   1901  CD  PRO A 248      -1.693 -47.015   5.931  1.00 35.59           C  
ATOM   1902  N   ALA A 249       0.589 -47.493   2.889  1.00 37.95           N  
ATOM   1903  CA  ALA A 249       1.151 -47.654   1.552  1.00 38.98           C  
ATOM   1904  C   ALA A 249       1.720 -46.339   1.027  1.00 40.25           C  
ATOM   1905  O   ALA A 249       2.741 -46.324   0.337  1.00 41.60           O  
ATOM   1906  CB  ALA A 249       0.102 -48.190   0.601  1.00 39.97           C  
ATOM   1907  N   GLU A 250       1.048 -45.237   1.346  1.00 39.35           N  
ATOM   1908  CA  GLU A 250       1.521 -43.911   0.965  1.00 37.79           C  
ATOM   1909  C   GLU A 250       2.769 -43.520   1.757  1.00 37.75           C  
ATOM   1910  O   GLU A 250       3.714 -42.946   1.212  1.00 38.88           O  
ATOM   1911  CB  GLU A 250       0.422 -42.868   1.178  1.00 37.52           C  
ATOM   1912  CG  GLU A 250      -0.683 -42.893   0.137  1.00 39.26           C  
ATOM   1913  CD  GLU A 250      -1.877 -42.046   0.534  1.00 40.27           C  
ATOM   1914  OE1 GLU A 250      -2.085 -41.840   1.747  1.00 40.74           O  
ATOM   1915  OE2 GLU A 250      -2.608 -41.584  -0.368  1.00 41.42           O  
ATOM   1916  N   ALA A 251       2.763 -43.837   3.048  1.00 35.89           N  
ATOM   1917  CA  ALA A 251       3.846 -43.447   3.941  1.00 35.19           C  
ATOM   1918  C   ALA A 251       5.103 -44.291   3.741  1.00 36.56           C  
ATOM   1919  O   ALA A 251       6.170 -43.956   4.256  1.00 37.37           O  
ATOM   1920  CB  ALA A 251       3.380 -43.535   5.389  1.00 34.69           C  
ATOM   1921  N   ALA A 252       4.972 -45.386   2.999  1.00 36.22           N  
ATOM   1922  CA  ALA A 252       6.073 -46.327   2.822  1.00 36.09           C  
ATOM   1923  C   ALA A 252       7.284 -45.690   2.142  1.00 37.19           C  
ATOM   1924  O   ALA A 252       8.425 -45.946   2.525  1.00 37.50           O  
ATOM   1925  CB  ALA A 252       5.603 -47.536   2.030  1.00 36.34           C  
ATOM   1926  N   ALA A 253       7.037 -44.848   1.145  1.00 37.97           N  
ATOM   1927  CA  ALA A 253       8.123 -44.246   0.378  1.00 38.72           C  
ATOM   1928  C   ALA A 253       8.871 -43.163   1.158  1.00 39.01           C  
ATOM   1929  O   ALA A 253       9.804 -42.553   0.636  1.00 39.90           O  
ATOM   1930  CB  ALA A 253       7.586 -43.672  -0.924  1.00 38.01           C  
ATOM   1931  N   TYR A 254       8.469 -42.930   2.404  1.00 36.96           N  
ATOM   1932  CA  TYR A 254       9.076 -41.879   3.213  1.00 36.04           C  
ATOM   1933  C   TYR A 254       9.695 -42.412   4.505  1.00 36.06           C  
ATOM   1934  O   TYR A 254      10.114 -41.636   5.364  1.00 35.20           O  
ATOM   1935  CB  TYR A 254       8.040 -40.801   3.540  1.00 36.24           C  
ATOM   1936  CG  TYR A 254       7.548 -40.045   2.329  1.00 37.53           C  
ATOM   1937  CD1 TYR A 254       6.498 -40.532   1.562  1.00 39.26           C  
ATOM   1938  CD2 TYR A 254       8.137 -38.847   1.948  1.00 37.44           C  
ATOM   1939  CE1 TYR A 254       6.047 -39.845   0.449  1.00 39.90           C  
ATOM   1940  CE2 TYR A 254       7.694 -38.155   0.838  1.00 37.74           C  
ATOM   1941  CZ  TYR A 254       6.648 -38.658   0.093  1.00 39.23           C  
ATOM   1942  OH  TYR A 254       6.204 -37.973  -1.014  1.00 40.48           O  
ATOM   1943  N   LYS A 255       9.753 -43.734   4.638  1.00 36.35           N  
ATOM   1944  CA  LYS A 255      10.353 -44.351   5.815  1.00 37.05           C  
ATOM   1945  C   LYS A 255      11.823 -43.956   5.935  1.00 37.78           C  
ATOM   1946  O   LYS A 255      12.591 -44.104   4.983  1.00 38.84           O  
ATOM   1947  CB  LYS A 255      10.212 -45.872   5.755  1.00 39.69           C  
ATOM   1948  CG  LYS A 255      10.793 -46.604   6.954  1.00 41.79           C  
ATOM   1949  CD  LYS A 255      10.099 -46.196   8.241  1.00 43.08           C  
ATOM   1950  CE  LYS A 255      10.687 -46.923   9.440  1.00 45.10           C  
ATOM   1951  NZ  LYS A 255      10.082 -46.459  10.719  1.00 45.31           N  
ATOM   1952  N   ASN A 256      12.197 -43.443   7.106  1.00 36.68           N  
ATOM   1953  CA  ASN A 256      13.562 -42.995   7.385  1.00 37.77           C  
ATOM   1954  C   ASN A 256      14.062 -41.928   6.408  1.00 39.64           C  
ATOM   1955  O   ASN A 256      15.242 -41.889   6.061  1.00 42.03           O  
ATOM   1956  CB  ASN A 256      14.520 -44.188   7.387  1.00 38.48           C  
ATOM   1957  CG  ASN A 256      14.101 -45.266   8.365  1.00 39.63           C  
ATOM   1958  OD1 ASN A 256      13.439 -44.990   9.368  1.00 40.54           O  
ATOM   1959  ND2 ASN A 256      14.481 -46.505   8.077  1.00 40.11           N  
ATOM   1960  N   THR A 257      13.153 -41.058   5.980  1.00 39.54           N  
ATOM   1961  CA  THR A 257      13.472 -39.961   5.070  1.00 39.35           C  
ATOM   1962  C   THR A 257      14.077 -38.770   5.813  1.00 39.07           C  
ATOM   1963  O   THR A 257      13.598 -38.403   6.888  1.00 39.52           O  
ATOM   1964  CB  THR A 257      12.208 -39.510   4.307  1.00 39.56           C  
ATOM   1965  OG1 THR A 257      11.952 -40.425   3.236  1.00 42.17           O  
ATOM   1966  CG2 THR A 257      12.363 -38.108   3.742  1.00 37.96           C  
ATOM   1967  N   PRO A 258      15.137 -38.167   5.247  1.00 38.35           N  
ATOM   1968  CA  PRO A 258      15.760 -36.986   5.857  1.00 37.15           C  
ATOM   1969  C   PRO A 258      14.795 -35.809   5.950  1.00 35.98           C  
ATOM   1970  O   PRO A 258      13.919 -35.673   5.097  1.00 35.96           O  
ATOM   1971  CB  PRO A 258      16.912 -36.654   4.900  1.00 37.69           C  
ATOM   1972  CG  PRO A 258      17.153 -37.897   4.127  1.00 39.71           C  
ATOM   1973  CD  PRO A 258      15.825 -38.573   4.009  1.00 39.67           C  
ATOM   1974  N   VAL A 259      14.952 -34.978   6.976  1.00 34.35           N  
ATOM   1975  CA  VAL A 259      14.193 -33.737   7.057  1.00 33.59           C  
ATOM   1976  C   VAL A 259      14.488 -32.882   5.832  1.00 34.07           C  
ATOM   1977  O   VAL A 259      15.644 -32.578   5.543  1.00 34.70           O  
ATOM   1978  CB  VAL A 259      14.524 -32.931   8.326  1.00 31.91           C  
ATOM   1979  CG1 VAL A 259      13.872 -31.560   8.261  1.00 29.84           C  
ATOM   1980  CG2 VAL A 259      14.078 -33.685   9.572  1.00 31.20           C  
ATOM   1981  N   ILE A 260      13.441 -32.509   5.106  1.00 33.18           N  
ATOM   1982  CA  ILE A 260      13.603 -31.689   3.913  1.00 33.60           C  
ATOM   1983  C   ILE A 260      13.301 -30.234   4.227  1.00 34.41           C  
ATOM   1984  O   ILE A 260      12.237 -29.919   4.755  1.00 33.41           O  
ATOM   1985  CB  ILE A 260      12.685 -32.158   2.774  1.00 33.00           C  
ATOM   1986  CG1 ILE A 260      12.846 -33.662   2.539  1.00 32.30           C  
ATOM   1987  CG2 ILE A 260      12.964 -31.361   1.508  1.00 33.57           C  
ATOM   1988  CD1 ILE A 260      14.251 -34.077   2.190  1.00 32.85           C  
ATOM   1989  N   TYR A 261      14.235 -29.348   3.897  1.00 36.47           N  
ATOM   1990  CA  TYR A 261      14.061 -27.930   4.187  1.00 38.13           C  
ATOM   1991  C   TYR A 261      14.408 -27.042   2.993  1.00 39.07           C  
ATOM   1992  O   TYR A 261      15.396 -27.271   2.296  1.00 40.45           O  
ATOM   1993  CB  TYR A 261      14.911 -27.529   5.396  1.00 39.44           C  
ATOM   1994  CG  TYR A 261      14.862 -26.053   5.722  1.00 41.42           C  
ATOM   1995  CD1 TYR A 261      13.800 -25.514   6.436  1.00 42.30           C  
ATOM   1996  CD2 TYR A 261      15.879 -25.199   5.317  1.00 43.31           C  
ATOM   1997  CE1 TYR A 261      13.751 -24.166   6.736  1.00 43.84           C  
ATOM   1998  CE2 TYR A 261      15.839 -23.850   5.611  1.00 44.99           C  
ATOM   1999  CZ  TYR A 261      14.774 -23.340   6.321  1.00 45.78           C  
ATOM   2000  OH  TYR A 261      14.731 -21.996   6.616  1.00 48.21           O  
ATOM   2001  N   ASP A 262      13.572 -26.034   2.761  1.00 37.85           N  
ATOM   2002  CA  ASP A 262      13.854 -24.991   1.783  1.00 38.43           C  
ATOM   2003  C   ASP A 262      13.469 -23.648   2.390  1.00 38.83           C  
ATOM   2004  O   ASP A 262      12.333 -23.461   2.829  1.00 37.89           O  
ATOM   2005  CB  ASP A 262      13.095 -25.239   0.475  1.00 39.55           C  
ATOM   2006  CG  ASP A 262      13.546 -24.317  -0.654  1.00 41.88           C  
ATOM   2007  OD1 ASP A 262      13.729 -23.104  -0.415  1.00 42.46           O  
ATOM   2008  OD2 ASP A 262      13.722 -24.813  -1.790  1.00 42.50           O  
ATOM   2009  N   GLY A 263      14.419 -22.718   2.411  1.00 40.69           N  
ATOM   2010  CA  GLY A 263      14.219 -21.420   3.034  1.00 40.56           C  
ATOM   2011  C   GLY A 263      13.088 -20.587   2.454  1.00 40.79           C  
ATOM   2012  O   GLY A 263      12.528 -19.731   3.139  1.00 40.84           O  
ATOM   2013  N   ASP A 264      12.747 -20.834   1.194  1.00 41.40           N  
ATOM   2014  CA  ASP A 264      11.696 -20.069   0.531  1.00 43.58           C  
ATOM   2015  C   ASP A 264      10.326 -20.741   0.613  1.00 43.25           C  
ATOM   2016  O   ASP A 264       9.385 -20.302  -0.048  1.00 44.83           O  
ATOM   2017  CB  ASP A 264      12.057 -19.828  -0.939  1.00 46.22           C  
ATOM   2018  CG  ASP A 264      13.247 -18.902  -1.106  1.00 49.40           C  
ATOM   2019  OD1 ASP A 264      13.567 -18.162  -0.153  1.00 50.81           O  
ATOM   2020  OD2 ASP A 264      13.857 -18.908  -2.195  1.00 50.90           O  
ATOM   2021  N   TYR A 265      10.212 -21.800   1.413  1.00 40.48           N  
ATOM   2022  CA  TYR A 265       8.954 -22.543   1.505  1.00 38.36           C  
ATOM   2023  C   TYR A 265       8.642 -23.054   2.912  1.00 36.57           C  
ATOM   2024  O   TYR A 265       7.515 -22.925   3.390  1.00 36.07           O  
ATOM   2025  CB  TYR A 265       8.964 -23.722   0.527  1.00 37.98           C  
ATOM   2026  CG  TYR A 265       9.004 -23.311  -0.930  1.00 39.03           C  
ATOM   2027  CD1 TYR A 265       7.858 -22.874  -1.581  1.00 39.58           C  
ATOM   2028  CD2 TYR A 265      10.190 -23.357  -1.651  1.00 39.01           C  
ATOM   2029  CE1 TYR A 265       7.891 -22.493  -2.908  1.00 40.56           C  
ATOM   2030  CE2 TYR A 265      10.233 -22.981  -2.977  1.00 40.04           C  
ATOM   2031  CZ  TYR A 265       9.080 -22.550  -3.603  1.00 40.72           C  
ATOM   2032  OH  TYR A 265       9.118 -22.176  -4.927  1.00 41.95           O  
ATOM   2033  N   GLY A 266       9.636 -23.640   3.571  1.00 35.50           N  
ATOM   2034  CA  GLY A 266       9.427 -24.245   4.875  1.00 33.11           C  
ATOM   2035  C   GLY A 266      10.028 -25.636   4.931  1.00 31.92           C  
ATOM   2036  O   GLY A 266      11.083 -25.876   4.347  1.00 32.23           O  
ATOM   2037  N   PHE A 267       9.363 -26.559   5.622  1.00 30.78           N  
ATOM   2038  CA  PHE A 267       9.878 -27.919   5.739  1.00 31.07           C  
ATOM   2039  C   PHE A 267       8.798 -28.942   6.077  1.00 30.01           C  
ATOM   2040  O   PHE A 267       7.675 -28.581   6.425  1.00 31.35           O  
ATOM   2041  CB  PHE A 267      10.989 -27.976   6.796  1.00 33.91           C  
ATOM   2042  CG  PHE A 267      10.555 -27.554   8.179  1.00 34.90           C  
ATOM   2043  CD1 PHE A 267      10.005 -28.472   9.063  1.00 34.98           C  
ATOM   2044  CD2 PHE A 267      10.730 -26.247   8.605  1.00 35.97           C  
ATOM   2045  CE1 PHE A 267       9.618 -28.088  10.339  1.00 35.31           C  
ATOM   2046  CE2 PHE A 267      10.346 -25.858   9.878  1.00 36.62           C  
ATOM   2047  CZ  PHE A 267       9.793 -26.781  10.748  1.00 35.39           C  
ATOM   2048  N   PHE A 268       9.146 -30.221   5.961  1.00 27.60           N  
ATOM   2049  CA  PHE A 268       8.287 -31.288   6.464  1.00 27.59           C  
ATOM   2050  C   PHE A 268       9.133 -32.400   7.076  1.00 29.24           C  
ATOM   2051  O   PHE A 268      10.337 -32.481   6.841  1.00 30.46           O  
ATOM   2052  CB  PHE A 268       7.380 -31.842   5.358  1.00 26.63           C  
ATOM   2053  CG  PHE A 268       8.058 -32.820   4.438  1.00 26.03           C  
ATOM   2054  CD1 PHE A 268       8.769 -32.376   3.338  1.00 26.14           C  
ATOM   2055  CD2 PHE A 268       7.959 -34.186   4.660  1.00 26.32           C  
ATOM   2056  CE1 PHE A 268       9.383 -33.272   2.483  1.00 27.13           C  
ATOM   2057  CE2 PHE A 268       8.575 -35.088   3.812  1.00 26.61           C  
ATOM   2058  CZ  PHE A 268       9.288 -34.630   2.721  1.00 26.88           C  
ATOM   2059  N   ILE A 269       8.492 -33.246   7.872  1.00 29.92           N  
ATOM   2060  CA  ILE A 269       9.168 -34.355   8.531  1.00 31.16           C  
ATOM   2061  C   ILE A 269       8.492 -35.661   8.113  1.00 31.48           C  
ATOM   2062  O   ILE A 269       7.308 -35.661   7.779  1.00 31.21           O  
ATOM   2063  CB  ILE A 269       9.144 -34.184  10.074  1.00 37.69           C  
ATOM   2064  CG1 ILE A 269       9.691 -32.805  10.458  1.00 36.88           C  
ATOM   2065  CG2 ILE A 269       9.937 -35.282  10.769  1.00 38.13           C  
ATOM   2066  CD1 ILE A 269       9.864 -32.595  11.948  1.00 35.80           C  
ATOM   2067  N   GLU A 270       9.245 -36.760   8.106  1.00 32.85           N  
ATOM   2068  CA  GLU A 270       8.697 -38.070   7.750  1.00 35.59           C  
ATOM   2069  C   GLU A 270       7.497 -38.424   8.625  1.00 36.69           C  
ATOM   2070  O   GLU A 270       7.431 -38.011   9.784  1.00 36.64           O  
ATOM   2071  CB  GLU A 270       9.769 -39.160   7.873  1.00 36.47           C  
ATOM   2072  CG  GLU A 270      10.243 -39.425   9.297  1.00 37.48           C  
ATOM   2073  CD  GLU A 270      10.924 -40.774   9.439  1.00 39.55           C  
ATOM   2074  OE1 GLU A 270      10.483 -41.734   8.772  1.00 40.21           O  
ATOM   2075  OE2 GLU A 270      11.900 -40.876  10.214  1.00 40.75           O  
ATOM   2076  N   PRO A 271       6.535 -39.178   8.064  1.00 37.47           N  
ATOM   2077  CA  PRO A 271       5.351 -39.617   8.812  1.00 38.70           C  
ATOM   2078  C   PRO A 271       5.712 -40.438  10.048  1.00 40.29           C  
ATOM   2079  O   PRO A 271       6.631 -41.261   9.995  1.00 40.72           O  
ATOM   2080  CB  PRO A 271       4.581 -40.468   7.793  1.00 38.84           C  
ATOM   2081  CG  PRO A 271       5.577 -40.816   6.735  1.00 38.75           C  
ATOM   2082  CD  PRO A 271       6.507 -39.648   6.669  1.00 37.90           C  
ATOM   2083  N   ASP A 272       4.995 -40.207  11.145  1.00 40.00           N  
ATOM   2084  CA  ASP A 272       5.254 -40.913  12.395  1.00 42.13           C  
ATOM   2085  C   ASP A 272       4.588 -42.287  12.398  1.00 43.90           C  
ATOM   2086  O   ASP A 272       4.252 -42.821  11.342  1.00 43.10           O  
ATOM   2087  CB  ASP A 272       4.779 -40.082  13.594  1.00 42.35           C  
ATOM   2088  CG  ASP A 272       3.266 -39.945  13.656  1.00 43.92           C  
ATOM   2089  OD1 ASP A 272       2.597 -40.126  12.617  1.00 44.42           O  
ATOM   2090  OD2 ASP A 272       2.743 -39.650  14.752  1.00 45.25           O  
ATOM   2091  N   GLU A 273       4.391 -42.845  13.591  1.00 46.82           N  
ATOM   2092  CA  GLU A 273       3.822 -44.183  13.745  1.00 48.94           C  
ATOM   2093  C   GLU A 273       2.427 -44.296  13.138  1.00 47.87           C  
ATOM   2094  O   GLU A 273       1.993 -45.383  12.760  1.00 49.22           O  
ATOM   2095  CB  GLU A 273       3.755 -44.580  15.225  1.00 52.17           C  
ATOM   2096  CG  GLU A 273       5.038 -44.363  16.006  1.00 54.01           C  
ATOM   2097  CD  GLU A 273       5.093 -43.001  16.675  1.00 54.96           C  
ATOM   2098  OE1 GLU A 273       6.053 -42.247  16.409  1.00 55.42           O  
ATOM   2099  OE2 GLU A 273       4.182 -42.688  17.472  1.00 54.70           O  
ATOM   2100  N   ASN A 274       1.730 -43.169  13.050  1.00 45.21           N  
ATOM   2101  CA  ASN A 274       0.346 -43.165  12.597  1.00 44.25           C  
ATOM   2102  C   ASN A 274       0.178 -42.529  11.215  1.00 42.85           C  
ATOM   2103  O   ASN A 274      -0.934 -42.187  10.810  1.00 42.55           O  
ATOM   2104  CB  ASN A 274      -0.528 -42.445  13.626  1.00 44.50           C  
ATOM   2105  CG  ASN A 274      -0.306 -42.962  15.042  1.00 46.14           C  
ATOM   2106  OD1 ASN A 274      -0.307 -44.169  15.284  1.00 47.25           O  
ATOM   2107  ND2 ASN A 274      -0.098 -42.045  15.982  1.00 45.95           N  
ATOM   2108  N   GLY A 275       1.288 -42.377  10.497  1.00 41.81           N  
ATOM   2109  CA  GLY A 275       1.271 -41.859   9.139  1.00 40.70           C  
ATOM   2110  C   GLY A 275       1.023 -40.366   9.043  1.00 40.71           C  
ATOM   2111  O   GLY A 275       0.551 -39.870   8.018  1.00 41.16           O  
ATOM   2112  N   ILE A 276       1.347 -39.644  10.110  1.00 39.89           N  
ATOM   2113  CA  ILE A 276       1.103 -38.209  10.165  1.00 38.66           C  
ATOM   2114  C   ILE A 276       2.335 -37.408   9.766  1.00 36.87           C  
ATOM   2115  O   ILE A 276       3.406 -37.573  10.347  1.00 37.65           O  
ATOM   2116  CB  ILE A 276       0.665 -37.767  11.572  1.00 39.54           C  
ATOM   2117  CG1 ILE A 276      -0.559 -38.565  12.026  1.00 39.29           C  
ATOM   2118  CG2 ILE A 276       0.387 -36.271  11.597  1.00 39.33           C  
ATOM   2119  CD1 ILE A 276      -1.755 -38.406  11.122  1.00 39.90           C  
ATOM   2120  N   ILE A 277       2.171 -36.538   8.773  1.00 35.21           N  
ATOM   2121  CA  ILE A 277       3.230 -35.621   8.356  1.00 32.42           C  
ATOM   2122  C   ILE A 277       2.916 -34.194   8.805  1.00 31.78           C  
ATOM   2123  O   ILE A 277       1.815 -33.692   8.574  1.00 32.22           O  
ATOM   2124  CB  ILE A 277       3.427 -35.642   6.823  1.00 30.17           C  
ATOM   2125  CG1 ILE A 277       4.115 -36.936   6.390  1.00 30.79           C  
ATOM   2126  CG2 ILE A 277       4.235 -34.438   6.358  1.00 27.17           C  
ATOM   2127  CD1 ILE A 277       4.446 -36.980   4.911  1.00 31.25           C  
ATOM   2128  N   LYS A 278       3.881 -33.550   9.454  1.00 30.89           N  
ATOM   2129  CA  LYS A 278       3.725 -32.162   9.875  1.00 30.77           C  
ATOM   2130  C   LYS A 278       4.407 -31.230   8.880  1.00 31.00           C  
ATOM   2131  O   LYS A 278       5.482 -31.543   8.369  1.00 31.87           O  
ATOM   2132  CB  LYS A 278       4.299 -31.950  11.279  1.00 30.05           C  
ATOM   2133  CG  LYS A 278       4.016 -30.571  11.857  1.00 30.51           C  
ATOM   2134  CD  LYS A 278       4.740 -30.345  13.176  1.00 31.19           C  
ATOM   2135  CE  LYS A 278       6.229 -30.141  12.967  1.00 31.74           C  
ATOM   2136  NZ  LYS A 278       6.938 -29.901  14.253  1.00 31.76           N  
ATOM   2137  N   VAL A 279       3.782 -30.090   8.601  1.00 30.80           N  
ATOM   2138  CA  VAL A 279       4.355 -29.119   7.674  1.00 31.47           C  
ATOM   2139  C   VAL A 279       4.359 -27.701   8.237  1.00 32.80           C  
ATOM   2140  O   VAL A 279       3.305 -27.131   8.514  1.00 34.35           O  
ATOM   2141  CB  VAL A 279       3.595 -29.104   6.333  1.00 31.67           C  
ATOM   2142  CG1 VAL A 279       4.192 -28.058   5.403  1.00 32.02           C  
ATOM   2143  CG2 VAL A 279       3.618 -30.478   5.686  1.00 31.47           C  
ATOM   2144  N   CYS A 280       5.549 -27.136   8.405  1.00 33.30           N  
ATOM   2145  CA  CYS A 280       5.681 -25.729   8.766  1.00 35.15           C  
ATOM   2146  C   CYS A 280       6.089 -24.920   7.540  1.00 38.05           C  
ATOM   2147  O   CYS A 280       6.582 -25.477   6.555  1.00 37.68           O  
ATOM   2148  CB  CYS A 280       6.711 -25.536   9.881  1.00 34.11           C  
ATOM   2149  SG  CYS A 280       6.385 -26.447  11.409  1.00 44.23           S  
ATOM   2150  N   ASP A 281       5.886 -23.608   7.599  1.00 39.97           N  
ATOM   2151  CA  ASP A 281       6.371 -22.726   6.546  1.00 42.91           C  
ATOM   2152  C   ASP A 281       7.580 -21.948   7.054  1.00 42.73           C  
ATOM   2153  O   ASP A 281       8.223 -22.358   8.017  1.00 42.96           O  
ATOM   2154  CB  ASP A 281       5.266 -21.776   6.071  1.00 45.96           C  
ATOM   2155  CG  ASP A 281       4.750 -20.876   7.175  1.00 48.47           C  
ATOM   2156  OD1 ASP A 281       4.898 -21.240   8.360  1.00 48.96           O  
ATOM   2157  OD2 ASP A 281       4.189 -19.807   6.857  1.00 50.20           O  
ATOM   2158  N   GLU A 282       7.892 -20.833   6.404  1.00 43.71           N  
ATOM   2159  CA  GLU A 282       9.024 -20.009   6.812  1.00 44.69           C  
ATOM   2160  C   GLU A 282       8.656 -18.530   6.812  1.00 43.07           C  
ATOM   2161  O   GLU A 282       8.483 -17.929   5.751  1.00 44.70           O  
ATOM   2162  CB  GLU A 282      10.222 -20.251   5.892  1.00 50.09           C  
ATOM   2163  CG  GLU A 282      11.461 -19.459   6.269  1.00 56.29           C  
ATOM   2164  CD  GLU A 282      12.026 -19.872   7.613  1.00 60.43           C  
ATOM   2165  OE1 GLU A 282      11.864 -21.053   7.988  1.00 60.55           O  
ATOM   2166  OE2 GLU A 282      12.627 -19.016   8.296  1.00 63.32           O  
ATOM   2167  N   PHE A 283       8.538 -17.948   8.003  1.00 39.79           N  
ATOM   2168  CA  PHE A 283       8.179 -16.539   8.133  1.00 37.68           C  
ATOM   2169  C   PHE A 283       8.613 -16.010   9.501  1.00 36.45           C  
ATOM   2170  O   PHE A 283       8.834 -16.796  10.421  1.00 35.93           O  
ATOM   2171  CB  PHE A 283       6.671 -16.349   7.905  1.00 36.31           C  
ATOM   2172  CG  PHE A 283       5.813 -16.749   9.071  1.00 33.87           C  
ATOM   2173  CD1 PHE A 283       5.828 -18.047   9.552  1.00 31.67           C  
ATOM   2174  CD2 PHE A 283       4.963 -15.829   9.663  1.00 33.25           C  
ATOM   2175  CE1 PHE A 283       5.028 -18.413  10.618  1.00 30.51           C  
ATOM   2176  CE2 PHE A 283       4.160 -16.190  10.724  1.00 32.36           C  
ATOM   2177  CZ  PHE A 283       4.193 -17.484  11.204  1.00 31.00           C  
ATOM   2178  N   PRO A 284       8.762 -14.678   9.634  1.00 36.21           N  
ATOM   2179  CA  PRO A 284       9.271 -14.071  10.873  1.00 36.29           C  
ATOM   2180  C   PRO A 284       8.393 -14.272  12.113  1.00 37.91           C  
ATOM   2181  O   PRO A 284       8.839 -13.944  13.213  1.00 39.80           O  
ATOM   2182  CB  PRO A 284       9.346 -12.583  10.524  1.00 37.74           C  
ATOM   2183  CG  PRO A 284       9.488 -12.549   9.045  1.00 38.12           C  
ATOM   2184  CD  PRO A 284       8.646 -13.683   8.552  1.00 36.28           C  
ATOM   2185  N   GLY A 285       7.179 -14.788  11.949  1.00 37.37           N  
ATOM   2186  CA  GLY A 285       6.317 -15.059  13.087  1.00 37.08           C  
ATOM   2187  C   GLY A 285       5.218 -14.033  13.294  1.00 39.05           C  
ATOM   2188  O   GLY A 285       5.251 -12.945  12.719  1.00 40.80           O  
ATOM   2189  N   PHE A 286       4.237 -14.387  14.120  1.00 39.41           N  
ATOM   2190  CA  PHE A 286       3.137 -13.487  14.458  1.00 40.20           C  
ATOM   2191  C   PHE A 286       3.166 -13.106  15.935  1.00 40.58           C  
ATOM   2192  O   PHE A 286       3.333 -13.967  16.796  1.00 40.60           O  
ATOM   2193  CB  PHE A 286       1.788 -14.134  14.130  1.00 39.79           C  
ATOM   2194  CG  PHE A 286       1.530 -14.299  12.661  1.00 40.11           C  
ATOM   2195  CD1 PHE A 286       1.754 -13.253  11.780  1.00 41.10           C  
ATOM   2196  CD2 PHE A 286       1.062 -15.506  12.160  1.00 38.43           C  
ATOM   2197  CE1 PHE A 286       1.514 -13.408  10.425  1.00 41.35           C  
ATOM   2198  CE2 PHE A 286       0.819 -15.669  10.809  1.00 37.45           C  
ATOM   2199  CZ  PHE A 286       1.046 -14.619   9.939  1.00 39.37           C  
ATOM   2200  N   THR A 287       2.995 -11.821  16.227  1.00 41.64           N  
ATOM   2201  CA  THR A 287       2.867 -11.370  17.610  1.00 41.38           C  
ATOM   2202  C   THR A 287       1.401 -11.285  18.022  1.00 43.28           C  
ATOM   2203  O   THR A 287       0.501 -11.399  17.188  1.00 43.37           O  
ATOM   2204  CB  THR A 287       3.519  -9.992  17.835  1.00 40.63           C  
ATOM   2205  OG1 THR A 287       2.881  -9.018  17.001  1.00 41.76           O  
ATOM   2206  CG2 THR A 287       5.002 -10.042  17.516  1.00 39.46           C  
ATOM   2207  N   HIS A 288       1.169 -11.078  19.315  1.00 44.95           N  
ATOM   2208  CA  HIS A 288      -0.181 -10.913  19.842  1.00 46.38           C  
ATOM   2209  C   HIS A 288      -0.157  -9.996  21.060  1.00 48.77           C  
ATOM   2210  O   HIS A 288      -0.226 -10.455  22.199  1.00 48.25           O  
ATOM   2211  CB  HIS A 288      -0.793 -12.270  20.200  1.00 45.49           C  
ATOM   2212  CG  HIS A 288      -2.201 -12.188  20.703  1.00 46.74           C  
ATOM   2213  ND1 HIS A 288      -2.552 -12.531  21.992  1.00 46.83           N  
ATOM   2214  CD2 HIS A 288      -3.346 -11.802  20.091  1.00 47.93           C  
ATOM   2215  CE1 HIS A 288      -3.852 -12.359  22.152  1.00 48.78           C  
ATOM   2216  NE2 HIS A 288      -4.357 -11.918  21.013  1.00 49.59           N  
ATOM   2217  N   PHE A 289      -0.054  -8.696  20.808  1.00 52.21           N  
ATOM   2218  CA  PHE A 289      -0.015  -7.708  21.878  1.00 54.74           C  
ATOM   2219  C   PHE A 289      -1.369  -7.562  22.568  1.00 59.41           C  
ATOM   2220  O   PHE A 289      -2.356  -7.151  21.955  1.00 60.69           O  
ATOM   2221  CB  PHE A 289       0.450  -6.352  21.340  1.00 53.92           C  
ATOM   2222  CG  PHE A 289       1.872  -6.348  20.861  1.00 51.19           C  
ATOM   2223  CD1 PHE A 289       2.915  -6.184  21.756  1.00 50.03           C  
ATOM   2224  CD2 PHE A 289       2.167  -6.511  19.518  1.00 50.70           C  
ATOM   2225  CE1 PHE A 289       4.225  -6.183  21.323  1.00 49.79           C  
ATOM   2226  CE2 PHE A 289       3.476  -6.511  19.076  1.00 50.27           C  
ATOM   2227  CZ  PHE A 289       4.507  -6.347  19.980  1.00 49.92           C  
ATOM   2228  N   LYS A 290      -1.401  -7.910  23.849  1.00 61.85           N  
ATOM   2229  CA  LYS A 290      -2.587  -7.734  24.675  1.00 64.65           C  
ATOM   2230  C   LYS A 290      -2.160  -7.104  25.991  1.00 66.99           C  
ATOM   2231  O   LYS A 290      -1.019  -7.275  26.422  1.00 67.12           O  
ATOM   2232  CB  LYS A 290      -3.299  -9.067  24.908  1.00 64.17           C  
ATOM   2233  CG  LYS A 290      -4.793  -8.931  25.141  1.00 66.69           C  
ATOM   2234  CD  LYS A 290      -5.527 -10.200  24.744  1.00 67.47           C  
ATOM   2235  CE  LYS A 290      -7.033 -10.001  24.779  1.00 70.65           C  
ATOM   2236  NZ  LYS A 290      -7.760 -11.182  24.234  1.00 70.96           N  
HETATM 2237  N   MSE A 291      -3.029  -6.329  26.613  1.00 70.06           N  
HETATM 2238  CA  MSE A 291      -2.636  -5.561  27.782  1.00 71.26           C  
HETATM 2239  C   MSE A 291      -2.394  -6.351  29.004  1.00 69.37           C  
HETATM 2240  O   MSE A 291      -3.230  -7.157  29.397  1.00 68.49           O  
HETATM 2241  CB  MSE A 291      -3.745  -4.590  28.043  1.00 20.00           C  
HETATM 2242  CG  MSE A 291      -3.594  -3.568  26.937  1.00 20.00           C  
HETATM 2243 SE   MSE A 291      -2.560  -2.053  27.593  1.00 20.00          SE  
HETATM 2244  CE  MSE A 291      -4.307  -1.298  28.019  1.00 20.00           C  
ATOM   2245  N   HIS A 292      -1.255  -6.115  29.624  1.00 69.93           N  
ATOM   2246  CA  HIS A 292      -0.796  -6.912  30.751  1.00 69.89           C  
ATOM   2247  C   HIS A 292       0.144  -6.139  31.669  1.00 71.39           C  
ATOM   2248  O   HIS A 292       0.893  -5.270  31.224  1.00 71.21           O  
ATOM   2249  CB  HIS A 292      -0.100  -8.177  30.250  1.00 69.34           C  
ATOM   2250  CG  HIS A 292      -0.344  -9.375  31.110  1.00 69.35           C  
ATOM   2251  ND1 HIS A 292      -1.394 -10.242  30.896  1.00 69.65           N  
ATOM   2252  CD2 HIS A 292       0.314  -9.842  32.197  1.00 69.26           C  
ATOM   2253  CE1 HIS A 292      -1.366 -11.196  31.809  1.00 69.52           C  
ATOM   2254  NE2 HIS A 292      -0.339 -10.976  32.611  1.00 69.47           N  
ATOM   2255  N   GLN A 293       0.093  -6.470  32.956  1.00 71.57           N  
ATOM   2256  CA  GLN A 293       0.998  -5.895  33.944  1.00 71.22           C  
ATOM   2257  C   GLN A 293       1.976  -6.944  34.456  1.00 65.67           C  
ATOM   2258  O   GLN A 293       1.653  -7.691  35.377  1.00 65.99           O  
ATOM   2259  CB  GLN A 293       0.222  -5.314  35.127  1.00 76.95           C  
ATOM   2260  CG  GLN A 293      -0.821  -4.279  34.765  1.00 83.11           C  
ATOM   2261  CD  GLN A 293      -1.473  -3.664  35.990  1.00 87.91           C  
ATOM   2262  OE1 GLN A 293      -1.677  -4.335  37.002  1.00 88.53           O  
ATOM   2263  NE2 GLN A 293      -1.796  -2.379  35.906  1.00 90.83           N  
ATOM   2264  N   PRO A 294       3.174  -7.012  33.863  1.00 61.62           N  
ATOM   2265  CA  PRO A 294       4.177  -7.925  34.415  1.00 56.84           C  
ATOM   2266  C   PRO A 294       4.705  -7.389  35.734  1.00 54.26           C  
ATOM   2267  O   PRO A 294       4.721  -6.172  35.926  1.00 54.57           O  
ATOM   2268  CB  PRO A 294       5.267  -7.942  33.343  1.00 57.51           C  
ATOM   2269  CG  PRO A 294       5.149  -6.613  32.680  1.00 60.37           C  
ATOM   2270  CD  PRO A 294       3.681  -6.266  32.698  1.00 61.48           C  
ATOM   2271  N   TYR A 295       5.120  -8.271  36.636  1.00 50.90           N  
ATOM   2272  CA  TYR A 295       5.645  -7.814  37.915  1.00 49.37           C  
ATOM   2273  C   TYR A 295       7.029  -7.204  37.728  1.00 49.62           C  
ATOM   2274  O   TYR A 295       7.869  -7.750  37.010  1.00 49.05           O  
ATOM   2275  CB  TYR A 295       5.702  -8.953  38.930  1.00 45.74           C  
ATOM   2276  CG  TYR A 295       5.974  -8.473  40.336  1.00 44.09           C  
ATOM   2277  CD1 TYR A 295       7.273  -8.339  40.806  1.00 43.11           C  
ATOM   2278  CD2 TYR A 295       4.932  -8.139  41.189  1.00 45.05           C  
ATOM   2279  CE1 TYR A 295       7.528  -7.894  42.088  1.00 44.73           C  
ATOM   2280  CE2 TYR A 295       5.175  -7.693  42.475  1.00 46.21           C  
ATOM   2281  CZ  TYR A 295       6.476  -7.572  42.919  1.00 46.51           C  
ATOM   2282  OH  TYR A 295       6.728  -7.130  44.197  1.00 48.73           O  
ATOM   2283  N   GLY A 296       7.259  -6.071  38.383  1.00 50.34           N  
ATOM   2284  CA  GLY A 296       8.495  -5.333  38.221  1.00 51.18           C  
ATOM   2285  C   GLY A 296       8.231  -4.067  37.433  1.00 54.03           C  
ATOM   2286  O   GLY A 296       8.981  -3.098  37.515  1.00 56.06           O  
ATOM   2287  N   SER A 297       7.153  -4.086  36.659  1.00 54.92           N  
ATOM   2288  CA  SER A 297       6.722  -2.910  35.919  1.00 57.20           C  
ATOM   2289  C   SER A 297       5.626  -2.193  36.695  1.00 59.57           C  
ATOM   2290  O   SER A 297       4.644  -2.812  37.105  1.00 58.55           O  
ATOM   2291  CB  SER A 297       6.227  -3.296  34.524  1.00 57.38           C  
ATOM   2292  OG  SER A 297       5.790  -2.156  33.805  1.00 59.59           O  
ATOM   2293  N   PRO A 298       5.796  -0.880  36.904  1.00 62.86           N  
ATOM   2294  CA  PRO A 298       4.842  -0.070  37.669  1.00 65.10           C  
ATOM   2295  C   PRO A 298       3.589   0.254  36.866  1.00 66.83           C  
ATOM   2296  O   PRO A 298       2.590   0.708  37.422  1.00 68.23           O  
ATOM   2297  CB  PRO A 298       5.637   1.201  37.970  1.00 66.29           C  
ATOM   2298  CG  PRO A 298       6.552   1.334  36.798  1.00 65.51           C  
ATOM   2299  CD  PRO A 298       6.929  -0.075  36.409  1.00 63.28           C  
ATOM   2300  N   VAL A 299       3.653   0.009  35.563  1.00 67.39           N  
ATOM   2301  CA  VAL A 299       2.614   0.432  34.635  1.00 69.78           C  
ATOM   2302  C   VAL A 299       2.249  -0.706  33.684  1.00 69.25           C  
ATOM   2303  O   VAL A 299       3.131  -1.424  33.214  1.00 67.72           O  
ATOM   2304  CB  VAL A 299       3.081   1.673  33.832  1.00 74.41           C  
ATOM   2305  CG1 VAL A 299       2.204   1.919  32.620  1.00 74.99           C  
ATOM   2306  CG2 VAL A 299       3.122   2.904  34.727  1.00 77.46           C  
ATOM   2307  N   PRO A 300       0.943  -0.891  33.417  1.00 69.99           N  
ATOM   2308  CA  PRO A 300       0.497  -1.879  32.427  1.00 69.59           C  
ATOM   2309  C   PRO A 300       1.097  -1.636  31.045  1.00 70.47           C  
ATOM   2310  O   PRO A 300       0.722  -0.679  30.369  1.00 72.98           O  
ATOM   2311  CB  PRO A 300      -1.030  -1.695  32.398  1.00 69.99           C  
ATOM   2312  CG  PRO A 300      -1.293  -0.398  33.082  1.00 72.30           C  
ATOM   2313  CD  PRO A 300      -0.193  -0.226  34.075  1.00 71.98           C  
ATOM   2314  N   LYS A 301       2.027  -2.494  30.640  1.00 67.60           N  
ATOM   2315  CA  LYS A 301       2.632  -2.392  29.319  1.00 67.13           C  
ATOM   2316  C   LYS A 301       1.806  -3.163  28.301  1.00 66.17           C  
ATOM   2317  O   LYS A 301       0.891  -3.904  28.660  1.00 66.67           O  
ATOM   2318  CB  LYS A 301       4.069  -2.917  29.336  1.00 66.46           C  
ATOM   2319  CG  LYS A 301       5.036  -2.090  30.168  1.00 68.92           C  
ATOM   2320  CD  LYS A 301       6.433  -2.693  30.129  1.00 68.84           C  
ATOM   2321  CE  LYS A 301       7.433  -1.853  30.910  1.00 70.28           C  
ATOM   2322  NZ  LYS A 301       8.792  -2.467  30.895  1.00 69.13           N  
ATOM   2323  N   LEU A 302       2.126  -2.980  27.026  1.00 64.96           N  
ATOM   2324  CA  LEU A 302       1.490  -3.755  25.975  1.00 61.58           C  
ATOM   2325  C   LEU A 302       2.485  -4.805  25.495  1.00 57.78           C  
ATOM   2326  O   LEU A 302       3.451  -4.491  24.800  1.00 57.71           O  
ATOM   2327  CB  LEU A 302       1.026  -2.850  24.833  1.00 62.75           C  
ATOM   2328  CG  LEU A 302      -0.099  -3.395  23.951  1.00 61.45           C  
ATOM   2329  CD1 LEU A 302      -1.057  -4.226  24.770  1.00 61.04           C  
ATOM   2330  CD2 LEU A 302      -0.848  -2.256  23.296  1.00 62.60           C  
ATOM   2331  N   ILE A 303       2.248  -6.049  25.899  1.00 54.64           N  
ATOM   2332  CA  ILE A 303       3.190  -7.139  25.679  1.00 50.68           C  
ATOM   2333  C   ILE A 303       2.599  -8.184  24.741  1.00 49.45           C  
ATOM   2334  O   ILE A 303       1.401  -8.462  24.788  1.00 50.76           O  
ATOM   2335  CB  ILE A 303       3.583  -7.817  27.020  1.00 46.59           C  
ATOM   2336  CG1 ILE A 303       4.128  -6.783  28.010  1.00 49.43           C  
ATOM   2337  CG2 ILE A 303       4.593  -8.939  26.804  1.00 43.64           C  
ATOM   2338  CD1 ILE A 303       5.369  -6.060  27.525  1.00 51.07           C  
ATOM   2339  N   SER A 304       3.436  -8.754  23.881  1.00 46.65           N  
ATOM   2340  CA  SER A 304       3.016  -9.868  23.047  1.00 43.25           C  
ATOM   2341  C   SER A 304       2.785 -11.101  23.920  1.00 41.91           C  
ATOM   2342  O   SER A 304       3.735 -11.735  24.380  1.00 40.39           O  
ATOM   2343  CB  SER A 304       4.058 -10.155  21.966  1.00 42.24           C  
ATOM   2344  OG  SER A 304       3.589 -11.124  21.045  1.00 41.39           O  
ATOM   2345  N   VAL A 305       1.516 -11.426  24.149  1.00 42.76           N  
ATOM   2346  CA  VAL A 305       1.132 -12.548  25.003  1.00 41.35           C  
ATOM   2347  C   VAL A 305       0.603 -13.711  24.163  1.00 41.03           C  
ATOM   2348  O   VAL A 305      -0.195 -13.501  23.251  1.00 42.36           O  
ATOM   2349  CB  VAL A 305       0.054 -12.126  26.028  1.00 41.86           C  
ATOM   2350  CG1 VAL A 305      -0.175 -13.221  27.054  1.00 40.69           C  
ATOM   2351  CG2 VAL A 305       0.449 -10.828  26.718  1.00 43.35           C  
ATOM   2352  N   PRO A 306       1.053 -14.943  24.458  1.00 39.80           N  
ATOM   2353  CA  PRO A 306       0.550 -16.110  23.723  1.00 39.46           C  
ATOM   2354  C   PRO A 306      -0.950 -16.287  23.917  1.00 42.54           C  
ATOM   2355  O   PRO A 306      -1.462 -16.002  24.999  1.00 42.80           O  
ATOM   2356  CB  PRO A 306       1.321 -17.282  24.340  1.00 37.20           C  
ATOM   2357  CG  PRO A 306       2.535 -16.667  24.944  1.00 37.72           C  
ATOM   2358  CD  PRO A 306       2.113 -15.309  25.414  1.00 39.20           C  
ATOM   2359  N   ARG A 307      -1.646 -16.748  22.884  1.00 45.45           N  
ATOM   2360  CA  ARG A 307      -3.090 -16.915  22.974  1.00 50.15           C  
ATOM   2361  C   ARG A 307      -3.464 -18.243  23.623  1.00 55.13           C  
ATOM   2362  O   ARG A 307      -2.785 -19.253  23.437  1.00 54.38           O  
ATOM   2363  CB  ARG A 307      -3.733 -16.812  21.593  1.00 48.84           C  
ATOM   2364  CG  ARG A 307      -4.778 -15.718  21.504  1.00 49.95           C  
ATOM   2365  CD  ARG A 307      -5.988 -16.167  20.716  1.00 50.25           C  
ATOM   2366  NE  ARG A 307      -7.097 -15.227  20.845  1.00 53.12           N  
ATOM   2367  CZ  ARG A 307      -8.290 -15.390  20.281  1.00 54.23           C  
ATOM   2368  NH1 ARG A 307      -8.536 -16.462  19.540  1.00 53.29           N  
ATOM   2369  NH2 ARG A 307      -9.239 -14.479  20.456  1.00 56.16           N  
ATOM   2370  N   SER A 308      -4.551 -18.231  24.389  1.00 60.95           N  
ATOM   2371  CA  SER A 308      -5.021 -19.427  25.077  1.00 65.55           C  
ATOM   2372  C   SER A 308      -5.953 -20.255  24.202  1.00 72.60           C  
ATOM   2373  O   SER A 308      -7.061 -19.822  23.882  1.00 72.91           O  
ATOM   2374  CB  SER A 308      -5.736 -19.051  26.373  1.00 65.78           C  
ATOM   2375  OG  SER A 308      -6.371 -20.183  26.943  1.00 65.53           O  
ATOM   2376  N   HIS A 309      -5.502 -21.448  23.823  1.00 76.63           N  
ATOM   2377  CA  HIS A 309      -6.323 -22.362  23.035  1.00 79.27           C  
ATOM   2378  C   HIS A 309      -7.534 -22.823  23.846  1.00 76.88           C  
ATOM   2379  O   HIS A 309      -8.579 -23.160  23.287  1.00 77.30           O  
ATOM   2380  CB  HIS A 309      -5.500 -23.568  22.564  1.00 82.64           C  
ATOM   2381  CG  HIS A 309      -5.078 -24.486  23.672  1.00 87.07           C  
ATOM   2382  ND1 HIS A 309      -3.858 -24.381  24.303  1.00 87.87           N  
ATOM   2383  CD2 HIS A 309      -5.718 -25.525  24.260  1.00 89.31           C  
ATOM   2384  CE1 HIS A 309      -3.763 -25.316  25.233  1.00 88.30           C  
ATOM   2385  NE2 HIS A 309      -4.878 -26.023  25.228  1.00 89.45           N  
ATOM   2386  N   ALA A 310      -7.382 -22.828  25.168  1.00 71.99           N  
ATOM   2387  CA  ALA A 310      -8.453 -23.234  26.072  1.00 67.64           C  
ATOM   2388  C   ALA A 310      -9.648 -22.289  25.987  1.00 63.98           C  
ATOM   2389  O   ALA A 310     -10.799 -22.727  25.965  1.00 64.38           O  
ATOM   2390  CB  ALA A 310      -7.937 -23.303  27.502  1.00 69.59           C  
ATOM   2391  N   LYS A 311      -9.366 -20.991  25.939  1.00 58.99           N  
ATOM   2392  CA  LYS A 311     -10.411 -19.974  25.872  1.00 55.20           C  
ATOM   2393  C   LYS A 311     -10.886 -19.738  24.444  1.00 53.44           C  
ATOM   2394  O   LYS A 311     -11.930 -19.125  24.225  1.00 53.77           O  
ATOM   2395  CB  LYS A 311      -9.916 -18.659  26.475  1.00 52.62           C  
ATOM   2396  CG  LYS A 311      -9.975 -18.604  27.994  1.00 52.14           C  
ATOM   2397  CD  LYS A 311      -9.263 -17.370  28.518  1.00 51.40           C  
ATOM   2398  CE  LYS A 311      -9.927 -16.839  29.774  1.00 53.07           C  
ATOM   2399  NZ  LYS A 311      -9.264 -15.596  30.255  1.00 54.09           N  
ATOM   2400  N   HIS A 312     -10.115 -20.222  23.476  1.00 52.28           N  
ATOM   2401  CA  HIS A 312     -10.455 -20.036  22.068  1.00 53.14           C  
ATOM   2402  C   HIS A 312     -10.257 -21.325  21.270  1.00 52.47           C  
ATOM   2403  O   HIS A 312      -9.206 -21.534  20.659  1.00 49.84           O  
ATOM   2404  CB  HIS A 312      -9.623 -18.903  21.467  1.00 51.75           C  
ATOM   2405  CG  HIS A 312      -9.674 -17.634  22.261  1.00 51.81           C  
ATOM   2406  ND1 HIS A 312     -10.769 -16.796  22.255  1.00 54.00           N  
ATOM   2407  CD2 HIS A 312      -8.768 -17.064  23.089  1.00 50.64           C  
ATOM   2408  CE1 HIS A 312     -10.533 -15.763  23.044  1.00 54.51           C  
ATOM   2409  NE2 HIS A 312      -9.325 -15.901  23.562  1.00 52.63           N  
ATOM   2410  N   PRO A 313     -11.279 -22.195  21.279  1.00 53.83           N  
ATOM   2411  CA  PRO A 313     -11.255 -23.514  20.637  1.00 52.66           C  
ATOM   2412  C   PRO A 313     -11.323 -23.449  19.115  1.00 51.11           C  
ATOM   2413  O   PRO A 313     -10.808 -24.343  18.451  1.00 50.05           O  
ATOM   2414  CB  PRO A 313     -12.509 -24.201  21.197  1.00 54.93           C  
ATOM   2415  CG  PRO A 313     -12.909 -23.384  22.391  1.00 55.56           C  
ATOM   2416  CD  PRO A 313     -12.515 -21.992  22.048  1.00 54.87           C  
ATOM   2417  N   THR A 314     -11.946 -22.405  18.577  1.00 52.22           N  
ATOM   2418  CA  THR A 314     -12.113 -22.261  17.132  1.00 52.48           C  
ATOM   2419  C   THR A 314     -10.800 -21.847  16.457  1.00 49.64           C  
ATOM   2420  O   THR A 314     -10.687 -21.855  15.232  1.00 49.23           O  
ATOM   2421  CB  THR A 314     -13.221 -21.229  16.809  1.00 55.81           C  
ATOM   2422  OG1 THR A 314     -14.340 -21.443  17.678  1.00 58.54           O  
ATOM   2423  CG2 THR A 314     -13.690 -21.348  15.362  1.00 56.47           C  
ATOM   2424  N   ASP A 315      -9.803 -21.507  17.268  1.00 48.16           N  
ATOM   2425  CA  ASP A 315      -8.518 -21.024  16.764  1.00 46.30           C  
ATOM   2426  C   ASP A 315      -7.775 -22.016  15.871  1.00 43.81           C  
ATOM   2427  O   ASP A 315      -7.634 -23.193  16.204  1.00 42.89           O  
ATOM   2428  CB  ASP A 315      -7.611 -20.637  17.932  1.00 46.28           C  
ATOM   2429  CG  ASP A 315      -7.868 -19.231  18.427  1.00 48.68           C  
ATOM   2430  OD1 ASP A 315      -8.936 -18.664  18.109  1.00 50.72           O  
ATOM   2431  OD2 ASP A 315      -7.000 -18.689  19.140  1.00 48.42           O  
ATOM   2432  N   THR A 316      -7.305 -21.520  14.731  1.00 42.84           N  
ATOM   2433  CA  THR A 316      -6.364 -22.248  13.890  1.00 42.22           C  
ATOM   2434  C   THR A 316      -5.160 -21.348  13.631  1.00 43.25           C  
ATOM   2435  O   THR A 316      -4.338 -21.129  14.522  1.00 42.35           O  
ATOM   2436  CB  THR A 316      -6.995 -22.693  12.556  1.00 40.57           C  
ATOM   2437  OG1 THR A 316      -7.739 -21.607  11.992  1.00 41.28           O  
ATOM   2438  CG2 THR A 316      -7.928 -23.874  12.774  1.00 39.76           C  
ATOM   2439  N   TYR A 317      -5.064 -20.822  12.413  1.00 44.11           N  
ATOM   2440  CA  TYR A 317      -4.041 -19.834  12.085  1.00 43.79           C  
ATOM   2441  C   TYR A 317      -4.548 -18.903  10.976  1.00 44.60           C  
ATOM   2442  O   TYR A 317      -5.539 -19.219  10.317  1.00 45.37           O  
ATOM   2443  CB  TYR A 317      -2.721 -20.520  11.691  1.00 42.39           C  
ATOM   2444  CG  TYR A 317      -2.807 -21.647  10.683  1.00 41.90           C  
ATOM   2445  CD1 TYR A 317      -3.504 -21.501   9.487  1.00 42.92           C  
ATOM   2446  CD2 TYR A 317      -2.143 -22.846  10.908  1.00 40.38           C  
ATOM   2447  CE1 TYR A 317      -3.564 -22.529   8.564  1.00 42.33           C  
ATOM   2448  CE2 TYR A 317      -2.193 -23.876   9.990  1.00 40.22           C  
ATOM   2449  CZ  TYR A 317      -2.904 -23.712   8.820  1.00 41.02           C  
ATOM   2450  OH  TYR A 317      -2.959 -24.736   7.904  1.00 40.83           O  
ATOM   2451  N   PRO A 318      -3.896 -17.738  10.792  1.00 44.47           N  
ATOM   2452  CA  PRO A 318      -4.334 -16.790   9.759  1.00 45.46           C  
ATOM   2453  C   PRO A 318      -4.433 -17.415   8.372  1.00 46.12           C  
ATOM   2454  O   PRO A 318      -3.730 -18.383   8.090  1.00 46.20           O  
ATOM   2455  CB  PRO A 318      -3.242 -15.722   9.784  1.00 45.17           C  
ATOM   2456  CG  PRO A 318      -2.735 -15.748  11.171  1.00 44.72           C  
ATOM   2457  CD  PRO A 318      -2.805 -17.180  11.614  1.00 43.41           C  
ATOM   2458  N   HIS A 319      -5.293 -16.859   7.523  1.00 47.04           N  
ATOM   2459  CA  HIS A 319      -5.492 -17.377   6.172  1.00 46.52           C  
ATOM   2460  C   HIS A 319      -4.214 -17.333   5.339  1.00 43.87           C  
ATOM   2461  O   HIS A 319      -3.995 -18.192   4.485  1.00 43.85           O  
ATOM   2462  CB  HIS A 319      -6.597 -16.599   5.459  1.00 50.01           C  
ATOM   2463  CG  HIS A 319      -6.765 -16.978   4.021  1.00 52.73           C  
ATOM   2464  ND1 HIS A 319      -6.093 -16.340   3.000  1.00 54.57           N  
ATOM   2465  CD2 HIS A 319      -7.527 -17.929   3.432  1.00 53.89           C  
ATOM   2466  CE1 HIS A 319      -6.435 -16.880   1.845  1.00 55.36           C  
ATOM   2467  NE2 HIS A 319      -7.304 -17.848   2.078  1.00 55.22           N  
ATOM   2468  N   ALA A 320      -3.376 -16.332   5.586  1.00 41.93           N  
ATOM   2469  CA  ALA A 320      -2.096 -16.228   4.894  1.00 40.62           C  
ATOM   2470  C   ALA A 320      -1.229 -17.465   5.138  1.00 40.09           C  
ATOM   2471  O   ALA A 320      -0.494 -17.902   4.250  1.00 39.59           O  
ATOM   2472  CB  ALA A 320      -1.359 -14.974   5.328  1.00 39.35           C  
ATOM   2473  N   SER A 321      -1.322 -18.029   6.339  1.00 38.61           N  
ATOM   2474  CA  SER A 321      -0.560 -19.227   6.676  1.00 36.77           C  
ATOM   2475  C   SER A 321      -1.035 -20.441   5.879  1.00 35.76           C  
ATOM   2476  O   SER A 321      -0.231 -21.288   5.486  1.00 34.53           O  
ATOM   2477  CB  SER A 321      -0.648 -19.512   8.175  1.00 36.76           C  
ATOM   2478  OG  SER A 321       0.012 -18.506   8.920  1.00 37.39           O  
ATOM   2479  N   GLU A 322      -2.342 -20.518   5.642  1.00 35.55           N  
ATOM   2480  CA  GLU A 322      -2.922 -21.610   4.865  1.00 35.94           C  
ATOM   2481  C   GLU A 322      -2.352 -21.650   3.448  1.00 37.58           C  
ATOM   2482  O   GLU A 322      -2.087 -22.723   2.907  1.00 38.18           O  
ATOM   2483  CB  GLU A 322      -4.446 -21.478   4.815  1.00 36.77           C  
ATOM   2484  CG  GLU A 322      -5.160 -22.580   4.040  1.00 36.42           C  
ATOM   2485  CD  GLU A 322      -5.336 -23.862   4.841  1.00 36.29           C  
ATOM   2486  OE1 GLU A 322      -6.119 -24.729   4.396  1.00 37.11           O  
ATOM   2487  OE2 GLU A 322      -4.699 -24.009   5.908  1.00 34.33           O  
ATOM   2488  N   VAL A 323      -2.154 -20.476   2.858  1.00 37.77           N  
ATOM   2489  CA  VAL A 323      -1.616 -20.377   1.507  1.00 37.22           C  
ATOM   2490  C   VAL A 323      -0.155 -20.828   1.439  1.00 38.16           C  
ATOM   2491  O   VAL A 323       0.218 -21.610   0.563  1.00 40.00           O  
ATOM   2492  CB  VAL A 323      -1.729 -18.936   0.967  1.00 37.15           C  
ATOM   2493  CG1 VAL A 323      -1.169 -18.848  -0.446  1.00 36.49           C  
ATOM   2494  CG2 VAL A 323      -3.178 -18.468   1.007  1.00 37.28           C  
ATOM   2495  N   THR A 324       0.666 -20.347   2.369  1.00 36.90           N  
ATOM   2496  CA  THR A 324       2.092 -20.666   2.357  1.00 35.77           C  
ATOM   2497  C   THR A 324       2.364 -22.125   2.725  1.00 35.72           C  
ATOM   2498  O   THR A 324       3.336 -22.718   2.255  1.00 36.04           O  
ATOM   2499  CB  THR A 324       2.881 -19.749   3.312  1.00 34.56           C  
ATOM   2500  OG1 THR A 324       2.340 -19.850   4.636  1.00 36.44           O  
ATOM   2501  CG2 THR A 324       2.801 -18.307   2.843  1.00 33.31           C  
ATOM   2502  N   ILE A 325       1.507 -22.701   3.561  1.00 35.66           N  
ATOM   2503  CA  ILE A 325       1.635 -24.109   3.921  1.00 35.04           C  
ATOM   2504  C   ILE A 325       1.275 -25.000   2.728  1.00 35.75           C  
ATOM   2505  O   ILE A 325       1.911 -26.030   2.496  1.00 35.70           O  
ATOM   2506  CB  ILE A 325       0.752 -24.466   5.142  1.00 34.52           C  
ATOM   2507  CG1 ILE A 325       1.348 -23.857   6.414  1.00 35.70           C  
ATOM   2508  CG2 ILE A 325       0.629 -25.973   5.306  1.00 32.25           C  
ATOM   2509  CD1 ILE A 325       0.567 -24.164   7.677  1.00 35.97           C  
ATOM   2510  N   LYS A 326       0.268 -24.594   1.962  1.00 36.38           N  
ATOM   2511  CA  LYS A 326      -0.109 -25.340   0.766  1.00 36.98           C  
ATOM   2512  C   LYS A 326       0.968 -25.237  -0.312  1.00 36.68           C  
ATOM   2513  O   LYS A 326       1.167 -26.170  -1.091  1.00 36.83           O  
ATOM   2514  CB  LYS A 326      -1.452 -24.849   0.221  1.00 40.70           C  
ATOM   2515  CG  LYS A 326      -2.653 -25.261   1.060  1.00 44.15           C  
ATOM   2516  CD  LYS A 326      -3.958 -24.931   0.350  1.00 48.50           C  
ATOM   2517  CE  LYS A 326      -5.153 -25.053   1.284  1.00 52.36           C  
ATOM   2518  NZ  LYS A 326      -5.311 -26.427   1.836  1.00 53.50           N  
ATOM   2519  N   LYS A 327       1.662 -24.104  -0.355  1.00 36.83           N  
ATOM   2520  CA  LYS A 327       2.758 -23.930  -1.301  1.00 37.52           C  
ATOM   2521  C   LYS A 327       3.929 -24.834  -0.936  1.00 36.89           C  
ATOM   2522  O   LYS A 327       4.613 -25.359  -1.817  1.00 37.76           O  
ATOM   2523  CB  LYS A 327       3.210 -22.470  -1.353  1.00 39.05           C  
ATOM   2524  CG  LYS A 327       2.228 -21.552  -2.059  1.00 42.51           C  
ATOM   2525  CD  LYS A 327       2.788 -20.148  -2.230  1.00 44.85           C  
ATOM   2526  CE  LYS A 327       1.805 -19.250  -2.970  1.00 47.07           C  
ATOM   2527  NZ  LYS A 327       2.356 -17.886  -3.210  1.00 48.92           N  
ATOM   2528  N   ALA A 328       4.155 -25.014   0.363  1.00 34.63           N  
ATOM   2529  CA  ALA A 328       5.218 -25.894   0.836  1.00 33.75           C  
ATOM   2530  C   ALA A 328       4.909 -27.339   0.464  1.00 33.58           C  
ATOM   2531  O   ALA A 328       5.798 -28.102   0.082  1.00 33.07           O  
ATOM   2532  CB  ALA A 328       5.401 -25.757   2.342  1.00 31.60           C  
ATOM   2533  N   ILE A 329       3.637 -27.704   0.574  1.00 33.36           N  
ATOM   2534  CA  ILE A 329       3.196 -29.050   0.233  1.00 33.16           C  
ATOM   2535  C   ILE A 329       3.319 -29.286  -1.275  1.00 33.79           C  
ATOM   2536  O   ILE A 329       3.732 -30.360  -1.710  1.00 31.63           O  
ATOM   2537  CB  ILE A 329       1.746 -29.298   0.701  1.00 31.11           C  
ATOM   2538  CG1 ILE A 329       1.680 -29.292   2.231  1.00 28.98           C  
ATOM   2539  CG2 ILE A 329       1.223 -30.620   0.166  1.00 30.42           C  
ATOM   2540  CD1 ILE A 329       0.280 -29.429   2.787  1.00 27.61           C  
ATOM   2541  N   ASN A 330       2.985 -28.272  -2.067  1.00 35.61           N  
ATOM   2542  CA  ASN A 330       3.101 -28.368  -3.518  1.00 36.80           C  
ATOM   2543  C   ASN A 330       4.558 -28.491  -3.968  1.00 37.79           C  
ATOM   2544  O   ASN A 330       4.846 -29.068  -5.019  1.00 37.33           O  
ATOM   2545  CB  ASN A 330       2.440 -27.156  -4.183  1.00 37.44           C  
ATOM   2546  CG  ASN A 330       2.520 -27.203  -5.700  1.00 37.73           C  
ATOM   2547  OD1 ASN A 330       1.723 -27.873  -6.357  1.00 37.22           O  
ATOM   2548  ND2 ASN A 330       3.482 -26.482  -6.263  1.00 37.79           N  
ATOM   2549  N   ARG A 331       5.471 -27.957  -3.162  1.00 38.99           N  
ATOM   2550  CA  ARG A 331       6.899 -28.013  -3.462  1.00 40.49           C  
ATOM   2551  C   ARG A 331       7.515 -29.366  -3.136  1.00 40.20           C  
ATOM   2552  O   ARG A 331       8.231 -29.943  -3.953  1.00 40.49           O  
ATOM   2553  CB  ARG A 331       7.646 -26.925  -2.694  1.00 41.81           C  
ATOM   2554  CG  ARG A 331       8.236 -25.848  -3.572  1.00 45.37           C  
ATOM   2555  CD  ARG A 331       9.572 -26.256  -4.175  1.00 47.97           C  
ATOM   2556  NE  ARG A 331       9.981 -25.318  -5.218  1.00 52.44           N  
ATOM   2557  CZ  ARG A 331      11.230 -25.159  -5.643  1.00 55.74           C  
ATOM   2558  NH1 ARG A 331      12.212 -25.869  -5.107  1.00 56.96           N  
ATOM   2559  NH2 ARG A 331      11.500 -24.281  -6.599  1.00 57.37           N  
ATOM   2560  N   PHE A 332       7.236 -29.863  -1.935  1.00 39.56           N  
ATOM   2561  CA  PHE A 332       7.885 -31.068  -1.432  1.00 39.54           C  
ATOM   2562  C   PHE A 332       7.077 -32.332  -1.710  1.00 40.68           C  
ATOM   2563  O   PHE A 332       7.642 -33.377  -2.033  1.00 41.55           O  
ATOM   2564  CB  PHE A 332       8.135 -30.941   0.072  1.00 38.72           C  
ATOM   2565  CG  PHE A 332       8.972 -29.752   0.455  1.00 38.28           C  
ATOM   2566  CD1 PHE A 332      10.044 -29.356  -0.329  1.00 38.66           C  
ATOM   2567  CD2 PHE A 332       8.682 -29.027   1.600  1.00 37.37           C  
ATOM   2568  CE1 PHE A 332      10.814 -28.264   0.024  1.00 38.10           C  
ATOM   2569  CE2 PHE A 332       9.447 -27.932   1.958  1.00 37.07           C  
ATOM   2570  CZ  PHE A 332      10.514 -27.552   1.169  1.00 37.88           C  
ATOM   2571  N   LEU A 333       5.756 -32.232  -1.577  1.00 39.80           N  
ATOM   2572  CA  LEU A 333       4.877 -33.391  -1.713  1.00 39.35           C  
ATOM   2573  C   LEU A 333       3.700 -33.135  -2.657  1.00 40.25           C  
ATOM   2574  O   LEU A 333       2.545 -33.210  -2.235  1.00 40.65           O  
ATOM   2575  CB  LEU A 333       4.338 -33.796  -0.339  1.00 39.20           C  
ATOM   2576  CG  LEU A 333       5.317 -33.786   0.837  1.00 38.66           C  
ATOM   2577  CD1 LEU A 333       4.573 -33.776   2.164  1.00 38.68           C  
ATOM   2578  CD2 LEU A 333       6.248 -34.979   0.758  1.00 38.07           C  
ATOM   2579  N   PRO A 334       3.980 -32.842  -3.937  1.00 40.87           N  
ATOM   2580  CA  PRO A 334       2.907 -32.460  -4.866  1.00 41.17           C  
ATOM   2581  C   PRO A 334       1.875 -33.565  -5.077  1.00 41.70           C  
ATOM   2582  O   PRO A 334       0.729 -33.280  -5.421  1.00 43.18           O  
ATOM   2583  CB  PRO A 334       3.657 -32.168  -6.167  1.00 41.84           C  
ATOM   2584  CG  PRO A 334       4.889 -32.995  -6.078  1.00 41.61           C  
ATOM   2585  CD  PRO A 334       5.276 -32.976  -4.625  1.00 41.17           C  
ATOM   2586  N   ARG A 335       2.283 -34.810  -4.865  1.00 41.88           N  
ATOM   2587  CA  ARG A 335       1.388 -35.954  -5.000  1.00 43.21           C  
ATOM   2588  C   ARG A 335       0.274 -35.930  -3.953  1.00 40.88           C  
ATOM   2589  O   ARG A 335      -0.753 -36.586  -4.113  1.00 41.59           O  
ATOM   2590  CB  ARG A 335       2.179 -37.260  -4.887  1.00 46.28           C  
ATOM   2591  CG  ARG A 335       2.835 -37.460  -3.527  1.00 49.40           C  
ATOM   2592  CD  ARG A 335       3.680 -38.722  -3.482  1.00 52.69           C  
ATOM   2593  NE  ARG A 335       4.874 -38.614  -4.316  1.00 55.90           N  
ATOM   2594  CZ  ARG A 335       5.808 -39.554  -4.409  1.00 57.86           C  
ATOM   2595  NH1 ARG A 335       5.690 -40.679  -3.719  1.00 59.23           N  
ATOM   2596  NH2 ARG A 335       6.862 -39.369  -5.193  1.00 58.86           N  
ATOM   2597  N   PHE A 336       0.484 -35.174  -2.881  1.00 38.45           N  
ATOM   2598  CA  PHE A 336      -0.472 -35.132  -1.782  1.00 36.94           C  
ATOM   2599  C   PHE A 336      -1.220 -33.808  -1.713  1.00 36.34           C  
ATOM   2600  O   PHE A 336      -1.726 -33.433  -0.658  1.00 35.89           O  
ATOM   2601  CB  PHE A 336       0.239 -35.395  -0.456  1.00 35.51           C  
ATOM   2602  CG  PHE A 336       0.827 -36.772  -0.349  1.00 35.09           C  
ATOM   2603  CD1 PHE A 336       0.066 -37.890  -0.645  1.00 35.62           C  
ATOM   2604  CD2 PHE A 336       2.145 -36.948   0.036  1.00 34.52           C  
ATOM   2605  CE1 PHE A 336       0.605 -39.159  -0.550  1.00 35.39           C  
ATOM   2606  CE2 PHE A 336       2.691 -38.215   0.130  1.00 34.59           C  
ATOM   2607  CZ  PHE A 336       1.919 -39.321  -0.163  1.00 34.61           C  
ATOM   2608  N   ASN A 337      -1.296 -33.108  -2.840  1.00 36.57           N  
ATOM   2609  CA  ASN A 337      -1.932 -31.794  -2.885  1.00 36.78           C  
ATOM   2610  C   ASN A 337      -3.433 -31.828  -2.607  1.00 37.19           C  
ATOM   2611  O   ASN A 337      -4.044 -30.791  -2.359  1.00 35.49           O  
ATOM   2612  CB  ASN A 337      -1.680 -31.132  -4.242  1.00 37.66           C  
ATOM   2613  CG  ASN A 337      -0.378 -30.353  -4.279  1.00 39.21           C  
ATOM   2614  OD1 ASN A 337       0.099 -29.869  -3.251  1.00 40.20           O  
ATOM   2615  ND2 ASN A 337       0.198 -30.220  -5.468  1.00 39.16           N  
ATOM   2616  N   ASP A 338      -4.027 -33.016  -2.650  1.00 40.78           N  
ATOM   2617  CA  ASP A 338      -5.458 -33.153  -2.400  1.00 43.46           C  
ATOM   2618  C   ASP A 338      -5.742 -33.679  -0.999  1.00 42.04           C  
ATOM   2619  O   ASP A 338      -6.899 -33.820  -0.606  1.00 43.13           O  
ATOM   2620  CB  ASP A 338      -6.100 -34.071  -3.440  1.00 46.77           C  
ATOM   2621  CG  ASP A 338      -6.191 -33.424  -4.804  1.00 51.57           C  
ATOM   2622  OD1 ASP A 338      -6.226 -32.177  -4.868  1.00 51.94           O  
ATOM   2623  OD2 ASP A 338      -6.232 -34.164  -5.812  1.00 55.05           O  
ATOM   2624  N   LYS A 339      -4.685 -33.976  -0.252  1.00 38.60           N  
ATOM   2625  CA  LYS A 339      -4.832 -34.380   1.139  1.00 38.59           C  
ATOM   2626  C   LYS A 339      -5.423 -33.235   1.954  1.00 39.17           C  
ATOM   2627  O   LYS A 339      -5.152 -32.065   1.678  1.00 40.23           O  
ATOM   2628  CB  LYS A 339      -3.487 -34.808   1.726  1.00 38.31           C  
ATOM   2629  CG  LYS A 339      -2.972 -36.144   1.211  1.00 38.81           C  
ATOM   2630  CD  LYS A 339      -3.767 -37.301   1.794  1.00 40.08           C  
ATOM   2631  CE  LYS A 339      -3.053 -38.628   1.577  1.00 40.67           C  
ATOM   2632  NZ  LYS A 339      -3.778 -39.757   2.222  1.00 41.39           N  
ATOM   2633  N   GLU A 340      -6.234 -33.573   2.950  1.00 39.24           N  
ATOM   2634  CA  GLU A 340      -6.863 -32.564   3.794  1.00 40.91           C  
ATOM   2635  C   GLU A 340      -5.960 -32.160   4.954  1.00 39.95           C  
ATOM   2636  O   GLU A 340      -5.321 -33.006   5.579  1.00 39.72           O  
ATOM   2637  CB  GLU A 340      -8.199 -33.076   4.332  1.00 44.02           C  
ATOM   2638  CG  GLU A 340      -8.946 -32.067   5.182  1.00 47.38           C  
ATOM   2639  CD  GLU A 340     -10.241 -32.621   5.737  1.00 51.60           C  
ATOM   2640  OE1 GLU A 340     -10.434 -33.854   5.677  1.00 52.86           O  
ATOM   2641  OE2 GLU A 340     -11.067 -31.823   6.231  1.00 53.53           O  
ATOM   2642  N   LEU A 341      -5.909 -30.863   5.236  1.00 40.32           N  
ATOM   2643  CA  LEU A 341      -5.149 -30.361   6.372  1.00 39.06           C  
ATOM   2644  C   LEU A 341      -5.995 -30.425   7.636  1.00 41.10           C  
ATOM   2645  O   LEU A 341      -7.180 -30.088   7.618  1.00 42.44           O  
ATOM   2646  CB  LEU A 341      -4.681 -28.922   6.134  1.00 38.21           C  
ATOM   2647  CG  LEU A 341      -4.026 -28.549   4.802  1.00 37.68           C  
ATOM   2648  CD1 LEU A 341      -3.384 -27.176   4.909  1.00 37.77           C  
ATOM   2649  CD2 LEU A 341      -3.007 -29.580   4.376  1.00 36.42           C  
ATOM   2650  N   PHE A 342      -5.386 -30.862   8.732  1.00 41.49           N  
ATOM   2651  CA  PHE A 342      -6.068 -30.872  10.020  1.00 42.57           C  
ATOM   2652  C   PHE A 342      -5.078 -30.617  11.152  1.00 43.56           C  
ATOM   2653  O   PHE A 342      -3.866 -30.618  10.935  1.00 43.33           O  
ATOM   2654  CB  PHE A 342      -6.811 -32.195  10.235  1.00 42.12           C  
ATOM   2655  CG  PHE A 342      -5.909 -33.378  10.443  1.00 40.40           C  
ATOM   2656  CD1 PHE A 342      -5.281 -33.986   9.368  1.00 38.89           C  
ATOM   2657  CD2 PHE A 342      -5.707 -33.896  11.714  1.00 39.83           C  
ATOM   2658  CE1 PHE A 342      -4.458 -35.078   9.557  1.00 38.92           C  
ATOM   2659  CE2 PHE A 342      -4.885 -34.989  11.911  1.00 39.21           C  
ATOM   2660  CZ  PHE A 342      -4.259 -35.581  10.833  1.00 39.38           C  
ATOM   2661  N   ASN A 343      -5.611 -30.399  12.353  1.00 44.68           N  
ATOM   2662  CA  ASN A 343      -4.813 -30.025  13.519  1.00 44.04           C  
ATOM   2663  C   ASN A 343      -3.979 -28.768  13.276  1.00 42.81           C  
ATOM   2664  O   ASN A 343      -2.827 -28.685  13.702  1.00 42.92           O  
ATOM   2665  CB  ASN A 343      -3.904 -31.182  13.949  1.00 44.45           C  
ATOM   2666  CG  ASN A 343      -4.598 -32.157  14.881  1.00 46.40           C  
ATOM   2667  OD1 ASN A 343      -5.816 -32.112  15.050  1.00 48.07           O  
ATOM   2668  ND2 ASN A 343      -3.823 -33.045  15.494  1.00 46.65           N  
ATOM   2669  N   ARG A 344      -4.568 -27.799  12.581  1.00 42.02           N  
ATOM   2670  CA  ARG A 344      -3.947 -26.491  12.391  1.00 41.36           C  
ATOM   2671  C   ARG A 344      -3.731 -25.809  13.741  1.00 41.88           C  
ATOM   2672  O   ARG A 344      -4.661 -25.702  14.541  1.00 42.98           O  
ATOM   2673  CB  ARG A 344      -4.812 -25.605  11.494  1.00 41.21           C  
ATOM   2674  CG  ARG A 344      -5.050 -26.135  10.089  1.00 41.38           C  
ATOM   2675  CD  ARG A 344      -6.018 -25.223   9.347  1.00 43.80           C  
ATOM   2676  NE  ARG A 344      -6.314 -25.683   7.993  1.00 45.03           N  
ATOM   2677  CZ  ARG A 344      -7.337 -26.471   7.677  1.00 45.81           C  
ATOM   2678  NH1 ARG A 344      -8.166 -26.896   8.621  1.00 46.63           N  
ATOM   2679  NH2 ARG A 344      -7.528 -26.836   6.416  1.00 45.36           N  
ATOM   2680  N   ALA A 345      -2.513 -25.344  13.998  1.00 40.36           N  
ATOM   2681  CA  ALA A 345      -2.218 -24.739  15.293  1.00 40.92           C  
ATOM   2682  C   ALA A 345      -1.108 -23.698  15.234  1.00 39.24           C  
ATOM   2683  O   ALA A 345      -0.346 -23.632  14.269  1.00 39.84           O  
ATOM   2684  CB  ALA A 345      -1.860 -25.821  16.301  1.00 41.26           C  
HETATM 2685  N   MSE A 346      -1.032 -22.885  16.283  1.00 37.72           N  
HETATM 2686  CA  MSE A 346       0.036 -21.905  16.436  1.00 36.32           C  
HETATM 2687  C   MSE A 346       0.911 -22.274  17.634  1.00 36.37           C  
HETATM 2688  O   MSE A 346       0.406 -22.610  18.705  1.00 36.69           O  
HETATM 2689  CB  MSE A 346      -0.538 -20.494  16.601  1.00 36.04           C  
HETATM 2690  CG  MSE A 346      -1.210 -19.954  15.355  1.00 36.31           C  
HETATM 2691 SE   MSE A 346      -2.063 -18.210  15.639  1.00 72.61          SE  
HETATM 2692  CE  MSE A 346      -3.539 -18.755  16.796  1.00 41.57           C  
ATOM   2693  N   CYS A 347       2.224 -22.217  17.445  1.00 35.64           N  
ATOM   2694  CA  CYS A 347       3.174 -22.555  18.501  1.00 33.84           C  
ATOM   2695  C   CYS A 347       3.992 -21.321  18.883  1.00 33.20           C  
ATOM   2696  O   CYS A 347       4.491 -20.607  18.014  1.00 35.78           O  
ATOM   2697  CB  CYS A 347       4.078 -23.705  18.047  1.00 32.45           C  
ATOM   2698  SG  CYS A 347       5.740 -23.718  18.738  1.00 60.40           S  
ATOM   2699  N   TRP A 348       4.127 -21.072  20.181  1.00 31.88           N  
ATOM   2700  CA  TRP A 348       4.702 -19.815  20.654  1.00 33.83           C  
ATOM   2701  C   TRP A 348       6.123 -19.935  21.199  1.00 32.92           C  
ATOM   2702  O   TRP A 348       6.437 -20.834  21.980  1.00 33.11           O  
ATOM   2703  CB  TRP A 348       3.802 -19.202  21.729  1.00 34.64           C  
ATOM   2704  CG  TRP A 348       2.434 -18.865  21.228  1.00 35.46           C  
ATOM   2705  CD1 TRP A 348       1.357 -19.701  21.164  1.00 35.55           C  
ATOM   2706  CD2 TRP A 348       1.993 -17.602  20.715  1.00 36.57           C  
ATOM   2707  NE1 TRP A 348       0.274 -19.037  20.645  1.00 36.93           N  
ATOM   2708  CE2 TRP A 348       0.637 -17.747  20.361  1.00 37.34           C  
ATOM   2709  CE3 TRP A 348       2.613 -16.363  20.522  1.00 37.70           C  
ATOM   2710  CZ2 TRP A 348      -0.112 -16.701  19.824  1.00 38.63           C  
ATOM   2711  CZ3 TRP A 348       1.867 -15.323  19.988  1.00 39.39           C  
ATOM   2712  CH2 TRP A 348       0.518 -15.500  19.646  1.00 39.73           C  
ATOM   2713  N   CYS A 349       6.970 -19.003  20.780  1.00 30.97           N  
ATOM   2714  CA  CYS A 349       8.325 -18.875  21.298  1.00 30.51           C  
ATOM   2715  C   CYS A 349       8.562 -17.417  21.665  1.00 31.75           C  
ATOM   2716  O   CYS A 349       7.688 -16.579  21.458  1.00 33.70           O  
ATOM   2717  CB  CYS A 349       9.351 -19.343  20.269  1.00 30.52           C  
ATOM   2718  SG  CYS A 349       9.129 -21.042  19.713  1.00 37.10           S  
ATOM   2719  N   THR A 350       9.734 -17.107  22.209  1.00 30.82           N  
ATOM   2720  CA  THR A 350      10.066 -15.721  22.512  1.00 31.63           C  
ATOM   2721  C   THR A 350      11.476 -15.407  22.001  1.00 31.73           C  
ATOM   2722  O   THR A 350      12.424 -16.157  22.237  1.00 31.33           O  
ATOM   2723  CB  THR A 350       9.916 -15.417  24.039  1.00 30.53           C  
ATOM   2724  OG1 THR A 350       9.893 -14.003  24.256  1.00 32.92           O  
ATOM   2725  CG2 THR A 350      11.030 -16.044  24.869  1.00 30.07           C  
ATOM   2726  N   ASP A 351      11.592 -14.311  21.256  1.00 32.25           N  
ATOM   2727  CA  ASP A 351      12.849 -13.936  20.613  1.00 34.09           C  
ATOM   2728  C   ASP A 351      13.639 -12.927  21.439  1.00 35.80           C  
ATOM   2729  O   ASP A 351      13.063 -12.024  22.043  1.00 37.36           O  
ATOM   2730  CB  ASP A 351      12.592 -13.342  19.220  1.00 36.38           C  
ATOM   2731  CG  ASP A 351      12.459 -14.399  18.136  1.00 36.83           C  
ATOM   2732  OD1 ASP A 351      12.876 -15.553  18.366  1.00 37.56           O  
ATOM   2733  OD2 ASP A 351      11.952 -14.068  17.041  1.00 36.30           O  
ATOM   2734  N   THR A 352      14.959 -13.080  21.460  1.00 34.79           N  
ATOM   2735  CA  THR A 352      15.833 -12.008  21.920  1.00 35.69           C  
ATOM   2736  C   THR A 352      16.390 -11.293  20.695  1.00 37.40           C  
ATOM   2737  O   THR A 352      16.178 -11.733  19.564  1.00 36.96           O  
ATOM   2738  CB  THR A 352      16.996 -12.519  22.798  1.00 35.34           C  
ATOM   2739  OG1 THR A 352      17.825 -13.403  22.034  1.00 35.38           O  
ATOM   2740  CG2 THR A 352      16.470 -13.246  24.028  1.00 34.36           C  
ATOM   2741  N   ALA A 353      17.102 -10.194  20.919  1.00 39.40           N  
ATOM   2742  CA  ALA A 353      17.639  -9.396  19.823  1.00 40.02           C  
ATOM   2743  C   ALA A 353      18.671 -10.172  19.008  1.00 40.12           C  
ATOM   2744  O   ALA A 353      18.618 -10.181  17.778  1.00 40.38           O  
ATOM   2745  CB  ALA A 353      18.248  -8.112  20.357  1.00 41.42           C  
ATOM   2746  N   ASP A 354      19.602 -10.826  19.696  1.00 40.25           N  
ATOM   2747  CA  ASP A 354      20.694 -11.530  19.029  1.00 41.64           C  
ATOM   2748  C   ASP A 354      20.468 -13.041  18.947  1.00 40.53           C  
ATOM   2749  O   ASP A 354      21.359 -13.780  18.524  1.00 41.52           O  
ATOM   2750  CB  ASP A 354      22.019 -11.240  19.741  1.00 42.73           C  
ATOM   2751  CG  ASP A 354      22.024 -11.707  21.185  1.00 44.08           C  
ATOM   2752  OD1 ASP A 354      20.944 -12.055  21.707  1.00 44.59           O  
ATOM   2753  OD2 ASP A 354      23.110 -11.715  21.803  1.00 45.02           O  
ATOM   2754  N   ALA A 355      19.280 -13.480  19.360  1.00 38.46           N  
ATOM   2755  CA  ALA A 355      18.882 -14.894  19.362  1.00 37.00           C  
ATOM   2756  C   ALA A 355      19.677 -15.746  20.360  1.00 34.63           C  
ATOM   2757  O   ALA A 355      19.623 -16.974  20.316  1.00 31.77           O  
ATOM   2758  CB  ALA A 355      18.989 -15.488  17.954  1.00 37.03           C  
ATOM   2759  N   ASN A 356      20.408 -15.092  21.259  1.00 35.25           N  
ATOM   2760  CA  ASN A 356      21.007 -15.782  22.395  1.00 33.89           C  
ATOM   2761  C   ASN A 356      19.955 -15.996  23.476  1.00 32.63           C  
ATOM   2762  O   ASN A 356      18.926 -15.321  23.488  1.00 31.64           O  
ATOM   2763  CB  ASN A 356      22.193 -14.994  22.963  1.00 35.67           C  
ATOM   2764  CG  ASN A 356      23.526 -15.414  22.362  1.00 36.58           C  
ATOM   2765  OD1 ASN A 356      23.771 -16.594  22.112  1.00 35.80           O  
ATOM   2766  ND2 ASN A 356      24.401 -14.441  22.139  1.00 38.15           N  
ATOM   2767  N   LEU A 357      20.212 -16.935  24.380  1.00 32.68           N  
ATOM   2768  CA  LEU A 357      19.287 -17.208  25.474  1.00 30.78           C  
ATOM   2769  C   LEU A 357      19.330 -16.100  26.518  1.00 32.57           C  
ATOM   2770  O   LEU A 357      20.279 -15.317  26.572  1.00 34.66           O  
ATOM   2771  CB  LEU A 357      19.610 -18.552  26.131  1.00 28.95           C  
ATOM   2772  CG  LEU A 357      19.484 -19.824  25.288  1.00 27.22           C  
ATOM   2773  CD1 LEU A 357      19.886 -21.041  26.103  1.00 25.34           C  
ATOM   2774  CD2 LEU A 357      18.074 -19.986  24.746  1.00 24.92           C  
ATOM   2775  N   LEU A 358      18.288 -16.030  27.339  1.00 31.73           N  
ATOM   2776  CA  LEU A 358      18.293 -15.150  28.497  1.00 32.06           C  
ATOM   2777  C   LEU A 358      18.311 -16.009  29.753  1.00 33.60           C  
ATOM   2778  O   LEU A 358      17.261 -16.368  30.292  1.00 33.67           O  
ATOM   2779  CB  LEU A 358      17.085 -14.216  28.493  1.00 31.41           C  
ATOM   2780  CG  LEU A 358      17.034 -13.214  29.650  1.00 33.10           C  
ATOM   2781  CD1 LEU A 358      18.197 -12.230  29.577  1.00 31.90           C  
ATOM   2782  CD2 LEU A 358      15.702 -12.483  29.682  1.00 30.92           C  
ATOM   2783  N   VAL A 359      19.514 -16.360  30.196  1.00 34.06           N  
ATOM   2784  CA  VAL A 359      19.688 -17.211  31.367  1.00 33.63           C  
ATOM   2785  C   VAL A 359      20.597 -16.528  32.381  1.00 35.26           C  
ATOM   2786  O   VAL A 359      21.822 -16.562  32.257  1.00 35.24           O  
ATOM   2787  CB  VAL A 359      20.277 -18.585  30.997  1.00 31.88           C  
ATOM   2788  CG1 VAL A 359      20.356 -19.470  32.228  1.00 31.17           C  
ATOM   2789  CG2 VAL A 359      19.442 -19.255  29.915  1.00 29.25           C  
ATOM   2790  N   CYS A 360      19.990 -15.912  33.388  1.00 36.81           N  
ATOM   2791  CA  CYS A 360      20.739 -15.111  34.344  1.00 38.87           C  
ATOM   2792  C   CYS A 360      19.940 -14.848  35.614  1.00 39.75           C  
ATOM   2793  O   CYS A 360      18.711 -14.914  35.614  1.00 39.68           O  
ATOM   2794  CB  CYS A 360      21.138 -13.780  33.712  1.00 39.66           C  
ATOM   2795  SG  CYS A 360      19.721 -12.728  33.315  1.00 37.61           S  
ATOM   2796  N   GLU A 361      20.644 -14.541  36.697  1.00 40.99           N  
ATOM   2797  CA  GLU A 361      19.987 -14.100  37.918  1.00 42.53           C  
ATOM   2798  C   GLU A 361      19.420 -12.704  37.694  1.00 43.50           C  
ATOM   2799  O   GLU A 361      20.002 -11.906  36.959  1.00 43.86           O  
ATOM   2800  CB  GLU A 361      20.959 -14.103  39.102  1.00 43.50           C  
ATOM   2801  CG  GLU A 361      20.298 -13.838  40.449  1.00 44.78           C  
ATOM   2802  CD  GLU A 361      21.282 -13.867  41.604  1.00 46.81           C  
ATOM   2803  OE1 GLU A 361      22.480 -13.597  41.380  1.00 48.33           O  
ATOM   2804  OE2 GLU A 361      20.856 -14.165  42.740  1.00 47.28           O  
ATOM   2805  N   HIS A 362      18.279 -12.417  38.311  1.00 43.29           N  
ATOM   2806  CA  HIS A 362      17.681 -11.094  38.217  1.00 43.29           C  
ATOM   2807  C   HIS A 362      18.624 -10.066  38.837  1.00 44.85           C  
ATOM   2808  O   HIS A 362      19.197 -10.311  39.896  1.00 46.27           O  
ATOM   2809  CB  HIS A 362      16.314 -11.070  38.907  1.00 42.56           C  
ATOM   2810  CG  HIS A 362      15.473  -9.887  38.543  1.00 42.83           C  
ATOM   2811  ND1 HIS A 362      15.597  -8.664  39.170  1.00 44.76           N  
ATOM   2812  CD2 HIS A 362      14.496  -9.737  37.619  1.00 42.22           C  
ATOM   2813  CE1 HIS A 362      14.733  -7.814  38.646  1.00 45.18           C  
ATOM   2814  NE2 HIS A 362      14.053  -8.440  37.702  1.00 44.07           N  
ATOM   2815  N   PRO A 363      18.800  -8.916  38.166  1.00 45.32           N  
ATOM   2816  CA  PRO A 363      19.719  -7.863  38.615  1.00 46.91           C  
ATOM   2817  C   PRO A 363      19.455  -7.383  40.042  1.00 49.60           C  
ATOM   2818  O   PRO A 363      20.404  -7.122  40.779  1.00 51.83           O  
ATOM   2819  CB  PRO A 363      19.472  -6.728  37.610  1.00 47.03           C  
ATOM   2820  CG  PRO A 363      18.175  -7.067  36.933  1.00 45.81           C  
ATOM   2821  CD  PRO A 363      18.135  -8.555  36.904  1.00 44.61           C  
ATOM   2822  N   ARG A 364      18.187  -7.274  40.425  1.00 49.21           N  
ATOM   2823  CA  ARG A 364      17.839  -6.782  41.753  1.00 49.89           C  
ATOM   2824  C   ARG A 364      17.320  -7.898  42.655  1.00 49.25           C  
ATOM   2825  O   ARG A 364      17.674  -7.975  43.831  1.00 50.57           O  
ATOM   2826  CB  ARG A 364      16.798  -5.665  41.652  1.00 50.88           C  
ATOM   2827  CG  ARG A 364      16.423  -5.044  42.989  1.00 52.68           C  
ATOM   2828  CD  ARG A 364      15.455  -3.889  42.808  1.00 55.08           C  
ATOM   2829  NE  ARG A 364      15.130  -3.239  44.076  1.00 58.41           N  
ATOM   2830  CZ  ARG A 364      15.816  -2.224  44.596  1.00 61.08           C  
ATOM   2831  NH1 ARG A 364      16.873  -1.736  43.960  1.00 62.28           N  
ATOM   2832  NH2 ARG A 364      15.446  -1.696  45.755  1.00 61.64           N  
ATOM   2833  N   TRP A 365      16.481  -8.763  42.098  1.00 47.27           N  
ATOM   2834  CA  TRP A 365      15.862  -9.831  42.874  1.00 45.75           C  
ATOM   2835  C   TRP A 365      16.823 -10.990  43.098  1.00 45.00           C  
ATOM   2836  O   TRP A 365      16.757 -12.000  42.399  1.00 43.96           O  
ATOM   2837  CB  TRP A 365      14.600 -10.332  42.176  1.00 38.09           C  
ATOM   2838  CG  TRP A 365      13.605  -9.254  41.887  1.00 42.20           C  
ATOM   2839  CD1 TRP A 365      13.528  -8.025  42.478  1.00 40.77           C  
ATOM   2840  CD2 TRP A 365      12.545  -9.303  40.925  1.00 41.47           C  
ATOM   2841  NE1 TRP A 365      12.482  -7.309  41.947  1.00 43.97           N  
ATOM   2842  CE2 TRP A 365      11.863  -8.072  40.990  1.00 42.63           C  
ATOM   2843  CE3 TRP A 365      12.104 -10.271  40.016  1.00 40.57           C  
ATOM   2844  CZ2 TRP A 365      10.767  -7.782  40.182  1.00 42.88           C  
ATOM   2845  CZ3 TRP A 365      11.015  -9.982  39.215  1.00 41.01           C  
ATOM   2846  CH2 TRP A 365      10.360  -8.747  39.303  1.00 42.16           C  
ATOM   2847  N   LYS A 366      17.713 -10.842  44.075  1.00 46.31           N  
ATOM   2848  CA  LYS A 366      18.670 -11.895  44.403  1.00 45.00           C  
ATOM   2849  C   LYS A 366      17.946 -13.172  44.815  1.00 43.17           C  
ATOM   2850  O   LYS A 366      17.077 -13.150  45.686  1.00 45.08           O  
ATOM   2851  CB  LYS A 366      19.619 -11.435  45.512  1.00 46.57           C  
ATOM   2852  CG  LYS A 366      20.588 -10.339  45.089  1.00 48.88           C  
ATOM   2853  CD  LYS A 366      21.539 -10.829  44.004  1.00 50.81           C  
ATOM   2854  CE  LYS A 366      22.479  -9.723  43.535  1.00 54.21           C  
ATOM   2855  NZ  LYS A 366      21.752  -8.619  42.847  1.00 56.06           N  
ATOM   2856  N   GLY A 367      18.301 -14.282  44.177  1.00 40.07           N  
ATOM   2857  CA  GLY A 367      17.634 -15.547  44.424  1.00 38.43           C  
ATOM   2858  C   GLY A 367      16.604 -15.862  43.357  1.00 38.28           C  
ATOM   2859  O   GLY A 367      16.097 -16.982  43.281  1.00 36.87           O  
ATOM   2860  N   PHE A 368      16.293 -14.866  42.531  1.00 39.00           N  
ATOM   2861  CA  PHE A 368      15.357 -15.041  41.423  1.00 38.20           C  
ATOM   2862  C   PHE A 368      16.115 -15.144  40.102  1.00 37.60           C  
ATOM   2863  O   PHE A 368      16.854 -14.231  39.732  1.00 38.25           O  
ATOM   2864  CB  PHE A 368      14.356 -13.882  41.375  1.00 37.61           C  
ATOM   2865  CG  PHE A 368      13.168 -14.139  40.490  1.00 35.56           C  
ATOM   2866  CD1 PHE A 368      13.250 -13.956  39.117  1.00 32.98           C  
ATOM   2867  CD2 PHE A 368      11.966 -14.554  41.033  1.00 33.73           C  
ATOM   2868  CE1 PHE A 368      12.155 -14.191  38.305  1.00 32.39           C  
ATOM   2869  CE2 PHE A 368      10.868 -14.788  40.227  1.00 34.34           C  
ATOM   2870  CZ  PHE A 368      10.964 -14.606  38.861  1.00 32.51           C  
ATOM   2871  N   TYR A 369      15.920 -16.249  39.390  1.00 36.43           N  
ATOM   2872  CA  TYR A 369      16.688 -16.521  38.177  1.00 37.60           C  
ATOM   2873  C   TYR A 369      15.797 -16.647  36.944  1.00 37.37           C  
ATOM   2874  O   TYR A 369      14.658 -17.099  37.036  1.00 38.03           O  
ATOM   2875  CB  TYR A 369      17.516 -17.797  38.356  1.00 37.32           C  
ATOM   2876  CG  TYR A 369      18.553 -17.714  39.457  1.00 39.43           C  
ATOM   2877  CD1 TYR A 369      18.183 -17.765  40.797  1.00 40.33           C  
ATOM   2878  CD2 TYR A 369      19.903 -17.598  39.156  1.00 40.15           C  
ATOM   2879  CE1 TYR A 369      19.126 -17.692  41.803  1.00 41.63           C  
ATOM   2880  CE2 TYR A 369      20.854 -17.526  40.156  1.00 41.53           C  
ATOM   2881  CZ  TYR A 369      20.461 -17.573  41.478  1.00 42.18           C  
ATOM   2882  OH  TYR A 369      21.407 -17.501  42.475  1.00 42.84           O  
ATOM   2883  N   LEU A 370      16.321 -16.245  35.791  1.00 37.63           N  
ATOM   2884  CA  LEU A 370      15.572 -16.320  34.540  1.00 38.43           C  
ATOM   2885  C   LEU A 370      16.147 -17.391  33.618  1.00 37.40           C  
ATOM   2886  O   LEU A 370      17.360 -17.475  33.435  1.00 38.16           O  
ATOM   2887  CB  LEU A 370      15.577 -14.963  33.831  1.00 40.73           C  
ATOM   2888  CG  LEU A 370      15.039 -13.769  34.625  1.00 43.69           C  
ATOM   2889  CD1 LEU A 370      15.628 -12.477  34.096  1.00 45.61           C  
ATOM   2890  CD2 LEU A 370      13.520 -13.717  34.568  1.00 43.26           C  
ATOM   2891  N   ALA A 371      15.270 -18.211  33.046  1.00 35.33           N  
ATOM   2892  CA  ALA A 371      15.681 -19.236  32.093  1.00 33.95           C  
ATOM   2893  C   ALA A 371      14.773 -19.215  30.867  1.00 33.96           C  
ATOM   2894  O   ALA A 371      13.965 -20.122  30.661  1.00 33.67           O  
ATOM   2895  CB  ALA A 371      15.665 -20.612  32.742  1.00 32.56           C  
ATOM   2896  N   THR A 372      14.914 -18.176  30.054  1.00 33.84           N  
ATOM   2897  CA  THR A 372      14.051 -18.002  28.895  1.00 33.30           C  
ATOM   2898  C   THR A 372      14.849 -17.477  27.696  1.00 32.91           C  
ATOM   2899  O   THR A 372      16.073 -17.598  27.660  1.00 31.86           O  
ATOM   2900  CB  THR A 372      12.877 -17.049  29.224  1.00 32.96           C  
ATOM   2901  OG1 THR A 372      11.985 -16.965  28.105  1.00 32.05           O  
ATOM   2902  CG2 THR A 372      13.391 -15.658  29.588  1.00 33.30           C  
ATOM   2903  N   GLY A 373      14.152 -16.906  26.718  1.00 34.46           N  
ATOM   2904  CA  GLY A 373      14.793 -16.383  25.524  1.00 35.90           C  
ATOM   2905  C   GLY A 373      15.173 -17.475  24.540  1.00 34.78           C  
ATOM   2906  O   GLY A 373      16.233 -17.416  23.917  1.00 35.55           O  
ATOM   2907  N   ASP A 374      14.295 -18.465  24.396  1.00 32.53           N  
ATOM   2908  CA  ASP A 374      14.545 -19.637  23.557  1.00 33.27           C  
ATOM   2909  C   ASP A 374      14.812 -19.298  22.086  1.00 33.03           C  
ATOM   2910  O   ASP A 374      15.545 -20.017  21.401  1.00 31.89           O  
ATOM   2911  CB  ASP A 374      13.359 -20.598  23.647  1.00 34.50           C  
ATOM   2912  CG  ASP A 374      12.124 -20.064  22.943  1.00 36.37           C  
ATOM   2913  OD1 ASP A 374      11.410 -19.225  23.531  1.00 36.46           O  
ATOM   2914  OD2 ASP A 374      11.874 -20.482  21.795  1.00 36.76           O  
ATOM   2915  N   SER A 375      14.201 -18.213  21.614  1.00 33.74           N  
ATOM   2916  CA  SER A 375      14.376 -17.720  20.247  1.00 34.21           C  
ATOM   2917  C   SER A 375      14.017 -18.753  19.173  1.00 34.86           C  
ATOM   2918  O   SER A 375      14.559 -18.725  18.067  1.00 34.32           O  
ATOM   2919  CB  SER A 375      15.811 -17.232  20.047  1.00 34.15           C  
ATOM   2920  OG  SER A 375      16.133 -16.231  20.998  1.00 34.69           O  
ATOM   2921  N   GLY A 376      13.098 -19.656  19.507  1.00 35.09           N  
ATOM   2922  CA  GLY A 376      12.553 -20.607  18.552  1.00 34.59           C  
ATOM   2923  C   GLY A 376      13.513 -21.631  17.972  1.00 36.01           C  
ATOM   2924  O   GLY A 376      13.310 -22.102  16.856  1.00 36.31           O  
ATOM   2925  N   HIS A 377      14.550 -21.990  18.722  1.00 38.43           N  
ATOM   2926  CA  HIS A 377      15.520 -22.975  18.248  1.00 39.01           C  
ATOM   2927  C   HIS A 377      16.195 -23.717  19.400  1.00 36.19           C  
ATOM   2928  O   HIS A 377      17.352 -24.123  19.284  1.00 35.77           O  
ATOM   2929  CB  HIS A 377      16.582 -22.295  17.375  1.00 43.01           C  
ATOM   2930  CG  HIS A 377      17.357 -21.229  18.085  1.00 48.56           C  
ATOM   2931  ND1 HIS A 377      18.214 -21.501  19.132  1.00 50.86           N  
ATOM   2932  CD2 HIS A 377      17.401 -19.888  17.906  1.00 51.19           C  
ATOM   2933  CE1 HIS A 377      18.750 -20.376  19.565  1.00 51.86           C  
ATOM   2934  NE2 HIS A 377      18.274 -19.380  18.838  1.00 52.70           N  
ATOM   2935  N   SER A 378      15.479 -23.899  20.505  1.00 33.53           N  
ATOM   2936  CA  SER A 378      16.111 -24.403  21.719  1.00 32.62           C  
ATOM   2937  C   SER A 378      15.574 -25.735  22.237  1.00 32.49           C  
ATOM   2938  O   SER A 378      16.085 -26.251  23.230  1.00 34.01           O  
ATOM   2939  CB  SER A 378      16.000 -23.360  22.831  1.00 32.54           C  
ATOM   2940  OG  SER A 378      16.913 -22.296  22.618  1.00 33.13           O  
ATOM   2941  N   PHE A 379      14.564 -26.306  21.587  1.00 29.99           N  
ATOM   2942  CA  PHE A 379      14.096 -27.614  22.033  1.00 29.33           C  
ATOM   2943  C   PHE A 379      15.179 -28.678  21.858  1.00 29.98           C  
ATOM   2944  O   PHE A 379      15.200 -29.679  22.577  1.00 29.43           O  
ATOM   2945  CB  PHE A 379      12.834 -28.066  21.301  1.00 29.30           C  
ATOM   2946  CG  PHE A 379      12.310 -29.372  21.815  1.00 30.44           C  
ATOM   2947  CD1 PHE A 379      11.526 -29.407  22.956  1.00 31.27           C  
ATOM   2948  CD2 PHE A 379      12.660 -30.570  21.209  1.00 30.54           C  
ATOM   2949  CE1 PHE A 379      11.069 -30.604  23.462  1.00 30.88           C  
ATOM   2950  CE2 PHE A 379      12.208 -31.772  21.716  1.00 30.29           C  
ATOM   2951  CZ  PHE A 379      11.415 -31.785  22.847  1.00 30.63           C  
ATOM   2952  N   LYS A 380      16.073 -28.463  20.898  1.00 30.13           N  
ATOM   2953  CA  LYS A 380      17.204 -29.359  20.689  1.00 30.70           C  
ATOM   2954  C   LYS A 380      18.099 -29.416  21.929  1.00 29.27           C  
ATOM   2955  O   LYS A 380      18.886 -30.345  22.098  1.00 28.54           O  
ATOM   2956  CB  LYS A 380      18.016 -28.914  19.467  1.00 32.98           C  
ATOM   2957  CG  LYS A 380      18.716 -27.566  19.629  1.00 35.52           C  
ATOM   2958  CD  LYS A 380      19.395 -27.125  18.338  1.00 38.13           C  
ATOM   2959  CE  LYS A 380      18.379 -26.898  17.225  1.00 42.23           C  
ATOM   2960  NZ  LYS A 380      19.020 -26.438  15.959  1.00 46.14           N  
ATOM   2961  N   LEU A 381      17.964 -28.415  22.794  1.00 28.60           N  
ATOM   2962  CA  LEU A 381      18.805 -28.302  23.977  1.00 27.72           C  
ATOM   2963  C   LEU A 381      18.147 -28.903  25.218  1.00 27.95           C  
ATOM   2964  O   LEU A 381      18.648 -28.735  26.328  1.00 29.62           O  
ATOM   2965  CB  LEU A 381      19.158 -26.835  24.236  1.00 26.07           C  
ATOM   2966  CG  LEU A 381      19.845 -26.086  23.093  1.00 25.78           C  
ATOM   2967  CD1 LEU A 381      20.164 -24.658  23.507  1.00 25.58           C  
ATOM   2968  CD2 LEU A 381      21.107 -26.810  22.641  1.00 26.23           C  
ATOM   2969  N   LEU A 382      17.034 -29.605  25.024  1.00 26.36           N  
ATOM   2970  CA  LEU A 382      16.328 -30.261  26.128  1.00 26.88           C  
ATOM   2971  C   LEU A 382      17.219 -31.129  27.031  1.00 29.96           C  
ATOM   2972  O   LEU A 382      17.081 -31.074  28.253  1.00 31.41           O  
ATOM   2973  CB  LEU A 382      15.175 -31.120  25.595  1.00 25.98           C  
ATOM   2974  CG  LEU A 382      14.384 -31.895  26.661  1.00 26.49           C  
ATOM   2975  CD1 LEU A 382      13.501 -30.957  27.476  1.00 26.74           C  
ATOM   2976  CD2 LEU A 382      13.560 -33.022  26.051  1.00 26.26           C  
ATOM   2977  N   PRO A 383      18.131 -31.937  26.451  1.00 30.97           N  
ATOM   2978  CA  PRO A 383      18.897 -32.780  27.380  1.00 31.24           C  
ATOM   2979  C   PRO A 383      19.948 -32.038  28.206  1.00 30.76           C  
ATOM   2980  O   PRO A 383      20.231 -32.461  29.326  1.00 30.75           O  
ATOM   2981  CB  PRO A 383      19.588 -33.792  26.454  1.00 31.85           C  
ATOM   2982  CG  PRO A 383      18.837 -33.727  25.164  1.00 31.66           C  
ATOM   2983  CD  PRO A 383      18.387 -32.311  25.048  1.00 30.54           C  
ATOM   2984  N   ASN A 384      20.517 -30.958  27.680  1.00 30.32           N  
ATOM   2985  CA  ASN A 384      21.696 -30.379  28.319  1.00 31.45           C  
ATOM   2986  C   ASN A 384      21.544 -28.968  28.889  1.00 31.16           C  
ATOM   2987  O   ASN A 384      22.397 -28.524  29.660  1.00 33.91           O  
ATOM   2988  CB  ASN A 384      22.867 -30.385  27.333  1.00 33.05           C  
ATOM   2989  CG  ASN A 384      22.582 -29.582  26.081  1.00 32.99           C  
ATOM   2990  OD1 ASN A 384      21.488 -29.648  25.521  1.00 33.14           O  
ATOM   2991  ND2 ASN A 384      23.570 -28.815  25.635  1.00 32.82           N  
ATOM   2992  N   ILE A 385      20.476 -28.262  28.527  1.00 27.85           N  
ATOM   2993  CA  ILE A 385      20.330 -26.873  28.960  1.00 27.92           C  
ATOM   2994  C   ILE A 385      20.149 -26.768  30.481  1.00 28.35           C  
ATOM   2995  O   ILE A 385      20.589 -25.797  31.097  1.00 27.26           O  
ATOM   2996  CB  ILE A 385      19.152 -26.166  28.235  1.00 23.73           C  
ATOM   2997  CG1 ILE A 385      19.172 -24.663  28.516  1.00 24.13           C  
ATOM   2998  CG2 ILE A 385      17.812 -26.770  28.631  1.00 25.65           C  
ATOM   2999  CD1 ILE A 385      20.490 -23.997  28.183  1.00 24.86           C  
ATOM   3000  N   GLY A 386      19.534 -27.781  31.085  1.00 30.16           N  
ATOM   3001  CA  GLY A 386      19.268 -27.771  32.513  1.00 32.99           C  
ATOM   3002  C   GLY A 386      20.529 -27.857  33.353  1.00 35.99           C  
ATOM   3003  O   GLY A 386      20.561 -27.395  34.493  1.00 36.62           O  
ATOM   3004  N   LYS A 387      21.568 -28.455  32.779  1.00 36.71           N  
ATOM   3005  CA  LYS A 387      22.859 -28.589  33.440  1.00 37.59           C  
ATOM   3006  C   LYS A 387      23.519 -27.226  33.660  1.00 36.75           C  
ATOM   3007  O   LYS A 387      24.123 -26.982  34.704  1.00 38.57           O  
ATOM   3008  CB  LYS A 387      23.770 -29.503  32.616  1.00 41.23           C  
ATOM   3009  CG  LYS A 387      25.235 -29.482  33.012  1.00 45.32           C  
ATOM   3010  CD  LYS A 387      26.038 -30.435  32.144  1.00 48.19           C  
ATOM   3011  CE  LYS A 387      27.531 -30.292  32.395  1.00 51.72           C  
ATOM   3012  NZ  LYS A 387      28.050 -28.970  31.940  1.00 53.57           N  
ATOM   3013  N   HIS A 388      23.389 -26.336  32.682  1.00 35.05           N  
ATOM   3014  CA  HIS A 388      23.993 -25.010  32.774  1.00 35.15           C  
ATOM   3015  C   HIS A 388      23.176 -24.067  33.658  1.00 35.79           C  
ATOM   3016  O   HIS A 388      23.729 -23.167  34.290  1.00 37.42           O  
ATOM   3017  CB  HIS A 388      24.170 -24.406  31.379  1.00 34.24           C  
ATOM   3018  CG  HIS A 388      24.956 -25.271  30.447  1.00 34.73           C  
ATOM   3019  ND1 HIS A 388      26.279 -25.599  30.670  1.00 35.58           N  
ATOM   3020  CD2 HIS A 388      24.610 -25.887  29.292  1.00 34.37           C  
ATOM   3021  CE1 HIS A 388      26.709 -26.375  29.695  1.00 36.18           C  
ATOM   3022  NE2 HIS A 388      25.716 -26.565  28.842  1.00 35.12           N  
ATOM   3023  N   VAL A 389      21.862 -24.272  33.698  1.00 34.10           N  
ATOM   3024  CA  VAL A 389      21.000 -23.492  34.581  1.00 33.29           C  
ATOM   3025  C   VAL A 389      21.368 -23.770  36.036  1.00 33.52           C  
ATOM   3026  O   VAL A 389      21.413 -22.857  36.861  1.00 33.77           O  
ATOM   3027  CB  VAL A 389      19.502 -23.808  34.354  1.00 30.86           C  
ATOM   3028  CG1 VAL A 389      18.636 -23.057  35.352  1.00 29.73           C  
ATOM   3029  CG2 VAL A 389      19.097 -23.458  32.937  1.00 29.06           C  
ATOM   3030  N   VAL A 390      21.643 -25.037  36.338  1.00 33.02           N  
ATOM   3031  CA  VAL A 390      22.080 -25.432  37.673  1.00 33.93           C  
ATOM   3032  C   VAL A 390      23.426 -24.787  38.008  1.00 36.65           C  
ATOM   3033  O   VAL A 390      23.629 -24.293  39.120  1.00 36.83           O  
ATOM   3034  CB  VAL A 390      22.191 -26.966  37.802  1.00 31.76           C  
ATOM   3035  CG1 VAL A 390      22.870 -27.346  39.108  1.00 32.44           C  
ATOM   3036  CG2 VAL A 390      20.815 -27.610  37.711  1.00 29.81           C  
ATOM   3037  N   GLU A 391      24.336 -24.790  37.036  1.00 37.46           N  
ATOM   3038  CA  GLU A 391      25.639 -24.149  37.189  1.00 39.08           C  
ATOM   3039  C   GLU A 391      25.478 -22.665  37.497  1.00 39.86           C  
ATOM   3040  O   GLU A 391      26.227 -22.100  38.298  1.00 40.99           O  
ATOM   3041  CB  GLU A 391      26.484 -24.340  35.926  1.00 40.10           C  
ATOM   3042  CG  GLU A 391      26.960 -25.769  35.713  1.00 41.36           C  
ATOM   3043  CD  GLU A 391      27.319 -26.066  34.267  1.00 42.76           C  
ATOM   3044  OE1 GLU A 391      27.254 -25.140  33.429  1.00 43.22           O  
ATOM   3045  OE2 GLU A 391      27.660 -27.230  33.968  1.00 43.10           O  
ATOM   3046  N   LEU A 392      24.494 -22.040  36.857  1.00 38.55           N  
ATOM   3047  CA  LEU A 392      24.162 -20.647  37.128  1.00 38.61           C  
ATOM   3048  C   LEU A 392      23.733 -20.456  38.583  1.00 39.68           C  
ATOM   3049  O   LEU A 392      24.209 -19.549  39.263  1.00 40.81           O  
ATOM   3050  CB  LEU A 392      23.055 -20.167  36.186  1.00 36.21           C  
ATOM   3051  CG  LEU A 392      22.510 -18.762  36.448  1.00 36.55           C  
ATOM   3052  CD1 LEU A 392      23.544 -17.710  36.094  1.00 37.13           C  
ATOM   3053  CD2 LEU A 392      21.227 -18.535  35.673  1.00 35.68           C  
ATOM   3054  N   LEU A 393      22.836 -21.320  39.050  1.00 38.57           N  
ATOM   3055  CA  LEU A 393      22.328 -21.244  40.417  1.00 38.19           C  
ATOM   3056  C   LEU A 393      23.446 -21.390  41.439  1.00 39.24           C  
ATOM   3057  O   LEU A 393      23.393 -20.796  42.514  1.00 40.23           O  
ATOM   3058  CB  LEU A 393      21.270 -22.322  40.664  1.00 37.78           C  
ATOM   3059  CG  LEU A 393      19.988 -22.286  39.831  1.00 36.70           C  
ATOM   3060  CD1 LEU A 393      19.147 -23.522  40.103  1.00 35.66           C  
ATOM   3061  CD2 LEU A 393      19.195 -21.030  40.126  1.00 36.44           C  
ATOM   3062  N   GLU A 394      24.458 -22.182  41.100  1.00 39.27           N  
ATOM   3063  CA  GLU A 394      25.547 -22.463  42.028  1.00 39.23           C  
ATOM   3064  C   GLU A 394      26.766 -21.579  41.760  1.00 40.87           C  
ATOM   3065  O   GLU A 394      27.805 -21.730  42.400  1.00 41.96           O  
ATOM   3066  CB  GLU A 394      25.931 -23.944  41.954  1.00 36.87           C  
ATOM   3067  CG  GLU A 394      24.797 -24.888  42.335  1.00 35.09           C  
ATOM   3068  CD  GLU A 394      25.178 -26.353  42.220  1.00 35.01           C  
ATOM   3069  OE1 GLU A 394      26.223 -26.656  41.604  1.00 33.78           O  
ATOM   3070  OE2 GLU A 394      24.431 -27.202  42.748  1.00 33.35           O  
ATOM   3071  N   GLY A 395      26.629 -20.654  40.815  1.00 40.76           N  
ATOM   3072  CA  GLY A 395      27.705 -19.739  40.480  1.00 40.15           C  
ATOM   3073  C   GLY A 395      28.890 -20.419  39.820  1.00 40.43           C  
ATOM   3074  O   GLY A 395      30.039 -20.060  40.079  1.00 40.37           O  
ATOM   3075  N   ARG A 396      28.616 -21.397  38.961  1.00 40.29           N  
ATOM   3076  CA  ARG A 396      29.680 -22.139  38.291  1.00 41.75           C  
ATOM   3077  C   ARG A 396      29.534 -22.117  36.772  1.00 43.46           C  
ATOM   3078  O   ARG A 396      30.133 -22.934  36.073  1.00 45.25           O  
ATOM   3079  CB  ARG A 396      29.707 -23.589  38.780  1.00 40.67           C  
ATOM   3080  CG  ARG A 396      29.977 -23.744  40.265  1.00 41.47           C  
ATOM   3081  CD  ARG A 396      30.005 -25.211  40.674  1.00 41.84           C  
ATOM   3082  NE  ARG A 396      28.721 -25.875  40.456  1.00 40.10           N  
ATOM   3083  CZ  ARG A 396      28.476 -26.729  39.468  1.00 38.74           C  
ATOM   3084  NH1 ARG A 396      29.429 -27.037  38.600  1.00 39.22           N  
ATOM   3085  NH2 ARG A 396      27.276 -27.280  39.352  1.00 37.93           N  
ATOM   3086  N   LEU A 397      28.731 -21.191  36.261  1.00 43.21           N  
ATOM   3087  CA  LEU A 397      28.513 -21.098  34.823  1.00 43.38           C  
ATOM   3088  C   LEU A 397      29.724 -20.454  34.156  1.00 49.52           C  
ATOM   3089  O   LEU A 397      30.172 -19.387  34.574  1.00 50.65           O  
ATOM   3090  CB  LEU A 397      27.240 -20.301  34.517  1.00 39.38           C  
ATOM   3091  CG  LEU A 397      26.805 -20.197  33.052  1.00 37.28           C  
ATOM   3092  CD1 LEU A 397      26.515 -21.574  32.471  1.00 35.85           C  
ATOM   3093  CD2 LEU A 397      25.591 -19.289  32.909  1.00 35.84           C  
ATOM   3094  N   GLU A 398      30.258 -21.107  33.128  1.00 53.03           N  
ATOM   3095  CA  GLU A 398      31.428 -20.586  32.428  1.00 57.05           C  
ATOM   3096  C   GLU A 398      31.072 -19.312  31.673  1.00 56.12           C  
ATOM   3097  O   GLU A 398      29.927 -19.125  31.262  1.00 55.38           O  
ATOM   3098  CB  GLU A 398      32.003 -21.631  31.472  1.00 62.10           C  
ATOM   3099  CG  GLU A 398      33.495 -21.881  31.662  1.00 68.81           C  
ATOM   3100  CD  GLU A 398      34.345 -20.650  31.381  1.00 74.27           C  
ATOM   3101  OE1 GLU A 398      34.331 -20.167  30.227  1.00 75.83           O  
ATOM   3102  OE2 GLU A 398      35.027 -20.164  32.312  1.00 75.55           O  
ATOM   3103  N   SER A 399      32.062 -18.443  31.496  1.00 55.74           N  
ATOM   3104  CA  SER A 399      31.844 -17.120  30.921  1.00 55.32           C  
ATOM   3105  C   SER A 399      31.312 -17.162  29.491  1.00 54.39           C  
ATOM   3106  O   SER A 399      30.585 -16.263  29.074  1.00 55.13           O  
ATOM   3107  CB  SER A 399      33.142 -16.309  30.965  1.00 57.53           C  
ATOM   3108  OG  SER A 399      34.205 -17.010  30.343  1.00 59.45           O  
ATOM   3109  N   VAL A 400      31.665 -18.201  28.742  1.00 53.27           N  
ATOM   3110  CA  VAL A 400      31.221 -18.308  27.356  1.00 52.50           C  
ATOM   3111  C   VAL A 400      29.694 -18.394  27.287  1.00 51.01           C  
ATOM   3112  O   VAL A 400      29.082 -17.944  26.318  1.00 51.65           O  
ATOM   3113  CB  VAL A 400      31.859 -19.527  26.643  1.00 59.44           C  
ATOM   3114  CG1 VAL A 400      31.404 -20.835  27.278  1.00 58.66           C  
ATOM   3115  CG2 VAL A 400      31.540 -19.508  25.154  1.00 58.64           C  
ATOM   3116  N   PHE A 401      29.082 -18.945  28.332  1.00 48.55           N  
ATOM   3117  CA  PHE A 401      27.629 -19.021  28.413  1.00 46.09           C  
ATOM   3118  C   PHE A 401      27.068 -17.827  29.174  1.00 45.68           C  
ATOM   3119  O   PHE A 401      26.049 -17.256  28.790  1.00 45.85           O  
ATOM   3120  CB  PHE A 401      27.189 -20.321  29.088  1.00 45.28           C  
ATOM   3121  CG  PHE A 401      27.555 -21.560  28.323  1.00 44.82           C  
ATOM   3122  CD1 PHE A 401      27.480 -21.586  26.942  1.00 44.24           C  
ATOM   3123  CD2 PHE A 401      27.979 -22.699  28.986  1.00 44.72           C  
ATOM   3124  CE1 PHE A 401      27.817 -22.724  26.238  1.00 44.07           C  
ATOM   3125  CE2 PHE A 401      28.319 -23.840  28.288  1.00 44.47           C  
ATOM   3126  CZ  PHE A 401      28.237 -23.853  26.912  1.00 44.42           C  
ATOM   3127  N   LYS A 402      27.745 -17.456  30.255  1.00 46.05           N  
ATOM   3128  CA  LYS A 402      27.267 -16.402  31.141  1.00 46.78           C  
ATOM   3129  C   LYS A 402      27.229 -15.043  30.449  1.00 47.70           C  
ATOM   3130  O   LYS A 402      26.332 -14.238  30.699  1.00 47.28           O  
ATOM   3131  CB  LYS A 402      28.142 -16.327  32.395  1.00 48.22           C  
ATOM   3132  CG  LYS A 402      27.614 -15.379  33.457  1.00 49.82           C  
ATOM   3133  CD  LYS A 402      28.548 -15.297  34.654  1.00 52.44           C  
ATOM   3134  CE  LYS A 402      28.001 -14.348  35.709  1.00 54.21           C  
ATOM   3135  NZ  LYS A 402      28.915 -14.217  36.878  1.00 57.00           N  
ATOM   3136  N   ASP A 403      28.203 -14.792  29.580  1.00 49.42           N  
ATOM   3137  CA  ASP A 403      28.290 -13.518  28.874  1.00 51.37           C  
ATOM   3138  C   ASP A 403      27.199 -13.369  27.820  1.00 51.10           C  
ATOM   3139  O   ASP A 403      26.613 -12.297  27.672  1.00 52.54           O  
ATOM   3140  CB  ASP A 403      29.664 -13.359  28.219  1.00 54.29           C  
ATOM   3141  CG  ASP A 403      30.786 -13.256  29.235  1.00 57.25           C  
ATOM   3142  OD1 ASP A 403      30.499 -12.913  30.401  1.00 57.50           O  
ATOM   3143  OD2 ASP A 403      31.952 -13.515  28.869  1.00 58.77           O  
ATOM   3144  N   ALA A 404      26.927 -14.447  27.092  1.00 49.01           N  
ATOM   3145  CA  ALA A 404      25.944 -14.408  26.015  1.00 47.37           C  
ATOM   3146  C   ALA A 404      24.518 -14.410  26.550  1.00 47.11           C  
ATOM   3147  O   ALA A 404      23.606 -13.893  25.905  1.00 48.49           O  
ATOM   3148  CB  ALA A 404      26.150 -15.581  25.068  1.00 45.83           C  
ATOM   3149  N   TRP A 405      24.330 -14.993  27.730  1.00 44.71           N  
ATOM   3150  CA  TRP A 405      22.999 -15.135  28.312  1.00 43.64           C  
ATOM   3151  C   TRP A 405      22.704 -14.048  29.338  1.00 46.81           C  
ATOM   3152  O   TRP A 405      21.688 -14.099  30.030  1.00 46.98           O  
ATOM   3153  CB  TRP A 405      22.844 -16.510  28.968  1.00 40.15           C  
ATOM   3154  CG  TRP A 405      23.035 -17.663  28.036  1.00 37.79           C  
ATOM   3155  CD1 TRP A 405      23.022 -17.629  26.671  1.00 36.90           C  
ATOM   3156  CD2 TRP A 405      23.273 -19.027  28.400  1.00 36.09           C  
ATOM   3157  NE1 TRP A 405      23.234 -18.888  26.164  1.00 35.59           N  
ATOM   3158  CE2 TRP A 405      23.391 -19.765  27.206  1.00 35.44           C  
ATOM   3159  CE3 TRP A 405      23.395 -19.697  29.622  1.00 35.54           C  
ATOM   3160  CZ2 TRP A 405      23.627 -21.138  27.197  1.00 35.46           C  
ATOM   3161  CZ3 TRP A 405      23.628 -21.059  29.612  1.00 34.80           C  
ATOM   3162  CH2 TRP A 405      23.743 -21.765  28.408  1.00 35.18           C  
ATOM   3163  N   ARG A 406      23.593 -13.064  29.427  1.00 49.71           N  
ATOM   3164  CA  ARG A 406      23.504 -12.036  30.459  1.00 52.50           C  
ATOM   3165  C   ARG A 406      22.261 -11.157  30.329  1.00 51.79           C  
ATOM   3166  O   ARG A 406      21.649 -11.069  29.263  1.00 52.90           O  
ATOM   3167  CB  ARG A 406      24.752 -11.152  30.428  1.00 56.85           C  
ATOM   3168  CG  ARG A 406      24.724 -10.105  29.327  1.00 59.24           C  
ATOM   3169  CD  ARG A 406      26.072  -9.426  29.144  1.00 63.11           C  
ATOM   3170  NE  ARG A 406      25.988  -8.332  28.180  1.00 68.02           N  
ATOM   3171  CZ  ARG A 406      25.978  -8.495  26.860  1.00 71.12           C  
ATOM   3172  NH1 ARG A 406      26.043  -9.712  26.337  1.00 71.46           N  
ATOM   3173  NH2 ARG A 406      25.897  -7.438  26.064  1.00 73.05           N  
ATOM   3174  N   TRP A 407      21.896 -10.519  31.437  1.00 49.89           N  
ATOM   3175  CA  TRP A 407      20.859  -9.495  31.452  1.00 49.17           C  
ATOM   3176  C   TRP A 407      21.304  -8.337  30.563  1.00 50.83           C  
ATOM   3177  O   TRP A 407      22.329  -7.711  30.827  1.00 52.81           O  
ATOM   3178  CB  TRP A 407      20.603  -9.035  32.892  1.00 37.16           C  
ATOM   3179  CG  TRP A 407      19.561  -7.970  33.055  1.00 44.41           C  
ATOM   3180  CD1 TRP A 407      19.773  -6.624  33.130  1.00 39.87           C  
ATOM   3181  CD2 TRP A 407      18.146  -8.161  33.198  1.00 37.29           C  
ATOM   3182  NE1 TRP A 407      18.579  -5.964  33.296  1.00 41.67           N  
ATOM   3183  CE2 TRP A 407      17.566  -6.885  33.341  1.00 38.77           C  
ATOM   3184  CE3 TRP A 407      17.315  -9.285  33.213  1.00 35.69           C  
ATOM   3185  CZ2 TRP A 407      16.192  -6.703  33.493  1.00 44.87           C  
ATOM   3186  CZ3 TRP A 407      15.953  -9.101  33.366  1.00 35.61           C  
ATOM   3187  CH2 TRP A 407      15.405  -7.822  33.503  1.00 37.11           C  
ATOM   3188  N   ARG A 408      20.549  -8.060  29.503  1.00 50.14           N  
ATOM   3189  CA  ARG A 408      20.993  -7.093  28.500  1.00 51.00           C  
ATOM   3190  C   ARG A 408      19.872  -6.262  27.858  1.00 51.93           C  
ATOM   3191  O   ARG A 408      19.654  -6.335  26.646  1.00 51.18           O  
ATOM   3192  CB  ARG A 408      21.776  -7.827  27.401  1.00 49.19           C  
ATOM   3193  CG  ARG A 408      21.057  -9.040  26.804  1.00 44.90           C  
ATOM   3194  CD  ARG A 408      21.965  -9.820  25.864  1.00 42.87           C  
ATOM   3195  NE  ARG A 408      21.225 -10.751  25.013  1.00 40.47           N  
ATOM   3196  CZ  ARG A 408      20.820 -11.959  25.394  1.00 38.43           C  
ATOM   3197  NH1 ARG A 408      21.071 -12.393  26.623  1.00 39.58           N  
ATOM   3198  NH2 ARG A 408      20.157 -12.735  24.548  1.00 35.23           N  
ATOM   3199  N   PRO A 409      19.170  -5.445  28.660  1.00 52.95           N  
ATOM   3200  CA  PRO A 409      18.113  -4.612  28.078  1.00 54.49           C  
ATOM   3201  C   PRO A 409      18.671  -3.522  27.164  1.00 58.39           C  
ATOM   3202  O   PRO A 409      19.743  -2.978  27.431  1.00 60.82           O  
ATOM   3203  CB  PRO A 409      17.430  -4.003  29.307  1.00 54.00           C  
ATOM   3204  CG  PRO A 409      18.489  -3.986  30.349  1.00 53.45           C  
ATOM   3205  CD  PRO A 409      19.322  -5.213  30.107  1.00 52.33           C  
ATOM   3206  N   GLY A 410      17.951  -3.218  26.090  1.00 58.98           N  
ATOM   3207  CA  GLY A 410      18.371  -2.191  25.156  1.00 61.10           C  
ATOM   3208  C   GLY A 410      19.580  -2.598  24.336  1.00 63.61           C  
ATOM   3209  O   GLY A 410      20.428  -1.768  24.013  1.00 66.51           O  
ATOM   3210  N   SER A 411      19.661  -3.880  23.996  1.00 61.78           N  
ATOM   3211  CA  SER A 411      20.772  -4.387  23.199  1.00 61.19           C  
ATOM   3212  C   SER A 411      20.344  -4.656  21.761  1.00 60.53           C  
ATOM   3213  O   SER A 411      21.085  -5.263  20.989  1.00 61.41           O  
ATOM   3214  CB  SER A 411      21.342  -5.662  23.822  1.00 59.13           C  
ATOM   3215  OG  SER A 411      20.355  -6.674  23.903  1.00 57.91           O  
ATOM   3216  N   GLY A 412      19.148  -4.202  21.403  1.00 60.30           N  
ATOM   3217  CA  GLY A 412      18.642  -4.394  20.057  1.00 59.77           C  
ATOM   3218  C   GLY A 412      17.149  -4.650  20.011  1.00 59.21           C  
ATOM   3219  O   GLY A 412      16.495  -4.759  21.048  1.00 60.21           O  
ATOM   3220  N   ASP A 413      16.612  -4.756  18.800  1.00 58.02           N  
ATOM   3221  CA  ASP A 413      15.178  -4.931  18.601  1.00 56.78           C  
ATOM   3222  C   ASP A 413      14.799  -6.403  18.450  1.00 52.86           C  
ATOM   3223  O   ASP A 413      15.145  -7.044  17.458  1.00 53.43           O  
ATOM   3224  CB  ASP A 413      14.721  -4.142  17.374  1.00 59.51           C  
ATOM   3225  CG  ASP A 413      13.226  -4.219  17.155  1.00 60.80           C  
ATOM   3226  OD1 ASP A 413      12.484  -4.349  18.150  1.00 61.16           O  
ATOM   3227  OD2 ASP A 413      12.792  -4.147  15.986  1.00 61.96           O  
ATOM   3228  N   ALA A 414      14.078  -6.932  19.433  1.00 49.83           N  
ATOM   3229  CA  ALA A 414      13.706  -8.343  19.431  1.00 47.53           C  
ATOM   3230  C   ALA A 414      12.468  -8.612  18.577  1.00 46.69           C  
ATOM   3231  O   ALA A 414      12.120  -9.767  18.326  1.00 45.28           O  
ATOM   3232  CB  ALA A 414      13.478  -8.830  20.856  1.00 46.15           C  
ATOM   3233  N   LEU A 415      11.801  -7.547  18.140  1.00 47.71           N  
ATOM   3234  CA  LEU A 415      10.613  -7.684  17.303  1.00 48.48           C  
ATOM   3235  C   LEU A 415      10.994  -8.160  15.904  1.00 49.05           C  
ATOM   3236  O   LEU A 415      10.240  -8.883  15.252  1.00 47.16           O  
ATOM   3237  CB  LEU A 415       9.850  -6.361  17.225  1.00 49.63           C  
ATOM   3238  CG  LEU A 415       8.538  -6.385  16.436  1.00 49.53           C  
ATOM   3239  CD1 LEU A 415       7.571  -7.389  17.040  1.00 36.35           C  
ATOM   3240  CD2 LEU A 415       7.912  -5.003  16.385  1.00 40.02           C  
ATOM   3241  N   LYS A 416      12.170  -7.744  15.449  1.00 50.71           N  
ATOM   3242  CA  LYS A 416      12.713  -8.211  14.182  1.00 50.42           C  
ATOM   3243  C   LYS A 416      13.694  -9.349  14.436  1.00 49.07           C  
ATOM   3244  O   LYS A 416      13.735 -10.327  13.687  1.00 47.30           O  
ATOM   3245  CB  LYS A 416      13.395  -7.064  13.431  1.00 52.92           C  
ATOM   3246  CG  LYS A 416      14.297  -7.505  12.290  1.00 53.96           C  
ATOM   3247  CD  LYS A 416      14.862  -6.311  11.535  1.00 58.13           C  
ATOM   3248  CE  LYS A 416      15.998  -6.723  10.610  1.00 59.99           C  
ATOM   3249  NZ  LYS A 416      15.633  -7.899   9.771  1.00 59.88           N  
ATOM   3250  N   SER A 417      14.467  -9.210  15.512  1.00 49.32           N  
ATOM   3251  CA  SER A 417      15.481 -10.187  15.902  1.00 49.26           C  
ATOM   3252  C   SER A 417      16.474 -10.437  14.771  1.00 50.87           C  
ATOM   3253  O   SER A 417      16.865  -9.510  14.063  1.00 52.17           O  
ATOM   3254  CB  SER A 417      14.826 -11.501  16.335  1.00 46.68           C  
ATOM   3255  OG  SER A 417      15.792 -12.413  16.831  1.00 45.88           O  
ATOM   3256  N   ARG A 418      16.877 -11.692  14.605  1.00 51.21           N  
ATOM   3257  CA  ARG A 418      17.801 -12.065  13.540  1.00 52.79           C  
ATOM   3258  C   ARG A 418      17.034 -12.493  12.292  1.00 49.99           C  
ATOM   3259  O   ARG A 418      17.617 -12.999  11.331  1.00 50.05           O  
ATOM   3260  CB  ARG A 418      18.728 -13.191  14.001  1.00 55.84           C  
ATOM   3261  CG  ARG A 418      19.517 -12.873  15.263  1.00 60.08           C  
ATOM   3262  CD  ARG A 418      20.605 -11.847  15.002  1.00 65.00           C  
ATOM   3263  NE  ARG A 418      21.654 -12.381  14.140  1.00 68.90           N  
ATOM   3264  CZ  ARG A 418      22.707 -13.062  14.580  1.00 71.59           C  
ATOM   3265  NH1 ARG A 418      22.856 -13.293  15.878  1.00 71.62           N  
ATOM   3266  NH2 ARG A 418      23.614 -13.512  13.722  1.00 73.91           N  
ATOM   3267  N   ARG A 419      15.724 -12.276  12.313  1.00 46.02           N  
ATOM   3268  CA  ARG A 419      14.854 -12.731  11.239  1.00 42.73           C  
ATOM   3269  C   ARG A 419      14.738 -11.692  10.124  1.00 43.53           C  
ATOM   3270  O   ARG A 419      15.230 -10.570  10.253  1.00 46.14           O  
ATOM   3271  CB  ARG A 419      13.479 -13.087  11.807  1.00 41.39           C  
ATOM   3272  CG  ARG A 419      13.571 -13.994  13.033  1.00 40.29           C  
ATOM   3273  CD  ARG A 419      12.236 -14.607  13.428  1.00 39.22           C  
ATOM   3274  NE  ARG A 419      12.352 -15.381  14.663  1.00 37.82           N  
ATOM   3275  CZ  ARG A 419      12.734 -16.654  14.719  1.00 35.32           C  
ATOM   3276  NH1 ARG A 419      13.030 -17.311  13.606  1.00 33.88           N  
ATOM   3277  NH2 ARG A 419      12.812 -17.276  15.888  1.00 34.00           N  
ATOM   3278  N   ALA A 420      14.087 -12.080   9.031  1.00 42.20           N  
ATOM   3279  CA  ALA A 420      14.043 -11.270   7.813  1.00 41.59           C  
ATOM   3280  C   ALA A 420      13.277  -9.960   7.982  1.00 43.92           C  
ATOM   3281  O   ALA A 420      13.632  -8.945   7.378  1.00 46.90           O  
ATOM   3282  CB  ALA A 420      13.436 -12.080   6.672  1.00 38.11           C  
ATOM   3283  N   ALA A 421      12.227  -9.984   8.795  1.00 42.39           N  
ATOM   3284  CA  ALA A 421      11.362  -8.819   8.957  1.00 43.24           C  
ATOM   3285  C   ALA A 421      10.786  -8.731  10.368  1.00 42.53           C  
ATOM   3286  O   ALA A 421      10.743  -9.732  11.085  1.00 34.54           O  
ATOM   3287  CB  ALA A 421      10.236  -8.861   7.932  1.00 36.96           C  
ATOM   3288  N   PRO A 422      10.355  -7.526  10.777  1.00 43.13           N  
ATOM   3289  CA  PRO A 422       9.592  -7.400  12.022  1.00 42.72           C  
ATOM   3290  C   PRO A 422       8.324  -8.243  11.960  1.00 41.62           C  
ATOM   3291  O   PRO A 422       7.675  -8.287  10.917  1.00 42.88           O  
ATOM   3292  CB  PRO A 422       9.258  -5.907  12.084  1.00 39.68           C  
ATOM   3293  CG  PRO A 422      10.314  -5.251  11.269  1.00 43.72           C  
ATOM   3294  CD  PRO A 422      10.639  -6.214  10.169  1.00 44.15           C  
ATOM   3295  N   ALA A 423       7.986  -8.913  13.054  1.00 40.97           N  
ATOM   3296  CA  ALA A 423       6.809  -9.769  13.080  1.00 40.99           C  
ATOM   3297  C   ALA A 423       5.528  -8.949  12.971  1.00 42.97           C  
ATOM   3298  O   ALA A 423       5.424  -7.864  13.543  1.00 43.36           O  
ATOM   3299  CB  ALA A 423       6.794 -10.608  14.347  1.00 40.13           C  
ATOM   3300  N   LYS A 424       4.561  -9.468  12.222  1.00 44.24           N  
ATOM   3301  CA  LYS A 424       3.248  -8.841  12.134  1.00 46.48           C  
ATOM   3302  C   LYS A 424       2.381  -9.327  13.289  1.00 46.08           C  
ATOM   3303  O   LYS A 424       2.687 -10.342  13.914  1.00 44.74           O  
ATOM   3304  CB  LYS A 424       2.584  -9.151  10.793  1.00 47.12           C  
ATOM   3305  CG  LYS A 424       3.354  -8.632   9.590  1.00 48.79           C  
ATOM   3306  CD  LYS A 424       2.693  -9.059   8.293  1.00 51.12           C  
ATOM   3307  CE  LYS A 424       3.452  -8.548   7.077  1.00 54.59           C  
ATOM   3308  NZ  LYS A 424       2.809  -8.987   5.804  1.00 56.00           N  
ATOM   3309  N   ASP A 425       1.303  -8.605  13.576  1.00 47.61           N  
ATOM   3310  CA  ASP A 425       0.436  -8.964  14.692  1.00 47.37           C  
ATOM   3311  C   ASP A 425      -0.843  -9.646  14.218  1.00 46.31           C  
ATOM   3312  O   ASP A 425      -1.334  -9.371  13.125  1.00 46.82           O  
ATOM   3313  CB  ASP A 425       0.092  -7.727  15.523  1.00 48.93           C  
ATOM   3314  CG  ASP A 425      -0.575  -8.079  16.835  1.00 49.14           C  
ATOM   3315  OD1 ASP A 425      -1.821  -8.086  16.890  1.00 50.35           O  
ATOM   3316  OD2 ASP A 425       0.149  -8.359  17.812  1.00 48.43           O  
ATOM   3317  N   LEU A 426      -1.382 -10.531  15.054  1.00 45.60           N  
ATOM   3318  CA  LEU A 426      -2.584 -11.286  14.711  1.00 44.25           C  
ATOM   3319  C   LEU A 426      -3.813 -10.392  14.549  1.00 45.96           C  
ATOM   3320  O   LEU A 426      -4.798 -10.791  13.931  1.00 46.49           O  
ATOM   3321  CB  LEU A 426      -2.861 -12.358  15.769  1.00 41.71           C  
ATOM   3322  CG  LEU A 426      -1.919 -13.564  15.831  1.00 38.28           C  
ATOM   3323  CD1 LEU A 426      -2.360 -14.526  16.924  1.00 36.81           C  
ATOM   3324  CD2 LEU A 426      -1.850 -14.274  14.488  1.00 35.28           C  
ATOM   3325  N   ALA A 427      -3.754  -9.182  15.097  1.00 46.53           N  
ATOM   3326  CA  ALA A 427      -4.865  -8.241  14.971  1.00 50.26           C  
ATOM   3327  C   ALA A 427      -4.972  -7.687  13.550  1.00 52.88           C  
ATOM   3328  O   ALA A 427      -5.944  -7.013  13.209  1.00 54.93           O  
ATOM   3329  CB  ALA A 427      -4.716  -7.104  15.970  1.00 42.99           C  
ATOM   3330  N   ASP A 428      -3.968  -7.972  12.726  1.00 52.93           N  
ATOM   3331  CA  ASP A 428      -3.949  -7.496  11.349  1.00 54.29           C  
ATOM   3332  C   ASP A 428      -4.072  -8.650  10.357  1.00 53.13           C  
ATOM   3333  O   ASP A 428      -4.114  -8.440   9.146  1.00 53.10           O  
ATOM   3334  CB  ASP A 428      -2.670  -6.702  11.082  1.00 54.71           C  
ATOM   3335  CG  ASP A 428      -2.537  -5.489  11.985  1.00 55.93           C  
ATOM   3336  OD1 ASP A 428      -3.566  -4.849  12.287  1.00 56.24           O  
ATOM   3337  OD2 ASP A 428      -1.400  -5.178  12.395  1.00 56.69           O  
HETATM 3338  N   MSE A 429      -4.132  -9.869  10.883  1.00 52.70           N  
HETATM 3339  CA  MSE A 429      -4.293 -11.063  10.061  1.00 52.00           C  
HETATM 3340  C   MSE A 429      -5.685 -11.652  10.255  1.00 53.84           C  
HETATM 3341  O   MSE A 429      -6.061 -11.993  11.374  1.00 54.69           O  
HETATM 3342  CB  MSE A 429      -3.231 -12.107  10.411  1.00 49.74           C  
HETATM 3343  CG  MSE A 429      -1.824 -11.547  10.585  1.00 49.74           C  
HETATM 3344 SE   MSE A 429      -1.100 -10.735   8.966  1.00 70.18          SE  
HETATM 3345  CE  MSE A 429      -1.210 -12.272   7.771  1.00 35.20           C  
ATOM   3346  N   PRO A 430      -6.463 -11.760   9.170  1.00 55.33           N  
ATOM   3347  CA  PRO A 430      -7.810 -12.333   9.265  1.00 57.19           C  
ATOM   3348  C   PRO A 430      -7.839 -13.847   9.049  1.00 56.93           C  
ATOM   3349  O   PRO A 430      -7.041 -14.373   8.272  1.00 55.49           O  
ATOM   3350  CB  PRO A 430      -8.561 -11.614   8.147  1.00 58.49           C  
ATOM   3351  CG  PRO A 430      -7.513 -11.385   7.106  1.00 57.69           C  
ATOM   3352  CD  PRO A 430      -6.211 -11.163   7.846  1.00 56.46           C  
ATOM   3353  N   GLY A 431      -8.748 -14.533   9.738  1.00 58.29           N  
ATOM   3354  CA  GLY A 431      -8.985 -15.943   9.488  1.00 58.07           C  
ATOM   3355  C   GLY A 431      -8.773 -16.890  10.655  1.00 58.14           C  
ATOM   3356  O   GLY A 431      -9.421 -17.933  10.729  1.00 59.25           O  
ATOM   3357  N   TRP A 432      -7.872 -16.538  11.566  1.00 58.18           N  
ATOM   3358  CA  TRP A 432      -7.469 -17.459  12.629  1.00 57.91           C  
ATOM   3359  C   TRP A 432      -8.514 -17.610  13.729  1.00 62.40           C  
ATOM   3360  O   TRP A 432      -8.517 -18.606  14.452  1.00 60.65           O  
ATOM   3361  CB  TRP A 432      -6.141 -17.014  13.246  1.00 55.73           C  
ATOM   3362  CG  TRP A 432      -6.127 -15.595  13.703  1.00 55.61           C  
ATOM   3363  CD1 TRP A 432      -5.930 -14.491  12.931  1.00 56.02           C  
ATOM   3364  CD2 TRP A 432      -6.304 -15.122  15.043  1.00 54.92           C  
ATOM   3365  NE1 TRP A 432      -5.979 -13.357  13.704  1.00 56.54           N  
ATOM   3366  CE2 TRP A 432      -6.207 -13.718  15.006  1.00 55.42           C  
ATOM   3367  CE3 TRP A 432      -6.538 -15.749  16.270  1.00 53.33           C  
ATOM   3368  CZ2 TRP A 432      -6.338 -12.930  16.146  1.00 55.84           C  
ATOM   3369  CZ3 TRP A 432      -6.664 -14.967  17.400  1.00 53.53           C  
ATOM   3370  CH2 TRP A 432      -6.565 -13.572  17.331  1.00 55.04           C  
ATOM   3371  N   ARG A 433      -9.397 -16.627  13.857  1.00 66.73           N  
ATOM   3372  CA  ARG A 433     -10.407 -16.664  14.907  1.00 69.23           C  
ATOM   3373  C   ARG A 433     -11.762 -17.097  14.359  1.00 70.92           C  
ATOM   3374  O   ARG A 433     -12.337 -18.086  14.813  1.00 71.14           O  
ATOM   3375  CB  ARG A 433     -10.525 -15.300  15.587  1.00 71.62           C  
ATOM   3376  CG  ARG A 433     -11.243 -15.346  16.922  1.00 74.60           C  
ATOM   3377  CD  ARG A 433     -11.271 -13.982  17.590  1.00 77.68           C  
ATOM   3378  NE  ARG A 433     -11.786 -14.058  18.954  1.00 80.02           N  
ATOM   3379  CZ  ARG A 433     -11.995 -13.003  19.733  1.00 83.35           C  
ATOM   3380  NH1 ARG A 433     -11.738 -11.782  19.282  1.00 85.33           N  
ATOM   3381  NH2 ARG A 433     -12.465 -13.165  20.963  1.00 84.45           N  
TER    3382      ARG A 433                                                      
HETATM 3383  PA  FAD A 501       8.041 -23.908  26.904  1.00 27.76           P  
HETATM 3384  O1A FAD A 501       8.198 -25.284  26.726  1.00 27.12           O  
HETATM 3385  O2A FAD A 501       6.952 -23.343  26.260  1.00 30.40           O  
HETATM 3386  O5B FAD A 501       7.936 -23.581  28.319  1.00 40.45           O  
HETATM 3387  C5B FAD A 501       6.915 -22.817  28.909  1.00 41.75           C  
HETATM 3388  C4B FAD A 501       6.244 -23.434  30.124  1.00 43.45           C  
HETATM 3389  O4B FAD A 501       5.829 -22.403  30.964  1.00 41.76           O  
HETATM 3390  C3B FAD A 501       4.974 -24.109  29.712  1.00 43.56           C  
HETATM 3391  O3B FAD A 501       4.848 -25.237  30.479  1.00 43.92           O  
HETATM 3392  C2B FAD A 501       3.939 -23.172  30.165  1.00 43.75           C  
HETATM 3393  O2B FAD A 501       2.809 -23.892  30.508  1.00 43.27           O  
HETATM 3394  C1B FAD A 501       4.574 -22.696  31.403  1.00 39.63           C  
HETATM 3395  N9A FAD A 501       3.970 -21.477  31.949  1.00 37.67           N  
HETATM 3396  C8A FAD A 501       3.564 -20.459  31.277  1.00 36.34           C  
HETATM 3397  N7A FAD A 501       3.103 -19.600  32.129  1.00 35.38           N  
HETATM 3398  C5A FAD A 501       3.216 -20.060  33.335  1.00 36.24           C  
HETATM 3399  C6A FAD A 501       2.904 -19.591  34.536  1.00 36.52           C  
HETATM 3400  N6A FAD A 501       2.362 -18.422  34.644  1.00 36.07           N  
HETATM 3401  N1A FAD A 501       3.113 -20.264  35.622  1.00 35.88           N  
HETATM 3402  C2A FAD A 501       3.657 -21.479  35.524  1.00 35.71           C  
HETATM 3403  N3A FAD A 501       3.963 -21.945  34.296  1.00 36.60           N  
HETATM 3404  C4A FAD A 501       3.740 -21.237  33.213  1.00 36.80           C  
HETATM 3405  N1  FAD A 501      13.237 -25.896  18.222  1.00 35.37           N  
HETATM 3406  C2  FAD A 501      14.163 -26.747  17.709  1.00 35.36           C  
HETATM 3407  O2  FAD A 501      15.215 -26.916  18.257  1.00 35.83           O  
HETATM 3408  N3  FAD A 501      13.935 -27.449  16.585  1.00 34.64           N  
HETATM 3409  C4  FAD A 501      12.775 -27.281  15.942  1.00 34.01           C  
HETATM 3410  O4  FAD A 501      12.580 -27.890  14.927  1.00 33.76           O  
HETATM 3411  C4X FAD A 501      11.841 -26.427  16.433  1.00 33.49           C  
HETATM 3412  N5  FAD A 501      10.705 -26.305  15.756  1.00 32.43           N  
HETATM 3413  C5X FAD A 501       9.772 -25.492  16.248  1.00 31.42           C  
HETATM 3414  C6  FAD A 501       8.609 -25.391  15.553  1.00 29.93           C  
HETATM 3415  C7  FAD A 501       7.633 -24.576  16.010  1.00 29.38           C  
HETATM 3416  C7M FAD A 501       6.477 -24.503  15.270  1.00 28.40           C  
HETATM 3417  C8  FAD A 501       7.830 -23.859  17.161  1.00 28.81           C  
HETATM 3418  C8M FAD A 501       6.876 -23.034  17.682  1.00 29.01           C  
HETATM 3419  C9  FAD A 501       8.991 -23.974  17.835  1.00 28.35           C  
HETATM 3420  C9A FAD A 501       9.986 -24.792  17.401  1.00 30.90           C  
HETATM 3421  N10 FAD A 501      11.127 -24.933  18.079  1.00 32.56           N  
HETATM 3422  C10 FAD A 501      12.047 -25.736  17.587  1.00 34.00           C  
HETATM 3423  C1' FAD A 501      11.419 -24.179  19.315  1.00 32.65           C  
HETATM 3424  C2' FAD A 501      11.165 -24.823  20.679  1.00 33.70           C  
HETATM 3425  O2' FAD A 501       9.884 -25.385  20.775  1.00 32.20           O  
HETATM 3426  C3' FAD A 501      11.304 -23.757  21.748  1.00 35.89           C  
HETATM 3427  O3' FAD A 501      12.545 -23.164  21.550  1.00 36.20           O  
HETATM 3428  C4' FAD A 501      11.244 -24.298  23.182  1.00 36.83           C  
HETATM 3429  O4' FAD A 501      10.355 -25.347  23.205  1.00 37.11           O  
HETATM 3430  C5' FAD A 501      10.783 -23.256  24.206  1.00 38.86           C  
HETATM 3431  O5' FAD A 501      11.234 -23.585  25.532  1.00 40.30           O  
HETATM 3432  P   FAD A 501      10.668 -23.152  26.696  1.00 29.12           P  
HETATM 3433  O1P FAD A 501      11.066 -21.846  26.603  1.00 30.35           O  
HETATM 3434  O2P FAD A 501      11.108 -23.966  27.713  1.00 29.13           O  
HETATM 3435  O3P FAD A 501       9.200 -23.187  26.396  1.00 31.64           O  
HETATM 3436  S1  D1D A 502      -7.736 -25.112  34.797  1.00101.05           S  
HETATM 3437  C1  D1D A 502      -7.329 -26.696  35.465  1.00 51.34           C  
HETATM 3438  C2  D1D A 502      -6.872 -27.718  34.424  1.00 51.70           C  
HETATM 3439  O2  D1D A 502      -7.917 -27.915  33.463  1.00 53.19           O  
HETATM 3440  C3  D1D A 502      -5.569 -27.362  33.707  1.00 50.26           C  
HETATM 3441  O3  D1D A 502      -4.551 -28.281  34.110  1.00 50.13           O  
HETATM 3442  C4  D1D A 502      -5.113 -25.939  33.996  1.00 49.79           C  
HETATM 3443  S4  D1D A 502      -6.347 -24.848  33.385  1.00 79.24           S  
HETATM 3444  S1  D1D A 503      -5.354 -31.154  31.118  1.00 68.82           S  
HETATM 3445  C1  D1D A 503      -5.399 -29.871  29.911  1.00 66.62           C  
HETATM 3446  C2  D1D A 503      -6.194 -30.272  28.677  1.00 66.36           C  
HETATM 3447  O2  D1D A 503      -6.338 -29.130  27.824  1.00 66.78           O  
HETATM 3448  C3  D1D A 503      -5.490 -31.386  27.915  1.00 65.75           C  
HETATM 3449  O3  D1D A 503      -6.117 -31.550  26.637  1.00 65.38           O  
HETATM 3450  C4  D1D A 503      -5.567 -32.699  28.685  1.00 65.69           C  
HETATM 3451  S4  D1D A 503      -4.492 -32.626  30.077  1.00 87.52           S  
HETATM 3452  S   SO4 A 504      -8.323 -28.513  12.135  1.00 57.44           S  
HETATM 3453  O1  SO4 A 504      -7.235 -28.076  11.269  1.00 58.38           O  
HETATM 3454  O2  SO4 A 504      -9.598 -28.177  11.506  1.00 57.66           O  
HETATM 3455  O3  SO4 A 504      -8.238 -29.957  12.342  1.00 56.73           O  
HETATM 3456  O4  SO4 A 504      -8.213 -27.834  13.421  1.00 57.94           O  
HETATM 3457  O   HOH A 601       4.004  -7.283  15.356  1.00 33.04           O  
HETATM 3458  O   HOH A 602      -2.284 -40.425  -2.433  1.00 42.23           O  
HETATM 3459  O   HOH A 603      18.361 -35.908  43.773  1.00 47.76           O  
HETATM 3460  O   HOH A 604      32.759 -14.171  26.045  1.00 54.76           O  
HETATM 3461  O   HOH A 605      24.324 -11.895  23.875  1.00 30.92           O  
HETATM 3462  O   HOH A 606      -9.260 -10.718  22.384  1.00 42.10           O  
HETATM 3463  O   HOH A 607      11.977 -18.892  26.498  1.00 27.18           O  
HETATM 3464  O   HOH A 608       7.751 -38.094  12.279  1.00 33.43           O  
HETATM 3465  O   HOH A 609      17.574 -30.042  48.184  1.00 32.67           O  
HETATM 3466  O   HOH A 610       2.122  -2.996  36.942  1.00 48.79           O  
HETATM 3467  O   HOH A 611      12.528  -6.825  36.475  1.00 36.59           O  
HETATM 3468  O   HOH A 612      10.261 -24.605  30.477  1.00 25.14           O  
HETATM 3469  O   HOH A 613     -11.457 -26.403  11.580  1.00 37.28           O  
HETATM 3470  O   HOH A 614       7.496 -40.562  27.278  1.00 30.80           O  
HETATM 3471  O   HOH A 615      10.441 -26.209  47.005  1.00 35.54           O  
HETATM 3472  O   HOH A 616       3.029 -11.739  36.692  1.00 42.71           O  
HETATM 3473  O   HOH A 617      12.190 -36.938   8.514  1.00 33.29           O  
HETATM 3474  O   HOH A 618      13.757  -7.725  50.291  1.00 43.95           O  
HETATM 3475  O   HOH A 619      23.352 -35.419  32.951  1.00 34.67           O  
HETATM 3476  O   HOH A 620      30.584 -27.869  -4.709  1.00 48.23           O  
HETATM 3477  O   HOH A 621      11.724 -20.560  29.212  1.00 37.21           O  
HETATM 3478  O   HOH A 622       2.004 -34.981  35.074  1.00 42.99           O  
HETATM 3479  O   HOH A 623       4.896 -24.542  -4.422  1.00 38.38           O  
HETATM 3480  O   HOH A 624      17.139 -23.601   1.519  1.00 38.69           O  
HETATM 3481  O   HOH A 625      24.039 -14.903  32.267  1.00 30.97           O  
HETATM 3482  O   HOH A 626       6.598 -20.895  24.991  1.00 29.06           O  
HETATM 3483  O   HOH A 627      19.935  -9.641  22.808  1.00 32.61           O  
HETATM 3484  O   HOH A 628       5.870 -35.876  10.666  1.00 33.57           O  
HETATM 3485  O   HOH A 629      15.258 -15.218  16.892  1.00 55.73           O  
HETATM 3486  O   HOH A 630      21.877 -15.351  45.096  1.00 49.83           O  
HETATM 3487  O   HOH A 631      34.775 -28.301  10.768  1.00 37.44           O  
HETATM 3488  O   HOH A 632      18.379 -21.518   1.175  1.00 44.44           O  
HETATM 3489  O   HOH A 633      37.472 -32.575  16.050  1.00 33.85           O  
HETATM 3490  O   HOH A 634       8.374 -24.039  47.953  1.00 34.89           O  
HETATM 3491  O   HOH A 635      23.429 -10.794  33.876  1.00 36.57           O  
HETATM 3492  O   HOH A 636      -8.703 -23.925   3.349  1.00 46.12           O  
HETATM 3493  O   HOH A 637       6.277  -8.152  24.027  1.00 40.89           O  
HETATM 3494  O   HOH A 638      -0.683 -33.079  29.477  1.00 46.08           O  
HETATM 3495  O   HOH A 639       0.650 -17.545  32.320  1.00 34.84           O  
HETATM 3496  O   HOH A 640      17.355  -6.035  24.042  1.00 38.88           O  
HETATM 3497  O   HOH A 641       2.080 -28.787  37.065  1.00 31.30           O  
HETATM 3498  O   HOH A 642      27.160 -14.379  19.829  1.00 46.54           O  
HETATM 3499  O   HOH A 643      25.660 -23.007 -10.081  1.00 41.33           O  
HETATM 3500  O   HOH A 644       5.119 -27.293  47.682  1.00 41.09           O  
HETATM 3501  O   HOH A 645      26.823 -12.346  23.480  1.00 37.13           O  
HETATM 3502  O   HOH A 646      16.805 -19.745   1.078  1.00 42.45           O  
CONECT   96  101                                                                
CONECT  101   96  102                                                           
CONECT  102  101  103  105                                                      
CONECT  103  102  104  109                                                      
CONECT  104  103                                                                
CONECT  105  102  106                                                           
CONECT  106  105  107                                                           
CONECT  107  106  108                                                           
CONECT  108  107                                                                
CONECT  109  103                                                                
CONECT  552  558                                                                
CONECT  558  552  559                                                           
CONECT  559  558  560  562                                                      
CONECT  560  559  561  566                                                      
CONECT  561  560                                                                
CONECT  562  559  563                                                           
CONECT  563  562  564                                                           
CONECT  564  563  565                                                           
CONECT  565  564                                                                
CONECT  566  560                                                                
CONECT  700  707                                                                
CONECT  707  700  708                                                           
CONECT  708  707  709  711                                                      
CONECT  709  708  710  715                                                      
CONECT  710  709                                                                
CONECT  711  708  712                                                           
CONECT  712  711  713                                                           
CONECT  713  712  714                                                           
CONECT  714  713                                                                
CONECT  715  709                                                                
CONECT  807  816                                                                
CONECT  816  807  817                                                           
CONECT  817  816  818  820                                                      
CONECT  818  817  819  824                                                      
CONECT  819  818                                                                
CONECT  820  817  821                                                           
CONECT  821  820  822                                                           
CONECT  822  821  823                                                           
CONECT  823  822                                                                
CONECT  824  818                                                                
CONECT 1173 1182                                                                
CONECT 1182 1173 1183                                                           
CONECT 1183 1182 1184 1186                                                      
CONECT 1184 1183 1185                                                           
CONECT 1185 1184 1188                                                           
CONECT 1186 1183 1187 1189                                                      
CONECT 1187 1186                                                                
CONECT 1188 1185                                                                
CONECT 1189 1186                                                                
CONECT 2230 2237                                                                
CONECT 2237 2230 2238                                                           
CONECT 2238 2237 2239 2241                                                      
CONECT 2239 2238 2240 2245                                                      
CONECT 2240 2239                                                                
CONECT 2241 2238 2242                                                           
CONECT 2242 2241 2243                                                           
CONECT 2243 2242 2244                                                           
CONECT 2244 2243                                                                
CONECT 2245 2239                                                                
CONECT 2682 2685                                                                
CONECT 2685 2682 2686                                                           
CONECT 2686 2685 2687 2689                                                      
CONECT 2687 2686 2688 2693                                                      
CONECT 2688 2687                                                                
CONECT 2689 2686 2690                                                           
CONECT 2690 2689 2691                                                           
CONECT 2691 2690 2692                                                           
CONECT 2692 2691                                                                
CONECT 2693 2687                                                                
CONECT 2698 3418                                                                
CONECT 3332 3338                                                                
CONECT 3338 3332 3339                                                           
CONECT 3339 3338 3340 3342                                                      
CONECT 3340 3339 3341 3346                                                      
CONECT 3341 3340                                                                
CONECT 3342 3339 3343                                                           
CONECT 3343 3342 3344                                                           
CONECT 3344 3343 3345                                                           
CONECT 3345 3344                                                                
CONECT 3346 3340                                                                
CONECT 3383 3384 3385 3386 3435                                                 
CONECT 3384 3383                                                                
CONECT 3385 3383                                                                
CONECT 3386 3383 3387                                                           
CONECT 3387 3386 3388                                                           
CONECT 3388 3387 3389 3390                                                      
CONECT 3389 3388 3394                                                           
CONECT 3390 3388 3391 3392                                                      
CONECT 3391 3390                                                                
CONECT 3392 3390 3393 3394                                                      
CONECT 3393 3392                                                                
CONECT 3394 3389 3392 3395                                                      
CONECT 3395 3394 3396 3404                                                      
CONECT 3396 3395 3397                                                           
CONECT 3397 3396 3398                                                           
CONECT 3398 3397 3399 3404                                                      
CONECT 3399 3398 3400 3401                                                      
CONECT 3400 3399                                                                
CONECT 3401 3399 3402                                                           
CONECT 3402 3401 3403                                                           
CONECT 3403 3402 3404                                                           
CONECT 3404 3395 3398 3403                                                      
CONECT 3405 3406 3422                                                           
CONECT 3406 3405 3407 3408                                                      
CONECT 3407 3406                                                                
CONECT 3408 3406 3409                                                           
CONECT 3409 3408 3410 3411                                                      
CONECT 3410 3409                                                                
CONECT 3411 3409 3412 3422                                                      
CONECT 3412 3411 3413                                                           
CONECT 3413 3412 3414 3420                                                      
CONECT 3414 3413 3415                                                           
CONECT 3415 3414 3416 3417                                                      
CONECT 3416 3415                                                                
CONECT 3417 3415 3418 3419                                                      
CONECT 3418 2698 3417                                                           
CONECT 3419 3417 3420                                                           
CONECT 3420 3413 3419 3421                                                      
CONECT 3421 3420 3422 3423                                                      
CONECT 3422 3405 3411 3421                                                      
CONECT 3423 3421 3424                                                           
CONECT 3424 3423 3425 3426                                                      
CONECT 3425 3424                                                                
CONECT 3426 3424 3427 3428                                                      
CONECT 3427 3426                                                                
CONECT 3428 3426 3429 3430                                                      
CONECT 3429 3428                                                                
CONECT 3430 3428 3431                                                           
CONECT 3431 3430 3432                                                           
CONECT 3432 3431 3433 3434 3435                                                 
CONECT 3433 3432                                                                
CONECT 3434 3432                                                                
CONECT 3435 3383 3432                                                           
CONECT 3436 3437 3443                                                           
CONECT 3437 3436 3438                                                           
CONECT 3438 3437 3439 3440                                                      
CONECT 3439 3438                                                                
CONECT 3440 3438 3441 3442                                                      
CONECT 3441 3440                                                                
CONECT 3442 3440 3443                                                           
CONECT 3443 3436 3442                                                           
CONECT 3444 3445 3451                                                           
CONECT 3445 3444 3446                                                           
CONECT 3446 3445 3447 3448                                                      
CONECT 3447 3446                                                                
CONECT 3448 3446 3449 3450                                                      
CONECT 3449 3448                                                                
CONECT 3450 3448 3451                                                           
CONECT 3451 3444 3450                                                           
CONECT 3452 3453 3454 3455 3456                                                 
CONECT 3453 3452                                                                
CONECT 3454 3452                                                                
CONECT 3455 3452                                                                
CONECT 3456 3452                                                                
MASTER      323    0   12   19   24    0   14    6 3501    1  154   34          
END                                                                             
