HEADER    BIOTIN BIOSYNTHESIS                     31-MAR-98   1A82              
TITLE     DETHIOBIOTIN SYNTHETASE FROM ESCHERICHIA COLI, COMPLEX WITH SUBSTRATES
TITLE    2 ATP AND DIAMINOPELARGONIC ACID                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DETHIOBIOTIN SYNTHETASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 6.3.3.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 CELLULAR_LOCATION: CYTOPLASM;                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_GENE: BIOD                                         
KEYWDS    PHOSPHORYL TRANSFER, BIOTIN BIOSYNTHESIS, LIGASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.KAECK,K.J.GIBSON,Y.LINDQVIST,G.SCHNEIDER                            
REVDAT   4   02-AUG-23 1A82    1       REMARK LINK   ATOM                       
REVDAT   3   13-JUL-11 1A82    1       VERSN                                    
REVDAT   2   24-FEB-09 1A82    1       VERSN                                    
REVDAT   1   11-MAY-99 1A82    0                                                
JRNL        AUTH   H.KACK,K.J.GIBSON,Y.LINDQVIST,G.SCHNEIDER                    
JRNL        TITL   SNAPSHOT OF A PHOSPHORYLATED SUBSTRATE INTERMEDIATE BY       
JRNL        TITL 2 KINETIC CRYSTALLOGRAPHY.                                     
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  95  5495 1998              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   9576910                                                      
JRNL        DOI    10.1073/PNAS.95.10.5495                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 17659                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 903                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.86                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1678                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1896                       
REMARK   3   BIN FREE R VALUE                    : 0.2461                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 6.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 101                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.024                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1692                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 45                                      
REMARK   3   SOLVENT ATOMS            : 219                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 11.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 9.00                           
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.530                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.350                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : PARAM11.DNA                                    
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1A82 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000170509.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : FEB-97                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18671                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.03000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.11600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER           
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: PDB ENTRY 1DAH, WITH NON-PROTEIN ATOMS EXCLUDED      
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       36.45000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.95000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       36.45000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.95000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 6090 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 688  LIES ON A SPECIAL POSITION.                          
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    ASP A  10     -177.10   -176.65                                   
REMARK 500    ASN A 209       61.90     28.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 901  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  16   OG1                                                    
REMARK 620 2 ASP A  54   OD2  84.3                                              
REMARK 620 3 GLU A 115   OE2  86.1  92.4                                        
REMARK 620 4 HOH A 444   O    90.5  79.8 171.7                                  
REMARK 620 5 ATP A 802   O3G 171.6  87.7  91.7  90.7                            
REMARK 620 6 ATP A 802   O1B  96.5 157.8 109.7  78.1  91.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DNN A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 802                 
DBREF  1A82 A    1   224  UNP    P13000   BIOD_ECOLI       1    224             
SEQRES   1 A  224  SER LYS ARG TYR PHE VAL THR GLY THR ASP THR GLU VAL          
SEQRES   2 A  224  GLY LYS THR VAL ALA SER CYS ALA LEU LEU GLN ALA ALA          
SEQRES   3 A  224  LYS ALA ALA GLY TYR ARG THR ALA GLY TYR LYS PRO VAL          
SEQRES   4 A  224  ALA SER GLY SER GLU LYS THR PRO GLU GLY LEU ARG ASN          
SEQRES   5 A  224  SER ASP ALA LEU ALA LEU GLN ARG ASN SER SER LEU GLN          
SEQRES   6 A  224  LEU ASP TYR ALA THR VAL ASN PRO TYR THR PHE ALA GLU          
SEQRES   7 A  224  PRO THR SER PRO HIS ILE ILE SER ALA GLN GLU GLY ARG          
SEQRES   8 A  224  PRO ILE GLU SER LEU VAL MET SER ALA GLY LEU ARG ALA          
SEQRES   9 A  224  LEU GLU GLN GLN ALA ASP TRP VAL LEU VAL GLU GLY ALA          
SEQRES  10 A  224  GLY GLY TRP PHE THR PRO LEU SER ASP THR PHE THR PHE          
SEQRES  11 A  224  ALA ASP TRP VAL THR GLN GLU GLN LEU PRO VAL ILE LEU          
SEQRES  12 A  224  VAL VAL GLY VAL LYS LEU GLY CYS ILE ASN HIS ALA MET          
SEQRES  13 A  224  LEU THR ALA GLN VAL ILE GLN HIS ALA GLY LEU THR LEU          
SEQRES  14 A  224  ALA GLY TRP VAL ALA ASN ASP VAL THR PRO PRO GLY LYS          
SEQRES  15 A  224  ARG HIS ALA GLU TYR MET THR THR LEU THR ARG MET ILE          
SEQRES  16 A  224  PRO ALA PRO LEU LEU GLY GLU ILE PRO TRP LEU ALA GLU          
SEQRES  17 A  224  ASN PRO GLU ASN ALA ALA THR GLY LYS TYR ILE ASN LEU          
SEQRES  18 A  224  ALA LEU LEU                                                  
HET     MG  A 901       1                                                       
HET    DNN  A 801      13                                                       
HET    ATP  A 802      31                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     DNN 7,8-DIAMINO-NONANOIC ACID                                        
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  DNN    C9 H20 N2 O2                                                 
FORMUL   4  ATP    C10 H16 N5 O13 P3                                            
FORMUL   5  HOH   *219(H2 O)                                                    
HELIX    1   1 LYS A   15  ALA A   28  1                                  14    
HELIX    2   2 SER A   53  ARG A   60  1                                   8    
HELIX    3   3 TYR A   68  VAL A   71  1                                   4    
HELIX    4   4 PRO A   82  GLU A   89  1                                   8    
HELIX    5   5 SER A   95  GLN A  107  1                                  13    
HELIX    6   6 PHE A  130  GLU A  137  1                                   8    
HELIX    7   7 CYS A  151  HIS A  164  1                                  14    
HELIX    8   8 HIS A  184  MET A  194  1                                  11    
HELIX    9   9 PRO A  210  ASN A  212  5                                   3    
HELIX   10  10 GLY A  216  TYR A  218  5                                   3    
SHEET    1   A 6 LEU A 199  ILE A 203  0                                        
SHEET    2   A 6 LEU A 169  ASN A 175  1  N  TRP A 172   O  LEU A 200           
SHEET    3   A 6 PRO A 140  GLY A 146  1  N  VAL A 141   O  ALA A 170           
SHEET    4   A 6 LYS A   2  GLY A   8  1  N  PHE A   5   O  PRO A 140           
SHEET    5   A 6 TRP A 111  GLU A 115  1  N  VAL A 112   O  LYS A   2           
SHEET    6   A 6 THR A  33  TYR A  36  1  N  ALA A  34   O  TRP A 111           
SHEET    1   B 2 VAL A  39  SER A  41  0                                        
SHEET    2   B 2 TYR A  74  PHE A  76  1  N  TYR A  74   O  ALA A  40           
SHEET    1   C 2 SER A  43  THR A  46  0                                        
SHEET    2   C 2 GLY A  49  ASN A  52 -1  N  ARG A  51   O  GLU A  44           
LINK         OG1 THR A  16                MG    MG A 901     1555   1555  2.18  
LINK         OD2 ASP A  54                MG    MG A 901     1555   1555  2.16  
LINK         OE2 GLU A 115                MG    MG A 901     1555   1555  2.06  
LINK         O   HOH A 444                MG    MG A 901     1555   1555  2.39  
LINK         O3G ATP A 802                MG    MG A 901     1555   1555  2.19  
LINK         O1B ATP A 802                MG    MG A 901     1555   1555  1.97  
SITE     1 AC1  5 THR A  16  ASP A  54  GLU A 115  HOH A 444                    
SITE     2 AC1  5 ATP A 802                                                     
SITE     1 AC2 15 THR A  11  SER A  41  PRO A  79  GLY A 118                    
SITE     2 AC2 15 LEU A 149  GLY A 150  CYS A 151  ILE A 152                    
SITE     3 AC2 15 ASN A 153  TYR A 187  HOH A 429  HOH A 655                    
SITE     4 AC2 15 HOH A 716  HOH A 728  ATP A 802                               
SITE     1 AC3 25 THR A  11  GLU A  12  VAL A  13  GLY A  14                    
SITE     2 AC3 25 LYS A  15  THR A  16  VAL A  17  LYS A  37                    
SITE     3 AC3 25 ASP A  54  GLU A 115  GLY A 118  ASN A 175                    
SITE     4 AC3 25 ASP A 176  PRO A 204  TRP A 205  LEU A 206                    
SITE     5 AC3 25 PRO A 210  GLU A 211  HOH A 444  HOH A 710                    
SITE     6 AC3 25 HOH A 711  HOH A 714  HOH A 716  DNN A 801                    
SITE     7 AC3 25  MG A 901                                                     
CRYST1   72.900   47.900   60.900  90.00 106.50  90.00 C 1 2 1       4          
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      0.013717  0.000000  0.004063        0.00000                         
SCALE2      0.000000  0.020877  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017126        0.00000                         
ATOM      1  N   SER A   1      13.362  42.410  26.332  1.00 25.76           N  
ATOM      2  CA  SER A   1      13.914  41.067  26.025  1.00 26.35           C  
ATOM      3  C   SER A   1      13.563  40.732  24.575  1.00 25.39           C  
ATOM      4  O   SER A   1      12.650  41.345  24.008  1.00 26.08           O  
ATOM      5  CB  SER A   1      13.329  40.023  26.982  1.00 28.53           C  
ATOM      6  OG  SER A   1      11.946  40.224  27.221  1.00 29.44           O  
ATOM      7  N   LYS A   2      14.287  39.788  23.975  1.00 20.33           N  
ATOM      8  CA  LYS A   2      14.039  39.420  22.589  1.00 15.89           C  
ATOM      9  C   LYS A   2      12.768  38.579  22.387  1.00 13.13           C  
ATOM     10  O   LYS A   2      12.449  37.735  23.225  1.00 12.21           O  
ATOM     11  CB  LYS A   2      15.285  38.753  22.017  1.00 17.24           C  
ATOM     12  CG  LYS A   2      16.485  39.709  22.041  1.00 18.65           C  
ATOM     13  CD  LYS A   2      17.594  39.276  21.109  1.00 21.84           C  
ATOM     14  CE  LYS A   2      18.463  40.463  20.715  1.00 20.84           C  
ATOM     15  NZ  LYS A   2      19.459  40.058  19.704  1.00 25.70           N  
ATOM     16  N   ARG A   3      12.017  38.875  21.316  1.00 10.68           N  
ATOM     17  CA  ARG A   3      10.772  38.170  20.983  1.00  9.36           C  
ATOM     18  C   ARG A   3      10.631  38.073  19.463  1.00  7.02           C  
ATOM     19  O   ARG A   3      10.966  39.014  18.736  1.00  6.20           O  
ATOM     20  CB  ARG A   3       9.527  38.892  21.543  1.00 12.24           C  
ATOM     21  CG  ARG A   3       9.802  40.064  22.476  1.00 20.15           C  
ATOM     22  CD  ARG A   3       9.158  41.358  21.971  1.00 22.40           C  
ATOM     23  NE  ARG A   3       7.756  41.461  22.363  1.00 24.23           N  
ATOM     24  CZ  ARG A   3       6.855  42.226  21.748  1.00 26.10           C  
ATOM     25  NH1 ARG A   3       7.211  42.961  20.696  1.00 24.81           N  
ATOM     26  NH2 ARG A   3       5.599  42.264  22.188  1.00 21.37           N  
ATOM     27  N   TYR A   4      10.149  36.935  18.985  1.00  4.30           N  
ATOM     28  CA  TYR A   4       9.969  36.731  17.552  1.00  5.26           C  
ATOM     29  C   TYR A   4       8.695  35.953  17.303  1.00  3.54           C  
ATOM     30  O   TYR A   4       8.296  35.107  18.119  1.00  5.66           O  
ATOM     31  CB  TYR A   4      11.141  35.934  16.957  1.00  5.28           C  
ATOM     32  CG  TYR A   4      12.479  36.580  17.178  1.00  7.49           C  
ATOM     33  CD1 TYR A   4      12.933  37.593  16.325  1.00  8.39           C  
ATOM     34  CD2 TYR A   4      13.259  36.234  18.283  1.00  8.52           C  
ATOM     35  CE1 TYR A   4      14.127  38.246  16.567  1.00  9.81           C  
ATOM     36  CE2 TYR A   4      14.458  36.881  18.535  1.00  9.31           C  
ATOM     37  CZ  TYR A   4      14.879  37.885  17.678  1.00 10.94           C  
ATOM     38  OH  TYR A   4      16.047  38.534  17.943  1.00 10.54           O  
ATOM     39  N   PHE A   5       8.018  36.291  16.215  1.00  3.17           N  
ATOM     40  CA  PHE A   5       6.830  35.549  15.842  1.00  3.19           C  
ATOM     41  C   PHE A   5       7.231  34.660  14.652  1.00  3.86           C  
ATOM     42  O   PHE A   5       7.823  35.134  13.678  1.00  3.49           O  
ATOM     43  CB  PHE A   5       5.671  36.468  15.442  1.00  2.27           C  
ATOM     44  CG  PHE A   5       4.417  35.719  15.105  1.00  2.05           C  
ATOM     45  CD1 PHE A   5       3.575  35.275  16.111  1.00  2.11           C  
ATOM     46  CD2 PHE A   5       4.087  35.442  13.781  1.00  2.78           C  
ATOM     47  CE1 PHE A   5       2.409  34.561  15.808  1.00  3.93           C  
ATOM     48  CE2 PHE A   5       2.927  34.730  13.460  1.00  3.06           C  
ATOM     49  CZ  PHE A   5       2.090  34.289  14.465  1.00  4.33           C  
ATOM     50  N   VAL A   6       6.919  33.374  14.750  1.00  3.16           N  
ATOM     51  CA  VAL A   6       7.227  32.439  13.697  1.00  3.83           C  
ATOM     52  C   VAL A   6       5.971  32.074  12.914  1.00  4.30           C  
ATOM     53  O   VAL A   6       4.985  31.558  13.469  1.00  3.04           O  
ATOM     54  CB  VAL A   6       7.859  31.149  14.253  1.00  5.08           C  
ATOM     55  CG1 VAL A   6       8.053  30.147  13.131  1.00  6.41           C  
ATOM     56  CG2 VAL A   6       9.203  31.449  14.910  1.00  5.26           C  
ATOM     57  N   THR A   7       5.996  32.398  11.628  1.00  6.09           N  
ATOM     58  CA  THR A   7       4.888  32.069  10.730  1.00  6.00           C  
ATOM     59  C   THR A   7       5.460  31.181   9.625  1.00  5.76           C  
ATOM     60  O   THR A   7       6.667  30.921   9.577  1.00  5.59           O  
ATOM     61  CB  THR A   7       4.192  33.330  10.131  1.00  3.59           C  
ATOM     62  OG1 THR A   7       2.979  32.928   9.475  1.00  4.27           O  
ATOM     63  CG2 THR A   7       5.108  34.030   9.120  1.00  2.37           C  
ATOM     64  N   GLY A   8       4.575  30.687   8.768  1.00  6.25           N  
ATOM     65  CA  GLY A   8       4.981  29.818   7.688  1.00  5.19           C  
ATOM     66  C   GLY A   8       4.194  30.115   6.433  1.00  4.13           C  
ATOM     67  O   GLY A   8       3.186  30.820   6.435  1.00  4.83           O  
ATOM     68  N   THR A   9       4.722  29.606   5.339  1.00  6.12           N  
ATOM     69  CA  THR A   9       4.108  29.758   4.038  1.00  7.03           C  
ATOM     70  C   THR A   9       2.736  29.041   3.961  1.00  9.17           C  
ATOM     71  O   THR A   9       1.937  29.305   3.053  1.00  7.52           O  
ATOM     72  CB  THR A   9       5.071  29.216   2.981  1.00  5.08           C  
ATOM     73  OG1 THR A   9       5.555  27.934   3.402  1.00  4.05           O  
ATOM     74  CG2 THR A   9       6.260  30.172   2.829  1.00  6.57           C  
ATOM     75  N   ASP A  10       2.444  28.192   4.951  1.00  9.81           N  
ATOM     76  CA  ASP A  10       1.189  27.428   5.015  1.00 10.37           C  
ATOM     77  C   ASP A  10       1.223  26.650   6.342  1.00  9.67           C  
ATOM     78  O   ASP A  10       2.131  26.823   7.150  1.00  9.19           O  
ATOM     79  CB  ASP A  10       1.187  26.415   3.852  1.00  8.76           C  
ATOM     80  CG  ASP A  10      -0.176  25.772   3.591  1.00 11.77           C  
ATOM     81  OD1 ASP A  10      -1.189  26.111   4.252  1.00 10.44           O  
ATOM     82  OD2 ASP A  10      -0.223  24.922   2.675  1.00  9.81           O  
ATOM     83  N   THR A  11       0.200  25.838   6.579  1.00  8.65           N  
ATOM     84  CA  THR A  11       0.183  24.972   7.740  1.00  9.04           C  
ATOM     85  C   THR A  11       0.997  23.753   7.253  1.00  8.43           C  
ATOM     86  O   THR A  11       1.127  23.541   6.039  1.00  7.77           O  
ATOM     87  CB  THR A  11      -1.278  24.564   8.138  1.00  9.07           C  
ATOM     88  OG1 THR A  11      -1.244  23.704   9.292  1.00  8.17           O  
ATOM     89  CG2 THR A  11      -2.001  23.852   6.983  1.00  9.24           C  
ATOM     90  N   GLU A  12       1.612  23.015   8.170  1.00  8.75           N  
ATOM     91  CA  GLU A  12       2.404  21.834   7.815  1.00 10.88           C  
ATOM     92  C   GLU A  12       3.625  22.082   6.922  1.00  8.96           C  
ATOM     93  O   GLU A  12       3.908  21.286   6.038  1.00  9.32           O  
ATOM     94  CB  GLU A  12       1.524  20.748   7.173  1.00 14.58           C  
ATOM     95  CG  GLU A  12       1.495  19.429   7.943  1.00 25.04           C  
ATOM     96  CD  GLU A  12       0.659  19.502   9.222  1.00 30.59           C  
ATOM     97  OE1 GLU A  12       0.655  20.558   9.903  1.00 36.01           O  
ATOM     98  OE2 GLU A  12      -0.020  18.502   9.541  1.00 35.30           O  
ATOM     99  N   VAL A  13       4.345  23.175   7.145  1.00  6.68           N  
ATOM    100  CA  VAL A  13       5.535  23.440   6.352  1.00  7.54           C  
ATOM    101  C   VAL A  13       6.784  23.356   7.222  1.00  8.74           C  
ATOM    102  O   VAL A  13       7.909  23.458   6.713  1.00  7.46           O  
ATOM    103  CB  VAL A  13       5.480  24.807   5.642  1.00  8.61           C  
ATOM    104  CG1 VAL A  13       4.319  24.828   4.660  1.00  9.07           C  
ATOM    105  CG2 VAL A  13       5.364  25.952   6.643  1.00  7.03           C  
ATOM    106  N   GLY A  14       6.579  23.217   8.534  1.00  7.70           N  
ATOM    107  CA  GLY A  14       7.690  23.104   9.463  1.00  6.32           C  
ATOM    108  C   GLY A  14       7.869  24.197  10.503  1.00  6.89           C  
ATOM    109  O   GLY A  14       8.957  24.314  11.061  1.00  7.07           O  
ATOM    110  N   LYS A  15       6.851  25.012  10.765  1.00  5.78           N  
ATOM    111  CA  LYS A  15       6.974  26.061  11.786  1.00  5.44           C  
ATOM    112  C   LYS A  15       7.468  25.477  13.115  1.00  4.59           C  
ATOM    113  O   LYS A  15       8.356  26.035  13.742  1.00  4.66           O  
ATOM    114  CB  LYS A  15       5.634  26.784  12.039  1.00  5.05           C  
ATOM    115  CG  LYS A  15       5.113  27.642  10.869  1.00  7.04           C  
ATOM    116  CD  LYS A  15       3.883  28.454  11.288  1.00  5.42           C  
ATOM    117  CE  LYS A  15       2.755  27.569  11.730  1.00  6.36           C  
ATOM    118  NZ  LYS A  15       2.291  26.727  10.585  1.00  7.84           N  
ATOM    119  N   THR A  16       6.899  24.350  13.533  1.00  4.33           N  
ATOM    120  CA  THR A  16       7.281  23.726  14.806  1.00  4.82           C  
ATOM    121  C   THR A  16       8.710  23.199  14.806  1.00  2.65           C  
ATOM    122  O   THR A  16       9.467  23.466  15.739  1.00  4.22           O  
ATOM    123  CB  THR A  16       6.240  22.640  15.237  1.00  6.85           C  
ATOM    124  OG1 THR A  16       4.980  23.289  15.475  1.00  4.03           O  
ATOM    125  CG2 THR A  16       6.673  21.907  16.525  1.00  3.82           C  
ATOM    126  N   VAL A  17       9.095  22.478  13.766  1.00  2.00           N  
ATOM    127  CA  VAL A  17      10.456  21.965  13.681  1.00  2.90           C  
ATOM    128  C   VAL A  17      11.467  23.136  13.681  1.00  4.38           C  
ATOM    129  O   VAL A  17      12.462  23.110  14.416  1.00  5.74           O  
ATOM    130  CB  VAL A  17      10.643  21.047  12.426  1.00  3.37           C  
ATOM    131  CG1 VAL A  17      12.143  20.808  12.118  1.00  4.73           C  
ATOM    132  CG2 VAL A  17       9.967  19.707  12.668  1.00  4.51           C  
ATOM    133  N   ALA A  18      11.227  24.149  12.855  1.00  2.71           N  
ATOM    134  CA  ALA A  18      12.123  25.300  12.810  1.00  3.09           C  
ATOM    135  C   ALA A  18      12.144  26.042  14.144  1.00  2.65           C  
ATOM    136  O   ALA A  18      13.199  26.500  14.562  1.00  2.93           O  
ATOM    137  CB  ALA A  18      11.726  26.236  11.695  1.00  2.94           C  
ATOM    138  N   SER A  19      10.993  26.172  14.804  1.00  2.28           N  
ATOM    139  CA  SER A  19      10.921  26.850  16.106  1.00  3.16           C  
ATOM    140  C   SER A  19      11.786  26.133  17.160  1.00  2.45           C  
ATOM    141  O   SER A  19      12.429  26.774  17.989  1.00  2.83           O  
ATOM    142  CB  SER A  19       9.456  26.938  16.591  1.00  2.83           C  
ATOM    143  OG  SER A  19       8.728  27.881  15.811  1.00  5.38           O  
ATOM    144  N   CYS A  20      11.780  24.805  17.135  1.00  3.17           N  
ATOM    145  CA  CYS A  20      12.595  24.021  18.050  1.00  2.62           C  
ATOM    146  C   CYS A  20      14.067  24.276  17.746  1.00  4.25           C  
ATOM    147  O   CYS A  20      14.879  24.421  18.672  1.00  2.92           O  
ATOM    148  CB  CYS A  20      12.261  22.536  17.944  1.00  4.73           C  
ATOM    149  SG  CYS A  20      10.607  22.111  18.600  1.00  7.74           S  
ATOM    150  N   ALA A  21      14.413  24.363  16.460  1.00  3.29           N  
ATOM    151  CA  ALA A  21      15.793  24.638  16.058  1.00  3.94           C  
ATOM    152  C   ALA A  21      16.182  26.039  16.544  1.00  3.42           C  
ATOM    153  O   ALA A  21      17.259  26.237  17.100  1.00  2.00           O  
ATOM    154  CB  ALA A  21      15.929  24.535  14.555  1.00  4.08           C  
ATOM    155  N   LEU A  22      15.285  27.003  16.374  1.00  2.18           N  
ATOM    156  CA  LEU A  22      15.543  28.357  16.820  1.00  3.56           C  
ATOM    157  C   LEU A  22      15.761  28.396  18.346  1.00  5.11           C  
ATOM    158  O   LEU A  22      16.750  28.983  18.826  1.00  5.65           O  
ATOM    159  CB  LEU A  22      14.399  29.280  16.405  1.00  2.40           C  
ATOM    160  CG  LEU A  22      14.425  29.754  14.943  1.00  3.11           C  
ATOM    161  CD1 LEU A  22      13.026  30.190  14.547  1.00  4.25           C  
ATOM    162  CD2 LEU A  22      15.442  30.891  14.726  1.00  2.11           C  
ATOM    163  N   LEU A  23      14.858  27.757  19.089  1.00  3.15           N  
ATOM    164  CA  LEU A  23      14.954  27.685  20.547  1.00  3.44           C  
ATOM    165  C   LEU A  23      16.273  27.036  21.035  1.00  4.10           C  
ATOM    166  O   LEU A  23      16.910  27.550  21.967  1.00  6.05           O  
ATOM    167  CB  LEU A  23      13.728  26.965  21.116  1.00  2.30           C  
ATOM    168  CG  LEU A  23      12.449  27.814  21.264  1.00  2.01           C  
ATOM    169  CD1 LEU A  23      11.215  26.910  21.480  1.00  2.04           C  
ATOM    170  CD2 LEU A  23      12.609  28.811  22.445  1.00  2.57           C  
ATOM    171  N   GLN A  24      16.679  25.934  20.403  1.00  3.46           N  
ATOM    172  CA  GLN A  24      17.930  25.239  20.737  1.00  2.78           C  
ATOM    173  C   GLN A  24      19.129  26.154  20.490  1.00  2.67           C  
ATOM    174  O   GLN A  24      20.046  26.228  21.301  1.00  3.04           O  
ATOM    175  CB  GLN A  24      18.081  23.976  19.897  1.00  2.22           C  
ATOM    176  CG  GLN A  24      17.195  22.835  20.319  1.00  4.06           C  
ATOM    177  CD  GLN A  24      17.233  21.691  19.321  1.00  7.23           C  
ATOM    178  OE1 GLN A  24      18.246  21.478  18.659  1.00  5.41           O  
ATOM    179  NE2 GLN A  24      16.127  20.948  19.208  1.00  7.28           N  
ATOM    180  N   ALA A  25      19.108  26.869  19.372  1.00  3.49           N  
ATOM    181  CA  ALA A  25      20.187  27.789  19.044  1.00  3.89           C  
ATOM    182  C   ALA A  25      20.280  28.938  20.063  1.00  2.05           C  
ATOM    183  O   ALA A  25      21.370  29.326  20.459  1.00  3.91           O  
ATOM    184  CB  ALA A  25      19.997  28.339  17.620  1.00  3.60           C  
ATOM    185  N   ALA A  26      19.149  29.478  20.500  1.00  2.31           N  
ATOM    186  CA  ALA A  26      19.168  30.578  21.468  1.00  2.00           C  
ATOM    187  C   ALA A  26      19.744  30.123  22.792  1.00  3.07           C  
ATOM    188  O   ALA A  26      20.486  30.864  23.442  1.00  3.12           O  
ATOM    189  CB  ALA A  26      17.759  31.137  21.675  1.00  4.29           C  
ATOM    190  N   LYS A  27      19.374  28.904  23.184  1.00  5.13           N  
ATOM    191  CA  LYS A  27      19.833  28.283  24.416  1.00  5.92           C  
ATOM    192  C   LYS A  27      21.326  28.114  24.301  1.00  6.20           C  
ATOM    193  O   LYS A  27      22.059  28.416  25.246  1.00  5.83           O  
ATOM    194  CB  LYS A  27      19.163  26.920  24.616  1.00  7.27           C  
ATOM    195  CG  LYS A  27      19.696  26.117  25.797  1.00 11.74           C  
ATOM    196  CD  LYS A  27      18.906  24.836  26.031  1.00 14.61           C  
ATOM    197  CE  LYS A  27      19.655  23.939  27.006  1.00 20.12           C  
ATOM    198  NZ  LYS A  27      18.870  22.779  27.502  1.00 21.20           N  
ATOM    199  N   ALA A  28      21.782  27.675  23.130  1.00  5.81           N  
ATOM    200  CA  ALA A  28      23.222  27.495  22.908  1.00  7.97           C  
ATOM    201  C   ALA A  28      23.959  28.835  23.048  1.00  7.86           C  
ATOM    202  O   ALA A  28      25.118  28.883  23.498  1.00  7.92           O  
ATOM    203  CB  ALA A  28      23.486  26.869  21.514  1.00  5.94           C  
ATOM    204  N   ALA A  29      23.288  29.918  22.665  1.00  7.35           N  
ATOM    205  CA  ALA A  29      23.856  31.257  22.762  1.00  6.96           C  
ATOM    206  C   ALA A  29      23.851  31.824  24.195  1.00  5.98           C  
ATOM    207  O   ALA A  29      24.476  32.844  24.455  1.00  7.71           O  
ATOM    208  CB  ALA A  29      23.137  32.210  21.796  1.00  7.77           C  
ATOM    209  N   GLY A  30      23.181  31.156  25.126  1.00  5.48           N  
ATOM    210  CA  GLY A  30      23.166  31.641  26.495  1.00  5.33           C  
ATOM    211  C   GLY A  30      21.873  32.283  26.976  1.00  5.50           C  
ATOM    212  O   GLY A  30      21.799  32.786  28.105  1.00  5.17           O  
ATOM    213  N   TYR A  31      20.864  32.323  26.116  1.00  5.31           N  
ATOM    214  CA  TYR A  31      19.573  32.894  26.486  1.00  6.01           C  
ATOM    215  C   TYR A  31      18.704  31.981  27.373  1.00  5.47           C  
ATOM    216  O   TYR A  31      18.864  30.746  27.412  1.00  5.06           O  
ATOM    217  CB  TYR A  31      18.764  33.272  25.229  1.00  5.01           C  
ATOM    218  CG  TYR A  31      19.345  34.415  24.420  1.00  4.93           C  
ATOM    219  CD1 TYR A  31      19.134  35.740  24.803  1.00  7.19           C  
ATOM    220  CD2 TYR A  31      20.098  34.175  23.268  1.00  4.26           C  
ATOM    221  CE1 TYR A  31      19.658  36.793  24.059  1.00  6.83           C  
ATOM    222  CE2 TYR A  31      20.619  35.223  22.516  1.00  5.76           C  
ATOM    223  CZ  TYR A  31      20.392  36.526  22.918  1.00  7.85           C  
ATOM    224  OH  TYR A  31      20.860  37.583  22.182  1.00 10.66           O  
ATOM    225  N   ARG A  32      17.835  32.639  28.138  1.00  6.43           N  
ATOM    226  CA  ARG A  32      16.841  31.994  29.003  1.00  7.68           C  
ATOM    227  C   ARG A  32      15.631  32.026  28.077  1.00  4.32           C  
ATOM    228  O   ARG A  32      15.016  33.073  27.874  1.00  5.34           O  
ATOM    229  CB  ARG A  32      16.619  32.822  30.272  1.00  7.69           C  
ATOM    230  CG  ARG A  32      17.801  32.751  31.211  1.00  9.29           C  
ATOM    231  CD  ARG A  32      17.716  33.786  32.310  1.00 13.65           C  
ATOM    232  NE  ARG A  32      16.435  33.744  33.010  1.00 16.37           N  
ATOM    233  CZ  ARG A  32      16.119  32.880  33.976  1.00 17.81           C  
ATOM    234  NH1 ARG A  32      17.002  31.959  34.380  1.00 17.88           N  
ATOM    235  NH2 ARG A  32      14.905  32.932  34.529  1.00 15.40           N  
ATOM    236  N   THR A  33      15.362  30.884  27.464  1.00  4.53           N  
ATOM    237  CA  THR A  33      14.328  30.766  26.444  1.00  3.95           C  
ATOM    238  C   THR A  33      12.935  30.248  26.831  1.00  4.49           C  
ATOM    239  O   THR A  33      12.757  29.509  27.804  1.00  2.34           O  
ATOM    240  CB  THR A  33      14.853  29.893  25.277  1.00  2.50           C  
ATOM    241  OG1 THR A  33      14.963  28.543  25.718  1.00  4.38           O  
ATOM    242  CG2 THR A  33      16.240  30.348  24.806  1.00  2.66           C  
ATOM    243  N   ALA A  34      11.957  30.623  26.016  1.00  4.04           N  
ATOM    244  CA  ALA A  34      10.574  30.199  26.203  1.00  7.15           C  
ATOM    245  C   ALA A  34       9.873  30.221  24.839  1.00  6.62           C  
ATOM    246  O   ALA A  34      10.079  31.154  24.037  1.00  6.65           O  
ATOM    247  CB  ALA A  34       9.834  31.124  27.185  1.00  3.18           C  
ATOM    248  N   GLY A  35       9.178  29.122  24.541  1.00  5.63           N  
ATOM    249  CA  GLY A  35       8.393  29.020  23.320  1.00  4.58           C  
ATOM    250  C   GLY A  35       6.956  29.326  23.743  1.00  3.94           C  
ATOM    251  O   GLY A  35       6.538  28.964  24.854  1.00  4.11           O  
ATOM    252  N   TYR A  36       6.193  29.982  22.880  1.00  2.28           N  
ATOM    253  CA  TYR A  36       4.824  30.347  23.193  1.00  2.37           C  
ATOM    254  C   TYR A  36       3.934  29.981  21.995  1.00  2.11           C  
ATOM    255  O   TYR A  36       4.205  30.386  20.874  1.00  2.02           O  
ATOM    256  CB  TYR A  36       4.766  31.862  23.471  1.00  2.00           C  
ATOM    257  CG  TYR A  36       3.427  32.408  23.959  1.00  2.23           C  
ATOM    258  CD1 TYR A  36       2.695  31.755  24.952  1.00  2.04           C  
ATOM    259  CD2 TYR A  36       2.913  33.599  23.444  1.00  4.24           C  
ATOM    260  CE1 TYR A  36       1.485  32.279  25.431  1.00  2.00           C  
ATOM    261  CE2 TYR A  36       1.707  34.136  23.916  1.00  3.28           C  
ATOM    262  CZ  TYR A  36       0.999  33.464  24.904  1.00  4.08           C  
ATOM    263  OH  TYR A  36      -0.203  33.976  25.346  1.00  2.78           O  
ATOM    264  N   LYS A  37       2.895  29.191  22.248  1.00  2.01           N  
ATOM    265  CA  LYS A  37       1.929  28.770  21.225  1.00  3.63           C  
ATOM    266  C   LYS A  37       0.581  29.200  21.825  1.00  2.05           C  
ATOM    267  O   LYS A  37      -0.156  28.368  22.338  1.00  4.10           O  
ATOM    268  CB  LYS A  37       2.004  27.233  21.050  1.00  4.52           C  
ATOM    269  CG  LYS A  37       1.012  26.612  20.049  1.00  6.93           C  
ATOM    270  CD  LYS A  37       1.433  26.786  18.579  1.00  8.27           C  
ATOM    271  CE  LYS A  37       0.431  26.100  17.626  1.00  5.91           C  
ATOM    272  NZ  LYS A  37       0.898  26.147  16.204  1.00  5.06           N  
ATOM    273  N   PRO A  38       0.224  30.502  21.718  1.00  2.95           N  
ATOM    274  CA  PRO A  38      -1.027  30.991  22.284  1.00  3.50           C  
ATOM    275  C   PRO A  38      -2.283  30.282  21.865  1.00  3.02           C  
ATOM    276  O   PRO A  38      -3.117  29.981  22.698  1.00  2.79           O  
ATOM    277  CB  PRO A  38      -1.042  32.480  21.905  1.00  2.57           C  
ATOM    278  CG  PRO A  38      -0.229  32.547  20.679  1.00  3.92           C  
ATOM    279  CD  PRO A  38       0.906  31.587  20.989  1.00  2.69           C  
ATOM    280  N   VAL A  39      -2.396  29.962  20.592  1.00  3.00           N  
ATOM    281  CA  VAL A  39      -3.599  29.297  20.110  1.00  4.04           C  
ATOM    282  C   VAL A  39      -3.215  28.006  19.406  1.00  5.08           C  
ATOM    283  O   VAL A  39      -2.369  28.004  18.499  1.00  5.19           O  
ATOM    284  CB  VAL A  39      -4.390  30.237  19.148  1.00  4.14           C  
ATOM    285  CG1 VAL A  39      -5.522  29.471  18.419  1.00  2.72           C  
ATOM    286  CG2 VAL A  39      -4.957  31.412  19.935  1.00  3.43           C  
ATOM    287  N   ALA A  40      -3.835  26.906  19.823  1.00  5.19           N  
ATOM    288  CA  ALA A  40      -3.545  25.605  19.226  1.00  7.28           C  
ATOM    289  C   ALA A  40      -4.823  24.792  18.908  1.00  6.34           C  
ATOM    290  O   ALA A  40      -5.822  24.849  19.638  1.00  6.06           O  
ATOM    291  CB  ALA A  40      -2.572  24.809  20.158  1.00  3.44           C  
ATOM    292  N   SER A  41      -4.796  24.079  17.788  1.00  6.94           N  
ATOM    293  CA  SER A  41      -5.910  23.231  17.374  1.00  6.52           C  
ATOM    294  C   SER A  41      -5.287  21.903  16.923  1.00  7.75           C  
ATOM    295  O   SER A  41      -4.189  21.889  16.334  1.00  8.07           O  
ATOM    296  CB  SER A  41      -6.729  23.875  16.239  1.00  8.37           C  
ATOM    297  OG  SER A  41      -5.971  24.044  15.043  1.00  6.64           O  
ATOM    298  N   GLY A  42      -5.979  20.797  17.189  1.00  6.81           N  
ATOM    299  CA  GLY A  42      -5.460  19.485  16.826  1.00  6.21           C  
ATOM    300  C   GLY A  42      -4.692  19.038  18.050  1.00  6.92           C  
ATOM    301  O   GLY A  42      -3.461  19.083  18.066  1.00  5.28           O  
ATOM    302  N   SER A  43      -5.436  18.595  19.062  1.00  6.67           N  
ATOM    303  CA  SER A  43      -4.868  18.208  20.354  1.00  7.04           C  
ATOM    304  C   SER A  43      -5.430  16.906  20.930  1.00  6.90           C  
ATOM    305  O   SER A  43      -6.574  16.534  20.652  1.00  8.43           O  
ATOM    306  CB  SER A  43      -5.118  19.350  21.341  1.00  6.43           C  
ATOM    307  OG  SER A  43      -4.662  20.591  20.808  1.00  6.75           O  
ATOM    308  N   GLU A  44      -4.620  16.230  21.744  1.00  7.10           N  
ATOM    309  CA  GLU A  44      -4.993  14.959  22.349  1.00  7.66           C  
ATOM    310  C   GLU A  44      -5.427  15.091  23.805  1.00  6.98           C  
ATOM    311  O   GLU A  44      -5.016  16.008  24.520  1.00  6.01           O  
ATOM    312  CB  GLU A  44      -3.825  13.970  22.261  1.00 11.38           C  
ATOM    313  CG  GLU A  44      -3.466  13.485  20.863  1.00 15.56           C  
ATOM    314  CD  GLU A  44      -2.854  14.573  19.976  1.00 19.35           C  
ATOM    315  OE1 GLU A  44      -1.854  15.199  20.399  1.00 19.57           O  
ATOM    316  OE2 GLU A  44      -3.373  14.795  18.851  1.00 19.06           O  
ATOM    317  N   LYS A  45      -6.291  14.182  24.231  1.00  5.29           N  
ATOM    318  CA  LYS A  45      -6.776  14.203  25.594  1.00  6.05           C  
ATOM    319  C   LYS A  45      -5.742  13.555  26.500  1.00  5.49           C  
ATOM    320  O   LYS A  45      -5.024  12.647  26.078  1.00  6.34           O  
ATOM    321  CB  LYS A  45      -8.087  13.436  25.724  1.00  8.37           C  
ATOM    322  CG  LYS A  45      -7.947  11.967  25.367  1.00 12.38           C  
ATOM    323  CD  LYS A  45      -9.171  11.171  25.759  1.00 17.25           C  
ATOM    324  CE  LYS A  45      -8.974   9.704  25.414  1.00 17.51           C  
ATOM    325  NZ  LYS A  45      -9.242   8.847  26.606  1.00 22.13           N  
ATOM    326  N   THR A  46      -5.615  14.083  27.709  1.00  5.75           N  
ATOM    327  CA  THR A  46      -4.713  13.514  28.724  1.00  7.52           C  
ATOM    328  C   THR A  46      -5.433  13.715  30.060  1.00  7.99           C  
ATOM    329  O   THR A  46      -6.499  14.362  30.113  1.00  7.61           O  
ATOM    330  CB  THR A  46      -3.274  14.191  28.787  1.00  6.21           C  
ATOM    331  OG1 THR A  46      -3.307  15.390  29.581  1.00  5.65           O  
ATOM    332  CG2 THR A  46      -2.724  14.473  27.399  1.00  4.91           C  
ATOM    333  N   PRO A  47      -4.883  13.151  31.155  1.00  7.02           N  
ATOM    334  CA  PRO A  47      -5.525  13.316  32.465  1.00  8.16           C  
ATOM    335  C   PRO A  47      -5.578  14.775  32.915  1.00  7.17           C  
ATOM    336  O   PRO A  47      -6.429  15.149  33.726  1.00  9.47           O  
ATOM    337  CB  PRO A  47      -4.627  12.496  33.398  1.00  7.55           C  
ATOM    338  CG  PRO A  47      -4.111  11.402  32.499  1.00  4.65           C  
ATOM    339  CD  PRO A  47      -3.812  12.137  31.206  1.00  4.59           C  
ATOM    340  N   GLU A  48      -4.672  15.598  32.397  1.00  4.89           N  
ATOM    341  CA  GLU A  48      -4.647  17.000  32.769  1.00  7.29           C  
ATOM    342  C   GLU A  48      -5.482  17.921  31.870  1.00  6.16           C  
ATOM    343  O   GLU A  48      -5.529  19.124  32.109  1.00  6.18           O  
ATOM    344  CB  GLU A  48      -3.220  17.508  32.772  1.00 11.24           C  
ATOM    345  CG  GLU A  48      -2.263  16.733  33.640  1.00 19.62           C  
ATOM    346  CD  GLU A  48      -1.057  17.580  33.997  1.00 24.75           C  
ATOM    347  OE1 GLU A  48      -1.237  18.480  34.855  1.00 29.14           O  
ATOM    348  OE2 GLU A  48       0.038  17.373  33.403  1.00 27.01           O  
ATOM    349  N   GLY A  49      -6.131  17.343  30.858  1.00  6.53           N  
ATOM    350  CA  GLY A  49      -6.918  18.108  29.903  1.00  6.33           C  
ATOM    351  C   GLY A  49      -6.277  17.929  28.539  1.00  4.41           C  
ATOM    352  O   GLY A  49      -5.381  17.103  28.376  1.00  4.85           O  
ATOM    353  N   LEU A  50      -6.659  18.756  27.577  1.00  6.58           N  
ATOM    354  CA  LEU A  50      -6.134  18.658  26.213  1.00  3.94           C  
ATOM    355  C   LEU A  50      -4.691  19.125  26.089  1.00  4.73           C  
ATOM    356  O   LEU A  50      -4.295  20.100  26.724  1.00  5.09           O  
ATOM    357  CB  LEU A  50      -7.046  19.440  25.249  1.00  6.21           C  
ATOM    358  CG  LEU A  50      -8.527  18.990  25.198  1.00  7.00           C  
ATOM    359  CD1 LEU A  50      -9.309  19.882  24.244  1.00  7.53           C  
ATOM    360  CD2 LEU A  50      -8.649  17.519  24.760  1.00 10.46           C  
ATOM    361  N   ARG A  51      -3.905  18.422  25.281  1.00  4.27           N  
ATOM    362  CA  ARG A  51      -2.500  18.770  25.081  1.00  4.28           C  
ATOM    363  C   ARG A  51      -2.149  18.789  23.589  1.00  5.25           C  
ATOM    364  O   ARG A  51      -2.417  17.827  22.873  1.00  5.86           O  
ATOM    365  CB  ARG A  51      -1.615  17.756  25.802  1.00  6.32           C  
ATOM    366  CG  ARG A  51      -1.680  17.822  27.337  1.00  5.80           C  
ATOM    367  CD  ARG A  51      -1.105  19.130  27.817  1.00  4.82           C  
ATOM    368  NE  ARG A  51      -1.037  19.261  29.276  1.00  6.59           N  
ATOM    369  CZ  ARG A  51      -1.876  19.991  30.006  1.00  7.26           C  
ATOM    370  NH1 ARG A  51      -2.929  20.577  29.448  1.00  8.62           N  
ATOM    371  NH2 ARG A  51      -1.703  20.084  31.316  1.00  9.03           N  
ATOM    372  N   ASN A  52      -1.575  19.894  23.119  1.00  4.60           N  
ATOM    373  CA  ASN A  52      -1.182  20.053  21.709  1.00  3.26           C  
ATOM    374  C   ASN A  52       0.299  19.702  21.526  1.00  3.47           C  
ATOM    375  O   ASN A  52       1.148  20.185  22.268  1.00  3.46           O  
ATOM    376  CB  ASN A  52      -1.451  21.504  21.279  1.00  3.73           C  
ATOM    377  CG  ASN A  52      -0.947  21.809  19.886  1.00  4.28           C  
ATOM    378  OD1 ASN A  52       0.125  22.382  19.706  1.00  7.60           O  
ATOM    379  ND2 ASN A  52      -1.685  21.391  18.900  1.00  2.03           N  
ATOM    380  N   SER A  53       0.613  18.913  20.502  1.00  5.13           N  
ATOM    381  CA  SER A  53       1.992  18.483  20.224  1.00  4.96           C  
ATOM    382  C   SER A  53       2.985  19.611  19.944  1.00  3.37           C  
ATOM    383  O   SER A  53       4.144  19.484  20.291  1.00  3.80           O  
ATOM    384  CB  SER A  53       2.026  17.438  19.095  1.00  5.43           C  
ATOM    385  OG  SER A  53       1.679  18.006  17.851  1.00  7.55           O  
ATOM    386  N   ASP A  54       2.550  20.676  19.270  1.00  2.85           N  
ATOM    387  CA  ASP A  54       3.413  21.836  19.003  1.00  3.87           C  
ATOM    388  C   ASP A  54       3.782  22.482  20.338  1.00  2.98           C  
ATOM    389  O   ASP A  54       4.935  22.800  20.608  1.00  4.31           O  
ATOM    390  CB  ASP A  54       2.671  22.910  18.187  1.00  5.92           C  
ATOM    391  CG  ASP A  54       2.422  22.509  16.748  1.00  4.03           C  
ATOM    392  OD1 ASP A  54       2.540  21.321  16.406  1.00  5.39           O  
ATOM    393  OD2 ASP A  54       2.111  23.426  15.950  1.00  4.43           O  
ATOM    394  N   ALA A  55       2.769  22.695  21.163  1.00  4.85           N  
ATOM    395  CA  ALA A  55       2.965  23.297  22.468  1.00  3.88           C  
ATOM    396  C   ALA A  55       3.932  22.423  23.275  1.00  5.11           C  
ATOM    397  O   ALA A  55       4.846  22.935  23.927  1.00  3.52           O  
ATOM    398  CB  ALA A  55       1.614  23.438  23.184  1.00  3.19           C  
ATOM    399  N   LEU A  56       3.759  21.106  23.198  1.00  4.43           N  
ATOM    400  CA  LEU A  56       4.654  20.201  23.915  1.00  5.24           C  
ATOM    401  C   LEU A  56       6.078  20.289  23.383  1.00  5.55           C  
ATOM    402  O   LEU A  56       7.031  20.268  24.173  1.00  4.86           O  
ATOM    403  CB  LEU A  56       4.160  18.762  23.856  1.00  5.66           C  
ATOM    404  CG  LEU A  56       2.869  18.435  24.613  1.00  6.44           C  
ATOM    405  CD1 LEU A  56       2.590  16.946  24.457  1.00  6.93           C  
ATOM    406  CD2 LEU A  56       2.976  18.805  26.089  1.00  5.98           C  
ATOM    407  N   ALA A  57       6.240  20.409  22.060  1.00  5.82           N  
ATOM    408  CA  ALA A  57       7.590  20.526  21.475  1.00  5.06           C  
ATOM    409  C   ALA A  57       8.283  21.831  21.910  1.00  4.93           C  
ATOM    410  O   ALA A  57       9.473  21.844  22.257  1.00  4.85           O  
ATOM    411  CB  ALA A  57       7.548  20.419  19.947  1.00  2.65           C  
ATOM    412  N   LEU A  58       7.536  22.927  21.899  1.00  5.14           N  
ATOM    413  CA  LEU A  58       8.066  24.219  22.316  1.00  5.25           C  
ATOM    414  C   LEU A  58       8.424  24.184  23.816  1.00  6.84           C  
ATOM    415  O   LEU A  58       9.477  24.685  24.208  1.00  6.44           O  
ATOM    416  CB  LEU A  58       7.060  25.339  22.029  1.00  6.79           C  
ATOM    417  CG  LEU A  58       6.749  25.699  20.576  1.00  5.62           C  
ATOM    418  CD1 LEU A  58       5.856  26.910  20.567  1.00  7.05           C  
ATOM    419  CD2 LEU A  58       8.002  25.994  19.801  1.00  4.51           C  
ATOM    420  N   GLN A  59       7.547  23.598  24.637  1.00  5.76           N  
ATOM    421  CA  GLN A  59       7.775  23.461  26.078  1.00  6.96           C  
ATOM    422  C   GLN A  59       9.086  22.678  26.361  1.00  7.25           C  
ATOM    423  O   GLN A  59       9.929  23.146  27.128  1.00  6.98           O  
ATOM    424  CB  GLN A  59       6.566  22.777  26.723  1.00  5.60           C  
ATOM    425  CG  GLN A  59       6.728  22.463  28.205  1.00  8.64           C  
ATOM    426  CD  GLN A  59       5.528  21.742  28.800  1.00  6.06           C  
ATOM    427  OE1 GLN A  59       4.969  20.819  28.211  1.00  6.58           O  
ATOM    428  NE2 GLN A  59       5.137  22.160  29.985  1.00  6.24           N  
ATOM    429  N   ARG A  60       9.253  21.516  25.717  1.00  8.75           N  
ATOM    430  CA  ARG A  60      10.454  20.658  25.846  1.00 10.10           C  
ATOM    431  C   ARG A  60      11.732  21.368  25.404  1.00  9.51           C  
ATOM    432  O   ARG A  60      12.815  21.109  25.923  1.00  7.47           O  
ATOM    433  CB  ARG A  60      10.338  19.405  24.951  1.00 10.59           C  
ATOM    434  CG  ARG A  60       9.162  18.526  25.247  1.00 16.65           C  
ATOM    435  CD  ARG A  60       9.076  17.317  24.350  1.00 14.53           C  
ATOM    436  NE  ARG A  60       7.844  16.601  24.663  1.00 18.65           N  
ATOM    437  CZ  ARG A  60       6.950  16.200  23.758  1.00 20.17           C  
ATOM    438  NH1 ARG A  60       7.142  16.438  22.468  1.00 21.19           N  
ATOM    439  NH2 ARG A  60       5.862  15.542  24.141  1.00 19.27           N  
ATOM    440  N   ASN A  61      11.614  22.169  24.351  1.00  9.54           N  
ATOM    441  CA  ASN A  61      12.767  22.870  23.830  1.00  8.06           C  
ATOM    442  C   ASN A  61      13.090  24.220  24.470  1.00  8.34           C  
ATOM    443  O   ASN A  61      14.037  24.890  24.050  1.00 10.09           O  
ATOM    444  CB  ASN A  61      12.694  22.953  22.303  1.00 10.25           C  
ATOM    445  CG  ASN A  61      13.051  21.625  21.629  1.00 11.37           C  
ATOM    446  OD1 ASN A  61      14.224  21.276  21.514  1.00 13.33           O  
ATOM    447  ND2 ASN A  61      12.043  20.871  21.214  1.00  8.45           N  
ATOM    448  N   SER A  62      12.332  24.608  25.498  1.00  6.64           N  
ATOM    449  CA  SER A  62      12.582  25.853  26.234  1.00  6.44           C  
ATOM    450  C   SER A  62      13.643  25.508  27.288  1.00  7.43           C  
ATOM    451  O   SER A  62      13.620  24.415  27.843  1.00  7.44           O  
ATOM    452  CB  SER A  62      11.320  26.331  26.947  1.00  7.78           C  
ATOM    453  OG  SER A  62      10.329  26.788  26.042  1.00  8.00           O  
ATOM    454  N   SER A  63      14.584  26.413  27.539  1.00  9.51           N  
ATOM    455  CA  SER A  63      15.644  26.156  28.515  1.00  9.15           C  
ATOM    456  C   SER A  63      15.071  26.207  29.926  1.00 10.93           C  
ATOM    457  O   SER A  63      15.607  25.582  30.840  1.00 12.65           O  
ATOM    458  CB  SER A  63      16.789  27.167  28.364  1.00  8.01           C  
ATOM    459  OG  SER A  63      16.398  28.497  28.716  1.00  7.41           O  
ATOM    460  N   LEU A  64      13.986  26.961  30.095  1.00 11.44           N  
ATOM    461  CA  LEU A  64      13.308  27.097  31.387  1.00 13.36           C  
ATOM    462  C   LEU A  64      12.220  26.034  31.536  1.00 14.65           C  
ATOM    463  O   LEU A  64      11.651  25.567  30.545  1.00 14.13           O  
ATOM    464  CB  LEU A  64      12.657  28.483  31.490  1.00 15.26           C  
ATOM    465  CG  LEU A  64      13.557  29.720  31.403  1.00 17.79           C  
ATOM    466  CD1 LEU A  64      12.732  30.962  31.149  1.00 16.14           C  
ATOM    467  CD2 LEU A  64      14.398  29.849  32.682  1.00 18.19           C  
ATOM    468  N   GLN A  65      11.939  25.625  32.766  1.00 14.97           N  
ATOM    469  CA  GLN A  65      10.872  24.660  32.970  1.00 16.43           C  
ATOM    470  C   GLN A  65       9.594  25.484  33.027  1.00 14.75           C  
ATOM    471  O   GLN A  65       9.427  26.328  33.913  1.00 14.13           O  
ATOM    472  CB  GLN A  65      11.077  23.851  34.245  1.00 22.51           C  
ATOM    473  CG  GLN A  65      12.175  22.797  34.119  1.00 30.93           C  
ATOM    474  CD  GLN A  65      11.784  21.471  34.755  1.00 34.90           C  
ATOM    475  OE1 GLN A  65      11.918  20.413  34.137  1.00 37.21           O  
ATOM    476  NE2 GLN A  65      11.299  21.523  35.995  1.00 36.94           N  
ATOM    477  N   LEU A  66       8.730  25.285  32.036  1.00 11.53           N  
ATOM    478  CA  LEU A  66       7.490  26.036  31.938  1.00  8.75           C  
ATOM    479  C   LEU A  66       6.268  25.173  32.122  1.00  6.01           C  
ATOM    480  O   LEU A  66       6.291  23.998  31.777  1.00  6.33           O  
ATOM    481  CB  LEU A  66       7.418  26.707  30.572  1.00  6.61           C  
ATOM    482  CG  LEU A  66       8.603  27.632  30.321  1.00  9.58           C  
ATOM    483  CD1 LEU A  66       8.706  27.977  28.841  1.00  9.86           C  
ATOM    484  CD2 LEU A  66       8.464  28.882  31.170  1.00  8.91           C  
ATOM    485  N   ASP A  67       5.222  25.744  32.723  1.00  5.99           N  
ATOM    486  CA  ASP A  67       3.945  25.042  32.892  1.00  5.46           C  
ATOM    487  C   ASP A  67       3.254  25.031  31.524  1.00  4.12           C  
ATOM    488  O   ASP A  67       3.316  26.011  30.779  1.00  5.11           O  
ATOM    489  CB  ASP A  67       3.028  25.766  33.887  1.00  7.21           C  
ATOM    490  CG  ASP A  67       3.633  25.872  35.269  1.00  8.74           C  
ATOM    491  OD1 ASP A  67       4.149  24.845  35.747  1.00 12.14           O  
ATOM    492  OD2 ASP A  67       3.580  26.968  35.865  1.00 10.42           O  
ATOM    493  N   TYR A  68       2.557  23.947  31.227  1.00  4.65           N  
ATOM    494  CA  TYR A  68       1.851  23.820  29.960  1.00  5.14           C  
ATOM    495  C   TYR A  68       0.976  25.027  29.624  1.00  3.96           C  
ATOM    496  O   TYR A  68       1.092  25.585  28.520  1.00  4.84           O  
ATOM    497  CB  TYR A  68       0.983  22.548  29.906  1.00  3.44           C  
ATOM    498  CG  TYR A  68       0.382  22.373  28.513  1.00  4.96           C  
ATOM    499  CD1 TYR A  68       1.158  21.878  27.458  1.00  5.22           C  
ATOM    500  CD2 TYR A  68      -0.918  22.791  28.228  1.00  3.49           C  
ATOM    501  CE1 TYR A  68       0.655  21.814  26.155  1.00  4.13           C  
ATOM    502  CE2 TYR A  68      -1.433  22.725  26.920  1.00  3.46           C  
ATOM    503  CZ  TYR A  68      -0.639  22.239  25.896  1.00  3.70           C  
ATOM    504  OH  TYR A  68      -1.128  22.197  24.614  1.00  3.49           O  
ATOM    505  N   ALA A  69       0.105  25.425  30.551  1.00  3.24           N  
ATOM    506  CA  ALA A  69      -0.800  26.554  30.305  1.00  4.80           C  
ATOM    507  C   ALA A  69      -0.112  27.865  29.972  1.00  4.58           C  
ATOM    508  O   ALA A  69      -0.662  28.695  29.247  1.00  4.45           O  
ATOM    509  CB  ALA A  69      -1.762  26.741  31.470  1.00  3.61           C  
ATOM    510  N   THR A  70       1.092  28.053  30.494  1.00  5.24           N  
ATOM    511  CA  THR A  70       1.861  29.259  30.237  1.00  5.20           C  
ATOM    512  C   THR A  70       2.335  29.241  28.771  1.00  4.64           C  
ATOM    513  O   THR A  70       2.426  30.281  28.114  1.00  4.18           O  
ATOM    514  CB  THR A  70       3.061  29.378  31.235  1.00  5.01           C  
ATOM    515  OG1 THR A  70       2.571  29.271  32.580  1.00  4.69           O  
ATOM    516  CG2 THR A  70       3.723  30.700  31.095  1.00  7.72           C  
ATOM    517  N   VAL A  71       2.607  28.046  28.262  1.00  4.49           N  
ATOM    518  CA  VAL A  71       3.028  27.886  26.871  1.00  5.36           C  
ATOM    519  C   VAL A  71       1.833  27.936  25.909  1.00  4.03           C  
ATOM    520  O   VAL A  71       1.915  28.565  24.853  1.00  2.52           O  
ATOM    521  CB  VAL A  71       3.815  26.558  26.661  1.00  5.74           C  
ATOM    522  CG1 VAL A  71       4.174  26.365  25.163  1.00  7.09           C  
ATOM    523  CG2 VAL A  71       5.091  26.572  27.534  1.00  3.20           C  
ATOM    524  N   ASN A  72       0.699  27.381  26.327  1.00  2.00           N  
ATOM    525  CA  ASN A  72      -0.476  27.322  25.454  1.00  2.02           C  
ATOM    526  C   ASN A  72      -1.820  27.495  26.187  1.00  3.58           C  
ATOM    527  O   ASN A  72      -2.448  26.515  26.613  1.00  3.91           O  
ATOM    528  CB  ASN A  72      -0.443  25.997  24.671  1.00  2.00           C  
ATOM    529  CG  ASN A  72      -1.704  25.760  23.863  1.00  3.67           C  
ATOM    530  OD1 ASN A  72      -2.270  24.670  23.861  1.00  5.80           O  
ATOM    531  ND2 ASN A  72      -2.145  26.789  23.166  1.00  3.26           N  
ATOM    532  N   PRO A  73      -2.273  28.754  26.331  1.00  3.79           N  
ATOM    533  CA  PRO A  73      -3.522  29.129  26.997  1.00  5.56           C  
ATOM    534  C   PRO A  73      -4.787  28.587  26.346  1.00  5.02           C  
ATOM    535  O   PRO A  73      -5.761  28.313  27.035  1.00  7.80           O  
ATOM    536  CB  PRO A  73      -3.502  30.655  26.912  1.00  5.38           C  
ATOM    537  CG  PRO A  73      -2.069  30.999  26.867  1.00  5.30           C  
ATOM    538  CD  PRO A  73      -1.500  29.954  25.970  1.00  4.97           C  
ATOM    539  N   TYR A  74      -4.781  28.481  25.021  1.00  5.37           N  
ATOM    540  CA  TYR A  74      -5.943  28.029  24.261  1.00  3.96           C  
ATOM    541  C   TYR A  74      -5.665  26.720  23.504  1.00  4.49           C  
ATOM    542  O   TYR A  74      -4.957  26.715  22.504  1.00  2.81           O  
ATOM    543  CB  TYR A  74      -6.355  29.122  23.262  1.00  5.80           C  
ATOM    544  CG  TYR A  74      -6.890  30.404  23.872  1.00  2.86           C  
ATOM    545  CD1 TYR A  74      -8.143  30.432  24.496  1.00  5.39           C  
ATOM    546  CD2 TYR A  74      -6.181  31.599  23.764  1.00  3.44           C  
ATOM    547  CE1 TYR A  74      -8.684  31.625  24.980  1.00  4.22           C  
ATOM    548  CE2 TYR A  74      -6.708  32.795  24.244  1.00  3.87           C  
ATOM    549  CZ  TYR A  74      -7.957  32.802  24.852  1.00  3.97           C  
ATOM    550  OH  TYR A  74      -8.495  33.982  25.303  1.00  2.67           O  
ATOM    551  N   THR A  75      -6.303  25.638  23.941  1.00  3.96           N  
ATOM    552  CA  THR A  75      -6.118  24.320  23.352  1.00  3.63           C  
ATOM    553  C   THR A  75      -7.438  23.725  22.852  1.00  6.24           C  
ATOM    554  O   THR A  75      -8.366  23.467  23.638  1.00  6.47           O  
ATOM    555  CB  THR A  75      -5.534  23.367  24.409  1.00  3.55           C  
ATOM    556  OG1 THR A  75      -4.522  24.063  25.146  1.00  5.19           O  
ATOM    557  CG2 THR A  75      -4.922  22.128  23.753  1.00  2.08           C  
ATOM    558  N   PHE A  76      -7.519  23.463  21.552  1.00  5.17           N  
ATOM    559  CA  PHE A  76      -8.730  22.894  20.979  1.00  5.89           C  
ATOM    560  C   PHE A  76      -8.377  21.519  20.406  1.00  4.96           C  
ATOM    561  O   PHE A  76      -7.332  21.354  19.773  1.00  5.62           O  
ATOM    562  CB  PHE A  76      -9.283  23.839  19.892  1.00  6.29           C  
ATOM    563  CG  PHE A  76      -9.719  25.195  20.415  1.00  3.74           C  
ATOM    564  CD1 PHE A  76     -10.956  25.352  21.020  1.00  5.95           C  
ATOM    565  CD2 PHE A  76      -8.906  26.315  20.271  1.00  4.48           C  
ATOM    566  CE1 PHE A  76     -11.383  26.602  21.472  1.00  5.44           C  
ATOM    567  CE2 PHE A  76      -9.331  27.582  20.725  1.00  4.83           C  
ATOM    568  CZ  PHE A  76     -10.574  27.716  21.325  1.00  5.81           C  
ATOM    569  N   ALA A  77      -9.228  20.528  20.651  1.00  5.55           N  
ATOM    570  CA  ALA A  77      -8.979  19.166  20.174  1.00  4.76           C  
ATOM    571  C   ALA A  77      -9.000  19.016  18.652  1.00  5.48           C  
ATOM    572  O   ALA A  77      -8.137  18.379  18.054  1.00  5.01           O  
ATOM    573  CB  ALA A  77      -9.998  18.190  20.805  1.00  5.13           C  
ATOM    574  N   GLU A  78     -10.002  19.614  18.028  1.00  6.08           N  
ATOM    575  CA  GLU A  78     -10.172  19.477  16.603  1.00  6.27           C  
ATOM    576  C   GLU A  78      -9.157  20.244  15.764  1.00  5.70           C  
ATOM    577  O   GLU A  78      -8.907  21.421  16.005  1.00  7.05           O  
ATOM    578  CB  GLU A  78     -11.606  19.845  16.214  1.00  5.07           C  
ATOM    579  CG  GLU A  78     -11.864  19.698  14.735  1.00  7.96           C  
ATOM    580  CD  GLU A  78     -13.293  20.005  14.345  1.00 10.79           C  
ATOM    581  OE1 GLU A  78     -14.209  19.886  15.191  1.00  8.74           O  
ATOM    582  OE2 GLU A  78     -13.488  20.354  13.169  1.00 11.17           O  
ATOM    583  N   PRO A  79      -8.529  19.557  14.792  1.00  7.27           N  
ATOM    584  CA  PRO A  79      -7.525  20.145  13.887  1.00  9.01           C  
ATOM    585  C   PRO A  79      -8.143  20.939  12.715  1.00  8.13           C  
ATOM    586  O   PRO A  79      -8.110  20.491  11.565  1.00  8.18           O  
ATOM    587  CB  PRO A  79      -6.748  18.920  13.407  1.00  9.74           C  
ATOM    588  CG  PRO A  79      -7.821  17.846  13.348  1.00  8.87           C  
ATOM    589  CD  PRO A  79      -8.616  18.089  14.616  1.00  7.57           C  
ATOM    590  N   THR A  80      -8.694  22.112  13.025  1.00  6.58           N  
ATOM    591  CA  THR A  80      -9.332  22.980  12.033  1.00  7.62           C  
ATOM    592  C   THR A  80      -8.953  24.438  12.345  1.00  6.79           C  
ATOM    593  O   THR A  80      -8.157  24.692  13.255  1.00  6.95           O  
ATOM    594  CB  THR A  80     -10.900  22.774  12.033  1.00  6.80           C  
ATOM    595  OG1 THR A  80     -11.486  23.467  10.923  1.00  7.71           O  
ATOM    596  CG2 THR A  80     -11.535  23.281  13.326  1.00  5.11           C  
ATOM    597  N   SER A  81      -9.481  25.395  11.588  1.00  4.82           N  
ATOM    598  CA  SER A  81      -9.157  26.802  11.834  1.00  3.93           C  
ATOM    599  C   SER A  81      -9.650  27.179  13.247  1.00  2.00           C  
ATOM    600  O   SER A  81     -10.760  26.824  13.644  1.00  2.00           O  
ATOM    601  CB  SER A  81      -9.777  27.688  10.740  1.00  2.78           C  
ATOM    602  OG  SER A  81      -9.305  29.021  10.810  1.00  5.71           O  
ATOM    603  N   PRO A  82      -8.803  27.866  14.037  1.00  3.34           N  
ATOM    604  CA  PRO A  82      -9.121  28.291  15.407  1.00  3.79           C  
ATOM    605  C   PRO A  82     -10.485  28.961  15.555  1.00  5.32           C  
ATOM    606  O   PRO A  82     -11.237  28.649  16.481  1.00  5.53           O  
ATOM    607  CB  PRO A  82      -7.983  29.257  15.734  1.00  2.92           C  
ATOM    608  CG  PRO A  82      -6.818  28.621  15.031  1.00  4.47           C  
ATOM    609  CD  PRO A  82      -7.433  28.262  13.677  1.00  2.11           C  
ATOM    610  N   HIS A  83     -10.821  29.861  14.632  1.00  4.83           N  
ATOM    611  CA  HIS A  83     -12.107  30.542  14.723  1.00  4.79           C  
ATOM    612  C   HIS A  83     -13.360  29.629  14.634  1.00  3.46           C  
ATOM    613  O   HIS A  83     -14.353  29.872  15.328  1.00  2.43           O  
ATOM    614  CB  HIS A  83     -12.165  31.713  13.723  1.00  2.56           C  
ATOM    615  CG  HIS A  83     -12.526  31.323  12.326  1.00  2.56           C  
ATOM    616  ND1 HIS A  83     -11.734  30.510  11.546  1.00  2.06           N  
ATOM    617  CD2 HIS A  83     -13.599  31.650  11.576  1.00  2.12           C  
ATOM    618  CE1 HIS A  83     -12.310  30.353  10.367  1.00  2.83           C  
ATOM    619  NE2 HIS A  83     -13.441  31.034  10.360  1.00  2.17           N  
ATOM    620  N   ILE A  84     -13.280  28.561  13.838  1.00  3.70           N  
ATOM    621  CA  ILE A  84     -14.386  27.623  13.641  1.00  3.80           C  
ATOM    622  C   ILE A  84     -14.650  26.806  14.891  1.00  4.27           C  
ATOM    623  O   ILE A  84     -15.782  26.724  15.349  1.00  3.56           O  
ATOM    624  CB  ILE A  84     -14.102  26.658  12.476  1.00  2.00           C  
ATOM    625  CG1 ILE A  84     -14.129  27.420  11.160  1.00  2.52           C  
ATOM    626  CG2 ILE A  84     -15.117  25.524  12.454  1.00  4.38           C  
ATOM    627  CD1 ILE A  84     -13.725  26.566   9.994  1.00  4.18           C  
ATOM    628  N   ILE A  85     -13.608  26.175  15.426  1.00  6.03           N  
ATOM    629  CA  ILE A  85     -13.738  25.374  16.640  1.00  6.01           C  
ATOM    630  C   ILE A  85     -13.993  26.241  17.914  1.00  5.84           C  
ATOM    631  O   ILE A  85     -14.732  25.833  18.812  1.00  6.49           O  
ATOM    632  CB  ILE A  85     -12.529  24.397  16.797  1.00  6.20           C  
ATOM    633  CG1 ILE A  85     -12.747  23.468  17.992  1.00  6.09           C  
ATOM    634  CG2 ILE A  85     -11.202  25.161  16.911  1.00  5.59           C  
ATOM    635  CD1 ILE A  85     -13.965  22.593  17.838  1.00  7.33           C  
ATOM    636  N   SER A  86     -13.421  27.441  17.972  1.00  4.07           N  
ATOM    637  CA  SER A  86     -13.657  28.350  19.097  1.00  5.15           C  
ATOM    638  C   SER A  86     -15.149  28.737  19.149  1.00  6.08           C  
ATOM    639  O   SER A  86     -15.771  28.720  20.230  1.00  6.15           O  
ATOM    640  CB  SER A  86     -12.783  29.604  18.954  1.00  6.80           C  
ATOM    641  OG  SER A  86     -13.301  30.691  19.698  1.00  8.22           O  
ATOM    642  N   ALA A  87     -15.735  29.043  17.983  1.00  5.25           N  
ATOM    643  CA  ALA A  87     -17.158  29.400  17.931  1.00  4.76           C  
ATOM    644  C   ALA A  87     -18.042  28.212  18.307  1.00  4.79           C  
ATOM    645  O   ALA A  87     -18.939  28.356  19.137  1.00  7.80           O  
ATOM    646  CB  ALA A  87     -17.547  29.963  16.563  1.00  3.76           C  
ATOM    647  N   GLN A  88     -17.752  27.036  17.749  1.00  6.60           N  
ATOM    648  CA  GLN A  88     -18.516  25.814  18.005  1.00  9.42           C  
ATOM    649  C   GLN A  88     -18.474  25.428  19.482  1.00 11.25           C  
ATOM    650  O   GLN A  88     -19.464  24.941  20.039  1.00 10.19           O  
ATOM    651  CB  GLN A  88     -17.966  24.656  17.168  1.00 12.81           C  
ATOM    652  CG  GLN A  88     -18.782  23.363  17.239  1.00 21.89           C  
ATOM    653  CD  GLN A  88     -19.879  23.244  16.159  1.00 25.69           C  
ATOM    654  OE1 GLN A  88     -20.127  22.153  15.637  1.00 29.23           O  
ATOM    655  NE2 GLN A  88     -20.558  24.349  15.855  1.00 28.05           N  
ATOM    656  N   GLU A  89     -17.320  25.616  20.113  1.00  9.83           N  
ATOM    657  CA  GLU A  89     -17.201  25.278  21.515  1.00 10.50           C  
ATOM    658  C   GLU A  89     -17.534  26.410  22.473  1.00  8.82           C  
ATOM    659  O   GLU A  89     -17.578  26.186  23.682  1.00  8.90           O  
ATOM    660  CB  GLU A  89     -15.835  24.646  21.798  1.00 12.84           C  
ATOM    661  CG  GLU A  89     -15.780  23.247  21.201  1.00 16.47           C  
ATOM    662  CD  GLU A  89     -14.508  22.485  21.484  1.00 19.57           C  
ATOM    663  OE1 GLU A  89     -13.459  23.112  21.748  1.00 19.11           O  
ATOM    664  OE2 GLU A  89     -14.566  21.238  21.408  1.00 20.91           O  
ATOM    665  N   GLY A  90     -17.792  27.603  21.936  1.00  7.76           N  
ATOM    666  CA  GLY A  90     -18.140  28.746  22.761  1.00  7.12           C  
ATOM    667  C   GLY A  90     -17.026  29.180  23.701  1.00  6.91           C  
ATOM    668  O   GLY A  90     -17.275  29.539  24.847  1.00  7.67           O  
ATOM    669  N   ARG A  91     -15.796  29.139  23.215  1.00  4.99           N  
ATOM    670  CA  ARG A  91     -14.651  29.537  24.007  1.00  4.15           C  
ATOM    671  C   ARG A  91     -13.929  30.596  23.183  1.00  3.60           C  
ATOM    672  O   ARG A  91     -13.062  30.276  22.371  1.00  5.56           O  
ATOM    673  CB  ARG A  91     -13.747  28.331  24.253  1.00  5.23           C  
ATOM    674  CG  ARG A  91     -12.646  28.617  25.266  1.00  7.56           C  
ATOM    675  CD  ARG A  91     -11.633  27.483  25.403  1.00  5.07           C  
ATOM    676  NE  ARG A  91     -12.216  26.321  26.054  1.00  7.11           N  
ATOM    677  CZ  ARG A  91     -12.464  26.227  27.360  1.00  8.20           C  
ATOM    678  NH1 ARG A  91     -12.182  27.230  28.196  1.00  7.36           N  
ATOM    679  NH2 ARG A  91     -13.016  25.121  27.827  1.00  7.31           N  
ATOM    680  N   PRO A  92     -14.299  31.877  23.360  1.00  5.06           N  
ATOM    681  CA  PRO A  92     -13.702  33.009  22.633  1.00  5.13           C  
ATOM    682  C   PRO A  92     -12.183  33.088  22.750  1.00  5.68           C  
ATOM    683  O   PRO A  92     -11.640  32.816  23.820  1.00  3.76           O  
ATOM    684  CB  PRO A  92     -14.335  34.237  23.319  1.00  6.04           C  
ATOM    685  CG  PRO A  92     -15.621  33.744  23.798  1.00  7.54           C  
ATOM    686  CD  PRO A  92     -15.294  32.362  24.331  1.00  5.52           C  
ATOM    687  N   ILE A  93     -11.509  33.450  21.658  1.00  3.60           N  
ATOM    688  CA  ILE A  93     -10.054  33.636  21.679  1.00  4.44           C  
ATOM    689  C   ILE A  93      -9.895  35.146  21.849  1.00  6.02           C  
ATOM    690  O   ILE A  93     -10.362  35.929  21.010  1.00  6.90           O  
ATOM    691  CB  ILE A  93      -9.381  33.150  20.362  1.00  3.39           C  
ATOM    692  CG1 ILE A  93      -9.523  31.634  20.238  1.00  3.71           C  
ATOM    693  CG2 ILE A  93      -7.893  33.552  20.334  1.00  2.54           C  
ATOM    694  CD1 ILE A  93      -9.091  31.060  18.887  1.00  2.55           C  
ATOM    695  N   GLU A  94      -9.283  35.560  22.953  1.00  4.81           N  
ATOM    696  CA  GLU A  94      -9.107  36.977  23.258  1.00  5.60           C  
ATOM    697  C   GLU A  94      -7.670  37.512  23.132  1.00  7.22           C  
ATOM    698  O   GLU A  94      -6.758  37.035  23.818  1.00  6.47           O  
ATOM    699  CB  GLU A  94      -9.641  37.264  24.676  1.00  7.95           C  
ATOM    700  CG  GLU A  94      -9.336  38.673  25.249  1.00  7.62           C  
ATOM    701  CD  GLU A  94      -9.963  39.816  24.456  1.00 12.09           C  
ATOM    702  OE1 GLU A  94     -11.204  39.832  24.343  1.00 15.70           O  
ATOM    703  OE2 GLU A  94      -9.228  40.706  23.963  1.00  8.36           O  
ATOM    704  N   SER A  95      -7.518  38.571  22.337  1.00  6.76           N  
ATOM    705  CA  SER A  95      -6.239  39.243  22.118  1.00  5.70           C  
ATOM    706  C   SER A  95      -5.570  39.573  23.453  1.00  6.07           C  
ATOM    707  O   SER A  95      -4.393  39.277  23.654  1.00  5.12           O  
ATOM    708  CB  SER A  95      -6.463  40.538  21.339  1.00  6.63           C  
ATOM    709  OG  SER A  95      -5.235  41.101  20.930  1.00  5.61           O  
ATOM    710  N   LEU A  96      -6.327  40.171  24.364  1.00  5.18           N  
ATOM    711  CA  LEU A  96      -5.814  40.524  25.688  1.00  7.06           C  
ATOM    712  C   LEU A  96      -5.197  39.338  26.435  1.00  4.61           C  
ATOM    713  O   LEU A  96      -4.147  39.488  27.055  1.00  6.61           O  
ATOM    714  CB  LEU A  96      -6.931  41.161  26.539  1.00 10.53           C  
ATOM    715  CG  LEU A  96      -7.068  42.691  26.558  1.00 13.60           C  
ATOM    716  CD1 LEU A  96      -6.619  43.297  25.250  1.00 15.54           C  
ATOM    717  CD2 LEU A  96      -8.491  43.098  26.914  1.00 12.29           C  
ATOM    718  N   VAL A  97      -5.827  38.165  26.359  1.00  3.82           N  
ATOM    719  CA  VAL A  97      -5.333  36.960  27.040  1.00  4.48           C  
ATOM    720  C   VAL A  97      -4.029  36.466  26.380  1.00  3.86           C  
ATOM    721  O   VAL A  97      -3.069  36.094  27.069  1.00  2.14           O  
ATOM    722  CB  VAL A  97      -6.423  35.834  27.067  1.00  2.23           C  
ATOM    723  CG1 VAL A  97      -5.829  34.514  27.534  1.00  2.01           C  
ATOM    724  CG2 VAL A  97      -7.593  36.254  27.981  1.00  4.27           C  
ATOM    725  N   MET A  98      -4.005  36.493  25.049  1.00  4.49           N  
ATOM    726  CA  MET A  98      -2.816  36.097  24.284  1.00  3.76           C  
ATOM    727  C   MET A  98      -1.636  37.032  24.619  1.00  4.27           C  
ATOM    728  O   MET A  98      -0.513  36.570  24.820  1.00  3.74           O  
ATOM    729  CB  MET A  98      -3.114  36.169  22.780  1.00  5.48           C  
ATOM    730  CG  MET A  98      -4.193  35.203  22.330  1.00  5.02           C  
ATOM    731  SD  MET A  98      -4.657  35.544  20.636  1.00  6.00           S  
ATOM    732  CE  MET A  98      -3.194  35.053  19.776  1.00  6.92           C  
ATOM    733  N   SER A  99      -1.903  38.336  24.701  1.00  3.66           N  
ATOM    734  CA  SER A  99      -0.874  39.319  25.049  1.00  4.58           C  
ATOM    735  C   SER A  99      -0.407  39.163  26.494  1.00  4.29           C  
ATOM    736  O   SER A  99       0.785  39.265  26.765  1.00  2.76           O  
ATOM    737  CB  SER A  99      -1.375  40.743  24.801  1.00  5.26           C  
ATOM    738  OG  SER A  99      -1.421  41.004  23.413  1.00  6.09           O  
ATOM    739  N   ALA A 100      -1.336  38.879  27.408  1.00  4.39           N  
ATOM    740  CA  ALA A 100      -0.996  38.681  28.818  1.00  3.70           C  
ATOM    741  C   ALA A 100      -0.073  37.467  28.944  1.00  3.36           C  
ATOM    742  O   ALA A 100       0.913  37.493  29.696  1.00  3.14           O  
ATOM    743  CB  ALA A 100      -2.266  38.490  29.661  1.00  2.95           C  
ATOM    744  N   GLY A 101      -0.360  36.422  28.172  1.00  2.52           N  
ATOM    745  CA  GLY A 101       0.470  35.222  28.199  1.00  3.54           C  
ATOM    746  C   GLY A 101       1.906  35.484  27.736  1.00  3.58           C  
ATOM    747  O   GLY A 101       2.851  34.884  28.255  1.00  3.69           O  
ATOM    748  N   LEU A 102       2.078  36.338  26.732  1.00  4.06           N  
ATOM    749  CA  LEU A 102       3.417  36.681  26.260  1.00  4.94           C  
ATOM    750  C   LEU A 102       4.205  37.417  27.374  1.00  5.70           C  
ATOM    751  O   LEU A 102       5.375  37.126  27.617  1.00  5.71           O  
ATOM    752  CB  LEU A 102       3.338  37.558  25.003  1.00  6.51           C  
ATOM    753  CG  LEU A 102       4.655  38.032  24.361  1.00  5.95           C  
ATOM    754  CD1 LEU A 102       5.666  36.884  24.250  1.00  6.37           C  
ATOM    755  CD2 LEU A 102       4.348  38.619  22.991  1.00  9.92           C  
ATOM    756  N   ARG A 103       3.563  38.391  28.017  1.00  8.35           N  
ATOM    757  CA  ARG A 103       4.196  39.152  29.090  1.00  8.53           C  
ATOM    758  C   ARG A 103       4.594  38.225  30.237  1.00  7.41           C  
ATOM    759  O   ARG A 103       5.662  38.395  30.838  1.00  8.22           O  
ATOM    760  CB  ARG A 103       3.248  40.233  29.616  1.00 10.20           C  
ATOM    761  CG  ARG A 103       2.712  41.211  28.584  1.00 15.90           C  
ATOM    762  CD  ARG A 103       3.714  42.267  28.192  1.00 22.01           C  
ATOM    763  NE  ARG A 103       4.566  41.879  27.066  1.00 28.05           N  
ATOM    764  CZ  ARG A 103       4.151  41.733  25.804  1.00 29.49           C  
ATOM    765  NH1 ARG A 103       2.872  41.926  25.480  1.00 26.85           N  
ATOM    766  NH2 ARG A 103       5.041  41.470  24.848  1.00 28.37           N  
ATOM    767  N   ALA A 104       3.737  37.248  30.537  1.00  6.92           N  
ATOM    768  CA  ALA A 104       3.994  36.299  31.614  1.00  6.58           C  
ATOM    769  C   ALA A 104       5.281  35.505  31.349  1.00  8.71           C  
ATOM    770  O   ALA A 104       6.080  35.299  32.259  1.00  8.51           O  
ATOM    771  CB  ALA A 104       2.795  35.355  31.811  1.00  6.38           C  
ATOM    772  N   LEU A 105       5.501  35.085  30.105  1.00  7.06           N  
ATOM    773  CA  LEU A 105       6.718  34.353  29.762  1.00  8.53           C  
ATOM    774  C   LEU A 105       7.943  35.259  29.912  1.00  9.63           C  
ATOM    775  O   LEU A 105       9.017  34.817  30.342  1.00 10.50           O  
ATOM    776  CB  LEU A 105       6.634  33.820  28.331  1.00  6.55           C  
ATOM    777  CG  LEU A 105       5.705  32.619  28.198  1.00  8.44           C  
ATOM    778  CD1 LEU A 105       5.671  32.140  26.779  1.00  6.10           C  
ATOM    779  CD2 LEU A 105       6.230  31.504  29.076  1.00 11.49           C  
ATOM    780  N   GLU A 106       7.767  36.531  29.566  1.00 10.97           N  
ATOM    781  CA  GLU A 106       8.830  37.519  29.659  1.00 12.49           C  
ATOM    782  C   GLU A 106       9.225  37.831  31.097  1.00 12.74           C  
ATOM    783  O   GLU A 106      10.228  38.487  31.322  1.00 13.31           O  
ATOM    784  CB  GLU A 106       8.469  38.791  28.890  1.00 13.51           C  
ATOM    785  CG  GLU A 106       8.458  38.572  27.389  1.00 14.05           C  
ATOM    786  CD  GLU A 106       7.989  39.773  26.592  1.00 16.44           C  
ATOM    787  OE1 GLU A 106       7.172  40.582  27.083  1.00 15.82           O  
ATOM    788  OE2 GLU A 106       8.428  39.883  25.431  1.00 21.03           O  
ATOM    789  N   GLN A 107       8.438  37.352  32.059  1.00 13.26           N  
ATOM    790  CA  GLN A 107       8.764  37.525  33.479  1.00 14.48           C  
ATOM    791  C   GLN A 107      10.009  36.698  33.775  1.00 13.80           C  
ATOM    792  O   GLN A 107      10.759  37.005  34.688  1.00 13.95           O  
ATOM    793  CB  GLN A 107       7.659  36.992  34.406  1.00 15.44           C  
ATOM    794  CG  GLN A 107       6.377  37.786  34.442  1.00 18.51           C  
ATOM    795  CD  GLN A 107       5.343  37.159  35.374  1.00 23.42           C  
ATOM    796  OE1 GLN A 107       5.638  36.221  36.108  1.00 26.54           O  
ATOM    797  NE2 GLN A 107       4.125  37.680  35.347  1.00 23.19           N  
ATOM    798  N   GLN A 108      10.180  35.598  33.052  1.00 13.26           N  
ATOM    799  CA  GLN A 108      11.319  34.736  33.282  1.00 13.01           C  
ATOM    800  C   GLN A 108      12.275  34.501  32.121  1.00 11.05           C  
ATOM    801  O   GLN A 108      13.408  34.121  32.357  1.00 12.09           O  
ATOM    802  CB  GLN A 108      10.863  33.396  33.866  1.00 17.73           C  
ATOM    803  CG  GLN A 108       9.712  32.732  33.141  1.00 23.12           C  
ATOM    804  CD  GLN A 108       8.570  32.405  34.073  1.00 26.42           C  
ATOM    805  OE1 GLN A 108       7.948  33.308  34.642  1.00 29.85           O  
ATOM    806  NE2 GLN A 108       8.283  31.115  34.240  1.00 26.01           N  
ATOM    807  N   ALA A 109      11.833  34.696  30.884  1.00  8.60           N  
ATOM    808  CA  ALA A 109      12.705  34.469  29.739  1.00  6.82           C  
ATOM    809  C   ALA A 109      13.187  35.766  29.135  1.00  5.95           C  
ATOM    810  O   ALA A 109      12.519  36.789  29.236  1.00  7.06           O  
ATOM    811  CB  ALA A 109      11.981  33.635  28.673  1.00  8.28           C  
ATOM    812  N   ASP A 110      14.375  35.746  28.544  1.00  6.26           N  
ATOM    813  CA  ASP A 110      14.887  36.945  27.888  1.00  5.46           C  
ATOM    814  C   ASP A 110      14.951  36.759  26.366  1.00  4.15           C  
ATOM    815  O   ASP A 110      15.460  37.610  25.631  1.00  4.17           O  
ATOM    816  CB  ASP A 110      16.233  37.390  28.455  1.00  6.11           C  
ATOM    817  CG  ASP A 110      17.326  36.338  28.314  1.00  8.33           C  
ATOM    818  OD1 ASP A 110      17.135  35.306  27.648  1.00  8.10           O  
ATOM    819  OD2 ASP A 110      18.408  36.555  28.894  1.00 11.47           O  
ATOM    820  N   TRP A 111      14.392  35.645  25.907  1.00  5.11           N  
ATOM    821  CA  TRP A 111      14.340  35.306  24.490  1.00  4.59           C  
ATOM    822  C   TRP A 111      13.053  34.494  24.330  1.00  3.92           C  
ATOM    823  O   TRP A 111      12.962  33.377  24.833  1.00  4.41           O  
ATOM    824  CB  TRP A 111      15.540  34.451  24.123  1.00  3.43           C  
ATOM    825  CG  TRP A 111      15.849  34.442  22.666  1.00  3.93           C  
ATOM    826  CD1 TRP A 111      16.731  35.256  22.002  1.00  3.44           C  
ATOM    827  CD2 TRP A 111      15.283  33.573  21.681  1.00  4.70           C  
ATOM    828  NE1 TRP A 111      16.744  34.938  20.665  1.00  4.62           N  
ATOM    829  CE2 TRP A 111      15.860  33.914  20.441  1.00  6.39           C  
ATOM    830  CE3 TRP A 111      14.344  32.532  21.729  1.00  3.44           C  
ATOM    831  CZ2 TRP A 111      15.519  33.248  19.247  1.00  7.02           C  
ATOM    832  CZ3 TRP A 111      14.011  31.870  20.542  1.00  6.31           C  
ATOM    833  CH2 TRP A 111      14.596  32.233  19.325  1.00  4.87           C  
ATOM    834  N   VAL A 112      12.050  35.061  23.673  1.00  3.55           N  
ATOM    835  CA  VAL A 112      10.780  34.363  23.512  1.00  3.89           C  
ATOM    836  C   VAL A 112      10.405  34.141  22.044  1.00  4.49           C  
ATOM    837  O   VAL A 112      10.461  35.058  21.225  1.00  5.94           O  
ATOM    838  CB  VAL A 112       9.622  35.124  24.215  1.00  4.63           C  
ATOM    839  CG1 VAL A 112       8.308  34.365  24.017  1.00  3.94           C  
ATOM    840  CG2 VAL A 112       9.914  35.305  25.711  1.00  7.10           C  
ATOM    841  N   LEU A 113       9.977  32.928  21.728  1.00  4.76           N  
ATOM    842  CA  LEU A 113       9.587  32.594  20.374  1.00  5.56           C  
ATOM    843  C   LEU A 113       8.106  32.282  20.392  1.00  3.46           C  
ATOM    844  O   LEU A 113       7.657  31.460  21.181  1.00  4.41           O  
ATOM    845  CB  LEU A 113      10.403  31.391  19.887  1.00  5.54           C  
ATOM    846  CG  LEU A 113      10.133  30.864  18.477  1.00  8.43           C  
ATOM    847  CD1 LEU A 113      11.387  30.210  17.896  1.00  5.78           C  
ATOM    848  CD2 LEU A 113       8.969  29.891  18.536  1.00  8.31           C  
ATOM    849  N   VAL A 114       7.365  32.888  19.477  1.00  3.76           N  
ATOM    850  CA  VAL A 114       5.915  32.688  19.399  1.00  4.22           C  
ATOM    851  C   VAL A 114       5.538  31.998  18.109  1.00  3.89           C  
ATOM    852  O   VAL A 114       5.775  32.541  17.036  1.00  4.04           O  
ATOM    853  CB  VAL A 114       5.127  34.037  19.459  1.00  2.79           C  
ATOM    854  CG1 VAL A 114       3.619  33.762  19.429  1.00  2.40           C  
ATOM    855  CG2 VAL A 114       5.488  34.827  20.737  1.00  3.28           C  
ATOM    856  N   GLU A 115       5.001  30.786  18.199  1.00  5.01           N  
ATOM    857  CA  GLU A 115       4.579  30.101  16.971  1.00  6.84           C  
ATOM    858  C   GLU A 115       3.102  30.416  16.699  1.00  6.92           C  
ATOM    859  O   GLU A 115       2.276  30.407  17.618  1.00  7.07           O  
ATOM    860  CB  GLU A 115       4.804  28.585  17.034  1.00  5.00           C  
ATOM    861  CG  GLU A 115       4.428  27.909  15.714  1.00  5.80           C  
ATOM    862  CD  GLU A 115       4.368  26.386  15.763  1.00  7.93           C  
ATOM    863  OE1 GLU A 115       5.001  25.769  16.647  1.00  7.70           O  
ATOM    864  OE2 GLU A 115       3.688  25.806  14.872  1.00  6.44           O  
ATOM    865  N   GLY A 116       2.804  30.792  15.460  1.00  6.43           N  
ATOM    866  CA  GLY A 116       1.436  31.096  15.091  1.00  7.88           C  
ATOM    867  C   GLY A 116       0.721  29.790  14.838  1.00  7.96           C  
ATOM    868  O   GLY A 116       1.154  28.747  15.321  1.00  8.93           O  
ATOM    869  N   ALA A 117      -0.378  29.838  14.095  1.00  6.77           N  
ATOM    870  CA  ALA A 117      -1.144  28.636  13.779  1.00  6.49           C  
ATOM    871  C   ALA A 117      -1.443  28.767  12.299  1.00  6.23           C  
ATOM    872  O   ALA A 117      -1.837  29.839  11.833  1.00  5.63           O  
ATOM    873  CB  ALA A 117      -2.440  28.567  14.601  1.00  4.36           C  
ATOM    874  N   GLY A 118      -1.194  27.705  11.546  1.00  7.11           N  
ATOM    875  CA  GLY A 118      -1.420  27.781  10.111  1.00  8.58           C  
ATOM    876  C   GLY A 118      -0.508  28.821   9.464  1.00  9.00           C  
ATOM    877  O   GLY A 118       0.691  28.910   9.774  1.00  9.10           O  
ATOM    878  N   GLY A 119      -1.083  29.624   8.580  1.00  7.92           N  
ATOM    879  CA  GLY A 119      -0.316  30.641   7.890  1.00  3.55           C  
ATOM    880  C   GLY A 119      -0.576  32.010   8.481  1.00  3.42           C  
ATOM    881  O   GLY A 119      -1.252  32.132   9.510  1.00  3.78           O  
ATOM    882  N   TRP A 120      -0.121  33.043   7.780  1.00  2.08           N  
ATOM    883  CA  TRP A 120      -0.245  34.418   8.247  1.00  3.00           C  
ATOM    884  C   TRP A 120      -1.658  34.890   8.654  1.00  3.29           C  
ATOM    885  O   TRP A 120      -1.866  35.434   9.761  1.00  2.22           O  
ATOM    886  CB  TRP A 120       0.363  35.370   7.203  1.00  2.43           C  
ATOM    887  CG  TRP A 120       0.426  36.792   7.645  1.00  3.06           C  
ATOM    888  CD1 TRP A 120      -0.275  37.834   7.134  1.00  3.29           C  
ATOM    889  CD2 TRP A 120       1.207  37.325   8.725  1.00  4.82           C  
ATOM    890  NE1 TRP A 120       0.010  38.979   7.823  1.00  4.39           N  
ATOM    891  CE2 TRP A 120       0.919  38.696   8.806  1.00  7.30           C  
ATOM    892  CE3 TRP A 120       2.117  36.767   9.631  1.00  3.93           C  
ATOM    893  CZ2 TRP A 120       1.515  39.532   9.764  1.00  7.30           C  
ATOM    894  CZ3 TRP A 120       2.705  37.594  10.579  1.00  4.40           C  
ATOM    895  CH2 TRP A 120       2.401  38.961  10.639  1.00  4.27           C  
ATOM    896  N   PHE A 121      -2.628  34.633   7.781  1.00  3.74           N  
ATOM    897  CA  PHE A 121      -3.993  35.088   7.992  1.00  4.82           C  
ATOM    898  C   PHE A 121      -4.997  34.194   8.708  1.00  4.72           C  
ATOM    899  O   PHE A 121      -6.199  34.468   8.652  1.00  8.79           O  
ATOM    900  CB  PHE A 121      -4.580  35.531   6.670  1.00  4.99           C  
ATOM    901  CG  PHE A 121      -4.147  36.886   6.237  1.00  5.80           C  
ATOM    902  CD1 PHE A 121      -4.298  37.989   7.089  1.00  5.74           C  
ATOM    903  CD2 PHE A 121      -3.674  37.083   4.936  1.00  5.38           C  
ATOM    904  CE1 PHE A 121      -3.992  39.280   6.650  1.00  8.06           C  
ATOM    905  CE2 PHE A 121      -3.367  38.363   4.481  1.00  6.94           C  
ATOM    906  CZ  PHE A 121      -3.531  39.472   5.341  1.00  6.57           C  
ATOM    907  N   THR A 122      -4.533  33.188   9.431  1.00  2.01           N  
ATOM    908  CA  THR A 122      -5.424  32.281  10.154  1.00  2.70           C  
ATOM    909  C   THR A 122      -6.398  33.026  11.081  1.00  2.19           C  
ATOM    910  O   THR A 122      -5.980  33.721  12.004  1.00  4.70           O  
ATOM    911  CB  THR A 122      -4.595  31.279  10.958  1.00  2.46           C  
ATOM    912  OG1 THR A 122      -3.795  30.523  10.048  1.00  5.39           O  
ATOM    913  CG2 THR A 122      -5.483  30.337  11.733  1.00  2.91           C  
ATOM    914  N   PRO A 123      -7.712  32.886  10.850  1.00  2.02           N  
ATOM    915  CA  PRO A 123      -8.679  33.577  11.695  1.00  2.00           C  
ATOM    916  C   PRO A 123      -8.784  33.012  13.119  1.00  2.68           C  
ATOM    917  O   PRO A 123      -8.635  31.802  13.311  1.00  2.85           O  
ATOM    918  CB  PRO A 123      -9.998  33.403  10.926  1.00  2.71           C  
ATOM    919  CG  PRO A 123      -9.570  33.159   9.501  1.00  2.00           C  
ATOM    920  CD  PRO A 123      -8.377  32.263   9.691  1.00  2.46           C  
ATOM    921  N   LEU A 124      -8.991  33.912  14.086  1.00  2.00           N  
ATOM    922  CA  LEU A 124      -9.171  33.607  15.515  1.00  2.74           C  
ATOM    923  C   LEU A 124     -10.654  33.803  15.891  1.00  3.71           C  
ATOM    924  O   LEU A 124     -11.175  33.143  16.797  1.00  5.31           O  
ATOM    925  CB  LEU A 124      -8.271  34.489  16.375  1.00  2.08           C  
ATOM    926  CG  LEU A 124      -6.766  34.286  16.150  1.00  4.61           C  
ATOM    927  CD1 LEU A 124      -5.982  35.052  17.229  1.00  5.48           C  
ATOM    928  CD2 LEU A 124      -6.412  32.787  16.196  1.00  3.74           C  
ATOM    929  N   SER A 125     -11.339  34.690  15.166  1.00  4.89           N  
ATOM    930  CA  SER A 125     -12.775  34.928  15.345  1.00  4.26           C  
ATOM    931  C   SER A 125     -13.299  35.335  13.973  1.00  4.28           C  
ATOM    932  O   SER A 125     -12.526  35.379  13.004  1.00  3.82           O  
ATOM    933  CB  SER A 125     -13.058  36.042  16.356  1.00  5.68           C  
ATOM    934  OG  SER A 125     -12.938  37.339  15.786  1.00  4.09           O  
ATOM    935  N   ASP A 126     -14.580  35.681  13.901  1.00  3.77           N  
ATOM    936  CA  ASP A 126     -15.188  36.122  12.646  1.00  5.93           C  
ATOM    937  C   ASP A 126     -14.717  37.513  12.225  1.00  5.08           C  
ATOM    938  O   ASP A 126     -14.926  37.918  11.090  1.00  6.07           O  
ATOM    939  CB  ASP A 126     -16.725  36.089  12.726  1.00  7.89           C  
ATOM    940  CG  ASP A 126     -17.296  34.702  12.492  0.80 12.11           C  
ATOM    941  OD1 ASP A 126     -16.509  33.751  12.266  0.80 16.92           O  
ATOM    942  OD2 ASP A 126     -18.537  34.555  12.538  0.80 13.18           O  
ATOM    943  N   THR A 127     -14.040  38.222  13.123  1.00  4.43           N  
ATOM    944  CA  THR A 127     -13.555  39.558  12.828  1.00  3.98           C  
ATOM    945  C   THR A 127     -12.091  39.818  13.223  1.00  4.23           C  
ATOM    946  O   THR A 127     -11.627  40.955  13.105  1.00  4.18           O  
ATOM    947  CB  THR A 127     -14.409  40.625  13.561  1.00  4.14           C  
ATOM    948  OG1 THR A 127     -14.315  40.434  14.980  1.00  3.37           O  
ATOM    949  CG2 THR A 127     -15.872  40.545  13.143  1.00  4.27           C  
ATOM    950  N   PHE A 128     -11.350  38.777  13.606  1.00  4.56           N  
ATOM    951  CA  PHE A 128      -9.963  38.940  14.082  1.00  7.07           C  
ATOM    952  C   PHE A 128      -9.103  37.773  13.597  1.00  5.54           C  
ATOM    953  O   PHE A 128      -9.510  36.626  13.720  1.00  3.41           O  
ATOM    954  CB  PHE A 128      -9.994  38.981  15.640  1.00  8.89           C  
ATOM    955  CG  PHE A 128      -8.663  39.293  16.313  1.00 12.02           C  
ATOM    956  CD1 PHE A 128      -8.144  40.586  16.319  1.00 14.77           C  
ATOM    957  CD2 PHE A 128      -7.990  38.309  17.028  1.00 13.65           C  
ATOM    958  CE1 PHE A 128      -6.980  40.887  17.032  1.00 15.26           C  
ATOM    959  CE2 PHE A 128      -6.823  38.609  17.746  1.00 15.97           C  
ATOM    960  CZ  PHE A 128      -6.329  39.894  17.742  1.00 13.63           C  
ATOM    961  N   THR A 129      -7.944  38.072  13.008  1.00  4.66           N  
ATOM    962  CA  THR A 129      -7.023  37.028  12.540  1.00  3.77           C  
ATOM    963  C   THR A 129      -5.732  37.080  13.381  1.00  2.00           C  
ATOM    964  O   THR A 129      -5.513  38.027  14.151  1.00  2.71           O  
ATOM    965  CB  THR A 129      -6.632  37.204  11.044  1.00  5.12           C  
ATOM    966  OG1 THR A 129      -5.770  38.351  10.892  1.00  5.18           O  
ATOM    967  CG2 THR A 129      -7.898  37.369  10.159  1.00  5.34           C  
ATOM    968  N   PHE A 130      -4.898  36.055  13.260  1.00  2.67           N  
ATOM    969  CA  PHE A 130      -3.627  36.018  13.985  1.00  2.03           C  
ATOM    970  C   PHE A 130      -2.760  37.201  13.549  1.00  2.27           C  
ATOM    971  O   PHE A 130      -2.072  37.809  14.361  1.00  2.69           O  
ATOM    972  CB  PHE A 130      -2.906  34.705  13.685  1.00  4.43           C  
ATOM    973  CG  PHE A 130      -2.331  34.037  14.893  1.00  4.21           C  
ATOM    974  CD1 PHE A 130      -1.529  34.741  15.771  1.00  6.24           C  
ATOM    975  CD2 PHE A 130      -2.614  32.709  15.157  1.00  6.32           C  
ATOM    976  CE1 PHE A 130      -1.007  34.130  16.891  1.00  8.71           C  
ATOM    977  CE2 PHE A 130      -2.101  32.083  16.276  1.00  7.90           C  
ATOM    978  CZ  PHE A 130      -1.296  32.802  17.146  1.00  7.01           C  
ATOM    979  N   ALA A 131      -2.800  37.530  12.258  1.00  3.63           N  
ATOM    980  CA  ALA A 131      -2.050  38.659  11.736  1.00  2.81           C  
ATOM    981  C   ALA A 131      -2.410  39.938  12.491  1.00  3.65           C  
ATOM    982  O   ALA A 131      -1.543  40.772  12.753  1.00  5.39           O  
ATOM    983  CB  ALA A 131      -2.315  38.835  10.258  1.00  2.03           C  
ATOM    984  N   ASP A 132      -3.686  40.102  12.833  1.00  4.18           N  
ATOM    985  CA  ASP A 132      -4.117  41.289  13.576  1.00  5.72           C  
ATOM    986  C   ASP A 132      -3.375  41.387  14.907  1.00  4.77           C  
ATOM    987  O   ASP A 132      -2.920  42.477  15.291  1.00  5.95           O  
ATOM    988  CB  ASP A 132      -5.636  41.290  13.827  1.00  5.23           C  
ATOM    989  CG  ASP A 132      -6.462  41.520  12.543  1.00  8.93           C  
ATOM    990  OD1 ASP A 132      -6.020  42.271  11.641  1.00  7.93           O  
ATOM    991  OD2 ASP A 132      -7.558  40.934  12.438  1.00 10.31           O  
ATOM    992  N   TRP A 133      -3.238  40.250  15.590  1.00  3.85           N  
ATOM    993  CA  TRP A 133      -2.554  40.195  16.880  1.00  2.74           C  
ATOM    994  C   TRP A 133      -1.066  40.459  16.744  1.00  3.32           C  
ATOM    995  O   TRP A 133      -0.500  41.209  17.529  1.00  2.81           O  
ATOM    996  CB  TRP A 133      -2.776  38.845  17.568  1.00  2.02           C  
ATOM    997  CG  TRP A 133      -2.131  38.766  18.916  1.00  3.04           C  
ATOM    998  CD1 TRP A 133      -2.599  39.302  20.083  1.00  4.56           C  
ATOM    999  CD2 TRP A 133      -0.913  38.098  19.240  1.00  3.74           C  
ATOM   1000  NE1 TRP A 133      -1.746  39.006  21.118  1.00  6.15           N  
ATOM   1001  CE2 TRP A 133      -0.704  38.261  20.631  1.00  5.03           C  
ATOM   1002  CE3 TRP A 133       0.025  37.375  18.484  1.00  3.88           C  
ATOM   1003  CZ2 TRP A 133       0.405  37.725  21.292  1.00  5.37           C  
ATOM   1004  CZ3 TRP A 133       1.125  36.842  19.127  1.00  6.96           C  
ATOM   1005  CH2 TRP A 133       1.310  37.020  20.532  1.00  7.47           C  
ATOM   1006  N   VAL A 134      -0.432  39.842  15.755  1.00  3.08           N  
ATOM   1007  CA  VAL A 134       1.000  40.047  15.537  1.00  5.50           C  
ATOM   1008  C   VAL A 134       1.268  41.540  15.271  1.00  4.82           C  
ATOM   1009  O   VAL A 134       2.248  42.098  15.771  1.00  5.04           O  
ATOM   1010  CB  VAL A 134       1.543  39.184  14.362  1.00  3.81           C  
ATOM   1011  CG1 VAL A 134       3.053  39.418  14.188  1.00  4.46           C  
ATOM   1012  CG2 VAL A 134       1.284  37.701  14.612  1.00  2.03           C  
ATOM   1013  N   THR A 135       0.396  42.186  14.503  1.00  4.93           N  
ATOM   1014  CA  THR A 135       0.540  43.606  14.204  1.00  6.42           C  
ATOM   1015  C   THR A 135       0.362  44.462  15.462  1.00  7.14           C  
ATOM   1016  O   THR A 135       1.049  45.456  15.661  1.00  7.19           O  
ATOM   1017  CB  THR A 135      -0.465  44.042  13.140  1.00  5.70           C  
ATOM   1018  OG1 THR A 135      -0.306  43.203  11.997  1.00  8.51           O  
ATOM   1019  CG2 THR A 135      -0.249  45.486  12.733  1.00  7.15           C  
ATOM   1020  N   GLN A 136      -0.582  44.070  16.303  1.00 10.19           N  
ATOM   1021  CA  GLN A 136      -0.852  44.775  17.537  1.00 11.64           C  
ATOM   1022  C   GLN A 136       0.397  44.720  18.410  1.00 10.62           C  
ATOM   1023  O   GLN A 136       0.858  45.746  18.910  1.00  9.48           O  
ATOM   1024  CB  GLN A 136      -2.030  44.104  18.239  1.00 16.81           C  
ATOM   1025  CG  GLN A 136      -2.788  45.007  19.174  1.00 27.16           C  
ATOM   1026  CD  GLN A 136      -4.230  44.567  19.346  1.00 32.41           C  
ATOM   1027  OE1 GLN A 136      -4.760  44.567  20.467  1.00 37.14           O  
ATOM   1028  NE2 GLN A 136      -4.883  44.199  18.237  1.00 30.79           N  
ATOM   1029  N   GLU A 137       0.985  43.530  18.519  1.00 10.23           N  
ATOM   1030  CA  GLU A 137       2.188  43.320  19.331  1.00  9.83           C  
ATOM   1031  C   GLU A 137       3.489  43.856  18.734  1.00  8.70           C  
ATOM   1032  O   GLU A 137       4.498  43.925  19.426  1.00  9.04           O  
ATOM   1033  CB  GLU A 137       2.365  41.832  19.669  1.00  9.15           C  
ATOM   1034  CG  GLU A 137       1.391  41.304  20.749  1.00 10.67           C  
ATOM   1035  CD  GLU A 137       1.568  41.995  22.088  1.00 10.35           C  
ATOM   1036  OE1 GLU A 137       2.714  42.233  22.502  1.00 10.83           O  
ATOM   1037  OE2 GLU A 137       0.558  42.333  22.723  1.00 13.64           O  
ATOM   1038  N   GLN A 138       3.473  44.202  17.450  1.00  7.27           N  
ATOM   1039  CA  GLN A 138       4.671  44.707  16.772  1.00  7.72           C  
ATOM   1040  C   GLN A 138       5.831  43.738  16.904  1.00  6.80           C  
ATOM   1041  O   GLN A 138       6.972  44.133  17.135  1.00  7.85           O  
ATOM   1042  CB  GLN A 138       5.055  46.078  17.318  1.00  8.11           C  
ATOM   1043  CG  GLN A 138       4.035  47.148  16.971  1.00 11.58           C  
ATOM   1044  CD  GLN A 138       4.073  47.498  15.510  1.00 12.79           C  
ATOM   1045  OE1 GLN A 138       5.038  48.089  15.045  1.00 14.56           O  
ATOM   1046  NE2 GLN A 138       3.028  47.145  14.774  1.00 14.39           N  
ATOM   1047  N   LEU A 139       5.526  42.457  16.762  1.00  5.42           N  
ATOM   1048  CA  LEU A 139       6.533  41.408  16.850  1.00  4.24           C  
ATOM   1049  C   LEU A 139       7.316  41.247  15.551  1.00  4.37           C  
ATOM   1050  O   LEU A 139       6.734  41.313  14.468  1.00  5.20           O  
ATOM   1051  CB  LEU A 139       5.841  40.070  17.120  1.00  4.82           C  
ATOM   1052  CG  LEU A 139       5.235  39.818  18.503  1.00  5.59           C  
ATOM   1053  CD1 LEU A 139       4.398  38.562  18.486  1.00  7.56           C  
ATOM   1054  CD2 LEU A 139       6.343  39.683  19.523  1.00  9.10           C  
ATOM   1055  N   PRO A 140       8.650  41.085  15.633  1.00  6.46           N  
ATOM   1056  CA  PRO A 140       9.456  40.885  14.404  1.00  5.20           C  
ATOM   1057  C   PRO A 140       9.061  39.471  13.931  1.00  4.39           C  
ATOM   1058  O   PRO A 140       8.872  38.562  14.755  1.00  6.23           O  
ATOM   1059  CB  PRO A 140      10.901  40.902  14.912  1.00  5.56           C  
ATOM   1060  CG  PRO A 140      10.819  41.700  16.218  1.00  9.32           C  
ATOM   1061  CD  PRO A 140       9.502  41.238  16.827  1.00  5.76           C  
ATOM   1062  N   VAL A 141       8.936  39.270  12.630  1.00  2.98           N  
ATOM   1063  CA  VAL A 141       8.481  37.985  12.120  1.00  3.92           C  
ATOM   1064  C   VAL A 141       9.560  37.142  11.431  1.00  3.20           C  
ATOM   1065  O   VAL A 141      10.381  37.673  10.673  1.00  3.70           O  
ATOM   1066  CB  VAL A 141       7.277  38.184  11.139  1.00  4.20           C  
ATOM   1067  CG1 VAL A 141       6.799  36.821  10.580  1.00  2.00           C  
ATOM   1068  CG2 VAL A 141       6.133  38.905  11.843  1.00  2.86           C  
ATOM   1069  N   ILE A 142       9.576  35.843  11.730  1.00  2.91           N  
ATOM   1070  CA  ILE A 142      10.501  34.914  11.091  1.00  2.22           C  
ATOM   1071  C   ILE A 142       9.632  34.015  10.199  1.00  3.17           C  
ATOM   1072  O   ILE A 142       8.656  33.425  10.670  1.00  2.00           O  
ATOM   1073  CB  ILE A 142      11.280  34.048  12.124  1.00  3.83           C  
ATOM   1074  CG1 ILE A 142      12.303  34.899  12.890  1.00  3.30           C  
ATOM   1075  CG2 ILE A 142      12.041  32.918  11.430  1.00  2.00           C  
ATOM   1076  CD1 ILE A 142      13.108  34.081  13.900  1.00  2.57           C  
ATOM   1077  N   LEU A 143       9.945  33.963   8.906  1.00  3.61           N  
ATOM   1078  CA  LEU A 143       9.172  33.165   7.958  1.00  5.72           C  
ATOM   1079  C   LEU A 143       9.792  31.786   7.697  1.00  3.64           C  
ATOM   1080  O   LEU A 143      10.927  31.679   7.236  1.00  3.79           O  
ATOM   1081  CB  LEU A 143       9.017  33.921   6.628  1.00  4.00           C  
ATOM   1082  CG  LEU A 143       8.329  33.172   5.478  1.00  6.16           C  
ATOM   1083  CD1 LEU A 143       6.920  32.760   5.903  1.00  3.53           C  
ATOM   1084  CD2 LEU A 143       8.305  34.037   4.210  1.00  5.13           C  
ATOM   1085  N   VAL A 144       9.041  30.732   7.983  1.00  2.91           N  
ATOM   1086  CA  VAL A 144       9.529  29.384   7.740  1.00  3.19           C  
ATOM   1087  C   VAL A 144       8.993  28.934   6.391  1.00  2.99           C  
ATOM   1088  O   VAL A 144       7.789  28.958   6.144  1.00  4.19           O  
ATOM   1089  CB  VAL A 144       9.126  28.404   8.853  1.00  3.62           C  
ATOM   1090  CG1 VAL A 144       9.661  27.008   8.532  1.00  2.03           C  
ATOM   1091  CG2 VAL A 144       9.676  28.913  10.208  1.00  2.02           C  
ATOM   1092  N   VAL A 145       9.913  28.616   5.495  1.00  3.14           N  
ATOM   1093  CA  VAL A 145       9.579  28.185   4.147  1.00  4.17           C  
ATOM   1094  C   VAL A 145       9.850  26.696   3.933  1.00  5.07           C  
ATOM   1095  O   VAL A 145      10.999  26.256   3.957  1.00  4.95           O  
ATOM   1096  CB  VAL A 145      10.409  28.992   3.092  1.00  5.22           C  
ATOM   1097  CG1 VAL A 145      10.051  28.533   1.668  1.00  4.17           C  
ATOM   1098  CG2 VAL A 145      10.190  30.496   3.272  1.00  4.18           C  
ATOM   1099  N   GLY A 146       8.793  25.915   3.747  1.00  4.11           N  
ATOM   1100  CA  GLY A 146       8.985  24.510   3.476  1.00  4.53           C  
ATOM   1101  C   GLY A 146       9.408  24.480   2.016  1.00  7.30           C  
ATOM   1102  O   GLY A 146       8.651  24.924   1.140  1.00  8.24           O  
ATOM   1103  N   VAL A 147      10.620  24.016   1.749  1.00  5.75           N  
ATOM   1104  CA  VAL A 147      11.130  23.958   0.393  1.00  9.27           C  
ATOM   1105  C   VAL A 147      10.438  22.868  -0.449  1.00  8.18           C  
ATOM   1106  O   VAL A 147      10.716  21.680  -0.318  1.00 10.01           O  
ATOM   1107  CB  VAL A 147      12.677  23.789   0.373  1.00  9.78           C  
ATOM   1108  CG1 VAL A 147      13.191  23.778  -1.075  1.00 12.68           C  
ATOM   1109  CG2 VAL A 147      13.341  24.931   1.154  1.00  9.20           C  
ATOM   1110  N   LYS A 148       9.521  23.304  -1.298  1.00  6.86           N  
ATOM   1111  CA  LYS A 148       8.769  22.428  -2.192  1.00  7.80           C  
ATOM   1112  C   LYS A 148       8.146  23.274  -3.295  1.00  7.40           C  
ATOM   1113  O   LYS A 148       8.159  24.503  -3.246  1.00  6.81           O  
ATOM   1114  CB  LYS A 148       7.659  21.668  -1.433  1.00  6.54           C  
ATOM   1115  CG  LYS A 148       6.634  22.554  -0.763  1.00  7.03           C  
ATOM   1116  CD  LYS A 148       5.578  21.726  -0.072  1.00 11.16           C  
ATOM   1117  CE  LYS A 148       4.718  22.565   0.844  1.00 11.82           C  
ATOM   1118  NZ  LYS A 148       3.556  21.776   1.389  1.00 11.21           N  
ATOM   1119  N   LEU A 149       7.607  22.608  -4.303  1.00  9.95           N  
ATOM   1120  CA  LEU A 149       6.941  23.283  -5.412  1.00  9.89           C  
ATOM   1121  C   LEU A 149       5.822  24.190  -4.865  1.00  7.15           C  
ATOM   1122  O   LEU A 149       5.003  23.742  -4.061  1.00  9.05           O  
ATOM   1123  CB  LEU A 149       6.317  22.206  -6.292  1.00 13.24           C  
ATOM   1124  CG  LEU A 149       6.093  22.528  -7.750  1.00 14.59           C  
ATOM   1125  CD1 LEU A 149       7.451  22.577  -8.457  1.00 16.40           C  
ATOM   1126  CD2 LEU A 149       5.177  21.447  -8.331  1.00 17.53           C  
ATOM   1127  N   GLY A 150       5.777  25.441  -5.300  1.00  3.88           N  
ATOM   1128  CA  GLY A 150       4.749  26.347  -4.830  1.00  3.23           C  
ATOM   1129  C   GLY A 150       5.197  27.260  -3.706  1.00  2.55           C  
ATOM   1130  O   GLY A 150       4.562  28.276  -3.435  1.00  3.32           O  
ATOM   1131  N   CYS A 151       6.340  26.957  -3.096  1.00  5.10           N  
ATOM   1132  CA  CYS A 151       6.836  27.750  -1.971  1.00  3.24           C  
ATOM   1133  C   CYS A 151       7.297  29.168  -2.328  1.00  2.98           C  
ATOM   1134  O   CYS A 151       7.166  30.067  -1.505  1.00  2.80           O  
ATOM   1135  CB  CYS A 151       7.936  26.983  -1.231  1.00  3.67           C  
ATOM   1136  SG  CYS A 151       9.550  26.909  -2.069  1.00  7.15           S  
ATOM   1137  N   ILE A 152       7.809  29.387  -3.549  1.00  3.08           N  
ATOM   1138  CA  ILE A 152       8.245  30.733  -3.961  1.00  2.86           C  
ATOM   1139  C   ILE A 152       7.057  31.720  -3.877  1.00  2.06           C  
ATOM   1140  O   ILE A 152       7.158  32.765  -3.242  1.00  2.02           O  
ATOM   1141  CB  ILE A 152       8.840  30.743  -5.384  1.00  2.01           C  
ATOM   1142  CG1 ILE A 152      10.145  29.963  -5.422  1.00  2.00           C  
ATOM   1143  CG2 ILE A 152       9.212  32.154  -5.795  1.00  3.00           C  
ATOM   1144  CD1 ILE A 152      10.591  29.629  -6.816  1.00  5.95           C  
ATOM   1145  N   ASN A 153       5.949  31.381  -4.529  1.00  2.43           N  
ATOM   1146  CA  ASN A 153       4.721  32.182  -4.514  1.00  2.52           C  
ATOM   1147  C   ASN A 153       4.256  32.438  -3.074  1.00  2.24           C  
ATOM   1148  O   ASN A 153       3.981  33.561  -2.703  1.00  2.35           O  
ATOM   1149  CB  ASN A 153       3.594  31.453  -5.277  1.00  2.28           C  
ATOM   1150  CG  ASN A 153       2.237  32.128  -5.112  1.00  2.28           C  
ATOM   1151  OD1 ASN A 153       2.086  33.307  -5.392  1.00  2.21           O  
ATOM   1152  ND2 ASN A 153       1.252  31.382  -4.625  1.00  3.37           N  
ATOM   1153  N   HIS A 154       4.168  31.389  -2.271  1.00  2.07           N  
ATOM   1154  CA  HIS A 154       3.737  31.538  -0.887  1.00  3.66           C  
ATOM   1155  C   HIS A 154       4.693  32.399  -0.054  1.00  2.16           C  
ATOM   1156  O   HIS A 154       4.255  33.247   0.716  1.00  3.17           O  
ATOM   1157  CB  HIS A 154       3.527  30.169  -0.248  1.00  2.88           C  
ATOM   1158  CG  HIS A 154       2.313  29.456  -0.752  1.00  3.82           C  
ATOM   1159  ND1 HIS A 154       2.159  28.095  -0.654  1.00  4.54           N  
ATOM   1160  CD2 HIS A 154       1.213  29.918  -1.399  1.00  4.65           C  
ATOM   1161  CE1 HIS A 154       1.020  27.741  -1.219  1.00  4.45           C  
ATOM   1162  NE2 HIS A 154       0.429  28.827  -1.679  1.00  2.96           N  
ATOM   1163  N   ALA A 155       6.000  32.218  -0.244  1.00  3.82           N  
ATOM   1164  CA  ALA A 155       6.961  33.020   0.503  1.00  2.41           C  
ATOM   1165  C   ALA A 155       6.810  34.474   0.092  1.00  3.66           C  
ATOM   1166  O   ALA A 155       6.810  35.368   0.940  1.00  4.52           O  
ATOM   1167  CB  ALA A 155       8.422  32.547   0.251  1.00  4.50           C  
ATOM   1168  N   MET A 156       6.700  34.714  -1.213  1.00  2.89           N  
ATOM   1169  CA  MET A 156       6.574  36.069  -1.714  1.00  3.69           C  
ATOM   1170  C   MET A 156       5.314  36.769  -1.226  1.00  2.40           C  
ATOM   1171  O   MET A 156       5.377  37.920  -0.819  1.00  4.09           O  
ATOM   1172  CB  MET A 156       6.669  36.080  -3.245  1.00  8.38           C  
ATOM   1173  CG  MET A 156       8.102  35.951  -3.738  1.00 13.89           C  
ATOM   1174  SD  MET A 156       8.227  36.264  -5.512  1.00 21.24           S  
ATOM   1175  CE  MET A 156       7.665  34.763  -6.155  1.00 23.52           C  
ATOM   1176  N   LEU A 157       4.183  36.070  -1.275  1.00  2.40           N  
ATOM   1177  CA  LEU A 157       2.898  36.594  -0.814  1.00  2.00           C  
ATOM   1178  C   LEU A 157       2.997  36.966   0.656  1.00  3.81           C  
ATOM   1179  O   LEU A 157       2.659  38.087   1.028  1.00  2.17           O  
ATOM   1180  CB  LEU A 157       1.782  35.543  -0.968  1.00  3.20           C  
ATOM   1181  CG  LEU A 157       1.251  35.234  -2.375  1.00  4.10           C  
ATOM   1182  CD1 LEU A 157       0.248  34.108  -2.289  1.00  6.51           C  
ATOM   1183  CD2 LEU A 157       0.604  36.472  -2.961  1.00  6.78           C  
ATOM   1184  N   THR A 158       3.497  36.042   1.478  1.00  3.48           N  
ATOM   1185  CA  THR A 158       3.594  36.282   2.920  1.00  3.92           C  
ATOM   1186  C   THR A 158       4.544  37.435   3.255  1.00  3.44           C  
ATOM   1187  O   THR A 158       4.202  38.326   4.025  1.00  2.48           O  
ATOM   1188  CB  THR A 158       3.957  34.974   3.658  1.00  3.22           C  
ATOM   1189  OG1 THR A 158       3.018  33.957   3.279  1.00  2.68           O  
ATOM   1190  CG2 THR A 158       3.906  35.162   5.182  1.00  2.85           C  
ATOM   1191  N   ALA A 159       5.713  37.460   2.627  1.00  5.71           N  
ATOM   1192  CA  ALA A 159       6.663  38.537   2.873  1.00  6.05           C  
ATOM   1193  C   ALA A 159       6.050  39.907   2.516  1.00  5.37           C  
ATOM   1194  O   ALA A 159       6.204  40.867   3.253  1.00  5.86           O  
ATOM   1195  CB  ALA A 159       7.962  38.302   2.073  1.00  6.03           C  
ATOM   1196  N   GLN A 160       5.362  40.005   1.379  1.00  5.90           N  
ATOM   1197  CA  GLN A 160       4.764  41.282   0.971  1.00  5.13           C  
ATOM   1198  C   GLN A 160       3.716  41.790   1.960  1.00  3.39           C  
ATOM   1199  O   GLN A 160       3.700  42.962   2.307  1.00  3.37           O  
ATOM   1200  CB  GLN A 160       4.139  41.197  -0.439  1.00  5.77           C  
ATOM   1201  CG  GLN A 160       3.540  42.544  -0.916  1.00  5.39           C  
ATOM   1202  CD  GLN A 160       2.991  42.528  -2.350  1.00  7.63           C  
ATOM   1203  OE1 GLN A 160       1.892  43.015  -2.599  1.00 12.05           O  
ATOM   1204  NE2 GLN A 160       3.776  42.038  -3.293  1.00  7.52           N  
ATOM   1205  N   VAL A 161       2.839  40.899   2.393  1.00  4.44           N  
ATOM   1206  CA  VAL A 161       1.776  41.245   3.327  1.00  6.62           C  
ATOM   1207  C   VAL A 161       2.333  41.668   4.696  1.00  4.96           C  
ATOM   1208  O   VAL A 161       1.871  42.640   5.294  1.00  6.99           O  
ATOM   1209  CB  VAL A 161       0.789  40.063   3.432  1.00  6.88           C  
ATOM   1210  CG1 VAL A 161      -0.110  40.220   4.605  1.00 10.25           C  
ATOM   1211  CG2 VAL A 161      -0.044  39.970   2.128  1.00  6.14           C  
ATOM   1212  N   ILE A 162       3.354  40.961   5.170  1.00  5.61           N  
ATOM   1213  CA  ILE A 162       3.979  41.285   6.443  1.00  5.16           C  
ATOM   1214  C   ILE A 162       4.558  42.697   6.367  1.00  5.28           C  
ATOM   1215  O   ILE A 162       4.279  43.536   7.214  1.00  5.92           O  
ATOM   1216  CB  ILE A 162       5.092  40.261   6.789  1.00  5.33           C  
ATOM   1217  CG1 ILE A 162       4.458  38.898   7.114  1.00  7.10           C  
ATOM   1218  CG2 ILE A 162       5.946  40.762   7.969  1.00  5.05           C  
ATOM   1219  CD1 ILE A 162       5.457  37.740   7.218  1.00  6.12           C  
ATOM   1220  N   GLN A 163       5.326  42.975   5.324  1.00  6.20           N  
ATOM   1221  CA  GLN A 163       5.922  44.293   5.169  1.00  8.50           C  
ATOM   1222  C   GLN A 163       4.870  45.393   5.042  1.00  9.94           C  
ATOM   1223  O   GLN A 163       5.027  46.492   5.592  1.00  8.65           O  
ATOM   1224  CB  GLN A 163       6.887  44.306   3.983  1.00  9.71           C  
ATOM   1225  CG  GLN A 163       8.123  43.450   4.226  1.00 12.80           C  
ATOM   1226  CD  GLN A 163       9.159  43.611   3.127  1.00 16.69           C  
ATOM   1227  OE1 GLN A 163      10.298  43.969   3.410  1.00 20.45           O  
ATOM   1228  NE2 GLN A 163       8.822  43.369   1.875  1.00 19.47           N  
ATOM   1229  N   HIS A 164       3.813  45.093   4.331  1.00 11.17           N  
ATOM   1230  CA  HIS A 164       2.730  46.059   4.125  1.00 12.58           C  
ATOM   1231  C   HIS A 164       2.104  46.469   5.477  1.00 11.35           C  
ATOM   1232  O   HIS A 164       1.774  47.644   5.697  1.00 12.13           O  
ATOM   1233  CB  HIS A 164       1.667  45.446   3.223  1.00 13.25           C  
ATOM   1234  CG  HIS A 164       0.442  46.330   3.067  1.00 18.33           C  
ATOM   1235  ND1 HIS A 164      -0.676  46.158   3.866  1.00 20.00           N  
ATOM   1236  CD2 HIS A 164       0.172  47.359   2.228  1.00 20.00           C  
ATOM   1237  CE1 HIS A 164      -1.570  47.055   3.508  1.00 20.00           C  
ATOM   1238  NE2 HIS A 164      -1.082  47.780   2.532  1.00 20.00           N  
ATOM   1239  N   ALA A 165       1.956  45.483   6.361  1.00  8.57           N  
ATOM   1240  CA  ALA A 165       1.356  45.682   7.707  1.00  7.56           C  
ATOM   1241  C   ALA A 165       2.273  46.553   8.577  1.00  8.74           C  
ATOM   1242  O   ALA A 165       1.965  46.833   9.743  1.00  9.31           O  
ATOM   1243  CB  ALA A 165       1.144  44.333   8.395  1.00  6.46           C  
ATOM   1244  N   GLY A 166       3.409  46.954   8.000  1.00  9.08           N  
ATOM   1245  CA  GLY A 166       4.378  47.784   8.686  1.00  9.16           C  
ATOM   1246  C   GLY A 166       5.286  47.012   9.626  1.00 10.17           C  
ATOM   1247  O   GLY A 166       6.020  47.620  10.410  1.00  9.75           O  
ATOM   1248  N   LEU A 167       5.270  45.681   9.521  1.00 10.28           N  
ATOM   1249  CA  LEU A 167       6.075  44.812  10.378  1.00  8.06           C  
ATOM   1250  C   LEU A 167       7.436  44.476   9.787  1.00  6.52           C  
ATOM   1251  O   LEU A 167       7.629  44.557   8.579  1.00  7.67           O  
ATOM   1252  CB  LEU A 167       5.309  43.510  10.674  1.00  7.19           C  
ATOM   1253  CG  LEU A 167       3.943  43.594  11.369  1.00  5.17           C  
ATOM   1254  CD1 LEU A 167       3.375  42.199  11.474  1.00  5.29           C  
ATOM   1255  CD2 LEU A 167       4.072  44.236  12.768  1.00  7.46           C  
ATOM   1256  N   THR A 168       8.359  44.072  10.654  1.00  6.94           N  
ATOM   1257  CA  THR A 168       9.714  43.696  10.269  1.00  7.43           C  
ATOM   1258  C   THR A 168       9.819  42.209  10.043  1.00  4.89           C  
ATOM   1259  O   THR A 168       9.426  41.425  10.897  1.00  5.08           O  
ATOM   1260  CB  THR A 168      10.719  44.027  11.376  1.00 11.02           C  
ATOM   1261  OG1 THR A 168      10.710  45.440  11.608  1.00 17.30           O  
ATOM   1262  CG2 THR A 168      12.136  43.555  10.991  1.00 11.05           C  
ATOM   1263  N   LEU A 169      10.317  41.829   8.874  1.00  6.60           N  
ATOM   1264  CA  LEU A 169      10.544  40.425   8.547  1.00  6.34           C  
ATOM   1265  C   LEU A 169      11.999  40.237   8.995  1.00  6.62           C  
ATOM   1266  O   LEU A 169      12.928  40.676   8.306  1.00  7.91           O  
ATOM   1267  CB  LEU A 169      10.370  40.186   7.028  1.00  6.77           C  
ATOM   1268  CG  LEU A 169      10.493  38.735   6.549  1.00  4.96           C  
ATOM   1269  CD1 LEU A 169       9.380  37.874   7.157  1.00  4.83           C  
ATOM   1270  CD2 LEU A 169      10.461  38.686   5.033  1.00  6.47           C  
ATOM   1271  N   ALA A 170      12.182  39.673  10.188  1.00  3.88           N  
ATOM   1272  CA  ALA A 170      13.505  39.477  10.786  1.00  3.61           C  
ATOM   1273  C   ALA A 170      14.380  38.437  10.092  1.00  2.72           C  
ATOM   1274  O   ALA A 170      15.591  38.512  10.141  1.00  4.64           O  
ATOM   1275  CB  ALA A 170      13.356  39.149  12.244  1.00  2.12           C  
ATOM   1276  N   GLY A 171      13.764  37.474   9.432  1.00  2.06           N  
ATOM   1277  CA  GLY A 171      14.528  36.457   8.737  1.00  2.92           C  
ATOM   1278  C   GLY A 171      13.643  35.327   8.239  1.00  2.08           C  
ATOM   1279  O   GLY A 171      12.435  35.317   8.487  1.00  2.89           O  
ATOM   1280  N   TRP A 172      14.222  34.408   7.479  1.00  2.80           N  
ATOM   1281  CA  TRP A 172      13.484  33.253   6.993  1.00  3.71           C  
ATOM   1282  C   TRP A 172      14.316  31.986   7.234  1.00  4.01           C  
ATOM   1283  O   TRP A 172      15.543  32.050   7.422  1.00  5.13           O  
ATOM   1284  CB  TRP A 172      13.069  33.407   5.520  1.00  2.14           C  
ATOM   1285  CG  TRP A 172      14.155  33.333   4.461  1.00  3.32           C  
ATOM   1286  CD1 TRP A 172      14.991  34.347   4.058  1.00  2.77           C  
ATOM   1287  CD2 TRP A 172      14.428  32.224   3.587  1.00  2.80           C  
ATOM   1288  NE1 TRP A 172      15.738  33.942   2.984  1.00  2.45           N  
ATOM   1289  CE2 TRP A 172      15.422  32.650   2.673  1.00  3.00           C  
ATOM   1290  CE3 TRP A 172      13.921  30.912   3.489  1.00  2.99           C  
ATOM   1291  CZ2 TRP A 172      15.922  31.814   1.666  1.00  4.73           C  
ATOM   1292  CZ3 TRP A 172      14.423  30.078   2.487  1.00  4.53           C  
ATOM   1293  CH2 TRP A 172      15.413  30.536   1.589  1.00  4.20           C  
ATOM   1294  N   VAL A 173      13.631  30.859   7.347  1.00  3.18           N  
ATOM   1295  CA  VAL A 173      14.294  29.590   7.571  1.00  3.70           C  
ATOM   1296  C   VAL A 173      13.842  28.628   6.484  1.00  3.71           C  
ATOM   1297  O   VAL A 173      12.648  28.499   6.222  1.00  4.67           O  
ATOM   1298  CB  VAL A 173      13.966  28.999   8.985  1.00  2.07           C  
ATOM   1299  CG1 VAL A 173      14.467  27.560   9.102  1.00  2.05           C  
ATOM   1300  CG2 VAL A 173      14.593  29.890  10.108  1.00  4.45           C  
ATOM   1301  N   ALA A 174      14.802  28.020   5.794  1.00  4.87           N  
ATOM   1302  CA  ALA A 174      14.485  27.044   4.758  1.00  4.77           C  
ATOM   1303  C   ALA A 174      14.352  25.691   5.454  1.00  4.30           C  
ATOM   1304  O   ALA A 174      15.238  25.283   6.202  1.00  4.38           O  
ATOM   1305  CB  ALA A 174      15.601  26.994   3.709  1.00  3.75           C  
ATOM   1306  N   ASN A 175      13.223  25.027   5.268  1.00  3.68           N  
ATOM   1307  CA  ASN A 175      13.020  23.727   5.875  1.00  3.91           C  
ATOM   1308  C   ASN A 175      12.821  22.649   4.821  1.00  3.67           C  
ATOM   1309  O   ASN A 175      11.909  22.744   3.998  1.00  6.08           O  
ATOM   1310  CB  ASN A 175      11.830  23.770   6.830  1.00  3.43           C  
ATOM   1311  CG  ASN A 175      11.641  22.465   7.565  1.00  4.25           C  
ATOM   1312  OD1 ASN A 175      12.601  21.886   8.037  1.00  4.50           O  
ATOM   1313  ND2 ASN A 175      10.407  21.982   7.642  1.00  2.64           N  
ATOM   1314  N   ASP A 176      13.689  21.644   4.818  1.00  5.29           N  
ATOM   1315  CA  ASP A 176      13.604  20.570   3.839  1.00  5.89           C  
ATOM   1316  C   ASP A 176      12.579  19.549   4.284  1.00  8.60           C  
ATOM   1317  O   ASP A 176      12.885  18.604   5.015  1.00  8.34           O  
ATOM   1318  CB  ASP A 176      14.970  19.923   3.630  1.00  7.41           C  
ATOM   1319  CG  ASP A 176      16.032  20.927   3.206  1.00  8.47           C  
ATOM   1320  OD1 ASP A 176      15.676  22.067   2.852  1.00  9.96           O  
ATOM   1321  OD2 ASP A 176      17.228  20.582   3.247  1.00  9.95           O  
ATOM   1322  N   VAL A 177      11.350  19.763   3.850  1.00  8.82           N  
ATOM   1323  CA  VAL A 177      10.250  18.886   4.205  1.00 11.34           C  
ATOM   1324  C   VAL A 177      10.337  17.521   3.529  1.00 12.18           C  
ATOM   1325  O   VAL A 177       9.790  16.535   4.035  1.00 15.22           O  
ATOM   1326  CB  VAL A 177       8.867  19.561   3.931  1.00 11.21           C  
ATOM   1327  CG1 VAL A 177       8.628  20.676   4.917  1.00 10.94           C  
ATOM   1328  CG2 VAL A 177       8.808  20.128   2.536  1.00  9.74           C  
ATOM   1329  N   THR A 178      11.072  17.441   2.428  1.00 11.30           N  
ATOM   1330  CA  THR A 178      11.214  16.174   1.722  1.00 11.81           C  
ATOM   1331  C   THR A 178      12.680  15.936   1.364  1.00  9.03           C  
ATOM   1332  O   THR A 178      13.509  16.840   1.505  1.00  9.41           O  
ATOM   1333  CB  THR A 178      10.393  16.175   0.401  1.00 12.51           C  
ATOM   1334  OG1 THR A 178      10.922  17.170  -0.486  1.00 13.27           O  
ATOM   1335  CG2 THR A 178       8.918  16.445   0.672  1.00 14.14           C  
ATOM   1336  N   PRO A 179      13.019  14.706   0.919  1.00  9.69           N  
ATOM   1337  CA  PRO A 179      14.401  14.387   0.539  1.00  8.99           C  
ATOM   1338  C   PRO A 179      14.815  15.289  -0.618  1.00  9.45           C  
ATOM   1339  O   PRO A 179      13.957  15.818  -1.349  1.00  8.39           O  
ATOM   1340  CB  PRO A 179      14.302  12.931   0.069  1.00  9.97           C  
ATOM   1341  CG  PRO A 179      13.158  12.389   0.828  1.00  9.89           C  
ATOM   1342  CD  PRO A 179      12.157  13.513   0.775  1.00  9.72           C  
ATOM   1343  N   PRO A 180      16.128  15.441  -0.830  1.00 10.87           N  
ATOM   1344  CA  PRO A 180      16.663  16.284  -1.904  1.00 11.05           C  
ATOM   1345  C   PRO A 180      16.002  16.028  -3.275  1.00 11.41           C  
ATOM   1346  O   PRO A 180      15.938  14.887  -3.758  1.00  7.92           O  
ATOM   1347  CB  PRO A 180      18.149  15.919  -1.900  1.00 10.24           C  
ATOM   1348  CG  PRO A 180      18.419  15.668  -0.456  1.00 10.93           C  
ATOM   1349  CD  PRO A 180      17.222  14.824  -0.054  1.00 11.02           C  
ATOM   1350  N   GLY A 181      15.451  17.098  -3.844  1.00 12.11           N  
ATOM   1351  CA  GLY A 181      14.811  17.040  -5.142  1.00 11.94           C  
ATOM   1352  C   GLY A 181      15.707  17.648  -6.212  1.00 12.53           C  
ATOM   1353  O   GLY A 181      16.707  18.317  -5.920  1.00 10.11           O  
ATOM   1354  N   LYS A 182      15.280  17.510  -7.462  1.00 12.91           N  
ATOM   1355  CA  LYS A 182      16.058  17.992  -8.594  1.00 11.81           C  
ATOM   1356  C   LYS A 182      16.482  19.451  -8.592  1.00  9.26           C  
ATOM   1357  O   LYS A 182      17.636  19.765  -8.855  1.00 10.23           O  
ATOM   1358  CB  LYS A 182      15.336  17.684  -9.914  1.00 12.16           C  
ATOM   1359  CG  LYS A 182      16.228  17.973 -11.082  1.00 12.82           C  
ATOM   1360  CD  LYS A 182      15.675  17.582 -12.424  1.00 12.58           C  
ATOM   1361  CE  LYS A 182      16.435  18.369 -13.474  1.00 13.75           C  
ATOM   1362  NZ  LYS A 182      16.190  17.918 -14.855  1.00 16.27           N  
ATOM   1363  N   ARG A 183      15.559  20.351  -8.297  1.00  7.53           N  
ATOM   1364  CA  ARG A 183      15.888  21.778  -8.322  1.00  7.71           C  
ATOM   1365  C   ARG A 183      16.049  22.423  -6.941  1.00  7.78           C  
ATOM   1366  O   ARG A 183      15.687  23.583  -6.751  1.00  5.43           O  
ATOM   1367  CB  ARG A 183      14.811  22.522  -9.120  1.00  6.88           C  
ATOM   1368  CG  ARG A 183      14.694  22.054 -10.566  1.00  7.57           C  
ATOM   1369  CD  ARG A 183      16.006  22.189 -11.295  1.00  6.80           C  
ATOM   1370  NE  ARG A 183      15.893  21.818 -12.703  1.00  8.84           N  
ATOM   1371  CZ  ARG A 183      16.796  22.098 -13.638  1.00 11.04           C  
ATOM   1372  NH1 ARG A 183      17.908  22.760 -13.338  1.00 12.67           N  
ATOM   1373  NH2 ARG A 183      16.570  21.747 -14.892  1.00 11.72           N  
ATOM   1374  N   HIS A 184      16.656  21.701  -5.999  1.00  8.26           N  
ATOM   1375  CA  HIS A 184      16.821  22.219  -4.633  1.00  7.75           C  
ATOM   1376  C   HIS A 184      17.611  23.513  -4.547  1.00  5.16           C  
ATOM   1377  O   HIS A 184      17.181  24.486  -3.923  1.00  6.19           O  
ATOM   1378  CB  HIS A 184      17.482  21.185  -3.728  1.00  7.18           C  
ATOM   1379  CG  HIS A 184      17.512  21.609  -2.295  1.00  8.66           C  
ATOM   1380  ND1 HIS A 184      16.423  21.468  -1.474  1.00 10.75           N  
ATOM   1381  CD2 HIS A 184      18.521  22.072  -1.517  1.00  9.10           C  
ATOM   1382  CE1 HIS A 184      16.756  21.819  -0.244  1.00  8.75           C  
ATOM   1383  NE2 HIS A 184      18.021  22.188  -0.244  1.00 11.33           N  
ATOM   1384  N   ALA A 185      18.767  23.520  -5.185  1.00  5.98           N  
ATOM   1385  CA  ALA A 185      19.725  24.584  -5.159  1.00  7.15           C  
ATOM   1386  C   ALA A 185      19.130  25.811  -5.851  1.00  7.95           C  
ATOM   1387  O   ALA A 185      19.252  26.931  -5.343  1.00  6.82           O  
ATOM   1388  CB  ALA A 185      21.046  24.184  -5.813  1.00  9.04           C  
ATOM   1389  N   GLU A 186      18.485  25.593  -7.001  1.00  7.67           N  
ATOM   1390  CA  GLU A 186      17.855  26.680  -7.765  1.00  6.41           C  
ATOM   1391  C   GLU A 186      16.711  27.316  -6.972  1.00  5.28           C  
ATOM   1392  O   GLU A 186      16.491  28.521  -7.052  1.00  4.61           O  
ATOM   1393  CB  GLU A 186      17.343  26.176  -9.116  1.00  5.69           C  
ATOM   1394  CG  GLU A 186      18.459  25.786 -10.078  1.00  7.50           C  
ATOM   1395  CD  GLU A 186      18.804  24.308 -10.018  1.00 10.71           C  
ATOM   1396  OE1 GLU A 186      18.656  23.651  -8.955  1.00 11.14           O  
ATOM   1397  OE2 GLU A 186      19.225  23.787 -11.062  1.00 11.08           O  
ATOM   1398  N   TYR A 187      15.980  26.508  -6.214  1.00  3.94           N  
ATOM   1399  CA  TYR A 187      14.894  27.042  -5.404  1.00  5.52           C  
ATOM   1400  C   TYR A 187      15.480  27.864  -4.253  1.00  4.37           C  
ATOM   1401  O   TYR A 187      15.005  28.966  -3.949  1.00  3.10           O  
ATOM   1402  CB  TYR A 187      13.994  25.907  -4.897  1.00  4.42           C  
ATOM   1403  CG  TYR A 187      12.652  25.822  -5.607  1.00  7.70           C  
ATOM   1404  CD1 TYR A 187      12.548  25.315  -6.897  1.00  7.29           C  
ATOM   1405  CD2 TYR A 187      11.489  26.309  -4.998  1.00  8.04           C  
ATOM   1406  CE1 TYR A 187      11.320  25.306  -7.576  1.00  9.81           C  
ATOM   1407  CE2 TYR A 187      10.268  26.302  -5.656  1.00 10.29           C  
ATOM   1408  CZ  TYR A 187      10.184  25.805  -6.954  1.00  9.41           C  
ATOM   1409  OH  TYR A 187       8.971  25.858  -7.621  1.00  9.26           O  
ATOM   1410  N   MET A 188      16.570  27.369  -3.668  1.00  6.03           N  
ATOM   1411  CA  MET A 188      17.224  28.079  -2.560  1.00  5.54           C  
ATOM   1412  C   MET A 188      17.768  29.432  -3.022  1.00  5.65           C  
ATOM   1413  O   MET A 188      17.629  30.423  -2.303  1.00  5.23           O  
ATOM   1414  CB  MET A 188      18.320  27.216  -1.906  1.00  4.43           C  
ATOM   1415  CG  MET A 188      17.760  26.110  -1.007  1.00  4.74           C  
ATOM   1416  SD  MET A 188      16.853  26.756   0.415  1.00  6.38           S  
ATOM   1417  CE  MET A 188      18.144  27.685   1.260  1.00  6.65           C  
ATOM   1418  N   THR A 189      18.312  29.488  -4.241  1.00  2.26           N  
ATOM   1419  CA  THR A 189      18.842  30.733  -4.786  1.00  3.89           C  
ATOM   1420  C   THR A 189      17.709  31.723  -5.056  1.00  2.97           C  
ATOM   1421  O   THR A 189      17.833  32.904  -4.734  1.00  3.36           O  
ATOM   1422  CB  THR A 189      19.628  30.487  -6.085  1.00  4.38           C  
ATOM   1423  OG1 THR A 189      20.749  29.661  -5.792  1.00  7.31           O  
ATOM   1424  CG2 THR A 189      20.122  31.776  -6.676  1.00  7.15           C  
ATOM   1425  N   THR A 190      16.598  31.227  -5.605  1.00  2.87           N  
ATOM   1426  CA  THR A 190      15.436  32.065  -5.913  1.00  2.90           C  
ATOM   1427  C   THR A 190      14.835  32.619  -4.632  1.00  2.09           C  
ATOM   1428  O   THR A 190      14.538  33.799  -4.541  1.00  3.14           O  
ATOM   1429  CB  THR A 190      14.352  31.277  -6.710  1.00  3.94           C  
ATOM   1430  OG1 THR A 190      14.909  30.818  -7.951  1.00  5.42           O  
ATOM   1431  CG2 THR A 190      13.121  32.159  -6.985  1.00  3.14           C  
ATOM   1432  N   LEU A 191      14.653  31.760  -3.648  1.00  2.03           N  
ATOM   1433  CA  LEU A 191      14.116  32.159  -2.351  1.00  2.44           C  
ATOM   1434  C   LEU A 191      15.017  33.202  -1.657  1.00  2.85           C  
ATOM   1435  O   LEU A 191      14.536  34.204  -1.134  1.00  2.03           O  
ATOM   1436  CB  LEU A 191      13.955  30.910  -1.474  1.00  3.90           C  
ATOM   1437  CG  LEU A 191      12.785  29.984  -1.828  1.00  3.65           C  
ATOM   1438  CD1 LEU A 191      12.911  28.683  -1.074  1.00  3.91           C  
ATOM   1439  CD2 LEU A 191      11.447  30.664  -1.526  1.00  3.49           C  
ATOM   1440  N   THR A 192      16.330  32.972  -1.693  1.00  3.67           N  
ATOM   1441  CA  THR A 192      17.306  33.893  -1.113  1.00  3.63           C  
ATOM   1442  C   THR A 192      17.237  35.287  -1.766  1.00  4.44           C  
ATOM   1443  O   THR A 192      17.298  36.303  -1.080  1.00  6.45           O  
ATOM   1444  CB  THR A 192      18.741  33.306  -1.208  1.00  3.37           C  
ATOM   1445  OG1 THR A 192      18.775  32.026  -0.559  1.00  3.56           O  
ATOM   1446  CG2 THR A 192      19.747  34.221  -0.535  1.00  3.10           C  
ATOM   1447  N   ARG A 193      17.113  35.339  -3.091  1.00  5.95           N  
ATOM   1448  CA  ARG A 193      17.005  36.624  -3.772  1.00  6.51           C  
ATOM   1449  C   ARG A 193      15.700  37.367  -3.459  1.00  6.37           C  
ATOM   1450  O   ARG A 193      15.689  38.582  -3.246  1.00  6.27           O  
ATOM   1451  CB  ARG A 193      17.096  36.454  -5.303  1.00  7.51           C  
ATOM   1452  CG  ARG A 193      16.787  37.767  -6.093  1.00  9.45           C  
ATOM   1453  CD  ARG A 193      16.913  37.635  -7.650  1.00 10.37           C  
ATOM   1454  NE  ARG A 193      15.945  36.708  -8.246  1.00  9.31           N  
ATOM   1455  CZ  ARG A 193      16.228  35.466  -8.639  1.00  7.17           C  
ATOM   1456  NH1 ARG A 193      17.452  34.974  -8.504  1.00  5.67           N  
ATOM   1457  NH2 ARG A 193      15.283  34.730  -9.206  1.00  9.14           N  
ATOM   1458  N   MET A 194      14.604  36.625  -3.454  1.00  6.33           N  
ATOM   1459  CA  MET A 194      13.277  37.202  -3.282  1.00  8.02           C  
ATOM   1460  C   MET A 194      12.771  37.591  -1.902  1.00  7.21           C  
ATOM   1461  O   MET A 194      11.966  38.519  -1.789  1.00  6.40           O  
ATOM   1462  CB  MET A 194      12.247  36.314  -3.997  1.00  9.97           C  
ATOM   1463  CG  MET A 194      12.572  36.129  -5.465  1.00 15.81           C  
ATOM   1464  SD  MET A 194      11.371  35.193  -6.408  1.00 23.26           S  
ATOM   1465  CE  MET A 194      10.581  36.567  -7.274  1.00 23.88           C  
ATOM   1466  N   ILE A 195      13.207  36.884  -0.868  1.00  5.76           N  
ATOM   1467  CA  ILE A 195      12.746  37.190   0.485  1.00  4.67           C  
ATOM   1468  C   ILE A 195      13.645  38.269   1.052  1.00  4.22           C  
ATOM   1469  O   ILE A 195      14.841  38.063   1.220  1.00  4.94           O  
ATOM   1470  CB  ILE A 195      12.733  35.945   1.402  1.00  2.81           C  
ATOM   1471  CG1 ILE A 195      11.791  34.874   0.809  1.00  3.22           C  
ATOM   1472  CG2 ILE A 195      12.287  36.373   2.810  1.00  2.08           C  
ATOM   1473  CD1 ILE A 195      11.925  33.496   1.386  1.00  4.28           C  
ATOM   1474  N   PRO A 196      13.085  39.458   1.311  1.00  5.57           N  
ATOM   1475  CA  PRO A 196      13.837  40.594   1.850  1.00  5.57           C  
ATOM   1476  C   PRO A 196      14.172  40.437   3.326  1.00  4.42           C  
ATOM   1477  O   PRO A 196      13.796  41.253   4.156  1.00  4.89           O  
ATOM   1478  CB  PRO A 196      12.895  41.766   1.595  1.00  4.90           C  
ATOM   1479  CG  PRO A 196      11.540  41.143   1.827  1.00  6.59           C  
ATOM   1480  CD  PRO A 196      11.655  39.792   1.146  1.00  5.77           C  
ATOM   1481  N   ALA A 197      14.914  39.390   3.634  1.00  5.51           N  
ATOM   1482  CA  ALA A 197      15.302  39.107   4.997  1.00  4.36           C  
ATOM   1483  C   ALA A 197      16.418  38.071   4.950  1.00  4.40           C  
ATOM   1484  O   ALA A 197      16.509  37.272   4.003  1.00  5.59           O  
ATOM   1485  CB  ALA A 197      14.101  38.581   5.797  1.00  3.43           C  
ATOM   1486  N   PRO A 198      17.284  38.059   5.971  1.00  3.95           N  
ATOM   1487  CA  PRO A 198      18.370  37.085   5.970  1.00  3.30           C  
ATOM   1488  C   PRO A 198      17.949  35.635   6.113  1.00  2.39           C  
ATOM   1489  O   PRO A 198      17.056  35.318   6.893  1.00  2.19           O  
ATOM   1490  CB  PRO A 198      19.220  37.518   7.175  1.00  5.14           C  
ATOM   1491  CG  PRO A 198      18.239  38.138   8.096  1.00  3.88           C  
ATOM   1492  CD  PRO A 198      17.374  38.950   7.142  1.00  2.26           C  
ATOM   1493  N   LEU A 199      18.592  34.753   5.358  1.00  2.00           N  
ATOM   1494  CA  LEU A 199      18.342  33.323   5.487  1.00  2.60           C  
ATOM   1495  C   LEU A 199      19.066  32.935   6.795  1.00  2.51           C  
ATOM   1496  O   LEU A 199      20.300  32.994   6.875  1.00  2.46           O  
ATOM   1497  CB  LEU A 199      18.964  32.571   4.302  1.00  4.17           C  
ATOM   1498  CG  LEU A 199      19.110  31.042   4.377  1.00  2.03           C  
ATOM   1499  CD1 LEU A 199      17.783  30.340   4.707  1.00  2.11           C  
ATOM   1500  CD2 LEU A 199      19.685  30.550   3.060  1.00  2.08           C  
ATOM   1501  N   LEU A 200      18.314  32.544   7.814  1.00  3.14           N  
ATOM   1502  CA  LEU A 200      18.915  32.201   9.111  1.00  4.59           C  
ATOM   1503  C   LEU A 200      19.585  30.838   9.133  1.00  6.70           C  
ATOM   1504  O   LEU A 200      20.424  30.565   9.995  1.00  8.47           O  
ATOM   1505  CB  LEU A 200      17.851  32.236  10.225  1.00  5.48           C  
ATOM   1506  CG  LEU A 200      17.031  33.515  10.423  1.00  3.49           C  
ATOM   1507  CD1 LEU A 200      16.131  33.370  11.660  1.00  5.99           C  
ATOM   1508  CD2 LEU A 200      17.967  34.691  10.564  1.00  5.98           C  
ATOM   1509  N   GLY A 201      19.144  29.957   8.243  1.00  6.85           N  
ATOM   1510  CA  GLY A 201      19.686  28.613   8.193  1.00  5.80           C  
ATOM   1511  C   GLY A 201      18.742  27.678   7.470  1.00  6.55           C  
ATOM   1512  O   GLY A 201      17.598  28.056   7.172  1.00  3.64           O  
ATOM   1513  N   GLU A 202      19.215  26.456   7.211  1.00  5.73           N  
ATOM   1514  CA  GLU A 202      18.433  25.435   6.508  1.00  5.27           C  
ATOM   1515  C   GLU A 202      18.390  24.124   7.316  1.00  4.17           C  
ATOM   1516  O   GLU A 202      19.430  23.596   7.734  1.00  4.78           O  
ATOM   1517  CB  GLU A 202      18.999  25.197   5.090  1.00  2.10           C  
ATOM   1518  CG  GLU A 202      18.252  24.110   4.325  1.00  5.13           C  
ATOM   1519  CD  GLU A 202      18.637  23.982   2.844  1.00 10.50           C  
ATOM   1520  OE1 GLU A 202      19.548  24.682   2.347  1.00 10.08           O  
ATOM   1521  OE2 GLU A 202      17.996  23.157   2.173  1.00  9.99           O  
ATOM   1522  N   ILE A 203      17.189  23.630   7.587  1.00  2.02           N  
ATOM   1523  CA  ILE A 203      17.057  22.399   8.345  1.00  2.45           C  
ATOM   1524  C   ILE A 203      16.963  21.245   7.352  1.00  3.37           C  
ATOM   1525  O   ILE A 203      16.113  21.243   6.459  1.00  4.68           O  
ATOM   1526  CB  ILE A 203      15.838  22.482   9.284  1.00  3.84           C  
ATOM   1527  CG1 ILE A 203      16.071  23.619  10.293  1.00  5.68           C  
ATOM   1528  CG2 ILE A 203      15.575  21.141   9.998  1.00  2.10           C  
ATOM   1529  CD1 ILE A 203      14.916  23.864  11.179  1.00  8.78           C  
ATOM   1530  N   PRO A 204      17.878  20.278   7.452  1.00  5.34           N  
ATOM   1531  CA  PRO A 204      17.877  19.125   6.538  1.00  6.66           C  
ATOM   1532  C   PRO A 204      16.636  18.260   6.691  1.00  6.51           C  
ATOM   1533  O   PRO A 204      15.901  18.382   7.682  1.00  5.50           O  
ATOM   1534  CB  PRO A 204      19.118  18.321   6.978  1.00  8.33           C  
ATOM   1535  CG  PRO A 204      19.963  19.307   7.728  1.00  7.52           C  
ATOM   1536  CD  PRO A 204      18.976  20.182   8.433  1.00  4.85           C  
ATOM   1537  N   TRP A 205      16.415  17.375   5.715  1.00  7.51           N  
ATOM   1538  CA  TRP A 205      15.291  16.444   5.771  1.00  8.92           C  
ATOM   1539  C   TRP A 205      15.643  15.408   6.843  1.00  8.94           C  
ATOM   1540  O   TRP A 205      16.537  14.576   6.645  1.00  7.84           O  
ATOM   1541  CB  TRP A 205      15.069  15.764   4.411  1.00  7.92           C  
ATOM   1542  CG  TRP A 205      14.049  14.668   4.473  1.00  9.17           C  
ATOM   1543  CD1 TRP A 205      12.708  14.788   4.780  1.00  9.28           C  
ATOM   1544  CD2 TRP A 205      14.290  13.275   4.287  1.00  9.00           C  
ATOM   1545  NE1 TRP A 205      12.113  13.547   4.801  1.00  8.76           N  
ATOM   1546  CE2 TRP A 205      13.061  12.602   4.503  1.00 12.15           C  
ATOM   1547  CE3 TRP A 205      15.426  12.527   3.965  1.00  9.07           C  
ATOM   1548  CZ2 TRP A 205      12.943  11.210   4.407  1.00 14.51           C  
ATOM   1549  CZ3 TRP A 205      15.309  11.145   3.872  1.00 13.26           C  
ATOM   1550  CH2 TRP A 205      14.077  10.501   4.092  1.00 13.77           C  
ATOM   1551  N   LEU A 206      14.978  15.501   7.995  1.00  9.94           N  
ATOM   1552  CA  LEU A 206      15.214  14.606   9.129  1.00 13.24           C  
ATOM   1553  C   LEU A 206      13.958  13.776   9.375  1.00 17.83           C  
ATOM   1554  O   LEU A 206      13.061  14.154  10.139  1.00 19.69           O  
ATOM   1555  CB  LEU A 206      15.585  15.429  10.366  1.00  9.12           C  
ATOM   1556  CG  LEU A 206      16.953  16.104  10.221  1.00 10.10           C  
ATOM   1557  CD1 LEU A 206      17.024  17.400  11.006  1.00 10.33           C  
ATOM   1558  CD2 LEU A 206      18.030  15.134  10.650  1.00 11.34           C  
ATOM   1559  N   ALA A 207      13.898  12.646   8.688  1.00 21.32           N  
ATOM   1560  CA  ALA A 207      12.755  11.742   8.736  1.00 24.38           C  
ATOM   1561  C   ALA A 207      12.193  11.402  10.116  1.00 25.99           C  
ATOM   1562  O   ALA A 207      10.990  11.571  10.357  1.00 26.60           O  
ATOM   1563  CB  ALA A 207      13.092  10.466   7.971  1.00 23.31           C  
ATOM   1564  N   GLU A 208      13.073  10.934  11.008  1.00 27.76           N  
ATOM   1565  CA  GLU A 208      12.711  10.511  12.362  1.00 27.96           C  
ATOM   1566  C   GLU A 208      12.748  11.624  13.401  1.00 25.97           C  
ATOM   1567  O   GLU A 208      13.770  12.277  13.572  1.00 25.06           O  
ATOM   1568  CB  GLU A 208      13.626   9.353  12.803  1.00 32.49           C  
ATOM   1569  CG  GLU A 208      13.172   8.598  14.056  1.00 40.54           C  
ATOM   1570  CD  GLU A 208      14.153   8.722  15.223  1.00 45.55           C  
ATOM   1571  OE1 GLU A 208      15.164   7.977  15.241  1.00 47.55           O  
ATOM   1572  OE2 GLU A 208      13.913   9.565  16.122  1.00 47.17           O  
ATOM   1573  N   ASN A 209      11.609  11.822  14.069  1.00 26.58           N  
ATOM   1574  CA  ASN A 209      11.403  12.812  15.142  1.00 27.22           C  
ATOM   1575  C   ASN A 209      12.264  14.072  15.069  1.00 24.73           C  
ATOM   1576  O   ASN A 209      12.982  14.395  16.021  1.00 25.28           O  
ATOM   1577  CB  ASN A 209      11.579  12.147  16.522  1.00 32.82           C  
ATOM   1578  CG  ASN A 209      10.725  10.890  16.679  1.00 38.40           C  
ATOM   1579  OD1 ASN A 209      11.047   9.841  16.111  1.00 41.83           O  
ATOM   1580  ND2 ASN A 209       9.618  10.992  17.425  1.00 41.87           N  
ATOM   1581  N   PRO A 210      12.114  14.863  13.991  1.00 21.35           N  
ATOM   1582  CA  PRO A 210      12.904  16.088  13.832  1.00 19.21           C  
ATOM   1583  C   PRO A 210      12.676  17.159  14.905  1.00 17.64           C  
ATOM   1584  O   PRO A 210      13.480  18.071  15.038  1.00 15.86           O  
ATOM   1585  CB  PRO A 210      12.511  16.567  12.434  1.00 18.25           C  
ATOM   1586  CG  PRO A 210      11.076  16.124  12.323  1.00 19.61           C  
ATOM   1587  CD  PRO A 210      11.124  14.729  12.907  1.00 20.05           C  
ATOM   1588  N   GLU A 211      11.586  17.043  15.665  1.00 16.66           N  
ATOM   1589  CA  GLU A 211      11.275  18.001  16.729  1.00 16.46           C  
ATOM   1590  C   GLU A 211      12.269  17.793  17.870  1.00 17.09           C  
ATOM   1591  O   GLU A 211      12.563  18.718  18.643  1.00 16.82           O  
ATOM   1592  CB  GLU A 211       9.839  17.808  17.267  1.00 15.18           C  
ATOM   1593  CG  GLU A 211       8.716  18.126  16.282  1.00 16.11           C  
ATOM   1594  CD  GLU A 211       8.482  17.035  15.227  1.00 17.16           C  
ATOM   1595  OE1 GLU A 211       8.968  15.896  15.391  1.00 19.16           O  
ATOM   1596  OE2 GLU A 211       7.793  17.308  14.223  1.00 14.84           O  
ATOM   1597  N   ASN A 212      12.793  16.574  17.957  1.00 16.00           N  
ATOM   1598  CA  ASN A 212      13.749  16.239  18.995  1.00 16.84           C  
ATOM   1599  C   ASN A 212      15.172  16.009  18.487  1.00 17.38           C  
ATOM   1600  O   ASN A 212      16.028  15.513  19.230  1.00 17.25           O  
ATOM   1601  CB  ASN A 212      13.253  15.041  19.786  1.00 18.75           C  
ATOM   1602  CG  ASN A 212      11.942  15.326  20.487  1.00 20.02           C  
ATOM   1603  OD1 ASN A 212      10.981  14.565  20.346  1.00 21.45           O  
ATOM   1604  ND2 ASN A 212      11.888  16.435  21.241  1.00 19.05           N  
ATOM   1605  N   ALA A 213      15.416  16.330  17.213  1.00 14.69           N  
ATOM   1606  CA  ALA A 213      16.756  16.198  16.627  1.00 12.24           C  
ATOM   1607  C   ALA A 213      17.535  17.445  17.046  1.00 10.65           C  
ATOM   1608  O   ALA A 213      16.928  18.471  17.358  1.00 11.42           O  
ATOM   1609  CB  ALA A 213      16.660  16.111  15.101  1.00  9.24           C  
ATOM   1610  N   ALA A 214      18.858  17.339  17.146  1.00  9.63           N  
ATOM   1611  CA  ALA A 214      19.694  18.487  17.512  1.00  8.09           C  
ATOM   1612  C   ALA A 214      19.838  19.328  16.251  1.00  6.82           C  
ATOM   1613  O   ALA A 214      20.701  19.061  15.413  1.00  6.45           O  
ATOM   1614  CB  ALA A 214      21.046  18.012  17.995  1.00  8.25           C  
ATOM   1615  N   THR A 215      18.969  20.324  16.111  1.00  5.73           N  
ATOM   1616  CA  THR A 215      18.933  21.173  14.923  1.00  3.89           C  
ATOM   1617  C   THR A 215      19.394  22.618  15.115  1.00  3.67           C  
ATOM   1618  O   THR A 215      19.438  23.384  14.138  1.00  3.27           O  
ATOM   1619  CB  THR A 215      17.501  21.197  14.355  1.00  5.71           C  
ATOM   1620  OG1 THR A 215      16.596  21.490  15.423  1.00  2.49           O  
ATOM   1621  CG2 THR A 215      17.125  19.852  13.736  1.00  3.60           C  
ATOM   1622  N   GLY A 216      19.667  23.004  16.366  1.00  2.33           N  
ATOM   1623  CA  GLY A 216      20.136  24.357  16.654  1.00  4.24           C  
ATOM   1624  C   GLY A 216      21.346  24.774  15.816  1.00  3.78           C  
ATOM   1625  O   GLY A 216      21.507  25.944  15.474  1.00  3.91           O  
ATOM   1626  N   LYS A 217      22.199  23.808  15.486  1.00  3.92           N  
ATOM   1627  CA  LYS A 217      23.395  24.042  14.678  1.00  5.66           C  
ATOM   1628  C   LYS A 217      23.106  24.600  13.269  1.00  5.55           C  
ATOM   1629  O   LYS A 217      23.988  25.176  12.626  1.00  7.48           O  
ATOM   1630  CB  LYS A 217      24.203  22.746  14.554  1.00  8.40           C  
ATOM   1631  CG  LYS A 217      23.383  21.536  14.026  1.00 10.90           C  
ATOM   1632  CD  LYS A 217      24.192  20.621  13.093  1.00 16.09           C  
ATOM   1633  CE  LYS A 217      25.461  20.084  13.731  1.00 19.24           C  
ATOM   1634  NZ  LYS A 217      26.280  19.243  12.784  1.00 23.81           N  
ATOM   1635  N   TYR A 218      21.883  24.419  12.789  1.00  5.53           N  
ATOM   1636  CA  TYR A 218      21.510  24.895  11.458  1.00  5.41           C  
ATOM   1637  C   TYR A 218      21.081  26.345  11.422  1.00  4.84           C  
ATOM   1638  O   TYR A 218      20.893  26.897  10.358  1.00  8.36           O  
ATOM   1639  CB  TYR A 218      20.406  24.001  10.877  1.00  5.33           C  
ATOM   1640  CG  TYR A 218      20.847  22.562  10.757  1.00  6.63           C  
ATOM   1641  CD1 TYR A 218      21.910  22.210   9.917  1.00  6.25           C  
ATOM   1642  CD2 TYR A 218      20.254  21.560  11.526  1.00  7.88           C  
ATOM   1643  CE1 TYR A 218      22.370  20.903   9.853  1.00  7.27           C  
ATOM   1644  CE2 TYR A 218      20.714  20.247  11.474  1.00  8.34           C  
ATOM   1645  CZ  TYR A 218      21.767  19.927  10.638  1.00  6.05           C  
ATOM   1646  OH  TYR A 218      22.216  18.632  10.592  1.00  6.78           O  
ATOM   1647  N   ILE A 219      20.973  26.970  12.586  1.00  4.39           N  
ATOM   1648  CA  ILE A 219      20.548  28.359  12.684  1.00  3.85           C  
ATOM   1649  C   ILE A 219      21.706  29.259  13.122  1.00  5.89           C  
ATOM   1650  O   ILE A 219      22.410  28.952  14.094  1.00  6.80           O  
ATOM   1651  CB  ILE A 219      19.425  28.509  13.734  1.00  3.43           C  
ATOM   1652  CG1 ILE A 219      18.205  27.644  13.363  1.00  2.46           C  
ATOM   1653  CG2 ILE A 219      19.119  29.983  13.966  1.00  2.01           C  
ATOM   1654  CD1 ILE A 219      17.558  27.969  12.050  1.00  3.19           C  
ATOM   1655  N   ASN A 220      21.906  30.357  12.404  1.00  5.55           N  
ATOM   1656  CA  ASN A 220      22.943  31.313  12.752  1.00  6.44           C  
ATOM   1657  C   ASN A 220      22.220  32.493  13.403  1.00  6.29           C  
ATOM   1658  O   ASN A 220      21.747  33.406  12.732  1.00  5.34           O  
ATOM   1659  CB  ASN A 220      23.733  31.771  11.523  1.00  7.56           C  
ATOM   1660  CG  ASN A 220      24.841  32.753  11.882  1.00 11.40           C  
ATOM   1661  OD1 ASN A 220      25.048  33.081  13.067  1.00 11.23           O  
ATOM   1662  ND2 ASN A 220      25.564  33.225  10.874  1.00 12.45           N  
ATOM   1663  N   LEU A 221      22.137  32.454  14.726  1.00  7.27           N  
ATOM   1664  CA  LEU A 221      21.436  33.480  15.483  1.00  9.27           C  
ATOM   1665  C   LEU A 221      22.024  34.896  15.341  1.00  8.96           C  
ATOM   1666  O   LEU A 221      21.323  35.875  15.553  1.00  9.83           O  
ATOM   1667  CB  LEU A 221      21.331  33.049  16.946  1.00  9.54           C  
ATOM   1668  CG  LEU A 221      19.970  33.105  17.638  1.00 11.59           C  
ATOM   1669  CD1 LEU A 221      18.920  32.273  16.945  1.00 12.35           C  
ATOM   1670  CD2 LEU A 221      20.157  32.642  19.034  1.00 12.69           C  
ATOM   1671  N   ALA A 222      23.284  35.012  14.931  1.00 10.71           N  
ATOM   1672  CA  ALA A 222      23.899  36.334  14.757  1.00 13.33           C  
ATOM   1673  C   ALA A 222      23.323  37.087  13.544  1.00 15.74           C  
ATOM   1674  O   ALA A 222      23.606  38.276  13.361  1.00 15.33           O  
ATOM   1675  CB  ALA A 222      25.420  36.225  14.634  1.00 14.07           C  
ATOM   1676  N   LEU A 223      22.593  36.379  12.678  1.00 15.29           N  
ATOM   1677  CA  LEU A 223      21.960  37.009  11.514  1.00 15.47           C  
ATOM   1678  C   LEU A 223      20.565  37.499  11.878  1.00 14.60           C  
ATOM   1679  O   LEU A 223      19.927  38.176  11.080  1.00 16.27           O  
ATOM   1680  CB  LEU A 223      21.844  36.041  10.337  1.00 14.80           C  
ATOM   1681  CG  LEU A 223      23.085  35.290   9.875  1.00 17.36           C  
ATOM   1682  CD1 LEU A 223      22.713  34.409   8.683  1.00 18.89           C  
ATOM   1683  CD2 LEU A 223      24.223  36.249   9.525  1.00 17.94           C  
ATOM   1684  N   LEU A 224      20.078  37.114  13.056  1.00 14.51           N  
ATOM   1685  CA  LEU A 224      18.755  37.514  13.513  1.00 14.30           C  
ATOM   1686  C   LEU A 224      18.825  38.861  14.203  1.00 15.07           C  
ATOM   1687  O   LEU A 224      19.709  39.037  15.058  1.00 16.48           O  
ATOM   1688  CB  LEU A 224      18.193  36.509  14.521  1.00 14.10           C  
ATOM   1689  CG  LEU A 224      16.832  35.877  14.255  1.00 13.28           C  
ATOM   1690  CD1 LEU A 224      16.311  35.273  15.551  1.00 10.06           C  
ATOM   1691  CD2 LEU A 224      15.848  36.856  13.637  1.00  9.90           C  
ATOM   1692  OXT LEU A 224      17.961  39.706  13.912  1.00 16.65           O  
TER    1693      LEU A 224                                                      
HETATM 1694 MG    MG A 901       3.314  23.888  14.212  1.00 12.42          MG  
HETATM 1695  C1  DNN A 801      -6.503  28.343   6.948  1.00  7.59           C  
HETATM 1696  O1  DNN A 801      -5.795  29.206   6.405  1.00  7.86           O  
HETATM 1697  O2  DNN A 801      -7.371  27.691   6.329  1.00  7.42           O  
HETATM 1698  C2  DNN A 801      -6.289  28.093   8.433  1.00  8.57           C  
HETATM 1699  C3  DNN A 801      -5.643  26.738   8.724  1.00  9.93           C  
HETATM 1700  C4  DNN A 801      -5.059  26.673  10.136  1.00 11.01           C  
HETATM 1701  C5  DNN A 801      -4.631  25.265  10.467  1.00 10.72           C  
HETATM 1702  C6  DNN A 801      -3.650  25.157  11.654  1.00 14.30           C  
HETATM 1703  C7  DNN A 801      -3.845  23.883  12.487  1.00 14.67           C  
HETATM 1704  C8  DNN A 801      -3.789  22.632  11.599  1.00 12.97           C  
HETATM 1705  C9  DNN A 801      -4.965  21.766  11.935  1.00 12.02           C  
HETATM 1706  N7  DNN A 801      -2.929  23.817  13.668  1.00 11.66           N  
HETATM 1707  N8  DNN A 801      -2.511  21.852  11.734  1.00 13.66           N  
HETATM 1708  PG  ATP A 802       0.942  23.641  11.956  1.00 23.47           P  
HETATM 1709  O1G ATP A 802       0.128  22.494  12.468  1.00 19.64           O  
HETATM 1710  O2G ATP A 802       0.294  24.710  11.096  1.00 20.82           O  
HETATM 1711  O3G ATP A 802       1.474  24.522  13.215  1.00 16.19           O  
HETATM 1712  PB  ATP A 802       3.828  23.334  11.082  1.00  8.29           P  
HETATM 1713  O1B ATP A 802       4.221  23.589  12.489  1.00  7.33           O  
HETATM 1714  O2B ATP A 802       4.030  24.384  10.053  1.00  8.31           O  
HETATM 1715  O3B ATP A 802       2.266  22.960  11.124  1.00 13.27           O  
HETATM 1716  PA  ATP A 802       5.562  20.965  11.527  1.00 11.56           P  
HETATM 1717  O1A ATP A 802       6.859  21.523  12.024  1.00 11.30           O  
HETATM 1718  O2A ATP A 802       4.642  20.301  12.470  1.00 10.53           O  
HETATM 1719  O3A ATP A 802       4.750  22.102  10.688  1.00  9.56           O  
HETATM 1720  O5' ATP A 802       5.945  19.986  10.293  1.00 11.00           O  
HETATM 1721  C5' ATP A 802       4.892  19.279   9.602  1.00  9.40           C  
HETATM 1722  C4' ATP A 802       5.249  17.800   9.447  1.00 11.76           C  
HETATM 1723  O4' ATP A 802       6.419  17.604   8.615  1.00  9.86           O  
HETATM 1724  C3' ATP A 802       5.505  17.072  10.772  1.00 10.89           C  
HETATM 1725  O3' ATP A 802       5.039  15.707  10.788  1.00 11.09           O  
HETATM 1726  C2' ATP A 802       7.022  17.119  10.877  1.00 11.15           C  
HETATM 1727  O2' ATP A 802       7.520  16.069  11.726  1.00 11.27           O  
HETATM 1728  C1' ATP A 802       7.440  16.999   9.417  1.00 10.57           C  
HETATM 1729  N9  ATP A 802       8.695  17.771   9.196  1.00 11.16           N  
HETATM 1730  C8  ATP A 802       8.832  19.082   9.389  1.00  9.82           C  
HETATM 1731  N7  ATP A 802      10.089  19.427   9.115  1.00 10.29           N  
HETATM 1732  C5  ATP A 802      10.762  18.341   8.753  1.00  9.02           C  
HETATM 1733  C6  ATP A 802      12.074  18.102   8.373  1.00  7.61           C  
HETATM 1734  N6  ATP A 802      12.978  19.070   8.320  1.00  6.14           N  
HETATM 1735  N1  ATP A 802      12.416  16.845   8.061  1.00  9.13           N  
HETATM 1736  C2  ATP A 802      11.528  15.839   8.106  1.00  9.63           C  
HETATM 1737  N3  ATP A 802      10.268  16.049   8.468  1.00  9.90           N  
HETATM 1738  C4  ATP A 802       9.871  17.284   8.794  1.00  9.17           C  
HETATM 1739  O   HOH A 301       2.178  28.563  -4.511  1.00  5.47           O  
HETATM 1740  O   HOH A 302      14.373  19.807  -3.062  1.00 15.07           O  
HETATM 1741  O   HOH A 304      12.275  20.018   0.923  1.00 14.88           O  
HETATM 1742  O   HOH A 306      13.994  13.594  -6.224  1.00 15.84           O  
HETATM 1743  O   HOH A 307      20.100  18.785   0.031  1.00 14.52           O  
HETATM 1744  O   HOH A 308      18.367  16.623   3.708  1.00 14.75           O  
HETATM 1745  O   HOH A 309      21.350  22.280   5.875  1.00 16.80           O  
HETATM 1746  O   HOH A 310      22.063  26.097   7.612  1.00  8.94           O  
HETATM 1747  O   HOH A 311      21.907  27.967   5.339  1.00 15.37           O  
HETATM 1748  O   HOH A 314      22.813  32.249   1.243  1.00 10.14           O  
HETATM 1749  O   HOH A 315      17.257  36.186   1.597  1.00  2.68           O  
HETATM 1750  O   HOH A 316      22.221  34.553   5.534  1.00  8.47           O  
HETATM 1751  O   HOH A 317      22.822  28.985   9.179  1.00 16.06           O  
HETATM 1752  O   HOH A 321      23.780  30.762  16.416  1.00 18.02           O  
HETATM 1753  O   HOH A 322      26.009  29.558  19.899  1.00 27.16           O  
HETATM 1754  O   HOH A 323      23.692  27.281  16.222  1.00 10.49           O  
HETATM 1755  O   HOH A 325      20.769  21.284  19.423  1.00 14.40           O  
HETATM 1756  O   HOH A 326      20.912  23.986  22.619  1.00  7.77           O  
HETATM 1757  O   HOH A 327      15.966  26.464  24.350  1.00  8.46           O  
HETATM 1758  O   HOH A 329       9.696  23.487  29.799  1.00 11.67           O  
HETATM 1759  O   HOH A 330      -0.670  15.465  30.470  1.00 16.02           O  
HETATM 1760  O   HOH A 331       3.144  21.158  32.589  1.00  7.92           O  
HETATM 1761  O   HOH A 332      -0.479  24.036  32.984  1.00  8.86           O  
HETATM 1762  O   HOH A 338     -12.706  33.525  18.951  1.00  5.56           O  
HETATM 1763  O   HOH A 339     -15.254  32.468  15.328  1.00 13.68           O  
HETATM 1764  O   HOH A 343     -10.755  23.334  24.612  1.00 16.45           O  
HETATM 1765  O   HOH A 344      -7.493  25.565  26.675  1.00 15.66           O  
HETATM 1766  O   HOH A 345     -16.257  30.612  27.398  1.00  6.05           O  
HETATM 1767  O   HOH A 348     -11.273  36.610  10.601  1.00 12.94           O  
HETATM 1768  O   HOH A 349     -11.369  39.237   9.841  1.00 11.17           O  
HETATM 1769  O   HOH A 350      -9.248  40.976  10.154  1.00 27.47           O  
HETATM 1770  O   HOH A 353       1.490  32.451   5.219  1.00  2.49           O  
HETATM 1771  O   HOH A 356      -1.260  41.575   7.494  1.00  9.48           O  
HETATM 1772  O   HOH A 357      -0.724  43.601   5.094  1.00 14.00           O  
HETATM 1773  O   HOH A 358       2.736  48.332  11.870  1.00 19.43           O  
HETATM 1774  O   HOH A 359       1.113  43.557  26.722  1.00 24.85           O  
HETATM 1775  O   HOH A 360      -3.468  41.880  28.113  1.00 15.06           O  
HETATM 1776  O   HOH A 361      -5.367  36.027  31.271  1.00 14.87           O  
HETATM 1777  O   HOH A 362      17.547  37.999  31.491  1.00 20.96           O  
HETATM 1778  O   HOH A 363      20.375  34.974  29.551  1.00  7.05           O  
HETATM 1779  O   HOH A 366       0.325  32.769  31.393  1.00  6.75           O  
HETATM 1780  O   HOH A 367      -1.036  35.129  31.299  1.00  4.24           O  
HETATM 1781  O   HOH A 368     -13.388  37.544  24.881  1.00 19.11           O  
HETATM 1782  O   HOH A 369      -3.349  34.957  29.765  1.00  8.04           O  
HETATM 1783  O   HOH A 370       2.101  32.601  29.504  1.00  9.27           O  
HETATM 1784  O   HOH A 371      -0.306  30.053  18.445  1.00  2.02           O  
HETATM 1785  O   HOH A 372      -1.446  17.633  18.962  1.00  8.86           O  
HETATM 1786  O   HOH A 373       5.528  17.249  20.434  1.00 23.95           O  
HETATM 1787  O   HOH A 376     -12.086  19.468  10.906  1.00 11.84           O  
HETATM 1788  O   HOH A 379      21.039  18.181  -7.732  1.00 20.99           O  
HETATM 1789  O   HOH A 380      21.501  27.396  -3.545  1.00 13.57           O  
HETATM 1790  O   HOH A 381      11.117  43.748   6.953  1.00 10.85           O  
HETATM 1791  O   HOH A 383      17.006  40.300  11.593  1.00  8.29           O  
HETATM 1792  O   HOH A 385      18.299  36.301  18.609  1.00 10.14           O  
HETATM 1793  O   HOH A 386      13.211  40.790  19.043  1.00 15.34           O  
HETATM 1794  O   HOH A 388      -4.062  42.667  23.330  1.00 13.95           O  
HETATM 1795  O   HOH A 390      27.201  30.508  24.604  1.00 22.09           O  
HETATM 1796  O   HOH A 393      14.103  20.663  15.295  1.00  8.17           O  
HETATM 1797  O   HOH A 395      21.816  28.149   0.749  1.00 13.04           O  
HETATM 1798  O   HOH A 396      21.996  34.505   2.652  1.00 11.76           O  
HETATM 1799  O   HOH A 398     -16.853  32.382  10.007  1.00 17.69           O  
HETATM 1800  O   HOH A 400      -8.427  28.152  27.504  1.00 19.79           O  
HETATM 1801  O   HOH A 402      17.987  28.933  31.122  1.00 20.17           O  
HETATM 1802  O   HOH A 404      -0.349  15.819  22.404  1.00 11.03           O  
HETATM 1803  O   HOH A 406       9.833  43.314  29.395  1.00 15.40           O  
HETATM 1804  O   HOH A 407     -10.332  10.859  28.772  1.00 24.90           O  
HETATM 1805  O   HOH A 412      -0.212  35.465  11.900  1.00  8.92           O  
HETATM 1806  O   HOH A 416      20.112  29.693 -10.062  1.00 27.88           O  
HETATM 1807  O   HOH A 417      22.264  21.131  -2.963  1.00 30.09           O  
HETATM 1808  O   HOH A 418      15.938  10.711  10.685  1.00 41.28           O  
HETATM 1809  O   HOH A 421       6.183  25.890   1.583  1.00  4.68           O  
HETATM 1810  O   HOH A 423       8.680  47.239  11.890  1.00 19.63           O  
HETATM 1811  O   HOH A 425      16.281  22.110  23.603  1.00 26.52           O  
HETATM 1812  O   HOH A 426      -0.396  32.769  12.428  1.00  7.02           O  
HETATM 1813  O   HOH A 427     -20.219  31.105  19.654  1.00 30.14           O  
HETATM 1814  O   HOH A 429      -2.522  20.376  14.211  1.00 17.70           O  
HETATM 1815  O   HOH A 430      19.874  36.285   2.789  1.00 10.75           O  
HETATM 1816  O   HOH A 433      -3.358  23.140  32.178  1.00 17.16           O  
HETATM 1817  O   HOH A 434      -0.101  42.372  29.149  1.00 15.36           O  
HETATM 1818  O   HOH A 436      27.378  33.327  14.677  1.00 51.82           O  
HETATM 1819  O   HOH A 438      -9.901  42.780  22.376  1.00 17.69           O  
HETATM 1820  O   HOH A 440      23.391  29.605  18.875  1.00  6.05           O  
HETATM 1821  O   HOH A 441       3.062  24.450  -2.323  1.00  6.84           O  
HETATM 1822  O   HOH A 444       2.796  21.594  13.773  1.00 10.78           O  
HETATM 1823  O   HOH A 446     -15.058  40.215   9.542  1.00  9.39           O  
HETATM 1824  O   HOH A 447       4.250  16.517  28.645  1.00 28.41           O  
HETATM 1825  O   HOH A 449       7.585  50.695   6.769  1.00 57.50           O  
HETATM 1826  O   HOH A 453       8.797  10.838  20.360  1.00 27.00           O  
HETATM 1827  O   HOH A 457      22.643  21.221  17.063  1.00  9.79           O  
HETATM 1828  O   HOH A 460       7.555  42.035  29.357  1.00 16.07           O  
HETATM 1829  O   HOH A 463     -12.132  39.812  21.831  1.00 14.30           O  
HETATM 1830  O   HOH A 466      20.575  23.777   0.140  1.00 10.22           O  
HETATM 1831  O   HOH A 470      13.153  20.960  -5.384  1.00 22.22           O  
HETATM 1832  O   HOH A 472      19.743  21.402  -6.877  1.00 23.86           O  
HETATM 1833  O   HOH A 474      18.369  27.451 -13.758  1.00 18.82           O  
HETATM 1834  O   HOH A 477       4.017  26.050  -0.164  1.00  9.82           O  
HETATM 1835  O   HOH A 481      22.623  23.918  24.632  1.00 25.10           O  
HETATM 1836  O   HOH A 486      -7.491  12.512  22.022  1.00 32.52           O  
HETATM 1837  O   HOH A 492       1.156  32.892  34.018  0.50  2.00           O  
HETATM 1838  O   HOH A 493      -7.140  30.952  28.057  1.00 15.94           O  
HETATM 1839  O   HOH A 496     -15.909  31.954  20.135  1.00 21.71           O  
HETATM 1840  O   HOH A 497     -13.159  37.294  21.933  1.00 35.33           O  
HETATM 1841  O   HOH A 498     -10.348  37.147  18.558  1.00 26.23           O  
HETATM 1842  O   HOH A 499       0.652  38.888  32.248  1.00  7.68           O  
HETATM 1843  O   HOH A 500      -3.694  32.188  30.279  1.00  4.20           O  
HETATM 1844  O   HOH A 504       6.560  40.770  31.562  1.00 15.16           O  
HETATM 1845  O   HOH A 505       3.100  39.304  33.484  1.00 19.30           O  
HETATM 1846  O   HOH A 506       3.749  32.274  34.733  1.00 14.62           O  
HETATM 1847  O   HOH A 507      -0.946  36.909  33.537  1.00 13.52           O  
HETATM 1848  O   HOH A 511      -8.146  44.070  10.321  1.00 27.01           O  
HETATM 1849  O   HOH A 512      28.166  20.712  14.844  1.00 23.55           O  
HETATM 1850  O   HOH A 513      -2.025  43.396   9.852  1.00 10.64           O  
HETATM 1851  O   HOH A 514       7.367  46.338  14.128  1.00 24.41           O  
HETATM 1852  O   HOH A 516      -9.623  39.572  20.492  1.00  8.87           O  
HETATM 1853  O   HOH A 518     -11.933  38.849  27.949  1.00 30.12           O  
HETATM 1854  O   HOH A 521      -2.371  46.216   8.677  1.00 18.76           O  
HETATM 1855  O   HOH A 522      -0.789  47.961  10.150  1.00 30.99           O  
HETATM 1856  O   HOH A 523       7.648  43.802  13.331  1.00  4.94           O  
HETATM 1857  O   HOH A 524      10.227  44.888  14.639  1.00 38.75           O  
HETATM 1858  O   HOH A 526       7.464  47.253   7.090  1.00 21.69           O  
HETATM 1859  O   HOH A 530      20.071  20.843   3.684  1.00 11.70           O  
HETATM 1860  O   HOH A 531      17.685  18.349   1.636  1.00 15.96           O  
HETATM 1861  O   HOH A 532      15.372  18.604   0.341  1.00 10.39           O  
HETATM 1862  O   HOH A 533      21.261  21.258   1.073  1.00 19.42           O  
HETATM 1863  O   HOH A 534      21.012  18.383   4.025  1.00 26.60           O  
HETATM 1864  O   HOH A 535      17.031  42.189   5.058  1.00 21.84           O  
HETATM 1865  O   HOH A 536      12.430  14.720  -3.243  1.00 21.82           O  
HETATM 1866  O   HOH A 538      14.406  15.042  -8.602  1.00 21.22           O  
HETATM 1867  O   HOH A 543      17.385  29.517 -12.307  1.00 18.73           O  
HETATM 1868  O   HOH A 544      17.620  29.888  -9.581  1.00 11.84           O  
HETATM 1869  O   HOH A 546      21.032  30.703  -0.133  1.00 11.30           O  
HETATM 1870  O   HOH A 547      21.900  30.470  -2.709  1.00 25.93           O  
HETATM 1871  O   HOH A 548      15.016  40.667  -1.308  1.00 20.78           O  
HETATM 1872  O   HOH A 551      21.417  26.573   2.972  1.00 16.39           O  
HETATM 1873  O   HOH A 559      -0.973  22.346   3.077  1.00 45.99           O  
HETATM 1874  O   HOH A 560      19.081  22.273  23.631  1.00 36.21           O  
HETATM 1875  O   HOH A 561      20.785  37.493  17.750  1.00 24.57           O  
HETATM 1876  O   HOH A 568      26.283  32.736  20.454  1.00 32.75           O  
HETATM 1877  O   HOH A 569      23.830  39.488  19.847  1.00 31.28           O  
HETATM 1878  O   HOH A 571      24.174  35.862  20.903  1.00 25.98           O  
HETATM 1879  O   HOH A 574      -2.810  10.688  25.564  1.00 31.82           O  
HETATM 1880  O   HOH A 578     -13.247  17.953  20.246  1.00 50.26           O  
HETATM 1881  O   HOH A 580      -7.736  21.011  28.070  1.00 12.00           O  
HETATM 1882  O   HOH A 581      -6.966  14.772  36.363  1.00 18.66           O  
HETATM 1883  O   HOH A 586       3.921  19.016  16.797  1.00  9.96           O  
HETATM 1884  O   HOH A 587       3.074  19.144  29.470  1.00 14.46           O  
HETATM 1885  O   HOH A 589      11.581  19.971  31.593  1.00 32.35           O  
HETATM 1886  O   HOH A 590      13.561  26.526  35.062  1.00 17.40           O  
HETATM 1887  O   HOH A 595      -4.727  25.277  27.634  1.00 10.62           O  
HETATM 1888  O   HOH A 596     -12.165  31.709  26.262  1.00  7.69           O  
HETATM 1889  O   HOH A 597     -10.827  29.864  27.654  1.00  9.19           O  
HETATM 1890  O   HOH A 598     -10.404  33.801  27.062  1.00  4.70           O  
HETATM 1891  O   HOH A 600     -15.052  18.836  17.629  1.00 10.22           O  
HETATM 1892  O   HOH A 602     -19.568  22.299  21.852  1.00 24.11           O  
HETATM 1893  O   HOH A 604     -18.006  32.268  21.632  1.00 20.10           O  
HETATM 1894  O   HOH A 607      -9.327  41.818  19.040  1.00 16.89           O  
HETATM 1895  O   HOH A 610      15.459  36.702  32.640  1.00 16.10           O  
HETATM 1896  O   HOH A 611      -6.149  40.713   9.083  1.00 24.62           O  
HETATM 1897  O   HOH A 612     -12.778  38.904  18.038  1.00  4.97           O  
HETATM 1898  O   HOH A 614      23.062  18.284  20.793  1.00 17.42           O  
HETATM 1899  O   HOH A 615       8.108  19.574  -4.545  1.00 19.22           O  
HETATM 1900  O   HOH A 616       5.604  20.797   3.753  1.00 24.59           O  
HETATM 1901  O   HOH A 622      12.016  16.601  -7.980  1.00 34.21           O  
HETATM 1902  O   HOH A 624      21.188  28.049  -8.125  1.00 16.48           O  
HETATM 1903  O   HOH A 626      19.922  35.735  -7.375  1.00 18.09           O  
HETATM 1904  O   HOH A 629      28.708  34.295   8.723  1.00 67.95           O  
HETATM 1905  O   HOH A 652       1.890  31.287  11.268  1.00  6.98           O  
HETATM 1906  O   HOH A 653      20.066  19.221  -2.645  1.00 16.29           O  
HETATM 1907  O   HOH A 655       3.176  28.723  -7.162  1.00  2.78           O  
HETATM 1908  O   HOH A 656      17.084  40.347  16.196  1.00 26.53           O  
HETATM 1909  O   HOH A 661       2.774  45.949  -0.297  1.00 15.60           O  
HETATM 1910  O   HOH A 663      12.841  35.382  -9.045  1.00 25.04           O  
HETATM 1911  O   HOH A 664      21.197  14.317  18.776  1.00 16.09           O  
HETATM 1912  O   HOH A 666      -5.366   9.623  28.419  1.00 29.39           O  
HETATM 1913  O   HOH A 671      -7.848  44.326  18.579  1.00 29.84           O  
HETATM 1914  O   HOH A 674     -11.597  42.669  28.120  1.00 28.50           O  
HETATM 1915  O   HOH A 675      25.028  34.259   5.803  1.00 25.78           O  
HETATM 1916  O   HOH A 676     -14.536  35.583  19.541  1.00 12.95           O  
HETATM 1917  O   HOH A 679       8.708  41.547  -0.189  1.00 23.34           O  
HETATM 1918  O   HOH A 684       7.133  21.120  33.289  1.00 21.53           O  
HETATM 1919  O   HOH A 685       5.510  14.406  26.896  1.00 21.06           O  
HETATM 1920  O   HOH A 688       0.000  43.983   0.000  0.50  4.17           O  
HETATM 1921  O   HOH A 689      -8.807  32.871  29.112  0.50  2.00           O  
HETATM 1922  O   HOH A 691      11.399   8.954   0.362  1.00 31.05           O  
HETATM 1923  O   HOH A 692      -9.011  15.600  29.579  0.50 21.92           O  
HETATM 1924  O   HOH A 693      14.197  17.726  24.972  1.00 11.90           O  
HETATM 1925  O   HOH A 694       8.410  13.956  20.971  1.00 18.89           O  
HETATM 1926  O   HOH A 700      -8.387  14.700  20.373  1.00 18.08           O  
HETATM 1927  O   HOH A 703     -12.036  41.608  18.159  1.00 14.39           O  
HETATM 1928  O   HOH A 706      -8.523  41.114   7.394  1.00 34.65           O  
HETATM 1929  O   HOH A 707      -7.118  45.432  29.424  1.00 32.99           O  
HETATM 1930  O   HOH A 709       3.654  16.560  14.614  1.00 19.76           O  
HETATM 1931  O   HOH A 710       7.355  13.328  11.152  1.00 33.09           O  
HETATM 1932  O   HOH A 711       8.948  13.569   9.079  1.00 32.44           O  
HETATM 1933  O   HOH A 712       7.425  13.801  14.282  1.00 18.82           O  
HETATM 1934  O   HOH A 713       8.701  11.690  13.304  1.00 33.89           O  
HETATM 1935  O   HOH A 714       5.385  18.660  14.408  1.00 18.28           O  
HETATM 1936  O   HOH A 716      -0.716  25.409  13.657  1.00 12.98           O  
HETATM 1937  O   HOH A 717      -0.718  22.191  15.643  1.00 15.79           O  
HETATM 1938  O   HOH A 719     -10.983  21.525  22.103  1.00  9.09           O  
HETATM 1939  O   HOH A 720     -11.805  20.397  19.525  1.00 10.54           O  
HETATM 1940  O   HOH A 722      -5.645  22.231  28.024  1.00 12.51           O  
HETATM 1941  O   HOH A 723      20.201  14.820  16.099  1.00 12.42           O  
HETATM 1942  O   HOH A 724      26.435  34.728  22.329  1.00 16.75           O  
HETATM 1943  O   HOH A 726       1.465  16.385  28.242  1.00 19.37           O  
HETATM 1944  O   HOH A 728      -2.241  24.749  16.371  1.00 14.03           O  
HETATM 1945  O   HOH A 729      26.582  31.233   8.724  1.00 17.13           O  
HETATM 1946  O   HOH A 730     -12.604  24.404  24.075  1.00 16.15           O  
HETATM 1947  O   HOH A 731       9.522  17.812  20.857  1.00 14.37           O  
HETATM 1948  O   HOH A 732      -0.624  13.823  24.591  1.00 16.77           O  
HETATM 1949  O   HOH A 734      20.043  15.542  21.401  1.00 21.79           O  
HETATM 1950  O   HOH A 736       2.065  24.203   1.525  1.00 13.38           O  
HETATM 1951  O   HOH A 737       1.740  21.717   3.675  1.00 20.61           O  
HETATM 1952  O   HOH A 738     -16.535  20.663  19.131  1.00 32.90           O  
HETATM 1953  O   HOH A 740      -2.996  16.247  36.209  1.00 37.80           O  
HETATM 1954  O   HOH A 742     -18.049  35.405  23.048  1.00 21.54           O  
HETATM 1955  O   HOH A 744       4.365  27.299  38.566  1.00 28.29           O  
HETATM 1956  O   HOH A 746      -3.575  20.706  33.392  1.00 23.10           O  
HETATM 1957  O   HOH A 748       8.533  14.259  17.597  1.00 24.23           O  
CONECT  124 1694                                                                
CONECT  393 1694                                                                
CONECT  864 1694                                                                
CONECT 1694  124  393  864 1711                                                 
CONECT 1694 1713 1822                                                           
CONECT 1695 1696 1697 1698                                                      
CONECT 1696 1695                                                                
CONECT 1697 1695                                                                
CONECT 1698 1695 1699                                                           
CONECT 1699 1698 1700                                                           
CONECT 1700 1699 1701                                                           
CONECT 1701 1700 1702                                                           
CONECT 1702 1701 1703                                                           
CONECT 1703 1702 1704 1706                                                      
CONECT 1704 1703 1705 1707                                                      
CONECT 1705 1704                                                                
CONECT 1706 1703                                                                
CONECT 1707 1704                                                                
CONECT 1708 1709 1710 1711 1715                                                 
CONECT 1709 1708                                                                
CONECT 1710 1708                                                                
CONECT 1711 1694 1708                                                           
CONECT 1712 1713 1714 1715 1719                                                 
CONECT 1713 1694 1712                                                           
CONECT 1714 1712                                                                
CONECT 1715 1708 1712                                                           
CONECT 1716 1717 1718 1719 1720                                                 
CONECT 1717 1716                                                                
CONECT 1718 1716                                                                
CONECT 1719 1712 1716                                                           
CONECT 1720 1716 1721                                                           
CONECT 1721 1720 1722                                                           
CONECT 1722 1721 1723 1724                                                      
CONECT 1723 1722 1728                                                           
CONECT 1724 1722 1725 1726                                                      
CONECT 1725 1724                                                                
CONECT 1726 1724 1727 1728                                                      
CONECT 1727 1726                                                                
CONECT 1728 1723 1726 1729                                                      
CONECT 1729 1728 1730 1738                                                      
CONECT 1730 1729 1731                                                           
CONECT 1731 1730 1732                                                           
CONECT 1732 1731 1733 1738                                                      
CONECT 1733 1732 1734 1735                                                      
CONECT 1734 1733                                                                
CONECT 1735 1733 1736                                                           
CONECT 1736 1735 1737                                                           
CONECT 1737 1736 1738                                                           
CONECT 1738 1729 1732 1737                                                      
CONECT 1822 1694                                                                
MASTER      267    0    3   10   10    0   13    6 1956    1   50   18          
END                                                                             
