HEADER    LIGASE                                  31-MAR-98   1DAK              
TITLE     DETHIOBIOTIN SYNTHETASE FROM ESCHERICHIA COLI, COMPLEX REACTION       
TITLE    2 INTERMEDIATE ADP AND MIXED ANHYDRIDE                                 
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    PHOSHPORYL TRANSFER, BIOTIN BIOSYNTHESIS, LIGASE, KINETIC             
KEYWDS   2 CRYSTALLOGRAPHY                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.KAECK,K.J.GIBSON,Y.LINDQVIST,G.SCHNEIDER                            
REVDAT   4   09-AUG-23 1DAK    1       REMARK LINK                              
REVDAT   3   13-JUL-11 1DAK    1       VERSN                                    
REVDAT   2   24-FEB-09 1DAK    1       VERSN                                    
REVDAT   1   06-APR-99 1DAK    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.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 29418                          
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 + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1505                            
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          : 54                                      
REMARK   3   SOLVENT ATOMS            : 216                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.60                          
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.006 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.020 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.021 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.017 ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.081 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.172 ; 0.300               
REMARK   3    MULTIPLE TORSION                (A) : 0.258 ; 0.300               
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 3.100 ; 7.000               
REMARK   3    STAGGERED                 (DEGREES) : 15.900; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.862 ; 2.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.335 ; 3.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.227 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 1.949 ; 3.000                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1DAK 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_1000172710.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : OCT-97                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID09                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.7606                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : PRINCETON 2K                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 86120                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.43000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER           
REMARK 200 SOFTWARE USED: CCP4                                                  
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   (%): 42.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.5                                   
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       36.34000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.09500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       36.34000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.09500            
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: 6950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -106.0 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 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     -176.17   -170.56                                   
REMARK 500    ASN A 209       74.49     28.62                                   
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  82.1                                              
REMARK 620 3 GLU A 115   OE2  79.3  91.4                                        
REMARK 620 4 HOH A 444   O    94.8  81.2 171.1                                  
REMARK 620 5 DPU A 801   O2B 161.3  89.6  84.2 100.5                            
REMARK 620 6 ADP A 802   O3B  92.6 160.8 105.8  80.9 100.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 902  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 429   O                                                      
REMARK 620 2 HOH A 444   O    88.1                                              
REMARK 620 3 HOH A 559   O    82.5 170.6                                        
REMARK 620 4 HOH A 754   O    81.8  95.6  84.2                                  
REMARK 620 5 DPU A 801   O3B 167.7  99.1  90.3  87.6                            
REMARK 620 6 ADP A 802   O2B  94.4  84.9  94.6 176.1  96.1                      
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 PO4 A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DPU A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 802                 
DBREF  1DAK 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    PO4  A 803       5                                                       
HET     MG  A 901       1                                                       
HET     MG  A 902       1                                                       
HET    DPU  A 801      20                                                       
HET    ADP  A 802      27                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     DPU MIXED CARBAMIC PHOSPHORIC ACID ANHYDRIDE OF 7,8-                 
HETNAM   2 DPU  DIAMINONONANIC ACID                                             
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
FORMUL   2  PO4    O4 P 3-                                                      
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   5  DPU    C10 H21 N2 O7 P                                              
FORMUL   6  ADP    C10 H15 N5 O10 P2                                            
FORMUL   7  HOH   *216(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  2.26  
LINK         OD2 ASP A  54                MG    MG A 901     1555   1555  2.14  
LINK         OE2 GLU A 115                MG    MG A 901     1555   1555  2.16  
LINK         O   HOH A 429                MG    MG A 902     1555   1555  2.17  
LINK         O   HOH A 444                MG    MG A 901     1555   1555  2.26  
LINK         O   HOH A 444                MG    MG A 902     1555   1555  2.06  
LINK         O   HOH A 559                MG    MG A 902     1555   1555  2.26  
LINK         O   HOH A 754                MG    MG A 902     1555   1555  2.10  
LINK         O2B DPU A 801                MG    MG A 901     1555   1555  2.19  
LINK         O3B DPU A 801                MG    MG A 902     1555   1555  2.11  
LINK         O3B ADP A 802                MG    MG A 901     1555   1555  2.01  
LINK         O2B ADP A 802                MG    MG A 902     1555   1555  2.10  
SITE     1 AC1  8 LYS A 148  LEU A 149  ARG A 183  HIS A 184                    
SITE     2 AC1  8 HOH A 767  HOH A 768  HOH A 769  HOH A 792                    
SITE     1 AC2  7 THR A  16  ASP A  54  GLU A 115  HOH A 444                    
SITE     2 AC2  7 DPU A 801  ADP A 802   MG A 902                               
SITE     1 AC3  7 HOH A 429  HOH A 444  HOH A 559  HOH A 754                    
SITE     2 AC3  7 DPU A 801  ADP A 802   MG A 901                               
SITE     1 AC4 23 THR A  11  LYS A  15  LYS A  37  ALA A  40                    
SITE     2 AC4 23 SER A  41  ASP A  54  PRO A  79  GLU A 115                    
SITE     3 AC4 23 ALA A 117  GLY A 118  GLY A 150  CYS A 151                    
SITE     4 AC4 23 ILE A 152  ASN A 153  TYR A 187  HOH A 559                    
SITE     5 AC4 23 HOH A 655  HOH A 717  HOH A 754  HOH A 755                    
SITE     6 AC4 23 ADP A 802   MG A 901   MG A 902                               
SITE     1 AC5 22 GLU A  12  VAL A  13  GLY A  14  LYS A  15                    
SITE     2 AC5 22 THR A  16  VAL A  17  GLU A 115  ASN A 175                    
SITE     3 AC5 22 ASP A 176  PRO A 204  TRP A 205  LEU A 206                    
SITE     4 AC5 22 PRO A 210  GLU A 211  HOH A 429  HOH A 444                    
SITE     5 AC5 22 HOH A 711  HOH A 714  HOH A 756  DPU A 801                    
SITE     6 AC5 22  MG A 901   MG A 902                                          
CRYST1   72.680   48.190   61.070  90.00 106.58  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      0.013759  0.000000  0.004096        0.00000                         
SCALE2      0.000000  0.020751  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017085        0.00000                         
ATOM      1  N   SER A   1      13.566  42.748  26.122  1.00 28.54           N  
ATOM      2  CA  SER A   1      14.078  41.417  25.699  1.00 27.64           C  
ATOM      3  C   SER A   1      13.659  41.071  24.272  1.00 26.25           C  
ATOM      4  O   SER A   1      12.705  41.651  23.756  1.00 26.43           O  
ATOM      5  CB  SER A   1      13.586  40.331  26.650  1.00 28.76           C  
ATOM      6  OG  SER A   1      12.170  40.249  26.578  1.00 29.99           O  
ATOM      7  N   LYS A   2      14.357  40.103  23.681  1.00 23.74           N  
ATOM      8  CA  LYS A   2      14.122  39.694  22.305  1.00 21.20           C  
ATOM      9  C   LYS A   2      12.880  38.830  22.145  1.00 18.30           C  
ATOM     10  O   LYS A   2      12.615  37.954  22.962  1.00 16.42           O  
ATOM     11  CB  LYS A   2      15.324  38.919  21.754  1.00 22.98           C  
ATOM     12  CG  LYS A   2      16.659  39.608  22.044  1.00 24.74           C  
ATOM     13  CD  LYS A   2      17.602  39.418  20.865  1.00 25.95           C  
ATOM     14  CE  LYS A   2      18.517  40.621  20.686  1.00 27.21           C  
ATOM     15  NZ  LYS A   2      19.313  40.489  19.431  1.00 28.38           N  
ATOM     16  N   ARG A   3      12.100  39.129  21.107  1.00 16.69           N  
ATOM     17  CA  ARG A   3      10.856  38.416  20.831  1.00 15.71           C  
ATOM     18  C   ARG A   3      10.691  38.239  19.322  1.00 13.55           C  
ATOM     19  O   ARG A   3      11.080  39.136  18.573  1.00 12.51           O  
ATOM     20  CB  ARG A   3       9.618  39.138  21.336  1.00 18.74           C  
ATOM     21  CG  ARG A   3       9.643  40.179  22.417  1.00 22.73           C  
ATOM     22  CD  ARG A   3       9.153  41.536  21.921  1.00 24.22           C  
ATOM     23  NE  ARG A   3       7.727  41.706  22.160  1.00 26.17           N  
ATOM     24  CZ  ARG A   3       6.895  42.438  21.433  1.00 26.91           C  
ATOM     25  NH1 ARG A   3       7.322  43.098  20.361  1.00 27.16           N  
ATOM     26  NH2 ARG A   3       5.609  42.510  21.764  1.00 27.26           N  
ATOM     27  N   TYR A   4      10.242  37.076  18.854  1.00 10.96           N  
ATOM     28  CA  TYR A   4      10.087  36.825  17.425  1.00  9.72           C  
ATOM     29  C   TYR A   4       8.787  36.050  17.200  1.00  8.54           C  
ATOM     30  O   TYR A   4       8.462  35.197  18.027  1.00 10.83           O  
ATOM     31  CB  TYR A   4      11.234  36.005  16.800  1.00 10.31           C  
ATOM     32  CG  TYR A   4      12.597  36.658  16.979  1.00 10.93           C  
ATOM     33  CD1 TYR A   4      13.021  37.672  16.136  1.00 10.95           C  
ATOM     34  CD2 TYR A   4      13.389  36.311  18.070  1.00 11.46           C  
ATOM     35  CE1 TYR A   4      14.246  38.290  16.339  1.00 12.01           C  
ATOM     36  CE2 TYR A   4      14.606  36.940  18.287  1.00 13.04           C  
ATOM     37  CZ  TYR A   4      15.018  37.924  17.418  1.00 12.85           C  
ATOM     38  OH  TYR A   4      16.232  38.550  17.634  1.00 14.52           O  
ATOM     39  N   PHE A   5       8.091  36.345  16.113  1.00  7.33           N  
ATOM     40  CA  PHE A   5       6.896  35.566  15.768  1.00  6.91           C  
ATOM     41  C   PHE A   5       7.259  34.666  14.582  1.00  6.90           C  
ATOM     42  O   PHE A   5       7.752  35.181  13.581  1.00  7.64           O  
ATOM     43  CB  PHE A   5       5.718  36.459  15.391  1.00  6.96           C  
ATOM     44  CG  PHE A   5       4.448  35.705  15.095  1.00  7.05           C  
ATOM     45  CD1 PHE A   5       3.613  35.272  16.111  1.00  7.05           C  
ATOM     46  CD2 PHE A   5       4.105  35.424  13.777  1.00  7.98           C  
ATOM     47  CE1 PHE A   5       2.453  34.583  15.821  1.00  7.84           C  
ATOM     48  CE2 PHE A   5       2.949  34.731  13.484  1.00  7.92           C  
ATOM     49  CZ  PHE A   5       2.109  34.323  14.508  1.00  7.84           C  
ATOM     50  N   VAL A   6       7.034  33.372  14.722  1.00  6.48           N  
ATOM     51  CA  VAL A   6       7.318  32.435  13.636  1.00  6.93           C  
ATOM     52  C   VAL A   6       6.052  32.079  12.868  1.00  7.58           C  
ATOM     53  O   VAL A   6       5.089  31.530  13.394  1.00  7.51           O  
ATOM     54  CB  VAL A   6       7.993  31.163  14.176  1.00  6.72           C  
ATOM     55  CG1 VAL A   6       8.177  30.117  13.073  1.00  6.97           C  
ATOM     56  CG2 VAL A   6       9.339  31.500  14.813  1.00  7.65           C  
ATOM     57  N   THR A   7       6.068  32.412  11.581  1.00  6.00           N  
ATOM     58  CA  THR A   7       4.975  32.054  10.675  1.00  7.40           C  
ATOM     59  C   THR A   7       5.522  31.116   9.607  1.00  6.98           C  
ATOM     60  O   THR A   7       6.711  30.764   9.620  1.00  6.57           O  
ATOM     61  CB  THR A   7       4.302  33.295  10.083  1.00  7.43           C  
ATOM     62  OG1 THR A   7       3.052  32.890   9.482  1.00  7.23           O  
ATOM     63  CG2 THR A   7       5.170  33.958   9.034  1.00  8.56           C  
ATOM     64  N   GLY A   8       4.648  30.602   8.759  1.00  7.27           N  
ATOM     65  CA  GLY A   8       5.030  29.660   7.721  1.00  6.84           C  
ATOM     66  C   GLY A   8       4.293  29.961   6.418  1.00  7.37           C  
ATOM     67  O   GLY A   8       3.293  30.657   6.370  1.00  7.15           O  
ATOM     68  N   THR A   9       4.785  29.322   5.354  1.00  6.79           N  
ATOM     69  CA  THR A   9       4.170  29.453   4.033  1.00  8.19           C  
ATOM     70  C   THR A   9       2.822  28.747   3.984  1.00  8.37           C  
ATOM     71  O   THR A   9       2.014  28.991   3.084  1.00  7.94           O  
ATOM     72  CB  THR A   9       5.093  28.909   2.936  1.00  8.36           C  
ATOM     73  OG1 THR A   9       5.668  27.682   3.390  1.00  7.98           O  
ATOM     74  CG2 THR A   9       6.239  29.878   2.661  1.00  8.12           C  
ATOM     75  N   ASP A  10       2.552  27.878   4.944  1.00  8.92           N  
ATOM     76  CA  ASP A  10       1.285  27.171   5.078  1.00  9.57           C  
ATOM     77  C   ASP A  10       1.294  26.456   6.429  1.00 10.09           C  
ATOM     78  O   ASP A  10       2.248  26.597   7.200  1.00 10.71           O  
ATOM     79  CB  ASP A  10       1.153  26.173   3.933  1.00  9.77           C  
ATOM     80  CG  ASP A  10      -0.218  25.561   3.727  1.00  9.99           C  
ATOM     81  OD1 ASP A  10      -1.161  25.896   4.472  1.00 11.61           O  
ATOM     82  OD2 ASP A  10      -0.360  24.723   2.824  1.00 11.07           O  
ATOM     83  N   THR A  11       0.248  25.683   6.711  1.00  9.99           N  
ATOM     84  CA  THR A  11       0.310  24.770   7.861  1.00 10.44           C  
ATOM     85  C   THR A  11       1.084  23.565   7.325  1.00 11.10           C  
ATOM     86  O   THR A  11       1.224  23.382   6.115  1.00 10.84           O  
ATOM     87  CB  THR A  11      -1.070  24.374   8.390  1.00 11.13           C  
ATOM     88  OG1 THR A  11      -0.949  23.600   9.599  1.00 11.76           O  
ATOM     89  CG2 THR A  11      -1.834  23.538   7.370  1.00 10.94           C  
ATOM     90  N   GLU A  12       1.682  22.747   8.160  1.00 11.38           N  
ATOM     91  CA  GLU A  12       2.428  21.551   7.812  1.00 12.65           C  
ATOM     92  C   GLU A  12       3.655  21.782   6.951  1.00 12.48           C  
ATOM     93  O   GLU A  12       3.924  20.991   6.052  1.00 12.84           O  
ATOM     94  CB  GLU A  12       1.489  20.521   7.164  1.00 14.94           C  
ATOM     95  CG  GLU A  12       1.980  19.088   7.314  1.00 18.53           C  
ATOM     96  CD  GLU A  12       1.669  18.460   8.649  1.00 21.48           C  
ATOM     97  OE1 GLU A  12       0.825  18.981   9.405  1.00 23.26           O  
ATOM     98  OE2 GLU A  12       2.262  17.401   8.964  1.00 23.63           O  
ATOM     99  N   VAL A  13       4.438  22.821   7.205  1.00 11.58           N  
ATOM    100  CA  VAL A  13       5.636  23.150   6.456  1.00 11.52           C  
ATOM    101  C   VAL A  13       6.917  23.127   7.288  1.00 12.49           C  
ATOM    102  O   VAL A  13       8.017  23.225   6.737  1.00 12.61           O  
ATOM    103  CB  VAL A  13       5.555  24.528   5.775  1.00 11.14           C  
ATOM    104  CG1 VAL A  13       4.417  24.572   4.768  1.00 10.55           C  
ATOM    105  CG2 VAL A  13       5.426  25.678   6.762  1.00 10.82           C  
ATOM    106  N   GLY A  14       6.801  23.059   8.603  1.00 13.22           N  
ATOM    107  CA  GLY A  14       7.964  23.049   9.477  1.00 13.35           C  
ATOM    108  C   GLY A  14       8.078  24.157  10.487  1.00 13.07           C  
ATOM    109  O   GLY A  14       9.149  24.335  11.094  1.00 13.33           O  
ATOM    110  N   LYS A  15       7.039  24.933  10.783  1.00 10.70           N  
ATOM    111  CA  LYS A  15       7.136  25.995  11.768  1.00 10.63           C  
ATOM    112  C   LYS A  15       7.654  25.421  13.092  1.00  9.66           C  
ATOM    113  O   LYS A  15       8.525  26.008  13.699  1.00  9.58           O  
ATOM    114  CB  LYS A  15       5.843  26.759  12.060  1.00 10.29           C  
ATOM    115  CG  LYS A  15       5.277  27.565  10.902  1.00 11.51           C  
ATOM    116  CD  LYS A  15       4.043  28.352  11.315  1.00 10.42           C  
ATOM    117  CE  LYS A  15       2.902  27.466  11.789  1.00 10.77           C  
ATOM    118  NZ  LYS A  15       2.288  26.712  10.657  1.00 11.31           N  
ATOM    119  N   THR A  16       7.099  24.297  13.545  1.00  8.94           N  
ATOM    120  CA  THR A  16       7.424  23.744  14.851  1.00  7.94           C  
ATOM    121  C   THR A  16       8.840  23.193  14.832  1.00  8.05           C  
ATOM    122  O   THR A  16       9.610  23.547  15.725  1.00  8.16           O  
ATOM    123  CB  THR A  16       6.400  22.695  15.317  1.00  9.15           C  
ATOM    124  OG1 THR A  16       5.106  23.344  15.413  1.00  7.78           O  
ATOM    125  CG2 THR A  16       6.742  22.083  16.660  1.00 10.64           C  
ATOM    126  N   VAL A  17       9.209  22.454  13.787  1.00  8.48           N  
ATOM    127  CA  VAL A  17      10.596  21.953  13.745  1.00  7.41           C  
ATOM    128  C   VAL A  17      11.593  23.100  13.703  1.00  7.56           C  
ATOM    129  O   VAL A  17      12.601  23.110  14.434  1.00  8.18           O  
ATOM    130  CB  VAL A  17      10.763  21.018  12.533  1.00  7.72           C  
ATOM    131  CG1 VAL A  17      12.226  20.746  12.214  1.00  8.54           C  
ATOM    132  CG2 VAL A  17      10.041  19.709  12.832  1.00  8.12           C  
ATOM    133  N   ALA A  18      11.347  24.108  12.872  1.00  7.85           N  
ATOM    134  CA  ALA A  18      12.217  25.276  12.785  1.00  8.07           C  
ATOM    135  C   ALA A  18      12.240  26.072  14.085  1.00  8.46           C  
ATOM    136  O   ALA A  18      13.294  26.576  14.483  1.00  8.59           O  
ATOM    137  CB  ALA A  18      11.810  26.176  11.617  1.00  8.20           C  
ATOM    138  N   SER A  19      11.101  26.178  14.772  1.00  8.35           N  
ATOM    139  CA  SER A  19      11.033  26.885  16.041  1.00  7.46           C  
ATOM    140  C   SER A  19      11.879  26.191  17.107  1.00  7.53           C  
ATOM    141  O   SER A  19      12.554  26.881  17.871  1.00  7.96           O  
ATOM    142  CB  SER A  19       9.585  26.959  16.537  1.00  8.12           C  
ATOM    143  OG  SER A  19       8.862  27.875  15.744  1.00  8.13           O  
ATOM    144  N   CYS A  20      11.884  24.858  17.098  1.00  7.79           N  
ATOM    145  CA  CYS A  20      12.723  24.119  18.045  1.00  7.98           C  
ATOM    146  C   CYS A  20      14.190  24.377  17.718  1.00  8.47           C  
ATOM    147  O   CYS A  20      15.014  24.514  18.623  1.00  8.37           O  
ATOM    148  CB  CYS A  20      12.400  22.627  18.040  1.00  9.71           C  
ATOM    149  SG  CYS A  20      10.727  22.242  18.669  1.00 11.51           S  
ATOM    150  N   ALA A  21      14.541  24.437  16.429  1.00  8.17           N  
ATOM    151  CA  ALA A  21      15.932  24.712  16.042  1.00  7.19           C  
ATOM    152  C   ALA A  21      16.353  26.101  16.496  1.00  7.90           C  
ATOM    153  O   ALA A  21      17.437  26.309  17.042  1.00  8.46           O  
ATOM    154  CB  ALA A  21      16.059  24.586  14.526  1.00  7.42           C  
ATOM    155  N   LEU A  22      15.473  27.079  16.311  1.00  6.80           N  
ATOM    156  CA  LEU A  22      15.719  28.451  16.756  1.00  7.12           C  
ATOM    157  C   LEU A  22      15.904  28.505  18.268  1.00  7.83           C  
ATOM    158  O   LEU A  22      16.856  29.139  18.738  1.00  7.02           O  
ATOM    159  CB  LEU A  22      14.565  29.338  16.284  1.00  7.93           C  
ATOM    160  CG  LEU A  22      14.637  29.742  14.802  1.00  8.27           C  
ATOM    161  CD1 LEU A  22      13.248  30.113  14.297  1.00  8.51           C  
ATOM    162  CD2 LEU A  22      15.582  30.909  14.595  1.00  8.44           C  
ATOM    163  N   LEU A  23      15.029  27.850  19.019  1.00  8.03           N  
ATOM    164  CA  LEU A  23      15.144  27.817  20.481  1.00  7.90           C  
ATOM    165  C   LEU A  23      16.451  27.171  20.927  1.00  8.27           C  
ATOM    166  O   LEU A  23      17.116  27.654  21.853  1.00  8.83           O  
ATOM    167  CB  LEU A  23      13.937  27.106  21.091  1.00  8.75           C  
ATOM    168  CG  LEU A  23      12.658  27.949  21.191  1.00  8.27           C  
ATOM    169  CD1 LEU A  23      11.458  27.044  21.433  1.00  9.06           C  
ATOM    170  CD2 LEU A  23      12.795  28.995  22.298  1.00  8.51           C  
ATOM    171  N   GLN A  24      16.833  26.057  20.318  1.00  9.12           N  
ATOM    172  CA  GLN A  24      18.111  25.412  20.634  1.00  8.41           C  
ATOM    173  C   GLN A  24      19.292  26.329  20.356  1.00  9.05           C  
ATOM    174  O   GLN A  24      20.207  26.442  21.184  1.00  8.77           O  
ATOM    175  CB  GLN A  24      18.237  24.118  19.822  1.00  8.96           C  
ATOM    176  CG  GLN A  24      17.285  23.018  20.261  1.00  9.17           C  
ATOM    177  CD  GLN A  24      17.368  21.803  19.366  1.00 10.42           C  
ATOM    178  OE1 GLN A  24      18.416  21.545  18.766  1.00 10.74           O  
ATOM    179  NE2 GLN A  24      16.284  21.040  19.242  1.00 10.71           N  
ATOM    180  N   ALA A  25      19.290  27.036  19.229  1.00  8.53           N  
ATOM    181  CA  ALA A  25      20.366  27.972  18.913  1.00  9.51           C  
ATOM    182  C   ALA A  25      20.438  29.102  19.929  1.00  9.31           C  
ATOM    183  O   ALA A  25      21.530  29.536  20.310  1.00  9.02           O  
ATOM    184  CB  ALA A  25      20.206  28.537  17.505  1.00 10.02           C  
ATOM    185  N   ALA A  26      19.285  29.631  20.354  1.00  9.80           N  
ATOM    186  CA  ALA A  26      19.251  30.706  21.338  1.00  9.06           C  
ATOM    187  C   ALA A  26      19.789  30.236  22.686  1.00  9.71           C  
ATOM    188  O   ALA A  26      20.522  30.986  23.342  1.00  9.59           O  
ATOM    189  CB  ALA A  26      17.832  31.239  21.484  1.00  9.74           C  
ATOM    190  N   LYS A  27      19.446  29.013  23.084  1.00 10.83           N  
ATOM    191  CA  LYS A  27      19.985  28.453  24.322  1.00 10.79           C  
ATOM    192  C   LYS A  27      21.499  28.310  24.212  1.00 11.70           C  
ATOM    193  O   LYS A  27      22.228  28.646  25.151  1.00 11.08           O  
ATOM    194  CB  LYS A  27      19.379  27.092  24.646  1.00 11.75           C  
ATOM    195  CG  LYS A  27      19.957  26.419  25.894  1.00 14.16           C  
ATOM    196  CD  LYS A  27      19.213  25.112  26.134  1.00 15.34           C  
ATOM    197  CE  LYS A  27      19.765  24.355  27.335  1.00 17.78           C  
ATOM    198  NZ  LYS A  27      19.007  23.088  27.540  1.00 19.34           N  
ATOM    199  N   ALA A  28      22.003  27.848  23.074  1.00 11.67           N  
ATOM    200  CA  ALA A  28      23.449  27.712  22.893  1.00 12.28           C  
ATOM    201  C   ALA A  28      24.173  29.046  22.979  1.00 12.63           C  
ATOM    202  O   ALA A  28      25.344  29.130  23.395  1.00 13.79           O  
ATOM    203  CB  ALA A  28      23.742  27.035  21.556  1.00 11.67           C  
ATOM    204  N   ALA A  29      23.523  30.133  22.598  1.00 11.90           N  
ATOM    205  CA  ALA A  29      24.013  31.491  22.654  1.00 11.86           C  
ATOM    206  C   ALA A  29      23.967  32.094  24.054  1.00 12.35           C  
ATOM    207  O   ALA A  29      24.533  33.179  24.240  1.00 13.50           O  
ATOM    208  CB  ALA A  29      23.230  32.375  21.682  1.00 12.72           C  
ATOM    209  N   GLY A  30      23.348  31.434  25.018  1.00 11.91           N  
ATOM    210  CA  GLY A  30      23.305  31.890  26.394  1.00 11.90           C  
ATOM    211  C   GLY A  30      22.028  32.571  26.831  1.00 11.69           C  
ATOM    212  O   GLY A  30      21.999  33.180  27.911  1.00 11.01           O  
ATOM    213  N   TYR A  31      20.993  32.559  25.998  1.00 10.98           N  
ATOM    214  CA  TYR A  31      19.727  33.181  26.369  1.00 10.93           C  
ATOM    215  C   TYR A  31      18.896  32.273  27.277  1.00 11.69           C  
ATOM    216  O   TYR A  31      19.043  31.048  27.321  1.00 12.22           O  
ATOM    217  CB  TYR A  31      18.905  33.478  25.101  1.00 10.64           C  
ATOM    218  CG  TYR A  31      19.408  34.626  24.260  1.00 10.89           C  
ATOM    219  CD1 TYR A  31      19.197  35.951  24.629  1.00 11.19           C  
ATOM    220  CD2 TYR A  31      20.106  34.385  23.081  1.00 11.62           C  
ATOM    221  CE1 TYR A  31      19.658  36.995  23.852  1.00 12.31           C  
ATOM    222  CE2 TYR A  31      20.568  35.429  22.300  1.00 11.71           C  
ATOM    223  CZ  TYR A  31      20.344  36.727  22.690  1.00 12.55           C  
ATOM    224  OH  TYR A  31      20.807  37.771  21.912  1.00 15.66           O  
ATOM    225  N   ARG A  32      17.981  32.913  27.990  1.00 11.66           N  
ATOM    226  CA  ARG A  32      17.012  32.248  28.858  1.00 12.41           C  
ATOM    227  C   ARG A  32      15.734  32.212  27.995  1.00 10.86           C  
ATOM    228  O   ARG A  32      15.184  33.277  27.749  1.00 10.84           O  
ATOM    229  CB  ARG A  32      16.790  33.046  30.130  1.00 14.42           C  
ATOM    230  CG  ARG A  32      17.920  32.939  31.147  1.00 17.49           C  
ATOM    231  CD  ARG A  32      17.792  34.081  32.154  1.00 19.55           C  
ATOM    232  NE  ARG A  32      16.483  34.047  32.815  1.00 22.11           N  
ATOM    233  CZ  ARG A  32      16.174  33.218  33.809  1.00 22.92           C  
ATOM    234  NH1 ARG A  32      17.074  32.352  34.263  1.00 23.64           N  
ATOM    235  NH2 ARG A  32      14.966  33.254  34.356  1.00 23.16           N  
ATOM    236  N   THR A  33      15.498  31.065  27.376  1.00 10.22           N  
ATOM    237  CA  THR A  33      14.491  31.011  26.322  1.00 10.20           C  
ATOM    238  C   THR A  33      13.140  30.460  26.757  1.00  9.83           C  
ATOM    239  O   THR A  33      13.003  29.694  27.702  1.00 10.79           O  
ATOM    240  CB  THR A  33      14.967  30.129  25.139  1.00 10.23           C  
ATOM    241  OG1 THR A  33      15.007  28.778  25.607  1.00 10.15           O  
ATOM    242  CG2 THR A  33      16.323  30.576  24.629  1.00 10.78           C  
ATOM    243  N   ALA A  34      12.142  30.847  25.965  1.00  9.07           N  
ATOM    244  CA  ALA A  34      10.777  30.377  26.148  1.00  9.26           C  
ATOM    245  C   ALA A  34      10.070  30.369  24.784  1.00  8.53           C  
ATOM    246  O   ALA A  34      10.191  31.318  24.017  1.00  8.41           O  
ATOM    247  CB  ALA A  34      10.000  31.279  27.100  1.00  8.79           C  
ATOM    248  N   GLY A  35       9.377  29.262  24.544  1.00  8.63           N  
ATOM    249  CA  GLY A  35       8.549  29.149  23.333  1.00  8.24           C  
ATOM    250  C   GLY A  35       7.103  29.426  23.768  1.00  8.56           C  
ATOM    251  O   GLY A  35       6.725  29.058  24.874  1.00  9.01           O  
ATOM    252  N   TYR A  36       6.333  30.028  22.877  1.00  7.23           N  
ATOM    253  CA  TYR A  36       4.942  30.367  23.184  1.00  7.62           C  
ATOM    254  C   TYR A  36       4.082  29.978  21.988  1.00  8.11           C  
ATOM    255  O   TYR A  36       4.343  30.474  20.885  1.00  8.26           O  
ATOM    256  CB  TYR A  36       4.847  31.864  23.449  1.00  7.19           C  
ATOM    257  CG  TYR A  36       3.531  32.430  23.945  1.00  6.86           C  
ATOM    258  CD1 TYR A  36       2.811  31.789  24.946  1.00  7.13           C  
ATOM    259  CD2 TYR A  36       3.027  33.615  23.420  1.00  7.32           C  
ATOM    260  CE1 TYR A  36       1.608  32.310  25.412  1.00  6.81           C  
ATOM    261  CE2 TYR A  36       1.825  34.146  23.874  1.00  6.87           C  
ATOM    262  CZ  TYR A  36       1.133  33.481  24.869  1.00  7.28           C  
ATOM    263  OH  TYR A  36      -0.067  34.016  25.305  1.00  7.33           O  
ATOM    264  N   LYS A  37       3.059  29.169  22.218  1.00  8.44           N  
ATOM    265  CA  LYS A  37       2.094  28.800  21.160  1.00  8.00           C  
ATOM    266  C   LYS A  37       0.742  29.211  21.742  1.00  7.67           C  
ATOM    267  O   LYS A  37       0.080  28.379  22.373  1.00  8.75           O  
ATOM    268  CB  LYS A  37       2.146  27.295  20.910  1.00  8.29           C  
ATOM    269  CG  LYS A  37       1.113  26.719  19.954  1.00  9.15           C  
ATOM    270  CD  LYS A  37       1.565  26.721  18.501  1.00  9.16           C  
ATOM    271  CE  LYS A  37       0.490  26.095  17.608  1.00  9.63           C  
ATOM    272  NZ  LYS A  37       0.918  26.050  16.169  1.00 10.87           N  
ATOM    273  N   PRO A  38       0.363  30.477  21.644  1.00  7.77           N  
ATOM    274  CA  PRO A  38      -0.832  30.980  22.305  1.00  7.57           C  
ATOM    275  C   PRO A  38      -2.110  30.265  21.918  1.00  7.93           C  
ATOM    276  O   PRO A  38      -2.954  30.028  22.783  1.00  7.97           O  
ATOM    277  CB  PRO A  38      -0.870  32.475  22.026  1.00  8.19           C  
ATOM    278  CG  PRO A  38       0.042  32.670  20.856  1.00  8.04           C  
ATOM    279  CD  PRO A  38       1.082  31.583  20.984  1.00  8.03           C  
ATOM    280  N   VAL A  39      -2.233  29.913  20.645  1.00  7.01           N  
ATOM    281  CA  VAL A  39      -3.440  29.244  20.160  1.00  7.26           C  
ATOM    282  C   VAL A  39      -3.054  27.960  19.433  1.00  7.06           C  
ATOM    283  O   VAL A  39      -2.211  27.978  18.529  1.00  7.40           O  
ATOM    284  CB  VAL A  39      -4.207  30.178  19.210  1.00  7.49           C  
ATOM    285  CG1 VAL A  39      -5.397  29.438  18.593  1.00  7.86           C  
ATOM    286  CG2 VAL A  39      -4.713  31.431  19.913  1.00  7.92           C  
ATOM    287  N   ALA A  40      -3.666  26.845  19.820  1.00  8.26           N  
ATOM    288  CA  ALA A  40      -3.384  25.563  19.189  1.00  9.38           C  
ATOM    289  C   ALA A  40      -4.669  24.754  19.005  1.00 10.55           C  
ATOM    290  O   ALA A  40      -5.525  24.745  19.879  1.00 11.65           O  
ATOM    291  CB  ALA A  40      -2.399  24.766  20.050  1.00  9.93           C  
ATOM    292  N   SER A  41      -4.794  24.105  17.859  1.00 11.23           N  
ATOM    293  CA  SER A  41      -5.927  23.245  17.546  1.00 12.61           C  
ATOM    294  C   SER A  41      -5.361  21.895  17.097  1.00 13.69           C  
ATOM    295  O   SER A  41      -4.375  21.889  16.349  1.00 14.90           O  
ATOM    296  CB  SER A  41      -6.844  23.841  16.488  1.00 13.24           C  
ATOM    297  OG  SER A  41      -6.138  24.190  15.304  1.00 15.81           O  
ATOM    298  N   GLY A  42      -5.954  20.800  17.549  1.00 12.74           N  
ATOM    299  CA  GLY A  42      -5.444  19.470  17.174  1.00 13.08           C  
ATOM    300  C   GLY A  42      -4.640  18.980  18.389  1.00 13.51           C  
ATOM    301  O   GLY A  42      -3.413  19.059  18.420  1.00 15.03           O  
ATOM    302  N   SER A  43      -5.381  18.589  19.419  1.00 13.01           N  
ATOM    303  CA  SER A  43      -4.790  18.223  20.700  1.00 13.25           C  
ATOM    304  C   SER A  43      -5.365  16.938  21.273  1.00 14.40           C  
ATOM    305  O   SER A  43      -6.481  16.527  20.959  1.00 15.40           O  
ATOM    306  CB  SER A  43      -4.996  19.378  21.696  1.00 12.71           C  
ATOM    307  OG  SER A  43      -4.563  20.609  21.136  1.00 12.65           O  
ATOM    308  N   GLU A  44      -4.551  16.270  22.098  1.00 14.88           N  
ATOM    309  CA  GLU A  44      -4.921  14.992  22.686  1.00 16.18           C  
ATOM    310  C   GLU A  44      -5.298  15.110  24.156  1.00 14.83           C  
ATOM    311  O   GLU A  44      -4.822  15.942  24.929  1.00 13.13           O  
ATOM    312  CB  GLU A  44      -3.774  13.994  22.500  1.00 18.60           C  
ATOM    313  CG  GLU A  44      -3.555  13.507  21.079  1.00 22.19           C  
ATOM    314  CD  GLU A  44      -2.885  14.513  20.168  1.00 23.72           C  
ATOM    315  OE1 GLU A  44      -1.829  15.075  20.532  1.00 24.95           O  
ATOM    316  OE2 GLU A  44      -3.429  14.763  19.069  1.00 25.55           O  
ATOM    317  N   LYS A  45      -6.214  14.229  24.573  1.00 15.19           N  
ATOM    318  CA  LYS A  45      -6.676  14.199  25.951  1.00 15.94           C  
ATOM    319  C   LYS A  45      -5.615  13.557  26.844  1.00 15.30           C  
ATOM    320  O   LYS A  45      -4.881  12.650  26.446  1.00 16.09           O  
ATOM    321  CB  LYS A  45      -7.976  13.394  26.085  1.00 18.01           C  
ATOM    322  CG  LYS A  45      -7.850  11.969  25.583  1.00 19.74           C  
ATOM    323  CD  LYS A  45      -9.164  11.205  25.728  1.00 21.88           C  
ATOM    324  CE  LYS A  45      -8.933   9.724  25.465  1.00 22.96           C  
ATOM    325  NZ  LYS A  45      -8.858   8.966  26.750  1.00 24.53           N  
ATOM    326  N   THR A  46      -5.441  14.122  28.024  1.00 14.07           N  
ATOM    327  CA  THR A  46      -4.575  13.622  29.081  1.00 14.64           C  
ATOM    328  C   THR A  46      -5.319  13.856  30.396  1.00 15.06           C  
ATOM    329  O   THR A  46      -6.285  14.626  30.480  1.00 15.31           O  
ATOM    330  CB  THR A  46      -3.180  14.274  29.189  1.00 14.21           C  
ATOM    331  OG1 THR A  46      -3.230  15.503  29.928  1.00 13.92           O  
ATOM    332  CG2 THR A  46      -2.522  14.560  27.844  1.00 14.61           C  
ATOM    333  N   PRO A  47      -4.813  13.316  31.500  1.00 15.06           N  
ATOM    334  CA  PRO A  47      -5.408  13.526  32.810  1.00 15.67           C  
ATOM    335  C   PRO A  47      -5.438  14.970  33.264  1.00 16.71           C  
ATOM    336  O   PRO A  47      -6.244  15.363  34.116  1.00 17.38           O  
ATOM    337  CB  PRO A  47      -4.541  12.684  33.758  1.00 14.49           C  
ATOM    338  CG  PRO A  47      -3.976  11.638  32.865  1.00 14.20           C  
ATOM    339  CD  PRO A  47      -3.684  12.354  31.560  1.00 15.08           C  
ATOM    340  N   GLU A  48      -4.565  15.819  32.732  1.00 17.43           N  
ATOM    341  CA  GLU A  48      -4.466  17.216  33.054  1.00 18.37           C  
ATOM    342  C   GLU A  48      -5.300  18.106  32.127  1.00 16.40           C  
ATOM    343  O   GLU A  48      -5.398  19.296  32.404  1.00 16.40           O  
ATOM    344  CB  GLU A  48      -3.011  17.686  32.908  1.00 21.21           C  
ATOM    345  CG  GLU A  48      -2.022  16.803  33.647  1.00 25.01           C  
ATOM    346  CD  GLU A  48      -1.850  17.239  35.086  1.00 27.27           C  
ATOM    347  OE1 GLU A  48      -2.697  16.879  35.926  1.00 29.24           O  
ATOM    348  OE2 GLU A  48      -0.855  17.946  35.360  1.00 29.26           O  
ATOM    349  N   GLY A  49      -5.856  17.509  31.085  1.00 15.83           N  
ATOM    350  CA  GLY A  49      -6.604  18.270  30.083  1.00 15.12           C  
ATOM    351  C   GLY A  49      -5.973  18.052  28.710  1.00 14.62           C  
ATOM    352  O   GLY A  49      -5.104  17.195  28.528  1.00 15.01           O  
ATOM    353  N   LEU A  50      -6.381  18.853  27.738  1.00 13.99           N  
ATOM    354  CA  LEU A  50      -5.878  18.725  26.372  1.00 12.97           C  
ATOM    355  C   LEU A  50      -4.433  19.196  26.276  1.00 11.88           C  
ATOM    356  O   LEU A  50      -4.025  20.166  26.918  1.00 12.00           O  
ATOM    357  CB  LEU A  50      -6.781  19.529  25.437  1.00 13.89           C  
ATOM    358  CG  LEU A  50      -8.231  19.047  25.293  1.00 13.96           C  
ATOM    359  CD1 LEU A  50      -8.988  19.944  24.318  1.00 14.24           C  
ATOM    360  CD2 LEU A  50      -8.297  17.612  24.802  1.00 14.09           C  
ATOM    361  N   ARG A  51      -3.642  18.479  25.481  1.00 11.10           N  
ATOM    362  CA  ARG A  51      -2.236  18.826  25.278  1.00 10.37           C  
ATOM    363  C   ARG A  51      -1.920  18.791  23.786  1.00  9.61           C  
ATOM    364  O   ARG A  51      -2.198  17.795  23.117  1.00 10.32           O  
ATOM    365  CB  ARG A  51      -1.306  17.838  25.994  1.00 11.57           C  
ATOM    366  CG  ARG A  51      -1.315  17.897  27.514  1.00 12.57           C  
ATOM    367  CD  ARG A  51      -0.908  19.257  28.015  1.00 13.30           C  
ATOM    368  NE  ARG A  51      -0.798  19.391  29.461  1.00 15.07           N  
ATOM    369  CZ  ARG A  51      -1.661  20.069  30.199  1.00 14.86           C  
ATOM    370  NH1 ARG A  51      -2.718  20.647  29.653  1.00 16.00           N  
ATOM    371  NH2 ARG A  51      -1.459  20.162  31.510  1.00 16.97           N  
ATOM    372  N   ASN A  52      -1.373  19.876  23.253  1.00  9.97           N  
ATOM    373  CA  ASN A  52      -1.019  19.966  21.834  1.00  9.90           C  
ATOM    374  C   ASN A  52       0.454  19.632  21.623  1.00  9.09           C  
ATOM    375  O   ASN A  52       1.274  20.116  22.389  1.00 10.21           O  
ATOM    376  CB  ASN A  52      -1.321  21.376  21.334  1.00  9.39           C  
ATOM    377  CG  ASN A  52      -0.753  21.703  19.971  1.00  9.65           C  
ATOM    378  OD1 ASN A  52       0.355  22.241  19.830  1.00 11.51           O  
ATOM    379  ND2 ASN A  52      -1.511  21.368  18.947  1.00  7.62           N  
ATOM    380  N   SER A  53       0.773  18.868  20.581  1.00 10.41           N  
ATOM    381  CA  SER A  53       2.145  18.449  20.319  1.00 10.80           C  
ATOM    382  C   SER A  53       3.094  19.582  19.959  1.00 10.22           C  
ATOM    383  O   SER A  53       4.257  19.520  20.385  1.00 10.73           O  
ATOM    384  CB  SER A  53       2.182  17.368  19.234  1.00 12.37           C  
ATOM    385  OG  SER A  53       1.707  17.858  17.994  1.00 14.66           O  
ATOM    386  N   ASP A  54       2.643  20.615  19.249  1.00 10.04           N  
ATOM    387  CA  ASP A  54       3.498  21.761  18.960  1.00 10.12           C  
ATOM    388  C   ASP A  54       3.907  22.422  20.273  1.00  8.83           C  
ATOM    389  O   ASP A  54       5.082  22.700  20.528  1.00  8.48           O  
ATOM    390  CB  ASP A  54       2.816  22.846  18.125  1.00 10.74           C  
ATOM    391  CG  ASP A  54       2.553  22.506  16.685  1.00 11.77           C  
ATOM    392  OD1 ASP A  54       2.658  21.328  16.289  1.00 11.70           O  
ATOM    393  OD2 ASP A  54       2.266  23.463  15.924  1.00 11.78           O  
ATOM    394  N   ALA A  55       2.924  22.688  21.134  1.00  7.95           N  
ATOM    395  CA  ALA A  55       3.155  23.303  22.430  1.00  7.83           C  
ATOM    396  C   ALA A  55       4.088  22.469  23.293  1.00  8.38           C  
ATOM    397  O   ALA A  55       5.009  23.034  23.904  1.00  8.79           O  
ATOM    398  CB  ALA A  55       1.819  23.533  23.132  1.00  6.90           C  
ATOM    399  N   LEU A  56       3.894  21.150  23.297  1.00  8.85           N  
ATOM    400  CA  LEU A  56       4.827  20.284  24.027  1.00  9.43           C  
ATOM    401  C   LEU A  56       6.235  20.406  23.460  1.00  9.55           C  
ATOM    402  O   LEU A  56       7.198  20.455  24.244  1.00  9.01           O  
ATOM    403  CB  LEU A  56       4.346  18.839  24.016  1.00 10.20           C  
ATOM    404  CG  LEU A  56       3.079  18.541  24.820  1.00 10.65           C  
ATOM    405  CD1 LEU A  56       2.637  17.094  24.622  1.00 11.89           C  
ATOM    406  CD2 LEU A  56       3.323  18.818  26.295  1.00 10.39           C  
ATOM    407  N   ALA A  57       6.406  20.448  22.134  1.00  8.68           N  
ATOM    408  CA  ALA A  57       7.746  20.589  21.562  1.00  9.24           C  
ATOM    409  C   ALA A  57       8.410  21.895  21.963  1.00  8.91           C  
ATOM    410  O   ALA A  57       9.599  21.920  22.309  1.00  8.83           O  
ATOM    411  CB  ALA A  57       7.713  20.452  20.043  1.00  8.94           C  
ATOM    412  N   LEU A  58       7.669  23.004  21.951  1.00  8.88           N  
ATOM    413  CA  LEU A  58       8.190  24.298  22.357  1.00  8.95           C  
ATOM    414  C   LEU A  58       8.524  24.319  23.848  1.00  9.14           C  
ATOM    415  O   LEU A  58       9.539  24.898  24.238  1.00 10.09           O  
ATOM    416  CB  LEU A  58       7.195  25.405  22.014  1.00  9.19           C  
ATOM    417  CG  LEU A  58       6.876  25.597  20.527  1.00 10.18           C  
ATOM    418  CD1 LEU A  58       5.864  26.723  20.361  1.00 10.00           C  
ATOM    419  CD2 LEU A  58       8.125  25.917  19.727  1.00 10.63           C  
ATOM    420  N   GLN A  59       7.712  23.660  24.665  1.00  9.55           N  
ATOM    421  CA  GLN A  59       7.966  23.572  26.100  1.00  9.84           C  
ATOM    422  C   GLN A  59       9.256  22.798  26.364  1.00 10.89           C  
ATOM    423  O   GLN A  59      10.108  23.248  27.140  1.00 11.81           O  
ATOM    424  CB  GLN A  59       6.777  22.869  26.765  1.00  9.82           C  
ATOM    425  CG  GLN A  59       6.935  22.626  28.258  1.00 11.08           C  
ATOM    426  CD  GLN A  59       5.773  21.850  28.849  1.00 11.40           C  
ATOM    427  OE1 GLN A  59       5.253  20.910  28.256  1.00 12.00           O  
ATOM    428  NE2 GLN A  59       5.366  22.268  30.053  1.00 11.90           N  
ATOM    429  N   ARG A  60       9.434  21.667  25.696  1.00 11.15           N  
ATOM    430  CA  ARG A  60      10.615  20.828  25.873  1.00 11.90           C  
ATOM    431  C   ARG A  60      11.878  21.496  25.346  1.00 11.80           C  
ATOM    432  O   ARG A  60      12.994  21.206  25.800  1.00 11.66           O  
ATOM    433  CB  ARG A  60      10.458  19.494  25.119  1.00 13.24           C  
ATOM    434  CG  ARG A  60       9.381  18.555  25.617  1.00 16.77           C  
ATOM    435  CD  ARG A  60       9.155  17.424  24.622  1.00 18.70           C  
ATOM    436  NE  ARG A  60       7.962  16.650  24.976  1.00 20.64           N  
ATOM    437  CZ  ARG A  60       7.034  16.317  24.085  1.00 21.46           C  
ATOM    438  NH1 ARG A  60       7.173  16.695  22.821  1.00 22.75           N  
ATOM    439  NH2 ARG A  60       5.977  15.614  24.456  1.00 22.04           N  
ATOM    440  N   ASN A  61      11.734  22.393  24.366  1.00 11.72           N  
ATOM    441  CA  ASN A  61      12.905  23.044  23.789  1.00 11.81           C  
ATOM    442  C   ASN A  61      13.212  24.384  24.434  1.00 12.25           C  
ATOM    443  O   ASN A  61      14.150  25.066  23.996  1.00 13.85           O  
ATOM    444  CB  ASN A  61      12.771  23.122  22.268  1.00 11.54           C  
ATOM    445  CG  ASN A  61      13.109  21.798  21.615  1.00 11.94           C  
ATOM    446  OD1 ASN A  61      14.290  21.502  21.397  1.00 13.58           O  
ATOM    447  ND2 ASN A  61      12.136  20.959  21.290  1.00 10.63           N  
ATOM    448  N   SER A  62      12.494  24.778  25.486  1.00 11.41           N  
ATOM    449  CA  SER A  62      12.766  26.014  26.197  1.00 10.57           C  
ATOM    450  C   SER A  62      13.855  25.751  27.244  1.00 11.51           C  
ATOM    451  O   SER A  62      13.901  24.658  27.803  1.00 11.64           O  
ATOM    452  CB  SER A  62      11.523  26.557  26.904  1.00 10.67           C  
ATOM    453  OG  SER A  62      10.513  26.854  25.955  1.00 10.79           O  
ATOM    454  N   SER A  63      14.716  26.735  27.511  1.00 12.62           N  
ATOM    455  CA  SER A  63      15.797  26.473  28.476  1.00 13.81           C  
ATOM    456  C   SER A  63      15.225  26.507  29.886  1.00 15.34           C  
ATOM    457  O   SER A  63      15.745  25.875  30.811  1.00 17.10           O  
ATOM    458  CB  SER A  63      16.960  27.441  28.318  1.00 13.26           C  
ATOM    459  OG  SER A  63      16.595  28.765  28.634  1.00 12.94           O  
ATOM    460  N   LEU A  64      14.158  27.272  30.049  1.00 16.29           N  
ATOM    461  CA  LEU A  64      13.457  27.382  31.315  1.00 16.96           C  
ATOM    462  C   LEU A  64      12.424  26.264  31.438  1.00 17.69           C  
ATOM    463  O   LEU A  64      11.887  25.794  30.433  1.00 16.87           O  
ATOM    464  CB  LEU A  64      12.716  28.719  31.398  1.00 17.98           C  
ATOM    465  CG  LEU A  64      13.567  29.987  31.329  1.00 18.57           C  
ATOM    466  CD1 LEU A  64      12.703  31.183  30.967  1.00 19.44           C  
ATOM    467  CD2 LEU A  64      14.297  30.207  32.649  1.00 19.95           C  
ATOM    468  N   GLN A  65      12.154  25.885  32.682  1.00 17.60           N  
ATOM    469  CA  GLN A  65      11.126  24.891  32.977  1.00 18.59           C  
ATOM    470  C   GLN A  65       9.804  25.660  33.074  1.00 16.97           C  
ATOM    471  O   GLN A  65       9.657  26.498  33.963  1.00 17.78           O  
ATOM    472  CB  GLN A  65      11.425  24.176  34.286  1.00 20.52           C  
ATOM    473  CG  GLN A  65      12.328  22.961  34.221  1.00 23.46           C  
ATOM    474  CD  GLN A  65      11.830  21.825  35.099  1.00 24.62           C  
ATOM    475  OE1 GLN A  65      11.998  20.650  34.769  1.00 25.22           O  
ATOM    476  NE2 GLN A  65      11.219  22.170  36.231  1.00 24.87           N  
ATOM    477  N   LEU A  66       8.933  25.489  32.088  1.00 14.62           N  
ATOM    478  CA  LEU A  66       7.697  26.247  32.010  1.00 13.43           C  
ATOM    479  C   LEU A  66       6.473  25.357  32.177  1.00 12.54           C  
ATOM    480  O   LEU A  66       6.508  24.209  31.743  1.00 12.47           O  
ATOM    481  CB  LEU A  66       7.601  26.924  30.629  1.00 13.15           C  
ATOM    482  CG  LEU A  66       8.758  27.861  30.266  1.00 13.72           C  
ATOM    483  CD1 LEU A  66       8.760  28.173  28.775  1.00 13.92           C  
ATOM    484  CD2 LEU A  66       8.694  29.149  31.067  1.00 14.50           C  
ATOM    485  N   ASP A  67       5.429  25.905  32.788  1.00 11.58           N  
ATOM    486  CA  ASP A  67       4.181  25.151  32.937  1.00 11.59           C  
ATOM    487  C   ASP A  67       3.474  25.144  31.582  1.00 10.28           C  
ATOM    488  O   ASP A  67       3.567  26.120  30.831  1.00 10.51           O  
ATOM    489  CB  ASP A  67       3.310  25.807  34.009  1.00 13.76           C  
ATOM    490  CG  ASP A  67       3.990  25.809  35.374  1.00 15.94           C  
ATOM    491  OD1 ASP A  67       4.472  24.725  35.751  1.00 18.18           O  
ATOM    492  OD2 ASP A  67       4.028  26.863  36.037  1.00 17.61           O  
ATOM    493  N   TYR A  68       2.777  24.065  31.273  1.00  9.74           N  
ATOM    494  CA  TYR A  68       2.092  23.916  29.995  1.00  9.49           C  
ATOM    495  C   TYR A  68       1.188  25.091  29.657  1.00  9.03           C  
ATOM    496  O   TYR A  68       1.257  25.609  28.534  1.00  8.09           O  
ATOM    497  CB  TYR A  68       1.272  22.607  29.923  1.00  9.99           C  
ATOM    498  CG  TYR A  68       0.667  22.488  28.524  1.00  9.61           C  
ATOM    499  CD1 TYR A  68       1.421  21.972  27.481  1.00  9.71           C  
ATOM    500  CD2 TYR A  68      -0.613  22.949  28.250  1.00  9.06           C  
ATOM    501  CE1 TYR A  68       0.904  21.887  26.201  1.00  8.18           C  
ATOM    502  CE2 TYR A  68      -1.141  22.864  26.977  1.00  9.04           C  
ATOM    503  CZ  TYR A  68      -0.381  22.336  25.957  1.00  8.61           C  
ATOM    504  OH  TYR A  68      -0.909  22.279  24.682  1.00  8.86           O  
ATOM    505  N   ALA A  69       0.319  25.521  30.578  1.00  8.55           N  
ATOM    506  CA  ALA A  69      -0.591  26.620  30.270  1.00  7.81           C  
ATOM    507  C   ALA A  69       0.106  27.932  29.959  1.00  8.17           C  
ATOM    508  O   ALA A  69      -0.457  28.829  29.323  1.00  7.92           O  
ATOM    509  CB  ALA A  69      -1.582  26.842  31.406  1.00  7.00           C  
ATOM    510  N   THR A  70       1.330  28.126  30.456  1.00  9.27           N  
ATOM    511  CA  THR A  70       2.085  29.333  30.160  1.00  9.76           C  
ATOM    512  C   THR A  70       2.585  29.291  28.714  1.00  9.34           C  
ATOM    513  O   THR A  70       2.738  30.332  28.082  1.00  9.42           O  
ATOM    514  CB  THR A  70       3.232  29.513  31.155  1.00 12.04           C  
ATOM    515  OG1 THR A  70       2.735  29.429  32.511  1.00 13.35           O  
ATOM    516  CG2 THR A  70       3.917  30.861  31.029  1.00 13.97           C  
ATOM    517  N   VAL A  71       2.844  28.097  28.193  1.00  8.96           N  
ATOM    518  CA  VAL A  71       3.274  27.955  26.802  1.00  8.66           C  
ATOM    519  C   VAL A  71       2.070  28.022  25.867  1.00  7.99           C  
ATOM    520  O   VAL A  71       2.188  28.561  24.769  1.00  8.58           O  
ATOM    521  CB  VAL A  71       3.990  26.611  26.588  1.00  9.00           C  
ATOM    522  CG1 VAL A  71       4.293  26.358  25.115  1.00  9.76           C  
ATOM    523  CG2 VAL A  71       5.295  26.599  27.388  1.00 10.20           C  
ATOM    524  N   ASN A  72       0.949  27.453  26.286  1.00  7.48           N  
ATOM    525  CA  ASN A  72      -0.229  27.401  25.427  1.00  7.73           C  
ATOM    526  C   ASN A  72      -1.543  27.585  26.174  1.00  8.10           C  
ATOM    527  O   ASN A  72      -2.227  26.627  26.558  1.00  9.21           O  
ATOM    528  CB  ASN A  72      -0.241  26.045  24.703  1.00  7.93           C  
ATOM    529  CG  ASN A  72      -1.498  25.810  23.886  1.00  8.07           C  
ATOM    530  OD1 ASN A  72      -2.024  24.688  23.849  1.00  9.79           O  
ATOM    531  ND2 ASN A  72      -1.957  26.846  23.206  1.00  6.02           N  
ATOM    532  N   PRO A  73      -1.947  28.840  26.338  1.00  8.02           N  
ATOM    533  CA  PRO A  73      -3.186  29.158  27.031  1.00  9.31           C  
ATOM    534  C   PRO A  73      -4.440  28.628  26.357  1.00  9.59           C  
ATOM    535  O   PRO A  73      -5.354  28.204  27.078  1.00 10.59           O  
ATOM    536  CB  PRO A  73      -3.208  30.678  27.113  1.00  9.27           C  
ATOM    537  CG  PRO A  73      -1.796  31.109  26.895  1.00 10.67           C  
ATOM    538  CD  PRO A  73      -1.192  30.066  25.981  1.00  8.69           C  
ATOM    539  N   TYR A  74      -4.529  28.638  25.032  1.00  8.65           N  
ATOM    540  CA  TYR A  74      -5.735  28.193  24.336  1.00  8.38           C  
ATOM    541  C   TYR A  74      -5.510  26.876  23.603  1.00  8.40           C  
ATOM    542  O   TYR A  74      -4.796  26.859  22.596  1.00  8.96           O  
ATOM    543  CB  TYR A  74      -6.156  29.246  23.314  1.00  9.22           C  
ATOM    544  CG  TYR A  74      -6.777  30.506  23.857  1.00  9.44           C  
ATOM    545  CD1 TYR A  74      -8.063  30.513  24.393  1.00 10.13           C  
ATOM    546  CD2 TYR A  74      -6.066  31.698  23.820  1.00  9.81           C  
ATOM    547  CE1 TYR A  74      -8.625  31.679  24.881  1.00 10.17           C  
ATOM    548  CE2 TYR A  74      -6.625  32.870  24.308  1.00  9.90           C  
ATOM    549  CZ  TYR A  74      -7.899  32.849  24.837  1.00  9.90           C  
ATOM    550  OH  TYR A  74      -8.423  34.028  25.306  1.00 10.57           O  
ATOM    551  N   THR A  75      -6.129  25.803  24.065  1.00  8.41           N  
ATOM    552  CA  THR A  75      -5.971  24.479  23.485  1.00  9.45           C  
ATOM    553  C   THR A  75      -7.312  23.906  23.040  1.00 10.21           C  
ATOM    554  O   THR A  75      -8.241  23.838  23.842  1.00 11.38           O  
ATOM    555  CB  THR A  75      -5.360  23.505  24.526  1.00 10.13           C  
ATOM    556  OG1 THR A  75      -4.345  24.204  25.267  1.00 10.90           O  
ATOM    557  CG2 THR A  75      -4.767  22.297  23.829  1.00 10.55           C  
ATOM    558  N   PHE A  76      -7.411  23.534  21.763  1.00 10.70           N  
ATOM    559  CA  PHE A  76      -8.636  22.961  21.214  1.00 10.79           C  
ATOM    560  C   PHE A  76      -8.319  21.559  20.706  1.00 10.60           C  
ATOM    561  O   PHE A  76      -7.244  21.331  20.136  1.00 10.36           O  
ATOM    562  CB  PHE A  76      -9.207  23.829  20.082  1.00 11.03           C  
ATOM    563  CG  PHE A  76      -9.601  25.200  20.565  1.00 10.19           C  
ATOM    564  CD1 PHE A  76     -10.802  25.403  21.223  1.00 10.78           C  
ATOM    565  CD2 PHE A  76      -8.755  26.276  20.368  1.00 10.16           C  
ATOM    566  CE1 PHE A  76     -11.148  26.663  21.671  1.00 10.87           C  
ATOM    567  CE2 PHE A  76      -9.100  27.543  20.809  1.00 11.12           C  
ATOM    568  CZ  PHE A  76     -10.302  27.735  21.461  1.00 11.06           C  
ATOM    569  N   ALA A  77      -9.236  20.606  20.898  1.00 11.80           N  
ATOM    570  CA  ALA A  77      -8.983  19.239  20.463  1.00 11.93           C  
ATOM    571  C   ALA A  77      -8.956  19.037  18.953  1.00 12.77           C  
ATOM    572  O   ALA A  77      -8.117  18.308  18.428  1.00 13.15           O  
ATOM    573  CB  ALA A  77     -10.023  18.294  21.076  1.00 13.31           C  
ATOM    574  N   GLU A  78      -9.921  19.619  18.242  1.00 12.76           N  
ATOM    575  CA  GLU A  78     -10.036  19.393  16.810  1.00 12.93           C  
ATOM    576  C   GLU A  78      -9.066  20.220  15.987  1.00 12.56           C  
ATOM    577  O   GLU A  78      -8.955  21.429  16.154  1.00 12.16           O  
ATOM    578  CB  GLU A  78     -11.478  19.689  16.362  1.00 13.07           C  
ATOM    579  CG  GLU A  78     -11.760  19.384  14.905  1.00 13.21           C  
ATOM    580  CD  GLU A  78     -13.174  19.755  14.493  1.00 13.43           C  
ATOM    581  OE1 GLU A  78     -14.077  19.773  15.354  1.00 13.71           O  
ATOM    582  OE2 GLU A  78     -13.358  20.017  13.291  1.00 12.91           O  
ATOM    583  N   PRO A  79      -8.391  19.565  15.051  1.00 12.84           N  
ATOM    584  CA  PRO A  79      -7.428  20.191  14.163  1.00 13.25           C  
ATOM    585  C   PRO A  79      -8.039  20.919  12.981  1.00 12.97           C  
ATOM    586  O   PRO A  79      -7.837  20.562  11.813  1.00 14.38           O  
ATOM    587  CB  PRO A  79      -6.562  19.015  13.716  1.00 13.74           C  
ATOM    588  CG  PRO A  79      -7.487  17.849  13.709  1.00 14.11           C  
ATOM    589  CD  PRO A  79      -8.476  18.095  14.820  1.00 13.33           C  
ATOM    590  N   THR A  80      -8.683  22.046  13.247  1.00 10.97           N  
ATOM    591  CA  THR A  80      -9.298  22.882  12.227  1.00 10.47           C  
ATOM    592  C   THR A  80      -8.877  24.331  12.417  1.00 10.26           C  
ATOM    593  O   THR A  80      -8.004  24.597  13.263  1.00 10.60           O  
ATOM    594  CB  THR A  80     -10.836  22.738  12.278  1.00 10.76           C  
ATOM    595  OG1 THR A  80     -11.406  23.409  11.143  1.00 11.57           O  
ATOM    596  CG2 THR A  80     -11.394  23.353  13.548  1.00 11.14           C  
ATOM    597  N   SER A  81      -9.451  25.294  11.707  1.00  8.31           N  
ATOM    598  CA  SER A  81      -9.094  26.700  11.954  1.00  7.99           C  
ATOM    599  C   SER A  81      -9.565  27.093  13.349  1.00  8.34           C  
ATOM    600  O   SER A  81     -10.686  26.778  13.757  1.00  7.46           O  
ATOM    601  CB  SER A  81      -9.760  27.570  10.890  1.00  8.24           C  
ATOM    602  OG  SER A  81      -9.341  28.910  10.975  1.00  8.90           O  
ATOM    603  N   PRO A  82      -8.718  27.772  14.114  1.00  8.48           N  
ATOM    604  CA  PRO A  82      -9.050  28.159  15.481  1.00  8.40           C  
ATOM    605  C   PRO A  82     -10.394  28.841  15.611  1.00  9.17           C  
ATOM    606  O   PRO A  82     -11.180  28.517  16.516  1.00  8.36           O  
ATOM    607  CB  PRO A  82      -7.891  29.041  15.919  1.00  8.68           C  
ATOM    608  CG  PRO A  82      -6.738  28.568  15.091  1.00  8.24           C  
ATOM    609  CD  PRO A  82      -7.336  28.163  13.761  1.00  8.19           C  
ATOM    610  N   HIS A  83     -10.754  29.764  14.712  1.00  9.09           N  
ATOM    611  CA  HIS A  83     -12.034  30.455  14.814  1.00  9.77           C  
ATOM    612  C   HIS A  83     -13.233  29.514  14.765  1.00  9.65           C  
ATOM    613  O   HIS A  83     -14.247  29.793  15.414  1.00  9.31           O  
ATOM    614  CB  HIS A  83     -12.141  31.540  13.747  1.00  9.91           C  
ATOM    615  CG  HIS A  83     -12.492  31.101  12.364  1.00  9.61           C  
ATOM    616  ND1 HIS A  83     -11.725  30.276  11.588  1.00 10.00           N  
ATOM    617  CD2 HIS A  83     -13.587  31.443  11.630  1.00  9.55           C  
ATOM    618  CE1 HIS A  83     -12.330  30.095  10.419  1.00 10.60           C  
ATOM    619  NE2 HIS A  83     -13.452  30.794  10.423  1.00 10.34           N  
ATOM    620  N   ILE A  84     -13.149  28.456  13.977  1.00  9.30           N  
ATOM    621  CA  ILE A  84     -14.251  27.509  13.842  1.00  9.23           C  
ATOM    622  C   ILE A  84     -14.481  26.721  15.121  1.00  9.20           C  
ATOM    623  O   ILE A  84     -15.608  26.659  15.608  1.00  9.82           O  
ATOM    624  CB  ILE A  84     -14.021  26.552  12.654  1.00  9.83           C  
ATOM    625  CG1 ILE A  84     -14.130  27.345  11.357  1.00 10.58           C  
ATOM    626  CG2 ILE A  84     -14.997  25.384  12.656  1.00 10.09           C  
ATOM    627  CD1 ILE A  84     -13.654  26.610  10.121  1.00 11.83           C  
ATOM    628  N   ILE A  85     -13.421  26.131  15.668  1.00  9.97           N  
ATOM    629  CA  ILE A  85     -13.564  25.337  16.895  1.00  9.86           C  
ATOM    630  C   ILE A  85     -13.833  26.250  18.084  1.00 10.40           C  
ATOM    631  O   ILE A  85     -14.636  25.875  18.953  1.00 11.54           O  
ATOM    632  CB  ILE A  85     -12.384  24.384  17.090  1.00 10.57           C  
ATOM    633  CG1 ILE A  85     -12.628  23.418  18.252  1.00 11.02           C  
ATOM    634  CG2 ILE A  85     -11.088  25.144  17.313  1.00  9.38           C  
ATOM    635  CD1 ILE A  85     -13.882  22.572  18.131  1.00 12.26           C  
ATOM    636  N   SER A  86     -13.265  27.448  18.091  1.00  9.24           N  
ATOM    637  CA  SER A  86     -13.547  28.418  19.149  1.00 10.32           C  
ATOM    638  C   SER A  86     -15.034  28.770  19.201  1.00 11.62           C  
ATOM    639  O   SER A  86     -15.618  28.781  20.286  1.00 11.63           O  
ATOM    640  CB  SER A  86     -12.739  29.699  18.912  1.00 10.70           C  
ATOM    641  OG  SER A  86     -13.201  30.739  19.759  1.00 10.56           O  
ATOM    642  N   ALA A  87     -15.639  29.041  18.046  1.00 11.26           N  
ATOM    643  CA  ALA A  87     -17.068  29.395  18.028  1.00 12.10           C  
ATOM    644  C   ALA A  87     -17.946  28.224  18.433  1.00 13.13           C  
ATOM    645  O   ALA A  87     -18.923  28.407  19.190  1.00 13.63           O  
ATOM    646  CB  ALA A  87     -17.447  29.937  16.655  1.00 12.03           C  
ATOM    647  N   GLN A  88     -17.632  27.019  17.981  1.00 13.83           N  
ATOM    648  CA  GLN A  88     -18.413  25.835  18.303  1.00 15.48           C  
ATOM    649  C   GLN A  88     -18.355  25.496  19.789  1.00 15.31           C  
ATOM    650  O   GLN A  88     -19.370  25.089  20.359  1.00 15.72           O  
ATOM    651  CB  GLN A  88     -17.981  24.607  17.493  1.00 18.90           C  
ATOM    652  CG  GLN A  88     -19.051  23.525  17.495  1.00 22.80           C  
ATOM    653  CD  GLN A  88     -19.874  23.454  16.229  1.00 24.83           C  
ATOM    654  OE1 GLN A  88     -19.951  22.399  15.594  1.00 26.33           O  
ATOM    655  NE2 GLN A  88     -20.536  24.547  15.850  1.00 26.70           N  
ATOM    656  N   GLU A  89     -17.205  25.699  20.428  1.00 13.90           N  
ATOM    657  CA  GLU A  89     -17.099  25.388  21.850  1.00 14.76           C  
ATOM    658  C   GLU A  89     -17.486  26.553  22.741  1.00 13.93           C  
ATOM    659  O   GLU A  89     -17.588  26.366  23.957  1.00 13.18           O  
ATOM    660  CB  GLU A  89     -15.674  24.890  22.154  1.00 16.63           C  
ATOM    661  CG  GLU A  89     -15.393  23.631  21.340  1.00 20.53           C  
ATOM    662  CD  GLU A  89     -14.213  22.818  21.807  1.00 22.82           C  
ATOM    663  OE1 GLU A  89     -13.161  23.404  22.117  1.00 24.24           O  
ATOM    664  OE2 GLU A  89     -14.331  21.572  21.856  1.00 25.51           O  
ATOM    665  N   GLY A  90     -17.712  27.733  22.188  1.00 13.84           N  
ATOM    666  CA  GLY A  90     -18.082  28.916  22.951  1.00 13.27           C  
ATOM    667  C   GLY A  90     -16.936  29.388  23.841  1.00 14.47           C  
ATOM    668  O   GLY A  90     -17.140  29.835  24.971  1.00 15.61           O  
ATOM    669  N   ARG A  91     -15.719  29.293  23.326  1.00 13.19           N  
ATOM    670  CA  ARG A  91     -14.523  29.725  24.038  1.00 12.99           C  
ATOM    671  C   ARG A  91     -13.809  30.775  23.193  1.00 12.27           C  
ATOM    672  O   ARG A  91     -12.968  30.423  22.366  1.00 12.81           O  
ATOM    673  CB  ARG A  91     -13.580  28.557  24.310  1.00 14.30           C  
ATOM    674  CG  ARG A  91     -12.494  28.924  25.320  1.00 16.61           C  
ATOM    675  CD  ARG A  91     -11.518  27.788  25.538  1.00 17.27           C  
ATOM    676  NE  ARG A  91     -12.062  26.629  26.215  1.00 17.15           N  
ATOM    677  CZ  ARG A  91     -12.328  26.550  27.521  1.00 16.93           C  
ATOM    678  NH1 ARG A  91     -12.128  27.581  28.328  1.00 16.47           N  
ATOM    679  NH2 ARG A  91     -12.811  25.418  28.012  1.00 17.12           N  
ATOM    680  N   PRO A  92     -14.163  32.035  23.364  1.00 11.97           N  
ATOM    681  CA  PRO A  92     -13.572  33.116  22.603  1.00 11.56           C  
ATOM    682  C   PRO A  92     -12.066  33.215  22.794  1.00 11.08           C  
ATOM    683  O   PRO A  92     -11.552  33.017  23.889  1.00  9.81           O  
ATOM    684  CB  PRO A  92     -14.256  34.382  23.105  1.00 13.04           C  
ATOM    685  CG  PRO A  92     -14.890  34.006  24.398  1.00 13.86           C  
ATOM    686  CD  PRO A  92     -15.189  32.533  24.315  1.00 13.19           C  
ATOM    687  N   ILE A  93     -11.374  33.507  21.699  1.00 10.28           N  
ATOM    688  CA  ILE A  93      -9.927  33.727  21.725  1.00 10.86           C  
ATOM    689  C   ILE A  93      -9.715  35.234  21.825  1.00 11.79           C  
ATOM    690  O   ILE A  93     -10.108  35.988  20.931  1.00 13.12           O  
ATOM    691  CB  ILE A  93      -9.242  33.180  20.462  1.00  8.73           C  
ATOM    692  CG1 ILE A  93      -9.402  31.662  20.396  1.00  8.43           C  
ATOM    693  CG2 ILE A  93      -7.764  33.561  20.463  1.00  8.55           C  
ATOM    694  CD1 ILE A  93      -9.028  31.046  19.064  1.00  8.12           C  
ATOM    695  N   GLU A  94      -9.212  35.696  22.961  1.00 11.51           N  
ATOM    696  CA  GLU A  94      -9.053  37.121  23.204  1.00 13.07           C  
ATOM    697  C   GLU A  94      -7.622  37.601  23.027  1.00 12.37           C  
ATOM    698  O   GLU A  94      -6.693  37.112  23.668  1.00 12.23           O  
ATOM    699  CB  GLU A  94      -9.555  37.419  24.622  1.00 15.37           C  
ATOM    700  CG  GLU A  94      -9.190  38.792  25.165  1.00 17.60           C  
ATOM    701  CD  GLU A  94      -9.803  39.919  24.359  1.00 18.94           C  
ATOM    702  OE1 GLU A  94     -11.054  39.888  24.226  1.00 21.41           O  
ATOM    703  OE2 GLU A  94      -9.073  40.803  23.863  1.00 18.18           O  
ATOM    704  N   SER A  95      -7.462  38.656  22.232  1.00 12.13           N  
ATOM    705  CA  SER A  95      -6.167  39.296  22.040  1.00 11.31           C  
ATOM    706  C   SER A  95      -5.490  39.646  23.356  1.00 11.59           C  
ATOM    707  O   SER A  95      -4.294  39.385  23.536  1.00  9.80           O  
ATOM    708  CB  SER A  95      -6.366  40.555  21.187  1.00 11.91           C  
ATOM    709  OG  SER A  95      -5.152  41.239  20.965  1.00 11.59           O  
ATOM    710  N   LEU A  96      -6.213  40.223  24.309  1.00 11.57           N  
ATOM    711  CA  LEU A  96      -5.660  40.584  25.608  1.00 12.10           C  
ATOM    712  C   LEU A  96      -5.088  39.405  26.377  1.00 10.63           C  
ATOM    713  O   LEU A  96      -4.057  39.561  27.045  1.00 10.86           O  
ATOM    714  CB  LEU A  96      -6.767  41.271  26.424  1.00 15.26           C  
ATOM    715  CG  LEU A  96      -6.836  42.794  26.446  1.00 17.74           C  
ATOM    716  CD1 LEU A  96      -6.312  43.447  25.185  1.00 19.58           C  
ATOM    717  CD2 LEU A  96      -8.269  43.249  26.731  1.00 18.50           C  
ATOM    718  N   VAL A  97      -5.704  38.231  26.321  1.00  9.22           N  
ATOM    719  CA  VAL A  97      -5.222  37.025  26.985  1.00  9.38           C  
ATOM    720  C   VAL A  97      -3.942  36.541  26.306  1.00  9.18           C  
ATOM    721  O   VAL A  97      -2.959  36.180  26.960  1.00  8.93           O  
ATOM    722  CB  VAL A  97      -6.296  35.923  26.984  1.00  9.31           C  
ATOM    723  CG1 VAL A  97      -5.767  34.587  27.477  1.00  9.39           C  
ATOM    724  CG2 VAL A  97      -7.473  36.362  27.867  1.00 11.25           C  
ATOM    725  N   MET A  98      -3.946  36.565  24.970  1.00  8.62           N  
ATOM    726  CA  MET A  98      -2.735  36.180  24.231  1.00  7.48           C  
ATOM    727  C   MET A  98      -1.570  37.102  24.576  1.00  7.96           C  
ATOM    728  O   MET A  98      -0.455  36.625  24.826  1.00  8.15           O  
ATOM    729  CB  MET A  98      -3.030  36.257  22.727  1.00  8.41           C  
ATOM    730  CG  MET A  98      -4.136  35.306  22.277  1.00  9.25           C  
ATOM    731  SD  MET A  98      -4.582  35.568  20.546  1.00  9.26           S  
ATOM    732  CE  MET A  98      -3.070  35.063  19.726  1.00  9.22           C  
ATOM    733  N   SER A  99      -1.809  38.407  24.657  1.00  7.81           N  
ATOM    734  CA  SER A  99      -0.770  39.372  25.013  1.00  8.75           C  
ATOM    735  C   SER A  99      -0.318  39.208  26.454  1.00  9.35           C  
ATOM    736  O   SER A  99       0.882  39.247  26.750  1.00  9.19           O  
ATOM    737  CB  SER A  99      -1.268  40.802  24.772  1.00  9.03           C  
ATOM    738  OG  SER A  99      -1.449  41.037  23.384  1.00  9.42           O  
ATOM    739  N   ALA A 100      -1.263  38.962  27.372  1.00 10.39           N  
ATOM    740  CA  ALA A 100      -0.885  38.757  28.774  1.00  9.91           C  
ATOM    741  C   ALA A 100       0.039  37.551  28.903  1.00  9.79           C  
ATOM    742  O   ALA A 100       1.008  37.579  29.675  1.00 10.85           O  
ATOM    743  CB  ALA A 100      -2.100  38.556  29.668  1.00  9.69           C  
ATOM    744  N   GLY A 101      -0.200  36.499  28.126  1.00  9.43           N  
ATOM    745  CA  GLY A 101       0.637  35.298  28.175  1.00  8.63           C  
ATOM    746  C   GLY A 101       2.057  35.614  27.705  1.00  8.55           C  
ATOM    747  O   GLY A 101       3.020  35.066  28.255  1.00  8.64           O  
ATOM    748  N   LEU A 102       2.185  36.472  26.695  1.00  9.07           N  
ATOM    749  CA  LEU A 102       3.526  36.846  26.222  1.00  9.97           C  
ATOM    750  C   LEU A 102       4.252  37.650  27.295  1.00 10.90           C  
ATOM    751  O   LEU A 102       5.412  37.364  27.595  1.00 11.44           O  
ATOM    752  CB  LEU A 102       3.414  37.617  24.915  1.00  9.99           C  
ATOM    753  CG  LEU A 102       4.710  38.138  24.282  1.00  9.83           C  
ATOM    754  CD1 LEU A 102       5.739  37.027  24.147  1.00 11.26           C  
ATOM    755  CD2 LEU A 102       4.410  38.751  22.917  1.00 10.84           C  
ATOM    756  N   ARG A 103       3.567  38.599  27.926  1.00 11.47           N  
ATOM    757  CA  ARG A 103       4.166  39.352  29.027  1.00 12.48           C  
ATOM    758  C   ARG A 103       4.599  38.431  30.160  1.00 11.80           C  
ATOM    759  O   ARG A 103       5.665  38.651  30.756  1.00 11.92           O  
ATOM    760  CB  ARG A 103       3.194  40.379  29.597  1.00 13.76           C  
ATOM    761  CG  ARG A 103       2.553  41.331  28.610  1.00 16.09           C  
ATOM    762  CD  ARG A 103       3.522  42.407  28.159  1.00 17.44           C  
ATOM    763  NE  ARG A 103       4.237  42.052  26.940  1.00 18.81           N  
ATOM    764  CZ  ARG A 103       3.679  41.989  25.729  1.00 19.08           C  
ATOM    765  NH1 ARG A 103       2.388  42.244  25.559  1.00 18.62           N  
ATOM    766  NH2 ARG A 103       4.431  41.661  24.687  1.00 19.15           N  
ATOM    767  N   ALA A 104       3.812  37.405  30.482  1.00 10.73           N  
ATOM    768  CA  ALA A 104       4.137  36.491  31.569  1.00 10.67           C  
ATOM    769  C   ALA A 104       5.422  35.728  31.265  1.00 11.61           C  
ATOM    770  O   ALA A 104       6.248  35.541  32.158  1.00 11.61           O  
ATOM    771  CB  ALA A 104       3.001  35.513  31.840  1.00 10.61           C  
ATOM    772  N   LEU A 105       5.638  35.333  30.008  1.00 11.45           N  
ATOM    773  CA  LEU A 105       6.889  34.660  29.654  1.00 12.87           C  
ATOM    774  C   LEU A 105       8.075  35.608  29.738  1.00 14.85           C  
ATOM    775  O   LEU A 105       9.133  35.198  30.228  1.00 16.34           O  
ATOM    776  CB  LEU A 105       6.809  34.050  28.255  1.00 12.28           C  
ATOM    777  CG  LEU A 105       5.952  32.781  28.202  1.00 12.97           C  
ATOM    778  CD1 LEU A 105       5.840  32.321  26.757  1.00 12.69           C  
ATOM    779  CD2 LEU A 105       6.535  31.681  29.077  1.00 12.40           C  
ATOM    780  N   GLU A 106       7.881  36.871  29.378  1.00 16.16           N  
ATOM    781  CA  GLU A 106       8.929  37.878  29.493  1.00 18.50           C  
ATOM    782  C   GLU A 106       9.321  38.166  30.938  1.00 19.50           C  
ATOM    783  O   GLU A 106      10.365  38.798  31.156  1.00 20.00           O  
ATOM    784  CB  GLU A 106       8.526  39.165  28.765  1.00 19.93           C  
ATOM    785  CG  GLU A 106       8.182  38.966  27.296  1.00 21.88           C  
ATOM    786  CD  GLU A 106       7.518  40.152  26.639  1.00 23.29           C  
ATOM    787  OE1 GLU A 106       6.966  41.034  27.330  1.00 24.23           O  
ATOM    788  OE2 GLU A 106       7.519  40.240  25.388  1.00 25.03           O  
ATOM    789  N   GLN A 107       8.593  37.698  31.939  1.00 20.38           N  
ATOM    790  CA  GLN A 107       8.943  37.809  33.339  1.00 21.06           C  
ATOM    791  C   GLN A 107      10.204  36.989  33.639  1.00 21.12           C  
ATOM    792  O   GLN A 107      10.975  37.356  34.529  1.00 21.11           O  
ATOM    793  CB  GLN A 107       7.851  37.276  34.268  1.00 21.98           C  
ATOM    794  CG  GLN A 107       6.557  38.050  34.374  1.00 23.45           C  
ATOM    795  CD  GLN A 107       5.571  37.381  35.316  1.00 24.38           C  
ATOM    796  OE1 GLN A 107       5.963  36.542  36.134  1.00 25.36           O  
ATOM    797  NE2 GLN A 107       4.295  37.729  35.228  1.00 24.62           N  
ATOM    798  N   GLN A 108      10.375  35.845  32.976  1.00 20.87           N  
ATOM    799  CA  GLN A 108      11.535  35.009  33.232  1.00 20.78           C  
ATOM    800  C   GLN A 108      12.448  34.782  32.035  1.00 19.04           C  
ATOM    801  O   GLN A 108      13.604  34.411  32.277  1.00 19.58           O  
ATOM    802  CB  GLN A 108      11.119  33.654  33.806  1.00 23.15           C  
ATOM    803  CG  GLN A 108      10.055  32.926  33.006  1.00 25.80           C  
ATOM    804  CD  GLN A 108       8.805  32.679  33.828  1.00 27.41           C  
ATOM    805  OE1 GLN A 108       8.159  33.632  34.273  1.00 29.06           O  
ATOM    806  NE2 GLN A 108       8.462  31.414  34.030  1.00 27.45           N  
ATOM    807  N   ALA A 109      12.009  34.981  30.804  1.00 16.36           N  
ATOM    808  CA  ALA A 109      12.871  34.728  29.650  1.00 14.18           C  
ATOM    809  C   ALA A 109      13.363  36.000  28.985  1.00 13.96           C  
ATOM    810  O   ALA A 109      12.647  37.004  29.004  1.00 13.38           O  
ATOM    811  CB  ALA A 109      12.098  33.887  28.631  1.00 15.00           C  
ATOM    812  N   ASP A 110      14.557  35.995  28.392  1.00 11.63           N  
ATOM    813  CA  ASP A 110      15.054  37.179  27.700  1.00 11.65           C  
ATOM    814  C   ASP A 110      15.084  36.943  26.189  1.00 10.45           C  
ATOM    815  O   ASP A 110      15.576  37.749  25.400  1.00 10.85           O  
ATOM    816  CB  ASP A 110      16.407  37.652  28.219  1.00 12.26           C  
ATOM    817  CG  ASP A 110      17.505  36.617  28.143  1.00 12.98           C  
ATOM    818  OD1 ASP A 110      17.323  35.517  27.595  1.00 12.13           O  
ATOM    819  OD2 ASP A 110      18.610  36.908  28.666  1.00 13.95           O  
ATOM    820  N   TRP A 111      14.497  35.828  25.768  1.00 10.23           N  
ATOM    821  CA  TRP A 111      14.426  35.485  24.335  1.00  9.42           C  
ATOM    822  C   TRP A 111      13.170  34.633  24.155  1.00  9.22           C  
ATOM    823  O   TRP A 111      13.139  33.527  24.683  1.00  9.65           O  
ATOM    824  CB  TRP A 111      15.647  34.689  23.898  1.00  9.63           C  
ATOM    825  CG  TRP A 111      15.945  34.652  22.432  1.00  9.60           C  
ATOM    826  CD1 TRP A 111      16.809  35.472  21.760  1.00  9.35           C  
ATOM    827  CD2 TRP A 111      15.400  33.754  21.454  1.00  9.47           C  
ATOM    828  NE1 TRP A 111      16.831  35.136  20.422  1.00 10.01           N  
ATOM    829  CE2 TRP A 111      15.973  34.092  20.210  1.00  9.51           C  
ATOM    830  CE3 TRP A 111      14.481  32.704  21.514  1.00  8.95           C  
ATOM    831  CZ2 TRP A 111      15.657  33.408  19.032  1.00  9.77           C  
ATOM    832  CZ3 TRP A 111      14.171  32.028  20.344  1.00  9.67           C  
ATOM    833  CH2 TRP A 111      14.761  32.381  19.120  1.00  9.68           C  
ATOM    834  N   VAL A 112      12.137  35.221  23.551  1.00  9.56           N  
ATOM    835  CA  VAL A 112      10.870  34.496  23.441  1.00  9.10           C  
ATOM    836  C   VAL A 112      10.528  34.280  21.970  1.00  8.63           C  
ATOM    837  O   VAL A 112      10.566  35.217  21.171  1.00  9.53           O  
ATOM    838  CB  VAL A 112       9.716  35.254  24.124  1.00  9.72           C  
ATOM    839  CG1 VAL A 112       8.407  34.481  23.978  1.00  9.49           C  
ATOM    840  CG2 VAL A 112      10.019  35.509  25.595  1.00 10.68           C  
ATOM    841  N   LEU A 113      10.161  33.048  21.647  1.00  9.05           N  
ATOM    842  CA  LEU A 113       9.739  32.705  20.293  1.00  9.04           C  
ATOM    843  C   LEU A 113       8.250  32.368  20.332  1.00  8.78           C  
ATOM    844  O   LEU A 113       7.862  31.520  21.134  1.00  8.70           O  
ATOM    845  CB  LEU A 113      10.540  31.502  19.789  1.00  9.54           C  
ATOM    846  CG  LEU A 113      10.237  30.991  18.379  1.00  9.77           C  
ATOM    847  CD1 LEU A 113      11.455  30.275  17.802  1.00  9.91           C  
ATOM    848  CD2 LEU A 113       9.040  30.039  18.365  1.00  9.80           C  
ATOM    849  N   VAL A 114       7.462  33.009  19.487  1.00  7.97           N  
ATOM    850  CA  VAL A 114       6.022  32.751  19.435  1.00  8.46           C  
ATOM    851  C   VAL A 114       5.682  32.031  18.140  1.00  8.25           C  
ATOM    852  O   VAL A 114       5.982  32.582  17.078  1.00  9.82           O  
ATOM    853  CB  VAL A 114       5.263  34.092  19.477  1.00  8.20           C  
ATOM    854  CG1 VAL A 114       3.752  33.886  19.499  1.00  8.72           C  
ATOM    855  CG2 VAL A 114       5.697  34.926  20.678  1.00  9.45           C  
ATOM    856  N   GLU A 115       5.109  30.840  18.221  1.00  7.93           N  
ATOM    857  CA  GLU A 115       4.744  30.122  17.001  1.00  8.35           C  
ATOM    858  C   GLU A 115       3.270  30.414  16.699  1.00  8.73           C  
ATOM    859  O   GLU A 115       2.441  30.290  17.601  1.00  8.88           O  
ATOM    860  CB  GLU A 115       4.958  28.606  17.082  1.00  9.49           C  
ATOM    861  CG  GLU A 115       4.665  27.904  15.765  1.00  9.98           C  
ATOM    862  CD  GLU A 115       4.532  26.405  15.764  1.00 10.42           C  
ATOM    863  OE1 GLU A 115       5.061  25.718  16.658  1.00 12.19           O  
ATOM    864  OE2 GLU A 115       3.905  25.825  14.830  1.00 10.85           O  
ATOM    865  N   GLY A 116       3.013  30.799  15.457  1.00  9.04           N  
ATOM    866  CA  GLY A 116       1.614  31.036  15.052  1.00  9.53           C  
ATOM    867  C   GLY A 116       0.917  29.704  14.794  1.00  9.48           C  
ATOM    868  O   GLY A 116       1.393  28.637  15.174  1.00  9.55           O  
ATOM    869  N   ALA A 117      -0.274  29.783  14.206  1.00  9.10           N  
ATOM    870  CA  ALA A 117      -1.022  28.575  13.852  1.00  9.73           C  
ATOM    871  C   ALA A 117      -1.380  28.734  12.370  1.00  9.57           C  
ATOM    872  O   ALA A 117      -1.780  29.818  11.944  1.00 10.84           O  
ATOM    873  CB  ALA A 117      -2.243  28.369  14.715  1.00  9.04           C  
ATOM    874  N   GLY A 118      -1.128  27.684  11.609  1.00  9.84           N  
ATOM    875  CA  GLY A 118      -1.339  27.745  10.162  1.00  9.65           C  
ATOM    876  C   GLY A 118      -0.416  28.800   9.571  1.00  9.81           C  
ATOM    877  O   GLY A 118       0.747  28.938   9.981  1.00 10.24           O  
ATOM    878  N   GLY A 119      -0.918  29.540   8.598  1.00  9.33           N  
ATOM    879  CA  GLY A 119      -0.177  30.597   7.938  1.00  8.44           C  
ATOM    880  C   GLY A 119      -0.492  31.972   8.512  1.00  8.14           C  
ATOM    881  O   GLY A 119      -1.074  32.117   9.589  1.00  9.05           O  
ATOM    882  N   TRP A 120      -0.102  33.018   7.793  1.00  6.64           N  
ATOM    883  CA  TRP A 120      -0.231  34.385   8.242  1.00  6.76           C  
ATOM    884  C   TRP A 120      -1.632  34.838   8.637  1.00  6.73           C  
ATOM    885  O   TRP A 120      -1.812  35.422   9.718  1.00  7.87           O  
ATOM    886  CB  TRP A 120       0.357  35.334   7.185  1.00  7.79           C  
ATOM    887  CG  TRP A 120       0.403  36.760   7.623  1.00  7.26           C  
ATOM    888  CD1 TRP A 120      -0.334  37.789   7.095  1.00  7.49           C  
ATOM    889  CD2 TRP A 120       1.200  37.337   8.662  1.00  7.65           C  
ATOM    890  NE1 TRP A 120      -0.041  38.963   7.750  1.00  7.89           N  
ATOM    891  CE2 TRP A 120       0.891  38.705   8.721  1.00  8.08           C  
ATOM    892  CE3 TRP A 120       2.119  36.798   9.570  1.00  6.35           C  
ATOM    893  CZ2 TRP A 120       1.485  39.572   9.637  1.00  7.84           C  
ATOM    894  CZ3 TRP A 120       2.708  37.660  10.469  1.00  6.74           C  
ATOM    895  CH2 TRP A 120       2.390  39.029  10.520  1.00  7.02           C  
ATOM    896  N   PHE A 121      -2.618  34.572   7.783  1.00  6.81           N  
ATOM    897  CA  PHE A 121      -3.963  35.084   8.013  1.00  7.59           C  
ATOM    898  C   PHE A 121      -4.916  34.136   8.700  1.00  8.43           C  
ATOM    899  O   PHE A 121      -6.140  34.346   8.636  1.00 10.39           O  
ATOM    900  CB  PHE A 121      -4.517  35.539   6.656  1.00  7.29           C  
ATOM    901  CG  PHE A 121      -4.142  36.925   6.217  1.00  8.42           C  
ATOM    902  CD1 PHE A 121      -4.286  38.017   7.055  1.00  8.96           C  
ATOM    903  CD2 PHE A 121      -3.660  37.130   4.928  1.00  9.04           C  
ATOM    904  CE1 PHE A 121      -3.948  39.286   6.624  1.00 10.40           C  
ATOM    905  CE2 PHE A 121      -3.319  38.396   4.494  1.00  9.52           C  
ATOM    906  CZ  PHE A 121      -3.463  39.482   5.343  1.00  9.77           C  
ATOM    907  N   THR A 122      -4.456  33.117   9.402  1.00  7.41           N  
ATOM    908  CA  THR A 122      -5.375  32.232  10.124  1.00  7.67           C  
ATOM    909  C   THR A 122      -6.328  33.000  11.022  1.00  7.59           C  
ATOM    910  O   THR A 122      -5.902  33.704  11.938  1.00  7.39           O  
ATOM    911  CB  THR A 122      -4.507  31.294  10.991  1.00  8.22           C  
ATOM    912  OG1 THR A 122      -3.742  30.477  10.095  1.00  8.15           O  
ATOM    913  CG2 THR A 122      -5.380  30.407  11.865  1.00  7.22           C  
ATOM    914  N   PRO A 123      -7.636  32.805  10.850  1.00  6.55           N  
ATOM    915  CA  PRO A 123      -8.615  33.507  11.669  1.00  7.39           C  
ATOM    916  C   PRO A 123      -8.694  33.000  13.105  1.00  7.58           C  
ATOM    917  O   PRO A 123      -8.610  31.794  13.323  1.00  8.61           O  
ATOM    918  CB  PRO A 123      -9.938  33.254  10.955  1.00  6.81           C  
ATOM    919  CG  PRO A 123      -9.547  32.904   9.543  1.00  6.89           C  
ATOM    920  CD  PRO A 123      -8.280  32.072   9.732  1.00  7.04           C  
ATOM    921  N   LEU A 124      -8.890  33.918  14.052  1.00  7.27           N  
ATOM    922  CA  LEU A 124      -9.064  33.580  15.463  1.00  8.15           C  
ATOM    923  C   LEU A 124     -10.506  33.785  15.917  1.00  8.48           C  
ATOM    924  O   LEU A 124     -11.011  33.134  16.843  1.00  7.83           O  
ATOM    925  CB  LEU A 124      -8.091  34.403  16.313  1.00  7.51           C  
ATOM    926  CG  LEU A 124      -6.605  34.113  16.047  1.00  8.05           C  
ATOM    927  CD1 LEU A 124      -5.748  34.969  16.966  1.00  8.12           C  
ATOM    928  CD2 LEU A 124      -6.269  32.641  16.213  1.00  8.27           C  
ATOM    929  N   SER A 125     -11.221  34.658  15.219  1.00  8.84           N  
ATOM    930  CA  SER A 125     -12.644  34.910  15.398  1.00  9.49           C  
ATOM    931  C   SER A 125     -13.183  35.301  14.020  1.00 10.19           C  
ATOM    932  O   SER A 125     -12.391  35.409  13.076  1.00  9.89           O  
ATOM    933  CB  SER A 125     -12.981  36.004  16.404  1.00  9.35           C  
ATOM    934  OG  SER A 125     -12.838  37.309  15.876  1.00  8.78           O  
ATOM    935  N   ASP A 126     -14.469  35.626  13.928  1.00 10.10           N  
ATOM    936  CA  ASP A 126     -15.000  36.093  12.648  1.00 11.96           C  
ATOM    937  C   ASP A 126     -14.552  37.501  12.293  1.00 11.07           C  
ATOM    938  O   ASP A 126     -14.823  37.964  11.170  1.00 11.15           O  
ATOM    939  CB  ASP A 126     -16.532  36.037  12.663  1.00 14.84           C  
ATOM    940  CG  ASP A 126     -17.081  34.632  12.559  1.00 18.46           C  
ATOM    941  OD1 ASP A 126     -16.285  33.672  12.461  1.00 20.75           O  
ATOM    942  OD2 ASP A 126     -18.323  34.474  12.586  1.00 20.47           O  
ATOM    943  N   THR A 127     -13.905  38.262  13.175  1.00 10.02           N  
ATOM    944  CA  THR A 127     -13.435  39.601  12.890  1.00  9.82           C  
ATOM    945  C   THR A 127     -11.968  39.821  13.250  1.00 10.32           C  
ATOM    946  O   THR A 127     -11.507  40.963  13.225  1.00 11.80           O  
ATOM    947  CB  THR A 127     -14.273  40.678  13.623  1.00  9.82           C  
ATOM    948  OG1 THR A 127     -14.112  40.519  15.043  1.00  9.53           O  
ATOM    949  CG2 THR A 127     -15.756  40.622  13.288  1.00 10.38           C  
ATOM    950  N   PHE A 128     -11.243  38.763  13.602  1.00 10.13           N  
ATOM    951  CA  PHE A 128      -9.858  38.922  14.058  1.00 11.28           C  
ATOM    952  C   PHE A 128      -8.997  37.774  13.543  1.00  9.84           C  
ATOM    953  O   PHE A 128      -9.385  36.616  13.680  1.00  9.47           O  
ATOM    954  CB  PHE A 128      -9.855  38.907  15.589  1.00 13.88           C  
ATOM    955  CG  PHE A 128      -8.576  39.251  16.297  1.00 16.95           C  
ATOM    956  CD1 PHE A 128      -8.062  40.533  16.263  1.00 18.27           C  
ATOM    957  CD2 PHE A 128      -7.905  38.287  17.030  1.00 18.49           C  
ATOM    958  CE1 PHE A 128      -6.896  40.854  16.942  1.00 19.31           C  
ATOM    959  CE2 PHE A 128      -6.734  38.594  17.708  1.00 18.74           C  
ATOM    960  CZ  PHE A 128      -6.230  39.876  17.648  1.00 18.88           C  
ATOM    961  N   THR A 129      -7.832  38.108  12.983  1.00  8.92           N  
ATOM    962  CA  THR A 129      -6.938  37.057  12.492  1.00  8.96           C  
ATOM    963  C   THR A 129      -5.657  37.053  13.325  1.00  8.62           C  
ATOM    964  O   THR A 129      -5.342  38.034  14.000  1.00  9.04           O  
ATOM    965  CB  THR A 129      -6.529  37.250  11.023  1.00  8.89           C  
ATOM    966  OG1 THR A 129      -5.682  38.412  10.953  1.00  9.90           O  
ATOM    967  CG2 THR A 129      -7.711  37.425  10.083  1.00  9.19           C  
ATOM    968  N   PHE A 130      -4.838  36.020  13.169  1.00  7.65           N  
ATOM    969  CA  PHE A 130      -3.542  36.000  13.847  1.00  7.25           C  
ATOM    970  C   PHE A 130      -2.703  37.195  13.431  1.00  7.34           C  
ATOM    971  O   PHE A 130      -2.019  37.810  14.257  1.00  7.36           O  
ATOM    972  CB  PHE A 130      -2.822  34.683  13.563  1.00  7.57           C  
ATOM    973  CG  PHE A 130      -2.335  34.000  14.815  1.00  6.89           C  
ATOM    974  CD1 PHE A 130      -1.567  34.698  15.739  1.00  7.43           C  
ATOM    975  CD2 PHE A 130      -2.591  32.659  15.011  1.00  7.98           C  
ATOM    976  CE1 PHE A 130      -1.112  34.054  16.880  1.00  7.93           C  
ATOM    977  CE2 PHE A 130      -2.139  32.008  16.150  1.00  8.53           C  
ATOM    978  CZ  PHE A 130      -1.394  32.718  17.078  1.00  7.81           C  
ATOM    979  N   ALA A 131      -2.772  37.584  12.157  1.00  7.35           N  
ATOM    980  CA  ALA A 131      -2.040  38.739  11.651  1.00  7.42           C  
ATOM    981  C   ALA A 131      -2.376  40.016  12.406  1.00  7.72           C  
ATOM    982  O   ALA A 131      -1.507  40.856  12.647  1.00  8.28           O  
ATOM    983  CB  ALA A 131      -2.311  38.929  10.164  1.00  7.51           C  
ATOM    984  N   ASP A 132      -3.642  40.184  12.797  1.00  7.57           N  
ATOM    985  CA  ASP A 132      -4.042  41.348  13.583  1.00  8.34           C  
ATOM    986  C   ASP A 132      -3.302  41.390  14.915  1.00  7.96           C  
ATOM    987  O   ASP A 132      -2.829  42.464  15.308  1.00  8.29           O  
ATOM    988  CB  ASP A 132      -5.546  41.359  13.831  1.00  8.05           C  
ATOM    989  CG  ASP A 132      -6.394  41.519  12.589  1.00  9.87           C  
ATOM    990  OD1 ASP A 132      -5.969  42.216  11.649  1.00 10.23           O  
ATOM    991  OD2 ASP A 132      -7.490  40.919  12.567  1.00 11.20           O  
ATOM    992  N   TRP A 133      -3.197  40.255  15.596  1.00  7.80           N  
ATOM    993  CA  TRP A 133      -2.487  40.218  16.875  1.00  7.65           C  
ATOM    994  C   TRP A 133      -1.003  40.507  16.715  1.00  8.44           C  
ATOM    995  O   TRP A 133      -0.416  41.289  17.476  1.00  8.08           O  
ATOM    996  CB  TRP A 133      -2.683  38.855  17.548  1.00  8.18           C  
ATOM    997  CG  TRP A 133      -2.048  38.775  18.904  1.00  7.29           C  
ATOM    998  CD1 TRP A 133      -2.520  39.355  20.050  1.00  7.94           C  
ATOM    999  CD2 TRP A 133      -0.839  38.103  19.271  1.00  8.25           C  
ATOM   1000  NE1 TRP A 133      -1.687  39.081  21.100  1.00  8.18           N  
ATOM   1001  CE2 TRP A 133      -0.644  38.303  20.647  1.00  7.72           C  
ATOM   1002  CE3 TRP A 133       0.092  37.331  18.561  1.00  8.39           C  
ATOM   1003  CZ2 TRP A 133       0.449  37.783  21.338  1.00  8.61           C  
ATOM   1004  CZ3 TRP A 133       1.173  36.807  19.248  1.00  8.65           C  
ATOM   1005  CH2 TRP A 133       1.346  37.033  20.624  1.00  8.86           C  
ATOM   1006  N   VAL A 134      -0.356  39.907  15.707  1.00  7.71           N  
ATOM   1007  CA  VAL A 134       1.076  40.143  15.490  1.00  8.58           C  
ATOM   1008  C   VAL A 134       1.323  41.620  15.210  1.00  9.47           C  
ATOM   1009  O   VAL A 134       2.287  42.216  15.702  1.00  9.43           O  
ATOM   1010  CB  VAL A 134       1.631  39.270  14.351  1.00  7.74           C  
ATOM   1011  CG1 VAL A 134       3.140  39.493  14.225  1.00  8.26           C  
ATOM   1012  CG2 VAL A 134       1.341  37.799  14.608  1.00  8.92           C  
ATOM   1013  N   THR A 135       0.427  42.230  14.438  1.00  9.98           N  
ATOM   1014  CA  THR A 135       0.505  43.658  14.137  1.00 11.14           C  
ATOM   1015  C   THR A 135       0.353  44.483  15.404  1.00 12.02           C  
ATOM   1016  O   THR A 135       1.101  45.439  15.643  1.00 12.68           O  
ATOM   1017  CB  THR A 135      -0.560  44.028  13.090  1.00 11.01           C  
ATOM   1018  OG1 THR A 135      -0.322  43.235  11.911  1.00 11.29           O  
ATOM   1019  CG2 THR A 135      -0.472  45.491  12.715  1.00 11.89           C  
ATOM   1020  N   GLN A 136      -0.591  44.132  16.272  1.00 12.50           N  
ATOM   1021  CA  GLN A 136      -0.786  44.829  17.537  1.00 14.80           C  
ATOM   1022  C   GLN A 136       0.465  44.782  18.401  1.00 13.96           C  
ATOM   1023  O   GLN A 136       0.888  45.777  18.998  1.00 12.12           O  
ATOM   1024  CB  GLN A 136      -1.942  44.171  18.308  1.00 18.11           C  
ATOM   1025  CG  GLN A 136      -3.069  45.141  18.603  1.00 23.30           C  
ATOM   1026  CD  GLN A 136      -4.368  44.451  18.967  1.00 26.02           C  
ATOM   1027  OE1 GLN A 136      -4.696  44.332  20.151  1.00 28.36           O  
ATOM   1028  NE2 GLN A 136      -5.104  44.014  17.950  1.00 27.35           N  
ATOM   1029  N   GLU A 137       1.066  43.599  18.507  1.00 13.17           N  
ATOM   1030  CA  GLU A 137       2.265  43.392  19.305  1.00 12.26           C  
ATOM   1031  C   GLU A 137       3.528  43.915  18.636  1.00 12.33           C  
ATOM   1032  O   GLU A 137       4.576  44.025  19.282  1.00 12.83           O  
ATOM   1033  CB  GLU A 137       2.432  41.905  19.636  1.00 13.04           C  
ATOM   1034  CG  GLU A 137       1.440  41.411  20.683  1.00 15.23           C  
ATOM   1035  CD  GLU A 137       1.730  41.922  22.077  1.00 16.68           C  
ATOM   1036  OE1 GLU A 137       2.889  42.281  22.382  1.00 17.30           O  
ATOM   1037  OE2 GLU A 137       0.792  41.991  22.899  1.00 18.62           O  
ATOM   1038  N   GLN A 138       3.487  44.205  17.341  1.00 11.85           N  
ATOM   1039  CA  GLN A 138       4.631  44.719  16.603  1.00 12.28           C  
ATOM   1040  C   GLN A 138       5.827  43.787  16.680  1.00 11.64           C  
ATOM   1041  O   GLN A 138       6.982  44.207  16.834  1.00 12.99           O  
ATOM   1042  CB  GLN A 138       4.995  46.130  17.098  1.00 13.59           C  
ATOM   1043  CG  GLN A 138       3.927  47.161  16.751  1.00 15.03           C  
ATOM   1044  CD  GLN A 138       3.960  47.554  15.290  1.00 17.17           C  
ATOM   1045  OE1 GLN A 138       4.959  48.105  14.804  1.00 18.72           O  
ATOM   1046  NE2 GLN A 138       2.879  47.286  14.566  1.00 17.33           N  
ATOM   1047  N   LEU A 139       5.572  42.484  16.588  1.00 10.63           N  
ATOM   1048  CA  LEU A 139       6.628  41.492  16.645  1.00  9.51           C  
ATOM   1049  C   LEU A 139       7.356  41.363  15.310  1.00  9.94           C  
ATOM   1050  O   LEU A 139       6.722  41.360  14.263  1.00 10.59           O  
ATOM   1051  CB  LEU A 139       6.016  40.110  16.930  1.00 10.33           C  
ATOM   1052  CG  LEU A 139       5.370  39.925  18.304  1.00 10.83           C  
ATOM   1053  CD1 LEU A 139       4.595  38.618  18.349  1.00 10.08           C  
ATOM   1054  CD2 LEU A 139       6.468  39.910  19.358  1.00 13.03           C  
ATOM   1055  N   PRO A 140       8.675  41.221  15.361  1.00 10.29           N  
ATOM   1056  CA  PRO A 140       9.485  40.943  14.182  1.00  9.41           C  
ATOM   1057  C   PRO A 140       9.164  39.514  13.755  1.00  8.53           C  
ATOM   1058  O   PRO A 140       8.966  38.649  14.616  1.00  9.38           O  
ATOM   1059  CB  PRO A 140      10.922  41.075  14.651  1.00 10.15           C  
ATOM   1060  CG  PRO A 140      10.868  41.571  16.049  1.00 11.32           C  
ATOM   1061  CD  PRO A 140       9.499  41.231  16.596  1.00 10.16           C  
ATOM   1062  N   VAL A 141       9.027  39.272  12.452  1.00  7.36           N  
ATOM   1063  CA  VAL A 141       8.551  37.983  11.983  1.00  7.37           C  
ATOM   1064  C   VAL A 141       9.619  37.127  11.310  1.00  6.65           C  
ATOM   1065  O   VAL A 141      10.414  37.647  10.530  1.00  7.62           O  
ATOM   1066  CB  VAL A 141       7.388  38.173  10.984  1.00  7.35           C  
ATOM   1067  CG1 VAL A 141       6.838  36.851  10.475  1.00  8.01           C  
ATOM   1068  CG2 VAL A 141       6.267  39.002  11.627  1.00  6.74           C  
ATOM   1069  N   ILE A 142       9.625  35.838  11.600  1.00  6.39           N  
ATOM   1070  CA  ILE A 142      10.523  34.874  10.969  1.00  6.95           C  
ATOM   1071  C   ILE A 142       9.668  33.967  10.076  1.00  6.93           C  
ATOM   1072  O   ILE A 142       8.673  33.416  10.561  1.00  7.21           O  
ATOM   1073  CB  ILE A 142      11.314  33.991  11.944  1.00  7.59           C  
ATOM   1074  CG1 ILE A 142      12.294  34.864  12.734  1.00  7.52           C  
ATOM   1075  CG2 ILE A 142      12.052  32.876  11.218  1.00  7.60           C  
ATOM   1076  CD1 ILE A 142      12.917  34.143  13.914  1.00  8.13           C  
ATOM   1077  N   LEU A 143      10.004  33.864   8.787  1.00  6.89           N  
ATOM   1078  CA  LEU A 143       9.202  33.049   7.878  1.00  7.43           C  
ATOM   1079  C   LEU A 143       9.797  31.671   7.636  1.00  7.16           C  
ATOM   1080  O   LEU A 143      10.920  31.574   7.144  1.00  9.06           O  
ATOM   1081  CB  LEU A 143       9.055  33.778   6.529  1.00  6.80           C  
ATOM   1082  CG  LEU A 143       8.407  33.000   5.377  1.00  8.31           C  
ATOM   1083  CD1 LEU A 143       6.936  32.722   5.685  1.00  8.42           C  
ATOM   1084  CD2 LEU A 143       8.523  33.788   4.083  1.00  8.78           C  
ATOM   1085  N   VAL A 144       9.045  30.620   7.947  1.00  6.67           N  
ATOM   1086  CA  VAL A 144       9.511  29.264   7.695  1.00  6.43           C  
ATOM   1087  C   VAL A 144       8.987  28.835   6.329  1.00  7.28           C  
ATOM   1088  O   VAL A 144       7.775  28.846   6.086  1.00  7.41           O  
ATOM   1089  CB  VAL A 144       9.109  28.245   8.775  1.00  6.49           C  
ATOM   1090  CG1 VAL A 144       9.631  26.873   8.399  1.00  5.81           C  
ATOM   1091  CG2 VAL A 144       9.672  28.708  10.119  1.00  6.92           C  
ATOM   1092  N   VAL A 145       9.898  28.493   5.426  1.00  7.34           N  
ATOM   1093  CA  VAL A 145       9.527  28.076   4.076  1.00  6.64           C  
ATOM   1094  C   VAL A 145       9.753  26.583   3.917  1.00  7.14           C  
ATOM   1095  O   VAL A 145      10.885  26.085   3.960  1.00  7.15           O  
ATOM   1096  CB  VAL A 145      10.382  28.836   3.031  1.00  6.95           C  
ATOM   1097  CG1 VAL A 145      10.013  28.418   1.610  1.00  8.02           C  
ATOM   1098  CG2 VAL A 145      10.251  30.345   3.196  1.00  8.11           C  
ATOM   1099  N   GLY A 146       8.667  25.835   3.737  1.00  7.42           N  
ATOM   1100  CA  GLY A 146       8.780  24.392   3.470  1.00  7.93           C  
ATOM   1101  C   GLY A 146       9.182  24.296   1.982  1.00  9.17           C  
ATOM   1102  O   GLY A 146       8.455  24.792   1.115  1.00  8.89           O  
ATOM   1103  N   VAL A 147      10.377  23.773   1.714  1.00  9.17           N  
ATOM   1104  CA  VAL A 147      10.848  23.741   0.328  1.00 10.12           C  
ATOM   1105  C   VAL A 147      10.162  22.665  -0.495  1.00 10.01           C  
ATOM   1106  O   VAL A 147      10.406  21.469  -0.383  1.00 11.58           O  
ATOM   1107  CB  VAL A 147      12.378  23.636   0.253  1.00 10.27           C  
ATOM   1108  CG1 VAL A 147      12.857  23.673  -1.196  1.00 11.66           C  
ATOM   1109  CG2 VAL A 147      13.000  24.788   1.040  1.00 10.67           C  
ATOM   1110  N   LYS A 148       9.272  23.136  -1.375  1.00  9.68           N  
ATOM   1111  CA  LYS A 148       8.493  22.273  -2.251  1.00 10.29           C  
ATOM   1112  C   LYS A 148       7.868  23.108  -3.365  1.00  9.57           C  
ATOM   1113  O   LYS A 148       7.907  24.336  -3.315  1.00  9.26           O  
ATOM   1114  CB  LYS A 148       7.407  21.535  -1.470  1.00 11.27           C  
ATOM   1115  CG  LYS A 148       6.385  22.445  -0.811  1.00 11.93           C  
ATOM   1116  CD  LYS A 148       5.456  21.595   0.062  1.00 13.63           C  
ATOM   1117  CE  LYS A 148       4.442  22.454   0.777  1.00 14.67           C  
ATOM   1118  NZ  LYS A 148       3.413  21.636   1.498  1.00 14.05           N  
ATOM   1119  N   LEU A 149       7.332  22.426  -4.377  1.00 10.33           N  
ATOM   1120  CA  LEU A 149       6.720  23.151  -5.492  1.00 10.37           C  
ATOM   1121  C   LEU A 149       5.607  24.051  -4.984  1.00  9.59           C  
ATOM   1122  O   LEU A 149       4.745  23.558  -4.245  1.00 10.35           O  
ATOM   1123  CB  LEU A 149       6.175  22.128  -6.489  1.00 11.76           C  
ATOM   1124  CG  LEU A 149       5.983  22.590  -7.933  1.00 13.45           C  
ATOM   1125  CD1 LEU A 149       7.317  22.781  -8.643  1.00 14.06           C  
ATOM   1126  CD2 LEU A 149       5.123  21.573  -8.679  1.00 14.60           C  
ATOM   1127  N   GLY A 150       5.645  25.325  -5.340  1.00  8.09           N  
ATOM   1128  CA  GLY A 150       4.641  26.281  -4.898  1.00  8.02           C  
ATOM   1129  C   GLY A 150       5.132  27.140  -3.738  1.00  7.33           C  
ATOM   1130  O   GLY A 150       4.524  28.165  -3.418  1.00  7.21           O  
ATOM   1131  N   CYS A 151       6.298  26.816  -3.164  1.00  7.59           N  
ATOM   1132  CA  CYS A 151       6.791  27.593  -2.031  1.00  7.58           C  
ATOM   1133  C   CYS A 151       7.291  28.982  -2.385  1.00  6.70           C  
ATOM   1134  O   CYS A 151       7.258  29.871  -1.525  1.00  6.26           O  
ATOM   1135  CB  CYS A 151       7.836  26.812  -1.232  1.00  7.48           C  
ATOM   1136  SG  CYS A 151       9.493  26.752  -1.962  1.00  8.73           S  
ATOM   1137  N   ILE A 152       7.704  29.208  -3.635  1.00  6.97           N  
ATOM   1138  CA  ILE A 152       8.172  30.542  -4.028  1.00  6.44           C  
ATOM   1139  C   ILE A 152       7.016  31.536  -3.921  1.00  6.60           C  
ATOM   1140  O   ILE A 152       7.095  32.580  -3.271  1.00  6.51           O  
ATOM   1141  CB  ILE A 152       8.793  30.552  -5.434  1.00  6.72           C  
ATOM   1142  CG1 ILE A 152      10.072  29.701  -5.480  1.00  7.42           C  
ATOM   1143  CG2 ILE A 152       9.178  31.971  -5.800  1.00  7.35           C  
ATOM   1144  CD1 ILE A 152      10.534  29.318  -6.869  1.00  8.07           C  
ATOM   1145  N   ASN A 153       5.886  31.194  -4.544  1.00  7.35           N  
ATOM   1146  CA  ASN A 153       4.687  32.024  -4.494  1.00  7.20           C  
ATOM   1147  C   ASN A 153       4.251  32.255  -3.045  1.00  6.22           C  
ATOM   1148  O   ASN A 153       4.030  33.401  -2.675  1.00  6.47           O  
ATOM   1149  CB  ASN A 153       3.554  31.324  -5.254  1.00  7.26           C  
ATOM   1150  CG  ASN A 153       2.215  32.024  -5.115  1.00  5.97           C  
ATOM   1151  OD1 ASN A 153       2.105  33.226  -5.335  1.00  6.33           O  
ATOM   1152  ND2 ASN A 153       1.185  31.248  -4.735  1.00  6.00           N  
ATOM   1153  N   HIS A 154       4.136  31.194  -2.251  1.00  7.29           N  
ATOM   1154  CA  HIS A 154       3.714  31.385  -0.856  1.00  7.16           C  
ATOM   1155  C   HIS A 154       4.672  32.255  -0.059  1.00  7.59           C  
ATOM   1156  O   HIS A 154       4.227  33.096   0.736  1.00  8.14           O  
ATOM   1157  CB  HIS A 154       3.485  30.056  -0.148  1.00  6.75           C  
ATOM   1158  CG  HIS A 154       2.310  29.297  -0.706  1.00  6.90           C  
ATOM   1159  ND1 HIS A 154       2.208  27.942  -0.634  1.00  6.78           N  
ATOM   1160  CD2 HIS A 154       1.192  29.748  -1.332  1.00  7.22           C  
ATOM   1161  CE1 HIS A 154       1.083  27.559  -1.217  1.00  7.72           C  
ATOM   1162  NE2 HIS A 154       0.446  28.642  -1.643  1.00  5.83           N  
ATOM   1163  N   ALA A 155       5.981  32.076  -0.270  1.00  6.92           N  
ATOM   1164  CA  ALA A 155       6.940  32.920   0.452  1.00  7.74           C  
ATOM   1165  C   ALA A 155       6.819  34.380   0.055  1.00  7.73           C  
ATOM   1166  O   ALA A 155       6.826  35.279   0.899  1.00  8.10           O  
ATOM   1167  CB  ALA A 155       8.359  32.399   0.215  1.00  7.26           C  
ATOM   1168  N   MET A 156       6.657  34.665  -1.240  1.00  8.25           N  
ATOM   1169  CA  MET A 156       6.543  36.033  -1.726  1.00  9.68           C  
ATOM   1170  C   MET A 156       5.259  36.710  -1.272  1.00  8.24           C  
ATOM   1171  O   MET A 156       5.256  37.877  -0.880  1.00  8.51           O  
ATOM   1172  CB  MET A 156       6.632  36.024  -3.262  1.00 12.68           C  
ATOM   1173  CG  MET A 156       7.959  35.449  -3.748  1.00 17.35           C  
ATOM   1174  SD  MET A 156       8.258  35.868  -5.485  1.00 23.46           S  
ATOM   1175  CE  MET A 156       7.511  34.457  -6.244  1.00 23.66           C  
ATOM   1176  N   LEU A 157       4.149  35.964  -1.274  1.00  7.61           N  
ATOM   1177  CA  LEU A 157       2.869  36.500  -0.819  1.00  7.44           C  
ATOM   1178  C   LEU A 157       2.986  36.902   0.658  1.00  6.07           C  
ATOM   1179  O   LEU A 157       2.587  37.999   1.052  1.00  6.86           O  
ATOM   1180  CB  LEU A 157       1.739  35.490  -0.960  1.00  7.84           C  
ATOM   1181  CG  LEU A 157       1.282  35.128  -2.386  1.00  8.51           C  
ATOM   1182  CD1 LEU A 157       0.405  33.889  -2.320  1.00  8.96           C  
ATOM   1183  CD2 LEU A 157       0.564  36.314  -3.016  1.00  8.95           C  
ATOM   1184  N   THR A 158       3.508  35.966   1.455  1.00  7.02           N  
ATOM   1185  CA  THR A 158       3.630  36.210   2.896  1.00  6.80           C  
ATOM   1186  C   THR A 158       4.558  37.381   3.175  1.00  7.37           C  
ATOM   1187  O   THR A 158       4.235  38.290   3.948  1.00  7.25           O  
ATOM   1188  CB  THR A 158       4.059  34.937   3.639  1.00  6.65           C  
ATOM   1189  OG1 THR A 158       3.133  33.881   3.307  1.00  7.44           O  
ATOM   1190  CG2 THR A 158       4.014  35.129   5.151  1.00  6.96           C  
ATOM   1191  N   ALA A 159       5.731  37.417   2.543  1.00  7.80           N  
ATOM   1192  CA  ALA A 159       6.655  38.531   2.750  1.00  8.10           C  
ATOM   1193  C   ALA A 159       6.028  39.870   2.372  1.00  8.25           C  
ATOM   1194  O   ALA A 159       6.187  40.859   3.094  1.00  8.65           O  
ATOM   1195  CB  ALA A 159       7.943  38.309   1.969  1.00  8.09           C  
ATOM   1196  N   GLN A 160       5.315  39.944   1.244  1.00  8.58           N  
ATOM   1197  CA  GLN A 160       4.701  41.190   0.825  1.00  9.46           C  
ATOM   1198  C   GLN A 160       3.646  41.680   1.814  1.00  9.15           C  
ATOM   1199  O   GLN A 160       3.647  42.847   2.178  1.00  9.44           O  
ATOM   1200  CB  GLN A 160       4.078  41.092  -0.579  1.00 10.17           C  
ATOM   1201  CG  GLN A 160       3.595  42.461  -1.032  1.00 12.59           C  
ATOM   1202  CD  GLN A 160       3.118  42.566  -2.461  1.00 13.81           C  
ATOM   1203  OE1 GLN A 160       2.001  43.025  -2.728  1.00 14.88           O  
ATOM   1204  NE2 GLN A 160       3.962  42.182  -3.401  1.00 14.58           N  
ATOM   1205  N   VAL A 161       2.797  40.767   2.291  1.00  9.81           N  
ATOM   1206  CA  VAL A 161       1.750  41.174   3.242  1.00 10.12           C  
ATOM   1207  C   VAL A 161       2.322  41.615   4.573  1.00 10.05           C  
ATOM   1208  O   VAL A 161       1.845  42.588   5.169  1.00 10.70           O  
ATOM   1209  CB  VAL A 161       0.726  40.037   3.358  1.00 10.26           C  
ATOM   1210  CG1 VAL A 161      -0.213  40.229   4.531  1.00 13.08           C  
ATOM   1211  CG2 VAL A 161      -0.060  39.936   2.042  1.00 10.51           C  
ATOM   1212  N   ILE A 162       3.377  40.971   5.049  1.00 10.30           N  
ATOM   1213  CA  ILE A 162       4.025  41.362   6.301  1.00 10.01           C  
ATOM   1214  C   ILE A 162       4.563  42.779   6.176  1.00 11.77           C  
ATOM   1215  O   ILE A 162       4.353  43.622   7.040  1.00 11.25           O  
ATOM   1216  CB  ILE A 162       5.152  40.380   6.654  1.00  9.52           C  
ATOM   1217  CG1 ILE A 162       4.580  39.040   7.145  1.00  9.17           C  
ATOM   1218  CG2 ILE A 162       6.087  40.960   7.713  1.00 10.00           C  
ATOM   1219  CD1 ILE A 162       5.599  37.919   7.163  1.00  9.13           C  
ATOM   1220  N   GLN A 163       5.271  43.057   5.080  1.00 13.33           N  
ATOM   1221  CA  GLN A 163       5.843  44.384   4.869  1.00 15.51           C  
ATOM   1222  C   GLN A 163       4.764  45.442   4.741  1.00 16.40           C  
ATOM   1223  O   GLN A 163       4.886  46.542   5.296  1.00 16.24           O  
ATOM   1224  CB  GLN A 163       6.781  44.356   3.661  1.00 17.50           C  
ATOM   1225  CG  GLN A 163       8.020  43.498   3.897  1.00 19.76           C  
ATOM   1226  CD  GLN A 163       9.067  43.691   2.816  1.00 22.21           C  
ATOM   1227  OE1 GLN A 163      10.227  43.996   3.102  1.00 24.11           O  
ATOM   1228  NE2 GLN A 163       8.670  43.509   1.564  1.00 23.10           N  
ATOM   1229  N   HIS A 164       3.626  45.113   4.136  1.00 16.30           N  
ATOM   1230  CA  HIS A 164       2.513  46.058   3.961  1.00 18.19           C  
ATOM   1231  C   HIS A 164       1.962  46.470   5.329  1.00 17.45           C  
ATOM   1232  O   HIS A 164       1.568  47.634   5.545  1.00 18.04           O  
ATOM   1233  CB  HIS A 164       1.405  45.407   3.138  1.00 19.81           C  
ATOM   1234  CG  HIS A 164       1.690  45.439   1.642  1.00 22.66           C  
ATOM   1235  ND1 HIS A 164       2.756  46.159   1.117  1.00 20.00           N  
ATOM   1236  CD2 HIS A 164       1.065  44.854   0.589  1.00 20.00           C  
ATOM   1237  CE1 HIS A 164       2.754  45.996  -0.192  1.00 20.00           C  
ATOM   1238  NE2 HIS A 164       1.752  45.220  -0.523  1.00 20.00           N  
ATOM   1239  N   ALA A 165       1.912  45.527   6.255  1.00 16.25           N  
ATOM   1240  CA  ALA A 165       1.422  45.770   7.603  1.00 15.08           C  
ATOM   1241  C   ALA A 165       2.360  46.663   8.402  1.00 15.08           C  
ATOM   1242  O   ALA A 165       2.040  47.019   9.541  1.00 16.10           O  
ATOM   1243  CB  ALA A 165       1.213  44.446   8.331  1.00 13.37           C  
ATOM   1244  N   GLY A 166       3.533  46.996   7.870  1.00 14.81           N  
ATOM   1245  CA  GLY A 166       4.493  47.848   8.534  1.00 14.27           C  
ATOM   1246  C   GLY A 166       5.373  47.053   9.485  1.00 13.50           C  
ATOM   1247  O   GLY A 166       6.126  47.637  10.266  1.00 13.76           O  
ATOM   1248  N   LEU A 167       5.325  45.723   9.396  1.00 12.22           N  
ATOM   1249  CA  LEU A 167       6.107  44.868  10.266  1.00 11.34           C  
ATOM   1250  C   LEU A 167       7.466  44.540   9.650  1.00 11.80           C  
ATOM   1251  O   LEU A 167       7.622  44.625   8.433  1.00 12.30           O  
ATOM   1252  CB  LEU A 167       5.360  43.552  10.541  1.00 10.98           C  
ATOM   1253  CG  LEU A 167       4.052  43.681  11.326  1.00 11.44           C  
ATOM   1254  CD1 LEU A 167       3.384  42.314  11.395  1.00 11.07           C  
ATOM   1255  CD2 LEU A 167       4.293  44.223  12.726  1.00 11.38           C  
ATOM   1256  N   THR A 168       8.396  44.114  10.490  1.00 11.07           N  
ATOM   1257  CA  THR A 168       9.727  43.731  10.059  1.00 12.12           C  
ATOM   1258  C   THR A 168       9.817  42.230   9.792  1.00 10.46           C  
ATOM   1259  O   THR A 168       9.492  41.423  10.666  1.00 10.84           O  
ATOM   1260  CB  THR A 168      10.783  44.109  11.119  1.00 13.42           C  
ATOM   1261  OG1 THR A 168      10.805  45.545  11.268  1.00 14.94           O  
ATOM   1262  CG2 THR A 168      12.173  43.644  10.710  1.00 14.25           C  
ATOM   1263  N   LEU A 169      10.273  41.867   8.594  1.00 10.56           N  
ATOM   1264  CA  LEU A 169      10.531  40.459   8.280  1.00  9.86           C  
ATOM   1265  C   LEU A 169      11.992  40.228   8.695  1.00 10.32           C  
ATOM   1266  O   LEU A 169      12.905  40.663   7.984  1.00  9.99           O  
ATOM   1267  CB  LEU A 169      10.306  40.127   6.810  1.00 10.15           C  
ATOM   1268  CG  LEU A 169      10.506  38.662   6.417  1.00 10.31           C  
ATOM   1269  CD1 LEU A 169       9.391  37.795   7.001  1.00 11.32           C  
ATOM   1270  CD2 LEU A 169      10.538  38.491   4.900  1.00 10.92           C  
ATOM   1271  N   ALA A 170      12.196  39.661   9.876  1.00  9.13           N  
ATOM   1272  CA  ALA A 170      13.514  39.496  10.469  1.00 10.11           C  
ATOM   1273  C   ALA A 170      14.384  38.444   9.799  1.00  9.48           C  
ATOM   1274  O   ALA A 170      15.619  38.506   9.900  1.00 10.88           O  
ATOM   1275  CB  ALA A 170      13.359  39.124  11.943  1.00 10.23           C  
ATOM   1276  N   GLY A 171      13.774  37.469   9.146  1.00  8.60           N  
ATOM   1277  CA  GLY A 171      14.577  36.432   8.495  1.00  8.55           C  
ATOM   1278  C   GLY A 171      13.673  35.295   8.041  1.00  8.60           C  
ATOM   1279  O   GLY A 171      12.464  35.329   8.260  1.00  8.98           O  
ATOM   1280  N   TRP A 172      14.287  34.319   7.382  1.00  8.28           N  
ATOM   1281  CA  TRP A 172      13.528  33.165   6.910  1.00  8.06           C  
ATOM   1282  C   TRP A 172      14.353  31.908   7.138  1.00  8.02           C  
ATOM   1283  O   TRP A 172      15.583  31.953   7.267  1.00  8.22           O  
ATOM   1284  CB  TRP A 172      13.077  33.282   5.472  1.00  8.27           C  
ATOM   1285  CG  TRP A 172      14.092  33.231   4.380  1.00  8.24           C  
ATOM   1286  CD1 TRP A 172      14.937  34.234   3.987  1.00  8.09           C  
ATOM   1287  CD2 TRP A 172      14.357  32.119   3.511  1.00  8.39           C  
ATOM   1288  NE1 TRP A 172      15.704  33.804   2.929  1.00  7.99           N  
ATOM   1289  CE2 TRP A 172      15.375  32.520   2.618  1.00  7.99           C  
ATOM   1290  CE3 TRP A 172      13.839  30.829   3.398  1.00  8.67           C  
ATOM   1291  CZ2 TRP A 172      15.875  31.664   1.638  1.00  8.96           C  
ATOM   1292  CZ3 TRP A 172      14.331  29.978   2.422  1.00  8.86           C  
ATOM   1293  CH2 TRP A 172      15.348  30.407   1.548  1.00  8.84           C  
ATOM   1294  N   VAL A 173      13.658  30.789   7.259  1.00  7.38           N  
ATOM   1295  CA  VAL A 173      14.306  29.503   7.487  1.00  7.17           C  
ATOM   1296  C   VAL A 173      13.857  28.546   6.384  1.00  7.31           C  
ATOM   1297  O   VAL A 173      12.652  28.441   6.109  1.00  8.19           O  
ATOM   1298  CB  VAL A 173      13.986  28.901   8.864  1.00  6.34           C  
ATOM   1299  CG1 VAL A 173      14.560  27.497   9.035  1.00  7.39           C  
ATOM   1300  CG2 VAL A 173      14.502  29.787  10.001  1.00  6.55           C  
ATOM   1301  N   ALA A 174      14.812  27.888   5.738  1.00  7.23           N  
ATOM   1302  CA  ALA A 174      14.498  26.882   4.731  1.00  7.96           C  
ATOM   1303  C   ALA A 174      14.330  25.538   5.428  1.00  9.07           C  
ATOM   1304  O   ALA A 174      15.205  25.116   6.184  1.00 10.79           O  
ATOM   1305  CB  ALA A 174      15.598  26.797   3.681  1.00  8.74           C  
ATOM   1306  N   ASN A 175      13.189  24.887   5.214  1.00  8.89           N  
ATOM   1307  CA  ASN A 175      12.966  23.586   5.836  1.00  8.61           C  
ATOM   1308  C   ASN A 175      12.757  22.516   4.778  1.00  8.84           C  
ATOM   1309  O   ASN A 175      11.859  22.604   3.936  1.00  8.80           O  
ATOM   1310  CB  ASN A 175      11.779  23.655   6.808  1.00  8.69           C  
ATOM   1311  CG  ASN A 175      11.628  22.359   7.575  1.00  9.84           C  
ATOM   1312  OD1 ASN A 175      12.597  21.845   8.148  1.00 10.34           O  
ATOM   1313  ND2 ASN A 175      10.447  21.756   7.629  1.00 10.79           N  
ATOM   1314  N   ASP A 176      13.645  21.525   4.772  1.00  9.38           N  
ATOM   1315  CA  ASP A 176      13.588  20.429   3.811  1.00 10.61           C  
ATOM   1316  C   ASP A 176      12.596  19.376   4.285  1.00 11.17           C  
ATOM   1317  O   ASP A 176      12.930  18.405   4.961  1.00 11.76           O  
ATOM   1318  CB  ASP A 176      15.003  19.859   3.630  1.00 11.60           C  
ATOM   1319  CG  ASP A 176      15.993  20.899   3.140  1.00 12.75           C  
ATOM   1320  OD1 ASP A 176      15.590  22.006   2.737  1.00 14.27           O  
ATOM   1321  OD2 ASP A 176      17.220  20.629   3.147  1.00 14.18           O  
ATOM   1322  N   VAL A 177      11.330  19.550   3.903  1.00 11.88           N  
ATOM   1323  CA  VAL A 177      10.249  18.666   4.300  1.00 13.07           C  
ATOM   1324  C   VAL A 177      10.340  17.299   3.647  1.00 13.62           C  
ATOM   1325  O   VAL A 177       9.774  16.327   4.154  1.00 15.18           O  
ATOM   1326  CB  VAL A 177       8.870  19.307   4.041  1.00 13.57           C  
ATOM   1327  CG1 VAL A 177       8.617  20.411   5.060  1.00 13.29           C  
ATOM   1328  CG2 VAL A 177       8.760  19.874   2.633  1.00 13.74           C  
ATOM   1329  N   THR A 178      11.021  17.184   2.513  1.00 12.93           N  
ATOM   1330  CA  THR A 178      11.192  15.906   1.831  1.00 14.29           C  
ATOM   1331  C   THR A 178      12.662  15.738   1.445  1.00 14.05           C  
ATOM   1332  O   THR A 178      13.404  16.712   1.461  1.00 14.20           O  
ATOM   1333  CB  THR A 178      10.381  15.801   0.523  1.00 15.00           C  
ATOM   1334  OG1 THR A 178      10.810  16.820  -0.393  1.00 15.93           O  
ATOM   1335  CG2 THR A 178       8.889  15.916   0.762  1.00 15.97           C  
ATOM   1336  N   PRO A 179      13.045  14.520   1.084  1.00 14.98           N  
ATOM   1337  CA  PRO A 179      14.393  14.256   0.617  1.00 15.16           C  
ATOM   1338  C   PRO A 179      14.698  15.166  -0.569  1.00 16.98           C  
ATOM   1339  O   PRO A 179      13.793  15.691  -1.226  1.00 16.38           O  
ATOM   1340  CB  PRO A 179      14.385  12.789   0.219  1.00 14.84           C  
ATOM   1341  CG  PRO A 179      13.237  12.185   0.957  1.00 14.50           C  
ATOM   1342  CD  PRO A 179      12.211  13.299   1.035  1.00 14.56           C  
ATOM   1343  N   PRO A 180      15.978  15.370  -0.838  1.00 18.51           N  
ATOM   1344  CA  PRO A 180      16.460  16.209  -1.909  1.00 19.34           C  
ATOM   1345  C   PRO A 180      15.876  15.889  -3.278  1.00 19.10           C  
ATOM   1346  O   PRO A 180      15.848  14.731  -3.690  1.00 18.67           O  
ATOM   1347  CB  PRO A 180      17.967  15.913  -1.934  1.00 19.43           C  
ATOM   1348  CG  PRO A 180      18.296  15.531  -0.537  1.00 19.72           C  
ATOM   1349  CD  PRO A 180      17.095  14.757  -0.061  1.00 18.95           C  
ATOM   1350  N   GLY A 181      15.433  16.927  -3.972  1.00 18.67           N  
ATOM   1351  CA  GLY A 181      14.924  16.812  -5.325  1.00 18.67           C  
ATOM   1352  C   GLY A 181      15.881  17.517  -6.288  1.00 18.04           C  
ATOM   1353  O   GLY A 181      16.790  18.270  -5.942  1.00 16.96           O  
ATOM   1354  N   LYS A 182      15.628  17.328  -7.569  1.00 18.82           N  
ATOM   1355  CA  LYS A 182      16.356  17.872  -8.682  1.00 17.79           C  
ATOM   1356  C   LYS A 182      16.694  19.349  -8.656  1.00 17.21           C  
ATOM   1357  O   LYS A 182      17.826  19.769  -8.912  1.00 17.65           O  
ATOM   1358  CB  LYS A 182      15.450  17.611  -9.929  1.00 18.41           C  
ATOM   1359  CG  LYS A 182      16.057  18.143 -11.195  1.00 18.37           C  
ATOM   1360  CD  LYS A 182      15.631  17.409 -12.456  1.00 18.59           C  
ATOM   1361  CE  LYS A 182      16.326  18.085 -13.632  1.00 18.57           C  
ATOM   1362  NZ  LYS A 182      15.939  17.500 -14.938  1.00 18.93           N  
ATOM   1363  N   ARG A 183      15.705  20.197  -8.388  1.00 14.92           N  
ATOM   1364  CA  ARG A 183      15.903  21.642  -8.423  1.00 13.64           C  
ATOM   1365  C   ARG A 183      16.044  22.291  -7.057  1.00 12.40           C  
ATOM   1366  O   ARG A 183      15.767  23.484  -6.919  1.00 11.20           O  
ATOM   1367  CB  ARG A 183      14.727  22.269  -9.187  1.00 13.19           C  
ATOM   1368  CG  ARG A 183      14.613  21.798 -10.633  1.00 13.20           C  
ATOM   1369  CD  ARG A 183      15.864  22.102 -11.433  1.00 13.34           C  
ATOM   1370  NE  ARG A 183      15.697  21.717 -12.841  1.00 13.31           N  
ATOM   1371  CZ  ARG A 183      16.608  21.973 -13.774  1.00 13.62           C  
ATOM   1372  NH1 ARG A 183      17.743  22.602 -13.487  1.00 14.93           N  
ATOM   1373  NH2 ARG A 183      16.372  21.581 -15.018  1.00 14.62           N  
ATOM   1374  N   HIS A 184      16.574  21.544  -6.087  1.00 12.73           N  
ATOM   1375  CA  HIS A 184      16.746  22.095  -4.745  1.00 12.75           C  
ATOM   1376  C   HIS A 184      17.625  23.331  -4.718  1.00 12.76           C  
ATOM   1377  O   HIS A 184      17.216  24.354  -4.163  1.00 12.81           O  
ATOM   1378  CB  HIS A 184      17.294  21.020  -3.796  1.00 13.57           C  
ATOM   1379  CG  HIS A 184      17.421  21.589  -2.410  1.00 14.60           C  
ATOM   1380  ND1 HIS A 184      16.469  21.366  -1.443  1.00 16.22           N  
ATOM   1381  CD2 HIS A 184      18.396  22.342  -1.844  1.00 15.57           C  
ATOM   1382  CE1 HIS A 184      16.851  21.970  -0.339  1.00 15.78           C  
ATOM   1383  NE2 HIS A 184      18.013  22.565  -0.544  1.00 16.06           N  
ATOM   1384  N   ALA A 185      18.831  23.276  -5.297  1.00 12.90           N  
ATOM   1385  CA  ALA A 185      19.714  24.439  -5.288  1.00 12.14           C  
ATOM   1386  C   ALA A 185      19.148  25.649  -6.013  1.00 12.05           C  
ATOM   1387  O   ALA A 185      19.252  26.773  -5.510  1.00 12.41           O  
ATOM   1388  CB  ALA A 185      21.086  24.060  -5.850  1.00 13.00           C  
ATOM   1389  N   GLU A 186      18.483  25.467  -7.157  1.00 11.89           N  
ATOM   1390  CA  GLU A 186      17.840  26.555  -7.876  1.00 11.79           C  
ATOM   1391  C   GLU A 186      16.685  27.165  -7.087  1.00 10.08           C  
ATOM   1392  O   GLU A 186      16.466  28.373  -7.167  1.00 10.21           O  
ATOM   1393  CB  GLU A 186      17.320  26.090  -9.241  1.00 13.56           C  
ATOM   1394  CG  GLU A 186      18.425  25.652 -10.173  1.00 16.66           C  
ATOM   1395  CD  GLU A 186      18.716  24.169 -10.155  1.00 17.82           C  
ATOM   1396  OE1 GLU A 186      18.762  23.510  -9.092  1.00 17.95           O  
ATOM   1397  OE2 GLU A 186      18.932  23.648 -11.271  1.00 19.19           O  
ATOM   1398  N   TYR A 187      15.954  26.340  -6.346  1.00  9.06           N  
ATOM   1399  CA  TYR A 187      14.861  26.853  -5.516  1.00  9.55           C  
ATOM   1400  C   TYR A 187      15.436  27.676  -4.379  1.00  8.90           C  
ATOM   1401  O   TYR A 187      15.022  28.810  -4.107  1.00  8.60           O  
ATOM   1402  CB  TYR A 187      14.007  25.682  -4.998  1.00  8.41           C  
ATOM   1403  CG  TYR A 187      12.649  25.687  -5.690  1.00  9.08           C  
ATOM   1404  CD1 TYR A 187      12.511  25.266  -7.000  1.00  8.92           C  
ATOM   1405  CD2 TYR A 187      11.534  26.171  -5.016  1.00  8.66           C  
ATOM   1406  CE1 TYR A 187      11.280  25.291  -7.638  1.00 10.27           C  
ATOM   1407  CE2 TYR A 187      10.303  26.208  -5.651  1.00  9.61           C  
ATOM   1408  CZ  TYR A 187      10.188  25.778  -6.957  1.00  9.67           C  
ATOM   1409  OH  TYR A 187       8.951  25.831  -7.562  1.00 10.00           O  
ATOM   1410  N   MET A 188      16.508  27.177  -3.744  1.00 10.02           N  
ATOM   1411  CA  MET A 188      17.153  27.931  -2.666  1.00 10.52           C  
ATOM   1412  C   MET A 188      17.679  29.275  -3.143  1.00 10.44           C  
ATOM   1413  O   MET A 188      17.537  30.305  -2.469  1.00 10.52           O  
ATOM   1414  CB  MET A 188      18.280  27.088  -2.052  1.00 10.44           C  
ATOM   1415  CG  MET A 188      17.770  25.942  -1.180  1.00 10.81           C  
ATOM   1416  SD  MET A 188      16.859  26.567   0.258  1.00 11.68           S  
ATOM   1417  CE  MET A 188      18.189  27.388   1.150  1.00 10.99           C  
ATOM   1418  N   THR A 189      18.303  29.325  -4.326  1.00  9.32           N  
ATOM   1419  CA  THR A 189      18.815  30.563  -4.888  1.00  9.93           C  
ATOM   1420  C   THR A 189      17.675  31.543  -5.161  1.00  9.05           C  
ATOM   1421  O   THR A 189      17.776  32.720  -4.823  1.00  9.03           O  
ATOM   1422  CB  THR A 189      19.615  30.336  -6.192  1.00 10.59           C  
ATOM   1423  OG1 THR A 189      20.757  29.518  -5.879  1.00 12.10           O  
ATOM   1424  CG2 THR A 189      20.078  31.670  -6.758  1.00 12.12           C  
ATOM   1425  N   THR A 190      16.578  31.049  -5.747  1.00  9.57           N  
ATOM   1426  CA  THR A 190      15.435  31.912  -6.021  1.00  9.61           C  
ATOM   1427  C   THR A 190      14.835  32.479  -4.737  1.00  8.20           C  
ATOM   1428  O   THR A 190      14.580  33.677  -4.643  1.00  9.77           O  
ATOM   1429  CB  THR A 190      14.333  31.171  -6.798  1.00  9.78           C  
ATOM   1430  OG1 THR A 190      14.886  30.679  -8.028  1.00 11.48           O  
ATOM   1431  CG2 THR A 190      13.164  32.093  -7.105  1.00  9.54           C  
ATOM   1432  N   LEU A 191      14.622  31.625  -3.743  1.00  8.65           N  
ATOM   1433  CA  LEU A 191      14.072  32.064  -2.459  1.00  8.63           C  
ATOM   1434  C   LEU A 191      14.978  33.087  -1.784  1.00  8.93           C  
ATOM   1435  O   LEU A 191      14.510  34.104  -1.273  1.00  8.63           O  
ATOM   1436  CB  LEU A 191      13.858  30.874  -1.516  1.00  8.34           C  
ATOM   1437  CG  LEU A 191      12.783  29.868  -1.918  1.00  7.79           C  
ATOM   1438  CD1 LEU A 191      12.873  28.590  -1.109  1.00  7.14           C  
ATOM   1439  CD2 LEU A 191      11.394  30.487  -1.753  1.00  8.07           C  
ATOM   1440  N   THR A 192      16.292  32.839  -1.844  1.00  8.47           N  
ATOM   1441  CA  THR A 192      17.253  33.782  -1.277  1.00  9.37           C  
ATOM   1442  C   THR A 192      17.180  35.142  -1.957  1.00  9.81           C  
ATOM   1443  O   THR A 192      17.212  36.174  -1.281  1.00 10.28           O  
ATOM   1444  CB  THR A 192      18.672  33.191  -1.347  1.00  9.52           C  
ATOM   1445  OG1 THR A 192      18.720  31.933  -0.658  1.00  9.82           O  
ATOM   1446  CG2 THR A 192      19.677  34.129  -0.687  1.00 10.79           C  
ATOM   1447  N   ARG A 193      17.078  35.192  -3.287  1.00 10.83           N  
ATOM   1448  CA  ARG A 193      16.948  36.457  -3.987  1.00 12.49           C  
ATOM   1449  C   ARG A 193      15.650  37.204  -3.678  1.00 12.89           C  
ATOM   1450  O   ARG A 193      15.648  38.432  -3.547  1.00 14.35           O  
ATOM   1451  CB  ARG A 193      16.995  36.251  -5.513  1.00 13.69           C  
ATOM   1452  CG  ARG A 193      16.690  37.528  -6.287  1.00 15.88           C  
ATOM   1453  CD  ARG A 193      16.840  37.385  -7.785  1.00 16.90           C  
ATOM   1454  NE  ARG A 193      15.834  36.513  -8.396  1.00 18.14           N  
ATOM   1455  CZ  ARG A 193      16.109  35.260  -8.750  1.00 17.47           C  
ATOM   1456  NH1 ARG A 193      17.325  34.778  -8.532  1.00 17.72           N  
ATOM   1457  NH2 ARG A 193      15.184  34.490  -9.313  1.00 18.30           N  
ATOM   1458  N   MET A 194      14.542  36.472  -3.651  1.00 12.73           N  
ATOM   1459  CA  MET A 194      13.228  37.079  -3.532  1.00 12.93           C  
ATOM   1460  C   MET A 194      12.761  37.434  -2.138  1.00 12.25           C  
ATOM   1461  O   MET A 194      11.994  38.391  -2.032  1.00 12.93           O  
ATOM   1462  CB  MET A 194      12.198  36.131  -4.184  1.00 14.85           C  
ATOM   1463  CG  MET A 194      12.597  35.809  -5.618  1.00 17.62           C  
ATOM   1464  SD  MET A 194      11.273  35.033  -6.555  1.00 20.25           S  
ATOM   1465  CE  MET A 194      10.709  36.477  -7.477  1.00 22.19           C  
ATOM   1466  N   ILE A 195      13.190  36.712  -1.111  1.00 11.19           N  
ATOM   1467  CA  ILE A 195      12.713  37.039   0.239  1.00 10.00           C  
ATOM   1468  C   ILE A 195      13.594  38.135   0.806  1.00 10.74           C  
ATOM   1469  O   ILE A 195      14.805  37.941   0.935  1.00  9.48           O  
ATOM   1470  CB  ILE A 195      12.731  35.794   1.147  1.00  9.33           C  
ATOM   1471  CG1 ILE A 195      11.826  34.689   0.595  1.00  8.37           C  
ATOM   1472  CG2 ILE A 195      12.288  36.175   2.564  1.00  9.73           C  
ATOM   1473  CD1 ILE A 195      11.977  33.349   1.282  1.00  8.64           C  
ATOM   1474  N   PRO A 196      13.012  39.272   1.169  1.00 10.76           N  
ATOM   1475  CA  PRO A 196      13.749  40.427   1.654  1.00 11.35           C  
ATOM   1476  C   PRO A 196      14.133  40.359   3.120  1.00 10.64           C  
ATOM   1477  O   PRO A 196      13.742  41.168   3.953  1.00 12.76           O  
ATOM   1478  CB  PRO A 196      12.778  41.584   1.403  1.00 11.44           C  
ATOM   1479  CG  PRO A 196      11.430  40.955   1.563  1.00 11.40           C  
ATOM   1480  CD  PRO A 196      11.570  39.579   0.972  1.00 11.40           C  
ATOM   1481  N   ALA A 197      14.893  39.336   3.488  1.00 10.09           N  
ATOM   1482  CA  ALA A 197      15.332  39.103   4.850  1.00  9.43           C  
ATOM   1483  C   ALA A 197      16.416  38.035   4.774  1.00  8.49           C  
ATOM   1484  O   ALA A 197      16.454  37.239   3.826  1.00  9.21           O  
ATOM   1485  CB  ALA A 197      14.160  38.601   5.687  1.00  9.33           C  
ATOM   1486  N   PRO A 198      17.296  38.004   5.759  1.00  8.07           N  
ATOM   1487  CA  PRO A 198      18.359  37.025   5.768  1.00  7.92           C  
ATOM   1488  C   PRO A 198      17.915  35.581   5.938  1.00  7.79           C  
ATOM   1489  O   PRO A 198      17.020  35.275   6.732  1.00  7.29           O  
ATOM   1490  CB  PRO A 198      19.215  37.440   6.972  1.00  8.59           C  
ATOM   1491  CG  PRO A 198      18.252  38.144   7.872  1.00  8.72           C  
ATOM   1492  CD  PRO A 198      17.377  38.931   6.917  1.00  8.37           C  
ATOM   1493  N   LEU A 199      18.573  34.697   5.184  1.00  7.43           N  
ATOM   1494  CA  LEU A 199      18.329  33.263   5.332  1.00  8.31           C  
ATOM   1495  C   LEU A 199      19.049  32.894   6.632  1.00  8.82           C  
ATOM   1496  O   LEU A 199      20.283  33.041   6.709  1.00  9.45           O  
ATOM   1497  CB  LEU A 199      18.898  32.488   4.156  1.00  8.18           C  
ATOM   1498  CG  LEU A 199      19.015  30.968   4.278  1.00  8.00           C  
ATOM   1499  CD1 LEU A 199      17.662  30.342   4.591  1.00  8.23           C  
ATOM   1500  CD2 LEU A 199      19.611  30.378   2.999  1.00  8.94           C  
ATOM   1501  N   LEU A 200      18.322  32.452   7.651  1.00  8.41           N  
ATOM   1502  CA  LEU A 200      18.963  32.138   8.929  1.00  8.53           C  
ATOM   1503  C   LEU A 200      19.578  30.755   8.963  1.00  9.67           C  
ATOM   1504  O   LEU A 200      20.421  30.465   9.821  1.00 11.55           O  
ATOM   1505  CB  LEU A 200      17.948  32.256  10.073  1.00  9.61           C  
ATOM   1506  CG  LEU A 200      17.151  33.559  10.172  1.00  9.59           C  
ATOM   1507  CD1 LEU A 200      16.176  33.470  11.335  1.00 10.33           C  
ATOM   1508  CD2 LEU A 200      18.087  34.748  10.356  1.00 10.17           C  
ATOM   1509  N   GLY A 201      19.176  29.881   8.045  1.00  9.68           N  
ATOM   1510  CA  GLY A 201      19.691  28.517   8.039  1.00  9.54           C  
ATOM   1511  C   GLY A 201      18.723  27.588   7.312  1.00 10.46           C  
ATOM   1512  O   GLY A 201      17.596  27.951   7.004  1.00  9.16           O  
ATOM   1513  N   GLU A 202      19.218  26.387   7.066  1.00 10.73           N  
ATOM   1514  CA  GLU A 202      18.473  25.357   6.364  1.00 10.79           C  
ATOM   1515  C   GLU A 202      18.445  24.070   7.177  1.00 10.16           C  
ATOM   1516  O   GLU A 202      19.500  23.520   7.494  1.00 10.49           O  
ATOM   1517  CB  GLU A 202      19.107  25.097   4.990  1.00 11.25           C  
ATOM   1518  CG  GLU A 202      18.400  23.999   4.222  1.00 13.65           C  
ATOM   1519  CD  GLU A 202      18.864  23.799   2.800  1.00 15.93           C  
ATOM   1520  OE1 GLU A 202      19.716  24.531   2.266  1.00 15.84           O  
ATOM   1521  OE2 GLU A 202      18.327  22.845   2.194  1.00 17.50           O  
ATOM   1522  N   ILE A 203      17.253  23.591   7.485  1.00  8.56           N  
ATOM   1523  CA  ILE A 203      17.104  22.353   8.249  1.00  9.83           C  
ATOM   1524  C   ILE A 203      16.944  21.193   7.278  1.00 10.26           C  
ATOM   1525  O   ILE A 203      16.058  21.224   6.424  1.00 10.08           O  
ATOM   1526  CB  ILE A 203      15.890  22.422   9.194  1.00 10.92           C  
ATOM   1527  CG1 ILE A 203      16.059  23.653  10.090  1.00 12.68           C  
ATOM   1528  CG2 ILE A 203      15.746  21.141   9.999  1.00 10.48           C  
ATOM   1529  CD1 ILE A 203      14.830  24.030  10.870  1.00 13.51           C  
ATOM   1530  N   PRO A 204      17.843  20.226   7.353  1.00 10.44           N  
ATOM   1531  CA  PRO A 204      17.802  19.100   6.441  1.00 11.19           C  
ATOM   1532  C   PRO A 204      16.622  18.182   6.704  1.00 11.20           C  
ATOM   1533  O   PRO A 204      15.964  18.246   7.745  1.00 10.27           O  
ATOM   1534  CB  PRO A 204      19.126  18.377   6.670  1.00 11.99           C  
ATOM   1535  CG  PRO A 204      19.621  18.822   7.987  1.00 11.70           C  
ATOM   1536  CD  PRO A 204      18.946  20.124   8.339  1.00 11.10           C  
ATOM   1537  N   TRP A 205      16.381  17.296   5.733  1.00 12.48           N  
ATOM   1538  CA  TRP A 205      15.308  16.314   5.875  1.00 13.15           C  
ATOM   1539  C   TRP A 205      15.706  15.300   6.942  1.00 15.49           C  
ATOM   1540  O   TRP A 205      16.668  14.543   6.790  1.00 15.45           O  
ATOM   1541  CB  TRP A 205      15.024  15.630   4.534  1.00 13.36           C  
ATOM   1542  CG  TRP A 205      14.013  14.530   4.659  1.00 13.15           C  
ATOM   1543  CD1 TRP A 205      12.679  14.678   4.934  1.00 13.74           C  
ATOM   1544  CD2 TRP A 205      14.237  13.126   4.515  1.00 13.36           C  
ATOM   1545  NE1 TRP A 205      12.068  13.451   4.975  1.00 13.18           N  
ATOM   1546  CE2 TRP A 205      12.999  12.480   4.720  1.00 13.82           C  
ATOM   1547  CE3 TRP A 205      15.366  12.352   4.233  1.00 13.59           C  
ATOM   1548  CZ2 TRP A 205      12.857  11.095   4.655  1.00 14.44           C  
ATOM   1549  CZ3 TRP A 205      15.221  10.979   4.174  1.00 14.23           C  
ATOM   1550  CH2 TRP A 205      13.980  10.359   4.381  1.00 14.53           C  
ATOM   1551  N   LEU A 206      14.989  15.314   8.057  1.00 16.71           N  
ATOM   1552  CA  LEU A 206      15.249  14.427   9.185  1.00 19.89           C  
ATOM   1553  C   LEU A 206      14.008  13.585   9.450  1.00 23.07           C  
ATOM   1554  O   LEU A 206      13.100  14.008  10.170  1.00 23.50           O  
ATOM   1555  CB  LEU A 206      15.615  15.263  10.413  1.00 19.31           C  
ATOM   1556  CG  LEU A 206      16.944  16.029  10.317  1.00 20.04           C  
ATOM   1557  CD1 LEU A 206      16.980  17.186  11.296  1.00 20.09           C  
ATOM   1558  CD2 LEU A 206      18.113  15.086  10.559  1.00 20.81           C  
ATOM   1559  N   ALA A 207      13.936  12.427   8.814  1.00 25.83           N  
ATOM   1560  CA  ALA A 207      12.787  11.543   8.920  1.00 28.11           C  
ATOM   1561  C   ALA A 207      12.298  11.258  10.329  1.00 29.65           C  
ATOM   1562  O   ALA A 207      11.101  11.432  10.600  1.00 31.12           O  
ATOM   1563  CB  ALA A 207      13.119  10.230   8.214  1.00 28.35           C  
ATOM   1564  N   GLU A 208      13.163  10.797  11.225  1.00 31.15           N  
ATOM   1565  CA  GLU A 208      12.759  10.440  12.576  1.00 32.23           C  
ATOM   1566  C   GLU A 208      12.797  11.573  13.587  1.00 31.74           C  
ATOM   1567  O   GLU A 208      13.809  12.211  13.852  1.00 31.74           O  
ATOM   1568  CB  GLU A 208      13.619   9.278  13.101  1.00 34.02           C  
ATOM   1569  CG  GLU A 208      12.928   8.452  14.176  1.00 36.12           C  
ATOM   1570  CD  GLU A 208      13.898   7.607  14.976  1.00 37.71           C  
ATOM   1571  OE1 GLU A 208      14.365   6.572  14.450  1.00 38.64           O  
ATOM   1572  OE2 GLU A 208      14.194   7.972  16.136  1.00 38.60           O  
ATOM   1573  N   ASN A 209      11.642  11.819  14.190  1.00 31.32           N  
ATOM   1574  CA  ASN A 209      11.414  12.823  15.211  1.00 31.01           C  
ATOM   1575  C   ASN A 209      12.327  14.031  15.126  1.00 28.70           C  
ATOM   1576  O   ASN A 209      13.180  14.281  15.980  1.00 29.27           O  
ATOM   1577  CB  ASN A 209      11.515  12.176  16.600  1.00 33.16           C  
ATOM   1578  CG  ASN A 209      10.584  10.989  16.751  1.00 34.85           C  
ATOM   1579  OD1 ASN A 209      10.780   9.945  16.121  1.00 36.13           O  
ATOM   1580  ND2 ASN A 209       9.562  11.126  17.589  1.00 35.73           N  
ATOM   1581  N   PRO A 210      12.065  14.898  14.151  1.00 26.57           N  
ATOM   1582  CA  PRO A 210      12.844  16.105  13.929  1.00 24.76           C  
ATOM   1583  C   PRO A 210      12.695  17.156  15.008  1.00 23.73           C  
ATOM   1584  O   PRO A 210      13.578  17.998  15.205  1.00 23.12           O  
ATOM   1585  CB  PRO A 210      12.371  16.606  12.569  1.00 24.49           C  
ATOM   1586  CG  PRO A 210      11.003  16.044  12.399  1.00 25.13           C  
ATOM   1587  CD  PRO A 210      11.023  14.714  13.104  1.00 25.78           C  
ATOM   1588  N   GLU A 211      11.605  17.125  15.765  1.00 22.99           N  
ATOM   1589  CA  GLU A 211      11.329  18.054  16.846  1.00 22.48           C  
ATOM   1590  C   GLU A 211      12.307  17.898  18.008  1.00 22.34           C  
ATOM   1591  O   GLU A 211      12.575  18.854  18.745  1.00 22.03           O  
ATOM   1592  CB  GLU A 211       9.892  17.871  17.351  1.00 21.49           C  
ATOM   1593  CG  GLU A 211       8.777  18.172  16.376  1.00 21.54           C  
ATOM   1594  CD  GLU A 211       8.465  17.079  15.382  1.00 21.45           C  
ATOM   1595  OE1 GLU A 211       8.999  15.956  15.496  1.00 21.64           O  
ATOM   1596  OE2 GLU A 211       7.671  17.314  14.439  1.00 21.58           O  
ATOM   1597  N   ASN A 212      12.853  16.699  18.184  1.00 22.26           N  
ATOM   1598  CA  ASN A 212      13.818  16.409  19.234  1.00 22.25           C  
ATOM   1599  C   ASN A 212      15.233  16.186  18.714  1.00 21.19           C  
ATOM   1600  O   ASN A 212      16.145  15.848  19.477  1.00 21.88           O  
ATOM   1601  CB  ASN A 212      13.342  15.196  20.043  1.00 23.52           C  
ATOM   1602  CG  ASN A 212      12.063  15.540  20.795  1.00 24.32           C  
ATOM   1603  OD1 ASN A 212      12.030  16.516  21.540  1.00 25.30           O  
ATOM   1604  ND2 ASN A 212      11.031  14.728  20.602  1.00 24.98           N  
ATOM   1605  N   ALA A 213      15.434  16.406  17.419  1.00 18.59           N  
ATOM   1606  CA  ALA A 213      16.766  16.285  16.822  1.00 16.65           C  
ATOM   1607  C   ALA A 213      17.597  17.493  17.231  1.00 14.95           C  
ATOM   1608  O   ALA A 213      17.033  18.553  17.567  1.00 14.49           O  
ATOM   1609  CB  ALA A 213      16.645  16.211  15.302  1.00 15.96           C  
ATOM   1610  N   ALA A 214      18.920  17.341  17.296  1.00 13.42           N  
ATOM   1611  CA  ALA A 214      19.769  18.496  17.641  1.00 12.11           C  
ATOM   1612  C   ALA A 214      19.928  19.321  16.371  1.00 11.84           C  
ATOM   1613  O   ALA A 214      20.787  19.027  15.536  1.00 11.90           O  
ATOM   1614  CB  ALA A 214      21.097  18.024  18.197  1.00 12.22           C  
ATOM   1615  N   THR A 215      19.069  20.319  16.207  1.00  8.94           N  
ATOM   1616  CA  THR A 215      19.007  21.118  14.997  1.00  9.04           C  
ATOM   1617  C   THR A 215      19.433  22.557  15.163  1.00  8.39           C  
ATOM   1618  O   THR A 215      19.497  23.315  14.188  1.00  9.28           O  
ATOM   1619  CB  THR A 215      17.544  21.135  14.481  1.00 10.06           C  
ATOM   1620  OG1 THR A 215      16.695  21.546  15.565  1.00 10.21           O  
ATOM   1621  CG2 THR A 215      17.121  19.756  14.013  1.00 10.43           C  
ATOM   1622  N   GLY A 216      19.786  22.973  16.381  1.00  8.20           N  
ATOM   1623  CA  GLY A 216      20.248  24.345  16.607  1.00  7.98           C  
ATOM   1624  C   GLY A 216      21.456  24.695  15.748  1.00  8.44           C  
ATOM   1625  O   GLY A 216      21.638  25.859  15.351  1.00  8.63           O  
ATOM   1626  N   LYS A 217      22.307  23.717  15.444  1.00  8.08           N  
ATOM   1627  CA  LYS A 217      23.491  23.922  14.621  1.00  9.74           C  
ATOM   1628  C   LYS A 217      23.191  24.436  13.221  1.00  9.38           C  
ATOM   1629  O   LYS A 217      24.082  24.999  12.563  1.00 11.38           O  
ATOM   1630  CB  LYS A 217      24.306  22.624  14.490  1.00 11.04           C  
ATOM   1631  CG  LYS A 217      23.556  21.495  13.792  1.00 12.09           C  
ATOM   1632  CD  LYS A 217      24.359  20.200  13.757  1.00 14.88           C  
ATOM   1633  CE  LYS A 217      25.473  20.267  12.731  1.00 16.78           C  
ATOM   1634  NZ  LYS A 217      26.181  18.960  12.561  1.00 18.72           N  
ATOM   1635  N   TYR A 218      21.975  24.240  12.723  1.00  9.31           N  
ATOM   1636  CA  TYR A 218      21.605  24.698  11.389  1.00  9.78           C  
ATOM   1637  C   TYR A 218      21.182  26.153  11.349  1.00  9.98           C  
ATOM   1638  O   TYR A 218      21.027  26.688  10.245  1.00 11.68           O  
ATOM   1639  CB  TYR A 218      20.468  23.809  10.829  1.00  9.78           C  
ATOM   1640  CG  TYR A 218      20.904  22.356  10.764  1.00 10.15           C  
ATOM   1641  CD1 TYR A 218      21.987  21.996   9.968  1.00 11.12           C  
ATOM   1642  CD2 TYR A 218      20.272  21.361  11.488  1.00 10.85           C  
ATOM   1643  CE1 TYR A 218      22.416  20.688   9.892  1.00 11.44           C  
ATOM   1644  CE2 TYR A 218      20.696  20.042  11.421  1.00 11.16           C  
ATOM   1645  CZ  TYR A 218      21.770  19.712  10.624  1.00 11.20           C  
ATOM   1646  OH  TYR A 218      22.202  18.403  10.550  1.00 11.73           O  
ATOM   1647  N   ILE A 219      21.038  26.815  12.485  1.00  9.58           N  
ATOM   1648  CA  ILE A 219      20.656  28.216  12.548  1.00 10.02           C  
ATOM   1649  C   ILE A 219      21.847  29.094  12.913  1.00 11.12           C  
ATOM   1650  O   ILE A 219      22.569  28.768  13.863  1.00 11.95           O  
ATOM   1651  CB  ILE A 219      19.572  28.408  13.634  1.00  9.46           C  
ATOM   1652  CG1 ILE A 219      18.328  27.582  13.319  1.00  9.58           C  
ATOM   1653  CG2 ILE A 219      19.255  29.885  13.821  1.00  8.46           C  
ATOM   1654  CD1 ILE A 219      17.613  27.948  12.038  1.00  9.75           C  
ATOM   1655  N   ASN A 220      22.040  30.183  12.171  1.00 11.82           N  
ATOM   1656  CA  ASN A 220      23.092  31.140  12.507  1.00 12.19           C  
ATOM   1657  C   ASN A 220      22.410  32.341  13.145  1.00 11.97           C  
ATOM   1658  O   ASN A 220      21.950  33.260  12.463  1.00 12.06           O  
ATOM   1659  CB  ASN A 220      23.903  31.558  11.283  1.00 13.06           C  
ATOM   1660  CG  ASN A 220      24.988  32.565  11.635  1.00 13.99           C  
ATOM   1661  OD1 ASN A 220      25.186  32.912  12.804  1.00 15.05           O  
ATOM   1662  ND2 ASN A 220      25.693  33.040  10.617  1.00 15.95           N  
ATOM   1663  N   LEU A 221      22.346  32.347  14.478  1.00 12.33           N  
ATOM   1664  CA  LEU A 221      21.655  33.401  15.202  1.00 13.80           C  
ATOM   1665  C   LEU A 221      22.254  34.788  15.049  1.00 13.99           C  
ATOM   1666  O   LEU A 221      21.571  35.798  15.281  1.00 14.53           O  
ATOM   1667  CB  LEU A 221      21.547  33.019  16.680  1.00 14.37           C  
ATOM   1668  CG  LEU A 221      20.189  33.268  17.338  1.00 16.00           C  
ATOM   1669  CD1 LEU A 221      19.040  32.677  16.530  1.00 15.58           C  
ATOM   1670  CD2 LEU A 221      20.226  32.691  18.747  1.00 16.47           C  
ATOM   1671  N   ALA A 222      23.510  34.907  14.615  1.00 13.92           N  
ATOM   1672  CA  ALA A 222      24.134  36.206  14.412  1.00 14.78           C  
ATOM   1673  C   ALA A 222      23.556  36.945  13.210  1.00 15.55           C  
ATOM   1674  O   ALA A 222      23.704  38.163  13.102  1.00 16.55           O  
ATOM   1675  CB  ALA A 222      25.646  36.062  14.262  1.00 14.78           C  
ATOM   1676  N   LEU A 223      22.825  36.255  12.335  1.00 14.62           N  
ATOM   1677  CA  LEU A 223      22.144  36.877  11.212  1.00 15.16           C  
ATOM   1678  C   LEU A 223      20.757  37.390  11.580  1.00 15.65           C  
ATOM   1679  O   LEU A 223      20.125  38.101  10.790  1.00 16.65           O  
ATOM   1680  CB  LEU A 223      22.017  35.882  10.051  1.00 14.44           C  
ATOM   1681  CG  LEU A 223      23.282  35.097   9.692  1.00 15.43           C  
ATOM   1682  CD1 LEU A 223      23.021  34.163   8.517  1.00 15.50           C  
ATOM   1683  CD2 LEU A 223      24.438  36.035   9.363  1.00 17.37           C  
ATOM   1684  N   LEU A 224      20.269  37.015  12.761  1.00 14.73           N  
ATOM   1685  CA  LEU A 224      18.936  37.415  13.187  1.00 14.67           C  
ATOM   1686  C   LEU A 224      18.926  38.704  13.969  1.00 15.49           C  
ATOM   1687  O   LEU A 224      19.859  38.989  14.745  1.00 15.87           O  
ATOM   1688  CB  LEU A 224      18.307  36.298  14.030  1.00 14.45           C  
ATOM   1689  CG  LEU A 224      16.908  36.571  14.582  1.00 14.05           C  
ATOM   1690  CD1 LEU A 224      15.933  36.913  13.458  1.00 14.21           C  
ATOM   1691  CD2 LEU A 224      16.403  35.381  15.379  1.00 13.93           C  
ATOM   1692  OXT LEU A 224      17.988  39.520  13.848  1.00 16.32           O  
TER    1693      LEU A 224                                                      
HETATM 1694  P   PO4 A 803      11.480  21.155  -5.358  0.50 17.43           P  
HETATM 1695  O1  PO4 A 803      12.969  21.781  -5.347  0.50 16.44           O  
HETATM 1696  O2  PO4 A 803      11.319  20.311  -6.820  0.50 15.45           O  
HETATM 1697  O3  PO4 A 803      10.513  22.278  -5.265  0.50 15.81           O  
HETATM 1698  O4  PO4 A 803      11.402  20.154  -4.245  0.50 16.41           O  
HETATM 1699 MG    MG A 901       3.337  23.870  14.115  1.00 11.78          MG  
HETATM 1700 MG    MG A 902       1.304  21.531  12.252  1.00 12.00          MG  
HETATM 1701  CA  DPU A 801      -6.435  28.163   8.487  1.00 10.33           C  
HETATM 1702  C   DPU A 801      -6.535  28.310   6.953  1.00 10.43           C  
HETATM 1703  OI1 DPU A 801      -7.280  27.518   6.316  1.00  9.42           O  
HETATM 1704  OI2 DPU A 801      -5.744  29.129   6.437  1.00  9.99           O  
HETATM 1705  CB  DPU A 801      -5.678  26.836   8.757  1.00 11.25           C  
HETATM 1706  CG  DPU A 801      -5.406  26.626  10.251  1.00 13.19           C  
HETATM 1707  CD  DPU A 801      -4.490  25.433  10.605  1.00 12.17           C  
HETATM 1708  CE  DPU A 801      -4.302  25.344  12.148  1.00 14.22           C  
HETATM 1709  CZ  DPU A 801      -3.369  24.248  12.577  1.00 14.34           C  
HETATM 1710  CH  DPU A 801      -3.359  22.841  11.954  1.00 13.66           C  
HETATM 1711  CS  DPU A 801      -4.636  22.100  12.394  1.00 14.03           C  
HETATM 1712  N1  DPU A 801      -3.393  24.339  14.277  1.00 14.43           N  
HETATM 1713  N2  DPU A 801      -2.224  22.079  12.607  1.00 14.03           N  
HETATM 1714  CN1 DPU A 801      -2.134  24.558  14.857  1.00 15.72           C  
HETATM 1715  O12 DPU A 801      -2.204  24.628  16.140  1.00 17.14           O  
HETATM 1716  O2B DPU A 801       1.580  24.912  13.328  1.00 16.36           O  
HETATM 1717  PB  DPU A 801       0.309  24.607  12.715  1.00 18.49           P  
HETATM 1718  O1B DPU A 801      -0.783  25.281  14.032  1.00 16.28           O  
HETATM 1719  O3B DPU A 801       0.073  23.153  12.803  1.00 15.70           O  
HETATM 1720  O2A DPU A 801       0.165  25.221  11.310  1.00 15.41           O  
HETATM 1721  PB  ADP A 802       3.947  23.295  10.910  1.00 12.94           P  
HETATM 1722  O1B ADP A 802       4.095  24.353   9.915  1.00 11.97           O  
HETATM 1723  O2B ADP A 802       2.617  22.645  11.048  1.00 13.01           O  
HETATM 1724  O3B ADP A 802       4.379  23.584  12.419  1.00 12.06           O  
HETATM 1725  PA  ADP A 802       5.802  20.960  11.623  1.00 14.61           P  
HETATM 1726  O1A ADP A 802       4.835  20.414  12.641  1.00 14.60           O  
HETATM 1727  O2A ADP A 802       7.083  21.488  12.159  1.00 13.06           O  
HETATM 1728  O3A ADP A 802       5.026  22.089  10.592  1.00 13.34           O  
HETATM 1729  O5' ADP A 802       6.148  19.831  10.449  1.00 14.65           O  
HETATM 1730  C5' ADP A 802       5.013  19.250   9.700  1.00 15.89           C  
HETATM 1731  C4' ADP A 802       5.269  17.748   9.574  1.00 16.99           C  
HETATM 1732  O4' ADP A 802       6.462  17.566   8.796  1.00 16.49           O  
HETATM 1733  C3' ADP A 802       5.549  17.079  10.918  1.00 17.37           C  
HETATM 1734  O3' ADP A 802       5.081  15.707  10.962  1.00 19.73           O  
HETATM 1735  C2' ADP A 802       7.074  17.133  11.077  1.00 17.26           C  
HETATM 1736  O2' ADP A 802       7.553  16.093  11.957  1.00 17.29           O  
HETATM 1737  C1' ADP A 802       7.517  16.960   9.624  1.00 16.34           C  
HETATM 1738  N9  ADP A 802       8.836  17.691   9.418  1.00 15.35           N  
HETATM 1739  C8  ADP A 802       8.977  19.014   9.517  1.00 15.17           C  
HETATM 1740  N7  ADP A 802      10.201  19.351   9.131  1.00 15.61           N  
HETATM 1741  C5  ADP A 802      10.907  18.252   8.907  1.00 14.99           C  
HETATM 1742  C6  ADP A 802      12.225  18.045   8.488  1.00 14.88           C  
HETATM 1743  N6  ADP A 802      13.073  19.055   8.254  1.00 13.51           N  
HETATM 1744  N1  ADP A 802      12.518  16.797   8.084  1.00 15.44           N  
HETATM 1745  C2  ADP A 802      11.610  15.824   8.066  1.00 15.75           C  
HETATM 1746  N3  ADP A 802      10.410  15.945   8.658  1.00 15.17           N  
HETATM 1747  C4  ADP A 802      10.011  17.198   8.974  1.00 15.44           C  
HETATM 1748  O   HOH A 301       2.067  28.398  -4.518  1.00  6.64           O  
HETATM 1749  O   HOH A 302       9.335  18.936  -0.863  1.00 29.87           O  
HETATM 1750  O   HOH A 304      12.237  19.803   0.854  1.00 17.08           O  
HETATM 1751  O   HOH A 306      13.833  13.324  -5.853  1.00 23.12           O  
HETATM 1752  O   HOH A 307      20.113  18.490   0.095  1.00 23.72           O  
HETATM 1753  O   HOH A 308      18.457  16.303   3.730  1.00 20.81           O  
HETATM 1754  O   HOH A 309      21.280  21.858   6.002  1.00 27.41           O  
HETATM 1755  O   HOH A 310      21.996  25.840   7.761  1.00 15.91           O  
HETATM 1756  O   HOH A 311      21.793  27.954   5.076  1.00 30.67           O  
HETATM 1757  O   HOH A 314      22.806  32.182   1.044  1.00 21.29           O  
HETATM 1758  O   HOH A 315      17.327  36.013   1.494  1.00  8.15           O  
HETATM 1759  O   HOH A 316      22.183  34.473   5.228  1.00 20.53           O  
HETATM 1760  O   HOH A 317      23.085  28.839   8.765  1.00 26.06           O  
HETATM 1761  O   HOH A 321      23.841  30.421  16.074  1.00 15.07           O  
HETATM 1762  O   HOH A 322      26.091  29.738  19.872  1.00 27.70           O  
HETATM 1763  O   HOH A 323      23.805  27.346  16.109  1.00 18.06           O  
HETATM 1764  O   HOH A 325      21.012  21.438  19.445  1.00 21.23           O  
HETATM 1765  O   HOH A 326      21.097  24.141  22.565  1.00 17.64           O  
HETATM 1766  O   HOH A 327      16.176  26.776  24.298  1.00 13.71           O  
HETATM 1767  O   HOH A 329       9.985  24.025  29.657  1.00 15.39           O  
HETATM 1768  O   HOH A 330      -0.642  15.419  31.135  1.00 21.88           O  
HETATM 1769  O   HOH A 331       3.308  21.419  32.526  1.00 20.58           O  
HETATM 1770  O   HOH A 332      -0.197  24.058  33.083  1.00 12.08           O  
HETATM 1771  O   HOH A 338     -12.634  33.428  18.992  1.00 11.00           O  
HETATM 1772  O   HOH A 339     -15.126  32.496  15.424  1.00 19.39           O  
HETATM 1773  O   HOH A 343     -10.840  23.287  24.585  1.00 19.81           O  
HETATM 1774  O   HOH A 344      -7.345  26.036  26.689  1.00 22.57           O  
HETATM 1775  O   HOH A 345     -16.149  30.794  27.528  1.00 12.54           O  
HETATM 1776  O   HOH A 348     -11.282  36.523  10.706  1.00 18.76           O  
HETATM 1777  O   HOH A 349     -11.315  39.070   9.956  1.00 19.31           O  
HETATM 1778  O   HOH A 350      -9.220  40.675  10.324  1.00 27.08           O  
HETATM 1779  O   HOH A 353       1.481  32.467   5.183  1.00  7.49           O  
HETATM 1780  O   HOH A 356      -1.317  41.570   7.535  1.00 11.65           O  
HETATM 1781  O   HOH A 357      -0.845  43.385   5.256  1.00 12.99           O  
HETATM 1782  O   HOH A 358       2.580  48.246  11.850  1.00 24.24           O  
HETATM 1783  O   HOH A 359       0.545  43.693  26.978  1.00 23.67           O  
HETATM 1784  O   HOH A 360      -3.305  42.034  28.033  1.00 19.12           O  
HETATM 1785  O   HOH A 361      -5.063  36.053  31.268  1.00 17.71           O  
HETATM 1786  O   HOH A 362      17.822  38.147  31.467  1.00 24.09           O  
HETATM 1787  O   HOH A 363      20.568  35.255  29.444  1.00 12.07           O  
HETATM 1788  O   HOH A 366       0.468  32.884  31.423  1.00 10.36           O  
HETATM 1789  O   HOH A 367      -0.850  35.185  31.250  1.00 11.64           O  
HETATM 1790  O   HOH A 368      -3.827  37.483  33.364  1.00 25.89           O  
HETATM 1791  O   HOH A 369      -3.122  34.989  29.662  1.00 10.79           O  
HETATM 1792  O   HOH A 370       2.250  32.688  29.446  1.00 12.62           O  
HETATM 1793  O   HOH A 371      -0.220  29.934  18.439  1.00  7.67           O  
HETATM 1794  O   HOH A 372      -1.346  17.523  19.233  1.00 13.69           O  
HETATM 1795  O   HOH A 373       5.674  17.176  20.791  1.00 25.90           O  
HETATM 1796  O   HOH A 376     -11.931  19.385  11.234  1.00 24.04           O  
HETATM 1797  O   HOH A 379      15.380  41.886   7.661  1.00 20.65           O  
HETATM 1798  O   HOH A 380      21.587  27.352  -3.761  1.00 17.98           O  
HETATM 1799  O   HOH A 381      11.352  43.914   6.830  1.00 23.82           O  
HETATM 1800  O   HOH A 383      16.778  40.505  11.597  1.00 17.34           O  
HETATM 1801  O   HOH A 385      18.355  36.582  18.444  1.00 16.34           O  
HETATM 1802  O   HOH A 386      13.149  41.039  18.909  1.00 20.05           O  
HETATM 1803  O   HOH A 388      -3.808  42.702  23.135  1.00 20.53           O  
HETATM 1804  O   HOH A 393      14.152  20.756  15.383  1.00 13.42           O  
HETATM 1805  O   HOH A 395      21.701  28.203   0.605  1.00 24.29           O  
HETATM 1806  O   HOH A 396      22.062  34.218   2.464  1.00 16.33           O  
HETATM 1807  O   HOH A 398     -16.770  32.436  10.287  1.00 24.18           O  
HETATM 1808  O   HOH A 400      -8.403  28.265  27.252  1.00 33.29           O  
HETATM 1809  O   HOH A 402      17.965  29.278  30.953  1.00 25.65           O  
HETATM 1810  O   HOH A 404      -0.240  15.869  22.649  1.00 27.41           O  
HETATM 1811  O   HOH A 406       9.786  43.673  29.493  1.00 25.55           O  
HETATM 1812  O   HOH A 412      -0.058  35.364  11.778  1.00  9.73           O  
HETATM 1813  O   HOH A 416      20.066  29.272  -9.890  1.00 34.45           O  
HETATM 1814  O   HOH A 417      22.058  20.835  -3.503  1.00 35.12           O  
HETATM 1815  O   HOH A 421       5.989  25.872   1.561  1.00 11.48           O  
HETATM 1816  O   HOH A 423       8.759  47.223  11.607  1.00 24.67           O  
HETATM 1817  O   HOH A 425      16.533  22.800  23.715  1.00 33.27           O  
HETATM 1818  O   HOH A 426      -0.290  32.620  12.333  1.00 12.35           O  
HETATM 1819  O   HOH A 427       4.472  29.820  35.927  1.00 36.12           O  
HETATM 1820  O   HOH A 429       2.180  19.613  11.722  1.00 15.19           O  
HETATM 1821  O   HOH A 430      19.832  36.006   2.661  1.00 13.71           O  
HETATM 1822  O   HOH A 432      26.051  26.598  13.597  1.00 56.78           O  
HETATM 1823  O   HOH A 433      -2.900  23.584  32.726  1.00 22.27           O  
HETATM 1824  O   HOH A 434      -0.662  42.335  29.033  1.00 27.45           O  
HETATM 1825  O   HOH A 438      -9.786  43.009  22.377  1.00 29.40           O  
HETATM 1826  O   HOH A 440      23.711  29.706  18.640  1.00 16.20           O  
HETATM 1827  O   HOH A 441       2.924  24.198  -2.189  1.00 10.87           O  
HETATM 1828  O   HOH A 444       2.763  21.721  13.700  1.00 13.96           O  
HETATM 1829  O   HOH A 446     -14.791  40.012   9.541  1.00 24.90           O  
HETATM 1830  O   HOH A 447       4.471  16.489  28.936  1.00 26.76           O  
HETATM 1831  O   HOH A 457      22.700  21.264  17.096  1.00 18.21           O  
HETATM 1832  O   HOH A 460       7.518  42.372  29.479  1.00 23.33           O  
HETATM 1833  O   HOH A 463     -11.958  39.812  21.898  1.00 25.08           O  
HETATM 1834  O   HOH A 466      20.933  23.647   0.021  1.00 19.41           O  
HETATM 1835  O   HOH A 472      21.904  26.240  -1.481  1.00 36.65           O  
HETATM 1836  O   HOH A 474     -18.026  27.180  14.272  1.00 24.50           O  
HETATM 1837  O   HOH A 477       3.841  25.798  -0.165  1.00 14.95           O  
HETATM 1838  O   HOH A 481      22.996  24.484  24.233  1.00 24.63           O  
HETATM 1839  O   HOH A 492       1.370  32.925  34.070  0.50  8.52           O  
HETATM 1840  O   HOH A 493      -6.587  31.069  28.309  1.00 30.29           O  
HETATM 1841  O   HOH A 496     -16.181  31.839  20.503  1.00 26.23           O  
HETATM 1842  O   HOH A 499       0.869  38.879  32.163  1.00 14.73           O  
HETATM 1843  O   HOH A 500      -3.725  32.298  30.318  1.00 14.19           O  
HETATM 1844  O   HOH A 504       6.555  41.039  31.696  1.00 18.08           O  
HETATM 1845  O   HOH A 505       3.206  39.367  33.407  1.00 19.30           O  
HETATM 1846  O   HOH A 506       4.011  32.467  34.804  1.00 22.05           O  
HETATM 1847  O   HOH A 507      -0.630  37.068  33.352  1.00 15.89           O  
HETATM 1848  O   HOH A 511      -8.010  43.901  10.617  1.00 24.69           O  
HETATM 1849  O   HOH A 513      -2.093  43.738   9.886  1.00 19.00           O  
HETATM 1850  O   HOH A 514       7.243  46.580  13.985  1.00 27.53           O  
HETATM 1851  O   HOH A 516      -9.496  39.748  20.445  1.00 17.13           O  
HETATM 1852  O   HOH A 518     -13.157  39.779  26.275  1.00 30.03           O  
HETATM 1853  O   HOH A 521      -2.172  46.180   8.592  1.00 22.10           O  
HETATM 1854  O   HOH A 522      -0.530  47.957   9.741  1.00 30.17           O  
HETATM 1855  O   HOH A 523       7.796  43.922  13.161  1.00 13.44           O  
HETATM 1856  O   HOH A 524      10.087  44.652  14.451  1.00 43.55           O  
HETATM 1857  O   HOH A 526       7.396  47.131   6.538  1.00 32.16           O  
HETATM 1858  O   HOH A 530      20.067  20.562   3.862  1.00 26.03           O  
HETATM 1859  O   HOH A 531      17.690  18.199   1.819  1.00 23.94           O  
HETATM 1860  O   HOH A 532      15.247  18.399   0.515  1.00 22.16           O  
HETATM 1861  O   HOH A 533      20.989  20.745   1.091  1.00 31.21           O  
HETATM 1862  O   HOH A 535      16.861  42.490   5.313  1.00 19.78           O  
HETATM 1863  O   HOH A 536      12.186  14.257  -3.085  1.00 32.05           O  
HETATM 1864  O   HOH A 538      14.454  15.047  -8.663  1.00 17.39           O  
HETATM 1865  O   HOH A 543      17.299  29.330 -12.541  1.00 24.63           O  
HETATM 1866  O   HOH A 544      17.621  29.862  -9.730  1.00 23.61           O  
HETATM 1867  O   HOH A 546      21.170  30.658  -0.273  1.00 19.09           O  
HETATM 1868  O   HOH A 547      22.067  30.152  -2.666  1.00 38.46           O  
HETATM 1869  O   HOH A 551      21.482  26.438   2.858  1.00 21.23           O  
HETATM 1870  O   HOH A 559      -0.103  21.022  10.565  1.00 22.88           O  
HETATM 1871  O   HOH A 560      19.277  22.402  23.559  1.00 33.41           O  
HETATM 1872  O   HOH A 561      20.646  37.341  17.237  1.00 29.83           O  
HETATM 1873  O   HOH A 569      23.663  39.877  20.621  1.00 45.59           O  
HETATM 1874  O   HOH A 580      -8.025  21.166  28.205  1.00 27.56           O  
HETATM 1875  O   HOH A 586       4.041  19.040  16.799  1.00 16.55           O  
HETATM 1876  O   HOH A 587       3.587  19.418  29.758  1.00 23.89           O  
HETATM 1877  O   HOH A 589      11.834  19.991  32.133  1.00 26.12           O  
HETATM 1878  O   HOH A 590      13.723  26.904  34.926  1.00 24.23           O  
HETATM 1879  O   HOH A 595      -4.234  25.256  27.893  1.00 19.76           O  
HETATM 1880  O   HOH A 596     -11.936  31.896  26.302  1.00 17.99           O  
HETATM 1881  O   HOH A 597     -10.590  30.191  27.810  1.00 31.42           O  
HETATM 1882  O   HOH A 598     -10.358  33.998  27.035  1.00 19.09           O  
HETATM 1883  O   HOH A 600     -14.935  18.972  17.917  1.00 24.70           O  
HETATM 1884  O   HOH A 602     -18.787  22.245  24.478  1.00 35.23           O  
HETATM 1885  O   HOH A 604     -18.162  32.289  21.948  1.00 29.41           O  
HETATM 1886  O   HOH A 607      -9.220  41.911  19.123  1.00 27.38           O  
HETATM 1887  O   HOH A 610      15.503  37.072  32.101  1.00 32.95           O  
HETATM 1888  O   HOH A 611      -6.119  40.458   9.253  1.00 23.29           O  
HETATM 1889  O   HOH A 612     -12.782  38.930  18.011  1.00 17.24           O  
HETATM 1890  O   HOH A 614      23.301  17.853  20.711  1.00 26.24           O  
HETATM 1891  O   HOH A 615       7.497  19.567  -4.605  1.00 25.06           O  
HETATM 1892  O   HOH A 616       5.040  20.462   3.507  1.00 15.58           O  
HETATM 1893  O   HOH A 622      12.087  16.278  -8.678  1.00 36.58           O  
HETATM 1894  O   HOH A 624      21.321  28.033  -8.000  1.00 23.69           O  
HETATM 1895  O   HOH A 652       1.866  31.286  11.193  1.00  8.63           O  
HETATM 1896  O   HOH A 653      20.189  18.834  -2.741  1.00 23.58           O  
HETATM 1897  O   HOH A 655       3.048  28.680  -7.218  1.00 13.76           O  
HETATM 1898  O   HOH A 656      17.027  40.451  16.067  1.00 25.94           O  
HETATM 1899  O   HOH A 663      12.713  35.078  -9.353  1.00 33.64           O  
HETATM 1900  O   HOH A 664      21.338  14.023  18.770  1.00 32.49           O  
HETATM 1901  O   HOH A 666      -5.417  10.125  29.231  1.00 25.89           O  
HETATM 1902  O   HOH A 676     -14.649  35.538  19.711  1.00 26.57           O  
HETATM 1903  O   HOH A 679       8.485  41.608  -0.271  1.00 34.93           O  
HETATM 1904  O   HOH A 684       9.612  21.708  31.058  1.00 37.58           O  
HETATM 1905  O   HOH A 685       5.498  14.552  27.326  1.00 31.11           O  
HETATM 1906  O   HOH A 693      14.366  17.693  25.144  1.00 24.32           O  
HETATM 1907  O   HOH A 694       8.700  13.893  21.433  1.00 28.80           O  
HETATM 1908  O   HOH A 700      -8.383  14.745  20.652  1.00 24.14           O  
HETATM 1909  O   HOH A 703     -11.759  41.562  18.386  1.00 21.55           O  
HETATM 1910  O   HOH A 704      -2.747  47.166  15.203  1.00 25.42           O  
HETATM 1911  O   HOH A 706      -8.220  40.935   7.829  1.00 30.31           O  
HETATM 1912  O   HOH A 707      -7.430  45.256  29.533  1.00 32.49           O  
HETATM 1913  O   HOH A 709       3.611  16.666  14.571  1.00 34.21           O  
HETATM 1914  O   HOH A 710       7.332  13.167  10.876  1.00 41.76           O  
HETATM 1915  O   HOH A 711       9.131  13.467   8.995  1.00 32.37           O  
HETATM 1916  O   HOH A 712       7.643  13.830  14.707  1.00 30.79           O  
HETATM 1917  O   HOH A 713       8.972  11.697  13.634  1.00 45.40           O  
HETATM 1918  O   HOH A 714       5.396  18.548  14.453  1.00 17.20           O  
HETATM 1919  O   HOH A 717      -0.547  22.141  16.153  1.00 25.11           O  
HETATM 1920  O   HOH A 719     -11.408  21.493  22.472  1.00 22.38           O  
HETATM 1921  O   HOH A 720     -12.247  20.293  19.673  1.00 35.21           O  
HETATM 1922  O   HOH A 722      -5.396  22.427  28.118  1.00 31.87           O  
HETATM 1923  O   HOH A 723      20.281  14.892  16.508  1.00 17.52           O  
HETATM 1924  O   HOH A 724      26.155  34.742  22.311  1.00 30.03           O  
HETATM 1925  O   HOH A 729      26.274  31.292   8.456  1.00 33.69           O  
HETATM 1926  O   HOH A 731       9.540  17.675  21.138  1.00 25.48           O  
HETATM 1927  O   HOH A 734      20.301  15.501  21.453  1.00 45.02           O  
HETATM 1928  O   HOH A 736       1.903  23.973   1.268  1.00 16.54           O  
HETATM 1929  O   HOH A 737       1.574  21.687   3.781  1.00 27.30           O  
HETATM 1930  O   HOH A 742       0.847  35.557  35.261  1.00 29.11           O  
HETATM 1931  O   HOH A 745       4.114  26.958  38.574  1.00 31.98           O  
HETATM 1932  O   HOH A 746      -3.399  21.040  33.251  1.00 32.21           O  
HETATM 1933  O   HOH A 748       8.977  14.299  17.732  1.00 30.91           O  
HETATM 1934  O   HOH A 751      16.865  42.236  25.108  1.00 28.03           O  
HETATM 1935  O   HOH A 754       0.040  20.297  13.393  1.00 17.39           O  
HETATM 1936  O   HOH A 755      -2.416  20.627  14.946  1.00 23.81           O  
HETATM 1937  O   HOH A 756       2.500  15.787  10.754  1.00 30.29           O  
HETATM 1938  O   HOH A 757      -0.242  41.389  31.508  1.00 22.22           O  
HETATM 1939  O   HOH A 758      16.120  22.778  26.763  1.00 30.79           O  
HETATM 1940  O   HOH A 759      13.326  20.711  28.589  1.00 26.60           O  
HETATM 1941  O   HOH A 760      13.441  22.770  30.006  1.00 32.04           O  
HETATM 1942  O   HOH A 761      16.876  19.095  25.763  1.00 35.32           O  
HETATM 1943  O   HOH A 762      21.222  29.501  27.696  1.00 21.56           O  
HETATM 1944  O   HOH A 763      25.942  24.338  23.385  1.00 26.69           O  
HETATM 1945  O   HOH A 764       5.809  28.696  33.546  1.00 24.87           O  
HETATM 1946  O   HOH A 767     -11.022  21.567   9.352  1.00 18.36           O  
HETATM 1947  O   HOH A 768      13.289  19.148  -8.010  1.00 24.96           O  
HETATM 1948  O   HOH A 769       9.323  18.818  -7.042  1.00 28.74           O  
HETATM 1949  O   HOH A 773     -19.627  22.630  22.028  1.00 24.48           O  
HETATM 1950  O   HOH A 775     -12.951  22.755  27.848  1.00 31.24           O  
HETATM 1951  O   HOH A 778      -3.813  42.308   8.384  1.00 26.42           O  
HETATM 1952  O   HOH A 779       4.519  43.779  -6.180  1.00 32.54           O  
HETATM 1953  O   HOH A 780      -1.904  45.674   5.933  1.00 23.24           O  
HETATM 1954  O   HOH A 781      -4.014  44.869  14.590  1.00 23.51           O  
HETATM 1955  O   HOH A 783       4.001  20.903  -3.615  1.00 24.00           O  
HETATM 1956  O   HOH A 784       6.850  42.335  -2.111  1.00 31.52           O  
HETATM 1957  O   HOH A 788       8.922  38.036  -3.217  1.00 25.72           O  
HETATM 1958  O   HOH A 789       1.491  18.776   3.911  1.00 24.23           O  
HETATM 1959  O   HOH A 790      -0.853  17.436   4.561  1.00 26.72           O  
HETATM 1960  O   HOH A 791      -0.455  13.937  24.911  1.00 25.41           O  
HETATM 1961  O   HOH A 792      13.815  19.540  -3.712  1.00 24.03           O  
HETATM 1962  O   HOH A 793       7.148  21.322  33.013  1.00 26.22           O  
HETATM 1963  O   HOH A 794       1.752  16.716  28.583  1.00 23.41           O  
CONECT  124 1699                                                                
CONECT  393 1699                                                                
CONECT  864 1699                                                                
CONECT 1694 1695 1696 1697 1698                                                 
CONECT 1695 1694                                                                
CONECT 1696 1694                                                                
CONECT 1697 1694                                                                
CONECT 1698 1694                                                                
CONECT 1699  124  393  864 1716                                                 
CONECT 1699 1724 1828                                                           
CONECT 1700 1719 1723 1820 1828                                                 
CONECT 1700 1870 1935                                                           
CONECT 1701 1702 1705                                                           
CONECT 1702 1701 1703 1704                                                      
CONECT 1703 1702                                                                
CONECT 1704 1702                                                                
CONECT 1705 1701 1706                                                           
CONECT 1706 1705 1707                                                           
CONECT 1707 1706 1708                                                           
CONECT 1708 1707 1709                                                           
CONECT 1709 1708 1710 1712                                                      
CONECT 1710 1709 1711 1713                                                      
CONECT 1711 1710                                                                
CONECT 1712 1709 1714                                                           
CONECT 1713 1710                                                                
CONECT 1714 1712 1715 1718                                                      
CONECT 1715 1714                                                                
CONECT 1716 1699 1717                                                           
CONECT 1717 1716 1718 1719 1720                                                 
CONECT 1718 1714 1717                                                           
CONECT 1719 1700 1717                                                           
CONECT 1720 1717                                                                
CONECT 1721 1722 1723 1724 1728                                                 
CONECT 1722 1721                                                                
CONECT 1723 1700 1721                                                           
CONECT 1724 1699 1721                                                           
CONECT 1725 1726 1727 1728 1729                                                 
CONECT 1726 1725                                                                
CONECT 1727 1725                                                                
CONECT 1728 1721 1725                                                           
CONECT 1729 1725 1730                                                           
CONECT 1730 1729 1731                                                           
CONECT 1731 1730 1732 1733                                                      
CONECT 1732 1731 1737                                                           
CONECT 1733 1731 1734 1735                                                      
CONECT 1734 1733                                                                
CONECT 1735 1733 1736 1737                                                      
CONECT 1736 1735                                                                
CONECT 1737 1732 1735 1738                                                      
CONECT 1738 1737 1739 1747                                                      
CONECT 1739 1738 1740                                                           
CONECT 1740 1739 1741                                                           
CONECT 1741 1740 1742 1747                                                      
CONECT 1742 1741 1743 1744                                                      
CONECT 1743 1742                                                                
CONECT 1744 1742 1745                                                           
CONECT 1745 1744 1746                                                           
CONECT 1746 1745 1747                                                           
CONECT 1747 1738 1741 1746                                                      
CONECT 1820 1700                                                                
CONECT 1828 1699 1700                                                           
CONECT 1870 1700                                                                
CONECT 1935 1700                                                                
MASTER      261    0    5   10   10    0   18    6 1962    1   63   18          
END                                                                             
