HEADER    PYROPHOSPHORYLASE                       21-JAN-00   1DY3              
TITLE     TERNARY COMPLEX OF                                                    
TITLE    2 7,8-DIHYDRO-6-HYDROXYMETHYLPTERINPYROPHOSPHOKINASE FROM              
TITLE    3 ESCHERICHIA COLI WITH ATP AND A SUBSTRATE ANALOGUE.                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE:                                                            
COMPND   3  7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-PYROPHOSPHOKINASE;                
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: PPPK, HPPK;                                                 
COMPND   6 EC: 2.7.6.3;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    PYROPHOSPHORYLASE, DE NOVO FOLATE BIOSYNTHESIS                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.K.STAMMERS,A.ACHARI,D.O.SOMERS,P.K.BRYANT,J.ROSEMOND,               
AUTHOR   2 D.L.SCOTT,J.N.CHAMPNESS                                              
REVDAT   3   24-FEB-09 1DY3    1       VERSN                                    
REVDAT   2   20-SEP-00 1DY3    1       COMPND                                   
REVDAT   1   18-AUG-00 1DY3    0                                                
JRNL        AUTH   D.K.STAMMERS,A.ACHARI,D.O.SOMERS,P.K.BRYANT,                 
JRNL        AUTH 2 J.ROSEMOND,D.L.SCOTT,J.N.CHAMPNESS                           
JRNL        TITL   2.0A X-RAY STRUCTURE OF THE TERNARY COMPLEX OF               
JRNL        TITL 2 7,8-DIHYDRO-6-HYDROXYMETHYLPTERINPYROPHOSPHOKINASE           
JRNL        TITL 3 FROM ESCHERICHIA COLI WITH ATP AND A SUBSTRATE               
JRNL        TITL 4 ANALOGUE                                                     
JRNL        REF    FEBS LETT.                    V. 456    49 1999              
JRNL        REFN                   ISSN 0014-5793                               
JRNL        PMID   10452528                                                     
JRNL        DOI    10.1016/S0014-5793(99)00860-1                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.0  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.0                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.0                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 10829                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.165                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1267                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 141                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.3                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.7                           
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) : 0.013 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 0.03  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.027 ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
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) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1DY3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JAN-00.                  
REMARK 100 THE PDBE ID CODE IS EBI-4524.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 290.0                              
REMARK 200  PH                             : 5.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : R-AXIS                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10879                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.10200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 10.600                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       57.74500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       57.74500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       20.48000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       34.50500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       20.48000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       34.50500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       57.74500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       20.48000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       34.50500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       57.74500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       20.48000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       34.50500            
REMARK 290   SMTRY3   8  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 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  27   CA  -  CB  -  CG  ANGL. DEV. =  23.1 DEGREES          
REMARK 500    ARG A  75   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A  82   CD  -  NE  -  CZ  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    ARG A  84   NE  -  CZ  -  NH2 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG A  88   N   -  CA  -  C   ANGL. DEV. =  19.5 DEGREES          
REMARK 500    ARG A 110   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 144   CD  -  NE  -  CZ  ANGL. DEV. =  34.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  10       16.32   -140.87                                   
REMARK 500    SER A  13       79.30     59.65                                   
REMARK 500    ALA A 132       69.68   -151.39                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
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 202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2141   O                                                      
REMARK 620 2 87Y A 201   O16  68.6                                              
REMARK 620 3 ASP A  95   OD2  88.1  98.9                                        
REMARK 620 4 ASP A  97   OD2 104.1 160.3  99.1                                  
REMARK 620 5 ATP A 200   O1G 104.2  76.2 163.6  88.6                            
REMARK 620 6 ATP A 200   O2B 154.9  87.8  87.2 101.0  77.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 203  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  95   OD1                                                    
REMARK 620 2 ASP A  97   OD1  92.9                                              
REMARK 620 3 ATP A 200   O2B  86.8 105.1                                        
REMARK 620 4 HOH A2068   O    89.2  88.4 166.0                                  
REMARK 620 5 HOH A2136   O   169.6  92.7  83.3  99.7                            
REMARK 620 6 ATP A 200   O1A  87.7 176.6  78.2  88.3  87.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD:                                                
REMARK 700 THERE IS A BIFURCATED SHEETS IN THIS STRUCTURE.                      
REMARK 700 THIS IS REPRESENTED BY TWO SHEETS WHICH HAVE ONE OR MORE             
REMARK 700 IDENTICAL STRANDS.                                                   
REMARK 700 SHEETS A AND A1 REPRESENT ONE BIFURCATED SHEET.                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 87Y A 201                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1HKA   RELATED DB: PDB                                   
REMARK 900  6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE                 
DBREF  1DY3 A    1   158  UNP    P26281   HPPK_ECOLI       1    158             
SEQRES   1 A  158  THR VAL ALA TYR ILE ALA ILE GLY SER ASN LEU ALA SER          
SEQRES   2 A  158  PRO LEU GLU GLN VAL ASN ALA ALA LEU LYS ALA LEU GLY          
SEQRES   3 A  158  ASP ILE PRO GLU SER HIS ILE LEU THR VAL SER SER PHE          
SEQRES   4 A  158  TYR ARG THR PRO PRO LEU GLY PRO GLN ASP GLN PRO ASP          
SEQRES   5 A  158  TYR LEU ASN ALA ALA VAL ALA LEU GLU THR SER LEU ALA          
SEQRES   6 A  158  PRO GLU GLU LEU LEU ASN HIS THR GLN ARG ILE GLU LEU          
SEQRES   7 A  158  GLN GLN GLY ARG VAL ARG LYS ALA GLU ARG TRP GLY PRO          
SEQRES   8 A  158  ARG THR LEU ASP LEU ASP ILE MET LEU PHE GLY ASN GLU          
SEQRES   9 A  158  VAL ILE ASN THR GLU ARG LEU THR VAL PRO HIS TYR ASP          
SEQRES  10 A  158  MET LYS ASN ARG GLY PHE MET LEU TRP PRO LEU PHE GLU          
SEQRES  11 A  158  ILE ALA PRO GLU LEU VAL PHE PRO ASP GLY GLU MET LEU          
SEQRES  12 A  158  ARG GLN ILE LEU HIS THR ARG ALA PHE ASP LYS LEU ASN          
SEQRES  13 A  158  LYS TRP                                                      
HET     MG  A 202       1                                                       
HET     MG  A 203       1                                                       
HET    ATP  A 200      31                                                       
HET    87Y  A 201      23                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM     87Y 7,8-DIHYDRO-6-HYDROXYMETHYL-7-METHYL-7-[2-                       
HETNAM   2 87Y  PHENYLETHYL]-PTERIN                                             
HETSYN     87Y 2-AMINO-6-HYDROXYMETHYL-7-METHYL-7-PHENETHYL-7,8-DIHYDRO-3H-     
HETSYN   2 87Y PTERIDIN-4-ONE                                                   
FORMUL   2   MG    2(MG 2+)                                                     
FORMUL   4  ATP    C10 H16 N5 O13 P3                                            
FORMUL   5  87Y    C16 H19 N5 O2                                                
FORMUL   6  HOH   *141(H2 O1)                                                   
HELIX    1   1 SER A   13  ASP A   27  1                                  15    
HELIX    2   2 ALA A   65  GLN A   80  1                                  16    
HELIX    3   3 ASP A  117  ASN A  120  5                                   4    
HELIX    4   4 ARG A  121  ALA A  132  1                                  12    
HELIX    5   5 MET A  142  ALA A  151  1                                  10    
SHEET    1   A 4 SER A  31  VAL A  36  0                                        
SHEET    2   A 4 TYR A  53  THR A  62 -1  O  ALA A  59   N  LEU A  34           
SHEET    3   A 4 VAL A   2  SER A   9 -1  O  ALA A   3   N  LEU A  60           
SHEET    4   A 4 ASP A  95  PHE A 101 -1  O  ASP A  95   N  GLY A   8           
SHEET    1  A1 4 SER A  31  VAL A  36  0                                        
SHEET    2  A1 4 TYR A  53  THR A  62 -1  O  ALA A  59   N  LEU A  34           
SHEET    3  A1 4 TYR A  40  THR A  42 -1  O  TYR A  40   N  ASN A  55           
SHEET    4  A1 4 ASN A 156  LYS A 157 -1  O  ASN A 156   N  ARG A  41           
SHEET    1   B 2 ILE A 106  ASN A 107  0                                        
SHEET    2   B 2 THR A 112  VAL A 113 -1  O  VAL A 113   N  ILE A 106           
LINK        MG    MG A 202                 O   HOH A2141     1555   1555  2.59  
LINK        MG    MG A 202                 O16 87Y A 201     1555   1555  2.63  
LINK        MG    MG A 202                 OD2 ASP A  95     1555   1555  2.50  
LINK        MG    MG A 202                 OD2 ASP A  97     1555   1555  2.44  
LINK        MG    MG A 202                 O1G ATP A 200     1555   1555  2.60  
LINK        MG    MG A 202                 O2B ATP A 200     1555   1555  2.42  
LINK        MG    MG A 203                 OD1 ASP A  97     1555   1555  2.33  
LINK        MG    MG A 203                 O2B ATP A 200     1555   1555  2.36  
LINK        MG    MG A 203                 O   HOH A2068     1555   1555  2.42  
LINK        MG    MG A 203                 O   HOH A2136     1555   1555  2.54  
LINK        MG    MG A 203                 O1A ATP A 200     1555   1555  2.45  
LINK        MG    MG A 203                 OD1 ASP A  95     1555   1555  2.41  
CISPEP   1 VAL A  113    PRO A  114          0        -2.22                     
SITE     1 AC1  6 ASP A  95  ASP A  97  ATP A 200  87Y A 201                    
SITE     2 AC1  6  MG A 203  HOH A2141                                          
SITE     1 AC2  6 ASP A  95  ASP A  97  ATP A 200   MG A 202                    
SITE     2 AC2  6 HOH A2068  HOH A2136                                          
SITE     1 AC3 23 ARG A  82  ARG A  84  ALA A  86  GLU A  87                    
SITE     2 AC3 23 ARG A  88  TRP A  89  ARG A  92  ASP A  95                    
SITE     3 AC3 23 ASP A  97  ILE A  98  ARG A 110  LEU A 111                    
SITE     4 AC3 23 THR A 112  HIS A 115  TYR A 116  ARG A 121                    
SITE     5 AC3 23 87Y A 201   MG A 202   MG A 203  HOH A2136                    
SITE     6 AC3 23 HOH A2138  HOH A2139  HOH A2140                               
SITE     1 AC4 13 THR A  42  PRO A  43  LEU A  45  TYR A  53                    
SITE     2 AC4 13 ASN A  55  TRP A  89  ARG A  92  PHE A 123                    
SITE     3 AC4 13 ATP A 200   MG A 202  HOH A2084  HOH A2103                    
SITE     4 AC4 13 HOH A2141                                                     
CRYST1   40.960   69.010  115.490  90.00  90.00  90.00 C 2 2 21      8          
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      0.024414  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014503  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008659        0.00000                         
ATOM      1  N   THR A   1      43.564  30.909  14.331  1.00 14.06           N  
ATOM      2  CA  THR A   1      42.567  30.020  14.997  1.00 15.17           C  
ATOM      3  C   THR A   1      41.310  29.912  14.154  1.00 14.67           C  
ATOM      4  O   THR A   1      41.002  30.886  13.463  1.00 14.96           O  
ATOM      5  CB  THR A   1      42.238  30.547  16.393  1.00 16.32           C  
ATOM      6  OG1 THR A   1      43.474  30.831  17.090  1.00 16.12           O  
ATOM      7  CG2 THR A   1      41.459  29.555  17.245  1.00 12.32           C  
ATOM      8  N   VAL A   2      40.576  28.800  14.224  1.00 14.44           N  
ATOM      9  CA  VAL A   2      39.330  28.686  13.463  1.00 14.48           C  
ATOM     10  C   VAL A   2      38.166  28.880  14.452  1.00 13.71           C  
ATOM     11  O   VAL A   2      38.106  28.213  15.487  1.00 13.87           O  
ATOM     12  CB  VAL A   2      39.141  27.373  12.719  1.00 19.71           C  
ATOM     13  CG1 VAL A   2      37.778  27.320  12.018  1.00 16.27           C  
ATOM     14  CG2 VAL A   2      40.257  27.152  11.687  1.00 23.80           C  
ATOM     15  N   ALA A   3      37.324  29.849  14.129  1.00 11.77           N  
ATOM     16  CA  ALA A   3      36.175  30.146  14.963  1.00 11.95           C  
ATOM     17  C   ALA A   3      34.911  29.818  14.170  1.00 11.23           C  
ATOM     18  O   ALA A   3      34.872  30.031  12.950  1.00 13.13           O  
ATOM     19  CB  ALA A   3      36.193  31.603  15.400  1.00 15.01           C  
ATOM     20  N   TYR A   4      33.902  29.319  14.855  1.00 10.42           N  
ATOM     21  CA  TYR A   4      32.628  29.025  14.196  1.00  9.98           C  
ATOM     22  C   TYR A   4      31.600  30.038  14.717  1.00  9.33           C  
ATOM     23  O   TYR A   4      31.455  30.161  15.933  1.00  8.50           O  
ATOM     24  CB  TYR A   4      32.174  27.596  14.431  1.00 10.31           C  
ATOM     25  CG  TYR A   4      33.083  26.616  13.727  1.00 12.33           C  
ATOM     26  CD1 TYR A   4      32.868  26.358  12.370  1.00 14.24           C  
ATOM     27  CD2 TYR A   4      34.106  25.959  14.383  1.00 14.38           C  
ATOM     28  CE1 TYR A   4      33.668  25.469  11.689  1.00 16.04           C  
ATOM     29  CE2 TYR A   4      34.915  25.050  13.706  1.00 13.72           C  
ATOM     30  CZ  TYR A   4      34.680  24.813  12.380  1.00 15.99           C  
ATOM     31  OH  TYR A   4      35.462  23.935  11.651  1.00 17.45           O  
ATOM     32  N   ILE A   5      30.990  30.761  13.816  1.00  9.57           N  
ATOM     33  CA  ILE A   5      30.028  31.800  14.168  1.00  9.49           C  
ATOM     34  C   ILE A   5      28.622  31.442  13.707  1.00 11.03           C  
ATOM     35  O   ILE A   5      28.440  31.049  12.557  1.00  9.40           O  
ATOM     36  CB  ILE A   5      30.490  33.130  13.556  1.00 11.21           C  
ATOM     37  CG1 ILE A   5      31.809  33.586  14.239  1.00 16.61           C  
ATOM     38  CG2 ILE A   5      29.429  34.216  13.675  1.00 11.44           C  
ATOM     39  CD1 ILE A   5      32.513  34.698  13.485  1.00 22.97           C  
ATOM     40  N   ALA A   6      27.635  31.596  14.593  1.00  9.31           N  
ATOM     41  CA  ALA A   6      26.253  31.346  14.206  1.00 10.52           C  
ATOM     42  C   ALA A   6      25.614  32.686  13.796  1.00 10.00           C  
ATOM     43  O   ALA A   6      25.877  33.695  14.438  1.00  8.60           O  
ATOM     44  CB  ALA A   6      25.436  30.721  15.313  1.00  9.66           C  
ATOM     45  N   ILE A   7      24.790  32.681  12.767  1.00  9.13           N  
ATOM     46  CA  ILE A   7      24.121  33.900  12.328  1.00 10.58           C  
ATOM     47  C   ILE A   7      22.612  33.727  12.418  1.00 11.51           C  
ATOM     48  O   ILE A   7      22.096  32.680  12.028  1.00  9.83           O  
ATOM     49  CB  ILE A   7      24.478  34.278  10.885  1.00 12.54           C  
ATOM     50  CG1 ILE A   7      26.006  34.399  10.731  1.00 10.31           C  
ATOM     51  CG2 ILE A   7      23.767  35.576  10.501  1.00 10.67           C  
ATOM     52  CD1 ILE A   7      26.451  34.597   9.287  1.00 13.08           C  
ATOM     53  N   GLY A   8      21.932  34.718  12.992  1.00 12.50           N  
ATOM     54  CA  GLY A   8      20.469  34.640  13.082  1.00 12.02           C  
ATOM     55  C   GLY A   8      19.889  36.020  12.737  1.00 12.24           C  
ATOM     56  O   GLY A   8      20.485  37.036  13.092  1.00 12.25           O  
ATOM     57  N   SER A   9      18.726  36.041  12.100  1.00 11.43           N  
ATOM     58  CA  SER A   9      18.028  37.278  11.779  1.00  9.13           C  
ATOM     59  C   SER A   9      16.541  36.996  11.533  1.00 10.36           C  
ATOM     60  O   SER A   9      16.251  36.027  10.808  1.00  7.81           O  
ATOM     61  CB  SER A   9      18.619  37.954  10.546  1.00  8.01           C  
ATOM     62  OG  SER A   9      17.831  39.077  10.136  1.00  8.88           O  
ATOM     63  N   ASN A  10      15.644  37.812  12.079  1.00 10.96           N  
ATOM     64  CA  ASN A  10      14.221  37.575  11.773  1.00 12.09           C  
ATOM     65  C   ASN A  10      13.503  38.917  11.587  1.00 13.56           C  
ATOM     66  O   ASN A  10      12.287  38.979  11.619  1.00 12.74           O  
ATOM     67  CB  ASN A  10      13.532  36.732  12.828  1.00  7.98           C  
ATOM     68  CG  ASN A  10      13.343  37.335  14.178  1.00 10.87           C  
ATOM     69  OD1 ASN A  10      14.060  38.236  14.633  1.00 10.27           O  
ATOM     70  ND2 ASN A  10      12.314  36.818  14.880  1.00 10.53           N  
ATOM     71  N   LEU A  11      14.265  40.000  11.388  1.00 12.78           N  
ATOM     72  CA  LEU A  11      13.676  41.303  11.196  1.00 14.03           C  
ATOM     73  C   LEU A  11      14.406  42.063  10.073  1.00 15.26           C  
ATOM     74  O   LEU A  11      15.577  41.843   9.783  1.00 13.48           O  
ATOM     75  CB  LEU A  11      13.735  42.223  12.409  1.00 12.73           C  
ATOM     76  CG  LEU A  11      12.997  41.959  13.685  1.00 15.29           C  
ATOM     77  CD1 LEU A  11      13.305  42.978  14.782  1.00 18.72           C  
ATOM     78  CD2 LEU A  11      11.470  41.969  13.418  1.00 17.63           C  
ATOM     79  N   ALA A  12      13.644  42.985   9.508  1.00 15.69           N  
ATOM     80  CA  ALA A  12      14.122  43.900   8.483  1.00 13.93           C  
ATOM     81  C   ALA A  12      14.833  43.216   7.326  1.00 13.26           C  
ATOM     82  O   ALA A  12      15.953  43.579   6.965  1.00 13.66           O  
ATOM     83  CB  ALA A  12      15.026  44.919   9.206  1.00 15.36           C  
ATOM     84  N   SER A  13      14.131  42.303   6.665  1.00 11.42           N  
ATOM     85  CA  SER A  13      14.603  41.531   5.526  1.00 11.84           C  
ATOM     86  C   SER A  13      15.838  40.693   5.877  1.00 10.70           C  
ATOM     87  O   SER A  13      16.973  41.064   5.571  1.00 10.79           O  
ATOM     88  CB  SER A  13      14.930  42.434   4.325  1.00 19.45           C  
ATOM     89  OG  SER A  13      13.792  43.224   4.010  1.00 26.44           O  
ATOM     90  N   PRO A  14      15.615  39.567   6.530  1.00  9.12           N  
ATOM     91  CA  PRO A  14      16.700  38.694   6.986  1.00  9.81           C  
ATOM     92  C   PRO A  14      17.721  38.333   5.938  1.00  9.34           C  
ATOM     93  O   PRO A  14      18.932  38.315   6.271  1.00 10.57           O  
ATOM     94  CB  PRO A  14      15.970  37.475   7.541  1.00  9.94           C  
ATOM     95  CG  PRO A  14      14.655  38.042   8.036  1.00 10.35           C  
ATOM     96  CD  PRO A  14      14.288  39.058   6.958  1.00  9.66           C  
ATOM     97  N   LEU A  15      17.336  38.077   4.682  1.00  9.27           N  
ATOM     98  CA  LEU A  15      18.312  37.759   3.654  1.00  9.82           C  
ATOM     99  C   LEU A  15      19.278  38.930   3.404  1.00 10.95           C  
ATOM    100  O   LEU A  15      20.489  38.712   3.230  1.00  8.20           O  
ATOM    101  CB  LEU A  15      17.663  37.374   2.319  1.00  8.42           C  
ATOM    102  CG  LEU A  15      18.629  36.994   1.203  1.00  9.33           C  
ATOM    103  CD1 LEU A  15      19.639  35.914   1.649  1.00 10.22           C  
ATOM    104  CD2 LEU A  15      17.896  36.477  -0.021  1.00 13.51           C  
ATOM    105  N   GLU A  16      18.774  40.154   3.369  1.00 10.64           N  
ATOM    106  CA  GLU A  16      19.648  41.315   3.196  1.00 12.03           C  
ATOM    107  C   GLU A  16      20.562  41.489   4.397  1.00 11.38           C  
ATOM    108  O   GLU A  16      21.738  41.819   4.310  1.00 11.32           O  
ATOM    109  CB  GLU A  16      18.826  42.597   2.976  1.00 14.48           C  
ATOM    110  CG  GLU A  16      18.005  42.585   1.681  1.00 16.57           C  
ATOM    111  CD  GLU A  16      17.202  43.884   1.540  1.00 22.75           C  
ATOM    112  OE1 GLU A  16      17.761  44.978   1.718  1.00 24.59           O  
ATOM    113  OE2 GLU A  16      15.998  43.783   1.248  1.00 25.47           O  
ATOM    114  N   GLN A  17      20.013  41.254   5.595  1.00 11.07           N  
ATOM    115  CA  GLN A  17      20.788  41.371   6.825  1.00 11.97           C  
ATOM    116  C   GLN A  17      21.962  40.376   6.849  1.00 12.34           C  
ATOM    117  O   GLN A  17      23.083  40.727   7.231  1.00 12.03           O  
ATOM    118  CB  GLN A  17      19.906  41.151   8.034  1.00 12.17           C  
ATOM    119  CG  GLN A  17      18.785  42.161   8.277  1.00 11.01           C  
ATOM    120  CD  GLN A  17      19.303  43.559   8.554  1.00 20.95           C  
ATOM    121  OE1 GLN A  17      20.456  43.810   8.908  1.00 14.77           O  
ATOM    122  NE2 GLN A  17      18.419  44.551   8.398  1.00 18.37           N  
ATOM    123  N   VAL A  18      21.695  39.155   6.451  1.00 10.92           N  
ATOM    124  CA  VAL A  18      22.717  38.101   6.475  1.00 10.64           C  
ATOM    125  C   VAL A  18      23.719  38.313   5.356  1.00 10.75           C  
ATOM    126  O   VAL A  18      24.913  38.148   5.643  1.00 11.27           O  
ATOM    127  CB  VAL A  18      22.074  36.712   6.421  1.00 12.97           C  
ATOM    128  CG1 VAL A  18      23.128  35.609   6.338  1.00 13.00           C  
ATOM    129  CG2 VAL A  18      21.211  36.516   7.663  1.00 10.76           C  
ATOM    130  N   ASN A  19      23.306  38.729   4.158  1.00 11.36           N  
ATOM    131  CA  ASN A  19      24.293  38.978   3.103  1.00 11.42           C  
ATOM    132  C   ASN A  19      25.188  40.149   3.526  1.00 10.82           C  
ATOM    133  O   ASN A  19      26.396  40.068   3.275  1.00 12.20           O  
ATOM    134  CB  ASN A  19      23.681  39.237   1.723  1.00  8.17           C  
ATOM    135  CG  ASN A  19      23.267  37.961   1.009  1.00 19.15           C  
ATOM    136  OD1 ASN A  19      22.488  37.950   0.044  1.00 17.67           O  
ATOM    137  ND2 ASN A  19      23.806  36.821   1.418  1.00 10.42           N  
ATOM    138  N   ALA A  20      24.655  41.165   4.167  1.00 11.22           N  
ATOM    139  CA  ALA A  20      25.444  42.297   4.628  1.00 12.49           C  
ATOM    140  C   ALA A  20      26.404  41.864   5.730  1.00 12.41           C  
ATOM    141  O   ALA A  20      27.560  42.293   5.740  1.00 12.54           O  
ATOM    142  CB  ALA A  20      24.549  43.428   5.138  1.00 11.91           C  
ATOM    143  N   ALA A  21      25.948  41.005   6.643  1.00 10.06           N  
ATOM    144  CA  ALA A  21      26.765  40.502   7.715  1.00 11.67           C  
ATOM    145  C   ALA A  21      27.952  39.688   7.180  1.00 10.43           C  
ATOM    146  O   ALA A  21      29.047  39.813   7.744  1.00 11.92           O  
ATOM    147  CB  ALA A  21      25.921  39.643   8.678  1.00  8.79           C  
ATOM    148  N   LEU A  22      27.760  38.890   6.146  1.00 10.04           N  
ATOM    149  CA  LEU A  22      28.836  38.104   5.551  1.00 11.58           C  
ATOM    150  C   LEU A  22      29.942  38.992   4.990  1.00 13.76           C  
ATOM    151  O   LEU A  22      31.134  38.681   5.154  1.00 12.55           O  
ATOM    152  CB  LEU A  22      28.275  37.181   4.457  1.00 15.36           C  
ATOM    153  CG  LEU A  22      27.378  36.055   5.023  1.00 16.21           C  
ATOM    154  CD1 LEU A  22      26.774  35.261   3.872  1.00 22.63           C  
ATOM    155  CD2 LEU A  22      28.151  35.158   5.956  1.00 19.71           C  
ATOM    156  N   LYS A  23      29.563  40.083   4.333  1.00 12.85           N  
ATOM    157  CA  LYS A  23      30.508  41.055   3.841  1.00 14.82           C  
ATOM    158  C   LYS A  23      31.295  41.705   4.993  1.00 14.41           C  
ATOM    159  O   LYS A  23      32.514  41.831   4.869  1.00 15.57           O  
ATOM    160  CB  LYS A  23      29.906  42.233   3.069  1.00 18.18           C  
ATOM    161  CG  LYS A  23      29.875  42.217   1.602  1.00 33.00           C  
ATOM    162  CD  LYS A  23      28.961  41.311   0.858  1.00 39.76           C  
ATOM    163  CE  LYS A  23      29.192  41.408  -0.653  1.00 41.82           C  
ATOM    164  NZ  LYS A  23      30.561  40.899  -0.993  1.00 47.85           N  
ATOM    165  N   ALA A  24      30.583  42.147   6.021  1.00 13.29           N  
ATOM    166  CA  ALA A  24      31.239  42.769   7.168  1.00 14.75           C  
ATOM    167  C   ALA A  24      32.144  41.785   7.892  1.00 14.93           C  
ATOM    168  O   ALA A  24      33.216  42.157   8.393  1.00 13.47           O  
ATOM    169  CB  ALA A  24      30.169  43.326   8.114  1.00 12.08           C  
ATOM    170  N   LEU A  25      31.734  40.502   7.988  1.00 14.57           N  
ATOM    171  CA  LEU A  25      32.583  39.507   8.654  1.00 14.02           C  
ATOM    172  C   LEU A  25      33.911  39.328   7.912  1.00 15.72           C  
ATOM    173  O   LEU A  25      34.961  39.161   8.535  1.00 14.18           O  
ATOM    174  CB  LEU A  25      31.895  38.157   8.780  1.00 14.97           C  
ATOM    175  CG  LEU A  25      30.839  37.973   9.856  1.00 16.08           C  
ATOM    176  CD1 LEU A  25      30.152  36.625   9.710  1.00 20.85           C  
ATOM    177  CD2 LEU A  25      31.449  38.094  11.254  1.00 16.68           C  
ATOM    178  N   GLY A  26      33.855  39.370   6.585  1.00 17.01           N  
ATOM    179  CA  GLY A  26      35.018  39.263   5.730  1.00 19.60           C  
ATOM    180  C   GLY A  26      35.942  40.474   5.897  1.00 20.72           C  
ATOM    181  O   GLY A  26      37.142  40.381   5.664  1.00 23.15           O  
ATOM    182  N   ASP A  27      35.420  41.589   6.338  1.00 19.54           N  
ATOM    183  CA  ASP A  27      36.146  42.845   6.559  1.00 20.54           C  
ATOM    184  C   ASP A  27      36.819  42.895   7.920  1.00 19.63           C  
ATOM    185  O   ASP A  27      37.601  43.846   8.150  1.00 18.56           O  
ATOM    186  CB  ASP A  27      35.110  43.907   6.353  1.00 32.62           C  
ATOM    187  CG  ASP A  27      35.082  45.354   6.313  1.00 47.13           C  
ATOM    188  OD1 ASP A  27      36.114  46.071   6.319  1.00 52.35           O  
ATOM    189  OD2 ASP A  27      33.949  45.956   6.234  1.00 52.12           O  
ATOM    190  N   ILE A  28      36.596  41.946   8.833  1.00 15.80           N  
ATOM    191  CA  ILE A  28      37.284  42.006  10.143  1.00 15.94           C  
ATOM    192  C   ILE A  28      38.775  41.860   9.925  1.00 16.54           C  
ATOM    193  O   ILE A  28      39.201  40.994   9.145  1.00 14.97           O  
ATOM    194  CB  ILE A  28      36.733  40.929  11.093  1.00 18.90           C  
ATOM    195  CG1 ILE A  28      35.253  41.247  11.409  1.00 16.02           C  
ATOM    196  CG2 ILE A  28      37.512  40.786  12.395  1.00  9.94           C  
ATOM    197  CD1 ILE A  28      34.539  40.166  12.195  1.00 17.54           C  
ATOM    198  N   PRO A  29      39.600  42.651  10.597  1.00 16.96           N  
ATOM    199  CA  PRO A  29      41.033  42.567  10.460  1.00 17.05           C  
ATOM    200  C   PRO A  29      41.585  41.226  10.891  1.00 16.09           C  
ATOM    201  O   PRO A  29      41.037  40.578  11.797  1.00 14.56           O  
ATOM    202  CB  PRO A  29      41.595  43.685  11.334  1.00 17.42           C  
ATOM    203  CG  PRO A  29      40.480  44.180  12.162  1.00 17.54           C  
ATOM    204  CD  PRO A  29      39.180  43.702  11.551  1.00 17.29           C  
ATOM    205  N   GLU A  30      42.663  40.778  10.266  1.00 15.63           N  
ATOM    206  CA  GLU A  30      43.365  39.547  10.577  1.00 16.62           C  
ATOM    207  C   GLU A  30      42.483  38.309  10.486  1.00 16.53           C  
ATOM    208  O   GLU A  30      42.704  37.327  11.209  1.00 17.29           O  
ATOM    209  CB  GLU A  30      43.952  39.558  12.001  1.00 18.89           C  
ATOM    210  CG  GLU A  30      45.021  40.568  12.305  1.00 25.65           C  
ATOM    211  CD  GLU A  30      45.602  40.503  13.700  1.00 27.78           C  
ATOM    212  OE1 GLU A  30      46.071  39.445  14.174  1.00 32.92           O  
ATOM    213  OE2 GLU A  30      45.628  41.544  14.393  1.00 34.59           O  
ATOM    214  N   SER A  31      41.449  38.366   9.658  1.00 16.98           N  
ATOM    215  CA  SER A  31      40.481  37.281   9.585  1.00 15.01           C  
ATOM    216  C   SER A  31      40.034  37.053   8.164  1.00 15.25           C  
ATOM    217  O   SER A  31      40.158  37.944   7.338  1.00 15.59           O  
ATOM    218  CB  SER A  31      39.271  37.640  10.452  1.00 13.76           C  
ATOM    219  OG  SER A  31      39.584  38.071  11.764  1.00 15.63           O  
ATOM    220  N   HIS A  32      39.491  35.876   7.856  1.00 16.15           N  
ATOM    221  CA  HIS A  32      38.967  35.649   6.508  1.00 15.30           C  
ATOM    222  C   HIS A  32      38.008  34.452   6.638  1.00 14.79           C  
ATOM    223  O   HIS A  32      38.211  33.587   7.460  1.00 13.15           O  
ATOM    224  CB  HIS A  32      40.019  35.420   5.449  1.00 24.97           C  
ATOM    225  CG  HIS A  32      40.800  34.158   5.610  1.00 26.24           C  
ATOM    226  ND1 HIS A  32      41.857  34.066   6.486  1.00 34.90           N  
ATOM    227  CD2 HIS A  32      40.700  32.955   5.009  1.00 29.79           C  
ATOM    228  CE1 HIS A  32      42.367  32.844   6.437  1.00 32.93           C  
ATOM    229  NE2 HIS A  32      41.682  32.148   5.543  1.00 32.81           N  
ATOM    230  N   ILE A  33      36.943  34.519   5.860  1.00 15.69           N  
ATOM    231  CA  ILE A  33      35.958  33.427   5.892  1.00 15.07           C  
ATOM    232  C   ILE A  33      36.451  32.190   5.183  1.00 15.29           C  
ATOM    233  O   ILE A  33      36.941  32.292   4.053  1.00 14.38           O  
ATOM    234  CB  ILE A  33      34.667  33.935   5.235  1.00 15.91           C  
ATOM    235  CG1 ILE A  33      34.058  35.019   6.168  1.00 19.35           C  
ATOM    236  CG2 ILE A  33      33.686  32.813   4.948  1.00 14.36           C  
ATOM    237  CD1 ILE A  33      32.859  35.698   5.506  1.00 23.34           C  
ATOM    238  N   LEU A  34      36.322  31.028   5.790  1.00 13.07           N  
ATOM    239  CA  LEU A  34      36.650  29.754   5.210  1.00 13.09           C  
ATOM    240  C   LEU A  34      35.450  29.155   4.465  1.00 15.06           C  
ATOM    241  O   LEU A  34      35.637  28.789   3.292  1.00 14.86           O  
ATOM    242  CB  LEU A  34      37.126  28.788   6.299  1.00 12.15           C  
ATOM    243  CG  LEU A  34      38.597  28.839   6.707  1.00 25.68           C  
ATOM    244  CD1 LEU A  34      39.166  30.223   6.763  1.00 29.55           C  
ATOM    245  CD2 LEU A  34      38.739  28.153   8.089  1.00 23.99           C  
ATOM    246  N   THR A  35      34.274  29.060   5.086  1.00 12.79           N  
ATOM    247  CA  THR A  35      33.115  28.473   4.500  1.00 16.57           C  
ATOM    248  C   THR A  35      31.812  29.103   5.070  1.00 13.51           C  
ATOM    249  O   THR A  35      31.913  29.619   6.168  1.00 13.93           O  
ATOM    250  CB  THR A  35      32.761  27.004   4.832  1.00 25.76           C  
ATOM    251  OG1 THR A  35      33.912  26.279   5.143  1.00 35.60           O  
ATOM    252  CG2 THR A  35      32.099  26.386   3.597  1.00 22.38           C  
ATOM    253  N   VAL A  36      30.748  28.957   4.328  1.00 12.77           N  
ATOM    254  CA  VAL A  36      29.441  29.452   4.738  1.00 13.71           C  
ATOM    255  C   VAL A  36      28.450  28.292   4.499  1.00 11.52           C  
ATOM    256  O   VAL A  36      28.533  27.617   3.482  1.00 10.61           O  
ATOM    257  CB  VAL A  36      28.919  30.692   4.010  1.00 18.24           C  
ATOM    258  CG1 VAL A  36      27.638  31.237   4.672  1.00 18.27           C  
ATOM    259  CG2 VAL A  36      29.965  31.799   3.960  1.00 28.50           C  
ATOM    260  N   SER A  37      27.570  28.063   5.469  1.00 12.58           N  
ATOM    261  CA  SER A  37      26.540  27.056   5.298  1.00 11.46           C  
ATOM    262  C   SER A  37      25.440  27.573   4.376  1.00 11.35           C  
ATOM    263  O   SER A  37      25.424  28.738   3.950  1.00 11.49           O  
ATOM    264  CB  SER A  37      25.877  26.675   6.630  1.00 14.85           C  
ATOM    265  OG  SER A  37      25.068  27.778   7.118  1.00 12.54           O  
ATOM    266  N   SER A  38      24.456  26.700   4.105  1.00 11.45           N  
ATOM    267  CA  SER A  38      23.277  27.073   3.379  1.00  9.66           C  
ATOM    268  C   SER A  38      22.471  28.006   4.302  1.00  9.69           C  
ATOM    269  O   SER A  38      22.755  28.078   5.514  1.00 11.09           O  
ATOM    270  CB  SER A  38      22.379  25.900   2.974  1.00 11.92           C  
ATOM    271  OG  SER A  38      23.082  25.021   2.092  1.00 13.64           O  
ATOM    272  N   PHE A  39      21.475  28.654   3.739  1.00  8.38           N  
ATOM    273  CA  PHE A  39      20.625  29.539   4.536  1.00  8.53           C  
ATOM    274  C   PHE A  39      19.323  28.786   4.874  1.00  8.83           C  
ATOM    275  O   PHE A  39      18.604  28.344   3.986  1.00  9.57           O  
ATOM    276  CB  PHE A  39      20.321  30.866   3.858  1.00 11.23           C  
ATOM    277  CG  PHE A  39      21.496  31.711   3.454  1.00 10.13           C  
ATOM    278  CD1 PHE A  39      22.708  31.642   4.096  1.00 12.17           C  
ATOM    279  CD2 PHE A  39      21.278  32.829   2.642  1.00 11.53           C  
ATOM    280  CE1 PHE A  39      23.765  32.484   3.771  1.00 14.94           C  
ATOM    281  CE2 PHE A  39      22.297  33.711   2.329  1.00 13.48           C  
ATOM    282  CZ  PHE A  39      23.548  33.522   2.890  1.00 15.18           C  
ATOM    283  N   TYR A  40      19.047  28.654   6.152  1.00  8.40           N  
ATOM    284  CA  TYR A  40      17.896  27.937   6.647  1.00 10.33           C  
ATOM    285  C   TYR A  40      16.783  28.835   7.171  1.00 10.92           C  
ATOM    286  O   TYR A  40      17.046  29.907   7.688  1.00 12.79           O  
ATOM    287  CB  TYR A  40      18.352  27.000   7.789  1.00  9.29           C  
ATOM    288  CG  TYR A  40      19.356  25.978   7.286  1.00 10.99           C  
ATOM    289  CD1 TYR A  40      18.886  24.791   6.727  1.00 13.49           C  
ATOM    290  CD2 TYR A  40      20.721  26.169   7.349  1.00 12.05           C  
ATOM    291  CE1 TYR A  40      19.760  23.825   6.274  1.00 14.27           C  
ATOM    292  CE2 TYR A  40      21.614  25.206   6.880  1.00 12.67           C  
ATOM    293  CZ  TYR A  40      21.112  24.040   6.349  1.00 15.44           C  
ATOM    294  OH  TYR A  40      21.956  23.049   5.858  1.00 16.52           O  
ATOM    295  N   ARG A  41      15.547  28.393   7.032  1.00  9.99           N  
ATOM    296  CA  ARG A  41      14.365  29.119   7.498  1.00 10.63           C  
ATOM    297  C   ARG A  41      13.835  28.341   8.689  1.00 11.85           C  
ATOM    298  O   ARG A  41      13.442  27.182   8.469  1.00 13.00           O  
ATOM    299  CB  ARG A  41      13.314  29.247   6.404  1.00 11.36           C  
ATOM    300  CG  ARG A  41      12.076  30.052   6.842  1.00 16.15           C  
ATOM    301  CD  ARG A  41      11.047  30.042   5.713  1.00 20.77           C  
ATOM    302  NE  ARG A  41      11.507  30.613   4.460  1.00 31.05           N  
ATOM    303  CZ  ARG A  41      11.496  31.872   4.046  1.00 35.30           C  
ATOM    304  NH1 ARG A  41      10.932  32.811   4.797  1.00 30.97           N  
ATOM    305  NH2 ARG A  41      11.978  32.216   2.841  1.00 28.08           N  
ATOM    306  N   THR A  42      13.907  28.854   9.902  1.00 10.37           N  
ATOM    307  CA  THR A  42      13.528  28.095  11.074  1.00 11.06           C  
ATOM    308  C   THR A  42      12.471  28.794  11.909  1.00 13.37           C  
ATOM    309  O   THR A  42      12.469  30.001  12.042  1.00 13.07           O  
ATOM    310  CB  THR A  42      14.774  27.823  11.958  1.00 13.77           C  
ATOM    311  OG1 THR A  42      15.313  29.054  12.462  1.00 11.45           O  
ATOM    312  CG2 THR A  42      15.890  27.108  11.179  1.00 11.46           C  
ATOM    313  N   PRO A  43      11.536  28.033  12.474  1.00 15.69           N  
ATOM    314  CA  PRO A  43      10.513  28.588  13.344  1.00 15.38           C  
ATOM    315  C   PRO A  43      11.192  29.003  14.622  1.00 13.35           C  
ATOM    316  O   PRO A  43      12.177  28.360  15.025  1.00 12.28           O  
ATOM    317  CB  PRO A  43       9.515  27.471  13.500  1.00 17.74           C  
ATOM    318  CG  PRO A  43      10.317  26.222  13.328  1.00 19.36           C  
ATOM    319  CD  PRO A  43      11.448  26.558  12.374  1.00 17.48           C  
ATOM    320  N   PRO A  44      10.742  30.043  15.302  1.00 13.40           N  
ATOM    321  CA  PRO A  44      11.377  30.483  16.510  1.00 11.72           C  
ATOM    322  C   PRO A  44      11.369  29.432  17.603  1.00 14.55           C  
ATOM    323  O   PRO A  44      10.326  28.787  17.816  1.00 14.73           O  
ATOM    324  CB  PRO A  44      10.590  31.709  16.947  1.00 13.39           C  
ATOM    325  CG  PRO A  44       9.317  31.662  16.171  1.00 14.63           C  
ATOM    326  CD  PRO A  44       9.588  30.879  14.906  1.00 12.51           C  
ATOM    327  N   LEU A  45      12.469  29.291  18.309  1.00 12.79           N  
ATOM    328  CA  LEU A  45      12.571  28.419  19.476  1.00 13.90           C  
ATOM    329  C   LEU A  45      12.431  29.360  20.675  1.00 13.94           C  
ATOM    330  O   LEU A  45      12.993  30.462  20.547  1.00 14.63           O  
ATOM    331  CB  LEU A  45      13.858  27.643  19.511  1.00 18.76           C  
ATOM    332  CG  LEU A  45      14.153  26.670  20.639  1.00 29.32           C  
ATOM    333  CD1 LEU A  45      13.095  25.581  20.732  1.00 29.01           C  
ATOM    334  CD2 LEU A  45      15.539  26.037  20.452  1.00 24.77           C  
ATOM    335  N   GLY A  46      11.726  29.012  21.731  1.00 13.79           N  
ATOM    336  CA  GLY A  46      11.632  30.017  22.859  1.00 15.29           C  
ATOM    337  C   GLY A  46      10.330  30.774  22.601  1.00 15.23           C  
ATOM    338  O   GLY A  46       9.335  30.147  22.199  1.00 16.91           O  
ATOM    339  N   PRO A  47      10.330  32.070  22.773  1.00 16.22           N  
ATOM    340  CA  PRO A  47       9.134  32.878  22.507  1.00 15.91           C  
ATOM    341  C   PRO A  47       8.661  32.651  21.083  1.00 16.90           C  
ATOM    342  O   PRO A  47       9.421  32.839  20.130  1.00 16.25           O  
ATOM    343  CB  PRO A  47       9.548  34.287  22.836  1.00 15.78           C  
ATOM    344  CG  PRO A  47      10.724  34.134  23.758  1.00 18.06           C  
ATOM    345  CD  PRO A  47      11.451  32.908  23.233  1.00 16.30           C  
ATOM    346  N   GLN A  48       7.403  32.233  20.922  1.00 16.50           N  
ATOM    347  CA  GLN A  48       6.826  31.941  19.626  1.00 17.84           C  
ATOM    348  C   GLN A  48       6.205  33.092  18.881  1.00 17.24           C  
ATOM    349  O   GLN A  48       5.875  32.964  17.683  1.00 17.94           O  
ATOM    350  CB  GLN A  48       5.671  30.898  19.796  1.00 21.15           C  
ATOM    351  CG  GLN A  48       6.178  29.573  20.312  1.00 23.02           C  
ATOM    352  CD  GLN A  48       7.158  28.998  19.288  1.00 28.80           C  
ATOM    353  OE1 GLN A  48       6.728  28.694  18.172  1.00 31.66           O  
ATOM    354  NE2 GLN A  48       8.419  28.918  19.654  1.00 25.21           N  
ATOM    355  N   ASP A  49       5.977  34.203  19.578  1.00 15.10           N  
ATOM    356  CA  ASP A  49       5.350  35.346  18.925  1.00 16.05           C  
ATOM    357  C   ASP A  49       6.356  36.232  18.205  1.00 13.63           C  
ATOM    358  O   ASP A  49       6.396  37.433  18.465  1.00 14.07           O  
ATOM    359  CB  ASP A  49       4.553  36.162  19.959  1.00 20.18           C  
ATOM    360  CG  ASP A  49       5.444  36.810  21.008  1.00 30.11           C  
ATOM    361  OD1 ASP A  49       6.386  36.152  21.502  1.00 30.72           O  
ATOM    362  OD2 ASP A  49       5.199  38.003  21.307  1.00 28.95           O  
ATOM    363  N   GLN A  50       7.035  35.670  17.203  1.00 12.18           N  
ATOM    364  CA  GLN A  50       7.997  36.484  16.422  1.00 12.21           C  
ATOM    365  C   GLN A  50       8.187  35.780  15.099  1.00 11.31           C  
ATOM    366  O   GLN A  50       7.815  34.607  14.957  1.00 11.07           O  
ATOM    367  CB  GLN A  50       9.266  36.690  17.243  1.00 12.76           C  
ATOM    368  CG  GLN A  50       9.956  35.366  17.564  1.00 12.01           C  
ATOM    369  CD  GLN A  50      11.245  35.583  18.341  1.00 16.32           C  
ATOM    370  OE1 GLN A  50      12.101  36.337  17.890  1.00 12.02           O  
ATOM    371  NE2 GLN A  50      11.348  34.918  19.487  1.00 15.67           N  
ATOM    372  N   PRO A  51       8.632  36.463  14.070  1.00 11.20           N  
ATOM    373  CA  PRO A  51       8.768  35.887  12.761  1.00 11.37           C  
ATOM    374  C   PRO A  51       9.794  34.756  12.709  1.00 10.96           C  
ATOM    375  O   PRO A  51      10.645  34.645  13.603  1.00 10.93           O  
ATOM    376  CB  PRO A  51       9.171  37.049  11.866  1.00 11.85           C  
ATOM    377  CG  PRO A  51       8.973  38.286  12.667  1.00 12.48           C  
ATOM    378  CD  PRO A  51       9.030  37.903  14.121  1.00 11.99           C  
ATOM    379  N   ASP A  52       9.725  33.959  11.660  1.00  8.65           N  
ATOM    380  CA  ASP A  52      10.657  32.890  11.403  1.00  9.47           C  
ATOM    381  C   ASP A  52      12.064  33.490  11.173  1.00  9.02           C  
ATOM    382  O   ASP A  52      12.202  34.576  10.623  1.00  6.78           O  
ATOM    383  CB  ASP A  52      10.324  32.069  10.178  1.00 14.25           C  
ATOM    384  CG  ASP A  52       9.074  31.213  10.281  1.00 17.35           C  
ATOM    385  OD1 ASP A  52       8.551  31.028  11.396  1.00 16.83           O  
ATOM    386  OD2 ASP A  52       8.668  30.739   9.207  1.00 22.43           O  
ATOM    387  N   TYR A  53      13.074  32.714  11.530  1.00  9.18           N  
ATOM    388  CA  TYR A  53      14.451  33.113  11.388  1.00  9.64           C  
ATOM    389  C   TYR A  53      15.177  32.578  10.169  1.00  9.86           C  
ATOM    390  O   TYR A  53      14.830  31.545   9.613  1.00  8.79           O  
ATOM    391  CB  TYR A  53      15.241  32.578  12.619  1.00 10.13           C  
ATOM    392  CG  TYR A  53      15.073  33.396  13.879  1.00 10.61           C  
ATOM    393  CD1 TYR A  53      13.960  33.284  14.694  1.00  8.81           C  
ATOM    394  CD2 TYR A  53      16.108  34.265  14.250  1.00  9.66           C  
ATOM    395  CE1 TYR A  53      13.843  34.070  15.841  1.00  7.67           C  
ATOM    396  CE2 TYR A  53      16.005  35.030  15.413  1.00  9.00           C  
ATOM    397  CZ  TYR A  53      14.873  34.935  16.179  1.00  9.03           C  
ATOM    398  OH  TYR A  53      14.771  35.706  17.310  1.00 11.66           O  
ATOM    399  N   LEU A  54      16.177  33.326   9.739  1.00  8.53           N  
ATOM    400  CA  LEU A  54      17.135  32.898   8.722  1.00  9.41           C  
ATOM    401  C   LEU A  54      18.360  32.569   9.614  1.00 10.11           C  
ATOM    402  O   LEU A  54      18.753  33.387  10.436  1.00  9.37           O  
ATOM    403  CB  LEU A  54      17.398  33.880   7.623  1.00 13.19           C  
ATOM    404  CG  LEU A  54      18.682  34.031   6.849  1.00 20.51           C  
ATOM    405  CD1 LEU A  54      19.514  32.770   6.706  1.00 12.16           C  
ATOM    406  CD2 LEU A  54      18.411  34.564   5.409  1.00 12.62           C  
ATOM    407  N   ASN A  55      18.816  31.326   9.544  1.00 10.24           N  
ATOM    408  CA  ASN A  55      19.947  30.899  10.361  1.00  8.34           C  
ATOM    409  C   ASN A  55      21.034  30.325   9.449  1.00  9.77           C  
ATOM    410  O   ASN A  55      20.723  29.662   8.467  1.00  9.59           O  
ATOM    411  CB  ASN A  55      19.568  29.859  11.415  1.00 10.98           C  
ATOM    412  CG  ASN A  55      18.866  30.414  12.627  1.00 13.06           C  
ATOM    413  OD1 ASN A  55      17.724  30.071  12.945  1.00 13.21           O  
ATOM    414  ND2 ASN A  55      19.568  31.289  13.363  1.00 10.25           N  
ATOM    415  N   ALA A  56      22.277  30.616   9.792  1.00 11.01           N  
ATOM    416  CA  ALA A  56      23.418  30.108   9.029  1.00  9.24           C  
ATOM    417  C   ALA A  56      24.627  29.982   9.968  1.00 10.85           C  
ATOM    418  O   ALA A  56      24.565  30.366  11.152  1.00  8.32           O  
ATOM    419  CB  ALA A  56      23.732  30.989   7.834  1.00  7.62           C  
ATOM    420  N   ALA A  57      25.690  29.375   9.454  1.00 11.48           N  
ATOM    421  CA  ALA A  57      26.930  29.215  10.225  1.00 12.05           C  
ATOM    422  C   ALA A  57      28.098  29.530   9.270  1.00 12.50           C  
ATOM    423  O   ALA A  57      28.012  29.310   8.069  1.00 10.87           O  
ATOM    424  CB  ALA A  57      27.107  27.853  10.830  1.00 15.31           C  
ATOM    425  N   VAL A  58      29.142  30.129   9.828  1.00 11.56           N  
ATOM    426  CA  VAL A  58      30.318  30.513   9.089  1.00 12.39           C  
ATOM    427  C   VAL A  58      31.581  30.038   9.803  1.00 10.69           C  
ATOM    428  O   VAL A  58      31.636  30.118  11.040  1.00 13.21           O  
ATOM    429  CB  VAL A  58      30.406  32.045   8.918  1.00 24.58           C  
ATOM    430  CG1 VAL A  58      31.690  32.443   8.188  1.00 28.41           C  
ATOM    431  CG2 VAL A  58      29.236  32.625   8.145  1.00 25.22           C  
ATOM    432  N   ALA A  59      32.562  29.561   9.070  1.00 11.02           N  
ATOM    433  CA  ALA A  59      33.859  29.210   9.624  1.00 11.43           C  
ATOM    434  C   ALA A  59      34.798  30.382   9.263  1.00 11.33           C  
ATOM    435  O   ALA A  59      34.871  30.737   8.077  1.00 10.79           O  
ATOM    436  CB  ALA A  59      34.420  27.906   9.110  1.00 16.55           C  
ATOM    437  N   LEU A  60      35.413  30.971  10.264  1.00 12.27           N  
ATOM    438  CA  LEU A  60      36.305  32.103  10.089  1.00 14.13           C  
ATOM    439  C   LEU A  60      37.700  31.783  10.612  1.00 15.22           C  
ATOM    440  O   LEU A  60      37.805  31.322  11.762  1.00 16.90           O  
ATOM    441  CB  LEU A  60      35.785  33.306  10.871  1.00 14.54           C  
ATOM    442  CG  LEU A  60      36.356  34.693  10.769  1.00 18.23           C  
ATOM    443  CD1 LEU A  60      35.804  35.467   9.572  1.00 19.84           C  
ATOM    444  CD2 LEU A  60      36.089  35.496  12.058  1.00 21.32           C  
ATOM    445  N   GLU A  61      38.748  32.039   9.871  1.00 13.37           N  
ATOM    446  CA  GLU A  61      40.102  31.858  10.341  1.00 14.51           C  
ATOM    447  C   GLU A  61      40.557  33.202  10.908  1.00 13.17           C  
ATOM    448  O   GLU A  61      40.448  34.176  10.158  1.00 13.53           O  
ATOM    449  CB  GLU A  61      41.030  31.433   9.223  1.00 19.70           C  
ATOM    450  CG  GLU A  61      42.499  31.414   9.599  1.00 31.80           C  
ATOM    451  CD  GLU A  61      42.840  30.204  10.436  1.00 40.66           C  
ATOM    452  OE1 GLU A  61      43.992  30.101  10.908  1.00 51.88           O  
ATOM    453  OE2 GLU A  61      41.962  29.339  10.618  1.00 48.62           O  
ATOM    454  N   THR A  62      41.004  33.294  12.144  1.00 14.26           N  
ATOM    455  CA  THR A  62      41.374  34.609  12.662  1.00 13.01           C  
ATOM    456  C   THR A  62      42.564  34.549  13.597  1.00 12.54           C  
ATOM    457  O   THR A  62      42.731  33.536  14.280  1.00 12.27           O  
ATOM    458  CB  THR A  62      40.178  35.226  13.417  1.00 11.29           C  
ATOM    459  OG1 THR A  62      40.476  36.576  13.821  1.00 11.99           O  
ATOM    460  CG2 THR A  62      39.856  34.432  14.677  1.00  8.94           C  
ATOM    461  N   SER A  63      43.336  35.627  13.657  1.00 12.98           N  
ATOM    462  CA  SER A  63      44.449  35.681  14.615  1.00 11.12           C  
ATOM    463  C   SER A  63      44.081  36.683  15.693  1.00 12.76           C  
ATOM    464  O   SER A  63      44.922  37.080  16.511  1.00 13.64           O  
ATOM    465  CB  SER A  63      45.770  36.008  13.930  1.00 18.41           C  
ATOM    466  OG  SER A  63      45.699  37.194  13.182  1.00 18.48           O  
ATOM    467  N   LEU A  64      42.795  37.078  15.742  1.00 10.10           N  
ATOM    468  CA  LEU A  64      42.375  37.956  16.843  1.00 10.66           C  
ATOM    469  C   LEU A  64      42.122  37.138  18.104  1.00  9.25           C  
ATOM    470  O   LEU A  64      41.803  35.976  17.951  1.00 10.44           O  
ATOM    471  CB  LEU A  64      41.090  38.708  16.530  1.00 10.82           C  
ATOM    472  CG  LEU A  64      41.081  39.700  15.387  1.00 13.55           C  
ATOM    473  CD1 LEU A  64      39.673  40.282  15.213  1.00 14.30           C  
ATOM    474  CD2 LEU A  64      42.098  40.813  15.616  1.00 11.77           C  
ATOM    475  N   ALA A  65      42.224  37.695  19.293  1.00  9.68           N  
ATOM    476  CA  ALA A  65      41.872  36.998  20.525  1.00 11.22           C  
ATOM    477  C   ALA A  65      40.334  36.891  20.567  1.00 11.76           C  
ATOM    478  O   ALA A  65      39.641  37.637  19.865  1.00 11.07           O  
ATOM    479  CB  ALA A  65      42.376  37.698  21.751  1.00 13.64           C  
ATOM    480  N   PRO A  66      39.800  35.953  21.342  1.00 12.31           N  
ATOM    481  CA  PRO A  66      38.377  35.752  21.428  1.00 12.81           C  
ATOM    482  C   PRO A  66      37.601  37.004  21.769  1.00 12.58           C  
ATOM    483  O   PRO A  66      36.604  37.290  21.092  1.00 11.55           O  
ATOM    484  CB  PRO A  66      38.176  34.683  22.505  1.00 14.03           C  
ATOM    485  CG  PRO A  66      39.513  34.130  22.792  1.00 13.37           C  
ATOM    486  CD  PRO A  66      40.559  35.007  22.182  1.00 12.46           C  
ATOM    487  N   GLU A  67      38.004  37.745  22.809  1.00 11.70           N  
ATOM    488  CA  GLU A  67      37.281  38.972  23.156  1.00 12.97           C  
ATOM    489  C   GLU A  67      37.476  40.054  22.096  1.00 11.90           C  
ATOM    490  O   GLU A  67      36.549  40.873  21.938  1.00 11.68           O  
ATOM    491  CB  GLU A  67      37.683  39.481  24.546  1.00 18.14           C  
ATOM    492  CG  GLU A  67      39.122  39.825  24.734  1.00 32.98           C  
ATOM    493  CD  GLU A  67      40.202  38.780  24.674  1.00 34.47           C  
ATOM    494  OE1 GLU A  67      40.009  37.545  24.715  1.00 21.01           O  
ATOM    495  OE2 GLU A  67      41.390  39.229  24.598  1.00 41.68           O  
ATOM    496  N   GLU A  68      38.580  40.082  21.347  1.00 10.87           N  
ATOM    497  CA  GLU A  68      38.720  41.066  20.262  1.00 11.79           C  
ATOM    498  C   GLU A  68      37.761  40.724  19.124  1.00 11.47           C  
ATOM    499  O   GLU A  68      37.134  41.604  18.493  1.00 11.58           O  
ATOM    500  CB  GLU A  68      40.167  41.136  19.749  1.00 14.37           C  
ATOM    501  CG  GLU A  68      41.158  41.467  20.869  1.00 14.98           C  
ATOM    502  CD  GLU A  68      42.605  41.262  20.482  1.00 21.94           C  
ATOM    503  OE1 GLU A  68      42.932  40.521  19.531  1.00 16.83           O  
ATOM    504  OE2 GLU A  68      43.499  41.841  21.153  1.00 27.67           O  
ATOM    505  N   LEU A  69      37.624  39.435  18.819  1.00  9.15           N  
ATOM    506  CA  LEU A  69      36.643  39.001  17.800  1.00 10.88           C  
ATOM    507  C   LEU A  69      35.241  39.447  18.244  1.00 10.93           C  
ATOM    508  O   LEU A  69      34.453  39.951  17.442  1.00 10.84           O  
ATOM    509  CB  LEU A  69      36.697  37.503  17.549  1.00 12.20           C  
ATOM    510  CG  LEU A  69      35.707  36.916  16.532  1.00 12.04           C  
ATOM    511  CD1 LEU A  69      35.944  37.480  15.130  1.00 16.33           C  
ATOM    512  CD2 LEU A  69      35.792  35.397  16.494  1.00 12.84           C  
ATOM    513  N   LEU A  70      34.904  39.277  19.515  1.00 11.27           N  
ATOM    514  CA  LEU A  70      33.611  39.706  20.056  1.00 12.51           C  
ATOM    515  C   LEU A  70      33.362  41.193  19.856  1.00 11.92           C  
ATOM    516  O   LEU A  70      32.234  41.617  19.554  1.00 11.80           O  
ATOM    517  CB  LEU A  70      33.497  39.391  21.555  1.00 10.35           C  
ATOM    518  CG  LEU A  70      32.125  39.567  22.204  1.00 12.19           C  
ATOM    519  CD1 LEU A  70      31.071  38.737  21.477  1.00 15.60           C  
ATOM    520  CD2 LEU A  70      32.128  39.153  23.677  1.00 10.82           C  
ATOM    521  N   ASN A  71      34.400  42.011  20.093  1.00 12.33           N  
ATOM    522  CA  ASN A  71      34.273  43.441  19.872  1.00 12.20           C  
ATOM    523  C   ASN A  71      33.812  43.711  18.439  1.00 11.15           C  
ATOM    524  O   ASN A  71      32.909  44.539  18.223  1.00  9.07           O  
ATOM    525  CB  ASN A  71      35.585  44.183  20.155  1.00 12.84           C  
ATOM    526  CG  ASN A  71      35.937  44.190  21.636  1.00 18.15           C  
ATOM    527  OD1 ASN A  71      35.087  44.021  22.516  1.00 15.10           O  
ATOM    528  ND2 ASN A  71      37.218  44.394  21.924  1.00 11.44           N  
ATOM    529  N   HIS A  72      34.379  43.022  17.460  1.00 10.12           N  
ATOM    530  CA  HIS A  72      33.985  43.215  16.061  1.00 10.51           C  
ATOM    531  C   HIS A  72      32.621  42.635  15.718  1.00 11.02           C  
ATOM    532  O   HIS A  72      31.867  43.287  14.961  1.00 12.76           O  
ATOM    533  CB  HIS A  72      35.053  42.601  15.121  1.00 13.36           C  
ATOM    534  CG  HIS A  72      36.257  43.498  14.994  1.00 14.49           C  
ATOM    535  ND1 HIS A  72      37.373  43.429  15.780  1.00 18.87           N  
ATOM    536  CD2 HIS A  72      36.464  44.523  14.133  1.00 12.83           C  
ATOM    537  CE1 HIS A  72      38.227  44.357  15.412  1.00 14.51           C  
ATOM    538  NE2 HIS A  72      37.694  45.051  14.410  1.00 19.85           N  
ATOM    539  N   THR A  73      32.274  41.475  16.265  1.00 10.55           N  
ATOM    540  CA  THR A  73      30.924  40.938  15.975  1.00 11.21           C  
ATOM    541  C   THR A  73      29.851  41.832  16.592  1.00 10.09           C  
ATOM    542  O   THR A  73      28.814  42.091  15.952  1.00 11.58           O  
ATOM    543  CB  THR A  73      30.793  39.472  16.438  1.00  8.67           C  
ATOM    544  OG1 THR A  73      31.116  39.344  17.809  1.00 11.77           O  
ATOM    545  CG2 THR A  73      31.710  38.614  15.566  1.00 11.85           C  
ATOM    546  N   GLN A  74      30.080  42.370  17.773  1.00 10.37           N  
ATOM    547  CA  GLN A  74      29.142  43.300  18.411  1.00 11.96           C  
ATOM    548  C   GLN A  74      29.061  44.619  17.656  1.00 12.97           C  
ATOM    549  O   GLN A  74      27.962  45.224  17.609  1.00 12.76           O  
ATOM    550  CB  GLN A  74      29.506  43.529  19.894  1.00 10.10           C  
ATOM    551  CG  GLN A  74      29.290  42.212  20.679  1.00 12.65           C  
ATOM    552  CD  GLN A  74      29.442  42.365  22.168  1.00 20.35           C  
ATOM    553  OE1 GLN A  74      28.856  41.587  22.950  1.00 22.93           O  
ATOM    554  NE2 GLN A  74      30.217  43.331  22.620  1.00 14.59           N  
ATOM    555  N   ARG A  75      30.153  45.083  17.072  1.00 11.38           N  
ATOM    556  CA  ARG A  75      30.146  46.294  16.249  1.00 12.28           C  
ATOM    557  C   ARG A  75      29.275  46.090  15.016  1.00 11.78           C  
ATOM    558  O   ARG A  75      28.531  46.978  14.604  1.00 11.79           O  
ATOM    559  CB  ARG A  75      31.552  46.714  15.782  1.00 13.25           C  
ATOM    560  CG  ARG A  75      31.520  47.778  14.676  1.00 19.85           C  
ATOM    561  CD  ARG A  75      32.917  48.165  14.218  1.00 24.23           C  
ATOM    562  NE  ARG A  75      33.667  47.062  13.645  1.00 30.98           N  
ATOM    563  CZ  ARG A  75      33.513  46.428  12.499  1.00 30.08           C  
ATOM    564  NH1 ARG A  75      32.592  46.757  11.599  1.00 28.00           N  
ATOM    565  NH2 ARG A  75      34.323  45.408  12.203  1.00 29.28           N  
ATOM    566  N   ILE A  76      29.371  44.921  14.383  1.00 10.98           N  
ATOM    567  CA  ILE A  76      28.566  44.604  13.209  1.00 10.78           C  
ATOM    568  C   ILE A  76      27.099  44.530  13.591  1.00 11.05           C  
ATOM    569  O   ILE A  76      26.238  45.083  12.878  1.00 12.28           O  
ATOM    570  CB  ILE A  76      29.058  43.287  12.564  1.00 13.53           C  
ATOM    571  CG1 ILE A  76      30.474  43.457  12.035  1.00 13.08           C  
ATOM    572  CG2 ILE A  76      28.113  42.835  11.454  1.00 13.55           C  
ATOM    573  CD1 ILE A  76      31.180  42.159  11.659  1.00 15.25           C  
ATOM    574  N   GLU A  77      26.762  43.884  14.711  1.00  9.59           N  
ATOM    575  CA  GLU A  77      25.381  43.832  15.165  1.00 10.89           C  
ATOM    576  C   GLU A  77      24.824  45.244  15.319  1.00 13.92           C  
ATOM    577  O   GLU A  77      23.753  45.567  14.810  1.00 13.97           O  
ATOM    578  CB  GLU A  77      25.239  43.098  16.504  1.00  8.70           C  
ATOM    579  CG  GLU A  77      25.508  41.594  16.403  1.00 11.05           C  
ATOM    580  CD  GLU A  77      25.438  40.945  17.773  1.00 11.85           C  
ATOM    581  OE1 GLU A  77      25.820  41.625  18.748  1.00 13.85           O  
ATOM    582  OE2 GLU A  77      25.026  39.780  17.874  1.00 13.86           O  
ATOM    583  N   LEU A  78      25.569  46.083  16.036  1.00 13.84           N  
ATOM    584  CA  LEU A  78      25.160  47.480  16.263  1.00 15.80           C  
ATOM    585  C   LEU A  78      24.993  48.229  14.959  1.00 16.48           C  
ATOM    586  O   LEU A  78      24.011  48.984  14.790  1.00 16.62           O  
ATOM    587  CB  LEU A  78      26.205  48.102  17.187  1.00 23.68           C  
ATOM    588  CG  LEU A  78      25.959  49.429  17.878  1.00 35.23           C  
ATOM    589  CD1 LEU A  78      25.879  50.581  16.891  1.00 39.16           C  
ATOM    590  CD2 LEU A  78      24.674  49.363  18.710  1.00 34.92           C  
ATOM    591  N   GLN A  79      25.890  48.060  13.993  1.00 16.26           N  
ATOM    592  CA  GLN A  79      25.851  48.687  12.700  1.00 18.66           C  
ATOM    593  C   GLN A  79      24.556  48.321  11.949  1.00 18.79           C  
ATOM    594  O   GLN A  79      24.044  49.088  11.128  1.00 16.21           O  
ATOM    595  CB  GLN A  79      26.975  48.272  11.735  1.00 23.71           C  
ATOM    596  CG  GLN A  79      28.392  48.633  12.029  1.00 38.12           C  
ATOM    597  CD  GLN A  79      29.430  48.097  11.061  1.00 42.57           C  
ATOM    598  OE1 GLN A  79      30.619  48.399  11.236  1.00 44.50           O  
ATOM    599  NE2 GLN A  79      29.068  47.316  10.041  1.00 44.59           N  
ATOM    600  N   GLN A  80      24.126  47.070  12.196  1.00 15.99           N  
ATOM    601  CA  GLN A  80      22.908  46.618  11.510  1.00 16.93           C  
ATOM    602  C   GLN A  80      21.663  46.820  12.352  1.00 16.62           C  
ATOM    603  O   GLN A  80      20.637  46.188  12.065  1.00 17.32           O  
ATOM    604  CB  GLN A  80      23.080  45.147  11.046  1.00 15.14           C  
ATOM    605  CG  GLN A  80      24.130  45.128   9.931  1.00 12.01           C  
ATOM    606  CD  GLN A  80      24.333  43.818   9.231  1.00 19.54           C  
ATOM    607  OE1 GLN A  80      25.478  43.460   8.881  1.00 14.95           O  
ATOM    608  NE2 GLN A  80      23.252  43.083   8.980  1.00 11.46           N  
ATOM    609  N   GLY A  81      21.706  47.708  13.336  1.00 16.83           N  
ATOM    610  CA  GLY A  81      20.548  48.074  14.113  1.00 18.78           C  
ATOM    611  C   GLY A  81      20.147  47.268  15.308  1.00 19.80           C  
ATOM    612  O   GLY A  81      19.016  47.438  15.795  1.00 20.85           O  
ATOM    613  N   ARG A  82      21.000  46.381  15.807  1.00 19.70           N  
ATOM    614  CA  ARG A  82      20.704  45.584  16.991  1.00 21.64           C  
ATOM    615  C   ARG A  82      20.713  46.476  18.231  1.00 23.54           C  
ATOM    616  O   ARG A  82      21.722  47.149  18.452  1.00 22.26           O  
ATOM    617  CB  ARG A  82      21.718  44.476  17.181  1.00 20.82           C  
ATOM    618  CG  ARG A  82      21.609  43.551  18.389  1.00 19.88           C  
ATOM    619  CD  ARG A  82      20.428  42.654  18.341  1.00 17.70           C  
ATOM    620  NE  ARG A  82      20.214  41.639  19.322  1.00 15.93           N  
ATOM    621  CZ  ARG A  82      20.751  40.466  19.543  1.00 17.07           C  
ATOM    622  NH1 ARG A  82      21.712  39.955  18.773  1.00 13.06           N  
ATOM    623  NH2 ARG A  82      20.309  39.709  20.534  1.00 17.82           N  
ATOM    624  N   VAL A  83      19.655  46.493  18.999  1.00 25.05           N  
ATOM    625  CA  VAL A  83      19.559  47.278  20.218  1.00 29.36           C  
ATOM    626  C   VAL A  83      19.150  46.266  21.297  1.00 32.54           C  
ATOM    627  O   VAL A  83      18.001  45.823  21.240  1.00 34.26           O  
ATOM    628  CB  VAL A  83      18.568  48.437  20.228  1.00 28.06           C  
ATOM    629  CG1 VAL A  83      18.511  49.041  21.638  1.00 24.45           C  
ATOM    630  CG2 VAL A  83      18.954  49.479  19.194  1.00 24.82           C  
ATOM    631  N   ARG A  84      20.065  45.915  22.186  1.00 34.62           N  
ATOM    632  CA  ARG A  84      19.669  44.923  23.166  1.00 39.34           C  
ATOM    633  C   ARG A  84      19.213  45.612  24.467  1.00 41.66           C  
ATOM    634  O   ARG A  84      19.566  46.706  24.865  1.00 41.74           O  
ATOM    635  CB  ARG A  84      20.760  43.990  23.635  1.00 42.59           C  
ATOM    636  CG  ARG A  84      21.992  43.920  22.758  1.00 44.89           C  
ATOM    637  CD  ARG A  84      23.048  43.080  23.440  1.00 45.49           C  
ATOM    638  NE  ARG A  84      23.239  41.745  22.864  1.00 45.89           N  
ATOM    639  CZ  ARG A  84      23.887  41.672  21.683  1.00 41.72           C  
ATOM    640  NH1 ARG A  84      24.316  42.806  21.122  1.00 44.22           N  
ATOM    641  NH2 ARG A  84      24.169  40.552  21.061  1.00 38.05           N  
ATOM    642  N   LYS A  85      18.436  44.808  25.151  1.00 43.73           N  
ATOM    643  CA  LYS A  85      17.921  45.188  26.493  1.00 45.13           C  
ATOM    644  C   LYS A  85      18.113  43.924  27.296  1.00 45.83           C  
ATOM    645  O   LYS A  85      18.413  42.877  26.692  1.00 47.13           O  
ATOM    646  CB  LYS A  85      16.548  45.772  26.300  1.00 45.15           C  
ATOM    647  CG  LYS A  85      15.684  45.055  25.261  1.00 50.79           C  
ATOM    648  CD  LYS A  85      14.513  45.935  24.856  1.00 51.60           C  
ATOM    649  CE  LYS A  85      13.631  45.273  23.815  1.00 56.06           C  
ATOM    650  NZ  LYS A  85      14.349  44.942  22.555  1.00 59.45           N  
ATOM    651  N   ALA A  86      18.015  43.970  28.618  1.00 47.03           N  
ATOM    652  CA  ALA A  86      18.229  42.752  29.414  1.00 46.16           C  
ATOM    653  C   ALA A  86      17.201  41.689  29.032  1.00 45.25           C  
ATOM    654  O   ALA A  86      17.486  40.496  29.222  1.00 46.44           O  
ATOM    655  CB  ALA A  86      18.180  43.069  30.893  1.00 50.38           C  
ATOM    656  N   GLU A  87      16.036  42.069  28.499  1.00 42.36           N  
ATOM    657  CA  GLU A  87      15.058  41.067  28.043  1.00 38.83           C  
ATOM    658  C   GLU A  87      15.549  40.586  26.658  1.00 34.68           C  
ATOM    659  O   GLU A  87      15.529  41.178  25.593  1.00 32.28           O  
ATOM    660  CB  GLU A  87      13.641  41.551  28.001  1.00 46.00           C  
ATOM    661  CG  GLU A  87      13.294  42.637  27.007  1.00 54.67           C  
ATOM    662  CD  GLU A  87      11.890  43.166  27.286  1.00 56.77           C  
ATOM    663  OE1 GLU A  87      11.620  43.428  28.481  1.00 57.75           O  
ATOM    664  OE2 GLU A  87      11.113  43.295  26.324  1.00 61.74           O  
ATOM    665  N   ARG A  88      16.085  39.381  26.722  1.00 30.96           N  
ATOM    666  CA  ARG A  88      16.802  38.711  25.697  1.00 27.86           C  
ATOM    667  C   ARG A  88      16.312  38.015  24.458  1.00 24.17           C  
ATOM    668  O   ARG A  88      17.096  38.097  23.486  1.00 26.37           O  
ATOM    669  CB  ARG A  88      17.384  37.418  26.487  1.00 33.10           C  
ATOM    670  CG  ARG A  88      18.660  37.801  27.198  1.00 40.48           C  
ATOM    671  CD  ARG A  88      19.150  36.588  28.000  1.00 46.38           C  
ATOM    672  NE  ARG A  88      18.349  36.377  29.197  1.00 42.19           N  
ATOM    673  CZ  ARG A  88      18.468  35.379  30.056  1.00 43.86           C  
ATOM    674  NH1 ARG A  88      19.353  34.406  29.852  1.00 46.04           N  
ATOM    675  NH2 ARG A  88      17.714  35.315  31.148  1.00 37.43           N  
ATOM    676  N   TRP A  89      15.262  37.234  24.485  1.00 19.87           N  
ATOM    677  CA  TRP A  89      14.952  36.404  23.315  1.00 17.08           C  
ATOM    678  C   TRP A  89      13.874  36.875  22.385  1.00 15.24           C  
ATOM    679  O   TRP A  89      13.084  36.059  21.898  1.00 16.04           O  
ATOM    680  CB  TRP A  89      14.589  35.000  23.904  1.00 14.93           C  
ATOM    681  CG  TRP A  89      15.761  34.497  24.716  1.00 17.79           C  
ATOM    682  CD1 TRP A  89      17.063  34.443  24.289  1.00 16.65           C  
ATOM    683  CD2 TRP A  89      15.721  33.818  25.971  1.00 19.48           C  
ATOM    684  NE1 TRP A  89      17.848  33.858  25.257  1.00 19.97           N  
ATOM    685  CE2 TRP A  89      17.040  33.443  26.285  1.00 21.94           C  
ATOM    686  CE3 TRP A  89      14.693  33.512  26.865  1.00 22.67           C  
ATOM    687  CZ2 TRP A  89      17.369  32.787  27.473  1.00 28.67           C  
ATOM    688  CZ3 TRP A  89      15.017  32.854  28.049  1.00 27.82           C  
ATOM    689  CH2 TRP A  89      16.342  32.509  28.341  1.00 30.92           C  
ATOM    690  N   GLY A  90      13.859  38.174  22.120  1.00 14.68           N  
ATOM    691  CA  GLY A  90      12.873  38.750  21.197  1.00 14.35           C  
ATOM    692  C   GLY A  90      13.518  38.846  19.812  1.00 13.86           C  
ATOM    693  O   GLY A  90      14.659  38.402  19.621  1.00 14.67           O  
ATOM    694  N   PRO A  91      12.778  39.369  18.844  1.00 11.82           N  
ATOM    695  CA  PRO A  91      13.217  39.478  17.484  1.00 10.92           C  
ATOM    696  C   PRO A  91      14.420  40.399  17.342  1.00 10.77           C  
ATOM    697  O   PRO A  91      14.624  41.298  18.160  1.00 11.12           O  
ATOM    698  CB  PRO A  91      12.007  39.975  16.703  1.00 10.98           C  
ATOM    699  CG  PRO A  91      11.170  40.650  17.739  1.00 12.23           C  
ATOM    700  CD  PRO A  91      11.377  39.875  19.034  1.00 12.15           C  
ATOM    701  N   ARG A  92      15.228  40.138  16.314  1.00  9.76           N  
ATOM    702  CA  ARG A  92      16.423  40.988  16.144  1.00  8.81           C  
ATOM    703  C   ARG A  92      16.828  41.048  14.697  1.00  8.66           C  
ATOM    704  O   ARG A  92      16.593  40.116  13.911  1.00  9.57           O  
ATOM    705  CB  ARG A  92      17.589  40.481  17.006  1.00 13.42           C  
ATOM    706  CG  ARG A  92      18.263  39.199  16.542  1.00 10.45           C  
ATOM    707  CD  ARG A  92      17.349  37.972  16.730  1.00 12.92           C  
ATOM    708  NE  ARG A  92      17.046  37.870  18.149  1.00 12.62           N  
ATOM    709  CZ  ARG A  92      17.771  37.362  19.130  1.00 17.49           C  
ATOM    710  NH1 ARG A  92      18.895  36.691  18.900  1.00 13.40           N  
ATOM    711  NH2 ARG A  92      17.324  37.476  20.383  1.00 12.38           N  
ATOM    712  N   THR A  93      17.447  42.177  14.308  1.00  7.79           N  
ATOM    713  CA  THR A  93      17.909  42.321  12.930  1.00  8.42           C  
ATOM    714  C   THR A  93      19.090  41.406  12.629  1.00  7.90           C  
ATOM    715  O   THR A  93      19.223  40.852  11.529  1.00  7.36           O  
ATOM    716  CB  THR A  93      18.325  43.769  12.639  1.00  8.92           C  
ATOM    717  OG1 THR A  93      19.280  44.155  13.662  1.00 10.38           O  
ATOM    718  CG2 THR A  93      17.117  44.685  12.661  1.00 10.05           C  
ATOM    719  N   LEU A  94      19.967  41.285  13.628  1.00  9.31           N  
ATOM    720  CA  LEU A  94      21.173  40.474  13.420  1.00  8.81           C  
ATOM    721  C   LEU A  94      21.698  39.968  14.744  1.00  8.47           C  
ATOM    722  O   LEU A  94      21.807  40.738  15.705  1.00  9.37           O  
ATOM    723  CB  LEU A  94      22.268  41.280  12.715  1.00  9.44           C  
ATOM    724  CG  LEU A  94      23.538  40.491  12.340  1.00 13.12           C  
ATOM    725  CD1 LEU A  94      23.228  39.492  11.245  1.00 12.38           C  
ATOM    726  CD2 LEU A  94      24.685  41.415  11.916  1.00 10.68           C  
ATOM    727  N   ASP A  95      22.049  38.689  14.764  1.00  6.87           N  
ATOM    728  CA  ASP A  95      22.596  38.062  15.941  1.00  8.15           C  
ATOM    729  C   ASP A  95      23.841  37.278  15.533  1.00  9.13           C  
ATOM    730  O   ASP A  95      23.716  36.390  14.687  1.00  8.37           O  
ATOM    731  CB  ASP A  95      21.538  37.153  16.558  1.00  5.37           C  
ATOM    732  CG  ASP A  95      22.038  36.537  17.837  1.00 12.83           C  
ATOM    733  OD1 ASP A  95      22.590  37.310  18.629  1.00 11.59           O  
ATOM    734  OD2 ASP A  95      21.902  35.338  18.032  1.00  9.30           O  
ATOM    735  N   LEU A  96      24.994  37.625  16.059  1.00  9.63           N  
ATOM    736  CA  LEU A  96      26.247  36.945  15.739  1.00  8.79           C  
ATOM    737  C   LEU A  96      26.776  36.333  17.030  1.00 10.57           C  
ATOM    738  O   LEU A  96      27.161  37.044  17.974  1.00 10.91           O  
ATOM    739  CB  LEU A  96      27.281  37.886  15.133  1.00  9.59           C  
ATOM    740  CG  LEU A  96      26.909  38.587  13.817  1.00 10.30           C  
ATOM    741  CD1 LEU A  96      27.986  39.574  13.386  1.00  9.74           C  
ATOM    742  CD2 LEU A  96      26.662  37.567  12.705  1.00 11.16           C  
ATOM    743  N   ASP A  97      26.754  35.006  17.126  1.00  8.67           N  
ATOM    744  CA  ASP A  97      27.223  34.293  18.267  1.00  7.71           C  
ATOM    745  C   ASP A  97      28.520  33.520  17.999  1.00  9.37           C  
ATOM    746  O   ASP A  97      28.544  32.842  16.973  1.00  9.92           O  
ATOM    747  CB  ASP A  97      26.264  33.178  18.744  1.00  8.20           C  
ATOM    748  CG  ASP A  97      25.045  33.765  19.410  1.00 13.81           C  
ATOM    749  OD1 ASP A  97      24.988  34.976  19.385  1.00 11.37           O  
ATOM    750  OD2 ASP A  97      24.215  33.079  19.957  1.00 16.98           O  
ATOM    751  N   ILE A  98      29.428  33.555  18.954  1.00  8.33           N  
ATOM    752  CA  ILE A  98      30.648  32.728  18.760  1.00  9.15           C  
ATOM    753  C   ILE A  98      30.315  31.347  19.292  1.00  7.51           C  
ATOM    754  O   ILE A  98      30.111  31.221  20.487  1.00  7.86           O  
ATOM    755  CB  ILE A  98      31.861  33.371  19.436  1.00 10.38           C  
ATOM    756  CG1 ILE A  98      32.121  34.750  18.838  1.00 10.12           C  
ATOM    757  CG2 ILE A  98      33.084  32.458  19.295  1.00  9.82           C  
ATOM    758  CD1 ILE A  98      33.236  35.524  19.535  1.00 20.49           C  
ATOM    759  N   MET A  99      30.160  30.324  18.453  1.00  6.69           N  
ATOM    760  CA  MET A  99      29.813  28.990  18.934  1.00  7.60           C  
ATOM    761  C   MET A  99      31.025  28.284  19.518  1.00  8.50           C  
ATOM    762  O   MET A  99      30.974  27.714  20.596  1.00  9.10           O  
ATOM    763  CB  MET A  99      29.206  28.121  17.808  1.00  7.66           C  
ATOM    764  CG  MET A  99      27.799  28.601  17.397  1.00 10.78           C  
ATOM    765  SD  MET A  99      27.004  27.477  16.206  1.00 11.71           S  
ATOM    766  CE  MET A  99      27.908  27.749  14.718  1.00 10.84           C  
ATOM    767  N   LEU A 100      32.133  28.315  18.768  1.00 10.02           N  
ATOM    768  CA  LEU A 100      33.379  27.709  19.163  1.00 11.39           C  
ATOM    769  C   LEU A 100      34.577  28.607  18.764  1.00 11.16           C  
ATOM    770  O   LEU A 100      34.495  29.241  17.728  1.00 10.94           O  
ATOM    771  CB  LEU A 100      33.666  26.368  18.510  1.00 13.39           C  
ATOM    772  CG  LEU A 100      32.827  25.114  18.645  1.00 20.05           C  
ATOM    773  CD1 LEU A 100      32.491  24.844  20.119  1.00 17.15           C  
ATOM    774  CD2 LEU A 100      31.570  25.188  17.796  1.00 24.32           C  
ATOM    775  N   PHE A 101      35.653  28.554  19.525  1.00 10.55           N  
ATOM    776  CA  PHE A 101      36.852  29.343  19.206  1.00  9.93           C  
ATOM    777  C   PHE A 101      38.023  28.372  19.320  1.00 10.79           C  
ATOM    778  O   PHE A 101      38.452  28.071  20.439  1.00 11.14           O  
ATOM    779  CB  PHE A 101      36.961  30.568  20.117  1.00  6.33           C  
ATOM    780  CG  PHE A 101      38.005  31.544  19.643  1.00 10.76           C  
ATOM    781  CD1 PHE A 101      39.341  31.360  19.962  1.00 15.10           C  
ATOM    782  CD2 PHE A 101      37.650  32.637  18.876  1.00 14.61           C  
ATOM    783  CE1 PHE A 101      40.301  32.258  19.502  1.00 16.69           C  
ATOM    784  CE2 PHE A 101      38.589  33.522  18.402  1.00 12.17           C  
ATOM    785  CZ  PHE A 101      39.926  33.327  18.731  1.00 12.59           C  
ATOM    786  N   GLY A 102      38.457  27.819  18.182  1.00 12.56           N  
ATOM    787  CA  GLY A 102      39.531  26.792  18.251  1.00 15.26           C  
ATOM    788  C   GLY A 102      38.993  25.702  19.185  1.00 16.84           C  
ATOM    789  O   GLY A 102      37.801  25.371  19.141  1.00 16.47           O  
ATOM    790  N   ASN A 103      39.811  25.190  20.084  1.00 17.68           N  
ATOM    791  CA  ASN A 103      39.370  24.240  21.091  1.00 18.97           C  
ATOM    792  C   ASN A 103      39.327  24.846  22.489  1.00 19.10           C  
ATOM    793  O   ASN A 103      39.392  24.102  23.479  1.00 20.57           O  
ATOM    794  CB  ASN A 103      40.261  22.988  21.179  1.00 32.20           C  
ATOM    795  CG  ASN A 103      39.649  21.879  20.343  1.00 40.18           C  
ATOM    796  OD1 ASN A 103      38.516  21.467  20.634  1.00 44.60           O  
ATOM    797  ND2 ASN A 103      40.377  21.419  19.347  1.00 44.79           N  
ATOM    798  N   GLU A 104      39.225  26.142  22.589  1.00 18.16           N  
ATOM    799  CA  GLU A 104      39.174  26.865  23.825  1.00 17.12           C  
ATOM    800  C   GLU A 104      37.856  26.687  24.577  1.00 18.21           C  
ATOM    801  O   GLU A 104      36.786  26.608  23.960  1.00 16.83           O  
ATOM    802  CB  GLU A 104      39.284  28.358  23.537  1.00 22.26           C  
ATOM    803  CG  GLU A 104      40.429  28.770  22.640  1.00 34.83           C  
ATOM    804  CD  GLU A 104      41.683  29.166  23.376  1.00 40.01           C  
ATOM    805  OE1 GLU A 104      42.291  28.306  24.032  1.00 42.98           O  
ATOM    806  OE2 GLU A 104      42.016  30.374  23.293  1.00 44.49           O  
ATOM    807  N   VAL A 105      37.976  26.659  25.892  1.00 16.24           N  
ATOM    808  CA  VAL A 105      36.851  26.624  26.811  1.00 17.64           C  
ATOM    809  C   VAL A 105      36.948  27.988  27.520  1.00 19.44           C  
ATOM    810  O   VAL A 105      37.970  28.236  28.180  1.00 18.45           O  
ATOM    811  CB  VAL A 105      36.831  25.482  27.795  1.00 20.94           C  
ATOM    812  CG1 VAL A 105      35.763  25.630  28.872  1.00 22.30           C  
ATOM    813  CG2 VAL A 105      36.571  24.153  27.052  1.00 19.22           C  
ATOM    814  N   ILE A 106      35.970  28.852  27.280  1.00 17.35           N  
ATOM    815  CA  ILE A 106      36.018  30.198  27.854  1.00 18.23           C  
ATOM    816  C   ILE A 106      34.803  30.470  28.707  1.00 17.53           C  
ATOM    817  O   ILE A 106      33.668  30.193  28.324  1.00 14.66           O  
ATOM    818  CB  ILE A 106      36.165  31.258  26.718  1.00 22.79           C  
ATOM    819  CG1 ILE A 106      37.357  30.953  25.807  1.00 22.44           C  
ATOM    820  CG2 ILE A 106      36.297  32.633  27.336  1.00 15.25           C  
ATOM    821  CD1 ILE A 106      37.472  31.800  24.557  1.00 25.80           C  
ATOM    822  N   ASN A 107      34.985  30.947  29.948  1.00 18.09           N  
ATOM    823  CA  ASN A 107      33.887  31.231  30.852  1.00 18.63           C  
ATOM    824  C   ASN A 107      34.072  32.569  31.583  1.00 19.40           C  
ATOM    825  O   ASN A 107      34.422  32.615  32.773  1.00 17.80           O  
ATOM    826  CB  ASN A 107      33.685  30.143  31.923  1.00 20.33           C  
ATOM    827  CG  ASN A 107      33.385  28.761  31.417  1.00 25.22           C  
ATOM    828  OD1 ASN A 107      34.234  27.859  31.457  1.00 27.45           O  
ATOM    829  ND2 ASN A 107      32.183  28.506  30.900  1.00 24.65           N  
ATOM    830  N   THR A 108      33.773  33.662  30.899  1.00 19.04           N  
ATOM    831  CA  THR A 108      33.880  34.995  31.483  1.00 19.78           C  
ATOM    832  C   THR A 108      32.523  35.684  31.431  1.00 20.10           C  
ATOM    833  O   THR A 108      31.612  35.168  30.800  1.00 20.06           O  
ATOM    834  CB  THR A 108      34.909  35.860  30.761  1.00 18.90           C  
ATOM    835  OG1 THR A 108      34.478  36.023  29.384  1.00 21.59           O  
ATOM    836  CG2 THR A 108      36.300  35.249  30.735  1.00 19.35           C  
ATOM    837  N   GLU A 109      32.409  36.871  32.022  1.00 21.09           N  
ATOM    838  CA  GLU A 109      31.128  37.597  32.012  1.00 21.08           C  
ATOM    839  C   GLU A 109      30.760  38.020  30.611  1.00 20.41           C  
ATOM    840  O   GLU A 109      29.575  38.065  30.245  1.00 23.78           O  
ATOM    841  CB  GLU A 109      31.274  38.757  32.995  1.00 33.60           C  
ATOM    842  CG  GLU A 109      30.031  39.394  33.545  1.00 37.19           C  
ATOM    843  CD  GLU A 109      30.318  40.585  34.451  1.00 40.29           C  
ATOM    844  OE1 GLU A 109      31.272  40.552  35.250  1.00 44.04           O  
ATOM    845  OE2 GLU A 109      29.558  41.576  34.331  1.00 41.59           O  
ATOM    846  N   ARG A 110      31.753  38.292  29.736  1.00 17.88           N  
ATOM    847  CA  ARG A 110      31.442  38.676  28.376  1.00 17.81           C  
ATOM    848  C   ARG A 110      31.324  37.477  27.428  1.00 17.68           C  
ATOM    849  O   ARG A 110      30.630  37.556  26.419  1.00 18.36           O  
ATOM    850  CB  ARG A 110      32.505  39.573  27.735  1.00 17.14           C  
ATOM    851  CG  ARG A 110      32.771  40.921  28.389  1.00 22.76           C  
ATOM    852  CD  ARG A 110      33.659  41.732  27.410  1.00 22.48           C  
ATOM    853  NE  ARG A 110      32.890  42.082  26.196  1.00 24.24           N  
ATOM    854  CZ  ARG A 110      33.480  42.510  25.083  1.00 22.39           C  
ATOM    855  NH1 ARG A 110      34.804  42.576  25.063  1.00 23.21           N  
ATOM    856  NH2 ARG A 110      32.817  42.819  23.977  1.00 25.59           N  
ATOM    857  N   LEU A 111      32.069  36.421  27.730  1.00 18.01           N  
ATOM    858  CA  LEU A 111      32.099  35.314  26.765  1.00 18.84           C  
ATOM    859  C   LEU A 111      32.119  33.927  27.341  1.00 18.29           C  
ATOM    860  O   LEU A 111      32.940  33.559  28.190  1.00 17.36           O  
ATOM    861  CB  LEU A 111      33.363  35.651  25.945  1.00 21.34           C  
ATOM    862  CG  LEU A 111      33.648  34.993  24.631  1.00 21.15           C  
ATOM    863  CD1 LEU A 111      32.477  35.145  23.654  1.00 20.23           C  
ATOM    864  CD2 LEU A 111      34.906  35.572  23.971  1.00 21.27           C  
ATOM    865  N   THR A 112      31.124  33.148  26.909  1.00 15.90           N  
ATOM    866  CA  THR A 112      30.980  31.740  27.304  1.00 13.95           C  
ATOM    867  C   THR A 112      31.062  30.933  26.012  1.00 13.09           C  
ATOM    868  O   THR A 112      30.265  31.099  25.094  1.00 10.78           O  
ATOM    869  CB  THR A 112      29.699  31.470  28.099  1.00 17.73           C  
ATOM    870  OG1 THR A 112      29.790  32.111  29.387  1.00 15.81           O  
ATOM    871  CG2 THR A 112      29.466  29.989  28.348  1.00 10.77           C  
ATOM    872  N   VAL A 113      32.122  30.137  25.864  1.00 11.22           N  
ATOM    873  CA  VAL A 113      32.427  29.304  24.723  1.00 13.24           C  
ATOM    874  C   VAL A 113      32.875  27.917  25.166  1.00 14.82           C  
ATOM    875  O   VAL A 113      33.735  27.854  26.069  1.00 13.36           O  
ATOM    876  CB  VAL A 113      33.576  29.900  23.888  1.00 14.79           C  
ATOM    877  CG1 VAL A 113      33.956  28.987  22.718  1.00 17.31           C  
ATOM    878  CG2 VAL A 113      33.254  31.279  23.320  1.00 12.45           C  
ATOM    879  N   PRO A 114      32.357  26.835  24.612  1.00 14.51           N  
ATOM    880  CA  PRO A 114      31.336  26.826  23.618  1.00 13.00           C  
ATOM    881  C   PRO A 114      30.068  27.546  24.050  1.00 12.10           C  
ATOM    882  O   PRO A 114      29.800  27.640  25.250  1.00 10.42           O  
ATOM    883  CB  PRO A 114      31.006  25.354  23.376  1.00 13.95           C  
ATOM    884  CG  PRO A 114      32.215  24.605  23.858  1.00 14.35           C  
ATOM    885  CD  PRO A 114      32.744  25.447  25.012  1.00 15.50           C  
ATOM    886  N   HIS A 115      29.308  28.037  23.083  1.00 10.72           N  
ATOM    887  CA  HIS A 115      28.052  28.721  23.361  1.00 11.30           C  
ATOM    888  C   HIS A 115      27.275  27.860  24.346  1.00 12.84           C  
ATOM    889  O   HIS A 115      27.103  26.662  24.069  1.00 12.39           O  
ATOM    890  CB  HIS A 115      27.276  28.962  22.076  1.00 12.72           C  
ATOM    891  CG  HIS A 115      25.946  29.620  22.281  1.00 18.74           C  
ATOM    892  ND1 HIS A 115      25.686  30.934  21.977  1.00 19.44           N  
ATOM    893  CD2 HIS A 115      24.803  29.103  22.818  1.00 11.38           C  
ATOM    894  CE1 HIS A 115      24.413  31.195  22.265  1.00 15.98           C  
ATOM    895  NE2 HIS A 115      23.882  30.115  22.797  1.00 19.39           N  
ATOM    896  N   TYR A 116      26.789  28.470  25.422  1.00 12.39           N  
ATOM    897  CA  TYR A 116      26.145  27.746  26.503  1.00 15.38           C  
ATOM    898  C   TYR A 116      24.947  26.902  26.130  1.00 15.39           C  
ATOM    899  O   TYR A 116      24.698  25.959  26.917  1.00 18.10           O  
ATOM    900  CB  TYR A 116      25.676  28.750  27.599  1.00 15.34           C  
ATOM    901  CG  TYR A 116      24.374  29.449  27.277  1.00 17.03           C  
ATOM    902  CD1 TYR A 116      24.279  30.444  26.327  1.00 16.30           C  
ATOM    903  CD2 TYR A 116      23.220  29.104  28.005  1.00 19.65           C  
ATOM    904  CE1 TYR A 116      23.075  31.079  26.066  1.00 17.69           C  
ATOM    905  CE2 TYR A 116      22.011  29.737  27.748  1.00 19.14           C  
ATOM    906  CZ  TYR A 116      21.946  30.712  26.790  1.00 18.71           C  
ATOM    907  OH  TYR A 116      20.753  31.339  26.532  1.00 19.34           O  
ATOM    908  N   ASP A 117      24.219  27.134  25.066  1.00 14.42           N  
ATOM    909  CA  ASP A 117      23.041  26.319  24.789  1.00 14.24           C  
ATOM    910  C   ASP A 117      23.043  25.660  23.439  1.00 13.45           C  
ATOM    911  O   ASP A 117      22.039  25.078  23.028  1.00 11.93           O  
ATOM    912  CB  ASP A 117      21.818  27.277  24.892  1.00 13.25           C  
ATOM    913  CG  ASP A 117      20.504  26.544  25.061  1.00 17.78           C  
ATOM    914  OD1 ASP A 117      20.471  25.565  25.845  1.00 17.49           O  
ATOM    915  OD2 ASP A 117      19.494  26.946  24.449  1.00 20.83           O  
ATOM    916  N   MET A 118      24.154  25.760  22.697  1.00 12.43           N  
ATOM    917  CA  MET A 118      24.175  25.270  21.315  1.00 12.18           C  
ATOM    918  C   MET A 118      23.874  23.782  21.196  1.00 12.79           C  
ATOM    919  O   MET A 118      23.253  23.434  20.170  1.00 11.42           O  
ATOM    920  CB  MET A 118      25.511  25.589  20.645  1.00 14.13           C  
ATOM    921  CG  MET A 118      26.744  24.926  21.254  1.00 16.87           C  
ATOM    922  SD  MET A 118      28.203  25.391  20.280  1.00 11.57           S  
ATOM    923  CE  MET A 118      27.871  24.595  18.731  1.00  8.71           C  
ATOM    924  N   LYS A 119      24.190  22.934  22.164  1.00 11.63           N  
ATOM    925  CA  LYS A 119      23.869  21.516  22.003  1.00 14.22           C  
ATOM    926  C   LYS A 119      22.370  21.249  22.074  1.00 14.80           C  
ATOM    927  O   LYS A 119      21.938  20.149  21.720  1.00 15.72           O  
ATOM    928  CB  LYS A 119      24.590  20.647  23.047  1.00 14.47           C  
ATOM    929  CG  LYS A 119      26.116  20.736  22.898  1.00 16.64           C  
ATOM    930  CD  LYS A 119      26.760  19.805  23.955  1.00 19.52           C  
ATOM    931  CE  LYS A 119      28.273  19.864  23.824  1.00 24.76           C  
ATOM    932  NZ  LYS A 119      28.938  18.949  24.810  1.00 26.98           N  
ATOM    933  N   ASN A 120      21.562  22.220  22.448  1.00 14.57           N  
ATOM    934  CA  ASN A 120      20.125  22.083  22.505  1.00 13.41           C  
ATOM    935  C   ASN A 120      19.421  22.760  21.343  1.00 13.71           C  
ATOM    936  O   ASN A 120      18.185  22.761  21.308  1.00 16.20           O  
ATOM    937  CB  ASN A 120      19.621  22.688  23.832  1.00 18.52           C  
ATOM    938  CG  ASN A 120      20.210  21.991  25.044  1.00 23.79           C  
ATOM    939  OD1 ASN A 120      20.300  20.769  25.050  1.00 22.73           O  
ATOM    940  ND2 ASN A 120      20.652  22.722  26.063  1.00 23.81           N  
ATOM    941  N   ARG A 121      20.154  23.366  20.404  1.00 12.39           N  
ATOM    942  CA  ARG A 121      19.537  24.124  19.327  1.00 11.27           C  
ATOM    943  C   ARG A 121      19.820  23.577  17.949  1.00 10.95           C  
ATOM    944  O   ARG A 121      20.913  23.742  17.383  1.00  9.41           O  
ATOM    945  CB  ARG A 121      20.043  25.588  19.385  1.00 12.18           C  
ATOM    946  CG  ARG A 121      19.780  26.250  20.740  1.00 12.09           C  
ATOM    947  CD  ARG A 121      20.227  27.699  20.761  1.00 10.97           C  
ATOM    948  NE  ARG A 121      19.985  28.302  22.083  1.00 14.28           N  
ATOM    949  CZ  ARG A 121      20.209  29.598  22.321  1.00 14.38           C  
ATOM    950  NH1 ARG A 121      20.661  30.388  21.352  1.00 11.49           N  
ATOM    951  NH2 ARG A 121      19.993  30.084  23.542  1.00 11.56           N  
ATOM    952  N   GLY A 122      18.795  22.964  17.341  1.00  9.92           N  
ATOM    953  CA  GLY A 122      18.993  22.414  15.992  1.00 11.15           C  
ATOM    954  C   GLY A 122      19.371  23.483  14.992  1.00 10.37           C  
ATOM    955  O   GLY A 122      20.054  23.193  14.002  1.00 10.27           O  
ATOM    956  N   PHE A 123      18.895  24.729  15.201  1.00 10.47           N  
ATOM    957  CA  PHE A 123      19.198  25.803  14.235  1.00 11.47           C  
ATOM    958  C   PHE A 123      20.657  26.229  14.309  1.00 10.51           C  
ATOM    959  O   PHE A 123      21.117  26.956  13.407  1.00 10.99           O  
ATOM    960  CB  PHE A 123      18.264  27.009  14.421  1.00 11.12           C  
ATOM    961  CG  PHE A 123      18.340  27.690  15.772  1.00 10.54           C  
ATOM    962  CD1 PHE A 123      19.324  28.615  16.033  1.00 11.71           C  
ATOM    963  CD2 PHE A 123      17.384  27.445  16.741  1.00 12.44           C  
ATOM    964  CE1 PHE A 123      19.398  29.257  17.265  1.00 16.05           C  
ATOM    965  CE2 PHE A 123      17.434  28.086  17.968  1.00 12.83           C  
ATOM    966  CZ  PHE A 123      18.442  28.984  18.223  1.00 13.47           C  
ATOM    967  N   MET A 124      21.406  25.830  15.326  1.00 10.38           N  
ATOM    968  CA  MET A 124      22.840  26.069  15.371  1.00 12.37           C  
ATOM    969  C   MET A 124      23.607  24.824  14.901  1.00 11.96           C  
ATOM    970  O   MET A 124      24.533  24.880  14.108  1.00 13.45           O  
ATOM    971  CB  MET A 124      23.341  26.424  16.778  1.00 13.00           C  
ATOM    972  CG  MET A 124      23.015  27.865  17.148  1.00 16.12           C  
ATOM    973  SD  MET A 124      23.531  28.241  18.843  1.00 14.31           S  
ATOM    974  CE  MET A 124      23.962  29.961  18.655  1.00 15.73           C  
ATOM    975  N   LEU A 125      23.171  23.665  15.399  1.00 12.25           N  
ATOM    976  CA  LEU A 125      23.867  22.409  15.077  1.00 12.68           C  
ATOM    977  C   LEU A 125      23.726  21.946  13.646  1.00 12.69           C  
ATOM    978  O   LEU A 125      24.744  21.458  13.101  1.00 13.61           O  
ATOM    979  CB  LEU A 125      23.366  21.297  16.027  1.00 13.26           C  
ATOM    980  CG  LEU A 125      23.605  21.500  17.520  1.00 15.89           C  
ATOM    981  CD1 LEU A 125      23.136  20.272  18.284  1.00 17.74           C  
ATOM    982  CD2 LEU A 125      25.065  21.768  17.842  1.00 16.21           C  
ATOM    983  N   TRP A 126      22.569  22.048  12.979  1.00 11.50           N  
ATOM    984  CA  TRP A 126      22.514  21.561  11.588  1.00 12.34           C  
ATOM    985  C   TRP A 126      23.400  22.342  10.616  1.00 12.39           C  
ATOM    986  O   TRP A 126      24.098  21.709   9.815  1.00  9.66           O  
ATOM    987  CB  TRP A 126      21.106  21.557  10.996  1.00 14.27           C  
ATOM    988  CG  TRP A 126      20.259  20.450  11.540  1.00 16.10           C  
ATOM    989  CD1 TRP A 126      19.187  20.527  12.378  1.00 20.22           C  
ATOM    990  CD2 TRP A 126      20.485  19.056  11.289  1.00 19.59           C  
ATOM    991  NE1 TRP A 126      18.702  19.271  12.635  1.00 18.45           N  
ATOM    992  CE2 TRP A 126      19.478  18.351  11.981  1.00 22.93           C  
ATOM    993  CE3 TRP A 126      21.420  18.348  10.535  1.00 22.95           C  
ATOM    994  CZ2 TRP A 126      19.390  16.966  11.933  1.00 28.55           C  
ATOM    995  CZ3 TRP A 126      21.322  16.963  10.485  1.00 29.04           C  
ATOM    996  CH2 TRP A 126      20.311  16.291  11.187  1.00 24.79           C  
ATOM    997  N   PRO A 127      23.348  23.655  10.623  1.00 11.82           N  
ATOM    998  CA  PRO A 127      24.192  24.474   9.764  1.00 11.94           C  
ATOM    999  C   PRO A 127      25.664  24.214  10.032  1.00 11.47           C  
ATOM   1000  O   PRO A 127      26.513  24.190   9.135  1.00 12.49           O  
ATOM   1001  CB  PRO A 127      23.775  25.893  10.072  1.00 12.50           C  
ATOM   1002  CG  PRO A 127      22.388  25.763  10.662  1.00 13.83           C  
ATOM   1003  CD  PRO A 127      22.473  24.485  11.490  1.00 11.74           C  
ATOM   1004  N   LEU A 128      26.036  24.037  11.294  1.00 10.81           N  
ATOM   1005  CA  LEU A 128      27.411  23.756  11.696  1.00 11.62           C  
ATOM   1006  C   LEU A 128      27.846  22.403  11.119  1.00 13.39           C  
ATOM   1007  O   LEU A 128      28.926  22.243  10.544  1.00 13.57           O  
ATOM   1008  CB  LEU A 128      27.553  23.783  13.209  1.00  7.29           C  
ATOM   1009  CG  LEU A 128      28.920  23.441  13.814  1.00 14.41           C  
ATOM   1010  CD1 LEU A 128      30.009  24.393  13.330  1.00 11.82           C  
ATOM   1011  CD2 LEU A 128      28.859  23.456  15.343  1.00 12.51           C  
ATOM   1012  N   PHE A 129      26.966  21.418  11.213  1.00 12.68           N  
ATOM   1013  CA  PHE A 129      27.223  20.070  10.722  1.00 13.42           C  
ATOM   1014  C   PHE A 129      27.468  20.040   9.228  1.00 14.65           C  
ATOM   1015  O   PHE A 129      28.279  19.258   8.703  1.00 14.64           O  
ATOM   1016  CB  PHE A 129      26.035  19.164  11.126  1.00 14.76           C  
ATOM   1017  CG  PHE A 129      26.238  17.744  10.660  1.00 18.86           C  
ATOM   1018  CD1 PHE A 129      27.200  16.955  11.287  1.00 19.97           C  
ATOM   1019  CD2 PHE A 129      25.439  17.194   9.680  1.00 20.15           C  
ATOM   1020  CE1 PHE A 129      27.394  15.643  10.879  1.00 25.10           C  
ATOM   1021  CE2 PHE A 129      25.629  15.883   9.274  1.00 25.47           C  
ATOM   1022  CZ  PHE A 129      26.608  15.106   9.878  1.00 23.07           C  
ATOM   1023  N   GLU A 130      26.771  20.905   8.489  1.00 12.56           N  
ATOM   1024  CA  GLU A 130      26.923  20.993   7.057  1.00 13.97           C  
ATOM   1025  C   GLU A 130      28.335  21.428   6.683  1.00 13.28           C  
ATOM   1026  O   GLU A 130      28.857  20.985   5.663  1.00 11.91           O  
ATOM   1027  CB  GLU A 130      25.887  21.990   6.495  1.00 15.67           C  
ATOM   1028  CG  GLU A 130      25.972  22.217   5.003  1.00 15.60           C  
ATOM   1029  CD  GLU A 130      25.009  23.264   4.482  1.00 19.43           C  
ATOM   1030  OE1 GLU A 130      24.333  23.951   5.272  1.00 15.42           O  
ATOM   1031  OE2 GLU A 130      24.945  23.452   3.255  1.00 20.06           O  
ATOM   1032  N   ILE A 131      28.922  22.338   7.469  1.00 11.04           N  
ATOM   1033  CA  ILE A 131      30.265  22.803   7.139  1.00 13.09           C  
ATOM   1034  C   ILE A 131      31.375  22.071   7.893  1.00 12.52           C  
ATOM   1035  O   ILE A 131      32.525  22.247   7.467  1.00 14.97           O  
ATOM   1036  CB  ILE A 131      30.409  24.328   7.390  1.00 12.84           C  
ATOM   1037  CG1 ILE A 131      30.194  24.741   8.829  1.00 14.10           C  
ATOM   1038  CG2 ILE A 131      29.395  25.037   6.460  1.00 18.51           C  
ATOM   1039  CD1 ILE A 131      30.470  26.241   9.093  1.00 13.56           C  
ATOM   1040  N   ALA A 132      31.114  21.333   8.933  1.00 10.95           N  
ATOM   1041  CA  ALA A 132      32.122  20.649   9.740  1.00 13.52           C  
ATOM   1042  C   ALA A 132      31.516  19.399  10.358  1.00 13.44           C  
ATOM   1043  O   ALA A 132      31.289  19.274  11.567  1.00 14.68           O  
ATOM   1044  CB  ALA A 132      32.661  21.555  10.839  1.00 14.18           C  
ATOM   1045  N   PRO A 133      31.239  18.415   9.503  1.00 14.37           N  
ATOM   1046  CA  PRO A 133      30.589  17.196   9.935  1.00 15.87           C  
ATOM   1047  C   PRO A 133      31.383  16.365  10.917  1.00 16.44           C  
ATOM   1048  O   PRO A 133      30.755  15.672  11.745  1.00 17.19           O  
ATOM   1049  CB  PRO A 133      30.316  16.442   8.638  1.00 16.17           C  
ATOM   1050  CG  PRO A 133      31.081  17.099   7.561  1.00 17.49           C  
ATOM   1051  CD  PRO A 133      31.453  18.474   8.039  1.00 14.88           C  
ATOM   1052  N   GLU A 134      32.729  16.454  10.896  1.00 14.98           N  
ATOM   1053  CA  GLU A 134      33.497  15.637  11.840  1.00 15.52           C  
ATOM   1054  C   GLU A 134      33.940  16.424  13.057  1.00 16.11           C  
ATOM   1055  O   GLU A 134      34.779  15.965  13.838  1.00 17.34           O  
ATOM   1056  CB  GLU A 134      34.719  15.015  11.144  1.00 20.69           C  
ATOM   1057  CG  GLU A 134      34.380  14.233   9.889  1.00 25.36           C  
ATOM   1058  CD  GLU A 134      33.324  13.170  10.056  1.00 27.14           C  
ATOM   1059  OE1 GLU A 134      33.118  12.616  11.155  1.00 36.22           O  
ATOM   1060  OE2 GLU A 134      32.644  12.870   9.046  1.00 37.87           O  
ATOM   1061  N   LEU A 135      33.353  17.605  13.272  1.00 13.69           N  
ATOM   1062  CA  LEU A 135      33.686  18.408  14.431  1.00 12.69           C  
ATOM   1063  C   LEU A 135      33.494  17.661  15.736  1.00 13.26           C  
ATOM   1064  O   LEU A 135      32.528  16.915  15.965  1.00 12.90           O  
ATOM   1065  CB  LEU A 135      32.820  19.687  14.414  1.00 15.92           C  
ATOM   1066  CG  LEU A 135      33.159  20.832  15.354  1.00 25.93           C  
ATOM   1067  CD1 LEU A 135      34.620  21.260  15.200  1.00 32.45           C  
ATOM   1068  CD2 LEU A 135      32.306  22.072  15.024  1.00 28.77           C  
ATOM   1069  N   VAL A 136      34.430  17.874  16.649  1.00 11.65           N  
ATOM   1070  CA  VAL A 136      34.421  17.330  17.991  1.00 13.30           C  
ATOM   1071  C   VAL A 136      34.465  18.514  18.963  1.00 15.00           C  
ATOM   1072  O   VAL A 136      35.264  19.415  18.692  1.00 15.32           O  
ATOM   1073  CB  VAL A 136      35.585  16.379  18.282  1.00 15.09           C  
ATOM   1074  CG1 VAL A 136      35.500  15.815  19.703  1.00 17.42           C  
ATOM   1075  CG2 VAL A 136      35.620  15.221  17.286  1.00 19.37           C  
ATOM   1076  N   PHE A 137      33.638  18.558  19.984  1.00 14.88           N  
ATOM   1077  CA  PHE A 137      33.647  19.634  20.963  1.00 15.50           C  
ATOM   1078  C   PHE A 137      34.834  19.528  21.887  1.00 16.84           C  
ATOM   1079  O   PHE A 137      35.388  18.435  22.065  1.00 17.08           O  
ATOM   1080  CB  PHE A 137      32.359  19.593  21.801  1.00 12.94           C  
ATOM   1081  CG  PHE A 137      31.133  20.069  21.063  1.00 18.85           C  
ATOM   1082  CD1 PHE A 137      30.380  19.212  20.279  1.00 20.17           C  
ATOM   1083  CD2 PHE A 137      30.732  21.390  21.178  1.00 20.34           C  
ATOM   1084  CE1 PHE A 137      29.256  19.648  19.604  1.00 19.05           C  
ATOM   1085  CE2 PHE A 137      29.602  21.840  20.509  1.00 21.06           C  
ATOM   1086  CZ  PHE A 137      28.869  20.978  19.725  1.00 22.91           C  
ATOM   1087  N   PRO A 138      35.212  20.598  22.591  1.00 17.24           N  
ATOM   1088  CA  PRO A 138      36.321  20.539  23.529  1.00 18.56           C  
ATOM   1089  C   PRO A 138      36.135  19.469  24.580  1.00 19.71           C  
ATOM   1090  O   PRO A 138      37.132  18.944  25.095  1.00 21.73           O  
ATOM   1091  CB  PRO A 138      36.384  21.934  24.138  1.00 17.03           C  
ATOM   1092  CG  PRO A 138      35.795  22.794  23.057  1.00 18.23           C  
ATOM   1093  CD  PRO A 138      34.647  21.956  22.483  1.00 16.89           C  
ATOM   1094  N   ASP A 139      34.897  19.108  24.934  1.00 18.70           N  
ATOM   1095  CA  ASP A 139      34.648  18.074  25.924  1.00 21.07           C  
ATOM   1096  C   ASP A 139      34.720  16.658  25.344  1.00 21.95           C  
ATOM   1097  O   ASP A 139      34.445  15.712  26.091  1.00 22.57           O  
ATOM   1098  CB  ASP A 139      33.278  18.259  26.599  1.00 27.54           C  
ATOM   1099  CG  ASP A 139      32.102  18.210  25.651  1.00 29.33           C  
ATOM   1100  OD1 ASP A 139      32.191  17.618  24.562  1.00 28.36           O  
ATOM   1101  OD2 ASP A 139      31.050  18.794  25.984  1.00 34.42           O  
ATOM   1102  N   GLY A 140      35.033  16.492  24.070  1.00 20.33           N  
ATOM   1103  CA  GLY A 140      35.128  15.187  23.462  1.00 20.90           C  
ATOM   1104  C   GLY A 140      33.860  14.695  22.791  1.00 20.38           C  
ATOM   1105  O   GLY A 140      33.955  13.700  22.050  1.00 18.88           O  
ATOM   1106  N   GLU A 141      32.715  15.353  23.005  1.00 18.17           N  
ATOM   1107  CA  GLU A 141      31.506  14.886  22.315  1.00 18.63           C  
ATOM   1108  C   GLU A 141      31.603  15.200  20.823  1.00 17.22           C  
ATOM   1109  O   GLU A 141      32.088  16.258  20.416  1.00 18.02           O  
ATOM   1110  CB  GLU A 141      30.212  15.493  22.814  1.00 22.35           C  
ATOM   1111  CG  GLU A 141      29.712  15.152  24.191  1.00 32.42           C  
ATOM   1112  CD  GLU A 141      28.262  15.624  24.343  1.00 35.34           C  
ATOM   1113  OE1 GLU A 141      27.352  14.879  23.909  1.00 42.97           O  
ATOM   1114  OE2 GLU A 141      28.051  16.730  24.851  1.00 35.78           O  
ATOM   1115  N   MET A 142      31.098  14.268  20.004  1.00 15.26           N  
ATOM   1116  CA  MET A 142      31.143  14.472  18.562  1.00 12.93           C  
ATOM   1117  C   MET A 142      29.846  15.130  18.112  1.00 12.30           C  
ATOM   1118  O   MET A 142      28.791  14.681  18.596  1.00 12.99           O  
ATOM   1119  CB  MET A 142      31.338  13.163  17.812  1.00 15.23           C  
ATOM   1120  CG  MET A 142      32.618  12.408  18.216  1.00 20.77           C  
ATOM   1121  SD  MET A 142      32.689  10.809  17.348  1.00 22.72           S  
ATOM   1122  CE  MET A 142      31.295   9.971  17.998  1.00 18.13           C  
ATOM   1123  N   LEU A 143      29.903  16.097  17.233  1.00 10.72           N  
ATOM   1124  CA  LEU A 143      28.708  16.768  16.724  1.00  9.90           C  
ATOM   1125  C   LEU A 143      27.736  15.797  16.066  1.00 12.84           C  
ATOM   1126  O   LEU A 143      26.514  15.824  16.274  1.00 13.92           O  
ATOM   1127  CB  LEU A 143      29.136  17.838  15.709  1.00 10.86           C  
ATOM   1128  CG  LEU A 143      27.976  18.576  14.983  1.00 14.97           C  
ATOM   1129  CD1 LEU A 143      27.081  19.290  15.981  1.00 10.76           C  
ATOM   1130  CD2 LEU A 143      28.538  19.534  13.951  1.00 13.11           C  
ATOM   1131  N   ARG A 144      28.252  14.916  15.218  1.00 12.34           N  
ATOM   1132  CA  ARG A 144      27.461  13.908  14.515  1.00 15.91           C  
ATOM   1133  C   ARG A 144      26.676  13.034  15.474  1.00 16.39           C  
ATOM   1134  O   ARG A 144      25.488  12.712  15.260  1.00 17.41           O  
ATOM   1135  CB  ARG A 144      28.407  13.085  13.596  1.00 20.90           C  
ATOM   1136  CG  ARG A 144      27.723  11.885  13.005  1.00 29.55           C  
ATOM   1137  CD  ARG A 144      28.391  11.041  11.975  1.00 35.84           C  
ATOM   1138  NE  ARG A 144      28.498  11.481  10.661  1.00 40.74           N  
ATOM   1139  CZ  ARG A 144      28.971  12.129   9.670  1.00 39.84           C  
ATOM   1140  NH1 ARG A 144      30.128  12.779   9.764  1.00 43.50           N  
ATOM   1141  NH2 ARG A 144      28.366  12.144   8.471  1.00 45.22           N  
ATOM   1142  N   GLN A 145      27.273  12.641  16.585  1.00 17.00           N  
ATOM   1143  CA  GLN A 145      26.647  11.865  17.638  1.00 19.60           C  
ATOM   1144  C   GLN A 145      25.530  12.633  18.322  1.00 20.35           C  
ATOM   1145  O   GLN A 145      24.458  12.053  18.587  1.00 21.21           O  
ATOM   1146  CB  GLN A 145      27.694  11.471  18.676  1.00 24.24           C  
ATOM   1147  CG  GLN A 145      27.262  11.159  20.060  1.00 36.54           C  
ATOM   1148  CD  GLN A 145      26.549   9.896  20.383  1.00 42.22           C  
ATOM   1149  OE1 GLN A 145      26.478   9.485  21.563  1.00 47.50           O  
ATOM   1150  NE2 GLN A 145      26.015   9.194  19.391  1.00 43.99           N  
ATOM   1151  N   ILE A 146      25.754  13.903  18.639  1.00 19.29           N  
ATOM   1152  CA  ILE A 146      24.713  14.713  19.284  1.00 18.50           C  
ATOM   1153  C   ILE A 146      23.459  14.771  18.415  1.00 19.20           C  
ATOM   1154  O   ILE A 146      22.338  14.555  18.912  1.00 19.78           O  
ATOM   1155  CB  ILE A 146      25.234  16.127  19.599  1.00 16.08           C  
ATOM   1156  CG1 ILE A 146      26.302  16.058  20.702  1.00 20.27           C  
ATOM   1157  CG2 ILE A 146      24.098  17.049  20.008  1.00 21.41           C  
ATOM   1158  CD1 ILE A 146      27.016  17.393  20.881  1.00 23.03           C  
ATOM   1159  N   LEU A 147      23.603  15.008  17.119  1.00 18.97           N  
ATOM   1160  CA  LEU A 147      22.472  15.062  16.191  1.00 20.38           C  
ATOM   1161  C   LEU A 147      21.768  13.729  15.999  1.00 23.17           C  
ATOM   1162  O   LEU A 147      20.536  13.659  15.988  1.00 22.05           O  
ATOM   1163  CB  LEU A 147      22.954  15.587  14.829  1.00 19.34           C  
ATOM   1164  CG  LEU A 147      23.246  17.091  14.791  1.00 19.30           C  
ATOM   1165  CD1 LEU A 147      24.084  17.451  13.585  1.00 18.47           C  
ATOM   1166  CD2 LEU A 147      21.940  17.876  14.785  1.00 15.33           C  
ATOM   1167  N   HIS A 148      22.515  12.649  15.828  1.00 23.45           N  
ATOM   1168  CA  HIS A 148      21.987  11.303  15.646  1.00 25.07           C  
ATOM   1169  C   HIS A 148      21.211  10.821  16.853  1.00 25.44           C  
ATOM   1170  O   HIS A 148      20.182  10.147  16.735  1.00 26.74           O  
ATOM   1171  CB  HIS A 148      23.188  10.386  15.351  1.00 23.60           C  
ATOM   1172  CG  HIS A 148      23.614  10.345  13.924  1.00 21.00           C  
ATOM   1173  ND1 HIS A 148      23.433  11.378  13.038  1.00 28.01           N  
ATOM   1174  CD2 HIS A 148      24.469   9.485  13.303  1.00 22.67           C  
ATOM   1175  CE1 HIS A 148      23.989  11.080  11.874  1.00 20.28           C  
ATOM   1176  NE2 HIS A 148      24.649   9.959  12.022  1.00 21.18           N  
ATOM   1177  N   THR A 149      21.664  11.165  18.036  1.00 24.87           N  
ATOM   1178  CA  THR A 149      21.115  10.818  19.317  1.00 27.48           C  
ATOM   1179  C   THR A 149      19.862  11.577  19.723  1.00 28.97           C  
ATOM   1180  O   THR A 149      18.924  10.954  20.255  1.00 30.57           O  
ATOM   1181  CB  THR A 149      22.187  11.066  20.428  1.00 26.42           C  
ATOM   1182  OG1 THR A 149      23.237  10.105  20.252  1.00 32.52           O  
ATOM   1183  CG2 THR A 149      21.625  10.944  21.825  1.00 32.65           C  
ATOM   1184  N   ARG A 150      19.835  12.874  19.542  1.00 28.24           N  
ATOM   1185  CA  ARG A 150      18.742  13.736  19.933  1.00 28.66           C  
ATOM   1186  C   ARG A 150      17.589  13.748  18.950  1.00 26.62           C  
ATOM   1187  O   ARG A 150      16.488  14.170  19.322  1.00 26.51           O  
ATOM   1188  CB  ARG A 150      19.319  15.169  20.104  1.00 31.74           C  
ATOM   1189  CG  ARG A 150      20.307  15.239  21.272  1.00 40.56           C  
ATOM   1190  CD  ARG A 150      19.631  15.666  22.562  1.00 43.51           C  
ATOM   1191  NE  ARG A 150      19.772  17.101  22.802  1.00 46.90           N  
ATOM   1192  CZ  ARG A 150      18.966  17.819  23.570  1.00 48.79           C  
ATOM   1193  NH1 ARG A 150      17.882  17.266  24.102  1.00 51.84           N  
ATOM   1194  NH2 ARG A 150      19.188  19.104  23.764  1.00 49.89           N  
ATOM   1195  N   ALA A 151      17.811  13.333  17.707  1.00 24.74           N  
ATOM   1196  CA  ALA A 151      16.715  13.338  16.732  1.00 25.85           C  
ATOM   1197  C   ALA A 151      16.104  14.708  16.508  1.00 25.61           C  
ATOM   1198  O   ALA A 151      14.868  14.865  16.557  1.00 25.57           O  
ATOM   1199  CB  ALA A 151      15.640  12.358  17.216  1.00 24.21           C  
ATOM   1200  N   PHE A 152      16.926  15.734  16.303  1.00 24.78           N  
ATOM   1201  CA  PHE A 152      16.437  17.065  16.020  1.00 24.22           C  
ATOM   1202  C   PHE A 152      15.771  17.053  14.642  1.00 25.15           C  
ATOM   1203  O   PHE A 152      16.353  16.424  13.746  1.00 25.67           O  
ATOM   1204  CB  PHE A 152      17.526  18.122  15.976  1.00 27.88           C  
ATOM   1205  CG  PHE A 152      18.274  18.404  17.236  1.00 23.29           C  
ATOM   1206  CD1 PHE A 152      17.784  19.290  18.167  1.00 26.74           C  
ATOM   1207  CD2 PHE A 152      19.494  17.782  17.482  1.00 28.05           C  
ATOM   1208  CE1 PHE A 152      18.489  19.559  19.334  1.00 29.59           C  
ATOM   1209  CE2 PHE A 152      20.197  18.055  18.633  1.00 26.46           C  
ATOM   1210  CZ  PHE A 152      19.698  18.942  19.568  1.00 24.96           C  
ATOM   1211  N   ASP A 153      14.655  17.721  14.461  1.00 26.18           N  
ATOM   1212  CA  ASP A 153      14.069  17.736  13.101  1.00 27.91           C  
ATOM   1213  C   ASP A 153      15.031  18.395  12.117  1.00 27.07           C  
ATOM   1214  O   ASP A 153      15.844  19.248  12.506  1.00 25.05           O  
ATOM   1215  CB  ASP A 153      12.719  18.432  13.108  1.00 34.82           C  
ATOM   1216  CG  ASP A 153      11.694  17.727  13.982  1.00 41.24           C  
ATOM   1217  OD1 ASP A 153      11.199  16.646  13.599  1.00 42.63           O  
ATOM   1218  OD2 ASP A 153      11.370  18.259  15.065  1.00 43.01           O  
ATOM   1219  N   LYS A 154      14.958  18.006  10.849  1.00 26.75           N  
ATOM   1220  CA  LYS A 154      15.821  18.625   9.832  1.00 27.74           C  
ATOM   1221  C   LYS A 154      15.254  19.990   9.477  1.00 25.64           C  
ATOM   1222  O   LYS A 154      14.054  20.221   9.661  1.00 26.92           O  
ATOM   1223  CB  LYS A 154      15.977  17.715   8.613  1.00 34.11           C  
ATOM   1224  CG  LYS A 154      16.710  16.436   9.018  1.00 40.69           C  
ATOM   1225  CD  LYS A 154      17.191  15.644   7.820  1.00 41.63           C  
ATOM   1226  CE  LYS A 154      18.010  14.447   8.297  1.00 44.88           C  
ATOM   1227  NZ  LYS A 154      18.574  13.681   7.150  1.00 46.59           N  
ATOM   1228  N   LEU A 155      16.085  20.906   8.993  1.00 23.46           N  
ATOM   1229  CA  LEU A 155      15.612  22.252   8.712  1.00 20.39           C  
ATOM   1230  C   LEU A 155      15.267  22.488   7.248  1.00 18.39           C  
ATOM   1231  O   LEU A 155      15.853  21.897   6.363  1.00 18.59           O  
ATOM   1232  CB  LEU A 155      16.693  23.258   9.149  1.00 17.90           C  
ATOM   1233  CG  LEU A 155      17.241  23.178  10.572  1.00 18.46           C  
ATOM   1234  CD1 LEU A 155      18.319  24.259  10.769  1.00 17.54           C  
ATOM   1235  CD2 LEU A 155      16.167  23.311  11.637  1.00 19.60           C  
ATOM   1236  N   ASN A 156      14.325  23.381   6.996  1.00 17.31           N  
ATOM   1237  CA  ASN A 156      13.946  23.808   5.671  1.00 16.88           C  
ATOM   1238  C   ASN A 156      14.891  24.922   5.222  1.00 15.48           C  
ATOM   1239  O   ASN A 156      15.454  25.584   6.099  1.00 11.99           O  
ATOM   1240  CB  ASN A 156      12.540  24.384   5.599  1.00 25.26           C  
ATOM   1241  CG  ASN A 156      11.463  23.359   5.893  1.00 32.73           C  
ATOM   1242  OD1 ASN A 156      11.435  22.331   5.223  1.00 33.56           O  
ATOM   1243  ND2 ASN A 156      10.609  23.628   6.866  1.00 31.32           N  
ATOM   1244  N   LYS A 157      15.012  25.150   3.927  1.00 16.74           N  
ATOM   1245  CA  LYS A 157      15.881  26.234   3.472  1.00 16.46           C  
ATOM   1246  C   LYS A 157      15.086  27.487   3.213  1.00 16.79           C  
ATOM   1247  O   LYS A 157      13.903  27.405   2.916  1.00 17.53           O  
ATOM   1248  CB  LYS A 157      16.662  25.806   2.212  1.00 22.71           C  
ATOM   1249  CG  LYS A 157      17.644  24.727   2.715  1.00 23.75           C  
ATOM   1250  CD  LYS A 157      18.747  24.442   1.754  1.00 31.55           C  
ATOM   1251  CE  LYS A 157      19.608  23.297   2.329  1.00 30.14           C  
ATOM   1252  NZ  LYS A 157      20.536  22.821   1.269  1.00 33.01           N  
ATOM   1253  N   TRP A 158      15.754  28.621   3.356  1.00 15.87           N  
ATOM   1254  CA  TRP A 158      15.178  29.918   3.096  1.00 14.85           C  
ATOM   1255  C   TRP A 158      14.905  29.992   1.600  1.00 15.17           C  
ATOM   1256  O   TRP A 158      13.983  30.656   1.110  1.00 17.82           O  
ATOM   1257  CB  TRP A 158      16.124  31.027   3.552  1.00 15.37           C  
ATOM   1258  CG  TRP A 158      15.514  32.401   3.522  1.00 17.10           C  
ATOM   1259  CD1 TRP A 158      15.494  33.288   2.480  1.00 13.37           C  
ATOM   1260  CD2 TRP A 158      14.839  33.036   4.611  1.00 12.83           C  
ATOM   1261  NE1 TRP A 158      14.835  34.430   2.859  1.00 15.47           N  
ATOM   1262  CE2 TRP A 158      14.421  34.298   4.167  1.00 12.86           C  
ATOM   1263  CE3 TRP A 158      14.545  32.643   5.935  1.00 13.84           C  
ATOM   1264  CZ2 TRP A 158      13.717  35.191   4.980  1.00 15.34           C  
ATOM   1265  CZ3 TRP A 158      13.822  33.504   6.726  1.00 14.12           C  
ATOM   1266  CH2 TRP A 158      13.440  34.778   6.257  1.00 15.48           C  
ATOM   1267  OXT TRP A 158      15.791  29.519   0.855  1.00 14.47           O  
TER    1268      TRP A 158                                                      
HETATM 1269  PG  ATP A 200      21.458  33.569  23.543  1.00 14.98           P  
HETATM 1270  O1G ATP A 200      21.649  32.730  22.351  1.00 14.01           O  
HETATM 1271  O2G ATP A 200      20.773  32.806  24.614  1.00 13.48           O  
HETATM 1272  O3G ATP A 200      22.790  34.015  24.029  1.00 16.16           O  
HETATM 1273  PB  ATP A 200      20.948  36.119  22.341  1.00 17.71           P  
HETATM 1274  O1B ATP A 200      19.803  36.794  21.727  1.00 20.59           O  
HETATM 1275  O2B ATP A 200      21.951  35.701  21.408  1.00 15.08           O  
HETATM 1276  O3B ATP A 200      20.553  34.848  23.238  1.00 15.75           O  
HETATM 1277  PA  ATP A 200      22.515  38.342  23.089  1.00 17.50           P  
HETATM 1278  O1A ATP A 200      22.895  38.568  21.735  1.00 11.54           O  
HETATM 1279  O2A ATP A 200      21.826  39.645  23.436  1.00 14.20           O  
HETATM 1280  O3A ATP A 200      21.652  37.049  23.443  1.00 15.18           O  
HETATM 1281  O5' ATP A 200      23.713  38.060  24.089  1.00 20.50           O  
HETATM 1282  C5' ATP A 200      24.724  39.054  24.181  1.00 21.21           C  
HETATM 1283  C4' ATP A 200      25.438  38.837  25.536  1.00 18.74           C  
HETATM 1284  O4' ATP A 200      25.947  37.496  25.559  1.00 20.34           O  
HETATM 1285  C3' ATP A 200      26.603  39.805  25.628  1.00 23.43           C  
HETATM 1286  O3' ATP A 200      26.678  40.287  27.003  1.00 34.49           O  
HETATM 1287  C2' ATP A 200      27.795  38.856  25.240  1.00 20.31           C  
HETATM 1288  O2' ATP A 200      28.916  39.322  26.042  1.00 19.31           O  
HETATM 1289  C1' ATP A 200      27.308  37.510  25.843  1.00 18.98           C  
HETATM 1290  N9  ATP A 200      27.960  36.340  25.287  1.00 15.97           N  
HETATM 1291  C8  ATP A 200      28.441  35.285  25.986  1.00 11.82           C  
HETATM 1292  N7  ATP A 200      28.887  34.286  25.290  1.00 15.86           N  
HETATM 1293  C5  ATP A 200      28.718  34.675  24.048  1.00 12.19           C  
HETATM 1294  C6  ATP A 200      29.010  34.011  22.879  1.00 15.01           C  
HETATM 1295  N6  ATP A 200      29.553  32.800  22.777  1.00 14.58           N  
HETATM 1296  N1  ATP A 200      28.732  34.654  21.721  1.00 15.16           N  
HETATM 1297  C2  ATP A 200      28.165  35.910  21.770  1.00 15.27           C  
HETATM 1298  N3  ATP A 200      27.843  36.603  22.847  1.00 14.89           N  
HETATM 1299  C4  ATP A 200      28.141  35.929  23.970  1.00 13.97           C  
HETATM 1300  N2  87Y A 201      16.636  30.962  15.501  1.00  7.79           N  
HETATM 1301  C3  87Y A 201      17.399  31.751  16.293  1.00 10.29           C  
HETATM 1302  O8  87Y A 201      18.472  32.210  15.789  1.00  9.92           O  
HETATM 1303  C7  87Y A 201      16.942  31.867  17.673  1.00 10.87           C  
HETATM 1304  N10 87Y A 201      17.718  32.599  18.607  1.00 12.74           N  
HETATM 1305  C12 87Y A 201      17.288  32.844  19.784  1.00 13.48           C  
HETATM 1306  C15 87Y A 201      17.924  33.745  20.807  1.00 16.76           C  
HETATM 1307  O16 87Y A 201      19.271  33.683  20.389  1.00 19.97           O  
HETATM 1308  C11 87Y A 201      15.929  32.422  20.289  1.00 14.39           C  
HETATM 1309  C14 87Y A 201      15.764  32.037  21.735  1.00 14.42           C  
HETATM 1310  C13 87Y A 201      15.181  33.836  20.108  1.00 10.34           C  
HETATM 1311  N9  87Y A 201      15.193  31.601  19.313  1.00 13.18           N  
HETATM 1312  C6  87Y A 201      15.741  31.402  18.103  1.00 11.45           C  
HETATM 1313  N4  87Y A 201      15.043  30.628  17.143  1.00 10.33           N  
HETATM 1314  C1  87Y A 201      15.512  30.392  15.941  1.00  9.31           C  
HETATM 1315  N5  87Y A 201      14.825  29.597  15.134  1.00  8.19           N  
HETATM 1316  C17 87Y A 201      16.578  30.697  21.847  1.00 17.14           C  
HETATM 1317  C18 87Y A 201      16.097  30.055  23.122  1.00 21.01           C  
HETATM 1318  C19 87Y A 201      16.283  30.607  24.376  1.00 22.71           C  
HETATM 1319  C20 87Y A 201      15.882  30.041  25.589  1.00 24.35           C  
HETATM 1320  C21 87Y A 201      15.235  28.798  25.525  1.00 25.10           C  
HETATM 1321  C22 87Y A 201      15.053  28.238  24.256  1.00 23.39           C  
HETATM 1322  C23 87Y A 201      15.459  28.797  23.039  1.00 22.62           C  
HETATM 1323 MG    MG A 202      21.866  33.755  19.969  1.00 17.30          MG  
HETATM 1324 MG    MG A 203      23.912  36.685  20.539  1.00 23.64          MG  
HETATM 1325  O   HOH A2001      43.473  33.578  17.850  1.00 22.09           O  
HETATM 1326  O   HOH A2002      41.670  26.398  15.186  1.00 25.68           O  
HETATM 1327  O   HOH A2003       7.498  39.409   9.681  1.00 48.28           O  
HETATM 1328  O   HOH A2004       8.499  42.041  11.154  1.00 46.62           O  
HETATM 1329  O   HOH A2005      11.855  38.517   4.142  1.00 33.84           O  
HETATM 1330  O   HOH A2006      10.810  39.375   9.469  1.00 29.18           O  
HETATM 1331  O   HOH A2007      10.489  43.562  10.020  1.00 30.02           O  
HETATM 1332  O   HOH A2008      11.540  41.281   7.296  1.00 25.25           O  
HETATM 1333  O   HOH A2009      12.852  45.474   5.339  1.00 45.64           O  
HETATM 1334  O   HOH A2010      49.738  43.545  15.686  1.00 46.06           O  
HETATM 1335  O   HOH A2011      14.576  38.656   3.375  1.00 16.26           O  
HETATM 1336  O   HOH A2012      17.489  47.093   0.175  1.00 40.22           O  
HETATM 1337  O   HOH A2013      14.056  45.451   0.984  1.00 57.64           O  
HETATM 1338  O   HOH A2014      22.679  43.539   2.661  1.00 44.47           O  
HETATM 1339  O   HOH A2015      13.588  23.533  13.836  1.00 40.89           O  
HETATM 1340  O   HOH A2016      26.864  36.652  -0.582  1.00 37.91           O  
HETATM 1341  O   HOH A2017      27.325  38.822   0.915  1.00 28.17           O  
HETATM 1342  O   HOH A2018      28.086  45.048   5.391  1.00 20.50           O  
HETATM 1343  O   HOH A2019      32.122  37.903   2.584  1.00 36.87           O  
HETATM 1344  O   HOH A2020      33.317  42.620  -0.278  1.00 63.03           O  
HETATM 1345  O   HOH A2021      30.086  37.714   0.679  1.00 41.53           O  
HETATM 1346  O   HOH A2022      34.052  41.405   2.845  1.00 42.02           O  
HETATM 1347  O   HOH A2023      33.743  44.476   9.647  1.00 23.60           O  
HETATM 1348  O   HOH A2024      39.735  40.607   6.706  1.00 29.17           O  
HETATM 1349  O   HOH A2025      44.300  34.812  10.144  1.00 29.80           O  
HETATM 1350  O   HOH A2026      48.801  42.124  13.788  1.00 50.50           O  
HETATM 1351  O   HOH A2027      43.871  42.584   8.576  1.00 38.86           O  
HETATM 1352  O   HOH A2028      25.323  47.199   6.716  1.00 44.73           O  
HETATM 1353  O   HOH A2029      36.837  36.531   4.015  1.00 26.80           O  
HETATM 1354  O   HOH A2030      25.644  29.626   1.274  1.00 34.60           O  
HETATM 1355  O   HOH A2031      21.969  26.363  -0.450  1.00 35.11           O  
HETATM 1356  O   HOH A2032      25.189  25.653  -0.805  1.00 58.75           O  
HETATM 1357  O   HOH A2033      21.111  28.419   0.757  1.00 10.94           O  
HETATM 1358  O   HOH A2034       9.221  32.265   6.686  1.00 49.48           O  
HETATM 1359  O   HOH A2035      13.250  24.605   9.351  1.00 21.04           O  
HETATM 1360  O   HOH A2036      28.360  26.433  29.673  1.00 37.47           O  
HETATM 1361  O   HOH A2037      38.228  38.734  30.092  1.00 51.31           O  
HETATM 1362  O   HOH A2038      37.668  39.598  27.579  1.00 45.51           O  
HETATM 1363  O   HOH A2039      13.806  25.776  15.159  1.00 30.24           O  
HETATM 1364  O   HOH A2040      29.533  23.079  26.261  1.00 43.48           O  
HETATM 1365  O   HOH A2041      10.235  26.738  22.058  1.00 47.18           O  
HETATM 1366  O   HOH A2042      24.634  21.163  26.980  1.00 46.52           O  
HETATM 1367  O   HOH A2043       5.356  31.553  15.334  1.00 18.31           O  
HETATM 1368  O   HOH A2044       6.164  28.709  14.897  1.00 43.38           O  
HETATM 1369  O   HOH A2045       2.920  33.537  20.719  1.00 33.24           O  
HETATM 1370  O   HOH A2046       6.933  37.621  23.594  1.00 42.44           O  
HETATM 1371  O   HOH A2047       8.898  37.545  21.462  1.00 42.61           O  
HETATM 1372  O   HOH A2048       6.915  32.645  13.282  1.00 16.08           O  
HETATM 1373  O   HOH A2049      30.412  11.043  15.279  1.00 64.24           O  
HETATM 1374  O   HOH A2050       5.903  32.423   8.829  1.00 60.47           O  
HETATM 1375  O   HOH A2051      10.910  36.056   8.800  1.00 23.97           O  
HETATM 1376  O   HOH A2052       7.446  34.411   9.735  1.00 21.61           O  
HETATM 1377  O   HOH A2053       6.756  29.351  12.024  1.00 25.58           O  
HETATM 1378  O   HOH A2054       9.196  27.958   8.813  1.00 53.14           O  
HETATM 1379  O   HOH A2055      21.788  31.501  15.857  1.00 17.43           O  
HETATM 1380  O   HOH A2056       9.787  26.604   4.724  1.00 44.59           O  
HETATM 1381  O   HOH A2057      43.860  27.329  12.942  1.00 41.76           O  
HETATM 1382  O   HOH A2058      45.359  32.621  11.694  1.00 38.23           O  
HETATM 1383  O   HOH A2059      46.189  39.204  16.746  1.00 34.41           O  
HETATM 1384  O   HOH A2060      46.621  36.854  10.612  1.00 30.28           O  
HETATM 1385  O   HOH A2061      44.125  38.048  25.154  1.00 41.03           O  
HETATM 1386  O   HOH A2062      38.661  35.817  26.717  1.00 51.02           O  
HETATM 1387  O   HOH A2063      45.507  39.849  19.071  1.00 45.86           O  
HETATM 1388  O   HOH A2064      39.432  43.628  24.436  1.00 54.57           O  
HETATM 1389  O   HOH A2065      32.156  46.708  19.902  1.00 25.15           O  
HETATM 1390  O   HOH A2066      26.051  44.763  19.466  1.00 35.12           O  
HETATM 1391  O   HOH A2067      31.246  45.848  22.106  1.00 35.80           O  
HETATM 1392  O   HOH A2068      25.646  38.194  19.789  1.00  9.90           O  
HETATM 1393  O   HOH A2069      22.268  49.593  16.721  1.00 36.19           O  
HETATM 1394  O   HOH A2070      27.219  45.422   8.202  1.00 27.87           O  
HETATM 1395  O   HOH A2071      19.147  46.977   9.898  1.00 28.78           O  
HETATM 1396  O   HOH A2072      16.367  46.560  16.161  1.00 26.52           O  
HETATM 1397  O   HOH A2073      18.103  42.227  21.137  1.00 43.14           O  
HETATM 1398  O   HOH A2074      23.727  46.287  20.152  1.00 38.15           O  
HETATM 1399  O   HOH A2075      16.617  46.450  18.678  1.00 43.85           O  
HETATM 1400  O   HOH A2076      17.465  48.907  25.866  1.00 47.59           O  
HETATM 1401  O   HOH A2077      22.408  47.406  22.071  1.00 55.91           O  
HETATM 1402  O   HOH A2078      17.955  42.152  24.202  1.00 43.67           O  
HETATM 1403  O   HOH A2079      14.516  40.946  23.230  1.00 45.75           O  
HETATM 1404  O   HOH A2080      13.644  37.509  26.231  1.00 51.93           O  
HETATM 1405  O   HOH A2081      14.540  42.067  20.624  1.00 39.41           O  
HETATM 1406  O   HOH A2082      16.629  43.481  18.992  1.00 30.51           O  
HETATM 1407  O   HOH A2083      17.228  44.216  16.444  1.00 21.99           O  
HETATM 1408  O   HOH A2084      19.476  34.819  16.682  1.00 11.78           O  
HETATM 1409  O   HOH A2085      23.390  33.626  16.185  1.00  9.97           O  
HETATM 1410  O   HOH A2086      28.378  39.362  18.765  1.00 14.33           O  
HETATM 1411  O   HOH A2087      42.501  26.112  20.449  1.00 48.47           O  
HETATM 1412  O   HOH A2088      41.252  31.736  25.284  1.00 64.75           O  
HETATM 1413  O   HOH A2089      35.789  26.309  21.442  1.00 13.97           O  
HETATM 1414  O   HOH A2090      40.672  26.454  27.071  1.00 36.50           O  
HETATM 1415  O   HOH A2091      35.827  31.637  34.814  1.00 29.65           O  
HETATM 1416  O   HOH A2092      29.707  28.200  31.767  1.00 40.96           O  
HETATM 1417  O   HOH A2093      37.771  31.419  31.068  1.00 25.52           O  
HETATM 1418  O   HOH A2094      32.296  27.254  28.669  1.00 23.42           O  
HETATM 1419  O   HOH A2095      36.244  37.125  27.974  1.00 35.15           O  
HETATM 1420  O   HOH A2096      34.366  39.498  31.516  1.00 49.44           O  
HETATM 1421  O   HOH A2097      32.976  40.075  37.382  1.00 45.63           O  
HETATM 1422  O   HOH A2098      29.825  30.831  31.771  1.00 35.04           O  
HETATM 1423  O   HOH A2099      27.439  31.420  25.515  1.00 14.07           O  
HETATM 1424  O   HOH A2100      29.285  34.639  29.553  1.00 34.80           O  
HETATM 1425  O   HOH A2101      29.994  26.310  27.522  1.00 19.19           O  
HETATM 1426  O   HOH A2102      27.585  24.007  24.856  1.00 30.20           O  
HETATM 1427  O   HOH A2103      18.797  29.504  26.121  1.00 43.43           O  
HETATM 1428  O   HOH A2104      21.740  25.101  28.233  1.00 33.75           O  
HETATM 1429  O   HOH A2105      25.178  23.420  24.983  1.00 20.67           O  
HETATM 1430  O   HOH A2106      19.084  19.112  27.437  1.00 59.15           O  
HETATM 1431  O   HOH A2107      16.098  22.593  18.302  1.00 26.16           O  
HETATM 1432  O   HOH A2108      15.963  24.318  15.942  1.00 31.20           O  
HETATM 1433  O   HOH A2109      22.533  29.488  13.502  1.00 17.90           O  
HETATM 1434  O   HOH A2110      27.723  17.407   6.524  1.00 24.53           O  
HETATM 1435  O   HOH A2111      33.384  22.813   5.072  1.00 47.96           O  
HETATM 1436  O   HOH A2112      31.023  15.026  14.275  1.00 18.91           O  
HETATM 1437  O   HOH A2113      32.156  12.296  14.185  1.00 35.00           O  
HETATM 1438  O   HOH A2114      34.478  18.182   9.484  1.00 30.08           O  
HETATM 1439  O   HOH A2115      36.913  19.039  15.495  1.00 33.08           O  
HETATM 1440  O   HOH A2116      36.275  21.805  19.185  1.00 41.18           O  
HETATM 1441  O   HOH A2117      38.361  18.039  21.032  1.00 40.67           O  
HETATM 1442  O   HOH A2118      32.245  21.171  25.224  1.00 33.19           O  
HETATM 1443  O   HOH A2119      30.233  11.736  21.194  1.00 26.04           O  
HETATM 1444  O   HOH A2120      28.037  14.863   6.228  1.00 44.07           O  
HETATM 1445  O   HOH A2121      25.281  11.443   9.164  1.00 50.04           O  
HETATM 1446  O   HOH A2122      27.007   8.330  17.283  1.00 48.48           O  
HETATM 1447  O   HOH A2123      18.894  13.052  13.453  1.00 43.81           O  
HETATM 1448  O   HOH A2124      16.387  20.417  23.006  1.00 52.66           O  
HETATM 1449  O   HOH A2125       9.228  15.729  15.282  1.00 59.31           O  
HETATM 1450  O   HOH A2126      15.673  21.301  14.637  1.00 30.62           O  
HETATM 1451  O   HOH A2127      14.168  19.698  16.815  1.00 36.11           O  
HETATM 1452  O   HOH A2128      13.143  15.644  10.417  1.00 48.49           O  
HETATM 1453  O   HOH A2129      18.433  20.176   5.825  1.00 49.81           O  
HETATM 1454  O   HOH A2130      18.659  20.063   8.564  1.00 31.33           O  
HETATM 1455  O   HOH A2131      13.457  23.180   2.193  1.00 42.34           O  
HETATM 1456  O   HOH A2132      11.517  28.123   3.034  1.00 41.60           O  
HETATM 1457  O   HOH A2133      15.342  28.617  -1.568  1.00 25.90           O  
HETATM 1458  O   HOH A2134      13.973  32.142  -1.143  1.00 21.41           O  
HETATM 1459  O   HOH A2135      18.491  28.823   1.198  1.00 14.38           O  
HETATM 1460  O   HOH A2136      24.899  35.968  22.763  1.00 18.28           O  
HETATM 1461  O   HOH A2137      25.761  33.262  24.793  1.00 25.71           O  
HETATM 1462  O   HOH A2138      19.144  40.042  23.235  1.00 30.41           O  
HETATM 1463  O   HOH A2139      29.858  41.939  25.864  1.00 26.31           O  
HETATM 1464  O   HOH A2140      27.219  39.301  21.630  1.00 16.16           O  
HETATM 1465  O   HOH A2141      20.708  32.030  18.428  1.00 14.81           O  
CONECT  733 1324                                                                
CONECT  734 1323                                                                
CONECT  749 1324                                                                
CONECT  750 1323                                                                
CONECT 1269 1270 1271 1272 1276                                                 
CONECT 1270 1269 1323                                                           
CONECT 1271 1269                                                                
CONECT 1272 1269                                                                
CONECT 1273 1274 1275 1276 1280                                                 
CONECT 1274 1273                                                                
CONECT 1275 1273 1323 1324                                                      
CONECT 1276 1269 1273                                                           
CONECT 1277 1278 1279 1280 1281                                                 
CONECT 1278 1277 1324                                                           
CONECT 1279 1277                                                                
CONECT 1280 1273 1277                                                           
CONECT 1281 1277 1282                                                           
CONECT 1282 1281 1283                                                           
CONECT 1283 1282 1284 1285                                                      
CONECT 1284 1283 1289                                                           
CONECT 1285 1283 1286 1287                                                      
CONECT 1286 1285                                                                
CONECT 1287 1285 1288 1289                                                      
CONECT 1288 1287                                                                
CONECT 1289 1284 1287 1290                                                      
CONECT 1290 1289 1291 1299                                                      
CONECT 1291 1290 1292                                                           
CONECT 1292 1291 1293                                                           
CONECT 1293 1292 1294 1299                                                      
CONECT 1294 1293 1295 1296                                                      
CONECT 1295 1294                                                                
CONECT 1296 1294 1297                                                           
CONECT 1297 1296 1298                                                           
CONECT 1298 1297 1299                                                           
CONECT 1299 1290 1293 1298                                                      
CONECT 1300 1301 1314                                                           
CONECT 1301 1300 1302 1303                                                      
CONECT 1302 1301                                                                
CONECT 1303 1301 1304 1312                                                      
CONECT 1304 1303 1305                                                           
CONECT 1305 1304 1306 1308                                                      
CONECT 1306 1305 1307                                                           
CONECT 1307 1306 1323                                                           
CONECT 1308 1305 1309 1310 1311                                                 
CONECT 1309 1308 1316                                                           
CONECT 1310 1308                                                                
CONECT 1311 1308 1312                                                           
CONECT 1312 1303 1311 1313                                                      
CONECT 1313 1312 1314                                                           
CONECT 1314 1300 1313 1315                                                      
CONECT 1315 1314                                                                
CONECT 1316 1309 1317                                                           
CONECT 1317 1316 1318 1322                                                      
CONECT 1318 1317 1319                                                           
CONECT 1319 1318 1320                                                           
CONECT 1320 1319 1321                                                           
CONECT 1321 1320 1322                                                           
CONECT 1322 1317 1321                                                           
CONECT 1323  734  750 1270 1275                                                 
CONECT 1323 1307 1465                                                           
CONECT 1324  733  749 1275 1278                                                 
CONECT 1324 1392 1460                                                           
CONECT 1392 1324                                                                
CONECT 1460 1324                                                                
CONECT 1465 1323                                                                
MASTER      313    0    4    5   10    0   14    6 1464    1   65   13          
END                                                                             
