HEADER    HYDROLASE                               27-MAR-24   9B7E              
TITLE     S_SAD STRUCTURE OF HEWL USING LOSSY COMPRESSION DATA WITH A           
TITLE    2 COMPRESSION RATIO OF 422                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LYSOZYME C;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: LYZOZYME;                                                  
COMPND   5 SYNONYM: 1,4-BETA-N-ACETYLMURAMIDASE C,ALLERGEN GAL D IV;            
COMPND   6 EC: 3.2.1.17;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE   3 ORGANISM_COMMON: CHICKEN;                                            
SOURCE   4 ORGANISM_TAXID: 9031;                                                
SOURCE   5 GENE: LYZ;                                                           
SOURCE   6 EXPRESSION_SYSTEM: GALLUS GALLUS;                                    
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9031                                        
KEYWDS    LOSSY COMPRESSION, INTENSITY PRESERVATION, STRUCTURAL INFORMATION     
KEYWDS   2 RETENTION, S_SAD PHASING, HYDROLASE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.JAKONCIC,H.J.BERNSTEIN,A.S.SOARES,K.HORVAT                          
REVDAT   1   10-APR-24 9B7E    0                                                
JRNL        AUTH   J.JAKONCIC,H.J.BERNSTEIN,A.S.SOARES,K.HORVAT                 
JRNL        TITL   INVESTIGATION OF FAST AND EFFICIENT LOSSLESS COMPRESSION     
JRNL        TITL 2 ALGORITHMS FOR MACROMOLECULAR CRYSTALLOGRAPHY EXPERIMENTS    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0267                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.73                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 11589                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.163                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.200                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 648                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 185                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 19.41                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1760                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 20                           
REMARK   3   BIN FREE R VALUE                    : 0.2150                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1001                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 118                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 9.78                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : -0.02000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.124         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.117         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.060         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.751         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1163 ; 0.022 ; 0.012       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1561 ; 1.727 ; 1.645       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   156 ; 6.492 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    75 ;33.036 ;19.733       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   201 ;16.064 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;20.070 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   146 ; 0.112 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   899 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   545 ; 0.691 ; 0.766       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   686 ; 1.135 ; 1.146       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   618 ; 1.151 ; 0.947       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: U VALUES : REFINED INDIVIDUALLY           
REMARK   4                                                                      
REMARK   4 9B7E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAR-24.                  
REMARK 100 THE DEPOSITION ID IS D_1000282734.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-NOV-23                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS-II                            
REMARK 200  BEAMLINE                       : 17-ID-1                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.65                               
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : KB MIRROS                          
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 9M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12280                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.640                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.730                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 83.2                               
REMARK 200  DATA REDUNDANCY                : 19.70                              
REMARK 200  R MERGE                    (I) : 0.04900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 49.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.67                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.11300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXDE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1000 MM NACL 100 MM NAACETATE PH 4.6     
REMARK 280  50 MM GLYCEROL 50 MM ETHYLEN GLYCOL DROP= 1 UL + 1UL, VAPOR         
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
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   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       18.47600            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       39.44650            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       39.44650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       27.71400            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       39.44650            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       39.44650            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        9.23800            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       39.44650            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       39.44650            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       27.71400            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       39.44650            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       39.44650            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        9.23800            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       18.47600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 372  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 415  LIES ON A SPECIAL POSITION.                          
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    ARG A  45   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 215  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A  53   O                                                      
REMARK 620 2 SER A  91   OG  119.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 213  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  60   O                                                      
REMARK 620 2 CYS A  64   O    89.5                                              
REMARK 620 3 SER A  72   OG   89.5 165.6                                        
REMARK 620 4 ARG A  73   O    97.8  93.8 100.5                                  
REMARK 620 5 HOH A 362   O    98.2  88.6  77.4 163.9                            
REMARK 620 6 HOH A 378   O   171.4  98.6  81.9  84.5  79.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 214  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A  82   O                                                      
REMARK 620 2 ASP A  87   O   108.7                                              
REMARK 620 3 HOH A 321   O   111.6  70.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 216  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 332   O                                                      
REMARK 620 2 HOH A 361   O   102.4                                              
REMARK 620 N                    1                                               
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1W6Z   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 9B7F   RELATED DB: PDB                                   
DBREF  9B7E A    1   129  UNP    P00698   LYSC_CHICK      19    147             
SEQRES   1 A  129  LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS          
SEQRES   2 A  129  ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY          
SEQRES   3 A  129  ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN          
SEQRES   4 A  129  THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP          
SEQRES   5 A  129  TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN          
SEQRES   6 A  129  ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE          
SEQRES   7 A  129  PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER          
SEQRES   8 A  129  VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY          
SEQRES   9 A  129  MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY          
SEQRES  10 A  129  THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU              
HET    EDO  A 201       4                                                       
HET    EDO  A 202       4                                                       
HET    EDO  A 203       4                                                       
HET    EDO  A 204       4                                                       
HET     CL  A 205       1                                                       
HET     CL  A 206       1                                                       
HET     CL  A 207       1                                                       
HET     CL  A 208       1                                                       
HET     CL  A 209       1                                                       
HET     CL  A 210       1                                                       
HET     CL  A 211       1                                                       
HET     CL  A 212       1                                                       
HET     NA  A 213       1                                                       
HET     NA  A 214       1                                                       
HET     NA  A 215       1                                                       
HET     NA  A 216       1                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      CL CHLORIDE ION                                                     
HETNAM      NA SODIUM ION                                                       
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  EDO    4(C2 H6 O2)                                                  
FORMUL   6   CL    8(CL 1-)                                                     
FORMUL  14   NA    4(NA 1+)                                                     
FORMUL  18  HOH   *118(H2 O)                                                    
HELIX    1 AA1 GLY A    4  HIS A   15  1                                  12    
HELIX    2 AA2 ASN A   19  TYR A   23  5                                   5    
HELIX    3 AA3 SER A   24  ASN A   37  1                                  14    
HELIX    4 AA4 ILE A   55  GLN A   57  5                                   3    
HELIX    5 AA5 PRO A   79  SER A   85  5                                   7    
HELIX    6 AA6 ILE A   88  SER A  100  1                                  13    
HELIX    7 AA7 ASN A  103  ALA A  107  5                                   5    
HELIX    8 AA8 TRP A  108  CYS A  115  1                                   8    
HELIX    9 AA9 ASP A  119  ARG A  125  5                                   7    
SHEET    1 AA1 3 THR A  43  ARG A  45  0                                        
SHEET    2 AA1 3 THR A  51  TYR A  53 -1  O  ASP A  52   N  ASN A  44           
SHEET    3 AA1 3 ILE A  58  ASN A  59 -1  O  ILE A  58   N  TYR A  53           
SSBOND   1 CYS A    6    CYS A  127                          1555   1555  2.01  
SSBOND   2 CYS A   30    CYS A  115                          1555   1555  2.10  
SSBOND   3 CYS A   64    CYS A   80                          1555   1555  2.07  
SSBOND   4 CYS A   76    CYS A   94                          1555   1555  2.06  
LINK         O   TYR A  53                NA    NA A 215     1555   1555  2.56  
LINK         O   SER A  60                NA    NA A 213     1555   1555  2.30  
LINK         O   CYS A  64                NA    NA A 213     1555   1555  2.35  
LINK         OG  SER A  72                NA    NA A 213     1555   1555  2.48  
LINK         O   ARG A  73                NA    NA A 213     1555   1555  2.35  
LINK         O   ALA A  82                NA    NA A 214     1555   1555  2.59  
LINK         O   ASP A  87                NA    NA A 214     1555   1555  2.59  
LINK         OG  SER A  91                NA    NA A 215     1555   1555  2.67  
LINK        NA    NA A 213                 O   HOH A 362     1555   1555  2.57  
LINK        NA    NA A 213                 O   HOH A 378     1555   1555  2.44  
LINK        NA    NA A 214                 O   HOH A 321     1555   1555  3.05  
LINK        NA    NA A 216                 O   HOH A 332     1555   1555  3.06  
LINK        NA    NA A 216                 O   HOH A 361     1555   3644  2.89  
CRYST1   78.893   78.893   36.952  90.00  90.00  90.00 P 43 21 2     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      0.012675  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012675  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.027062        0.00000                         
ATOM      1  N   LYS A   1      82.062  10.053  28.291  1.00  7.18           N  
ATOM      2  CA ALYS A   1      81.065  10.428  27.234  0.50  7.31           C  
ATOM      3  CA BLYS A   1      81.079  10.427  27.226  0.50  7.26           C  
ATOM      4  C   LYS A   1      81.139  11.934  27.007  1.00  7.29           C  
ATOM      5  O   LYS A   1      81.126  12.707  27.969  1.00  7.72           O  
ATOM      6  CB ALYS A   1      79.656  10.024  27.682  0.50  7.54           C  
ATOM      7  CB BLYS A   1      79.666  10.018  27.651  0.50  7.43           C  
ATOM      8  CG ALYS A   1      78.564  10.268  26.652  0.50  7.67           C  
ATOM      9  CG BLYS A   1      78.574  10.496  26.709  0.50  7.44           C  
ATOM     10  CD ALYS A   1      77.176   9.991  27.170  0.50  7.69           C  
ATOM     11  CD BLYS A   1      77.207  10.015  27.086  0.50  7.46           C  
ATOM     12  CE ALYS A   1      76.133  10.668  26.308  0.50  8.00           C  
ATOM     13  CE BLYS A   1      76.171  10.662  26.196  0.50  7.69           C  
ATOM     14  NZ ALYS A   1      76.066  10.066  24.956  0.50  7.96           N  
ATOM     15  NZ BLYS A   1      74.907   9.897  26.231  0.50  7.54           N  
ATOM     16  N   VAL A   2      81.213  12.338  25.734  1.00  7.06           N  
ATOM     17  CA  VAL A   2      81.086  13.746  25.414  1.00  6.77           C  
ATOM     18  C   VAL A   2      79.669  13.977  24.917  1.00  6.86           C  
ATOM     19  O   VAL A   2      79.318  13.474  23.844  1.00  7.07           O  
ATOM     20  CB  VAL A   2      82.133  14.214  24.387  1.00  6.89           C  
ATOM     21  CG1 VAL A   2      81.877  15.655  23.984  1.00  6.94           C  
ATOM     22  CG2 VAL A   2      83.559  14.078  24.924  1.00  6.75           C  
ATOM     23  N   PHE A   3      78.871  14.712  25.705  1.00  6.71           N  
ATOM     24  CA  PHE A   3      77.492  14.997  25.323  1.00  6.90           C  
ATOM     25  C   PHE A   3      77.474  16.067  24.241  1.00  7.01           C  
ATOM     26  O   PHE A   3      78.314  16.971  24.221  1.00  6.96           O  
ATOM     27  CB  PHE A   3      76.690  15.535  26.527  1.00  6.73           C  
ATOM     28  CG  PHE A   3      76.156  14.472  27.453  1.00  6.87           C  
ATOM     29  CD1 PHE A   3      76.992  13.836  28.372  1.00  6.96           C  
ATOM     30  CD2 PHE A   3      74.808  14.120  27.419  1.00  7.08           C  
ATOM     31  CE1 PHE A   3      76.488  12.865  29.230  1.00  6.90           C  
ATOM     32  CE2 PHE A   3      74.304  13.139  28.267  1.00  6.83           C  
ATOM     33  CZ  PHE A   3      75.146  12.514  29.179  1.00  7.06           C  
ATOM     34  N   GLY A   4      76.444  15.991  23.379  1.00  7.27           N  
ATOM     35  CA  GLY A   4      76.009  17.145  22.606  1.00  7.68           C  
ATOM     36  C   GLY A   4      75.285  18.158  23.498  1.00  7.97           C  
ATOM     37  O   GLY A   4      74.784  17.836  24.572  1.00  7.92           O  
ATOM     38  N   ARG A   5      75.263  19.415  23.055  1.00  8.28           N  
ATOM     39  CA  ARG A   5      74.642  20.493  23.812  1.00  8.58           C  
ATOM     40  C   ARG A   5      73.175  20.183  24.149  1.00  8.42           C  
ATOM     41  O   ARG A   5      72.776  20.221  25.318  1.00  8.32           O  
ATOM     42  CB  ARG A   5      74.756  21.774  22.978  1.00  8.82           C  
ATOM     43  CG  ARG A   5      74.122  22.978  23.647  1.00  9.40           C  
ATOM     44  CD  ARG A   5      74.350  24.251  22.839  1.00  9.75           C  
ATOM     45  NE  ARG A   5      73.782  24.206  21.486  1.00 10.13           N  
ATOM     46  CZ  ARG A   5      72.530  24.533  21.163  1.00 10.67           C  
ATOM     47  NH1 ARG A   5      71.663  24.907  22.087  1.00 10.26           N  
ATOM     48  NH2 ARG A   5      72.141  24.475  19.894  1.00 11.56           N  
ATOM     49  N   CYS A   6      72.334  19.937  23.129  1.00  8.65           N  
ATOM     50  CA  CYS A   6      70.925  19.668  23.407  1.00  9.22           C  
ATOM     51  C   CYS A   6      70.759  18.322  24.127  1.00  8.69           C  
ATOM     52  O   CYS A   6      69.863  18.145  24.944  1.00  8.66           O  
ATOM     53  CB  CYS A   6      70.096  19.684  22.124  1.00  9.82           C  
ATOM     54  SG  CYS A   6      70.041  21.325  21.357  1.00 11.67           S  
ATOM     55  N   GLU A   7      71.621  17.352  23.821  1.00  8.22           N  
ATOM     56  CA  GLU A   7      71.561  16.060  24.483  1.00  7.96           C  
ATOM     57  C   GLU A   7      71.757  16.225  25.991  1.00  7.45           C  
ATOM     58  O   GLU A   7      71.040  15.616  26.789  1.00  7.14           O  
ATOM     59  CB  GLU A   7      72.621  15.141  23.859  1.00  8.80           C  
ATOM     60  CG  GLU A   7      72.623  13.744  24.441  1.00  9.17           C  
ATOM     61  CD  GLU A   7      73.830  12.905  24.080  1.00  9.73           C  
ATOM     62  OE1 GLU A   7      74.858  13.474  23.639  1.00  9.75           O  
ATOM     63  OE2 GLU A   7      73.745  11.681  24.305  1.00 10.85           O  
ATOM     64  N   LEU A   8      72.731  17.058  26.402  1.00  6.81           N  
ATOM     65  CA  LEU A   8      72.943  17.270  27.837  1.00  6.70           C  
ATOM     66  C   LEU A   8      71.808  18.086  28.458  1.00  6.77           C  
ATOM     67  O   LEU A   8      71.402  17.854  29.593  1.00  6.80           O  
ATOM     68  CB  LEU A   8      74.285  17.977  28.076  1.00  6.66           C  
ATOM     69  CG  LEU A   8      74.578  18.271  29.551  1.00  6.63           C  
ATOM     70  CD1 LEU A   8      74.747  16.974  30.331  1.00  6.85           C  
ATOM     71  CD2 LEU A   8      75.827  19.126  29.685  1.00  6.89           C  
ATOM     72  N   ALA A   9      71.312  19.089  27.738  1.00  7.20           N  
ATOM     73  CA  ALA A   9      70.170  19.841  28.241  1.00  7.23           C  
ATOM     74  C   ALA A   9      69.018  18.887  28.557  1.00  7.32           C  
ATOM     75  O   ALA A   9      68.386  18.978  29.607  1.00  7.17           O  
ATOM     76  CB  ALA A   9      69.765  20.888  27.237  1.00  7.36           C  
ATOM     77  N   ALA A  10      68.741  17.952  27.640  1.00  7.75           N  
ATOM     78  CA  ALA A  10      67.636  17.025  27.854  1.00  7.69           C  
ATOM     79  C   ALA A  10      67.899  16.121  29.060  1.00  7.96           C  
ATOM     80  O   ALA A  10      66.998  15.824  29.830  1.00  7.87           O  
ATOM     81  CB  ALA A  10      67.402  16.231  26.584  1.00  7.85           C  
ATOM     82  N   ALA A  11      69.145  15.662  29.220  1.00  7.56           N  
ATOM     83  CA  ALA A  11      69.485  14.782  30.324  1.00  7.95           C  
ATOM     84  C   ALA A  11      69.346  15.548  31.635  1.00  7.94           C  
ATOM     85  O   ALA A  11      68.857  15.012  32.641  1.00  7.88           O  
ATOM     86  CB  ALA A  11      70.887  14.248  30.130  1.00  8.09           C  
ATOM     87  N   MET A  12      69.785  16.814  31.620  1.00  7.76           N  
ATOM     88  CA  MET A  12      69.707  17.601  32.847  1.00  8.08           C  
ATOM     89  C   MET A  12      68.250  17.848  33.250  1.00  9.25           C  
ATOM     90  O   MET A  12      67.912  17.783  34.437  1.00  9.73           O  
ATOM     91  CB  MET A  12      70.455  18.923  32.683  1.00  7.14           C  
ATOM     92  CG  MET A  12      71.977  18.735  32.774  1.00  6.84           C  
ATOM     93  SD  MET A  12      72.782  20.309  32.381  1.00  6.76           S  
ATOM     94  CE  MET A  12      74.376  20.025  33.166  1.00  6.27           C  
ATOM     95  N   LYS A  13      67.395  18.090  32.253  1.00 10.48           N  
ATOM     96  CA  LYS A  13      65.980  18.328  32.520  1.00 12.48           C  
ATOM     97  C   LYS A  13      65.333  17.059  33.070  1.00 12.69           C  
ATOM     98  O   LYS A  13      64.565  17.110  34.020  1.00 12.62           O  
ATOM     99  CB  LYS A  13      65.271  18.750  31.232  1.00 13.53           C  
ATOM    100  CG  LYS A  13      63.775  19.008  31.352  1.00 16.02           C  
ATOM    101  CD  LYS A  13      63.255  19.564  30.038  1.00 17.31           C  
ATOM    102  CE  LYS A  13      62.092  20.513  30.226  1.00 21.69           C  
ATOM    103  NZ  LYS A  13      60.828  19.844  29.864  1.00 21.13           N  
ATOM    104  N   ARG A  14      65.682  15.913  32.487  1.00 13.34           N  
ATOM    105  CA AARG A  14      65.120  14.641  32.915  0.50 13.14           C  
ATOM    106  CA BARG A  14      65.174  14.613  32.896  0.50 13.36           C  
ATOM    107  C   ARG A  14      65.471  14.399  34.381  1.00 13.28           C  
ATOM    108  O   ARG A  14      64.641  13.882  35.116  1.00 13.18           O  
ATOM    109  CB AARG A  14      65.519  13.499  31.969  0.50 13.80           C  
ATOM    110  CB BARG A  14      65.810  13.550  31.989  0.50 14.31           C  
ATOM    111  CG AARG A  14      65.600  12.129  32.636  0.50 14.88           C  
ATOM    112  CG BARG A  14      65.467  12.112  32.346  0.50 15.81           C  
ATOM    113  CD AARG A  14      65.418  10.901  31.756  0.50 14.83           C  
ATOM    114  CD BARG A  14      64.069  11.724  31.909  0.50 15.83           C  
ATOM    115  NE AARG A  14      66.401   9.899  32.150  0.50 16.16           N  
ATOM    116  NE BARG A  14      63.695  10.573  32.704  0.50 17.76           N  
ATOM    117  CZ AARG A  14      66.265   9.041  33.151  0.50 15.25           C  
ATOM    118  CZ BARG A  14      62.651  10.542  33.506  0.50 17.33           C  
ATOM    119  NH1AARG A  14      65.163   9.021  33.876  0.50 15.43           N  
ATOM    120  NH1BARG A  14      61.850  11.593  33.592  0.50 18.61           N  
ATOM    121  NH2AARG A  14      67.238   8.194  33.417  0.50 16.75           N  
ATOM    122  NH2BARG A  14      62.404   9.450  34.198  0.50 18.65           N  
ATOM    123  N   HIS A  15      66.681  14.810  34.817  1.00 11.81           N  
ATOM    124  CA  HIS A  15      67.109  14.602  36.193  1.00 12.16           C  
ATOM    125  C   HIS A  15      66.697  15.751  37.116  1.00 11.36           C  
ATOM    126  O   HIS A  15      67.146  15.814  38.249  1.00 12.05           O  
ATOM    127  CB  HIS A  15      68.613  14.314  36.247  1.00 12.83           C  
ATOM    128  CG  HIS A  15      68.970  12.944  35.753  1.00 13.23           C  
ATOM    129  ND1 HIS A  15      69.193  12.674  34.410  1.00 14.44           N  
ATOM    130  CD2 HIS A  15      69.136  11.770  36.402  1.00 14.90           C  
ATOM    131  CE1 HIS A  15      69.479  11.389  34.254  1.00 14.36           C  
ATOM    132  NE2 HIS A  15      69.459  10.822  35.459  1.00 15.13           N  
ATOM    133  N   GLY A  16      65.877  16.679  36.623  1.00 11.45           N  
ATOM    134  CA  GLY A  16      65.252  17.686  37.477  1.00 10.68           C  
ATOM    135  C   GLY A  16      66.113  18.902  37.820  1.00 10.26           C  
ATOM    136  O   GLY A  16      65.842  19.592  38.811  1.00  9.99           O  
ATOM    137  N   LEU A  17      67.074  19.258  36.955  1.00 10.38           N  
ATOM    138  CA ALEU A  17      67.943  20.400  37.205  0.50 10.63           C  
ATOM    139  CA BLEU A  17      67.943  20.408  37.199  0.50 10.62           C  
ATOM    140  C   LEU A  17      67.330  21.685  36.639  1.00 10.88           C  
ATOM    141  O   LEU A  17      67.724  22.794  36.993  1.00 11.16           O  
ATOM    142  CB ALEU A  17      69.283  20.063  36.546  0.50 10.27           C  
ATOM    143  CB BLEU A  17      69.295  20.188  36.517  0.50 10.22           C  
ATOM    144  CG ALEU A  17      70.534  20.731  37.100  0.50  9.88           C  
ATOM    145  CG BLEU A  17      70.384  19.526  37.347  0.50  9.76           C  
ATOM    146  CD1ALEU A  17      70.633  20.563  38.612  0.50 10.02           C  
ATOM    147  CD1BLEU A  17      71.707  19.594  36.592  0.50  9.24           C  
ATOM    148  CD2ALEU A  17      71.765  20.155  36.407  0.50  9.43           C  
ATOM    149  CD2BLEU A  17      70.514  20.188  38.718  0.50  9.97           C  
ATOM    150  N   ASP A  18      66.375  21.555  35.715  1.00 12.36           N  
ATOM    151  CA  ASP A  18      65.790  22.738  35.102  1.00 12.81           C  
ATOM    152  C   ASP A  18      64.997  23.549  36.136  1.00 12.51           C  
ATOM    153  O   ASP A  18      64.031  23.065  36.732  1.00 11.99           O  
ATOM    154  CB  ASP A  18      65.021  22.362  33.834  1.00 15.41           C  
ATOM    155  CG  ASP A  18      63.941  21.339  34.098  1.00 18.54           C  
ATOM    156  OD1 ASP A  18      64.236  20.262  34.756  1.00 17.82           O  
ATOM    157  OD2 ASP A  18      62.815  21.618  33.660  1.00 22.07           O  
ATOM    158  N   ASN A  19      65.472  24.782  36.364  1.00 11.51           N  
ATOM    159  CA AASN A  19      64.976  25.689  37.393  0.50 10.82           C  
ATOM    160  CA BASN A  19      65.010  25.706  37.392  0.50 11.33           C  
ATOM    161  C   ASN A  19      65.221  25.177  38.817  1.00 10.22           C  
ATOM    162  O   ASN A  19      64.612  25.673  39.762  1.00  8.93           O  
ATOM    163  CB AASN A  19      63.523  26.132  37.176  0.50 11.35           C  
ATOM    164  CB BASN A  19      63.639  26.317  37.071  0.50 12.98           C  
ATOM    165  CG AASN A  19      63.268  27.503  37.773  0.50 11.68           C  
ATOM    166  CG BASN A  19      63.759  27.570  36.225  0.50 14.12           C  
ATOM    167  OD1AASN A  19      64.178  28.330  37.868  0.50 12.14           O  
ATOM    168  OD1BASN A  19      64.416  28.538  36.615  0.50 16.27           O  
ATOM    169  ND2AASN A  19      62.044  27.759  38.191  0.50 11.98           N  
ATOM    170  ND2BASN A  19      63.132  27.566  35.062  0.50 14.83           N  
ATOM    171  N   TYR A  20      66.172  24.245  39.016  1.00  9.39           N  
ATOM    172  CA  TYR A  20      66.492  23.830  40.378  1.00  8.56           C  
ATOM    173  C   TYR A  20      67.117  25.005  41.147  1.00  8.40           C  
ATOM    174  O   TYR A  20      68.050  25.627  40.639  1.00  7.70           O  
ATOM    175  CB  TYR A  20      67.432  22.608  40.378  1.00  8.61           C  
ATOM    176  CG  TYR A  20      67.553  21.961  41.739  1.00  8.63           C  
ATOM    177  CD1 TYR A  20      66.654  20.988  42.158  1.00  8.39           C  
ATOM    178  CD2 TYR A  20      68.551  22.347  42.631  1.00  8.50           C  
ATOM    179  CE1 TYR A  20      66.740  20.438  43.429  1.00  8.78           C  
ATOM    180  CE2 TYR A  20      68.659  21.800  43.902  1.00  8.87           C  
ATOM    181  CZ  TYR A  20      67.728  20.857  44.302  1.00  9.17           C  
ATOM    182  OH  TYR A  20      67.851  20.283  45.527  1.00 10.00           O  
ATOM    183  N   ARG A  21      66.595  25.285  42.358  1.00  8.51           N  
ATOM    184  CA AARG A  21      66.996  26.435  43.166  0.50  8.67           C  
ATOM    185  CA BARG A  21      66.951  26.440  43.178  0.50  8.37           C  
ATOM    186  C   ARG A  21      66.889  27.712  42.327  1.00  8.01           C  
ATOM    187  O   ARG A  21      67.616  28.674  42.573  1.00  7.51           O  
ATOM    188  CB AARG A  21      68.433  26.276  43.684  0.50 10.24           C  
ATOM    189  CB BARG A  21      68.318  26.243  43.844  0.50  9.37           C  
ATOM    190  CG AARG A  21      68.586  25.788  45.121  0.50 11.68           C  
ATOM    191  CG BARG A  21      68.388  25.113  44.867  0.50 10.26           C  
ATOM    192  CD AARG A  21      68.162  26.809  46.155  0.50 13.50           C  
ATOM    193  CD BARG A  21      67.776  25.526  46.193  0.50 10.64           C  
ATOM    194  NE AARG A  21      68.728  26.504  47.461  0.50 14.56           N  
ATOM    195  NE BARG A  21      67.800  24.521  47.248  0.50 11.75           N  
ATOM    196  CZ AARG A  21      68.155  25.718  48.366  0.50 15.62           C  
ATOM    197  CZ BARG A  21      67.734  24.820  48.543  0.50 12.07           C  
ATOM    198  NH1AARG A  21      68.755  25.512  49.526  0.50 16.54           N  
ATOM    199  NH1BARG A  21      67.750  23.858  49.453  0.50 12.32           N  
ATOM    200  NH2AARG A  21      66.985  25.145  48.118  0.50 16.79           N  
ATOM    201  NH2BARG A  21      67.639  26.088  48.917  0.50 12.51           N  
ATOM    202  N   GLY A  22      65.976  27.714  41.344  1.00  7.19           N  
ATOM    203  CA  GLY A  22      65.698  28.905  40.546  1.00  6.49           C  
ATOM    204  C   GLY A  22      66.691  29.118  39.397  1.00  6.06           C  
ATOM    205  O   GLY A  22      66.678  30.165  38.775  1.00  6.28           O  
ATOM    206  N   TYR A  23      67.568  28.142  39.132  1.00  5.34           N  
ATOM    207  CA  TYR A  23      68.523  28.309  38.041  1.00  5.17           C  
ATOM    208  C   TYR A  23      68.014  27.591  36.799  1.00  5.28           C  
ATOM    209  O   TYR A  23      67.883  26.362  36.802  1.00  5.62           O  
ATOM    210  CB  TYR A  23      69.886  27.746  38.445  1.00  4.70           C  
ATOM    211  CG  TYR A  23      70.555  28.603  39.481  1.00  4.25           C  
ATOM    212  CD1 TYR A  23      71.339  29.679  39.080  1.00  4.14           C  
ATOM    213  CD2 TYR A  23      70.426  28.343  40.843  1.00  4.07           C  
ATOM    214  CE1 TYR A  23      71.951  30.502  40.016  1.00  3.93           C  
ATOM    215  CE2 TYR A  23      71.022  29.171  41.786  1.00  4.01           C  
ATOM    216  CZ  TYR A  23      71.801  30.248  41.363  1.00  4.03           C  
ATOM    217  OH  TYR A  23      72.432  31.070  42.271  1.00  3.89           O  
ATOM    218  N   SER A  24      67.751  28.377  35.748  1.00  5.70           N  
ATOM    219  CA  SER A  24      67.192  27.849  34.511  1.00  5.96           C  
ATOM    220  C   SER A  24      68.171  26.856  33.887  1.00  6.11           C  
ATOM    221  O   SER A  24      69.388  26.934  34.100  1.00  6.49           O  
ATOM    222  CB  SER A  24      66.859  28.969  33.534  1.00  6.32           C  
ATOM    223  OG  SER A  24      68.025  29.638  33.072  1.00  6.82           O  
ATOM    224  N   LEU A  25      67.639  25.992  33.011  1.00  6.00           N  
ATOM    225  CA  LEU A  25      68.434  24.961  32.350  1.00  5.60           C  
ATOM    226  C   LEU A  25      69.671  25.532  31.651  1.00  5.26           C  
ATOM    227  O   LEU A  25      70.733  24.902  31.669  1.00  5.02           O  
ATOM    228  CB  LEU A  25      67.517  24.223  31.373  1.00  6.08           C  
ATOM    229  CG  LEU A  25      68.076  22.954  30.734  1.00  6.31           C  
ATOM    230  CD1 LEU A  25      68.485  21.925  31.803  1.00  6.55           C  
ATOM    231  CD2 LEU A  25      66.984  22.345  29.847  1.00  6.51           C  
ATOM    232  N   GLY A  26      69.548  26.700  31.004  1.00  4.72           N  
ATOM    233  CA  GLY A  26      70.678  27.298  30.301  1.00  4.44           C  
ATOM    234  C   GLY A  26      71.869  27.592  31.219  1.00  4.18           C  
ATOM    235  O   GLY A  26      73.023  27.519  30.787  1.00  4.05           O  
ATOM    236  N   ASN A  27      71.586  27.977  32.478  1.00  4.09           N  
ATOM    237  CA  ASN A  27      72.648  28.180  33.459  1.00  3.85           C  
ATOM    238  C   ASN A  27      73.483  26.912  33.637  1.00  3.70           C  
ATOM    239  O   ASN A  27      74.708  26.981  33.687  1.00  3.61           O  
ATOM    240  CB  ASN A  27      72.094  28.640  34.813  1.00  3.84           C  
ATOM    241  CG  ASN A  27      71.756  30.111  34.744  1.00  3.89           C  
ATOM    242  OD1 ASN A  27      72.657  30.943  34.820  1.00  3.76           O  
ATOM    243  ND2 ASN A  27      70.480  30.423  34.539  1.00  3.89           N  
ATOM    244  N   TRP A  28      72.812  25.772  33.733  1.00  3.63           N  
ATOM    245  CA  TRP A  28      73.470  24.499  34.002  1.00  3.54           C  
ATOM    246  C   TRP A  28      74.261  24.047  32.780  1.00  3.53           C  
ATOM    247  O   TRP A  28      75.359  23.495  32.907  1.00  3.57           O  
ATOM    248  CB  TRP A  28      72.417  23.453  34.422  1.00  3.68           C  
ATOM    249  CG  TRP A  28      71.784  23.779  35.744  1.00  3.85           C  
ATOM    250  CD1 TRP A  28      70.537  24.295  35.962  1.00  3.98           C  
ATOM    251  CD2 TRP A  28      72.389  23.617  37.044  1.00  3.96           C  
ATOM    252  NE1 TRP A  28      70.325  24.480  37.301  1.00  3.96           N  
ATOM    253  CE2 TRP A  28      71.442  24.059  37.993  1.00  3.96           C  
ATOM    254  CE3 TRP A  28      73.654  23.178  37.487  1.00  4.09           C  
ATOM    255  CZ2 TRP A  28      71.708  24.040  39.370  1.00  4.00           C  
ATOM    256  CZ3 TRP A  28      73.907  23.124  38.843  1.00  4.09           C  
ATOM    257  CH2 TRP A  28      72.948  23.573  39.767  1.00  4.13           C  
ATOM    258  N   VAL A  29      73.668  24.239  31.598  1.00  3.39           N  
ATOM    259  CA  VAL A  29      74.354  23.856  30.365  1.00  3.38           C  
ATOM    260  C   VAL A  29      75.605  24.717  30.158  1.00  3.38           C  
ATOM    261  O   VAL A  29      76.664  24.229  29.770  1.00  3.28           O  
ATOM    262  CB  VAL A  29      73.407  23.906  29.156  1.00  3.38           C  
ATOM    263  CG1 VAL A  29      74.145  23.611  27.862  1.00  3.31           C  
ATOM    264  CG2 VAL A  29      72.252  22.937  29.349  1.00  3.54           C  
ATOM    265  N   CYS A  30      75.461  26.027  30.398  1.00  3.51           N  
ATOM    266  CA  CYS A  30      76.579  26.953  30.302  1.00  3.68           C  
ATOM    267  C   CYS A  30      77.705  26.526  31.252  1.00  3.56           C  
ATOM    268  O   CYS A  30      78.881  26.517  30.878  1.00  3.26           O  
ATOM    269  CB  CYS A  30      76.098  28.374  30.604  1.00  4.01           C  
ATOM    270  SG  CYS A  30      77.368  29.647  30.358  1.00  4.69           S  
ATOM    271  N   ALA A  31      77.344  26.250  32.507  1.00  3.43           N  
ATOM    272  CA  ALA A  31      78.349  25.852  33.483  1.00  3.61           C  
ATOM    273  C   ALA A  31      79.057  24.577  33.024  1.00  3.72           C  
ATOM    274  O   ALA A  31      80.283  24.492  33.084  1.00  3.91           O  
ATOM    275  CB  ALA A  31      77.697  25.667  34.848  1.00  3.67           C  
ATOM    276  N   ALA A  32      78.295  23.597  32.531  1.00  3.75           N  
ATOM    277  CA  ALA A  32      78.930  22.367  32.062  1.00  3.89           C  
ATOM    278  C   ALA A  32      79.869  22.634  30.884  1.00  4.11           C  
ATOM    279  O   ALA A  32      80.939  22.017  30.776  1.00  3.94           O  
ATOM    280  CB  ALA A  32      77.883  21.337  31.713  1.00  3.86           C  
ATOM    281  N   LYS A  33      79.434  23.497  29.961  1.00  4.14           N  
ATOM    282  CA  LYS A  33      80.268  23.848  28.811  1.00  4.62           C  
ATOM    283  C   LYS A  33      81.648  24.314  29.263  1.00  4.57           C  
ATOM    284  O   LYS A  33      82.668  23.809  28.791  1.00  4.38           O  
ATOM    285  CB  LYS A  33      79.627  24.961  27.974  1.00  4.99           C  
ATOM    286  CG  LYS A  33      80.511  25.473  26.831  1.00  5.67           C  
ATOM    287  CD  LYS A  33      80.697  24.455  25.728  1.00  6.31           C  
ATOM    288  CE  LYS A  33      81.675  24.948  24.671  1.00  7.35           C  
ATOM    289  NZ  LYS A  33      81.793  23.940  23.581  1.00  8.49           N  
ATOM    290  N   PHE A  34      81.689  25.261  30.212  1.00  4.67           N  
ATOM    291  CA  PHE A  34      82.980  25.853  30.536  1.00  4.98           C  
ATOM    292  C   PHE A  34      83.723  25.041  31.597  1.00  4.92           C  
ATOM    293  O   PHE A  34      84.945  25.196  31.755  1.00  5.10           O  
ATOM    294  CB  PHE A  34      82.779  27.319  30.925  1.00  5.17           C  
ATOM    295  CG  PHE A  34      82.343  28.134  29.730  1.00  5.31           C  
ATOM    296  CD1 PHE A  34      83.106  28.127  28.564  1.00  5.58           C  
ATOM    297  CD2 PHE A  34      81.183  28.901  29.773  1.00  5.73           C  
ATOM    298  CE1 PHE A  34      82.707  28.880  27.470  1.00  5.99           C  
ATOM    299  CE2 PHE A  34      80.781  29.658  28.677  1.00  5.90           C  
ATOM    300  CZ  PHE A  34      81.549  29.643  27.529  1.00  6.05           C  
ATOM    301  N   GLU A  35      82.999  24.215  32.345  1.00  4.84           N  
ATOM    302  CA  GLU A  35      83.707  23.349  33.286  1.00  4.68           C  
ATOM    303  C   GLU A  35      84.390  22.180  32.569  1.00  4.64           C  
ATOM    304  O   GLU A  35      85.526  21.849  32.905  1.00  4.67           O  
ATOM    305  CB  GLU A  35      82.749  22.788  34.344  1.00  4.97           C  
ATOM    306  CG  GLU A  35      82.289  23.834  35.339  1.00  5.18           C  
ATOM    307  CD  GLU A  35      83.319  24.445  36.272  1.00  5.40           C  
ATOM    308  OE1 GLU A  35      84.513  24.091  36.164  1.00  5.40           O  
ATOM    309  OE2 GLU A  35      82.936  25.361  37.068  1.00  6.21           O  
ATOM    310  N   SER A  36      83.688  21.531  31.623  1.00  4.07           N  
ATOM    311  CA  SER A  36      84.129  20.231  31.121  1.00  4.15           C  
ATOM    312  C   SER A  36      84.070  20.121  29.607  1.00  4.42           C  
ATOM    313  O   SER A  36      84.425  19.066  29.063  1.00  4.51           O  
ATOM    314  CB  SER A  36      83.279  19.113  31.690  1.00  3.99           C  
ATOM    315  OG  SER A  36      81.943  19.236  31.206  1.00  3.69           O  
ATOM    316  N   ASN A  37      83.575  21.167  28.918  1.00  4.74           N  
ATOM    317  CA  ASN A  37      83.245  21.018  27.496  1.00  5.12           C  
ATOM    318  C   ASN A  37      82.344  19.798  27.236  1.00  4.70           C  
ATOM    319  O   ASN A  37      82.439  19.152  26.190  1.00  4.50           O  
ATOM    320  CB  ASN A  37      84.507  20.955  26.629  1.00  5.92           C  
ATOM    321  CG  ASN A  37      84.250  21.397  25.206  1.00  7.03           C  
ATOM    322  OD1 ASN A  37      83.212  21.989  24.909  1.00  8.07           O  
ATOM    323  ND2 ASN A  37      85.159  21.031  24.320  1.00  8.33           N  
ATOM    324  N   PHE A  38      81.436  19.512  28.183  1.00  4.40           N  
ATOM    325  CA  PHE A  38      80.405  18.484  28.088  1.00  4.36           C  
ATOM    326  C   PHE A  38      80.989  17.068  28.157  1.00  4.26           C  
ATOM    327  O   PHE A  38      80.312  16.123  27.764  1.00  4.22           O  
ATOM    328  CB  PHE A  38      79.528  18.623  26.832  1.00  4.55           C  
ATOM    329  CG  PHE A  38      78.839  19.954  26.660  1.00  4.68           C  
ATOM    330  CD1 PHE A  38      78.322  20.655  27.749  1.00  4.85           C  
ATOM    331  CD2 PHE A  38      78.628  20.461  25.381  1.00  4.70           C  
ATOM    332  CE1 PHE A  38      77.647  21.857  27.549  1.00  4.70           C  
ATOM    333  CE2 PHE A  38      77.970  21.668  25.191  1.00  4.89           C  
ATOM    334  CZ  PHE A  38      77.472  22.354  26.274  1.00  4.93           C  
ATOM    335  N   ASN A  39      82.198  16.923  28.721  1.00  4.09           N  
ATOM    336  CA  ASN A  39      82.856  15.617  28.777  1.00  4.20           C  
ATOM    337  C   ASN A  39      82.754  15.072  30.199  1.00  4.24           C  
ATOM    338  O   ASN A  39      83.321  15.667  31.109  1.00  4.65           O  
ATOM    339  CB  ASN A  39      84.341  15.785  28.400  1.00  4.35           C  
ATOM    340  CG  ASN A  39      85.109  14.487  28.310  1.00  4.45           C  
ATOM    341  OD1 ASN A  39      84.602  13.436  28.669  1.00  4.54           O  
ATOM    342  ND2 ASN A  39      86.329  14.570  27.788  1.00  4.89           N  
ATOM    343  N   THR A  40      82.065  13.939  30.384  1.00  4.35           N  
ATOM    344  CA  THR A  40      81.871  13.355  31.705  1.00  4.47           C  
ATOM    345  C   THR A  40      83.212  12.925  32.298  1.00  4.55           C  
ATOM    346  O   THR A  40      83.301  12.800  33.517  1.00  4.62           O  
ATOM    347  CB  THR A  40      80.897  12.164  31.728  1.00  4.49           C  
ATOM    348  OG1 THR A  40      81.532  11.064  31.066  1.00  4.72           O  
ATOM    349  CG2 THR A  40      79.569  12.469  31.058  1.00  4.58           C  
ATOM    350  N   GLN A  41      84.225  12.666  31.460  1.00  4.56           N  
ATOM    351  CA  GLN A  41      85.470  12.125  32.007  1.00  4.98           C  
ATOM    352  C   GLN A  41      86.489  13.205  32.373  1.00  5.13           C  
ATOM    353  O   GLN A  41      87.628  12.864  32.726  1.00  5.57           O  
ATOM    354  CB  GLN A  41      86.108  11.104  31.054  1.00  5.04           C  
ATOM    355  CG  GLN A  41      85.181   9.920  30.805  1.00  5.31           C  
ATOM    356  CD  GLN A  41      85.870   8.778  30.116  1.00  5.64           C  
ATOM    357  OE1 GLN A  41      85.804   8.630  28.881  1.00  6.52           O  
ATOM    358  NE2 GLN A  41      86.587   8.007  30.910  1.00  5.18           N  
ATOM    359  N   ALA A  42      86.110  14.486  32.271  1.00  4.92           N  
ATOM    360  CA  ALA A  42      87.016  15.592  32.572  1.00  5.13           C  
ATOM    361  C   ALA A  42      87.487  15.502  34.031  1.00  5.31           C  
ATOM    362  O   ALA A  42      86.693  15.245  34.936  1.00  5.10           O  
ATOM    363  CB  ALA A  42      86.311  16.918  32.361  1.00  4.73           C  
ATOM    364  N   THR A  43      88.793  15.714  34.245  1.00  5.77           N  
ATOM    365  CA  THR A  43      89.349  15.827  35.590  1.00  6.51           C  
ATOM    366  C   THR A  43      90.321  16.999  35.617  1.00  7.05           C  
ATOM    367  O   THR A  43      90.925  17.331  34.597  1.00  7.29           O  
ATOM    368  CB  THR A  43      90.128  14.573  36.042  1.00  6.59           C  
ATOM    369  OG1 THR A  43      91.226  14.290  35.166  1.00  7.36           O  
ATOM    370  CG2 THR A  43      89.265  13.340  36.209  1.00  6.57           C  
ATOM    371  N   ASN A  44      90.461  17.666  36.770  1.00  7.18           N  
ATOM    372  CA AASN A  44      91.398  18.776  36.887  0.50  7.42           C  
ATOM    373  CA BASN A  44      91.439  18.738  36.865  0.50  7.79           C  
ATOM    374  C   ASN A  44      91.971  18.790  38.296  1.00  7.73           C  
ATOM    375  O   ASN A  44      91.200  18.867  39.230  1.00  7.17           O  
ATOM    376  CB AASN A  44      90.695  20.126  36.715  0.50  7.37           C  
ATOM    377  CB BASN A  44      90.876  20.048  36.291  0.50  8.46           C  
ATOM    378  CG AASN A  44      91.619  21.293  36.991  0.50  7.42           C  
ATOM    379  CG BASN A  44      90.822  20.046  34.772  0.50  9.18           C  
ATOM    380  OD1AASN A  44      92.508  21.566  36.196  0.50  7.26           O  
ATOM    381  OD1BASN A  44      91.866  20.066  34.112  0.50  9.94           O  
ATOM    382  ND2AASN A  44      91.437  21.969  38.119  0.50  7.48           N  
ATOM    383  ND2BASN A  44      89.626  20.003  34.187  0.50  9.67           N  
ATOM    384  N   ARG A  45      93.312  18.737  38.443  1.00  8.76           N  
ATOM    385  CA AARG A  45      93.897  18.793  39.782  0.40  9.52           C  
ATOM    386  CA BARG A  45      93.986  18.799  39.739  0.60  9.61           C  
ATOM    387  C   ARG A  45      94.079  20.256  40.191  1.00 10.40           C  
ATOM    388  O   ARG A  45      94.486  21.115  39.395  1.00  9.75           O  
ATOM    389  CB AARG A  45      95.166  17.931  39.921  0.40  9.97           C  
ATOM    390  CB BARG A  45      95.420  18.274  39.575  0.60 10.15           C  
ATOM    391  CG AARG A  45      95.705  17.783  41.347  0.40  9.85           C  
ATOM    392  CG BARG A  45      96.204  18.128  40.873  0.60 10.60           C  
ATOM    393  CD AARG A  45      95.258  16.579  42.183  0.40 10.25           C  
ATOM    394  CD BARG A  45      95.752  17.039  41.832  0.60 11.44           C  
ATOM    395  NE AARG A  45      96.369  15.742  42.669  0.40 10.89           N  
ATOM    396  NE BARG A  45      94.883  15.930  41.439  0.60 12.17           N  
ATOM    397  CZ AARG A  45      96.366  14.866  43.678  0.40 10.51           C  
ATOM    398  CZ BARG A  45      95.149  14.599  41.454  0.60 13.50           C  
ATOM    399  NH1AARG A  45      95.308  14.615  44.415  0.40 10.82           N  
ATOM    400  NH1BARG A  45      96.314  14.139  41.855  0.60 14.73           N  
ATOM    401  NH2AARG A  45      97.443  14.184  43.971  0.40 10.47           N  
ATOM    402  NH2BARG A  45      94.228  13.702  41.151  0.60 12.52           N  
ATOM    403  N   ASN A  46      93.762  20.529  41.466  1.00 11.26           N  
ATOM    404  CA  ASN A  46      93.889  21.871  42.023  1.00 13.87           C  
ATOM    405  C   ASN A  46      95.211  22.012  42.771  1.00 14.96           C  
ATOM    406  O   ASN A  46      95.757  21.026  43.250  1.00 16.03           O  
ATOM    407  CB  ASN A  46      92.694  22.188  42.919  1.00 14.07           C  
ATOM    408  CG  ASN A  46      91.423  22.161  42.103  1.00 14.68           C  
ATOM    409  OD1 ASN A  46      91.361  22.810  41.069  1.00 17.09           O  
ATOM    410  ND2 ASN A  46      90.457  21.367  42.511  1.00 15.04           N  
ATOM    411  N   THR A  47      95.702  23.253  42.882  1.00 17.49           N  
ATOM    412  CA  THR A  47      96.943  23.544  43.586  1.00 20.70           C  
ATOM    413  C   THR A  47      96.916  22.953  45.001  1.00 20.52           C  
ATOM    414  O   THR A  47      97.962  22.528  45.489  1.00 24.42           O  
ATOM    415  CB  THR A  47      97.251  25.052  43.557  1.00 21.89           C  
ATOM    416  OG1 THR A  47      96.108  25.708  44.105  1.00 27.31           O  
ATOM    417  CG2 THR A  47      97.486  25.569  42.159  1.00 20.34           C  
ATOM    418  N   ASP A  48      95.730  22.918  45.635  1.00 18.74           N  
ATOM    419  CA  ASP A  48      95.536  22.475  47.013  1.00 17.24           C  
ATOM    420  C   ASP A  48      95.524  20.951  47.139  1.00 16.71           C  
ATOM    421  O   ASP A  48      95.332  20.438  48.243  1.00 16.85           O  
ATOM    422  CB  ASP A  48      94.278  23.068  47.677  1.00 17.38           C  
ATOM    423  CG  ASP A  48      92.930  22.484  47.247  1.00 18.50           C  
ATOM    424  OD1 ASP A  48      92.879  21.737  46.234  1.00 18.11           O  
ATOM    425  OD2 ASP A  48      91.928  22.760  47.925  1.00 19.69           O  
ATOM    426  N   GLY A  49      95.685  20.233  46.021  1.00 14.32           N  
ATOM    427  CA  GLY A  49      95.729  18.779  46.087  1.00 12.53           C  
ATOM    428  C   GLY A  49      94.369  18.117  45.844  1.00 11.11           C  
ATOM    429  O   GLY A  49      94.317  16.898  45.625  1.00 11.22           O  
ATOM    430  N   SER A  50      93.284  18.911  45.878  1.00  9.04           N  
ATOM    431  CA  SER A  50      91.970  18.383  45.547  1.00  7.88           C  
ATOM    432  C   SER A  50      91.883  18.212  44.026  1.00  6.84           C  
ATOM    433  O   SER A  50      92.720  18.727  43.285  1.00  6.84           O  
ATOM    434  CB  SER A  50      90.816  19.234  46.068  1.00  7.82           C  
ATOM    435  OG  SER A  50      90.786  20.477  45.379  1.00  8.04           O  
ATOM    436  N   THR A  51      90.861  17.477  43.577  1.00  5.70           N  
ATOM    437  CA  THR A  51      90.639  17.277  42.148  1.00  5.13           C  
ATOM    438  C   THR A  51      89.166  17.543  41.856  1.00  4.86           C  
ATOM    439  O   THR A  51      88.316  17.245  42.696  1.00  4.42           O  
ATOM    440  CB  THR A  51      90.993  15.829  41.752  1.00  4.91           C  
ATOM    441  OG1 THR A  51      92.367  15.647  42.136  1.00  4.90           O  
ATOM    442  CG2 THR A  51      90.860  15.532  40.269  1.00  4.92           C  
ATOM    443  N   ASP A  52      88.889  18.062  40.652  1.00  4.79           N  
ATOM    444  CA  ASP A  52      87.539  18.305  40.167  1.00  5.01           C  
ATOM    445  C   ASP A  52      87.179  17.216  39.166  1.00  4.53           C  
ATOM    446  O   ASP A  52      88.027  16.830  38.355  1.00  4.27           O  
ATOM    447  CB  ASP A  52      87.449  19.654  39.438  1.00  6.24           C  
ATOM    448  CG  ASP A  52      87.780  20.847  40.309  1.00  7.71           C  
ATOM    449  OD1 ASP A  52      87.504  20.820  41.493  1.00  8.00           O  
ATOM    450  OD2 ASP A  52      88.306  21.790  39.763  1.00 10.36           O  
ATOM    451  N   TYR A  53      85.910  16.762  39.219  1.00  4.24           N  
ATOM    452  CA  TYR A  53      85.453  15.603  38.471  1.00  4.46           C  
ATOM    453  C   TYR A  53      84.123  15.860  37.728  1.00  4.57           C  
ATOM    454  O   TYR A  53      83.041  16.273  38.239  1.00  5.64           O  
ATOM    455  CB  TYR A  53      85.304  14.407  39.418  1.00  4.05           C  
ATOM    456  CG  TYR A  53      86.555  13.932  40.122  1.00  3.95           C  
ATOM    457  CD1 TYR A  53      86.937  14.490  41.336  1.00  3.85           C  
ATOM    458  CD2 TYR A  53      87.327  12.889  39.615  1.00  3.81           C  
ATOM    459  CE1 TYR A  53      88.068  14.052  42.004  1.00  3.78           C  
ATOM    460  CE2 TYR A  53      88.457  12.426  40.282  1.00  3.77           C  
ATOM    461  CZ  TYR A  53      88.831  13.026  41.476  1.00  3.76           C  
ATOM    462  OH  TYR A  53      89.923  12.601  42.175  1.00  3.80           O  
ATOM    463  N   GLY A  54      84.221  15.493  36.438  1.00  4.58           N  
ATOM    464  CA  GLY A  54      83.023  15.224  35.664  1.00  4.72           C  
ATOM    465  C   GLY A  54      82.482  16.465  34.957  1.00  5.21           C  
ATOM    466  O   GLY A  54      83.155  17.487  34.880  1.00  4.87           O  
ATOM    467  N   ILE A  55      81.231  16.355  34.483  1.00  5.33           N  
ATOM    468  CA  ILE A  55      80.674  17.387  33.643  1.00  6.52           C  
ATOM    469  C   ILE A  55      80.543  18.674  34.433  1.00  6.43           C  
ATOM    470  O   ILE A  55      80.584  19.713  33.742  1.00  6.51           O  
ATOM    471  CB  ILE A  55      79.292  17.035  33.077  1.00  7.58           C  
ATOM    472  CG1 ILE A  55      78.275  16.715  34.177  1.00  8.27           C  
ATOM    473  CG2 ILE A  55      79.375  16.011  31.975  1.00  8.72           C  
ATOM    474  CD1 ILE A  55      76.839  16.862  33.694  1.00  9.98           C  
ATOM    475  N   LEU A  56      80.388  18.590  35.790  1.00  6.36           N  
ATOM    476  CA  LEU A  56      80.313  19.899  36.441  1.00  5.33           C  
ATOM    477  C   LEU A  56      81.520  20.166  37.361  1.00  4.81           C  
ATOM    478  O   LEU A  56      81.490  21.054  38.223  1.00  4.54           O  
ATOM    479  CB  LEU A  56      78.986  20.047  37.204  1.00  5.51           C  
ATOM    480  CG  LEU A  56      77.766  20.324  36.321  1.00  5.59           C  
ATOM    481  CD1 LEU A  56      76.479  20.025  37.063  1.00  5.54           C  
ATOM    482  CD2 LEU A  56      77.786  21.772  35.816  1.00  6.02           C  
ATOM    483  N   GLN A  57      82.599  19.386  37.175  1.00  4.24           N  
ATOM    484  CA  GLN A  57      83.882  19.614  37.831  1.00  4.22           C  
ATOM    485  C   GLN A  57      83.700  19.781  39.345  1.00  4.28           C  
ATOM    486  O   GLN A  57      84.161  20.762  39.947  1.00  4.12           O  
ATOM    487  CB  GLN A  57      84.616  20.787  37.169  1.00  4.07           C  
ATOM    488  CG  GLN A  57      85.114  20.434  35.750  1.00  4.12           C  
ATOM    489  CD  GLN A  57      86.203  19.380  35.813  1.00  4.30           C  
ATOM    490  OE1 GLN A  57      85.975  18.160  35.663  1.00  4.74           O  
ATOM    491  NE2 GLN A  57      87.417  19.838  36.022  1.00  3.94           N  
ATOM    492  N   ILE A  58      83.060  18.777  39.939  1.00  4.46           N  
ATOM    493  CA  ILE A  58      82.775  18.750  41.366  1.00  4.77           C  
ATOM    494  C   ILE A  58      84.024  18.341  42.128  1.00  5.23           C  
ATOM    495  O   ILE A  58      84.689  17.391  41.718  1.00  4.99           O  
ATOM    496  CB  ILE A  58      81.564  17.840  41.604  1.00  4.82           C  
ATOM    497  CG1 ILE A  58      80.310  18.508  41.024  1.00  4.71           C  
ATOM    498  CG2 ILE A  58      81.408  17.461  43.067  1.00  4.79           C  
ATOM    499  CD1 ILE A  58      79.094  17.584  40.992  1.00  5.12           C  
ATOM    500  N   ASN A  59      84.327  19.078  43.223  1.00  5.63           N  
ATOM    501  CA AASN A  59      85.620  19.049  43.894  0.50  5.93           C  
ATOM    502  CA BASN A  59      85.646  18.980  43.844  0.50  6.09           C  
ATOM    503  C   ASN A  59      85.647  18.013  45.025  1.00  6.12           C  
ATOM    504  O   ASN A  59      84.649  17.820  45.714  1.00  6.25           O  
ATOM    505  CB AASN A  59      85.920  20.452  44.427  0.50  6.26           C  
ATOM    506  CB BASN A  59      86.204  20.320  44.332  0.50  6.72           C  
ATOM    507  CG AASN A  59      87.324  20.604  44.958  0.50  6.31           C  
ATOM    508  CG BASN A  59      85.416  20.895  45.489  0.50  7.08           C  
ATOM    509  OD1AASN A  59      88.286  20.667  44.191  0.50  6.66           O  
ATOM    510  OD1BASN A  59      85.579  20.500  46.653  0.50  7.53           O  
ATOM    511  ND2AASN A  59      87.439  20.677  46.268  0.50  6.30           N  
ATOM    512  ND2BASN A  59      84.559  21.848  45.176  0.50  7.36           N  
ATOM    513  N   SER A  60      86.816  17.395  45.250  1.00  6.01           N  
ATOM    514  CA  SER A  60      86.963  16.353  46.259  1.00  6.72           C  
ATOM    515  C   SER A  60      87.192  16.920  47.661  1.00  7.42           C  
ATOM    516  O   SER A  60      87.214  16.140  48.601  1.00  8.34           O  
ATOM    517  CB  SER A  60      88.103  15.418  45.900  1.00  6.50           C  
ATOM    518  OG  SER A  60      89.317  16.169  45.861  1.00  6.04           O  
ATOM    519  N   ARG A  61      87.374  18.233  47.805  1.00  8.67           N  
ATOM    520  CA AARG A  61      87.630  18.809  49.120  0.50  9.47           C  
ATOM    521  CA BARG A  61      87.609  18.866  49.100  0.50  9.67           C  
ATOM    522  C   ARG A  61      86.379  18.664  49.987  1.00  9.60           C  
ATOM    523  O   ARG A  61      86.482  18.357  51.177  1.00  8.79           O  
ATOM    524  CB AARG A  61      88.103  20.265  48.996  0.50 10.69           C  
ATOM    525  CB BARG A  61      87.899  20.356  48.861  0.50 11.18           C  
ATOM    526  CG AARG A  61      88.473  20.934  50.314  0.50 12.38           C  
ATOM    527  CG BARG A  61      88.013  21.229  50.104  0.50 13.52           C  
ATOM    528  CD AARG A  61      88.881  22.380  50.066  0.50 14.32           C  
ATOM    529  CD BARG A  61      89.438  21.677  50.373  0.50 15.46           C  
ATOM    530  NE AARG A  61      88.798  23.251  51.232  0.50 16.27           N  
ATOM    531  NE BARG A  61      89.959  20.675  51.273  0.50 18.31           N  
ATOM    532  CZ AARG A  61      89.236  24.507  51.260  0.50 16.86           C  
ATOM    533  CZ BARG A  61      91.037  19.930  51.083  0.50 18.31           C  
ATOM    534  NH1AARG A  61      89.798  25.030  50.182  0.50 17.43           N  
ATOM    535  NH1BARG A  61      91.340  19.024  51.994  0.50 17.90           N  
ATOM    536  NH2AARG A  61      89.114  25.235  52.359  0.50 16.85           N  
ATOM    537  NH2BARG A  61      91.791  20.087  50.007  0.50 17.96           N  
ATOM    538  N   TRP A  62      85.196  18.842  49.379  1.00  8.83           N  
ATOM    539  CA  TRP A  62      83.945  18.785  50.115  1.00  8.80           C  
ATOM    540  C   TRP A  62      83.037  17.635  49.707  1.00  7.62           C  
ATOM    541  O   TRP A  62      82.253  17.172  50.533  1.00  7.57           O  
ATOM    542  CB  TRP A  62      83.183  20.110  49.977  1.00 10.94           C  
ATOM    543  CG  TRP A  62      83.806  21.204  50.785  1.00 13.45           C  
ATOM    544  CD1 TRP A  62      84.590  22.228  50.348  1.00 14.92           C  
ATOM    545  CD2 TRP A  62      83.729  21.333  52.215  1.00 15.91           C  
ATOM    546  NE1 TRP A  62      84.977  23.014  51.406  1.00 16.29           N  
ATOM    547  CE2 TRP A  62      84.447  22.495  52.559  1.00 16.83           C  
ATOM    548  CE3 TRP A  62      83.080  20.604  53.220  1.00 18.13           C  
ATOM    549  CZ2 TRP A  62      84.549  22.925  53.883  1.00 19.09           C  
ATOM    550  CZ3 TRP A  62      83.177  21.028  54.530  1.00 19.62           C  
ATOM    551  CH2 TRP A  62      83.912  22.174  54.847  1.00 19.90           C  
ATOM    552  N   TRP A  63      83.025  17.254  48.420  1.00  6.29           N  
ATOM    553  CA  TRP A  63      81.802  16.670  47.866  1.00  5.94           C  
ATOM    554  C   TRP A  63      81.895  15.178  47.570  1.00  5.64           C  
ATOM    555  O   TRP A  63      80.863  14.518  47.538  1.00  5.79           O  
ATOM    556  CB  TRP A  63      81.329  17.459  46.627  1.00  5.41           C  
ATOM    557  CG  TRP A  63      81.164  18.915  46.942  1.00  5.35           C  
ATOM    558  CD1 TRP A  63      81.954  19.960  46.545  1.00  5.27           C  
ATOM    559  CD2 TRP A  63      80.145  19.474  47.787  1.00  5.39           C  
ATOM    560  NE1 TRP A  63      81.475  21.136  47.066  1.00  5.42           N  
ATOM    561  CE2 TRP A  63      80.380  20.866  47.849  1.00  5.35           C  
ATOM    562  CE3 TRP A  63      79.055  18.918  48.482  1.00  5.34           C  
ATOM    563  CZ2 TRP A  63      79.550  21.729  48.580  1.00  5.59           C  
ATOM    564  CZ3 TRP A  63      78.240  19.770  49.206  1.00  5.31           C  
ATOM    565  CH2 TRP A  63      78.510  21.143  49.274  1.00  5.54           C  
ATOM    566  N   CYS A  64      83.101  14.668  47.285  1.00  5.23           N  
ATOM    567  CA  CYS A  64      83.233  13.266  46.924  1.00  5.23           C  
ATOM    568  C   CYS A  64      84.535  12.723  47.502  1.00  5.16           C  
ATOM    569  O   CYS A  64      85.422  13.494  47.878  1.00  6.04           O  
ATOM    570  CB  CYS A  64      83.148  13.055  45.411  1.00  4.88           C  
ATOM    571  SG  CYS A  64      84.472  13.875  44.483  1.00  4.97           S  
ATOM    572  N   ASN A  65      84.600  11.388  47.615  1.00  5.12           N  
ATOM    573  CA  ASN A  65      85.798  10.735  48.120  1.00  5.21           C  
ATOM    574  C   ASN A  65      86.666  10.196  46.983  1.00  5.09           C  
ATOM    575  O   ASN A  65      86.195   9.382  46.167  1.00  4.86           O  
ATOM    576  CB  ASN A  65      85.473   9.581  49.067  1.00  5.24           C  
ATOM    577  CG  ASN A  65      86.777   8.949  49.526  1.00  5.54           C  
ATOM    578  OD1 ASN A  65      87.649   9.639  50.051  1.00  5.86           O  
ATOM    579  ND2 ASN A  65      86.943   7.665  49.260  1.00  5.87           N  
ATOM    580  N   ASP A  66      87.944  10.622  46.969  1.00  5.10           N  
ATOM    581  CA  ASP A  66      88.919  10.064  46.032  1.00  5.63           C  
ATOM    582  C   ASP A  66      90.116   9.448  46.765  1.00  5.85           C  
ATOM    583  O   ASP A  66      91.024   8.922  46.126  1.00  6.40           O  
ATOM    584  CB  ASP A  66      89.377  11.050  44.944  1.00  5.52           C  
ATOM    585  CG  ASP A  66      90.158  12.264  45.455  1.00  5.61           C  
ATOM    586  OD1 ASP A  66      90.518  12.301  46.671  1.00  5.37           O  
ATOM    587  OD2 ASP A  66      90.393  13.195  44.643  1.00  5.92           O  
ATOM    588  N   GLY A  67      90.120   9.513  48.095  1.00  6.34           N  
ATOM    589  CA  GLY A  67      91.152   8.835  48.865  1.00  6.82           C  
ATOM    590  C   GLY A  67      92.484   9.562  48.872  1.00  7.36           C  
ATOM    591  O   GLY A  67      93.433   9.061  49.479  1.00  7.98           O  
ATOM    592  N   ARG A  68      92.584  10.710  48.182  1.00  7.73           N  
ATOM    593  CA AARG A  68      93.869  11.391  48.080  0.60  8.02           C  
ATOM    594  CA BARG A  68      93.850  11.405  47.986  0.40  8.48           C  
ATOM    595  C   ARG A  68      93.701  12.892  48.313  1.00  8.40           C  
ATOM    596  O   ARG A  68      94.477  13.708  47.804  1.00  9.31           O  
ATOM    597  CB AARG A  68      94.565  11.070  46.747  0.60  7.96           C  
ATOM    598  CB BARG A  68      94.445  11.146  46.584  0.40  9.21           C  
ATOM    599  CG AARG A  68      93.766  11.443  45.498  0.60  7.84           C  
ATOM    600  CG BARG A  68      93.806  11.891  45.406  0.40  9.95           C  
ATOM    601  CD AARG A  68      94.594  11.942  44.311  0.60  8.33           C  
ATOM    602  CD BARG A  68      94.566  11.996  44.058  0.40 10.96           C  
ATOM    603  NE AARG A  68      95.048  13.313  44.560  0.60  8.44           N  
ATOM    604  NE BARG A  68      94.616  13.278  43.319  0.40 12.20           N  
ATOM    605  CZ AARG A  68      96.308  13.752  44.477  0.60  9.49           C  
ATOM    606  CZ BARG A  68      95.126  13.494  42.074  0.40 13.24           C  
ATOM    607  NH1AARG A  68      97.255  12.891  44.139  0.60  9.18           N  
ATOM    608  NH1BARG A  68      95.575  12.457  41.391  0.40 13.66           N  
ATOM    609  NH2AARG A  68      96.621  15.011  44.767  0.60  9.10           N  
ATOM    610  NH2BARG A  68      95.098  14.708  41.522  0.40 14.11           N  
ATOM    611  N   THR A  69      92.690  13.275  49.118  1.00  7.64           N  
ATOM    612  CA  THR A  69      92.527  14.692  49.422  1.00  7.50           C  
ATOM    613  C   THR A  69      92.545  14.875  50.943  1.00  7.90           C  
ATOM    614  O   THR A  69      91.508  14.874  51.597  1.00  7.26           O  
ATOM    615  CB  THR A  69      91.278  15.310  48.752  1.00  7.47           C  
ATOM    616  OG1 THR A  69      91.246  14.920  47.366  1.00  7.41           O  
ATOM    617  CG2 THR A  69      91.251  16.828  48.853  1.00  7.07           C  
ATOM    618  N   PRO A  70      93.728  15.000  51.585  1.00  8.78           N  
ATOM    619  CA  PRO A  70      93.770  15.088  53.045  1.00  8.99           C  
ATOM    620  C   PRO A  70      92.807  16.089  53.679  1.00  9.58           C  
ATOM    621  O   PRO A  70      92.715  17.246  53.266  1.00 10.34           O  
ATOM    622  CB  PRO A  70      95.261  15.379  53.303  1.00  9.84           C  
ATOM    623  CG  PRO A  70      95.943  14.612  52.182  1.00  9.62           C  
ATOM    624  CD  PRO A  70      95.079  14.977  50.982  1.00  9.38           C  
ATOM    625  N   GLY A  71      92.067  15.606  54.683  1.00  9.78           N  
ATOM    626  CA  GLY A  71      91.271  16.476  55.521  1.00 10.22           C  
ATOM    627  C   GLY A  71      89.916  16.759  54.895  1.00 10.35           C  
ATOM    628  O   GLY A  71      89.161  17.571  55.420  1.00 11.55           O  
ATOM    629  N   SER A  72      89.631  16.113  53.759  1.00  9.38           N  
ATOM    630  CA  SER A  72      88.436  16.400  52.978  1.00  9.00           C  
ATOM    631  C   SER A  72      87.202  15.681  53.513  1.00  9.31           C  
ATOM    632  O   SER A  72      87.270  14.779  54.352  1.00  9.49           O  
ATOM    633  CB  SER A  72      88.658  16.069  51.506  1.00  8.57           C  
ATOM    634  OG  SER A  72      88.550  14.665  51.312  1.00  8.90           O  
ATOM    635  N   ARG A  73      86.049  16.105  52.994  1.00  8.28           N  
ATOM    636  CA  ARG A  73      84.761  15.509  53.268  1.00  8.52           C  
ATOM    637  C   ARG A  73      84.233  14.875  51.984  1.00  8.01           C  
ATOM    638  O   ARG A  73      84.875  14.969  50.929  1.00  7.78           O  
ATOM    639  CB  ARG A  73      83.804  16.602  53.757  1.00  9.14           C  
ATOM    640  CG  ARG A  73      84.252  17.240  55.069  1.00 10.97           C  
ATOM    641  CD  ARG A  73      84.235  16.265  56.259  1.00 12.43           C  
ATOM    642  NE  ARG A  73      82.851  16.012  56.663  1.00 13.88           N  
ATOM    643  CZ  ARG A  73      82.141  16.862  57.413  1.00 14.18           C  
ATOM    644  NH1 ARG A  73      82.698  17.964  57.888  1.00 14.68           N  
ATOM    645  NH2 ARG A  73      80.877  16.603  57.688  1.00 16.15           N  
ATOM    646  N   ASN A  74      83.095  14.190  52.131  1.00  7.48           N  
ATOM    647  CA  ASN A  74      82.447  13.454  51.061  1.00  7.23           C  
ATOM    648  C   ASN A  74      80.947  13.668  51.242  1.00  7.33           C  
ATOM    649  O   ASN A  74      80.226  12.726  51.578  1.00  7.45           O  
ATOM    650  CB  ASN A  74      82.823  11.964  51.120  1.00  7.14           C  
ATOM    651  CG  ASN A  74      82.092  11.120  50.093  1.00  7.16           C  
ATOM    652  OD1 ASN A  74      81.467  11.655  49.163  1.00  7.28           O  
ATOM    653  ND2 ASN A  74      82.185   9.798  50.230  1.00  7.20           N  
ATOM    654  N   LEU A  75      80.499  14.925  51.089  1.00  7.48           N  
ATOM    655  CA ALEU A  75      79.144  15.306  51.471  0.50  7.91           C  
ATOM    656  CA BLEU A  75      79.142  15.270  51.487  0.50  7.60           C  
ATOM    657  C   LEU A  75      78.119  14.683  50.525  1.00  7.86           C  
ATOM    658  O   LEU A  75      76.959  14.501  50.888  1.00  8.30           O  
ATOM    659  CB ALEU A  75      79.026  16.834  51.482  0.50  8.32           C  
ATOM    660  CB BLEU A  75      79.017  16.789  51.602  0.50  7.48           C  
ATOM    661  CG ALEU A  75      79.368  17.567  52.778  0.50  9.05           C  
ATOM    662  CG BLEU A  75      79.855  17.381  52.725  0.50  7.76           C  
ATOM    663  CD1ALEU A  75      80.730  17.156  53.334  0.50  9.40           C  
ATOM    664  CD1BLEU A  75      79.990  18.887  52.583  0.50  7.67           C  
ATOM    665  CD2ALEU A  75      79.325  19.071  52.554  0.50  9.10           C  
ATOM    666  CD2BLEU A  75      79.270  16.985  54.078  0.50  7.31           C  
ATOM    667  N   CYS A  76      78.537  14.340  49.297  1.00  7.37           N  
ATOM    668  CA  CYS A  76      77.581  13.725  48.398  1.00  7.61           C  
ATOM    669  C   CYS A  76      77.532  12.213  48.588  1.00  8.15           C  
ATOM    670  O   CYS A  76      76.730  11.544  47.950  1.00  8.16           O  
ATOM    671  CB  CYS A  76      77.863  14.087  46.939  1.00  6.82           C  
ATOM    672  SG  CYS A  76      77.480  15.829  46.632  1.00  6.72           S  
ATOM    673  N   ASN A  77      78.406  11.687  49.451  1.00  9.10           N  
ATOM    674  CA  ASN A  77      78.460  10.262  49.783  1.00 10.07           C  
ATOM    675  C   ASN A  77      78.679   9.382  48.557  1.00  8.64           C  
ATOM    676  O   ASN A  77      77.956   8.404  48.358  1.00  8.02           O  
ATOM    677  CB  ASN A  77      77.181   9.804  50.494  1.00 12.97           C  
ATOM    678  CG  ASN A  77      76.920  10.653  51.719  1.00 17.61           C  
ATOM    679  OD1 ASN A  77      77.721  10.668  52.658  1.00 22.39           O  
ATOM    680  ND2 ASN A  77      75.818  11.387  51.713  1.00 20.26           N  
ATOM    681  N   ILE A  78      79.694   9.714  47.757  1.00  7.55           N  
ATOM    682  CA  ILE A  78      80.002   8.996  46.529  1.00  6.84           C  
ATOM    683  C   ILE A  78      81.515   8.944  46.345  1.00  6.22           C  
ATOM    684  O   ILE A  78      82.235   9.872  46.736  1.00  5.81           O  
ATOM    685  CB  ILE A  78      79.379   9.704  45.301  1.00  7.10           C  
ATOM    686  CG1 ILE A  78      79.584  11.220  45.376  1.00  7.51           C  
ATOM    687  CG2 ILE A  78      77.923   9.291  45.065  1.00  7.43           C  
ATOM    688  CD1 ILE A  78      79.349  11.959  44.053  1.00  8.62           C  
ATOM    689  N   PRO A  79      82.031   7.909  45.649  1.00  6.02           N  
ATOM    690  CA  PRO A  79      83.399   7.950  45.129  1.00  5.78           C  
ATOM    691  C   PRO A  79      83.413   8.960  43.979  1.00  5.37           C  
ATOM    692  O   PRO A  79      82.440   9.081  43.226  1.00  5.11           O  
ATOM    693  CB  PRO A  79      83.637   6.508  44.640  1.00  6.16           C  
ATOM    694  CG  PRO A  79      82.265   5.996  44.308  1.00  6.42           C  
ATOM    695  CD  PRO A  79      81.330   6.654  45.313  1.00  6.11           C  
ATOM    696  N   CYS A  80      84.489   9.762  43.907  1.00  4.96           N  
ATOM    697  CA  CYS A  80      84.577  10.790  42.873  1.00  4.70           C  
ATOM    698  C   CYS A  80      84.449  10.153  41.487  1.00  4.73           C  
ATOM    699  O   CYS A  80      83.952  10.773  40.520  1.00  4.64           O  
ATOM    700  CB  CYS A  80      85.888  11.567  43.002  1.00  4.53           C  
ATOM    701  SG  CYS A  80      86.017  12.500  44.556  1.00  4.38           S  
ATOM    702  N   SER A  81      84.900   8.895  41.375  1.00  4.60           N  
ATOM    703  CA  SER A  81      84.767   8.185  40.106  1.00  4.86           C  
ATOM    704  C   SER A  81      83.323   8.137  39.549  1.00  5.06           C  
ATOM    705  O   SER A  81      83.153   8.066  38.338  1.00  5.41           O  
ATOM    706  CB  SER A  81      85.367   6.800  40.207  1.00  5.14           C  
ATOM    707  OG  SER A  81      84.650   6.036  41.153  1.00  5.04           O  
ATOM    708  N   ALA A  82      82.275   8.142  40.374  1.00  5.43           N  
ATOM    709  CA  ALA A  82      80.873   8.115  39.913  1.00  6.07           C  
ATOM    710  C   ALA A  82      80.469   9.370  39.108  1.00  6.26           C  
ATOM    711  O   ALA A  82      79.421   9.492  38.378  1.00  8.18           O  
ATOM    712  CB  ALA A  82      80.006   7.977  41.147  1.00  6.58           C  
ATOM    713  N   LEU A  83      81.308  10.391  39.356  1.00  5.69           N  
ATOM    714  CA  LEU A  83      81.123  11.669  38.680  1.00  5.82           C  
ATOM    715  C   LEU A  83      81.661  11.606  37.249  1.00  5.65           C  
ATOM    716  O   LEU A  83      81.524  12.582  36.506  1.00  5.53           O  
ATOM    717  CB  LEU A  83      81.778  12.793  39.496  1.00  5.68           C  
ATOM    718  CG  LEU A  83      81.200  13.008  40.899  1.00  5.68           C  
ATOM    719  CD1 LEU A  83      82.044  14.031  41.644  1.00  5.71           C  
ATOM    720  CD2 LEU A  83      79.739  13.509  40.815  1.00  6.18           C  
ATOM    721  N   LEU A  84      82.287  10.478  36.859  1.00  5.96           N  
ATOM    722  CA  LEU A  84      82.883  10.385  35.530  1.00  6.28           C  
ATOM    723  C   LEU A  84      82.043   9.508  34.599  1.00  6.59           C  
ATOM    724  O   LEU A  84      82.385   9.365  33.421  1.00  6.94           O  
ATOM    725  CB  LEU A  84      84.322   9.839  35.581  1.00  6.68           C  
ATOM    726  CG  LEU A  84      85.317  10.609  36.448  1.00  6.91           C  
ATOM    727  CD1 LEU A  84      86.717  10.007  36.291  1.00  8.02           C  
ATOM    728  CD2 LEU A  84      85.352  12.093  36.049  1.00  6.45           C  
ATOM    729  N   SER A  85      80.981   8.919  35.141  1.00  6.70           N  
ATOM    730  CA  SER A  85      80.090   8.001  34.443  1.00  7.18           C  
ATOM    731  C   SER A  85      79.440   8.647  33.212  1.00  7.68           C  
ATOM    732  O   SER A  85      79.112   9.832  33.216  1.00  7.31           O  
ATOM    733  CB  SER A  85      79.040   7.534  35.416  1.00  7.37           C  
ATOM    734  OG  SER A  85      78.155   6.654  34.754  1.00  7.57           O  
ATOM    735  N   SER A  86      79.145   7.831  32.188  1.00  8.11           N  
ATOM    736  CA  SER A  86      78.275   8.297  31.109  1.00  8.96           C  
ATOM    737  C   SER A  86      76.860   8.650  31.602  1.00  9.54           C  
ATOM    738  O   SER A  86      76.159   9.423  30.940  1.00  9.72           O  
ATOM    739  CB  SER A  86      78.250   7.303  29.962  1.00  9.49           C  
ATOM    740  OG  SER A  86      77.784   6.056  30.437  1.00 10.63           O  
ATOM    741  N   ASP A  87      76.462   8.085  32.751  1.00  9.32           N  
ATOM    742  CA  ASP A  87      75.269   8.408  33.527  1.00 10.55           C  
ATOM    743  C   ASP A  87      75.531   9.585  34.502  1.00  9.29           C  
ATOM    744  O   ASP A  87      76.372   9.607  35.475  1.00 12.28           O  
ATOM    745  CB  ASP A  87      74.686   7.115  34.123  1.00 12.10           C  
ATOM    746  CG  ASP A  87      73.403   7.281  34.922  1.00 15.23           C  
ATOM    747  OD1 ASP A  87      72.993   8.426  35.200  1.00 13.99           O  
ATOM    748  OD2 ASP A  87      72.810   6.235  35.261  1.00 18.30           O  
ATOM    749  N   ILE A  88      74.786  10.657  34.149  1.00  9.26           N  
ATOM    750  CA  ILE A  88      74.983  11.926  34.826  1.00  8.65           C  
ATOM    751  C   ILE A  88      74.240  11.946  36.154  1.00  8.56           C  
ATOM    752  O   ILE A  88      74.360  12.935  36.853  1.00  7.86           O  
ATOM    753  CB  ILE A  88      74.645  13.170  33.960  1.00  8.24           C  
ATOM    754  CG1 ILE A  88      73.139  13.393  33.733  1.00  8.44           C  
ATOM    755  CG2 ILE A  88      75.450  13.207  32.670  1.00  8.36           C  
ATOM    756  CD1 ILE A  88      72.808  14.787  33.176  1.00  8.78           C  
ATOM    757  N   THR A  89      73.556  10.855  36.534  1.00  8.60           N  
ATOM    758  CA  THR A  89      72.748  10.877  37.758  1.00  8.55           C  
ATOM    759  C   THR A  89      73.561  11.369  38.959  1.00  8.37           C  
ATOM    760  O   THR A  89      73.110  12.250  39.683  1.00  7.79           O  
ATOM    761  CB  THR A  89      72.122   9.518  38.115  1.00  9.35           C  
ATOM    762  OG1 THR A  89      71.299   9.101  37.022  1.00  9.98           O  
ATOM    763  CG2 THR A  89      71.250   9.615  39.346  1.00 10.07           C  
ATOM    764  N   ALA A  90      74.755  10.790  39.159  1.00  7.68           N  
ATOM    765  CA  ALA A  90      75.530  11.121  40.337  1.00  7.64           C  
ATOM    766  C   ALA A  90      76.017  12.554  40.194  1.00  7.63           C  
ATOM    767  O   ALA A  90      75.919  13.287  41.220  1.00  7.40           O  
ATOM    768  CB  ALA A  90      76.679  10.165  40.561  1.00  7.56           C  
ATOM    769  N   SER A  91      76.537  12.904  38.984  1.00  8.03           N  
ATOM    770  CA  SER A  91      76.780  14.365  38.906  1.00  7.23           C  
ATOM    771  C   SER A  91      75.599  15.309  39.277  1.00  6.61           C  
ATOM    772  O   SER A  91      75.765  16.344  39.935  1.00  6.29           O  
ATOM    773  CB  SER A  91      77.459  14.766  37.588  1.00  7.64           C  
ATOM    774  OG  SER A  91      78.890  14.623  37.633  1.00  8.53           O  
ATOM    775  N   VAL A  92      74.385  15.017  38.806  1.00  6.51           N  
ATOM    776  CA  VAL A  92      73.258  15.927  39.011  1.00  6.58           C  
ATOM    777  C   VAL A  92      72.855  15.971  40.483  1.00  6.71           C  
ATOM    778  O   VAL A  92      72.603  17.042  41.035  1.00  6.30           O  
ATOM    779  CB  VAL A  92      72.057  15.488  38.154  1.00  6.67           C  
ATOM    780  CG1 VAL A  92      70.778  16.202  38.598  1.00  6.82           C  
ATOM    781  CG2 VAL A  92      72.338  15.713  36.671  1.00  6.87           C  
ATOM    782  N   ASN A  93      72.746  14.794  41.116  1.00  6.82           N  
ATOM    783  CA  ASN A  93      72.341  14.720  42.509  1.00  7.36           C  
ATOM    784  C   ASN A  93      73.305  15.519  43.389  1.00  6.73           C  
ATOM    785  O   ASN A  93      72.886  16.162  44.363  1.00  6.25           O  
ATOM    786  CB  ASN A  93      72.228  13.277  43.015  1.00  8.78           C  
ATOM    787  CG  ASN A  93      71.025  12.592  42.399  1.00 10.46           C  
ATOM    788  OD1 ASN A  93      70.212  13.258  41.750  1.00 12.45           O  
ATOM    789  ND2 ASN A  93      70.969  11.269  42.488  1.00 11.83           N  
ATOM    790  N   CYS A  94      74.605  15.403  43.066  1.00  6.05           N  
ATOM    791  CA  CYS A  94      75.614  16.102  43.851  1.00  6.04           C  
ATOM    792  C   CYS A  94      75.544  17.618  43.598  1.00  5.67           C  
ATOM    793  O   CYS A  94      75.599  18.410  44.538  1.00  5.34           O  
ATOM    794  CB  CYS A  94      76.989  15.461  43.651  1.00  6.03           C  
ATOM    795  SG  CYS A  94      78.241  16.167  44.751  1.00  6.59           S  
ATOM    796  N   ALA A  95      75.370  18.034  42.325  1.00  5.32           N  
ATOM    797  CA  ALA A  95      75.183  19.446  42.001  1.00  5.34           C  
ATOM    798  C   ALA A  95      73.968  20.037  42.740  1.00  5.45           C  
ATOM    799  O   ALA A  95      73.984  21.190  43.156  1.00  5.62           O  
ATOM    800  CB  ALA A  95      75.041  19.592  40.505  1.00  5.22           C  
ATOM    801  N   LYS A  96      72.906  19.257  42.946  1.00  5.52           N  
ATOM    802  CA  LYS A  96      71.761  19.806  43.661  1.00  5.85           C  
ATOM    803  C   LYS A  96      72.150  20.146  45.106  1.00  5.99           C  
ATOM    804  O   LYS A  96      71.725  21.167  45.642  1.00  5.84           O  
ATOM    805  CB  LYS A  96      70.622  18.778  43.638  1.00  6.19           C  
ATOM    806  CG  LYS A  96      69.910  18.652  42.302  1.00  6.53           C  
ATOM    807  CD  LYS A  96      68.838  17.561  42.295  1.00  6.75           C  
ATOM    808  CE  LYS A  96      68.081  17.536  40.978  1.00  7.62           C  
ATOM    809  NZ  LYS A  96      67.027  16.492  40.971  1.00  8.92           N  
ATOM    810  N   LYS A  97      72.974  19.302  45.754  1.00  6.05           N  
ATOM    811  CA ALYS A  97      73.415  19.577  47.110  0.50  6.02           C  
ATOM    812  CA BLYS A  97      73.421  19.573  47.107  0.50  6.08           C  
ATOM    813  C   LYS A  97      74.340  20.798  47.112  1.00  6.05           C  
ATOM    814  O   LYS A  97      74.247  21.659  47.986  1.00  5.88           O  
ATOM    815  CB ALYS A  97      74.145  18.378  47.724  0.50  6.17           C  
ATOM    816  CB BLYS A  97      74.175  18.364  47.660  0.50  6.32           C  
ATOM    817  CG ALYS A  97      73.313  17.119  47.929  0.50  6.36           C  
ATOM    818  CG BLYS A  97      74.493  18.389  49.147  0.50  6.76           C  
ATOM    819  CD ALYS A  97      74.161  15.920  48.327  0.50  6.85           C  
ATOM    820  CD BLYS A  97      74.577  16.960  49.644  0.50  6.95           C  
ATOM    821  CE ALYS A  97      74.315  15.763  49.827  0.50  7.01           C  
ATOM    822  CE BLYS A  97      73.236  16.264  49.483  0.50  7.44           C  
ATOM    823  NZ ALYS A  97      72.993  15.812  50.506  0.50  7.47           N  
ATOM    824  NZ BLYS A  97      73.379  14.806  49.231  0.50  7.52           N  
ATOM    825  N   ILE A  98      75.229  20.880  46.117  1.00  5.68           N  
ATOM    826  CA  ILE A  98      76.191  21.982  46.066  1.00  5.90           C  
ATOM    827  C   ILE A  98      75.458  23.318  45.898  1.00  6.12           C  
ATOM    828  O   ILE A  98      75.755  24.288  46.592  1.00  5.64           O  
ATOM    829  CB  ILE A  98      77.240  21.774  44.949  1.00  6.00           C  
ATOM    830  CG1 ILE A  98      78.106  20.542  45.200  1.00  6.10           C  
ATOM    831  CG2 ILE A  98      78.129  23.010  44.801  1.00  5.56           C  
ATOM    832  CD1 ILE A  98      78.814  20.045  43.955  1.00  6.20           C  
ATOM    833  N   VAL A  99      74.493  23.358  44.976  1.00  6.37           N  
ATOM    834  CA  VAL A  99      73.827  24.622  44.675  1.00  6.64           C  
ATOM    835  C   VAL A  99      72.907  25.058  45.819  1.00  7.66           C  
ATOM    836  O   VAL A  99      72.492  26.221  45.886  1.00  7.66           O  
ATOM    837  CB  VAL A  99      73.102  24.562  43.315  1.00  6.39           C  
ATOM    838  CG1 VAL A  99      71.828  23.726  43.422  1.00  6.41           C  
ATOM    839  CG2 VAL A  99      72.788  25.968  42.812  1.00  6.30           C  
ATOM    840  N   SER A 100      72.604  24.131  46.743  1.00  8.53           N  
ATOM    841  CA  SER A 100      71.777  24.382  47.919  1.00  9.57           C  
ATOM    842  C   SER A 100      72.614  24.895  49.096  1.00 10.74           C  
ATOM    843  O   SER A 100      72.082  25.185  50.168  1.00 11.22           O  
ATOM    844  CB  SER A 100      70.987  23.135  48.294  1.00  9.05           C  
ATOM    845  OG  SER A 100      70.096  22.799  47.235  1.00  9.67           O  
ATOM    846  N   ASP A 101      73.935  25.010  48.915  1.00 12.03           N  
ATOM    847  CA  ASP A 101      74.874  25.155  50.033  1.00 13.22           C  
ATOM    848  C   ASP A 101      74.901  26.576  50.598  1.00 13.16           C  
ATOM    849  O   ASP A 101      75.466  26.766  51.673  1.00 13.73           O  
ATOM    850  CB  ASP A 101      76.313  24.752  49.648  1.00 15.52           C  
ATOM    851  CG  ASP A 101      77.333  24.705  50.785  1.00 17.31           C  
ATOM    852  OD1 ASP A 101      77.119  23.936  51.733  1.00 19.18           O  
ATOM    853  OD2 ASP A 101      78.344  25.441  50.712  1.00 22.60           O  
ATOM    854  N   GLY A 102      74.299  27.562  49.914  1.00 12.65           N  
ATOM    855  CA  GLY A 102      74.336  28.934  50.423  1.00 11.00           C  
ATOM    856  C   GLY A 102      74.638  29.979  49.347  1.00 10.88           C  
ATOM    857  O   GLY A 102      74.027  31.051  49.352  1.00 10.52           O  
ATOM    858  N   ASN A 103      75.574  29.662  48.435  1.00  9.64           N  
ATOM    859  CA  ASN A 103      76.056  30.622  47.450  1.00  9.12           C  
ATOM    860  C   ASN A 103      75.523  30.326  46.058  1.00  7.59           C  
ATOM    861  O   ASN A 103      75.950  30.969  45.103  1.00  7.08           O  
ATOM    862  CB  ASN A 103      77.578  30.747  47.446  1.00 10.68           C  
ATOM    863  CG  ASN A 103      78.060  31.263  48.785  1.00 12.85           C  
ATOM    864  OD1 ASN A 103      77.480  32.190  49.341  1.00 14.75           O  
ATOM    865  ND2 ASN A 103      79.053  30.598  49.355  1.00 14.98           N  
ATOM    866  N   GLY A 104      74.531  29.444  45.974  1.00  6.16           N  
ATOM    867  CA  GLY A 104      73.931  29.189  44.682  1.00  5.51           C  
ATOM    868  C   GLY A 104      75.008  28.729  43.697  1.00  5.00           C  
ATOM    869  O   GLY A 104      75.941  28.003  44.067  1.00  4.62           O  
ATOM    870  N   MET A 105      74.880  29.187  42.458  1.00  4.56           N  
ATOM    871  CA  MET A 105      75.776  28.680  41.434  1.00  4.46           C  
ATOM    872  C   MET A 105      77.139  29.368  41.486  1.00  4.30           C  
ATOM    873  O   MET A 105      78.044  28.995  40.747  1.00  4.32           O  
ATOM    874  CB  MET A 105      75.170  28.745  40.031  1.00  4.35           C  
ATOM    875  CG  MET A 105      74.147  27.608  39.801  1.00  4.35           C  
ATOM    876  SD  MET A 105      73.643  27.402  38.053  1.00  4.71           S  
ATOM    877  CE  MET A 105      75.118  26.616  37.372  1.00  4.81           C  
ATOM    878  N   ASN A 106      77.302  30.349  42.378  1.00  4.35           N  
ATOM    879  CA  ASN A 106      78.613  30.948  42.578  1.00  4.39           C  
ATOM    880  C   ASN A 106      79.637  29.913  43.070  1.00  4.66           C  
ATOM    881  O   ASN A 106      80.843  30.159  42.951  1.00  4.81           O  
ATOM    882  CB  ASN A 106      78.550  32.192  43.472  1.00  4.47           C  
ATOM    883  CG  ASN A 106      77.674  33.277  42.890  1.00  4.41           C  
ATOM    884  OD1 ASN A 106      78.056  33.969  41.929  1.00  4.68           O  
ATOM    885  ND2 ASN A 106      76.528  33.485  43.525  1.00  4.59           N  
ATOM    886  N   ALA A 107      79.176  28.763  43.590  1.00  4.82           N  
ATOM    887  CA  ALA A 107      80.088  27.685  43.974  1.00  5.06           C  
ATOM    888  C   ALA A 107      80.959  27.282  42.783  1.00  5.25           C  
ATOM    889  O   ALA A 107      82.106  26.858  42.967  1.00  5.61           O  
ATOM    890  CB  ALA A 107      79.321  26.493  44.494  1.00  5.17           C  
ATOM    891  N   TRP A 108      80.420  27.413  41.554  1.00  5.04           N  
ATOM    892  CA  TRP A 108      81.190  27.150  40.347  1.00  4.93           C  
ATOM    893  C   TRP A 108      81.810  28.457  39.861  1.00  5.07           C  
ATOM    894  O   TRP A 108      81.132  29.282  39.261  1.00  5.27           O  
ATOM    895  CB  TRP A 108      80.339  26.488  39.257  1.00  4.63           C  
ATOM    896  CG  TRP A 108      79.909  25.080  39.559  1.00  4.43           C  
ATOM    897  CD1 TRP A 108      80.578  23.937  39.208  1.00  4.51           C  
ATOM    898  CD2 TRP A 108      78.714  24.654  40.245  1.00  4.35           C  
ATOM    899  NE1 TRP A 108      79.879  22.830  39.615  1.00  4.30           N  
ATOM    900  CE2 TRP A 108      78.740  23.235  40.275  1.00  4.38           C  
ATOM    901  CE3 TRP A 108      77.637  25.332  40.853  1.00  4.39           C  
ATOM    902  CZ2 TRP A 108      77.717  22.476  40.846  1.00  4.27           C  
ATOM    903  CZ3 TRP A 108      76.621  24.580  41.418  1.00  4.40           C  
ATOM    904  CH2 TRP A 108      76.673  23.173  41.433  1.00  4.34           C  
ATOM    905  N   VAL A 109      83.113  28.629  40.096  1.00  5.30           N  
ATOM    906  CA AVAL A 109      83.770  29.882  39.737  0.60  5.51           C  
ATOM    907  CA BVAL A 109      83.763  29.883  39.741  0.40  5.42           C  
ATOM    908  C   VAL A 109      83.609  30.162  38.238  1.00  5.43           C  
ATOM    909  O   VAL A 109      83.416  31.318  37.830  1.00  5.58           O  
ATOM    910  CB AVAL A 109      85.229  29.914  40.232  0.60  5.80           C  
ATOM    911  CB BVAL A 109      85.217  29.920  40.255  0.40  5.57           C  
ATOM    912  CG1AVAL A 109      86.038  31.025  39.577  0.60  5.67           C  
ATOM    913  CG1BVAL A 109      85.317  29.374  41.680  0.40  5.57           C  
ATOM    914  CG2AVAL A 109      85.267  30.049  41.756  0.60  5.96           C  
ATOM    915  CG2BVAL A 109      86.167  29.174  39.342  0.40  5.46           C  
ATOM    916  N   ALA A 110      83.649  29.117  37.399  1.00  5.34           N  
ATOM    917  CA  ALA A 110      83.467  29.331  35.968  1.00  5.35           C  
ATOM    918  C   ALA A 110      82.056  29.822  35.632  1.00  5.16           C  
ATOM    919  O   ALA A 110      81.895  30.625  34.716  1.00  4.71           O  
ATOM    920  CB  ALA A 110      83.836  28.121  35.160  1.00  5.62           C  
ATOM    921  N   TRP A 111      81.043  29.346  36.370  1.00  4.94           N  
ATOM    922  CA  TRP A 111      79.704  29.896  36.174  1.00  4.73           C  
ATOM    923  C   TRP A 111      79.691  31.393  36.483  1.00  5.15           C  
ATOM    924  O   TRP A 111      79.149  32.170  35.707  1.00  4.93           O  
ATOM    925  CB  TRP A 111      78.633  29.145  36.976  1.00  4.55           C  
ATOM    926  CG  TRP A 111      77.290  29.793  36.835  1.00  4.23           C  
ATOM    927  CD1 TRP A 111      76.382  29.563  35.843  1.00  4.19           C  
ATOM    928  CD2 TRP A 111      76.705  30.805  37.688  1.00  4.28           C  
ATOM    929  NE1 TRP A 111      75.275  30.356  36.028  1.00  4.02           N  
ATOM    930  CE2 TRP A 111      75.436  31.116  37.151  1.00  4.08           C  
ATOM    931  CE3 TRP A 111      77.095  31.454  38.867  1.00  4.15           C  
ATOM    932  CZ2 TRP A 111      74.591  32.073  37.727  1.00  4.10           C  
ATOM    933  CZ3 TRP A 111      76.249  32.374  39.455  1.00  4.13           C  
ATOM    934  CH2 TRP A 111      75.002  32.676  38.898  1.00  4.11           C  
ATOM    935  N   ARG A 112      80.259  31.787  37.622  1.00  5.89           N  
ATOM    936  CA  ARG A 112      80.264  33.200  37.986  1.00  6.65           C  
ATOM    937  C   ARG A 112      80.981  34.018  36.908  1.00  6.47           C  
ATOM    938  O   ARG A 112      80.532  35.104  36.539  1.00  6.38           O  
ATOM    939  CB  ARG A 112      80.918  33.401  39.361  1.00  8.06           C  
ATOM    940  CG  ARG A 112      80.859  34.840  39.861  1.00 10.90           C  
ATOM    941  CD  ARG A 112      81.343  35.117  41.291  1.00 12.64           C  
ATOM    942  NE  ARG A 112      82.597  34.441  41.585  1.00 14.03           N  
ATOM    943  CZ  ARG A 112      83.818  34.859  41.239  1.00 16.99           C  
ATOM    944  NH1 ARG A 112      83.977  35.990  40.566  1.00 17.60           N  
ATOM    945  NH2 ARG A 112      84.866  34.110  41.543  1.00 17.31           N  
ATOM    946  N   ASN A 113      82.106  33.508  36.406  1.00  5.97           N  
ATOM    947  CA  ASN A 113      82.961  34.331  35.553  1.00  6.02           C  
ATOM    948  C   ASN A 113      82.512  34.302  34.090  1.00  6.17           C  
ATOM    949  O   ASN A 113      82.841  35.223  33.329  1.00  5.96           O  
ATOM    950  CB  ASN A 113      84.425  33.893  35.687  1.00  5.76           C  
ATOM    951  CG  ASN A 113      85.019  34.331  37.009  1.00  5.90           C  
ATOM    952  OD1 ASN A 113      84.630  35.376  37.549  1.00  6.09           O  
ATOM    953  ND2 ASN A 113      85.975  33.567  37.513  1.00  5.76           N  
ATOM    954  N   ARG A 114      81.789  33.244  33.674  1.00  6.09           N  
ATOM    955  CA  ARG A 114      81.516  33.097  32.246  1.00  6.02           C  
ATOM    956  C   ARG A 114      80.031  32.980  31.889  1.00  6.20           C  
ATOM    957  O   ARG A 114      79.698  33.055  30.702  1.00  6.66           O  
ATOM    958  CB  ARG A 114      82.302  31.899  31.706  1.00  6.12           C  
ATOM    959  CG  ARG A 114      83.783  32.048  32.022  1.00  6.37           C  
ATOM    960  CD  ARG A 114      84.617  31.003  31.366  1.00  6.51           C  
ATOM    961  NE  ARG A 114      84.713  31.137  29.909  1.00  7.27           N  
ATOM    962  CZ  ARG A 114      85.510  30.273  29.271  1.00  6.53           C  
ATOM    963  NH1 ARG A 114      86.164  29.348  29.960  1.00  6.36           N  
ATOM    964  NH2 ARG A 114      85.652  30.325  27.965  1.00  6.07           N  
ATOM    965  N   CYS A 115      79.161  32.730  32.875  1.00  5.73           N  
ATOM    966  CA  CYS A 115      77.767  32.438  32.581  1.00  5.47           C  
ATOM    967  C   CYS A 115      76.853  33.458  33.260  1.00  5.46           C  
ATOM    968  O   CYS A 115      75.873  33.909  32.663  1.00  5.23           O  
ATOM    969  CB  CYS A 115      77.365  31.030  33.039  1.00  5.15           C  
ATOM    970  SG  CYS A 115      78.298  29.688  32.239  1.00  5.22           S  
ATOM    971  N   LYS A 116      77.109  33.728  34.546  1.00  5.58           N  
ATOM    972  CA  LYS A 116      76.313  34.662  35.339  1.00  5.68           C  
ATOM    973  C   LYS A 116      76.058  35.963  34.585  1.00  6.02           C  
ATOM    974  O   LYS A 116      76.998  36.613  34.114  1.00  6.22           O  
ATOM    975  CB  LYS A 116      77.029  34.953  36.659  1.00  5.57           C  
ATOM    976  CG  LYS A 116      76.224  35.754  37.683  1.00  5.36           C  
ATOM    977  CD  LYS A 116      76.982  35.840  39.002  1.00  5.35           C  
ATOM    978  CE  LYS A 116      76.243  36.571  40.118  1.00  5.35           C  
ATOM    979  NZ  LYS A 116      77.104  36.741  41.330  1.00  5.04           N  
ATOM    980  N   GLY A 117      74.775  36.349  34.497  1.00  6.61           N  
ATOM    981  CA  GLY A 117      74.424  37.642  33.913  1.00  7.80           C  
ATOM    982  C   GLY A 117      74.368  37.632  32.377  1.00  8.56           C  
ATOM    983  O   GLY A 117      73.948  38.628  31.792  1.00  9.68           O  
ATOM    984  N   THR A 118      74.742  36.517  31.722  1.00  8.33           N  
ATOM    985  CA  THR A 118      74.797  36.437  30.262  1.00  7.98           C  
ATOM    986  C   THR A 118      73.483  35.873  29.725  1.00  8.52           C  
ATOM    987  O   THR A 118      72.607  35.461  30.495  1.00  7.46           O  
ATOM    988  CB  THR A 118      75.977  35.585  29.754  1.00  8.05           C  
ATOM    989  OG1 THR A 118      75.710  34.206  30.030  1.00  7.76           O  
ATOM    990  CG2 THR A 118      77.313  35.992  30.345  1.00  7.71           C  
ATOM    991  N   ASP A 119      73.372  35.844  28.393  1.00  8.87           N  
ATOM    992  CA  ASP A 119      72.179  35.296  27.785  1.00 10.18           C  
ATOM    993  C   ASP A 119      72.246  33.769  27.828  1.00 10.21           C  
ATOM    994  O   ASP A 119      72.474  33.133  26.804  1.00 11.20           O  
ATOM    995  CB  ASP A 119      72.020  35.837  26.361  1.00 11.81           C  
ATOM    996  CG  ASP A 119      70.725  35.374  25.711  1.00 15.02           C  
ATOM    997  OD1 ASP A 119      69.752  35.046  26.441  1.00 15.09           O  
ATOM    998  OD2 ASP A 119      70.699  35.332  24.477  1.00 18.41           O  
ATOM    999  N   VAL A 120      72.005  33.179  29.009  1.00  9.54           N  
ATOM   1000  CA  VAL A 120      72.219  31.741  29.164  1.00  9.42           C  
ATOM   1001  C   VAL A 120      71.203  30.915  28.365  1.00  9.59           C  
ATOM   1002  O   VAL A 120      71.457  29.742  28.072  1.00  9.50           O  
ATOM   1003  CB  VAL A 120      72.260  31.312  30.643  1.00  8.75           C  
ATOM   1004  CG1 VAL A 120      73.460  31.897  31.382  1.00  9.18           C  
ATOM   1005  CG2 VAL A 120      70.960  31.620  31.354  1.00  8.69           C  
ATOM   1006  N   GLN A 121      70.044  31.496  28.017  1.00 10.82           N  
ATOM   1007  CA AGLN A 121      69.030  30.781  27.257  0.60 11.53           C  
ATOM   1008  CA BGLN A 121      69.050  30.728  27.286  0.40 10.58           C  
ATOM   1009  C   GLN A 121      69.603  30.342  25.912  1.00 10.10           C  
ATOM   1010  O   GLN A 121      69.139  29.372  25.311  1.00  9.91           O  
ATOM   1011  CB AGLN A 121      67.794  31.660  27.027  0.60 14.69           C  
ATOM   1012  CB BGLN A 121      67.685  31.431  27.282  0.40 11.83           C  
ATOM   1013  CG AGLN A 121      66.682  31.439  28.043  0.60 18.36           C  
ATOM   1014  CG BGLN A 121      66.816  31.070  26.088  0.40 12.71           C  
ATOM   1015  CD AGLN A 121      65.475  32.303  27.755  0.60 21.27           C  
ATOM   1016  CD BGLN A 121      65.352  30.879  26.394  0.40 14.05           C  
ATOM   1017  OE1AGLN A 121      64.985  32.351  26.625  0.60 23.91           O  
ATOM   1018  OE1BGLN A 121      64.934  30.844  27.551  0.40 15.06           O  
ATOM   1019  NE2AGLN A 121      64.982  32.996  28.779  0.60 22.74           N  
ATOM   1020  NE2BGLN A 121      64.551  30.744  25.342  0.40 14.37           N  
ATOM   1021  N   ALA A 122      70.613  31.067  25.420  1.00  9.07           N  
ATOM   1022  CA  ALA A 122      71.256  30.681  24.157  1.00  8.44           C  
ATOM   1023  C   ALA A 122      71.706  29.215  24.204  1.00  8.15           C  
ATOM   1024  O   ALA A 122      71.720  28.516  23.186  1.00  7.55           O  
ATOM   1025  CB  ALA A 122      72.425  31.593  23.835  1.00  8.60           C  
ATOM   1026  N   TRP A 123      72.046  28.732  25.403  1.00  7.78           N  
ATOM   1027  CA  TRP A 123      72.586  27.377  25.548  1.00  8.56           C  
ATOM   1028  C   TRP A 123      71.544  26.276  25.274  1.00  9.03           C  
ATOM   1029  O   TRP A 123      71.927  25.134  25.009  1.00  8.21           O  
ATOM   1030  CB  TRP A 123      73.296  27.227  26.910  1.00  8.35           C  
ATOM   1031  CG  TRP A 123      74.566  28.026  26.908  1.00  8.27           C  
ATOM   1032  CD1 TRP A 123      74.794  29.242  27.482  1.00  8.54           C  
ATOM   1033  CD2 TRP A 123      75.796  27.666  26.235  1.00  8.01           C  
ATOM   1034  NE1 TRP A 123      76.072  29.660  27.212  1.00  7.83           N  
ATOM   1035  CE2 TRP A 123      76.696  28.736  26.416  1.00  8.06           C  
ATOM   1036  CE3 TRP A 123      76.212  26.558  25.477  1.00  8.00           C  
ATOM   1037  CZ2 TRP A 123      78.001  28.696  25.907  1.00  8.00           C  
ATOM   1038  CZ3 TRP A 123      77.474  26.550  24.916  1.00  8.27           C  
ATOM   1039  CH2 TRP A 123      78.364  27.601  25.150  1.00  8.22           C  
ATOM   1040  N   ILE A 124      70.231  26.608  25.337  1.00  9.24           N  
ATOM   1041  CA AILE A 124      69.195  25.608  25.103  0.50 10.07           C  
ATOM   1042  CA BILE A 124      69.186  25.614  25.111  0.50 10.00           C  
ATOM   1043  C   ILE A 124      68.382  25.956  23.855  1.00 10.63           C  
ATOM   1044  O   ILE A 124      67.426  25.239  23.516  1.00 11.00           O  
ATOM   1045  CB AILE A 124      68.319  25.373  26.357  0.50  9.73           C  
ATOM   1046  CB BILE A 124      68.280  25.424  26.351  0.50  9.59           C  
ATOM   1047  CG1AILE A 124      67.717  26.669  26.913  0.50  9.85           C  
ATOM   1048  CG1BILE A 124      67.395  26.647  26.616  0.50  9.57           C  
ATOM   1049  CG2AILE A 124      69.110  24.625  27.425  0.50  9.75           C  
ATOM   1050  CG2BILE A 124      69.099  25.032  27.576  0.50  9.67           C  
ATOM   1051  CD1AILE A 124      66.631  27.282  26.058  0.50  9.86           C  
ATOM   1052  CD1BILE A 124      66.284  26.407  27.614  0.50  9.43           C  
ATOM   1053  N   ARG A 125      68.777  27.038  23.171  1.00 11.83           N  
ATOM   1054  CA  ARG A 125      68.079  27.529  21.983  1.00 14.82           C  
ATOM   1055  C   ARG A 125      68.167  26.461  20.900  1.00 14.86           C  
ATOM   1056  O   ARG A 125      69.238  25.910  20.663  1.00 15.01           O  
ATOM   1057  CB  ARG A 125      68.713  28.846  21.525  1.00 17.55           C  
ATOM   1058  CG  ARG A 125      68.001  29.582  20.398  1.00 22.00           C  
ATOM   1059  CD  ARG A 125      67.361  30.901  20.815  1.00 27.85           C  
ATOM   1060  NE  ARG A 125      68.254  31.895  21.407  1.00 30.05           N  
ATOM   1061  CZ  ARG A 125      68.166  32.379  22.647  1.00 32.20           C  
ATOM   1062  NH1 ARG A 125      67.209  31.954  23.459  1.00 36.08           N  
ATOM   1063  NH2 ARG A 125      69.035  33.285  23.074  1.00 30.12           N  
ATOM   1064  N   GLY A 126      67.019  26.143  20.287  1.00 15.28           N  
ATOM   1065  CA  GLY A 126      66.967  25.181  19.203  1.00 15.22           C  
ATOM   1066  C   GLY A 126      66.653  23.760  19.669  1.00 16.23           C  
ATOM   1067  O   GLY A 126      66.248  22.929  18.856  1.00 18.69           O  
ATOM   1068  N   CYS A 127      66.857  23.469  20.959  1.00 14.28           N  
ATOM   1069  CA  CYS A 127      66.771  22.101  21.458  1.00 13.96           C  
ATOM   1070  C   CYS A 127      65.315  21.660  21.642  1.00 14.69           C  
ATOM   1071  O   CYS A 127      64.516  22.403  22.196  1.00 14.35           O  
ATOM   1072  CB  CYS A 127      67.456  21.994  22.818  1.00 12.93           C  
ATOM   1073  SG  CYS A 127      69.219  22.454  22.801  1.00 11.96           S  
ATOM   1074  N   ARG A 128      65.013  20.402  21.295  1.00 14.97           N  
ATOM   1075  CA  ARG A 128      63.709  19.831  21.609  1.00 16.95           C  
ATOM   1076  C   ARG A 128      63.713  19.375  23.064  1.00 17.80           C  
ATOM   1077  O   ARG A 128      64.348  18.373  23.390  1.00 20.44           O  
ATOM   1078  CB  ARG A 128      63.391  18.673  20.657  1.00 17.07           C  
ATOM   1079  CG  ARG A 128      61.933  18.227  20.688  1.00 18.47           C  
ATOM   1080  CD  ARG A 128      61.678  17.161  19.635  1.00 19.54           C  
ATOM   1081  NE  ARG A 128      60.263  16.821  19.407  1.00 20.12           N  
ATOM   1082  CZ  ARG A 128      59.370  17.528  18.708  1.00 20.70           C  
ATOM   1083  NH1 ARG A 128      59.690  18.703  18.187  1.00 20.95           N  
ATOM   1084  NH2 ARG A 128      58.146  17.052  18.530  1.00 21.49           N  
ATOM   1085  N   LEU A 129      63.016  20.116  23.934  1.00 18.17           N  
ATOM   1086  CA  LEU A 129      63.089  19.858  25.362  1.00 20.44           C  
ATOM   1087  C   LEU A 129      61.683  19.731  25.952  1.00 23.76           C  
ATOM   1088  O   LEU A 129      61.482  19.045  26.976  1.00 25.46           O  
ATOM   1089  CB  LEU A 129      63.827  21.018  26.038  1.00 20.48           C  
ATOM   1090  CG  LEU A 129      65.340  21.016  25.836  1.00 20.24           C  
ATOM   1091  CD1 LEU A 129      65.923  22.351  26.267  1.00 21.66           C  
ATOM   1092  CD2 LEU A 129      65.986  19.872  26.614  1.00 17.89           C  
ATOM   1093  OXT LEU A 129      60.763  20.352  25.392  1.00 25.82           O  
TER    1094      LEU A 129                                                      
HETATM 1095  C1  EDO A 201      82.098  23.537  42.331  1.00 19.14           C  
HETATM 1096  O1  EDO A 201      83.381  24.022  41.962  1.00 20.96           O  
HETATM 1097  C2  EDO A 201      82.147  22.074  42.435  1.00 17.19           C  
HETATM 1098  O2  EDO A 201      82.971  21.718  43.508  1.00 14.52           O  
HETATM 1099  C1  EDO A 202      76.367  28.957  21.670  1.00 35.65           C  
HETATM 1100  O1  EDO A 202      75.579  27.781  21.581  1.00 34.31           O  
HETATM 1101  C2  EDO A 202      75.551  30.136  22.027  1.00 34.25           C  
HETATM 1102  O2  EDO A 202      75.967  30.795  23.211  1.00 35.59           O  
HETATM 1103  C1  EDO A 203      88.154  20.592  53.634  1.00 28.91           C  
HETATM 1104  O1  EDO A 203      88.467  21.887  54.095  1.00 31.13           O  
HETATM 1105  C2  EDO A 203      86.933  19.986  54.224  1.00 27.82           C  
HETATM 1106  O2  EDO A 203      87.154  19.333  55.481  1.00 24.97           O  
HETATM 1107  C1  EDO A 204      66.471  12.496  28.502  0.50 23.61           C  
HETATM 1108  O1  EDO A 204      67.793  12.169  28.887  0.50 23.74           O  
HETATM 1109  C2  EDO A 204      66.067  11.865  27.222  0.50 23.11           C  
HETATM 1110  O2  EDO A 204      66.677  10.608  26.990  0.50 23.21           O  
HETATM 1111 CL    CL A 205      90.598  11.736  50.900  1.00  8.62          CL  
HETATM 1112 CL    CL A 206      70.544  31.586  44.560  1.00  9.01          CL  
HETATM 1113 CL    CL A 207      89.267   5.702  49.303  1.00 20.05          CL  
HETATM 1114 CL    CL A 208      67.743  29.044  30.157  1.00 16.16          CL  
HETATM 1115 CL    CL A 209      72.457  10.447  31.657  1.00 20.53          CL  
HETATM 1116 CL    CL A 210      81.837  13.539  54.889  1.00 23.07          CL  
HETATM 1117 CL    CL A 211      78.506  23.899  22.248  1.00 18.67          CL  
HETATM 1118 CL    CL A 212      84.318   5.990  48.180  1.00 17.70          CL  
HETATM 1119 NA    NA A 213      86.723  14.188  49.712  1.00  7.66          NA  
HETATM 1120 NA    NA A 214      77.579  10.975  37.317  1.00 13.02          NA  
HETATM 1121 NA    NA A 215      80.585  16.680  37.630  1.00  9.32          NA  
HETATM 1122 NA    NA A 216      83.518  32.827  28.478  1.00 12.56          NA  
HETATM 1123  O   HOH A 301      91.801  20.235  33.053  0.50  9.42           O  
HETATM 1124  O   HOH A 302      91.334  24.938  49.335  0.50  7.23           O  
HETATM 1125  O   HOH A 303      83.224  23.377  46.301  1.00 17.85           O  
HETATM 1126  O  AHOH A 304      86.672  24.288  37.135  0.50  8.49           O  
HETATM 1127  O  BHOH A 304      86.974  26.215  36.828  0.50  6.82           O  
HETATM 1128  O   HOH A 305      64.374  16.324  24.647  1.00 24.12           O  
HETATM 1129  O   HOH A 306      82.625  32.224  42.857  1.00 21.40           O  
HETATM 1130  O   HOH A 307      75.639   7.539  24.938  1.00 27.76           O  
HETATM 1131  O   HOH A 308      65.740   9.049  28.799  1.00 11.45           O  
HETATM 1132  O   HOH A 309      84.840  26.566  38.295  1.00  8.60           O  
HETATM 1133  O   HOH A 310      64.896  24.775  23.418  1.00 23.65           O  
HETATM 1134  O   HOH A 311      69.133  11.151  30.847  1.00 20.92           O  
HETATM 1135  O   HOH A 312      84.532  23.306  39.562  1.00 25.32           O  
HETATM 1136  O   HOH A 313      79.881  13.948  34.997  1.00 10.90           O  
HETATM 1137  O   HOH A 314      79.516  18.389  22.373  1.00 10.95           O  
HETATM 1138  O   HOH A 315      70.949  15.591  46.053  1.00 17.54           O  
HETATM 1139  O   HOH A 316      74.319   9.009  29.096  1.00 20.18           O  
HETATM 1140  O   HOH A 317      87.483  23.199  34.048  1.00 18.22           O  
HETATM 1141  O   HOH A 318      83.776  37.879  37.525  1.00 19.15           O  
HETATM 1142  O   HOH A 319      77.062  12.158  22.983  1.00 18.97           O  
HETATM 1143  O   HOH A 320      86.401  26.167  33.749  1.00 11.27           O  
HETATM 1144  O   HOH A 321      78.413  12.011  34.569  1.00  6.92           O  
HETATM 1145  O   HOH A 322      93.591   7.501  51.632  1.00 15.50           O  
HETATM 1146  O   HOH A 323      80.263  37.679  37.190  1.00 20.08           O  
HETATM 1147  O   HOH A 324      66.408  18.084  45.985  1.00 23.08           O  
HETATM 1148  O   HOH A 325      72.494  28.175  47.709  1.00  8.83           O  
HETATM 1149  O   HOH A 326      73.921  21.725  50.640  1.00 18.31           O  
HETATM 1150  O   HOH A 327      94.693  17.981  49.090  1.00 29.87           O  
HETATM 1151  O   HOH A 328      92.556  14.820  44.682  1.00  4.81           O  
HETATM 1152  O   HOH A 329      75.574   8.393  37.734  1.00  8.76           O  
HETATM 1153  O   HOH A 330      90.386  13.384  32.781  1.00  6.77           O  
HETATM 1154  O   HOH A 331      60.027  11.755  35.566  1.00 20.49           O  
HETATM 1155  O   HOH A 332      80.574  33.626  28.211  1.00 10.69           O  
HETATM 1156  O   HOH A 333      88.027  22.322  36.906  1.00  7.86           O  
HETATM 1157  O   HOH A 334      64.929  17.196  42.548  1.00 22.33           O  
HETATM 1158  O   HOH A 335      74.997  33.236  25.797  1.00 16.61           O  
HETATM 1159  O   HOH A 336      82.887   7.265  31.763  1.00  9.75           O  
HETATM 1160  O   HOH A 337      96.225  15.788  48.013  1.00 21.28           O  
HETATM 1161  O   HOH A 338      83.104   6.156  36.387  1.00 16.79           O  
HETATM 1162  O   HOH A 339      94.350  18.358  51.382  1.00 32.10           O  
HETATM 1163  O   HOH A 340      64.461  31.772  38.748  1.00 15.17           O  
HETATM 1164  O   HOH A 341      64.364  15.443  29.142  1.00 24.40           O  
HETATM 1165  O   HOH A 342      84.572  10.903  27.524  1.00  7.92           O  
HETATM 1166  O   HOH A 343      68.242  31.325  42.132  1.00 10.04           O  
HETATM 1167  O   HOH A 344      85.521  24.027  43.763  1.00 29.01           O  
HETATM 1168  O   HOH A 345      89.206   8.902  52.220  1.00 19.56           O  
HETATM 1169  O   HOH A 346      78.944  38.603  40.399  1.00 15.07           O  
HETATM 1170  O   HOH A 347      76.365  27.007  46.812  1.00  9.56           O  
HETATM 1171  O   HOH A 348      89.169  22.759  46.971  1.00 27.83           O  
HETATM 1172  O   HOH A 349      77.724  39.118  33.099  1.00 17.50           O  
HETATM 1173  O   HOH A 350      85.382  19.307  57.660  1.00 22.62           O  
HETATM 1174  O   HOH A 351      88.153  14.422  56.996  1.00 21.84           O  
HETATM 1175  O   HOH A 352      76.227  32.515  27.843  1.00  8.77           O  
HETATM 1176  O   HOH A 353      75.653  12.038  43.737  1.00 16.56           O  
HETATM 1177  O   HOH A 354      76.942  31.267  51.955  1.00 30.31           O  
HETATM 1178  O   HOH A 355      75.099  37.378  26.760  1.00 12.17           O  
HETATM 1179  O   HOH A 356      68.892   7.687  37.489  1.00 24.87           O  
HETATM 1180  O   HOH A 357      74.797  12.803  46.298  1.00 14.76           O  
HETATM 1181  O   HOH A 358      79.785  36.150  33.830  1.00  7.74           O  
HETATM 1182  O   HOH A 359      82.279   4.778  40.201  1.00 18.35           O  
HETATM 1183  O   HOH A 360      81.849   7.375  29.249  1.00 11.10           O  
HETATM 1184  O   HOH A 361      72.860  33.779  35.090  1.00 10.44           O  
HETATM 1185  O   HOH A 362      88.653  12.755  48.802  1.00  2.83           O  
HETATM 1186  O   HOH A 363      84.751  26.332  40.943  1.00  8.99           O  
HETATM 1187  O   HOH A 364      80.421   5.233  32.226  1.00 14.75           O  
HETATM 1188  O   HOH A 365      67.658  14.229  42.722  1.00 24.14           O  
HETATM 1189  O   HOH A 366      64.741  25.862  32.941  1.00  8.84           O  
HETATM 1190  O   HOH A 367      67.479  31.257  35.979  1.00  6.57           O  
HETATM 1191  O   HOH A 368      94.864  18.654  35.991  1.00 14.40           O  
HETATM 1192  O   HOH A 369      71.694  35.450  33.270  1.00 10.57           O  
HETATM 1193  O   HOH A 370      87.158  18.042  28.931  1.00 20.62           O  
HETATM 1194  O   HOH A 371      84.754  24.721  26.958  1.00 18.84           O  
HETATM 1195  O   HOH A 372      91.688  12.795  55.428  0.50 16.21           O  
HETATM 1196  O   HOH A 373      71.723  10.844  26.274  1.00 21.11           O  
HETATM 1197  O   HOH A 374      84.754  17.624  25.199  1.00 14.22           O  
HETATM 1198  O   HOH A 375      81.786  19.661  23.353  1.00 11.93           O  
HETATM 1199  O   HOH A 376      93.923  25.321  41.714  1.00 34.98           O  
HETATM 1200  O   HOH A 377      64.313  23.814  43.604  1.00 18.61           O  
HETATM 1201  O   HOH A 378      86.497  12.196  51.095  1.00  7.64           O  
HETATM 1202  O   HOH A 379      66.960  31.601  31.077  1.00 32.73           O  
HETATM 1203  O   HOH A 380      69.687  33.301  34.203  1.00 13.08           O  
HETATM 1204  O   HOH A 381      82.394  21.736  21.604  1.00 31.40           O  
HETATM 1205  O   HOH A 382      93.390  24.814  45.087  1.00 22.31           O  
HETATM 1206  O   HOH A 383      87.072  17.246  26.545  1.00 18.70           O  
HETATM 1207  O   HOH A 384      72.911  17.281  21.061  1.00  9.05           O  
HETATM 1208  O   HOH A 385      81.346  10.164  23.597  1.00 13.28           O  
HETATM 1209  O   HOH A 386      77.745   6.955  38.643  1.00 16.97           O  
HETATM 1210  O   HOH A 387      69.012  34.059  29.325  1.00 17.20           O  
HETATM 1211  O   HOH A 388      73.228  19.871  20.205  1.00 16.55           O  
HETATM 1212  O   HOH A 389      75.794  41.032  32.320  1.00 34.00           O  
HETATM 1213  O   HOH A 390      93.714  15.950  35.905  1.00 22.37           O  
HETATM 1214  O   HOH A 391      97.316  10.096  42.808  1.00 12.41           O  
HETATM 1215  O   HOH A 392      78.246  27.497  48.366  1.00 25.85           O  
HETATM 1216  O   HOH A 393      78.503  36.485  44.109  1.00 19.38           O  
HETATM 1217  O   HOH A 394      81.834  38.110  39.730  1.00 28.37           O  
HETATM 1218  O   HOH A 395      79.268   5.556  48.284  1.00 28.90           O  
HETATM 1219  O   HOH A 396      81.507   7.024  48.909  1.00 13.57           O  
HETATM 1220  O   HOH A 397      84.235   8.832  52.426  1.00 14.58           O  
HETATM 1221  O   HOH A 398      86.142  11.821  53.687  1.00 25.12           O  
HETATM 1222  O   HOH A 399      89.684  12.690  53.781  1.00 20.74           O  
HETATM 1223  O   HOH A 400      84.925  22.166  21.259  1.00 21.92           O  
HETATM 1224  O   HOH A 401      67.268  32.928  33.259  1.00 26.48           O  
HETATM 1225  O   HOH A 402      85.444  17.242  59.724  1.00 21.75           O  
HETATM 1226  O   HOH A 403      75.459  39.126  36.565  1.00  9.83           O  
HETATM 1227  O   HOH A 404      93.354  11.573  52.558  1.00 16.44           O  
HETATM 1228  O   HOH A 405      81.204   4.553  34.906  1.00 19.15           O  
HETATM 1229  O   HOH A 406      74.168   9.636  43.510  1.00 17.76           O  
HETATM 1230  O   HOH A 407      70.669  37.831  33.545  1.00 15.88           O  
HETATM 1231  O   HOH A 408      78.897  32.144  26.563  1.00 17.65           O  
HETATM 1232  O   HOH A 409      80.896  25.302  47.846  1.00 30.49           O  
HETATM 1233  O   HOH A 410      71.144  29.630  51.651  1.00 30.06           O  
HETATM 1234  O   HOH A 411      76.247  39.208  28.392  1.00 27.52           O  
HETATM 1235  O   HOH A 412      90.865   6.376  51.746  1.00 25.66           O  
HETATM 1236  O   HOH A 413      76.816  35.586  25.697  1.00 34.18           O  
HETATM 1237  O   HOH A 414      78.110  39.154  37.741  1.00 15.01           O  
HETATM 1238  O   HOH A 415      97.719  18.826  36.952  0.50 21.26           O  
HETATM 1239  O   HOH A 416      80.125   4.236  41.883  1.00 33.58           O  
HETATM 1240  O   HOH A 417      78.477   5.319  43.484  1.00 26.98           O  
HETATM 1241  O   HOH A 418      66.566  30.523  51.001  1.00 37.07           O  
CONECT   54 1073                                                                
CONECT  270  970                                                                
CONECT  454 1121                                                                
CONECT  516 1119                                                                
CONECT  569 1119                                                                
CONECT  571  701                                                                
CONECT  634 1119                                                                
CONECT  638 1119                                                                
CONECT  672  795                                                                
CONECT  701  571                                                                
CONECT  711 1120                                                                
CONECT  744 1120                                                                
CONECT  774 1121                                                                
CONECT  795  672                                                                
CONECT  970  270                                                                
CONECT 1073   54                                                                
CONECT 1095 1096 1097                                                           
CONECT 1096 1095                                                                
CONECT 1097 1095 1098                                                           
CONECT 1098 1097                                                                
CONECT 1099 1100 1101                                                           
CONECT 1100 1099                                                                
CONECT 1101 1099 1102                                                           
CONECT 1102 1101                                                                
CONECT 1103 1104 1105                                                           
CONECT 1104 1103                                                                
CONECT 1105 1103 1106                                                           
CONECT 1106 1105                                                                
CONECT 1107 1108 1109                                                           
CONECT 1108 1107                                                                
CONECT 1109 1107 1110                                                           
CONECT 1110 1109                                                                
CONECT 1119  516  569  634  638                                                 
CONECT 1119 1185 1201                                                           
CONECT 1120  711  744 1144                                                      
CONECT 1121  454  774                                                           
CONECT 1122 1155                                                                
CONECT 1144 1120                                                                
CONECT 1155 1122                                                                
CONECT 1185 1119                                                                
CONECT 1201 1119                                                                
MASTER      319    0   16    9    3    0    0    6 1147    1   41   10          
END                                                                             
