HEADER    OXIDOREDUCTASE                          14-FEB-14   4OZ7              
TITLE     METHANOBACTIN PRODUCTION BY METHANOTROPHIC BACTERIA AND THEIR         
TITLE    2 STRUCTURAL DIVERSITY FROM METHYLOSINUS STRAINS: INSIGHTS INTO COPPER 
TITLE    3 RELEASE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METHANOBACTIN;                                             
COMPND   3 CHAIN: A, B                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: METHYLOSINUS SPORIUM;                           
SOURCE   3 ORGANISM_TAXID: 428;                                                 
SOURCE   4 STRAIN: NR3K                                                         
KEYWDS    COPPER UPTAKE, PARTICULATE METHANE MONOOXYGENASE, OXIDOREDUCTASE      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.EL GHAZOUANI,A.BASLE,C.DENNISON                                     
REVDAT   1   20-MAY-15 4OZ7    0                                                
JRNL        AUTH   A.EL GHAZOUANI,A.BASLE,C.DENNISON                            
JRNL        TITL   METHANOBACTIN PRODUCTION BY METHANOTROPHIC BACTERIA AND      
JRNL        TITL 2 THEIR STRUCTURAL DIVERSITY FROM METHYLOSINUS STRAINS:        
JRNL        TITL 3 INSIGHTS INTO COPPER RELEASE                                 
JRNL        REF    TO BE PUBLISHED                                              
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
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) : 28.16                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 3512                           
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) : 0.222                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 164                             
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) : 233                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.08                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2430                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 12                           
REMARK   3   BIN FREE R VALUE                    : 0.1300                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 154                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 25                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.95000                                             
REMARK   3    B22 (A**2) : 2.45000                                              
REMARK   3    B33 (A**2) : -1.50000                                             
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): 0.095         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.096         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.069         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.187         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   160 ; 0.012 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):   206 ; 2.859 ; 2.363       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):    12 ; 4.046 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):     2 ;34.537 ;30.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):    10 ; 9.969 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):    22 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   108 ; 0.004 ; 0.022       
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):    71 ; 0.795 ; 2.352       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):    72 ; 1.281 ; 3.574       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):    88 ; 0.842 ; 2.285       
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):   236 ; 3.993 ;22.208       
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: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4OZ7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000200303.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-NOV-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 3677                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.160                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.08700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.1 M SODIUM MALONATE, 100 MM HEPES PH   
REMARK 280  7.0, 0.5% V/V JEFFAMINE ED-2001, 0.5% W/V OCTYL-BETA-D-GLUCOSIDE,   
REMARK 280  CRYSTAL WERE CRYOPROTECTED WITH THE ABOVE CONDITION                 
REMARK 280  SUPPLEMENTED WITH 20% GLYCEROL., VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+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        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       18.36000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       19.71000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       20.12000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       18.36000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       19.71000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       20.12000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       18.36000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       19.71000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       20.12000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       18.36000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       19.71000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       20.12000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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 B 209  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    22W A   6   CA  -  C   -  N   ANGL. DEV. =  21.9 DEGREES          
REMARK 500    22W A   6   O   -  C   -  N   ANGL. DEV. = -15.7 DEGREES          
REMARK 500    22W B   6   CA  -  C   -  N   ANGL. DEV. =  18.1 DEGREES          
REMARK 500    22W B   6   O   -  C   -  N   ANGL. DEV. = -19.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    22W A   6        178.46                                           
REMARK 500    22W B   6       -173.18                                           
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                             CU1 A 101  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 22W A   6   S                                                      
REMARK 620 2 22W A   6   NB   86.4                                              
REMARK 620 3 22Q B   1   N   104.9  45.9                                        
REMARK 620 4 22Q B   1   S   108.9  48.1   4.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 B 101  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 22W B   6   S                                                      
REMARK 620 2 22W B   6   NB   87.3                                              
REMARK 620 3 22Q A   1   N   100.6  52.5                                        
REMARK 620 4 22Q A   1   S   104.8  53.8   4.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU1 A 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU1 B 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues 22W A 6 through   
REMARK 800  GLY A 7 bound to SER A 5                                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues 22W B 6 through   
REMARK 800  GLY B 7 bound to SER B 5                                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 22Q B 1 and ALA B 2    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4OZ8   RELATED DB: PDB                                   
DBREF  4OZ7 A    1    10  PDB    4OZ7     4OZ7             1     10             
DBREF  4OZ7 B    1    10  PDB    4OZ7     4OZ7             1     10             
SEQRES   1 A   10  22Q ALA SER CYS SER 22W GLY PRO ASN CYS                      
SEQRES   1 B   10  22Q ALA SER CYS SER 22W GLY PRO ASN CYS                      
HET    22Q  A   1      14                                                       
HET    22W  A   6      14                                                       
HET    22Q  B   1      14                                                       
HET    22W  B   6      14                                                       
HET    CU1  A 101       1                                                       
HET    CU1  B 101       1                                                       
HETNAM     22Q (3Z)-5-(2-METHYLPROPYL)-3-(SULFANYLMETHYLIDENE)                  
HETNAM   2 22Q  PYRAZINE-2,6(1H,3H)-DIONE                                       
HETNAM     22W 2-[(1S,2S)-1-AMINO-2-METHYLBUTYL]-4-                             
HETNAM   2 22W  (THIOXOMETHYLIDENE)-1,3-OXAZOL-5(4H)-ONE                        
HETNAM     CU1 COPPER (I) ION                                                   
FORMUL   1  22Q    2(C9 H12 N2 O2 S)                                            
FORMUL   1  22W    2(C9 H12 N2 O2 S)                                            
FORMUL   3  CU1    2(CU 1+)                                                     
FORMUL   5  HOH   *25(H2 O)                                                     
SSBOND   1 CYS A    4    CYS A   10                          1555   1555  2.03  
SSBOND   2 CYS B    4    CYS B   10                          1555   1555  2.03  
LINK         C   22Q A   1                 N   ALA A   2     1555   1555  1.34  
LINK         C   SER A   5                 N   22W A   6     1555   1555  1.35  
LINK         C   22W A   6                 N   GLY A   7     1555   1555  1.34  
LINK         S   22W A   6                CU   CU1 A 101     1555   1555  2.35  
LINK         NB  22W A   6                CU   CU1 A 101     1555   1555  2.14  
LINK         C   22Q B   1                 N   ALA B   2     1555   1555  1.34  
LINK         C   SER B   5                 N   22W B   6     1555   1555  1.35  
LINK         C   22W B   6                 N   GLY B   7     1555   1555  1.34  
LINK         S   22W B   6                CU   CU1 B 101     1555   1555  2.23  
LINK         NB  22W B   6                CU   CU1 B 101     1555   1555  2.17  
LINK         N   22Q A   1                CU   CU1 B 101     1555   6345  2.05  
LINK         S   22Q A   1                CU   CU1 B 101     1555   6345  2.26  
LINK         N   22Q B   1                CU   CU1 A 101     1555   6344  2.07  
LINK         S   22Q B   1                CU   CU1 A 101     1555   6344  2.22  
SITE     1 AC1  2 22W A   6  22Q B   1                                          
SITE     1 AC2  2 22Q A   1  22W B   6                                          
SITE     1 AC3 10 CYS A   4  SER A   5  PRO A   8  ASN A   9                    
SITE     2 AC3 10 CYS A  10  CU1 A 101  HOH A 203  22Q B   1                    
SITE     3 AC3 10 PRO B   8  HOH B 202                                          
SITE     1 AC4 11 22Q A   1  SER A   5  PRO A   8  HOH A 201                    
SITE     2 AC4 11 CYS B   4  SER B   5  PRO B   8  ASN B   9                    
SITE     3 AC4 11 CYS B  10  CU1 B 101  HOH B 205                               
SITE     1 AC5  8 SER A   3  CYS A   4  SER A   5  22W A   6                    
SITE     2 AC5  8 CU1 A 101  SER B   3  HOH B 203  HOH B 210                    
CRYST1   36.720   39.420   40.240  90.00  90.00  90.00 I 2 2 2      16          
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      0.027233  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.025368  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.024851        0.00000                         
HETATM    1  C   22Q A   1     -23.828 -13.217  15.763  1.00 22.06           C  
HETATM    2  N   22Q A   1     -23.121 -12.941  18.023  1.00 22.71           N  
HETATM    3  S   22Q A   1     -22.855 -11.890  15.256  1.00 20.75           S  
HETATM    4  C1  22Q A   1     -23.218 -13.160  19.348  1.00 23.29           C  
HETATM    5  N1  22Q A   1     -25.145 -14.553  18.944  1.00 23.83           N  
HETATM    6  C2  22Q A   1     -25.006 -14.299  17.577  1.00 23.25           C  
HETATM    7  O2  22Q A   1     -25.808 -14.814  16.800  1.00 24.43           O  
HETATM    8  O3  22Q A   1     -24.374 -14.201  21.044  1.00 24.70           O  
HETATM    9  C4  22Q A   1     -22.286 -12.553  20.203  1.00 23.16           C  
HETATM   10  C5  22Q A   1     -24.244 -13.974  19.842  1.00 23.86           C  
HETATM   11  C6  22Q A   1     -21.258 -13.470  20.901  1.00 23.48           C  
HETATM   12  C7  22Q A   1     -20.428 -14.268  19.885  1.00 23.53           C  
HETATM   13  C8  22Q A   1     -20.313 -12.611  21.746  1.00 24.07           C  
HETATM   14  CA  22Q A   1     -23.974 -13.474  17.130  1.00 22.47           C  
ATOM     15  N   ALA A   2     -24.495 -13.859  14.799  1.00 22.22           N  
ATOM     16  CA  ALA A   2     -24.523 -13.670  13.326  1.00 23.23           C  
ATOM     17  C   ALA A   2     -25.897 -14.032  12.797  1.00 23.77           C  
ATOM     18  O   ALA A   2     -26.601 -14.864  13.377  1.00 24.36           O  
ATOM     19  CB  ALA A   2     -23.448 -14.513  12.654  1.00 23.25           C  
ATOM     20  N   SER A   3     -26.288 -13.373  11.715  1.00 24.14           N  
ATOM     21  CA  SER A   3     -27.520 -13.711  11.028  1.00 24.71           C  
ATOM     22  C   SER A   3     -27.239 -13.863   9.542  1.00 24.52           C  
ATOM     23  O   SER A   3     -26.257 -13.319   9.019  1.00 24.11           O  
ATOM     24  CB  SER A   3     -28.609 -12.666  11.287  1.00 25.64           C  
ATOM     25  OG  SER A   3     -28.214 -11.390  10.823  1.00 27.86           O  
ATOM     26  N   CYS A   4     -28.088 -14.632   8.873  1.00 23.46           N  
ATOM     27  CA  CYS A   4     -27.974 -14.805   7.442  1.00 22.85           C  
ATOM     28  C   CYS A   4     -28.521 -13.570   6.743  1.00 23.04           C  
ATOM     29  O   CYS A   4     -29.712 -13.255   6.843  1.00 24.32           O  
ATOM     30  CB  CYS A   4     -28.719 -16.056   6.991  1.00 22.80           C  
ATOM     31  SG  CYS A   4     -28.497 -16.362   5.233  1.00 22.64           S  
ATOM     32  N   SER A   5     -27.638 -12.868   6.045  1.00 21.84           N  
ATOM     33  CA  SER A   5     -27.989 -11.616   5.400  1.00 21.75           C  
ATOM     34  C   SER A   5     -28.175 -11.813   3.905  1.00 21.22           C  
ATOM     35  O   SER A   5     -28.727 -10.948   3.229  1.00 21.81           O  
ATOM     36  CB  SER A   5     -26.910 -10.563   5.666  1.00 21.62           C  
ATOM     37  OG  SER A   5     -25.630 -11.070   5.326  1.00 21.78           O  
HETATM   38  C   22W A   6     -27.414 -18.020   1.929  1.00 19.81           C  
HETATM   39  N   22W A   6     -27.560 -12.822   3.261  1.00 19.91           N  
HETATM   40  O   22W A   6     -29.323 -14.902   1.057  1.00 19.69           O  
HETATM   41  S   22W A   6     -25.985 -18.276   2.540  1.00 20.77           S  
HETATM   42  CA  22W A   6     -27.672 -13.105   1.800  1.00 19.45           C  
HETATM   43  CB  22W A   6     -26.389 -12.723   1.054  1.00 19.25           C  
HETATM   44  NB  22W A   6     -27.314 -15.567   1.929  1.00 19.45           N  
HETATM   45  CE  22W A   6     -28.045 -14.574   1.604  1.00 19.52           C  
HETATM   46  CF  22W A   6     -27.926 -16.652   1.686  1.00 19.71           C  
HETATM   47  O26 22W A   6     -30.098 -17.090   0.760  1.00 20.03           O  
HETATM   48  C83 22W A   6     -29.222 -16.327   1.121  1.00 19.58           C  
HETATM   49  CD1 22W A   6     -24.686 -10.900   0.836  1.00 19.41           C  
HETATM   50  CG1 22W A   6     -26.101 -11.235   1.259  1.00 19.40           C  
HETATM   51  CG2 22W A   6     -26.559 -13.015  -0.436  1.00 18.83           C  
ATOM     52  N   GLY A   7     -28.167 -19.068   1.568  1.00 19.72           N  
ATOM     53  CA  GLY A   7     -27.934 -20.478   1.978  1.00 20.70           C  
ATOM     54  C   GLY A   7     -29.227 -21.235   2.211  1.00 21.41           C  
ATOM     55  O   GLY A   7     -30.300 -20.629   2.234  1.00 21.11           O  
ATOM     56  N   PRO A   8     -29.129 -22.566   2.391  1.00 22.28           N  
ATOM     57  CA  PRO A   8     -30.287 -23.465   2.483  1.00 23.15           C  
ATOM     58  C   PRO A   8     -31.247 -23.144   3.635  1.00 23.99           C  
ATOM     59  O   PRO A   8     -32.462 -23.289   3.483  1.00 24.15           O  
ATOM     60  CB  PRO A   8     -29.649 -24.850   2.671  1.00 22.80           C  
ATOM     61  CG  PRO A   8     -28.278 -24.580   3.172  1.00 22.68           C  
ATOM     62  CD  PRO A   8     -27.861 -23.311   2.490  1.00 22.57           C  
ATOM     63  N   ASN A   9     -30.714 -22.706   4.769  1.00 25.02           N  
ATOM     64  CA  ASN A   9     -31.567 -22.347   5.897  1.00 26.89           C  
ATOM     65  C   ASN A   9     -31.508 -20.868   6.302  1.00 26.78           C  
ATOM     66  O   ASN A   9     -31.736 -20.526   7.463  1.00 27.54           O  
ATOM     67  CB  ASN A   9     -31.331 -23.284   7.099  1.00 29.04           C  
ATOM     68  CG  ASN A   9     -29.865 -23.616   7.319  1.00 30.79           C  
ATOM     69  OD1 ASN A   9     -29.516 -24.767   7.584  1.00 32.54           O  
ATOM     70  ND2 ASN A   9     -29.000 -22.612   7.221  1.00 32.47           N  
ATOM     71  N   CYS A  10     -31.218 -20.000   5.333  1.00 25.69           N  
ATOM     72  CA  CYS A  10     -31.192 -18.557   5.553  1.00 25.73           C  
ATOM     73  C   CYS A  10     -32.515 -18.061   6.139  1.00 27.03           C  
ATOM     74  O   CYS A  10     -32.557 -17.420   7.190  1.00 28.38           O  
ATOM     75  CB  CYS A  10     -30.897 -17.825   4.242  1.00 24.35           C  
ATOM     76  SG  CYS A  10     -30.352 -16.115   4.453  1.00 23.18           S  
ATOM     77  OXT CYS A  10     -33.582 -18.304   5.576  1.00 28.08           O  
TER      78      CYS A  10                                                      
HETATM   79  C   22Q B   1     -31.369  -5.522 -15.614  1.00 21.08           C  
HETATM   80  N   22Q B   1     -31.268  -4.746 -17.864  1.00 20.78           N  
HETATM   81  S   22Q B   1     -29.946  -4.628 -15.217  1.00 20.20           S  
HETATM   82  C1  22Q B   1     -31.616  -4.787 -19.166  1.00 21.33           C  
HETATM   83  N1  22Q B   1     -33.054  -6.676 -18.697  1.00 21.34           N  
HETATM   84  C2  22Q B   1     -32.673  -6.600 -17.356  1.00 21.37           C  
HETATM   85  O2  22Q B   1     -33.154  -7.408 -16.562  1.00 21.48           O  
HETATM   86  O3  22Q B   1     -32.870  -5.855 -20.790  1.00 22.05           O  
HETATM   87  C4  22Q B   1     -31.032  -3.850 -20.028  1.00 21.61           C  
HETATM   88  C5  22Q B   1     -32.522  -5.764 -19.614  1.00 21.44           C  
HETATM   89  C6  22Q B   1     -31.930  -2.740 -20.607  1.00 22.02           C  
HETATM   90  C7  22Q B   1     -32.617  -1.938 -19.496  1.00 22.26           C  
HETATM   91  C8  22Q B   1     -31.065  -1.804 -21.453  1.00 22.14           C  
HETATM   92  CA  22Q B   1     -31.757  -5.614 -16.955  1.00 20.81           C  
ATOM     93  N   ALA B   2     -31.881  -6.203 -14.584  1.00 22.30           N  
ATOM     94  CA  ALA B   2     -31.432  -6.397 -13.182  1.00 23.07           C  
ATOM     95  C   ALA B   2     -31.769  -7.804 -12.741  1.00 23.34           C  
ATOM     96  O   ALA B   2     -32.653  -8.444 -13.312  1.00 23.65           O  
ATOM     97  CB  ALA B   2     -32.089  -5.376 -12.265  1.00 23.16           C  
ATOM     98  N   SER B   3     -31.045  -8.287 -11.740  1.00 23.85           N  
ATOM     99  CA  SER B   3     -31.328  -9.581 -11.141  1.00 24.19           C  
ATOM    100  C   SER B   3     -31.374  -9.448  -9.627  1.00 24.19           C  
ATOM    101  O   SER B   3     -30.788  -8.526  -9.055  1.00 23.76           O  
ATOM    102  CB  SER B   3     -30.285 -10.618 -11.558  1.00 25.31           C  
ATOM    103  OG  SER B   3     -29.010 -10.294 -11.034  1.00 27.12           O  
ATOM    104  N   CYS B   4     -32.096 -10.365  -8.991  1.00 23.50           N  
ATOM    105  CA  CYS B   4     -32.190 -10.399  -7.545  1.00 23.56           C  
ATOM    106  C   CYS B   4     -30.922 -11.010  -6.996  1.00 23.53           C  
ATOM    107  O   CYS B   4     -30.681 -12.208  -7.147  1.00 25.01           O  
ATOM    108  CB  CYS B   4     -33.396 -11.215  -7.098  1.00 23.24           C  
ATOM    109  SG  CYS B   4     -33.590 -11.201  -5.306  1.00 23.23           S  
ATOM    110  N   SER B   5     -30.105 -10.178  -6.369  1.00 23.12           N  
ATOM    111  CA  SER B   5     -28.821 -10.620  -5.864  1.00 23.13           C  
ATOM    112  C   SER B   5     -28.929 -11.043  -4.402  1.00 22.51           C  
ATOM    113  O   SER B   5     -28.042 -11.731  -3.888  1.00 23.47           O  
ATOM    114  CB  SER B   5     -27.784  -9.510  -6.036  1.00 22.91           C  
ATOM    115  OG  SER B   5     -28.240  -8.308  -5.446  1.00 23.14           O  
HETATM  116  C   22W B   6     -34.956 -10.355  -1.926  1.00 20.07           C  
HETATM  117  N   22W B   6     -29.898 -10.501  -3.638  1.00 20.52           N  
HETATM  118  O   22W B   6     -31.797 -12.329  -1.378  1.00 20.12           O  
HETATM  119  S   22W B   6     -35.202  -8.879  -2.416  1.00 20.49           S  
HETATM  120  CA  22W B   6     -30.060 -10.639  -2.158  1.00 19.80           C  
HETATM  121  CB  22W B   6     -29.585  -9.389  -1.408  1.00 19.96           C  
HETATM  122  NB  22W B   6     -32.518 -10.264  -2.043  1.00 20.07           N  
HETATM  123  CE  22W B   6     -31.506 -11.013  -1.845  1.00 19.75           C  
HETATM  124  CF  22W B   6     -33.586 -10.897  -1.790  1.00 20.19           C  
HETATM  125  O26 22W B   6     -33.968 -13.140  -1.028  1.00 20.52           O  
HETATM  126  C83 22W B   6     -33.227 -12.234  -1.354  1.00 19.97           C  
HETATM  127  CD1 22W B   6     -27.572  -7.893  -1.098  1.00 20.36           C  
HETATM  128  CG1 22W B   6     -28.089  -9.199  -1.661  1.00 20.16           C  
HETATM  129  CG2 22W B   6     -29.836  -9.561   0.092  1.00 19.75           C  
ATOM    130  N   GLY B   7     -35.931 -11.224  -1.623  1.00 19.80           N  
ATOM    131  CA  GLY B   7     -37.377 -10.987  -1.876  1.00 21.62           C  
ATOM    132  C   GLY B   7     -38.149 -12.288  -1.950  1.00 21.96           C  
ATOM    133  O   GLY B   7     -37.550 -13.364  -1.888  1.00 21.60           O  
ATOM    134  N   PRO B   8     -39.488 -12.197  -2.081  1.00 23.07           N  
ATOM    135  CA  PRO B   8     -40.365 -13.376  -2.140  1.00 23.79           C  
ATOM    136  C   PRO B   8     -40.040 -14.341  -3.284  1.00 24.76           C  
ATOM    137  O   PRO B   8     -40.103 -15.557  -3.095  1.00 24.84           O  
ATOM    138  CB  PRO B   8     -41.767 -12.767  -2.318  1.00 23.55           C  
ATOM    139  CG  PRO B   8     -41.533 -11.366  -2.791  1.00 22.96           C  
ATOM    140  CD  PRO B   8     -40.267 -10.945  -2.111  1.00 22.68           C  
ATOM    141  N   ASN B   9     -39.681 -13.807  -4.450  1.00 26.02           N  
ATOM    142  CA  ASN B   9     -39.396 -14.647  -5.614  1.00 26.93           C  
ATOM    143  C   ASN B   9     -37.981 -14.464  -6.179  1.00 26.64           C  
ATOM    144  O   ASN B   9     -37.777 -14.466  -7.392  1.00 27.17           O  
ATOM    145  CB  ASN B   9     -40.467 -14.454  -6.696  1.00 29.18           C  
ATOM    146  CG  ASN B   9     -40.506 -13.043  -7.245  1.00 31.31           C  
ATOM    147  OD1 ASN B   9     -40.058 -12.092  -6.601  1.00 33.53           O  
ATOM    148  ND2 ASN B   9     -41.047 -12.901  -8.449  1.00 32.83           N  
ATOM    149  N   CYS B  10     -37.012 -14.335  -5.280  1.00 26.05           N  
ATOM    150  CA  CYS B  10     -35.624 -14.057  -5.646  1.00 26.04           C  
ATOM    151  C   CYS B  10     -34.984 -15.180  -6.470  1.00 27.45           C  
ATOM    152  O   CYS B  10     -34.344 -14.935  -7.493  1.00 28.81           O  
ATOM    153  CB  CYS B  10     -34.799 -13.795  -4.392  1.00 24.50           C  
ATOM    154  SG  CYS B  10     -33.171 -13.108  -4.736  1.00 23.78           S  
ATOM    155  OXT CYS B  10     -35.090 -16.358  -6.133  1.00 28.88           O  
TER     156      CYS B  10                                                      
HETATM  157 CU   CU1 A 101     -25.467 -16.015   2.915  1.00 19.71          CU  
HETATM  158 CU   CU1 B 101     -33.082  -8.321  -2.839  1.00 19.83          CU  
HETATM  159  O   HOH A 201     -33.876 -23.493   1.363  1.00 27.22           O  
HETATM  160  O   HOH A 202     -24.355  -9.052   4.082  1.00 31.95           O  
HETATM  161  O   HOH A 203     -32.872 -20.050   1.274  1.00 39.95           O  
HETATM  162  O   HOH A 204     -28.731  -8.180   3.710  1.00 34.11           O  
HETATM  163  O   HOH A 205     -28.629 -14.958  17.158  1.00 37.59           O  
HETATM  164  O   HOH A 206     -30.090 -16.179  10.398  1.00 29.33           O  
HETATM  165  O   HOH A 207     -26.339  -7.127   2.313  1.00 33.57           O  
HETATM  166  O   HOH A 208     -27.926 -21.106   5.289  1.00 37.04           O  
HETATM  167  O   HOH A 209     -29.378 -15.095  20.164  1.00 41.85           O  
HETATM  168  O   HOH A 210     -27.185 -16.815  20.149  1.00 33.26           O  
HETATM  169  O   HOH B 201     -26.116  -7.088  -4.556  1.00 31.74           O  
HETATM  170  O   HOH B 202     -40.601 -17.054  -0.966  1.00 32.62           O  
HETATM  171  O   HOH B 203     -31.339  -5.688 -23.247  1.00 39.78           O  
HETATM  172  O   HOH B 204     -34.653 -18.737  -7.735  1.00 36.12           O  
HETATM  173  O   HOH B 205     -36.670 -16.107  -2.754  1.00 37.69           O  
HETATM  174  O   HOH B 206     -25.138 -10.743  -3.280  1.00 41.79           O  
HETATM  175  O   HOH B 207     -36.121  -7.734 -21.812  1.00 38.76           O  
HETATM  176  O   HOH B 208     -38.030 -18.230   0.128  1.00101.29           O  
HETATM  177  O   HOH B 209     -36.720 -19.710  -9.622  0.50 45.79           O  
HETATM  178  O   HOH B 210     -34.780  -8.762 -19.554  1.00 29.33           O  
HETATM  179  O   HOH B 211     -33.199 -11.046 -19.678  1.00 35.36           O  
HETATM  180  O   HOH B 212     -38.685 -10.355  -4.928  1.00 33.79           O  
HETATM  181  O   HOH B 213     -35.496  -9.068 -10.534  1.00 45.91           O  
HETATM  182  O   HOH B 214     -33.730  -2.422 -15.478  1.00 39.96           O  
HETATM  183  O   HOH B 215     -33.926 -12.108 -10.526  1.00 38.36           O  
CONECT    1    3   14   15                                                      
CONECT    2    4   14                                                           
CONECT    3    1                                                                
CONECT    4    2    9   10                                                      
CONECT    5    6   10                                                           
CONECT    6    5    7   14                                                      
CONECT    7    6                                                                
CONECT    8   10                                                                
CONECT    9    4   11                                                           
CONECT   10    4    5    8                                                      
CONECT   11    9   12   13                                                      
CONECT   12   11                                                                
CONECT   13   11                                                                
CONECT   14    1    2    6                                                      
CONECT   15    1                                                                
CONECT   31   76                                                                
CONECT   34   39                                                                
CONECT   38   41   46   52                                                      
CONECT   39   34   42                                                           
CONECT   40   45   48                                                           
CONECT   41   38  157                                                           
CONECT   42   39   43   45                                                      
CONECT   43   42   50   51                                                      
CONECT   44   45   46  157                                                      
CONECT   45   40   42   44                                                      
CONECT   46   38   44   48                                                      
CONECT   47   48                                                                
CONECT   48   40   46   47                                                      
CONECT   49   50                                                                
CONECT   50   43   49                                                           
CONECT   51   43                                                                
CONECT   52   38                                                                
CONECT   76   31                                                                
CONECT   79   81   92   93                                                      
CONECT   80   82   92                                                           
CONECT   81   79                                                                
CONECT   82   80   87   88                                                      
CONECT   83   84   88                                                           
CONECT   84   83   85   92                                                      
CONECT   85   84                                                                
CONECT   86   88                                                                
CONECT   87   82   89                                                           
CONECT   88   82   83   86                                                      
CONECT   89   87   90   91                                                      
CONECT   90   89                                                                
CONECT   91   89                                                                
CONECT   92   79   80   84                                                      
CONECT   93   79                                                                
CONECT  109  154                                                                
CONECT  112  117                                                                
CONECT  116  119  124  130                                                      
CONECT  117  112  120                                                           
CONECT  118  123  126                                                           
CONECT  119  116  158                                                           
CONECT  120  117  121  123                                                      
CONECT  121  120  128  129                                                      
CONECT  122  123  124  158                                                      
CONECT  123  118  120  122                                                      
CONECT  124  116  122  126                                                      
CONECT  125  126                                                                
CONECT  126  118  124  125                                                      
CONECT  127  128                                                                
CONECT  128  121  127                                                           
CONECT  129  121                                                                
CONECT  130  116                                                                
CONECT  154  109                                                                
CONECT  157   41   44                                                           
CONECT  158  119  122                                                           
MASTER      352    0    6    0    0    0   10    6  181    2   68    2          
END                                                                             
