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Database: PDB
Entry: 5OEX
LinkDB: 5OEX
Original site: 5OEX 
HEADER    OXIDOREDUCTASE                          10-JUL-17   5OEX              
TITLE     COMPLEX WITH IODINE ION FOR THIOCYANATE DEHYDROGENASE FROM            
TITLE    2 THIOALKALIVIBRIO PARADOXUS                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THIOCYANATE DEHYDROGENASE;                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THIOALKALIVIBRIO PARADOXUS ARH 1;               
SOURCE   3 ORGANISM_TAXID: 713585;                                              
SOURCE   4 GENE: THITH_13335;                                                   
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VARIANT: STAR                                      
KEYWDS    OXIDOREDUCTASE, THIOCYANATE DEHYDROGENASE, COPPER CENTERS             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.M.POLYAKOV,S.I.TSALLAGOV,T.V.TIKHONOVA,V.O.POPOV                    
REVDAT   2   03-OCT-18 5OEX    1       REMARK                                   
REVDAT   1   01-AUG-18 5OEX    0                                                
SPRSDE     01-AUG-18 5OEX      5F30                                             
JRNL        AUTH   T.V.TIKHONOVA,D.I.SOROKIN,S.I.TSALLAGOV,K.M.POLYAKOV,        
JRNL        AUTH 2 A.A.TROFIMOV,I.G.SHABALIN,M.G.KHRENOVA,G.MUYSER,             
JRNL        AUTH 3 T.V.RAKITINA,V.O.POPOV                                       
JRNL        TITL   DISCOVERY AND CHARACTERIZATION OF A NOVEL COPPER CONTAINING  
JRNL        TITL 2 ENZYME - THIOCYANATE DEHYDROGENASE.                          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 118078                         
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) : 0.158                           
REMARK   3   R VALUE            (WORKING SET) : 0.156                           
REMARK   3   FREE R VALUE                     : 0.198                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6102                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8827                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.39                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2610                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 403                          
REMARK   3   BIN FREE R VALUE                    : 0.3050                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14572                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 919                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.18                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.95000                                              
REMARK   3    B22 (A**2) : -1.02000                                             
REMARK   3    B33 (A**2) : 0.19000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.47000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.171         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.150         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.106         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.970         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15082 ; 0.019 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 20529 ; 2.018 ; 1.942       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1869 ; 7.322 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   671 ;35.275 ;24.456       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2358 ;14.593 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    70 ;18.746 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2225 ; 0.143 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11598 ; 0.012 ; 0.021       
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):  7474 ; 1.652 ; 1.937       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9337 ; 2.344 ; 2.895       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7608 ; 2.908 ; 2.171       
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): 24141 ; 5.367 ; 9.206       
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 : NULL                                                 
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: NULL                                      
REMARK   4                                                                      
REMARK   4 5OEX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-JUL-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200005626.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-DEC-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.900                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 124180                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.350                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 5F30                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 10 MG/ML PROTEIN, 25   
REMARK 280  MM BORATE BUFFER (PH 9.5). PRECIPITANT SOLUTION: 0.025 M            
REMARK 280  AMMONIUM IODIDE, 20.0 % W/V PEG 3350. VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 296K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       79.72500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -119.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7290 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -133.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH C   902     O    HOH C   935              1.89            
REMARK 500   O    HOH D   891     O    HOH D   909              1.91            
REMARK 500   O    HOH A   903     O    HOH A   904              1.96            
REMARK 500   N    ASP C   172     O    HOH C   701              2.01            
REMARK 500   O    HOH A   860     O    HOH A   906              2.02            
REMARK 500   O    HOH A   784     O    HOH A   870              2.04            
REMARK 500   OD2  ASP A    88     O    HOH A   702              2.10            
REMARK 500   O    HOH C   925     O    HOH C   937              2.13            
REMARK 500   O    HOH A   908     O    HOH A   917              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 294   CG    GLU A 294   CD      0.102                       
REMARK 500    GLU A 294   CD    GLU A 294   OE2     0.074                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 188   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    MET A 189   CG  -  SD  -  CE  ANGL. DEV. = -12.8 DEGREES          
REMARK 500    ASP A 214   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    LYS A 264   CD  -  CE  -  NZ  ANGL. DEV. = -16.0 DEGREES          
REMARK 500    ASP A 407   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP A 407   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG B 193   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG B 306   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP B 314   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG C 188   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG C 193   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG C 193   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP C 214   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP C 314   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG D 188   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ASP D 214   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP D 245   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP D 314   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP D 465   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP D 465   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 103     -118.40     54.49                                   
REMARK 500    HIS A 135      -87.02   -105.33                                   
REMARK 500    GLU A 148      153.97    178.37                                   
REMARK 500    THR A 187      -47.52   -134.77                                   
REMARK 500    VAL A 205     -133.37   -109.15                                   
REMARK 500    ASP A 276       57.69   -114.26                                   
REMARK 500    LYS A 323      -48.92     75.74                                   
REMARK 500    HIS A 381      -89.08   -141.97                                   
REMARK 500    LEU A 398      -89.68     76.26                                   
REMARK 500    LYS A 473      146.67   -172.58                                   
REMARK 500    LEU A 477      -41.41   -132.45                                   
REMARK 500    HIS A 482     -120.93   -119.61                                   
REMARK 500    ASN A 502       -6.75   -145.53                                   
REMARK 500    THR A 503     -152.91   -120.99                                   
REMARK 500    HIS A 527      123.63    -37.90                                   
REMARK 500    SER A 543     -156.12   -125.92                                   
REMARK 500    SER A 545      -60.61   -154.62                                   
REMARK 500    LYS B 103     -116.54     52.06                                   
REMARK 500    HIS B 135      -84.14   -109.64                                   
REMARK 500    THR B 187      -47.64   -131.32                                   
REMARK 500    VAL B 205     -125.04   -114.88                                   
REMARK 500    ASP B 234       18.93     54.64                                   
REMARK 500    ASP B 276       55.04   -110.76                                   
REMARK 500    LYS B 323      -51.08     70.61                                   
REMARK 500    ASP B 365     -169.36   -160.47                                   
REMARK 500    HIS B 381      -84.63   -146.41                                   
REMARK 500    LEU B 398      -77.23     76.68                                   
REMARK 500    ARG B 429      -78.37    -40.31                                   
REMARK 500    LEU B 477      -54.07   -123.17                                   
REMARK 500    HIS B 482     -128.56   -112.80                                   
REMARK 500    GLN B 501       -4.03     75.39                                   
REMARK 500    THR B 503     -147.90   -124.63                                   
REMARK 500    SER B 523       89.44   -159.89                                   
REMARK 500    HIS B 527      121.34    -30.84                                   
REMARK 500    SER B 543     -161.72   -125.73                                   
REMARK 500    SER B 545      -55.97   -148.98                                   
REMARK 500    LYS C 103     -117.78     55.30                                   
REMARK 500    HIS C 135      -87.96   -102.86                                   
REMARK 500    ASP C 172       66.03   -116.25                                   
REMARK 500    VAL C 205     -128.93   -111.19                                   
REMARK 500    LYS C 249       49.16    -90.40                                   
REMARK 500    ASP C 276       58.22   -111.39                                   
REMARK 500    LEU C 277       38.90   -140.77                                   
REMARK 500    LYS C 323      -49.31     73.72                                   
REMARK 500    ASP C 365     -167.44   -160.68                                   
REMARK 500    HIS C 381      -83.27   -145.94                                   
REMARK 500    LEU C 398      -74.35     67.81                                   
REMARK 500    LEU C 477      -50.53   -122.36                                   
REMARK 500    ASP C 480       66.64     62.04                                   
REMARK 500    HIS C 482     -120.39   -113.12                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      72 RAMACHANDRAN OUTLIERS.                        
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                              CU A 602  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS A 103   NZ                                                     
REMARK 620 2 HIS A 135   NE2  95.2                                              
REMARK 620 3 HIS A 528   ND1 104.4 138.3                                        
REMARK 620 4 HOH A 734   O    82.0 107.2 111.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 603  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 135   NE2                                                    
REMARK 620 2 HIS A 528   ND1 118.4                                              
REMARK 620 3 HOH A 734   O    93.7  96.7                                        
REMARK 620 4 HOH A 771   O    86.3 154.9  85.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 601  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 206   NE2                                                    
REMARK 620 2 ASP A 314   OD2 101.1                                              
REMARK 620 3 HIS A 381   NE2 177.0  80.4                                        
REMARK 620 4 HOH A 756   O    80.2 149.6  97.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 604  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 437   NE2                                                    
REMARK 620 2 HIS A 482   ND1 122.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 602  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS B 103   NZ                                                     
REMARK 620 2 HIS B 135   NE2  91.9                                              
REMARK 620 3 HIS B 528   ND1  92.0 152.6                                        
REMARK 620 4 HOH B 819   O    86.2  97.5 109.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 603  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 135   NE2                                                    
REMARK 620 2 HIS B 528   ND1 107.9                                              
REMARK 620 3 HOH B 819   O    93.4  98.8                                        
REMARK 620 4 HOH B 831   O    91.4 160.6  81.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 601  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 206   NE2                                                    
REMARK 620 2 ASP B 314   OD1 103.3                                              
REMARK 620 3 ASP B 314   OD2  92.3  52.4                                        
REMARK 620 4 HIS B 381   NE2 176.2  79.6  91.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 603  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS C 103   NZ                                                     
REMARK 620 2 HIS C 135   NE2  97.7                                              
REMARK 620 3 HIS C 528   ND1 100.7 146.3                                        
REMARK 620 4 HOH C 839   O    83.8  98.8 111.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 602  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 135   NE2                                                    
REMARK 620 2 HIS C 528   ND1 121.0                                              
REMARK 620 3 HOH C 839   O    90.0 102.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 601  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 206   NE2                                                    
REMARK 620 2 ASP C 314   OD1  93.8                                              
REMARK 620 3 ASP C 314   OD2  96.8  53.2                                        
REMARK 620 4 HIS C 381   NE2 172.1  90.7  80.7                                  
REMARK 620 5 HOH C 800   O    84.7 142.2  89.4  87.8                            
REMARK 620 6 HOH C 919   O    87.8 125.6 175.2  94.9  92.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 604  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 437   NE2                                                    
REMARK 620 2 HIS C 482   ND1 132.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 603  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 135   NE2                                                    
REMARK 620 2 HIS D 528   ND1 144.0                                              
REMARK 620 3 HOH D 711   O    95.9 120.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 604  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 135   NE2                                                    
REMARK 620 2 HIS D 528   ND1 103.3                                              
REMARK 620 3 HOH D 711   O    83.2  96.0                                        
REMARK 620 4 HOH D 742   O    88.6 165.0  94.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 601  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 206   NE2                                                    
REMARK 620 2 ASP D 314   OD2  89.8                                              
REMARK 620 3 HIS D 381   NE2 176.6  86.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 602  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 437   NE2                                                    
REMARK 620 2 HIS D 482   ND1 133.5                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU A 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU A 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue P4G A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU B 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU B 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU C 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU C 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU C 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU C 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD C 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD C 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU D 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU D 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU D 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU D 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD D 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD D 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD D 607                 
DBREF  5OEX A   82   548  UNP    W0DP94   W0DP94_9GAMM    82    548             
DBREF  5OEX B   82   548  UNP    W0DP94   W0DP94_9GAMM    82    548             
DBREF  5OEX C   82   548  UNP    W0DP94   W0DP94_9GAMM    82    548             
DBREF  5OEX D   82   548  UNP    W0DP94   W0DP94_9GAMM    82    548             
SEQRES   1 A  467  LYS TYR VAL LYS VAL GLN ASP PHE TYR ASP GLN LEU GLY          
SEQRES   2 A  467  LYS TYR VAL LEU VAL ALA PRO GLY LYS PHE SER GLY THR          
SEQRES   3 A  467  VAL ALA ALA THR ASP LEU SER THR GLY TRP THR MET ALA          
SEQRES   4 A  467  TRP LEU ALA ALA TRP ASN TYR GLY ASP THR CYS PRO ILE          
SEQRES   5 A  467  MET HIS HIS MET ALA ALA PHE PRO SER PRO ASP PRO TYR          
SEQRES   6 A  467  LYS GLU PHE GLU PHE VAL VAL ASN THR GLN GLY GLY LYS          
SEQRES   7 A  467  ASN LEU PHE ILE TYR GLY VAL PRO VAL THR VAL GLU ASP          
SEQRES   8 A  467  PRO GLY GLU GLY MET LYS ILE TYR ARG ILE LYS TYR ASP          
SEQRES   9 A  467  GLY THR ARG MET ASN LEU GLN ARG ASP ALA ALA GLU VAL          
SEQRES  10 A  467  SER GLY LEU GLY LEU GLY VAL HIS VAL THR ILE THR PRO          
SEQRES  11 A  467  GLU ALA ASP GLY TYR ALA VAL GLY ASP GLY GLN LYS ASP          
SEQRES  12 A  467  ILE CYS ALA GLU PHE ASP ARG GLU THR ASP MET VAL ARG          
SEQRES  13 A  467  TYR ALA TRP ALA PHE ASP TRP ASP PRO ASN VAL LYS ASP          
SEQRES  14 A  467  LEU LYS ARG ALA TRP LEU ASP GLY GLY THR MET THR ILE          
SEQRES  15 A  467  LYS ARG LEU LYS PRO THR LEU PRO GLY GLY ARG TYR ASP          
SEQRES  16 A  467  LEU GLN GLY SER LYS GLY ASN LYS ILE ASP TRP GLU LEU          
SEQRES  17 A  467  VAL PRO GLY GLY GLU LEU ALA ILE GLU ASP GLY LYS VAL          
SEQRES  18 A  467  SER GLY ASP ARG PRO LEU HIS SER VAL ALA ASN ASP ALA          
SEQRES  19 A  467  LEU VAL PHE ASP PRO ARG GLY LYS TRP ALA VAL ALA SER          
SEQRES  20 A  467  MET ARG LEU PRO GLY VAL CYS VAL VAL PHE ASP ARG GLU          
SEQRES  21 A  467  ASN GLN VAL PRO VAL ALA VAL LEU ALA GLY PRO LYS GLY          
SEQRES  22 A  467  THR PRO SER GLN PHE GLN LEU VAL LYS VAL ASP ASP ASP          
SEQRES  23 A  467  THR TRP THR VAL ASP ILE PRO GLU VAL ILE SER ALA GLY          
SEQRES  24 A  467  HIS GLN ALA GLY PHE SER PRO ASP GLY GLN SER PHE LEU          
SEQRES  25 A  467  PHE MET ASN SER LEU ARG GLN ASN ASN ILE MET VAL TRP          
SEQRES  26 A  467  ASP SER SER ASN HIS ASP ASP PRO THR THR TRP GLU LYS          
SEQRES  27 A  467  LYS ALA VAL VAL GLU SER PRO ASP TRP ARG GLY ALA TYR          
SEQRES  28 A  467  PRO ASN THR PHE HIS MET VAL PHE THR PRO ASP ALA LYS          
SEQRES  29 A  467  LYS ILE TYR VAL THR MET TRP TRP PRO SER PRO THR PRO          
SEQRES  30 A  467  ASN GLY ILE ALA VAL ILE ASP ALA VAL ASN TRP GLU VAL          
SEQRES  31 A  467  LEU LYS GLU VAL ASP LEU GLY PRO ASP MET HIS THR LEU          
SEQRES  32 A  467  ALA ILE THR TYR ASP GLY LYS PHE VAL VAL GLY THR LEU          
SEQRES  33 A  467  SER GLY TYR GLN ASN THR ALA SER ALA ILE VAL VAL MET          
SEQRES  34 A  467  GLU THR GLU THR ASP GLU VAL LEU GLY PHE LEU PRO SER          
SEQRES  35 A  467  PRO MET GLY HIS HIS ASP ASN VAL ILE VAL PRO ARG THR          
SEQRES  36 A  467  LEU GLU ASP LEU ARG ILE SER ARG SER THR THR THR              
SEQRES   1 B  467  LYS TYR VAL LYS VAL GLN ASP PHE TYR ASP GLN LEU GLY          
SEQRES   2 B  467  LYS TYR VAL LEU VAL ALA PRO GLY LYS PHE SER GLY THR          
SEQRES   3 B  467  VAL ALA ALA THR ASP LEU SER THR GLY TRP THR MET ALA          
SEQRES   4 B  467  TRP LEU ALA ALA TRP ASN TYR GLY ASP THR CYS PRO ILE          
SEQRES   5 B  467  MET HIS HIS MET ALA ALA PHE PRO SER PRO ASP PRO TYR          
SEQRES   6 B  467  LYS GLU PHE GLU PHE VAL VAL ASN THR GLN GLY GLY LYS          
SEQRES   7 B  467  ASN LEU PHE ILE TYR GLY VAL PRO VAL THR VAL GLU ASP          
SEQRES   8 B  467  PRO GLY GLU GLY MET LYS ILE TYR ARG ILE LYS TYR ASP          
SEQRES   9 B  467  GLY THR ARG MET ASN LEU GLN ARG ASP ALA ALA GLU VAL          
SEQRES  10 B  467  SER GLY LEU GLY LEU GLY VAL HIS VAL THR ILE THR PRO          
SEQRES  11 B  467  GLU ALA ASP GLY TYR ALA VAL GLY ASP GLY GLN LYS ASP          
SEQRES  12 B  467  ILE CYS ALA GLU PHE ASP ARG GLU THR ASP MET VAL ARG          
SEQRES  13 B  467  TYR ALA TRP ALA PHE ASP TRP ASP PRO ASN VAL LYS ASP          
SEQRES  14 B  467  LEU LYS ARG ALA TRP LEU ASP GLY GLY THR MET THR ILE          
SEQRES  15 B  467  LYS ARG LEU LYS PRO THR LEU PRO GLY GLY ARG TYR ASP          
SEQRES  16 B  467  LEU GLN GLY SER LYS GLY ASN LYS ILE ASP TRP GLU LEU          
SEQRES  17 B  467  VAL PRO GLY GLY GLU LEU ALA ILE GLU ASP GLY LYS VAL          
SEQRES  18 B  467  SER GLY ASP ARG PRO LEU HIS SER VAL ALA ASN ASP ALA          
SEQRES  19 B  467  LEU VAL PHE ASP PRO ARG GLY LYS TRP ALA VAL ALA SER          
SEQRES  20 B  467  MET ARG LEU PRO GLY VAL CYS VAL VAL PHE ASP ARG GLU          
SEQRES  21 B  467  ASN GLN VAL PRO VAL ALA VAL LEU ALA GLY PRO LYS GLY          
SEQRES  22 B  467  THR PRO SER GLN PHE GLN LEU VAL LYS VAL ASP ASP ASP          
SEQRES  23 B  467  THR TRP THR VAL ASP ILE PRO GLU VAL ILE SER ALA GLY          
SEQRES  24 B  467  HIS GLN ALA GLY PHE SER PRO ASP GLY GLN SER PHE LEU          
SEQRES  25 B  467  PHE MET ASN SER LEU ARG GLN ASN ASN ILE MET VAL TRP          
SEQRES  26 B  467  ASP SER SER ASN HIS ASP ASP PRO THR THR TRP GLU LYS          
SEQRES  27 B  467  LYS ALA VAL VAL GLU SER PRO ASP TRP ARG GLY ALA TYR          
SEQRES  28 B  467  PRO ASN THR PHE HIS MET VAL PHE THR PRO ASP ALA LYS          
SEQRES  29 B  467  LYS ILE TYR VAL THR MET TRP TRP PRO SER PRO THR PRO          
SEQRES  30 B  467  ASN GLY ILE ALA VAL ILE ASP ALA VAL ASN TRP GLU VAL          
SEQRES  31 B  467  LEU LYS GLU VAL ASP LEU GLY PRO ASP MET HIS THR LEU          
SEQRES  32 B  467  ALA ILE THR TYR ASP GLY LYS PHE VAL VAL GLY THR LEU          
SEQRES  33 B  467  SER GLY TYR GLN ASN THR ALA SER ALA ILE VAL VAL MET          
SEQRES  34 B  467  GLU THR GLU THR ASP GLU VAL LEU GLY PHE LEU PRO SER          
SEQRES  35 B  467  PRO MET GLY HIS HIS ASP ASN VAL ILE VAL PRO ARG THR          
SEQRES  36 B  467  LEU GLU ASP LEU ARG ILE SER ARG SER THR THR THR              
SEQRES   1 C  467  LYS TYR VAL LYS VAL GLN ASP PHE TYR ASP GLN LEU GLY          
SEQRES   2 C  467  LYS TYR VAL LEU VAL ALA PRO GLY LYS PHE SER GLY THR          
SEQRES   3 C  467  VAL ALA ALA THR ASP LEU SER THR GLY TRP THR MET ALA          
SEQRES   4 C  467  TRP LEU ALA ALA TRP ASN TYR GLY ASP THR CYS PRO ILE          
SEQRES   5 C  467  MET HIS HIS MET ALA ALA PHE PRO SER PRO ASP PRO TYR          
SEQRES   6 C  467  LYS GLU PHE GLU PHE VAL VAL ASN THR GLN GLY GLY LYS          
SEQRES   7 C  467  ASN LEU PHE ILE TYR GLY VAL PRO VAL THR VAL GLU ASP          
SEQRES   8 C  467  PRO GLY GLU GLY MET LYS ILE TYR ARG ILE LYS TYR ASP          
SEQRES   9 C  467  GLY THR ARG MET ASN LEU GLN ARG ASP ALA ALA GLU VAL          
SEQRES  10 C  467  SER GLY LEU GLY LEU GLY VAL HIS VAL THR ILE THR PRO          
SEQRES  11 C  467  GLU ALA ASP GLY TYR ALA VAL GLY ASP GLY GLN LYS ASP          
SEQRES  12 C  467  ILE CYS ALA GLU PHE ASP ARG GLU THR ASP MET VAL ARG          
SEQRES  13 C  467  TYR ALA TRP ALA PHE ASP TRP ASP PRO ASN VAL LYS ASP          
SEQRES  14 C  467  LEU LYS ARG ALA TRP LEU ASP GLY GLY THR MET THR ILE          
SEQRES  15 C  467  LYS ARG LEU LYS PRO THR LEU PRO GLY GLY ARG TYR ASP          
SEQRES  16 C  467  LEU GLN GLY SER LYS GLY ASN LYS ILE ASP TRP GLU LEU          
SEQRES  17 C  467  VAL PRO GLY GLY GLU LEU ALA ILE GLU ASP GLY LYS VAL          
SEQRES  18 C  467  SER GLY ASP ARG PRO LEU HIS SER VAL ALA ASN ASP ALA          
SEQRES  19 C  467  LEU VAL PHE ASP PRO ARG GLY LYS TRP ALA VAL ALA SER          
SEQRES  20 C  467  MET ARG LEU PRO GLY VAL CYS VAL VAL PHE ASP ARG GLU          
SEQRES  21 C  467  ASN GLN VAL PRO VAL ALA VAL LEU ALA GLY PRO LYS GLY          
SEQRES  22 C  467  THR PRO SER GLN PHE GLN LEU VAL LYS VAL ASP ASP ASP          
SEQRES  23 C  467  THR TRP THR VAL ASP ILE PRO GLU VAL ILE SER ALA GLY          
SEQRES  24 C  467  HIS GLN ALA GLY PHE SER PRO ASP GLY GLN SER PHE LEU          
SEQRES  25 C  467  PHE MET ASN SER LEU ARG GLN ASN ASN ILE MET VAL TRP          
SEQRES  26 C  467  ASP SER SER ASN HIS ASP ASP PRO THR THR TRP GLU LYS          
SEQRES  27 C  467  LYS ALA VAL VAL GLU SER PRO ASP TRP ARG GLY ALA TYR          
SEQRES  28 C  467  PRO ASN THR PHE HIS MET VAL PHE THR PRO ASP ALA LYS          
SEQRES  29 C  467  LYS ILE TYR VAL THR MET TRP TRP PRO SER PRO THR PRO          
SEQRES  30 C  467  ASN GLY ILE ALA VAL ILE ASP ALA VAL ASN TRP GLU VAL          
SEQRES  31 C  467  LEU LYS GLU VAL ASP LEU GLY PRO ASP MET HIS THR LEU          
SEQRES  32 C  467  ALA ILE THR TYR ASP GLY LYS PHE VAL VAL GLY THR LEU          
SEQRES  33 C  467  SER GLY TYR GLN ASN THR ALA SER ALA ILE VAL VAL MET          
SEQRES  34 C  467  GLU THR GLU THR ASP GLU VAL LEU GLY PHE LEU PRO SER          
SEQRES  35 C  467  PRO MET GLY HIS HIS ASP ASN VAL ILE VAL PRO ARG THR          
SEQRES  36 C  467  LEU GLU ASP LEU ARG ILE SER ARG SER THR THR THR              
SEQRES   1 D  467  LYS TYR VAL LYS VAL GLN ASP PHE TYR ASP GLN LEU GLY          
SEQRES   2 D  467  LYS TYR VAL LEU VAL ALA PRO GLY LYS PHE SER GLY THR          
SEQRES   3 D  467  VAL ALA ALA THR ASP LEU SER THR GLY TRP THR MET ALA          
SEQRES   4 D  467  TRP LEU ALA ALA TRP ASN TYR GLY ASP THR CYS PRO ILE          
SEQRES   5 D  467  MET HIS HIS MET ALA ALA PHE PRO SER PRO ASP PRO TYR          
SEQRES   6 D  467  LYS GLU PHE GLU PHE VAL VAL ASN THR GLN GLY GLY LYS          
SEQRES   7 D  467  ASN LEU PHE ILE TYR GLY VAL PRO VAL THR VAL GLU ASP          
SEQRES   8 D  467  PRO GLY GLU GLY MET LYS ILE TYR ARG ILE LYS TYR ASP          
SEQRES   9 D  467  GLY THR ARG MET ASN LEU GLN ARG ASP ALA ALA GLU VAL          
SEQRES  10 D  467  SER GLY LEU GLY LEU GLY VAL HIS VAL THR ILE THR PRO          
SEQRES  11 D  467  GLU ALA ASP GLY TYR ALA VAL GLY ASP GLY GLN LYS ASP          
SEQRES  12 D  467  ILE CYS ALA GLU PHE ASP ARG GLU THR ASP MET VAL ARG          
SEQRES  13 D  467  TYR ALA TRP ALA PHE ASP TRP ASP PRO ASN VAL LYS ASP          
SEQRES  14 D  467  LEU LYS ARG ALA TRP LEU ASP GLY GLY THR MET THR ILE          
SEQRES  15 D  467  LYS ARG LEU LYS PRO THR LEU PRO GLY GLY ARG TYR ASP          
SEQRES  16 D  467  LEU GLN GLY SER LYS GLY ASN LYS ILE ASP TRP GLU LEU          
SEQRES  17 D  467  VAL PRO GLY GLY GLU LEU ALA ILE GLU ASP GLY LYS VAL          
SEQRES  18 D  467  SER GLY ASP ARG PRO LEU HIS SER VAL ALA ASN ASP ALA          
SEQRES  19 D  467  LEU VAL PHE ASP PRO ARG GLY LYS TRP ALA VAL ALA SER          
SEQRES  20 D  467  MET ARG LEU PRO GLY VAL CYS VAL VAL PHE ASP ARG GLU          
SEQRES  21 D  467  ASN GLN VAL PRO VAL ALA VAL LEU ALA GLY PRO LYS GLY          
SEQRES  22 D  467  THR PRO SER GLN PHE GLN LEU VAL LYS VAL ASP ASP ASP          
SEQRES  23 D  467  THR TRP THR VAL ASP ILE PRO GLU VAL ILE SER ALA GLY          
SEQRES  24 D  467  HIS GLN ALA GLY PHE SER PRO ASP GLY GLN SER PHE LEU          
SEQRES  25 D  467  PHE MET ASN SER LEU ARG GLN ASN ASN ILE MET VAL TRP          
SEQRES  26 D  467  ASP SER SER ASN HIS ASP ASP PRO THR THR TRP GLU LYS          
SEQRES  27 D  467  LYS ALA VAL VAL GLU SER PRO ASP TRP ARG GLY ALA TYR          
SEQRES  28 D  467  PRO ASN THR PHE HIS MET VAL PHE THR PRO ASP ALA LYS          
SEQRES  29 D  467  LYS ILE TYR VAL THR MET TRP TRP PRO SER PRO THR PRO          
SEQRES  30 D  467  ASN GLY ILE ALA VAL ILE ASP ALA VAL ASN TRP GLU VAL          
SEQRES  31 D  467  LEU LYS GLU VAL ASP LEU GLY PRO ASP MET HIS THR LEU          
SEQRES  32 D  467  ALA ILE THR TYR ASP GLY LYS PHE VAL VAL GLY THR LEU          
SEQRES  33 D  467  SER GLY TYR GLN ASN THR ALA SER ALA ILE VAL VAL MET          
SEQRES  34 D  467  GLU THR GLU THR ASP GLU VAL LEU GLY PHE LEU PRO SER          
SEQRES  35 D  467  PRO MET GLY HIS HIS ASP ASN VAL ILE VAL PRO ARG THR          
SEQRES  36 D  467  LEU GLU ASP LEU ARG ILE SER ARG SER THR THR THR              
HET     CU  A 601       1                                                       
HET     CU  A 602       1                                                       
HET     CU  A 603       1                                                       
HET     CU  A 604       1                                                       
HET    P4G  A 605      11                                                       
HET    IOD  A 606       1                                                       
HET    IOD  A 607       1                                                       
HET    IOD  A 608       1                                                       
HET     CU  B 601       1                                                       
HET     CU  B 602       1                                                       
HET     CU  B 603       1                                                       
HET    EDO  B 604       4                                                       
HET    EDO  B 605       4                                                       
HET    EDO  B 606       4                                                       
HET    GOL  B 607       6                                                       
HET     CU  C 601       1                                                       
HET     CU  C 602       1                                                       
HET     CU  C 603       1                                                       
HET     CU  C 604       1                                                       
HET    IOD  C 605       1                                                       
HET    IOD  C 606       1                                                       
HET     CU  D 601       1                                                       
HET     CU  D 602       1                                                       
HET     CU  D 603       1                                                       
HET     CU  D 604       1                                                       
HET    IOD  D 605       1                                                       
HET    IOD  D 606       1                                                       
HET    IOD  D 607       1                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM     P4G 1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE                                
HETNAM     IOD IODIDE ION                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     GOL GLYCEROL                                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5   CU    15(CU 2+)                                                    
FORMUL   9  P4G    C8 H18 O3                                                    
FORMUL  10  IOD    8(I 1-)                                                      
FORMUL  16  EDO    3(C2 H6 O2)                                                  
FORMUL  19  GOL    C3 H8 O3                                                     
FORMUL  33  HOH   *919(H2 O)                                                    
HELIX    1 AA1 LYS A   85  GLN A   92  1                                   8    
HELIX    2 AA2 LYS A  103  SER A  105  5                                   3    
HELIX    3 AA3 TRP A  125  GLY A  128  5                                   4    
HELIX    4 AA4 GLY A  158  ILE A  163  5                                   6    
HELIX    5 AA5 ALA A  195  GLY A  200  1                                   6    
HELIX    6 AA6 GLY A  292  ASP A  299  1                                   8    
HELIX    7 AA7 ARG A  306  SER A  310  5                                   5    
HELIX    8 AA8 ASP A  413  TRP A  417  5                                   5    
HELIX    9 AA9 SER A  425  ARG A  429  5                                   5    
HELIX   10 AB1 TYR A  500  ASN A  502  5                                   3    
HELIX   11 AB2 GLU A  538  SER A  543  5                                   6    
HELIX   12 AB3 LYS B   85  GLN B   92  1                                   8    
HELIX   13 AB4 LYS B  103  SER B  105  5                                   3    
HELIX   14 AB5 TRP B  125  GLY B  128  5                                   4    
HELIX   15 AB6 GLY B  158  ILE B  163  5                                   6    
HELIX   16 AB7 ALA B  195  GLY B  200  1                                   6    
HELIX   17 AB8 GLY B  292  ASP B  299  1                                   8    
HELIX   18 AB9 ARG B  306  SER B  310  5                                   5    
HELIX   19 AC1 ASP B  413  TRP B  417  5                                   5    
HELIX   20 AC2 TYR B  500  ASN B  502  5                                   3    
HELIX   21 AC3 GLU B  538  SER B  543  5                                   6    
HELIX   22 AC4 LYS C   85  GLY C   94  1                                  10    
HELIX   23 AC5 LYS C  103  SER C  105  5                                   3    
HELIX   24 AC6 TRP C  125  GLY C  128  5                                   4    
HELIX   25 AC7 GLY C  158  ILE C  163  5                                   6    
HELIX   26 AC8 ALA C  195  GLY C  200  1                                   6    
HELIX   27 AC9 LEU C  270  ARG C  274  5                                   5    
HELIX   28 AD1 GLY C  292  ASP C  299  1                                   8    
HELIX   29 AD2 ARG C  306  SER C  310  5                                   5    
HELIX   30 AD3 ASP C  413  TRP C  417  5                                   5    
HELIX   31 AD4 SER C  425  ARG C  429  5                                   5    
HELIX   32 AD5 TYR C  500  ASN C  502  5                                   3    
HELIX   33 AD6 THR C  536  ARG C  541  1                                   6    
HELIX   34 AD7 VAL D   86  GLN D   92  1                                   7    
HELIX   35 AD8 LYS D  103  SER D  105  5                                   3    
HELIX   36 AD9 TRP D  125  GLY D  128  5                                   4    
HELIX   37 AE1 GLY D  158  ILE D  163  5                                   6    
HELIX   38 AE2 ALA D  195  GLY D  200  1                                   6    
HELIX   39 AE3 LEU D  270  ARG D  274  5                                   5    
HELIX   40 AE4 GLY D  292  ASP D  299  1                                   8    
HELIX   41 AE5 ARG D  306  SER D  310  5                                   5    
HELIX   42 AE6 ASP D  413  TRP D  417  5                                   5    
HELIX   43 AE7 SER D  425  ARG D  429  5                                   5    
HELIX   44 AE8 TYR D  500  ASN D  502  5                                   3    
HELIX   45 AE9 GLU D  538  SER D  543  5                                   6    
SHEET    1 AA1 4 THR A 118  ALA A 123  0                                        
SHEET    2 AA1 4 THR A 107  ASP A 112 -1  N  ALA A 110   O  MET A 119           
SHEET    3 AA1 4 VAL A  97  PRO A 101 -1  N  LEU A  98   O  THR A 111           
SHEET    4 AA1 4 VAL A 531  ILE A 532 -1  O  VAL A 531   N  VAL A  99           
SHEET    1 AA2 4 ILE A 133  ALA A 139  0                                        
SHEET    2 AA2 4 PHE A 149  GLN A 156 -1  O  ASN A 154   N  HIS A 135           
SHEET    3 AA2 4 GLY A 176  TYR A 184 -1  O  ILE A 182   N  PHE A 151           
SHEET    4 AA2 4 MET A 189  ASP A 194 -1  O  GLN A 192   N  ARG A 181           
SHEET    1 AA3 7 VAL A 207  ILE A 209  0                                        
SHEET    2 AA3 7 GLY A 215  ASP A 220 -1  O  ALA A 217   N  THR A 208           
SHEET    3 AA3 7 ILE A 225  ASP A 230 -1  O  PHE A 229   N  TYR A 216           
SHEET    4 AA3 7 VAL A 236  PRO A 246 -1  O  ARG A 237   N  GLU A 228           
SHEET    5 AA3 7 GLY A 259  ARG A 265 -1  O  LYS A 264   N  ALA A 241           
SHEET    6 AA3 7 THR A 368  ILE A 373 -1  O  ILE A 373   N  GLY A 259           
SHEET    7 AA3 7 LEU A 361  ASP A 365 -1  N  VAL A 364   O  THR A 368           
SHEET    1 AA4 5 ASN A 313  PHE A 318  0                                        
SHEET    2 AA4 5 TRP A 324  MET A 329 -1  O  VAL A 326   N  VAL A 317           
SHEET    3 AA4 5 VAL A 334  ASP A 339 -1  O  PHE A 338   N  ALA A 325           
SHEET    4 AA4 5 VAL A 344  ALA A 350 -1  O  VAL A 346   N  VAL A 337           
SHEET    5 AA4 5 GLN A 358  PHE A 359 -1  O  PHE A 359   N  VAL A 348           
SHEET    1 AA5 4 GLY A 380  PHE A 385  0                                        
SHEET    2 AA5 4 SER A 391  ASN A 396 -1  O  LEU A 393   N  GLY A 384           
SHEET    3 AA5 4 ASN A 402  ASP A 407 -1  O  TRP A 406   N  PHE A 392           
SHEET    4 AA5 4 GLU A 418  VAL A 423 -1  O  LYS A 420   N  VAL A 405           
SHEET    1 AA6 4 MET A 438  PHE A 440  0                                        
SHEET    2 AA6 4 LYS A 446  MET A 451 -1  O  TYR A 448   N  VAL A 439           
SHEET    3 AA6 4 ASN A 459  ASP A 465 -1  O  ILE A 464   N  ILE A 447           
SHEET    4 AA6 4 GLU A 470  GLY A 478 -1  O  GLU A 470   N  ASP A 465           
SHEET    1 AA7 4 MET A 481  ILE A 486  0                                        
SHEET    2 AA7 4 PHE A 492  SER A 498 -1  O  THR A 496   N  HIS A 482           
SHEET    3 AA7 4 SER A 505  GLU A 511 -1  O  ALA A 506   N  LEU A 497           
SHEET    4 AA7 4 GLU A 516  PRO A 522 -1  O  LEU A 518   N  VAL A 509           
SHEET    1 AA8 4 THR B 118  ALA B 123  0                                        
SHEET    2 AA8 4 THR B 107  ASP B 112 -1  N  ALA B 110   O  ALA B 120           
SHEET    3 AA8 4 VAL B  97  PRO B 101 -1  N  LEU B  98   O  THR B 111           
SHEET    4 AA8 4 VAL B 531  ILE B 532 -1  O  VAL B 531   N  VAL B  99           
SHEET    1 AA9 4 ILE B 133  ALA B 139  0                                        
SHEET    2 AA9 4 PHE B 149  GLN B 156 -1  O  ASN B 154   N  HIS B 135           
SHEET    3 AA9 4 GLY B 176  TYR B 184 -1  O  TYR B 184   N  PHE B 149           
SHEET    4 AA9 4 MET B 189  ASP B 194 -1  O  GLN B 192   N  ARG B 181           
SHEET    1 AB1 7 VAL B 207  ILE B 209  0                                        
SHEET    2 AB1 7 GLY B 215  ASP B 220 -1  O  ALA B 217   N  THR B 208           
SHEET    3 AB1 7 ILE B 225  ASP B 230 -1  O  PHE B 229   N  TYR B 216           
SHEET    4 AB1 7 VAL B 236  PRO B 246 -1  O  ARG B 237   N  GLU B 228           
SHEET    5 AB1 7 GLY B 259  ARG B 265 -1  O  THR B 260   N  ASP B 245           
SHEET    6 AB1 7 THR B 368  ILE B 373 -1  O  ILE B 373   N  GLY B 259           
SHEET    7 AB1 7 LEU B 361  ASP B 365 -1  N  VAL B 362   O  THR B 370           
SHEET    1 AB2 5 ASN B 313  PHE B 318  0                                        
SHEET    2 AB2 5 TRP B 324  MET B 329 -1  O  VAL B 326   N  VAL B 317           
SHEET    3 AB2 5 VAL B 334  ASP B 339 -1  O  PHE B 338   N  ALA B 325           
SHEET    4 AB2 5 VAL B 344  ALA B 350 -1  O  VAL B 344   N  ASP B 339           
SHEET    5 AB2 5 GLN B 358  PHE B 359 -1  O  PHE B 359   N  VAL B 348           
SHEET    1 AB3 4 GLY B 380  PHE B 385  0                                        
SHEET    2 AB3 4 SER B 391  ASN B 396 -1  O  LEU B 393   N  GLY B 384           
SHEET    3 AB3 4 ASN B 402  ASP B 407 -1  O  MET B 404   N  PHE B 394           
SHEET    4 AB3 4 GLU B 418  VAL B 423 -1  O  GLU B 418   N  ASP B 407           
SHEET    1 AB4 4 MET B 438  PHE B 440  0                                        
SHEET    2 AB4 4 LYS B 446  MET B 451 -1  O  TYR B 448   N  VAL B 439           
SHEET    3 AB4 4 ASN B 459  ASP B 465 -1  O  ILE B 464   N  ILE B 447           
SHEET    4 AB4 4 GLU B 470  GLY B 478 -1  O  GLU B 470   N  ASP B 465           
SHEET    1 AB5 4 MET B 481  ILE B 486  0                                        
SHEET    2 AB5 4 PHE B 492  SER B 498 -1  O  VAL B 494   N  ALA B 485           
SHEET    3 AB5 4 SER B 505  GLU B 511 -1  O  ALA B 506   N  LEU B 497           
SHEET    4 AB5 4 GLU B 516  PRO B 522 -1  O  LEU B 518   N  VAL B 509           
SHEET    1 AB6 4 THR C 118  ALA C 123  0                                        
SHEET    2 AB6 4 THR C 107  ASP C 112 -1  N  ALA C 110   O  ALA C 120           
SHEET    3 AB6 4 VAL C  97  PRO C 101 -1  N  LEU C  98   O  THR C 111           
SHEET    4 AB6 4 VAL C 531  ILE C 532 -1  O  VAL C 531   N  VAL C  99           
SHEET    1 AB7 4 ILE C 133  ALA C 139  0                                        
SHEET    2 AB7 4 PHE C 149  GLN C 156 -1  O  ASN C 154   N  HIS C 135           
SHEET    3 AB7 4 GLY C 176  TYR C 184 -1  O  TYR C 184   N  PHE C 149           
SHEET    4 AB7 4 MET C 189  ASP C 194 -1  O  ARG C 193   N  ARG C 181           
SHEET    1 AB8 7 VAL C 207  ILE C 209  0                                        
SHEET    2 AB8 7 GLY C 215  ASP C 220 -1  O  ALA C 217   N  THR C 208           
SHEET    3 AB8 7 ILE C 225  ASP C 230 -1  O  PHE C 229   N  TYR C 216           
SHEET    4 AB8 7 VAL C 236  PRO C 246 -1  O  ARG C 237   N  GLU C 228           
SHEET    5 AB8 7 GLY C 259  ARG C 265 -1  O  LYS C 264   N  ALA C 241           
SHEET    6 AB8 7 THR C 368  ILE C 373 -1  O  ILE C 373   N  GLY C 259           
SHEET    7 AB8 7 VAL C 362  ASP C 365 -1  N  VAL C 364   O  THR C 368           
SHEET    1 AB9 5 ASN C 313  PHE C 318  0                                        
SHEET    2 AB9 5 TRP C 324  MET C 329 -1  O  VAL C 326   N  VAL C 317           
SHEET    3 AB9 5 VAL C 334  ASP C 339 -1  O  PHE C 338   N  ALA C 325           
SHEET    4 AB9 5 VAL C 344  ALA C 350 -1  O  VAL C 346   N  VAL C 337           
SHEET    5 AB9 5 GLN C 358  PHE C 359 -1  O  PHE C 359   N  VAL C 348           
SHEET    1 AC1 4 GLY C 380  PHE C 385  0                                        
SHEET    2 AC1 4 SER C 391  ASN C 396 -1  O  MET C 395   N  HIS C 381           
SHEET    3 AC1 4 ASN C 402  ASP C 407 -1  O  TRP C 406   N  PHE C 392           
SHEET    4 AC1 4 GLU C 418  VAL C 423 -1  O  GLU C 418   N  ASP C 407           
SHEET    1 AC2 4 MET C 438  PHE C 440  0                                        
SHEET    2 AC2 4 LYS C 446  MET C 451 -1  O  TYR C 448   N  VAL C 439           
SHEET    3 AC2 4 ASN C 459  ASP C 465 -1  O  ALA C 462   N  VAL C 449           
SHEET    4 AC2 4 GLU C 470  GLY C 478 -1  O  LEU C 472   N  VAL C 463           
SHEET    1 AC3 4 MET C 481  ILE C 486  0                                        
SHEET    2 AC3 4 PHE C 492  SER C 498 -1  O  THR C 496   N  HIS C 482           
SHEET    3 AC3 4 SER C 505  GLU C 511 -1  O  MET C 510   N  VAL C 493           
SHEET    4 AC3 4 GLU C 516  PRO C 522 -1  O  LEU C 521   N  ILE C 507           
SHEET    1 AC4 4 THR D 118  ALA D 123  0                                        
SHEET    2 AC4 4 THR D 107  ASP D 112 -1  N  ALA D 110   O  ALA D 120           
SHEET    3 AC4 4 VAL D  97  PRO D 101 -1  N  LEU D  98   O  THR D 111           
SHEET    4 AC4 4 VAL D 531  ILE D 532 -1  O  VAL D 531   N  VAL D  99           
SHEET    1 AC5 4 ILE D 133  ALA D 139  0                                        
SHEET    2 AC5 4 PHE D 149  GLN D 156 -1  O  ASN D 154   N  HIS D 135           
SHEET    3 AC5 4 GLY D 176  TYR D 184 -1  O  TYR D 184   N  PHE D 149           
SHEET    4 AC5 4 MET D 189  ASP D 194 -1  O  ASN D 190   N  LYS D 183           
SHEET    1 AC6 7 VAL D 207  ILE D 209  0                                        
SHEET    2 AC6 7 GLY D 215  ASP D 220 -1  O  ALA D 217   N  THR D 208           
SHEET    3 AC6 7 ILE D 225  ASP D 230 -1  O  PHE D 229   N  TYR D 216           
SHEET    4 AC6 7 VAL D 236  PRO D 246 -1  O  ARG D 237   N  GLU D 228           
SHEET    5 AC6 7 GLY D 259  LEU D 266 -1  O  LYS D 264   N  ALA D 241           
SHEET    6 AC6 7 THR D 368  ILE D 373 -1  O  ILE D 373   N  GLY D 259           
SHEET    7 AC6 7 LEU D 361  ASP D 365 -1  N  VAL D 362   O  THR D 370           
SHEET    1 AC7 5 ASN D 313  PHE D 318  0                                        
SHEET    2 AC7 5 TRP D 324  MET D 329 -1  O  VAL D 326   N  VAL D 317           
SHEET    3 AC7 5 VAL D 334  ASP D 339 -1  O  PHE D 338   N  ALA D 325           
SHEET    4 AC7 5 VAL D 344  ALA D 350 -1  O  VAL D 344   N  ASP D 339           
SHEET    5 AC7 5 GLN D 358  PHE D 359 -1  O  PHE D 359   N  VAL D 348           
SHEET    1 AC8 4 GLY D 380  PHE D 385  0                                        
SHEET    2 AC8 4 SER D 391  ASN D 396 -1  O  LEU D 393   N  GLY D 384           
SHEET    3 AC8 4 ASN D 402  ASP D 407 -1  O  TRP D 406   N  PHE D 392           
SHEET    4 AC8 4 GLU D 418  VAL D 423 -1  O  GLU D 418   N  ASP D 407           
SHEET    1 AC9 4 MET D 438  PHE D 440  0                                        
SHEET    2 AC9 4 LYS D 446  MET D 451 -1  O  TYR D 448   N  VAL D 439           
SHEET    3 AC9 4 ASN D 459  ASP D 465 -1  O  ILE D 464   N  ILE D 447           
SHEET    4 AC9 4 GLU D 470  GLY D 478 -1  O  GLU D 470   N  ASP D 465           
SHEET    1 AD1 4 MET D 481  ILE D 486  0                                        
SHEET    2 AD1 4 PHE D 492  SER D 498 -1  O  VAL D 494   N  ALA D 485           
SHEET    3 AD1 4 SER D 505  GLU D 511 -1  O  MET D 510   N  VAL D 493           
SHEET    4 AD1 4 GLU D 516  PRO D 522 -1  O  LEU D 518   N  VAL D 509           
LINK         NZ  LYS A 103                CU    CU A 602     1555   1555  2.68  
LINK         NE2 HIS A 135                CU    CU A 602     1555   1555  1.98  
LINK         NE2 HIS A 135                CU    CU A 603     1555   1555  2.15  
LINK         NE2 HIS A 206                CU    CU A 601     1555   1555  2.04  
LINK         OD2 ASP A 314                CU    CU A 601     1555   1555  2.06  
LINK         NE2 HIS A 381                CU    CU A 601     1555   1555  2.05  
LINK         NE2 HIS A 437                CU    CU A 604     1555   1555  2.18  
LINK         ND1 HIS A 482                CU    CU A 604     1555   1555  2.17  
LINK         ND1 HIS A 528                CU    CU A 602     1555   1555  1.97  
LINK         ND1 HIS A 528                CU    CU A 603     1555   1555  2.15  
LINK         NZ  LYS B 103                CU    CU B 602     1555   1555  2.69  
LINK         NE2 HIS B 135                CU    CU B 602     1555   1555  2.00  
LINK         NE2 HIS B 135                CU    CU B 603     1555   1555  2.30  
LINK         NE2 HIS B 206                CU    CU B 601     1555   1555  2.04  
LINK         OD1 ASP B 314                CU    CU B 601     1555   1555  2.62  
LINK         OD2 ASP B 314                CU    CU B 601     1555   1555  2.07  
LINK         NE2 HIS B 381                CU    CU B 601     1555   1555  2.09  
LINK         ND1 HIS B 528                CU    CU B 602     1555   1555  1.86  
LINK         ND1 HIS B 528                CU    CU B 603     1555   1555  2.34  
LINK         NZ  LYS C 103                CU    CU C 603     1555   1555  2.60  
LINK         NE2 HIS C 135                CU    CU C 602     1555   1555  2.19  
LINK         NE2 HIS C 135                CU    CU C 603     1555   1555  1.97  
LINK         NE2 HIS C 206                CU    CU C 601     1555   1555  2.04  
LINK         OD1 ASP C 314                CU    CU C 601     1555   1555  2.62  
LINK         OD2 ASP C 314                CU    CU C 601     1555   1555  2.09  
LINK         NE2 HIS C 381                CU    CU C 601     1555   1555  2.06  
LINK         NE2 HIS C 437                CU    CU C 604     1555   1555  2.16  
LINK         ND1 HIS C 482                CU    CU C 604     1555   1555  2.15  
LINK         ND1 HIS C 528                CU    CU C 602     1555   1555  2.17  
LINK         ND1 HIS C 528                CU    CU C 603     1555   1555  2.00  
LINK         NE2 HIS D 135                CU    CU D 603     1555   1555  2.00  
LINK         NE2 HIS D 135                CU    CU D 604     1555   1555  2.32  
LINK         NE2 HIS D 206                CU    CU D 601     1555   1555  2.04  
LINK         OD2 ASP D 314                CU    CU D 601     1555   1555  2.06  
LINK         NE2 HIS D 381                CU    CU D 601     1555   1555  2.05  
LINK         NE2 HIS D 437                CU    CU D 602     1555   1555  2.17  
LINK         ND1 HIS D 482                CU    CU D 602     1555   1555  2.15  
LINK         ND1 HIS D 528                CU    CU D 603     1555   1555  1.83  
LINK         ND1 HIS D 528                CU    CU D 604     1555   1555  2.32  
LINK        CU    CU A 601                 O   HOH A 756     1555   1555  2.12  
LINK        CU    CU A 602                 O   HOH A 734     1555   1555  2.20  
LINK        CU    CU A 603                 O   HOH A 734     1555   1555  2.46  
LINK        CU    CU A 603                 O   HOH A 771     1555   1555  2.54  
LINK        CU    CU B 602                 O   HOH B 819     1555   1555  2.26  
LINK        CU    CU B 603                 O   HOH B 819     1555   1555  2.10  
LINK        CU    CU B 603                 O   HOH B 831     1555   1555  2.43  
LINK        CU    CU C 601                 O   HOH C 800     1555   1555  2.52  
LINK        CU    CU C 601                 O   HOH C 919     1555   1555  2.60  
LINK        CU    CU C 602                 O   HOH C 839     1555   1555  2.38  
LINK        CU    CU C 603                 O   HOH C 839     1555   1555  2.28  
LINK        CU    CU D 603                 O   HOH D 711     1555   1555  2.25  
LINK        CU    CU D 604                 O   HOH D 711     1555   1555  2.44  
LINK        CU    CU D 604                 O   HOH D 742     1555   1555  2.31  
CISPEP   1 TYR A  432    PRO A  433          0         6.23                     
CISPEP   2 SER A  455    PRO A  456          0        13.47                     
CISPEP   3 TYR B  432    PRO B  433          0         6.01                     
CISPEP   4 SER B  455    PRO B  456          0         1.95                     
CISPEP   5 TYR C  432    PRO C  433          0        12.76                     
CISPEP   6 SER C  455    PRO C  456          0         9.62                     
CISPEP   7 TYR D  432    PRO D  433          0        12.99                     
CISPEP   8 SER D  455    PRO D  456          0         4.07                     
SITE     1 AC1  5 HIS A 206  ASP A 314  HIS A 381  HOH A 756                    
SITE     2 AC1  5 HOH A 902                                                     
SITE     1 AC2  5 LYS A 103  HIS A 135  HIS A 528   CU A 603                    
SITE     2 AC2  5 HOH A 734                                                     
SITE     1 AC3  7 HIS A 135  HIS A 136  HIS A 528   CU A 602                    
SITE     2 AC3  7 IOD A 608  HOH A 734  HOH A 771                               
SITE     1 AC4  5 HIS A 437  HIS A 482  HIS A 528  IOD A 608                    
SITE     2 AC4  5 HOH A 901                                                     
SITE     1 AC5  6 ASP A 214  ARG A 237  HOH A 782  ARG C 253                    
SITE     2 AC5  6 LEU C 256  GLU C 375                                          
SITE     1 AC6  3 ARG A 274  GLN A 278  GLN C 278                               
SITE     1 AC7  3 TRP A 287  VAL A 290  ALA A 296                               
SITE     1 AC8  6 HIS A 528   CU A 603   CU A 604  HOH A 771                    
SITE     2 AC8  6 HOH A 901  HOH A 902                                          
SITE     1 AC9  3 HIS B 206  ASP B 314  HIS B 381                               
SITE     1 AD1  5 LYS B 103  HIS B 135  HIS B 528   CU B 603                    
SITE     2 AD1  5 HOH B 819                                                     
SITE     1 AD2  6 HIS B 135  HIS B 136  HIS B 528   CU B 602                    
SITE     2 AD2  6 HOH B 819  HOH B 831                                          
SITE     1 AD3  4 LYS B  95  ASP B 112  SER B 114  TYR B 146                    
SITE     1 AD4  4 TRP B 287  VAL B 290  GLY B 293  ALA B 296                    
SITE     1 AD5  5 PRO B 141  GLU B 148  GLU B 150  ARG B 231                    
SITE     2 AD5  5 HOH B 814                                                     
SITE     1 AD6  9 MET B 451  TRP B 453  PRO B 458  ASN B 459                    
SITE     2 AD6  9 GLY B 460  GLU B 474  ASP B 476  HOH B 739                    
SITE     3 AD6  9 HOH B 822                                                     
SITE     1 AD7  5 HIS C 206  ASP C 314  HIS C 381  HOH C 800                    
SITE     2 AD7  5 HOH C 919                                                     
SITE     1 AD8  8 LYS C 103  HIS C 135  HIS C 136  HIS C 528                    
SITE     2 AD8  8  CU C 603  IOD C 606  HOH C 785  HOH C 839                    
SITE     1 AD9  5 LYS C 103  HIS C 135  HIS C 528   CU C 602                    
SITE     2 AD9  5 HOH C 839                                                     
SITE     1 AE1  4 HIS C 437  HIS C 482  HIS C 528  IOD C 606                    
SITE     1 AE2  2 TRP C 287  VAL C 290                                          
SITE     1 AE3  7 HIS C 437  HIS C 528   CU C 602   CU C 604                    
SITE     2 AE3  7 HOH C 785  HOH C 919  HOH C 931                               
SITE     1 AE4  4 HIS D 206  ASP D 314  HIS D 381  HOH D 904                    
SITE     1 AE5  5 HIS D 437  HIS D 482  HIS D 528  IOD D 607                    
SITE     2 AE5  5 HOH D 889                                                     
SITE     1 AE6  6 LYS D 103  HIS D 135  HIS D 528   CU D 604                    
SITE     2 AE6  6 IOD D 607  HOH D 711                                          
SITE     1 AE7  7 HIS D 135  HIS D 136  HIS D 528   CU D 603                    
SITE     2 AE7  7 IOD D 607  HOH D 711  HOH D 742                               
SITE     1 AE8  3 TRP D 287  VAL D 290  GLY D 293                               
SITE     1 AE9  1 HOH D 906                                                     
SITE     1 AF1  8 HIS D 437  HIS D 528   CU D 602   CU D 603                    
SITE     2 AF1  8  CU D 604  HOH D 742  HOH D 889  HOH D 904                    
CRYST1   69.820  159.450   91.000  90.00  97.77  90.00 P 1 21 1      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      0.014323  0.000000  0.001953        0.00000                         
SCALE2      0.000000  0.006272  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011091        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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