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Database: PDB
Entry: 5YUL
LinkDB: 5YUL
Original site: 5YUL 
HEADER    OXIDOREDUCTASE                          22-NOV-17   5YUL              
TITLE     NATIVE STRUCTURE OF HSOD1 IN P6322 SPACE GROUP                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, H, B, C, D, E, F, G, I, J;                                 
COMPND   4 SYNONYM: SUPEROXIDE DISMUTASE 1,HSOD1;                               
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SOD1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PETM11                                    
KEYWDS    DIMER, NATIVE, OXIDOREDUCTASE, DISMUTASE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.MANJULA,B.PADMANABHAN                                               
REVDAT   1   21-NOV-18 5YUL    0                                                
JRNL        AUTH   R.MANJULA,G.S.A.WRIGHT,R.W.STRANGE,B.PADMANABHAN             
JRNL        TITL   ASSESSMENT OF LIGAND BINDING AT A SITE RELEVANT TO SOD1      
JRNL        TITL 2 OXIDATION AND AGGREGATION                                    
JRNL        REF    FEBS LETT.                    V. 592  1725 2018              
JRNL        REFN                   ISSN 1873-3468                               
JRNL        PMID   29679384                                                     
JRNL        DOI    10.1002/1873-3468.13055                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 183647                         
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) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9635                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 13213                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.02                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 723                          
REMARK   3   BIN FREE R VALUE                    : 0.3070                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10957                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 31                                      
REMARK   3   SOLVENT ATOMS            : 1377                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.50000                                              
REMARK   3    B22 (A**2) : 0.50000                                              
REMARK   3    B33 (A**2) : -1.62000                                             
REMARK   3    B12 (A**2) : 0.50000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.110         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.114         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.079         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.683         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11292 ; 0.018 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15261 ; 1.839 ; 1.945       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1535 ; 6.605 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   474 ;41.845 ;25.591       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1846 ;14.292 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ;19.526 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1685 ; 0.138 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8638 ; 0.009 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5YUL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-NOV-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300005911.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUL-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95372                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 193714                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.00000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: 1HL5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE PH 6.0, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 300K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       72.05650            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       72.05650            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       72.05650            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       72.05650            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       72.05650            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       72.05650            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H                                  
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: 1760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
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: 1550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E                                  
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: 4                                                       
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: 1460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G                                  
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: 5                                                       
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: 1570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J                                  
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET F     0                                                      
REMARK 465     MET J     0                                                      
REMARK 465     LEU J    67                                                      
REMARK 465     SER J    68                                                      
REMARK 465     ARG J    69                                                      
REMARK 465     LYS J    70                                                      
REMARK 465     HIS J    71                                                      
REMARK 465     GLY J    72                                                      
REMARK 465     GLY J    73                                                      
REMARK 465     PRO J    74                                                      
REMARK 465     LYS J    75                                                      
REMARK 465     ASP J    76                                                      
REMARK 465     GLU J    77                                                      
REMARK 465     GLU J    78                                                      
REMARK 465     LEU J   126                                                      
REMARK 465     GLY J   127                                                      
REMARK 465     LYS J   128                                                      
REMARK 465     GLY J   129                                                      
REMARK 465     GLY J   130                                                      
REMARK 465     ASN J   131                                                      
REMARK 465     GLU J   132                                                      
REMARK 465     GLU J   133                                                      
REMARK 465     SER J   134                                                      
REMARK 465     THR J   135                                                      
REMARK 465     LYS J   136                                                      
REMARK 465     THR J   137                                                      
REMARK 465     GLY J   138                                                      
REMARK 465     ASN J   139                                                      
REMARK 465     ALA J   140                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     MET C   0    CG   SD   CE                                        
REMARK 470     MET D   0    CG   SD   CE                                        
REMARK 470     MET E   0    CG   SD   CE                                        
REMARK 470     MET I   0    CG   SD   CE                                        
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 B   406     O    HOH B   409              2.15            
REMARK 500   O    HOH A   350     O    HOH H   398              2.16            
REMARK 500   O    HOH A   490     O    HOH A   497              2.17            
REMARK 500   O    HOH D   403     O    HOH D   410              2.19            
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    LEU A  67   CB  -  CG  -  CD2 ANGL. DEV. = -10.3 DEGREES          
REMARK 500    ASP A  90   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP H  90   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ARG H 115   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG H 115   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG B 115   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG B 115   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ASP B 125   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP G  90   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP J  90   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 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    ASN F  26      -33.87     66.39                                   
REMARK 500    ASP F  90     -177.67    -67.87                                   
REMARK 500    LYS G 136      -65.89   -104.20                                   
REMARK 500    ASN I  65       60.74   -150.17                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 501        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH B 504        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH B 505        DISTANCE =  6.39 ANGSTROMS                       
REMARK 525    HOH B 506        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH B 507        DISTANCE =  7.09 ANGSTROMS                       
REMARK 525    HOH B 508        DISTANCE =  7.92 ANGSTROMS                       
REMARK 525    HOH C 446        DISTANCE =  6.46 ANGSTROMS                       
REMARK 525    HOH D 494        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH D 495        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH D 496        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH D 497        DISTANCE =  6.26 ANGSTROMS                       
REMARK 525    HOH D 498        DISTANCE =  6.28 ANGSTROMS                       
REMARK 525    HOH D 499        DISTANCE =  6.31 ANGSTROMS                       
REMARK 525    HOH E 417        DISTANCE =  7.03 ANGSTROMS                       
REMARK 525    HOH G 392        DISTANCE =  5.96 ANGSTROMS                       
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                              ZN A 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  63   ND1                                                    
REMARK 620 2 HIS A  71   ND1 108.2                                              
REMARK 620 3 HIS A  80   ND1 108.9 124.3                                        
REMARK 620 4 ASP A  83   OD1 104.5  96.0 112.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  63   ND1                                                    
REMARK 620 2 HIS H  71   ND1 106.1                                              
REMARK 620 3 HIS H  80   ND1 112.1 122.5                                        
REMARK 620 4 ASP H  83   OD1 105.6  85.9 121.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  63   ND1                                                    
REMARK 620 2 HIS B  71   ND1 103.6                                              
REMARK 620 3 HIS B  80   ND1 110.5 125.7                                        
REMARK 620 4 ASP B  83   OD1 104.1  92.4 117.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  63   ND1                                                    
REMARK 620 2 HIS C  71   ND1 106.2                                              
REMARK 620 3 HIS C  80   ND1 112.3 124.7                                        
REMARK 620 4 ASP C  83   OD1 105.7  85.2 118.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  63   ND1                                                    
REMARK 620 2 HIS D  71   ND1 105.2                                              
REMARK 620 3 HIS D  80   ND1 112.4 123.2                                        
REMARK 620 4 ASP D  83   OD2 105.0  91.5 116.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  63   ND1                                                    
REMARK 620 2 HIS E  71   ND1  93.6                                              
REMARK 620 3 HIS E  80   ND1 118.6 115.7                                        
REMARK 620 4 ASP E  83   OD1 106.4  99.5 118.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  63   ND1                                                    
REMARK 620 2 HIS F  71   ND1 100.7                                              
REMARK 620 3 HIS F  80   ND1 112.1 124.7                                        
REMARK 620 4 ASP F  83   OD1 103.6  96.2 116.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  63   ND1                                                    
REMARK 620 2 HIS G  71   ND1 102.5                                              
REMARK 620 3 HIS G  80   ND1 113.5 120.6                                        
REMARK 620 4 ASP G  83   OD1 114.9  85.9 116.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN I 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I  63   ND1                                                    
REMARK 620 2 HIS I  71   ND1 106.6                                              
REMARK 620 3 HIS I  80   ND1 106.2 127.5                                        
REMARK 620 4 ASP I  83   OD1 106.6  92.9 115.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue S4P A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN H 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN E 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN I 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue S4P J 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide S4P C 202 and CYS C    
REMARK 800  111                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide S4P D 202 and CYS E    
REMARK 800  111                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide S4P D 202 and CYS D    
REMARK 800  111                                                                 
DBREF  5YUL A    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  5YUL H    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  5YUL B    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  5YUL C    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  5YUL D    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  5YUL E    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  5YUL F    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  5YUL G    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  5YUL I    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  5YUL J    0   153  UNP    P00441   SODC_HUMAN       1    154             
SEQRES   1 A  154  MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 A  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 A  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 A  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 A  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 A  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 A  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 A  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 A  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 A  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 A  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 A  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 H  154  MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 H  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 H  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 H  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 H  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 H  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 H  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 H  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 H  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 H  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 H  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 H  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 B  154  MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 B  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 B  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 B  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 B  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 B  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 B  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 B  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 B  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 B  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 B  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 B  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 C  154  MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 C  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 C  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 C  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 C  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 C  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 C  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 C  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 C  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 C  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 C  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 C  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 D  154  MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 D  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 D  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 D  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 D  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 D  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 D  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 D  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 D  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 D  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 D  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 D  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 E  154  MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 E  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 E  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 E  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 E  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 E  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 E  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 E  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 E  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 E  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 E  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 E  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 F  154  MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 F  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 F  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 F  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 F  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 F  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 F  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 F  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 F  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 F  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 F  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 F  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 G  154  MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 G  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 G  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 G  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 G  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 G  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 G  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 G  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 G  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 G  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 G  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 G  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 I  154  MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 I  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 I  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 I  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 I  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 I  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 I  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 I  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 I  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 I  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 I  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 I  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 J  154  MET ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 J  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 J  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 J  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 J  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 J  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 J  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 J  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 J  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 J  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 J  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 J  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
HET     ZN  A 201       1                                                       
HET    S4P  A 202       4                                                       
HET     ZN  H 201       1                                                       
HET     ZN  B 201       1                                                       
HET     ZN  C 201       1                                                       
HET    S4P  C 202       4                                                       
HET    GOL  C 203       6                                                       
HET     ZN  D 201       1                                                       
HET    S4P  D 202       4                                                       
HET     ZN  E 201       1                                                       
HET     ZN  F 201       1                                                       
HET     ZN  G 201       1                                                       
HET     ZN  I 201       1                                                       
HET    S4P  J 201       4                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     S4P DIHYDROGEN TETRASULFIDE                                          
HETNAM     GOL GLYCEROL                                                         
HETSYN     S4P TETRASULFANE                                                     
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL  11   ZN    9(ZN 2+)                                                     
FORMUL  12  S4P    4(H2 S4)                                                     
FORMUL  17  GOL    C3 H8 O3                                                     
FORMUL  25  HOH   *1377(H2 O)                                                   
HELIX    1 AA1 ALA A   55  GLY A   61  5                                   7    
HELIX    2 AA2 SER A  107  CYS A  111  5                                   5    
HELIX    3 AA3 GLU A  133  GLY A  138  1                                   6    
HELIX    4 AA4 ALA H   55  GLY H   61  5                                   7    
HELIX    5 AA5 ASN H  131  GLY H  138  1                                   8    
HELIX    6 AA6 ALA B   55  GLY B   61  5                                   7    
HELIX    7 AA7 SER B  107  CYS B  111  5                                   5    
HELIX    8 AA8 GLU B  133  GLY B  138  1                                   6    
HELIX    9 AA9 ALA C   55  GLY C   61  5                                   7    
HELIX   10 AB1 GLU C  132  LYS C  136  5                                   5    
HELIX   11 AB2 ALA D   55  GLY D   61  5                                   7    
HELIX   12 AB3 SER D  107  CYS D  111  5                                   5    
HELIX   13 AB4 GLU D  133  GLY D  138  1                                   6    
HELIX   14 AB5 ALA E   55  GLY E   61  5                                   7    
HELIX   15 AB6 ASN E  131  GLY E  138  1                                   8    
HELIX   16 AB7 ALA F   55  GLY F   61  5                                   7    
HELIX   17 AB8 SER F  107  CYS F  111  5                                   5    
HELIX   18 AB9 GLU F  133  GLY F  138  1                                   6    
HELIX   19 AC1 ALA G   55  GLY G   61  5                                   7    
HELIX   20 AC2 GLU G  132  LYS G  136  5                                   5    
HELIX   21 AC3 ALA I   55  GLY I   61  5                                   7    
HELIX   22 AC4 ASN I  131  GLY I  138  1                                   8    
HELIX   23 AC5 ALA J   55  GLY J   61  5                                   7    
SHEET    1 AA1 5 ALA A  95  ASP A 101  0                                        
SHEET    2 AA1 5 VAL A  29  LYS A  36 -1  N  ILE A  35   O  ALA A  95           
SHEET    3 AA1 5 GLN A  15  GLU A  21 -1  N  ASN A  19   O  TRP A  32           
SHEET    4 AA1 5 LYS A   3  LEU A   8 -1  N  CYS A   6   O  ILE A  18           
SHEET    5 AA1 5 GLY A 150  ILE A 151 -1  O  GLY A 150   N  VAL A   5           
SHEET    1 AA2 4 ASP A  83  ALA A  89  0                                        
SHEET    2 AA2 4 GLY A  41  HIS A  48 -1  N  GLY A  41   O  ALA A  89           
SHEET    3 AA2 4 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    4 AA2 4 ARG A 143  VAL A 148 -1  O  LEU A 144   N  VAL A 119           
SHEET    1 AA3 5 ALA H  95  ASP H 101  0                                        
SHEET    2 AA3 5 VAL H  29  LYS H  36 -1  N  VAL H  29   O  ASP H 101           
SHEET    3 AA3 5 GLN H  15  GLU H  21 -1  N  ASN H  19   O  TRP H  32           
SHEET    4 AA3 5 LYS H   3  LEU H   8 -1  N  LEU H   8   O  GLY H  16           
SHEET    5 AA3 5 GLY H 150  ILE H 151 -1  O  GLY H 150   N  VAL H   5           
SHEET    1 AA4 4 ASP H  83  ALA H  89  0                                        
SHEET    2 AA4 4 GLY H  41  HIS H  48 -1  N  GLY H  41   O  ALA H  89           
SHEET    3 AA4 4 THR H 116  HIS H 120 -1  O  THR H 116   N  HIS H  48           
SHEET    4 AA4 4 ARG H 143  VAL H 148 -1  O  LEU H 144   N  VAL H 119           
SHEET    1 AA5 5 ALA B  95  ASP B 101  0                                        
SHEET    2 AA5 5 VAL B  29  LYS B  36 -1  N  VAL B  31   O  ILE B  99           
SHEET    3 AA5 5 GLN B  15  GLU B  21 -1  N  ASN B  19   O  TRP B  32           
SHEET    4 AA5 5 LYS B   3  LEU B   8 -1  N  LEU B   8   O  GLY B  16           
SHEET    5 AA5 5 GLY B 150  ILE B 151 -1  O  GLY B 150   N  VAL B   5           
SHEET    1 AA6 4 ASP B  83  ALA B  89  0                                        
SHEET    2 AA6 4 GLY B  41  HIS B  48 -1  N  GLY B  41   O  ALA B  89           
SHEET    3 AA6 4 THR B 116  HIS B 120 -1  O  THR B 116   N  HIS B  48           
SHEET    4 AA6 4 ARG B 143  VAL B 148 -1  O  LEU B 144   N  VAL B 119           
SHEET    1 AA7 5 ALA C  95  ASP C 101  0                                        
SHEET    2 AA7 5 VAL C  29  LYS C  36 -1  N  VAL C  31   O  ILE C  99           
SHEET    3 AA7 5 GLN C  15  GLU C  21 -1  N  ASN C  19   O  TRP C  32           
SHEET    4 AA7 5 LYS C   3  LEU C   8 -1  N  CYS C   6   O  ILE C  18           
SHEET    5 AA7 5 GLY C 150  ILE C 151 -1  O  GLY C 150   N  VAL C   5           
SHEET    1 AA8 4 ASP C  83  ALA C  89  0                                        
SHEET    2 AA8 4 GLY C  41  HIS C  48 -1  N  GLY C  41   O  ALA C  89           
SHEET    3 AA8 4 THR C 116  HIS C 120 -1  O  VAL C 118   N  HIS C  46           
SHEET    4 AA8 4 ARG C 143  VAL C 148 -1  O  ALA C 145   N  VAL C 119           
SHEET    1 AA9 5 ALA D  95  ASP D 101  0                                        
SHEET    2 AA9 5 VAL D  29  LYS D  36 -1  N  VAL D  29   O  ASP D 101           
SHEET    3 AA9 5 GLN D  15  GLU D  21 -1  N  ASN D  19   O  TRP D  32           
SHEET    4 AA9 5 LYS D   3  LEU D   8 -1  N  CYS D   6   O  ILE D  18           
SHEET    5 AA9 5 GLY D 150  ILE D 151 -1  O  GLY D 150   N  VAL D   5           
SHEET    1 AB1 4 ASP D  83  ALA D  89  0                                        
SHEET    2 AB1 4 GLY D  41  HIS D  48 -1  N  GLY D  41   O  ALA D  89           
SHEET    3 AB1 4 THR D 116  HIS D 120 -1  O  THR D 116   N  HIS D  48           
SHEET    4 AB1 4 ARG D 143  VAL D 148 -1  O  GLY D 147   N  LEU D 117           
SHEET    1 AB2 5 ALA E  95  ASP E 101  0                                        
SHEET    2 AB2 5 VAL E  29  LYS E  36 -1  N  VAL E  31   O  ILE E  99           
SHEET    3 AB2 5 GLN E  15  GLU E  21 -1  N  ASN E  19   O  TRP E  32           
SHEET    4 AB2 5 LYS E   3  LEU E   8 -1  N  LEU E   8   O  GLY E  16           
SHEET    5 AB2 5 GLY E 150  ILE E 151 -1  O  GLY E 150   N  VAL E   5           
SHEET    1 AB3 4 ASP E  83  ALA E  89  0                                        
SHEET    2 AB3 4 GLY E  41  HIS E  48 -1  N  GLY E  41   O  ALA E  89           
SHEET    3 AB3 4 THR E 116  HIS E 120 -1  O  THR E 116   N  HIS E  48           
SHEET    4 AB3 4 ARG E 143  VAL E 148 -1  O  GLY E 147   N  LEU E 117           
SHEET    1 AB4 5 ALA F  95  ASP F 101  0                                        
SHEET    2 AB4 5 VAL F  29  LYS F  36 -1  N  VAL F  29   O  ASP F 101           
SHEET    3 AB4 5 GLN F  15  GLU F  21 -1  N  ASN F  19   O  TRP F  32           
SHEET    4 AB4 5 LYS F   3  LYS F   9 -1  N  LEU F   8   O  GLY F  16           
SHEET    5 AB4 5 GLY F 150  ILE F 151 -1  O  GLY F 150   N  VAL F   5           
SHEET    1 AB5 4 ASP F  83  ALA F  89  0                                        
SHEET    2 AB5 4 GLY F  41  HIS F  48 -1  N  GLY F  41   O  ALA F  89           
SHEET    3 AB5 4 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48           
SHEET    4 AB5 4 ARG F 143  VAL F 148 -1  O  LEU F 144   N  VAL F 119           
SHEET    1 AB6 5 ALA G  95  ASP G 101  0                                        
SHEET    2 AB6 5 VAL G  29  LYS G  36 -1  N  ILE G  35   O  ALA G  95           
SHEET    3 AB6 5 GLN G  15  GLU G  21 -1  N  ASN G  19   O  TRP G  32           
SHEET    4 AB6 5 LYS G   3  LEU G   8 -1  N  LEU G   8   O  GLY G  16           
SHEET    5 AB6 5 GLY G 150  ILE G 151 -1  O  GLY G 150   N  VAL G   5           
SHEET    1 AB7 4 ASP G  83  ALA G  89  0                                        
SHEET    2 AB7 4 GLY G  41  HIS G  48 -1  N  GLY G  41   O  ALA G  89           
SHEET    3 AB7 4 THR G 116  HIS G 120 -1  O  THR G 116   N  HIS G  48           
SHEET    4 AB7 4 ARG G 143  VAL G 148 -1  O  GLY G 147   N  LEU G 117           
SHEET    1 AB8 5 ALA I  95  ASP I 101  0                                        
SHEET    2 AB8 5 VAL I  29  LYS I  36 -1  N  VAL I  31   O  ILE I  99           
SHEET    3 AB8 5 GLN I  15  GLU I  21 -1  N  ASN I  19   O  TRP I  32           
SHEET    4 AB8 5 LYS I   3  LYS I   9 -1  N  CYS I   6   O  ILE I  18           
SHEET    5 AB8 5 GLY I 150  ILE I 151 -1  O  GLY I 150   N  VAL I   5           
SHEET    1 AB9 4 ASP I  83  ALA I  89  0                                        
SHEET    2 AB9 4 GLY I  41  HIS I  48 -1  N  GLY I  41   O  ALA I  89           
SHEET    3 AB9 4 THR I 116  HIS I 120 -1  O  THR I 116   N  HIS I  48           
SHEET    4 AB9 4 ARG I 143  VAL I 148 -1  O  ALA I 145   N  VAL I 119           
SHEET    1 AC1 5 ALA J  95  ASP J 101  0                                        
SHEET    2 AC1 5 VAL J  29  LYS J  36 -1  N  GLY J  33   O  VAL J  97           
SHEET    3 AC1 5 GLN J  15  GLU J  21 -1  N  ASN J  19   O  TRP J  32           
SHEET    4 AC1 5 LYS J   3  LEU J   8 -1  N  LEU J   8   O  GLY J  16           
SHEET    5 AC1 5 GLY J 150  ILE J 151 -1  O  GLY J 150   N  VAL J   5           
SHEET    1 AC2 4 ASP J  83  ALA J  89  0                                        
SHEET    2 AC2 4 GLY J  41  HIS J  48 -1  N  HIS J  43   O  VAL J  87           
SHEET    3 AC2 4 THR J 116  HIS J 120 -1  O  THR J 116   N  HIS J  48           
SHEET    4 AC2 4 ARG J 143  VAL J 148 -1  O  GLY J 147   N  LEU J 117           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.31  
SSBOND   2 CYS H   57    CYS H  146                          1555   1555  2.30  
SSBOND   3 CYS B   57    CYS B  146                          1555   1555  2.30  
SSBOND   4 CYS C   57    CYS C  146                          1555   1555  2.33  
SSBOND   5 CYS D   57    CYS D  146                          1555   1555  2.30  
SSBOND   6 CYS E   57    CYS E  146                          1555   1555  2.25  
SSBOND   7 CYS F   57    CYS F  146                          1555   1555  2.16  
SSBOND   8 CYS G   57    CYS G  146                          1555   1555  2.17  
SSBOND   9 CYS I   57    CYS I  146                          1555   1555  2.21  
SSBOND  10 CYS J   57    CYS J  146                          1555   1555  2.27  
LINK         ND1 HIS A  63                ZN    ZN A 201     1555   1555  2.02  
LINK         ND1 HIS A  71                ZN    ZN A 201     1555   1555  2.15  
LINK         ND1 HIS A  80                ZN    ZN A 201     1555   1555  2.07  
LINK         OD1 ASP A  83                ZN    ZN A 201     1555   1555  1.96  
LINK         ND1 HIS H  63                ZN    ZN H 201     1555   1555  2.19  
LINK         ND1 HIS H  71                ZN    ZN H 201     1555   1555  2.34  
LINK         ND1 HIS H  80                ZN    ZN H 201     1555   1555  2.06  
LINK         OD1 ASP H  83                ZN    ZN H 201     1555   1555  1.88  
LINK         ND1 HIS B  63                ZN    ZN B 201     1555   1555  2.05  
LINK         ND1 HIS B  71                ZN    ZN B 201     1555   1555  2.18  
LINK         ND1 HIS B  80                ZN    ZN B 201     1555   1555  2.00  
LINK         OD1 ASP B  83                ZN    ZN B 201     1555   1555  1.87  
LINK         ND1 HIS C  63                ZN    ZN C 201     1555   1555  2.01  
LINK         ND1 HIS C  71                ZN    ZN C 201     1555   1555  2.34  
LINK         ND1 HIS C  80                ZN    ZN C 201     1555   1555  2.04  
LINK         OD1 ASP C  83                ZN    ZN C 201     1555   1555  1.91  
LINK         SG  CYS C 111                 S4  S4P C 202     1555   1555  2.09  
LINK         ND1 HIS D  63                ZN    ZN D 201     1555   1555  2.03  
LINK         ND1 HIS D  71                ZN    ZN D 201     1555   1555  2.17  
LINK         ND1 HIS D  80                ZN    ZN D 201     1555   1555  2.00  
LINK         OD2 ASP D  83                ZN    ZN D 201     1555   1555  1.93  
LINK         SG  CYS D 111                 S4  S4P D 202     1555   1555  2.09  
LINK         ND1 HIS E  63                ZN    ZN E 201     1555   1555  2.25  
LINK         ND1 HIS E  71                ZN    ZN E 201     1555   1555  2.50  
LINK         ND1 HIS E  80                ZN    ZN E 201     1555   1555  2.01  
LINK         OD1 ASP E  83                ZN    ZN E 201     1555   1555  2.03  
LINK         SG  CYS E 111                 S1  S4P D 202     1555   1555  2.20  
LINK         ND1 HIS F  63                ZN    ZN F 201     1555   1555  2.10  
LINK         ND1 HIS F  71                ZN    ZN F 201     1555   1555  2.25  
LINK         ND1 HIS F  80                ZN    ZN F 201     1555   1555  2.07  
LINK         OD1 ASP F  83                ZN    ZN F 201     1555   1555  1.92  
LINK         ND1 HIS G  63                ZN    ZN G 201     1555   1555  1.96  
LINK         ND1 HIS G  71                ZN    ZN G 201     1555   1555  2.35  
LINK         ND1 HIS G  80                ZN    ZN G 201     1555   1555  2.02  
LINK         OD1 ASP G  83                ZN    ZN G 201     1555   1555  1.98  
LINK         ND1 HIS I  63                ZN    ZN I 201     1555   1555  2.10  
LINK         ND1 HIS I  71                ZN    ZN I 201     1555   1555  2.09  
LINK         ND1 HIS I  80                ZN    ZN I 201     1555   1555  2.03  
LINK         OD1 ASP I  83                ZN    ZN I 201     1555   1555  1.89  
SITE     1 AC1  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC2  4 CYS A 111  ILE A 113  HOH A 473  CYS H 111                    
SITE     1 AC3  4 HIS H  63  HIS H  71  HIS H  80  ASP H  83                    
SITE     1 AC4  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     1 AC5  4 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
SITE     1 AC6  8 HIS C  48  HIS C 120  THR C 137  GLY C 141                    
SITE     2 AC6  8 ARG C 143  HOH C 314  HOH C 347  HOH C 421                    
SITE     1 AC7  4 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     1 AC8  4 HIS E  63  HIS E  71  HIS E  80  ASP E  83                    
SITE     1 AC9  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 AD1  4 HIS G  63  HIS G  71  HIS G  80  ASP G  83                    
SITE     1 AD2  4 HIS I  63  HIS I  71  HIS I  80  ASP I  83                    
SITE     1 AD3  2 CYS I 111  CYS J 111                                          
SITE     1 AD4 11 CYS B 111  SER C 105  LEU C 106  SER C 107                    
SITE     2 AD4 11 GLY C 108  ASP C 109  HIS C 110  ILE C 112                    
SITE     3 AD4 11 ILE C 113  ARG C 115  HOH C 354                               
SITE     1 AD5 21 PHE D  64  SER D 105  LEU D 106  SER D 107                    
SITE     2 AD5 21 GLY D 108  ASP D 109  HIS D 110  ILE D 112                    
SITE     3 AD5 21 ILE D 113  ARG D 115  HOH D 339  SER E 105                    
SITE     4 AD5 21 SER E 107  GLY E 108  ASP E 109  HIS E 110                    
SITE     5 AD5 21 ILE E 112  ILE E 113  ARG E 115  HOH E 313                    
SITE     6 AD5 21 HOH E 320                                                     
SITE     1 AD6 12 PHE D  64  SER D 105  LEU D 106  SER D 107                    
SITE     2 AD6 12 GLY D 108  ASP D 109  HIS D 110  ILE D 112                    
SITE     3 AD6 12 ILE D 113  ARG D 115  HOH D 339  CYS E 111                    
CRYST1  242.634  242.634  144.113  90.00  90.00 120.00 P 63 2 2    120          
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      0.004121  0.002380  0.000000        0.00000                         
SCALE2      0.000000  0.004759  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006939        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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