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Database: PDB
Entry: 2WYT
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Original site: 2WYT 
HEADER    OXIDOREDUCTASE                          20-NOV-09   2WYT              
TITLE     1.0 A RESOLUTION STRUCTURE OF L38V SOD1 MUTANT                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, F;                                                         
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 4932                                        
KEYWDS    OXIDOREDUCTASE, DISEASE MUTATION, AMYOTROPHIC LATERAL SCLEROSIS,      
KEYWDS   2 ANTIOXIDANT                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.V.ANTONYUK,R.W.STRANGE,S.S.HASNAIN                                  
REVDAT   2   12-JUL-17 2WYT    1                                                
REVDAT   1   27-OCT-10 2WYT    0                                                
JRNL        AUTH   S.V.ANTONYUK,R.W.STRANGE,S.S.HASNAIN                         
JRNL        TITL   STRUCTURAL DISCOVERY OF SMALL MOLECULE BINDING SITES IN      
JRNL        TITL 2 CU-ZN HUMAN SUPEROXIDE DISMUTASE FAMILIAL AMYOTROPHIC        
JRNL        TITL 3 LATERAL SCLEROSIS MUTANTS PROVIDES INSIGHTS FOR LEAD         
JRNL        TITL 4 OPTIMIZATION.                                                
JRNL        REF    J.MED.CHEM.                   V.  53  1402 2010              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   20067275                                                     
JRNL        DOI    10.1021/JM9017948                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0106                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 129879                         
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) : 0.125                           
REMARK   3   R VALUE            (WORKING SET) : 0.124                           
REMARK   3   FREE R VALUE                     : 0.147                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6887                            
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) : 1.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.03                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7650                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 404                          
REMARK   3   BIN FREE R VALUE                    : 0.2830                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2216                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 624                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 6.50                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.18000                                             
REMARK   3    B22 (A**2) : -0.35000                                             
REMARK   3    B33 (A**2) : -0.01000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.95000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.022         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.023         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.017         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.700         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.982                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.975                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2600 ; 0.018 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2245 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3569 ; 1.838 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5271 ; 1.533 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   381 ; 6.980 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   119 ;38.841 ;26.218       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   451 ;11.703 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;10.806 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   384 ; 0.123 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3060 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   520 ; 0.003 ; 0.020       
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):  1652 ; 1.652 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   716 ; 0.545 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2671 ; 2.381 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   948 ; 3.178 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   862 ; 4.485 ; 4.500       
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):  4845 ; 1.351 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. U VALUES REFINED INDIVIDUALLY.                           
REMARK   4                                                                      
REMARK   4 2WYT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-NOV-09.                  
REMARK 100 THE DEPOSITION ID IS D_1290041776.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-FEB-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.75                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX10.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : SI111                              
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 136867                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 77.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
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: PDB ENTRY 2C9V                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 150 MM NACL, 2-3M AMMONIUM SULPHATE,     
REMARK 280  100 MM NA ACETATE BUFFER PH 4.75                                    
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       33.67250            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 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: 3420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -222.8 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F                                  
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, LEU  39 TO VAL                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, LEU  39 TO VAL                        
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     GLU F 100    OE1  OE2                                            
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   HE2  HIS F    48    CU     CU F   154              1.11            
REMARK 500   HE2  HIS A    48    CU     CU A   154              1.13            
REMARK 500   HD1  HIS F    63    ZN     ZN F   155              1.16            
REMARK 500   HD1  HIS A    46    CU     CU A   154              1.17            
REMARK 500   HD1  HIS A    71    ZN     ZN A   155              1.18            
REMARK 500   HD1  HIS A    63    ZN     ZN A   155              1.19            
REMARK 500   HE2  HIS F   120    ZN     ZN F   154A             1.23            
REMARK 500   HD1  HIS F    71    ZN     ZN F   155              1.24            
REMARK 500   HE2  HIS A   120    ZN     ZN A   154A             1.24            
REMARK 500   HD1  HIS F    46    CU     CU F   154              1.24            
REMARK 500   HE2  HIS F   120    CU     CU F   154              1.25            
REMARK 500   HE2  HIS A   120    CU     CU A   154              1.26            
REMARK 500   HD1  HIS A    80    ZN     ZN A   155              1.29            
REMARK 500   HD1  HIS F    80    ZN     ZN F   155              1.33            
REMARK 500   HD1  HIS A    46    CU     CU A   154              1.41            
REMARK 500   HD1  HIS F    46    CU     CU F   154              1.45            
REMARK 500   O    HOH A  2326     O    HOH F  2131              1.48            
REMARK 500   O4   SO4 A   161     O    HOH A  2316              1.57            
REMARK 500  HH11  ARG F    69     O    HOH F  2158              1.58            
REMARK 500   HE2  HIS A    48    ZN     ZN A   154A             1.58            
REMARK 500   OD2  ASP F    96     O    HOH F  2197              1.59            
REMARK 500   O4   SO4 F   156     O    HOH F  2295              1.66            
REMARK 500   OD2  ASP F    92     O    HOH F  2191              1.76            
REMARK 500   O    GLU F    77     O    HOH F  2158              1.81            
REMARK 500   OD1  ASP F    90     O    HOH F  2177              1.84            
REMARK 500   ND2  ASN F    53     O    HOH F  2121              1.88            
REMARK 500   ND2  ASN F   131     O    HOH F  2257              1.92            
REMARK 500   OE2  GLU A    77     O    HOH A  2177              1.99            
REMARK 500   O2   SO4 A   157     O    HOH A  2307              2.06            
REMARK 500   ND2  ASN F    26     O    HOH F  2056              2.09            
REMARK 500   ND2  ASN A   131     O    HOH A  2263              2.12            
REMARK 500   NZ   LYS A   122     O    HOH A  2243              2.13            
REMARK 500   OD2  ASP F    92     O    HOH F  2183              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS A   128     O    THR F    54     2546     1.92            
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 A  26       16.69     55.25                                   
REMARK 500    LYS F 136      -55.07   -121.40                                   
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 A2004        DISTANCE =  6.43 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 154A ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 100.9                                              
REMARK 620 3 HIS A 120   NE2  90.0 117.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 138.7                                              
REMARK 620 3 HIS A 120   NE2 102.3 118.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 113.3                                              
REMARK 620 3 HIS A  63   NE2 105.0 106.5                                        
REMARK 620 4 HIS A 120   NE2  90.9  86.4 152.8                                  
REMARK 620 5 SO4 A 161   O1  146.3 100.0  69.2  85.3                            
REMARK 620 6 HOH A2319   O   106.2 139.8  69.2  85.4  40.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  63   ND1                                                    
REMARK 620 2 HIS A  71   ND1 105.1                                              
REMARK 620 3 HIS A  80   ND1 110.6 120.7                                        
REMARK 620 4 ASP A  83   OD1 104.6 100.1 114.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU F 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  46   ND1                                                    
REMARK 620 2 HIS F  48   NE2 139.0                                              
REMARK 620 3 HIS F 120   NE2 101.6 118.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU F 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  46   ND1                                                    
REMARK 620 2 HIS F  48   NE2 120.2                                              
REMARK 620 3 HIS F  63   NE2  92.5 105.4                                        
REMARK 620 4 HIS F 120   NE2  96.7  98.8 145.1                                  
REMARK 620 5 SO4 F 156   O1  133.0 104.7  60.8  89.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 154A ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  48   NE2                                                    
REMARK 620 2 HIS F 120   NE2 118.3                                              
REMARK 620 3 HOH F2297   O   107.4 117.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  63   ND1                                                    
REMARK 620 2 HIS F  71   ND1 104.8                                              
REMARK 620 3 HIS F  80   ND1 110.5 119.5                                        
REMARK 620 4 ASP F  83   OD1 106.5  98.5 115.5                                  
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 CU A 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 154A                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 157                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 158                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 160                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 161                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 163                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU F 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 154A                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 160                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1OEZ   RELATED DB: PDB                                   
REMARK 900 ZN HIS46ARG MUTANT OF HUMAN CU, ZN SUPEROXIDE DISMUTASE              
REMARK 900 RELATED ID: 1PTZ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CU, ZN SUPEROXIDE DISMUTASE,FAMILIAL  
REMARK 900 AMYOTROPHIC LATERAL SCLEROSIS (FALS) MUTANT H43R                     
REMARK 900 RELATED ID: 1AZV   RELATED DB: PDB                                   
REMARK 900 FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)                             
REMARK 900 RELATED ID: 1HL4   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF APO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE          
REMARK 900 RELATED ID: 1OZU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FAMILIAL ALS MUTANT S134N OF HUMAN CU,ZN        
REMARK 900 SUPEROXIDE DISMUTASE ( CUZNSOD) TO 1.3A RESOLUTION                   
REMARK 900 RELATED ID: 2VR6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE       
REMARK 900 DISMUTASE (CUZNSOD) AT 1.3 A RESOLUTION                              
REMARK 900 RELATED ID: 2C9V   RELATED DB: PDB                                   
REMARK 900 ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN SUPEROXIDE DISMUTASE      
REMARK 900 RELATED ID: 1PU0   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN CU,ZN SUPEROXIDE DISMUTASE                        
REMARK 900 RELATED ID: 1FUN   RELATED DB: PDB                                   
REMARK 900 SUPEROXIDE DISMUTASE MUTANT WITH LYS 136 REPLACED BY GLU, CYS 6      
REMARK 900 REPLACED BY ALA AND CYS 111 REPLACED BY SER (K136E, C6A, C111S)      
REMARK 900 RELATED ID: 1SOS   RELATED DB: PDB                                   
REMARK 900 SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA AND CYS 111   
REMARK 900 REPLACED BY SER (C6A, C111S)                                         
REMARK 900 RELATED ID: 1N19   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE HSOD A4V MUTANT                                     
REMARK 900 RELATED ID: 1P1V   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FALS-ASSOCIATED HUMAN COPPER-ZINCSUPEROXIDE     
REMARK 900 DISMUTASE (CUZNSOD) MUTANT D125H TO 1.4A                             
REMARK 900 RELATED ID: 1L3N   RELATED DB: PDB                                   
REMARK 900 THE SOLUTION STRUCTURE OF REDUCED DIMERIC COPPER ZINC SOD:THE        
REMARK 900 STRUCTURAL EFFECTS OF DIMERIZATION                                   
REMARK 900 RELATED ID: 2WKO   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF METAL LOADED PATHOGENIC SOD1 MUTANT G93A.               
REMARK 900 RELATED ID: 1UXL   RELATED DB: PDB                                   
REMARK 900 I113T MUTANT OF HUMAN SOD1                                           
REMARK 900 RELATED ID: 2AF2   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF DISULFIDE REDUCED AND COPPER DEPLETEDHUMAN     
REMARK 900 SUPEROXIDE DISMUTASE                                                 
REMARK 900 RELATED ID: 2VR8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE       
REMARK 900 DISMUTASE (CUZNSOD) AT 1.36 A RESOLUTION                             
REMARK 900 RELATED ID: 1RK7   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF APO CU,ZN SUPEROXIDE DISMUTASE: ROLEOF METAL   
REMARK 900 IONS IN PROTEIN FOLDING                                              
REMARK 900 RELATED ID: 2VR7   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE       
REMARK 900 DISMUTASE (CUZNSOD) AT 1.58 A RESOLUTION                             
REMARK 900 RELATED ID: 2V0A   RELATED DB: PDB                                   
REMARK 900 ATOMIC RESOLUTION CRYSTAL STRUCTURE OF HUMAN SUPEROXIDE DISMUTASE    
REMARK 900 RELATED ID: 1MFM   RELATED DB: PDB                                   
REMARK 900 MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q AT ATOMIC RESOLUTION      
REMARK 900 RELATED ID: 4SOD   RELATED DB: PDB                                   
REMARK 900 CU,ZN SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA AND     
REMARK 900 CYS 111 REPLACED BY SER (C6A,C111S) WITH AN 18-RESIDUE HEPARIN-      
REMARK 900 BINDING PEPTIDE FUSED TO THE C- TERMINUS (THEORETICAL MODEL)         
REMARK 900 RELATED ID: 2C9S   RELATED DB: PDB                                   
REMARK 900 1.24 ANGSTROMS RESOLUTION STRUCTURE OF ZN- ZN HUMAN SUPEROXIDE       
REMARK 900 DISMUTASE                                                            
REMARK 900 RELATED ID: 1DSW   RELATED DB: PDB                                   
REMARK 900 THE SOLUTION STRUCTURE OF A MONOMERIC, REDUCED FORM OFHUMAN COPPER,  
REMARK 900 ZINC SUPEROXIDE DISMUTASE BEARING THE SAMECHARGE AS THE NATIVE       
REMARK 900 PROTEIN                                                              
REMARK 900 RELATED ID: 1KMG   RELATED DB: PDB                                   
REMARK 900 THE SOLUTION STRUCTURE OF MONOMERIC COPPER- FREE SUPEROXIDEDISMUTASE 
REMARK 900 RELATED ID: 1OZT   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF APO-H46R FAMILIAL ALS MUTANT HUMAN CU,ZN        
REMARK 900 SUPEROXIDE DISMUTASE ( CUZNSOD) TO 2.5A RESOLUTION                   
REMARK 900 RELATED ID: 1N18   RELATED DB: PDB                                   
REMARK 900 THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE DISMUTASE, C6A,C111S         
REMARK 900 RELATED ID: 1BA9   RELATED DB: PDB                                   
REMARK 900 THE SOLUTION STRUCTURE OF REDUCED MONOMERIC SUPEROXIDE DISMUTASE,    
REMARK 900 NMR, 36 STRUCTURES                                                   
REMARK 900 RELATED ID: 2C9U   RELATED DB: PDB                                   
REMARK 900 1.24 ANGSTROMS RESOLUTION STRUCTURE OF AS- ISOLATED CU-ZN HUMAN      
REMARK 900 SUPEROXIDE DISMUTASE                                                 
REMARK 900 RELATED ID: 1HL5   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE         
REMARK 900 RELATED ID: 1UXM   RELATED DB: PDB                                   
REMARK 900 A4V MUTANT OF HUMAN SOD1                                             
REMARK 900 RELATED ID: 1SPD   RELATED DB: PDB                                   
REMARK 900 SUPEROXIDE DISMUTASE                                                 
REMARK 900 RELATED ID: 2WZ0   RELATED DB: PDB                                   
REMARK 900 L38V SOD1 MUTANT COMPLEXED WITH ANILINE.                             
REMARK 900 RELATED ID: 2WYZ   RELATED DB: PDB                                   
REMARK 900 L38V SOD1 MUTANT COMPLEXED WITH UMP                                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 MUTATION LEU38 TO VAL                                                
DBREF  2WYT A    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  2WYT F    1   153  UNP    P00441   SODC_HUMAN       2    154             
SEQADV 2WYT VAL A   38  UNP  P00441    LEU    39 ENGINEERED MUTATION            
SEQADV 2WYT VAL F   38  UNP  P00441    LEU    39 ENGINEERED MUTATION            
SEQRES   1 A  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 A  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 A  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY VAL THR          
SEQRES   4 A  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 A  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 A  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 A  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 A  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 A  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 A  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 A  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 A  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 F  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 F  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 F  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY VAL THR          
SEQRES   4 F  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 F  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 F  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 F  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 F  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 F  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 F  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 F  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 F  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
HET     CU  A 154       2                                                       
HET     ZN  A 154A      1                                                       
HET     ZN  A 155       1                                                       
HET    SO4  A 156       5                                                       
HET    SO4  A 157      10                                                       
HET    SO4  A 158      10                                                       
HET    ACT  A 160       7                                                       
HET    SO4  A 161       5                                                       
HET     CL  A 162       1                                                       
HET    SO4  A 163      10                                                       
HET     CU  F 154       2                                                       
HET     ZN  F 154A      1                                                       
HET     ZN  F 155       1                                                       
HET    SO4  F 156       5                                                       
HET     CL  F 160       1                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ACT ACETATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3   CU    2(CU 2+)                                                     
FORMUL   4   ZN    4(ZN 2+)                                                     
FORMUL   6  SO4    6(O4 S 2-)                                                   
FORMUL   9  ACT    C2 H3 O2 1-                                                  
FORMUL  11   CL    2(CL 1-)                                                     
FORMUL  18  HOH   *624(H2 O)                                                    
HELIX    1   1 ALA A   55  GLY A   61  5                                   7    
HELIX    2   2 SER A  107  HIS A  110  5                                   4    
HELIX    3   3 ASN A  131  LYS A  136  5                                   6    
HELIX    4   4 ALA F   55  GLY F   61  5                                   7    
HELIX    5   5 GLU F  133  GLY F  138  1                                   6    
SHEET    1  AA 5 ALA A  95  ASP A 101  0                                        
SHEET    2  AA 5 VAL A  29  LYS A  36 -1  O  VAL A  29   N  ASP A 101           
SHEET    3  AA 5 GLN A  15  GLN A  22 -1  O  GLN A  15   N  LYS A  36           
SHEET    4  AA 5 THR A   2  LEU A   8 -1  O  THR A   2   N  GLN A  22           
SHEET    5  AA 5 GLY A 150  ILE A 151 -1  O  GLY A 150   N  VAL A   5           
SHEET    1  AB 4 ASP A  83  ALA A  89  0                                        
SHEET    2  AB 4 GLY A  41  HIS A  48 -1  O  GLY A  41   N  ALA A  89           
SHEET    3  AB 4 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    4  AB 4 ARG A 143  VAL A 148 -1  N  LEU A 144   O  VAL A 119           
SHEET    1  FA 5 VAL F  94  ASP F 101  0                                        
SHEET    2  FA 5 VAL F  29  LYS F  36 -1  O  VAL F  29   N  ASP F 101           
SHEET    3  FA 5 VAL F  14  GLN F  22 -1  O  GLN F  15   N  LYS F  36           
SHEET    4  FA 5 LYS F   3  GLY F  10 -1  O  ALA F   4   N  PHE F  20           
SHEET    5  FA 5 GLY F 150  ILE F 151 -1  O  GLY F 150   N  VAL F   5           
SHEET    1  FB 4 ASP F  83  ALA F  89  0                                        
SHEET    2  FB 4 GLY F  41  HIS F  48 -1  O  GLY F  41   N  ALA F  89           
SHEET    3  FB 4 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48           
SHEET    4  FB 4 ARG F 143  VAL F 148 -1  N  LEU F 144   O  VAL F 119           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.26  
SSBOND   2 CYS F   57    CYS F  146                          1555   1555  2.22  
LINK         ND1 HIS A  46                ZN  B ZN A 154A    1555   1555  2.56  
LINK         ND1 HIS A  46                CU  A CU A 154     1555   1555  1.98  
LINK         ND1 HIS A  46                CU  C CU A 154     1555   1555  1.86  
LINK         NE2 HIS A  48                ZN  B ZN A 154A    1555   1555  2.19  
LINK         NE2 HIS A  48                CU  A CU A 154     1555   1555  1.95  
LINK         NE2 HIS A  48                CU  C CU A 154     1555   1555  2.52  
LINK         ND1 HIS A  63                ZN    ZN A 155     1555   1555  2.03  
LINK         NE2 HIS A  63                CU  C CU A 154     1555   1555  2.36  
LINK         ND1 HIS A  71                ZN    ZN A 155     1555   1555  2.00  
LINK         ND1 HIS A  80                ZN    ZN A 155     1555   1555  2.00  
LINK         OD1 ASP A  83                ZN    ZN A 155     1555   1555  1.98  
LINK         NE2 HIS A 120                ZN  B ZN A 154A    1555   1555  1.81  
LINK         NE2 HIS A 120                CU  A CU A 154     1555   1555  2.05  
LINK         NE2 HIS A 120                CU  C CU A 154     1555   1555  2.50  
LINK         ND1 HIS F  46                CU  A CU F 154     1555   1555  2.05  
LINK         ND1 HIS F  46                CU  C CU F 154     1555   1555  2.01  
LINK         NE2 HIS F  48                CU  A CU F 154     1555   1555  1.93  
LINK         NE2 HIS F  48                CU  C CU F 154     1555   1555  2.28  
LINK         NE2 HIS F  48                ZN  B ZN F 154A    1555   1555  2.19  
LINK         ND1 HIS F  63                ZN    ZN F 155     1555   1555  2.00  
LINK         NE2 HIS F  63                CU  C CU F 154     1555   1555  2.66  
LINK         ND1 HIS F  71                ZN    ZN F 155     1555   1555  2.06  
LINK         ND1 HIS F  80                ZN    ZN F 155     1555   1555  2.02  
LINK         OD1 ASP F  83                ZN    ZN F 155     1555   1555  1.94  
LINK         NE2 HIS F 120                CU  A CU F 154     1555   1555  2.04  
LINK         NE2 HIS F 120                CU  C CU F 154     1555   1555  2.22  
LINK         NE2 HIS F 120                ZN  B ZN F 154A    1555   1555  1.78  
LINK        CU  C CU A 154                 O1 CSO4 A 161     1555   1555  2.25  
LINK        CU  C CU A 154                 O   HOH A2319     1555   1555  2.63  
LINK        CU  C CU F 154                 O1 CSO4 F 156     1555   1555  2.37  
LINK        ZN  B ZN F 154A                O   HOH F2297     1555   1555  2.65  
CISPEP   1 GLY F   12    PRO F   13          0        -0.42                     
SITE     1 AC1  6 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC1  6 SO4 A 161  HOH A2319                                          
SITE     1 AC2  6 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC2  6 SO4 A 161  HOH A2319                                          
SITE     1 AC3  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC4  9 THR A  58  SER A 142  ARG A 143  HOH A2143                    
SITE     2 AC4  9 HOH A2299  HOH A2300  HOH A2301  HOH A2302                    
SITE     3 AC4  9 HOH A2303                                                     
SITE     1 AC5 11 HOH A2304  HOH A2305  HOH A2306  HOH A2307                    
SITE     2 AC5 11 HOH A2308  THR F 137  ASN F 139  ALA F 140                    
SITE     3 AC5 11 GLY F 141  SO4 F 156  HOH F2290                               
SITE     1 AC6 11 THR A 137  ASN A 139  ALA A 140  GLY A 141                    
SITE     2 AC6 11 SO4 A 161  HOH A2309  HOH A2310  HOH A2311                    
SITE     3 AC6 11 HOH A2312  HOH A2313  HOH A2317                               
SITE     1 AC7  5 GLU A  49  PHE A  64  ASN A  65  PRO A  66                    
SITE     2 AC7  5 HOH A2314                                                     
SITE     1 AC8 14 HIS A  48  HIS A  63  HIS A 120  THR A 137                    
SITE     2 AC8 14 ARG A 143   CU A 154   ZN A 154A SO4 A 158                    
SITE     3 AC8 14 HOH A2276  HOH A2315  HOH A2316  HOH A2317                    
SITE     4 AC8 14 HOH A2319  HOH A2320                                          
SITE     1 AC9 11 HOH A2321  HOH A2322  HOH A2323  HOH A2324                    
SITE     2 AC9 11 HOH A2325  HOH A2326  THR F  58  SER F 142                    
SITE     3 AC9 11 ARG F 143  HOH F2131  HOH F2293                               
SITE     1 BC1  7 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     2 BC1  7 SO4 F 156  HOH F2294  HOH F2297                               
SITE     1 BC2  7 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     2 BC2  7 SO4 F 156  HOH F2294  HOH F2297                               
SITE     1 BC3  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 BC4 15 SO4 A 157  HIS F  48  HIS F  63  HIS F 120                    
SITE     2 BC4 15 THR F 137  ARG F 143   CU F 154   ZN F 154A                   
SITE     3 BC4 15 HOH F2290  HOH F2292  HOH F2293  HOH F2294                    
SITE     4 BC4 15 HOH F2295  HOH F2296  HOH F2297                               
SITE     1 BC5  1 HOH F2063                                                     
CRYST1   38.690   67.345   52.577  90.00 106.57  90.00 P 1 21 1      4          
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      0.025846  0.000000  0.007690        0.00000                         
SCALE2      0.000000  0.014849  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019844        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system