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Database: PDB
Entry: 2VR6
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Original site: 2VR6 
HEADER    OXIDOREDUCTASE                          28-MAR-08   2VR6              
TITLE     CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN                   
TITLE    2 SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.3 A RESOLUTION                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, F;                                                         
COMPND   4 FRAGMENT: RESIDUES 2-154;                                            
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 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, ZINC, COPPER, HUMAN CU, CYTOPLASM,                    
KEYWDS   2 ACETYLATION, UBL CONJUGATION, DISEASE MUTATION, ZN                   
KEYWDS   3 SUPEROXIDE DISMUTASE, AMYOTROPHIC LATERAL SCLEROSIS,                 
KEYWDS   4 ANTIOXIDANT, METAL-BINDING                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.ANTONYUK,X.CAO,S.V.SEETHARAMAN,L.J.WHITSON,A.B.TAYLOR,              
AUTHOR   2 S.P.HOLLOWAY,R.W.STRANGE,P.A.DOUCETTE,A.TIWARI,L.J.HAYWARD,          
AUTHOR   3 S.PADUA,J.A.COHLBERG,J.SELVERSTONE VALENTINE,S.S.HASNAIN,            
AUTHOR   4 P.J.HART                                                             
REVDAT   3   24-FEB-09 2VR6    1       VERSN                                    
REVDAT   2   17-JUN-08 2VR6    1       JRNL                                     
REVDAT   1   15-APR-08 2VR6    0                                                
JRNL        AUTH   X.CAO,S.ANTONYUK,S.V.SEETHARAMAN,L.J.WHITSON,                
JRNL        AUTH 2 A.B.TAYLOR,S.P.HOLLOWAY,R.W.STRANGE,P.A.DOUCETTE,            
JRNL        AUTH 3 J.S.VALENTINE,A.TIWARI,L.J.HAYWARD,S.PADUA,                  
JRNL        AUTH 4 J.A.COHLBERG,S.S.HASNAIN,P.J.HART                            
JRNL        TITL   STRUCTURES OF THE G85R VARIANT OF SOD1 IN FAMILIAL           
JRNL        TITL 2 AMYOTROPHIC LATERAL SCLEROSIS.                               
JRNL        REF    J.BIOL.CHEM.                  V. 283 16169 2008              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   18378676                                                     
JRNL        DOI    10.1074/JBC.M801522200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.3  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.9999                                      
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) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 66304                          
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) : 0.135                           
REMARK   3   R VALUE            (WORKING SET) : 0.132                           
REMARK   3   FREE R VALUE                     : 0.182                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3532                            
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) : 1.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.33                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4226                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2100                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 207                          
REMARK   3   BIN FREE R VALUE                    : 0.2800                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2377                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 19                                      
REMARK   3   SOLVENT ATOMS            : 779                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 11.05                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 10.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.03000                                              
REMARK   3    B22 (A**2) : -0.04000                                             
REMARK   3    B33 (A**2) : 0.01000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.051         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.053         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.031         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.616         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.978                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.961                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2427 ; 0.019 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2153 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3268 ; 1.903 ; 1.948       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5095 ; 2.290 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   318 ; 6.857 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   435 ;13.374 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ; 9.083 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   356 ; 0.140 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2754 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   430 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   528 ; 0.255 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2378 ; 0.204 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1438 ; 0.098 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   610 ; 0.241 ; 0.200       
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):    16 ; 0.368 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    36 ; 0.308 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    95 ; 0.243 ; 0.200       
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):  1552 ; 1.923 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2491 ; 2.734 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   875 ; 3.494 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   777 ; 4.846 ; 4.500       
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: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2VR6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAR-08.                  
REMARK 100 THE PDBE ID CODE IS EBI-35794.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70210                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.30                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 3.5                                
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.8                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.9                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.58                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.70                               
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 1C9S                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% P3350 0.2 M NA THYOCYANATE           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       17.64800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.71200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.87300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.71200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       17.64800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.87300            
REMARK 290   SMTRY3   4  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: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 1260 ANGSTROM**2                          
REMARK 350 TOTAL SURFACE AREA OF THE COMPLEX: 17060 ANGSTROM**2                 
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.1 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, GLY 86 TO ARG                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, GLY 86 TO ARG                         
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   ND1  HIS F   110  -  O    HOH F  2301              1.87            
REMARK 500   O    GLN F   153  -  O    HOH F  2378              2.20            
REMARK 500   O    HOH A  2052  -  O    HOH F  2371              2.08            
REMARK 500   O    HOH A  2061  -  O    HOH A  2194              2.16            
REMARK 500   O    HOH A  2173  -  O    HOH A  2395              2.12            
REMARK 500   O    HOH A  2365  -  O    HOH A  2367              2.05            
REMARK 500   O    HOH F  2083  -  O    HOH F  2351              2.15            
REMARK 500   O    HOH F  2182  -  O    HOH A  2384              2.17            
REMARK 500   O    HOH F  2204  -  O    HOH F  2212              1.94            
REMARK 500   O    HOH F  2263  -  O    HOH F  2265              2.17            
REMARK 500   O    HOH F  2340  -  O    HOH F  2352              2.18            
REMARK 500   O    HOH F  2343  -  O    HOH F  2345              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                                                                      
REMARK 500   O    HOH A  2030     O    HOH F  2178     3655      2.19           
REMARK 500   O    HOH F  2045     O    HOH A  2295     3645      2.15           
REMARK 500   O    HOH F  2095     O    HOH A  2102     3655      2.11           
REMARK 500   O    HOH F  2132     O    HOH A  2229     3645      2.20           
REMARK 500   O    HOH F  2155     O    HOH A  2351     2565      2.13           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LYS F  75   CE A  LYS F  75   NZ A    0.165                       
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    ASP F  96   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 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 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    ARG F  85     -127.94     66.68                                   
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 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A1154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 132.9                                              
REMARK 620 3 HIS A 120   NE2 107.2 111.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU F1155  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F 120   NE2                                                    
REMARK 620 2 HIS F  46   ND1  97.9                                              
REMARK 620 3 HIS F  48   NE2 105.5 123.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 115.9                                              
REMARK 620 3 HIS A 120   NE2  97.4 126.7                                        
REMARK 620 4 SO4 A1157   O1  104.7 106.2 103.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1156  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  71   ND1                                                    
REMARK 620 2 HIS A  63   ND1 106.0                                              
REMARK 620 3 ASP A  83   OD1  98.3 106.7                                        
REMARK 620 4 HIS A  80   ND1 120.3 107.4 117.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F1154  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F 120   NE2                                                    
REMARK 620 2 HIS F  46   ND1  96.3                                              
REMARK 620 3 HIS F  48   NE2 125.2 117.7                                        
REMARK 620 4 SO4 F1157   O1  104.7 106.3 105.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F1156  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  63   ND1                                                    
REMARK 620 2 HIS F  71   ND1 105.0                                              
REMARK 620 3 HIS F  80   ND1 108.3 120.9                                        
REMARK 620 4 ASP F  83   OD1 106.4  99.3 115.6                                  
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 A1154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1157                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A1158                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN F1154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU F1155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN F1156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F1157                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1L3N   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF REDUCED DIMERIC                           
REMARK 900  COPPER ZINC SOD:THE STRUCTURAL EFFECTS OF                           
REMARK 900  DIMERIZATION                                                        
REMARK 900 RELATED ID: 2AF2   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF DISULFIDE REDUCED AND                         
REMARK 900  COPPER DEPLETEDHUMAN SUPEROXIDE DISMUTASE                           
REMARK 900 RELATED ID: 1UXL   RELATED DB: PDB                                   
REMARK 900  I113T MUTANT OF HUMAN SOD1                                          
REMARK 900 RELATED ID: 1PTZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN CU, ZN                               
REMARK 900  SUPEROXIDE DISMUTASE,FAMILIAL AMYOTROPHIC                           
REMARK 900  LATERAL SCLEROSIS (FALS) MUTANT H43R                                
REMARK 900 RELATED ID: 1OEZ   RELATED DB: PDB                                   
REMARK 900  ZN HIS46ARG MUTANT OF HUMAN CU, ZN                                  
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 1RK7   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF APO CU,ZN SUPEROXIDE                          
REMARK 900  DISMUTASE: ROLEOF METAL IONS IN PROTEIN                             
REMARK 900  FOLDING                                                             
REMARK 900 RELATED ID: 1HL4   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF APO TYPE HUMAN CU, ZN                              
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 1AZV   RELATED DB: PDB                                   
REMARK 900  FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)                            
REMARK 900 RELATED ID: 2V0A   RELATED DB: PDB                                   
REMARK 900  ATOMIC RESOLUTION CRYSTAL STRUCTURE OF HUMAN                        
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 2C9S   RELATED DB: PDB                                   
REMARK 900  1.24 ANGSTROMS RESOLUTION STRUCTURE OF ZN-                          
REMARK 900  ZN HUMAN SUPEROXIDE DISMUTASE                                       
REMARK 900 RELATED ID: 4SOD   RELATED DB: PDB                                   
REMARK 900  CU,ZN SUPEROXIDE DISMUTASE MUTANT WITH CYS                          
REMARK 900  6 REPLACED BY ALA AND CYS 111 REPLACED                              
REMARK 900  BY SER (C6A,C111S) WITH AN 18-RESIDUE                               
REMARK 900  HEPARIN-BINDING PEPTIDE FUSED TO THE C-                             
REMARK 900  TERMINUS (THEORETICAL MODEL)                                        
REMARK 900 RELATED ID: 1MFM   RELATED DB: PDB                                   
REMARK 900  MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q                          
REMARK 900  AT ATOMIC RESOLUTION                                                
REMARK 900 RELATED ID: 1OZU   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF FAMILIAL ALS MUTANT                            
REMARK 900  S134N OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (                         
REMARK 900  CUZNSOD) TO 1.3A RESOLUTION                                         
REMARK 900 RELATED ID: 1DSW   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF A MONOMERIC,                              
REMARK 900  REDUCED FORM OFHUMAN COPPER, ZINC SUPEROXIDE                        
REMARK 900  DISMUTASE BEARING THE SAMECHARGE AS THE                             
REMARK 900  NATIVE PROTEIN                                                      
REMARK 900 RELATED ID: 1OZT   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF APO-H46R FAMILIAL ALS                          
REMARK 900  MUTANT HUMAN CU,ZN SUPEROXIDE DISMUTASE (                           
REMARK 900  CUZNSOD) TO 2.5A RESOLUTION                                         
REMARK 900 RELATED ID: 1KMG   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF MONOMERIC COPPER-                         
REMARK 900  FREE SUPEROXIDEDISMUTASE                                            
REMARK 900 RELATED ID: 2C9V   RELATED DB: PDB                                   
REMARK 900  ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN                          
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 1N18   RELATED DB: PDB                                   
REMARK 900  THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE                             
REMARK 900  DISMUTASE, C6A,C111S                                                
REMARK 900 RELATED ID: 1BA9   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF REDUCED MONOMERIC                         
REMARK 900  SUPEROXIDE DISMUTASE, NMR, 36 STRUCTURES                            
REMARK 900 RELATED ID: 1PU0   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN CU,ZN SUPEROXIDE                                 
REMARK 900  DISMUTASE                                                           
REMARK 900 RELATED ID: 1FUN   RELATED DB: PDB                                   
REMARK 900  SUPEROXIDE DISMUTASE MUTANT WITH LYS 136                            
REMARK 900  REPLACED BY GLU, CYS 6 REPLACED BY ALA                              
REMARK 900  AND CYS 111 REPLACED BY SER (K136E, C6A,                            
REMARK 900  C111S)                                                              
REMARK 900 RELATED ID: 1SOS   RELATED DB: PDB                                   
REMARK 900  SUPEROXIDE DISMUTASE MUTANT WITH CYS 6                              
REMARK 900  REPLACED BY ALA AND CYS 111 REPLACED BY                             
REMARK 900  SER (C6A, C111S)                                                    
REMARK 900 RELATED ID: 1N19   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE HSOD A4V MUTANT                                    
REMARK 900 RELATED ID: 2C9U   RELATED DB: PDB                                   
REMARK 900  1.24 ANGSTROMS RESOLUTION STRUCTURE OF AS-                          
REMARK 900  ISOLATED CU-ZN HUMAN SUPEROXIDE DISMUTASE                           
REMARK 900 RELATED ID: 1HL5   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN                             
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 1P1V   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF FALS-ASSOCIATED HUMAN                          
REMARK 900  COPPER-ZINCSUPEROXIDE DISMUTASE (CUZNSOD) MUTANT                    
REMARK 900   D125H TO 1.4A                                                      
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 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 G85R MUTANT                                                          
DBREF  2VR6 A    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  2VR6 F    1   153  UNP    P00441   SODC_HUMAN       2    154             
SEQADV 2VR6 ARG A   85  UNP  P00441    GLY    86 ENGINEERED MUTATION            
SEQADV 2VR6 ARG F   85  UNP  P00441    GLY    86 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 LEU 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 ARG 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 LEU 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 ARG 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  A1154       1                                                       
HET     ZN  A1155       1                                                       
HET     ZN  A1156       1                                                       
HET    SO4  A1157       5                                                       
HET    SCN  A1158       3                                                       
HET     ZN  F1154       1                                                       
HET     CU  F1155       1                                                       
HET     ZN  F1156       1                                                       
HET    SO4  F1157       5                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM     SO4 SULFATE ION                                                      
HETNAM      ZN ZINC ION                                                         
HETNAM     SCN THIOCYANATE ION                                                  
FORMUL   3   CU    2(CU 2+)                                                     
FORMUL   4  SO4    2(O4 S 2-)                                                   
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   6  SCN    C N S 1-                                                     
FORMUL   7  HOH   *779(H2 O1)                                                   
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 SER F  107  HIS F  110  5                                   4    
HELIX    6   6 ASN F  131  LYS F  136  5                                   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  GLU A  21 -1  O  GLN A  15   N  LYS A  36           
SHEET    4  AA 5 LYS A   3  LEU A   8 -1  O  ALA A   4   N  PHE A  20           
SHEET    5  AA 5 GLY A 150  ILE A 151 -1  O  GLY A 150   N  VAL A   5           
SHEET    1  AB 2 GLY A  41  HIS A  43  0                                        
SHEET    2  AB 2 VAL A  87  ALA A  89 -1  O  VAL A  87   N  HIS A  43           
SHEET    1  AC 3 PHE A  45  HIS A  48  0                                        
SHEET    2  AC 3 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    3  AC 3 ARG A 143  VAL A 148 -1  N  LEU A 144   O  VAL A 119           
SHEET    1  FA 5 ALA F  95  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 GLN F  15  GLN F  22 -1  O  GLN F  15   N  LYS F  36           
SHEET    4  FA 5 THR F   2  LEU F   8 -1  O  THR F   2   N  GLN F  22           
SHEET    5  FA 5 GLY F 150  ALA F 152 -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  2.17  
SSBOND   2 CYS F   57    CYS F  146                          1555   1555  2.12  
LINK        CU    CU A1154                 ND1 HIS A  46     1555   1555  1.64  
LINK        CU    CU A1154                 NE2 HIS A  48     1555   1555  2.21  
LINK        CU    CU A1154                 NE2 HIS A 120     1555   1555  2.22  
LINK        ZN    ZN A1155                 ND1 HIS A  46     1555   1555  2.12  
LINK        ZN    ZN A1155                 NE2 HIS A  48     1555   1555  2.05  
LINK        ZN    ZN A1155                 NE2 HIS A 120     1555   1555  2.04  
LINK        ZN    ZN A1155                 O1  SO4 A1157     1555   1555  1.96  
LINK        ZN    ZN A1156                 ND1 HIS A  71     1555   1555  2.04  
LINK        ZN    ZN A1156                 ND1 HIS A  63     1555   1555  2.02  
LINK        ZN    ZN A1156                 ND1 HIS A  80     1555   1555  2.02  
LINK        ZN    ZN A1156                 OD1 ASP A  83     1555   1555  1.98  
LINK        ZN    ZN F1154                 NE2 HIS F 120     1555   1555  2.03  
LINK        ZN    ZN F1154                 ND1 HIS F  46     1555   1555  2.11  
LINK        ZN    ZN F1154                 NE2 HIS F  48     1555   1555  2.04  
LINK        ZN    ZN F1154                 O1  SO4 F1157     1555   1555  2.01  
LINK        CU    CU F1155                 NE2 HIS F 120     1555   1555  2.29  
LINK        CU    CU F1155                 NE2 HIS F  48     1555   1555  2.26  
LINK        CU    CU F1155                 ND1 HIS F  46     1555   1555  1.78  
LINK        ZN    ZN F1156                 ND1 HIS F  71     1555   1555  2.07  
LINK        ZN    ZN F1156                 ND1 HIS F  80     1555   1555  2.06  
LINK        ZN    ZN F1156                 OD1 ASP F  83     1555   1555  1.97  
LINK        ZN    ZN F1156                 ND1 HIS F  63     1555   1555  1.99  
SITE     1 AC1  5 HIS A  46  HIS A  48  HIS A 120   ZN A1155                    
SITE     2 AC1  5 SO4 A1157                                                     
SITE     1 AC2  6 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC2  6  CU A1154  SO4 A1157                                          
SITE     1 AC3  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC4 14 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC4 14 THR A 137  ARG A 143   CU A1154   ZN A1155                    
SITE     3 AC4 14 HOH A2366  HOH A2372  HOH A2394  HOH A2395                    
SITE     4 AC4 14 HOH A2396  HOH A2397                                          
SITE     1 AC5  4 THR A  88  ASP A  96  ILE A  99  LYS F 128                    
SITE     1 AC6  6 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     2 AC6  6  CU F1155  SO4 F1157                                          
SITE     1 AC7  5 HIS F  46  HIS F  48  HIS F 120   ZN F1154                    
SITE     2 AC7  5 SO4 F1157                                                     
SITE     1 AC8  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 AC9 14 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     2 AC9 14 THR F 137  ARG F 143   ZN F1154   CU F1155                    
SITE     3 AC9 14 HOH F2352  HOH F2353  HOH F2379  HOH F2380                    
SITE     4 AC9 14 HOH F2381  HOH F2382                                          
CRYST1   35.296   73.746  111.424  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.028332  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013560  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008975        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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