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Database: PDB
Entry: 2VR8
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Original site: 2VR8 
HEADER    OXIDOREDUCTASE                          28-MAR-08   2VR8              
TITLE     CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN                   
TITLE    2 SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.36 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    ZINC, COPPER, HUMAN CU, CYTOPLASM, ACETYLATION, UBL                   
KEYWDS   2 CONJUGATION, DISEASE MUTATION, ZN SUPEROXIDE DISMUTASE,              
KEYWDS   3 AMYOTROPHIC LATERAL SCLEROSIS, ANTIOXIDANT, METAL-BINDING,           
KEYWDS   4 OXIDOREDUCTASE                                                       
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   4   24-FEB-09 2VR8    1       VERSN                                    
REVDAT   3   17-JUN-08 2VR8    1       JRNL                                     
REVDAT   2   29-APR-08 2VR8    1       JRNL                                     
REVDAT   1   08-APR-08 2VR8    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 A.TIWARI,L.J.HAYWARD,S.PADUA,J.A.COHLBERG,                   
JRNL        AUTH 4 J.SELVERSTONE VALENTINE,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.    1.36 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) : 1.36                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 52158                          
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) : 0.115                           
REMARK   3   R VALUE            (WORKING SET) : 0.113                           
REMARK   3   FREE R VALUE                     : 0.153                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2789                            
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) : 1.36                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.40                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2313                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2290                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 122                          
REMARK   3   BIN FREE R VALUE                    : 0.3280                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2287                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 50                                      
REMARK   3   SOLVENT ATOMS            : 520                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 12.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.16000                                              
REMARK   3    B22 (A**2) : -0.13000                                             
REMARK   3    B33 (A**2) : -0.04000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.04000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.053         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.051         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.033         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.776         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.982                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.966                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2366 ; 0.017 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2069 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3190 ; 1.770 ; 1.943       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4877 ; 1.977 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   321 ;12.729 ; 5.125       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   398 ;10.992 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;18.641 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   347 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2700 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   424 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   498 ; 0.241 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2189 ; 0.192 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1489 ; 0.090 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   391 ; 0.251 ; 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):    75 ; 0.600 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):   124 ; 0.513 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    49 ; 0.270 ; 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):  1530 ; 1.712 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2444 ; 2.498 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   836 ; 3.524 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   741 ; 4.562 ; 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 2VR8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAR-08.                  
REMARK 100 THE PDBE ID CODE IS EBI-35801.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-OCT-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                       : PX10.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.28                               
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   : 55091                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.36                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NONE                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : 3.4                                
REMARK 200  R MERGE                    (I) : 0.04                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.60                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.36                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 70.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.2                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.33                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.40                               
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 2C9S                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.4                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.2M  SODIUM                
REMARK 280  THIOCYANATE                                                         
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       28.32350            
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: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 1510 ANGSTROM**2                          
REMARK 350 TOTAL SURFACE AREA FOR THE COMPLEX: 17510 ANGSTROM**2                
REMARK 350 GAIN IN SOLVENT FREE ENERGY: -15.5 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   O    HOH A  2003  -  O    HOH A  2012              2.04            
REMARK 500   O    HOH A  2011  -  O    HOH A  2039              2.20            
REMARK 500   O    HOH A  2027  -  O    HOH A  2208              2.19            
REMARK 500   O    HOH A  2089  -  O    HOH A  2100              2.10            
REMARK 500   O    HOH A  2104  -  O    HOH A  2219              2.16            
REMARK 500   O    HOH A  2148  -  O    HOH A  2193              1.88            
REMARK 500   O    HOH A  2242  -  O    HOH A  2244              2.09            
REMARK 500   O    HOH F  2027  -  O    HOH F  2076              2.14            
REMARK 500   O    HOH F  2150  -  O    HOH F  2180              1.85            
REMARK 500   O    HOH F  2150  -  O    HOH F  2177              2.09            
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 A  96   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 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    ASN A  65       65.57   -155.15                                   
REMARK 500    ASN F  65       64.42   -157.61                                   
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 A1156  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 137.2                                              
REMARK 620 3 HIS A 120   NE2 100.2 114.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU F1156  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F 120   NE2                                                    
REMARK 620 2 HIS F  46   ND1  97.8                                              
REMARK 620 3 HIS F  48   NE2 113.5 140.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1157  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 110.5                                              
REMARK 620 3 HIS A 120   NE2  90.3 124.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1158  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  83   OD1                                                    
REMARK 620 2 HIS A  71   ND1  98.6                                              
REMARK 620 3 HIS A  63   ND1 107.1 106.0                                        
REMARK 620 4 HIS A  80   ND1 115.1 120.7 108.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1160  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  24   OE1                                                    
REMARK 620 2 SCN A1161   N   116.0                                              
REMARK 620 3 SCN A1162   N   104.3 108.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F1157  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F 120   NE2                                                    
REMARK 620 2 HIS F  46   ND1  91.4                                              
REMARK 620 3 HIS F  48   NE2 125.6 111.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F1158  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  80   ND1                                                    
REMARK 620 2 HIS F  63   ND1 109.2                                              
REMARK 620 3 HIS F  71   ND1 119.9 106.5                                        
REMARK 620 4 ASP F  83   OD1 115.0 106.3  98.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F1160  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU F  24   OE1                                                    
REMARK 620 2 SCN F1161   N   102.7                                              
REMARK 620 3 SCN F1162   N   116.3 110.4                                        
REMARK 620 N                    1     2                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU A1156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1157                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1158                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1159                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1160                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A1161                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A1162                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU F1156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN F1157                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN F1158                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F1159                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN F1160                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN F1161                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN F1162                 
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: 2VR6   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF G85R ALS MUTANT OF                             
REMARK 900  HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD)                          
REMARK 900  AT 1.3 A 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 900 RELATED ID: 2VR7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF G85R ALS MUTANT OF                             
REMARK 900  HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD)                          
REMARK 900  AT 1.58 A RESOLUTION                                                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 G85R MUTANT                                                          
DBREF  2VR8 A    0     0  PDB    2VR8     2VR8             0      0             
DBREF  2VR8 A    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  2VR8 F    0     0  PDB    2VR8     2VR8             0      0             
DBREF  2VR8 F    1   153  UNP    P00441   SODC_HUMAN       2    154             
SEQADV 2VR8 ARG A   85  UNP  P00441    GLY    86 ENGINEERED MUTATION            
SEQADV 2VR8 ARG F   85  UNP  P00441    GLY    86 ENGINEERED MUTATION            
SEQRES   1 A  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 A  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 A  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 A  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 A  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 A  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 A  154  GLU ARG HIS VAL GLY ASP LEU ARG ASN VAL THR ALA ASP          
SEQRES   8 A  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 A  154  ILE SER LEU SER GLY ASP HIS CSO ILE ILE GLY ARG THR          
SEQRES  10 A  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 A  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 A  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 F  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 F  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 F  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 F  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 F  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 F  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 F  154  GLU ARG HIS VAL GLY ASP LEU ARG ASN VAL THR ALA ASP          
SEQRES   8 F  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 F  154  ILE SER LEU SER GLY ASP HIS CSO ILE ILE GLY ARG THR          
SEQRES  10 F  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 F  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 F  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
MODRES 2VR8 CSO F  111  CYS  S-HYDROXYCYSTEINE                                  
MODRES 2VR8 CSO A  111  CYS  S-HYDROXYCYSTEINE                                  
HET    ACE  A   0       3                                                       
HET    CSO  A 111       7                                                       
HET     CU  A1156       1     MICROHETEROGENEITY                                
HET     ZN  A1157       1     MICROHETEROGENEITY                                
HET     ZN  A1158       1                                                       
HET    SO4  A1159       5                                                       
HET     ZN  A1160       1                                                       
HET    SCN  A1161       3                                                       
HET    SCN  A1162       3                                                       
HET    ACE  F   0       3                                                       
HET    CSO  F 111       7                                                       
HET     CU  F1156       1     MICROHETEROGENEITY                                
HET     ZN  F1157       1     MICROHETEROGENEITY                                
HET     ZN  F1158       1                                                       
HET    SO4  F1159       5                                                       
HET     ZN  F1160       1                                                       
HET    SCN  F1161       3                                                       
HET    SCN  F1162       3                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     SO4 SULFATE ION                                                      
HETNAM      ZN ZINC ION                                                         
HETNAM     CSO S-HYDROXYCYSTEINE                                                
HETNAM     SCN THIOCYANATE ION                                                  
FORMUL   3   CU    2(CU 2+)                                                     
FORMUL   4  ACE    2(C2 H4 O)                                                   
FORMUL   5  SO4    2(O4 S 2-)                                                   
FORMUL   6   ZN    6(ZN 2+)                                                     
FORMUL   7  CSO    2(C3 H7 N O3 S)                                              
FORMUL   8  SCN    4(C N S 1-)                                                  
FORMUL   9  HOH   *520(H2 O1)                                                   
HELIX    1   1 ALA A   55  GLY A   61  5                                   7    
HELIX    2   2 GLU A  133  GLY A  138  1                                   6    
HELIX    3   3 ALA F   55  GLY F   61  5                                   7    
HELIX    4   4 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  ALA A 152 -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 7 PHE F  45  HIS F  48  0                                        
SHEET    2  FA 7 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48           
SHEET    3  FA 7 ARG F 143  VAL F 148 -1  N  LEU F 144   O  VAL F 119           
SHEET    4  FA 7 THR F   2  GLY F  10 -1  O  LYS F   9   N  CYS F 146           
SHEET    5  FA 7 GLN F  15  GLN F  22 -1  O  GLY F  16   N  LEU F   8           
SHEET    6  FA 7 VAL F  29  LYS F  36 -1  O  LYS F  30   N  GLU F  21           
SHEET    7  FA 7 ALA F  95  ASP F 101 -1  O  ALA F  95   N  ILE F  35           
SHEET    1  FB 5 PHE F  45  HIS F  48  0                                        
SHEET    2  FB 5 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48           
SHEET    3  FB 5 ARG F 143  VAL F 148 -1  N  LEU F 144   O  VAL F 119           
SHEET    4  FB 5 THR F   2  GLY F  10 -1  O  LYS F   9   N  CYS F 146           
SHEET    5  FB 5 GLY F 150  ALA F 152 -1  O  GLY F 150   N  VAL F   5           
SHEET    1  FC 2 GLY F  41  HIS F  43  0                                        
SHEET    2  FC 2 VAL F  87  ALA F  89 -1  O  VAL F  87   N  HIS F  43           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.10  
SSBOND   2 CYS F   57    CYS F  146                          1555   1555  2.09  
LINK         N   ALA A   1                 C   ACE A   0     1555   1555  1.31  
LINK         C   HIS A 110                 N   CSO A 111     1555   1555  1.33  
LINK         C   CSO A 111                 N   ILE A 112     1555   1555  1.32  
LINK        CU  B CU A1156                 ND1 HIS A  46     1555   1555  1.78  
LINK        CU  B CU A1156                 NE2 HIS A  48     1555   1555  2.11  
LINK        CU  B CU A1156                 NE2 HIS A 120     1555   1555  2.11  
LINK        ZN  A ZN A1157                 ND1 HIS A  46     1555   1555  2.30  
LINK        ZN  A ZN A1157                 NE2 HIS A  48     1555   1555  2.10  
LINK        ZN  A ZN A1157                 NE2 HIS A 120     1555   1555  1.90  
LINK        ZN    ZN A1158                 OD1 ASP A  83     1555   1555  1.96  
LINK        ZN    ZN A1158                 ND1 HIS A  71     1555   1555  2.05  
LINK        ZN    ZN A1158                 ND1 HIS A  63     1555   1555  2.02  
LINK        ZN    ZN A1158                 ND1 HIS A  80     1555   1555  2.05  
LINK        ZN    ZN A1160                 OE1 GLU A  24     1555   1555  1.99  
LINK        ZN    ZN A1160                 N   SCN A1161     1555   1555  1.94  
LINK        ZN    ZN A1160                 N   SCN A1162     1555   1555  1.91  
LINK         N   ALA F   1                 C   ACE F   0     1555   1555  1.33  
LINK         C   HIS F 110                 N   CSO F 111     1555   1555  1.33  
LINK         C   CSO F 111                 N   ILE F 112     1555   1555  1.34  
LINK        CU  B CU F1156                 NE2 HIS F  48     1555   1555  2.07  
LINK        CU  B CU F1156                 ND1 HIS F  46     1555   1555  1.75  
LINK        CU  B CU F1156                 NE2 HIS F 120     1555   1555  2.23  
LINK        ZN  A ZN F1157                 NE2 HIS F  48     1555   1555  2.10  
LINK        ZN  A ZN F1157                 ND1 HIS F  46     1555   1555  2.26  
LINK        ZN  A ZN F1157                 NE2 HIS F 120     1555   1555  1.94  
LINK        ZN    ZN F1158                 OD1 ASP F  83     1555   1555  1.96  
LINK        ZN    ZN F1158                 ND1 HIS F  71     1555   1555  2.05  
LINK        ZN    ZN F1158                 ND1 HIS F  63     1555   1555  2.02  
LINK        ZN    ZN F1158                 ND1 HIS F  80     1555   1555  2.05  
LINK        ZN    ZN F1160                 N   SCN F1162     1555   1555  1.88  
LINK        ZN    ZN F1160                 N   SCN F1161     1555   1555  1.91  
LINK        ZN    ZN F1160                 OE1 GLU F  24     1555   1555  1.95  
SITE     1 AC1  6 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC1  6  ZN A1157  SO4 A1159                                          
SITE     1 AC2  7 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC2  7  CU A1156  SO4 A1159  HOH A2265                               
SITE     1 AC3  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC4 15 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC4 15 THR A 137  ARG A 143   CU A1156   ZN A1157                    
SITE     3 AC4 15 HOH A2241  HOH A2265  HOH A2266  HOH A2267                    
SITE     4 AC4 15 HOH A2268  HOH A2269  HOH A2270                               
SITE     1 AC5  3 GLU A  24  SCN A1161  SCN A1162                               
SITE     1 AC6  3 GLU A  24   ZN A1160  SCN A1162                               
SITE     1 AC7  3 GLU A  24   ZN A1160  SCN A1161                               
SITE     1 AC8  6 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     2 AC8  6  ZN F1157  SO4 F1159                                          
SITE     1 AC9  6 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     2 AC9  6  CU F1156  SO4 F1159                                          
SITE     1 BC1  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 BC2 13 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     2 BC2 13 THR F 137  ARG F 143   CU F1156   ZN F1157                    
SITE     3 BC2 13 HOH F2224  HOH F2246  HOH F2247  HOH F2248                    
SITE     4 BC2 13 HOH F2250                                                     
SITE     1 BC3  3 GLU F  24  SCN F1161  SCN F1162                               
SITE     1 BC4  3 GLU F  24   ZN F1160  SCN F1162                               
SITE     1 BC5  3 GLU F  24   ZN F1160  SCN F1161                               
CRYST1   34.210   56.647   74.714  90.00 102.14  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      0.029231  0.000000  0.006288        0.00000                         
SCALE2      0.000000  0.017653  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013691        0.00000                         
HETATM    1  C   ACE A   0     -10.988  -8.418  33.075  0.50 19.78           C  
ANISOU    1  C   ACE A   0     2487   2639   2388     63    222    -42       C  
HETATM    2  O   ACE A   0      -9.760  -8.544  33.074  0.50 21.05           O  
ANISOU    2  O   ACE A   0     2713   2851   2434     24    262    -66       O  
HETATM    3  CH3 ACE A   0     -11.749  -7.809  34.235  0.50 20.29           C  
ANISOU    3  CH3 ACE A   0     2554   2721   2434     40    252    -53       C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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