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Database: PDB
Entry: 2ZKW
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Original site: 2ZKW 
HEADER    OXIDOREDUCTASE                          31-MAR-08   2ZKW              
TITLE     CRYSTAL STRUCTURE OF HUMAN CU-ZN SUPEROXIDE DISMUTASE MUTANT G85R IN  
TITLE    2 SPACE GROUP P21                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SOD1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX6P                                    
KEYWDS    OXIDOREDUCTASE, HUMAN CU-ZN SUPEROXIDE DISMUTASE, ALS, FALS, METAL-   
KEYWDS   2 BINDING, DISEASE MUTATION, E.C.1.15.1.1, AMYOTROPHIC LATERAL         
KEYWDS   3 SCLEROSIS, ANTIOXIDANT, STRUCTURAL GENOMICS, NPPSFA, NATIONAL        
KEYWDS   4 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN         
KEYWDS   5 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.YOSHIKAWA,M.KUKIMOTO-NIINO,K.ITO,L.CHEN,Z.Q.FU,J.CHRZAS,B.C.WANG,   
AUTHOR   2 M.SHIROUZU,M.URUSHITANI,R.TAKAHASHI,S.YOKOYAMA,RIKEN STRUCTURAL      
AUTHOR   3 GENOMICS/PROTEOMICS INITIATIVE (RSGI)                                
REVDAT   2   04-APR-12 2ZKW    1       SPRSDE VERSN                             
REVDAT   1   24-MAR-09 2ZKW    0                                                
SPRSDE     04-APR-12 2ZKW      2YQV                                             
JRNL        AUTH   S.YOSHIKAWA,M.KUKIMOTO-NIINO,K.ITO,L.CHEN,Z.Q.FU,J.CHRZAS,   
JRNL        AUTH 2 B.C.WANG,M.SHIROUZU,M.URUSHITANI,R.TAKAHASHI,S.YOKOYAMA      
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN CU-ZN SUPEROXIDE DISMUTASE MUTANT 
JRNL        TITL 2 G85R IN SPACE GROUP P21                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.46                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 185773.230                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 17328                          
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 SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1707                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2226                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2240                       
REMARK   3   BIN FREE R VALUE                    : 0.2940                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 242                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2151                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 46                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 10.66000                                             
REMARK   3    B22 (A**2) : -1.89000                                             
REMARK   3    B33 (A**2) : -8.76000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 6.01000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.13                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.28                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.16                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.94                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 4.440 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 5.490 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 6.830 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 8.760 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.42                                                 
REMARK   3   BSOL        : 54.25                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2ZKW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-APR-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB028100.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-JAN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17839                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 3.583                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.3670                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.26400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.250                              
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 1HL5                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 31.54                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM IODIDE, 20%(W/V)           
REMARK 280  PEG3350, PH 6.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K    
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       23.11650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.1 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     LEU A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     LYS A    23                                                      
REMARK 465     GLU A    24                                                      
REMARK 465     GLN A   153                                                      
REMARK 465     GLY B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     LEU B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     MET B     0                                                      
REMARK 465     LYS B    23                                                      
REMARK 465     GLU B    24                                                      
REMARK 465     SER B    25                                                      
REMARK 465     THR B    54                                                      
REMARK 465     ALA B    55                                                      
REMARK 465     GLY B    56                                                      
REMARK 465     GLN B   153                                                      
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   OE1  GLU B    78     OE2  GLU B   121     2547     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A 110       22.51    -75.25                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 A 301  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 138.9                                              
REMARK 620 3 HIS A 120   NE2  97.9 121.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  63   ND1                                                    
REMARK 620 2 HIS A  71   ND1 101.3                                              
REMARK 620 3 HIS A  80   ND1 110.6 123.0                                        
REMARK 620 4 ASP A  83   OD1  98.2  97.4 122.1                                  
REMARK 620 5 ASP A  83   OD2 150.9  76.3  94.1  54.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 B 302  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  46   ND1                                                    
REMARK 620 2 HIS B  48   NE2 139.0                                              
REMARK 620 3 HIS B 120   NE2 100.4 120.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  63   ND1                                                    
REMARK 620 2 HIS B  71   ND1 101.5                                              
REMARK 620 3 HIS B  80   ND1 112.4 121.5                                        
REMARK 620 4 ASP B  83   OD1 105.6 102.6 111.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 402                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ZKX   RELATED DB: PDB                                   
REMARK 900 HUMAN CU-ZN SUPEROXIDE DISMUTASE MUTANT G85R IN SPACE GROUP          
REMARK 900 I212121                                                              
REMARK 900 RELATED ID: 2ZKY   RELATED DB: PDB                                   
REMARK 900 HUMAN CU-ZN SUPEROXIDE DISMUTASE MUTANT G93A                         
REMARK 900 RELATED ID: AR_001000134.2   RELATED DB: TARGETDB                    
DBREF  2ZKW A    0   153  UNP    P00441   SODC_HUMAN       1    154             
DBREF  2ZKW B    0   153  UNP    P00441   SODC_HUMAN       1    154             
SEQADV 2ZKW GLY A   -5  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKW PRO A   -4  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKW LEU A   -3  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKW GLY A   -2  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKW SER A   -1  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKW ARG A   85  UNP  P00441    GLY    86 ENGINEERED                     
SEQADV 2ZKW GLY B   -5  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKW PRO B   -4  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKW LEU B   -3  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKW GLY B   -2  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKW SER B   -1  UNP  P00441              EXPRESSION TAG                 
SEQADV 2ZKW ARG B   85  UNP  P00441    GLY    86 ENGINEERED                     
SEQRES   1 A  159  GLY PRO LEU GLY SER MET ALA THR LYS ALA VAL CYS VAL          
SEQRES   2 A  159  LEU LYS GLY ASP GLY PRO VAL GLN GLY ILE ILE ASN PHE          
SEQRES   3 A  159  GLU GLN LYS GLU SER ASN GLY PRO VAL LYS VAL TRP GLY          
SEQRES   4 A  159  SER ILE LYS GLY LEU THR GLU GLY LEU HIS GLY PHE HIS          
SEQRES   5 A  159  VAL HIS GLU PHE GLY ASP ASN THR ALA GLY CYS THR SER          
SEQRES   6 A  159  ALA GLY PRO HIS PHE ASN PRO LEU SER ARG LYS HIS GLY          
SEQRES   7 A  159  GLY PRO LYS ASP GLU GLU ARG HIS VAL GLY ASP LEU ARG          
SEQRES   8 A  159  ASN VAL THR ALA ASP LYS ASP GLY VAL ALA ASP VAL SER          
SEQRES   9 A  159  ILE GLU ASP SER VAL ILE SER LEU SER GLY ASP HIS CYS          
SEQRES  10 A  159  ILE ILE GLY ARG THR LEU VAL VAL HIS GLU LYS ALA ASP          
SEQRES  11 A  159  ASP LEU GLY LYS GLY GLY ASN GLU GLU SER THR LYS THR          
SEQRES  12 A  159  GLY ASN ALA GLY SER ARG LEU ALA CYS GLY VAL ILE GLY          
SEQRES  13 A  159  ILE ALA GLN                                                  
SEQRES   1 B  159  GLY PRO LEU GLY SER MET ALA THR LYS ALA VAL CYS VAL          
SEQRES   2 B  159  LEU LYS GLY ASP GLY PRO VAL GLN GLY ILE ILE ASN PHE          
SEQRES   3 B  159  GLU GLN LYS GLU SER ASN GLY PRO VAL LYS VAL TRP GLY          
SEQRES   4 B  159  SER ILE LYS GLY LEU THR GLU GLY LEU HIS GLY PHE HIS          
SEQRES   5 B  159  VAL HIS GLU PHE GLY ASP ASN THR ALA GLY CYS THR SER          
SEQRES   6 B  159  ALA GLY PRO HIS PHE ASN PRO LEU SER ARG LYS HIS GLY          
SEQRES   7 B  159  GLY PRO LYS ASP GLU GLU ARG HIS VAL GLY ASP LEU ARG          
SEQRES   8 B  159  ASN VAL THR ALA ASP LYS ASP GLY VAL ALA ASP VAL SER          
SEQRES   9 B  159  ILE GLU ASP SER VAL ILE SER LEU SER GLY ASP HIS CYS          
SEQRES  10 B  159  ILE ILE GLY ARG THR LEU VAL VAL HIS GLU LYS ALA ASP          
SEQRES  11 B  159  ASP LEU GLY LYS GLY GLY ASN GLU GLU SER THR LYS THR          
SEQRES  12 B  159  GLY ASN ALA GLY SER ARG LEU ALA CYS GLY VAL ILE GLY          
SEQRES  13 B  159  ILE ALA GLN                                                  
HET    CU1  A 301       1                                                       
HET     ZN  A 401       1                                                       
HET    CU1  B 302       1                                                       
HET     ZN  B 402       1                                                       
HETNAM     CU1 COPPER (I) ION                                                   
HETNAM      ZN ZINC ION                                                         
FORMUL   3  CU1    2(CU 1+)                                                     
FORMUL   4   ZN    2(ZN 2+)                                                     
FORMUL   7  HOH   *46(H2 O)                                                     
HELIX    1   1 ALA A   55  GLY A   61  5                                   7    
HELIX    2   2 GLU A  132  LYS A  136  5                                   5    
HELIX    3   3 CYS B   57  GLY B   61  5                                   5    
HELIX    4   4 SER B  107  CYS B  111  5                                   5    
HELIX    5   5 GLU B  132  LYS B  136  5                                   5    
SHEET    1   A 5 ALA A  95  ASP A 101  0                                        
SHEET    2   A 5 VAL A  29  LYS A  36 -1  N  VAL A  31   O  ILE A  99           
SHEET    3   A 5 GLN A  15  GLU A  21 -1  N  ASN A  19   O  TRP A  32           
SHEET    4   A 5 LYS A   3  LYS A   9 -1  N  ALA A   4   O  PHE A  20           
SHEET    5   A 5 GLY A 150  ILE A 151 -1  O  GLY A 150   N  VAL A   5           
SHEET    1   B 2 GLY A  41  HIS A  43  0                                        
SHEET    2   B 2 VAL A  87  ALA A  89 -1  O  VAL A  87   N  HIS A  43           
SHEET    1   C 3 PHE A  45  HIS A  48  0                                        
SHEET    2   C 3 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    3   C 3 ARG A 143  VAL A 148 -1  O  GLY A 147   N  LEU A 117           
SHEET    1   D 5 ALA B  95  ASP B 101  0                                        
SHEET    2   D 5 VAL B  29  LYS B  36 -1  N  GLY B  33   O  VAL B  97           
SHEET    3   D 5 GLN B  15  GLN B  22 -1  N  ASN B  19   O  TRP B  32           
SHEET    4   D 5 THR B   2  LYS B   9 -1  N  ALA B   4   O  PHE B  20           
SHEET    5   D 5 GLY B 150  ILE B 151 -1  O  GLY B 150   N  VAL B   5           
SHEET    1   E 2 GLY B  41  HIS B  43  0                                        
SHEET    2   E 2 VAL B  87  ALA B  89 -1  O  VAL B  87   N  HIS B  43           
SHEET    1   F 3 PHE B  45  HIS B  48  0                                        
SHEET    2   F 3 THR B 116  HIS B 120 -1  O  THR B 116   N  HIS B  48           
SHEET    3   F 3 ARG B 143  VAL B 148 -1  O  GLY B 147   N  LEU B 117           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.05  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.07  
LINK         ND1 HIS A  46                CU   CU1 A 301     1555   1555  1.94  
LINK         NE2 HIS A  48                CU   CU1 A 301     1555   1555  2.01  
LINK         ND1 HIS A  63                ZN    ZN A 401     1555   1555  2.11  
LINK         ND1 HIS A  71                ZN    ZN A 401     1555   1555  1.97  
LINK         ND1 HIS A  80                ZN    ZN A 401     1555   1555  1.93  
LINK         OD1 ASP A  83                ZN    ZN A 401     1555   1555  2.03  
LINK         NE2 HIS A 120                CU   CU1 A 301     1555   1555  2.09  
LINK         ND1 HIS B  46                CU   CU1 B 302     1555   1555  2.07  
LINK         NE2 HIS B  48                CU   CU1 B 302     1555   1555  1.93  
LINK         ND1 HIS B  63                ZN    ZN B 402     1555   1555  1.96  
LINK         ND1 HIS B  71                ZN    ZN B 402     1555   1555  2.00  
LINK         ND1 HIS B  80                ZN    ZN B 402     1555   1555  2.16  
LINK         OD1 ASP B  83                ZN    ZN B 402     1555   1555  2.07  
LINK         NE2 HIS B 120                CU   CU1 B 302     1555   1555  2.11  
LINK         OD2 ASP A  83                ZN    ZN A 401     1555   1555  2.69  
SITE     1 AC1  4 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     1 AC2  4 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     1 AC3  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC4  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
CRYST1   48.616   46.233   52.818  90.00  94.42  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      0.020569  0.000000  0.001588        0.00000                         
SCALE2      0.000000  0.021630  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018989        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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