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Database: PDB
Entry: 3QQD
LinkDB: 3QQD
Original site: 3QQD 
HEADER    OXIDOREDUCTASE                          15-FEB-11   3QQD              
TITLE     HUMAN SOD1 H80R VARIANT, P212121 CRYSTAL FORM                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   9 CHAIN: B;                                                            
COMPND  10 EC: 1.15.1.1;                                                        
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 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: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: EGY118;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: YEP351-HSOD;                              
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: SOD1;                                                          
SOURCE  16 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: EGY118;                                    
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: YEP351-HSOD                               
KEYWDS    OXIDOREDUCTASE, HUMAN CU, ZN SUPEROXIDE DISMUTASE, ANTIOXIDANT,       
KEYWDS   2 METAL-BINDING, AMYOTROPHIC LATERAL SCLEROSIS, DISEASE MUTATION,      
KEYWDS   3 DISULFIDE BOND                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.V.SEETHARAMAN,D.D.WINKLER,A.B.TAYLOR,X.CAO,L.J.WHITSON,             
AUTHOR   2 P.A.DOUCETTE,J.S.VALENTINE,V.SCHIRF,B.DEMELER,M.C.CARROLL,           
AUTHOR   3 V.C.CULOTTA,P.J.HART                                                 
REVDAT   1   09-MAR-11 3QQD    0                                                
SPRSDE     09-MAR-11 3QQD      3H2R                                             
JRNL        AUTH   S.V.SEETHARAMAN,D.D.WINKLER,A.B.TAYLOR,X.CAO,L.J.WHITSON,    
JRNL        AUTH 2 P.A.DOUCETTE,J.S.VALENTINE,V.SCHIRF,B.DEMELER,M.C.CARROLL,   
JRNL        AUTH 3 V.C.CULOTTA,P.J.HART                                         
JRNL        TITL   DISRUPTED ZINC-BINDING SITES IN STRUCTURES OF PATHOGENIC     
JRNL        TITL 2 SOD1 VARIANTS D124V AND H80R.                                
JRNL        REF    BIOCHEMISTRY                  V.  49  5714 2010              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   20515040                                                     
JRNL        DOI    10.1021/BI100314N                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.02                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.320                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 30227                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.147                           
REMARK   3   R VALUE            (WORKING SET) : 0.144                           
REMARK   3   FREE R VALUE                     : 0.183                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1533                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 39.0257 -  3.6757    1.00     2770   171  0.1635 0.1928        
REMARK   3     2  3.6757 -  2.9178    1.00     2655   157  0.1530 0.1790        
REMARK   3     3  2.9178 -  2.5491    1.00     2628   144  0.1644 0.1839        
REMARK   3     4  2.5491 -  2.3160    1.00     2614   145  0.1469 0.1912        
REMARK   3     5  2.3160 -  2.1501    1.00     2614   125  0.1219 0.1820        
REMARK   3     6  2.1501 -  2.0233    1.00     2588   140  0.0996 0.1387        
REMARK   3     7  2.0233 -  1.9220    1.00     2585   144  0.1004 0.1409        
REMARK   3     8  1.9220 -  1.8383    1.00     2572   137  0.0967 0.1845        
REMARK   3     9  1.8383 -  1.7675    1.00     2585   129  0.1232 0.1997        
REMARK   3    10  1.7675 -  1.7065    0.99     2583   128  0.1546 0.2112        
REMARK   3    11  1.7065 -  1.6532    0.97     2500   113  0.2264 0.2737        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.41                                          
REMARK   3   B_SOL              : 40.00                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.040           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.81940                                             
REMARK   3    B22 (A**2) : 0.96620                                              
REMARK   3    B33 (A**2) : -0.58230                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           1862                                  
REMARK   3   ANGLE     :  0.913           2518                                  
REMARK   3   CHIRALITY :  0.063            287                                  
REMARK   3   PLANARITY :  0.003            332                                  
REMARK   3   DIHEDRAL  : 10.365            649                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3QQD COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063970.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-NOV-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.282                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30227                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.38500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.500                              
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 1AZV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.61                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.3 M AMMONIUM SULFATE, 0.1 M TRIS,      
REMARK 280  TEMPERATURE 298K, PH 8.0, VAPOR DIFFUSION, HANGING DROP             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       20.12250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.41250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.21350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.41250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.12250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       29.21350            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 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     ACE A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     LEU A    67                                                      
REMARK 465     SER A    68                                                      
REMARK 465     ARG A    69                                                      
REMARK 465     LYS A    70                                                      
REMARK 465     HIS A    71                                                      
REMARK 465     GLY A    72                                                      
REMARK 465     GLY A    73                                                      
REMARK 465     PRO A    74                                                      
REMARK 465     LYS A    75                                                      
REMARK 465     ASP A    76                                                      
REMARK 465     GLU A    77                                                      
REMARK 465     GLU A    78                                                      
REMARK 465     ARG A    79                                                      
REMARK 465     ASP A   125                                                      
REMARK 465     LEU A   126                                                      
REMARK 465     GLY A   127                                                      
REMARK 465     LYS A   128                                                      
REMARK 465     GLY A   129                                                      
REMARK 465     GLY A   130                                                      
REMARK 465     ASN A   131                                                      
REMARK 465     GLU A   132                                                      
REMARK 465     GLU A   133                                                      
REMARK 465     SER A   134                                                      
REMARK 465     THR A   135                                                      
REMARK 465     LYS A   136                                                      
REMARK 465     THR A   137                                                      
REMARK 465     GLY A   138                                                      
REMARK 465     ASN A   139                                                      
REMARK 465     ALA A   140                                                      
REMARK 465     ARG B    69                                                      
REMARK 465     LYS B    70                                                      
REMARK 465     HIS B    71                                                      
REMARK 465     GLY B    72                                                      
REMARK 465     GLY B    73                                                      
REMARK 465     PRO B    74                                                      
REMARK 465     LYS B    75                                                      
REMARK 465     ASP B    76                                                      
REMARK 465     GLU B    77                                                      
REMARK 465     GLU B    78                                                      
REMARK 465     ARG B    79                                                      
REMARK 465     ASP B   125                                                      
REMARK 465     LEU B   126                                                      
REMARK 465     GLY B   127                                                      
REMARK 465     LYS B   128                                                      
REMARK 465     GLY B   129                                                      
REMARK 465     GLY B   130                                                      
REMARK 465     ASN B   131                                                      
REMARK 465     GLU B   132                                                      
REMARK 465     GLU B   133                                                      
REMARK 465     SER B   134                                                      
REMARK 465     THR B   135                                                      
REMARK 465     LYS B   136                                                      
REMARK 465     THR B   137                                                      
REMARK 465     GLY B   138                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  65       75.46   -160.51                                   
REMARK 500    ASN B  65       75.92   -164.02                                   
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                              ZN A 154  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 133.6                                              
REMARK 620 3 HIS A 120   NE2  96.5  99.1                                        
REMARK 620 4 HIS A  63   NE2  84.6 107.6 141.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 154  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  46   ND1                                                    
REMARK 620 2 HIS B  48   NE2 134.0                                              
REMARK 620 3 HIS B 120   NE2 100.3 105.7                                        
REMARK 620 4 SO4 B 155   O1   90.9 107.5 119.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE B 0                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 155                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3H2P   RELATED DB: PDB                                   
REMARK 900 HUMAN SOD1 D124V VARIANT                                             
REMARK 900 RELATED ID: 3H2Q   RELATED DB: PDB                                   
REMARK 900 HUMAN SOD1 H80R VARIANT, P21 CRYSTAL FORM                            
DBREF  3QQD A    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3QQD B    1   153  UNP    P00441   SODC_HUMAN       2    154             
SEQADV 3QQD ACE A    0  UNP  P00441              ACETYLATION                    
SEQADV 3QQD ARG A   80  UNP  P00441    HIS    81 ENGINEERED MUTATION            
SEQADV 3QQD ACE B    0  UNP  P00441              ACETYLATION                    
SEQADV 3QQD ARG B   80  UNP  P00441    HIS    81 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 ARG VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 A  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 A  154  ILE SER LEU SER GLY ASP HIS OCS 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 B  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 B  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 B  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 B  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 B  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 B  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 B  154  GLU ARG ARG VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 B  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 B  154  ILE SER LEU SER GLY ASP HIS CSX ILE ILE GLY ARG THR          
SEQRES  10 B  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 B  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 B  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
MODRES 3QQD OCS A  111  CYS  CYSTEINESULFONIC ACID                              
MODRES 3QQD CSX B  111  CYS  S-OXY CYSTEINE                                     
HET    OCS  A 111       9                                                       
HET    ACE  B   0       3                                                       
HET    CSX  B 111       7                                                       
HET     ZN  A 154       1                                                       
HET    SO4  A 155       5                                                       
HET     ZN  B 154       1                                                       
HET    SO4  B 155       5                                                       
HETNAM     OCS CYSTEINESULFONIC ACID                                            
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     CSX S-OXY CYSTEINE                                                   
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  OCS    C3 H7 N O5 S                                                 
FORMUL   2  ACE    C2 H4 O                                                      
FORMUL   2  CSX    C3 H7 N O3 S                                                 
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  SO4    2(O4 S 2-)                                                   
FORMUL   7  HOH   *188(H2 O)                                                    
HELIX    1   1 ALA A   55  GLY A   61  5                                   7    
HELIX    2   2 SER A  107  OCS A  111  5                                   5    
HELIX    3   3 ALA B   55  ALA B   60  5                                   6    
SHEET    1   A 9 ARG A 143  VAL A 148  0                                        
SHEET    2   A 9 THR A 116  HIS A 120 -1  N  LEU A 117   O  GLY A 147           
SHEET    3   A 9 GLY A  41  HIS A  48 -1  N  HIS A  48   O  THR A 116           
SHEET    4   A 9 ASP A  83  ALA A  89 -1  O  ALA A  89   N  GLY A  41           
SHEET    5   A 9 ALA A  95  ASP A 101 -1  O  ASP A  96   N  THR A  88           
SHEET    6   A 9 VAL A  29  LYS A  36 -1  N  VAL A  29   O  ASP A 101           
SHEET    7   A 9 GLN A  15  GLU A  21 -1  N  ASN A  19   O  TRP A  32           
SHEET    8   A 9 LYS A   3  LEU A   8 -1  N  CYS A   6   O  ILE A  18           
SHEET    9   A 9 GLY A 150  ILE A 151 -1  O  GLY A 150   N  VAL A   5           
SHEET    1   B 5 ALA B  95  ASP B 101  0                                        
SHEET    2   B 5 VAL B  29  LYS B  36 -1  N  ILE B  35   O  ALA B  95           
SHEET    3   B 5 GLN B  15  GLU B  21 -1  N  ASN B  19   O  TRP B  32           
SHEET    4   B 5 LYS B   3  LEU B   8 -1  N  LEU B   8   O  GLY B  16           
SHEET    5   B 5 GLY B 150  ILE B 151 -1  O  GLY B 150   N  VAL B   5           
SHEET    1   C 4 ASP B  83  ALA B  89  0                                        
SHEET    2   C 4 GLY B  41  HIS B  48 -1  N  GLY B  41   O  ALA B  89           
SHEET    3   C 4 THR B 116  HIS B 120 -1  O  THR B 116   N  HIS B  48           
SHEET    4   C 4 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  2.79  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.78  
LINK         C   HIS A 110                 N   OCS A 111     1555   1555  1.33  
LINK         C   OCS A 111                 N   ILE A 112     1555   1555  1.33  
LINK         C   HIS B 110                 N   CSX B 111     1555   1555  1.33  
LINK         C   CSX B 111                 N   ILE B 112     1555   1555  1.33  
LINK         ND1 HIS A  46                ZN    ZN A 154     1555   1555  2.27  
LINK         NE2 HIS A  48                ZN    ZN A 154     1555   1555  2.25  
LINK         NE2 HIS A 120                ZN    ZN A 154     1555   1555  2.11  
LINK         ND1 HIS B  46                ZN    ZN B 154     1555   1555  2.14  
LINK         NE2 HIS B  48                ZN    ZN B 154     1555   1555  2.13  
LINK         NE2 HIS B 120                ZN    ZN B 154     1555   1555  2.10  
LINK        ZN    ZN B 154                 O1  SO4 B 155     1555   1555  2.17  
LINK         N   ALA B   1                 C   ACE B   0     1555   1555  1.33  
LINK         NE2 HIS A  63                ZN    ZN A 154     1555   1555  2.44  
SITE     1 AC1  5 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC1  5 SO4 A 155                                                     
SITE     1 AC2  5 HIS A  48  HIS A  63  HIS A 120  ARG A 143                    
SITE     2 AC2  5  ZN A 154                                                     
SITE     1 AC3  2 ALA B   1  THR B   2                                          
SITE     1 AC4  4 HIS B  46  HIS B  48  HIS B 120  SO4 B 155                    
SITE     1 AC5  7 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     2 AC5  7  ZN B 154  HOH B 227  HOH B 250                               
CRYST1   40.245   58.427  104.825  90.00  90.00  90.00 P 21 21 21    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      0.024848  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017115  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009540        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system