GenomeNet

Database: PDB
Entry: 3H2Q
LinkDB: 3H2Q
Original site: 3H2Q 
HEADER    OXIDOREDUCTASE                          14-APR-09   3H2Q              
TITLE     HUMAN SOD1 H80R VARIANT, P21 CRYSTAL FORM                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B, C, D;                                                   
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: 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                               
KEYWDS    OXIDOREDUCTASE, HUMAN CU, ZN SUPEROXIDE DISMUTASE, ANTIOXIDANT,       
KEYWDS   2 METAL-BINDING, COPPER, ZINC, AMYOTROPHIC LATERAL SCLEROSIS, DISEASE  
KEYWDS   3 MUTATION, ACETYLATION, CYTOPLASM, DISULFIDE BOND, PHOSPHOPROTEIN,    
KEYWDS   4 UBL CONJUGATION                                                      
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,M.C.CARROLL,V.C.CULOTTA,P.J.HART          
REVDAT   1   05-MAY-10 3H2Q    0                                                
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,M.C.CARROLL,V.C.CULOTTA,P.J.HART  
JRNL        TITL   STRUCTURES OF PATHOGENIC SOD1 MUTANTS H80R AND D124V:        
JRNL        TITL 2 DISRUPTED ZINC-BINDING AND COMPROMISED POST-TRANSLATIONAL    
JRNL        TITL 3 MODIFICATION BY THE COPPER CHAPERONE CCS                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.34                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 41462                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.950                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2052                            
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 25.3373 -  4.5543    1.00     2800   155  0.1700 0.1808        
REMARK   3     2  4.5543 -  3.6182    0.89     2495   134  0.1483 0.1815        
REMARK   3     3  3.6182 -  3.1618    0.78     2158   114  0.1692 0.2029        
REMARK   3     4  3.1618 -  2.8732    0.98     2750   156  0.1928 0.2554        
REMARK   3     5  2.8732 -  2.6675    0.98     2700   147  0.2022 0.2602        
REMARK   3     6  2.6675 -  2.5104    0.98     2730   136  0.1992 0.2540        
REMARK   3     7  2.5104 -  2.3847    0.97     2697   146  0.1807 0.2020        
REMARK   3     8  2.3847 -  2.2810    0.95     2653   130  0.1754 0.2331        
REMARK   3     9  2.2810 -  2.1932    0.96     2653   143  0.1717 0.2508        
REMARK   3    10  2.1932 -  2.1176    0.95     2633   160  0.1731 0.2247        
REMARK   3    11  2.1176 -  2.0514    0.95     2616   124  0.1650 0.2242        
REMARK   3    12  2.0514 -  1.9928    0.95     2640   135  0.1649 0.2246        
REMARK   3    13  1.9928 -  1.9404    0.95     2624   113  0.1839 0.2246        
REMARK   3    14  1.9404 -  1.8930    0.94     2656   139  0.1852 0.2682        
REMARK   3    15  1.8930 -  1.8500    0.94     2605   120  0.1957 0.2464        
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              : 0.42                                          
REMARK   3   B_SOL              : 59.55                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.99                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.90510                                             
REMARK   3    B22 (A**2) : -4.68550                                             
REMARK   3    B33 (A**2) : -4.24160                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.61440                                              
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      :  0.006           NULL                                  
REMARK   3   ANGLE     :  1.040           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
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 3H2Q COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB052617.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-FEB-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-D                        
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : CONFOCAL OPTICS                    
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS VII                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41506                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.53100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
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: 1AZV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.3 M AMMONIUM SULFATE, 0.1 M TRIS, PH   
REMARK 280  8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
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       68.40050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 2030 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -124.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 2070 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -122.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     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     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     LEU B    67                                                      
REMARK 465     SER B    68                                                      
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     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 465     ASN B   139                                                      
REMARK 465     LEU C    67                                                      
REMARK 465     SER C    68                                                      
REMARK 465     ARG C    69                                                      
REMARK 465     LYS C    70                                                      
REMARK 465     HIS C    71                                                      
REMARK 465     GLY C    72                                                      
REMARK 465     GLY C    73                                                      
REMARK 465     PRO C    74                                                      
REMARK 465     LYS C    75                                                      
REMARK 465     ASP C    76                                                      
REMARK 465     GLU C    77                                                      
REMARK 465     GLU C    78                                                      
REMARK 465     ARG C    79                                                      
REMARK 465     ASP C   125                                                      
REMARK 465     LEU C   126                                                      
REMARK 465     GLY C   127                                                      
REMARK 465     LYS C   128                                                      
REMARK 465     GLY C   129                                                      
REMARK 465     GLY C   130                                                      
REMARK 465     ASN C   131                                                      
REMARK 465     GLU C   132                                                      
REMARK 465     GLU C   133                                                      
REMARK 465     SER C   134                                                      
REMARK 465     THR C   135                                                      
REMARK 465     LYS C   136                                                      
REMARK 465     THR C   137                                                      
REMARK 465     GLY C   138                                                      
REMARK 465     ASN C   139                                                      
REMARK 465     ALA C   140                                                      
REMARK 465     LEU D    67                                                      
REMARK 465     SER D    68                                                      
REMARK 465     ARG D    69                                                      
REMARK 465     LYS D    70                                                      
REMARK 465     HIS D    71                                                      
REMARK 465     GLY D    72                                                      
REMARK 465     GLY D    73                                                      
REMARK 465     PRO D    74                                                      
REMARK 465     LYS D    75                                                      
REMARK 465     ASP D    76                                                      
REMARK 465     GLU D    77                                                      
REMARK 465     GLU D    78                                                      
REMARK 465     LEU D   126                                                      
REMARK 465     GLY D   127                                                      
REMARK 465     LYS D   128                                                      
REMARK 465     GLY D   129                                                      
REMARK 465     GLY D   130                                                      
REMARK 465     ASN D   131                                                      
REMARK 465     GLU D   132                                                      
REMARK 465     GLU D   133                                                      
REMARK 465     SER D   134                                                      
REMARK 465     THR D   135                                                      
REMARK 465     LYS D   136                                                      
REMARK 465     THR D   137                                                      
REMARK 465     GLY D   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    HIS B  63      128.81    -39.33                                   
REMARK 500    ASN B  65       87.35   -164.83                                   
REMARK 500    ASN C  65       80.06   -161.03                                   
REMARK 500    SER C  98       88.82   -159.04                                   
REMARK 500    ASN D  65       88.68   -162.03                                   
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 128.7                                              
REMARK 620 3 HIS A 120   NE2  99.8 107.6                                        
REMARK 620 4 SO4 A 155   O3  112.9  96.1 111.8                                  
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 130.0                                              
REMARK 620 3 HIS B 120   NE2  97.1  98.8                                        
REMARK 620 4 SO4 B 155   S   104.4 118.0 101.7                                  
REMARK 620 5 SO4 B 155   O4   96.7 107.1 131.3  29.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 154  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  63   NE2                                                    
REMARK 620 2 HIS C 120   NE2 162.1                                              
REMARK 620 3 HIS C  48   NE2 110.1  82.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 154  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  46   ND1                                                    
REMARK 620 2 HIS D  48   NE2 127.8                                              
REMARK 620 3 HIS D 120   NE2 102.0 104.1                                        
REMARK 620 4 SO4 D 155   S   104.1 110.7 106.4                                  
REMARK 620 5 SO4 D 155   O1   90.8  98.9 137.7  31.5                            
REMARK 620 N                    1     2     3     4                             
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 ZN B 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 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: 3H2R   RELATED DB: PDB                                   
REMARK 900 HUMAN SOD1 H80R VARIANT, P212121 CRYSTAL FORM                        
DBREF  3H2Q A    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3H2Q B    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3H2Q C    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3H2Q D    1   153  UNP    P00441   SODC_HUMAN       2    154             
SEQADV 3H2Q ARG A   80  UNP  P00441    HIS    81 ENGINEERED                     
SEQADV 3H2Q ARG B   80  UNP  P00441    HIS    81 ENGINEERED                     
SEQADV 3H2Q ARG C   80  UNP  P00441    HIS    81 ENGINEERED                     
SEQADV 3H2Q ARG D   80  UNP  P00441    HIS    81 ENGINEERED                     
SEQRES   1 A  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 A  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 A  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 A  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 A  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 A  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 A  153  ARG ARG VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 A  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 A  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 A  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 A  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 A  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 B  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 B  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 B  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 B  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 B  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 B  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 B  153  ARG ARG VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 B  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 B  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 B  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 B  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 B  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 C  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 C  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 C  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 C  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 C  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 C  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 C  153  ARG ARG VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 C  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 C  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 C  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 C  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 C  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 D  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 D  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 D  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 D  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 D  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 D  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 D  153  ARG ARG VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 D  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 D  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 D  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 D  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 D  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
HET     ZN  A 154       1                                                       
HET    SO4  A 155       5                                                       
HET     ZN  B 154       1                                                       
HET    SO4  B 155      10                                                       
HET     ZN  C 154       1                                                       
HET    SO4  C 155       5                                                       
HET     ZN  D 154       1                                                       
HET    SO4  D 155       5                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   6  SO4    4(O4 S 2-)                                                   
FORMUL  13  HOH   *369(H2 O)                                                    
HELIX    1   1 CYS A   57  GLY A   61  5                                   5    
HELIX    2   2 ALA B   55  GLY B   61  5                                   7    
HELIX    3   3 SER B  107  CYS B  111  5                                   5    
HELIX    4   4 ALA C   55  GLY C   61  5                                   7    
HELIX    5   5 SER C  107  CYS C  111  5                                   5    
HELIX    6   6 CYS D   57  GLY D   61  5                                   5    
HELIX    7   7 SER D  107  CYS D  111  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  ILE A  35   O  ALA A  95           
SHEET    3   A 5 GLN A  15  GLN A  22 -1  N  ASN A  19   O  TRP A  32           
SHEET    4   A 5 THR A   2  LEU A   8 -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 4 ASP A  83  ALA A  89  0                                        
SHEET    2   B 4 GLY A  41  HIS A  48 -1  N  HIS A  43   O  VAL A  87           
SHEET    3   B 4 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    4   B 4 ARG A 143  VAL A 148 -1  O  ALA A 145   N  VAL A 119           
SHEET    1   C 5 ALA B  95  ASP B 101  0                                        
SHEET    2   C 5 VAL B  29  LYS B  36 -1  N  ILE B  35   O  ALA B  95           
SHEET    3   C 5 GLN B  15  GLU B  21 -1  N  ASN B  19   O  TRP B  32           
SHEET    4   C 5 LYS B   3  LEU B   8 -1  N  CYS B   6   O  ILE B  18           
SHEET    5   C 5 GLY B 150  ILE B 151 -1  O  GLY B 150   N  VAL B   5           
SHEET    1   D 4 ASP B  83  ALA B  89  0                                        
SHEET    2   D 4 GLY B  41  HIS B  48 -1  N  GLY B  41   O  ALA B  89           
SHEET    3   D 4 THR B 116  HIS B 120 -1  O  THR B 116   N  HIS B  48           
SHEET    4   D 4 ARG B 143  VAL B 148 -1  O  GLY B 147   N  LEU B 117           
SHEET    1   E 5 ALA C  95  ASP C 101  0                                        
SHEET    2   E 5 VAL C  29  LYS C  36 -1  N  VAL C  31   O  ILE C  99           
SHEET    3   E 5 GLN C  15  GLN C  22 -1  N  ASN C  19   O  TRP C  32           
SHEET    4   E 5 THR C   2  LEU C   8 -1  N  ALA C   4   O  PHE C  20           
SHEET    5   E 5 GLY C 150  ALA C 152 -1  O  GLY C 150   N  VAL C   5           
SHEET    1   F 4 ASP C  83  ALA C  89  0                                        
SHEET    2   F 4 GLY C  41  HIS C  48 -1  N  GLY C  41   O  ALA C  89           
SHEET    3   F 4 THR C 116  HIS C 120 -1  O  THR C 116   N  HIS C  48           
SHEET    4   F 4 ARG C 143  VAL C 148 -1  O  GLY C 147   N  LEU C 117           
SHEET    1   G 5 ALA D  95  ASP D 101  0                                        
SHEET    2   G 5 VAL D  29  LYS D  36 -1  N  ILE D  35   O  ALA D  95           
SHEET    3   G 5 GLN D  15  GLU D  21 -1  N  ASN D  19   O  TRP D  32           
SHEET    4   G 5 LYS D   3  LEU D   8 -1  N  ALA D   4   O  PHE D  20           
SHEET    5   G 5 GLY D 150  ILE D 151 -1  O  GLY D 150   N  VAL D   5           
SHEET    1   H 4 ASP D  83  ALA D  89  0                                        
SHEET    2   H 4 GLY D  41  HIS D  48 -1  N  HIS D  43   O  VAL D  87           
SHEET    3   H 4 THR D 116  HIS D 120 -1  O  THR D 116   N  HIS D  48           
SHEET    4   H 4 ARG D 143  VAL D 148 -1  O  ALA D 145   N  VAL D 119           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.42  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.47  
SSBOND   3 CYS C   57    CYS C  146                          1555   1555  2.51  
SSBOND   4 CYS D   57    CYS D  146                          1555   1555  2.56  
LINK         ND1 HIS A  46                ZN    ZN A 154     1555   1555  2.08  
LINK         NE2 HIS A  48                ZN    ZN A 154     1555   1555  2.14  
LINK         NE2 HIS A 120                ZN    ZN A 154     1555   1555  2.06  
LINK         ND1 HIS B  46                ZN    ZN B 154     1555   1555  2.30  
LINK         NE2 HIS B  48                ZN    ZN B 154     1555   1555  2.27  
LINK         NE2 HIS B 120                ZN    ZN B 154     1555   1555  2.11  
LINK         NE2 HIS C  63                ZN    ZN C 154     1555   1555  2.31  
LINK         NE2 HIS C 120                ZN    ZN C 154     1555   1555  2.18  
LINK         ND1 HIS D  46                ZN    ZN D 154     1555   1555  2.19  
LINK         NE2 HIS D  48                ZN    ZN D 154     1555   1555  2.12  
LINK         NE2 HIS D 120                ZN    ZN D 154     1555   1555  2.14  
LINK        ZN    ZN A 154                 O3  SO4 A 155     1555   1555  1.92  
LINK        ZN    ZN B 154                 S  ASO4 B 155     1555   1555  2.96  
LINK        ZN    ZN D 154                 S   SO4 D 155     1555   1555  2.78  
LINK        ZN    ZN D 154                 O1  SO4 D 155     1555   1555  2.24  
LINK        ZN    ZN B 154                 O4 ASO4 B 155     1555   1555  2.47  
LINK         NE2 HIS C  48                ZN    ZN C 154     1555   1555  2.55  
SITE     1 AC1  4 HIS A  46  HIS A  48  HIS A 120  SO4 A 155                    
SITE     1 AC2 10 HIS A  46  HIS A  48  HIS A  63  ARG A  80                    
SITE     2 AC2 10 HIS A 120  ALA A 140   ZN A 154  HOH A 195                    
SITE     3 AC2 10 HOH A 309  LYS C  91                                          
SITE     1 AC3  4 HIS B  46  HIS B  48  HIS B 120  SO4 B 155                    
SITE     1 AC4  9 LYS B  23  HIS B  46  HIS B  48  HIS B  63                    
SITE     2 AC4  9 HIS B 120  GLY B 141  ARG B 143   ZN B 154                    
SITE     3 AC4  9 HOH B 306                                                     
SITE     1 AC5  5 HIS C  46  HIS C  48  HIS C  63  HIS C 120                    
SITE     2 AC5  5 SO4 C 155                                                     
SITE     1 AC6  7 LYS C  23  HIS C  48  HIS C  63  HIS C 120                    
SITE     2 AC6  7 GLY C 141  ARG C 143   ZN C 154                               
SITE     1 AC7  4 HIS D  46  HIS D  48  HIS D 120  SO4 D 155                    
SITE     1 AC8  5 HIS D  46  HIS D  48  HIS D  63  HIS D 120                    
SITE     2 AC8  5  ZN D 154                                                     
CRYST1   35.240  136.801   56.364  90.00 104.58  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.028377  0.000000  0.007379        0.00000                         
SCALE2      0.000000  0.007310  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018332        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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