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Database: PDB
Entry: 3LTV
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Original site: 3LTV 
HEADER    OXIDOREDUCTASE                          16-FEB-10   3LTV              
TITLE     MOUSE-HUMAN SOD1 CHIMERA                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN],SUPEROXIDE DISMUTASE [CU-ZN]; 
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: RESIDUES 2-81 FROM MOUSE PROTEIN, RESIDUES 82-154 FROM     
COMPND   5 HUMAN PROTEIN,RESIDUES 2-81 FROM MOUSE PROTEIN, RESIDUES 82-154 FROM 
COMPND   6 HUMAN PROTEIN;                                                       
COMPND   7 SYNONYM: SUPEROXIDE DISMUTASE 1,HSOD1;                               
COMPND   8 EC: 1.15.1.1,1.15.1.1;                                               
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS;                     
SOURCE   3 ORGANISM_COMMON: MOUSE, HUMAN;                                       
SOURCE   4 ORGANISM_TAXID: 10090, 9606;                                         
SOURCE   5 GENE: SOD1, SOD1;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PKA8H                                     
KEYWDS    OXIDOREDUCTASE, ANTIOXIDANT, METAL-BINDING, AMYOTROPHIC LATERAL       
KEYWDS   2 SCLEROSIS, DISEASE MUTATION, PHOSPHOPROTEIN                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.V.SEETHARAMAN,A.B.TAYLOR,P.J.HART                                   
REVDAT   3   07-JUN-17 3LTV    1       COMPND SOURCE REMARK                     
REVDAT   2   05-JAN-11 3LTV    1       JRNL                                     
REVDAT   1   08-SEP-10 3LTV    0                                                
JRNL        AUTH   S.V.SEETHARAMAN,A.B.TAYLOR,S.HOLLOWAY,P.J.HART               
JRNL        TITL   STRUCTURES OF MOUSE SOD1 AND HUMAN/MOUSE SOD1 CHIMERAS.      
JRNL        REF    ARCH.BIOCHEM.BIOPHYS.         V. 503   183 2010              
JRNL        REFN                   ISSN 0003-9861                               
JRNL        PMID   20727846                                                     
JRNL        DOI    10.1016/J.ABB.2010.08.014                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.5_2)                        
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.56                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 34219                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1724                            
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 37.5614 -  5.6105    0.97     2730   135  0.1702 0.2302        
REMARK   3     2  5.6105 -  4.4555    0.98     2712   154  0.1674 0.2139        
REMARK   3     3  4.4555 -  3.8930    0.98     2689   151  0.1621 0.2358        
REMARK   3     4  3.8930 -  3.5374    0.99     2712   136  0.1761 0.2256        
REMARK   3     5  3.5374 -  3.2840    0.99     2738   126  0.1894 0.2428        
REMARK   3     6  3.2840 -  3.0904    0.99     2694   143  0.2055 0.2938        
REMARK   3     7  3.0904 -  2.9357    0.99     2736   138  0.2234 0.3187        
REMARK   3     8  2.9357 -  2.8080    0.99     2721   133  0.2320 0.3142        
REMARK   3     9  2.8080 -  2.6999    0.99     2711   149  0.2429 0.3335        
REMARK   3    10  2.6999 -  2.6068    0.99     2704   158  0.2462 0.3591        
REMARK   3    11  2.6068 -  2.5253    1.00     2738   138  0.2446 0.3373        
REMARK   3    12  2.5253 -  2.4531    0.97     2610   163  0.2374 0.3001        
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              : 0.36                                          
REMARK   3   B_SOL              : 36.43                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.33970                                              
REMARK   3    B22 (A**2) : 2.33970                                              
REMARK   3    B33 (A**2) : -4.29560                                             
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      :  0.009           6704                                  
REMARK   3   ANGLE     :  1.178           9046                                  
REMARK   3   CHIRALITY :  0.075           1000                                  
REMARK   3   PLANARITY :  0.004           1235                                  
REMARK   3   DIHEDRAL  : 19.391           2381                                  
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 3LTV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000057723.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-FEB-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
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                  : SINGLE CRYSTAL SIDE-BOUNCE         
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34238                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450                              
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     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.55000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2VR7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, 25% PEG 4000, PH   
REMARK 280  4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       34.16467            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       68.32933            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       51.24700            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       85.41167            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       17.08233            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: 1300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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: 1260 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 1310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     LYS C   128                                                      
REMARK 465     GLY C   129                                                      
REMARK 465     GLY C   130                                                      
REMARK 465     GLN D   153                                                      
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       54.50   -143.65                                   
REMARK 500    ALA B 145      148.69   -178.13                                   
REMARK 500    HIS C  63      139.02    -39.54                                   
REMARK 500    ASN C  65       63.90   -159.78                                   
REMARK 500    LYS C  69     -157.06    -61.42                                   
REMARK 500    ASP C  76      137.40    -39.29                                   
REMARK 500    ASP C  90     -153.96    -66.09                                   
REMARK 500    ASP C  92       34.73    -95.64                                   
REMARK 500    CYS C 111      108.59    -47.06                                   
REMARK 500    PRO D  28      152.09    -40.35                                   
REMARK 500    SER E  25     -108.30    -35.94                                   
REMARK 500    GLN E  34      128.14   -171.93                                   
REMARK 500    GLN E  55       63.78   -112.99                                   
REMARK 500    ASN E  65       77.13   -164.66                                   
REMARK 500    SER E  68       55.45     28.51                                   
REMARK 500    ASP E  76      165.52    -46.10                                   
REMARK 500    SER E 107      163.31    176.37                                   
REMARK 500    SER F  25      -88.09    -19.87                                   
REMARK 500    GLN F  55       51.53   -106.94                                   
REMARK 500    ASN F  65       59.56   -154.96                                   
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 D1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  71   ND1                                                    
REMARK 620 2 HIS D  63   ND1 109.5                                              
REMARK 620 3 ASP D  83   OD1 109.4 113.1                                        
REMARK 620 4 HIS D  80   ND1 125.1 100.3  99.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  83   OD2                                                    
REMARK 620 2 HIS B  71   ND1  93.7                                              
REMARK 620 3 HIS B  80   ND1 121.2 121.7                                        
REMARK 620 4 HIS B  63   ND1 107.9 100.4 109.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  80   ND1                                                    
REMARK 620 2 HIS E  63   ND1 127.8                                              
REMARK 620 3 ASP E  83   OD2 134.7  84.8                                        
REMARK 620 4 HIS E  71   ND1 121.9  91.9  80.8                                  
REMARK 620 5 ASP E  83   OD1  83.6 137.8  54.7  92.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  63   ND1                                                    
REMARK 620 2 ASP F  83   OD2 101.9                                              
REMARK 620 3 HIS F  80   ND1 106.6 112.1                                        
REMARK 620 4 HIS F  71   ND1 108.1 100.6 125.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  83   OD2                                                    
REMARK 620 2 HIS A  80   ND1 107.2                                              
REMARK 620 3 HIS A  63   ND1  97.2 115.1                                        
REMARK 620 4 HIS A  71   ND1 102.1 121.2 110.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  80   ND1                                                    
REMARK 620 2 HIS C  71   ND1 116.6                                              
REMARK 620 3 ASP C  83   OD1 138.0  77.5                                        
REMARK 620 N                    1     2                                         
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 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 1001                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3GTT   RELATED DB: PDB                                   
REMARK 900 MOUSE SOD1                                                           
REMARK 900 RELATED ID: 3GTV   RELATED DB: PDB                                   
REMARK 900 HUMAN-MOUSE SOD1 CHIMERA                                             
DBREF  3LTV A    1    80  UNP    P08228   SODC_MOUSE       2     81             
DBREF  3LTV A   81   153  UNP    P00441   SODC_HUMAN      82    154             
DBREF  3LTV B    1    80  UNP    P08228   SODC_MOUSE       2     81             
DBREF  3LTV B   81   153  UNP    P00441   SODC_HUMAN      82    154             
DBREF  3LTV C    1    80  UNP    P08228   SODC_MOUSE       2     81             
DBREF  3LTV C   81   153  UNP    P00441   SODC_HUMAN      82    154             
DBREF  3LTV D    1    80  UNP    P08228   SODC_MOUSE       2     81             
DBREF  3LTV D   81   153  UNP    P00441   SODC_HUMAN      82    154             
DBREF  3LTV E    1    80  UNP    P08228   SODC_MOUSE       2     81             
DBREF  3LTV E   81   153  UNP    P00441   SODC_HUMAN      82    154             
DBREF  3LTV F    1    80  UNP    P08228   SODC_MOUSE       2     81             
DBREF  3LTV F   81   153  UNP    P00441   SODC_HUMAN      82    154             
SEQRES   1 A  153  ALA MET LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 A  153  VAL GLN GLY THR ILE HIS PHE GLU GLN LYS ALA SER GLY          
SEQRES   3 A  153  GLU PRO VAL VAL LEU SER GLY GLN ILE THR GLY LEU THR          
SEQRES   4 A  153  GLU GLY GLN HIS GLY PHE HIS VAL HIS GLN TYR GLY ASP          
SEQRES   5 A  153  ASN THR GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 A  153  PRO HIS SER LYS LYS HIS GLY GLY PRO ALA ASP GLU GLU          
SEQRES   7 A  153  ARG HIS 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 MET LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 B  153  VAL GLN GLY THR ILE HIS PHE GLU GLN LYS ALA SER GLY          
SEQRES   3 B  153  GLU PRO VAL VAL LEU SER GLY GLN ILE THR GLY LEU THR          
SEQRES   4 B  153  GLU GLY GLN HIS GLY PHE HIS VAL HIS GLN TYR GLY ASP          
SEQRES   5 B  153  ASN THR GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 B  153  PRO HIS SER LYS LYS HIS GLY GLY PRO ALA ASP GLU GLU          
SEQRES   7 B  153  ARG HIS 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 MET LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 C  153  VAL GLN GLY THR ILE HIS PHE GLU GLN LYS ALA SER GLY          
SEQRES   3 C  153  GLU PRO VAL VAL LEU SER GLY GLN ILE THR GLY LEU THR          
SEQRES   4 C  153  GLU GLY GLN HIS GLY PHE HIS VAL HIS GLN TYR GLY ASP          
SEQRES   5 C  153  ASN THR GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 C  153  PRO HIS SER LYS LYS HIS GLY GLY PRO ALA ASP GLU GLU          
SEQRES   7 C  153  ARG HIS 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 MET LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 D  153  VAL GLN GLY THR ILE HIS PHE GLU GLN LYS ALA SER GLY          
SEQRES   3 D  153  GLU PRO VAL VAL LEU SER GLY GLN ILE THR GLY LEU THR          
SEQRES   4 D  153  GLU GLY GLN HIS GLY PHE HIS VAL HIS GLN TYR GLY ASP          
SEQRES   5 D  153  ASN THR GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 D  153  PRO HIS SER LYS LYS HIS GLY GLY PRO ALA ASP GLU GLU          
SEQRES   7 D  153  ARG HIS 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                      
SEQRES   1 E  153  ALA MET LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 E  153  VAL GLN GLY THR ILE HIS PHE GLU GLN LYS ALA SER GLY          
SEQRES   3 E  153  GLU PRO VAL VAL LEU SER GLY GLN ILE THR GLY LEU THR          
SEQRES   4 E  153  GLU GLY GLN HIS GLY PHE HIS VAL HIS GLN TYR GLY ASP          
SEQRES   5 E  153  ASN THR GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 E  153  PRO HIS SER LYS LYS HIS GLY GLY PRO ALA ASP GLU GLU          
SEQRES   7 E  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 E  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 E  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 E  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 E  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 E  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 F  153  ALA MET LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 F  153  VAL GLN GLY THR ILE HIS PHE GLU GLN LYS ALA SER GLY          
SEQRES   3 F  153  GLU PRO VAL VAL LEU SER GLY GLN ILE THR GLY LEU THR          
SEQRES   4 F  153  GLU GLY GLN HIS GLY PHE HIS VAL HIS GLN TYR GLY ASP          
SEQRES   5 F  153  ASN THR GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 F  153  PRO HIS SER LYS LYS HIS GLY GLY PRO ALA ASP GLU GLU          
SEQRES   7 F  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 F  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 F  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 F  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 F  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 F  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
HET     ZN  A1001       1                                                       
HET     ZN  B1001       1                                                       
HET     ZN  C1001       1                                                       
HET     ZN  D1001       1                                                       
HET     ZN  E1001       1                                                       
HET     ZN  F1001       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   7   ZN    6(ZN 2+)                                                     
FORMUL  13  HOH   *145(H2 O)                                                    
HELIX    1   1 GLN A   55  GLY A   61  5                                   7    
HELIX    2   2 SER A  107  CYS A  111  5                                   5    
HELIX    3   3 ASN A  131  GLY A  138  1                                   8    
HELIX    4   4 GLN B   55  GLY B   61  5                                   7    
HELIX    5   5 SER B  107  CYS B  111  5                                   5    
HELIX    6   6 ASN B  131  GLY B  138  1                                   8    
HELIX    7   7 GLN C   55  GLY C   61  5                                   7    
HELIX    8   8 SER C  107  CYS C  111  5                                   5    
HELIX    9   9 CYS D   57  GLY D   61  5                                   5    
HELIX   10  10 SER D  107  CYS D  111  5                                   5    
HELIX   11  11 GLU D  132  LYS D  136  5                                   5    
HELIX   12  12 GLN E   55  GLY E   61  5                                   7    
HELIX   13  13 ASN E  131  THR E  137  1                                   7    
HELIX   14  14 GLN F   55  GLY F   61  5                                   7    
HELIX   15  15 SER F  107  CYS F  111  5                                   5    
HELIX   16  16 ASN F  131  GLY F  138  1                                   8    
SHEET    1   A 5 ALA A  95  ASP A 101  0                                        
SHEET    2   A 5 VAL A  29  THR A  36 -1  N  LEU A  31   O  ILE A  99           
SHEET    3   A 5 GLN A  15  GLN A  22 -1  N  GLU A  21   O  VAL A  30           
SHEET    4   A 5 MET A   2  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 4 ASP A  83  ALA A  89  0                                        
SHEET    2   B 4 GLY A  41  HIS A  48 -1  N  GLY A  41   O  ALA A  89           
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  GLY A 147   N  LEU A 117           
SHEET    1   C 5 ALA B  95  ASP B 101  0                                        
SHEET    2   C 5 VAL B  29  THR B  36 -1  N  VAL B  29   O  ASP B 101           
SHEET    3   C 5 GLN B  15  GLN B  22 -1  N  HIS B  19   O  SER B  32           
SHEET    4   C 5 MET B   2  LYS B   9 -1  N  LEU B   8   O  GLY B  16           
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  ALA B 145   N  VAL B 119           
SHEET    1   E 5 VAL C  97  ASP C 101  0                                        
SHEET    2   E 5 VAL C  29  THR C  36 -1  N  LEU C  31   O  ILE C  99           
SHEET    3   E 5 GLN C  15  GLN C  22 -1  N  HIS C  19   O  SER C  32           
SHEET    4   E 5 MET C   2  LEU C   8 -1  N  LEU C   8   O  GLY C  16           
SHEET    5   E 5 GLY C 150  ILE C 151 -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  VAL C 118   N  HIS C  46           
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  THR D  36 -1  N  ILE D  35   O  ALA D  95           
SHEET    3   G 5 GLN D  15  GLN D  22 -1  N  GLN D  15   O  THR D  36           
SHEET    4   G 5 MET D   2  LEU D   8 -1  N  MET D   2   O  GLN D  22           
SHEET    5   G 5 GLY D 150  ILE D 151 -1  O  GLY D 150   N  VAL D   5           
SHEET    1   H 4 ASN D  86  ALA D  89  0                                        
SHEET    2   H 4 GLY D  41  HIS D  48 -1  N  GLY D  41   O  ALA D  89           
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  GLY D 147   N  LEU D 117           
SHEET    1   I 5 ALA E  95  ASP E 101  0                                        
SHEET    2   I 5 VAL E  29  THR E  36 -1  N  VAL E  29   O  ASP E 101           
SHEET    3   I 5 GLN E  15  GLN E  22 -1  N  GLU E  21   O  VAL E  30           
SHEET    4   I 5 MET E   2  LEU E   8 -1  N  ALA E   4   O  PHE E  20           
SHEET    5   I 5 GLY E 150  ILE E 151 -1  O  GLY E 150   N  VAL E   5           
SHEET    1   J 4 ASP E  83  ALA E  89  0                                        
SHEET    2   J 4 GLY E  41  HIS E  48 -1  N  GLY E  41   O  ALA E  89           
SHEET    3   J 4 THR E 116  HIS E 120 -1  O  VAL E 118   N  HIS E  46           
SHEET    4   J 4 ARG E 143  VAL E 148 -1  O  GLY E 147   N  LEU E 117           
SHEET    1   K 5 ALA F  95  ASP F 101  0                                        
SHEET    2   K 5 VAL F  29  THR F  36 -1  N  LEU F  31   O  ILE F  99           
SHEET    3   K 5 GLN F  15  GLN F  22 -1  N  HIS F  19   O  SER F  32           
SHEET    4   K 5 MET F   2  LYS F   9 -1  N  ALA F   4   O  PHE F  20           
SHEET    5   K 5 GLY F 150  ILE F 151 -1  O  GLY F 150   N  VAL F   5           
SHEET    1   L 4 ASP F  83  ALA F  89  0                                        
SHEET    2   L 4 GLY F  41  HIS F  48 -1  N  GLY F  41   O  ALA F  89           
SHEET    3   L 4 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48           
SHEET    4   L 4 ARG F 143  VAL F 148 -1  O  ALA F 145   N  VAL F 119           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.11  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.07  
SSBOND   3 CYS C   57    CYS C  146                          1555   1555  2.05  
SSBOND   4 CYS D   57    CYS D  146                          1555   1555  2.08  
SSBOND   5 CYS E   57    CYS E  146                          1555   1555  2.07  
SSBOND   6 CYS F   57    CYS F  146                          1555   1555  2.08  
LINK         ND1 HIS D  71                ZN    ZN D1001     1555   1555  1.87  
LINK         OD2 ASP B  83                ZN    ZN B1001     1555   1555  1.92  
LINK         ND1 HIS E  80                ZN    ZN E1001     1555   1555  1.93  
LINK         ND1 HIS D  63                ZN    ZN D1001     1555   1555  1.95  
LINK         ND1 HIS F  63                ZN    ZN F1001     1555   1555  1.98  
LINK         OD2 ASP A  83                ZN    ZN A1001     1555   1555  1.98  
LINK         OD2 ASP F  83                ZN    ZN F1001     1555   1555  2.02  
LINK         ND1 HIS A  80                ZN    ZN A1001     1555   1555  2.06  
LINK         ND1 HIS A  63                ZN    ZN A1001     1555   1555  2.10  
LINK         ND1 HIS B  71                ZN    ZN B1001     1555   1555  2.11  
LINK         OD1 ASP D  83                ZN    ZN D1001     1555   1555  2.11  
LINK         ND1 HIS F  80                ZN    ZN F1001     1555   1555  2.11  
LINK         ND1 HIS F  71                ZN    ZN F1001     1555   1555  2.12  
LINK         ND1 HIS B  80                ZN    ZN B1001     1555   1555  2.12  
LINK         ND1 HIS A  71                ZN    ZN A1001     1555   1555  2.13  
LINK         ND1 HIS C  80                ZN    ZN C1001     1555   1555  2.14  
LINK         ND1 HIS B  63                ZN    ZN B1001     1555   1555  2.20  
LINK         ND1 HIS E  63                ZN    ZN E1001     1555   1555  2.22  
LINK         OD2 ASP E  83                ZN    ZN E1001     1555   1555  2.30  
LINK         ND1 HIS E  71                ZN    ZN E1001     1555   1555  2.39  
LINK         OD1 ASP E  83                ZN    ZN E1001     1555   1555  2.50  
LINK         ND1 HIS C  71                ZN    ZN C1001     1555   1555  2.60  
LINK         OD1 ASP C  83                ZN    ZN C1001     1555   1555  2.63  
LINK         ND1 HIS D  80                ZN    ZN D1001     1555   1555  2.68  
SITE     1 AC1  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC2  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     1 AC3  4 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
SITE     1 AC4  4 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     1 AC5  4 HIS E  63  HIS E  71  HIS E  80  ASP E  83                    
SITE     1 AC6  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
CRYST1  127.480  127.480  102.494  90.00  90.00 120.00 P 61         36          
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      0.007844  0.004529  0.000000        0.00000                         
SCALE2      0.000000  0.009058  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009757        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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