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Database: PDB
Entry: 1HL4
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HEADER    OXIDOREDUCTASE                          13-MAR-03   1HL4              
TITLE     THE STRUCTURE OF APO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE;                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: EG118;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: YEP351                                     
KEYWDS    OXIDOREDUCTASE, HUMAN CU, ZN SUPEROXIDE DISMUTASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.W.STRANGE,S.ANTONYUK,M.A.HOUGH,P.DOUCETTE,J.RODRIGUEZ,P.J.HART,     
AUTHOR   2 L.J.HAYWARD,J.S.VALENTINE,S.S.HASNAIN                                
REVDAT   3   13-JUL-11 1HL4    1       VERSN                                    
REVDAT   2   24-FEB-09 1HL4    1       VERSN                                    
REVDAT   1   08-MAY-03 1HL4    0                                                
JRNL        AUTH   R.W.STRANGE,S.ANTONYUK,M.A.HOUGH,P.DOUCETTE,J.RODRIGUEZ,     
JRNL        AUTH 2 P.J.HART,L.J.HAYWARD,J.S.VALENTINE,S.S.HASNAIN               
JRNL        TITL   THE STRUCTURE OF HOLO AND METAL-DEFICIENT WILD-TYPE HUMAN    
JRNL        TITL 2 CU, ZN SUPEROXIDE DISMUTASE AND ITS RELEVANCE TO FAMILIAL    
JRNL        TITL 3 AMYOTROPHIC LATERAL SCLEROSIS                                
JRNL        REF    J.MOL.BIOL.                   V. 328   877 2003              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   12729761                                                     
JRNL        DOI    10.1016/S0022-2836(03)00355-3                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.82 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 47806                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.234                           
REMARK   3   R VALUE            (WORKING SET) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2545                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.82                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2938                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3690                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 167                          
REMARK   3   BIN FREE R VALUE                    : 0.3880                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3994                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 311                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.96000                                             
REMARK   3    B22 (A**2) : 8.87000                                              
REMARK   3    B33 (A**2) : -5.95000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -2.69000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.164         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.160         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.144         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.695         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4062 ; 0.016 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5492 ; 1.819 ; 1.941       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   549 ; 4.762 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   656 ;21.915 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   623 ; 0.119 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3090 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1873 ; 0.222 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   479 ; 0.193 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     6 ; 0.190 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    39 ; 0.185 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.334 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2714 ; 1.198 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4304 ; 1.608 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1348 ; 2.910 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1188 ; 3.758 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.3230  -2.5300  20.7480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1922 T22:   0.1108                                     
REMARK   3      T33:   0.1997 T12:  -0.0052                                     
REMARK   3      T13:   0.0202 T23:   0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2765 L22:   0.7852                                     
REMARK   3      L33:   1.9569 L12:   0.1158                                     
REMARK   3      L13:   0.5674 L23:   0.1294                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0469 S12:   0.1603 S13:  -0.0890                       
REMARK   3      S21:  -0.0800 S22:  -0.0491 S23:  -0.0227                       
REMARK   3      S31:   0.0730 S32:   0.0248 S33:   0.0021                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     0        B   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.8120   2.5550  46.5030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1585 T22:   0.1559                                     
REMARK   3      T33:   0.2102 T12:  -0.0249                                     
REMARK   3      T13:   0.0079 T23:   0.0205                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1759 L22:   0.6777                                     
REMARK   3      L33:   1.9011 L12:  -0.0593                                     
REMARK   3      L13:   0.2634 L23:  -0.0656                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0044 S12:  -0.2088 S13:   0.0367                       
REMARK   3      S21:   0.0104 S22:   0.0213 S23:  -0.0295                       
REMARK   3      S31:   0.0043 S32:   0.0004 S33:  -0.0169                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.9140  11.7480  30.4600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1839 T22:   0.0101                                     
REMARK   3      T33:   0.2097 T12:  -0.0400                                     
REMARK   3      T13:   0.0079 T23:   0.0152                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0460 L22:   0.9230                                     
REMARK   3      L33:   2.9785 L12:   0.3265                                     
REMARK   3      L13:  -0.1157 L23:   0.0417                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0364 S12:  -0.2785 S13:   0.0774                       
REMARK   3      S21:  -0.0237 S22:  -0.0181 S23:  -0.0128                       
REMARK   3      S31:  -0.0973 S32:   0.2112 S33:  -0.0183                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.7840   5.2450   8.5970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2253 T22:   0.0122                                     
REMARK   3      T33:   0.2179 T12:  -0.0273                                     
REMARK   3      T13:  -0.0071 T23:   0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6552 L22:   1.4424                                     
REMARK   3      L33:   3.2502 L12:   0.0299                                     
REMARK   3      L13:   0.2515 L23:   0.0485                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0116 S12:   0.2408 S13:  -0.0718                       
REMARK   3      S21:  -0.0622 S22:  -0.0191 S23:   0.0385                       
REMARK   3      S31:   0.0728 S32:  -0.0322 S33:   0.0075                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: DISORDERED REGIONS IN MONOMERS B AND      
REMARK   3  D WERE REMOVED FROM THE STRUCTURE                                   
REMARK   4                                                                      
REMARK   4 1HL4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-MAR-03.                  
REMARK 100 THE PDBE ID CODE IS EBI-12324.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JAN-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 265996                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
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     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1SOS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 45.4                                       
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.4                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NH4CL, 20%PEG2000,                  
REMARK 280  10% ETHYLENE GLYCOL, 0.1 M MES PH 5.6                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       78.20200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       17.48900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       78.20200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       17.48900            
REMARK 290   SMTRY3   4  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: 1550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 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: 1410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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     ACE A     0                                                      
REMARK 465     ACE C     0                                                      
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     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     ACE D     0                                                      
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     ASP D   125                                                      
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 465     ASN D   139                                                      
REMARK 465     ALA D   140                                                      
REMARK 465     GLY D   141                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  23    CG   CD   CE   NZ                                   
REMARK 470     GLU A  24    CD   OE1  OE2                                       
REMARK 470     LYS A  30    CG   CD   CE   NZ                                   
REMARK 470     LYS A  70    CE   NZ                                             
REMARK 470     GLU A 132    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 136    NZ                                                  
REMARK 470     LYS B   9    CD   CE   NZ                                        
REMARK 470     LYS B  75    CE   NZ                                             
REMARK 470     GLU B  77    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  91    NZ                                                  
REMARK 470     LYS B 122    CE   NZ                                             
REMARK 470     SER C  68    C    O    OG                                        
REMARK 470     HIS C  80    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS C  91    CE   NZ                                             
REMARK 470     LYS C 122    CD   CE   NZ                                        
REMARK 470     HIS D  80    C    O    CB   CG   ND1  CD2  CE1  NE2              
REMARK 470     ASP D  83    CG   OD1  OD2                                       
REMARK 470     LYS D  91    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP B   124     O    HOH B  2078              2.17            
REMARK 500   NH2  ARG C    79     OD1  ASP C   101              2.01            
REMARK 500   O    HOH C  2049     O    HOH B  2069              1.98            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B  2013     O    HOH B  2026     2556     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  76   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP A 101   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A 109   CB  -  CG  -  OD2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG A 115   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG B 143   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ASP C  11   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    LEU C  38   CA  -  CB  -  CG  ANGL. DEV. =  15.9 DEGREES          
REMARK 500    ASP C  52   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP C 124   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP D 124   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
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    LYS B 136      -53.66   -125.50                                   
REMARK 500    ASN C  65       87.13   -159.78                                   
REMARK 500    ASP C  90     -168.92    -76.29                                   
REMARK 500    ASN D  65       72.96   -152.05                                   
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 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  71   ND1                                                    
REMARK 620 2 ASP A  83   OD1  75.2                                              
REMARK 620 3 HIS A  63   ND1 119.9 131.8                                        
REMARK 620 4 HIS A  80   ND1 122.1 113.8  96.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  63   ND1                                                    
REMARK 620 2 HIS B  80   ND1  97.7                                              
REMARK 620 3 ASP B  83   OD1 110.9 109.1                                        
REMARK 620 4 HIS B  71   ND1 125.8 121.4  91.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
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 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B 155                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WZ6   RELATED DB: PDB                                   
REMARK 900  G93A SOD1 MUTANT COMPLEXED WITH QUINAZOLINE.                        
REMARK 900 RELATED ID: 1OEZ   RELATED DB: PDB                                   
REMARK 900  ZN HIS46ARG MUTANT OF HUMAN CU, ZN                                  
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 1PTZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE HUMAN CU, ZN                               
REMARK 900  SUPEROXIDE DISMUTASE,FAMILIAL AMYOTROPHIC                           
REMARK 900  LATERAL SCLEROSIS (FALS) MUTANT H43R                                
REMARK 900 RELATED ID: 1AZV   RELATED DB: PDB                                   
REMARK 900  FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)                            
REMARK 900 RELATED ID: 2WYZ   RELATED DB: PDB                                   
REMARK 900  L38V SOD1 MUTANT COMPLEXED WITH UMP                                 
REMARK 900 RELATED ID: 1OZU   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF FAMILIAL ALS MUTANT                            
REMARK 900  S134N OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (                         
REMARK 900  CUZNSOD) TO 1.3A RESOLUTION                                         
REMARK 900 RELATED ID: 2VR6   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF G85R ALS MUTANT OF                             
REMARK 900  HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD)                          
REMARK 900  AT 1.3 A RESOLUTION                                                 
REMARK 900 RELATED ID: 2C9V   RELATED DB: PDB                                   
REMARK 900  ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN                          
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 2WZ5   RELATED DB: PDB                                   
REMARK 900  L38V SOD1 MUTANT COMPLEXED WITH L-METHIONINE                        
REMARK 900  .                                                                   
REMARK 900 RELATED ID: 2XJL   RELATED DB: PDB                                   
REMARK 900  MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE                          
REMARK 900  WITHOUT CU LIGANDS                                                  
REMARK 900 RELATED ID: 1PU0   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN CU,ZN SUPEROXIDE                                 
REMARK 900  DISMUTASE                                                           
REMARK 900 RELATED ID: 1FUN   RELATED DB: PDB                                   
REMARK 900  SUPEROXIDE DISMUTASE MUTANT WITH LYS 136                            
REMARK 900  REPLACED BY GLU, CYS 6 REPLACED BY ALA                              
REMARK 900  AND CYS 111 REPLACED BY SER (K136E, C6A,                            
REMARK 900  C111S)                                                              
REMARK 900 RELATED ID: 2XJK   RELATED DB: PDB                                   
REMARK 900  MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE                          
REMARK 900 RELATED ID: 1SOS   RELATED DB: PDB                                   
REMARK 900  SUPEROXIDE DISMUTASE MUTANT WITH CYS 6                              
REMARK 900  REPLACED BY ALA AND CYS 111 REPLACED BY                             
REMARK 900  SER (C6A, C111S)                                                    
REMARK 900 RELATED ID: 1N19   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE HSOD A4V MUTANT                                    
REMARK 900 RELATED ID: 1P1V   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF FALS-ASSOCIATED HUMAN                          
REMARK 900  COPPER-ZINCSUPEROXIDE DISMUTASE (CUZNSOD) MUTANT                    
REMARK 900   D125H TO 1.4A                                                      
REMARK 900 RELATED ID: 1L3N   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF REDUCED DIMERIC                           
REMARK 900  COPPER ZINC SOD:THE STRUCTURAL EFFECTS OF                           
REMARK 900  DIMERIZATION                                                        
REMARK 900 RELATED ID: 2WKO   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF METAL LOADED PATHOGENIC SOD1                           
REMARK 900  MUTANT G93A.                                                        
REMARK 900 RELATED ID: 2WZ0   RELATED DB: PDB                                   
REMARK 900  L38V SOD1 MUTANT COMPLEXED WITH ANILINE.                            
REMARK 900 RELATED ID: 1UXL   RELATED DB: PDB                                   
REMARK 900  I113T MUTANT OF HUMAN SOD1                                          
REMARK 900 RELATED ID: 2AF2   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF DISULFIDE REDUCED AND                         
REMARK 900  COPPER DEPLETEDHUMAN SUPEROXIDE DISMUTASE                           
REMARK 900 RELATED ID: 2VR8   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF G85R ALS MUTANT OF                             
REMARK 900  HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD)                          
REMARK 900  AT 1.36 A RESOLUTION                                                
REMARK 900 RELATED ID: 1RK7   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF APO CU,ZN SUPEROXIDE                          
REMARK 900  DISMUTASE: ROLEOF METAL IONS IN PROTEIN                             
REMARK 900  FOLDING                                                             
REMARK 900 RELATED ID: 2VR7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF G85R ALS MUTANT OF                             
REMARK 900  HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD)                          
REMARK 900  AT 1.58 A RESOLUTION                                                
REMARK 900 RELATED ID: 2V0A   RELATED DB: PDB                                   
REMARK 900  ATOMIC RESOLUTION CRYSTAL STRUCTURE OF HUMAN                        
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 1MFM   RELATED DB: PDB                                   
REMARK 900  MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q                          
REMARK 900  AT ATOMIC RESOLUTION                                                
REMARK 900 RELATED ID: 2C9S   RELATED DB: PDB                                   
REMARK 900  1.24 ANGSTROMS RESOLUTION STRUCTURE OF ZN-                          
REMARK 900  ZN HUMAN SUPEROXIDE DISMUTASE                                       
REMARK 900 RELATED ID: 4SOD   RELATED DB: PDB                                   
REMARK 900  CU,ZN SUPEROXIDE DISMUTASE MUTANT WITH CYS                          
REMARK 900  6 REPLACED BY ALA AND CYS 111 REPLACED                              
REMARK 900  BY SER (C6A,C111S) WITH AN 18-RESIDUE                               
REMARK 900  HEPARIN-BINDING PEPTIDE FUSED TO THE C-                             
REMARK 900  TERMINUS (THEORETICAL MODEL)                                        
REMARK 900 RELATED ID: 2WYT   RELATED DB: PDB                                   
REMARK 900  1.0 A RESOLUTION STRUCTURE OF L38V SOD1                             
REMARK 900  MUTANT                                                              
REMARK 900 RELATED ID: 1DSW   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF A MONOMERIC,                              
REMARK 900  REDUCED FORM OFHUMAN COPPER, ZINC SUPEROXIDE                        
REMARK 900  DISMUTASE BEARING THE SAMECHARGE AS THE                             
REMARK 900  NATIVE PROTEIN                                                      
REMARK 900 RELATED ID: 1KMG   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF MONOMERIC COPPER-                         
REMARK 900  FREE SUPEROXIDEDISMUTASE                                            
REMARK 900 RELATED ID: 1OZT   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF APO-H46R FAMILIAL ALS                          
REMARK 900  MUTANT HUMAN CU,ZN SUPEROXIDE DISMUTASE (                           
REMARK 900  CUZNSOD) TO 2.5A RESOLUTION                                         
REMARK 900 RELATED ID: 1N18   RELATED DB: PDB                                   
REMARK 900  THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE                             
REMARK 900  DISMUTASE, C6A,C111S                                                
REMARK 900 RELATED ID: 1BA9   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF REDUCED MONOMERIC                         
REMARK 900  SUPEROXIDE DISMUTASE, NMR, 36 STRUCTURES                            
REMARK 900 RELATED ID: 1HL5   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN                             
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 2C9U   RELATED DB: PDB                                   
REMARK 900  1.24 ANGSTROMS RESOLUTION STRUCTURE OF AS-                          
REMARK 900  ISOLATED CU-ZN HUMAN SUPEROXIDE DISMUTASE                           
REMARK 900 RELATED ID: 1UXM   RELATED DB: PDB                                   
REMARK 900  A4V MUTANT OF HUMAN SOD1                                            
REMARK 900 RELATED ID: 1SPD   RELATED DB: PDB                                   
REMARK 900  SUPEROXIDE DISMUTASE                                                
DBREF  1HL4 A    0     0  PDB    1HL4     1HL4             0      0             
DBREF  1HL4 A    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  1HL4 B    0     0  PDB    1HL4     1HL4             0      0             
DBREF  1HL4 B    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  1HL4 C    0     0  PDB    1HL4     1HL4             0      0             
DBREF  1HL4 C    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  1HL4 D    0     0  PDB    1HL4     1HL4             0      0             
DBREF  1HL4 D    1   153  UNP    P00441   SODC_HUMAN       2    154             
SEQRES   1 A  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 A  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 A  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 A  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 A  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 A  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 A  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 A  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 A  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 A  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 A  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 A  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 B  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 B  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 B  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 B  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 B  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 B  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 B  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 B  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 B  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 B  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 B  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 B  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 C  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 C  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 C  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 C  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 C  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 C  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 C  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 C  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 C  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 C  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 C  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 C  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 D  154  ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY          
SEQRES   2 D  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 D  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 D  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 D  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 D  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 D  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 D  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 D  154  ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR          
SEQRES  10 D  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 D  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 D  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
HET     ZN  A 155       1                                                       
HET     ZN  B 155       1                                                       
HET    ACE  B   0       3                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     ACE ACETYL GROUP                                                     
FORMUL   5   ZN    2(ZN 2+)                                                     
FORMUL   6  ACE    C2 H4 O                                                      
FORMUL   7  HOH   *311(H2 O)                                                    
HELIX    1   1 ALA A   55  GLY A   61  5                                   7    
HELIX    2   2 GLU A  132  LYS A  136  5                                   5    
HELIX    3   3 GLY B   56  GLY B   61  5                                   6    
HELIX    4   4 GLU B  133  GLY B  138  1                                   6    
HELIX    5   5 ALA C   55  GLY C   61  5                                   7    
HELIX    6   6 SER C  107  HIS C  110  5                                   4    
HELIX    7   7 ALA D   55  GLY D   61  5                                   7    
SHEET    1  AA11 THR A   2  GLY A  10  0                                        
SHEET    2  AA11 GLN A  15  GLN A  22 -1  O  GLY A  16   N  LEU A   8           
SHEET    3  AA11 VAL A  29  LYS A  36 -1  O  LYS A  30   N  GLU A  21           
SHEET    4  AA11 ALA A  95  ASP A 101 -1  O  ALA A  95   N  ILE A  35           
SHEET    5  AA11 ASP A  83  ALA A  89 -1  O  THR A  88   N  ASP A  96           
SHEET    6  AA11 GLY A  41  HIS A  48 -1  O  GLY A  41   N  ALA A  89           
SHEET    7  AA11 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    8  AA11 ARG A 143  VAL A 148 -1  N  LEU A 144   O  VAL A 119           
SHEET    9  AA11 THR A   2  GLY A  10 -1  O  LYS A   9   N  CYS A 146           
SHEET   10  AA11 GLN A  15  GLN A  22 -1  O  GLY A  16   N  LEU A   8           
SHEET   11  AA11 THR A   2  GLY A  10 -1  O  THR A   2   N  GLN A  22           
SHEET    1  BA 5 ALA B  95  ASP B 101  0                                        
SHEET    2  BA 5 VAL B  29  LYS B  36 -1  O  VAL B  29   N  ASP B 101           
SHEET    3  BA 5 GLN B  15  GLU B  21 -1  O  GLN B  15   N  LYS B  36           
SHEET    4  BA 5 LYS B   3  LYS B   9 -1  O  ALA B   4   N  PHE B  20           
SHEET    5  BA 5 GLY B 150  ILE B 151 -1  O  GLY B 150   N  VAL B   5           
SHEET    1  BB 4 ASP B  83  ALA B  89  0                                        
SHEET    2  BB 4 GLY B  41  HIS B  48 -1  O  GLY B  41   N  ALA B  89           
SHEET    3  BB 4 THR B 116  HIS B 120 -1  O  THR B 116   N  HIS B  48           
SHEET    4  BB 4 ARG B 143  VAL B 148 -1  N  LEU B 144   O  VAL B 119           
SHEET    1  CA 5 ALA C  95  ASP C 101  0                                        
SHEET    2  CA 5 VAL C  29  LYS C  36 -1  O  VAL C  29   N  ASP C 101           
SHEET    3  CA 5 GLN C  15  GLN C  22 -1  O  GLN C  15   N  LYS C  36           
SHEET    4  CA 5 LYS C   3  LEU C   8 -1  O  ALA C   4   N  PHE C  20           
SHEET    5  CA 5 GLY C 150  ILE C 151 -1  O  GLY C 150   N  VAL C   5           
SHEET    1  CB 4 ASP C  83  ALA C  89  0                                        
SHEET    2  CB 4 GLY C  41  HIS C  48 -1  O  GLY C  41   N  ALA C  89           
SHEET    3  CB 4 THR C 116  HIS C 120 -1  O  THR C 116   N  HIS C  48           
SHEET    4  CB 4 ARG C 143  VAL C 148 -1  N  LEU C 144   O  VAL C 119           
SHEET    1  DA 5 ALA D  95  ASP D 101  0                                        
SHEET    2  DA 5 VAL D  29  LYS D  36 -1  O  VAL D  29   N  ASP D 101           
SHEET    3  DA 5 GLN D  15  GLN D  22 -1  O  GLN D  15   N  LYS D  36           
SHEET    4  DA 5 LYS D   3  LYS D   9 -1  O  ALA D   4   N  PHE D  20           
SHEET    5  DA 5 GLY D 150  ILE D 151 -1  O  GLY D 150   N  VAL D   5           
SHEET    1  DB 4 ASP D  83  ALA D  89  0                                        
SHEET    2  DB 4 GLY D  41  HIS D  48 -1  O  GLY D  41   N  ALA D  89           
SHEET    3  DB 4 THR D 116  HIS D 120 -1  O  THR D 116   N  HIS D  48           
SHEET    4  DB 4 ARG D 143  VAL D 148 -1  N  LEU D 144   O  VAL D 119           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.03  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.07  
SSBOND   3 CYS C   57    CYS C  146                          1555   1555  2.08  
SSBOND   4 CYS D   57    CYS D  146                          1555   1555  2.05  
LINK        ZN    ZN A 155                 ND1 HIS A  71     1555   1555  2.45  
LINK        ZN    ZN A 155                 OD1 ASP A  83     1555   1555  2.08  
LINK        ZN    ZN A 155                 ND1 HIS A  63     1555   1555  2.03  
LINK        ZN    ZN A 155                 ND1 HIS A  80     1555   1555  1.91  
LINK         C   ACE B   0                 N   ALA B   1     1555   1555  1.33  
LINK        ZN    ZN B 155                 OD1 ASP B  83     1555   1555  1.90  
LINK        ZN    ZN B 155                 ND1 HIS B  71     1555   1555  2.17  
LINK        ZN    ZN B 155                 ND1 HIS B  80     1555   1555  1.98  
LINK        ZN    ZN B 155                 ND1 HIS B  63     1555   1555  1.97  
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                    
CRYST1  156.404   34.978  114.809  90.00 112.26  90.00 C 1 2 1      16          
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      0.006394  0.000000  0.002617        0.00000                         
SCALE2      0.000000  0.028589  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009411        0.00000                         
MTRIX1   1  0.763240 -0.016790 -0.645900       19.85701    1                    
MTRIX2   1 -0.025800 -0.999660 -0.004490        0.08071    1                    
MTRIX3   1 -0.645610  0.020090 -0.763410       53.73026    1                    
MTRIX1   2 -0.969750 -0.244100  0.001570       17.90989    1                    
MTRIX2   2 -0.205170  0.811570 -0.547040        9.16435    1                    
MTRIX3   2  0.132260 -0.530820 -0.837100       51.25463    1                    
MTRIX1   3 -0.834840  0.141310  0.532040        0.75498    1                    
MTRIX2   3  0.207630 -0.814280  0.542070       -9.10994    1                    
MTRIX3   3  0.509830  0.563010  0.650450        3.23855    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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