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Database: PDB
Entry: 3CQP
LinkDB: 3CQP
Original site: 3CQP 
HEADER    OXIDOREDUCTASE                          03-APR-08   3CQP              
TITLE     HUMAN SOD1 G85R VARIANT, STRUCTURE I                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SOD1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: EGY118;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: YEP351-HSOD                               
KEYWDS    OXIDOREDUCTASE, HUMAN CU, ZN SUPEROXIDE DISMUTASE, ANTIOXIDANT,       
KEYWDS   2 METAL-BINDING, AMYOTROPHIC LATERAL SCLEROSIS, DISEASE MUTATION       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.CAO,S.ANTONYUK,S.V.SEETHARAMAN,L.J.WHITSON,A.B.TAYLOR,S.P.HOLLOWAY, 
AUTHOR   2 R.W.STRANGE,P.A.DOUCETTE,J.S.VALENTINE,A.TIWARI,L.J.HAYWARD,S.PADUA, 
AUTHOR   3 J.A.COHLBERG,S.S.HASNAIN,P.J.HART                                    
REVDAT   4   13-JUL-11 3CQP    1       VERSN                                    
REVDAT   3   24-FEB-09 3CQP    1       VERSN                                    
REVDAT   2   01-JUL-08 3CQP    1       JRNL                                     
REVDAT   1   29-APR-08 3CQP    0                                                
JRNL        AUTH   X.CAO,S.V.ANTONYUK,S.V.SEETHARAMAN,L.J.WHITSON,A.B.TAYLOR,   
JRNL        AUTH 2 S.P.HOLLOWAY,R.W.STRANGE,P.A.DOUCETTE,J.S.VALENTINE,         
JRNL        AUTH 3 A.TIWARI,L.J.HAYWARD,S.PADUA,J.A.COHLBERG,S.S.HASNAIN,       
JRNL        AUTH 4 P.J.HART                                                     
JRNL        TITL   STRUCTURES OF THE G85R VARIANT OF SOD1 IN FAMILIAL           
JRNL        TITL 2 AMYOTROPHIC LATERAL SCLEROSIS.                               
JRNL        REF    J.BIOL.CHEM.                  V. 283 16169 2008              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   18378676                                                     
JRNL        DOI    10.1074/JBC.M801522200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 43936                          
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) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2347                            
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) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3168                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.67                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 148                          
REMARK   3   BIN FREE R VALUE                    : 0.2480                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4271                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 343                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 23.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.32000                                              
REMARK   3    B22 (A**2) : 0.99000                                              
REMARK   3    B33 (A**2) : -1.31000                                             
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.155         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.144         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.095         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.080         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4356 ; 0.009 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5872 ; 1.178 ; 1.947       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   578 ; 5.882 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   187 ;41.010 ;25.348       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   718 ;12.323 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;18.812 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   651 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3320 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1818 ; 0.195 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2912 ; 0.295 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   338 ; 0.138 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    13 ; 0.089 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    88 ; 0.270 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    23 ; 0.153 ; 0.200       
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):  2849 ; 0.542 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4535 ; 1.002 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1507 ; 1.534 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1337 ; 2.344 ; 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     2        A   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.5592 123.1538  60.2013              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1112 T22:  -0.0902                                     
REMARK   3      T33:  -0.1071 T12:   0.0182                                     
REMARK   3      T13:  -0.0085 T23:   0.0066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3962 L22:   1.7706                                     
REMARK   3      L33:   2.3354 L12:  -0.0044                                     
REMARK   3      L13:   0.1509 L23:  -0.4538                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0296 S12:  -0.0203 S13:   0.1122                       
REMARK   3      S21:  -0.0449 S22:   0.1062 S23:   0.0249                       
REMARK   3      S31:  -0.0773 S32:   0.0813 S33:  -0.0766                       
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     2        B   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.9296 102.8853  78.8347              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1191 T22:  -0.0769                                     
REMARK   3      T33:  -0.1015 T12:  -0.0036                                     
REMARK   3      T13:  -0.0041 T23:   0.0256                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0473 L22:   1.9043                                     
REMARK   3      L33:   2.7961 L12:   0.1560                                     
REMARK   3      L13:   0.4785 L23:  -0.3853                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0721 S12:  -0.0505 S13:  -0.0042                       
REMARK   3      S21:   0.0768 S22:  -0.0927 S23:   0.1077                       
REMARK   3      S31:   0.0591 S32:  -0.1353 S33:   0.0206                       
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     2        C   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.8395 148.7290  50.5314              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0893 T22:   0.0087                                     
REMARK   3      T33:   0.0117 T12:  -0.0032                                     
REMARK   3      T13:  -0.0026 T23:  -0.0648                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5055 L22:   4.1408                                     
REMARK   3      L33:   3.2006 L12:  -0.9550                                     
REMARK   3      L13:  -0.7806 L23:   1.4494                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0100 S12:  -0.2434 S13:   0.2330                       
REMARK   3      S21:   0.1023 S22:   0.2314 S23:  -0.5586                       
REMARK   3      S31:  -0.1048 S32:   0.4224 S33:  -0.2214                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     2        D   153                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.1478 135.6563  28.1759              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0864 T22:  -0.0969                                     
REMARK   3      T33:  -0.0992 T12:   0.0186                                     
REMARK   3      T13:   0.0249 T23:   0.0206                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2399 L22:   1.5342                                     
REMARK   3      L33:   3.4554 L12:   0.2101                                     
REMARK   3      L13:  -0.7031 L23:   0.2453                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0314 S12:   0.0312 S13:   0.0448                       
REMARK   3      S21:  -0.1237 S22:   0.0127 S23:  -0.0577                       
REMARK   3      S31:  -0.0354 S32:  -0.2056 S33:  -0.0442                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3CQP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB047097.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-NOV-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.37865                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : CUSTOM-MADE                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46284                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.3700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.36900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.390                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1AZV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M SODIUM MALONATE, PH 7.0, VAPOR     
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y+1/2,Z                                             
REMARK 290       7555   -X+1/2,Y,-Z                                             
REMARK 290       8555   X,-Y,-Z+1/2                                             
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       36.73600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.88200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.40400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       73.88200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.73600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       58.40400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       36.73600            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       58.40400            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       73.88200            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       58.40400            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       36.73600            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       73.88200            
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: 1730 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.3 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: 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: 1780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.2 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 241  LIES ON A SPECIAL POSITION.                          
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     ALA A     1                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     ASP B    76                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     SER C    68                                                      
REMARK 465     ARG C    69                                                      
REMARK 465     LYS C    70                                                      
REMARK 465     HIS C    71                                                      
REMARK 465     GLY C    72                                                      
REMARK 465     GLY C    73                                                      
REMARK 465     PRO C    74                                                      
REMARK 465     LYS C    75                                                      
REMARK 465     ASP C    76                                                      
REMARK 465     GLU C    77                                                      
REMARK 465     GLU C    78                                                      
REMARK 465     ARG C    79                                                      
REMARK 465     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     ALA D     1                                                      
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    ARG A  85     -131.55     62.80                                   
REMARK 500    ASN B  65       59.41   -146.12                                   
REMARK 500    ARG B  85     -128.53     64.75                                   
REMARK 500    ASN C  65       82.07   -151.18                                   
REMARK 500    ASP C  83       91.75    -68.77                                   
REMARK 500    ARG C  85     -122.48     74.75                                   
REMARK 500    ARG D  85     -131.20     64.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 247        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH A 258        DISTANCE =  5.50 ANGSTROMS                       
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                              CU A 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 139.4                                              
REMARK 620 3 HIS A 120   NE2 100.8 118.2                                        
REMARK 620 4 MLI A 157   O6   89.8 103.7  85.0                                  
REMARK 620 N                    1     2     3                                   
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  63   ND1                                                    
REMARK 620 2 HIS A  71   ND1 106.3                                              
REMARK 620 3 HIS A  80   ND1 107.5 122.5                                        
REMARK 620 4 ASP A  83   OD1 104.1  96.5 118.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  46   ND1                                                    
REMARK 620 2 HIS B  48   NE2 143.3                                              
REMARK 620 3 HIS B 120   NE2 102.6 112.2                                        
REMARK 620 N                    1     2                                         
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  71   ND1 103.0                                              
REMARK 620 3 HIS B  80   ND1 113.4 119.2                                        
REMARK 620 4 ASP B  83   OD1 101.5  97.7 119.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  46   ND1                                                    
REMARK 620 2 HIS C  48   NE2 128.4                                              
REMARK 620 3 HIS C 120   NE2  97.5 107.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  46   ND1                                                    
REMARK 620 2 HIS D  48   NE2 130.1                                              
REMARK 620 3 HIS D 120   NE2  96.2 115.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  63   ND1                                                    
REMARK 620 2 HIS D  71   ND1 102.6                                              
REMARK 620 3 HIS D  80   ND1 109.5 122.0                                        
REMARK 620 4 ASP D  83   OD1 106.7  98.2 116.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU D 154                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 155                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI A 156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI A 157                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3CQQ   RELATED DB: PDB                                   
REMARK 900 HUMAN SOD1 G85R VARIANT, STRUCTURE II                                
DBREF  3CQP A    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3CQP B    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3CQP C    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  3CQP D    1   153  UNP    P00441   SODC_HUMAN       2    154             
SEQADV 3CQP ARG A   85  UNP  P00441    GLY    86 VARIANT                        
SEQADV 3CQP ARG B   85  UNP  P00441    GLY    86 VARIANT                        
SEQADV 3CQP ARG C   85  UNP  P00441    GLY    86 VARIANT                        
SEQADV 3CQP ARG D   85  UNP  P00441    GLY    86 VARIANT                        
SEQRES   1 A  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 A  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 A  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 A  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 A  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 A  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 A  153  ARG HIS VAL GLY ASP LEU ARG ASN VAL THR ALA ASP LYS          
SEQRES   8 A  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 A  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 A  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 A  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 A  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 B  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 B  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 B  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 B  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 B  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 B  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 B  153  ARG HIS VAL GLY ASP LEU ARG ASN VAL THR ALA ASP LYS          
SEQRES   8 B  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 B  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 B  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 B  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 B  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 C  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 C  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 C  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 C  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 C  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 C  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 C  153  ARG HIS VAL GLY ASP LEU ARG ASN VAL THR ALA ASP LYS          
SEQRES   8 C  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 C  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 C  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 C  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 C  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 D  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 D  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 D  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 D  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 D  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 D  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 D  153  ARG HIS VAL GLY ASP LEU ARG ASN VAL THR ALA ASP LYS          
SEQRES   8 D  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 D  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 D  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 D  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 D  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
HET     CU  A 154       1                                                       
HET     ZN  A 155       1                                                       
HET     CU  B 154       1                                                       
HET     ZN  B 155       1                                                       
HET     CU  C 154       1                                                       
HET     CU  D 154       1                                                       
HET     ZN  D 155       1                                                       
HET    MLI  A 156       7                                                       
HET    MLI  A 157       7                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
HETNAM     MLI MALONATE ION                                                     
FORMUL   5   CU    4(CU 2+)                                                     
FORMUL   6   ZN    3(ZN 2+)                                                     
FORMUL  12  MLI    2(C3 H2 O4 2-)                                               
FORMUL  14  HOH   *343(H2 O)                                                    
HELIX    1   1 ALA A   55  GLY A   61  5                                   7    
HELIX    2   2 ASN A  131  LYS A  136  5                                   6    
HELIX    3   3 ALA B   55  GLY B   61  5                                   7    
HELIX    4   4 ASN B  131  GLY B  138  1                                   8    
HELIX    5   5 ALA C   55  GLY C   61  5                                   7    
HELIX    6   6 SER C  107  CYS C  111  5                                   5    
HELIX    7   7 ALA D   55  GLY D   61  5                                   7    
HELIX    8   8 GLU D  133  GLY D  138  1                                   6    
SHEET    1   A 5 ALA A  95  ASP A 101  0                                        
SHEET    2   A 5 VAL A  29  LYS A  36 -1  N  VAL A  31   O  ILE A  99           
SHEET    3   A 5 GLN A  15  GLU A  21 -1  N  ASN A  19   O  TRP A  32           
SHEET    4   A 5 LYS A   3  LEU A   8 -1  N  ALA A   4   O  PHE A  20           
SHEET    5   A 5 GLY A 150  ALA A 152 -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  ALA A 145   N  VAL A 119           
SHEET    1   C 5 ALA B  95  ASP B 101  0                                        
SHEET    2   C 5 VAL B  29  LYS B  36 -1  N  ILE B  35   O  ALA B  95           
SHEET    3   C 5 GLN B  15  GLU B  21 -1  N  ASN B  19   O  TRP B  32           
SHEET    4   C 5 LYS B   3  LEU B   8 -1  N  ALA B   4   O  PHE B  20           
SHEET    5   C 5 GLY B 150  ILE B 151 -1  O  GLY B 150   N  VAL B   5           
SHEET    1   D 4 ASP B  83  ALA B  89  0                                        
SHEET    2   D 4 GLY B  41  HIS B  48 -1  N  GLY B  41   O  ALA B  89           
SHEET    3   D 4 THR B 116  HIS B 120 -1  O  THR B 116   N  HIS B  48           
SHEET    4   D 4 ARG B 143  VAL B 148 -1  O  GLY B 147   N  LEU B 117           
SHEET    1   E 5 ALA C  95  ASP C 101  0                                        
SHEET    2   E 5 VAL C  29  LYS C  36 -1  N  VAL C  31   O  ILE C  99           
SHEET    3   E 5 GLN C  15  GLU C  21 -1  N  ASN C  19   O  TRP C  32           
SHEET    4   E 5 LYS C   3  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  THR C 116   N  HIS C  48           
SHEET    4   F 4 ARG C 143  VAL C 148 -1  O  LEU C 144   N  VAL C 119           
SHEET    1   G 5 ALA D  95  ASP D 101  0                                        
SHEET    2   G 5 VAL D  29  LYS D  36 -1  N  VAL D  31   O  ILE D  99           
SHEET    3   G 5 GLN D  15  GLU D  21 -1  N  ASN D  19   O  TRP D  32           
SHEET    4   G 5 LYS D   3  LYS D   9 -1  N  ALA D   4   O  PHE D  20           
SHEET    5   G 5 GLY D 150  ILE D 151 -1  O  GLY D 150   N  VAL D   5           
SHEET    1   H 4 ASP D  83  ALA D  89  0                                        
SHEET    2   H 4 GLY D  41  HIS D  48 -1  N  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  LEU D 144   N  VAL D 119           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.45  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.54  
SSBOND   3 CYS C   57    CYS C  146                          1555   1555  2.60  
SSBOND   4 CYS D   57    CYS D  146                          1555   1555  2.65  
LINK         ND1 HIS A  46                CU    CU A 154     1555   1555  2.36  
LINK         NE2 HIS A  48                CU    CU A 154     1555   1555  2.04  
LINK         ND1 HIS A  63                ZN    ZN A 155     1555   1555  1.95  
LINK         ND1 HIS A  71                ZN    ZN A 155     1555   1555  2.11  
LINK         ND1 HIS A  80                ZN    ZN A 155     1555   1555  2.06  
LINK         OD1 ASP A  83                ZN    ZN A 155     1555   1555  1.96  
LINK         NE2 HIS A 120                CU    CU A 154     1555   1555  1.94  
LINK         ND1 HIS B  46                CU    CU B 154     1555   1555  2.26  
LINK         NE2 HIS B  48                CU    CU B 154     1555   1555  2.02  
LINK         ND1 HIS B  63                ZN    ZN B 155     1555   1555  2.07  
LINK         ND1 HIS B  71                ZN    ZN B 155     1555   1555  2.11  
LINK         ND1 HIS B  80                ZN    ZN B 155     1555   1555  2.04  
LINK         OD1 ASP B  83                ZN    ZN B 155     1555   1555  2.01  
LINK         NE2 HIS B 120                CU    CU B 154     1555   1555  1.90  
LINK         ND1 HIS C  46                CU    CU C 154     1555   1555  2.31  
LINK         NE2 HIS C  48                CU    CU C 154     1555   1555  2.13  
LINK         NE2 HIS C 120                CU    CU C 154     1555   1555  2.10  
LINK         ND1 HIS D  46                CU    CU D 154     1555   1555  2.28  
LINK         NE2 HIS D  48                CU    CU D 154     1555   1555  2.00  
LINK         ND1 HIS D  63                ZN    ZN D 155     1555   1555  2.05  
LINK         ND1 HIS D  71                ZN    ZN D 155     1555   1555  2.09  
LINK         ND1 HIS D  80                ZN    ZN D 155     1555   1555  2.03  
LINK         OD1 ASP D  83                ZN    ZN D 155     1555   1555  1.94  
LINK         NE2 HIS D 120                CU    CU D 154     1555   1555  2.03  
LINK        CU    CU A 154                 O6  MLI A 157     1555   1555  1.76  
SITE     1 AC1  4 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     1 AC2  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC3  4 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     1 AC4  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     1 AC5  4 HIS C  46  HIS C  48  HIS C 120  HOH C 204                    
SITE     1 AC6  4 HIS D  46  HIS D  48  HIS D  63  HIS D 120                    
SITE     1 AC7  4 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     1 AC8  7 PRO A  74  ARG A  85  LEU A 126  LYS A 128                    
SITE     2 AC8  7 GLY C  10  GLY C  56  CYS C  57                               
SITE     1 AC9  9 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC9  9 THR A 137  GLY A 141  ARG A 143  HOH A 192                    
SITE     3 AC9  9 HOH A 244                                                     
CRYST1   73.472  116.808  147.764  90.00  90.00  90.00 I 21 21 21   32          
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      0.013611  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008561  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006768        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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