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Database: PDB
Entry: 4A7G
LinkDB: 4A7G
Original site: 4A7G 
HEADER    OXIDOREDUCTASE                          14-NOV-11   4A7G              
TITLE     STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH 4-METHYLPIPERAZIN-
TITLE    2 1-YL)QUINAZOLINE IN THE P21 SPACE GROUP.                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SUPEROXIDE DISMUTASE-1, SUPEROXIDE DISMUTASE 1, HSOD1;      
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND  10 CHAIN: F;                                                            
COMPND  11 SYNONYM: SUPEROXIDE DISMUTASE-1, SUPEROXIDE DISMUTASE 1, HSOD1;      
COMPND  12 EC: 1.15.1.1;                                                        
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MUTATION: 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: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET303;                                   
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PET303                                    
KEYWDS    OXIDOREDUCTASE, AMYOTROPHIC LATERAL SCLEROSIS, ANTIOXIDANT, DISEASE   
KEYWDS   2 MUTATION, METAL-BINDING, ZN SUPEROXIDE DISMUTASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.S.A.WRIGHT,N.M.KERSHAW,R.SHARMA,S.V.ANTONYUK,R.W.STRANGE,N.G.BERRY, 
AUTHOR   2 P.M.O'NEIL,S.S.HASNAIN                                               
REVDAT   5   21-NOV-18 4A7G    1       SOURCE                                   
REVDAT   4   14-NOV-18 4A7G    1       JRNL                                     
REVDAT   3   28-AUG-13 4A7G    1       JRNL                                     
REVDAT   2   13-MAR-13 4A7G    1       JRNL                                     
REVDAT   1   24-OCT-12 4A7G    0                                                
JRNL        AUTH   N.M.KERSHAW,G.S.WRIGHT,R.SHARMA,S.V.ANTONYUK,R.W.STRANGE,    
JRNL        AUTH 2 N.G.BERRY,P.M.O'NEILL,S.S.HASNAIN                            
JRNL        TITL   X-RAY CRYSTALLOGRAPHY AND COMPUTATIONAL DOCKING FOR THE      
JRNL        TITL 2 DETECTION AND DEVELOPMENT OF PROTEIN-LIGAND INTERACTIONS.    
JRNL        REF    CURR. MED. CHEM.              V.  20   569 2013              
JRNL        REFN                   ISSN 1875-533X                               
JRNL        PMID   23278398                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.24 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.24                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.33                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 67694                          
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) : 0.141                           
REMARK   3   R VALUE            (WORKING SET) : 0.139                           
REMARK   3   FREE R VALUE                     : 0.175                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3616                            
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) : 1.24                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.27                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4882                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.44                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2500                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 262                          
REMARK   3   BIN FREE R VALUE                    : 0.2850                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2217                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 84                                      
REMARK   3   SOLVENT ATOMS            : 388                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 10.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.05                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.19000                                             
REMARK   3    B22 (A**2) : -0.12000                                             
REMARK   3    B33 (A**2) : 0.36000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.11000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.046         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.046         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.029         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.485         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.978                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.966                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2533 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1654 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3456 ; 1.612 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4089 ; 0.902 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   349 ; 6.805 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   103 ;38.441 ;25.728       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   403 ;11.751 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;16.406 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   363 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3012 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   471 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  1633 ; 1.575 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   699 ; 0.499 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2626 ; 2.426 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   900 ; 3.361 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   830 ; 4.736 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  4187 ; 1.272 ; 3.000       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. U VALUES REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 4A7G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-NOV-11.                  
REMARK 100 THE DEPOSITION ID IS D_1290050307.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.866                              
REMARK 200  MONOCHROMATOR                  : SI111                              
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 71339                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.240                              
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     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.24                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.69000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 34.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM ACETATE PH 5, 150 MM        
REMARK 280  SODIUM CHLORIDE, 2.5 M AMMONIUM SULPHATE                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       34.17600            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2480 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.8 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ILE 114 TO THR                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, ILE 114 TO THR                        
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   OD1  ASN F    53     O    HOH F  2066              1.53            
REMARK 500   OD1  ASP F    90     OD1  ASP F    92              1.65            
REMARK 500   OG1  THR A   135     O    HOH A  2188              1.80            
REMARK 500   O3   SO4 F  1158     O    HOH F  2076              1.84            
REMARK 500   O    HOH F  2114     O    HOH F  2115              1.93            
REMARK 500   ND1  HIS A   110     O    HOH A  2156              1.98            
REMARK 500   ND2  ASN F    53     O    HOH F  2070              2.05            
REMARK 500   OE2  GLU A   100     O    HOH A  2154              2.15            
REMARK 500   OE2  GLU A   133     O    HOH A  2192              2.16            
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 A  2085     O    HOH F  2081     2546     1.95            
REMARK 500   OE2  GLU A    40     O    HOH F  2081     2546     1.99            
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 F 109   CB  -  CG  -  OD2 ANGL. DEV. =   6.9 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    PRO F  13       49.51   -103.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY F   12     PRO F   13                  -30.87                    
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                              CU A1157  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  48   NE2                                                    
REMARK 620 2 HIS A 120   NE2 111.4                                              
REMARK 620 3 HIS A  46   ND1 146.4 101.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1158  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  83   OD1                                                    
REMARK 620 2 HIS A  71   ND1  98.6                                              
REMARK 620 3 HIS A  63   ND1 102.6 104.6                                        
REMARK 620 4 HIS A  80   ND1 115.2 121.9 111.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU F1156  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F 120   NE2                                                    
REMARK 620 2 HIS F  48   NE2 108.9                                              
REMARK 620 3 HIS F  46   ND1 102.5 147.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU F1156  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  46   ND1                                                    
REMARK 620 2 HIS F  48   NE2 123.0                                              
REMARK 620 3 HIS F 120   NE2  93.5 125.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F1157  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F  83   OD1                                                    
REMARK 620 2 HIS F  80   ND1 116.1                                              
REMARK 620 3 HIS F  71   ND1  98.9 122.0                                        
REMARK 620 4 HIS F  63   ND1 104.3 109.8 103.7                                  
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 12I A 1000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 12I A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1154                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1156                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 1157                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1158                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1159                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 12I F 1000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 1154                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU F 1156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 1157                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 1155                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 1158                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 12I F 1000                
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: 1PTZ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CU, ZN SUPEROXIDE DISMUTASE,FAMILIAL  
REMARK 900 AMYOTROPHIC LATERAL SCLEROSIS (FALS) MUTANT H43R                     
REMARK 900 RELATED ID: 1OEZ   RELATED DB: PDB                                   
REMARK 900 ZN HIS46ARG MUTANT OF HUMAN CU, ZN SUPEROXIDE DISMUTASE              
REMARK 900 RELATED ID: 1AZV   RELATED DB: PDB                                   
REMARK 900 FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)                             
REMARK 900 RELATED ID: 1HL4   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF APO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE          
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 S134N OF HUMAN CU,ZN        
REMARK 900 SUPEROXIDE DISMUTASE (CUZNSOD) TO 1.3A RESOLUTION                    
REMARK 900 RELATED ID: 2VR6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE       
REMARK 900 DISMUTASE (CUZNSOD) AT 1.3 A RESOLUTION                              
REMARK 900 RELATED ID: 2C9V   RELATED DB: PDB                                   
REMARK 900 ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN SUPEROXIDE DISMUTASE      
REMARK 900 RELATED ID: 2WZ5   RELATED DB: PDB                                   
REMARK 900 L38V SOD1 MUTANT COMPLEXED WITH L-METHIONINE.                        
REMARK 900 RELATED ID: 2XJL   RELATED DB: PDB                                   
REMARK 900 MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE WITHOUT CU LIGANDS        
REMARK 900 RELATED ID: 1PU0   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN CU,ZN SUPEROXIDE DISMUTASE                        
REMARK 900 RELATED ID: 1FUN   RELATED DB: PDB                                   
REMARK 900 SUPEROXIDE DISMUTASE MUTANT WITH LYS 136 REPLACED BY GLU, CYS 6      
REMARK 900 REPLACED BY ALA AND CYS 111 REPLACED BY SER (K136E, C6A, 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 REPLACED BY ALA AND CYS 111   
REMARK 900 REPLACED BY 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 COPPER- ZINCSUPEROXIDE    
REMARK 900 DISMUTASE (CUZNSOD) MUTANT D125H TO 1.4A                             
REMARK 900 RELATED ID: 2WZ0   RELATED DB: PDB                                   
REMARK 900 L38V SOD1 MUTANT COMPLEXED WITH ANILINE.                             
REMARK 900 RELATED ID: 1L3N   RELATED DB: PDB                                   
REMARK 900 THE SOLUTION STRUCTURE OF REDUCED DIMERIC COPPER ZINC SOD:THE        
REMARK 900 STRUCTURAL EFFECTS OF DIMERIZATION                                   
REMARK 900 RELATED ID: 2WKO   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF METAL LOADED PATHOGENIC SOD1 MUTANT G93A.               
REMARK 900 RELATED ID: 2AF2   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF DISULFIDE REDUCED AND COPPER DEPLETEDHUMAN     
REMARK 900 SUPEROXIDE DISMUTASE                                                 
REMARK 900 RELATED ID: 1UXL   RELATED DB: PDB                                   
REMARK 900 I113T MUTANT OF HUMAN SOD1                                           
REMARK 900 RELATED ID: 2VR8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE       
REMARK 900 DISMUTASE (CUZNSOD) AT 1.36 A RESOLUTION                             
REMARK 900 RELATED ID: 1RK7   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF APO CU,ZN SUPEROXIDE DISMUTASE: ROLEOF METAL   
REMARK 900 IONS IN PROTEIN FOLDING                                              
REMARK 900 RELATED ID: 2VR7   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE       
REMARK 900 DISMUTASE (CUZNSOD) AT 1.58 A RESOLUTION                             
REMARK 900 RELATED ID: 4SOD   RELATED DB: PDB                                   
REMARK 900 CU,ZN SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA AND     
REMARK 900 CYS 111 REPLACED BY SER (C6A,C111S) WITH AN 18-RESIDUE HEPARIN-      
REMARK 900 BINDING PEPTIDE FUSED TO THE C-TERMINUS (THEORETICAL MODEL)          
REMARK 900 RELATED ID: 2C9S   RELATED DB: PDB                                   
REMARK 900 1.24 ANGSTROMS RESOLUTION STRUCTURE OF ZN-ZN HUMAN SUPEROXIDE        
REMARK 900 DISMUTASE                                                            
REMARK 900 RELATED ID: 2V0A   RELATED DB: PDB                                   
REMARK 900 ATOMIC RESOLUTION CRYSTAL STRUCTURE OF HUMAN SUPEROXIDE DISMUTASE    
REMARK 900 RELATED ID: 1MFM   RELATED DB: PDB                                   
REMARK 900 MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q AT ATOMIC RESOLUTION      
REMARK 900 RELATED ID: 2WYT   RELATED DB: PDB                                   
REMARK 900 1.0 A RESOLUTION STRUCTURE OF L38V SOD1 MUTANT                       
REMARK 900 RELATED ID: 1DSW   RELATED DB: PDB                                   
REMARK 900 THE SOLUTION STRUCTURE OF A MONOMERIC, REDUCED FORM OFHUMAN COPPER,  
REMARK 900 ZINC SUPEROXIDE DISMUTASE BEARING THE SAMECHARGE AS THE NATIVE       
REMARK 900 PROTEIN                                                              
REMARK 900 RELATED ID: 1KMG   RELATED DB: PDB                                   
REMARK 900 THE SOLUTION STRUCTURE OF MONOMERIC COPPER-FREE SUPEROXIDEDISMUTASE  
REMARK 900 RELATED ID: 1OZT   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF APO-H46R FAMILIAL ALS MUTANT HUMAN CU,ZN        
REMARK 900 SUPEROXIDE DISMUTASE (CUZNSOD) TO 2.5A RESOLUTION                    
REMARK 900 RELATED ID: 1N18   RELATED DB: PDB                                   
REMARK 900 THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE DISMUTASE, C6A, C111S        
REMARK 900 RELATED ID: 1BA9   RELATED DB: PDB                                   
REMARK 900 THE SOLUTION STRUCTURE OF REDUCED MONOMERIC SUPEROXIDE DISMUTASE,    
REMARK 900 NMR, 36 STRUCTURES                                                   
REMARK 900 RELATED ID: 2C9U   RELATED DB: PDB                                   
REMARK 900 1.24 ANGSTROMS RESOLUTION STRUCTURE OF AS-ISOLATED CU -ZN HUMAN      
REMARK 900 SUPEROXIDE DISMUTASE                                                 
REMARK 900 RELATED ID: 1HL5   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE         
REMARK 900 RELATED ID: 1SPD   RELATED DB: PDB                                   
REMARK 900 SUPEROXIDE DISMUTASE                                                 
REMARK 900 RELATED ID: 1UXM   RELATED DB: PDB                                   
REMARK 900 A4V MUTANT OF HUMAN SOD1                                             
DBREF  4A7G A    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  4A7G F    1   153  UNP    P00441   SODC_HUMAN       2    154             
SEQADV 4A7G THR A   99  UNP  P00441    ILE   100 CONFLICT                       
SEQADV 4A7G THR A  113  UNP  P00441    ILE   114 ENGINEERED MUTATION            
SEQADV 4A7G THR F  113  UNP  P00441    ILE   114 ENGINEERED MUTATION            
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 GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 A  153  ASP GLY VAL ALA ASP VAL SER THR GLU ASP SER VAL ILE          
SEQRES   9 A  153  SER LEU SER GLY ASP HIS CYS ILE THR 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 F  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 F  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 F  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 F  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 F  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 F  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 F  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 F  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 F  153  SER LEU SER GLY ASP HIS CYS ILE THR GLY ARG THR LEU          
SEQRES  10 F  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 F  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 F  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
HET    SO4  A1154       5                                                       
HET    12I  A1000      17                                                       
HET    SO4  A1156       5                                                       
HET    12I  A1001      17                                                       
HET     CU  A1157       1                                                       
HET     ZN  A1158       1                                                       
HET    ACT  A1159       4                                                       
HET    SO4  F1154       5                                                       
HET    SO4  F1155       5                                                       
HET     CU  F1156       2                                                       
HET    SO4  F1158       5                                                       
HET     ZN  F1157       1                                                       
HET    12I  F1000      17                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     12I 4-(4-METHYLPIPERAZIN-1-YL)QUINAZOLINE                            
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
HETNAM     ACT ACETATE ION                                                      
FORMUL   3  SO4    5(O4 S 2-)                                                   
FORMUL   4  12I    3(C13 H16 N4)                                                
FORMUL   7   CU    2(CU 2+)                                                     
FORMUL   8   ZN    2(ZN 2+)                                                     
FORMUL   9  ACT    C2 H3 O2 1-                                                  
FORMUL  16  HOH   *388(H2 O)                                                    
HELIX    1   1 GLY A   56  GLY A   61  5                                   6    
HELIX    2   2 GLU A  132  LYS A  136  5                                   5    
HELIX    3   3 GLY F   56  GLY F   61  5                                   6    
HELIX    4   4 GLU F  132  LYS F  136  5                                   5    
SHEET    1  AA 5 ALA A  95  ASP A 101  0                                        
SHEET    2  AA 5 VAL A  29  LYS A  36 -1  O  VAL A  29   N  ASP A 101           
SHEET    3  AA 5 GLN A  15  GLN A  22 -1  O  GLN A  15   N  LYS A  36           
SHEET    4  AA 5 THR A   2  LEU A   8 -1  O  THR A   2   N  GLN A  22           
SHEET    5  AA 5 GLY A 150  ILE A 151 -1  O  GLY A 150   N  VAL A   5           
SHEET    1  AB 4 ASP A  83  ALA A  89  0                                        
SHEET    2  AB 4 GLY A  41  HIS A  48 -1  O  GLY A  41   N  ALA A  89           
SHEET    3  AB 4 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    4  AB 4 ARG A 143  VAL A 148 -1  N  LEU A 144   O  VAL A 119           
SHEET    1  FA 5 ALA F  95  ASP F 101  0                                        
SHEET    2  FA 5 VAL F  29  LYS F  36 -1  O  VAL F  29   N  ASP F 101           
SHEET    3  FA 5 VAL F  14  GLN F  22 -1  O  GLN F  15   N  LYS F  36           
SHEET    4  FA 5 THR F   2  GLY F  10 -1  O  THR F   2   N  GLN F  22           
SHEET    5  FA 5 GLY F 150  ILE F 151 -1  O  GLY F 150   N  VAL F   5           
SHEET    1  FB 4 ASP F  83  ALA F  89  0                                        
SHEET    2  FB 4 GLY F  41  HIS F  48 -1  O  GLY F  41   N  ALA F  89           
SHEET    3  FB 4 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48           
SHEET    4  FB 4 ARG F 143  VAL F 148 -1  N  LEU F 144   O  VAL F 119           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.17  
SSBOND   2 CYS F   57    CYS F  146                          1555   1555  2.17  
LINK        CU    CU A1157                 NE2 HIS A  48     1555   1555  1.92  
LINK        CU    CU A1157                 NE2 HIS A 120     1555   1555  1.94  
LINK        CU    CU A1157                 ND1 HIS A  46     1555   1555  2.05  
LINK        ZN    ZN A1158                 OD1 ASP A  83     1555   1555  1.97  
LINK        ZN    ZN A1158                 ND1 HIS A  71     1555   1555  2.06  
LINK        ZN    ZN A1158                 ND1 HIS A  63     1555   1555  2.04  
LINK        ZN    ZN A1158                 ND1 HIS A  80     1555   1555  2.04  
LINK        CU  A CU F1156                 NE2 HIS F 120     1555   1555  1.99  
LINK        CU  A CU F1156                 NE2 HIS F  48     1555   1555  1.95  
LINK        CU  A CU F1156                 ND1 HIS F  46     1555   1555  2.05  
LINK        CU  B CU F1156                 ND1 HIS F  46     1555   1555  2.51  
LINK        CU  B CU F1156                 NE2 HIS F  48     1555   1555  1.85  
LINK        CU  B CU F1156                 NE2 HIS F 120     1555   1555  1.75  
LINK        ZN    ZN F1157                 OD1 ASP F  83     1555   1555  1.97  
LINK        ZN    ZN F1157                 ND1 HIS F  80     1555   1555  2.04  
LINK        ZN    ZN F1157                 ND1 HIS F  71     1555   1555  2.06  
LINK        ZN    ZN F1157                 ND1 HIS F  63     1555   1555  2.03  
CISPEP   1 GLY F   12    PRO F   13          0         2.48                     
SITE     1 AC1 15 SER A  25  ASN A  26  GLY A  27  LYS A  91                    
SITE     2 AC1 15 ASP A  92  GLY A  93  SER A 102  VAL A 103                    
SITE     3 AC1 15 SER A 105  SER A 107  ASP A 109  HIS A 110                    
SITE     4 AC1 15 ACT A1159  HOH A2060  HOH A2156                               
SITE     1 AC2  6 GLU A  21  LYS A  30  TRP A  32  SER A  98                    
SITE     2 AC2  6 HOH A2062  HOH A2214                                          
SITE     1 AC3  8 GLU A 133  THR A 137  ASN A 139  ALA A 140                    
SITE     2 AC3  8 GLY A 141  HOH A2172  HOH A2175  HOH A2192                    
SITE     1 AC4  6 THR A  58  SER A 142  ARG A 143  HOH A2196                    
SITE     2 AC4  6 HOH A2199  HOH A2212                                          
SITE     1 AC5  4 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     1 AC6  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC7  5 ASN A  26  GLY A  27  PRO A  28  SER A 102                    
SITE     2 AC7  5 12I A1000                                                     
SITE     1 AC8  1 TRP F  32                                                     
SITE     1 AC9  7 GLU F 133  THR F 137  ASN F 139  GLY F 141                    
SITE     2 AC9  7 HOH F2143  HOH F2164  HOH F2177                               
SITE     1 BC1  4 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     1 BC2  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 BC3  8 THR F  58  SER F 142  ARG F 143  SO4 F1158                    
SITE     2 BC3  8 HOH F2079  HOH F2163  HOH F2165  HOH F2166                    
SITE     1 BC4  9 ASP F  11  GLY F  56  CYS F  57  THR F  58                    
SITE     2 BC4  9 ARG F 143  SO4 F1155  HOH F2017  HOH F2074                    
SITE     3 BC4  9 HOH F2076                                                     
SITE     1 BC5  1 TRP F  32                                                     
CRYST1   38.793   68.352   49.920  90.00 104.49  90.00 P 1 21 1      2          
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      0.025778  0.000000  0.006662        0.00000                         
SCALE2      0.000000  0.014630  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020690        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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