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Database: PDB
Entry: 4A7S
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HEADER    OXIDOREDUCTASE                          14-NOV-11   4A7S              
TITLE     STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH 5-                
TITLE    2 FLUOROURIDINE IN THE P21 SPACE GROUP                                 
CAVEAT     4A7S   5UD A 1159  HAS WRONG CHIRALITY AT ATOM  C3'                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, F;                                                         
COMPND   4 SYNONYM: SUPEROXIDE DISMUTASE 1, HSOD1;                              
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 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;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET303                                     
KEYWDS    OXIDOREDUCTASE, AMYOTROPHIC LATERAL SCLEROSIS, ANTIOXIDANT            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.S.A.WRIGHT,S.V.ANTONYUK,N.M.KERSHAW,R.W.STRANGE,S.S.HASNAIN         
REVDAT   3   08-MAY-13 4A7S    1       JRNL                                     
REVDAT   2   24-APR-13 4A7S    1       JRNL                                     
REVDAT   1   05-DEC-12 4A7S    0                                                
JRNL        AUTH   G.S.A.WRIGHT,S.V.ANTONYUK,N.M.KERSHAW,R.W.STRANGE,           
JRNL        AUTH 2 S.S.HASNAIN                                                  
JRNL        TITL   LIGAND BINDING AND AGGREGATION OF PATHOGENIC SOD1.           
JRNL        REF    NAT.COMMUN.                   V.   4  1758 2013              
JRNL        REFN                   ISSN 2041-1723                               
JRNL        PMID   23612299                                                     
JRNL        DOI    10.1038/NCOMMS2750                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.06 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 1.06                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.00                         
REMARK   3   NUMBER OF REFLECTIONS             : 99352                          
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) : 0.16394                         
REMARK   3   R VALUE            (WORKING SET) : 0.16202                         
REMARK   3   FREE R VALUE                     : 0.20002                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 5229                            
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) : 1.057                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.084                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4843                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.244                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 254                          
REMARK   3   BIN FREE R VALUE                    : 0.264                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2360                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 75                                      
REMARK   3   SOLVENT ATOMS            : 462                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 11.6                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 9.470                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.82                                                 
REMARK   3    B22 (A**2) : -0.25                                                
REMARK   3    B33 (A**2) : -0.58                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -0.01                                                
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.035         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.037         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.025         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.111         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.954                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2486 ; 0.015 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1613 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3398 ; 1.717 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4008 ; 1.217 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   346 ; 6.871 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   105 ;37.411 ;25.905       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   406 ;11.499 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;11.603 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   372 ; 0.140 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2896 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   452 ; 0.003 ; 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):  1592 ; 1.772 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   681 ; 0.649 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2559 ; 2.520 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   894 ; 3.358 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   827 ; 4.595 ; 4.500       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  4099 ; 1.494 ; 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          
REMARK   3   RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY.                   
REMARK   4                                                                      
REMARK   4 4A7S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-NOV-11.                  
REMARK 100 THE PDBE ID CODE IS EBI-50326.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-FEB-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) : 0.787                              
REMARK 200  MONOCHROMATOR                  : SI111                              
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 104581                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.06                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.8                               
REMARK 200  DATA REDUNDANCY                : 2.4                                
REMARK 200  R MERGE                    (I) : 0.01                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.50                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.06                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 68.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.6                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.42                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.50                               
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   (%): 31.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM ACETATE, 150 MM            
REMARK 280  SODIUM CHLORIDE, 2.5 AMMONIUM SULPHATE PH 5                         
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       34.07000            
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: 2920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.9 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 A    19     O    HOH A  2047              1.57            
REMARK 500   NZ A LYS A    30     F5   5UD A  1159              2.07            
REMARK 500   CG2B THR A    58     O1   SO4 A  1156              2.11            
REMARK 500   CA   GLY A   138     O    HOH A  2195              1.88            
REMARK 500   ND2  ASN A   139     O    HOH A  2194              1.79            
REMARK 500   OXT  GLN A   153     O    HOH A  2214              1.99            
REMARK 500   O    ASP F    92     O    HOH F  2167              2.20            
REMARK 500   O    HOH A  2016     O  B HOH A  2211              2.09            
REMARK 500   O    HOH A  2055     O  A HOH F  2227              2.05            
REMARK 500   O    HOH A  2085     O    HOH A  2087              1.89            
REMARK 500   O    HOH A  2104     O    HOH A  2106              1.67            
REMARK 500   O    HOH A  2108     O    HOH A  2115              2.10            
REMARK 500   O    HOH A  2163     O    HOH A  2164              2.12            
REMARK 500   O    HOH A  2177     O    HOH A  2178              2.13            
REMARK 500   O    HOH A  2194     O    HOH A  2195              1.84            
REMARK 500   O    HOH F  2010     O    HOH F  2014              2.12            
REMARK 500   O    HOH F  2010     O    HOH F  2011              2.03            
REMARK 500   O    HOH F  2067     O    HOH F  2175              2.09            
REMARK 500   O    HOH F  2073     O    HOH F  2074              2.19            
REMARK 500   O    HOH F  2081     O    HOH F  2083              1.68            
REMARK 500   O    HOH F  2097     O    HOH F  2099              2.06            
REMARK 500   O    HOH F  2127     O    HOH F  2128              1.22            
REMARK 500   O    HOH F  2146     O    HOH F  2147              1.49            
REMARK 500   O    HOH F  2147     O    HOH F  2149              1.86            
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   OE2A GLU A    40     O    HOH F  2098     2646     1.36            
REMARK 500   OG B SER A    98     O    HOH F  2232     2646     2.14            
REMARK 500   OD2B ASP A   109     O    HOH A  2089     1655     2.09            
REMARK 500   O  A HOH A  2099     O  B HOH A  2099     2646     1.65            
REMARK 500   O  A HOH F  2112     O    HOH A  2153     2656     1.76            
REMARK 500   O    HOH F  2127     O    HOH A  2159     2656     1.63            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  92   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    HIS F  43         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  71   ND1                                                    
REMARK 620 2 HIS A  63   ND1 104.8                                              
REMARK 620 3 HIS A  80   ND1 121.1 111.3                                        
REMARK 620 4 ASP A  83   OD1  99.8 102.1 115.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F1156  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  63   ND1                                                    
REMARK 620 2 HIS F  71   ND1 105.3                                              
REMARK 620 3 HIS F  80   ND1 111.2 121.2                                        
REMARK 620 4 ASP F  83   OD1 103.9  99.3 114.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A1154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 120   NE2                                                    
REMARK 620 2 HIS A  48   NE2 108.8                                              
REMARK 620 3 HIS A  46   ND1 101.5 149.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU F1155  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  46   ND1                                                    
REMARK 620 2 HIS F  48   NE2 150.0                                              
REMARK 620 3 HIS F 120   NE2 101.3 108.5                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU A1154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F1154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1157                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU F1155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN F1156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F1157                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F1158                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1158                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT F1159                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5UD A1159                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5UD F1160                 
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                    
REMARK 900  DISMUTASE,FAMILIAL AMYOTROPHIC LATERAL SCLEROSIS (FALS)             
REMARK 900  MUTANT H43R                                                         
REMARK 900 RELATED ID: 1OEZ   RELATED DB: PDB                                   
REMARK 900  ZN HIS46ARG MUTANT OF HUMAN CU, ZN SUPEROXIDE                       
REMARK 900  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                   
REMARK 900  DISMUTASE                                                           
REMARK 900 RELATED ID: 2WYZ   RELATED DB: PDB                                   
REMARK 900  L38V SOD1 MUTANT COMPLEXED WITH UMP                                 
REMARK 900 RELATED ID: 4A7Q   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH 4               
REMARK 900  -(4-METHYL-1,4-DIAZEPAN-1-YL)QUINAZOLINE IN THE                     
REMARK 900  P21 SPACE GROUP.                                                    
REMARK 900 RELATED ID: 1OZU   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF FAMILIAL ALS MUTANT S134N OF                   
REMARK 900  HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) TO 1.3A                  
REMARK 900  RESOLUTION                                                          
REMARK 900 RELATED ID: 2VR6   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN                 
REMARK 900   SUPEROXIDE 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               
REMARK 900  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               
REMARK 900  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                
REMARK 900  GLU, CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY                  
REMARK 900   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              
REMARK 900   AND CYS 111 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-                  
REMARK 900  ZINCSUPEROXIDE 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               
REMARK 900  SOD:THE 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                  
REMARK 900  DEPLETEDHUMAN 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                 
REMARK 900   SUPEROXIDE 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:               
REMARK 900  ROLEOF METAL IONS IN PROTEIN FOLDING                                
REMARK 900 RELATED ID: 2VR7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN                 
REMARK 900   SUPEROXIDE 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               
REMARK 900   BY ALA AND CYS 111 REPLACED BY SER (C6A,C111S)                     
REMARK 900  WITH AN 18-RESIDUE HEPARIN-BINDING PEPTIDE FUSED TO                 
REMARK 900  THE C-TERMINUS (THEORETICAL MODEL)                                  
REMARK 900 RELATED ID: 2C9S   RELATED DB: PDB                                   
REMARK 900  1.24 ANGSTROMS RESOLUTION STRUCTURE OF ZN-ZN HUMAN                  
REMARK 900  SUPEROXIDE DISMUTASE                                                
REMARK 900 RELATED ID: 2V0A   RELATED DB: PDB                                   
REMARK 900  ATOMIC RESOLUTION CRYSTAL STRUCTURE OF HUMAN SUPEROXIDE             
REMARK 900  DISMUTASE                                                           
REMARK 900 RELATED ID: 1MFM   RELATED DB: PDB                                   
REMARK 900  MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q AT ATOMIC                
REMARK 900  RESOLUTION                                                          
REMARK 900 RELATED ID: 2WYT   RELATED DB: PDB                                   
REMARK 900  1.0 A RESOLUTION STRUCTURE OF L38V SOD1 MUTANT                      
REMARK 900 RELATED ID: 4A7G   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH 4               
REMARK 900  -METHYLPIPERAZIN-1-YL)QUINAZOLINE IN THE P21 SPACE                  
REMARK 900  GROUP.                                                              
REMARK 900 RELATED ID: 1DSW   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF A MONOMERIC, REDUCED FORM                 
REMARK 900  OFHUMAN COPPER, ZINC SUPEROXIDE DISMUTASE BEARING THE               
REMARK 900  SAMECHARGE AS THE NATIVE PROTEIN                                    
REMARK 900 RELATED ID: 1KMG   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF MONOMERIC COPPER-FREE                     
REMARK 900  SUPEROXIDEDISMUTASE                                                 
REMARK 900 RELATED ID: 1OZT   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF APO-H46R FAMILIAL ALS MUTANT                   
REMARK 900  HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) TO 2.5A                  
REMARK 900  RESOLUTION                                                          
REMARK 900 RELATED ID: 1N18   RELATED DB: PDB                                   
REMARK 900  THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE DISMUTASE, C6A,             
REMARK 900  C111S                                                               
REMARK 900 RELATED ID: 1BA9   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF REDUCED MONOMERIC SUPEROXIDE              
REMARK 900  DISMUTASE, NMR, 36 STRUCTURES                                       
REMARK 900 RELATED ID: 2C9U   RELATED DB: PDB                                   
REMARK 900  1.24 ANGSTROMS RESOLUTION STRUCTURE OF AS-ISOLATED CU               
REMARK 900  -ZN HUMAN SUPEROXIDE DISMUTASE                                      
REMARK 900 RELATED ID: 1HL5   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE                  
REMARK 900  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                                            
REMARK 900 RELATED ID: 4A7U   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN I113T SOD1 COMPLEXED WITH DOPAMINE               
REMARK 900  IN THE P21 SPACE GROUP.                                             
REMARK 900 RELATED ID: 4A7T   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH                 
REMARK 900  ISOPROTERANOL IN THE P21 SPACE GROUP                                
REMARK 900 RELATED ID: 4A7R   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH 4               
REMARK 900  -(4-METHYL-1,4-DIAZEPAN-1-YL)-2-(TRIFLUOROMETHYL)                   
REMARK 900  QUINAZOLINE IN THE P21 SPACE GROUP                                  
REMARK 900 RELATED ID: 4A7V   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH                 
REMARK 900  EPINEPHRINE (ADRENALINE) IN THE P21 SPACE GROUP                     
DBREF  4A7S A    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  4A7S F    1   153  UNP    P00441   SODC_HUMAN       2    154             
SEQADV 4A7S THR A  113  UNP  P00441    ILE   114 ENGINEERED MUTATION            
SEQADV 4A7S 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 ILE 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     CU  A1154       2                                                       
HET     ZN  A1155       1                                                       
HET    SO4  A1156       5                                                       
HET    SO4  F1154       5                                                       
HET    SO4  A1157       5                                                       
HET     CU  F1155       2                                                       
HET     ZN  F1156       1                                                       
HET    SO4  F1157       5                                                       
HET    SO4  F1158       5                                                       
HET    ACT  A1158       4                                                       
HET    ACT  F1159       4                                                       
HET    5UD  A1159      18                                                       
HET    5UD  F1160      18                                                       
HETNAM     5UD 5-FLUOROURIDINE                                                  
HETNAM     SO4 SULFATE ION                                                      
HETNAM      ZN ZINC ION                                                         
HETNAM     ACT ACETATE ION                                                      
HETNAM      CU COPPER (II) ION                                                  
FORMUL   3  5UD    2(C9 H11 F N2 O6)                                            
FORMUL   4  SO4    5(O4 S 2-)                                                   
FORMUL   5   ZN    2(ZN 2+)                                                     
FORMUL   6  ACT    2(C2 H3 O2 1-)                                               
FORMUL   7   CU    2(CU 2+)                                                     
FORMUL   8  HOH   *462(H2 O)                                                    
HELIX    1   1 GLY A   56  GLY A   61  5                                   6    
HELIX    2   2 SER A  107  HIS A  110  5                                   4    
HELIX    3   3 GLU A  132  LYS A  136  5                                   5    
HELIX    4   4 GLY F   56  GLY F   61  5                                   6    
HELIX    5   5 GLU F  133  GLY F  138  1                                   6    
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 GLN F  15  GLN F  22 -1  O  GLN F  15   N  LYS F  36           
SHEET    4  FA 5 THR F   2  LEU F   8 -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  2.04  
SSBOND   2 CYS F   57    CYS F  146                          1555   1555  2.03  
LINK        CU  A CU A1154                 NE2 HIS A 120     1555   1555  1.85  
LINK        CU  A CU A1154                 NE2 HIS A  48     1555   1555  1.90  
LINK        CU  A CU A1154                 ND1 HIS A  46     1555   1555  2.08  
LINK        CU  B CU A1154                 NE2 HIS A 120     1555   1555  2.36  
LINK        CU  B CU A1154                 NE2 HIS A  48     1555   1555  2.45  
LINK        CU  B CU A1154                 NE2 HIS A  63     1555   1555  2.17  
LINK        CU  B CU A1154                 ND1 HIS A  46     1555   1555  2.00  
LINK        ZN    ZN A1155                 ND1 HIS A  71     1555   1555  2.02  
LINK        ZN    ZN A1155                 ND1 HIS A  63     1555   1555  2.02  
LINK        ZN    ZN A1155                 ND1 HIS A  80     1555   1555  2.08  
LINK        ZN    ZN A1155                 OD1 ASP A  83     1555   1555  1.94  
LINK        CU  B CU F1155                 ND1 HIS F  46     1555   1555  2.08  
LINK        CU  A CU F1155                 NE2 HIS F 120     1555   1555  1.83  
LINK        CU  A CU F1155                 NE2 HIS F  48     1555   1555  1.87  
LINK        CU  A CU F1155                 ND1 HIS F  46     1555   1555  2.13  
LINK        CU  B CU F1155                 NE2 HIS F  48     1555   1555  2.49  
LINK        CU  B CU F1155                 NE2 HIS F 120     1555   1555  2.23  
LINK        CU  B CU F1155                 NE2 HIS F  63     1555   1555  2.23  
LINK        CU  B CU F1155                 O   HOH F2096     1555   1555  2.63  
LINK        ZN    ZN F1156                 OD1 ASP F  83     1555   1555  1.93  
LINK        ZN    ZN F1156                 ND1 HIS F  80     1555   1555  2.03  
LINK        ZN    ZN F1156                 ND1 HIS F  71     1555   1555  2.04  
LINK        ZN    ZN F1156                 ND1 HIS F  63     1555   1555  1.99  
SITE     1 AC1  5 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC1  5 HOH A2100                                                     
SITE     1 AC2  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC3  9 THR A  58  SER A 142  ARG A 143  HOH A2119                    
SITE     2 AC3  9 HOH A2120  HOH A2206  HOH A2208  HOH A2220                    
SITE     3 AC3  9 HOH A2221                                                     
SITE     1 AC4  8 ASN A 131  GLU A 132  HOH A2200  HOH A2201                    
SITE     2 AC4  8 ASN F 131  GLU F 132  HOH F2215  HOH F2216                    
SITE     1 AC5  9 GLU A 133  THR A 137  ASN A 139  ALA A 140                    
SITE     2 AC5  9 GLY A 141  HOH A2188  HOH A2191  HOH A2205                    
SITE     3 AC5  9 HOH A2222                                                     
SITE     1 AC6  5 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     2 AC6  5 HOH F2096                                                     
SITE     1 AC7  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 AC8 10 GLU F 133  THR F 137  ASN F 139  ALA F 140                    
SITE     2 AC8 10 GLY F 141  HOH F2197  HOH F2203  HOH F2220                    
SITE     3 AC8 10 HOH F2222  HOH F2232                                          
SITE     1 AC9  8 THR F  58  SER F 142  ARG F 143  HOH F2111                    
SITE     2 AC9  8 HOH F2221  HOH F2224  HOH F2233  HOH F2235                    
SITE     1 BC1  5 GLU A  49  ARG A 115  HOH A2223  HOH A2225                    
SITE     2 BC1  5 ILE F 151                                                     
SITE     1 BC2  3 GLN F  15  LYS F  36  HOH F2027                               
SITE     1 BC3  6 LYS A  30  TRP A  32  SER A  98  HOH A2071                    
SITE     2 BC3  6 HOH A2165  HOH F2238                                          
SITE     1 BC4  4 GLU F  21  LYS F  30  TRP F  32  SER F  98                    
CRYST1   38.030   68.140   49.050  90.00 104.19  90.00 P 1 21 1      4          
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      0.026295  0.000000  0.006649        0.00000                         
SCALE2      0.000000  0.014676  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021029        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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