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Database: PDB
Entry: 4A7Q
LinkDB: 4A7Q
Original site: 4A7Q 
HEADER    OXIDOREDUCTASE                          14-NOV-11   4A7Q              
TITLE     STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH 4-(4-             
TITLE    2 METHYL-1,4-DIAZEPAN-1-YL)QUINAZOLINE IN THE P21 SPACE                
TITLE    3 GROUP.                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, F;                                                         
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                                                        
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, 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.ONEIL,S.S.HASNAIN                                                
REVDAT   3   28-AUG-13 4A7Q    1       JRNL                                     
REVDAT   2   13-MAR-13 4A7Q    1       JRNL                                     
REVDAT   1   24-OCT-12 4A7Q    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 0929-8673                               
JRNL        PMID   23278398                                                     
JRNL        DOI    10.2174/0929867311320040008                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.22 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) : 1.22                           
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             : 66844                          
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) : 0.12664                         
REMARK   3   R VALUE            (WORKING SET) : 0.12488                         
REMARK   3   FREE R VALUE                     : 0.15925                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3519                            
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) : 1.218                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.250                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4006                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.207                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 211                          
REMARK   3   BIN FREE R VALUE                    : 0.234                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2441                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 72                                      
REMARK   3   SOLVENT ATOMS            : 477                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.3                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 10.156                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.45                                                 
REMARK   3    B22 (A**2) : -0.23                                                
REMARK   3    B33 (A**2) : -0.22                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.042         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.042         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.028         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.394         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.980                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.970                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2570 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1672 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3517 ; 1.638 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4140 ; 0.953 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   359 ; 6.675 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   109 ;38.701 ;25.780       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   415 ;11.053 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;12.567 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   372 ; 0.105 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3083 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   481 ; 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):  1657 ; 1.671 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   706 ; 0.549 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2679 ; 2.492 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   913 ; 3.444 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   838 ; 4.911 ; 4.500       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  4242 ; 1.398 ; 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 4A7Q 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-50315.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-JUN-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 (QUANTUM 315R)                 
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   : 70164                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.22                               
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     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 3.5                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.70                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.22                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.29                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.8                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.52                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.90                               
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 PH 5, 150 MM       
REMARK 280  SODIUM CHLORIDE, 2.5 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       34.10500            
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: 14220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 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   ND2  ASN A    19     O    HOH A  2055              1.85            
REMARK 500   CG2B THR A    58     O1   SO4 A  1156              2.08            
REMARK 500   OE1  GLU A    78     O    HOH A  2156              1.83            
REMARK 500   OG1  THR A   135     O    HOH A  2245              1.47            
REMARK 500   CD1B ILE F    17     O    HOH A  2131              2.15            
REMARK 500   OD1B ASN F    53     O    HOH A  2033              1.80            
REMARK 500   CG2B THR F    58     O3   SO4 F  1158              2.16            
REMARK 500   NH2B ARG F    69     OE1  GLU F    78              1.38            
REMARK 500   O    HOH A  2001     O    HOH A  2264              1.92            
REMARK 500   O    HOH A  2038     O    HOH A  2252              2.08            
REMARK 500   O    HOH A  2061     O  B HOH F  2206              1.96            
REMARK 500   O    HOH A  2092     O    HOH A  2203              2.12            
REMARK 500   O    HOH A  2105     O    HOH A  2106              1.75            
REMARK 500   O    HOH A  2120     O    HOH A  2228              1.95            
REMARK 500   O    HOH A  2124     O    HOH A  2127              1.77            
REMARK 500   O    HOH A  2156     O    HOH A  2159              1.93            
REMARK 500   O  B HOH A  2184     O    HOH A  2186              1.89            
REMARK 500   O    HOH A  2192     O    HOH A  2200              1.64            
REMARK 500   O    HOH A  2201     O    HOH A  2202              2.08            
REMARK 500   O    HOH A  2202     O    HOH A  2203              2.19            
REMARK 500   O    HOH F  2011     O    HOH F  2101              2.19            
REMARK 500   O    HOH F  2023     O    HOH F  2029              2.09            
REMARK 500   O    HOH F  2094     O    HOH F  2095              1.90            
REMARK 500   O    HOH F  2098     O  B HOH A  2255              2.10            
REMARK 500   O    HOH F  2120     O    HOH F  2130              1.88            
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   OD2A ASP A   109     O  B HOH A  2110     1655     1.62            
REMARK 500   O    HOH A  2002     O  B HOH F  2136     2545     2.02            
REMARK 500   O  B HOH F  2062     O    HOH A  2065     2555     2.06            
REMARK 500   O    HOH F  2095     O    HOH A  2119     2556     2.02            
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. =   6.8 DEGREES          
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  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 119.4                                              
REMARK 620 3 HIS A  63   NE2 101.2 114.5                                        
REMARK 620 4 HIS A 120   NE2  88.7  78.5 155.6                                  
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  46   ND1                                                    
REMARK 620 2 HIS F  48   NE2 149.6                                              
REMARK 620 3 HIS F 120   NE2 100.5 108.9                                        
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 HIS A  71   ND1                                                    
REMARK 620 2 HIS A  63   ND1 102.9                                              
REMARK 620 3 HIS A  80   ND1 123.0 111.8                                        
REMARK 620 4 ASP A  83   OD1  99.6 102.4 114.5                                  
REMARK 620 N                    1     2     3                                   
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 HIS F  63   ND1                                                    
REMARK 620 2 HIS F  71   ND1 105.3                                              
REMARK 620 3 HIS F  80   ND1 111.0 121.7                                        
REMARK 620 4 ASP F  83   OD1 103.6  99.5 113.7                                  
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 4MQ A1000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU A1157                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1158                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4MQ F1000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F1154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F1155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CU F1156                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN F1157                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F1158                 
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: 1HL4   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF APO TYPE 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: 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                   
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: 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: 2WZ0   RELATED DB: PDB                                   
REMARK 900  L38V SOD1 MUTANT COMPLEXED WITH ANILINE.                            
REMARK 900 RELATED ID: 2WKO   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF METAL LOADED PATHOGENIC SOD1 MUTANT G93A.              
REMARK 900 RELATED ID: 1UXL   RELATED DB: PDB                                   
REMARK 900  I113T MUTANT OF HUMAN SOD1                                          
REMARK 900 RELATED ID: 2AF2   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF DISULFIDE REDUCED AND COPPER                  
REMARK 900  DEPLETEDHUMAN SUPEROXIDE DISMUTASE                                  
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: 2C9S   RELATED DB: PDB                                   
REMARK 900  1.24 ANGSTROMS RESOLUTION STRUCTURE OF ZN-ZN HUMAN                  
REMARK 900  SUPEROXIDE DISMUTASE                                                
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: 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: 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: 1KMG   RELATED DB: PDB                                   
REMARK 900  THE SOLUTION STRUCTURE OF MONOMERIC COPPER-FREE                     
REMARK 900  SUPEROXIDEDISMUTASE                                                 
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: 1HL5   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE                  
REMARK 900  DISMUTASE                                                           
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: 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                     
REMARK 900 RELATED ID: 4A7S   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH 5               
REMARK 900  -FLUOROURIDINE IN THE P21 SPACE GROUP                               
DBREF  4A7Q A    1   153  UNP    P00441   SODC_HUMAN       2    154             
DBREF  4A7Q F    1   153  UNP    P00441   SODC_HUMAN       2    154             
SEQADV 4A7Q THR A  113  UNP  P00441    ILE   114 ENGINEERED MUTATION            
SEQADV 4A7Q 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    4MQ  A1000      18                                                       
HET    SO4  A1154       5                                                       
HET    SO4  A1155       5                                                       
HET    SO4  A1156       5                                                       
HET     CU  A1157       2                                                       
HET     ZN  A1158       1                                                       
HET    4MQ  F1000      18                                                       
HET    SO4  F1154       5                                                       
HET    SO4  F1155       5                                                       
HET     CU  F1156       2                                                       
HET     ZN  F1157       1                                                       
HET    SO4  F1158       5                                                       
HETNAM     4MQ 4-(4-METHYL-1,4-DIAZEPAN-1-YL)QUINAZOLINE                        
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
FORMUL   2  4MQ    2(C14 H18 N4)                                                
FORMUL   3  SO4    6(O4 S 2-)                                                   
FORMUL   4   CU    2(CU 2+)                                                     
FORMUL   5   ZN    2(ZN 2+)                                                     
FORMUL   6  HOH   *477(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 SER F  107  HIS F  110  5                                   4    
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 A1157                 ND1 HIS A  46     1555   1555  1.99  
LINK        CU  A CU A1157                 NE2 HIS A  48     1555   1555  2.43  
LINK        CU  A CU A1157                 NE2 HIS A  63     1555   1555  2.19  
LINK        CU  A CU A1157                 NE2 HIS A 120     1555   1555  2.38  
LINK        CU  B CU A1157                 ND1 HIS A  46     1555   1555  2.12  
LINK        CU  B CU A1157                 NE2 HIS A  48     1555   1555  1.83  
LINK        CU  B CU A1157                 NE2 HIS A 120     1555   1555  1.90  
LINK        ZN    ZN A1158                 OD1 ASP A  83     1555   1555  1.95  
LINK        ZN    ZN A1158                 ND1 HIS A  80     1555   1555  2.01  
LINK        ZN    ZN A1158                 ND1 HIS A  63     1555   1555  2.02  
LINK        ZN    ZN A1158                 ND1 HIS A  71     1555   1555  2.05  
LINK        CU  B CU F1156                 NE2 HIS F 120     1555   1555  2.22  
LINK        CU  B CU F1156                 NE2 HIS F  63     1555   1555  2.24  
LINK        CU  B CU F1156                 O   HOH F2089     1555   1555  2.63  
LINK        CU  B CU F1156                 NE2 HIS F  48     1555   1555  2.50  
LINK        CU  B CU F1156                 ND1 HIS F  46     1555   1555  2.06  
LINK        CU  A CU F1156                 NE2 HIS F 120     1555   1555  1.88  
LINK        CU  A CU F1156                 NE2 HIS F  48     1555   1555  1.86  
LINK        CU  A CU F1156                 ND1 HIS F  46     1555   1555  2.17  
LINK        ZN    ZN F1157                 ND1 HIS F  71     1555   1555  2.03  
LINK        ZN    ZN F1157                 ND1 HIS F  80     1555   1555  2.04  
LINK        ZN    ZN F1157                 OD1 ASP F  83     1555   1555  1.98  
LINK        ZN    ZN F1157                 ND1 HIS F  63     1555   1555  2.02  
SITE     1 AC1  5 LYS A  30  TRP A  32  SER A  98  HOH A2096                    
SITE     2 AC1  5 HOH A2098                                                     
SITE     1 AC2  9 GLU A 133  THR A 137  ASN A 139  ALA A 140                    
SITE     2 AC2  9 GLY A 141  HOH A2227  HOH A2231  HOH A2248                    
SITE     3 AC2  9 HOH A2250                                                     
SITE     1 AC3  5 GLU A  49  ARG A 115  HOH A2262  HOH A2263                    
SITE     2 AC3  5 HOH A2264                                                     
SITE     1 AC4  7 THR A  58  SER A 142  ARG A 143  HOH A2137                    
SITE     2 AC4  7 HOH A2138  HOH A2249  HOH A2266                               
SITE     1 AC5  5 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     2 AC5  5 HOH A2121                                                     
SITE     1 AC6  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC7  3 LYS F   3  GLU F  21  TRP F  32                               
SITE     1 AC8 10 GLU F 133  THR F 137  ASN F 139  ALA F 140                    
SITE     2 AC8 10 GLY F 141  HOH F2180  HOH F2188  HOH F2201                    
SITE     3 AC8 10 HOH F2203  HOH F2213                                          
SITE     1 AC9  9 ASN A 131  GLU A 132  HOH A2244  ASN F 131                    
SITE     2 AC9  9 GLU F 132  HOH F2198  HOH F2199  HOH F2214                    
SITE     3 AC9  9 HOH F2215                                                     
SITE     1 BC1  5 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     2 BC1  5 HOH F2089                                                     
SITE     1 BC2  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 BC3  7 THR F  58  SER F 142  ARG F 143  HOH F2202                    
SITE     2 BC3  7 HOH F2216  HOH F2217  HOH F2218                               
CRYST1   38.010   68.210   49.010  90.00 104.11  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      0.026309  0.000000  0.006613        0.00000                         
SCALE2      0.000000  0.014661  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021039        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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