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Database: PDB
Entry: 1T6U
LinkDB: 1T6U
Original site: 1T6U 
HEADER    OXIDOREDUCTASE                          07-MAY-04   1T6U              
TITLE     NICKEL SUPEROXIDE DISMUTASE (NISOD) NATIVE 1.30 A STRUCTURE           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [NI];                                 
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;                           
COMPND   4 SYNONYM: NISOD, NICKEL- CONTAINING SUPEROXIDE DISMUTASE;             
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOLOR;                        
SOURCE   3 ORGANISM_TAXID: 1902;                                                
SOURCE   4 GENE: SODN, SOD1, SCO5254, 2SC7G11.16C;                              
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;                              
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET26                                     
KEYWDS    NICKEL, 4-HELIX BUNDLE, HEXAMER, SUPEROXIDE DISMUTASE,                
KEYWDS   2 NISOD, SOD, HIGH RESOLUTION, OXIDOREDUCTASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.P.BARONDEAU,C.J.KASSMANN,C.K.BRUNS,J.A.TAINER,E.D.GETZOFF           
REVDAT   2   24-FEB-09 1T6U    1       VERSN                                    
REVDAT   1   13-JUL-04 1T6U    0                                                
JRNL        AUTH   D.P.BARONDEAU,C.J.KASSMANN,C.K.BRUNS,J.A.TAINER,             
JRNL        AUTH 2 E.D.GETZOFF                                                  
JRNL        TITL   NICKEL SUPEROXIDE DISMUTASE STRUCTURE AND                    
JRNL        TITL 2 MECHANISM.                                                   
JRNL        REF    BIOCHEMISTRY                  V.  43  8038 2004              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   15209499                                                     
JRNL        DOI    10.1021/BI0496081                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.3                           
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.158                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.201                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 4.700                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 15723                  
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 347567                 
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.123                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.172                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 11680                  
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 232269                 
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 11254                                         
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 12                                            
REMARK   3   SOLVENT ATOMS      : 1926                                          
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 13110.00                
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 10899.00                
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 17                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 119964                  
REMARK   3   NUMBER OF RESTRAINTS                     : 143755                  
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.011                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.028                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.021                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.050                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.059                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.000                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.003                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.042                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.084                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT REDUCED FREE       
REMARK   3  R (NO CUTOFF) BY ?                                                  
REMARK   4                                                                      
REMARK   4 1T6U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAY-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB022385.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-NOV-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : DOUBLE-CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 347567                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.36500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1T6I                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MPEG 5000, HEPES, METHANOL, CALCIUM      
REMARK 280  CHLORIDE, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE        
REMARK 280  295K                                                                
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       55.84000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS HEXAMERIC                         
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14300 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14250 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J, K, L                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA D   117                                                      
REMARK 465     ALA E   117                                                      
REMARK 465     LYS F   116                                                      
REMARK 465     ALA F   117                                                      
REMARK 465     ALA H   117                                                      
REMARK 465     ALA K   117                                                      
REMARK 465     ALA L   117                                                      
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   O    HOH G  1903     O    HOH G  2369              2.08            
REMARK 500   O    HOH F  1525     O    HOH F  1526              2.11            
REMARK 500   O    HOH D  1428     O    HOH D  2687              2.12            
REMARK 500   O    HOH H  2193     O    HOH H  2683              2.12            
REMARK 500   O    HOH A  1502     O    HOH A  2657              2.12            
REMARK 500   NZ   LYS D    22     O    HOH D  2799              2.12            
REMARK 500   O    HOH G  1881     O    HOH G  2113              2.13            
REMARK 500   O    HOH H  2192     O    HOH K  2381              2.14            
REMARK 500   O    HOH E  1711     O    HOH E  1931              2.14            
REMARK 500   O    HOH G  2158     O    HOH G  2935              2.14            
REMARK 500   O    HOH I  2280     O    HOH J  1877              2.15            
REMARK 500   O    HOH A  1459     O    HOH A  2309              2.15            
REMARK 500   O    HOH I  2097     O    HOH I  2891              2.16            
REMARK 500   O    GLY F     7     O    HOH F  2824              2.16            
REMARK 500   O    HOH D  2184     O    HOH D  2804              2.17            
REMARK 500   O    HOH J  2082     O    HOH K  2922              2.17            
REMARK 500   O    HOH C  1604     O    HOH C  2318              2.17            
REMARK 500   O    HOH L  1531     O    HOH L  2312              2.18            
REMARK 500   O    HOH C  1176     O    HOH D  2019              2.18            
REMARK 500   O    HOH H  2105     O    HOH H  2439              2.18            
REMARK 500   O    HOH A  2600     O    HOH A  2613              2.19            
REMARK 500   O    HOH H  2467     O    HOH H  2586              2.19            
REMARK 500   O    HOH I  2656     O    HOH I  2902              2.19            
REMARK 500   O    HOH B  2760     O    HOH E  2660              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ALA A 117   C     ALA A 117   OXT     0.350                       
REMARK 500    LYS H 116   C     LYS H 116   O       0.430                       
REMARK 500    ALA J 117   C     ALA J 117   O       0.133                       
REMARK 500    LYS L 116   C     LYS L 116   O       1.240                       
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    ARG A  15   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    LYS A 116   C   -  N   -  CA  ANGL. DEV. =  16.3 DEGREES          
REMARK 500    ALA A 117   C   -  N   -  CA  ANGL. DEV. =  26.8 DEGREES          
REMARK 500    ARG B  15   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG C  15   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG C  47   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ASP C  61   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG D  15   NE  -  CZ  -  NH1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP D  32   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP D  32   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP D  93   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ASP D 102   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG E  15   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG E  15   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    MET E  85   CG  -  SD  -  CE  ANGL. DEV. = -12.0 DEGREES          
REMARK 500    TYR E 103   CB  -  CG  -  CD2 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    TYR G   9   CB  -  CG  -  CD2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    TYR G   9   CB  -  CG  -  CD1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG G  15   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ASP G  32   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG H  15   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG H  39   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ASP H  80   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    MET H  85   CG  -  SD  -  CE  ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    LYS H 116   CA  -  C   -  O   ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ARG J  15   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG J  15   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG J  39   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    TYR K   9   CB  -  CG  -  CD2 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG K  15   CD  -  NE  -  CZ  ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ARG K  15   NE  -  CZ  -  NH1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG K  15   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG K  39   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    LYS K  99   CD  -  CE  -  NZ  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    TYR K 103   CB  -  CG  -  CD1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    TYR K 103   CG  -  CD2 -  CE2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    TYR K 103   CD1 -  CE1 -  CZ  ANGL. DEV. =   5.6 DEGREES          
REMARK 500    TYR L   9   CB  -  CG  -  CD2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    MET L  85   CG  -  SD  -  CE  ANGL. DEV. = -13.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  71       78.08   -119.69                                   
REMARK 500    LYS A 116       10.12    130.87                                   
REMARK 500    ASN D  31      102.27   -166.71                                   
REMARK 500    ASN I  31      106.20   -163.62                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS A  115     LYS A  116                  144.09                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH H2462        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH H2720        DISTANCE =  7.96 ANGSTROMS                       
REMARK 525    HOH C2783        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH H2941        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525    HOH B2762        DISTANCE =  5.70 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI A 201  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A   1   N                                                      
REMARK 620 2 HIS A   1   N     3.9                                              
REMARK 620 3 HIS A   1   ND1  77.9  81.6                                        
REMARK 620 4 CYS A   2   N    82.5  81.8  81.4                                  
REMARK 620 5 CYS A   2   SG  170.5 168.2 103.8  88.5                            
REMARK 620 6 CYS A   6   SG   94.2  95.0  96.2 176.3  94.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI B 202  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B   1   N                                                      
REMARK 620 2 HIS B   1   N     6.8                                              
REMARK 620 3 HIS B   1   ND1  74.5  80.9                                        
REMARK 620 4 CYS B   2   N    85.0  83.6  80.9                                  
REMARK 620 5 CYS B   2   SG  172.9 168.0 106.7  88.3                            
REMARK 620 6 CYS B   6   SG   91.9  93.7  95.0 175.4  94.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI C 203  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C   1   N                                                      
REMARK 620 2 HIS C   1   N     9.5                                              
REMARK 620 3 HIS C   1   ND1  74.0  82.7                                        
REMARK 620 4 CYS C   2   N    84.3  81.4  82.8                                  
REMARK 620 5 CYS C   2   SG  171.6 163.8 108.2  87.9                            
REMARK 620 6 CYS C   6   SG   93.3  96.6  94.2 176.5  94.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI D 204  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D   1   N                                                      
REMARK 620 2 HIS D   1   N    12.1                                              
REMARK 620 3 HIS D   1   ND1  70.7  82.3                                        
REMARK 620 4 CYS D   2   N    82.9  80.2  83.8                                  
REMARK 620 5 CYS D   2   SG  172.0 165.2 106.9  89.2                            
REMARK 620 6 CYS D   6   SG   93.3  96.6  93.1 175.7  94.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI E 205  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E   1   N                                                      
REMARK 620 2 HIS E   1   N     8.0                                              
REMARK 620 3 HIS E   1   ND1  71.7  79.1                                        
REMARK 620 4 CYS E   2   N    83.9  81.8  83.5                                  
REMARK 620 5 CYS E   2   SG  171.4 166.3 108.3  87.6                            
REMARK 620 6 CYS E   6   SG   93.6  96.3  92.3 175.6  94.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI F 206  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F   1   N                                                      
REMARK 620 2 HIS F   1   N     3.3                                              
REMARK 620 3 HIS F   1   ND1  79.1  82.0                                        
REMARK 620 4 CYS F   2   N    80.9  79.6  83.0                                  
REMARK 620 5 CYS F   2   SG  168.5 165.5 106.5  89.6                            
REMARK 620 6 CYS F   6   SG   95.0  96.4  93.5 175.0  94.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI G 207  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G   1   N                                                      
REMARK 620 2 HIS G   1   N    12.6                                              
REMARK 620 3 HIS G   1   ND1  73.0  84.9                                        
REMARK 620 4 CYS G   2   N    84.5  81.2  85.3                                  
REMARK 620 5 CYS G   2   SG  172.8 163.4 107.1  88.3                            
REMARK 620 6 CYS G   6   SG   92.7  96.6  91.8 176.5  94.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI H 208  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H   1   N                                                      
REMARK 620 2 HIS H   1   N     9.0                                              
REMARK 620 3 HIS H   1   ND1  73.7  82.1                                        
REMARK 620 4 CYS H   2   N    81.9  79.4  82.8                                  
REMARK 620 5 CYS H   2   SG  168.8 162.8 106.8  87.0                            
REMARK 620 6 CYS H   6   SG   94.8  97.6  95.0 176.5  96.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI I 209  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I   1   N                                                      
REMARK 620 2 HIS I   1   N     6.2                                              
REMARK 620 3 HIS I   1   ND1  76.2  82.2                                        
REMARK 620 4 CYS I   2   N    82.7  82.1  81.0                                  
REMARK 620 5 CYS I   2   SG  170.9 167.3 104.7  88.5                            
REMARK 620 6 CYS I   6   SG   94.4  95.2  96.2 176.3  94.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI J 210  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J   1   N                                                      
REMARK 620 2 HIS J   1   N     7.9                                              
REMARK 620 3 HIS J   1   ND1  72.6  79.3                                        
REMARK 620 4 CYS J   2   N    83.6  80.5  80.1                                  
REMARK 620 5 CYS J   2   SG  170.9 164.3 109.2  87.9                            
REMARK 620 6 CYS J   6   SG   92.7  96.1  96.3 175.5  95.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI K 211  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS K   1   N                                                      
REMARK 620 2 HIS K   1   N    10.4                                              
REMARK 620 3 HIS K   1   ND1  72.0  81.0                                        
REMARK 620 4 CYS K   2   N    87.0  83.0  81.4                                  
REMARK 620 5 CYS K   2   SG  174.3 167.3 105.8  87.5                            
REMARK 620 6 CYS K   6   SG   90.4  94.7  96.2 176.9  95.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI L 212  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS L   1   N                                                      
REMARK 620 2 HIS L   1   N     2.4                                              
REMARK 620 3 HIS L   1   ND1  78.1  80.3                                        
REMARK 620 4 CYS L   2   N    83.9  83.1  81.9                                  
REMARK 620 5 CYS L   2   SG  169.8 167.8 106.3  87.6                            
REMARK 620 6 CYS L   6   SG   93.6  94.6  93.4 175.0  95.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 201                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 202                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI C 203                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI D 204                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI E 205                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI F 206                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI G 207                  
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI H 208                  
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI I 209                  
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI J 210                  
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI K 211                  
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI L 212                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1T6I   RELATED DB: PDB                                   
REMARK 900 NICKEL SUPEROXIDE DISMUTASE (NISOD) APO STRUCTURE                    
REMARK 900 RELATED ID: 1T6Q   RELATED DB: PDB                                   
REMARK 900 NICKEL SUPEROXIDE DISMUTASE (NISOD) CN-TREATED APO STRUCTURE         
DBREF  1T6U A    1   117  UNP    P80735   SODN_STRCO      15    131             
DBREF  1T6U B    1   117  UNP    P80735   SODN_STRCO      15    131             
DBREF  1T6U C    1   117  UNP    P80735   SODN_STRCO      15    131             
DBREF  1T6U D    1   117  UNP    P80735   SODN_STRCO      15    131             
DBREF  1T6U E    1   117  UNP    P80735   SODN_STRCO      15    131             
DBREF  1T6U F    1   117  UNP    P80735   SODN_STRCO      15    131             
DBREF  1T6U G    1   117  UNP    P80735   SODN_STRCO      15    131             
DBREF  1T6U H    1   117  UNP    P80735   SODN_STRCO      15    131             
DBREF  1T6U I    1   117  UNP    P80735   SODN_STRCO      15    131             
DBREF  1T6U J    1   117  UNP    P80735   SODN_STRCO      15    131             
DBREF  1T6U K    1   117  UNP    P80735   SODN_STRCO      15    131             
DBREF  1T6U L    1   117  UNP    P80735   SODN_STRCO      15    131             
SEQADV 1T6U MET A   85  UNP  P80735    LEU    99 ENGINEERED                     
SEQADV 1T6U MET B   85  UNP  P80735    LEU    99 ENGINEERED                     
SEQADV 1T6U MET C   85  UNP  P80735    LEU    99 ENGINEERED                     
SEQADV 1T6U MET D   85  UNP  P80735    LEU    99 ENGINEERED                     
SEQADV 1T6U MET E   85  UNP  P80735    LEU    99 ENGINEERED                     
SEQADV 1T6U MET F   85  UNP  P80735    LEU    99 ENGINEERED                     
SEQADV 1T6U MET G   85  UNP  P80735    LEU    99 ENGINEERED                     
SEQADV 1T6U MET H   85  UNP  P80735    LEU    99 ENGINEERED                     
SEQADV 1T6U MET I   85  UNP  P80735    LEU    99 ENGINEERED                     
SEQADV 1T6U MET J   85  UNP  P80735    LEU    99 ENGINEERED                     
SEQADV 1T6U MET K   85  UNP  P80735    LEU    99 ENGINEERED                     
SEQADV 1T6U MET L   85  UNP  P80735    LEU    99 ENGINEERED                     
SEQRES   1 A  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN          
SEQRES   2 A  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN GLU          
SEQRES   3 A  117  LYS MET ALA GLY ASN ASP ASP PRO HIS PHE GLN THR ARG          
SEQRES   4 A  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS          
SEQRES   5 A  117  HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS PRO          
SEQRES   6 A  117  PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU VAL          
SEQRES   7 A  117  ASN ASP THR LEU LYS ALA MET SER ALA ALA LYS GLY SER          
SEQRES   8 A  117  LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE          
SEQRES   9 A  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA          
SEQRES   1 B  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN          
SEQRES   2 B  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN GLU          
SEQRES   3 B  117  LYS MET ALA GLY ASN ASP ASP PRO HIS PHE GLN THR ARG          
SEQRES   4 B  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS          
SEQRES   5 B  117  HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS PRO          
SEQRES   6 B  117  PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU VAL          
SEQRES   7 B  117  ASN ASP THR LEU LYS ALA MET SER ALA ALA LYS GLY SER          
SEQRES   8 B  117  LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE          
SEQRES   9 B  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA          
SEQRES   1 C  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN          
SEQRES   2 C  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN GLU          
SEQRES   3 C  117  LYS MET ALA GLY ASN ASP ASP PRO HIS PHE GLN THR ARG          
SEQRES   4 C  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS          
SEQRES   5 C  117  HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS PRO          
SEQRES   6 C  117  PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU VAL          
SEQRES   7 C  117  ASN ASP THR LEU LYS ALA MET SER ALA ALA LYS GLY SER          
SEQRES   8 C  117  LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE          
SEQRES   9 C  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA          
SEQRES   1 D  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN          
SEQRES   2 D  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN GLU          
SEQRES   3 D  117  LYS MET ALA GLY ASN ASP ASP PRO HIS PHE GLN THR ARG          
SEQRES   4 D  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS          
SEQRES   5 D  117  HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS PRO          
SEQRES   6 D  117  PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU VAL          
SEQRES   7 D  117  ASN ASP THR LEU LYS ALA MET SER ALA ALA LYS GLY SER          
SEQRES   8 D  117  LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE          
SEQRES   9 D  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA          
SEQRES   1 E  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN          
SEQRES   2 E  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN GLU          
SEQRES   3 E  117  LYS MET ALA GLY ASN ASP ASP PRO HIS PHE GLN THR ARG          
SEQRES   4 E  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS          
SEQRES   5 E  117  HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS PRO          
SEQRES   6 E  117  PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU VAL          
SEQRES   7 E  117  ASN ASP THR LEU LYS ALA MET SER ALA ALA LYS GLY SER          
SEQRES   8 E  117  LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE          
SEQRES   9 E  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA          
SEQRES   1 F  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN          
SEQRES   2 F  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN GLU          
SEQRES   3 F  117  LYS MET ALA GLY ASN ASP ASP PRO HIS PHE GLN THR ARG          
SEQRES   4 F  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS          
SEQRES   5 F  117  HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS PRO          
SEQRES   6 F  117  PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU VAL          
SEQRES   7 F  117  ASN ASP THR LEU LYS ALA MET SER ALA ALA LYS GLY SER          
SEQRES   8 F  117  LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE          
SEQRES   9 F  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA          
SEQRES   1 G  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN          
SEQRES   2 G  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN GLU          
SEQRES   3 G  117  LYS MET ALA GLY ASN ASP ASP PRO HIS PHE GLN THR ARG          
SEQRES   4 G  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS          
SEQRES   5 G  117  HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS PRO          
SEQRES   6 G  117  PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU VAL          
SEQRES   7 G  117  ASN ASP THR LEU LYS ALA MET SER ALA ALA LYS GLY SER          
SEQRES   8 G  117  LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE          
SEQRES   9 G  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA          
SEQRES   1 H  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN          
SEQRES   2 H  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN GLU          
SEQRES   3 H  117  LYS MET ALA GLY ASN ASP ASP PRO HIS PHE GLN THR ARG          
SEQRES   4 H  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS          
SEQRES   5 H  117  HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS PRO          
SEQRES   6 H  117  PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU VAL          
SEQRES   7 H  117  ASN ASP THR LEU LYS ALA MET SER ALA ALA LYS GLY SER          
SEQRES   8 H  117  LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE          
SEQRES   9 H  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA          
SEQRES   1 I  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN          
SEQRES   2 I  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN GLU          
SEQRES   3 I  117  LYS MET ALA GLY ASN ASP ASP PRO HIS PHE GLN THR ARG          
SEQRES   4 I  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS          
SEQRES   5 I  117  HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS PRO          
SEQRES   6 I  117  PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU VAL          
SEQRES   7 I  117  ASN ASP THR LEU LYS ALA MET SER ALA ALA LYS GLY SER          
SEQRES   8 I  117  LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE          
SEQRES   9 I  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA          
SEQRES   1 J  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN          
SEQRES   2 J  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN GLU          
SEQRES   3 J  117  LYS MET ALA GLY ASN ASP ASP PRO HIS PHE GLN THR ARG          
SEQRES   4 J  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS          
SEQRES   5 J  117  HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS PRO          
SEQRES   6 J  117  PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU VAL          
SEQRES   7 J  117  ASN ASP THR LEU LYS ALA MET SER ALA ALA LYS GLY SER          
SEQRES   8 J  117  LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE          
SEQRES   9 J  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA          
SEQRES   1 K  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN          
SEQRES   2 K  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN GLU          
SEQRES   3 K  117  LYS MET ALA GLY ASN ASP ASP PRO HIS PHE GLN THR ARG          
SEQRES   4 K  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS          
SEQRES   5 K  117  HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS PRO          
SEQRES   6 K  117  PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU VAL          
SEQRES   7 K  117  ASN ASP THR LEU LYS ALA MET SER ALA ALA LYS GLY SER          
SEQRES   8 K  117  LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE          
SEQRES   9 K  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA          
SEQRES   1 L  117  HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA GLN          
SEQRES   2 L  117  ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN GLU          
SEQRES   3 L  117  LYS MET ALA GLY ASN ASP ASP PRO HIS PHE GLN THR ARG          
SEQRES   4 L  117  ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA LYS          
SEQRES   5 L  117  HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS PRO          
SEQRES   6 L  117  PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU VAL          
SEQRES   7 L  117  ASN ASP THR LEU LYS ALA MET SER ALA ALA LYS GLY SER          
SEQRES   8 L  117  LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR ILE          
SEQRES   9 L  117  ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS ALA          
HET     NI  A 201       1                                                       
HET     NI  B 202       1                                                       
HET     NI  C 203       1                                                       
HET     NI  D 204       1                                                       
HET     NI  E 205       1                                                       
HET     NI  F 206       1                                                       
HET     NI  G 207       1                                                       
HET     NI  H 208       1                                                       
HET     NI  I 209       1                                                       
HET     NI  J 210       1                                                       
HET     NI  K 211       1                                                       
HET     NI  L 212       1                                                       
HETNAM      NI NICKEL (II) ION                                                  
FORMUL  13   NI    12(NI 2+)                                                    
FORMUL  25  HOH   *1926(H2 O)                                                   
HELIX    1   1 PRO A   11  ASN A   31  1                                  21    
HELIX    2   2 ASP A   33  TYR A   62  1                                  30    
HELIX    3   3 LYS A   64  TYR A   71  1                                   8    
HELIX    4   4 GLU A   73  GLY A   90  1                                  18    
HELIX    5   5 ASP A   93  LYS A  115  1                                  23    
HELIX    6   6 PRO B   11  ALA B   29  1                                  19    
HELIX    7   7 ASP B   33  TYR B   62  1                                  30    
HELIX    8   8 LYS B   64  TYR B   71  1                                   8    
HELIX    9   9 GLU B   73  GLY B   90  1                                  18    
HELIX   10  10 ASP B   93  LYS B  115  1                                  23    
HELIX   11  11 PRO C   11  ALA C   29  1                                  19    
HELIX   12  12 ASP C   33  TYR C   62  1                                  30    
HELIX   13  13 LYS C   64  TYR C   71  1                                   8    
HELIX   14  14 GLU C   73  GLY C   90  1                                  18    
HELIX   15  15 ASP C   93  ALA C  117  1                                  25    
HELIX   16  16 PRO D   11  ALA D   29  1                                  19    
HELIX   17  17 ASP D   33  ASP D   61  1                                  29    
HELIX   18  18 LYS D   64  TYR D   71  1                                   8    
HELIX   19  19 GLU D   73  GLY D   90  1                                  18    
HELIX   20  20 ASP D   93  LYS D  116  1                                  24    
HELIX   21  21 PRO E   11  ALA E   29  1                                  19    
HELIX   22  22 ASP E   33  TYR E   62  1                                  30    
HELIX   23  23 LYS E   64  TYR E   71  1                                   8    
HELIX   24  24 GLU E   73  GLY E   90  1                                  18    
HELIX   25  25 ASP E   93  LYS E  116  1                                  24    
HELIX   26  26 PRO F   11  ALA F   29  1                                  19    
HELIX   27  27 ASP F   33  TYR F   62  1                                  30    
HELIX   28  28 LYS F   64  TYR F   71  1                                   8    
HELIX   29  29 GLU F   73  GLY F   90  1                                  18    
HELIX   30  30 ASP F   93  LYS F  115  1                                  23    
HELIX   31  31 PRO G   11  ALA G   29  1                                  19    
HELIX   32  32 ASP G   33  TYR G   62  1                                  30    
HELIX   33  33 LYS G   64  TYR G   71  1                                   8    
HELIX   34  34 GLU G   73  GLY G   90  1                                  18    
HELIX   35  35 ASP G   93  ALA G  117  1                                  25    
HELIX   36  36 PRO H   11  ALA H   29  1                                  19    
HELIX   37  37 ASP H   33  TYR H   62  1                                  30    
HELIX   38  38 LYS H   64  TYR H   71  1                                   8    
HELIX   39  39 GLU H   73  GLY H   90  1                                  18    
HELIX   40  40 ASP H   93  LYS H  116  1                                  24    
HELIX   41  41 PRO I   11  ALA I   29  1                                  19    
HELIX   42  42 ASP I   33  TYR I   62  1                                  30    
HELIX   43  43 LYS I   64  TYR I   71  1                                   8    
HELIX   44  44 GLU I   73  GLY I   90  1                                  18    
HELIX   45  45 ASP I   93  LYS I  115  1                                  23    
HELIX   46  46 PRO J   11  ALA J   29  1                                  19    
HELIX   47  47 ASP J   33  TYR J   62  1                                  30    
HELIX   48  48 LYS J   64  TYR J   71  1                                   8    
HELIX   49  49 GLU J   73  GLY J   90  1                                  18    
HELIX   50  50 ASP J   93  LYS J  115  1                                  23    
HELIX   51  51 PRO K   11  ALA K   29  1                                  19    
HELIX   52  52 ASP K   33  ASP K   61  1                                  29    
HELIX   53  53 LYS K   64  TYR K   71  1                                   8    
HELIX   54  54 GLU K   73  GLY K   90  1                                  18    
HELIX   55  55 ASP K   93  LYS K  116  1                                  24    
HELIX   56  56 PRO L   11  ALA L   29  1                                  19    
HELIX   57  57 ASP L   33  TYR L   62  1                                  30    
HELIX   58  58 LYS L   64  TYR L   71  1                                   8    
HELIX   59  59 GLU L   73  GLY L   90  1                                  18    
HELIX   60  60 ASP L   93  LYS L  116  1                                  24    
LINK        NI    NI A 201                 N  AHIS A   1     1555   1555  1.88  
LINK        NI    NI A 201                 N  BHIS A   1     1555   1555  1.88  
LINK        NI    NI A 201                 ND1BHIS A   1     1555   1555  2.31  
LINK        NI    NI A 201                 N   CYS A   2     1555   1555  1.93  
LINK        NI    NI A 201                 SG  CYS A   2     1555   1555  2.16  
LINK        NI    NI A 201                 SG  CYS A   6     1555   1555  2.20  
LINK        NI    NI B 202                 N  AHIS B   1     1555   1555  1.96  
LINK        NI    NI B 202                 N  BHIS B   1     1555   1555  2.03  
LINK        NI    NI B 202                 ND1BHIS B   1     1555   1555  2.40  
LINK        NI    NI B 202                 N   CYS B   2     1555   1555  1.91  
LINK        NI    NI B 202                 SG  CYS B   2     1555   1555  2.18  
LINK        NI    NI B 202                 SG  CYS B   6     1555   1555  2.19  
LINK        NI    NI C 203                 N  AHIS C   1     1555   1555  1.83  
LINK        NI    NI C 203                 N  BHIS C   1     1555   1555  2.04  
LINK        NI    NI C 203                 ND1BHIS C   1     1555   1555  2.29  
LINK        NI    NI C 203                 N   CYS C   2     1555   1555  1.88  
LINK        NI    NI C 203                 SG  CYS C   2     1555   1555  2.18  
LINK        NI    NI C 203                 SG  CYS C   6     1555   1555  2.19  
LINK        NI    NI D 204                 N  AHIS D   1     1555   1555  1.92  
LINK        NI    NI D 204                 N  BHIS D   1     1555   1555  2.02  
LINK        NI    NI D 204                 ND1BHIS D   1     1555   1555  2.40  
LINK        NI    NI D 204                 N   CYS D   2     1555   1555  1.92  
LINK        NI    NI D 204                 SG  CYS D   2     1555   1555  2.14  
LINK        NI    NI D 204                 SG  CYS D   6     1555   1555  2.19  
LINK        NI    NI E 205                 N  AHIS E   1     1555   1555  1.88  
LINK        NI    NI E 205                 N  BHIS E   1     1555   1555  2.00  
LINK        NI    NI E 205                 ND1BHIS E   1     1555   1555  2.45  
LINK        NI    NI E 205                 N   CYS E   2     1555   1555  1.94  
LINK        NI    NI E 205                 SG  CYS E   2     1555   1555  2.16  
LINK        NI    NI E 205                 SG  CYS E   6     1555   1555  2.17  
LINK        NI    NI F 206                 N  AHIS F   1     1555   1555  1.90  
LINK        NI    NI F 206                 N  BHIS F   1     1555   1555  2.12  
LINK        NI    NI F 206                 ND1BHIS F   1     1555   1555  2.31  
LINK        NI    NI F 206                 N   CYS F   2     1555   1555  1.91  
LINK        NI    NI F 206                 SG  CYS F   2     1555   1555  2.13  
LINK        NI    NI F 206                 SG  CYS F   6     1555   1555  2.18  
LINK        NI    NI G 207                 N  AHIS G   1     1555   1555  1.85  
LINK        NI    NI G 207                 N  BHIS G   1     1555   1555  2.02  
LINK        NI    NI G 207                 ND1BHIS G   1     1555   1555  2.28  
LINK        NI    NI G 207                 N   CYS G   2     1555   1555  1.89  
LINK        NI    NI G 207                 SG  CYS G   2     1555   1555  2.19  
LINK        NI    NI G 207                 SG  CYS G   6     1555   1555  2.21  
LINK        NI    NI H 208                 N  AHIS H   1     1555   1555  1.81  
LINK        NI    NI H 208                 N  BHIS H   1     1555   1555  2.01  
LINK        NI    NI H 208                 ND1BHIS H   1     1555   1555  2.39  
LINK        NI    NI H 208                 N   CYS H   2     1555   1555  1.91  
LINK        NI    NI H 208                 SG  CYS H   2     1555   1555  2.17  
LINK        NI    NI H 208                 SG  CYS H   6     1555   1555  2.13  
LINK        NI    NI I 209                 N  AHIS I   1     1555   1555  1.87  
LINK        NI    NI I 209                 N  BHIS I   1     1555   1555  1.85  
LINK        NI    NI I 209                 ND1BHIS I   1     1555   1555  2.33  
LINK        NI    NI I 209                 N   CYS I   2     1555   1555  1.92  
LINK        NI    NI I 209                 SG  CYS I   2     1555   1555  2.17  
LINK        NI    NI I 209                 SG  CYS I   6     1555   1555  2.20  
LINK        NI    NI J 210                 N  AHIS J   1     1555   1555  1.94  
LINK        NI    NI J 210                 N  BHIS J   1     1555   1555  2.24  
LINK        NI    NI J 210                 ND1BHIS J   1     1555   1555  2.35  
LINK        NI    NI J 210                 N   CYS J   2     1555   1555  1.91  
LINK        NI    NI J 210                 SG  CYS J   2     1555   1555  2.15  
LINK        NI    NI J 210                 SG  CYS J   6     1555   1555  2.18  
LINK        NI    NI K 211                 N  AHIS K   1     1555   1555  1.75  
LINK        NI    NI K 211                 N  BHIS K   1     1555   1555  2.13  
LINK        NI    NI K 211                 ND1BHIS K   1     1555   1555  2.32  
LINK        NI    NI K 211                 N   CYS K   2     1555   1555  1.85  
LINK        NI    NI K 211                 SG  CYS K   2     1555   1555  2.16  
LINK        NI    NI K 211                 SG  CYS K   6     1555   1555  2.22  
LINK        NI    NI L 212                 N  AHIS L   1     1555   1555  1.86  
LINK        NI    NI L 212                 N  BHIS L   1     1555   1555  1.93  
LINK        NI    NI L 212                 ND1BHIS L   1     1555   1555  2.38  
LINK        NI    NI L 212                 N   CYS L   2     1555   1555  1.93  
LINK        NI    NI L 212                 SG  CYS L   2     1555   1555  2.15  
LINK        NI    NI L 212                 SG  CYS L   6     1555   1555  2.19  
CISPEP   1 LEU A    4    PRO A    5          0        -0.60                     
CISPEP   2 LEU B    4    PRO B    5          0         0.72                     
CISPEP   3 LEU C    4    PRO C    5          0         0.42                     
CISPEP   4 LEU D    4    PRO D    5          0         3.52                     
CISPEP   5 LEU E    4    PRO E    5          0         3.99                     
CISPEP   6 LEU F    4    PRO F    5          0        -1.23                     
CISPEP   7 LEU G    4    PRO G    5          0         0.69                     
CISPEP   8 LEU H    4    PRO H    5          0         0.08                     
CISPEP   9 LEU I    4    PRO I    5          0        -0.69                     
CISPEP  10 LEU J    4    PRO J    5          0        -0.03                     
CISPEP  11 LEU K    4    PRO K    5          0         1.68                     
CISPEP  12 LEU L    4    PRO L    5          0         2.13                     
SITE     1 AC1  3 HIS A   1  CYS A   2  CYS A   6                               
SITE     1 AC2  4 HIS B   1  CYS B   2  ASP B   3  CYS B   6                    
SITE     1 AC3  3 HIS C   1  CYS C   2  CYS C   6                               
SITE     1 AC4  4 HIS D   1  CYS D   2  ASP D   3  CYS D   6                    
SITE     1 AC5  3 HIS E   1  CYS E   2  CYS E   6                               
SITE     1 AC6  3 HIS F   1  CYS F   2  CYS F   6                               
SITE     1 AC7  3 HIS G   1  CYS G   2  CYS G   6                               
SITE     1 AC8  3 HIS H   1  CYS H   2  CYS H   6                               
SITE     1 AC9  3 HIS I   1  CYS I   2  CYS I   6                               
SITE     1 BC1  4 HIS J   1  CYS J   2  ASP J   3  CYS J   6                    
SITE     1 BC2  3 HIS K   1  CYS K   2  CYS K   6                               
SITE     1 BC3  3 HIS L   1  CYS L   2  CYS L   6                               
CRYST1   64.147  111.680  106.834  90.00  94.51  90.00 P 1 21 1     24          
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      0.015589  0.000000  0.001230        0.00000                         
SCALE2      0.000000  0.008954  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009389        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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