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Database: PDB
Entry: 1XX6
LinkDB: 1XX6
Original site: 1XX6 
HEADER    TRANSFERASE                             04-NOV-04   1XX6              
TITLE     X-RAY STRUCTURE OF CLOSTRIDIUM ACETOBUTYLICUM THYMIDINE KINASE WITH   
TITLE    2 ADP. NORTHEAST STRUCTURAL GENOMICS TARGET CAR26.                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THYMIDINE KINASE;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.7.1.21;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM ACETOBUTYLICUM;                     
SOURCE   3 ORGANISM_TAXID: 272562;                                              
SOURCE   4 STRAIN: ATCC 824;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;                           
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET21                                     
KEYWDS    NESG, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, PROTEIN STRUCTURE     
KEYWDS   2 INITIATIVE, PSI, STRUCTURAL GENOMICS, DNA SYNTHESIS, KINASE,         
KEYWDS   3 TRANSFERASE, THYMIDINE                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.P.KUZIN,M.ABASHIDZE,F.FOROUHAR,S.M.VOROBIEV,T.B.ACTON,L.-C.MA,      
AUTHOR   2 R.XIAO,G.T.MONTELIONE,L.TONG,J.F.HUNT,NORTHEAST STRUCTURAL GENOMICS  
AUTHOR   3 CONSORTIUM (NESG)                                                    
REVDAT   4   13-JUL-11 1XX6    1       VERSN                                    
REVDAT   3   24-FEB-09 1XX6    1       VERSN                                    
REVDAT   2   18-JAN-05 1XX6    1       AUTHOR                                   
REVDAT   1   21-DEC-04 1XX6    0                                                
JRNL        AUTH   A.P.KUZIN,M.ABASHIDZE,F.FOROUHAR,S.M.VOROBIEV,T.B.ACTON,     
JRNL        AUTH 2 L.-C.MA,R.XIAO,G.T.MONTELIONE,L.TONG,J.F.HUNT                
JRNL        TITL   X-RAY STRUCTURE OF CLOSTRIDIUM ACETOBUTYLICUM THYMIDINE      
JRNL        TITL 2 KINASE WITH ADP. NORTHEAST STRUCTURAL GENOMICS TARGET CAR26. 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.49                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 274236.170                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 85.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 42063                          
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 SET) : 0.241                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2079                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 70.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5491                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2490                       
REMARK   3   BIN FREE R VALUE                    : 0.2950                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 258                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.018                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2761                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 171                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.98000                                             
REMARK   3    B22 (A**2) : -6.11500                                             
REMARK   3    B33 (A**2) : 10.09500                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.16                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.32                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.24                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.80                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.520 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.474 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.345 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.395 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 53.59                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA-REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : ADP.PARAM                                      
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : ADP.TOP                                        
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1XX6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB030870.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-SEP-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48667                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 8.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NA, K-CITRATE, P 20% EG3350, 2 MM   
REMARK 280  ATP, 2 MM MGCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       26.89650            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.58300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.89650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.58300            
REMARK 290   SMTRY3   4  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 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: 3750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10950 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 30280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       53.79300            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       67.16600            
REMARK 350   BIOMT3   2  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     MET A     1                                                      
REMARK 465     ILE A    46                                                      
REMARK 465     ASP A    47                                                      
REMARK 465     ASN A    48                                                      
REMARK 465     ARG A    49                                                      
REMARK 465     TYR A    50                                                      
REMARK 465     SER A    51                                                      
REMARK 465     LYS A    52                                                      
REMARK 465     VAL A   171                                                      
REMARK 465     LEU A   172                                                      
REMARK 465     ILE A   173                                                      
REMARK 465     GLY A   174                                                      
REMARK 465     ALA A   175                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ILE B    46                                                      
REMARK 465     ASP B    47                                                      
REMARK 465     ASN B    48                                                      
REMARK 465     ARG B    49                                                      
REMARK 465     TYR B    50                                                      
REMARK 465     SER B    51                                                      
REMARK 465     LYS B    52                                                      
REMARK 465     GLU B    53                                                      
REMARK 465     ASP B    54                                                      
REMARK 465     VAL B    55                                                      
REMARK 465     VAL B    56                                                      
REMARK 465     SER B    57                                                      
REMARK 465     HIS B    58                                                      
REMARK 465     MSE B    59                                                      
REMARK 465     GLY B    60                                                      
REMARK 465     GLU B    61                                                      
REMARK 465     LYS B    62                                                      
REMARK 465     GLU B    63                                                      
REMARK 465     GLN B    64                                                      
REMARK 465     VAL B   171                                                      
REMARK 465     LEU B   172                                                      
REMARK 465     ILE B   173                                                      
REMARK 465     GLY B   174                                                      
REMARK 465     ALA B   175                                                      
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    ALA A 143     -167.90   -102.72                                   
REMARK 500    ASP A 167       44.19    -80.37                                   
REMARK 500    PRO A 169     -166.72    -63.68                                   
REMARK 500    LYS B  69     -125.15    -82.59                                   
REMARK 500    ASN B  70     -177.18    -54.54                                   
REMARK 500    ALA B 143     -167.15   -102.31                                   
REMARK 500    ASP B 167       31.44    -99.01                                   
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 B 484        DISTANCE =  6.80 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                              ZN A 302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 183   SG                                                     
REMARK 620 2 CYS A 145   SG  114.5                                              
REMARK 620 3 CYS A 148   SG  113.5 112.8                                        
REMARK 620 4 CYS A 186   SG  100.2 102.7 111.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 148   SG                                                     
REMARK 620 2 CYS B 145   SG  118.0                                              
REMARK 620 3 CYS B 186   SG  116.2 118.2                                        
REMARK 620 4 CYS B 183   SG  115.0 122.9  47.6                                  
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 ZN A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: CAR26   RELATED DB: TARGETDB                             
DBREF  1XX6 A    1   191  UNP    Q97F65   KITH_CLOAB       1    191             
DBREF  1XX6 B    1   191  UNP    Q97F65   KITH_CLOAB       1    191             
SEQADV 1XX6 MSE A   17  UNP  Q97F65    MET    17 MODIFIED RESIDUE               
SEQADV 1XX6 MSE A   59  UNP  Q97F65    MET    59 MODIFIED RESIDUE               
SEQADV 1XX6 MSE A  118  UNP  Q97F65    MET   118 MODIFIED RESIDUE               
SEQADV 1XX6 MSE A  132  UNP  Q97F65    MET   132 MODIFIED RESIDUE               
SEQADV 1XX6 MSE A  176  UNP  Q97F65    MET   176 MODIFIED RESIDUE               
SEQADV 1XX6 MSE B   17  UNP  Q97F65    MET    17 MODIFIED RESIDUE               
SEQADV 1XX6 MSE B   59  UNP  Q97F65    MET    59 MODIFIED RESIDUE               
SEQADV 1XX6 MSE B  118  UNP  Q97F65    MET   118 MODIFIED RESIDUE               
SEQADV 1XX6 MSE B  132  UNP  Q97F65    MET   132 MODIFIED RESIDUE               
SEQADV 1XX6 MSE B  176  UNP  Q97F65    MET   176 MODIFIED RESIDUE               
SEQRES   1 A  191  MET TYR ARG PRO LYS ASP HIS GLY TRP VAL GLU VAL ILE          
SEQRES   2 A  191  VAL GLY PRO MSE TYR SER GLY LYS SER GLU GLU LEU ILE          
SEQRES   3 A  191  ARG ARG ILE ARG ARG ALA LYS ILE ALA LYS GLN LYS ILE          
SEQRES   4 A  191  GLN VAL PHE LYS PRO GLU ILE ASP ASN ARG TYR SER LYS          
SEQRES   5 A  191  GLU ASP VAL VAL SER HIS MSE GLY GLU LYS GLU GLN ALA          
SEQRES   6 A  191  VAL ALA ILE LYS ASN SER ARG GLU ILE LEU LYS TYR PHE          
SEQRES   7 A  191  GLU GLU ASP THR GLU VAL ILE ALA ILE ASP GLU VAL GLN          
SEQRES   8 A  191  PHE PHE ASP ASP GLU ILE VAL GLU ILE VAL ASN LYS ILE          
SEQRES   9 A  191  ALA GLU SER GLY ARG ARG VAL ILE CYS ALA GLY LEU ASP          
SEQRES  10 A  191  MSE ASP PHE ARG GLY LYS PRO PHE GLY PRO ILE PRO GLU          
SEQRES  11 A  191  LEU MSE ALA ILE ALA GLU PHE VAL ASP LYS ILE GLN ALA          
SEQRES  12 A  191  ILE CYS VAL VAL CYS GLY ASN PRO ALA THR ARG THR GLN          
SEQRES  13 A  191  ARG LEU ILE ASN GLY LYS PRO ALA PHE TYR ASP ASP PRO          
SEQRES  14 A  191  VAL VAL LEU ILE GLY ALA MSE GLU SER TYR GLU ALA ARG          
SEQRES  15 A  191  CYS ARG LYS CYS HIS VAL VAL PRO GLN                          
SEQRES   1 B  191  MET TYR ARG PRO LYS ASP HIS GLY TRP VAL GLU VAL ILE          
SEQRES   2 B  191  VAL GLY PRO MSE TYR SER GLY LYS SER GLU GLU LEU ILE          
SEQRES   3 B  191  ARG ARG ILE ARG ARG ALA LYS ILE ALA LYS GLN LYS ILE          
SEQRES   4 B  191  GLN VAL PHE LYS PRO GLU ILE ASP ASN ARG TYR SER LYS          
SEQRES   5 B  191  GLU ASP VAL VAL SER HIS MSE GLY GLU LYS GLU GLN ALA          
SEQRES   6 B  191  VAL ALA ILE LYS ASN SER ARG GLU ILE LEU LYS TYR PHE          
SEQRES   7 B  191  GLU GLU ASP THR GLU VAL ILE ALA ILE ASP GLU VAL GLN          
SEQRES   8 B  191  PHE PHE ASP ASP GLU ILE VAL GLU ILE VAL ASN LYS ILE          
SEQRES   9 B  191  ALA GLU SER GLY ARG ARG VAL ILE CYS ALA GLY LEU ASP          
SEQRES  10 B  191  MSE ASP PHE ARG GLY LYS PRO PHE GLY PRO ILE PRO GLU          
SEQRES  11 B  191  LEU MSE ALA ILE ALA GLU PHE VAL ASP LYS ILE GLN ALA          
SEQRES  12 B  191  ILE CYS VAL VAL CYS GLY ASN PRO ALA THR ARG THR GLN          
SEQRES  13 B  191  ARG LEU ILE ASN GLY LYS PRO ALA PHE TYR ASP ASP PRO          
SEQRES  14 B  191  VAL VAL LEU ILE GLY ALA MSE GLU SER TYR GLU ALA ARG          
SEQRES  15 B  191  CYS ARG LYS CYS HIS VAL VAL PRO GLN                          
MODRES 1XX6 MSE A   17  MET  SELENOMETHIONINE                                   
MODRES 1XX6 MSE A   59  MET  SELENOMETHIONINE                                   
MODRES 1XX6 MSE A  118  MET  SELENOMETHIONINE                                   
MODRES 1XX6 MSE A  132  MET  SELENOMETHIONINE                                   
MODRES 1XX6 MSE A  176  MET  SELENOMETHIONINE                                   
MODRES 1XX6 MSE B   17  MET  SELENOMETHIONINE                                   
MODRES 1XX6 MSE B  118  MET  SELENOMETHIONINE                                   
MODRES 1XX6 MSE B  132  MET  SELENOMETHIONINE                                   
MODRES 1XX6 MSE B  176  MET  SELENOMETHIONINE                                   
HET    MSE  A  17       8                                                       
HET    MSE  A  59       8                                                       
HET    MSE  A 118       8                                                       
HET    MSE  A 132       8                                                       
HET    MSE  A 176       8                                                       
HET    MSE  B  17       8                                                       
HET    MSE  B 118       8                                                       
HET    MSE  B 132       8                                                       
HET    MSE  B 176       8                                                       
HET     ZN  A 302       1                                                       
HET     ZN  B 402       1                                                       
HET    ADP  A 301      27                                                       
HET    ADP  B 401      27                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      ZN ZINC ION                                                         
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
FORMUL   1  MSE    9(C5 H11 N O2 SE)                                            
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   5  ADP    2(C10 H15 N5 O10 P2)                                         
FORMUL   7  HOH   *171(H2 O)                                                    
HELIX    1   1 GLY A   20  ALA A   35  1                                  16    
HELIX    2   2 ARG A   72  PHE A   78  1                                   7    
HELIX    3   3 GLU A   89  PHE A   93  5                                   5    
HELIX    4   4 ASP A   94  ASP A   95  5                                   2    
HELIX    5   5 GLU A   96  SER A  107  1                                  12    
HELIX    6   6 PRO A  127  ALA A  135  1                                   9    
HELIX    7   7 GLY B   20  ALA B   35  1                                  16    
HELIX    8   8 ARG B   72  PHE B   78  1                                   7    
HELIX    9   9 GLU B   89  ASP B   94  5                                   6    
HELIX   10  10 ASP B   95  SER B  107  1                                  13    
HELIX   11  11 PRO B  127  ALA B  135  1                                   9    
SHEET    1   A 6 VAL A  66  ILE A  68  0                                        
SHEET    2   A 6 ILE A  39  PRO A  44  1  N  LYS A  43   O  ILE A  68           
SHEET    3   A 6 VAL A  84  ILE A  87  1  O  ALA A  86   N  PHE A  42           
SHEET    4   A 6 ARG A 110  GLY A 115  1  O  ILE A 112   N  ILE A  87           
SHEET    5   A 6 TRP A   9  VAL A  14  1  N  GLU A  11   O  CYS A 113           
SHEET    6   A 6 PHE A 137  LYS A 140  1  O  PHE A 137   N  VAL A  12           
SHEET    1   B 2 ASP A  54  VAL A  56  0                                        
SHEET    2   B 2 LYS A  62  GLN A  64 -1  O  GLU A  63   N  VAL A  55           
SHEET    1   C 2 ALA A 143  ILE A 144  0                                        
SHEET    2   C 2 PRO A 151  ALA A 152 -1  O  ALA A 152   N  ALA A 143           
SHEET    1   D 3 LYS A 162  PRO A 163  0                                        
SHEET    2   D 3 ARG A 154  ILE A 159 -1  N  ILE A 159   O  LYS A 162           
SHEET    3   D 3 GLU A 177  ARG A 182 -1  O  GLU A 180   N  GLN A 156           
SHEET    1   E 6 VAL B  66  ALA B  67  0                                        
SHEET    2   E 6 ILE B  39  LYS B  43  1  N  LYS B  43   O  VAL B  66           
SHEET    3   E 6 VAL B  84  ILE B  87  1  O  ALA B  86   N  GLN B  40           
SHEET    4   E 6 ARG B 110  GLY B 115  1  O  ILE B 112   N  ILE B  87           
SHEET    5   E 6 TRP B   9  VAL B  14  1  N  GLU B  11   O  CYS B 113           
SHEET    6   E 6 PHE B 137  LYS B 140  1  O  PHE B 137   N  VAL B  12           
SHEET    1   F 2 ALA B 143  ILE B 144  0                                        
SHEET    2   F 2 PRO B 151  ALA B 152 -1  O  ALA B 152   N  ALA B 143           
SHEET    1   G 3 LYS B 162  PRO B 163  0                                        
SHEET    2   G 3 ARG B 154  ILE B 159 -1  N  ILE B 159   O  LYS B 162           
SHEET    3   G 3 GLU B 177  ARG B 182 -1  O  GLU B 180   N  GLN B 156           
SSBOND   1 CYS B  183    CYS B  186                          1555   1555  2.07  
LINK         C   PRO A  16                 N   MSE A  17     1555   1555  1.33  
LINK         C   MSE A  17                 N   TYR A  18     1555   1555  1.33  
LINK         C   HIS A  58                 N   MSE A  59     1555   1555  1.33  
LINK         C   MSE A  59                 N   GLY A  60     1555   1555  1.33  
LINK         C   ASP A 117                 N   MSE A 118     1555   1555  1.34  
LINK         C   MSE A 118                 N   ASP A 119     1555   1555  1.33  
LINK         C   LEU A 131                 N   MSE A 132     1555   1555  1.33  
LINK         C   MSE A 132                 N   ALA A 133     1555   1555  1.33  
LINK         C   MSE A 176                 N   GLU A 177     1555   1555  1.33  
LINK        ZN    ZN A 302                 SG  CYS A 183     1555   1555  2.36  
LINK        ZN    ZN A 302                 SG  CYS A 145     1555   1555  2.51  
LINK        ZN    ZN A 302                 SG  CYS A 148     1555   1555  2.42  
LINK        ZN    ZN A 302                 SG  CYS A 186     1555   1555  2.39  
LINK         C   PRO B  16                 N   MSE B  17     1555   1555  1.33  
LINK         C   MSE B  17                 N   TYR B  18     1555   1555  1.33  
LINK         C   ASP B 117                 N   MSE B 118     1555   1555  1.33  
LINK         C   MSE B 118                 N   ASP B 119     1555   1555  1.34  
LINK         C   LEU B 131                 N   MSE B 132     1555   1555  1.33  
LINK         C   MSE B 132                 N   ALA B 133     1555   1555  1.33  
LINK         C   MSE B 176                 N   GLU B 177     1555   1555  1.33  
LINK        ZN    ZN B 402                 SG  CYS B 148     1555   1555  2.37  
LINK        ZN    ZN B 402                 SG  CYS B 145     1555   1555  2.36  
LINK        ZN    ZN B 402                 SG  CYS B 186     1555   1555  2.08  
LINK         SG  CYS B 183                ZN    ZN B 402     1555   1555  2.79  
SITE     1 AC1  4 CYS A 145  CYS A 148  CYS A 183  CYS A 186                    
SITE     1 AC2  4 CYS B 145  CYS B 148  CYS B 183  CYS B 186                    
SITE     1 AC3 17 TYR A  18  SER A  19  GLY A  20  LYS A  21                    
SITE     2 AC3 17 SER A  22  GLU A  23  SER A  57  HIS A  58                    
SITE     3 AC3 17 MSE A  59  ALA A 143  ILE A 144  HOH A 313                    
SITE     4 AC3 17 HOH A 322  HOH A 331  HOH A 334  HOH A 335                    
SITE     5 AC3 17 ILE B  34                                                     
SITE     1 AC4 12 ILE A  34  TYR B  18  SER B  19  GLY B  20                    
SITE     2 AC4 12 LYS B  21  SER B  22  GLU B  23  ALA B 143                    
SITE     3 AC4 12 ILE B 144  VAL B 146  HOH B 405  HOH B 424                    
CRYST1   53.793   67.166  103.638  90.00  90.00  90.00 P 21 21 2     8          
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      0.018590  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014888  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009649        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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