GenomeNet

Database: PDB
Entry: 1OVX
LinkDB: 1OVX
Original site: 1OVX 
HEADER    METAL BINDING PROTEIN                   27-MAR-03   1OVX              
TITLE     NMR STRUCTURE OF THE E. COLI CLPX CHAPERONE ZINC BINDING DOMAIN DIMER 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX;       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN (RESIDUES 1-60);                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: CLPX;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    TREBLE CLEF ZINC FINGER, HOMODIMER, METAL BINDING PROTEIN             
EXPDTA    SOLUTION NMR                                                          
AUTHOR    L.W.DONALDSON,J.KWAN,U.WOJTYRA,W.A.HOURY                              
REVDAT   3   13-JUL-11 1OVX    1       VERSN                                    
REVDAT   2   24-FEB-09 1OVX    1       VERSN                                    
REVDAT   1   30-DEC-03 1OVX    0                                                
JRNL        AUTH   L.W.DONALDSON,U.WOJTYRA,W.A.HOURY                            
JRNL        TITL   SOLUTION STRUCTURE OF THE DIMERIC ZINC BINDING DOMAIN OF THE 
JRNL        TITL 2 CHAPERONE CLPX.                                              
JRNL        REF    J.BIOL.CHEM.                  V. 278 48991 2003              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   14525985                                                     
JRNL        DOI    10.1074/JBC.M307826200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR NIH                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON 463             
REMARK   3  INTRAMOLECULAR DISTANCE RESTRAINTS, 47 INTERMOLECULAR RESTRAINTS    
REMARK   3  AND 24 HYDROGEN BOND RESTRAINTS. 30 PHI/PSI DIHEDRAL ANGLE          
REMARK   3  RESTRAINTS WERE INCORPORATED BASED ON ANALYSIS OF CHEMICAL SHIFTS   
REMARK   3  BY TALOS                                                            
REMARK   4                                                                      
REMARK   4 1OVX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAR-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB018718.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 303                                
REMARK 210  PH                             : 7.5                                
REMARK 210  IONIC STRENGTH                 : 150 MM NACL                        
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 1.3 MM CLPX U-15N,13C              
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D_13C/15N-SEPARATED_NOESY         
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ; 500 MHZ                   
REMARK 210  SPECTROMETER MODEL             : AVANCE; INOVA                      
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER; VARIAN                     
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : X-PLOR NIH, NMRPIPE 2.1, NMRVIEW   
REMARK 210                                   5.0                                
REMARK 210   METHOD USED                   : SIMULATED ANNEALING CARTESIAN      
REMARK 210                                   DYNAMICS                           
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 500                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 1                                  
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH ACCEPTABLE         
REMARK 210                                   COVALENT GEOMETRY                  
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD TRIPLE-         
REMARK 210  RESONANCE NMR METHODS                                               
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;                   
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                            
REMARK 465     RES C SSSEQI                                                     
REMARK 465     GLY A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     THR A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     ARG A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     LYS A    10                                                      
REMARK 465     GLU A    49                                                      
REMARK 465     GLU A    50                                                      
REMARK 465     ILE A    51                                                      
REMARK 465     LYS A    52                                                      
REMARK 465     GLU A    53                                                      
REMARK 465     VAL A    54                                                      
REMARK 465     ALA A    55                                                      
REMARK 465     PRO A    56                                                      
REMARK 465     HIS A    57                                                      
REMARK 465     ARG A    58                                                      
REMARK 465     GLU A    59                                                      
REMARK 465     ARG A    60                                                      
REMARK 465     GLY B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     THR B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     ARG B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     ASP B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     SER B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     LYS B    10                                                      
REMARK 465     GLU B    49                                                      
REMARK 465     GLU B    50                                                      
REMARK 465     ILE B    51                                                      
REMARK 465     LYS B    52                                                      
REMARK 465     GLU B    53                                                      
REMARK 465     VAL B    54                                                      
REMARK 465     ALA B    55                                                      
REMARK 465     PRO B    56                                                      
REMARK 465     HIS B    57                                                      
REMARK 465     ARG B    58                                                      
REMARK 465     GLU B    59                                                      
REMARK 465     ARG B    60                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
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   HG   SER A    20     H    GLU A    23              1.23            
REMARK 500   HG   SER B    20     H    GLU B    23              1.23            
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    SER A  32        4.40   -160.89                                   
REMARK 500    PHE B  16      -60.74    -93.72                                   
REMARK 500    SER B  32        1.77   -161.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A  61  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  14   SG                                                     
REMARK 620 2 CYS A  17   SG  109.5                                              
REMARK 620 3 CYS A  36   SG  109.3 109.8                                        
REMARK 620 4 CYS A  39   SG  108.9 108.7 110.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B  61  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  14   SG                                                     
REMARK 620 2 CYS B  17   SG  109.6                                              
REMARK 620 3 CYS B  36   SG  109.4 109.8                                        
REMARK 620 4 CYS B  39   SG  109.0 108.4 110.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 61                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 61                   
DBREF  1OVX A    1    60  UNP    P0A6H1   CLPX_ECOLI       1     60             
DBREF  1OVX B    1    60  UNP    P0A6H1   CLPX_ECOLI       1     60             
SEQADV 1OVX GLY A   -6  UNP  P0A6H1              EXPRESSION TAG                 
SEQADV 1OVX HIS A   -5  UNP  P0A6H1              EXPRESSION TAG                 
SEQADV 1OVX HIS A   -4  UNP  P0A6H1              EXPRESSION TAG                 
SEQADV 1OVX HIS A   -3  UNP  P0A6H1              EXPRESSION TAG                 
SEQADV 1OVX HIS A   -2  UNP  P0A6H1              EXPRESSION TAG                 
SEQADV 1OVX HIS A   -1  UNP  P0A6H1              EXPRESSION TAG                 
SEQADV 1OVX HIS A    0  UNP  P0A6H1              EXPRESSION TAG                 
SEQADV 1OVX GLY B   -6  UNP  P0A6H1              EXPRESSION TAG                 
SEQADV 1OVX HIS B   -5  UNP  P0A6H1              EXPRESSION TAG                 
SEQADV 1OVX HIS B   -4  UNP  P0A6H1              EXPRESSION TAG                 
SEQADV 1OVX HIS B   -3  UNP  P0A6H1              EXPRESSION TAG                 
SEQADV 1OVX HIS B   -2  UNP  P0A6H1              EXPRESSION TAG                 
SEQADV 1OVX HIS B   -1  UNP  P0A6H1              EXPRESSION TAG                 
SEQADV 1OVX HIS B    0  UNP  P0A6H1              EXPRESSION TAG                 
SEQRES   1 A   67  GLY HIS HIS HIS HIS HIS HIS THR ASP LYS ARG LYS ASP          
SEQRES   2 A   67  GLY SER GLY LYS LEU LEU TYR CYS SER PHE CYS GLY LYS          
SEQRES   3 A   67  SER GLN HIS GLU VAL ARG LYS LEU ILE ALA GLY PRO SER          
SEQRES   4 A   67  VAL TYR ILE CYS ASP GLU CYS VAL ASP LEU CYS ASN ASP          
SEQRES   5 A   67  ILE ILE ARG GLU GLU ILE LYS GLU VAL ALA PRO HIS ARG          
SEQRES   6 A   67  GLU ARG                                                      
SEQRES   1 B   67  GLY HIS HIS HIS HIS HIS HIS THR ASP LYS ARG LYS ASP          
SEQRES   2 B   67  GLY SER GLY LYS LEU LEU TYR CYS SER PHE CYS GLY LYS          
SEQRES   3 B   67  SER GLN HIS GLU VAL ARG LYS LEU ILE ALA GLY PRO SER          
SEQRES   4 B   67  VAL TYR ILE CYS ASP GLU CYS VAL ASP LEU CYS ASN ASP          
SEQRES   5 B   67  ILE ILE ARG GLU GLU ILE LYS GLU VAL ALA PRO HIS ARG          
SEQRES   6 B   67  GLU ARG                                                      
HET     ZN  A  61       1                                                       
HET     ZN  B  61       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   3   ZN    2(ZN 2+)                                                     
HELIX    1   1 ASP A   37  ARG A   48  1                                  12    
HELIX    2   2 ASP B   37  ARG B   48  1                                  12    
SHEET    1   A 2 LEU A  27  ALA A  29  0                                        
SHEET    2   A 2 TYR A  34  CYS A  36 -1  O  ILE A  35   N  ILE A  28           
SHEET    1   B 2 LEU B  27  ALA B  29  0                                        
SHEET    2   B 2 TYR B  34  CYS B  36 -1  O  ILE B  35   N  ILE B  28           
LINK         SG  CYS A  14                ZN    ZN A  61     1555   1555  2.30  
LINK         SG  CYS A  17                ZN    ZN A  61     1555   1555  2.32  
LINK         SG  CYS A  36                ZN    ZN A  61     1555   1555  2.29  
LINK         SG  CYS A  39                ZN    ZN A  61     1555   1555  2.27  
LINK         SG  CYS B  14                ZN    ZN B  61     1555   1555  2.30  
LINK         SG  CYS B  17                ZN    ZN B  61     1555   1555  2.32  
LINK         SG  CYS B  36                ZN    ZN B  61     1555   1555  2.29  
LINK         SG  CYS B  39                ZN    ZN B  61     1555   1555  2.27  
SITE     1 AC1  4 CYS A  14  CYS A  17  CYS A  36  CYS A  39                    
SITE     1 AC2  4 CYS B  14  CYS B  17  CYS B  36  CYS B  39                    
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system