Header list of 1ovx.pdb file
Complete list - 25 20 Bytes
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
Complete list - 25 20 Bytes