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HEADER ZN-BINDING PROTEIN 11-JUN-98 1WJE TITLE SOLUTION STRUCTURE OF H12C MUTANT OF THE N-TERMINAL ZN BINDING DOMAIN TITLE 2 OF HIV-1 INTEGRASE COMPLEXED TO CADMIUM, NMR, MINIMIZED AVERAGE TITLE 3 STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: HIV-1 INTEGRASE; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 CELL_LINE: BL21; SOURCE 5 GENE: POTENTIAL; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: T7; SOURCE 10 EXPRESSION_SYSTEM_VECTOR: T7 RNA POLYMERASE; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET-15B; SOURCE 12 EXPRESSION_SYSTEM_GENE: T7 KEYWDS ZN-BINDING PROTEIN, AIDS, POLYPROTEIN, HYDROLASE, ASPARTYL PROTEASE EXPDTA SOLUTION NMR AUTHOR M.CAI,A.M.GRONENBORN,G.M.CLORE REVDAT 3 14-MAR-18 1WJE 1 REMARK SEQADV REVDAT 2 24-FEB-09 1WJE 1 VERSN REVDAT 1 16-DEC-98 1WJE 0 JRNL AUTH M.CAI,Y.HUANG,M.CAFFREY,R.ZHENG,R.CRAIGIE,G.M.CLORE, JRNL AUTH 2 A.M.GRONENBORN JRNL TITL SOLUTION STRUCTURE OF THE HIS12 --> CYS MUTANT OF THE JRNL TITL 2 N-TERMINAL ZINC BINDING DOMAIN OF HIV-1 INTEGRASE COMPLEXED JRNL TITL 3 TO CADMIUM. JRNL REF PROTEIN SCI. V. 7 2669 1998 JRNL REFN ISSN 0961-8368 JRNL PMID 9865962 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE, REMARK 3 SIMONSON,WARREN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES WERE CALCULATED USING THE SIMULATED REMARK 3 ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. REMARK 3 229, 129-136, USING THE PROGRAM XPLOR 3.1 (BRUNGER) REMARK 3 MODIFIED TO INCORPORATE COUPLING CONSTANT (GARRETT ET AL. REMARK 3 (1984) J. MAGN RESON. SERIES B 104, 99-103), CARBON REMARK 3 CHEMICAL SHIFT (KUSZEWSKI ET AL. (1995) J. MAGN. RESON. REMARK 3 SERIES B 106, 92-96) RESTRAINTS AND A CONFORMATIONAL REMARK 3 DATABASE POTENTIAL (KUSZEWSKI ET AL. (1996) PROTEIN SCI 5, REMARK 3 1067-1080 AND (1997) J. MAGN. RESON. 125, 171-177). REMARK 3 REMARK 3 THE 3D STRUCTURE OF THE N-TERMINAL DOMAIN OF THE H12C REMARK 3 MUTANT OF HIV-1 INTEGRASE COMPLEXED TO CADMIUM WAS SOLVED REMARK 3 BY MULTI-DIMENSIONAL HETERONUCLEAR-EDITED AND -FILTERED REMARK 3 NMR IS BASED ON 757 EXPERIMENTAL RESTRAINTS (PER REMARK 3 MONOMER): (A) INTRASUBUNIT: 203 SEQUENTIAL (|I-J|=1), REMARK 3 161 MEDIUM RANGE (1 < |I-J| >=5) AND 82 LONG RANGE REMARK 3 (|I-J| >5) INTERRESIDUE, AND 5 INTRARESIDUE APPROXIMATE REMARK 3 INTERPROTON DISTANCE RESTRAINTS; 16 DISTANCE RESTRAINTS REMARK 3 FOR 8 HYDROGEN BONDS; 117 TORSION ANGLE (45 PHI, 35 PSI, REMARK 3 26 CHI1, 10 CHI2 AND 1 CHI3) RESTRAINTS; 47 THREE-BOND REMARK 3 HN-HA COUPLING CONSTANT RESTRAINTS; 99 (50 CALPHA AND REMARK 3 49 CBETA) 13C SHIFT RESTRAINTS. (B) 20 INTERSUBUNIT REMARK 3 INTERPROTON DISTANCE RESTRAINTS. (C) 7 AMBIGUOUS REMARK 3 INTERPROTON DISTANCE RESTRAINTS THAT CAN ARISE FROM INTRA REMARK 3 AND/OR INTERSUBUNIT INTERACTIONS. REMARK 3 REMARK 3 THE STRUCTURES WERE CALCULATED USING THE SIMULATED REMARK 3 ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. REMARK 3 229, 129-136, USING THE PROGRAM XPLOR 3.1 (BRUNGER) REMARK 3 MODIFIED TO INCORPORATE COUPLING CONSTANT (GARRETT ET AL. REMARK 3 (1984) J. MAGN RESON. SERIES B 104, 99-103), CARBON REMARK 3 CHEMICAL SHIFT (KUSZEWSKI ET AL. (1995) J. MAGN. RESON. REMARK 3 SERIES B 106, 92-96) RESTRAINTS AND A CONFORMATIONAL REMARK 3 DATABASE POTENTIAL (KUSZEWSKI ET AL. (1996) PROTEIN SCI 5, REMARK 3 1067-1080 AND (1997) J. MAGN. RESON. 125, 171-177). REMARK 3 REMARK 3 THE 3D STRUCTURE OF THE N-TERMINAL DOMAIN OF THE H12C REMARK 3 MUTANT OF HIV-1 INTEGRASE COMPLEXED TO CADMIUM WAS SOLVED REMARK 3 BY MULTI-DIMENSIONAL HETERONUCLEAR-EDITED AND -FILTERED REMARK 3 NMR IS BASED ON 757 EXPERIMENTAL RESTRAINTS (PER REMARK 3 MONOMER): (A) INTRASUBUNIT: 203 SEQUENTIAL (|I-J|=1), REMARK 3 161 MEDIUM RANGE (1 < |I-J| >=5) AND 82 LONG RANGE REMARK 3 (|I-J| >5) INTERRESIDUE, AND 5 INTRARESIDUE APPROXIMATE REMARK 3 INTERPROTON DISTANCE RESTRAINTS; 16 DISTANCE RESTRAINTS REMARK 3 FOR 8 HYDROGEN BONDS; 117 TORSION ANGLE (45 PHI, 35 PSI, REMARK 3 26 CHI1, 10 CHI2 AND 1 CHI3) RESTRAINTS; 47 THREE-BOND REMARK 3 HN-HA COUPLING CONSTANT RESTRAINTS; 99 (50 CALPHA AND REMARK 3 49 CBETA) 13C SHIFT RESTRAINTS. (B) 20 INTERSUBUNIT REMARK 3 INTERPROTON DISTANCE RESTRAINTS. (C) 7 AMBIGUOUS REMARK 3 INTERPROTON DISTANCE RESTRAINTS THAT CAN ARISE FROM INTRA REMARK 3 AND/OR INTERSUBUNIT INTERACTIONS. REMARK 4 REMARK 4 1WJE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000177210. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 4.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX600; DMX500 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS MODIFIED MODIFIED REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 40 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : REGULARIZED MEAN STRUCTURE REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: NULL 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: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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 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 HIS A 16 -134.69 57.74 REMARK 500 HIS B 16 -134.73 57.81 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 CD A 56 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 12 SG REMARK 620 2 CYS A 40 SG 107.6 REMARK 620 3 CYS A 43 SG 110.5 107.4 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CD B 56 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS B 12 SG REMARK 620 2 CYS B 40 SG 107.6 REMARK 620 3 CYS B 43 SG 110.5 107.4 REMARK 620 N 1 2 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 56 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 56 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1WJF RELATED DB: PDB REMARK 900 ENSEMBLE OF 40 SIMULATED ANNEALING STRUCTURES DBREF 1WJE A 1 46 UNP P04587 POL_HV1B5 728 773 DBREF 1WJE B 1 46 UNP P04587 POL_HV1B5 728 773 SEQADV 1WJE CYS A 12 UNP P04587 HIS 739 ENGINEERED MUTATION SEQADV 1WJE CYS B 12 UNP P04587 HIS 739 ENGINEERED MUTATION SEQRES 1 A 46 PHE LEU ASP GLY ILE ASP LYS ALA GLN GLU GLU CYS GLU SEQRES 2 A 46 LYS TYR HIS SER ASN TRP ARG ALA MET ALA SER ASP PHE SEQRES 3 A 46 ASN LEU PRO PRO VAL VAL ALA LYS GLU ILE VAL ALA SER SEQRES 4 A 46 CYS ASP LYS CYS GLN LEU LYS SEQRES 1 B 46 PHE LEU ASP GLY ILE ASP LYS ALA GLN GLU GLU CYS GLU SEQRES 2 B 46 LYS TYR HIS SER ASN TRP ARG ALA MET ALA SER ASP PHE SEQRES 3 B 46 ASN LEU PRO PRO VAL VAL ALA LYS GLU ILE VAL ALA SER SEQRES 4 B 46 CYS ASP LYS CYS GLN LEU LYS HET CD A 56 1 HET CD B 56 1 HETNAM CD CADMIUM ION FORMUL 3 CD 2(CD 2+) HELIX 1 1 ASP A 3 TYR A 15 5 13 HELIX 2 2 TRP A 19 PHE A 26 1 8 HELIX 3 3 PRO A 30 SER A 39 1 10 HELIX 4 4 ASP A 41 GLN A 44 1 4 HELIX 5 5 ASP B 3 TYR B 15 5 13 HELIX 6 6 TRP B 19 PHE B 26 1 8 HELIX 7 7 PRO B 30 SER B 39 1 10 HELIX 8 8 ASP B 41 GLN B 44 1 4 LINK CD CD A 56 SG CYS A 12 1555 1555 2.61 LINK CD CD A 56 SG CYS A 40 1555 1555 2.59 LINK CD CD A 56 SG CYS A 43 1555 1555 2.61 LINK CD CD B 56 SG CYS B 12 1555 1555 2.61 LINK CD CD B 56 SG CYS B 40 1555 1555 2.58 LINK CD CD B 56 SG CYS B 43 1555 1555 2.61 SITE 1 AC1 3 CYS A 12 CYS A 40 CYS A 43 SITE 1 AC2 3 CYS B 12 CYS B 40 CYS B 43 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 - 14 20 Bytes