Header list of 1wja.pdb file
Complete list - 2 20 Bytes
HEADER ZN-BINDING PROTEIN 13-MAY-97 1WJA
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL ZN BINDING DOMAIN OF HIV-1
TITLE 2 INTEGRASE (D FORM), NMR, REGULARIZED MEAN STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIV-1 INTEGRASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 GENE: POTENTIAL;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ZN-BINDING PROTEIN, AIDS, POLYPROTEIN, HYDROLASE, ASPARTYL PROTEASE,
KEYWDS 2 ENDONUCLEASE
EXPDTA SOLUTION NMR
AUTHOR G.M.CLORE,M.CAI,M.CAFFREY,A.M.GRONENBORN
REVDAT 3 02-MAR-22 1WJA 1 REMARK LINK
REVDAT 2 24-FEB-09 1WJA 1 VERSN
REVDAT 1 13-MAY-98 1WJA 0
JRNL AUTH M.CAI,R.ZHENG,M.CAFFREY,R.CRAIGIE,G.M.CLORE,A.M.GRONENBORN
JRNL TITL SOLUTION STRUCTURE OF THE N-TERMINAL ZINC BINDING DOMAIN OF
JRNL TITL 2 HIV-1 INTEGRASE.
JRNL REF NAT.STRUCT.BIOL. V. 4 567 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9228950
JRNL DOI 10.1038/NSB0797-567
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
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 HIV-1
REMARK 3 INTEGRASE WAS SOLVED BY
REMARK 3 MULTI-DIMENSIONAL HETERONUCLEAR-EDITED AND -FILTERED NMR
REMARK 3 IS BASED ON 640 EXPERIMENTAL RESTRAINTS (PER MONOMER):
REMARK 3 (A) INTRASUBUNIT: 156 SEQUENTIAL (|I-J|=1), 137 MEDIUM
REMARK 3 RANGE (1 < |I-J| >=5) AND 47 LONG RANGE (|I-J| >5)
REMARK 3 INTERRESIDUE, AND 15 INTRARESIDUE APPROXIMATE INTERPROTON
REMARK 3 DISTANCE RESTRAINTS; 14 DISTANCE RESTRAINTS FOR 7
REMARK 3 HYDROGEN BONDS; 92 TORSION ANGLE (45 PHI, 5 PSI, 30 CHI1
REMARK 3 AND 12 CHI2) RESTRAINTS; 36 THREE-BOND HN-HA COUPLING
REMARK 3 CONSTANT RESTRAINTS; 97 (50 CALPHA AND 47 CBETA) 13C
REMARK 3 SHIFT RESTRAINTS.
REMARK 3 (B) 28 INTERSUBUNIT INTERPROTON DISTANCE RESTRAINTS.
REMARK 3 (C) 23 AMBIGUOUS INTERPROTON DISTANCE RESTRAINTS THAT CAN
REMARK 3 ARISE FROM INTRA AND/OR INTERSUBUNIT INTERACTIONS.
REMARK 3
REMARK 3 THE STRUCTURE IN THIS ENTRY IS THE RESTRAINED REGULARIZED
REMARK 3 MEAN STRUCTURE AND THE LAST NUMERIC COLUMN REPRESENTS THE
REMARK 3 RMS OF THE 40 INDIVIDUAL SIMULATED ANNEALING STRUCTURES
REMARK 3 FOUND IN THE RELATED PDB ENTRY ABOUT THE MEAN COORDINATE
REMARK 3 POSITIONS. THE LAST NUMERIC COLUMN IN THE INDIVIDUAL SA
REMARK 3 STRUCTURES HAS NO MEANING. THE LAST LETTER COLUMN
REMARK 3 SIGNIFIES THE SUBUNIT (A OR B).
REMARK 4
REMARK 4 1WJA 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_1000177206.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.4
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 : 600 MHZ; 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX600; DMX500; DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR MODIFIED MODIFIED
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
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: 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 RES CSSEQI ATOMS
REMARK 470 GLY A 47 O
REMARK 470 GLY B 47 O
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 O PRO A 30 H LYS A 34 1.58
REMARK 500 O PRO B 30 H LYS B 34 1.58
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 GLN A 44 -75.22 -77.43
REMARK 500 GLN B 44 -75.85 -77.35
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 56 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 12 ND1
REMARK 620 2 HIS A 16 ND1 109.4
REMARK 620 3 CYS A 40 SG 122.6 119.3
REMARK 620 4 CYS A 43 SG 90.1 106.1 103.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 56 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 12 ND1
REMARK 620 2 HIS B 16 ND1 109.4
REMARK 620 3 CYS B 40 SG 122.6 119.3
REMARK 620 4 CYS B 43 SG 90.1 106.1 103.1
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 56
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 56
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WJB RELATED DB: PDB
DBREF 1WJA A 1 47 UNP P35963 POL_HV1Y2 716 762
DBREF 1WJA B 1 47 UNP P35963 POL_HV1Y2 716 762
SEQRES 1 A 47 PHE LEU ASP GLY ILE ASP LYS ALA GLN GLU GLU HIS GLU
SEQRES 2 A 47 LYS TYR HIS SER ASN TRP ARG ALA MET ALA SER ASP PHE
SEQRES 3 A 47 ASN LEU PRO PRO VAL VAL ALA LYS GLU ILE VAL ALA SER
SEQRES 4 A 47 CYS ASP LYS CYS GLN LEU LYS GLY
SEQRES 1 B 47 PHE LEU ASP GLY ILE ASP LYS ALA GLN GLU GLU HIS GLU
SEQRES 2 B 47 LYS TYR HIS SER ASN TRP ARG ALA MET ALA SER ASP PHE
SEQRES 3 B 47 ASN LEU PRO PRO VAL VAL ALA LYS GLU ILE VAL ALA SER
SEQRES 4 B 47 CYS ASP LYS CYS GLN LEU LYS GLY
HET ZN A 56 1
HET ZN B 56 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 2(ZN 2+)
HELIX 1 1 LEU A 2 ALA A 8 1 7
HELIX 2 2 LYS A 14 SER A 17 1 4
HELIX 3 3 TRP A 19 PHE A 26 1 8
HELIX 4 4 PRO A 30 SER A 39 1 10
HELIX 5 5 ASP A 41 GLN A 44 1 4
HELIX 6 6 LEU B 2 ALA B 8 1 7
HELIX 7 7 LYS B 14 SER B 17 1 4
HELIX 8 8 TRP B 19 PHE B 26 1 8
HELIX 9 9 PRO B 30 SER B 39 1 10
HELIX 10 10 ASP B 41 GLN B 44 1 4
LINK ND1 HIS A 12 ZN ZN A 56 1555 1555 2.12
LINK ND1 HIS A 16 ZN ZN A 56 1555 1555 2.22
LINK SG CYS A 40 ZN ZN A 56 1555 1555 2.31
LINK SG CYS A 43 ZN ZN A 56 1555 1555 2.21
LINK ND1 HIS B 12 ZN ZN B 56 1555 1555 2.12
LINK ND1 HIS B 16 ZN ZN B 56 1555 1555 2.22
LINK SG CYS B 40 ZN ZN B 56 1555 1555 2.31
LINK SG CYS B 43 ZN ZN B 56 1555 1555 2.21
SITE 1 AC1 4 HIS A 12 HIS A 16 CYS A 40 CYS A 43
SITE 1 AC2 4 HIS B 12 HIS B 16 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 - 2 20 Bytes