Header list of 1e0e.pdb file
Complete list - n 15 2 Bytes
HEADER INTEGRASE 25-MAR-00 1E0E
TITLE N-TERMINAL ZINC-BINDING HHCC DOMAIN OF HIV-2 INTEGRASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HUMAN IMMUNODEFICIENCY VIRUS TYPE 2 INTEGRASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL HHCC DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 2 (ISOLATE
SOURCE 3 ROD);
SOURCE 4 ORGANISM_COMMON: HIV-2;
SOURCE 5 ORGANISM_TAXID: 11720;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS INTEGRASE, AIDS, POLYPROTEIN, DIMER, ZINC-BINDING PROTEIN, HELIX-
KEYWDS 2 TURN-HELIX MOTIF
EXPDTA SOLUTION NMR
NUMMDL 32
AUTHOR A.P.A.M.EIJKELENBOOM,F.M.I.VAN DEN ENT,R.H.A.PLASTERK,R.KAPTEIN,
AUTHOR 2 R.BOELENS
REVDAT 5 15-JAN-20 1E0E 1 REMARK
REVDAT 4 14-JUN-17 1E0E 1 REMARK
REVDAT 3 24-FEB-09 1E0E 1 VERSN
REVDAT 2 24-JUN-03 1E0E 1 HELIX CRYST1
REVDAT 1 19-MAR-01 1E0E 0
SPRSDE 11-APR-00 1E0E 1AUB
JRNL AUTH A.P.A.M.EIJKELENBOOM,F.M.I.VAN DEN ENT,R.WECHSELBERGER,
JRNL AUTH 2 R.H.A.PLASTERK,R.KAPTEIN,R.BOELENS
JRNL TITL REFINED SOLUTION STRUCTURE OF THE DIMERIC N-TERMINAL HHCC
JRNL TITL 2 DOMAIN OF HIV-2 INTEGRASE
JRNL REF J.BIOMOL.NMR V. 18 119 2000
JRNL REFN ISSN 0925-2738
JRNL PMID 11101216
JRNL DOI 10.1023/A:1008342312269
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.P.A.M.EIJKELENBOOM,F.M.I.VAN DEN ENT,A.VOS,
REMARK 1 AUTH 2 J.F.DORELEIJERS,K.HARD,T.D.TULLIUS,R.H.A.PLASTERK,R.KAPTEIN,
REMARK 1 AUTH 3 R.BOELENS
REMARK 1 TITL SOLUTION STRUCTURE OF THE N-TERMINAL HHCC DOMAIN OF HIV-2
REMARK 1 TITL 2 INTEGRASE: A THREE-HELIX BUNDLE STABILIZED BY ZINC
REMARK 1 REF CURR.BIOL. V. 7 739 1997
REMARK 1 REFN ISSN 0960-9822
REMARK 1 PMID 9368756
REMARK 1 DOI 10.1016/S0960-9822(06)00332-0
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION
REMARK 4
REMARK 4 1E0E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-MAR-00.
REMARK 100 THE DEPOSITION ID IS D_1290004760.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : D2O AND 5% D2O/95% H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS; AMX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 32
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOW OVERALL ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: DETAILS CAN BE FOUND IN THE JRNL CITATION
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 MODELS 1-32
REMARK 465 RES C SSSEQI
REMARK 465 GLU A 48
REMARK 465 ALA A 49
REMARK 465 ILE A 50
REMARK 465 HIS A 51
REMARK 465 GLY A 52
REMARK 465 GLN A 53
REMARK 465 VAL A 54
REMARK 465 ASN A 55
REMARK 465 GLU B 48
REMARK 465 ALA B 49
REMARK 465 ILE B 50
REMARK 465 HIS B 51
REMARK 465 GLY B 52
REMARK 465 GLN B 53
REMARK 465 VAL B 54
REMARK 465 ASN B 55
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 MODELS 1-32
REMARK 470 RES CSSEQI ATOMS
REMARK 470 GLY A 47 CA C O
REMARK 470 GLY B 47 CA C O
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 1 TYR A 15 17.65 -148.04
REMARK 500 1 TYR B 15 17.68 -148.06
REMARK 500 2 TYR A 15 16.92 -145.50
REMARK 500 2 TYR B 15 16.89 -145.48
REMARK 500 3 TYR A 15 15.80 -147.84
REMARK 500 3 PRO A 29 -165.77 -56.04
REMARK 500 3 TYR B 15 15.69 -147.88
REMARK 500 3 PRO B 29 -165.80 -55.93
REMARK 500 4 TYR A 15 14.97 -146.04
REMARK 500 4 LYS A 46 -86.41 59.42
REMARK 500 4 TYR B 15 15.06 -145.96
REMARK 500 4 LYS B 46 -86.46 59.42
REMARK 500 5 TYR A 15 12.67 -145.28
REMARK 500 5 TYR B 15 12.65 -145.32
REMARK 500 6 PHE A 26 -62.35 -92.54
REMARK 500 6 PRO A 29 -177.94 -55.53
REMARK 500 6 PHE B 26 -62.45 -92.49
REMARK 500 6 PRO B 29 -177.76 -55.66
REMARK 500 7 TYR A 15 18.05 -148.52
REMARK 500 7 HIS A 16 44.45 39.98
REMARK 500 7 PHE A 26 -69.81 -99.97
REMARK 500 7 LYS A 46 -85.16 -136.35
REMARK 500 7 TYR B 15 17.98 -148.33
REMARK 500 7 HIS B 16 44.44 39.99
REMARK 500 7 PHE B 26 -69.73 -100.08
REMARK 500 7 LYS B 46 -85.01 -136.28
REMARK 500 8 TYR A 15 14.88 -148.22
REMARK 500 8 TYR B 15 14.80 -148.25
REMARK 500 9 TYR A 15 14.10 -143.25
REMARK 500 9 PHE A 26 -71.17 -115.33
REMARK 500 9 LYS A 46 -66.72 -103.41
REMARK 500 9 TYR B 15 14.39 -143.20
REMARK 500 9 PHE B 26 -71.21 -115.37
REMARK 500 9 LYS B 46 -66.67 -103.46
REMARK 500 10 TYR A 15 15.72 -146.68
REMARK 500 10 PHE A 26 -67.20 -107.76
REMARK 500 10 TYR B 15 15.88 -146.63
REMARK 500 10 PHE B 26 -67.28 -107.70
REMARK 500 11 GLN A 45 -177.94 -67.34
REMARK 500 11 LYS A 46 103.85 60.23
REMARK 500 11 GLN B 45 -177.76 -67.34
REMARK 500 11 LYS B 46 103.76 60.11
REMARK 500 12 LYS A 46 -166.81 -113.93
REMARK 500 12 LYS B 46 -166.92 -113.98
REMARK 500 13 TYR A 15 20.15 -142.26
REMARK 500 13 PHE A 26 -64.52 -94.63
REMARK 500 13 PRO A 29 179.52 -56.97
REMARK 500 13 TYR B 15 19.94 -142.11
REMARK 500 13 PHE B 26 -64.55 -94.68
REMARK 500 13 PRO B 29 179.45 -57.04
REMARK 500
REMARK 500 THIS ENTRY HAS 107 RAMACHANDRAN OUTLIERS.
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 147 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 16 ND1
REMARK 620 2 CYS A 43 SG 109.7
REMARK 620 3 CYS A 40 SG 108.9 109.4
REMARK 620 4 HIS A 12 NE2 109.6 109.8 109.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 147 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 16 ND1
REMARK 620 2 CYS B 40 SG 108.9
REMARK 620 3 CYS B 43 SG 109.7 109.5
REMARK 620 4 HIS B 12 NE2 109.6 109.4 109.7
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 147
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 147
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4619 RELATED DB: BMRB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 TER
REMARK 999 LYS: RESIDUES 47-55 ARE DISORDERED IN CHAIN A AND B, AND
REMARK 999 NOT INCLUDED IN THE STRUCTURE CALCULATIONS
DBREF 1E0E A 1 55 UNP P04584 POL_HV2RO 744 798
DBREF 1E0E B 1 55 UNP P04584 POL_HV2RO 744 798
SEQRES 1 A 55 PHE LEU GLU LYS ILE GLU PRO ALA GLN GLU GLU HIS GLU
SEQRES 2 A 55 LYS TYR HIS SER ASN VAL LYS GLU LEU SER HIS LYS PHE
SEQRES 3 A 55 GLY ILE PRO ASN LEU VAL ALA ARG GLN ILE VAL ASN SER
SEQRES 4 A 55 CYS ALA GLN CYS GLN GLN LYS GLY GLU ALA ILE HIS GLY
SEQRES 5 A 55 GLN VAL ASN
SEQRES 1 B 55 PHE LEU GLU LYS ILE GLU PRO ALA GLN GLU GLU HIS GLU
SEQRES 2 B 55 LYS TYR HIS SER ASN VAL LYS GLU LEU SER HIS LYS PHE
SEQRES 3 B 55 GLY ILE PRO ASN LEU VAL ALA ARG GLN ILE VAL ASN SER
SEQRES 4 B 55 CYS ALA GLN CYS GLN GLN LYS GLY GLU ALA ILE HIS GLY
SEQRES 5 B 55 GLN VAL ASN
HET ZN A 147 1
HET ZN B 147 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 2(ZN 2+)
HELIX 1 1 ILE A 5 TYR A 15 1 11
HELIX 2 2 VAL A 19 LYS A 25 1 7
HELIX 3 3 ASN A 30 SER A 39 1 10
HELIX 4 4 ALA A 41 GLN A 44 1 4
HELIX 5 1 ILE B 5 TYR B 15 1 11
HELIX 6 2 VAL B 19 LYS B 25 1 7
HELIX 7 3 ASN B 30 SER B 39 1 10
HELIX 8 4 ALA B 41 GLN B 44 1 4
LINK ZN ZN A 147 ND1 HIS A 16 1555 1555 2.01
LINK ZN ZN A 147 SG CYS A 43 1555 1555 2.30
LINK ZN ZN A 147 SG CYS A 40 1555 1555 2.30
LINK ZN ZN A 147 NE2 HIS A 12 1555 1555 2.00
LINK ZN ZN B 147 ND1 HIS B 16 1555 1555 2.01
LINK ZN ZN B 147 SG CYS B 40 1555 1555 2.30
LINK ZN ZN B 147 SG CYS B 43 1555 1555 2.30
LINK ZN ZN B 147 NE2 HIS B 12 1555 1555 2.00
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 2
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
MODEL 1
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