Header list of 1qmc.pdb file
Complete list - t 14 2 Bytes
HEADER TRANSFERASE 27-SEP-99 1QMC
TITLE C-TERMINAL DNA-BINDING DOMAIN OF HIV-1 INTEGRASE, NMR, 42
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIV-1 INTEGRASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL DNA-BINDING DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 BH10;
SOURCE 3 ORGANISM_TAXID: 11678;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS INTEGRASE, DNA-BINDING PROTEIN, SRC HOMOLOGY 3 (SH3)-LIKE
KEYWDS 2 FOLD, AIDS, POLYPROTEIN, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 42
AUTHOR A.P.A.M.EIJKELENBOOM,R.SPRANGERS,K.HARD,R.A.PURAS LUTZKE,
AUTHOR 2 R.H.A.PLASTERK,R.BOELENS,R.KAPTEIN
REVDAT 3 14-OCT-15 1QMC 1 HEADER SOURCE KEYWDS REMARK
REVDAT 3 2 VERSN SEQADV
REVDAT 2 24-FEB-09 1QMC 1 VERSN
REVDAT 1 14-DEC-99 1QMC 0
JRNL AUTH A.P.A.M.EIJKELENBOOM,R.SPRANGERS,K.HARD,
JRNL AUTH 2 R.A.PURAS LUTZKE,R.H.A.PLASTERK,R.BOELENS,R.KAPTEIN
JRNL TITL REFINED SOLUTION STRUCTURE OF THE C-TERMINAL DNA-
JRNL TITL 2 BINDING DOMAIN OF HUMAN IMMUNOVIRUS-1 INTEGRASE.
JRNL REF PROTEINS: STRUCT.,FUNCT., V. 36 556 1999
JRNL REF 2 GENET.
JRNL REFN ISSN 0887-3585
JRNL PMID 10450096
JRNL DOI 10.1002/(SICI)1097-0134(19990901)36:4<556::AI
JRNL DOI 2 D-PROT18>3.3.CO;2-Y
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.P.A.M.EIJKELENBOOM,R.A.PURAS LUTZKE,R.BOELENS,
REMARK 1 AUTH 2 R.H.A.PLASTERK,R.KAPTEIN,K.HARD
REMARK 1 TITL THE DNA-BINDING DOMAIN OF HIV-1 INTEGRASE HAS AN
REMARK 1 TITL 2 SH3-LIKE FOLD
REMARK 1 REF NAT.STRUCT.BIOL. V. 2 807 1995
REMARK 1 REFN ISSN 1072-8368
REMARK 1 PMID 7552753
REMARK 1 DOI 10.1038/NSB0995-807
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
REMARK 3 THE JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1QMC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-SEP-99.
REMARK 100 THE PDBE ID CODE IS EBI-1996.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.7
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 : 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY+ 750; AMX 600
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR 3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 42
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOW OVERALL ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: MODEL 1 IS CLOSEST TO THE AVERAGE FOR RESIDUES 220-270.
REMARK 210 RESIDUE 219 IS DISORDERED.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 720 ANGSTROM**2
REMARK 350 SURFACE AREA FOR THE COMPLEX: 7810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7 KCAL/MOL
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 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 GLN A 221 -65.13 -139.26
REMARK 500 1 GLU A 246 -149.20 -60.95
REMARK 500 1 ASN A 254 -77.20 -158.20
REMARK 500 1 GLN B 221 -64.97 -139.26
REMARK 500 1 GLU B 246 -149.27 -60.92
REMARK 500 1 ASN B 254 -77.25 -158.13
REMARK 500 2 GLN A 221 -67.25 -142.88
REMARK 500 2 LEU A 242 -50.70 -132.83
REMARK 500 2 GLU A 246 -149.55 -67.13
REMARK 500 2 ASN A 254 -75.36 -170.31
REMARK 500 2 GLN B 221 -67.24 -142.87
REMARK 500 2 LEU B 242 -50.79 -132.84
REMARK 500 2 GLU B 246 -149.68 -67.14
REMARK 500 2 ASN B 254 -75.24 -170.41
REMARK 500 3 GLN A 221 -59.85 -130.53
REMARK 500 3 LEU A 242 -50.25 -127.44
REMARK 500 3 GLU A 246 -150.07 -64.63
REMARK 500 3 ASN A 254 -79.87 -165.51
REMARK 500 3 GLN B 221 -59.80 -130.39
REMARK 500 3 LEU B 242 -50.26 -127.57
REMARK 500 3 GLU B 246 -150.07 -64.63
REMARK 500 3 ASN B 254 -79.90 -165.38
REMARK 500 4 GLN A 221 -62.72 -130.61
REMARK 500 4 LEU A 242 -42.93 -133.19
REMARK 500 4 GLU A 246 -154.50 -85.20
REMARK 500 4 ALA A 248 108.12 -173.61
REMARK 500 4 ASN A 254 -71.28 -173.05
REMARK 500 4 GLN B 221 -62.71 -130.71
REMARK 500 4 LEU B 242 -42.99 -133.14
REMARK 500 4 GLU B 246 -154.53 -85.09
REMARK 500 4 ALA B 248 108.14 -173.56
REMARK 500 4 ASN B 254 -71.33 -173.02
REMARK 500 5 GLN A 221 -66.16 -139.92
REMARK 500 5 GLU A 246 -149.74 -67.12
REMARK 500 5 ASN A 254 -78.31 -171.04
REMARK 500 5 GLN B 221 -66.24 -139.83
REMARK 500 5 GLU B 246 -149.65 -67.18
REMARK 500 5 ASN B 254 -78.34 -171.02
REMARK 500 6 GLN A 221 -63.51 -151.53
REMARK 500 6 GLU A 246 -155.43 -72.74
REMARK 500 6 ALA A 248 115.13 -167.57
REMARK 500 6 ASN A 254 -75.90 -175.35
REMARK 500 6 GLN B 221 -63.55 -151.59
REMARK 500 6 GLU B 246 -155.33 -72.82
REMARK 500 6 ALA B 248 115.12 -167.67
REMARK 500 6 ASN B 254 -75.93 -175.31
REMARK 500 7 GLN A 221 -66.87 -144.95
REMARK 500 7 ASN A 222 80.37 -150.96
REMARK 500 7 SER A 230 -70.45 -51.62
REMARK 500 7 GLU A 246 -150.98 -73.25
REMARK 500
REMARK 500 THIS ENTRY HAS 372 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE FIVE-STRANDED SHEET STRUCTURE OF THIS MOLECULE CONTAINS
REMARK 700 TWO BIFURCATED SHEETS IN THIS STRUCTURE. EACH IS REPRESENTED
REMARK 700 BY SHEETS WHICH HAVE ONE OR MORE IDENTICAL STRANDS.
REMARK 700 SHEETS AB AND AC (CHAIN A) REPRESENT THE BIFURCATED CONTRIBUTIONS
REMARK 700 TO THE MAIN 5-STRANDED SHEET STRUCTURE.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A5V RELATED DB: PDB
REMARK 900 ASV INTEGRASE CORE DOMAIN WITH HIV-1 INTEGRASE INHIBITOR Y3
REMARK 900 AND MN CATION
REMARK 900 RELATED ID: 1A5W RELATED DB: PDB
REMARK 900 ASV INTEGRASE CORE DOMAIN WITH HIV-1 INTEGRASE INHIBITOR Y3
REMARK 900 RELATED ID: 1A5X RELATED DB: PDB
REMARK 900 ASV INTEGRASE CORE DOMAIN WITH HIV-1 INTEGRASE INHIBITOR Y3
REMARK 900 RELATED ID: 1AUB RELATED DB: PDB
REMARK 900 N-TERMINAL DOMAIN OF HIV-2 INTEGRASE, NMR, 20 STRUCTURES
REMARK 900 RELATED ID: 1B9D RELATED DB: PDB
REMARK 900 MOBILITY OF AN HIV-1 INTEGRASE ACTIVE SITE LOOP IS
REMARK 900 CORRELATED WITH CATALYTIC ACTIVITY
REMARK 900 RELATED ID: 1B9F RELATED DB: PDB
REMARK 900 MOBILITY OF AN HIV-1 INTEGRASE ACTIVE SITE LOOP IS
REMARK 900 CORRELATED WITH CATALYTIC ACTIVITY
REMARK 900 RELATED ID: 1BHL RELATED DB: PDB
REMARK 900 CACODYLATED CATALYTIC DOMAIN OF HIV-1 INTEGRASE
REMARK 900 RELATED ID: 1BI4 RELATED DB: PDB
REMARK 900 CATALYTIC DOMAIN OF HIV-1 INTEGRASE
REMARK 900 RELATED ID: 1BIS RELATED DB: PDB
REMARK 900 HIV-1 INTEGRASE CORE DOMAIN
REMARK 900 RELATED ID: 1BIU RELATED DB: PDB
REMARK 900 HIV-1 INTEGRASE CORE DOMAIN COMPLEXED WITH MG++
REMARK 900 RELATED ID: 1BL3 RELATED DB: PDB
REMARK 900 CATALYTIC DOMAIN OF HIV-1 INTEGRASE
REMARK 900 RELATED ID: 1WJA RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE N-TERMINAL ZN BINDING DOMAIN
REMARK 900 OF HIV-1 INTEGRASE (D FORM), NMR, REGULARIZED MEAN
REMARK 900 STRUCTURE
REMARK 900 RELATED ID: 1WJB RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE N-TERMINAL ZN BINDING DOMAIN
REMARK 900 OF HIV-1 INTEGRASE (D FORM), NMR, 40 STRUCTURES
REMARK 900 RELATED ID: 1WJC RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE N-TERMINAL ZN BINDING DOMAIN
REMARK 900 OF HIV-1 INTEGRASE (E FORM), NMR, REGULARIZED MEAN
REMARK 900 STRUCTURE
REMARK 900 RELATED ID: 1WJD RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE N-TERMINAL ZN BINDING DOMAIN
REMARK 900 OF HIV-1 INTEGRASE (E FORM), NMR, 38 STRUCTURES
REMARK 900 RELATED ID: 1WJE RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF H12C MUTANT OF THE N-TERMINAL ZN
REMARK 900 BINDING DOMAIN OF HIV-1 INTEGRASE COMPLEXED TO CADMIUM,
REMARK 900 NMR, MINIMIZED AVERAGE STRUCTURE
REMARK 900 RELATED ID: 1WJF RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF H12C MUTANT OF THE N-TERMINAL ZN
REMARK 900 BINDING DOMAIN OF HIV-1 INTEGRASE COMPLEXED TO CADMIUM,
REMARK 900 NMR, 40 STRUCTURES
REMARK 900 RELATED ID: 2ITG RELATED DB: PDB
REMARK 900 CATALYTIC DOMAIN OF HIV-1 INTEGRASE: ORDERED ACTIVE SITE
REMARK 900 IN THE F185H CONSTRUCT
DBREF 1QMC A 220 270 UNP P03366 POL_HV1B1 947 997
DBREF 1QMC B 220 270 UNP P03366 POL_HV1B1 947 997
SEQADV 1QMC MET A 219 UNP P03366 CLONING ARTIFACT
SEQADV 1QMC MET B 219 UNP P03366 CLONING ARTIFACT
SEQRES 1 A 52 MET ILE GLN ASN PHE ARG VAL TYR TYR ARG ASP SER ARG
SEQRES 2 A 52 ASN PRO LEU TRP LYS GLY PRO ALA LYS LEU LEU TRP LYS
SEQRES 3 A 52 GLY GLU GLY ALA VAL VAL ILE GLN ASP ASN SER ASP ILE
SEQRES 4 A 52 LYS VAL VAL PRO ARG ARG LYS ALA LYS ILE ILE ARG ASP
SEQRES 1 B 52 MET ILE GLN ASN PHE ARG VAL TYR TYR ARG ASP SER ARG
SEQRES 2 B 52 ASN PRO LEU TRP LYS GLY PRO ALA LYS LEU LEU TRP LYS
SEQRES 3 B 52 GLY GLU GLY ALA VAL VAL ILE GLN ASP ASN SER ASP ILE
SEQRES 4 B 52 LYS VAL VAL PRO ARG ARG LYS ALA LYS ILE ILE ARG ASP
HELIX 1 1 ARG A 262 LYS A 264 5 3
HELIX 2 2 ARG B 262 LYS B 264 5 3
SHEET 1 AA 5 ILE A 257 PRO A 261 0
SHEET 2 AA 5 ALA A 248 GLN A 252 -1 N ILE A 251 O LYS A 258
SHEET 3 AA 5 LYS A 236 LYS A 244 -1 N ALA A 239 O GLN A 252
SHEET 4 AA 5 PHE A 223 TYR A 227 -1 N VAL A 225 O PRO A 238
SHEET 5 AA 5 ALA A 265 ARG A 269 -1 N ILE A 268 O ARG A 224
SHEET 1 AB 3 ILE A 257 PRO A 261 0
SHEET 2 AB 3 ALA A 248 GLN A 252 -1 N ILE A 251 O LYS A 258
SHEET 3 AB 3 LYS A 240 LYS A 244 -1 N LYS A 240 O GLN A 252
SHEET 1 AC 3 LYS A 236 ALA A 239 0
SHEET 2 AC 3 PHE A 223 TYR A 227 -1 N VAL A 225 O PRO A 238
SHEET 3 AC 3 ALA B 265 ARG B 269 -1 N ILE B 268 O ARG B 224
SHEET 1 BA 5 ILE B 257 PRO B 261 0
SHEET 2 BA 5 ALA B 248 GLN B 252 -1 N ILE B 251 O LYS B 258
SHEET 3 BA 5 LYS B 236 LYS B 244 -1 N ALA B 239 O GLN B 252
SHEET 4 BA 5 PHE B 223 TYR B 227 -1 N VAL B 225 O PRO B 238
SHEET 5 BA 5 ALA B 265 ARG B 269 -1 N ILE B 268 O ARG B 224
SHEET 1 BB 3 ILE B 257 PRO B 261 0
SHEET 2 BB 3 ALA B 248 GLN B 252 -1 N ILE B 251 O LYS B 258
SHEET 3 BB 3 LYS B 240 LYS B 244 -1 N LYS B 240 O GLN B 252
SHEET 1 BC 3 LYS B 236 ALA B 239 0
SHEET 2 BC 3 PHE B 223 TYR B 227 -1 N VAL B 225 O PRO B 238
SHEET 3 BC 3 ALA B 265 ARG B 269 -1 N ILE B 268 O ARG B 224
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
MODEL 1
Complete list - t 14 2 Bytes