Header list of 1ihw.pdb file
Complete list - b 23 2 Bytes
HEADER DNA BINDING PROTEIN 12-MAY-95 1IHW
TITLE SOLUTION STRUCTURE OF THE DNA BINDING DOMAIN OF HIV-1 INTEGRASE, NMR,
TITLE 2 40 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIV-1 INTEGRASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: DNA BINDING DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: NMR, 40 STRUCTURES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DNA-BINDING PROTEIN, AIDS, POLYPROTEIN, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 40
AUTHOR G.M.CLORE,P.J.LODI,J.A.ERNST,A.M.GRONENBORN
REVDAT 4 23-FEB-22 1IHW 1 KEYWDS REMARK SEQADV
REVDAT 3 24-FEB-09 1IHW 1 VERSN
REVDAT 2 12-NOV-96 1IHW 1 HEADER KEYWDS
REVDAT 1 11-JUL-96 1IHW 0
JRNL AUTH P.J.LODI,J.A.ERNST,J.KUSZEWSKI,A.B.HICKMAN,A.ENGELMAN,
JRNL AUTH 2 R.CRAIGIE,G.M.CLORE,A.M.GRONENBORN
JRNL TITL SOLUTION STRUCTURE OF THE DNA BINDING DOMAIN OF HIV-1
JRNL TITL 2 INTEGRASE.
JRNL REF BIOCHEMISTRY V. 34 9826 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7632683
JRNL DOI 10.1021/BI00031A002
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) AND 1H CHEMICAL SHIFT (KUSZEWSKI ET
REMARK 3 AL., 1995 J. MAGN RESON. SERIES B IN PRESS) RESTRAINTS
REMARK 3
REMARK 3 THE 3D STRUCTURE OF THE HUMAN SRY-DNA COMPLEX SOLVED BY
REMARK 3 MULTI-DIMENSIONAL HETERONUCLEAR-EDITED AND -FILTERED NMR
REMARK 3 IS BASED ON 2386 EXPERIMENTAL RESTRAINTS (FOR THE DIMER):
REMARK 3 (A) INTRASUBUNIT: 332 SEQUENTIAL (|I-J|=1), 202 MEDIUM
REMARK 3 RANGE (1 < |I-J| >=5) AND 530 LONG RANGE (|I-J| >5)
REMARK 3 INTERRESIDUES 318 INTRARESIDUE APPROXIMATE INTERPROTON
REMARK 3 DISTANCE RESTRAINTS; 74 DISTANCE RESTRAINTS FOR 37 HYDROGEN
REMARK 3 BONDS; 192 TORSION ANGLE (98 PHI, 20 PSI, 50 CHI1 AND 24
REMARK 3 CHI2) RESTRAINTS; 78 THREE-BOND HN-HA COUPLING CONSTANT
REMARK 3 RESTRAINTS; 194 (100 CALPHA AND 94 CBETA) 13C SHIFT
REMARK 3 RESTRAINTS; AND 392 1H CHEMICAL SHIFT RESTRAINTS (102 CAH,
REMARK 3 52 METHYL AND 238 OTHERS). (B) 44 INTERSUBUNIT INTERPROTON
REMARK 3 DISTANCE RESTRAINTS (C) 30 AMBIGUOUS INTERPROTON DISTANCE
REMARK 3 RESTRAINTS THAT CAN ARISE FROM INTRA AND/OR INTERSUBUNIT
REMARK 3 INTERACTIONS.
REMARK 3
REMARK 3 THE STRUCTURE FOUND IN PDB ENTRY 1IHV IS THE RESTRAINED
REMARK 3 REGULARIZED MEAN STRUCTURE AND THE LAST COLUMN REPRESENTS
REMARK 3 THE RMS OF THE 40 INDIVIDUAL SIMULATED ANNEALING STRUCTURES
REMARK 3 FOUND IN THIS ENTRY ABOUT THE MEAN COORDINATE POSITIONS.
REMARK 3 THE LAST COLUMN IN THE INDIVIDUAL SA STRUCTURES HAS NO
REMARK 3 MEANING.
REMARK 4
REMARK 4 1IHW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174165.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
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 : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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 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
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 1 GLN A 221 -119.00 -84.75
REMARK 500 1 PRO A 233 18.00 -67.13
REMARK 500 1 LEU A 242 -74.39 -117.86
REMARK 500 1 GLU A 246 -155.42 -67.69
REMARK 500 1 ASP A 253 -81.81 -87.95
REMARK 500 1 ASN A 254 -137.36 -78.60
REMARK 500 1 SER A 255 54.13 -97.97
REMARK 500 1 GLN B 221 -119.00 -84.78
REMARK 500 1 PRO B 233 18.16 -67.28
REMARK 500 1 LEU B 242 -74.49 -117.86
REMARK 500 1 GLU B 246 -155.42 -67.63
REMARK 500 1 ASP B 253 -81.83 -87.97
REMARK 500 1 ASN B 254 -137.42 -78.61
REMARK 500 1 SER B 255 54.25 -97.95
REMARK 500 2 GLN A 221 -146.82 -87.46
REMARK 500 2 LEU A 242 -74.55 -110.19
REMARK 500 2 GLU A 246 -153.66 -67.86
REMARK 500 2 ASP A 253 -81.54 -91.49
REMARK 500 2 ASN A 254 -129.71 -78.65
REMARK 500 2 SER A 255 54.29 -105.60
REMARK 500 2 GLN B 221 -146.75 -87.49
REMARK 500 2 LEU B 242 -74.56 -110.25
REMARK 500 2 GLU B 246 -153.82 -67.84
REMARK 500 2 ASP B 253 -81.62 -91.32
REMARK 500 2 ASN B 254 -129.77 -78.57
REMARK 500 2 SER B 255 54.32 -105.63
REMARK 500 3 GLN A 221 -136.77 -84.14
REMARK 500 3 PRO A 233 10.23 -62.95
REMARK 500 3 GLU A 246 -156.93 -68.68
REMARK 500 3 ASP A 253 -77.41 -90.37
REMARK 500 3 ASN A 254 -132.27 -81.81
REMARK 500 3 SER A 255 53.04 -104.26
REMARK 500 3 GLN B 221 -136.77 -84.24
REMARK 500 3 PRO B 233 10.25 -62.99
REMARK 500 3 LEU B 242 -70.08 -115.04
REMARK 500 3 GLU B 246 -156.80 -68.76
REMARK 500 3 ASP B 253 -77.39 -90.36
REMARK 500 3 ASN B 254 -132.31 -81.80
REMARK 500 3 SER B 255 53.07 -104.25
REMARK 500 4 GLN A 221 -142.90 -89.26
REMARK 500 4 PRO A 233 9.22 -67.62
REMARK 500 4 GLU A 246 -150.30 -69.88
REMARK 500 4 ASP A 253 -78.49 -91.12
REMARK 500 4 ASN A 254 -131.31 -80.59
REMARK 500 4 SER A 255 54.50 -105.35
REMARK 500 4 GLN B 221 -142.73 -89.16
REMARK 500 4 PRO B 233 9.34 -67.56
REMARK 500 4 GLU B 246 -150.31 -69.90
REMARK 500 4 ASP B 253 -78.44 -91.26
REMARK 500 4 ASN B 254 -131.39 -80.53
REMARK 500
REMARK 500 THIS ENTRY HAS 581 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IHV RELATED DB: PDB
DBREF 1IHW A 220 270 UNP P04586 POL_HV1Z6 80 130
DBREF 1IHW B 220 270 UNP P04586 POL_HV1Z6 80 130
SEQADV 1IHW VAL A 234 UNP P04586 ILE 94 CONFLICT
SEQADV 1IHW ALA A 265 UNP P04586 VAL 125 CONFLICT
SEQADV 1IHW VAL B 234 UNP P04586 ILE 94 CONFLICT
SEQADV 1IHW ALA B 265 UNP P04586 VAL 125 CONFLICT
SEQRES 1 A 52 MET ILE GLN ASN PHE ARG VAL TYR TYR ARG ASP SER ARG
SEQRES 2 A 52 ASP PRO VAL 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 ASP PRO VAL 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 A 2 PHE A 223 TYR A 227 0
SHEET 2 A 2 ALA A 265 ARG A 269 -1 N ILE A 268 O ARG A 224
SHEET 1 B 3 ILE A 257 PRO A 261 0
SHEET 2 B 3 ALA A 248 GLN A 252 -1 N ILE A 251 O LYS A 258
SHEET 3 B 3 LYS A 240 LYS A 244 -1 N TRP A 243 O VAL A 250
SHEET 1 C 2 PHE B 223 TYR B 227 0
SHEET 2 C 2 ALA B 265 ARG B 269 -1 N ILE B 268 O ARG B 224
SHEET 1 D 3 ILE B 257 PRO B 261 0
SHEET 2 D 3 ALA B 248 GLN B 252 -1 N ILE B 251 O LYS B 258
SHEET 3 D 3 LYS B 240 LYS B 244 -1 N TRP B 243 O VAL B 250
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 - b 23 2 Bytes