Header list of 1ihv.pdb file
Complete list - 23 20 Bytes
HEADER DNA BINDING PROTEIN 12-MAY-95 1IHV TITLE SOLUTION STRUCTURE OF THE DNA BINDING DOMAIN OF HIV-1 INTEGRASE, NMR, TITLE 2 MINIMIZED AVERAGE 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS DNA-BINDING PROTEIN, AIDS, POLYPROTEIN, DNA BINDING PROTEIN EXPDTA SOLUTION NMR AUTHOR G.M.CLORE,P.J.LODI,J.A.ERNST,A.M.GRONENBORN REVDAT 4 23-FEB-22 1IHV 1 KEYWDS REMARK SEQADV REVDAT 3 24-FEB-09 1IHV 1 VERSN REVDAT 2 12-NOV-96 1IHV 1 HEADER REMARK REVDAT 1 14-OCT-96 1IHV 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 HIV-1 INTEGRASE 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 REMARK 3 HYDROGEN BONDS; 192 TORSION ANGLE (98 PHI, 20 PSI, 50 CHI1 REMARK 3 AND 24 CHI2) RESTRAINTS; 78 THREE-BOND HN-HA COUPLING REMARK 3 CONSTANT RESTRAINTS; 194 (100 CALPHA AND 94 CBETA) 13C REMARK 3 SHIFT RESTRAINTS; AND 392 1H CHEMICAL SHIFT RESTRAINTS REMARK 3 (102 CAH, 52 METHYL AND 238 OTHERS). (B) 44 INTERSUBUNIT REMARK 3 INTERPROTON DISTANCE RESTRAINTS (C) 30 AMBIGUOUS REMARK 3 INTERPROTON DISTANCE RESTRAINTS THAT CAN ARISE FROM INTRA REMARK 3 AND/OR INTERSUBUNIT INTERACTIONS. REMARK 3 REMARK 3 THE STRUCTURE IN THIS ENTRY IS THE RESTRAINED REGULARIZED REMARK 3 MEAN STRUCTURE AND THE LAST COLUMN REPRESENTS THE RMS OF REMARK 3 THE 40 INDIVIDUAL SIMULATED ANNEALING STRUCTURES FOUND IN REMARK 3 PDB ENTRY 1IHW ABOUT THE MEAN COORDINATE POSITIONS. THE REMARK 3 LAST COLUMN IN THE INDIVIDUAL SA STRUCTURES HAS NO MEANING. REMARK 4 REMARK 4 1IHV 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_1000174164. 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 : 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 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 221 -121.44 -79.70 REMARK 500 PRO A 233 4.25 -67.72 REMARK 500 LEU A 242 -72.91 -114.61 REMARK 500 GLU A 246 -153.32 -70.23 REMARK 500 ASP A 253 -77.80 -92.95 REMARK 500 ASN A 254 -133.29 -81.65 REMARK 500 SER A 255 55.27 -104.03 REMARK 500 GLN B 221 -121.49 -79.52 REMARK 500 PRO B 233 4.25 -67.68 REMARK 500 LEU B 242 -72.92 -114.55 REMARK 500 GLU B 246 -153.35 -70.25 REMARK 500 ASP B 253 -77.78 -92.92 REMARK 500 ASN B 254 -133.24 -81.63 REMARK 500 SER B 255 55.23 -104.08 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1IHW RELATED DB: PDB DBREF 1IHV A 220 270 UNP P04586 POL_HV1Z6 80 130 DBREF 1IHV B 220 270 UNP P04586 POL_HV1Z6 80 130 SEQADV 1IHV VAL A 234 UNP P04586 ILE 94 CONFLICT SEQADV 1IHV ALA A 265 UNP P04586 VAL 125 CONFLICT SEQADV 1IHV VAL B 234 UNP P04586 ILE 94 CONFLICT SEQADV 1IHV 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
Complete list - 23 20 Bytes