Header list of 1b03.pdb file
Complete list - 29 20 Bytes
HEADER VIRAL PROTEIN 17-NOV-98 1B03 TITLE SOLUTION STRUCTURE OF THE ANTIBODY-BOUND HIV-1IIIB V3 PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (P1053 PEPTIDE); COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: P1053 PEPTIDE REPRESENTS THE FULL ANTIBODY RECOGNIZED COMPND 6 EPITOPE OF THE HIV-1IIIB GP120 V3 LOOP. SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. KEYWDS P1053 STRUCTURE, VIRAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 35 AUTHOR V.TUGARINOV,A.ZVI,R.LEVY,J.ANGLISTER REVDAT 5 29-NOV-17 1B03 1 REMARK HELIX REVDAT 4 24-FEB-09 1B03 1 VERSN REVDAT 3 01-APR-03 1B03 1 JRNL REVDAT 2 15-DEC-99 1B03 4 HEADER COMPND REMARK JRNL REVDAT 2 2 4 ATOM SOURCE SEQRES REVDAT 1 25-NOV-98 1B03 0 JRNL AUTH V.TUGARINOV,A.ZVI,R.LEVY,J.ANGLISTER JRNL TITL A CIS PROLINE TURN LINKING TWO BETA-HAIRPIN STRANDS IN THE JRNL TITL 2 SOLUTION STRUCTURE OF AN ANTIBODY-BOUND HIV-1IIIB V3 JRNL TITL 3 PEPTIDE. JRNL REF NAT.STRUCT.BIOL. V. 6 331 1999 JRNL REFN ISSN 1072-8368 JRNL PMID 10201400 JRNL DOI 10.1038/7567 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.ZVI,D.J.FEIGELSON,Y.HAYEK,J.ANGLISTER REMARK 1 TITL CONFORMATION OF THE PRINCIPAL NEUTRALIZING DETERMINANT OF REMARK 1 TITL 2 HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 IN COMPLEX WITH AN REMARK 1 TITL 3 ANTI-GP120 VIRUS NEUTRALIZING ANTIBODY STUDIED BY REMARK 1 TITL 4 TWO-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE DIFFERENCE REMARK 1 TITL 5 SPECTROSCOPY. REMARK 1 REF BIOCHEMISTRY V. 36 8619 1997 REMARK 1 REFN ISSN 0006-2960 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 AFTER INITIAL SIMULATED ANNEALING CALCULATIONS THE STRUCTURES WERE REMARK 3 MINIMIZED REMARK 3 USING A FULL L-J POTENTIAL REPRESENTATION. THE CIS PEPTIDE BOND REMARK 3 BETWEEN GLY 12 REMARK 3 AND PRO 13 WAS PATHED CIS IN THE PROCESS OF STRUCTURE GENERATION. REMARK 4 REMARK 4 1B03 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-NOV-98. REMARK 100 THE DEPOSITION ID IS D_1000000097. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 305 REMARK 210 PH : 7.1 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N; 13C FILTERED NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE REMARK 210 METHOD USED : HYBRID DG-SA REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 35 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: REMARK 210 THE STRUCTURE WAS DETERMINED IN COMPLEX WITH THE FV ANTIBODY REMARK 210 FRAGMENT USING REMARK 210 ISOTOPE-FILTERED AND ISOTOPE-EDITED NMR WITH EITHER THE FV OR THE REMARK 210 PEPTIDE REMARK 210 LABELLED WITH 15N AND 13C. 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: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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 2 ALA A 16 -166.47 -169.52 REMARK 500 4 ARG A 15 88.22 -62.28 REMARK 500 5 ALA A 16 -168.12 -170.28 REMARK 500 6 ALA A 16 -165.16 -160.48 REMARK 500 8 ALA A 16 -169.32 -160.96 REMARK 500 10 ALA A 16 -166.63 -168.85 REMARK 500 14 ALA A 16 -168.13 -170.42 REMARK 500 19 ALA A 16 -168.86 -163.29 REMARK 500 21 ALA A 16 -174.74 -170.22 REMARK 500 23 ALA A 16 -164.61 -168.31 REMARK 500 35 ARG A 15 98.84 -61.58 REMARK 500 REMARK 500 REMARK: NULL DBREF 1B03 A 4 21 UNP Q79428 Q79428_9HIV1 108 125 SEQRES 1 A 18 ARG LYS SER ILE ARG ILE GLN ARG GLY PRO GLY ARG ALA SEQRES 2 A 18 PHE VAL THR ILE GLY SHEET 1 A 2 LYS A 5 ILE A 9 0 SHEET 2 A 2 ALA A 16 ILE A 20 -1 N ILE A 20 O LYS A 5 CISPEP 1 GLY A 12 PRO A 13 1 0.07 CISPEP 2 GLY A 12 PRO A 13 2 0.14 CISPEP 3 GLY A 12 PRO A 13 3 0.04 CISPEP 4 GLY A 12 PRO A 13 4 0.01 CISPEP 5 GLY A 12 PRO A 13 5 0.18 CISPEP 6 GLY A 12 PRO A 13 6 0.13 CISPEP 7 GLY A 12 PRO A 13 7 0.12 CISPEP 8 GLY A 12 PRO A 13 8 0.13 CISPEP 9 GLY A 12 PRO A 13 9 -0.15 CISPEP 10 GLY A 12 PRO A 13 10 -0.07 CISPEP 11 GLY A 12 PRO A 13 11 0.06 CISPEP 12 GLY A 12 PRO A 13 12 -0.05 CISPEP 13 GLY A 12 PRO A 13 13 -0.03 CISPEP 14 GLY A 12 PRO A 13 14 0.11 CISPEP 15 GLY A 12 PRO A 13 15 0.00 CISPEP 16 GLY A 12 PRO A 13 16 -0.11 CISPEP 17 GLY A 12 PRO A 13 17 -0.02 CISPEP 18 GLY A 12 PRO A 13 18 0.24 CISPEP 19 GLY A 12 PRO A 13 19 0.16 CISPEP 20 GLY A 12 PRO A 13 20 -0.02 CISPEP 21 GLY A 12 PRO A 13 21 0.13 CISPEP 22 GLY A 12 PRO A 13 22 0.17 CISPEP 23 GLY A 12 PRO A 13 23 0.00 CISPEP 24 GLY A 12 PRO A 13 24 0.02 CISPEP 25 GLY A 12 PRO A 13 25 0.03 CISPEP 26 GLY A 12 PRO A 13 26 0.08 CISPEP 27 GLY A 12 PRO A 13 27 0.35 CISPEP 28 GLY A 12 PRO A 13 28 0.24 CISPEP 29 GLY A 12 PRO A 13 29 -0.17 CISPEP 30 GLY A 12 PRO A 13 30 0.04 CISPEP 31 GLY A 12 PRO A 13 31 -0.07 CISPEP 32 GLY A 12 PRO A 13 32 -0.12 CISPEP 33 GLY A 12 PRO A 13 33 0.05 CISPEP 34 GLY A 12 PRO A 13 34 -0.02 CISPEP 35 GLY A 12 PRO A 13 35 0.31 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 - 29 20 Bytes