Header list of 1ibo.pdb file
Complete list - 23 20 Bytes
HEADER VIRAL PROTEIN 28-MAR-01 1IBO
TITLE NMR STRUCTURE OF HEMAGGLUTININ FUSION PEPTIDE IN DPC MICELLES AT PH
TITLE 2 7.4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMAGGLUTININ HA2 CHAIN PEPTIDE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1 TO 20 OF N-TERMINUS OF HA2 SUBUNIT;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN
SOURCE 4 INFLUENZA VIRUS STRAIN X31.
KEYWDS HELIX-KINK-IRREGULAR, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR X.HAN,J.H.BUSHWELLER,D.S.CAFISO,L.K.TAMM
REVDAT 3 23-FEB-22 1IBO 1 REMARK
REVDAT 2 24-FEB-09 1IBO 1 VERSN
REVDAT 1 08-AUG-01 1IBO 0
JRNL AUTH X.HAN,J.H.BUSHWELLER,D.S.CAFISO,L.K.TAMM
JRNL TITL MEMBRANE STRUCTURE AND FUSION-TRIGGERING CONFORMATIONAL
JRNL TITL 2 CHANGE OF THE FUSION DOMAIN FROM INFLUENZA HEMAGGLUTININ.
JRNL REF NAT.STRUCT.BIOL. V. 8 715 2001
JRNL REFN ISSN 1072-8368
JRNL PMID 11473264
JRNL DOI 10.1038/90434
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, OPAL 2.6
REMARK 3 AUTHORS : GUNTERT (DYANA), LUGINBULH (OPAL)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 398 RESTRAINTS, 135 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 58
REMARK 3 DIHEDRAL ANGLE RESTRAINTS,
REMARK 4
REMARK 4 1IBO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013133.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 0.02
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM PEPTIDE IN THE PRESENCE OF
REMARK 210 200 MM D38-DPC IN 0.05% NAN3, 5
REMARK 210 MM DTT, 20 MM D4-ACETIC ACID, PH
REMARK 210 7.4
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D-NOESY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS
REMARK 210 ARE THE 20 STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 5
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR
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 1 ASN A 12 -41.53 -140.37
REMARK 500 1 GLU A 15 116.67 -161.95
REMARK 500 1 MET A 17 12.08 -144.44
REMARK 500 2 ASN A 12 -43.11 -138.05
REMARK 500 2 GLU A 15 116.42 -160.73
REMARK 500 3 ASN A 12 -41.68 -139.55
REMARK 500 3 GLU A 15 116.56 -160.83
REMARK 500 3 MET A 17 14.35 -143.86
REMARK 500 4 ASN A 12 -32.45 -139.23
REMARK 500 4 ILE A 18 42.00 -103.34
REMARK 500 5 ASN A 12 -48.64 -139.09
REMARK 500 5 ILE A 18 44.29 -103.37
REMARK 500 6 ILE A 18 42.13 -103.31
REMARK 500 7 ILE A 18 42.60 -103.29
REMARK 500 8 GLU A 15 104.06 -162.16
REMARK 500 9 GLU A 15 102.65 -160.35
REMARK 500 9 ILE A 18 43.63 -103.26
REMARK 500 10 ASN A 12 81.97 -150.32
REMARK 500 10 MET A 17 10.05 -143.67
REMARK 500 10 ILE A 18 40.73 -103.14
REMARK 500 11 MET A 17 10.77 -147.91
REMARK 500 11 ILE A 18 44.07 -103.14
REMARK 500 12 ASN A 12 -45.87 -138.84
REMARK 500 12 ILE A 18 42.29 -103.30
REMARK 500 14 ILE A 18 56.90 -104.03
REMARK 500 15 ASN A 12 -33.45 -137.31
REMARK 500 15 ILE A 18 53.19 -104.10
REMARK 500 16 ILE A 18 54.05 -104.18
REMARK 500 17 GLU A 15 116.32 -166.34
REMARK 500 17 MET A 17 7.78 -167.92
REMARK 500 18 ASN A 12 81.19 -151.96
REMARK 500 18 GLU A 15 -115.68 -141.79
REMARK 500 18 ILE A 18 41.68 -103.30
REMARK 500 19 GLU A 15 -105.73 -123.94
REMARK 500 19 ILE A 18 47.12 -103.59
REMARK 500 20 GLU A 15 -107.11 -140.02
REMARK 500 20 ASP A 19 66.56 -68.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IBN RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF HEMAGGLUTININ FUSION PEPTIDE IN DPC MICELLES AT PH
REMARK 900 5
DBREF 1IBO A 1 20 UNP P03442 HEMA_IADU3 346 365
SEQRES 1 A 20 GLY LEU PHE GLY ALA ILE ALA GLY PHE ILE GLU ASN GLY
SEQRES 2 A 20 TRP GLU GLY MET ILE ASP GLY
HELIX 1 1 GLY A 1 ILE A 10 1 10
CRYST1 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 - 23 20 Bytes