Header list of 1kzt.pdb file
Complete list - 23 20 Bytes
HEADER VIRAL PROTEIN 08-FEB-02 1KZT
TITLE STRUCTURE OF HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 VPR(34-51) PEPTIDE IN
TITLE 2 DPC MICELLE CONTAINING AQUEOUS SOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VPR PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 34-51;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. IT IS
SOURCE 4 NATURALLY FOUND IN HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 (NEW YORK-5
SOURCE 5 ISOLATE) (HIV-1).
KEYWDS HIV-1, VPR, SOLUTION STRUCTURE, DODECYLPHOSPHOCHOLINE, MICELLES,
KEYWDS 2 VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.ENGLER,T.STANGLER,D.WILLBOLD
REVDAT 3 23-FEB-22 1KZT 1 REMARK LINK
REVDAT 2 24-FEB-09 1KZT 1 VERSN
REVDAT 1 28-AUG-02 1KZT 0
JRNL AUTH A.ENGLER,T.STANGLER,D.WILLBOLD
JRNL TITL STRUCTURE OF HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 VPR(34-51)
JRNL TITL 2 PEPTIDE IN MICELLE CONTAINING AQUEOUS SOLUTION.
JRNL REF EUR.J.BIOCHEM. V. 269 3264 2002
JRNL REFN ISSN 0014-2956
JRNL PMID 12084067
JRNL DOI 10.1046/J.1432-1033.2002.03005.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851, X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES WERE CALCULATED USING
REMARK 3 FLOATING CHIRALITY.
REMARK 4
REMARK 4 1KZT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-02.
REMARK 100 THE DEPOSITION ID IS D_1000015516.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : 100MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM VPR(34-51); 100MM
REMARK 210 DODECYLPHOSPHOCHOLINE D38; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 5.3, NDEE
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 97
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: 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 ILE A 37 -156.14 -59.73
REMARK 500 3 ILE A 37 -162.90 -58.68
REMARK 500 6 LEU A 39 -50.72 69.11
REMARK 500 6 TYR A 50 98.94 -174.87
REMARK 500 9 LEU A 39 -44.72 72.49
REMARK 500 9 THR A 49 -73.52 -101.72
REMARK 500 11 ILE A 37 -151.09 -60.61
REMARK 500 13 ARG A 36 92.36 171.67
REMARK 500 15 ILE A 37 -131.24 -73.47
REMARK 500 16 ARG A 36 85.22 -162.67
REMARK 500 16 THR A 49 -54.12 71.82
REMARK 500 18 ILE A 37 -139.42 -68.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 36 0.12 SIDE CHAIN
REMARK 500 2 ARG A 36 0.13 SIDE CHAIN
REMARK 500 3 ARG A 36 0.31 SIDE CHAIN
REMARK 500 4 ARG A 36 0.32 SIDE CHAIN
REMARK 500 5 ARG A 36 0.10 SIDE CHAIN
REMARK 500 6 ARG A 36 0.23 SIDE CHAIN
REMARK 500 7 ARG A 36 0.11 SIDE CHAIN
REMARK 500 8 ARG A 36 0.31 SIDE CHAIN
REMARK 500 9 ARG A 36 0.31 SIDE CHAIN
REMARK 500 10 ARG A 36 0.32 SIDE CHAIN
REMARK 500 11 ARG A 36 0.30 SIDE CHAIN
REMARK 500 12 ARG A 36 0.32 SIDE CHAIN
REMARK 500 13 ARG A 36 0.32 SIDE CHAIN
REMARK 500 14 ARG A 36 0.31 SIDE CHAIN
REMARK 500 15 ARG A 36 0.29 SIDE CHAIN
REMARK 500 16 ARG A 36 0.16 SIDE CHAIN
REMARK 500 17 ARG A 36 0.27 SIDE CHAIN
REMARK 500 18 ARG A 36 0.21 SIDE CHAIN
REMARK 500 19 ARG A 36 0.19 SIDE CHAIN
REMARK 500 20 ARG A 36 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 52
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KZS RELATED DB: PDB
REMARK 900 1KZS IS THE STRUCTURE OF HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 VPR(34-
REMARK 900 51) PEPTIDE IN AQUEOUS TFE SOLUTION.
REMARK 900 RELATED ID: 1KZV RELATED DB: PDB
REMARK 900 1KZV IS THE STRUCTURE OF HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 VPR(34-
REMARK 900 51) PEPTIDE IN CHLOROFORM METHANOL.
DBREF 1KZT A 34 51 UNP P12520 VPR_HV1N5 34 51
SEQRES 1 A 20 ACE PHE PRO ARG ILE TRP LEU HIS ASN LEU GLY GLN HIS
SEQRES 2 A 20 ILE TYR GLU THR TYR GLY NH2
HET ACE A 33 6
HET NH2 A 52 3
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
FORMUL 1 ACE C2 H4 O
FORMUL 1 NH2 H2 N
HELIX 1 1 ILE A 37 TYR A 50 1 14
LINK C ACE A 33 N PHE A 34 1555 1555 1.30
LINK C GLY A 51 N NH2 A 52 1555 1555 1.31
SITE 1 AC2 1 GLY A 51
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 - 23 20 Bytes