Header list of 1fi0.pdb file
Complete list - 23 20 Bytes
HEADER VIRAL PROTEIN 03-AUG-00 1FI0
TITLE SOLUTION STRUCTURE OF HIV-1 VPR (13-33) PEPTIDE IN MICELLS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VPR PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: R ORF PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PROTEIN WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 IS NATURALLY FOUND IN HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 (RF/HAT
SOURCE 5 ISOLATE).
KEYWDS HELIX, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 22
AUTHOR A.ENGLER,T.STANGLER,D.WILLBOLD
REVDAT 3 23-FEB-22 1FI0 1 REMARK LINK
REVDAT 2 24-FEB-09 1FI0 1 VERSN
REVDAT 1 28-FEB-01 1FI0 0
JRNL AUTH A.ENGLER,T.STANGLER,D.WILLBOLD
JRNL TITL SOLUTION STRUCTURE OF HUMAN IMMUNODEFICIENCY VIRUS TYPE 1
JRNL TITL 2 VPR(13-33) PEPTIDE IN MICELLES.
JRNL REF EUR.J.BIOCHEM. V. 268 389 2001
JRNL REFN ISSN 0014-2956
JRNL PMID 11168374
JRNL DOI 10.1046/J.1432-1033.2001.01895.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 5.3, X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: MODIFIED AB INITIO SIMULATED ANNEALING
REMARK 3 PROTOCOL WHICH INCLUDES FLOATING ASSIGNMENT OF PROCHIRAL GROUPS
REMARK 4
REMARK 4 1FI0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011606.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.2MM VPR(13-33); 100MM DPC; 90%
REMARK 210 H20, 10%D20
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 : NDEE
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 160
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22
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 : 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: 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: 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 O LYS A 27 H VAL A 31 1.54
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 3 ASN A 16 82.40 44.86
REMARK 500 8 GLU A 17 18.67 59.43
REMARK 500 11 ASN A 16 -87.12 41.95
REMARK 500 17 ASN A 16 71.88 38.53
REMARK 500 17 GLU A 17 19.55 58.38
REMARK 500 22 ASN A 16 -53.67 -22.16
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 2 ARG A 32 0.14 SIDE CHAIN
REMARK 500 3 ARG A 32 0.28 SIDE CHAIN
REMARK 500 4 ARG A 32 0.27 SIDE CHAIN
REMARK 500 5 ARG A 32 0.18 SIDE CHAIN
REMARK 500 6 ARG A 32 0.29 SIDE CHAIN
REMARK 500 7 ARG A 32 0.30 SIDE CHAIN
REMARK 500 8 ARG A 32 0.32 SIDE CHAIN
REMARK 500 9 ARG A 32 0.19 SIDE CHAIN
REMARK 500 10 ARG A 32 0.30 SIDE CHAIN
REMARK 500 12 ARG A 32 0.27 SIDE CHAIN
REMARK 500 13 ARG A 32 0.22 SIDE CHAIN
REMARK 500 14 ARG A 32 0.22 SIDE CHAIN
REMARK 500 15 ARG A 32 0.29 SIDE CHAIN
REMARK 500 16 ARG A 32 0.19 SIDE CHAIN
REMARK 500 17 ARG A 32 0.32 SIDE CHAIN
REMARK 500 18 ARG A 32 0.20 SIDE CHAIN
REMARK 500 19 ARG A 32 0.32 SIDE CHAIN
REMARK 500 20 ARG A 32 0.15 SIDE CHAIN
REMARK 500 21 ARG A 32 0.27 SIDE CHAIN
REMARK 500 22 ARG A 32 0.19 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE A 12
DBREF 1FI0 A 13 33 UNP P05954 VPR_HV1RH 13 33
SEQRES 1 A 22 ACE GLU PRO TYR ASN GLU TRP THR LEU GLU LEU LEU GLU
SEQRES 2 A 22 GLU LEU LYS SER GLU ALA VAL ARG HIS
HET ACE A 12 6
HETNAM ACE ACETYL GROUP
FORMUL 1 ACE C2 H4 O
HELIX 1 1 GLU A 13 HIS A 33 1 21
LINK C ACE A 12 N GLU A 13 1555 1555 1.31
SITE 1 AC1 1 PRO A 14
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