Header list of 2goh.pdb file
Complete list - 20 20 Bytes
HEADER VIRAL PROTEIN 12-APR-06 2GOH
TITLE THREE-DIMENSIONAL STRUCTURE OF THE TRANS-MEMBRANE DOMAIN OF VPU FROM
TITLE 2 HIV-1 IN ALIGNED PHOSPHOLIPID BICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VPU PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TRANS-MEMBRANE DOMAIN, RESIDUES 2-30;
COMPND 5 SYNONYM: U ORF PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 GENE: VPU;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: C43(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET31-B(+)
KEYWDS TRANS-MEMBRANE HELIX, 16C BICELLES, MAGNETIC ALIGNMENT, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 21
MDLTYP MINIMIZED AVERAGE
AUTHOR S.H.PARK,A.A.DE ANGELIS,A.A.NEVZOROV,C.H.WU,S.J.OPELLA
REVDAT 5 20-OCT-21 2GOH 1 SEQADV
REVDAT 4 04-DEC-19 2GOH 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2GOH 1 VERSN
REVDAT 2 10-OCT-06 2GOH 1 JRNL
REVDAT 1 08-AUG-06 2GOH 0
JRNL AUTH S.H.PARK,A.A.DE ANGELIS,A.A.NEVZOROV,C.H.WU,S.J.OPELLA
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE TRANSMEMBRANE DOMAIN OF
JRNL TITL 2 VPU FROM HIV-1 IN ALIGNED PHOSPHOLIPID BICELLES.
JRNL REF BIOPHYS.J. V. 91 3032 2006
JRNL REFN ISSN 0006-3495
JRNL PMID 16861273
JRNL DOI 10.1529/BIOPHYSJ.106.087106
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : STRUCTURAL FITTING
REMARK 3 AUTHORS : NEVZOROV, A.A. ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ORIENTATIONAL FREQUENCIES (15N CHEMICAL
REMARK 3 SHIFT AND 15N-1H DIPOLAR COUPLING) FOR EACH AMIDE SITE WERE USED.
REMARK 4
REMARK 4 2GOH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037363.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 15N-UNIFORMLY OR SELECTIVELY
REMARK 210 PEPTIDE ALIGNED IN 16C BICELLES (1,2-DI-O-HEXADECYL-SN-GLYCERO-3-
REMARK 210 PHOSPHOCHOLINE (16- O-PC) / 1,2-DI-O-HEXYL-SN-GLYCERO-3-
REMARK 210 PHOSPHOCHOLINE (6-O-PC) = 3.0, 28% W/V, 100% H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : PISEMA
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : STRUCTURAL FITTING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : FIRST 21 STRUCTURES
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-21
REMARK 465 RES C SSSEQI
REMARK 465 GLN A 2
REMARK 465 PRO A 3
REMARK 465 ILE A 4
REMARK 465 GLN A 5
REMARK 465 ILE A 6
REMARK 465 ILE A 26
REMARK 465 ILE A 27
REMARK 465 GLU A 28
REMARK 465 GLY A 29
REMARK 465 ARG A 30
REMARK 465 GLY A 31
REMARK 465 GLY A 32
REMARK 465 LYS A 33
REMARK 465 LYS A 34
REMARK 465 LYS A 35
REMARK 465 LYS A 36
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 VAL A 12 H ILE A 16 1.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GOF RELATED DB: PDB
REMARK 900 THREE-DIMENSIONAL STRUCTURE OF THE TRANS-MEMBRANE DOMAIN OF VPU
REMARK 900 FROM HIV-1 IN ALIGNED PHOSPHOLIPID BICELLES
DBREF 2GOH A 2 30 UNP Q70625 VPU_HV1LW 2 30
SEQADV 2GOH GLY A 29 UNP Q70625 TYR 29 ENGINEERED MUTATION
SEQADV 2GOH GLY A 31 UNP Q70625 CLONING ARTIFACT
SEQADV 2GOH GLY A 32 UNP Q70625 CLONING ARTIFACT
SEQADV 2GOH LYS A 33 UNP Q70625 CLONING ARTIFACT
SEQADV 2GOH LYS A 34 UNP Q70625 CLONING ARTIFACT
SEQADV 2GOH LYS A 35 UNP Q70625 CLONING ARTIFACT
SEQADV 2GOH LYS A 36 UNP Q70625 CLONING ARTIFACT
SEQRES 1 A 35 GLN PRO ILE GLN ILE ALA ILE VAL ALA LEU VAL VAL ALA
SEQRES 2 A 35 ILE ILE ILE ALA ILE VAL VAL TRP SER ILE VAL ILE ILE
SEQRES 3 A 35 GLU GLY ARG GLY GLY LYS LYS LYS LYS
HELIX 1 1 ALA A 7 VAL A 25 1 19
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 - 20 20 Bytes