Header list of 1pje.pdb file
Complete list - 27 202 Bytes
HEADER VIRAL PROTEIN 02-JUN-03 1PJE
TITLE STRUCTURE OF THE CHANNEL-FORMING TRANS-MEMBRANE DOMAIN OF VIRUS
TITLE 2 PROTEIN "U"(VPU) FROM HIV-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VPU PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TRANS-MEMBRANE DOMAIN;
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: BLR(DE3)PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-31B(+)
KEYWDS ALPHA-HELIX, VIRAL PROTEIN
EXPDTA SOLID-STATE NMR
AUTHOR S.H.PARK,A.A.MRSE,A.A.NEVZOROV,M.F.MESLEH,M.OBLATT-MONTAL,M.MONTAL,
AUTHOR 2 S.J.OPELLA
REVDAT 3 27-OCT-21 1PJE 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1PJE 1 VERSN
REVDAT 1 14-OCT-03 1PJE 0
JRNL AUTH S.H.PARK,A.A.MRSE,A.A.NEVZOROV,M.F.MESLEH,M.OBLATT-MONTAL,
JRNL AUTH 2 M.MONTAL,S.J.OPELLA
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE CHANNEL-FORMING
JRNL TITL 2 TRANS-MEMBRANE DOMAIN OF VIRUS PROTEIN "U" (VPU) FROM HIV-1
JRNL REF J.MOL.BIOL. V. 333 409 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 14529626
JRNL DOI 10.1016/J.JMB.2003.08.048
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.1, STRUCTURAL FITTING 1.0
REMARK 3 AUTHORS : DELAGLIO, GRZESIEK, VUISTER, ZHU, PFEIFER, BAX
REMARK 3 (NMRPIPE), NEVZOROV, OPELLA (STRUCTURAL FITTING)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THIS STRUCTURE WAS CALCULATED BY USING
REMARK 3 A STRUCTURAL FITTING ALGORITHM THAT FINDS TORSION ANGLES BETWEEN
REMARK 3 CONSECUTIVE RESIDUES BASED ON THEIR NMR FREQUENCIES
REMARK 4
REMARK 4 1PJE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000019359.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : COMPLETELY ALIGNED SAMPLE IN
REMARK 210 GLASS PLATES: 3.5 MG VPU2-30+ U-
REMARK 210 15N, 75 MG LIPID MIXTURE (DOPC:
REMARK 210 DOPG, 9:1)
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : PISEMA
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : STRUCTURAL FITTING 1.0
REMARK 210 METHOD USED : DIRECT STRUCTURAL FITTING OF 2D
REMARK 210 SOLID-STATE NMR DATA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMIZED AVERAGE STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: PISEMA: POLARIZATION INVERSION SPIN EXCHANGE AT THE MAGIC
REMARK 210 ANGLE
REMARK 217
REMARK 217 SOLID STATE NMR STUDY
REMARK 217 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLID
REMARK 217 STATE NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 217 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 217 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 RES C SSSEQI
REMARK 465 MET A 1
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 LEU A 11 H ILE A 15 1.38
REMARK 500 O ALA A 18 H TRP A 22 1.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PI8 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE CHANNEL-FORMING TRANS-MEMBRANE DOMAIN OF VIRUS
REMARK 900 PROTEIN "U" (VPU) FROM HIV-1-NMR, 4 STRUCTURES
DBREF 1PJE A 1 30 UNP Q70625 VPU_HV1LW 1 30
SEQADV 1PJE GLY A 29 UNP Q70625 TYR 29 ENGINEERED MUTATION
SEQADV 1PJE GLY A 31 UNP Q70625 CLONING ARTIFACT
SEQADV 1PJE GLY A 32 UNP Q70625 CLONING ARTIFACT
SEQADV 1PJE LYS A 33 UNP Q70625 CLONING ARTIFACT
SEQADV 1PJE LYS A 34 UNP Q70625 CLONING ARTIFACT
SEQADV 1PJE LYS A 35 UNP Q70625 CLONING ARTIFACT
SEQADV 1PJE LYS A 36 UNP Q70625 CLONING ARTIFACT
SEQRES 1 A 36 MET GLN PRO ILE GLN ILE ALA ILE VAL ALA LEU VAL VAL
SEQRES 2 A 36 ALA ILE ILE ILE ALA ILE VAL VAL TRP SER ILE VAL ILE
SEQRES 3 A 36 ILE GLU GLY ARG GLY GLY LYS LYS LYS LYS
HELIX 1 1 ILE A 8 VAL A 25 1 18
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
Complete list - 27 202 Bytes