Header list of 2hmx.pdb file
Complete list - r 9 2 Bytes
HEADER MATRIX PROTEIN 22-SEP-95 2HMX
TITLE HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 MATRIX PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 MATRIX PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HIV-1 MA, HIVP17, P17, MA;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 CELL_LINE: BL21;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: WISP93-93
KEYWDS HIV-1 P17, HIV-1 MA, MATRIX PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.A.MASSIAH,M.R.STARICH,C.PASCHALL,A.M.CHRISTENSEN,W.I.SUNDQUIST,
AUTHOR 2 M.F.SUMMERS
REVDAT 3 09-MAR-22 2HMX 1 REMARK
REVDAT 2 24-FEB-09 2HMX 1 VERSN
REVDAT 1 29-JAN-96 2HMX 0
SPRSDE 29-JAN-96 2HMX 1HMX
JRNL AUTH M.A.MASSIAH,M.R.STARICH,C.PASCHALL,M.F.SUMMERS,
JRNL AUTH 2 A.M.CHRISTENSEN,W.I.SUNDQUIST
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE HUMAN IMMUNODEFICIENCY
JRNL TITL 2 VIRUS TYPE 1 MATRIX PROTEIN.
JRNL REF J.MOL.BIOL. V. 244 198 1994
JRNL REFN ISSN 0022-2836
JRNL PMID 7966331
JRNL DOI 10.1006/JMBI.1994.1719
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DSPACE
REMARK 3 AUTHORS : BIOSYM
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HMX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178208.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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
DBREF 2HMX A 3 133 UNP P12497 POL_HV1N5 1 131
SEQRES 1 A 133 HIS MET GLY ALA ARG ALA SER VAL LEU SER GLY GLY GLU
SEQRES 2 A 133 LEU ASP LYS TRP GLU LYS ILE ARG LEU ARG PRO GLY GLY
SEQRES 3 A 133 LYS LYS GLN TYR LYS LEU LYS HIS ILE VAL TRP ALA SER
SEQRES 4 A 133 ARG GLU LEU GLU ARG PHE ALA VAL ASN PRO GLY LEU LEU
SEQRES 5 A 133 GLU THR SER GLU GLY CYS ARG GLN ILE LEU GLY GLN LEU
SEQRES 6 A 133 GLN PRO SER LEU GLN THR GLY SER GLU GLU LEU ARG SER
SEQRES 7 A 133 LEU TYR ASN THR ILE ALA VAL LEU TYR CYS VAL HIS GLN
SEQRES 8 A 133 ARG ILE ASP VAL LYS ASP THR LYS GLU ALA LEU ASP LYS
SEQRES 9 A 133 ILE GLU GLU GLU GLN ASN LYS SER LYS LYS LYS ALA GLN
SEQRES 10 A 133 GLN ALA ALA ALA ASP THR GLY ASN ASN SER GLN VAL SER
SEQRES 11 A 133 GLN ASN TYR
HELIX 1 1 GLY A 11 LYS A 19 1 9
HELIX 2 2 LEU A 32 ALA A 46 1 15
HELIX 3 3 PRO A 49 GLU A 53 1 5
HELIX 4 4 SER A 55 GLY A 72 1 18
HELIX 5 5 GLU A 74 GLN A 91 1 18
HELIX 6 6 THR A 98 GLU A 107 1 10
SHEET 1 A 3 ILE A 20 LEU A 22 0
SHEET 2 A 3 LYS A 28 TYR A 30 -1
SHEET 3 A 3 LYS A 96 THR A 98 -1
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 - r 9 2 Bytes