Header list of 1tam.pdb file
Complete list - 2 20 Bytes
HEADER MATRIX PROTEIN 07-FEB-96 1TAM
TITLE HUMAN IMMUNODEFICIENCY VIRUS, NMR, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIV-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: HIV-1 M:B_HXB2R;
SOURCE 3 ORGANISM_TAXID: 11706;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS AIDS, CORE PROTEIN, POLYPROTEIN, MYRISTYLATION, PHOSPHORYLATION,
KEYWDS 2 MATRIX PROTEIN
EXPDTA SOLUTION NMR
AUTHOR S.MATTHEWS,P.BARLOW,N.CLARK,S.KINGSMAN,A.KINGSMAN,I.CAMPBELL
REVDAT 4 02-MAR-22 1TAM 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1TAM 1 VERSN
REVDAT 2 12-NOV-96 1TAM 1 HEADER
REVDAT 1 11-JUL-96 1TAM 0
JRNL AUTH S.MATTHEWS,P.BARLOW,N.CLARK,S.KINGSMAN,A.KINGSMAN,I.CAMPBELL
JRNL TITL REFINED SOLUTION STRUCTURE OF P17, THE HIV MATRIX PROTEIN.
JRNL REF BIOCHEM.SOC.TRANS. V. 23 725 1995
JRNL REFN ISSN 0300-5127
JRNL PMID 8654825
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.MATTHEWS,P.BARLOW,J.BOYD,G.BARTON,R.RUSSELL,H.MILLS,
REMARK 1 AUTH 2 M.CUNNINGHAM,N.MEYERS,N.BURNS,N.CLARK,ET AL.
REMARK 1 TITL STRUCTURAL SIMILARITY BETWEEN THE P17 MATRIX PROTEIN OF
REMARK 1 TITL 2 HIV-1 AND INTERFERON-GAMMA
REMARK 1 REF NATURE V. 370 666 1994
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TAM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176582.
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 : 1
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
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 ASP A 121
REMARK 465 THR A 122
REMARK 465 GLY A 123
REMARK 465 HIS A 124
REMARK 465 SER A 125
REMARK 465 SER A 126
REMARK 465 GLN A 127
REMARK 465 VAL A 128
REMARK 465 SER A 129
REMARK 465 GLN A 130
REMARK 465 ASN A 131
REMARK 465 TYR A 132
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 ALA A 5 49.06 -92.93
REMARK 500 VAL A 7 34.71 -98.14
REMARK 500 LEU A 8 116.32 61.36
REMARK 500 SER A 9 -44.41 -158.63
REMARK 500 VAL A 46 44.46 38.00
REMARK 500 ASN A 47 -55.81 177.74
REMARK 500 ILE A 92 2.19 91.78
REMARK 500 GLU A 93 47.69 -91.54
REMARK 500 LYS A 113 65.36 -100.47
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 ARG A 4 0.31 SIDE CHAIN
REMARK 500 ARG A 15 0.18 SIDE CHAIN
REMARK 500 ARG A 20 0.22 SIDE CHAIN
REMARK 500 ARG A 22 0.24 SIDE CHAIN
REMARK 500 ARG A 39 0.29 SIDE CHAIN
REMARK 500 ARG A 43 0.29 SIDE CHAIN
REMARK 500 ARG A 58 0.31 SIDE CHAIN
REMARK 500 ARG A 76 0.24 SIDE CHAIN
REMARK 500 ARG A 91 0.18 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1TAM A 2 132 UNP P04585 POL_HV1H2 1 131
SEQADV 1TAM SER A 126 UNP P04585 ASN 125 CONFLICT
SEQRES 1 A 132 MET GLY ALA ARG ALA SER VAL LEU SER GLY GLY GLU LEU
SEQRES 2 A 132 ASP ARG TRP GLU LYS ILE ARG LEU ARG PRO GLY GLY LYS
SEQRES 3 A 132 LYS LYS TYR LYS LEU LYS HIS ILE VAL TRP ALA SER ARG
SEQRES 4 A 132 GLU LEU GLU ARG PHE ALA VAL ASN PRO GLY LEU LEU GLU
SEQRES 5 A 132 THR SER GLU GLY CYS ARG GLN ILE LEU GLY GLN LEU GLN
SEQRES 6 A 132 PRO SER LEU GLN THR GLY SER GLU GLU LEU ARG SER LEU
SEQRES 7 A 132 TYR ASN THR VAL ALA THR LEU TYR CYS VAL HIS GLN ARG
SEQRES 8 A 132 ILE GLU ILE LYS ASP THR LYS GLU ALA LEU ASP LYS ILE
SEQRES 9 A 132 GLU GLU GLU GLN ASN LYS SER LYS LYS LYS ALA GLN GLN
SEQRES 10 A 132 ALA ALA ALA ASP THR GLY HIS SER SER GLN VAL SER GLN
SEQRES 11 A 132 ASN TYR
HELIX 1 1 GLY A 11 LYS A 18 1 8
HELIX 2 2 LEU A 31 ALA A 45 1 15
HELIX 3 3 SER A 54 GLN A 69 1 16
HELIX 4 4 SER A 72 GLN A 90 1 19
HELIX 5 5 THR A 97 LYS A 112 1 16
SHEET 1 A 2 ARG A 20 LEU A 21 0
SHEET 2 A 2 LYS A 27 LYS A 28 -1 N LYS A 27 O LEU A 21
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 - 2 20 Bytes