Header list of 2h3i.pdb file
Complete list - r 9 2 Bytes
HEADER VIRAL PROTEIN 22-MAY-06 2H3I
TITLE SOLUTION STRUCTURE OF THE HIV-1 MYRISTOYLATED MATRIX PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GAG POLYPROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 2-132;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HIV-1 MYRISTOYLATED MATRIX PROTEIN, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.S.SAAD,J.MILLER,J.TAI,A.KIM,R.H.GHANAM,M.F.SUMMERS
REVDAT 3 09-MAR-22 2H3I 1 REMARK LINK
REVDAT 2 24-FEB-09 2H3I 1 VERSN
REVDAT 1 25-JUL-06 2H3I 0
JRNL AUTH J.S.SAAD,J.MILLER,J.TAI,A.KIM,R.H.GHANAM,M.F.SUMMERS
JRNL TITL STRUCTURAL BASIS FOR TARGETING HIV-1 GAG PROTEINS TO THE
JRNL TITL 2 PLASMA MEMBRANE FOR VIRUS ASSEMBLY.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 103 11364 2006
JRNL REFN ISSN 0027-8424
JRNL PMID 16840558
JRNL DOI 10.1073/PNAS.0602818103
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA
REMARK 3 AUTHORS : P.GUNTERT ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2H3I COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAY-06.
REMARK 100 THE DEPOSITION ID IS D_1000037883.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 50MM PHOSPHATE BUFFER, 5MM DTT,
REMARK 210 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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 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 1 SER A 6 129.95 66.74
REMARK 500 1 VAL A 7 -78.44 -96.70
REMARK 500 1 LEU A 8 114.34 -14.55
REMARK 500 1 ASP A 96 178.68 178.57
REMARK 500 1 VAL A 128 136.40 -170.99
REMARK 500 2 ALA A 5 -173.04 -60.44
REMARK 500 2 SER A 6 82.29 63.37
REMARK 500 2 GLU A 52 44.23 -100.26
REMARK 500 2 THR A 53 119.75 -178.17
REMARK 500 2 PRO A 66 2.08 -69.73
REMARK 500 2 THR A 70 46.22 -142.58
REMARK 500 2 ASP A 96 -179.01 175.73
REMARK 500 2 LYS A 98 -66.76 -93.43
REMARK 500 2 LYS A 114 27.24 -148.23
REMARK 500 2 ALA A 119 27.71 -158.54
REMARK 500 3 SER A 6 79.61 63.39
REMARK 500 3 LYS A 114 -63.58 -94.82
REMARK 500 3 ASP A 121 57.72 -106.89
REMARK 500 3 ASN A 125 29.22 -144.49
REMARK 500 3 GLN A 127 73.41 -165.13
REMARK 500 4 ALA A 3 38.98 -165.92
REMARK 500 4 ARG A 4 67.20 62.70
REMARK 500 4 VAL A 7 -77.17 -94.21
REMARK 500 4 LEU A 8 117.42 -16.25
REMARK 500 4 GLN A 117 -63.27 -134.31
REMARK 500 4 ALA A 120 -54.53 -149.97
REMARK 500 4 GLN A 127 -59.28 -146.43
REMARK 500 4 VAL A 128 89.43 -69.31
REMARK 500 4 GLN A 130 27.85 -163.31
REMARK 500 5 SER A 6 116.12 179.40
REMARK 500 5 VAL A 7 -78.09 -96.76
REMARK 500 5 LEU A 8 113.50 -14.51
REMARK 500 5 THR A 70 40.98 -89.82
REMARK 500 5 ASP A 96 178.21 178.91
REMARK 500 5 LYS A 98 -60.71 -90.35
REMARK 500 5 ASN A 125 -71.91 -58.12
REMARK 500 5 GLN A 130 -172.64 -68.75
REMARK 500 6 ARG A 4 -176.26 -58.37
REMARK 500 6 ALA A 5 154.82 64.88
REMARK 500 6 LYS A 18 -70.47 -63.74
REMARK 500 6 ALA A 45 18.89 55.56
REMARK 500 6 ASP A 96 -179.17 176.83
REMARK 500 6 SER A 126 86.33 56.29
REMARK 500 6 GLN A 127 130.57 -173.98
REMARK 500 6 ASN A 131 -70.01 -115.23
REMARK 500 7 ALA A 3 -41.28 -153.11
REMARK 500 7 ALA A 5 -168.33 -104.07
REMARK 500 7 SER A 6 70.01 61.20
REMARK 500 7 ALA A 45 2.15 90.13
REMARK 500 7 THR A 70 40.00 -145.41
REMARK 500
REMARK 500 THIS ENTRY HAS 183 RAMACHANDRAN OUTLIERS.
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 MYR A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2H3F RELATED DB: PDB
REMARK 900 RELATED ID: 2H3Q RELATED DB: PDB
REMARK 900 RELATED ID: 2H3V RELATED DB: PDB
REMARK 900 RELATED ID: 2H3Z RELATED DB: PDB
DBREF 2H3I A 2 132 UNP P12497 POL_HV1N5 1 131
SEQRES 1 A 131 GLY ALA ARG ALA SER VAL LEU SER GLY GLY GLU LEU ASP
SEQRES 2 A 131 LYS TRP GLU LYS ILE ARG LEU ARG PRO GLY GLY LYS LYS
SEQRES 3 A 131 GLN TYR LYS LEU LYS HIS ILE VAL TRP ALA SER ARG GLU
SEQRES 4 A 131 LEU GLU ARG PHE ALA VAL ASN PRO GLY LEU LEU GLU THR
SEQRES 5 A 131 SER GLU GLY CYS ARG GLN ILE LEU GLY GLN LEU GLN PRO
SEQRES 6 A 131 SER LEU GLN THR GLY SER GLU GLU LEU ARG SER LEU TYR
SEQRES 7 A 131 ASN THR ILE ALA VAL LEU TYR CYS VAL HIS GLN ARG ILE
SEQRES 8 A 131 ASP VAL LYS ASP THR LYS GLU ALA LEU ASP LYS ILE GLU
SEQRES 9 A 131 GLU GLU GLN ASN LYS SER LYS LYS LYS ALA GLN GLN ALA
SEQRES 10 A 131 ALA ALA ASP THR GLY ASN ASN SER GLN VAL SER GLN ASN
SEQRES 11 A 131 TYR
HET MYR A 1 42
HETNAM MYR MYRISTIC ACID
FORMUL 2 MYR C14 H28 O2
HELIX 1 1 SER A 9 GLU A 17 1 9
HELIX 2 2 LYS A 30 GLU A 42 1 13
HELIX 3 3 THR A 53 GLN A 65 1 13
HELIX 4 4 PRO A 66 LEU A 68 5 3
HELIX 5 5 SER A 72 GLN A 90 1 19
HELIX 6 6 ASP A 96 GLN A 116 1 21
HELIX 7 7 GLN A 117 GLY A 123 1 7
LINK C1 MYR A 1 N GLY A 2 1555 1555 1.33
SITE 1 AC1 9 GLY A 2 SER A 6 VAL A 7 LEU A 8
SITE 2 AC1 9 ILE A 34 SER A 38 PRO A 48 LEU A 51
SITE 3 AC1 9 LEU A 85
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