Header list of 2cop.pdb file
Complete list - r 9 2 Bytes
HEADER LIPID BINDING PROTEIN 18-MAY-05 2COP
TITLE SOLUTION STRUCTURE OF RSGI RUH-040, AN ACBP DOMAIN FROM HUMAN CDNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYL-COENZYME A BINDING DOMAIN CONTAINING 6;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACYL COA BINDING DOMAIN, ACBP;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GENEID:84320;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040830-11;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS (E.COLI)
KEYWDS ACYL COA BINDING PROTEIN, COA BINDING PROTEIN, LIPID BINDING PROTEIN,
KEYWDS 2 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL
KEYWDS 3 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.Z.M.RUHUL MOMEN,H.HIROTA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2COP 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2COP 1 VERSN
REVDAT 1 18-NOV-05 2COP 0
JRNL AUTH A.Z.M.RUHUL MOMEN,H.HIROTA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF RSGI RUH-040, AN ACBP DOMAIN FROM
JRNL TITL 2 HUMAN CDNA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C
REMARK 3 AUTHORS : VARIAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2COP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024457.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.26MM ACBP DOMAIN U-15N, 13C;
REMARK 210 20MM D-TRIS-HCL (PH7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 10%
REMARK 210 D20
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9295, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
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 3 160.72 -44.49
REMARK 500 1 VAL A 43 -65.19 -96.23
REMARK 500 1 ASN A 47 35.26 35.19
REMARK 500 1 ASP A 55 78.70 -68.82
REMARK 500 1 ILE A 81 -65.34 -90.56
REMARK 500 1 GLU A 97 167.54 -47.51
REMARK 500 1 SER A 104 100.84 -51.43
REMARK 500 1 PRO A 106 -175.04 -69.75
REMARK 500 2 ARG A 28 -32.24 -39.53
REMARK 500 2 VAL A 43 -63.90 -91.66
REMARK 500 2 ASN A 45 106.55 -46.18
REMARK 500 2 CYS A 46 129.03 -38.12
REMARK 500 2 SER A 52 152.23 -48.23
REMARK 500 2 GLU A 97 152.82 -46.33
REMARK 500 2 GLU A 102 88.27 -52.17
REMARK 500 3 SER A 2 94.68 -68.72
REMARK 500 3 VAL A 43 -65.53 -95.18
REMARK 500 3 GLU A 63 -71.76 -62.72
REMARK 500 3 ILE A 81 -65.39 -91.63
REMARK 500 3 LYS A 99 170.37 -51.99
REMARK 500 3 LYS A 101 42.16 -109.08
REMARK 500 3 ALA A 103 140.58 -172.76
REMARK 500 3 PRO A 106 2.61 -69.75
REMARK 500 4 VAL A 43 -64.65 -94.76
REMARK 500 4 ASP A 70 51.12 -109.38
REMARK 500 4 LYS A 101 113.15 -172.35
REMARK 500 4 ALA A 103 42.07 -83.83
REMARK 500 4 SER A 107 52.25 -93.63
REMARK 500 4 SER A 108 -60.96 -125.17
REMARK 500 5 GLU A 10 -39.80 -36.31
REMARK 500 5 VAL A 43 -66.52 -99.00
REMARK 500 5 ASN A 45 108.34 -54.03
REMARK 500 5 CYS A 46 106.63 -36.33
REMARK 500 5 PRO A 51 -177.49 -69.71
REMARK 500 5 ASP A 55 79.73 -69.11
REMARK 500 5 GLU A 63 -71.61 -61.45
REMARK 500 5 LEU A 68 50.94 -90.34
REMARK 500 5 GLU A 97 171.77 -49.46
REMARK 500 6 GLU A 10 -36.48 -38.98
REMARK 500 6 ARG A 28 -30.88 -37.50
REMARK 500 6 VAL A 43 -69.86 -91.24
REMARK 500 6 GLU A 63 -70.27 -61.18
REMARK 500 6 ASP A 70 51.79 -103.82
REMARK 500 6 GLU A 97 167.88 -45.14
REMARK 500 6 GLU A 102 153.21 -44.06
REMARK 500 6 ALA A 103 42.92 -82.87
REMARK 500 6 SER A 104 83.60 -59.68
REMARK 500 7 LEU A 8 -61.49 -90.19
REMARK 500 7 VAL A 43 -64.97 -97.35
REMARK 500 7 CYS A 46 105.30 -35.94
REMARK 500
REMARK 500 THIS ENTRY HAS 147 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002006003.1 RELATED DB: TARGETDB
DBREF 2COP A 8 103 UNP Q9BR61 Q9BR61_HUMAN 42 137
SEQADV 2COP GLY A 1 UNP Q9BR61 CLONING ARTIFACT
SEQADV 2COP SER A 2 UNP Q9BR61 CLONING ARTIFACT
SEQADV 2COP SER A 3 UNP Q9BR61 CLONING ARTIFACT
SEQADV 2COP GLY A 4 UNP Q9BR61 CLONING ARTIFACT
SEQADV 2COP SER A 5 UNP Q9BR61 CLONING ARTIFACT
SEQADV 2COP SER A 6 UNP Q9BR61 CLONING ARTIFACT
SEQADV 2COP GLY A 7 UNP Q9BR61 CLONING ARTIFACT
SEQADV 2COP SER A 104 UNP Q9BR61 CLONING ARTIFACT
SEQADV 2COP GLY A 105 UNP Q9BR61 CLONING ARTIFACT
SEQADV 2COP PRO A 106 UNP Q9BR61 CLONING ARTIFACT
SEQADV 2COP SER A 107 UNP Q9BR61 CLONING ARTIFACT
SEQADV 2COP SER A 108 UNP Q9BR61 CLONING ARTIFACT
SEQADV 2COP GLY A 109 UNP Q9BR61 CLONING ARTIFACT
SEQRES 1 A 109 GLY SER SER GLY SER SER GLY LEU ALA GLU LEU PHE GLU
SEQRES 2 A 109 LYS ALA ALA ALA HIS LEU GLN GLY LEU ILE GLN VAL ALA
SEQRES 3 A 109 SER ARG GLU GLN LEU LEU TYR LEU TYR ALA ARG TYR LYS
SEQRES 4 A 109 GLN VAL LYS VAL GLY ASN CYS ASN THR PRO LYS PRO SER
SEQRES 5 A 109 PHE PHE ASP PHE GLU GLY LYS GLN LYS TRP GLU ALA TRP
SEQRES 6 A 109 LYS ALA LEU GLY ASP SER SER PRO SER GLN ALA MET GLN
SEQRES 7 A 109 GLU TYR ILE ALA VAL VAL LYS LYS LEU ASP PRO GLY TRP
SEQRES 8 A 109 ASN PRO GLN ILE PRO GLU LYS LYS GLY LYS GLU ALA SER
SEQRES 9 A 109 GLY PRO SER SER GLY
HELIX 1 1 LEU A 8 GLN A 20 1 13
HELIX 2 2 SER A 27 VAL A 43 1 17
HELIX 3 3 ASP A 55 ALA A 67 1 13
HELIX 4 4 SER A 72 ASP A 88 1 17
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