Header list of 2d9x.pdb file
Complete list - r 9 2 Bytes
HEADER LIPID TRANSPORT 13-DEC-05 2D9X
TITLE SOLUTION STRUCTURE OF THE PH DOMAIN OF OXYSTEROL BINDING PROTEIN-
TITLE 2 RELATED PROTEIN 11 FROM HUMAN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OXYSTEROL BINDING PROTEIN-RELATED PROTEIN 11;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PH DOMAIN;
COMPND 5 SYNONYM: OSBP-RELATED PROTEIN 11, ORP-11;
COMPND 6 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: OSBPL11;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050404-14;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS PH DOMAIN, OSBP-RELATED PROTEIN 11, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, LIPID
KEYWDS 4 TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.LI,M.SATO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2D9X 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2D9X 1 VERSN
REVDAT 1 13-JUN-06 2D9X 0
JRNL AUTH H.LI,M.SATO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE PH DOMAIN OF OXYSTEROL BINDING
JRNL TITL 2 PROTEIN-RELATED PROTEIN 11 FROM HUMAN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2D9X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025168.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.16MM PH DOMAIN U-15N, 13C;
REMARK 210 20MM D-TRIS-HCL(PH 7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.932, 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 LEAST RESTRAINT 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 ASN A 19 -176.27 -172.62
REMARK 500 1 SER A 46 50.87 -111.07
REMARK 500 1 ALA A 58 102.85 -45.79
REMARK 500 1 HIS A 106 -64.36 -92.38
REMARK 500 1 LYS A 112 127.51 -36.04
REMARK 500 1 PRO A 117 2.80 -69.79
REMARK 500 2 SER A 6 103.47 -43.64
REMARK 500 2 VAL A 42 -37.15 -36.08
REMARK 500 2 SER A 46 52.25 -90.18
REMARK 500 2 ASN A 48 40.75 -86.62
REMARK 500 2 ALA A 58 101.74 -42.14
REMARK 500 2 SER A 65 -179.55 -53.20
REMARK 500 2 ASP A 66 -47.51 -131.01
REMARK 500 2 GLU A 67 -74.15 -39.61
REMARK 500 2 ASP A 68 -175.65 -62.95
REMARK 500 2 SER A 69 -60.40 -96.05
REMARK 500 2 PHE A 72 148.80 -174.95
REMARK 500 2 VAL A 96 -36.85 -38.70
REMARK 500 2 HIS A 105 -28.02 -38.23
REMARK 500 2 ALA A 109 -39.23 -37.19
REMARK 500 2 SER A 115 113.05 -162.02
REMARK 500 3 ASN A 9 141.44 -35.81
REMARK 500 3 VAL A 42 -31.16 -35.52
REMARK 500 3 SER A 46 47.44 -77.56
REMARK 500 3 ALA A 58 94.28 -42.78
REMARK 500 3 PHE A 72 149.37 -170.77
REMARK 500 4 SER A 2 43.21 35.98
REMARK 500 4 ASN A 43 -177.10 -170.16
REMARK 500 4 ALA A 58 105.01 -43.67
REMARK 500 4 GLU A 67 -71.54 -82.66
REMARK 500 4 HIS A 106 -62.04 -92.06
REMARK 500 4 ALA A 109 -37.33 -39.61
REMARK 500 5 SER A 2 48.47 39.99
REMARK 500 5 SER A 5 132.62 -38.58
REMARK 500 5 GLN A 49 177.17 -55.09
REMARK 500 5 ALA A 58 98.50 -56.88
REMARK 500 5 ASP A 66 -36.79 -131.68
REMARK 500 5 HIS A 105 -26.02 -39.90
REMARK 500 5 ASN A 114 120.60 -39.55
REMARK 500 6 SER A 5 132.52 -170.16
REMARK 500 6 LEU A 20 -74.57 -68.38
REMARK 500 6 SER A 46 41.97 -94.95
REMARK 500 6 ASN A 48 33.20 -84.20
REMARK 500 6 ALA A 58 107.91 -45.81
REMARK 500 6 ASP A 66 -35.23 -132.10
REMARK 500 6 PHE A 72 149.83 -174.98
REMARK 500 6 ILE A 110 107.33 -37.58
REMARK 500 6 SER A 118 45.81 34.58
REMARK 500 7 SER A 6 110.91 -167.80
REMARK 500 7 GLU A 8 42.52 -89.13
REMARK 500
REMARK 500 THIS ENTRY HAS 169 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK003000224.1 RELATED DB: TARGETDB
DBREF 2D9X A 8 114 UNP Q9BXB4 OSR11_HUMAN 59 165
SEQADV 2D9X GLY A 1 UNP Q9BXB4 CLONING ARTIFACT
SEQADV 2D9X SER A 2 UNP Q9BXB4 CLONING ARTIFACT
SEQADV 2D9X SER A 3 UNP Q9BXB4 CLONING ARTIFACT
SEQADV 2D9X GLY A 4 UNP Q9BXB4 CLONING ARTIFACT
SEQADV 2D9X SER A 5 UNP Q9BXB4 CLONING ARTIFACT
SEQADV 2D9X SER A 6 UNP Q9BXB4 CLONING ARTIFACT
SEQADV 2D9X GLY A 7 UNP Q9BXB4 CLONING ARTIFACT
SEQADV 2D9X SER A 115 UNP Q9BXB4 CLONING ARTIFACT
SEQADV 2D9X GLY A 116 UNP Q9BXB4 CLONING ARTIFACT
SEQADV 2D9X PRO A 117 UNP Q9BXB4 CLONING ARTIFACT
SEQADV 2D9X SER A 118 UNP Q9BXB4 CLONING ARTIFACT
SEQADV 2D9X SER A 119 UNP Q9BXB4 CLONING ARTIFACT
SEQADV 2D9X GLY A 120 UNP Q9BXB4 CLONING ARTIFACT
SEQRES 1 A 120 GLY SER SER GLY SER SER GLY GLU ASN VAL TYR GLY TYR
SEQRES 2 A 120 LEU MET LYS TYR THR ASN LEU VAL THR GLY TRP GLN TYR
SEQRES 3 A 120 ARG PHE PHE VAL LEU ASN ASN GLU ALA GLY LEU LEU GLU
SEQRES 4 A 120 TYR PHE VAL ASN GLU GLN SER ARG ASN GLN LYS PRO ARG
SEQRES 5 A 120 GLY THR LEU GLN LEU ALA GLY ALA VAL ILE SER PRO SER
SEQRES 6 A 120 ASP GLU ASP SER HIS THR PHE THR VAL ASN ALA ALA SER
SEQRES 7 A 120 GLY GLU GLN TYR LYS LEU ARG ALA THR ASP ALA LYS GLU
SEQRES 8 A 120 ARG GLN HIS TRP VAL SER ARG LEU GLN ILE CYS THR GLN
SEQRES 9 A 120 HIS HIS THR GLU ALA ILE GLY LYS ASN ASN SER GLY PRO
SEQRES 10 A 120 SER SER GLY
HELIX 1 1 ALA A 89 ALA A 109 1 21
SHEET 1 A 4 VAL A 10 LYS A 16 0
SHEET 2 A 4 GLN A 25 LEU A 31 -1 O ARG A 27 N LEU A 14
SHEET 3 A 4 LEU A 37 PHE A 41 -1 O PHE A 41 N PHE A 28
SHEET 4 A 4 GLY A 53 GLN A 56 -1 O LEU A 55 N LEU A 38
SHEET 1 B 3 ILE A 62 SER A 63 0
SHEET 2 B 3 PHE A 72 VAL A 74 -1 O THR A 73 N SER A 63
SHEET 3 B 3 TYR A 82 ARG A 85 -1 O TYR A 82 N VAL A 74
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