Header list of 1v88.pdb file
Complete list - r 2 2 Bytes
HEADER LIPID TRANSPORT 29-DEC-03 1V88
TITLE SOLUTION STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF OXYSTEROL-
TITLE 2 BINDING PROTEIN-RELATED PROTEIN 8 (KIAA1451 PROTEIN)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OXYSTEROL BINDING PROTEIN-RELATED PROTEIN 8;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PLECKSTRIN HOMOLOGY (PH) DOMAIN;
COMPND 5 SYNONYM: KIAA1451 PROTEIN;
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: KAZUSA CDNA BG00289;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030428-85;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS VESICLE TRANSPORT, OXYSTEROL-BINDING PROTEIN-RELATED PROTEIN 8,
KEYWDS 2 PLECKSTRIN HOMOLOGY DOMAIN, PHOSPHATIDYLINOSITOL BINDING, STRUCTURAL
KEYWDS 3 GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 4 LIPID TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.LI,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1V88 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1V88 1 VERSN
REVDAT 1 29-JUN-04 1V88 0
JRNL AUTH H.LI,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF
JRNL TITL 2 OXYSTEROL-BINDING PROTEIN-RELATED PROTEIN 8 (KIAA1451
JRNL TITL 3 PROTEIN)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 1.0.7
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1V88 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-JAN-04.
REMARK 100 THE DEPOSITION ID IS D_1000006329.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.21MM PLECKSTRIN HOMOLOGY
REMARK 210 DOMAIN U-13C, 15N; 20MM
REMARK 210 PHOSPHATE BUFFER NA; 100MM NACL;
REMARK 210 1MM D-DTT; 0.02% NAN3; 90% H2O,
REMARK 210 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 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.854, CYANA 1.0.7
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 : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, TARGET
REMARK 210 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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 H VAL A 29 O LEU A 36 1.51
REMARK 500 O LEU A 35 H VAL A 50 1.51
REMARK 500 O ALA A 118 H ALA A 122 1.52
REMARK 500 H TRP A 27 O TYR A 38 1.53
REMARK 500 O MET A 10 H LEU A 30 1.53
REMARK 500 H ARG A 60 O CYS A 68 1.53
REMARK 500 H VAL A 9 O LEU A 30 1.55
REMARK 500 O CYS A 114 H ALA A 118 1.59
REMARK 500 O ALA A 122 H SER A 125 1.60
REMARK 500
REMARK 500 REMARK: NULL
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 5 -57.32 -179.05
REMARK 500 1 ARG A 17 124.05 -37.39
REMARK 500 1 LYS A 21 -36.72 178.72
REMARK 500 1 LYS A 42 -87.81 -58.36
REMARK 500 1 TRP A 46 145.53 67.16
REMARK 500 1 ALA A 54 58.19 -176.04
REMARK 500 1 GLU A 59 155.32 84.11
REMARK 500 1 ARG A 60 67.21 -164.16
REMARK 500 1 SER A 62 174.27 53.36
REMARK 500 1 LYS A 63 -77.40 -44.71
REMARK 500 1 ASP A 65 72.38 -171.04
REMARK 500 1 GLU A 76 90.26 36.49
REMARK 500 1 ILE A 79 49.59 -84.27
REMARK 500 1 LYS A 83 -134.40 -127.19
REMARK 500 1 LYS A 86 40.48 -97.08
REMARK 500 1 THR A 94 -161.03 -116.35
REMARK 500 1 GLN A 95 159.99 -42.39
REMARK 500 1 PRO A 98 -162.68 -74.99
REMARK 500 1 SER A 99 -44.83 -141.47
REMARK 500 1 LEU A 102 110.11 -163.04
REMARK 500 1 SER A 128 77.28 46.08
REMARK 500 2 SER A 5 -63.84 -99.04
REMARK 500 2 SER A 6 -66.71 -129.10
REMARK 500 2 ARG A 17 135.31 -38.92
REMARK 500 2 LYS A 21 -54.65 -147.29
REMARK 500 2 LYS A 42 -94.93 -68.05
REMARK 500 2 TRP A 46 152.05 67.90
REMARK 500 2 VAL A 47 -56.35 -125.43
REMARK 500 2 ALA A 54 62.92 -178.53
REMARK 500 2 GLU A 59 153.86 91.82
REMARK 500 2 ARG A 60 74.16 -166.54
REMARK 500 2 SER A 62 -179.82 52.82
REMARK 500 2 LYS A 64 114.81 60.39
REMARK 500 2 ASP A 65 71.02 168.68
REMARK 500 2 PHE A 67 126.04 -177.69
REMARK 500 2 GLU A 76 60.38 65.21
REMARK 500 2 GLN A 77 -82.34 -117.20
REMARK 500 2 SER A 78 141.25 -170.15
REMARK 500 2 LYS A 83 -133.54 -126.59
REMARK 500 2 LYS A 86 35.94 -93.09
REMARK 500 2 GLN A 95 159.19 -40.77
REMARK 500 2 LEU A 97 178.14 52.27
REMARK 500 2 PRO A 98 -162.04 -74.96
REMARK 500 2 SER A 99 -46.78 -139.75
REMARK 500 2 GLU A 120 -37.52 -38.65
REMARK 500 3 SER A 2 81.54 66.00
REMARK 500 3 SER A 3 133.08 -172.03
REMARK 500 3 SER A 5 85.88 55.50
REMARK 500 3 SER A 6 -64.47 -128.94
REMARK 500 3 VAL A 9 -62.65 -91.42
REMARK 500
REMARK 500 THIS ENTRY HAS 476 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002101423.1 RELATED DB: TARGETDB
DBREF 1V88 A 8 124 UNP Q9BZF1 OSBL8_HUMAN 214 330
SEQADV 1V88 GLY A 1 UNP Q9BZF1 CLONING ARTIFACT
SEQADV 1V88 SER A 2 UNP Q9BZF1 CLONING ARTIFACT
SEQADV 1V88 SER A 3 UNP Q9BZF1 CLONING ARTIFACT
SEQADV 1V88 GLY A 4 UNP Q9BZF1 CLONING ARTIFACT
SEQADV 1V88 SER A 5 UNP Q9BZF1 CLONING ARTIFACT
SEQADV 1V88 SER A 6 UNP Q9BZF1 CLONING ARTIFACT
SEQADV 1V88 GLY A 7 UNP Q9BZF1 CLONING ARTIFACT
SEQADV 1V88 SER A 125 UNP Q9BZF1 CLONING ARTIFACT
SEQADV 1V88 GLY A 126 UNP Q9BZF1 CLONING ARTIFACT
SEQADV 1V88 PRO A 127 UNP Q9BZF1 CLONING ARTIFACT
SEQADV 1V88 SER A 128 UNP Q9BZF1 CLONING ARTIFACT
SEQADV 1V88 SER A 129 UNP Q9BZF1 CLONING ARTIFACT
SEQADV 1V88 GLY A 130 UNP Q9BZF1 CLONING ARTIFACT
SEQRES 1 A 130 GLY SER SER GLY SER SER GLY ILE VAL MET ALA ASP TRP
SEQRES 2 A 130 LEU LYS ILE ARG GLY THR LEU LYS SER TRP THR LYS LEU
SEQRES 3 A 130 TRP CYS VAL LEU LYS PRO GLY VAL LEU LEU ILE TYR LYS
SEQRES 4 A 130 THR GLN LYS ASN GLY GLN TRP VAL GLY THR VAL LEU LEU
SEQRES 5 A 130 ASN ALA CYS GLU ILE ILE GLU ARG PRO SER LYS LYS ASP
SEQRES 6 A 130 GLY PHE CYS PHE LYS LEU PHE HIS PRO LEU GLU GLN SER
SEQRES 7 A 130 ILE TRP ALA VAL LYS GLY PRO LYS GLY GLU ALA VAL GLY
SEQRES 8 A 130 SER ILE THR GLN PRO LEU PRO SER SER TYR LEU ILE ILE
SEQRES 9 A 130 ARG ALA THR SER GLU SER ASP GLY ARG CYS TRP MET ASP
SEQRES 10 A 130 ALA LEU GLU LEU ALA LEU LYS SER GLY PRO SER SER GLY
HELIX 1 1 GLU A 109 LEU A 123 1 15
SHEET 1 A 4 MET A 10 ILE A 16 0
SHEET 2 A 4 THR A 24 LYS A 31 -1 O LEU A 30 N MET A 10
SHEET 3 A 4 VAL A 34 TYR A 38 -1 O TYR A 38 N TRP A 27
SHEET 4 A 4 GLY A 48 LEU A 51 -1 O VAL A 50 N LEU A 35
SHEET 1 B 3 GLU A 56 ILE A 57 0
SHEET 2 B 3 CYS A 68 PHE A 72 -1 O PHE A 72 N GLU A 56
SHEET 3 B 3 ILE A 103 ARG A 105 -1 O ILE A 104 N PHE A 69
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 2 2 Bytes