Header list of 1ujs.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL PROTEIN 11-AUG-03 1UJS
TITLE SOLUTION STRUCTURE OF THE VILLIN HEADPIECE DOMAIN OF HUMAN ACTIN-
TITLE 2 BINDING LIM PROTEIN HOMOLOGUE (KIAA0843 PROTEIN)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACTIN-BINDING LIM PROTEIN HOMOLOGUE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: VHP DOMAIN;
COMPND 5 SYNONYM: KIAA0843 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 HK05155;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P020930-61;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS VHP DOMAIN, ACTIN BINDING, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.TOCHIO,S.KOSHIBA,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1UJS 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1UJS 1 VERSN
REVDAT 1 11-FEB-04 1UJS 0
JRNL AUTH N.TOCHIO,S.KOSHIBA,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE VILLIN HEADPIECE DOMAIN OF HUMAN
JRNL TITL 2 ACTIN-BINDING LIM PROTEIN HOMOLOGUE (KIAA0843 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 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UJS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1000005904.
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 : 1.2MM VHP DOMAIN U-15N, 13C;
REMARK 210 20MM PHOSPHATE BUFFER NA; 100MM
REMARK 210 NACL; 0.02% NAN3; 10% D2O
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 : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 200204025, NMRVIEW
REMARK 210 5.0.4, KUJIRA 0.816, 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 : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY, 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 ALA A 9 -176.54 -171.03
REMARK 500 1 ASN A 11 26.75 41.32
REMARK 500 1 TRP A 12 178.93 -49.14
REMARK 500 1 PRO A 36 -173.94 -69.80
REMARK 500 1 PHE A 53 -29.72 -37.70
REMARK 500 1 ILE A 61 -39.64 -38.85
REMARK 500 1 SER A 86 117.05 -39.83
REMARK 500 2 ALA A 9 147.57 -171.77
REMARK 500 2 VAL A 10 135.02 -36.21
REMARK 500 2 PRO A 36 -173.36 -69.78
REMARK 500 2 GLN A 50 -25.36 -39.86
REMARK 500 2 PHE A 53 -31.65 -37.51
REMARK 500 2 ILE A 61 -39.17 -39.18
REMARK 500 3 ALA A 9 147.74 -173.95
REMARK 500 3 VAL A 10 135.95 -33.73
REMARK 500 3 ASN A 11 31.31 -85.64
REMARK 500 3 TRP A 12 -175.81 -69.16
REMARK 500 3 PRO A 36 -174.64 -69.78
REMARK 500 3 PHE A 53 -31.60 -37.50
REMARK 500 3 ILE A 61 -38.91 -39.37
REMARK 500 4 VAL A 10 131.96 -34.95
REMARK 500 4 PRO A 36 -174.63 -69.73
REMARK 500 4 GLN A 50 -25.69 -39.20
REMARK 500 4 PHE A 53 -33.29 -36.28
REMARK 500 4 PRO A 85 2.56 -69.74
REMARK 500 5 SER A 6 110.23 -36.68
REMARK 500 5 ASN A 11 33.52 34.32
REMARK 500 5 MET A 14 -72.76 -59.88
REMARK 500 5 THR A 28 101.28 -39.95
REMARK 500 5 ARG A 30 37.48 -84.63
REMARK 500 5 ARG A 32 76.44 -59.83
REMARK 500 5 PRO A 36 -172.47 -69.77
REMARK 500 5 PHE A 53 -29.77 -37.75
REMARK 500 5 ILE A 61 -39.54 -38.87
REMARK 500 6 ASN A 8 113.65 -35.26
REMARK 500 6 VAL A 10 -179.40 -67.11
REMARK 500 6 PRO A 36 -175.59 -69.85
REMARK 500 6 GLN A 50 -25.81 -38.94
REMARK 500 6 PHE A 53 -33.15 -36.48
REMARK 500 6 ILE A 61 -39.33 -39.24
REMARK 500 6 SER A 83 -37.63 -132.28
REMARK 500 6 PRO A 85 -175.76 -69.77
REMARK 500 7 ALA A 9 146.39 -170.92
REMARK 500 7 VAL A 10 -25.24 -39.62
REMARK 500 7 MET A 14 -72.44 -72.53
REMARK 500 7 PRO A 36 -172.45 -69.76
REMARK 500 7 PHE A 53 -32.19 -37.73
REMARK 500 7 ILE A 61 -39.76 -38.76
REMARK 500 8 VAL A 10 141.52 -33.79
REMARK 500 8 ASN A 11 39.96 -95.27
REMARK 500
REMARK 500 THIS ENTRY HAS 162 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002000824.1 RELATED DB: TARGETDB
DBREF 1UJS A 8 82 UNP O94929 ABLM3_HUMAN 609 683
SEQADV 1UJS GLY A 1 UNP O94929 CLONING ARTIFACT
SEQADV 1UJS SER A 2 UNP O94929 CLONING ARTIFACT
SEQADV 1UJS SER A 3 UNP O94929 CLONING ARTIFACT
SEQADV 1UJS GLY A 4 UNP O94929 CLONING ARTIFACT
SEQADV 1UJS SER A 5 UNP O94929 CLONING ARTIFACT
SEQADV 1UJS SER A 6 UNP O94929 CLONING ARTIFACT
SEQADV 1UJS GLY A 7 UNP O94929 CLONING ARTIFACT
SEQADV 1UJS SER A 83 UNP O94929 CLONING ARTIFACT
SEQADV 1UJS GLY A 84 UNP O94929 CLONING ARTIFACT
SEQADV 1UJS PRO A 85 UNP O94929 CLONING ARTIFACT
SEQADV 1UJS SER A 86 UNP O94929 CLONING ARTIFACT
SEQADV 1UJS SER A 87 UNP O94929 CLONING ARTIFACT
SEQADV 1UJS GLY A 88 UNP O94929 CLONING ARTIFACT
SEQRES 1 A 88 GLY SER SER GLY SER SER GLY ASN ALA VAL ASN TRP GLY
SEQRES 2 A 88 MET ARG GLU TYR LYS ILE TYR PRO TYR GLU LEU LEU LEU
SEQRES 3 A 88 VAL THR THR ARG GLY ARG ASN ARG LEU PRO LYS ASP VAL
SEQRES 4 A 88 ASP ARG THR ARG LEU GLU ARG HIS LEU SER GLN GLU GLU
SEQRES 5 A 88 PHE TYR GLN VAL PHE GLY MET THR ILE SER GLU PHE ASP
SEQRES 6 A 88 ARG LEU ALA LEU TRP LYS ARG ASN GLU LEU LYS LYS GLN
SEQRES 7 A 88 ALA ARG LEU PHE SER GLY PRO SER SER GLY
HELIX 1 1 ARG A 43 LEU A 48 5 6
HELIX 2 2 GLU A 51 GLY A 58 1 8
HELIX 3 3 THR A 60 ASP A 65 1 6
HELIX 4 4 ALA A 68 ALA A 79 1 12
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