HEADER SIGNALING PROTEIN 20-MAY-05 2CS0
TITLE SOLUTION STRUCTURE OF THE SH2 DOMAIN OF HUMAN HSH2D PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMATOPOIETIC SH2 DOMAIN CONTAINING;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH2 DOMAIN;
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: HSH2D;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P041108-15;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS ALX, FLJ14886, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.KUROSAKI,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CS0 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CS0 1 VERSN
REVDAT 1 20-NOV-05 2CS0 0
JRNL AUTH C.KUROSAKI,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SH2 DOMAIN OF HUMAN HSH2D PROTEIN
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, CYANA 2.0.17
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CS0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024557.
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
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.46MM 13C, 15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS-HCL; 100MM NACL; 1MM
REMARK 210 D-DTT; 0.02% NAN3; 90% H2O, 10%
REMARK 210 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; 900 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 0.9298, 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 GLN A 12 42.32 -109.43
REMARK 500 1 HIS A 20 39.67 -90.04
REMARK 500 1 ARG A 25 -39.56 -34.61
REMARK 500 1 PRO A 77 86.68 -69.75
REMARK 500 1 PRO A 97 -166.51 -69.76
REMARK 500 1 THR A 106 -55.28 -130.29
REMARK 500 1 GLN A 111 162.97 -49.12
REMARK 500 2 VAL A 44 135.27 -37.30
REMARK 500 2 LEU A 69 -177.44 -51.47
REMARK 500 2 PRO A 77 86.06 -69.78
REMARK 500 2 PRO A 97 -167.79 -69.69
REMARK 500 2 THR A 106 -57.72 -125.63
REMARK 500 2 LYS A 112 171.83 -52.87
REMARK 500 3 HIS A 20 38.15 -87.78
REMARK 500 3 VAL A 44 133.25 -34.11
REMARK 500 3 HIS A 46 -51.82 -131.58
REMARK 500 3 LEU A 69 178.78 -49.88
REMARK 500 3 PRO A 97 -169.77 -69.74
REMARK 500 3 THR A 106 -62.06 -134.96
REMARK 500 3 LYS A 112 41.81 -103.57
REMARK 500 4 SER A 2 48.85 39.80
REMARK 500 4 PRO A 16 -177.66 -69.79
REMARK 500 4 HIS A 46 -52.55 -125.78
REMARK 500 4 LEU A 69 173.56 -55.08
REMARK 500 4 PRO A 77 92.89 -69.78
REMARK 500 4 PRO A 97 -171.50 -69.79
REMARK 500 4 THR A 106 -59.47 -129.82
REMARK 500 4 GLN A 111 157.89 -42.22
REMARK 500 4 LYS A 112 132.52 -37.04
REMARK 500 4 SER A 114 -74.31 -72.82
REMARK 500 5 SER A 2 114.09 -167.84
REMARK 500 5 LEU A 10 41.06 -99.52
REMARK 500 5 ASP A 13 75.67 -105.44
REMARK 500 5 PRO A 16 -174.99 -69.70
REMARK 500 5 ALA A 22 37.76 34.79
REMARK 500 5 ILE A 23 170.28 -50.51
REMARK 500 5 VAL A 44 130.68 -33.95
REMARK 500 5 VAL A 49 33.30 -84.79
REMARK 500 5 PRO A 77 84.94 -69.66
REMARK 500 5 PRO A 97 -166.31 -69.82
REMARK 500 5 THR A 106 -55.68 -129.69
REMARK 500 5 GLN A 111 148.44 -39.17
REMARK 500 5 SER A 117 145.62 -34.60
REMARK 500 6 SER A 2 124.02 -174.29
REMARK 500 6 PRO A 16 -176.86 -69.82
REMARK 500 6 HIS A 20 34.96 -85.93
REMARK 500 6 LEU A 69 176.71 -55.32
REMARK 500 6 PRO A 77 80.37 -69.74
REMARK 500 6 PRO A 97 -174.93 -69.76
REMARK 500 6 THR A 106 -57.33 -130.27
REMARK 500
REMARK 500 THIS ENTRY HAS 196 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002014623.1 RELATED DB: TARGETDB
DBREF 2CS0 A 8 113 UNP Q96JZ2 Q96JZ2_HUMAN 24 129
SEQADV 2CS0 GLY A 1 UNP Q96JZ2 CLONING ARTIFACT
SEQADV 2CS0 SER A 2 UNP Q96JZ2 CLONING ARTIFACT
SEQADV 2CS0 SER A 3 UNP Q96JZ2 CLONING ARTIFACT
SEQADV 2CS0 GLY A 4 UNP Q96JZ2 CLONING ARTIFACT
SEQADV 2CS0 SER A 5 UNP Q96JZ2 CLONING ARTIFACT
SEQADV 2CS0 SER A 6 UNP Q96JZ2 CLONING ARTIFACT
SEQADV 2CS0 GLY A 7 UNP Q96JZ2 CLONING ARTIFACT
SEQADV 2CS0 SER A 114 UNP Q96JZ2 CLONING ARTIFACT
SEQADV 2CS0 GLY A 115 UNP Q96JZ2 CLONING ARTIFACT
SEQADV 2CS0 PRO A 116 UNP Q96JZ2 CLONING ARTIFACT
SEQADV 2CS0 SER A 117 UNP Q96JZ2 CLONING ARTIFACT
SEQADV 2CS0 SER A 118 UNP Q96JZ2 CLONING ARTIFACT
SEQADV 2CS0 GLY A 119 UNP Q96JZ2 CLONING ARTIFACT
SEQRES 1 A 119 GLY SER SER GLY SER SER GLY GLY GLN LEU ALA GLN ASP
SEQRES 2 A 119 GLY VAL PRO GLU TRP PHE HIS GLY ALA ILE SER ARG GLU
SEQRES 3 A 119 ASP ALA GLU ASN LEU LEU GLU SER GLN PRO LEU GLY SER
SEQRES 4 A 119 PHE LEU ILE ARG VAL SER HIS SER HIS VAL GLY TYR THR
SEQRES 5 A 119 LEU SER TYR LYS ALA GLN SER SER CYS CYS HIS PHE MET
SEQRES 6 A 119 VAL LYS LEU LEU ASP ASP GLY THR PHE MET ILE PRO GLY
SEQRES 7 A 119 GLU LYS VAL ALA HIS THR SER LEU ASP ALA LEU VAL THR
SEQRES 8 A 119 PHE HIS GLN GLN LYS PRO ILE GLU PRO ARG ARG GLU LEU
SEQRES 9 A 119 LEU THR GLN PRO CYS ARG GLN LYS ASP SER GLY PRO SER
SEQRES 10 A 119 SER GLY
HELIX 1 1 SER A 24 SER A 34 1 11
HELIX 2 2 SER A 85 GLN A 94 1 10
SHEET 1 A 4 PHE A 40 VAL A 44 0
SHEET 2 A 4 TYR A 51 TYR A 55 -1 O SER A 54 N LEU A 41
SHEET 3 A 4 CYS A 62 LEU A 68 -1 O VAL A 66 N TYR A 51
SHEET 4 A 4 PHE A 74 MET A 75 -1 O MET A 75 N LYS A 67
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
(ATOM LINES ARE NOT SHOWN.)
END