HEADER SIGNALING PROTEIN 20-APR-06 2DM1
TITLE SOLUTION STRUCTURE OF THE SECOND SH3 DOMAIN OF HUMAN
TITLE 2 PROTEIN VAV-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN VAV-2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 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: VAV2;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050620-03;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS RHO FAMILY GUANINE NUCLEOTIDE EXCHANGE FACTOR, STRUCTURAL
KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL
KEYWDS 3 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.ENDO,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 2 24-FEB-09 2DM1 1 VERSN
REVDAT 1 03-APR-07 2DM1 0
JRNL AUTH H.ENDO,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SECOND SH3 DOMAIN OF
JRNL TITL 2 HUMAN PROTEIN VAV-2
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.0.17
REMARK 3 AUTHORS : GUNTERT, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DM1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-APR-06.
REMARK 100 THE RCSB ID CODE IS RCSB025572.
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 : 1.07MM 13C,15N-LABELED
REMARK 210 PROTEIN; 20MM D-TRIS-
REMARK 210 HCL(PH7.0); 100MM NACL; 1MM D-
REMARK 210 DTT; 0.02% NAN3; 90% H2O; 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY, 3D_
REMARK 210 13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5, NMRPIPE
REMARK 210 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.955, 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
REMARK 210 WITH THE LOWEST ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 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 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 GLU A 28 106.27 -47.97
REMARK 500 1 GLU A 63 107.98 -58.60
REMARK 500 1 PRO A 70 84.98 -69.73
REMARK 500 2 ALA A 18 105.06 -55.97
REMARK 500 2 GLU A 28 103.79 -39.79
REMARK 500 2 ASN A 50 28.10 48.13
REMARK 500 2 SER A 68 -60.25 -101.39
REMARK 500 2 PRO A 70 94.45 -69.74
REMARK 500 3 GLU A 28 102.42 -49.83
REMARK 500 3 ASP A 41 153.44 -44.42
REMARK 500 3 GLN A 42 104.01 -51.88
REMARK 500 4 SER A 3 41.95 -105.77
REMARK 500 4 ALA A 12 107.24 -59.34
REMARK 500 4 GLU A 28 104.46 -38.70
REMARK 500 4 ASP A 41 149.73 -38.15
REMARK 500 4 GLN A 42 45.75 -85.24
REMARK 500 4 ILE A 66 154.34 -36.56
REMARK 500 4 PRO A 70 2.77 -69.73
REMARK 500 5 GLU A 28 103.77 -47.22
REMARK 500 5 ASP A 30 108.53 -51.55
REMARK 500 5 ASP A 41 46.26 -79.16
REMARK 500 5 GLN A 42 32.43 36.08
REMARK 500 6 ALA A 18 108.39 -54.94
REMARK 500 6 GLU A 23 -177.24 -54.60
REMARK 500 6 GLU A 28 105.63 -43.65
REMARK 500 6 ILE A 66 158.02 -48.56
REMARK 500 7 ALA A 18 98.13 -57.54
REMARK 500 7 GLU A 28 107.38 -42.12
REMARK 500 7 TRP A 44 157.02 -47.04
REMARK 500 7 SER A 72 41.29 36.31
REMARK 500 8 ALA A 12 103.12 -58.57
REMARK 500 8 ALA A 18 108.10 -50.20
REMARK 500 8 GLU A 48 130.47 -174.37
REMARK 500 8 GLU A 63 88.88 -68.10
REMARK 500 8 ILE A 66 152.24 -45.13
REMARK 500 9 SER A 2 102.36 -45.70
REMARK 500 9 SER A 3 42.43 -83.41
REMARK 500 9 ALA A 18 102.58 -54.78
REMARK 500 9 GLU A 28 106.28 -46.54
REMARK 500 9 ILE A 34 101.06 -59.24
REMARK 500 9 ILE A 66 -32.60 -34.84
REMARK 500 9 PRO A 70 -176.77 -69.73
REMARK 500 10 SER A 3 163.92 -49.91
REMARK 500 10 GLU A 28 103.57 -40.85
REMARK 500 10 ILE A 34 107.96 -54.98
REMARK 500 10 ASP A 41 173.34 -55.20
REMARK 500 10 GLU A 64 162.00 -44.31
REMARK 500 11 SER A 3 105.98 -54.78
REMARK 500 11 SER A 6 171.60 -49.13
REMARK 500 11 ALA A 18 97.62 -57.25
REMARK 500 11 GLU A 28 102.20 -46.38
REMARK 500 11 GLU A 48 140.51 -173.25
REMARK 500 11 TYR A 60 33.58 -93.98
REMARK 500 11 ILE A 66 156.78 -40.95
REMARK 500 12 ALA A 18 97.70 -37.68
REMARK 500 12 GLU A 28 111.73 -39.20
REMARK 500 12 GLU A 64 170.88 -46.18
REMARK 500 12 SER A 72 101.43 -58.26
REMARK 500 13 SER A 2 45.06 35.07
REMARK 500 13 GLU A 23 174.50 -55.71
REMARK 500 13 ILE A 34 102.92 -58.97
REMARK 500 13 GLU A 48 144.07 -172.17
REMARK 500 13 THR A 49 135.84 -172.26
REMARK 500 13 SER A 68 97.94 -63.60
REMARK 500 13 PRO A 70 -177.62 -69.75
REMARK 500 13 SER A 72 108.05 -42.46
REMARK 500 14 GLU A 28 104.00 -43.69
REMARK 500 14 ILE A 66 28.26 38.83
REMARK 500 14 SER A 72 163.41 -43.82
REMARK 500 15 SER A 2 139.92 -36.97
REMARK 500 15 GLU A 28 87.32 -53.99
REMARK 500 15 ILE A 34 101.87 -59.49
REMARK 500 15 GLN A 42 45.67 34.75
REMARK 500 15 GLU A 63 82.22 -60.96
REMARK 500 15 SER A 71 96.33 -51.30
REMARK 500 16 SER A 2 158.84 -40.87
REMARK 500 16 SER A 6 146.40 -173.95
REMARK 500 16 ALA A 12 102.88 -57.74
REMARK 500 16 GLU A 28 113.61 -39.77
REMARK 500 16 ILE A 34 98.86 -59.59
REMARK 500 16 GLN A 42 99.55 -66.02
REMARK 500 16 GLU A 48 143.47 -172.14
REMARK 500 16 ASN A 50 38.21 70.56
REMARK 500 16 PRO A 57 -176.13 -69.80
REMARK 500 17 GLN A 42 34.49 -86.03
REMARK 500 17 ILE A 66 26.85 47.72
REMARK 500 17 SER A 72 -62.37 -95.34
REMARK 500 18 ALA A 18 108.17 -34.55
REMARK 500 18 GLU A 23 -176.37 -55.64
REMARK 500 18 GLU A 28 108.32 -51.32
REMARK 500 18 ASP A 30 109.86 -55.93
REMARK 500 18 ILE A 34 100.50 -56.36
REMARK 500 18 ILE A 66 172.21 -59.56
REMARK 500 19 GLU A 28 105.03 -46.45
REMARK 500 20 GLU A 48 141.88 -170.46
REMARK 500 20 GLU A 63 98.99 -69.44
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2DM1 A 8 67 UNP P52735 VAV2_HUMAN 819 878
SEQADV 2DM1 GLY A 1 UNP P52735 CLONING ARTIFACT
SEQADV 2DM1 SER A 2 UNP P52735 CLONING ARTIFACT
SEQADV 2DM1 SER A 3 UNP P52735 CLONING ARTIFACT
SEQADV 2DM1 GLY A 4 UNP P52735 CLONING ARTIFACT
SEQADV 2DM1 SER A 5 UNP P52735 CLONING ARTIFACT
SEQADV 2DM1 SER A 6 UNP P52735 CLONING ARTIFACT
SEQADV 2DM1 GLY A 7 UNP P52735 CLONING ARTIFACT
SEQADV 2DM1 SER A 68 UNP P52735 CLONING ARTIFACT
SEQADV 2DM1 GLY A 69 UNP P52735 CLONING ARTIFACT
SEQADV 2DM1 PRO A 70 UNP P52735 CLONING ARTIFACT
SEQADV 2DM1 SER A 71 UNP P52735 CLONING ARTIFACT
SEQADV 2DM1 SER A 72 UNP P52735 CLONING ARTIFACT
SEQADV 2DM1 GLY A 73 UNP P52735 CLONING ARTIFACT
SEQRES 1 A 73 GLY SER SER GLY SER SER GLY GLY THR ALA VAL ALA ARG
SEQRES 2 A 73 TYR ASN PHE ALA ALA ARG ASP MET ARG GLU LEU SER LEU
SEQRES 3 A 73 ARG GLU GLY ASP VAL VAL ARG ILE TYR SER ARG ILE GLY
SEQRES 4 A 73 GLY ASP GLN GLY TRP TRP LYS GLY GLU THR ASN GLY ARG
SEQRES 5 A 73 ILE GLY TRP PHE PRO SER THR TYR VAL GLU GLU GLU GLY
SEQRES 6 A 73 ILE GLN SER GLY PRO SER SER GLY
SHEET 1 A 3 VAL A 31 ARG A 33 0
SHEET 2 A 3 THR A 9 ALA A 12 -1 N ALA A 10 O VAL A 32
SHEET 3 A 3 VAL A 61 GLU A 63 -1 O GLU A 62 N VAL A 11
SHEET 1 B 2 TRP A 45 THR A 49 0
SHEET 2 B 2 ARG A 52 PHE A 56 -1 O PHE A 56 N TRP A 45
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
