HEADER SIGNALING PROTEIN 20-APR-06 2DLZ
TITLE SOLUTION STRUCTURE OF THE SH2 DOMAIN OF HUMAN PROTEIN VAV-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN VAV-2;
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: VAV2;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050620-24;
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 2DLZ 1 VERSN
REVDAT 1 03-APR-07 2DLZ 0
JRNL AUTH H.ENDO,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SH2 DOMAIN OF HUMAN
JRNL TITL 2 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 2DLZ 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 RCSB025570.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.16MM 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 : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1C, NMRPIPE 20031121,
REMARK 210 NMRVIEW 5.0.4, KUJIRA 0.955,
REMARK 210 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 ASN A 22 54.54 -94.00
REMARK 500 1 MET A 23 -178.67 -68.26
REMARK 500 1 HIS A 35 -177.13 -53.57
REMARK 500 1 SER A 37 35.08 -84.83
REMARK 500 1 PRO A 46 84.25 -69.81
REMARK 500 1 THR A 77 27.63 47.19
REMARK 500 1 GLU A 78 50.89 38.64
REMARK 500 1 ASP A 83 -35.90 -39.65
REMARK 500 1 LEU A 108 103.14 -37.79
REMARK 500 1 LYS A 109 -74.81 -94.76
REMARK 500 1 PRO A 111 -176.35 -69.90
REMARK 500 1 PRO A 115 94.53 -69.85
REMARK 500 2 ASN A 22 78.83 -67.18
REMARK 500 2 HIS A 35 -179.33 -59.28
REMARK 500 2 ARG A 51 -64.18 -94.81
REMARK 500 2 THR A 77 25.24 44.22
REMARK 500 2 SER A 84 -177.27 -175.21
REMARK 500 2 LEU A 108 96.64 -42.23
REMARK 500 2 LYS A 109 -73.47 -87.71
REMARK 500 2 PRO A 111 -165.21 -69.79
REMARK 500 3 HIS A 35 -176.72 -58.35
REMARK 500 3 ASP A 60 26.38 49.33
REMARK 500 3 THR A 77 25.60 44.47
REMARK 500 3 SER A 84 -176.89 -172.74
REMARK 500 3 LEU A 108 97.66 -46.36
REMARK 500 3 LYS A 109 -70.16 -85.74
REMARK 500 3 PRO A 111 -163.75 -69.75
REMARK 500 4 ARG A 9 96.18 -58.00
REMARK 500 4 HIS A 35 174.66 -52.34
REMARK 500 4 PRO A 46 85.17 -69.79
REMARK 500 4 ALA A 49 -73.10 -60.20
REMARK 500 4 THR A 77 25.34 44.38
REMARK 500 4 LEU A 108 106.53 -34.53
REMARK 500 4 LYS A 109 -75.03 -98.05
REMARK 500 4 PRO A 111 -175.95 -69.73
REMARK 500 4 SER A 113 -75.18 -96.85
REMARK 500 4 PRO A 115 86.55 -69.78
REMARK 500 5 ASN A 22 54.64 33.70
REMARK 500 5 HIS A 35 -178.38 -68.07
REMARK 500 5 ALA A 49 -64.63 -98.18
REMARK 500 5 GLU A 50 96.26 -67.94
REMARK 500 5 THR A 77 25.12 46.51
REMARK 500 5 LEU A 108 91.31 -46.54
REMARK 500 5 PRO A 111 -168.49 -69.71
REMARK 500 5 SER A 113 72.12 -68.02
REMARK 500 6 SER A 8 39.20 38.61
REMARK 500 6 ILE A 11 130.59 -34.62
REMARK 500 6 ASN A 22 55.04 33.74
REMARK 500 6 SER A 37 31.95 -87.62
REMARK 500 6 ALA A 49 -72.70 -129.38
REMARK 500 6 THR A 77 25.37 42.69
REMARK 500 6 LEU A 108 99.95 -53.21
REMARK 500 6 LYS A 109 -72.05 -91.97
REMARK 500 6 PRO A 111 -166.42 -69.74
REMARK 500 6 SER A 116 97.86 -36.46
REMARK 500 7 ASN A 22 76.97 -61.46
REMARK 500 7 HIS A 35 179.87 -54.40
REMARK 500 7 GLU A 50 148.70 -37.52
REMARK 500 7 THR A 77 35.49 32.02
REMARK 500 7 GLU A 78 50.55 34.66
REMARK 500 7 SER A 84 -175.68 -174.97
REMARK 500 7 LEU A 108 102.64 -40.80
REMARK 500 7 LYS A 109 -74.56 -91.02
REMARK 500 7 PRO A 111 -163.79 -69.61
REMARK 500 7 SER A 113 79.33 -65.40
REMARK 500 7 SER A 116 -45.43 -131.74
REMARK 500 7 SER A 117 93.69 -64.56
REMARK 500 8 SER A 6 166.48 -48.66
REMARK 500 8 ALA A 20 -62.82 -92.71
REMARK 500 8 ASN A 22 52.99 34.29
REMARK 500 8 HIS A 35 -175.50 -61.33
REMARK 500 8 PRO A 46 97.41 -69.77
REMARK 500 8 ARG A 51 -46.22 -131.51
REMARK 500 8 ASN A 59 41.81 71.91
REMARK 500 8 THR A 77 25.20 44.67
REMARK 500 8 LEU A 108 105.78 -34.41
REMARK 500 8 LYS A 109 -74.97 -97.67
REMARK 500 8 PRO A 111 -176.66 -69.71
REMARK 500 8 SER A 113 -74.91 -98.35
REMARK 500 8 PRO A 115 80.72 -69.80
REMARK 500 9 ARG A 9 43.34 -88.83
REMARK 500 9 HIS A 35 -176.21 -61.67
REMARK 500 9 SER A 37 31.31 -84.93
REMARK 500 9 ALA A 49 -72.33 -48.59
REMARK 500 9 ALA A 79 -72.06 -97.25
REMARK 500 9 LEU A 108 100.82 -52.01
REMARK 500 9 LYS A 109 -68.42 -94.16
REMARK 500 9 PRO A 111 -163.70 -69.80
REMARK 500 10 SER A 2 148.75 -37.09
REMARK 500 10 HIS A 35 -179.45 -61.56
REMARK 500 10 GLU A 50 81.95 -65.40
REMARK 500 10 ASN A 59 34.01 72.78
REMARK 500 10 THR A 77 37.42 30.66
REMARK 500 10 GLU A 78 49.38 37.65
REMARK 500 10 SER A 84 -177.57 -171.26
REMARK 500 10 LEU A 108 104.32 -44.41
REMARK 500 10 LYS A 109 -74.34 -94.35
REMARK 500 10 PRO A 111 -171.31 -69.72
REMARK 500 10 SER A 117 34.83 -83.99
REMARK 500 11 ASP A 12 92.94 -68.50
REMARK 500 11 ALA A 47 137.32 -174.54
REMARK 500 11 THR A 77 36.40 31.86
REMARK 500 11 GLU A 78 49.06 34.33
REMARK 500 11 LEU A 108 102.62 -39.65
REMARK 500 11 LYS A 109 -74.07 -92.41
REMARK 500 11 PRO A 111 -163.69 -69.78
REMARK 500 11 PRO A 115 90.40 -69.74
REMARK 500 12 HIS A 35 177.75 -57.04
REMARK 500 12 GLU A 48 -72.10 -80.48
REMARK 500 12 THR A 77 24.92 46.45
REMARK 500 12 SER A 84 -179.14 -173.92
REMARK 500 12 LEU A 108 105.36 -41.54
REMARK 500 12 LYS A 109 -66.29 -95.25
REMARK 500 12 PRO A 111 -168.55 -69.82
REMARK 500 12 SER A 113 -172.97 -64.86
REMARK 500 12 PRO A 115 97.78 -69.78
REMARK 500 13 ASN A 22 45.48 36.71
REMARK 500 13 MET A 23 -176.99 -69.77
REMARK 500 13 HIS A 35 179.06 -51.01
REMARK 500 13 SER A 37 34.96 -86.74
REMARK 500 13 ALA A 47 -178.86 -170.32
REMARK 500 13 ALA A 49 -60.03 -107.64
REMARK 500 13 GLU A 50 84.39 -66.54
REMARK 500 13 ASN A 59 44.39 73.53
REMARK 500 13 ASN A 72 31.53 70.24
REMARK 500 13 THR A 77 35.81 32.01
REMARK 500 13 LYS A 80 132.92 -174.61
REMARK 500 13 ASP A 83 -37.18 -36.77
REMARK 500 13 LEU A 108 102.59 -34.84
REMARK 500 13 LYS A 109 -73.85 -90.56
REMARK 500 13 PRO A 111 -169.76 -69.83
REMARK 500 14 ALA A 20 -63.41 -98.17
REMARK 500 14 ASN A 22 54.31 33.22
REMARK 500 14 PRO A 46 -169.53 -69.73
REMARK 500 14 ALA A 47 89.04 -49.59
REMARK 500 14 THR A 77 27.66 38.56
REMARK 500 14 LEU A 108 107.75 -45.07
REMARK 500 14 LYS A 109 -71.16 -100.08
REMARK 500 14 PRO A 111 -172.73 -69.69
REMARK 500 14 SER A 117 32.62 -89.26
REMARK 500 15 SER A 6 175.72 -59.17
REMARK 500 15 ASN A 22 54.66 -94.48
REMARK 500 15 LYS A 33 -30.85 -35.74
REMARK 500 15 HIS A 35 171.00 -46.14
REMARK 500 15 SER A 37 30.95 -87.18
REMARK 500 15 PRO A 46 91.11 -69.82
REMARK 500 15 THR A 77 25.11 42.86
REMARK 500 15 LEU A 108 103.74 -34.56
REMARK 500 15 LYS A 109 -74.02 -93.05
REMARK 500 15 PRO A 111 -166.42 -69.77
REMARK 500 15 SER A 117 39.04 37.04
REMARK 500 16 ALA A 20 -61.22 -94.92
REMARK 500 16 HIS A 35 -177.16 -62.23
REMARK 500 16 PRO A 46 94.37 -69.79
REMARK 500 16 THR A 77 38.82 29.81
REMARK 500 16 GLU A 78 50.14 36.48
REMARK 500 16 LEU A 108 102.46 -33.93
REMARK 500 16 LYS A 109 -74.14 -91.16
REMARK 500 16 PRO A 111 -169.66 -69.76
REMARK 500 17 GLU A 10 149.66 -34.61
REMARK 500 17 ASN A 22 48.56 39.73
REMARK 500 17 HIS A 35 -176.86 -59.20
REMARK 500 17 PRO A 46 86.42 -69.74
REMARK 500 17 ALA A 49 -70.41 -98.75
REMARK 500 17 GLU A 50 88.10 -66.77
REMARK 500 17 ASP A 60 25.17 48.74
REMARK 500 17 THR A 77 25.05 48.42
REMARK 500 17 ALA A 79 -75.03 -88.47
REMARK 500 17 ASP A 83 -37.39 -34.29
REMARK 500 17 LEU A 108 112.15 -38.98
REMARK 500 17 LYS A 109 -74.07 -104.55
REMARK 500 17 PRO A 111 -173.13 -69.74
REMARK 500 18 SER A 2 41.53 34.67
REMARK 500 18 ARG A 9 41.07 -98.12
REMARK 500 18 ASN A 22 76.58 -63.54
REMARK 500 18 HIS A 35 -175.02 -53.67
REMARK 500 18 ALA A 47 -35.69 -34.94
REMARK 500 18 ALA A 49 -75.02 -71.92
REMARK 500 18 PHE A 58 145.68 -173.33
REMARK 500 18 ASP A 60 28.43 44.92
REMARK 500 18 THR A 77 26.24 39.61
REMARK 500 18 ASP A 83 -33.01 -36.34
REMARK 500 18 SER A 84 -176.25 -174.73
REMARK 500 18 LEU A 108 102.86 -34.36
REMARK 500 18 LYS A 109 -75.09 -88.90
REMARK 500 18 PRO A 111 -163.55 -69.78
REMARK 500 18 SER A 113 89.96 -66.71
REMARK 500 18 SER A 116 41.15 -83.09
REMARK 500 19 ASN A 22 42.45 34.09
REMARK 500 19 HIS A 35 178.27 -48.62
REMARK 500 19 SER A 37 36.45 -88.15
REMARK 500 19 PRO A 46 -163.00 -69.73
REMARK 500 19 ALA A 47 43.93 75.03
REMARK 500 19 GLU A 48 36.12 32.56
REMARK 500 19 GLU A 50 103.84 -31.31
REMARK 500 19 ASN A 59 31.03 74.27
REMARK 500 19 THR A 77 36.93 30.86
REMARK 500 19 GLU A 78 52.13 37.02
REMARK 500 19 LYS A 80 124.94 -174.33
REMARK 500 19 SER A 84 -175.00 -175.51
REMARK 500 19 GLN A 93 -19.83 -48.87
REMARK 500 19 LEU A 108 105.33 -34.93
REMARK 500 19 LYS A 109 -74.17 -96.25
REMARK 500 19 PRO A 111 -176.06 -69.65
REMARK 500 19 PRO A 115 0.42 -69.68
REMARK 500 20 SER A 2 94.60 -64.72
REMARK 500 20 ARG A 9 94.80 -63.18
REMARK 500 20 HIS A 35 -177.57 -60.72
REMARK 500 20 GLU A 48 -71.01 -80.23
REMARK 500 20 THR A 77 32.00 33.92
REMARK 500 20 LEU A 108 100.78 -34.24
REMARK 500 20 LYS A 109 -73.31 -89.31
REMARK 500 20 PRO A 111 -169.03 -69.83
REMARK 500 20 SER A 113 -75.93 -35.23
REMARK 500 20 SER A 117 93.25 -61.47
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2DLZ A 8 112 UNP P52735 VAV2_HUMAN 663 767
SEQADV 2DLZ GLY A 1 UNP P52735 CLONING ARTIFACT
SEQADV 2DLZ SER A 2 UNP P52735 CLONING ARTIFACT
SEQADV 2DLZ SER A 3 UNP P52735 CLONING ARTIFACT
SEQADV 2DLZ GLY A 4 UNP P52735 CLONING ARTIFACT
SEQADV 2DLZ SER A 5 UNP P52735 CLONING ARTIFACT
SEQADV 2DLZ SER A 6 UNP P52735 CLONING ARTIFACT
SEQADV 2DLZ GLY A 7 UNP P52735 CLONING ARTIFACT
SEQADV 2DLZ SER A 113 UNP P52735 CLONING ARTIFACT
SEQADV 2DLZ GLY A 114 UNP P52735 CLONING ARTIFACT
SEQADV 2DLZ PRO A 115 UNP P52735 CLONING ARTIFACT
SEQADV 2DLZ SER A 116 UNP P52735 CLONING ARTIFACT
SEQADV 2DLZ SER A 117 UNP P52735 CLONING ARTIFACT
SEQADV 2DLZ GLY A 118 UNP P52735 CLONING ARTIFACT
SEQRES 1 A 118 GLY SER SER GLY SER SER GLY SER ARG GLU ILE ASP TYR
SEQRES 2 A 118 THR ALA TYR PRO TRP PHE ALA GLY ASN MET GLU ARG GLN
SEQRES 3 A 118 GLN THR ASP ASN LEU LEU LYS SER HIS ALA SER GLY THR
SEQRES 4 A 118 TYR LEU ILE ARG GLU ARG PRO ALA GLU ALA GLU ARG PHE
SEQRES 5 A 118 ALA ILE SER ILE LYS PHE ASN ASP GLU VAL LYS HIS ILE
SEQRES 6 A 118 LYS VAL VAL GLU LYS ASP ASN TRP ILE HIS ILE THR GLU
SEQRES 7 A 118 ALA LYS LYS PHE ASP SER LEU LEU GLU LEU VAL GLU TYR
SEQRES 8 A 118 TYR GLN CYS HIS SER LEU LYS GLU SER PHE LYS GLN LEU
SEQRES 9 A 118 ASP THR THR LEU LYS TYR PRO TYR SER GLY PRO SER SER
SEQRES 10 A 118 GLY
HELIX 1 1 ASP A 12 TYR A 16 5 5
HELIX 2 2 GLU A 24 HIS A 35 1 12
HELIX 3 3 SER A 84 GLN A 93 1 10
SHEET 1 A 5 PHE A 19 GLY A 21 0
SHEET 2 A 5 TYR A 40 ARG A 43 1 O ILE A 42 N ALA A 20
SHEET 3 A 5 PHE A 52 LYS A 57 -1 O ALA A 53 N ARG A 43
SHEET 4 A 5 VAL A 62 LYS A 70 -1 O ILE A 65 N ILE A 54
SHEET 5 A 5 TRP A 73 HIS A 75 -1 O HIS A 75 N VAL A 68
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
