HEADER PEPTIDE BINDING PROTEIN 24-MAR-05 1X0N
TITLE NMR STRUCTURE OF GROWTH FACTOR RECEPTOR BINDING PROTEIN SH2 DOMAIN
TITLE 2 COMPLEXED WITH THE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH2 DOMAIN;
COMPND 5 SYNONYM: GRB2, GRB2 ADAPTER PROTEIN, SH2/SH3 ADAPTER GRB2, ASH
COMPND 6 PROTEIN;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-2
KEYWDS PEPTIDE BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.OGURA,T.SHIGA,S.YUZAWA,M.YOKOCHI,T.R.BURKE,F.INAGAKI
REVDAT 3 02-MAR-22 1X0N 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X0N 1 VERSN
REVDAT 1 19-APR-05 1X0N 0
JRNL AUTH K.OGURA,T.SHIGA,S.YUZAWA,M.YOKOCHI,T.R.BURKE,F.INAGAKI
JRNL TITL NMR STRUCTURE OF GROWTH FACTOR RECEPTOR BINDING PROTEIN SH2
JRNL TITL 2 DOMAIN COMPLEXED WITH THE INHIBITOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, CYANA
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X0N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000024230.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM SH2 U-13C, 15N; 20MM SODIUM
REMARK 210 PHOSPHATE; 150MM NACL
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 : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA, SPARKY
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
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 56
REMARK 465 SER A 57
REMARK 465 HIS A 58
REMARK 465 PRO A 59
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 77 -173.20 -61.69
REMARK 500 1 ALA A 115 -62.85 -170.34
REMARK 500 1 LEU A 120 -71.39 -125.85
REMARK 500 1 SER A 139 160.34 -42.01
REMARK 500 1 VAL A 140 -36.31 -142.77
REMARK 500 1 ASN A 143 -49.31 -130.45
REMARK 500 1 GLN A 153 163.23 -43.80
REMARK 500 2 LYS A 64 90.79 -64.50
REMARK 500 2 HIS A 79 -171.77 -62.74
REMARK 500 2 SER A 88 174.30 -58.13
REMARK 500 2 ALA A 115 -58.25 -173.20
REMARK 500 2 LEU A 120 -88.51 -120.49
REMARK 500 2 TRP A 121 19.65 -159.25
REMARK 500 2 VAL A 122 -41.53 -145.29
REMARK 500 2 SER A 139 159.34 -39.19
REMARK 500 2 VAL A 140 -37.24 -135.26
REMARK 500 2 ARG A 142 32.56 -87.09
REMARK 500 2 ASN A 143 -53.01 -131.49
REMARK 500 3 LYS A 64 85.03 69.05
REMARK 500 3 ASP A 113 -169.61 -100.93
REMARK 500 3 ALA A 115 -41.21 -136.53
REMARK 500 3 LEU A 120 -92.87 -125.92
REMARK 500 3 VAL A 122 -38.00 -146.65
REMARK 500 3 SER A 139 160.29 -42.80
REMARK 500 3 VAL A 140 -52.16 -131.47
REMARK 500 3 ARG A 142 33.50 -87.57
REMARK 500 3 ASN A 143 -52.14 -129.87
REMARK 500 3 GLN A 153 150.89 -35.43
REMARK 500 3 VAL A 154 138.19 -35.72
REMARK 500 3 GLN A 157 117.97 -34.41
REMARK 500 4 HIS A 79 -175.23 -62.91
REMARK 500 4 SER A 88 165.93 -44.22
REMARK 500 4 ALA A 115 -52.50 -178.59
REMARK 500 4 LEU A 120 -84.89 -138.31
REMARK 500 4 TRP A 121 -81.57 -79.46
REMARK 500 4 GLN A 153 170.35 -57.46
REMARK 500 4 GLN A 156 77.88 -157.08
REMARK 500 5 LYS A 64 97.84 -58.81
REMARK 500 5 HIS A 79 -171.44 -69.80
REMARK 500 5 ALA A 115 -20.23 161.47
REMARK 500 5 LEU A 120 -94.96 -136.30
REMARK 500 5 TRP A 121 14.95 -151.55
REMARK 500 5 VAL A 122 -31.56 -132.65
REMARK 500 5 SER A 139 160.51 -48.55
REMARK 500 5 VAL A 140 -36.38 -143.07
REMARK 500 5 ASN A 143 -51.61 -126.46
REMARK 500 5 VAL A 154 125.99 -38.37
REMARK 500 5 GLN A 156 80.34 -165.53
REMARK 500 5 GLN A 157 114.75 -171.89
REMARK 500 6 ARG A 67 -38.67 -33.41
REMARK 500
REMARK 500 THIS ENTRY HAS 201 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTF A 174
DBREF 1X0N A 58 159 UNP P62993 GRB2_HUMAN 58 159
SEQADV 1X0N GLY A 56 UNP P62993 CLONING ARTIFACT
SEQADV 1X0N SER A 57 UNP P62993 CLONING ARTIFACT
SEQRES 1 A 104 GLY SER HIS PRO TRP PHE PHE GLY LYS ILE PRO ARG ALA
SEQRES 2 A 104 LYS ALA GLU GLU MET LEU SER LYS GLN ARG HIS ASP GLY
SEQRES 3 A 104 ALA PHE LEU ILE ARG GLU SER GLU SER ALA PRO GLY ASP
SEQRES 4 A 104 PHE SER LEU SER VAL LYS PHE GLY ASN ASP VAL GLN HIS
SEQRES 5 A 104 PHE LYS VAL LEU ARG ASP GLY ALA GLY LYS TYR PHE LEU
SEQRES 6 A 104 TRP VAL VAL LYS PHE ASN SER LEU ASN GLU LEU VAL ASP
SEQRES 7 A 104 TYR HIS ARG SER THR SER VAL SER ARG ASN GLN GLN ILE
SEQRES 8 A 104 PHE LEU ARG ASP ILE GLU GLN VAL PRO GLN GLN PRO THR
HET DTF A 174 92
HETNAM DTF 4-[(10S,14S,18S)-18-(2-AMINO-2-OXOETHYL)-14-(1-
HETNAM 2 DTF NAPHTHYLMETHYL)-8,17,20-TRIOXO-7,16,19-
HETNAM 3 DTF TRIAZASPIRO[5.14]ICOS-11-EN-10-YL]BENZYLPHOSPHONIC
HETNAM 4 DTF ACID
FORMUL 2 DTF C37 H45 N4 O7 P
HELIX 1 1 PRO A 66 LYS A 76 1 11
HELIX 2 2 SER A 127 THR A 138 1 12
SHEET 1 A 6 PHE A 61 PHE A 62 0
SHEET 2 A 6 PHE A 83 ARG A 86 1 O ILE A 85 N PHE A 62
SHEET 3 A 6 PHE A 95 PHE A 101 -1 O SER A 96 N ARG A 86
SHEET 4 A 6 ASP A 104 ARG A 112 -1 O ASP A 104 N PHE A 101
SHEET 5 A 6 TYR A 118 PHE A 119 -1 O PHE A 119 N LEU A 111
SHEET 6 A 6 LYS A 124 PHE A 125 -1 O PHE A 125 N TYR A 118
SITE 1 AC1 8 ARG A 67 ARG A 86 GLN A 106 HIS A 107
SITE 2 AC1 8 PHE A 108 LYS A 109 LEU A 111 TRP A 121
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
