HEADER HORMONE/GROWTH FACTOR 19-APR-99 1QG1
TITLE GROWTH FACTOR RECEPTOR BINDING PROTEIN SH2 DOMAIN COMPLEXED WITH AN
TITLE 2 SHC-DERIVED PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (GROWTH FACTOR RECEPTOR BINDING PROTEIN);
COMPND 3 CHAIN: E;
COMPND 4 FRAGMENT: SH2;
COMPND 5 SYNONYM: GRB2-SH2;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: RESIDUES HIS-58 - THR-159 AND THE EXTRINSIC N-TERMINAL
COMPND 8 TWO RESIDUES, GLY-56 AND SER-57;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: PROTEIN (SHC-DERIVED PEPTIDE);
COMPND 11 CHAIN: I;
COMPND 12 FRAGMENT: 423-435;
COMPND 13 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;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PGEX-4T-2;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_GENE: PROTEIN WAS EXPRESSED WITH PGEX-4T-2 VECTOR
SOURCE 10 AND BL21 (DE3) CELL AS GST-FUSION PROTEIN, AND CLEAVED WITH TRYPSIN;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED BY THE SOLID-
SOURCE 14 PHASE FMOC STRATEGY. THE SEQUENCE OF THIS PEPTIDE IS NATURALLY FOUND
SOURCE 15 IN HOMO SAPIENS (HUMAN).
KEYWDS SIGNAL TRANSDUCTION, SH2 DOMAIN, PHOSPHOTYROSYL PEPTIDE, COMPLEX
KEYWDS 2 (SIGNAL TRANSDUCTION-PEPTIDE), HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
AUTHOR K.OGURA
REVDAT 6 27-DEC-23 1QG1 1 REMARK
REVDAT 5 02-MAR-22 1QG1 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 1QG1 1 VERSN
REVDAT 3 01-APR-03 1QG1 1 JRNL
REVDAT 2 17-JUN-99 1QG1 1 JRNL
REVDAT 1 27-APR-99 1QG1 0
JRNL AUTH K.OGURA,S.TSUCHIYA,H.TERASAWA,S.YUZAWA,H.HATANAKA,
JRNL AUTH 2 V.MANDIYAN,J.SCHLESSINGER,F.INAGAKI
JRNL TITL SOLUTION STRUCTURE OF THE SH2 DOMAIN OF GRB2 COMPLEXED WITH
JRNL TITL 2 THE SHC-DERIVED PHOSPHOTYROSINE-CONTAINING PEPTIDE.
JRNL REF J.MOL.BIOL. V. 289 439 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10356320
JRNL DOI 10.1006/JMBI.1999.2792
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QG1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000886.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 301
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: MEAN STRUCTURE. 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY E 1 N - CA - C ANGL. DEV. = 24.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 SER E 2 -147.83 -162.15
REMARK 500 TRP E 5 -37.80 -149.88
REMARK 500 LYS E 9 68.77 -118.72
REMARK 500 GLN E 22 177.35 -51.53
REMARK 500 ALA E 27 137.34 -36.48
REMARK 500 GLU E 32 57.66 -96.62
REMARK 500 SER E 33 94.84 34.53
REMARK 500 SER E 41 -177.85 -170.71
REMARK 500 ASN E 48 -23.33 158.47
REMARK 500 LEU E 65 57.22 -176.41
REMARK 500 TRP E 66 -78.01 159.18
REMARK 500 VAL E 67 -74.02 -133.58
REMARK 500 SER E 84 -170.55 -52.55
REMARK 500 VAL E 85 -36.62 -138.93
REMARK 500 GLU E 97 -175.93 41.34
REMARK 500 GLN E 98 -14.05 73.99
REMARK 500 VAL E 99 169.47 48.12
REMARK 500 GLN E 101 112.33 1.10
REMARK 500 GLN E 102 10.73 98.69
REMARK 500 SER I 4 -177.27 77.53
REMARK 500 VAL I 6 -68.82 -5.77
REMARK 500 VAL I 8 123.18 -9.30
REMARK 500 ASN I 10 166.57 -43.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG E 12 0.32 SIDE CHAIN
REMARK 500 ARG E 81 0.28 SIDE CHAIN
REMARK 500 ARG E 87 0.22 SIDE CHAIN
REMARK 500 ARG E 94 0.27 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1QG1 E 3 104 UNP P62993 GRB2_HUMAN 58 159
DBREF 1QG1 I 1 13 UNP P29353 SHC1_HUMAN 423 435
SEQADV 1QG1 GLY E 1 UNP P62993 CLONING ARTIFACT
SEQADV 1QG1 SER E 2 UNP P62993 CLONING ARTIFACT
SEQADV 1QG1 PTR I 5 UNP P29353 TYR 427 MODIFIED RESIDUE
SEQRES 1 E 104 GLY SER HIS PRO TRP PHE PHE GLY LYS ILE PRO ARG ALA
SEQRES 2 E 104 LYS ALA GLU GLU MET LEU SER LYS GLN ARG HIS ASP GLY
SEQRES 3 E 104 ALA PHE LEU ILE ARG GLU SER GLU SER ALA PRO GLY ASP
SEQRES 4 E 104 PHE SER LEU SER VAL LYS PHE GLY ASN ASP VAL GLN HIS
SEQRES 5 E 104 PHE LYS VAL LEU ARG ASP GLY ALA GLY LYS TYR PHE LEU
SEQRES 6 E 104 TRP VAL VAL LYS PHE ASN SER LEU ASN GLU LEU VAL ASP
SEQRES 7 E 104 TYR HIS ARG SER THR SER VAL SER ARG ASN GLN GLN ILE
SEQRES 8 E 104 PHE LEU ARG ASP ILE GLU GLN VAL PRO GLN GLN PRO THR
SEQRES 1 I 13 ASP ASP PRO SER PTR VAL ASN VAL GLN ASN LEU ASP LYS
MODRES 1QG1 PTR I 5 TYR O-PHOSPHOTYROSINE
HET PTR I 5 24
HETNAM PTR O-PHOSPHOTYROSINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 2 PTR C9 H12 N O6 P
HELIX 1 1 PRO E 11 LEU E 19 1 9
HELIX 2 2 SER E 72 THR E 83 1 12
SHEET 1 A 4 ASP E 49 LYS E 54 0
SHEET 2 A 4 SER E 41 PHE E 46 -1 O LEU E 42 N PHE E 53
SHEET 3 A 4 ALA E 27 ARG E 31 -1 O ALA E 27 N LYS E 45
SHEET 4 A 4 PHE E 6 GLY E 8 1 N PHE E 7 O ILE E 30
SHEET 1 A1 4 ASP E 49 LYS E 54 0
SHEET 2 A1 4 SER E 41 PHE E 46 -1 O LEU E 42 N PHE E 53
SHEET 3 A1 4 ALA E 27 ARG E 31 -1 O ALA E 27 N LYS E 45
SHEET 4 A1 4 ARG E 94 ASP E 95 1 O ARG E 94 N PHE E 28
SHEET 1 B 3 LEU E 56 ARG E 57 0
SHEET 2 B 3 TYR E 63 PHE E 64 -1 O PHE E 64 N LEU E 56
SHEET 3 B 3 LYS E 69 PHE E 70 -1 O PHE E 70 N TYR E 63
LINK C SER I 4 N PTR I 5 1555 1555 1.30
LINK C PTR I 5 N VAL I 6 1555 1555 1.31
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
(ATOM LINES ARE NOT SHOWN.)
END
