HEADER COMPLEX (SIGNAL TRANSDUCTION/PEPTIDE) 09-NOV-95 1QWF
TITLE C-SRC SH3 DOMAIN COMPLEXED WITH LIGAND VSL12
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE TRANSFORMING PROTEIN SRC;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN;
COMPND 5 SYNONYM: P60-SRC;
COMPND 6 EC: 2.7.1.112;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: VAL-SER-LEU-ALA-ARG-ARG-PRO-LEU-PRO-PRO-LEU-PRO;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: VSL12;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AVIAN SARCOMA VIRUS;
SOURCE 3 ORGANISM_TAXID: 11876;
SOURCE 4 GENE: CHICKEN;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PGEX-2T;
SOURCE 8 EXPRESSION_SYSTEM_GENE: CHICKEN;
SOURCE 9 OTHER_DETAILS: GST-FUSION;
SOURCE 10 MOL_ID: 2
KEYWDS SRC SH3 DOMAIN, CLASS I LIGAND COMPLEX, COMPLEX (SIGNAL TRANSDUCTION-
KEYWDS 2 PEPTIDE) COMPLEX
EXPDTA SOLUTION NMR
AUTHOR S.FENG,K.CHIYOSHI,R.J.RICKLES,S.L.SCHREIBER
REVDAT 3 02-MAR-22 1QWF 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1QWF 1 VERSN
REVDAT 1 08-MAR-96 1QWF 0
JRNL AUTH S.FENG,C.KASAHARA,R.J.RICKLES,S.L.SCHREIBER
JRNL TITL SPECIFIC INTERACTIONS OUTSIDE THE PROLINE-RICH CORE OF TWO
JRNL TITL 2 CLASSES OF SRC HOMOLOGY 3 LIGANDS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 92 12408 1995
JRNL REFN ISSN 0027-8424
JRNL PMID 8618911
JRNL DOI 10.1073/PNAS.92.26.12408
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.YU,J.K.CHEN,S.FENG,D.C.DALGARNO,A.W.BRAUER,S.L.SCHREIBER
REMARK 1 TITL STRUCTURAL BASIS FOR THE BINDING OF PROLINE-RICH PEPTIDES TO
REMARK 1 TITL 2 SH3 DOMAINS
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 76 933 1994
REMARK 1 REFN ISSN 0092-8674
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.FENG,J.K.CHEN,H.YU,J.A.SIMON,S.L.SCHREIBER
REMARK 1 TITL TWO BINDING ORIENTATIONS FOR PEPTIDES TO THE SRC SH3 DOMAIN:
REMARK 1 TITL 2 DEVELOPMENT OF A GENERAL MODEL FOR SH3-LIGAND INTERACTIONS
REMARK 1 REF SCIENCE V. 266 1241 1994
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 3
REMARK 1 AUTH H.YU,M.K.ROSEN,T.B.SHIN,C.SEIDEL-DUGAN,J.S.BRUGGE,
REMARK 1 AUTH 2 S.L.SCHREIBER
REMARK 1 TITL SOLUTION STRUCTURE OF THE SH3 DOMAIN OF SRC AND
REMARK 1 TITL 2 IDENTIFICATION OF ITS LIGAND-BINDING SITE
REMARK 1 REF SCIENCE V. 258 1665 1992
REMARK 1 REFN ISSN 0036-8075
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 1QWF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175945.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
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 : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 RES C SSSEQI
REMARK 465 GLY A 1
REMARK 465 SER A 2
REMARK 465 HIS A 3
REMARK 465 MET A 4
REMARK 465 GLY A 5
REMARK 465 GLY A 6
REMARK 465 VAL A 7
REMARK 465 THR A 8
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 LEU A 13 -32.37 -39.48
REMARK 500 VAL A 35 -73.46 -120.44
REMARK 500 TYR A 55 177.91 -51.43
REMARK 500 SER B 72 -32.71 -160.67
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1QWF A 1 64 UNP P00525 SRC_AVISR 77 140
DBREF 1QWF B 71 82 PDB 1QWF 1QWF 71 82
SEQADV 1QWF SER A 2 UNP P00525 ALA 78 CONFLICT
SEQADV 1QWF HIS A 3 UNP P00525 LEU 79 CONFLICT
SEQADV 1QWF MET A 4 UNP P00525 ALA 80 CONFLICT
SEQRES 1 A 64 GLY SER HIS MET GLY GLY VAL THR THR PHE VAL ALA LEU
SEQRES 2 A 64 TYR ASP TYR GLU SER ARG THR GLU THR ASP LEU SER PHE
SEQRES 3 A 64 LYS LYS GLY GLU ARG LEU GLN ILE VAL ASN ASN THR GLU
SEQRES 4 A 64 GLY ASP TRP TRP LEU ALA HIS SER LEU THR THR GLY GLN
SEQRES 5 A 64 THR GLY TYR ILE PRO SER ASN TYR VAL ALA PRO SER
SEQRES 1 B 12 VAL SER LEU ALA ARG ARG PRO LEU PRO PRO LEU PRO
HELIX 1 1 SER A 58 TYR A 60 5 3
SHEET 1 A 3 GLN A 52 PRO A 57 0
SHEET 2 A 3 TRP A 42 SER A 47 -1 N SER A 47 O GLN A 52
SHEET 3 A 3 GLN A 33 ASN A 36 -1 N ASN A 36 O LEU A 44
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
