HEADER HYDROLASE(SH2 DOMAIN) 15-MAY-94 1AYA 1AYA 2 COMPND TYROSINE PHOSPHATASE SYP (N-TERMINAL SH2 DOMAIN) 1AYA 3 COMPND 2 (PTP1D, SHPTP2) (E.C.3.1.3.48) COMPLEXED WITH THE PEPTIDE 1AYA 4 COMPND 3 PDGFR-1009 1AYA 5 SOURCE TYROSINE PHOSPHATASE: MOUSE (MUS MUSCULUS) RECOMBINANT FORM 1AYA 6 SOURCE 2 EXPRESSED IN (ESCHERICHIA COLI); PEPTIDE: SYNTHETIC 1AYA 7 AUTHOR C.-H.LEE,J.KURIYAN 1AYA 8 REVDAT 1 31-AUG-94 1AYA 0 1AYA 9 JRNL AUTH C.-H.LEE,D.KOMINOS,S.JACQUES,B.MARGOLIS, 1AYA 10 JRNL AUTH 2 J.SCHLESSINGER,S.E.SHOELSON,J.KURIYAN 1AYA 11 JRNL TITL CRYSTAL STRUCTURES OF PEPTIDE COMPLEXES OF THE 1AYA 12 JRNL TITL 2 AMINO-TERMINAL SH2 DOMAIN OF THE SYP TYROSINE 1AYA 13 JRNL TITL 3 PHOSPHATASE 1AYA 14 JRNL REF STRUCTURE V. 2 423 1994 1AYA 15 JRNL REFN ASTM UK ISSN 0969-2126 2005 1AYA 16 REMARK 1 1AYA 17 REMARK 1 REFERENCE 1 1AYA 18 REMARK 1 AUTH G.WAKSMAN,S.E.SHOELSON,N.PANT,D.COWBURN,J.KURIYAN 1AYA 19 REMARK 1 TITL BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE 1AYA 20 REMARK 1 TITL 2 TO THE SRC SH2 DOMAIN: CRYSTAL STRUCTURES OF THE 1AYA 21 REMARK 1 TITL 3 COMPLEXED AND PEPTIDE-FREE FORMS 1AYA 22 REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 72 779 1993 1AYA 23 REMARK 1 REFN ASTM CELLB5 US ISSN 0092-8674 0998 1AYA 24 REMARK 1 REFERENCE 2 1AYA 25 REMARK 1 AUTH J.KURIYAN,D.COWBURN 1AYA 26 REMARK 1 TITL STRUCTURES OF SH2 AND SH3 DOMAINS 1AYA 27 REMARK 1 REF CURR.OPIN.STRUCT.BIOL. V. 3 828 1993 1AYA 28 REMARK 1 REFN ASTM COSBEF UK ISSN 0959-440X 0801 1AYA 29 REMARK 1 REFERENCE 3 1AYA 30 REMARK 1 AUTH G.WAKSMAN,D.KOMINOS,S.R.ROBERTSON,N.PANT, 1AYA 31 REMARK 1 AUTH 2 D.BALTIMORE,R.B.BIRGE,D.COWBURN,H.HANAFUSA, 1AYA 32 REMARK 1 AUTH 3 B.J.MAYER,M.OVERDUIN,M.D.RESH,C.B.RIOS,L.SILVERMAN, 1AYA 33 REMARK 1 AUTH 4 J.KURIYAN 1AYA 34 REMARK 1 TITL CRYSTAL STRUCTURE OF THE PHOSPHOTYROSINE 1AYA 35 REMARK 1 TITL 2 RECOGNITION DOMAIN SH2 OF V-SRC COMPLEXED WITH 1AYA 36 REMARK 1 TITL 3 TYROSINE-PHOSPHORYLATED PEPTIDES 1AYA 37 REMARK 1 REF NATURE V. 358 646 1992 1AYA 38 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006 1AYA 39 REMARK 2 1AYA 40 REMARK 2 RESOLUTION. 2.05 ANGSTROMS. 1AYA 41 REMARK 3 1AYA 42 REMARK 3 REFINEMENT. 1AYA 43 REMARK 3 PROGRAM X-PLOR 1AYA 44 REMARK 3 AUTHORS BRUNGER 1AYA 45 REMARK 3 R VALUE 0.180 1AYA 46 REMARK 3 RMSD BOND DISTANCES 0.014 ANGSTROMS 1AYA 47 REMARK 3 RMSD BOND ANGLES 3.0 DEGREES 1AYA 48 REMARK 3 1AYA 49 REMARK 3 NUMBER OF REFLECTIONS 10547 1AYA 50 REMARK 3 RESOLUTION RANGE 6.0 - 2.05 ANGSTROMS 1AYA 51 REMARK 3 DATA CUTOFF 2. SIGMA(F) 1AYA 52 REMARK 3 1AYA 53 REMARK 3 NUMBER OF PROTEIN ATOMS 1731 1AYA 54 REMARK 3 NUMBER OF SOLVENT ATOMS 141 1AYA 55 REMARK 4 1AYA 56 REMARK 4 THIS ENTRY CONTAINS TWO MOLECULES, EACH CONTAINING THE 1AYA 57 REMARK 4 N-TERMINAL DOMAIN OF SYP (101 RESIDUES) AND THE PDGFR-1009 1AYA 58 REMARK 4 PEPTIDE (11 RESIDUES). IN MOLECULE 1 THE PROTEIN HAS BEEN 1AYA 59 REMARK 4 ASSIGNED CHAIN IDENTIFIER *A* AND THE PEPTIDE HAS BEEN 1AYA 60 REMARK 4 ASSIGNED CHAIN IDENTIFIER *P*. IN MOLECULE 2 THE PROTEIN 1AYA 61 REMARK 4 HAS BEEN ASSIGNED CHAIN IDENTIFIER *B* AND THE PEPTIDE HAS 1AYA 62 REMARK 4 BEEN ASSIGNED CHAIN IDENTIFIER *Q*. RESIDUE 0 OF 1AYA 63 REMARK 4 PDGFR-1009 CORRESPONDS TO RESIDUE 1009 OF THE PDGFR 1AYA 64 REMARK 4 COMPLETE PROTEIN. 1AYA 65 REMARK 5 1AYA 66 REMARK 5 NO COORDINATES ARE PRESENT FOR THE FOLLOWING RESIDUES: 1AYA 67 REMARK 5 ASN P 6 1AYA 68 REMARK 5 GLU P 7 1AYA 69 REMARK 5 SER Q -3 1AYA 70 REMARK 5 ASN Q 6 1AYA 71 REMARK 5 GLU Q 7 1AYA 72 REMARK 5 1AYA 73 REMARK 5 THE FOLLOWING RESIDUES HAVE MISSING ATOMS AS INDICATED 1AYA 74 REMARK 5 BELOW: 1AYA 75 REMARK 5 M RES C SEQ ATOMS 1AYA 76 REMARK 5 MET A 3 ( CG SD CE ) 1AYA 77 REMARK 5 ARG A 23 ( CD NE CZ NH1 NH2) 1AYA 78 REMARK 5 GLU A 69 ( CG CD OE1 OE2) 1AYA 79 REMARK 5 MET B 3 ( CG SD CE ) 1AYA 80 REMARK 5 LYS B 35 ( CG CD CE NZ ) 1AYA 81 REMARK 5 GLN B 79 ( CD OE1 NE2 1AYA 82 REMARK 5 HIS B 85 ( CG ND1 CE1 NE2 CD2) 1AYA 83 REMARK 5 LYS B 91 ( CG CD CE NZ ) 1AYA 84 REMARK 5 GLN Q 4 ( CG CD OE1 NE2) 1AYA 85 SEQRES 1 A 101 MET ARG ARG TRP PHE HIS PRO ASN ILE THR GLY VAL GLU 1AYA 86 SEQRES 2 A 101 ALA GLU ASN LEU LEU LEU THR ARG GLY VAL ASP GLY SER 1AYA 87 SEQRES 3 A 101 PHE LEU ALA ARG PRO SER LYS SER ASN PRO GLY ASP PHE 1AYA 88 SEQRES 4 A 101 THR LEU SER VAL ARG ARG ASN GLY ALA VAL THR HIS ILE 1AYA 89 SEQRES 5 A 101 LYS ILE GLN ASN THR GLY ASP TYR TYR ASP LEU TYR GLY 1AYA 90 SEQRES 6 A 101 GLY GLU LYS PHE ALA THR LEU ALA GLU LEU VAL GLN TYR 1AYA 91 SEQRES 7 A 101 TYR MET GLU HIS HIS GLY GLN LEU LYS GLU LYS ASN GLY 1AYA 92 SEQRES 8 A 101 ASP VAL ILE GLU LEU LYS TYR PRO LEU ASN 1AYA 93 SEQRES 1 P 11 SER VAL LEU TYR THR ALA VAL GLN PRO ASN GLU 1AYA 94 SEQRES 1 B 101 MET ARG ARG TRP PHE HIS PRO ASN ILE THR GLY VAL GLU 1AYA 95 SEQRES 2 B 101 ALA GLU ASN LEU LEU LEU THR ARG GLY VAL ASP GLY SER 1AYA 96 SEQRES 3 B 101 PHE LEU ALA ARG PRO SER LYS SER ASN PRO GLY ASP PHE 1AYA 97 SEQRES 4 B 101 THR LEU SER VAL ARG ARG ASN GLY ALA VAL THR HIS ILE 1AYA 98 SEQRES 5 B 101 LYS ILE GLN ASN THR GLY ASP TYR TYR ASP LEU TYR GLY 1AYA 99 SEQRES 6 B 101 GLY GLU LYS PHE ALA THR LEU ALA GLU LEU VAL GLN TYR 1AYA 100 SEQRES 7 B 101 TYR MET GLU HIS HIS GLY GLN LEU LYS GLU LYS ASN GLY 1AYA 101 SEQRES 8 B 101 ASP VAL ILE GLU LEU LYS TYR PRO LEU ASN 1AYA 102 SEQRES 1 Q 11 SER VAL LEU TYR THR ALA VAL GLN PRO ASN GLU 1AYA 103 HET PHS P 0 4 PHOSPHONO GROUP 1AYA 104 HET PHS Q 0 4 PHOSPHONO GROUP 1AYA 105 FORMUL 5 PHS 2(H2 O3 P1) 1AYA 106 FORMUL 6 HOH *141(H2 O1) 1AYA 107 CRYST1 33.800 52.700 56.400 90.00 101.10 90.00 P 21 4 1AYA 108 ORIGX1 1.000000 0.000000 0.000000 0.00000 1AYA 109 ORIGX2 0.000000 1.000000 0.000000 0.00000 1AYA 110 ORIGX3 0.000000 0.000000 1.000000 0.00000 1AYA 111 SCALE1 0.029586 0.000000 0.005805 0.00000 1AYA 112 SCALE2 0.000000 0.018975 0.000000 0.00000 1AYA 113 SCALE3 0.000000 0.000000 0.018069 0.00000 1AYA 114