HEADER IMMUNE SYSTEM 31-OCT-01 1KA6
TITLE SAP/SH2D1A BOUND TO PEPTIDE N-PY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SH2 DOMAIN PROTEIN 1A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SLAM-ASSOCIATED PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PEPTIDE N-PY;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: CYTOPLASMIC REGION (RESIDUES 275-282);
COMPND 10 SYNONYM: SIGNALING LYMPHOCYTIC ACTIVATION MOLECULE;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: 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: PET3A;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED (SOLID PHASE
SOURCE 13 SYNTHESIS). THE SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN HOMO
SOURCE 14 SAPIENS (HUMAN).
KEYWDS SH2 DOMAIN, PROTEIN-PEPTIDE COMPLEX, IMMUNE SYSTEM
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR P.M.HWANG,C.LI,M.MORRA,J.LILLYWHITE,F.GERTLER,C.TERHORST,L.E.KAY,
AUTHOR 2 T.PAWSON,J.FORMAN-KAY,S.-C.LI
REVDAT 5 27-OCT-21 1KA6 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 1KA6 1 VERSN
REVDAT 3 30-SEP-03 1KA6 1 JRNL DBREF
REVDAT 2 28-AUG-02 1KA6 1 JRNL
REVDAT 1 07-NOV-01 1KA6 0
JRNL AUTH P.M.HWANG,C.LI,M.MORRA,J.LILLYWHITE,D.R.MUHANDIRAM,
JRNL AUTH 2 F.GERTLER,C.TERHORST,L.E.KAY,T.PAWSON,J.D.FORMAN-KAY,S.C.LI
JRNL TITL A "THREE-PRONGED" BINDING MECHANISM FOR THE SAP/SH2D1A SH2
JRNL TITL 2 DOMAIN: STRUCTURAL BASIS AND RELEVANCE TO THE XLP SYNDROME.
JRNL REF EMBO J. V. 21 314 2002
JRNL REFN ISSN 0261-4189
JRNL PMID 11823424
JRNL DOI 10.1093/EMBOJ/21.3.314
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 1.0, ARIA 1.0
REMARK 3 AUTHORS : NILGES (ARIA), NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KA6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1000014752.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 120 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM SAP U-15N, 13C; 1MM N-PY;
REMARK 210 20 MM PHOSPHATE BUFFER, 100MM
REMARK 210 NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N,13C-SEPARATED NOESY; 3D
REMARK 210 HNHB; 3D_HN(CO)HB
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.8, NMRVIEW 3.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 ALA A 108
REMARK 465 ARG A 109
REMARK 465 SER A 110
REMARK 465 THR A 111
REMARK 465 GLN A 112
REMARK 465 GLY A 113
REMARK 465 THR A 114
REMARK 465 THR A 115
REMARK 465 GLY A 116
REMARK 465 ILE A 117
REMARK 465 ARG A 118
REMARK 465 GLU A 119
REMARK 465 ASP A 120
REMARK 465 PRO A 121
REMARK 465 ASP A 122
REMARK 465 VAL A 123
REMARK 465 CYS A 124
REMARK 465 LEU A 125
REMARK 465 LYS A 126
REMARK 465 ALA A 127
REMARK 465 PRO A 128
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 VAL A 6 49.60 -83.88
REMARK 500 TYR A 47 115.28 -164.34
REMARK 500 THR A 68 -157.65 -109.32
REMARK 500 ASP A 91 73.71 57.74
REMARK 500 GLN A 92 11.11 -144.33
REMARK 500 GLN A 99 -22.16 -152.61
REMARK 500 SER A 106 10.48 -151.55
REMARK 500 LYS B 276 -74.57 -165.02
REMARK 500 SER B 277 101.73 -167.26
REMARK 500 PTR B 281 -179.62 60.11
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 NH2 B 283
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KA7 RELATED DB: PDB
REMARK 900 SAP/SH2D1A BOUND TO PEPTIDE N-Y-C
DBREF 1KA6 A 1 128 UNP O60880 SH21A_HUMAN 1 128
DBREF 1KA6 B 275 282 UNP Q13291 SLAF1_HUMAN 275 282
SEQADV 1KA6 ARG B 275 UNP Q13291 LYS 275 ENGINEERED MUTATION
SEQADV 1KA6 PTR B 281 UNP Q13291 TYR 281 MODIFIED RESIDUE
SEQRES 1 A 128 MET ASP ALA VAL ALA VAL TYR HIS GLY LYS ILE SER ARG
SEQRES 2 A 128 GLU THR GLY GLU LYS LEU LEU LEU ALA THR GLY LEU ASP
SEQRES 3 A 128 GLY SER TYR LEU LEU ARG ASP SER GLU SER VAL PRO GLY
SEQRES 4 A 128 VAL TYR CYS LEU CYS VAL LEU TYR HIS GLY TYR ILE TYR
SEQRES 5 A 128 THR TYR ARG VAL SER GLN THR GLU THR GLY SER TRP SER
SEQRES 6 A 128 ALA GLU THR ALA PRO GLY VAL HIS LYS ARG TYR PHE ARG
SEQRES 7 A 128 LYS ILE LYS ASN LEU ILE SER ALA PHE GLN LYS PRO ASP
SEQRES 8 A 128 GLN GLY ILE VAL ILE PRO LEU GLN TYR PRO VAL GLU LYS
SEQRES 9 A 128 LYS SER SER ALA ARG SER THR GLN GLY THR THR GLY ILE
SEQRES 10 A 128 ARG GLU ASP PRO ASP VAL CYS LEU LYS ALA PRO
SEQRES 1 B 9 ARG LYS SER LEU THR ILE PTR ALA NH2
MODRES 1KA6 PTR B 281 TYR O-PHOSPHOTYROSINE
HET PTR B 281 24
HET NH2 B 283 3
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM NH2 AMINO GROUP
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 2 PTR C9 H12 N O6 P
FORMUL 2 NH2 H2 N
HELIX 1 1 SER A 12 GLY A 24 1 13
HELIX 2 2 LYS A 79 PHE A 87 1 9
SHEET 1 A 5 TYR A 29 ASP A 33 0
SHEET 2 A 5 TYR A 41 LEU A 46 -1 O CYS A 42 N ARG A 32
SHEET 3 A 5 ILE A 51 GLN A 58 -1 O VAL A 56 N TYR A 41
SHEET 4 A 5 TRP A 64 GLU A 67 -1 O GLU A 67 N ARG A 55
SHEET 5 A 5 TYR A 76 PHE A 77 -1 O PHE A 77 N TRP A 64
LINK C ILE B 280 N PTR B 281 1555 1555 1.33
LINK C PTR B 281 N ALA B 282 1555 1555 1.33
LINK C ALA B 282 N NH2 B 283 1555 1555 1.33
SITE 1 AC1 2 THR A 68 ALA B 282
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