HEADER COMPLEX (SIGNAL TRANSDUCTION/PEPTIDE) 22-MAR-96 1IRS
TITLE IRS-1 PTB DOMAIN COMPLEXED WITH A IL-4 RECEPTOR PHOSPHOPEPTIDE, NMR,
TITLE 2 MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IRS-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PTB DOMAIN;
COMPND 5 SYNONYM: INSULIN RECEPTOR SUBSTRATE 1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: IL-4 RECEPTOR PHOSPHOPEPTIDE;
COMPND 9 CHAIN: B;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 STRAIN: BL21 (DE2) PLYSS;
SOURCE 6 CELL_LINE: BL21;
SOURCE 7 ORGAN: SKELETAL;
SOURCE 8 GENE: PTB DOMAIN OF IRS-1;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET30B;
SOURCE 12 EXPRESSION_SYSTEM_GENE: PTB DOMAIN OF IRS-1;
SOURCE 13 MOL_ID: 2;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_COMMON: HUMAN;
SOURCE 16 ORGANISM_TAXID: 9606;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHOSPHOTYROSINE BINDING DOMAIN (PTB), COMPLEX, SIGNAL TRANSDUCTION,
KEYWDS 2 COMPLEX (SIGNAL TRANSDUCTION-PEPTIDE), COMPLEX (SIGNAL TRANSDUCTION-
KEYWDS 3 PEPTIDE) COMPLEX
EXPDTA SOLUTION NMR
AUTHOR M.-M.ZHOU,B.HUANG,E.T.OLEJNICZAK,R.P.MEADOWS,S.B.SHUKER,M.MIYAZAKI,
AUTHOR 2 T.TRUB,S.E.SHOELSON,S.W.FEISK
REVDAT 3 23-FEB-22 1IRS 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1IRS 1 VERSN
REVDAT 1 15-MAY-97 1IRS 0
JRNL AUTH M.M.ZHOU,B.HUANG,E.T.OLEJNICZAK,R.P.MEADOWS,S.B.SHUKER,
JRNL AUTH 2 M.MIYAZAKI,T.TRUB,S.E.SHOELSON,S.W.FESIK
JRNL TITL STRUCTURAL BASIS FOR IL-4 RECEPTOR PHOSPHOPEPTIDE
JRNL TITL 2 RECOGNITION BY THE IRS-1 PTB DOMAIN.
JRNL REF NAT.STRUCT.BIOL. V. 3 388 1996
JRNL REFN ISSN 1072-8368
JRNL PMID 8599766
JRNL DOI 10.1038/NSB0496-388
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.WOLF,T.TRUB,E.OTTINGER,L.GRONINGA,A.LYNCH,M.F.WHITE,
REMARK 1 AUTH 2 M.MIYAZAKI,J.LEE,S.E.SHOELSON
REMARK 1 TITL PTB DOMAINS OF IRS-1 AND SHC HAVE DISTINCT BUT OVERLAPPING
REMARK 1 TITL 2 BINDING SPECIFICITIES
REMARK 1 REF J.BIOL.CHEM. V. 270 27407 1995
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.M.ZHOU,K.S.RAVICHANDRAN,E.F.OLEJNICZAK,A.M.PETROS,
REMARK 1 AUTH 2 R.P.MEADOWS,M.SATTLER,J.E.HARLAN,W.S.WADE,S.J.BURAKOFF,
REMARK 1 AUTH 3 S.W.FESIK
REMARK 1 TITL STRUCTURE AND LIGAND RECOGNITION OF THE PHOSPHOTYROSINE
REMARK 1 TITL 2 BINDING DOMAIN OF SHC
REMARK 1 REF NATURE V. 378 584 1995
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 3
REMARK 1 AUTH T.J.O'NEILL,A.CRAPARO,T.A.GUSTAFSON
REMARK 1 TITL CHARACTERIZATION OF AN INTERACTION BETWEEN INSULIN RECEPTOR
REMARK 1 TITL 2 SUBSTRATE 1 AND THE INSULIN RECEPTOR BY USING THE TWO-HYBRID
REMARK 1 TITL 3 SYSTEM
REMARK 1 REF MOL.CELL.BIOL. V. 14 6433 1994
REMARK 1 REFN ISSN 0270-7306
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SET OF IDEAL BOND LENGTHS AND ANGLES
REMARK 3 USED DURING REFINEMENT: PARALLHDG.PRO IN X-PLOR.
REMARK 4
REMARK 4 1IRS 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_1000174245.
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 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 PRO A 158 47.10 -83.94
REMARK 500 LEU A 168 157.63 -45.06
REMARK 500 GLN A 175 -45.21 -150.05
REMARK 500 THR A 188 46.08 -99.16
REMARK 500 SER A 189 28.74 38.61
REMARK 500 LYS A 190 -34.83 169.35
REMARK 500 ASN A 198 37.11 -99.52
REMARK 500 GLU A 200 -54.78 -133.27
REMARK 500 SER A 217 90.35 -64.14
REMARK 500 GLU A 218 -88.53 64.01
REMARK 500 VAL A 240 -163.93 -107.86
REMARK 500 ASP A 242 -146.93 -171.81
REMARK 500 PHE A 264 -70.49 -81.13
REMARK 500 ARG A 265 145.98 171.37
REMARK 500 PRO A 266 -152.33 -55.68
REMARK 500 ARG B 498 -81.78 72.84
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 A 184 0.22 SIDE CHAIN
REMARK 500 ARG A 212 0.20 SIDE CHAIN
REMARK 500 ARG A 213 0.18 SIDE CHAIN
REMARK 500 ARG A 227 0.31 SIDE CHAIN
REMARK 500 ARG A 258 0.29 SIDE CHAIN
REMARK 500 ARG A 265 0.24 SIDE CHAIN
REMARK 500 ARG A 267 0.26 SIDE CHAIN
REMARK 500 ARG B 498 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1IRS A 157 267 UNP P35568 IRS1_HUMAN 157 267
DBREF 1IRS B 489 499 UNP P24394 IL4RA_HUMAN 489 499
SEQADV 1IRS PTR B 497 UNP P24394 TYR 497 MODIFIED RESIDUE
SEQRES 1 A 112 MET GLY PRO ALA PHE LYS GLU VAL TRP GLN VAL ILE LEU
SEQRES 2 A 112 LYS PRO LYS GLY LEU GLY GLN THR LYS ASN LEU ILE GLY
SEQRES 3 A 112 ILE TYR ARG LEU CYS LEU THR SER LYS THR ILE SER PHE
SEQRES 4 A 112 VAL LYS LEU ASN SER GLU ALA ALA ALA VAL VAL LEU GLN
SEQRES 5 A 112 LEU MET ASN ILE ARG ARG CYS GLY HIS SER GLU ASN PHE
SEQRES 6 A 112 PHE PHE ILE GLU VAL GLY ARG SER ALA VAL THR GLY PRO
SEQRES 7 A 112 GLY GLU PHE TRP MET GLN VAL ASP ASP SER VAL VAL ALA
SEQRES 8 A 112 GLN ASN MET HIS GLU THR ILE LEU GLU ALA MET ARG ALA
SEQRES 9 A 112 MET SER ASP GLU PHE ARG PRO ARG
SEQRES 1 B 11 LEU VAL ILE ALA GLY ASN PRO ALA PTR ARG SER
MODRES 1IRS PTR B 497 TYR O-PHOSPHOTYROSINE
HET PTR B 497 25
HETNAM PTR O-PHOSPHOTYROSINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 2 PTR C9 H12 N O6 P
HELIX 1 1 LEU A 173 THR A 176 1 4
HELIX 2 2 VAL A 245 ASP A 262 1 18
HELIX 3 3 PRO B 495 PTR B 497 5 3
SHEET 1 A 4 GLU A 162 ILE A 167 0
SHEET 2 A 4 ILE A 182 THR A 188 -1 N LEU A 187 O GLU A 162
SHEET 3 A 4 THR A 191 LYS A 196 -1 N VAL A 195 O ARG A 184
SHEET 4 A 4 VAL A 204 GLN A 207 -1 N LEU A 206 O ILE A 192
SHEET 1 B 3 GLY A 234 PHE A 236 0
SHEET 2 B 3 PHE A 220 VAL A 225 -1 N VAL A 225 O GLY A 234
SHEET 3 B 3 ILE A 211 SER A 217 -1 N SER A 217 O PHE A 220
LINK C ALA B 496 N PTR B 497 1555 1555 1.31
LINK C PTR B 497 N ARG B 498 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
