HEADER COMPLEX (PHOSPHOTRANSFERASE/PEPTIDE) 03-OCT-95 1CSY
TITLE SYK TYROSINE KINASE C-TERMINAL SH2 DOMAIN COMPLEXED WITH A
TITLE 2 PHOSPHOPEPTIDEFROM THE GAMMA CHAIN OF THE HIGH AFFINITY IMMUNOGLOBIN
TITLE 3 G RECEPTOR, NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SYK PROTEIN TYROSINE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL SH2 DOMAIN;
COMPND 5 EC: 2.7.1.112;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ACETYL-THR-PTR-GLU-THR-LEU-NH2;
COMPND 9 CHAIN: B;
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: THE LIGAND IS A PHOSPHOTYROSINE CONTAINING PEPTIDE
COMPND 12 DERIVED FROM THE HIGH-AFFINITY IGE RECEPTOR
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: BL21;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 17 OTHER_DETAILS: RECOMBINANT CONSTRUCT ADDED TO PROTEIN DOMAIN
KEYWDS PROTEIN-TYROSINE KINASE SH2 DOMAIN, COMPLEX (PHOSPHOTRANSFERASE-
KEYWDS 2 PEPTIDE), COMPLEX (PHOSPHOTRANSFERASE-PEPTIDE) COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.S.NARULA,R.W.YUAN,S.E.ADAMS,O.M.GREEN,J.GREEN,T.B.PHILLIPS,
AUTHOR 2 L.D.ZYDOWSKY,M.C.BOTFIELD,M.H.HATADA,E.R.LAIRD,M.J.ZOLLER,J.L.KARAS,
AUTHOR 3 D.C.DALGARNO
REVDAT 4 22-FEB-12 1CSY 1 JRNL VERSN
REVDAT 3 24-FEB-09 1CSY 1 VERSN
REVDAT 2 01-APR-03 1CSY 1 JRNL
REVDAT 1 08-NOV-96 1CSY 0
JRNL AUTH S.S.NARULA,R.W.YUAN,S.E.ADAMS,O.M.GREEN,J.GREEN,T.B.PHILIPS,
JRNL AUTH 2 L.D.ZYDOWSKY,M.C.BOTFIELD,M.HATADA,E.R.LAIRD,M.J.ZOLLER,
JRNL AUTH 3 J.L.KARAS,D.C.DALGARNO
JRNL TITL SOLUTION STRUCTURE OF THE C-TERMINAL SH2 DOMAIN OF THE HUMAN
JRNL TITL 2 TYROSINE KINASE SYK COMPLEXED WITH A PHOSPHOTYROSINE
JRNL TITL 3 PENTAPEPTIDE.
JRNL REF STRUCTURE V. 3 1061 1995
JRNL REFN ISSN 0969-2126
JRNL PMID 8590001
JRNL DOI 10.1016/S0969-2126(01)00242-8
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: NULL
REMARK 4
REMARK 4 1CSY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
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 : 20
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 H SER A 33 HZ1 LYS A 38 1.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 9 HIS A 62 CG HIS A 62 CD2 0.054
REMARK 500 11 HIS A 62 CG HIS A 62 CD2 0.054
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 1 SER A 2 -165.81 -106.07
REMARK 500 1 ARG A 4 136.56 -173.17
REMARK 500 1 ALA A 5 -94.86 -78.24
REMARK 500 1 SER A 6 -156.63 -92.54
REMARK 500 1 VAL A 7 161.80 -43.90
REMARK 500 1 SER A 9 134.90 63.57
REMARK 500 1 LYS A 12 99.23 -36.19
REMARK 500 1 MET A 13 153.33 155.57
REMARK 500 1 TRP A 15 11.88 -68.42
REMARK 500 1 ILE A 20 164.26 -41.45
REMARK 500 1 SER A 21 -72.27 -84.53
REMARK 500 1 ARG A 22 -41.22 175.49
REMARK 500 1 SER A 33 122.52 72.83
REMARK 500 1 LYS A 34 -44.77 -150.97
REMARK 500 1 ASN A 46 -45.26 -145.66
REMARK 500 1 ASN A 47 46.21 -169.43
REMARK 500 1 HIS A 56 57.46 -108.00
REMARK 500 1 GLU A 57 110.66 55.87
REMARK 500 1 LYS A 67 -168.81 -110.17
REMARK 500 1 ASP A 68 50.41 -107.31
REMARK 500 1 LYS A 69 29.86 47.96
REMARK 500 1 LYS A 79 -138.83 -139.86
REMARK 500 1 ASP A 96 -9.82 71.90
REMARK 500 1 LEU A 98 -169.64 -52.31
REMARK 500 1 VAL A 101 175.75 -52.35
REMARK 500 1 THR A 103 -36.00 -152.11
REMARK 500 1 GLN A 107 161.65 -36.63
REMARK 500 1 ILE A 109 -70.05 -119.08
REMARK 500 1 THR A 111 -83.18 -88.51
REMARK 500 1 GLU B 3 -175.13 -55.59
REMARK 500 2 SER A 2 76.28 -109.04
REMARK 500 2 ARG A 4 133.07 -176.38
REMARK 500 2 ALA A 5 -92.08 -178.27
REMARK 500 2 VAL A 7 67.77 36.02
REMARK 500 2 HIS A 10 -37.97 -36.65
REMARK 500 2 TRP A 15 8.69 -69.41
REMARK 500 2 LYS A 19 -121.05 -110.90
REMARK 500 2 ILE A 20 162.54 52.45
REMARK 500 2 SER A 21 -68.30 -90.96
REMARK 500 2 ARG A 22 -45.91 171.46
REMARK 500 2 SER A 33 -144.32 62.85
REMARK 500 2 LYS A 34 -59.61 82.68
REMARK 500 2 THR A 35 4.30 -65.58
REMARK 500 2 ASN A 36 97.83 51.25
REMARK 500 2 ARG A 44 -90.49 -161.05
REMARK 500 2 ASP A 45 -122.95 -108.76
REMARK 500 2 ASN A 47 -88.13 -92.29
REMARK 500 2 HIS A 56 -86.80 -81.10
REMARK 500 2 ASP A 68 50.29 -117.31
REMARK 500 2 SER A 74 -156.26 -148.62
REMARK 500
REMARK 500 THIS ENTRY HAS 619 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 B 6
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CSZ RELATED DB: PDB
DBREF 1CSY A 10 112 UNP P43405 KSYK_HUMAN 163 265
DBREF 1CSY B 0 6 PDB 1CSY 1CSY 0 6
SEQRES 1 A 112 GLY SER ARG ARG ALA SER VAL GLY SER HIS GLU LYS MET
SEQRES 2 A 112 PRO TRP PHE HIS GLY LYS ILE SER ARG GLU GLU SER GLU
SEQRES 3 A 112 GLN ILE VAL LEU ILE GLY SER LYS THR ASN GLY LYS PHE
SEQRES 4 A 112 LEU ILE ARG ALA ARG ASP ASN ASN GLY SER TYR ALA LEU
SEQRES 5 A 112 CYS LEU LEU HIS GLU GLY LYS VAL LEU HIS TYR ARG ILE
SEQRES 6 A 112 ASP LYS ASP LYS THR GLY LYS LEU SER ILE PRO GLU GLY
SEQRES 7 A 112 LYS LYS PHE ASP THR LEU TRP GLN LEU VAL GLU HIS TYR
SEQRES 8 A 112 SER TYR LYS ALA ASP GLY LEU LEU ARG VAL LEU THR VAL
SEQRES 9 A 112 PRO CYS GLN LYS ILE GLY THR GLN
SEQRES 1 B 7 ACE THR PTR GLU THR LEU NH2
MODRES 1CSY PTR B 2 TYR O-PHOSPHOTYROSINE
HET ACE B 0 6
HET PTR B 2 24
HET NH2 B 6 3
HETNAM ACE ACETYL GROUP
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM NH2 AMINO GROUP
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 2 ACE C2 H4 O
FORMUL 2 PTR C9 H12 N O6 P
FORMUL 2 NH2 H2 N
HELIX 1 1 GLU A 23 ILE A 31 1 9
HELIX 2 2 LEU A 84 TYR A 93 1 10
SHEET 1 A 3 PHE A 39 ALA A 43 0
SHEET 2 A 3 TYR A 50 LEU A 55 -1 N CYS A 53 O LEU A 40
SHEET 3 A 3 LYS A 59 ILE A 65 -1 N ILE A 65 O TYR A 50
LINK C ACE B 0 N THR B 1 1555 1555 1.34
LINK N PTR B 2 C THR B 1 1555 1555 1.34
LINK C PTR B 2 N GLU B 3 1555 1555 1.33
LINK N NH2 B 6 C LEU B 5 1555 1555 1.35
SITE 1 AC2 3 GLU A 77 THR B 4 LEU B 5
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
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END