HEADER SIGNALING PROTEIN 31-JUL-06 2DVJ
TITLE PHOSPHORYLATED CRK-II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: V-CRK SARCOMA VIRUS CT10 ONCOGENE HOMOLOG, ISOFORM A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-228;
COMPND 5 SYNONYM: V-CRK SARCOMA VIRUS CT10 ONCOGENE HOMOLOG, AVIAN,
COMPND 6 PHOSPHORYLATED CRK-II;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CRK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL-21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22
KEYWDS SH3, SH2, SIGNAL TRANSDUCTION, ADAPTER MOLECULE, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR Y.KOBASHIGAWA,F.INAGAKI
REVDAT 4 09-MAR-22 2DVJ 1 REMARK SEQADV LINK
REVDAT 3 08-JUL-08 2DVJ 1 JRNL VERSN
REVDAT 2 05-JUN-07 2DVJ 1 JRNL
REVDAT 1 08-MAY-07 2DVJ 0
JRNL AUTH Y.KOBASHIGAWA,M.SAKAI,M.NAITO,M.YOKOCHI,H.KUMETA,Y.MAKINO,
JRNL AUTH 2 K.OGURA,S.TANAKA,F.INAGAKI
JRNL TITL STRUCTURAL BASIS FOR THE TRANSFORMING ACTIVITY OF HUMAN
JRNL TITL 2 CANCER-RELATED SIGNALING ADAPTOR PROTEIN CRK.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 14 503 2007
JRNL REFN ISSN 1545-9993
JRNL PMID 17515907
JRNL DOI 10.1038/NSMB1241
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER AT
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DVJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-AUG-06.
REMARK 100 THE DEPOSITION ID IS D_1000025894.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8MM PYCRK-II (1-228) U
REMARK 210 -15N,13C; 200MM NACL, 50MM
REMARK 210 PHOSPHATE BUFFER NA; 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 2.0
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 ALA A 0
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 O TYR A 104 H LEU A 114 1.59
REMARK 500 H ARG A 162 O ASN A 171 1.59
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 ALA A 2 -61.25 71.88
REMARK 500 ASN A 4 38.66 -141.06
REMARK 500 SER A 11 -42.18 -132.56
REMARK 500 ARG A 17 58.01 -110.94
REMARK 500 ARG A 31 -148.60 -159.04
REMARK 500 SER A 40 110.11 57.15
REMARK 500 SER A 43 67.95 -112.45
REMARK 500 SER A 52 95.43 -35.84
REMARK 500 GLU A 53 -82.42 -92.51
REMARK 500 ASN A 54 -142.23 -109.81
REMARK 500 VAL A 57 -152.23 -99.73
REMARK 500 PRO A 67 87.28 -58.36
REMARK 500 PRO A 69 -175.31 -58.99
REMARK 500 VAL A 71 -41.30 102.33
REMARK 500 SER A 74 65.44 172.63
REMARK 500 GLN A 77 -59.33 -160.99
REMARK 500 ILE A 89 -96.58 -91.98
REMARK 500 PHE A 94 -115.79 -147.27
REMARK 500 ASP A 95 -69.26 -105.58
REMARK 500 SER A 96 -162.11 -125.29
REMARK 500 ILE A 106 33.14 -156.45
REMARK 500 TYR A 108 98.42 63.23
REMARK 500 THR A 111 70.94 139.46
REMARK 500 THR A 112 -18.06 170.60
REMARK 500 THR A 113 157.00 61.27
REMARK 500 ILE A 115 -158.60 -121.25
REMARK 500 SER A 119 -165.97 58.09
REMARK 500 SER A 121 -65.01 66.48
REMARK 500 ARG A 122 -102.38 -174.57
REMARK 500 GLN A 123 -76.29 -140.47
REMARK 500 SER A 125 -89.66 -55.45
REMARK 500 VAL A 127 -177.87 -57.56
REMARK 500 ARG A 130 80.41 50.45
REMARK 500 TYR A 136 93.13 166.55
REMARK 500 VAL A 137 140.88 179.86
REMARK 500 ALA A 139 160.02 -37.56
REMARK 500 LEU A 140 20.28 -144.36
REMARK 500 PRO A 152 -74.39 -89.71
REMARK 500 PHE A 153 162.65 58.20
REMARK 500 ASN A 171 122.18 -36.40
REMARK 500 SER A 175 0.39 -59.49
REMARK 500 PRO A 185 10.00 -66.65
REMARK 500 ALA A 193 34.66 -179.42
REMARK 500 SER A 194 47.24 -153.32
REMARK 500 SER A 196 -174.45 62.54
REMARK 500 SER A 198 175.83 65.59
REMARK 500 ALA A 199 -45.41 -158.73
REMARK 500 LEU A 200 -53.69 77.67
REMARK 500 GLN A 205 29.48 -144.72
REMARK 500 GLN A 211 149.95 60.76
REMARK 500
REMARK 500 THIS ENTRY HAS 55 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2EYV RELATED DB: PDB
REMARK 900 RELATED ID: 2EYW RELATED DB: PDB
REMARK 900 RELATED ID: 2EYX RELATED DB: PDB
REMARK 900 RELATED ID: 2EYY RELATED DB: PDB
REMARK 900 RELATED ID: 2EYZ RELATED DB: PDB
DBREF 2DVJ A 1 228 UNP Q96HJ0 Q96HJ0_HUMAN 1 228
SEQADV 2DVJ GLY A -1 UNP Q96HJ0 EXPRESSION TAG
SEQADV 2DVJ ALA A 0 UNP Q96HJ0 EXPRESSION TAG
SEQRES 1 A 230 GLY ALA MET ALA GLY ASN PHE ASP SER GLU GLU ARG SER
SEQRES 2 A 230 SER TRP TYR TRP GLY ARG LEU SER ARG GLN GLU ALA VAL
SEQRES 3 A 230 ALA LEU LEU GLN GLY GLN ARG HIS GLY VAL PHE LEU VAL
SEQRES 4 A 230 ARG ASP SER SER THR SER PRO GLY ASP TYR VAL LEU SER
SEQRES 5 A 230 VAL SER GLU ASN SER ARG VAL SER HIS TYR ILE ILE ASN
SEQRES 6 A 230 SER SER GLY PRO ARG PRO PRO VAL PRO PRO SER PRO ALA
SEQRES 7 A 230 GLN PRO PRO PRO GLY VAL SER PRO SER ARG LEU ARG ILE
SEQRES 8 A 230 GLY ASP GLN GLU PHE ASP SER LEU PRO ALA LEU LEU GLU
SEQRES 9 A 230 PHE TYR LYS ILE HIS TYR LEU ASP THR THR THR LEU ILE
SEQRES 10 A 230 GLU PRO VAL SER ARG SER ARG GLN GLY SER GLY VAL ILE
SEQRES 11 A 230 LEU ARG GLN GLU GLU ALA GLU TYR VAL ARG ALA LEU PHE
SEQRES 12 A 230 ASP PHE ASN GLY ASN ASP GLU GLU ASP LEU PRO PHE LYS
SEQRES 13 A 230 LYS GLY ASP ILE LEU ARG ILE ARG ASP LYS PRO GLU GLU
SEQRES 14 A 230 GLN TRP TRP ASN ALA GLU ASP SER GLU GLY LYS ARG GLY
SEQRES 15 A 230 MET ILE PRO VAL PRO TYR VAL GLU LYS TYR ARG PRO ALA
SEQRES 16 A 230 SER ALA SER VAL SER ALA LEU ILE GLY GLY ASN GLN GLU
SEQRES 17 A 230 GLY SER HIS PRO GLN PRO LEU GLY GLY PRO GLU PRO GLY
SEQRES 18 A 230 PRO PTR ALA GLN PRO SER VAL ASN THR
MODRES 2DVJ PTR A 221 TYR O-PHOSPHOTYROSINE
HET PTR A 221 24
HETNAM PTR O-PHOSPHOTYROSINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 PTR C9 H12 N O6 P
HELIX 1 1 GLN A 21 GLN A 28 1 8
HELIX 2 2 SER A 96 GLU A 102 1 7
HELIX 3 3 PRO A 185 VAL A 187 5 3
SHEET 1 A 3 LEU A 36 ARG A 38 0
SHEET 2 A 3 VAL A 48 SER A 50 -1 O SER A 50 N LEU A 36
SHEET 3 A 3 TYR A 60 ILE A 61 -1 O TYR A 60 N LEU A 49
SHEET 1 B 2 LEU A 87 ARG A 88 0
SHEET 2 B 2 GLU A 93 PHE A 94 -1 O PHE A 94 N LEU A 87
SHEET 1 C 2 TRP A 169 GLU A 173 0
SHEET 2 C 2 ARG A 179 PRO A 183 -1 O GLY A 180 N ALA A 172
LINK C PRO A 220 N PTR A 221 1555 1555 1.33
LINK C PTR A 221 N ALA A 222 1555 1555 1.33
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
