Header list of 1jeg.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSFERASE/HYDROLASE 17-JUN-01 1JEG
TITLE SOLUTION STRUCTURE OF THE SH3 DOMAIN FROM C-TERMINAL SRC KINASE
TITLE 2 COMPLEXED WITH A PEPTIDE FROM THE TYROSINE PHOSPHATASE PEP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE CSK;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN;
COMPND 5 SYNONYM: C-SRC KINASE, PROTEIN-TYROSINE KINASE CYL;
COMPND 6 EC: 2.7.1.112;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: HEMATOPOIETIC CELL PROTEIN-TYROSINE PHOSPHATASE 70Z-PEP;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: 25 RESIDUE PEPTIDE (RESIDUES 612-629);
COMPND 12 EC: 3.1.3.48;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 9 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 10 ORGANISM_TAXID: 10090;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SH3 DOMAIN, PROTEIN-PEPTIDE COMPLEX, TYROSINE PHOSPHATASE, KINASE,
KEYWDS 2 TRANSFERASE-HYDROLASE COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR R.GHOSE,A.SHEKHTMAN,M.J.GOGER,H.JI,D.COWBURN
REVDAT 4 23-FEB-22 1JEG 1 REMARK
REVDAT 3 24-FEB-09 1JEG 1 VERSN
REVDAT 2 01-APR-03 1JEG 1 JRNL
REVDAT 1 31-OCT-01 1JEG 0
JRNL AUTH R.GHOSE,A.SHEKHTMAN,M.J.GOGER,H.JI,D.COWBURN
JRNL TITL A NOVEL, SPECIFIC INTERACTION INVOLVING THE CSK SH3 DOMAIN
JRNL TITL 2 AND ITS NATURAL LIGAND.
JRNL REF NAT.STRUCT.BIOL. V. 8 998 2001
JRNL REFN ISSN 1072-8368
JRNL PMID 11685249
JRNL DOI 10.1038/NSB1101-998
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5
REMARK 3 AUTHORS : GUENTERT, MUMENTHALER, HERMANN (DYANA), GUENTERT,
REMARK 3 MUMENTHALER, HERMANN (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JEG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUN-01.
REMARK 100 THE DEPOSITION ID IS D_1000013680.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSIONAL
REMARK 210 ANGLE DYNMAICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
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: 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 MODELS 1-25
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 ALA A 3
REMARK 465 ILE A 4
REMARK 465 GLN A 5
REMARK 465 ALA A 6
REMARK 465 ALA A 7
REMARK 465 TRP A 8
REMARK 465 PRO A 9
REMARK 465 GLY A 70
REMARK 465 VAL A 71
REMARK 465 LYS A 72
REMARK 465 ALA A 73
REMARK 465 GLY A 74
REMARK 465 THR A 75
REMARK 465 LYS A 76
REMARK 465 LEU A 77
REMARK 465 SER A 78
REMARK 465 LEU A 79
REMARK 465 MET A 80
REMARK 465 PRO A 81
REMARK 465 TRP A 82
REMARK 465 PHE A 83
REMARK 465 SER B 1
REMARK 465 ARG B 2
REMARK 465 ARG B 3
REMARK 465 THR B 4
REMARK 465 ASP B 5
REMARK 465 ASP B 6
REMARK 465 GLU B 7
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
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 ASN A 19 72.87 -106.35
REMARK 500 1 LYS A 32 124.73 -36.09
REMARK 500 1 PRO A 45 -82.72 -75.02
REMARK 500 1 ASN A 46 -35.04 -33.63
REMARK 500 1 LEU B 12 175.88 -48.99
REMARK 500 2 ASN A 46 -33.90 75.09
REMARK 500 2 LEU B 12 174.26 -47.05
REMARK 500 3 LYS A 32 134.08 -35.71
REMARK 500 3 PRO A 45 -77.29 -75.02
REMARK 500 3 ASN A 46 -36.04 -33.15
REMARK 500 3 ARG A 68 -30.83 -37.86
REMARK 500 3 LEU B 12 174.86 -48.52
REMARK 500 4 ASN A 19 76.35 -116.72
REMARK 500 4 HIS A 21 175.21 -59.37
REMARK 500 4 LYS A 32 145.25 -39.52
REMARK 500 4 PRO A 45 -90.55 -74.98
REMARK 500 4 ASN A 46 41.91 -86.64
REMARK 500 4 LEU B 12 176.06 -48.92
REMARK 500 5 ASN A 46 29.44 38.36
REMARK 500 5 LEU B 12 175.28 -48.47
REMARK 500 6 LYS A 32 125.71 -39.61
REMARK 500 6 PRO A 45 -82.61 -75.03
REMARK 500 6 ASN A 46 -40.88 -27.20
REMARK 500 6 LEU B 12 174.59 -48.32
REMARK 500 7 PRO A 45 -79.02 -75.04
REMARK 500 7 ASN A 46 -35.11 -33.54
REMARK 500 7 ARG A 68 -32.55 -39.16
REMARK 500 7 LEU B 12 175.87 -48.40
REMARK 500 8 ASN A 19 72.54 -119.98
REMARK 500 8 HIS A 21 41.35 -89.24
REMARK 500 8 PRO A 45 -81.58 -74.91
REMARK 500 8 ASN A 46 -35.99 -33.04
REMARK 500 8 LEU B 12 175.40 -48.43
REMARK 500 9 HIS A 21 37.55 -89.23
REMARK 500 9 LYS A 32 128.74 -39.69
REMARK 500 9 PRO A 45 -82.73 -75.02
REMARK 500 9 ASN A 46 -35.67 -32.99
REMARK 500 9 LEU B 12 174.34 -48.05
REMARK 500 9 ARG B 15 89.77 -68.40
REMARK 500 10 PRO A 45 -81.87 -75.03
REMARK 500 10 LEU B 12 174.70 -47.76
REMARK 500 11 LYS A 32 126.21 -37.26
REMARK 500 11 PRO A 45 -80.40 -74.84
REMARK 500 11 ASN A 46 -37.15 -31.48
REMARK 500 11 LEU B 12 175.38 -47.70
REMARK 500 12 ASN A 46 31.60 37.92
REMARK 500 12 LEU B 12 175.44 -47.94
REMARK 500 13 ASP A 27 -170.24 -62.98
REMARK 500 13 ASN A 46 42.84 -75.87
REMARK 500 13 LEU B 12 174.59 -48.16
REMARK 500
REMARK 500 THIS ENTRY HAS 96 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JEG A 1 83 UNP P41241 CSK_MOUSE 1 83
DBREF 1JEG B 1 25 UNP P29352 PTN8_MOUSE 605 629
SEQRES 1 A 83 MET SER ALA ILE GLN ALA ALA TRP PRO SER GLY THR GLU
SEQRES 2 A 83 CYS ILE ALA LYS TYR ASN PHE HIS GLY THR ALA GLU GLN
SEQRES 3 A 83 ASP LEU PRO PHE CYS LYS GLY ASP VAL LEU THR ILE VAL
SEQRES 4 A 83 ALA VAL THR LYS ASP PRO ASN TRP TYR LYS ALA LYS ASN
SEQRES 5 A 83 LYS VAL GLY ARG GLU GLY ILE ILE PRO ALA ASN TYR VAL
SEQRES 6 A 83 GLN LYS ARG GLU GLY VAL LYS ALA GLY THR LYS LEU SER
SEQRES 7 A 83 LEU MET PRO TRP PHE
SEQRES 1 B 25 SER ARG ARG THR ASP ASP GLU ILE PRO PRO PRO LEU PRO
SEQRES 2 B 25 GLU ARG THR PRO GLU SER PHE ILE VAL VAL GLU GLU
HELIX 1 1 THR B 16 ILE B 21 5 6
SHEET 1 A 5 GLU A 57 PRO A 61 0
SHEET 2 A 5 TRP A 47 LYS A 51 -1 O TYR A 48 N ILE A 60
SHEET 3 A 5 VAL A 35 VAL A 41 -1 O THR A 37 N LYS A 51
SHEET 4 A 5 GLU A 13 ALA A 16 -1 N CYS A 14 O LEU A 36
SHEET 5 A 5 VAL A 65 LYS A 67 -1 N GLN A 66 O ILE A 15
CRYST1 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
Complete list - b 23 2 Bytes