Header list of 1aou.pdb file
Complete list - v 3 2 Bytes
HEADER COMPLEX (PROTO-ONCOGENE/EARLY PROTEIN) 10-JUL-97 1AOU
TITLE NMR STRUCTURE OF THE FYN SH2 DOMAIN COMPLEXED WITH A PHOSPHOTYROSYL
TITLE 2 PEPTIDE, 22 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FYN PROTEIN-TYROSINE KINASE;
COMPND 3 CHAIN: F;
COMPND 4 FRAGMENT: SH2 DOMAIN;
COMPND 5 SYNONYM: SRC HOMOLOGY 2 DOMAIN;
COMPND 6 EC: 2.7.1.112;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: PHOSPHOTYROSYL PEPTIDE;
COMPND 11 CHAIN: P
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 GENE: LYSS;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PRK172;
SOURCE 12 EXPRESSION_SYSTEM_GENE: LYSS;
SOURCE 13 MOL_ID: 2;
SOURCE 14 ORGANISM_SCIENTIFIC: HAMSTER POLYOMAVIRUS;
SOURCE 15 ORGANISM_TAXID: 10626
KEYWDS SH2 DOMAIN, SIGNAL TRANSDUCTION, PEPTIDE COMPLEX, COMPLEX (PROTO-
KEYWDS 2 ONCOGENE-EARLY PROTEIN), COMPLEX (PROTO-ONCOGENE-EARLY PROTEIN)
KEYWDS 3 COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 22
AUTHOR T.D.MULHERN,G.L.SHAW,C.J.MORTON,A.J.DAY,I.D.CAMPBELL
REVDAT 3 03-NOV-21 1AOU 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1AOU 1 VERSN
REVDAT 1 14-JAN-98 1AOU 0
JRNL AUTH T.D.MULHERN,G.L.SHAW,C.J.MORTON,A.J.DAY,I.D.CAMPBELL
JRNL TITL THE SH2 DOMAIN FROM THE TYROSINE KINASE FYN IN COMPLEX WITH
JRNL TITL 2 A PHOSPHOTYROSYL PEPTIDE REVEALS INSIGHTS INTO DOMAIN
JRNL TITL 3 STABILITY AND BINDING SPECIFICITY.
JRNL REF STRUCTURE V. 5 1313 1997
JRNL REFN ISSN 0969-2126
JRNL PMID 9351806
JRNL DOI 10.1016/S0969-2126(97)00283-9
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.PINTAR,M.HENSMANN,K.JUMEL,M.PITKEATHLY,S.E.HARDING,
REMARK 1 AUTH 2 I.D.CAMPBELL
REMARK 1 TITL SOLUTION STUDIES OF THE SH2 DOMAIN FROM THE FYN TYROSINE
REMARK 1 TITL 2 KINASE: SECONDARY STRUCTURE, BACKBONE DYNAMICS AND PROTEIN
REMARK 1 TITL 3 ASSOCIATION
REMARK 1 REF EUR.BIOPHYS.J. V. 24 371 1996
REMARK 1 REFN ISSN 0175-7571
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1AOU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171075.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQF-COSY; TOCSY; HSQC;
REMARK 210 NOESY-HSQC; TOCSY-HSQC; CBCA(CO)
REMARK 210 NH; HCCH-TOCSY; XF-NOESY; XF-
REMARK 210 TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : OMEGA
REMARK 210 SPECTROMETER MANUFACTURER : HOME-BUILT
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DYNAMICAL SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST VIOLATIONS
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: F, P
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 1 ILE F 2 -92.77 -43.69
REMARK 500 1 GLN F 3 -97.16 -89.28
REMARK 500 1 ALA F 4 -47.88 -167.75
REMARK 500 1 GLU F 5 33.65 166.48
REMARK 500 1 LYS F 11 71.43 -107.00
REMARK 500 1 ARG F 19 -77.52 -66.96
REMARK 500 1 ARG F 28 176.86 -48.79
REMARK 500 1 ARG F 34 154.35 175.63
REMARK 500 1 ASP F 52 32.84 -83.89
REMARK 500 1 MET F 53 39.69 -161.78
REMARK 500 1 LYS F 54 -28.78 178.94
REMARK 500 1 VAL F 58 118.93 -160.04
REMARK 500 1 TYR F 72 125.81 178.00
REMARK 500 1 PHE F 79 -158.90 -148.83
REMARK 500 1 ALA F 94 -8.34 81.53
REMARK 500 1 SER F 98 -167.05 164.15
REMARK 500 1 ARG F 99 -151.07 -61.29
REMARK 500 1 LEU F 100 -163.22 -118.61
REMARK 500 1 SER F 104 51.60 -106.43
REMARK 500 1 GLN P 203 -173.25 57.80
REMARK 500 1 ILE P 209 -36.61 -167.70
REMARK 500 1 TYR P 210 -171.13 -58.64
REMARK 500 2 GLU F 5 -12.01 147.27
REMARK 500 2 GLU F 6 -58.49 -130.08
REMARK 500 2 LYS F 11 72.10 -105.70
REMARK 500 2 ARG F 19 -75.79 -65.96
REMARK 500 2 PRO F 27 -159.35 -78.09
REMARK 500 2 ARG F 34 162.03 173.64
REMARK 500 2 ASP F 52 36.59 -84.07
REMARK 500 2 MET F 53 36.35 -161.86
REMARK 500 2 LYS F 54 -28.42 178.01
REMARK 500 2 VAL F 58 115.91 -160.23
REMARK 500 2 ALA F 94 -12.37 95.33
REMARK 500 2 LEU F 100 -170.59 -50.81
REMARK 500 2 PRO F 103 -159.62 -79.39
REMARK 500 2 SER F 104 76.96 -153.05
REMARK 500 2 HIS F 105 -151.52 -67.77
REMARK 500 2 PTR P 204 118.15 60.93
REMARK 500 2 PRO P 208 -169.84 -78.82
REMARK 500 2 ILE P 209 -34.72 -175.32
REMARK 500 2 TYR P 210 -173.44 -55.66
REMARK 500 3 ALA F 4 84.30 42.74
REMARK 500 3 GLU F 5 -37.31 -164.70
REMARK 500 3 GLU F 6 -36.03 -136.66
REMARK 500 3 LYS F 11 67.72 -104.39
REMARK 500 3 ARG F 19 -74.04 -63.77
REMARK 500 3 PHE F 24 96.18 -44.01
REMARK 500 3 PRO F 27 -169.48 -78.06
REMARK 500 3 ARG F 28 158.58 -45.25
REMARK 500 3 ARG F 34 140.46 174.67
REMARK 500
REMARK 500 THIS ENTRY HAS 459 RAMACHANDRAN OUTLIERS.
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 1 ARG F 14 0.10 SIDE CHAIN
REMARK 500 1 ARG F 19 0.27 SIDE CHAIN
REMARK 500 1 ARG F 28 0.25 SIDE CHAIN
REMARK 500 1 ARG F 34 0.19 SIDE CHAIN
REMARK 500 1 ARG F 48 0.32 SIDE CHAIN
REMARK 500 1 ARG F 64 0.15 SIDE CHAIN
REMARK 500 1 ARG F 76 0.22 SIDE CHAIN
REMARK 500 1 ARG F 92 0.15 SIDE CHAIN
REMARK 500 1 ARG F 99 0.31 SIDE CHAIN
REMARK 500 2 ARG F 14 0.25 SIDE CHAIN
REMARK 500 2 ARG F 19 0.28 SIDE CHAIN
REMARK 500 2 ARG F 28 0.13 SIDE CHAIN
REMARK 500 2 ARG F 48 0.14 SIDE CHAIN
REMARK 500 2 ARG F 64 0.17 SIDE CHAIN
REMARK 500 2 ARG F 76 0.30 SIDE CHAIN
REMARK 500 2 ARG F 92 0.26 SIDE CHAIN
REMARK 500 2 ARG F 99 0.22 SIDE CHAIN
REMARK 500 3 ARG F 14 0.25 SIDE CHAIN
REMARK 500 3 ARG F 19 0.21 SIDE CHAIN
REMARK 500 3 ARG F 28 0.31 SIDE CHAIN
REMARK 500 3 ARG F 34 0.08 SIDE CHAIN
REMARK 500 3 ARG F 48 0.08 SIDE CHAIN
REMARK 500 3 ARG F 64 0.12 SIDE CHAIN
REMARK 500 3 ARG F 76 0.28 SIDE CHAIN
REMARK 500 3 ARG F 92 0.24 SIDE CHAIN
REMARK 500 3 ARG F 99 0.22 SIDE CHAIN
REMARK 500 4 ARG F 14 0.32 SIDE CHAIN
REMARK 500 4 ARG F 19 0.32 SIDE CHAIN
REMARK 500 4 ARG F 28 0.21 SIDE CHAIN
REMARK 500 4 ARG F 34 0.20 SIDE CHAIN
REMARK 500 4 ARG F 48 0.25 SIDE CHAIN
REMARK 500 4 ARG F 64 0.11 SIDE CHAIN
REMARK 500 4 ARG F 76 0.22 SIDE CHAIN
REMARK 500 4 ARG F 92 0.17 SIDE CHAIN
REMARK 500 4 ARG F 99 0.32 SIDE CHAIN
REMARK 500 5 ARG F 14 0.08 SIDE CHAIN
REMARK 500 5 ARG F 19 0.14 SIDE CHAIN
REMARK 500 5 ARG F 28 0.30 SIDE CHAIN
REMARK 500 5 ARG F 34 0.25 SIDE CHAIN
REMARK 500 5 ARG F 48 0.16 SIDE CHAIN
REMARK 500 5 ARG F 64 0.31 SIDE CHAIN
REMARK 500 5 ARG F 76 0.23 SIDE CHAIN
REMARK 500 5 ARG F 92 0.31 SIDE CHAIN
REMARK 500 5 ARG F 99 0.17 SIDE CHAIN
REMARK 500 6 ARG F 14 0.17 SIDE CHAIN
REMARK 500 6 ARG F 19 0.31 SIDE CHAIN
REMARK 500 6 ARG F 28 0.31 SIDE CHAIN
REMARK 500 6 ARG F 34 0.16 SIDE CHAIN
REMARK 500 6 ARG F 48 0.23 SIDE CHAIN
REMARK 500 6 ARG F 64 0.16 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 188 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: PTR
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: PHOSPHOTYROSINE BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: 3IB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: +3 ILE BINDING SITE.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AOT RELATED DB: PDB
REMARK 900 REPRESENTATIVE STRUCTURE
DBREF 1AOU F 1 106 UNP P06241 FYN_HUMAN 142 247
DBREF 1AOU P 201 211 UNP P03079 TAMI_POVHA 321 331
SEQADV 1AOU SER F 97 UNP P06241 CYS 238 ENGINEERED MUTATION
SEQADV 1AOU SER F 98 UNP P06241 CYS 239 ENGINEERED MUTATION
SEQADV 1AOU SER F 104 UNP P06241 CYS 245 ENGINEERED MUTATION
SEQRES 1 F 106 SER ILE GLN ALA GLU GLU TRP TYR PHE GLY LYS LEU GLY
SEQRES 2 F 106 ARG LYS ASP ALA GLU ARG GLN LEU LEU SER PHE GLY ASN
SEQRES 3 F 106 PRO ARG GLY THR PHE LEU ILE ARG GLU SER GLU THR THR
SEQRES 4 F 106 LYS GLY ALA TYR SER LEU SER ILE ARG ASP TRP ASP ASP
SEQRES 5 F 106 MET LYS GLY ASP HIS VAL LYS HIS TYR LYS ILE ARG LYS
SEQRES 6 F 106 LEU ASP ASN GLY GLY TYR TYR ILE THR THR ARG ALA GLN
SEQRES 7 F 106 PHE GLU THR LEU GLN GLN LEU VAL GLN HIS TYR SER GLU
SEQRES 8 F 106 ARG ALA ALA GLY LEU SER SER ARG LEU VAL VAL PRO SER
SEQRES 9 F 106 HIS LYS
SEQRES 1 P 11 GLU PRO GLN PTR GLU GLU ILE PRO ILE TYR LEU
MODRES 1AOU PTR P 204 TYR O-PHOSPHOTYROSINE
HET PTR P 204 23
HETNAM PTR O-PHOSPHOTYROSINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 2 PTR C9 H12 N O6 P
HELIX 1 1 ARG F 14 SER F 23 1 10
HELIX 2 2 LEU F 82 GLU F 91 1 10
SHEET 1 A 2 SER F 46 ARG F 48 0
SHEET 2 A 2 VAL F 58 HIS F 60 -1 N LYS F 59 O ILE F 47
SHEET 1 B 2 TYR F 71 THR F 74 0
SHEET 2 B 2 ALA F 77 PHE F 79 -1 N PHE F 79 O TYR F 71
LINK C GLN P 203 N PTR P 204 1555 1555 1.30
LINK C PTR P 204 N GLU P 205 1555 1555 1.31
SITE 1 PTR 7 ARG F 34 SER F 36 THR F 38 SER F 44
SITE 2 PTR 7 HIS F 60 TYR F 61 LYS F 62
SITE 1 3IB 5 TYR F 61 ILE F 73 THR F 74 GLY F 95
SITE 2 3IB 5 LEU F 96
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
Complete list - v 3 2 Bytes