BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 16219

Title: Solution structure of SH3 domain of PTK6   PubMed: 19401189

Deposition date: 2009-03-18 Original release date: 2009-10-16

Authors: Lee, Weontae; Ko, Sunggeon

Citation: Ko, Sunggeon; Ahn, Kyo-Eun; Lee, Young-Min; Ahn, Hee-Chul; Lee, Weontae. "Structural basis of the auto-inhibition mechanism of nonreceptor tyrosine kinase PTK6."  Biochem. Biophys. Res. Commun. 384, 236-242 (2009).

Assembly members:
SH_domain, polymer, 72 residues, 8334.291 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
SH_domain: MVSRDQAHLGPKYVGLWDFK SRTDEELSFRAGDVFHVARK EEQWWWATLLDEAGGAVAQG YVPHNYLAERET

Data sets:
Data typeCount
13C chemical shifts256
15N chemical shifts72
1H chemical shifts440

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1SH_domain1

Entities:

Entity 1, SH_domain 72 residues - 8334.291 Da.

1   METVALSERARGASPGLNALAHISLEUGLY
2   PROLYSTYRVALGLYLEUTRPASPPHELYS
3   SERARGTHRASPGLUGLULEUSERPHEARG
4   ALAGLYASPVALPHEHISVALALAARGLYS
5   GLUGLUGLNTRPTRPTRPALATHRLEULEU
6   ASPGLUALAGLYGLYALAVALALAGLNGLY
7   TYRVALPROHISASNTYRLEUALAGLUARG
8   GLUTHR

Samples:

sample_1: SH domain, [U-99% 15N], 0.2 mM; H2O 90%; D2O 10%

sample_2: SH domain, [U-99% 13C; U-99% 15N], 0.2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

CYANA v2.2.5, P.GUNTERT ET AL. - refinement, structure solution

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, peak picking

Molmol, Koradi, Billeter and Wuthrich - structure analysis

PyMol, DeLano Scientific LLC. - peak picking, structure analysis

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Varian INOVA 900 MHz

Related Database Links:

PDB
DBJ BAG37660 BAG63163 BAI45737
EMBL CAA55295
GB AAC34935 AAH35843 EAW75262 EAW75263 EHH19516
REF NP_001243287 NP_005966 XP_003280201 XP_003809959 XP_003904548
SP Q13882

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts