BMRB Entry 16353

Title:
SOLUTION STRUCTURE OF SH2 DOMAIN OF PROTO-ONCOGENE TYROSINE-PROTEIN KINASE FER FROM HOMO SAPIENS, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET HR3461D
Deposition date:
2009-06-15
Original release date:
2009-08-06
Authors:
Tang, Yuefeng; Wang, Dongyan; Nwosu, Chioma; Owens, Leah; Xiao, Rong; Liu, Jinfeng; Baran, Micheal; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano
Citation:

Citation: Tang, Yuefeng; Montelione, Gaetano. "SOLUTION STRUCTURE OF SH2 DOMAIN OF PROTO-ONCOGENE TYROSINE-PROTEIN KINASE FER FROM HOMO SAPIENS, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET HR3461D"  .

Assembly members:

Assembly members:
SH2 domain, polymer, 116 residues, 13645.706 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 14-15C

Data sets:
Data typeCount
13C chemical shifts500
15N chemical shifts115
1H chemical shifts796

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SH2 domain1

Entities:

Entity 1, SH2 domain 116 residues - 13645.706 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   METLYSPROLEUALAGLUGLNASPTRPTYR
3   HISGLYALAILEPROARGILEGLUALAGLN
4   GLULEULEULYSLYSGLNGLYASPPHELEU
5   VALARGGLUSERHISGLYLYSPROGLYGLU
6   TYRVALLEUSERVALTYRSERASPGLYGLN
7   ARGARGHISPHEILEILEGLNTYRVALASP
8   ASNMETTYRARGPHEGLUGLYTHRGLYPHE
9   SERASNILEPROGLNLEUILEASPHISHIS
10   TYRTHRTHRLYSGLNVALILETHRLYSLYS
11   SERGLYVALVALLEULEUASNPROILEPRO
12   LYSASPLYSLYSTRPILE

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1.03 mM; H2O 95%; D2O 5%

sample_2: entity, [U-10% 13C; U-100% 15N], 1.20 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis

SPARKY v2.1, Goddard - chemical shift assignment, data analysis, peak picking

NMRPipe v2.1, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN v2.1, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAG37661 BAG61714 BAJ20192 BAO24701 BAO24702
GB AAA61190 AAI41560 AEY69041 EAW49055 EHH54435
REF NP_001294957 NP_001294960 NP_005237 XP_001099988 XP_001140014
SP P16591
AlphaFold P16591

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks