BMRB Entry 11573

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11573

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Title:
Solution structure of the human BMX SH2 domain
Deposition date:
2014-07-31
Original release date:
2018-12-11
Authors:
Kasai, Takuma; Koshiba, Seizo; Watanabe, Satoru; Harada, Takushi; Kigawa, Takanori; Yokoyama, Shigeyuki
Citation:

Citation: Kasai, Takuma; Koshiba, Seizo; Yokoyama, Jun; Kigawa, Takanori. "Stable isotope labeling strategy based on coding theory."  J. Biomol. NMR 63, 213-221 (2015).
PubMed: 26293126

Assembly members:

Assembly members:
BMX_SH2_domain, polymer, 110 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P061225-65

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BMX_SH2_domain: GSSGSSGLDDYDWFAGNISR SQSEQLLRQKGKEGAFMVRN SSQVGMYTVSLFSKAVNDKK GTVKHYHVHTNAENKLYLAE NYCFDSIPKLIHYHQHNSAG MITRLRHPVS

Data sets:
Data typeCount
13C chemical shifts468
15N chemical shifts116
1H chemical shifts739

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BMX SH2 domain1

Entities:

Entity 1, BMX SH2 domain 110 residues - Formula weight is not available

Residues 1-7 represent a non-native cloning artifact. This is the SH2 domain of human BMX protein.

1   GLYSERSERGLYSERSERGLYLEUASPASP
2   TYRASPTRPPHEALAGLYASNILESERARG
3   SERGLNSERGLUGLNLEULEUARGGLNLYS
4   GLYLYSGLUGLYALAPHEMETVALARGASN
5   SERSERGLNVALGLYMETTYRTHRVALSER
6   LEUPHESERLYSALAVALASNASPLYSLYS
7   GLYTHRVALLYSHISTYRHISVALHISTHR
8   ASNALAGLUASNLYSLEUTYRLEUALAGLU
9   ASNTYRCYSPHEASPSERILEPROLYSLEU
10   ILEHISTYRHISGLNHISASNSERALAGLY
11   METILETHRARGLEUARGHISPROVALSER

Samples:

sample_1: BMX SH2 domain, [U-13C; U-15N], 1.13 mM; Tris-Cl, [U-2H], 20 mM; sodium chloride 100 mM; DTT, [U-2H], 1 mM; sodium azide 0.02 % (w/v); H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

xwinnmr v3.5, Bruker Biospin - collection

NMRPipe v20031121, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v5.0.4, Johnson, One Moon Scientific - data analysis, peak picking

Kujira v0.9810, Naohiro Kobayashi - chemical shift assignment, data analysis, peak picking

CYANA v2.0.17, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

UNP P51813
AlphaFold Q12871

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