BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17065

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the Binary Tandem Ubiquitin Binding Domains of Signal Transducing Adapter Molecule 1   PubMed: 20927613

Deposition date: 2010-07-17 Original release date: 2010-10-14

Authors: Ahn, Hee-Chul; Lim, Jongsoo; Hong, Yoon-Hun; Lee, Bong-Jin

Citation: Lim, Jongsoo; Hong, Yoon-Hun; Lee, Bong-Jin; Ahn, Hee-Chul. "Backbone (1)H, (13)C, and (15)N assignments for the tandem ubiquitin binding domains of signal transducing adapter molecule 1."  Biomol. NMR Assignments 5, 51-54 (2011).

Assembly members:
Tandem_ubiquitin_binding_domains_of_STAM1, polymer, 191 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):
Tandem_ubiquitin_binding_domains_of_STAM1: MPLFATNPFDQDVEKATSEM NTAEDWGLILDICDKVGQSR TGPKDCLRSIMRRVNHKDPH VAMQALTLLGACVSNCGKIF HLEVCSRDFASEVSNVLNKG HPKVCEKLKALMVEWTDEFK NDPQLSLISAMIKNLKEQGV TFPAIGSQAAEQAKASPALV AKDPGTVANKKEEEDLAKAI ELSLKEQRQQS

Data sets:
Data typeCount
13C chemical shifts523
15N chemical shifts177
1H chemical shifts177

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1STAM1 VHS-UIM1

Entities:

Entity 1, STAM1 VHS-UIM 191 residues - Formula weight is not available

1   METPROLEUPHEALATHRASNPROPHEASP
2   GLNASPVALGLULYSALATHRSERGLUMET
3   ASNTHRALAGLUASPTRPGLYLEUILELEU
4   ASPILECYSASPLYSVALGLYGLNSERARG
5   THRGLYPROLYSASPCYSLEUARGSERILE
6   METARGARGVALASNHISLYSASPPROHIS
7   VALALAMETGLNALALEUTHRLEULEUGLY
8   ALACYSVALSERASNCYSGLYLYSILEPHE
9   HISLEUGLUVALCYSSERARGASPPHEALA
10   SERGLUVALSERASNVALLEUASNLYSGLY
11   HISPROLYSVALCYSGLULYSLEULYSALA
12   LEUMETVALGLUTRPTHRASPGLUPHELYS
13   ASNASPPROGLNLEUSERLEUILESERALA
14   METILELYSASNLEULYSGLUGLNGLYVAL
15   THRPHEPROALAILEGLYSERGLNALAALA
16   GLUGLNALALYSALASERPROALALEUVAL
17   ALALYSASPPROGLYTHRVALALAASNLYS
18   LYSGLUGLUGLUASPLEUALALYSALAILE
19   GLULEUSERLEULYSGLUGLNARGGLNGLN
20   SER

Samples:

sample_1: Tandem ubiquitin binding domains of STAM1, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%; sodium phosphate 50 mM; NaCl .1 M

sample_conditions_1: ionic strength: 0.1 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 900 MHz

Related Database Links:

BMRB 16763 17059
PDB
DBJ BAE26170 BAE28168 BAE34187 BAE37536 BAE40949
GB AAC50734 AAC52840 AAH30586 AAH44666 AAH55326
REF NP_001070310 NP_001102591 NP_003464 NP_035614 XP_001094352
SP P70297 Q92783
TPG DAA23567
AlphaFold P70297 Q92783

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