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 19906

Title: Backbone and side chain 1H, 13C, and 15N Chemical Shift Assignments for EDB and specific binding aptide   PubMed: 24985319

Deposition date: 2014-04-10 Original release date: 2014-09-22

Authors: Suh, Jeong-Yong; Yu, Tae-Kyung

Citation: Yu, T.K.; Shin, S.A.; Kim, E.H.; Kim, S.; Ryu, K.S.; Cheong, H.; Ahn, H.C.; Jon, S.; Suh, Jeong-Yong. "An Unusual Protein-Protein Interaction through Coupled Unfolding and Binding"  Angew. Chem. Int. Ed. Engl. 53, 9784-9787 (2014).

Assembly members:
EDB, polymer, 93 residues, Formula weight is not available
APT, polymer, 26 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

Entity Sequences (FASTA):
EDB: GSEVPQLTDLSFVDITDSSI GLRWTPLNSSTIIGYRITVV AAGEGIPIFEDFVDSSVGYY TVTGLEPGIDYDISVITLIN GGESAPTTLTQQT
APT: SSSPIQGSWTWENGKWTWKG IIRLEQ

Data sets:
Data typeCount
1H chemical shifts681
13C chemical shifts328
15N chemical shifts104

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EDB1
2APT2

Entities:

Entity 1, EDB 93 residues - Formula weight is not available

1   GLYSERGLUVALPROGLNLEUTHRASPLEU
2   SERPHEVALASPILETHRASPSERSERILE
3   GLYLEUARGTRPTHRPROLEUASNSERSER
4   THRILEILEGLYTYRARGILETHRVALVAL
5   ALAALAGLYGLUGLYILEPROILEPHEGLU
6   ASPPHEVALASPSERSERVALGLYTYRTYR
7   THRVALTHRGLYLEUGLUPROGLYILEASP
8   TYRASPILESERVALILETHRLEUILEASN
9   GLYGLYGLUSERALAPROTHRTHRLEUTHR
10   GLNGLNTHR

Entity 2, APT 26 residues - Formula weight is not available

1   SERSERSERPROILEGLNGLYSERTRPTHR
2   TRPGLUASNGLYLYSTRPTHRTRPLYSGLY
3   ILEILEARGLEUGLUGLN

Samples:

sample_1: EDB, [U-100% 13C; U-100% 15N], 0.3 mM; APT, [U-100% 13C; U-100% 15N], 0.3 mM; H2O 90%; D2O 10%

sample_conditions_1: temperature: 273 K; pH: 6; pressure: 1 atm; ionic strength: 20 mM

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

X-PLOR_NIH, Garrett, Schwieters, Kuszewski, Tjandra and Clore - chemical shift assignment, refinement

NMR spectrometers:

  • Bruker Avance 900 MHz

Related Database Links:

BMRB 4283
PDB
EMBL CAB52437
GB AAA52461 AAA67749

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