BMRB Entry 50091

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50091

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Title:
Fce4 domain of Immunoglobulin E
Deposition date:
2019-11-18
Original release date:
2020-11-18
Authors:
Benjamin, Stefi; McDonnell, James
Citation:

Citation: Benjamin, Stefi; Creeke, Paul; Henry, Alistair; McDonnell, James. "NMR backbone assignment of the Ce4 domain of immunoglobulin E"  Biomol. NMR Assign. 14, 151-155 (2020).
PubMed: 32108310

Assembly members:

Assembly members:
entity_1, polymer, 130 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: recombinant technology   Host organism: Escherichia coli   Vector: pET15a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSSHHHHHHSSGLVPRGSHM GPRAAPEVYAFATPEWPGSR DKRTLACLIQNFMPEDISVQ WLHNEVQLPDARHSTTQPRK TKGSGFFVFSRLEVTRAEWE QKDEFICRAVHEAASPSQTV QRAVSVNPGK

Data sets:
Data typeCount
13C chemical shifts338
15N chemical shifts103
1H chemical shifts103

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Fce4, chain 11
2Fce4, chain 21

Entities:

Entity 1, Fce4, chain 1 130 residues - Formula weight is not available

The second number is the residue author seq code and it is the residue number in the context of whole Immunoglobulin E.

1   GLYSERSERHISHISHISHISHISHISSER
2   SERGLYLEUVALPROARGGLYSERHISMET
3   GLYPROARGALAALAPROGLUVALTYRALA
4   PHEALATHRPROGLUTRPPROGLYSERARG
5   ASPLYSARGTHRLEUALACYSLEUILEGLN
6   ASNPHEMETPROGLUASPILESERVALGLN
7   TRPLEUHISASNGLUVALGLNLEUPROASP
8   ALAARGHISSERTHRTHRGLNPROARGLYS
9   THRLYSGLYSERGLYPHEPHEVALPHESER
10   ARGLEUGLUVALTHRARGALAGLUTRPGLU
11   GLNLYSASPGLUPHEILECYSARGALAVAL
12   HISGLUALAALASERPROSERGLNTHRVAL
13   GLNARGALAVALSERVALASNPROGLYLYS

Samples:

sample_1: sodium phosphate 20 mM; sodium chloride 50 mM; Fce4, [U-100% 13C; U-100% 15N; U-80% 2H], 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6; 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 HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1

Software:

Analysis v2.4, Vranken, WF - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

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