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Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 25690

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25690
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Title: NMR structure of the C-terminal region of human eukaryotic elongation factor 1B   PubMed: 26762120

Deposition date: 2015-07-02 Original release date: 2016-05-23

Authors: Wu, Huiwen; Feng, Yingang

Citation: Wu, Huiwen; Gong, Weibin; Wang, Jinfeng; Perrett, Sarah; Feng, Yingang. "The C-terminal region of human eukaryotic elongation factor 1B delta"  J. Biomol. NMR 64, 181-187 (2016).

Assembly members:
entity, polymer, 133 residues, 14893.776 Da.

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):
entity: GPGSEDDDIDLFGSDNEEED KEAAQLREERLRQYAEKKAK KPALVAKSSILLDVKPWDDE TDMAQLEACVRSIQLDGLVW GASKLVPVGYGIRKLQIQCV VEDDKVGTDLLEEEITKFEE HVQSVDIAAFNKI

Data sets:
Data typeCount
13C chemical shifts579
15N chemical shifts137
1H chemical shifts931

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 133 residues - 14893.776 Da.

1   GLYPROGLYSERGLUASPASPASPILEASP
2   LEUPHEGLYSERASPASNGLUGLUGLUASP
3   LYSGLUALAALAGLNLEUARGGLUGLUARG
4   LEUARGGLNTYRALAGLULYSLYSALALYS
5   LYSPROALALEUVALALALYSSERSERILE
6   LEULEUASPVALLYSPROTRPASPASPGLU
7   THRASPMETALAGLNLEUGLUALACYSVAL
8   ARGSERILEGLNLEUASPGLYLEUVALTRP
9   GLYALASERLYSLEUVALPROVALGLYTYR
10   GLYILEARGLYSLEUGLNILEGLNCYSVAL
11   VALGLUASPASPLYSVALGLYTHRASPLEU
12   LEUGLUGLUGLUILETHRLYSPHEGLUGLU
13   HISVALGLNSERVALASPILEALAALAPHE
14   ASNLYSILE

Samples:

sample_1: entity, [U-13C; U-15N], 0.8 mM; TRIS 20 mM; sodium chloride 200 mM; DSS 0.01 % w/v; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 220 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

Felix, Accelrys Software Inc. - processing

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

SANE, Duggan, Legge, Dyson & Wright - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker DMX 600 MHz

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