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 36026

Title: Solution structure of human Gelsolin protein domain 1 at pH 5.0   PubMed: 28349924

Deposition date: 2016-10-26 Original release date: 2017-10-30

Authors: Fan, J.; Yang, D.

Citation: Fan, Jing-Song; Goh, Honzhen; Ding, Ke; Xue, Bo; Robinson, Robert; Yang, Daiwen. "Structural Basis for pH-mediated Regulation of F-actin Severing by Gelsolin Domain 1."  Sci. Rep. 7, 45230-45230 (2017).

Assembly members:
entity_1, polymer, 133 residues, 14973.815 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_1: EHPEFLKAGKEPGLQIWRVE KFDLVPVPTNLYGDFFTGDA YVILKTVQLRNGNLQYDLHY WLGNECSQDESGAAAIFTVQ LDDYLNGRAVQHREVQGFES ATFLGYFKSGLKYKKGGVAS GFKHVVPNEVVVQ

Data sets:
Data typeCount
13C chemical shifts114
15N chemical shifts127
1H chemical shifts742

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 133 residues - 14973.815 Da.

1   GLUHISPROGLUPHELEULYSALAGLYLYS
2   GLUPROGLYLEUGLNILETRPARGVALGLU
3   LYSPHEASPLEUVALPROVALPROTHRASN
4   LEUTYRGLYASPPHEPHETHRGLYASPALA
5   TYRVALILELEULYSTHRVALGLNLEUARG
6   ASNGLYASNLEUGLNTYRASPLEUHISTYR
7   TRPLEUGLYASNGLUCYSSERGLNASPGLU
8   SERGLYALAALAALAILEPHETHRVALGLN
9   LEUASPASPTYRLEUASNGLYARGALAVAL
10   GLNHISARGGLUVALGLNGLYPHEGLUSER
11   ALATHRPHELEUGLYTYRPHELYSSERGLY
12   LEULYSTYRLYSLYSGLYGLYVALALASER
13   GLYPHELYSHISVALVALPROASNGLUVAL
14   VALVALGLN

Samples:

sample_1: gelsolin domain 1, [U-13C; U-15N], 0.65 ± 0.1 mM; Acetate 10 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0 M; pH: 5.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
4D 13C_15N_edited NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY v3.13, Goddard - data analysis, peak picking

XPLOR-NIH, C.D. Schwieters, J.J. Kuszewski - structure calculation

NMRPipe v8.7, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker Avance 800 MHz

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