BMRB Entry 30798

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30798
MolProbity Validation Chart

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Title:
Solution Structure of the Dysferlin C2A Domain in its Calcium-free State
Deposition date:
2020-09-19
Original release date:
2021-01-29
Authors:
Wang, Y.; Mercier, P.; Santamaria, L.; Shaw, G.
Citation:

Citation: Wang, Y.; Tadayon, R.; Santamaria, L.; Mercier, P.; Forristal, C.; Shaw, G.. "Calcium binds and rigidifies the dysferlin C2A domain in a tightly coupled manner"  Biochem. J. 478, 197-215 (2021).
PubMed: 33449082

Assembly members:

Assembly members:
entity_1, polymer, 138 residues, 14822.910 Da.

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 BL21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSGGGGGMLRVFILYAENVH TPDTDISDAYCSAVFAGVKK RTKVIKNSVNPVWNEGFEWD LKGIPLDQGSELHVVVKDHE TMGRNRFLGEAKVPLREVLA TPSLSASFNAPLLDTKKQPT GASLVLQVSYTPLPGAVL

Data sets:
Data typeCount
13C chemical shifts332
15N chemical shifts114
1H chemical shifts746

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 138 residues - 14822.910 Da.

1   GLYSERGLYGLYGLYGLYGLYMETLEUARG
2   VALPHEILELEUTYRALAGLUASNVALHIS
3   THRPROASPTHRASPILESERASPALATYR
4   CYSSERALAVALPHEALAGLYVALLYSLYS
5   ARGTHRLYSVALILELYSASNSERVALASN
6   PROVALTRPASNGLUGLYPHEGLUTRPASP
7   LEULYSGLYILEPROLEUASPGLNGLYSER
8   GLULEUHISVALVALVALLYSASPHISGLU
9   THRMETGLYARGASNARGPHELEUGLYGLU
10   ALALYSVALPROLEUARGGLUVALLEUALA
11   THRPROSERLEUSERALASERPHEASNALA
12   PROLEULEUASPTHRLYSLYSGLNPROTHR
13   GLYALASERLEUVALLEUGLNVALSERTYR
14   THRPROLEUPROGLYALAVALLEU

Samples:

sample_1: DSS 1 mM; MES 25 mM; NaCl 150 mM; EDTA 5 mM; DTT 1 mM; Protein, [U-13C; U-15N], 0.3 mM

sample_2: DSS 1 mM; MES 25 mM; NaCl 150 mM; EDTA 5 mM; DTT 1 mM; Protein, [U-13C; U-15N], 0.3 mM

sample_conditions_1: ionic strength: 150 mM; pH: 5.5; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC NH2 onlysample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

VnmrJ, Varian - collection

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

NMRView, Johnson, One Moon Scientific - data analysis, peak picking

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

X-PLOR NIH v2.37, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz

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