BMRB Entry 30877

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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/BMR30877
MolProbity Validation Chart

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Title:
Magic Angle Spinning NMR Structure of Human Cofilin-2 Assembled on Actin Filaments
Deposition date:
2021-03-10
Original release date:
2022-04-15
Authors:
Kraus, J.; Polenova, T.; Perilla, J.; Xu, C.
Citation:

Citation: Kraus, Jodi; Russell, Ryan; Kudryashova, Elena; Xu, Chaoyi; Katyal, Nidhi; Perilla, Juan; Kudryashov, Dmitri; Polenova, Tatyana. "Magic angle spinning NMR structure of human cofilin-2 assembled on actin filaments reveals isoform-specific conformation and binding mode"  Nat. Commun. 13, 2114-2114 (2022).
PubMed: 35440100

Assembly members:

Assembly members:
entity_1, polymer, 166 residues, 18765.627 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MASGVTVNDEVIKVFNDMKV RKSSTQEEIKKRKKAVLFCL SDDKRQIIVEEAKQILVGDI GDTVEDPYTSFVKLLPLNDC RYALYDATYETKESKKEDLV FIFWAPESAPLKSKMIYASS KDAIKKKFTGIKHEWQVNGL DDIKDRSTLGEKLGGNVVVS LEGKPL

Data sets:
Data typeCount
13C chemical shifts779
15N chemical shifts163

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 166 residues - 18765.627 Da.

1   METALASERGLYVALTHRVALASNASPGLU
2   VALILELYSVALPHEASNASPMETLYSVAL
3   ARGLYSSERSERTHRGLNGLUGLUILELYS
4   LYSARGLYSLYSALAVALLEUPHECYSLEU
5   SERASPASPLYSARGGLNILEILEVALGLU
6   GLUALALYSGLNILELEUVALGLYASPILE
7   GLYASPTHRVALGLUASPPROTYRTHRSER
8   PHEVALLYSLEULEUPROLEUASNASPCYS
9   ARGTYRALALEUTYRASPALATHRTYRGLU
10   THRLYSGLUSERLYSLYSGLUASPLEUVAL
11   PHEILEPHETRPALAPROGLUSERALAPRO
12   LEULYSSERLYSMETILETYRALASERSER
13   LYSASPALAILELYSLYSLYSPHETHRGLY
14   ILELYSHISGLUTRPGLNVALASNGLYLEU
15   ASPASPILELYSASPARGSERTHRLEUGLY
16   GLULYSLEUGLYGLYASNVALVALVALSER
17   LEUGLUGLYLYSPROLEU

Samples:

sample_1: human cofilin-2, [U-13C; U-15N], 20.8 % w/w; F-actin, NA-actin, 79.2 % w/w

sample_2: human cofilin-2, [1,6-13C]-glucose, U-15N, 20.8 % w/w; F-actin, NA-actin, 79.2 % w/w

sample_3: human cofilin-2, [2-13C]-glucose, U-15N, 20.8 % w/w; F-actin, NA-actin, 79.2 % w/w

sample_conditions_1: ionic strength: 50 mM; pH: 6.6; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
Exp1_CORD50mssample_1isotropicsample_conditions_1
Exp2_CORD200mssample_1isotropicsample_conditions_1
Exp3_CORD50mssample_2isotropicsample_conditions_1
Exp4_CORD200mssample_2isotropicsample_conditions_1
Exp5_CORD500mssample_2isotropicsample_conditions_1
Exp6_CORD50mssample_3isotropicsample_conditions_1
Exp7_CORD200mssample_3isotropicsample_conditions_1
Exp8_CORD500mssample_3isotropicsample_conditions_1
Exp9_PAINCPsample_3isotropicsample_conditions_1
Exp10_NCACX2dsample_1isotropicsample_conditions_1
Exp11_NCACX3dsample_1isotropicsample_conditions_1
Exp12_NCOCX2dsample_1isotropicsample_conditions_1
Exp13_NCOCX3dsample_1isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

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

Rowland NMR Toolkit (RNMRTK), Hoch and Stern - processing

CcpNmr Analysis, CCPN - chemical shift assignment, peak picking

TALOS-N, Cornilescu, Delaglio and Bax - structure calculation

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMR spectrometers:

  • Bruker AVANCE III 850 MHz