BMRB Entry 11520

Name: The chemical shift assignments of the headpiece subdomain of chicken villin protein under the crowded condition
Published: 2013-02-15

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR11520

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

The chemical shift assignments of the headpiece subdomain of chicken villin protein under the crowded condition

Deposition date:

2012-12-12

Original release date:

2013-02-15

Authors:

Tochio, Naoya; Kigawa, Takanori

Citation:

Citation: Harada, Ryuhei; Tochio, Naoya; Kigawa, Takanori; Sugita, Yuji; Feig, Michael. "Reduced native state stability in crowded cellular environment due to protein-protein interactions" .

Assembly members:

Assembly members:
protein, polymer, 36 residues, Formula weight is not available

Natural source:

Natural source: Common Name: chicken Taxonomy ID: 9031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Gallus gallus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: E. coli - cell free Vector: P120522-02

Entity Sequences (FASTA):

Entity Sequences (FASTA):
protein: MLSDEDFKAVFGMTRSAFAN LPLWKQQNLKKEKGLF

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	33
1H chemical shifts	33

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Villin	1

Entities:

Entity 1, Villin 36 residues - Formula weight is not available

1

MET

LEU

SER

ASP

GLU

ASP

PHE

LYS

ALA

VAL

2

PHE

GLY

MET

THR

ARG

SER

ALA

PHE

ALA

ASN

3

LEU

PRO

LEU

TRP

LYS

GLN

ASN

LEU

LYS

4

LYS

GLU

LYS

GLY

LEU

PHE

Samples:

sample_1: protein, [U-15N], 32 mM; HEPES 50 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 0 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

NMRView, Johnson, One Moon Scientific - data analysis

Kujira, N. Kobayashi - data analysis

NMR spectrometers:

Bruker Avance 600 MHz

BMRB	11519 11521 15097 15245 17698 19911 4428
PDB	1QQV 1VII 1YRF 1YRI 1YU5 1YU7 1YU8 2PPZ 2RJV 2RJW 2RJX 2RJY 3MYA 3MYC 3MYE 3NKJ 4CZ3
GB	AAA49133
REF	NP_990773 XP_003207697 XP_010711916 XP_010711917
SP	P02640
AlphaFold	P02640