BMRB Entry 11026

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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/BMR11026
MolProbity Validation Chart

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Title:
SOLUTION STRUCTURE OF ALPHA-SPECTRIN SH3-BERGERAC FROM CHICKEN
Deposition date:
2008-01-17
Original release date:
2009-05-21
Authors:
Kutyshenko, Victor; Prokhorov, Dmitry; Timchenko, Maria; Kudrevatykh, Yuri; Fedyukina, Daria; Guschina, Lyubov; Khristoforov, Vladimir; Filimonov, Vladimir
Citation:

Citation: Viguera, A.; Serrano, L.. "Bergerac-SH3: "frustation" induced by stabilizing the folding nucleus."  J. Mol. Biol. 311, 357-371 (2001).
PubMed: 11478866

Assembly members:

Assembly members:
alpha-spectrin SH3-bergerac, polymer, 70 residues, 8068.312 Da.

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: Escherichia coli   Vector: pBAT-4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
alpha-spectrin SH3-bergerac: MDETGKELVLALYDYQEKSP REVTMKKGDILTLLNSTNKD WWKVEVKATANGKTYERQGF VPAAYVKKLD

Data sets:
Data typeCount
13C chemical shifts320
15N chemical shifts69
1H chemical shifts489

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1alpha-spectrin SH3-bergerac1

Entities:

Entity 1, alpha-spectrin SH3-bergerac 70 residues - 8068.312 Da.

This is the mutant of alpa-spectrin wild type SH3-domain. The difference between this mutant and wild type protein consists of 10 extra residues placed between 45th and 48th polypeptides' residues.

1   METASPGLUTHRGLYLYSGLULEUVALLEU
2   ALALEUTYRASPTYRGLNGLULYSSERPRO
3   ARGGLUVALTHRMETLYSLYSGLYASPILE
4   LEUTHRLEULEUASNSERTHRASNLYSASP
5   TRPTRPLYSVALGLUVALLYSALATHRALA
6   ASNGLYLYSTHRTYRGLUARGGLNGLYPHE
7   VALPROALAALATYRVALLYSLYSLEUASP

Samples:

sample_1: alpha-spectrin SH3-bergerac, [U-98% 13C; U-98% 15N], 2.5 mM; sodium acetate, [U-99% 2H], 25 mM; sodium azide 0.03%; H2O 90%; D2O, [U-99% 2H], 10%

sample_conditions_1: ionic strength: 25 mM; pH: 4; pressure: 744 mmHg; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSY-alisample_1isotropicsample_conditions_1
3D HCCH-TOCSY-arosample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY-alisample_1isotropicsample_conditions_1
3D 1H-13C NOESY-arosample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

CARA, Rochus Keller and Kurt Wuthrich - chemical shift assignment, data collection, processing

TALOS, Cornilescu, Delaglio and Bax - dihedral angles calculation

PREDITOR, PREDITOR - dihedral angles calculation

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

Molmol, Koradi, Billeter and Wuthrich - Data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 11043 16622
PDB
REF XP_011816868 XP_012717136

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