BMRB Entry 11027

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11027

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Title:
SPECTRIN SH3 CHIMERA WITH A LIGAND LINKED TO BE BOUND IN ORIENTATION II
Deposition date:
2008-01-17
Original release date:
2009-05-21
Authors:
Kutyshenko, Victor; Prokhorov, Dmitry; Timchenko, Maria; Kudrevatykh, Yuri; Fedyukina, Daria; Gushchina, Lyubov; Khristoforov, Vladimir; Filimonov, Vladimir
Citation:

Citation: Viguera, A.; Serrano, L.; Wilmanns, M.. "Different folding transition states may result in the same native structure."  Nat. Struct. Biol. 3, 874-880 (1996).
PubMed: 8836105

Assembly members:

Assembly members:
alpha-spectrin SH3-F2, polymer, 73 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-F2: MGAPPLPPYSAGGREVTMKK GDILTLLNSTNKDWWKVEVN DRQGFVPAAYVKKLDSGTGK ELVLALYDYQEKS

Data sets:
Data typeCount
13C chemical shifts319
15N chemical shifts69
1H chemical shifts501

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1alpha-spectrin SH3-F21

Entities:

Entity 1, alpha-spectrin SH3-F2 73 residues - 8068.312 Da.

This is chimeric protein with the ligand-linker-SH3 topology where ligand is a sequence MGAPPLPPYSA; linker is GG and SH3 is a s19-p20 circular permutant of the WT alpha-spectrin SH3(PDB ID 1tuc)

1   METGLYALAPROPROLEUPROPROTYRSER
2   ALAGLYGLYARGGLUVALTHRMETLYSLYS
3   GLYASPILELEUTHRLEULEUASNSERTHR
4   ASNLYSASPTRPTRPLYSVALGLUVALASN
5   ASPARGGLNGLYPHEVALPROALAALATYR
6   VALLYSLYSLEUASPSERGLYTHRGLYLYS
7   GLULEUVALLEUALALEUTYRASPTYRGLN
8   GLULYSSER

Samples:

sample_1: alpha-spectrin SH3-F2, [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

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

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 17089
PDB
REF XP_006119095

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