BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17306

Title: NRC consensus ankyrin repeat protein backbone and sidechain assignments   PubMed: 21397186

Authors: Aksel, Tural; Majumdar, Ananya; Barrick, Doug

Citation: Aksel, Tural; Majumdar, Ananya; Barrick, Doug. "The contribution of entropy, enthalpy, and hydrophobic desolvation to cooperativity in repeat-protein folding."  Structure 19, 349-360 (2011).

Assembly members:
NR1C, polymer, 115 residues, Formula weight is not available

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
NR1C: GHMWGSKDGNTPLHNAAKNG HAEEVKKLLSKGADVNARSK DGNTPLHLAAKNGHAEIVKL LLAKGADVNARSKDGNTPEH LAKKNGHHEIVKLLDAKGAD VNARSWGSSHHHHHH

Data sets:
Data typeCount
13C chemical shifts413
15N chemical shifts103
1H chemical shifts661
heteronuclear NOE values94
order parameters85
T1 relaxation values94
T2 relaxation values94

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NR1C_assembly1

Entities:

Entity 1, NR1C_assembly 115 residues - Formula weight is not available

1   GLYHISMETTRPGLYSERLYSASPGLYASN
2   THRPROLEUHISASNALAALALYSASNGLY
3   HISALAGLUGLUVALLYSLYSLEULEUSER
4   LYSGLYALAASPVALASNALAARGSERLYS
5   ASPGLYASNTHRPROLEUHISLEUALAALA
6   LYSASNGLYHISALAGLUILEVALLYSLEU
7   LEULEUALALYSGLYALAASPVALASNALA
8   ARGSERLYSASPGLYASNTHRPROGLUHIS
9   LEUALALYSLYSASNGLYHISHISGLUILE
10   VALLYSLEULEUASPALALYSGLYALAASP
11   VALASNALAARGSERTRPGLYSERSERHIS
12   HISHISHISHISHIS

Samples:

sample_1: NR1C, [U-100% 13C; U-100% 15N], 2 mM; sodium phosphate 25 mM; sodium chloride 25 mM; H2O 90%; D2O 10%

NR1C_conditions: ionic strength: 63 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicNR1C_conditions
3D CBCA(CO)NHsample_1isotropicNR1C_conditions
3D HNCACBsample_1isotropicNR1C_conditions
3D HBHA(CO)NHsample_1isotropicNR1C_conditions
3D HNCOsample_1isotropicNR1C_conditions
3D HNHAsample_1isotropicNR1C_conditions
3D 1H-15N NOESYsample_1isotropicNR1C_conditions
3D 1H-13C NOESYsample_1isotropicNR1C_conditions
3D HCCH-TOCSYsample_1isotropicNR1C_conditions
3D H(CCO)NHsample_1isotropicNR1C_conditions
2D 1H-15N HSQCsample_1anisotropicNR1C_conditions

Software:

CYANA v2, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, refinement, structure solution

UNIO v2.0.1, Dr. Torsten Herrmann - chemical shift assignment, structure solution

CARA v1.8.4, Kurt Wuthrich - chemical shift assignment, data analysis

X-PLOR NIH v2.24, Schwieters, Kuszewski, Tjandra and Clore - refinement

ModelFree v4.2, Palmer - data analysis

NMRPipe v5.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

PDB
GB ADR82636