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 18901

Title: NMR structure of the C-terminal domain of the protein HCFC1 from MUS MUSCULUS

Authors: Serrano, Pedro; Geralt, Michael; Dutta, Samit; Wuthrich, Kurt

Citation: Serrano, Pedro; Wuthrich, Kurt. "NMR structure of the C-terminal domain of the protein HCFC1 from MUS MUSCULUS"  Not known ., .-..

Assembly members:
entity, polymer, 126 residues, 13347.151 Da.

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

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

Entity Sequences (FASTA):
entity: GCLPGFPGAPCAIKISKSPD GAHLTWEPPSVTSGKIIEYS VYLAIQSSQASGEPKSSTPA QLAFMRVYCGPSPSCLVQSS SLSNAHIDYTTKPAIIFRIA ARNEKGYGPATQVRWLQETS KDSSGT

Data sets:
Data typeCount
13C chemical shifts464
15N chemical shifts111
1H chemical shifts736

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C-terminal domain of the protein HCFC11

Entities:

Entity 1, C-terminal domain of the protein HCFC1 126 residues - 13347.151 Da.

1   GLYCYSLEUPROGLYPHEPROGLYALAPRO
2   CYSALAILELYSILESERLYSSERPROASP
3   GLYALAHISLEUTHRTRPGLUPROPROSER
4   VALTHRSERGLYLYSILEILEGLUTYRSER
5   VALTYRLEUALAILEGLNSERSERGLNALA
6   SERGLYGLUPROLYSSERSERTHRPROALA
7   GLNLEUALAPHEMETARGVALTYRCYSGLY
8   PROSERPROSERCYSLEUVALGLNSERSER
9   SERLEUSERASNALAHISILEASPTYRTHR
10   THRLYSPROALAILEILEPHEARGILEALA
11   ALAARGASNGLULYSGLYTYRGLYPROALA
12   THRGLNVALARGTRPLEUGLNGLUTHRSER
13   LYSASPSERSERGLYTHR

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 5 mM

sample_conditions_1: ionic strength: 0.220 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
4D APSY HACANHsample_1isotropicsample_conditions_1
5D APSY CBCACONHsample_1isotropicsample_conditions_1
5D APSY HACACONHsample_1isotropicsample_conditions_1

Software:

CYANA, G ntert P. - refinement

UNIO, Herrmann & Wuthrich - chemical shift assignment, structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAA08258
EMBL CAA55790
GB AAB01163 AAB27583 AAD09225 AAH53742 ABX10979
REF NP_001132979 NP_001162266 NP_001268286 NP_005325 NP_032250
SP P51610 P51611 Q61191
TPG DAA13208