BMRB Entry 17821

Title:
Human C30S/C59S-Cox17 mutant
Deposition date:
2011-08-01
Original release date:
2011-09-13
Authors:
Bertini, Ivano; Ciofi-Baffoni, Simone; Gallo, Angelo
Citation:

Citation: Banci, Lucia; Bertini, Ivano; Cefaro, Chiara; Ciofi-Baffoni, Simone; Gallo, Angelo. "Functional role of two interhelical disulfide bonds in human Cox17 protein from a structural perspective."  J. Biol. Chem. 286, 34382-34390 (2011).
PubMed: 21816817

Assembly members:

Assembly members:
Human C30S/C59S-Cox17 mutant, polymer, 67 residues, 7288.475 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-11c

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Human C30S/C59S-Cox17 mutant: GSFTMPGLVDSNPAPPESQE KKPLKPCCASPETKKARDAC IIEKGEEHCGHLIEAHKESM RALGFKI

Data sets:
Data typeCount
13C chemical shifts244
15N chemical shifts54
1H chemical shifts221

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Human C30S/C59S-Cox17 mutant1

Entities:

Entity 1, Human C30S/C59S-Cox17 mutant 67 residues - 7288.475 Da.

GSFT residues are present as cloning artifacts

1   GLYSERPHETHRMETPROGLYLEUVALASP
2   SERASNPROALAPROPROGLUSERGLNGLU
3   LYSLYSPROLEULYSPROCYSCYSALASER
4   PROGLUTHRLYSLYSALAARGASPALACYS
5   ILEILEGLULYSGLYGLUGLUHISCYSGLY
6   HISLEUILEGLUALAHISLYSGLUSERMET
7   ARGALALEUGLYPHELYSILE

Samples:

sample_1: C30S/C59S-Cox17_mutant, [U-100% 15N], 0.5 mM; sodium phosphate 50 mM; EDTA 0.5 mM; DTT 1 mM; D2O 10%; H2O 90%

sample_2: C30S/C59S-Cox17_mutant, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 50 mM; EDTA 0.5 mM; DTT 1 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, data analysis, processing

CARA v2.1, Keller and Wuthrich - chemical shift assignment

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

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

PECAN, Eghbalnia, Wang, Bahrami, Assadi, and Markley - data analysis

AMBER v11.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 500 MHz

Related Database Links:

BMRB 11019 11020
PDB

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