BMRB Entry 11020

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11020
MolProbity Validation Chart

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Title:
Solution structure of human Cu(I)Cox17
Deposition date:
2007-12-10
Original release date:
2008-01-09
Authors:
Banci, Lucia; Bertini, Ivano; Ciofi Baffoni, Simone; Janicka, Anna; Martinelli, Manuele; Kozlowski, Henryk; Palumaa, Peep
Citation:

Citation: Banci, Lucia; Bertini, Ivano; Ciofi Baffoni, Simone; Janicka, Anna; Martinelli, Manuele; Kozlowski, Henryk; Palumaa, Peep. "A structural-dynamical characterization of human Cox17"  J. Biol. Chem. 283, 7912-7920 (2008).
PubMed: 18093982

Assembly members:

Assembly members:
Cox17, polymer, 67 residues, 7327.652 Da.
CU1, non-polymer, 63.546 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: pETG-30A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Cox17: GSFTMPGLVDSNPAPPESQE KKPLKPCCACPETKKARDAC IIEKGEEHCGHLIEAHKECM RALGFKI

Data sets:
Data typeCount
13C chemical shifts207
15N chemical shifts64
1H chemical shifts440

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Cu(I)Cox171
2COPPER (I) ION2

Entities:

Entity 1, Cu(I)Cox17 67 residues - 7327.652 Da.

Cox17 protein contains four additional amino acids (GSFT) at the N-terminus, corresponding to the TEV protease recognition site.

1   GLYSERPHETHRMETPROGLYLEUVALASP
2   SERASNPROALAPROPROGLUSERGLNGLU
3   LYSLYSPROLEULYSPROCYSCYSALACYS
4   PROGLUTHRLYSLYSALAARGASPALACYS
5   ILEILEGLULYSGLYGLUGLUHISCYSGLY
6   HISLEUILEGLUALAHISLYSGLUCYSMET
7   ARGALALEUGLYPHELYSILE

Entity 2, COPPER (I) ION - Cu - 63.546 Da.

1   CU1

Samples:

sample_1: Cox170.5 – 1 mM; COPPER (I) ION0.5 – 1 mM; DTT 1 mM; potassium phosphate 50 mM; H2O 90%; D2O 10%

sample_2: Cox17, [U-100% 15N], 0.5 – 1 mM; COPPER (I) ION0.5 – 1 mM; DTT 1 mM; potassium phosphate 50 mM; H2O 90%; D2O 10%

sample_3: Cox17, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; COPPER (I) ION0.5 – 1 mM; DTT 1 mM; potassium phosphate 50 mM; H2O 90%; D2O 10%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D HBHA(CO)NHsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

ATNOS, Herrmann, Guntert, Wuthrich - peak picking

CARA, Keller and Wuthrich - data analysis

CANDID, Herrmann, Guntert and Wuthrich - NOEs assignment

AMBER v8.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Koll - refinement

TALOS, Cornilescu, Delaglio and Bax - structure solution

WhatIF, Vriend - data analysis

NMR spectrometers:

  • Bruker AVANCE 900 MHz
  • Bruker AVANCE 500 MHz
  • Bruker AVANCE 700 MHz

Related Database Links:

BMRB 11019 17821
PDB
DBJ BAG35079
GB AAA98114 AAF82569 AAH10933 AAI05281 AAI08318
REF NP_001239469 NP_001254468 NP_005685 XP_002758821 XP_003261908
SP Q14061
AlphaFold Q14061

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