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 15894

Title: Mechanism of metal delivery to the CuA center in terminal oxidases from bacteria: a redox m nage- -trois   PubMed: 18758441

Deposition date: 2008-07-28 Original release date: 2008-11-14

Authors: Banci, Lucia; Bertini, Ivano; Ciofi-Baffoni, Simone; Wang, Shenlin

Citation: Abriata, Luciano; Banci, Lucia; Bertini, Ivano; Ciofi-Baffoni, Simone; Gkazonis, Petros; Spyroulias, Georgios; Vila, Alejandro; Wang, Shenlin. "Mechanism of Cu(A) assembly."  Nat. Chem. Biol. 4, 599-601 (2008).

Assembly members:
CuA center, polymer, 120 residues, 13222.670 Da.

Natural source:   Common Name: Thermus thermophilus   Taxonomy ID: 274   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermus thermophilus

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

Entity Sequences (FASTA):
CuA center: GSFTEGWVRFSPGPNAAAYL TLENPGDLPLRLVGARTPVA ERVELHETFMREVEGKKVMG MRPVPFLEVPPKGRVELKPG GYHFMLLGLKRPLKAGEEVE LDLLFAGGKVLKVVLPVEAR

Data sets:
Data typeCount
13C chemical shifts482
15N chemical shifts104
1H chemical shifts850

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CuA center1

Entities:

Entity 1, CuA center 120 residues - 13222.670 Da.

1   GLYSERPHETHRGLUGLYTRPVALARGPHE
2   SERPROGLYPROASNALAALAALATYRLEU
3   THRLEUGLUASNPROGLYASPLEUPROLEU
4   ARGLEUVALGLYALAARGTHRPROVALALA
5   GLUARGVALGLULEUHISGLUTHRPHEMET
6   ARGGLUVALGLUGLYLYSLYSVALMETGLY
7   METARGPROVALPROPHELEUGLUVALPRO
8   PROLYSGLYARGVALGLULEULYSPROGLY
9   GLYTYRHISPHEMETLEULEUGLYLEULYS
10   ARGPROLEULYSALAGLYGLUGLUVALGLU
11   LEUASPLEULEUPHEALAGLYGLYLYSVAL
12   LEULYSVALVALLEUPROVALGLUALAARG

Samples:

sample_1: entity, [U-100% 15N], 0.8 ± 0.1 mM; D2O, [U-99.9% 2H], 10%; H2O 90%; Pi 50 mM

sample_2: entity, [U-100% 13C; U-100% 15N], 0.8 ± 0.1 mM; D2O, [U-99.9% 2H], 10%; H2O 90%; Pi 50 mM

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
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
15N R1sample_1isotropicsample_conditions_1
15N R2sample_1isotropicsample_conditions_1
1H-15N NOEsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA v2.0, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 500 MHz
  • Bruker Avance 400 MHz

Related Database Links:

BMRB 15895 15896 15897
PDB
DBJ BAD71766
GB AAS81922 AEG34334 AFH39883
REF WP_011173952 WP_011229034 WP_014510965 WP_014630387 YP_145209

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts