BMRB Entry 18081

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18081
MolProbity Validation Chart

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Title:
Solution structure of Thermus thermophilus apo-CuA
Deposition date:
2011-11-15
Original release date:
2012-06-19
Authors:
Zaballa, Maria-Eugenia; Abriata, Luciano; Donaire, Antonio; Vila, Alejandro
Citation:

Citation: Zaballa, Maria-Eugenia; Abriata, Luciano; Donaire, Antonio; Vila, Alejandro. "Flexibility of the metal-binding region in apo-cupredoxins."  Proc. Natl. Acad. Sci. U.S.A. 109, 9254-9259 (2012).
PubMed: 22645370

Assembly members:

Assembly members:
apoCuA_polypeptide, polymer, 126 residues, 13959.982 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET9aCuA

Entity Sequences (FASTA):

Entity Sequences (FASTA):
apoCuA_polypeptide: MVIPAGKLERVDPTTVRQEG PWADPAQAVVQTGPNQYTVY VLAFAFGYQPNPIEVPQGAE IVFKITSPDVIHGFHVEGTN INVEVLPGEVSTVRYTFKRP GEYRIICNQYCGLGHQNMFG TIVVKE

Data sets:
Data typeCount
13C chemical shifts477
15N chemical shifts137
1H chemical shifts802

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1apoCuA_polypeptide1

Entities:

Entity 1, apoCuA_polypeptide 126 residues - 13959.982 Da.

1   METVALILEPROALAGLYLYSLEUGLUARG
2   VALASPPROTHRTHRVALARGGLNGLUGLY
3   PROTRPALAASPPROALAGLNALAVALVAL
4   GLNTHRGLYPROASNGLNTYRTHRVALTYR
5   VALLEUALAPHEALAPHEGLYTYRGLNPRO
6   ASNPROILEGLUVALPROGLNGLYALAGLU
7   ILEVALPHELYSILETHRSERPROASPVAL
8   ILEHISGLYPHEHISVALGLUGLYTHRASN
9   ILEASNVALGLUVALLEUPROGLYGLUVAL
10   SERTHRVALARGTYRTHRPHELYSARGPRO
11   GLYGLUTYRARGILEILECYSASNGLNTYR
12   CYSGLYLEUGLYHISGLNASNMETPHEGLY
13   THRILEVALVALLYSGLU

Samples:

sample_1: apoCuA_polypeptide, [U-99% 13C; U-99% 15N], 0.8 – 1.0 mM; potassium phosphate 100 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_2: apoCuA_polypeptide, [U-99% 15N], 0.8 – 1.0 mM; potassium phosphate 100 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_3: apoCuA_polypeptide0.8 – 1.0 mM; potassium phosphate 100 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.1 M; pH: 6; pressure: 1 atm; temperature: 298 K

sample_conditions_3: ionic strength: 0.1 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_2
2D 1H-1H TOCSYsample_3isotropicsample_conditions_3
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_3
3D 1H-15N NOESYsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1

Software:

UNIO v2.0.1, Torsten Hermann - data analysis, peak picking, structure solution

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS+, Cornilescu, Delaglio and Bax - constraints calculation

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
DBJ BAD70957
GB AAB00369 AAS81115 AFH38826
REF WP_011173203 WP_014629505 YP_144400
SP P98052 Q5SJ80
AlphaFold P98052 Q5SJ80

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