BMRB Entry 25732

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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/BMR25732
MolProbity Validation Chart

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Title:
Solution structure of the cyanobacterial cytochrome b6f complex subunit PetP
Deposition date:
2015-07-29
Original release date:
2016-04-12
Authors:
Veit, Sebastian; Ikegami, Takahisa; Roegner, Matthias
Citation:

Citation: Veit, Sebastian; Nagadoi, Aritaka; Rogner, Matthias; Rexroth, Sascha; Stoll, Raphael; Ikegami, Takahisa. "The cyanobacterial cytochrome b6f subunit PetP adopts an SH3 fold in solution"  Biochim. Biophys. Acta 1857, 705-714 (2016).
PubMed: 27033306

Assembly members:

Assembly members:
PetP, polymer, 79 residues, 8916.176 Da.

Natural source:

Natural source:   Common Name: Thermosynechococcus elongatus BP-1   Taxonomy ID: 197221   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermosynechococcus Thermosynechococcus elongatus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pASK-IBA7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PetP: MASWSHPQFEKIEGRMDVGQ KVRVCRIRDRVAQDIIQKLG QVGQITGFKMTDGSGVGVIV TFDDRSSTWFFEDEVEVVG

Data sets:
Data typeCount
13C chemical shifts347
15N chemical shifts83
1H chemical shifts543

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1PetP1

Entities:

Entity 1, PetP 79 residues - 8916.176 Da.

1   METALASERTRPSERHISPROGLNPHEGLU
2   LYSILEGLUGLYARGMETASPVALGLYGLN
3   LYSVALARGVALCYSARGILEARGASPARG
4   VALALAGLNASPILEILEGLNLYSLEUGLY
5   GLNVALGLYGLNILETHRGLYPHELYSMET
6   THRASPGLYSERGLYVALGLYVALILEVAL
7   THRPHEASPASPARGSERSERTHRTRPPHE
8   PHEGLUASPGLUVALGLUVALVALGLY

Samples:

sample_buffer: PetP, [U-13C; U-15N], 0.1 – 0.5 mM; sodium phosphate 20 mM; DTT, [U-2H], 10 mM; H2O 90%; D2O, [U-2H], 10%

sample_condition: ionic strength: 0 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESY aliphaticsample_bufferisotropicsample_condition
3D 1H-13C NOESY aromaticsample_bufferisotropicsample_condition
3D 1H-15N NOESYsample_bufferisotropicsample_condition
2D 1H-15N HSQCsample_bufferisotropicsample_condition
2D 1H-13C HSQC aliphaticsample_bufferisotropicsample_condition
2D 1H-13C HSQC aromaticsample_bufferisotropicsample_condition
2D 1H-13C HSQC aliphaticsample_bufferisotropicsample_condition
2D 1H-13C HSQC aromaticsample_bufferisotropicsample_condition
2D 1H-1H NOESYsample_bufferisotropicsample_condition
3D CBCA(CO)NHsample_bufferisotropicsample_condition
3D C(CO)NHsample_bufferisotropicsample_condition
3D HNCOsample_bufferisotropicsample_condition
3D HNCAsample_bufferisotropicsample_condition
3D HNCACBsample_bufferisotropicsample_condition
3D HBHA(CO)NHsample_bufferisotropicsample_condition
3D HN(CA)COsample_bufferisotropicsample_condition
3D H(CCO)NHsample_bufferisotropicsample_condition
3D HCCH-TOCSYsample_bufferisotropicsample_condition
3D HCCH-COSYsample_bufferisotropicsample_condition

Software:

SPARKY, Goddard - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

XPLOR, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker Avance 950 MHz
  • Bruker Avance 800 MHz
  • Bruker DRX-600 600 MHz
  • Bruker DRX-400 400 MHz

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