BMRB Entry 30286

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30286
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Title:
Solution NMR structure of the membrane electron transporter CcdA
Deposition date:
2017-04-24
Original release date:
2018-01-25
Authors:
Zhou, Y.; Bushweller, J.
Citation:

Citation: Zhou, Y.; Bushweller, J.. "Solution structure and elevator mechanism of the membrane electron transporter CcdA"  Nat. Struct. Mol. Biol. 25, 163-169 (2018).
PubMed: 29379172

Assembly members:

Assembly members:
entity_1, polymer, 232 residues, 25292.143 Da.

Natural source:

Natural source:   Common Name: Thermus thermophilus   Taxonomy ID: 300852   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermus thermophilus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pET22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSLSLTAAFLAGVLSFLSPC VLPLVPTYLFYLGGARGRPL FNALFFILGFGAVFFLLGLP FTLLGGLLFEHRQTLARVGG VVLVLFGLYMLGLRPRWGVS LRYEGETSRPLGAFLLGATL ALGWTPCIGPILGAILTLTA VGGGVGFLLAYILGLAVPFF VVALFADRIKGWLRRAGRIS HYVEVLAGVVLVLVGVLLFT GTFTALNTFFLRITPEWLQR YLPSHHHHHHHH

Data sets:
Data typeCount
13C chemical shifts509
15N chemical shifts185
1H chemical shifts186

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 232 residues - 25292.143 Da.

1   METSERLEUSERLEUTHRALAALAPHELEU
2   ALAGLYVALLEUSERPHELEUSERPROCYS
3   VALLEUPROLEUVALPROTHRTYRLEUPHE
4   TYRLEUGLYGLYALAARGGLYARGPROLEU
5   PHEASNALALEUPHEPHEILELEUGLYPHE
6   GLYALAVALPHEPHELEULEUGLYLEUPRO
7   PHETHRLEULEUGLYGLYLEULEUPHEGLU
8   HISARGGLNTHRLEUALAARGVALGLYGLY
9   VALVALLEUVALLEUPHEGLYLEUTYRMET
10   LEUGLYLEUARGPROARGTRPGLYVALSER
11   LEUARGTYRGLUGLYGLUTHRSERARGPRO
12   LEUGLYALAPHELEULEUGLYALATHRLEU
13   ALALEUGLYTRPTHRPROCYSILEGLYPRO
14   ILELEUGLYALAILELEUTHRLEUTHRALA
15   VALGLYGLYGLYVALGLYPHELEULEUALA
16   TYRILELEUGLYLEUALAVALPROPHEPHE
17   VALVALALALEUPHEALAASPARGILELYS
18   GLYTRPLEUARGARGALAGLYARGILESER
19   HISTYRVALGLUVALLEUALAGLYVALVAL
20   LEUVALLEUVALGLYVALLEULEUPHETHR
21   GLYTHRPHETHRALALEUASNTHRPHEPHE
22   LEUARGILETHRPROGLUTRPLEUGLNARG
23   TYRLEUPROSERHISHISHISHISHISHIS
24   HISHIS

Samples:

sample_2: CcdA, [U-13C; U-15N; U-2H], 0.37 mM; potassium phosphate 25 mM; sodium acetate 25 mM; sodium azide 0.05%; sodium chloride 50 mM

sample_3: CcdA, [U-15N; U-2H], 0.7 mM; potassium phosphate 25 mM; sodium acetate 25 mM; sodium azide 0.05%; sodium chloride 50 mM

sample_4: CcdA, [U-15N; U-2H], 0.7 mM; potassium phosphate 25 mM; sodium acetate 25 mM; sodium azide 0.05%; sodium chloride 50 mM

sample_5: CcdA single Cys mutants labeled with MTSL, [U-15N], 0.2 mM; potassium phosphate 25 mM; sodium acetate 25 mM; sodium azide 0.05%; sodium chloride 50 mM

sample_conditions_1: ionic strength: 100 mM; pH: 5.5; pressure: 1 atm; temperature: 343 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3anisotropicsample_conditions_1
2D 1H-15N HSQCsample_4anisotropicsample_conditions_1
2D 1H-15N HSQCsample_5isotropicsample_conditions_1

Software:

Analysis v2.4.2, CCPN - chemical shift assignment, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS-N, Yang Shen, and Ad Bax - data analysis

TOPSPIN, Bruker Biospin - collection

X-PLOR NIH v2.39, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

XPLOR-NIH v2.39, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker AvanceIII 800 MHz

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