BMRB Entry 25642

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25642
MolProbity Validation Chart

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Title:
Atomic structure of the cytoskeletal bactofilin BacA revealed by solid-state NMR
Deposition date:
2015-05-29
Original release date:
2015-12-14
Authors:
Shi, Chaowei; Fricke, Pascal; Lin, Lin; Chevelkov, Veniamin; Wegstroth, Melanie; Becker, Stefan; Thanbichler, Martin; Lange, Adam
Citation:

Citation: Shi, Chaowei; Fricke, Pascal; Lin, Lin; Chevelkov, Veniamin; Wegstroth, Melanie; Becker, Stefan; Thanbichler, Martin; Lange, Adam. "Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR"  Sci. Adv. 1, e1501087-e1501087 (2015).
PubMed: 26665178

Assembly members:

Assembly members:
sample_uni, polymer, 184 residues, 10938.355 Da.

Natural source:

Natural source:   Common Name: a-proteobacteria   Taxonomy ID: 155892   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Caulobacter crescentus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
sample_uni: MFSKQAKSNNKAPARIEPLP TPMAATPAEPARRAPPKVAS LLSADLTIEGGVTGEGELQI DGVVKGDVRVGRLTVGETGH VEGSVYAEAVEVRGRVVGAI TSKQVRLYGTSYVDGDITHE QLAMETGAFFQGRSLKFQRP APAPSQPAPHPEHLAIAKSA GGAPENSSSVDKLAAALEHH HHHH

Data sets:
Data typeCount
13C chemical shifts418
15N chemical shifts102
1H chemical shifts97

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 184 residues - 10938.355 Da.

1   METPHESERLYSGLNALALYSSERASNASN
2   LYSALAPROALAARGILEGLUPROLEUPRO
3   THRPROMETALAALATHRPROALAGLUPRO
4   ALAARGARGALAPROPROLYSVALALASER
5   LEULEUSERALAASPLEUTHRILEGLUGLY
6   GLYVALTHRGLYGLUGLYGLULEUGLNILE
7   ASPGLYVALVALLYSGLYASPVALARGVAL
8   GLYARGLEUTHRVALGLYGLUTHRGLYHIS
9   VALGLUGLYSERVALTYRALAGLUALAVAL
10   GLUVALARGGLYARGVALVALGLYALAILE
11   THRSERLYSGLNVALARGLEUTYRGLYTHR
12   SERTYRVALASPGLYASPILETHRHISGLU
13   GLNLEUALAMETGLUTHRGLYALAPHEPHE
14   GLNGLYARGSERLEULYSPHEGLNARGPRO
15   ALAPROALAPROSERGLNPROALAPROHIS
16   PROGLUHISLEUALAILEALALYSSERALA
17   GLYGLYALAPROGLUASNSERSERSERVAL
18   ASPLYSLEUALAALAALALEUGLUHISHIS
19   HISHISHISHIS

Samples:

sample_uni: sample_uni, [U-100% 13C; U-100% 15N], 95%; TRIS 20 mM; H2O 3%; DSS 0.1%

sample_2gly: sample_uni, [2- 13C] Glycerol, 95%; TRIS 20 mM; H2O 3%; DSS 0.1%

sample_13gly: sample_uni, [1,3- 13C] Glycerol, 95%; TRIS 20 mM; H2O 3%; DSS 0.1%

sample_deu: sample_deu, [U-100% 13C; U-100% 15N; U-100% 2H], 95%; TRIS 50 mM; H2O 3%; DSS 0.1%; EDTA 0.5 mM; DTT 1 mM

sample_conditions_1: ionic strength: 20 mM; pH: 7.5; pressure: 1 atm; temperature: 277 K

sample_conditions_2: ionic strength: 50 mM; pH: 8; pressure: 1 atm; temperature: 301 K

Experiments:

NameSampleSample stateSample conditions
PDSDsample_unisolidsample_conditions_1
3D NCACXsample_unisolidsample_conditions_1
3D NCOCXsample_unisolidsample_conditions_1
3D NCOCAsample_unisolidsample_conditions_1
3D NCACOsample_unisolidsample_conditions_1
PDSDsample_2glysolidsample_conditions_1
PDSDsample_2glysolidsample_conditions_1
PDSDsample_13glysolidsample_conditions_1
PDSDsample_13glysolidsample_conditions_1
2D NHHCsample_13glysolidsample_conditions_1
3D (H)CANHsample_deusolidsample_conditions_2
3D (H)CONHsample_deusolidsample_conditions_2
3D (H)CACO(N)Hsample_deusolidsample_conditions_2
3D (H)COCA(N)Hsample_deusolidsample_conditions_2
3D (H)CA(CO)NHsample_deusolidsample_conditions_2
4D HN(H)(H)NHsample_deusolidsample_conditions_2

Software:

SPARKY v3.114, Goddard - chemical shift assignment, chemical shift calculation, peak picking

CCPN v2.4, CCPN - chemical shift assignment, chemical shift calculation, peak picking

TOPSPIN, Bruker Biospin - chemical shift calculation, collection, processing

X-PLOR_NIH v2.37, Schwieters, Kuszewski, Tjandra and Clore - chemical shift assignment, refinement, structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz
  • Bruker Avance 850 MHz

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