BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 27130

Title: 1H, 13C, and 15N chemical shift assignments of the FnIII-2 domain from Vibrio cholerae RbmA

Authors: Parsley, Nicole; Lee, Hsiau-Wei; Partch, Carrie

Citation: Fong, Jiunn; Rogers, Andrew; Michael, Alicia; Parsley, Nicole; Cornell, William-Cole; Lin, Yu-Cheng; Singh, Praveen; Hartmann, Raimo; Drescher, Knut; Vinogradov, Evgeny; Dietrich, Lars; Partch, Carrie; Yildiz, Fitnat. "Structural dynamics of RbmA governs plasticity of Vibrio cholerae biofilms"  Elife 6, e26163-e26163 (2017).

Assembly members:
RbmA_FnIII-2_domain, polymer, 117 residues, 12683.23 Da.

Natural source:   Common Name: Vibrio cholerae   Taxonomy ID: 666   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Vibrio cholerae

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

Entity Sequences (FASTA):
RbmA_FnIII-2_domain: GAMDPELNGLTIDIKNQFGI NSVESTGGFVPFTVDLNNGR EGEANVEFWMTAVGPDGLII PVNAREKWVIASGDTYSKVR GINFDKSYPAGEYTINAQVV DIVSGERVEQSMTVVKK

Data sets:
Data typeCount
13C chemical shifts219
15N chemical shifts121
1H chemical shifts134

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1RbmA FnIII-2 domain1

Entities:

Entity 1, RbmA FnIII-2 domain 117 residues - 12683.23 Da.

Residues 155-159 represent a vector artifact (GAMDP) left after TEV cleavage

1   GLYALAMETASPPROGLULEUASNGLYLEU
2   THRILEASPILELYSASNGLNPHEGLYILE
3   ASNSERVALGLUSERTHRGLYGLYPHEVAL
4   PROPHETHRVALASPLEUASNASNGLYARG
5   GLUGLYGLUALAASNVALGLUPHETRPMET
6   THRALAVALGLYPROASPGLYLEUILEILE
7   PROVALASNALAARGGLULYSTRPVALILE
8   ALASERGLYASPTHRTYRSERLYSVALARG
9   GLYILEASNPHEASPLYSSERTYRPROALA
10   GLYGLUTYRTHRILEASNALAGLNVALVAL
11   ASPILEVALSERGLYGLUARGVALGLUGLN
12   SERMETTHRVALVALLYSLYS

Samples:

sample_1: RbmA FnIII-2 domain, [U-100% 13C; U-100% 15N], 300 mM; HEPES 10 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRView vv9.2.0-b4, Johnson, One Moon Scientific - chemical shift assignment

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

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

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

GB APF52364.1