BMRB Entry 27130

Name: 1H, 13C, and 15N chemical shift assignments of the FnIII-2 domain from Vibrio cholerae RbmA
Published: 2017-09-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27130

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

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

Deposition date:

2017-06-09

Original release date:

2017-09-14

Authors:

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

Citation:

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:

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

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pHisGST-TEV

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	219
15N chemical shifts	121
1H chemical shifts	134

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RbmA FnIII-2 domain	1

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

GLY

ALA

MET

ASP

PRO

GLU

LEU

ASN

GLY

LEU

2

THR

ILE

ASP

ILE

LYS

ASN

GLN

PHE

GLY

ILE

3

ASN

SER

VAL

GLU

SER

THR

GLY

PHE

VAL

4

PRO

PHE

THR

VAL

ASP

LEU

ASN

GLY

ARG

5

GLU

GLY

GLU

ALA

ASN

VAL

GLU

PHE

TRP

MET

6

THR

ALA

VAL

GLY

PRO

ASP

GLY

LEU

ILE

7

PRO

VAL

ASN

ALA

ARG

GLU

LYS

TRP

VAL

ILE

8

ALA

SER

GLY

ASP

THR

TYR

SER

LYS

VAL

ARG

9

GLY

ILE

ASN

PHE

ASP

LYS

SER

TYR

PRO

ALA

10

GLY

GLU

TYR

THR

ILE

ASN

ALA

GLN

VAL

11

ASP

ILE

VAL

SER

GLY

GLU

ARG

VAL

GLU

GLN

12

SER

MET

THR

VAL

LYS

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_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