BMRB Entry 28131

Name: 1H 15N 13C Resonance Assignments of Receptor Binding Domain 2 of CDTb (757-876)
Published: 2021-07-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28131

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title: 1H 15N 13C Resonance Assignments of Receptor Binding Domain 2 of CDTb (757-876) PubMed: 33034833

Deposition date: 2020-06-10 Original release date: 2021-07-16

Authors: Cook, Mary; Varney, Kristen; Godoy-Ruiz, Raquel; Weber, David

Citation: Cook, Mary; Varney, Kristen; Godoy-Ruiz, Raquel; Weber, David. "1HN, 13C, AND 15N RESONANCE ASSIGNMENTS OF RECEPTOR BINDING DOMAIN 2 (CDTB, RESIDUES 757-876)" Biomol. NMR Assign. 15, 35-39 (2021).

Assembly members:
CDTb_receptor_binding_domain_2, polymer, 125 residues, Formula weight is not available

Natural source: Common Name: Clostridium difficile Taxonomy ID: 1496 Superkingdom: Bacteria Kingdom: not available Genus/species: Clostridium difficile

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21

Entity Sequences (FASTA):
CDTb_receptor_binding_domain_2: DDDDKTDQEIMDAHKIYFAD LNFNPSTGNTYINGMYFAPT QTNKEALDYIQKYRVEATLQ YSGFKDIGTKDKEMRNYLGD PNQPKTNYVNLRSYFTGGEN IMTYKKLRIYAITPDDRELL VLSVD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	431
15N chemical shifts	116
1H chemical shifts	574

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RBD2	1

Entities:

Entity 1, RBD2 125 residues - Formula weight is not available

6 THR corresponds to 757 THR in full-length CDTb; start author sequence numbering at 6 THR. (There is a HIS-tag present).

1

ASP

LYS

THR

ASP

GLN

GLU

ILE

2

MET

ASP

ALA

HIS

LYS

ILE

TYR

PHE

ALA

ASP

3

LEU

ASN

PHE

ASN

PRO

SER

THR

GLY

ASN

THR

4

TYR

ILE

ASN

GLY

MET

TYR

PHE

ALA

PRO

THR

5

GLN

THR

ASN

LYS

GLU

ALA

LEU

ASP

TYR

ILE

6

GLN

LYS

TYR

ARG

VAL

GLU

ALA

THR

LEU

GLN

7

TYR

SER

GLY

PHE

LYS

ASP

ILE

GLY

THR

LYS

8

ASP

LYS

GLU

MET

ARG

ASN

TYR

LEU

GLY

ASP

9

PRO

ASN

GLN

PRO

LYS

THR

ASN

TYR

VAL

ASN

10

LEU

ARG

SER

TYR

PHE

THR

GLY

GLU

ASN

11

ILE

MET

THR

TYR

LYS

LEU

ARG

ILE

TYR

12

ALA

ILE

THR

PRO

ASP

ARG

GLU

LEU

13

VAL

LEU

SER

VAL

ASP

Samples:

RBD2: HEPES 15 mM; sodium chloride 150 mM; D2O 10%; RBD2, [U-13C; U-15N], 0.5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	RBD2	isotropic	sample_conditions_1
3D HNCA	RBD2	isotropic	sample_conditions_1
3D HN(CO)CA	RBD2	isotropic	sample_conditions_1
3D HNCACB	RBD2	isotropic	sample_conditions_1
3D CBCA(CO)NH	RBD2	isotropic	sample_conditions_1
3D HNCO	RBD2	isotropic	sample_conditions_1
3D H(CCO)NH	RBD2	isotropic	sample_conditions_1
3D C(CO)NH	RBD2	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

CcpNMR, CCPN - chemical shift assignment, peak picking

CSI, Berjanskii, Wishart - secondary structure prediction

NMR spectrometers:

Bruker Avance III 950 MHz
Bruker Avance III 600 MHz
Bruker Avance 800 MHz

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