BMRB Entry 27935

Name: Backbone 13C, and 15N Chemical Shift Assignments for C3 domain of Adhesin P1.
Published: 2019-12-10

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27935

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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:

Backbone 13C, and 15N Chemical Shift Assignments for C3 domain of Adhesin P1.

Deposition date:

2019-06-04

Original release date:

2019-12-10

Authors:

Riviere, Gwladys; Long, Joanna; Brady, Jeannine

Citation:

Citation: Riviere, Gwladys; Peng, Emily-Qingqing; Brotgandel, Albert; Andring, Jacob; Lakshmanan, Renuk; Agbandje-McKenna, M; McKenna, Robert; Brady, L Jeannine; Long, Joanna. "Characterization of an intermolecular quaternary interaction between discrete segments of the Streptococcus mutans adhesin P1 by NMR Spectroscopy" FEBS J. 287, 2597-2611 (2020).
PubMed: 31782893

Assembly members:

Assembly members:
C3, polymer, 175 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 23

Entity Sequences (FASTA):

Entity Sequences (FASTA):
C3: MASMTGGQQMGRIQINPKKD VTLTLDPADTNNVDGQTIPL NTVFNYRLIGGIIPANHSEE LFKYNFYDDYDQTGDHYTGQ YKVFAKVDITLKNGVIIKSG TELTQYTTAEVDTTKGAITI KFKEAFLRSVSIDSAFQAES YIQMKRIAVGTFENTYINTV NGVTYSSLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	344
15N chemical shifts	117
1H chemical shifts	117

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C3 monomer	1

Entities:

Entity 1, C3 monomer 175 residues - Formula weight is not available

1

MET

ALA

SER

MET

THR

GLY

GLN

MET

2

GLY

ARG

ILE

GLN

ILE

ASN

PRO

LYS

ASP

3

VAL

THR

LEU

THR

LEU

ASP

PRO

ALA

ASP

THR

4

ASN

VAL

ASP

GLY

GLN

THR

ILE

PRO

LEU

5

ASN

THR

VAL

PHE

ASN

TYR

ARG

LEU

ILE

GLY

6

GLY

ILE

PRO

ALA

ASN

HIS

SER

GLU

7

LEU

PHE

LYS

TYR

ASN

PHE

TYR

ASP

TYR

8

ASP

GLN

THR

GLY

ASP

HIS

TYR

THR

GLY

GLN

9

TYR

LYS

VAL

PHE

ALA

LYS

VAL

ASP

ILE

THR

10

LEU

LYS

ASN

GLY

VAL

ILE

LYS

SER

GLY

11

THR

GLU

LEU

THR

GLN

TYR

THR

ALA

GLU

12

VAL

ASP

THR

LYS

GLY

ALA

ILE

THR

ILE

13

LYS

PHE

LYS

GLU

ALA

PHE

LEU

ARG

SER

VAL

14

SER

ILE

ASP

SER

ALA

PHE

GLN

ALA

GLU

SER

15

TYR

ILE

GLN

MET

LYS

ARG

ILE

ALA

VAL

GLY

16

THR

PHE

GLU

ASN

THR

TYR

ILE

ASN

THR

VAL

17

ASN

GLY

VAL

THR

TYR

SER

LEU

GLU

HIS

18

HIS

Samples:

sample_1: C3, [U-100% 15N], 200 uM; C3, [U-100% 13C; U-100% 15N], 500 uM; MES 10 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 5; pressure: 1 atm; temperature: 273 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY-HSQC	sample_1	isotropic	sample_conditions_1

Software:

CCPNMR, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

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