BMRB Entry 19254

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19254

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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:

NMR assignments and backbone amide relaxation data (T1-T2) for the complex of the Y48A mutant of the FimH adhesin carbohydrate-binding domain with heptyl-mannose

Deposition date:

2013-05-22

Original release date:

2014-02-13

Authors:

Vanwetswinkel, Sophie; Van Nuland, N.

Citation:

Citation: Vanwetswinkel, Sophie; Volkov, Alexander; Sterckx, Yann; Garcia-Pino, Abel; Buts, Lieven; Vranken, Wim; Bouckaert, Julie; Roy, Rene; Wyns, Lode; van Nuland, Nico. "Study of the Structural and Dynamic Effects in the FimH Adhesin upon alfa-D-Heptyl Mannose Binding" J. Med. Chem. 57, 1416-1427 (2014).
PubMed: 24476493

Assembly members:

Assembly members:
FIMH_Y48A_mutant, polymer, 158 residues, 16904.8881 Da.
Heptyl Alpha-D-mannopyrannoside, non-polymer, 278.342 Da.

Natural source:

Natural source: Common Name: Enterobacteria 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: pET24a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FIMH_Y48A_mutant: FACKTANGTAIPIGGGSANV YVNLAPVVNVGQNLVVDLST QIFCHNDAPETITDYVTLQR GSAYGGVLSNFSGTVKYSGS SYPFPTTSETPRVVYNSRTD KPWPVALYLTPVSSAGGVAI KAGSLIAVLILRQTNNYNSD DFQFVWNIYANNDVVVPT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T2_relaxation
- heteronuclear_T2_list_1

Data type	Count
15N chemical shifts	170
1H chemical shifts	188
T1 relaxation values	133
T2 relaxation values	130

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FIMH Y48A mutant	1
2	heptyl-mannose	2

Entities:

Entity 1, FIMH Y48A mutant 158 residues - 16904.8881 Da.

1

PHE

ALA

CYS

LYS

THR

ALA

ASN

GLY

THR

ALA

2

ILE

PRO

ILE

GLY

SER

ALA

ASN

VAL

3

TYR

VAL

ASN

LEU

ALA

PRO

VAL

ASN

VAL

4

GLY

GLN

ASN

LEU

VAL

ASP

LEU

SER

THR

5

GLN

ILE

PHE

CYS

HIS

ASN

ASP

ALA

PRO

GLU

6

THR

ILE

THR

ASP

TYR

VAL

THR

LEU

GLN

ARG

7

GLY

SER

ALA

TYR

GLY

VAL

LEU

SER

ASN

8

PHE

SER

GLY

THR

VAL

LYS

TYR

SER

GLY

SER

9

SER

TYR

PRO

PHE

PRO

THR

SER

GLU

THR

10

PRO

ARG

VAL

TYR

ASN

SER

ARG

THR

ASP

11

LYS

PRO

TRP

PRO

VAL

ALA

LEU

TYR

LEU

THR

12

PRO

VAL

SER

ALA

GLY

VAL

ALA

ILE

13

LYS

ALA

GLY

SER

LEU

ILE

ALA

VAL

LEU

ILE

14

LEU

ARG

GLN

THR

ASN

TYR

ASN

SER

ASP

15

ASP

PHE

GLN

PHE

VAL

TRP

ASN

ILE

TYR

ALA

16

ASN

ASP

VAL

PRO

THR

Entity 2, heptyl-mannose - C13 H26 O6 - 278.342 Da.

1

KGM

Samples:

sample_1: FIMH Y48A mutant, [U-100% 15N], 0.0011 M; sodium phosphate 0.02 M; sodium chloride 0.1 M; heptyl alpha-D-mannopyranoside (heptyl mannose) 1.3 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0.12 M; pH: 6.000; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	solution	sample_conditions_1
3D 1H-15N NOESY	sample_1	solution	sample_conditions_1
2D 1H-15N HSQC (inverse recovery)	sample_1	solution	sample_conditions_1
2D 1H-15N HSQC (CPMG)	sample_1	solution	sample_conditions_1

Software:

ANALYSIS v2.1 -

NMRPipe vany -

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - spectrum analysis, spectrum display

NMR spectrometers:

Varian Direct-Drive 600 MHz

UNP	A2IC68_ECOLX
AlphaFold	A2IC68