BMRB Entry 26541

Name: Backbone Chemical Shift Assignment of the FimH lectin domain from Escherichia coli
Published: 2015-05-11

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26541

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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 Chemical Shift Assignment of the FimH lectin domain from Escherichia coli

Deposition date:

2015-03-13

Original release date:

2015-05-11

Authors:

Fiege, Brigitte; Ernst, Beat

Citation:

Citation: Fiege, Brigitte; Rabbani, Said; Preston, Roland; Jakob, Roman; Zihlmann, Pascal; Schwardt, Oliver; Jiang, Xiaohua; Maier, Timm; Ernst, Beat. "he Tyrosine Gate of the Bacterial Lectin FimH: A Conformational Analysis by NMR Spectroscopy and X-ray Crystallography" Chembiochem 16, 1235-1246 (2015).
PubMed: 25940742

Assembly members:

Assembly members:
FimH-CRD, polymer, 173 residues, 18643.8386 Da.

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: pDsbA3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FimH-CRD: FACKTANGTAIPIGGGSANV YVNLAPVVNVGQNLVVDLST QIFCHNDYPETITDYVTLQR GSAYGGVLSNFSGTVKYSGS SYPFPTTSETPRVVYNSRTD KPWPVALYLTPVSSAGGVAI KAGSLIAVLILRQTNNYNSD DFQFVWNIYANNDVVVPTGL VPRGSLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	510
15N chemical shifts	173
1H chemical shifts	191

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FimH-CRD	1

Entities:

Entity 1, FimH-CRD 173 residues - 18643.8386 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

TYR

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

GLY

LEU

17

VAL

PRO

ARG

GLY

SER

LEU

GLU

HIS

18

HIS

Samples:

sample_1: FimH-CRD, [U-100% 13C; U-100% 15N], 0.6 mM; sodium phosphate 25.0 mM; TSP-d4 0.1 mM; H2O 90%; D2O 10%

condition_1: ionic strength: 0.025 M; pH: 6.800; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	condition_1
3D HNCA	sample_1	isotropic	condition_1
3D HN(CO)CA	sample_1	isotropic	condition_1
3D HN(CA)CO	sample_1	isotropic	condition_1
3D HNCO	sample_1	isotropic	condition_1
3D HNCACB	sample_1	isotropic	condition_1
3D CBCA(CO)NH	sample_1	isotropic	condition_1

Software:

CcpNmr_Analysis v2.3, CCPN - chemical shift assignment

Sparta vany, Yang Shen, Ad Bax - chemical shift calculation

Topspin v3.2, Bruker - data acquisition, processing

NMR spectrometers:

Bruker Avance 700 MHz

UniProt	A2IC68_ECOLX
PDB	4BUQ 4CST 1UWF 1TR7 3MCY 4CSS 4AV5 4AV4 2VCO 1KLF 4AUU 1QUN 4CA4 4LOV 3ZPD 4X50 4X5Q 4X5R 4X5P
BMRB	19066
GB	CAM92099.1
AlphaFold	A2IC68