BMRB Entry 34042

Name: Structural studies of the Aggregative Adherence Fimbriae of Enteroaggregative Escherichia coli
Published: 2017-10-13

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PDB ID: 5lvy
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34042
MolProbity Validation Chart

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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:

Structural studies of the Aggregative Adherence Fimbriae of Enteroaggregative Escherichia coli

Deposition date:

2016-09-14

Original release date:

2017-10-13

Authors:

Liu, B.; Matthews, S.

Citation:

Citation: Jnsson, R.; Liu, B.; Struve, C.; Yang, Y.; Jrgensen, R.; Xu, Y.; Jenssen, H.; Krogfelt, K.; Matthews, S.. "Structural and functional studies of Escherichia coli aggregative adherence fimbriae (AAF/V) reveal a deficiency in extracellular matrix binding." Biochim. Biophys. Acta 1865, 304-311 (2017).
PubMed: 27939608

Assembly members:

Assembly members:
entity_1, polymer, 154 residues, 16493.498 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-Pichia pastoris shuttle vector pPpARG4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: NSCSLSISSPDPVTYTIPTD KGDKYINFKLDVPDPRCKAL GGTVYFWGADTRDGKLVMKK GQDKYTLMTTYGGAVQQQLG GGYGYYHVSQKTPPQTISGV VSKNVGYKPGQYTVELTGFF SLNDNKQANPTPSSLTSKAA GKNIVSSTGTITIS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	614
15N chemical shifts	130
1H chemical shifts	917

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 154 residues - 16493.498 Da.

1

ASN

SER

CYS

SER

LEU

SER

ILE

SER

PRO

2

ASP

PRO

VAL

THR

TYR

THR

ILE

PRO

THR

ASP

3

LYS

GLY

ASP

LYS

TYR

ILE

ASN

PHE

LYS

LEU

4

ASP

VAL

PRO

ASP

PRO

ARG

CYS

LYS

ALA

LEU

5

GLY

THR

VAL

TYR

PHE

TRP

GLY

ALA

ASP

6

THR

ARG

ASP

GLY

LYS

LEU

VAL

MET

LYS

7

GLY

GLN

ASP

LYS

TYR

THR

LEU

MET

THR

8

TYR

GLY

ALA

VAL

GLN

LEU

GLY

9

GLY

TYR

GLY

TYR

HIS

VAL

SER

GLN

10

LYS

THR

PRO

GLN

THR

ILE

SER

GLY

VAL

11

VAL

SER

LYS

ASN

VAL

GLY

TYR

LYS

PRO

GLY

12

GLN

TYR

THR

VAL

GLU

LEU

THR

GLY

PHE

13

SER

LEU

ASN

ASP

ASN

LYS

GLN

ALA

ASN

PRO

14

THR

PRO

SER

LEU

THR

SER

LYS

ALA

15

GLY

LYS

ASN

ILE

VAL

SER

THR

GLY

THR

16

ILE

THR

ILE

SER

Samples:

sample_1: entity_1, na, mM; sodium acetate 50 ± 0.2 mM; sodium chloride 50 ± 0.2 nM

sample_conditions_1: ionic strength: 100 mM; pH: 5.0; pressure: 1 bar; temperature: 298 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 HN(CO)CA	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 HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - structure calculation

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

NMR spectrometers:

Bruker DRX 800 MHz
Bruker DRX 600 MHz

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