BMRB Entry 34704

Name: Solution structure of the DNA-binding minor pilin FimT from Legionella pneumophila
Published: 2022-02-25

Click here to enlarge.

PDB ID: 7qyi
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34704
MolProbity Validation Chart

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:

Solution structure of the DNA-binding minor pilin FimT from Legionella pneumophila

Deposition date:

2022-01-28

Original release date:

2022-02-25

Authors:

Braus, S.; Hospenthal, M.; Gossert, A.

Citation:

Citation: Braus, Sebastian; Short, Francesca; Holz, Stefanie; Stedman, Matthew; Gossert, Alvar; Hospenthal, Manuela. "The molecular basis of FimT-mediated DNA uptake during bacterial natural transformation" Nat. Commun. 13, 1065-1065 (2022).
PubMed: 35246533

Assembly members:

Assembly members:
entity_1, polymer, 125 residues, 14379.359 Da.

Natural source:

Natural source: Common Name: Legionella pneumophila Taxonomy ID: 446 Superkingdom: Bacteria Kingdom: not available Genus/species: Legionella pneumophila

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: IQNNERETLVNSIKTAIQYS KIQAIHLGHPIYLLPFGSNE NWSRGMVLAKLNQTTNKTEL IHQWQWSSNSWNINWKGVDS NHRIIISNIPNRAMSNGKFI LNNKRTNEKVVVTLNRLGRV RVGGN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	446
15N chemical shifts	139
1H chemical shifts	926

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 125 residues - 14379.359 Da.

1

ILE

GLN

ASN

GLU

ARG

GLU

THR

LEU

VAL

2

ASN

SER

ILE

LYS

THR

ALA

ILE

GLN

TYR

SER

3

LYS

ILE

GLN

ALA

ILE

HIS

LEU

GLY

HIS

PRO

4

ILE

TYR

LEU

PRO

PHE

GLY

SER

ASN

GLU

5

ASN

TRP

SER

ARG

GLY

MET

VAL

LEU

ALA

LYS

6

LEU

ASN

GLN

THR

ASN

LYS

THR

GLU

LEU

7

ILE

HIS

GLN

TRP

GLN

TRP

SER

ASN

SER

8

TRP

ASN

ILE

ASN

TRP

LYS

GLY

VAL

ASP

SER

9

ASN

HIS

ARG

ILE

SER

ASN

ILE

PRO

10

ASN

ARG

ALA

MET

SER

ASN

GLY

LYS

PHE

ILE

11

LEU

ASN

LYS

ARG

THR

ASN

GLU

LYS

VAL

12

VAL

THR

LEU

ASN

ARG

LEU

GLY

ARG

VAL

13

ARG

VAL

GLY

ASN

Samples:

sample_1: FimT, [U-13C; U-15N], 580 uM; NaPi 25 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.2; pressure: 1 Pa; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D NOESY combined	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

CcpNmr Analysis v2.51, CCPN - peak picking

CYANA v3.98.2, Guntert, Mumenthaler and Wuthrich - structure calculation

Amber v20, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - geometry optimization

TopSpin v4.07, Bruker Biospin - collection

NMR spectrometers:

Bruker AVANCE III HD 900 MHz
Bruker AVANCE III HD 600 MHz
Bruker AVANCE NEO 700 MHz

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