BMRB Entry 19053

Name: Solution structure of FimA wt
Published: 2013-11-11

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PDB ID: 2m5g
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19053
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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:

Solution structure of FimA wt

Deposition date:

2013-02-24

Original release date:

2013-11-11

Authors:

Walczak, Michal; Puorger, Chasper; Glockshuber, Rudi; Wider, Gerhard

Citation:

Citation: Walczak, Michal; Puorger, Chasper; Glockshuber, Rudi; Wider, Gerhard. "Intramolecular Donor Strand Complementation in the E. coli Type 1 Pilus Subunit FimA Explains the Existence of FimA Monomers As Off-Pathway Products of Pilus Assembly That Inhibit Host Cell Apoptosis." J. Mol. Biol. 426, 542-549 (2014).
PubMed: 24184277

Assembly members:

Assembly members:
FimA_wt, polymer, 159 residues, 15835.380 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: pET-11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FimA_wt: AATTVNGGTVHFKGEVVNAA CAVDAGSVDQTVQLGQVRTA SLAQEGATSSAVGFNIQLND CDTNVASKAAVAFLGTAIDA GHTNVLALQSSAAGSATNVG VQILDRTGAALTLDGATFSS ETTLNNGTNTIPFQARYFAT GAATPGAANADATFKVQYQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	668

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FimA wt	1

Entities:

Entity 1, FimA wt 159 residues - 15835.380 Da.

1

ALA

THR

VAL

ASN

GLY

THR

VAL

2

HIS

PHE

LYS

GLY

GLU

VAL

ASN

ALA

3

CYS

ALA

VAL

ASP

ALA

GLY

SER

VAL

ASP

GLN

4

THR

VAL

GLN

LEU

GLY

GLN

VAL

ARG

THR

ALA

5

SER

LEU

ALA

GLN

GLU

GLY

ALA

THR

SER

6

ALA

VAL

GLY

PHE

ASN

ILE

GLN

LEU

ASN

ASP

7

CYS

ASP

THR

ASN

VAL

ALA

SER

LYS

ALA

8

VAL

ALA

PHE

LEU

GLY

THR

ALA

ILE

ASP

ALA

9

GLY

HIS

THR

ASN

VAL

LEU

ALA

LEU

GLN

SER

10

SER

ALA

GLY

SER

ALA

THR

ASN

VAL

GLY

11

VAL

GLN

ILE

LEU

ASP

ARG

THR

GLY

ALA

12

LEU

THR

LEU

ASP

GLY

ALA

THR

PHE

SER

13

GLU

THR

LEU

ASN

GLY

THR

ASN

THR

14

ILE

PRO

PHE

GLN

ALA

ARG

TYR

PHE

ALA

THR

15

GLY

ALA

THR

PRO

GLY

ALA

ASN

ALA

16

ASP

ALA

THR

PHE

LYS

VAL

GLN

TYR

GLN

Samples:

sample_1: FimA_wt, [U-99% 13C; U-99% 15N], 2 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0.08 M; pH: 7; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Brunger, Adams, Clore, Gros, Nilges and Read, Goddard, Guntert, Mumenthaler and Wuthrich, Keller and Wuthrich - chemical shift assignment, refinement, structure solution

NMR spectrometers:

Bruker Avance 750 MHz
Bruker Avance 900 MHz

BMRB	25334
PDB	2M5G 2MX3 2N7H 3SQB 4DWH
DBJ	BAE78307 BAJ46028
EMBL	CAA25489 CAQ34662 CAR16032 CAS12169 CCJ47011
GB	AAA24389 AAA97210 AAC77270 AAG35683 AAO84630
REF	NP_418734 WP_000695553 WP_000695557 WP_000695559 WP_000695560
SP	P04128
AlphaFold	P04128