BMRB Entry 6779

Name: Solution Structure of the type 1 pilus assembly platform FimD(25-125)
Published: 2005-10-18

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PDB ID: 1zdx
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6779
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution Structure of the type 1 pilus assembly platform FimD(25-125)

Deposition date:

2005-08-17

Original release date:

2005-10-18

Authors:

Nishiyama, M.; Horst, R.; Herrmann, R.; Vetsch, M.; Bettendorff, P.; Ignatov, O.; Grutter, M.; Wuthrich, K.; Glockshuber, R.; Capitani, G.

Citation:

Citation: Nishiyama, M.; Horst, R.; Herrmann, R.; Vetsch, M.; Bettendorff, P.; Ignatov, O.; Grutter, M.; Wuthrich, K.; Glockshuber, R.; Capitani, G.. "Structural basis of chaperone-subunit complex recognition by type 1 pilus assembly platform FimD" EMBO J. 24, 2075-2086 (2005).
PubMed: 15920478

Assembly members:

Assembly members:
FimD, polymer, 101 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FimD: GQELPPGTYRVDIYLNNGYM ATRDVTFNTGDSEQGIVPCL TRAQLASMGLNTASVAGMNL LADDACVPLTTMVQDATAHL DVGQQRLNLTIPQAFMSNRA R

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
1H chemical shifts	657
13C chemical shifts	310
15N chemical shifts	107

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Outer membrane usher protein FimD	1

Entities:

Entity 1, Outer membrane usher protein FimD 101 residues - Formula weight is not available

1

GLY

GLN

GLU

LEU

PRO

GLY

THR

TYR

ARG

2

VAL

ASP

ILE

TYR

LEU

ASN

GLY

TYR

MET

3

ALA

THR

ARG

ASP

VAL

THR

PHE

ASN

THR

GLY

4

ASP

SER

GLU

GLN

GLY

ILE

VAL

PRO

CYS

LEU

5

THR

ARG

ALA

GLN

LEU

ALA

SER

MET

GLY

LEU

6

ASN

THR

ALA

SER

VAL

ALA

GLY

MET

ASN

LEU

7

LEU

ALA

ASP

ALA

CYS

VAL

PRO

LEU

THR

8

THR

MET

VAL

GLN

ASP

ALA

THR

ALA

HIS

LEU

9

ASP

VAL

GLY

GLN

ARG

LEU

ASN

LEU

THR

10

ILE

PRO

GLN

ALA

PHE

MET

SER

ASN

ARG

ALA

11

ARG

Samples:

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

sample_cond_1: pH: 7.0; temperature: 293 K; pressure: 1 atm

Experiments:

Name	Sample	Sample state	Sample conditions
3D 15N-separated NOESY	not available	not available	not available
3D 13C-separated NOESY	not available	not available	not available

Software:

XWINNMR v3.5 - collection

ATHNOS-CANDID - structure solution, refinement

NMR spectrometers:

Bruker AVANCE 900 MHz

BMRB	6629
PDB	1ZDV 1ZDX 1ZE3 3BWU 3RFZ 4J3O
DBJ	BAB38699 BAE78310 BAI28636 BAI33777 BAJ46031
EMBL	CAQ34665 CAR16035 CCP96085 CCQ07908 CCW23202
GB	AAA97213 AAC77273 AAG59499 AAY89700 ABF06193
REF	NP_290933 NP_313303 NP_418737 WP_000120908 WP_000120909
SP	P30130
AlphaFold	P30130