BMRB Entry 34719

Name: Solution structure of the PulM C-terminal domain from Klebsiella oxytoca
Published: 2023-01-13

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PDB ID: 7ze0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34719
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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 the PulM C-terminal domain from Klebsiella oxytoca

Deposition date:

2022-03-30

Original release date:

2023-01-13

Authors:

Lopez-Castilla, A.; Bardiaux, B.; Nilges, M.; Francetic, O.; Izadi-Pruneyre, N.

Citation:

Citation: Dazzoni, R.; Li, Y.; Lopez-Castilla, A.; Brier, S.; Mechaly, A.; Cordier, F.; Haouz, A.; Nilges, M.; Francetic, O.; Bardiaux, B.; Izadi-Pruneyre, N.. "Structure and dynamic association of an assembly platform subcomplex of the bacterial type II secretion system" Structure 31, 152-165 (2023).
PubMed: 36586404

Assembly members:

Assembly members:
entity_1, polymer, 83 residues, 8938.165 Da.

Natural source:

Natural source: Common Name: Klebsiella oxytoca Taxonomy ID: 571 Superkingdom: Bacteria Kingdom: not available Genus/species: Klebsiella oxytoca

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SEEPSTVIMREAARHGLTIV RLQPQGSRLSLTVQPADFQA LMAWLDALGQAGMTTATLAV TAVAQQPGWVTVNTLVLERS DEK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	311
15N chemical shifts	78
1H chemical shifts	437

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	1

Entities:

Entity 1, unit_1 83 residues - 8938.165 Da.

1

SER

GLU

PRO

SER

THR

VAL

ILE

MET

ARG

2

GLU

ALA

ARG

HIS

GLY

LEU

THR

ILE

VAL

3

ARG

LEU

GLN

PRO

GLN

GLY

SER

ARG

LEU

SER

4

LEU

THR

VAL

GLN

PRO

ALA

ASP

PHE

GLN

ALA

5

LEU

MET

ALA

TRP

LEU

ASP

ALA

LEU

GLY

GLN

6

ALA

GLY

MET

THR

ALA

THR

LEU

ALA

VAL

7

THR

ALA

VAL

ALA

GLN

PRO

GLY

TRP

VAL

8

THR

VAL

ASN

THR

LEU

VAL

LEU

GLU

ARG

SER

9

ASP

GLU

LYS

Samples:

sample_1: PulM, [U-100% 13C; U-100% 15N], 400 uM; Hepes 50 mM; sodium chloride 50 mM

sample_2: PulM, 50% [13C, 15N] and 50% [12C, 14N], 400 uM; Hepes 50 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HMQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	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 13C/15N-filtered NOESY	sample_2	isotropic	sample_conditions_1
2D HBCBCGCDHD	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDCEHE	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

CcpNmr Analysis, CCPN - chemical shift assignment, peak picking

TopSpin, Bruker Biospin - processing

NMR spectrometers:

Bruker AVANCE NEO 800 MHz

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