BMRB Entry 51861

Name: Backbone resonance assignment of the PPIase domain (100-213) of the Legionella pneumophila Mip protein
Published: 2024-04-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51861

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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:

Backbone resonance assignment of the PPIase domain (100-213) of the Legionella pneumophila Mip protein

Deposition date:

2023-02-27

Original release date:

2024-04-16

Authors:

Wiedemann, Christoph; Perez Carrillo, Victor Hugo; Hellmich, Ute

Citation:

Citation: Wiedemann, C.; Whittaker, J.; Perez Carrillo, V.; Goretzki, B.; Dajka, M.; Tebbe, F.; Harder, J-M; Krajczy, P.; Joseph, B.; Hausch, F.; Guskov, A.; Hellmich, U.. "Legionella pneumophila macrophage infectivity potentiator protein appendage domains modulate protein dynamics and inhibitor binding" Int. J. Biol. Macromol. 252, 126366-126366 (2023).
PubMed: 37633566

Assembly members:

Assembly members:
entity_1, polymer, 114 residues, Formula weight is not available

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 Vector: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GVVVLPSGLQYKVINSGNGV KPGKSDTVTVEYTGRLIDGT VFDSTEKTGKPATFQVSQVI PGWTEALQLMPAGSTWEIYV PSGLAYGPRSVGGPIGPNET LIFKIHLISVKKSS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	111
15N chemical shifts	100
1H chemical shifts	100

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	LpMIP	1

Entities:

Entity 1, LpMIP 114 residues - Formula weight is not available

1

GLY

VAL

LEU

PRO

SER

GLY

LEU

GLN

2

TYR

LYS

VAL

ILE

ASN

SER

GLY

ASN

GLY

VAL

3

LYS

PRO

GLY

LYS

SER

ASP

THR

VAL

THR

VAL

4

GLU

TYR

THR

GLY

ARG

LEU

ILE

ASP

GLY

THR

5

VAL

PHE

ASP

SER

THR

GLU

LYS

THR

GLY

LYS

6

PRO

ALA

THR

PHE

GLN

VAL

SER

GLN

VAL

ILE

7

PRO

GLY

TRP

THR

GLU

ALA

LEU

GLN

LEU

MET

8

PRO

ALA

GLY

SER

THR

TRP

GLU

ILE

TYR

VAL

9

PRO

SER

GLY

LEU

ALA

TYR

GLY

PRO

ARG

SER

10

VAL

GLY

PRO

ILE

GLY

PRO

ASN

GLU

THR

11

LEU

ILE

PHE

LYS

ILE

HIS

LEU

ILE

SER

VAL

12

LYS

SER

Samples:

sample_1: LpMip100-213, [U-99% 13C; U-99% 15N], 120 uM; TRIS 25 mM; sodium chloride 150 mM; sodium azide 0.05%; DSS 0.1 mM; D2O, [U-99% 2H], 10%

sample_conditions_1: ionic strength: 0.175 M; pH: 7; pressure: 1 atm; temperature: 298.2 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
T1/R1 relaxation	sample_1	isotropic	sample_conditions_1
T2/R2 relaxation	sample_1	isotropic	sample_conditions_1
1H-15N heteronoe	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR v2.5 - chemical shift assignment, data analysis, peak picking

TOPSPIN - collection, processing

SPARKY - processing

NMR spectrometers:

Bruker AVANCE NEO 600 MHz