BMRB Entry 25745

Name: Structure of the N-terminal domain of the metalloprotease PrtV from Vibrio cholerae
Published: 2015-08-24

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PDB ID: 5abk
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25745
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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:

Structure of the N-terminal domain of the metalloprotease PrtV from Vibrio cholerae

Deposition date:

2015-08-07

Original release date:

2015-08-24

Authors:

Persson, Cecilia; Mayzel, M.; Edwin, A.; Wai, S.; Ohman, A.; Sauer-eriksson, A.; Karlsson, G.

Citation:

Citation: Edwin, A.; Mayzel, M.; Persson, Cecilia; Wai, S.; Ohman, A.; Karlsson, G.; Sauer-eriksson, A.. "Structure of the N-terminal domain of the metalloprotease PrtV from Vibrio cholerae" Protein Sci. 24, 2076-2080 (2015).
PubMed: 26434928

Assembly members:

Assembly members:
METALLOPROTEASE, polymer, 84 residues, 9348.8769 Da.

Natural source:

Natural source: Common Name: Vibrio cholerae Taxonomy ID: 666 Superkingdom: Bacteria Kingdom: not available Genus/species: Vibrio cholerae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET1a-TrxA

Entity Sequences (FASTA):

Entity Sequences (FASTA):
METALLOPROTEASE: GAMAQTPIDLGVVNEDKLIE MLVRTGQIPADASDVDKRIA LERYLEEKIRSGFKGDAQFG KKALEQRAKILKVIDKQKGP HKAR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	357
15N chemical shifts	79
1H chemical shifts	549

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	METALLOPROTEASE	1

Entities:

Entity 1, METALLOPROTEASE 84 residues - 9348.8769 Da.

1

GLY

ALA

MET

ALA

GLN

THR

PRO

ILE

ASP

LEU

2

GLY

VAL

ASN

GLU

ASP

LYS

LEU

ILE

GLU

3

MET

LEU

VAL

ARG

THR

GLY

GLN

ILE

PRO

ALA

4

ASP

ALA

SER

ASP

VAL

ASP

LYS

ARG

ILE

ALA

5

LEU

GLU

ARG

TYR

LEU

GLU

LYS

ILE

ARG

6

SER

GLY

PHE

LYS

GLY

ASP

ALA

GLN

PHE

GLY

7

LYS

ALA

LEU

GLU

GLN

ARG

ALA

LYS

ILE

8

LEU

LYS

VAL

ILE

ASP

LYS

GLN

LYS

GLY

PRO

9

HIS

LYS

ALA

ARG

Samples:

sample_1: METALLOPROTEASE, [U-13C; U-15N], 0.7 mM; Pi 20 mM

sample_conditions_1: pH: 7.000; pressure: 1 atm; temperature: 283.000 K

Experiments:

Name	Sample	Sample state	Sample conditions
Backbone exps	sample_1	solution	sample_conditions_1
NOE exps	sample_1	solution	sample_conditions_1

Software:

AutoDep v4.3, PDBe - chemical shift assignment

ccpn vany, CCPN - chemical shift assignment

x-plor vany, Brunger - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

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