BMRB Entry 18338

Name: C-terminal propeptide (PPc) region of vibrio extracellular metalloprotease
Published: 2013-01-03

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PDB ID: 2luw
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18338
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

C-terminal propeptide (PPc) region of vibrio extracellular metalloprotease

Deposition date:

2012-03-20

Original release date:

2013-01-03

Authors:

Yun, Ji-Hye

Citation:

Citation: Yun, Ji-Hye; Kim, Heeyoun; Park, Jung Eun; Lee, Jung Sup; Lee, Weontae. "Solution structure and dynamics of C-terminal regulatory domain of Vibrio vulnificus extracellular metalloprotease." Biochem. Biophys. Res. Commun. 430, 541-546 (2013).
PubMed: 23228665

Assembly members:

Assembly members:
C-terminal_propeptide_(PPc)_region_of_vibrio_extracellular_metalloprotease, polymer, 101 residues, Formula weight is not available

Natural source:

Natural source: Common Name: vibrio vulnificus Taxonomy ID: 672 Superkingdom: Bacteria Kingdom: not available Genus/species: vibrio vulnificus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
C-terminal_propeptide_(PPc)_region_of_vibrio_extracellular_metalloprotease: GNVLKNNTPVSNLTGNKGSE VFYTFTVDRNATAVVSISGG SGDADLYLKAGSKPTTSSWD CRPYRYGNNESCSVSAAPGT TYHVMIKGYSNYSGVTLKLQ Y

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_of_PPc_region

Data type	Count
13C chemical shifts	368
15N chemical shifts	102
1H chemical shifts	631

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PPc	1

Entities:

Entity 1, PPc 101 residues - Formula weight is not available

1

GLY

ASN

VAL

LEU

LYS

ASN

THR

PRO

VAL

2

SER

ASN

LEU

THR

GLY

ASN

LYS

GLY

SER

GLU

3

VAL

PHE

TYR

THR

PHE

THR

VAL

ASP

ARG

ASN

4

ALA

THR

ALA

VAL

SER

ILE

SER

GLY

5

SER

GLY

ASP

ALA

ASP

LEU

TYR

LEU

LYS

ALA

6

GLY

SER

LYS

PRO

THR

SER

TRP

ASP

7

CYS

ARG

PRO

TYR

ARG

TYR

GLY

ASN

GLU

8

SER

CYS

SER

VAL

SER

ALA

PRO

GLY

THR

9

THR

TYR

HIS

VAL

MET

ILE

LYS

GLY

TYR

SER

10

ASN

TYR

SER

GLY

VAL

THR

LEU

LYS

LEU

GLN

11

TYR

Samples:

PPc_domain_of_vEP: PPc protein, [U-100% 15N], 0.6 mM; HEPES (pH 7.0) 20 mM; Sodium chloride 100 mM; DTT 10 mM; NaN3 0.01%; H2O 90%; D2O 10%

PPc_domain_of_vEP_2: PPc protein, [U-100% 13C; U-100% 15N], 0.6 mM; HEPES (pH 7.0) 20 mM; Sodium chloride 100 mM; DTT 10 mM; NaN3 0.01%; H2O 90%; D2O 10%

0.6mM_PPc_protein: ionic strength: 20 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	PPc_domain_of_vEP	isotropic	0.6mM_PPc_protein
3D 1H-15N NOESY	PPc_domain_of_vEP	isotropic	0.6mM_PPc_protein
3D 1H-13C NOESY	PPc_domain_of_vEP_2	isotropic	0.6mM_PPc_protein
3D HNCACB	PPc_domain_of_vEP_2	isotropic	0.6mM_PPc_protein
3D HBHA(CO)NH	PPc_domain_of_vEP_2	isotropic	0.6mM_PPc_protein
3D HNCA	PPc_domain_of_vEP_2	isotropic	0.6mM_PPc_protein
3D HNCO	PPc_domain_of_vEP_2	isotropic	0.6mM_PPc_protein
3D HBHA(CO)NH	PPc_domain_of_vEP_2	isotropic	0.6mM_PPc_protein
3D HCCH-TOCSY	PPc_domain_of_vEP_2	isotropic	0.6mM_PPc_protein

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker DRX 500 MHz
Bruker DRX 900 MHz

PDB	2LUW
DBJ	BAC22940 BAC97491 BAI66359 BAI66360 BAI66361
EMBL	CAM34546
GB	AAC44789 AAC45343 AAC72410 AAO07886 ABI95803
REF	WP_011081880 WP_015728348 WP_026050529 WP_026130953 WP_038940484