BMRB Entry 17720

Name: Solution Structure of N-terminal Cytosolic Domain of Rhomboid Intramembrane Protease from Escherichia Coli
Published: 2012-09-24

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PDB ID: 2lep
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17720
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution Structure of N-terminal Cytosolic Domain of Rhomboid Intramembrane Protease from Escherichia Coli PubMed: 22963263

Deposition date: 2011-06-20 Original release date: 2012-09-24

Authors: Sherratt, Allison; Ghasriani, Houman; Goto, Natalie

Citation: Sherratt, Allison; Blais, David; Ghasriani, Houman; Pezacki, John Paul; Goto, Natalie. "Activity-based protein profiling of the Escherichia coli GlpG rhomboid protein delineates the catalytic core." Biochemistry 51, 7794-7803 (2012).

Assembly members:
NGlpG, polymer, 63 residues, 7142.065 Da.

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

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

Entity Sequences (FASTA):
NGlpG: MLMITSFANPRVAQAFVDYM ATQGVILTIQQHNQSDVWLA DESQAERVRAELARFLENPA DLD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	251
15N chemical shifts	68
1H chemical shifts	394

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NGlpG	1

Entities:

Entity 1, NGlpG 63 residues - 7142.065 Da.

1

MET

LEU

MET

ILE

THR

SER

PHE

ALA

ASN

PRO

2

ARG

VAL

ALA

GLN

ALA

PHE

VAL

ASP

TYR

MET

3

ALA

THR

GLN

GLY

VAL

ILE

LEU

THR

ILE

GLN

4

GLN

HIS

ASN

GLN

SER

ASP

VAL

TRP

LEU

ALA

5

ASP

GLU

SER

GLN

ALA

GLU

ARG

VAL

ARG

ALA

6

GLU

LEU

ALA

ARG

PHE

LEU

GLU

ASN

PRO

ALA

7

ASP

LEU

ASP

Samples:

sample_1: Nglpg, [U-100% 13C; U-100% 15N], 1.0 ± 0.05 mM; H2O 90%; D2O 10%

sample_2: Nglpg, [U-100% 13C; U-100% 15N], 1.0 ± 0.05 mM; D2O 100%

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 293.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR NIH v2.22, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

Varian INOVA 500 MHz

BMRB	19713
PDB	2LEP 2MJA
DBJ	BAB37690 BAE77868 BAG79214 BAI27681 BAI32850
EMBL	CAP77869 CAQ33744 CAR00366 CAR05025 CAR10074
GB	AAG58528 AAN44906 AAN82639 AAP19275 AAT48182
REF	NP_312294 NP_709199 WP_000541600 WP_000928708 WP_000928709
SP	A1AGU7 A7ZSV4 A8A5N2 A8AQX4 B1IP42

Biological Magnetic Resonance Data Bank