BMRB Entry 25235

Name: The solution structure of the FtsH periplasmic N-domain
Published: 2015-01-27

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PDB ID: 2muy
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25235
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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:

The solution structure of the FtsH periplasmic N-domain

Deposition date:

2014-09-18

Original release date:

2015-01-27

Authors:

Scharfenberg, Franka; Serek-Heuberger, Justyna; Martin, Joerg; Lupas, Andrei; Coles, Murray

Citation:

Citation: Scharfenberg, Franka; Serek-Heuberger, Justyna; Coles, Murray; Hartmann, Marcus; Habeck, Michael; Martin, Joerg; Lupas, Andrei; Alva, Vikram. "Structure and Evolution of N-domains in AAA Metalloproteases" J. Mol. Biol. 427, 910-923 (2015).
PubMed: 25576874

Assembly members:

Assembly members:
FtsH-N, polymer, 82 residues, 9545.674 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FtsH-N: MASESNGRKVDYSTFLQEVN NDQVREARINGREINVTKKD SNRYTTYIPVQDPKLLDNLL TKNVKVVGEPPEEPLEHHHH HH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	12
15N chemical shifts	3
1H chemical shifts	19

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FtsH periplasmic N-domain	1

Entities:

Entity 1, FtsH periplasmic N-domain 82 residues - 9545.674 Da.

Residues 97-104 represent a non-native affinity tag, residues 23-24 are a cloning artefact

1

MET

ALA

SER

GLU

SER

ASN

GLY

ARG

LYS

VAL

2

ASP

TYR

SER

THR

PHE

LEU

GLN

GLU

VAL

ASN

3

ASN

ASP

GLN

VAL

ARG

GLU

ALA

ARG

ILE

ASN

4

GLY

ARG

GLU

ILE

ASN

VAL

THR

LYS

ASP

5

SER

ASN

ARG

TYR

THR

TYR

ILE

PRO

VAL

6

GLN

ASP

PRO

LYS

LEU

ASP

ASN

LEU

7

THR

LYS

ASN

VAL

LYS

VAL

GLY

GLU

PRO

8

PRO

GLU

PRO

LEU

GLU

HIS

9

HIS

Samples:

15N-labelled: FtsH-N, [U-100% 15N], 0.7 mM; sodium phosphate 15 mM; sodium chloride 75 mM

13C-15N-labelled: FtsH-N, [U-100% 13C; U-100% 15N], 0.7 mM; sodium phosphate 15 mM; sodium chloride 75 mM

sample_conditions_1: ionic strength: 0.105 M; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D CBCA(CO)NH	13C-15N-labelled	isotropic	sample_conditions_1
3D HNCACB	13C-15N-labelled	isotropic	sample_conditions_1
3D HNCO	13C-15N-labelled	isotropic	sample_conditions_1
3D HN(CA)CO	13C-15N-labelled	isotropic	sample_conditions_1
3D C(CO)NH	13C-15N-labelled	isotropic	sample_conditions_1
3D HCCH-TOCSY	13C-15N-labelled	isotropic	sample_conditions_1
3D CCH NOESY	13C-15N-labelled	isotropic	sample_conditions_1
3D CNH NOESY	13C-15N-labelled	isotropic	sample_conditions_1
3D 1H-15N NOESY	15N-labelled	isotropic	sample_conditions_1
3D 1H-13C NOESY	13C-15N-labelled	isotropic	sample_conditions_1
3D HNHA	15N-labelled	isotropic	sample_conditions_1
3D HNHB	15N-labelled	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis

X-PLOR_NIH v2.9.4, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMR-SPIRIT v1.1, In house - refinement

NMR spectrometers:

Bruker Avance 600 MHz
Bruker DMX 750 MHz
Bruker Avance 900 MHz