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PDB ID: 37ct
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31308
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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

Please specify the pdb ID.

Title:

Solid-State NMR Structure of FtsL, a Cell Division Protein from Mycobacterium tuberculosis, in Lipid Bilayers

Deposition date:

2026-07-14

Original release date:

2026-08-21

Authors:

Fan, J.; Prasad, R.; Zhang, R.; Hu, W.; Cross, T.; Zhou, H.; Hu, Y.

Citation:

Citation: Fan, J.; Prasad, R.; Zhang, R.; Hu, W.; Cross, T.; Zhou, H.; Hu, Y.. "Structure and Membrane Interactions of Two Helices from Mycobacterium tuberculosis FtsL, One Transmembrane and One Amphipathic " .

Assembly members:

Assembly members:
entity_1, polymer, 49 residues, 5212.143 Da.

Natural source:

Natural source: Common Name: Mycobacterium tuberculosis H37Rv Taxonomy ID: 83332 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SNAMERLAARLTSIDLRPRT LANKVPFVVLVIGSLGVGLG LTLWLSTDA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	21

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 49 residues - 5212.143 Da.

1

SER

ASN

ALA

MET

GLU

ARG

LEU

ALA

ARG

2

LEU

THR

SER

ILE

ASP

LEU

ARG

PRO

ARG

THR

3

LEU

ALA

ASN

LYS

VAL

PRO

PHE

VAL

LEU

4

VAL

ILE

GLY

SER

LEU

GLY

VAL

GLY

LEU

GLY

5

LEU

THR

LEU

TRP

LEU

SER

THR

ASP

ALA

Samples:

sample_1: FtsL101-146 protein, [U-100% 15N], 3.6 mM

sample_2: FtsL101-146 protein, [U-15N]-Leu, 3.6 mM

sample_3: FtsL101-146 protein, [U-15N]-Val, 3.6 mM

sample_4: FtsL101-146 protein, [U-15N]-Ile, 3.6 mM

sample_5: FtsL101-146 protein, [U-15N]-Thr, 3.6 mM

sample_6: FtsL101-146 protein, [U-100% 13C], 3.6 mM

sample_conditions_1: ionic strength: 5 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N SAMPI4	sample_1	anisotropic	sample_conditions_1
2D 1H-15N SAMPI4	sample_2	anisotropic	sample_conditions_1
2D 1H-15N SAMPI4	sample_3	anisotropic	sample_conditions_1
2D 1H-15N SAMPI4	sample_4	anisotropic	sample_conditions_1
2D 1H-15N SAMPI4	sample_5	anisotropic	sample_conditions_1
2D 13C-13C DARR	sample_6	isotropic	sample_conditions_1

Software:

TopSpin, Bruker Biospin - chemical shift assignment, collection, data analysis, processing

PyMOL, Schrodinger Inc. - structure calculation

NAMD, NAMD - refinement

VMD, VMD - data analysis

NMR spectrometers:

Bruker AVANCE NEO 600 MHz
Bruker AVANCE III HD 800 MHz

BMRB Entry 31308