BMRB Entry 19683

Name: NMR structure of the S-linked glycopeptide sublancin 168
Published: 2014-03-10

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PDB ID: 2mij
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19683
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure of the S-linked glycopeptide sublancin 168

Deposition date:

2013-12-13

Original release date:

2014-03-10

Authors:

Garcia De Gonzalo, Chantal; Zhu, Lingyang; Oman, Trent; van der Donk, Wilfred

Citation:

Citation: Garcia De Gonzalo, Chantal; Zhu, Lingyang; Oman, Trent; van der Donk, Wilfred. "NMR structure of the s-linked glycopeptide sublancin 168." ACS Chem. Biol. 9, 796-801 (2014).
PubMed: 24405370

Assembly members:

Assembly members:
sublancin, polymer, 37 residues, 3723.305 Da.
entity_GLC, non-polymer, 180.156 Da.

Natural source:

Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis

Experimental source:

Experimental source: Production method: purified from the natural source Host organism: Bacillus subtilis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
sublancin: GLGKAQCAALWLQCASGGTI GCGGGAVACQNYRQFCR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	65
15N chemical shifts	42
1H chemical shifts	220

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	sublancin	1
2	entity_GLC	2

Entities:

Entity 1, sublancin 37 residues - 3723.305 Da.

1

GLY

LEU

GLY

LYS

ALA

GLN

CYS

ALA

LEU

2

TRP

LEU

GLN

CYS

ALA

SER

GLY

THR

ILE

3

GLY

CYS

GLY

ALA

VAL

ALA

CYS

GLN

4

ASN

TYR

ARG

GLN

PHE

CYS

ARG

Entity 2, entity_GLC - C6 H12 O6 - 180.156 Da.

1

entity_GLC

Samples:

sample_1: 13C,15N-labeled sublancin, [U-98% 13C; U-98% 15N], 2 mM; H2O 90%; D2O 10%

sample_2: sublancin 2 mM; H2O 90%; D2O 10%

sample_3: 15N-labeled sublancin, [U-100% 15N], 2 mM; H2O 90%; D2O 10%

sample_conditions: pH: 7; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions
2D DQF-COSY	sample_2	isotropic	sample_conditions
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions
3D HNCA	sample_1	isotropic	sample_conditions
3D HNHA	sample_3	isotropic	sample_conditions
3D 1H-15N NOESY	sample_3	isotropic	sample_conditions
3D 1H-15N TOCSY	sample_3	isotropic	sample_conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions

Software:

X-PLOR_NIH v2.34, Schwieters, Kuszewski, Tjandra and Clore - refinement

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

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

Varian INOVA 600 MHz
Agilent VNMRS 750 MHz

PDB	2MIJ
EMBL	CAB14066 CEI57357 CEJ77782
GB	AAC12992 AAC63531 AFQ58095 AGG61541 AIC40591
REF	NP_046571 NP_390031 WP_009967544
SP	P68577 P68578
AlphaFold	P68577 P68578