BMRB Entry 25158

Name: Solution structure of Doc48S
Published: 2014-10-13

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PDB ID: 2mte
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25158
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of Doc48S PubMed: 25270376

Deposition date: 2014-08-18 Original release date: 2014-10-13

Authors: Chen, Chao; Feng, Yingang

Citation: Chen, Chao; Cui, Zhenling; Xiao, Yan; Cui, Qiu; Smith, Steven; Lamed, Raphael; Bayer, Edward; Feng, Yingang. "Revisiting the NMR solution structure of the Cel48S type-I dockerin module from Clostridium thermocellum reveals a cohesin-primed conformation" J. Struct. Biol. 188, 188-193 (2014).

Assembly members:
entity_1, polymer, 69 residues, 7670.590 Da.

Natural source: Common Name: firmicutes Taxonomy ID: 1515 Superkingdom: Bacteria Kingdom: not available Genus/species: Clostridium thermocellum

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

Entity Sequences (FASTA):
entity_1: STKLYGDVNDDGKVNSTDAV ALKRYVLRSGISINTDNADL NEDGRVNSTDLGILKRYILK EIDTLPYKN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	299
15N chemical shifts	78
1H chemical shifts	482

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 69 residues - 7670.590 Da.

1

SER

THR

LYS

LEU

TYR

GLY

ASP

VAL

ASN

ASP

2

ASP

GLY

LYS

VAL

ASN

SER

THR

ASP

ALA

VAL

3

ALA

LEU

LYS

ARG

TYR

VAL

LEU

ARG

SER

GLY

4

ILE

SER

ILE

ASN

THR

ASP

ASN

ALA

ASP

LEU

5

ASN

GLU

ASP

GLY

ARG

VAL

ASN

SER

THR

ASP

6

LEU

GLY

ILE

LEU

LYS

ARG

TYR

ILE

LEU

LYS

7

GLU

ILE

ASP

THR

LEU

PRO

TYR

LYS

ASN

Samples:

sample_1: entity_1, [U-13C; U-15N], 0.3 – 0.5 mM; Bis-Tris 50 mM; potassium chloride 100 mM; CaCl2 20 mM; DSS 0.02 % w/v; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 150 mM; pH: 6.6; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

TOPSPIN, Bruker Biospin - collection

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

SANE, Duggan, Legge, Dyson & Wright - refinement

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Bruker Avance 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts