BMRB Entry 15822

Name: NMR solution structure of A3DK08 protein from Clostridium thermocellum: Northeast Structural Genomics Consortium Target CmR9
Published: 2008-08-21

Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15822

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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:

NMR solution structure of A3DK08 protein from Clostridium thermocellum: Northeast Structural Genomics Consortium Target CmR9

Deposition date:

2008-06-24

Original release date:

2008-08-21

Authors:

Swapna, G; Huang, Wang; Jiang, Mei; Foote, Erika; Xiao, Rong; Nair, Rajesh; Everett, John; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano

Citation:

Citation: Swapna, G; Huang, Wang; Jiang, Mei; Foote, Erika; Xiao, Rong; Nair, Rajesh; Everett, John; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano. "NMR Solution Structure of A3DK08 protein from Clostridium thermocellum: Northeast Structural Genomics Consortium Target CmR9" .

Assembly members:

Assembly members:
A3DK08_Protein, polymer, 76 residues, 9053.35 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
A3DK08_Protein: MKITKDMIIADVLQMDRGTA PIFINNGMHCLGCPSSMGES IEDACAVHGIDADKLVKELN EYFEKKEVLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	305
15N chemical shifts	73
1H chemical shifts	503

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 76 residues - 9053.35 Da.

1

MET

LYS

ILE

THR

LYS

ASP

MET

ILE

ALA

2

ASP

VAL

LEU

GLN

MET

ASP

ARG

GLY

THR

ALA

3

PRO

ILE

PHE

ILE

ASN

GLY

MET

HIS

CYS

4

LEU

GLY

CYS

PRO

SER

MET

GLY

GLU

SER

5

ILE

GLU

ASP

ALA

CYS

ALA

VAL

HIS

GLY

ILE

6

ASP

ALA

ASP

LYS

LEU

VAL

LYS

GLU

LEU

ASN

7

GLU

TYR

PHE

GLU

LYS

GLU

VAL

LEU

GLU

8

HIS

Samples:

sample_1: A3DK08 Protein, [U-100% 13C; U-100% 15N], 0.91 ± 0.2 mM; DTT 10 mM; DSS 50 uM; NaN3 0.02%; CaCl2 2 mM; NaCl 100 mM; MES 20 mM; protease inhibitor 1x mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_2: A3DK08 Protein, [U-10% 13C; U-99% 15N], 1.05 ± 0.2 mM; DTT 10 mM; DSS 50 uM; NaN3 0.02%; CaCl2 2 mM; NaCl 100 mM; MES 20 mM; protease inhibitor 1x mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 105 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D simultaneous CN NOESY	sample_1	isotropic	sample_conditions_1

Software:

CNS v2.0.6, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

NMR spectrometers:

Varian INOVA 600 MHz
Bruker Avance 800 MHz

PDB	2K53
DBJ	GAE89622
EMBL	CDG37571
GB	ABN54287 ADU73722 EEU00234 EFB38242 EIC03356
REF	WP_037294975 WP_038290015