BMRB Entry 16897

Name: The solution structure of MTH1821
Published: 2011-04-08

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PDB ID: 2kx2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16897
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

The solution structure of MTH1821

Deposition date:

2010-04-23

Original release date:

2011-04-08

Authors:

Lee, Weontae; Ko, Sunggeon

Citation:

Citation: Ko, Sunggeon; Kim, Heeyoun; Yun, Jihye; Yee, Adelinda; Arrowsmith, Cheryl; Cheong, Chaejoon; Lee, Weontae. "Solution structure of MTH1821, a putative structure homologue to RNA polymerase subunit from Methanobacterium thermoautotrophicum." Proteins 79, 1347-1351 (2011).
PubMed: 21387412

Assembly members:

Assembly members:
MTH1821, polymer, 96 residues, 11484.018 Da.

Natural source:

Natural source: Common Name: Methanobacterium thermoautotrophicum Taxonomy ID: 145262 Superkingdom: Archaea Kingdom: not available Genus/species: Methanobacterium thermoautotrophicum

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET27a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MTH1821: MVFYLKVKVEDFGFREDMGL NYVRYRVSGLDEELTEKLIE RLDEDTERDDGDLIITVFYE REYFPFGSEESKVKMADFIA REEIEMMVFLSSVLED

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	375
15N chemical shifts	92
1H chemical shifts	651

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MTH1821	1

Entities:

Entity 1, MTH1821 96 residues - 11484.018 Da.

1

MET

VAL

PHE

TYR

LEU

LYS

VAL

LYS

VAL

GLU

2

ASP

PHE

GLY

PHE

ARG

GLU

ASP

MET

GLY

LEU

3

ASN

TYR

VAL

ARG

TYR

ARG

VAL

SER

GLY

LEU

4

ASP

GLU

LEU

THR

GLU

LYS

LEU

ILE

GLU

5

ARG

LEU

ASP

GLU

ASP

THR

GLU

ARG

ASP

6

GLY

ASP

LEU

ILE

THR

VAL

PHE

TYR

GLU

7

ARG

GLU

TYR

PHE

PRO

PHE

GLY

SER

GLU

8

SER

LYS

VAL

LYS

MET

ALA

ASP

PHE

ILE

ALA

9

ARG

GLU

ILE

GLU

MET

VAL

PHE

LEU

10

SER

VAL

LEU

GLU

ASP

Samples:

sample_1: MTH1821, [U-99% 15N], 1.2 mM; H2O 90%; D2O 10%; HEPES 20 mM; NaCl 100 mM

sample_3: MTH1821, [U-100% 13C], 1.2 mM; D2O 100%; HEPES 20 mM; NaCl 100 mM

sample_2: MTH1821, [U-99% 13C; U-99% 15N], 1.2 mM; H2O 90%; D2O 10%; HEPES 20 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1

Software:

CYANA v2.2.5, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, refinement, structure solution

xwinnmr, Bruker Biospin - collection

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

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

SPARKY, Goddard - peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

Bruker DRX 500 MHz
Bruker DRX 900 MHz

PDB	2KX2
GB	AAB86287
REF	WP_048061147