BMRB Entry 15804

Name: Solution NMR Structure of M. thermoautotrophicum protein MTH_1000, Northeast Structural Genomics Consortium Target TR8
Published: 2008-06-23

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PDB ID: 2k4m
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15804
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR Structure of M. thermoautotrophicum protein MTH_1000, Northeast Structural Genomics Consortium Target TR8

Deposition date:

2008-06-13

Original release date:

2008-06-23

Authors:

Eletsky, Alexander; Sukumaran, Dinesh; Semesi, Anthony; Guido, Valerie; Yee, Adelinda; Arrowsmith, Cheryl; Szyperski, Thomas

Citation:

Citation: Eletsky, Alexander; Sukumaran, Dinesh; Semesi, Anthony; Guido, Valerie; Yee, Adelinda; Arrowsmith, Cheryl; Szyperski, Thomas. "Solution NMR Structure of M. thermoautotrophicum protein MTH_1000, Northeast Structural Genomics Consortium Target TR8" Proteins: Struct. Funct. Genet. ., .-..

Assembly members:

Assembly members:
TR8_protein, polymer, 153 residues, 17284.062 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: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TR8_protein: MGSSHHHHHHSSGLVPRGSH MWNDLAVYIIRCSGPGTRVV EVGAGRFLYVSDYIRKHSKV DLVLTDIKPSHGGIVRDDIT SPRMEIYRGAALIYSIRPPA EIHSSLMRVADAVGARLIIK PLTGEDIVTERKMKLVNYGR TYFYEYIAEVRSR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	613
15N chemical shifts	136
1H chemical shifts	989

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TR8_protein	1

Entities:

Entity 1, TR8_protein 153 residues - 17284.062 Da.

20-residue N-terminal tag MGSSHHHHHHSSGLVPRGSH

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

TRP

ASN

ASP

LEU

ALA

VAL

TYR

ILE

4

ARG

CYS

SER

GLY

PRO

GLY

THR

ARG

VAL

5

GLU

VAL

GLY

ALA

GLY

ARG

PHE

LEU

TYR

VAL

6

SER

ASP

TYR

ILE

ARG

LYS

HIS

SER

LYS

VAL

7

ASP

LEU

VAL

LEU

THR

ASP

ILE

LYS

PRO

SER

8

HIS

GLY

ILE

VAL

ARG

ASP

ILE

THR

9

SER

PRO

ARG

MET

GLU

ILE

TYR

ARG

GLY

ALA

10

ALA

LEU

ILE

TYR

SER

ILE

ARG

PRO

ALA

11

GLU

ILE

HIS

SER

LEU

MET

ARG

VAL

ALA

12

ASP

ALA

VAL

GLY

ALA

ARG

LEU

ILE

LYS

13

PRO

LEU

THR

GLY

GLU

ASP

ILE

VAL

THR

GLU

14

ARG

LYS

MET

LYS

LEU

VAL

ASN

TYR

GLY

ARG

15

THR

TYR

PHE

TYR

GLU

TYR

ILE

ALA

GLU

VAL

16

ARG

SER

ARG

Samples:

NC: TR8 protein, [U-100% 13C; U-100% 15N], 0.8 mM; sodium phosphate 10 mM; sodium chloride 300 mM; benzamidine 1 mM; DTT 10 mM

NC5: TR8 protein, [U-5% 13C; U-100% 15N], 0.8 mM; sodium phosphate 10 mM; sodium chloride 450 mM; benzamidine 1 mM; DTT 10 mM

sample_conditions_NC: ionic strength: 300 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_NC5: ionic strength: 450 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC	isotropic	sample_conditions_NC
2D 1H-13C HSQC	NC	isotropic	sample_conditions_NC
3D HNCO	NC	isotropic	sample_conditions_NC
3D HNCACB	NC	isotropic	sample_conditions_NC
3D HNCA	NC	isotropic	sample_conditions_NC
3D CBCA(CO)NH	NC	isotropic	sample_conditions_NC
3D HBHA(CO)NH	NC	isotropic	sample_conditions_NC
3D 1H-15N,13Cali,13Caro NOESY	NC	isotropic	sample_conditions_NC
3D HCCH-COSY aliphatic	NC	isotropic	sample_conditions_NC
3D HCCH-TOCSY aliphatic	NC	isotropic	sample_conditions_NC
3D HCCH-COSY aromatic	NC	isotropic	sample_conditions_NC
2D 1H-13C HSQC methyl	NC5	isotropic	sample_conditions_NC5
2D LR 1H-15N HSQC (His)	NC5	isotropic	sample_conditions_NC5

Software:

TOPSPIN v1.3, Bruker Biospin - collection, processing

VNMR v6.1C, Varian - collection

VNMRJ v2.1B, Varian - collection

PROSA v6.0.2, Guntert - processing

XEASY v1.3.13, Bartels et al. - data analysis

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

CSI v2.0, Wishart and Sykes - data analysis

TALOS v2003.027.13.05, Cornilescu, Delaglio and Bax - data analysis

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

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution

AutoAssign v1.15.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

PSVS, Bhattacharya and Montelione - structure validation

NMR spectrometers:

Bruker Avance 800 MHz
Varian INOVA 600 MHz
Varian INOVA 750 MHz

PDB	2K4M
GB	AAB85479
REF	WP_010876631
SP	O27081
AlphaFold	O27081