BMRB Entry 16357

Name: Solution NMR Structure of a dimeric protein of unknown function from Methanobacterium thermoautotrophicum, Northeast Structural Genomics Consortium Target TR5
Published: 2009-07-07

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PDB ID: 2kke
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16357
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR Structure of a dimeric protein of unknown function from Methanobacterium thermoautotrophicum, Northeast Structural Genomics Consortium Target TR5

Deposition date:

2009-06-17

Original release date:

2009-07-07

Authors:

Swapna, G.V.T.; Gunsalus, K.; Huang, Y.; Xiao, R.; Everett, J.; Acton, T.; Montelione, G.; NESG, NESG

Citation:

Citation: Swapna, S.; Gunsalus, X.; Huang, L.; Xiao, G.; Everett, K.; Acton, A.; Montelione, G.. "Solution NMR Structure of a dimeric protein of unknown function from Methanobacterium thermoautotrophicum, Northeast Structural Genomics Consortium Target TR5" To be Published ., .-..

Assembly members:

Assembly members:
TR5, polymer, 106 residues, 11927.964 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: BL21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TR5: MVGRRPGGGLKDTKPVVVRL YPDEIEALKSRVPANTSMSA YIRRIILNHLEDEMVGRRPG GGLKDTKPVVVRLYPDEIEA LKSRVPANTSMSAYIRRIIL NHLEDE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	434
15N chemical shifts	100
1H chemical shifts	750

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TR5	1

Entities:

Entity 1, TR5 106 residues - 11927.964 Da.

Chain B of the dimer has been numbered from 201-253 with the first residue M at 201.

1

MET

VAL

GLY

ARG

PRO

GLY

LEU

2

LYS

ASP

THR

LYS

PRO

VAL

ARG

LEU

3

TYR

PRO

ASP

GLU

ILE

GLU

ALA

LEU

LYS

SER

4

ARG

VAL

PRO

ALA

ASN

THR

SER

MET

SER

ALA

5

TYR

ILE

ARG

ILE

LEU

ASN

HIS

LEU

6

GLU

ASP

GLU

MET

VAL

GLY

ARG

PRO

GLY

7

GLY

LEU

LYS

ASP

THR

LYS

PRO

VAL

8

VAL

ARG

LEU

TYR

PRO

ASP

GLU

ILE

GLU

ALA

9

LEU

LYS

SER

ARG

VAL

PRO

ALA

ASN

THR

SER

10

MET

SER

ALA

TYR

ILE

ARG

ILE

LEU

11

ASN

HIS

LEU

GLU

ASP

GLU

Samples:

sample_1: TR5-1, [U-100% 13C; U-100% 15N], 0.4 mM; Na2HPO4 25 mM; NaCl 300 mM; H2O 95%; D2O 5%

sample_2: TR5-2, [U-10% 13C; U-100% 15N], 0.95 mM; Na2HPO4 25 mM; NaCl 300 mM; H2O 95%; D2O 5%

sample_3: TR5-3, [U-10% 13C; U-100% 15N] + unlabeled TR5 protein, 0.4 mM; Na2HPO4 25 mM; NaCl 300 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.300 M; pH: 6.5; pressure: 1 atm; temperature: 303 K

sample_conditions_2: ionic strength: 0.300 M; pH: 6.5; pressure: 1 atm; temperature: 303 K

sample_conditions_3: ionic strength: 0.300 M; pH: 6.5; pressure: 1 atm; temperature: 303 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	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 HNCO	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D- X-filtered NOESY	sample_3	isotropic	sample_conditions_3
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_2
2D HNOE	sample_2	isotropic	sample_conditions_2

Software:

AutoAssign v2.2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - geometry optimization

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

NMR spectrometers:

Varian INOVA 600 MHz
Varian Unity 500 MHz

PDB	2KKE
DBJ	BAM69652
GB	AAB84973