BMRB Entry 4740

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PDB ID: 1gh9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4740
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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:

Solution Structure of a 8.3 kDa Protein (gene MTH1184) from Methanobacterium thermoautotrophicum

Deposition date:

2000-05-18

Original release date:

2002-04-01

Authors:

Kozlov, G.; Ekiel, I.; Gehring, K.

Citation:

Citation: Christendat, D.; Yee, A.; Dharamsi, A.; Kluger, Y.; Savchenko, A.; Cort, J.; Booth, V.; Mackereth, C.; Saridakis, V.; Ekiel, I.; Kozlov, G.; Maxwell, K.; Wu, N.; Mcintosh, L.; Gehring, K.; Kennedy, M.; Davidson, A.; Pai, E.; Gerstein, M.; Edwards, A.; Arrowsmith, C.. "Structural proteomics of an archaeon" Nat. Struct. Biol. 7, 903-909 (2000).
PubMed: 11017201

Assembly members:

Assembly members:
8.3 KDA PROTEIN (GENE MTH1184), polymer, 71 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Bacteria Taxonomy ID: 2166 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):
8.3 KDA PROTEIN (GENE MTH1184): MYIIFRCDCGRALYSREGAK TRKCVCGRTVNVKDRRIFGR ADDFEEASELVRKLQEEKYG SCHFTNPSKRE

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1
coupling_constants
- J_values

Data type	Count
1H chemical shifts	331
13C chemical shifts	127
15N chemical shifts	68
coupling constants	60

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	8.3 KDA PROTEIN (GENE MTH1184)	1

Entities:

Entity 1, 8.3 KDA PROTEIN (GENE MTH1184) 71 residues - Formula weight is not available

1

MET

TYR

ILE

PHE

ARG

CYS

ASP

CYS

GLY

2

ARG

ALA

LEU

TYR

SER

ARG

GLU

GLY

ALA

LYS

3

THR

ARG

LYS

CYS

VAL

CYS

GLY

ARG

THR

VAL

4

ASN

VAL

LYS

ASP

ARG

ILE

PHE

GLY

ARG

5

ALA

ASP

PHE

GLU

ALA

SER

GLU

LEU

6

VAL

ARG

LYS

LEU

GLN

GLU

LYS

TYR

GLY

7

SER

CYS

HIS

PHE

THR

ASN

PRO

SER

LYS

ARG

8

GLU

Samples:

sample_1: 8.3 KDA PROTEIN (GENE MTH1184), [U-13C; U-15N], 1 – 2 mM; phosphate buffer 50 mM; NaCl 0.15 M; DTT 1 mM

sample_2: 8.3 KDA PROTEIN (GENE MTH1184), [U-13C], 1 – 2 mM; phosphate buffer 50 mM; NaCl 0.15 M; DTT 1 mM

sample_3: 8.3 KDA PROTEIN (GENE MTH1184), [U-15N], 1 – 2 mM; phosphate buffer 50 mM; NaCl 0.15 M; DTT 1 mM

sample_4: 8.3 KDA PROTEIN (GENE MTH1184)1 – 2 mM; phosphate buffer 50 mM; NaCl 0.15 M; DTT 1 mM

sample_cond_1: pH: 6.3; temperature: 305 K; ionic strength: 0.15 M

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-SEPARATED NOESY	not available	not available	not available
3D 15N-SEPARATED NOESY	not available	not available	not available
HNHA	not available	not available	not available
2D NOESY	not available	not available	not available

Software:

XWINNMR v2.1 - COLLECTION

GIFA vV.4 - PROCESSING

XEASY v1.3.13 - DATA ANALYSIS

CNS v0.5 - STRUCTURE SOLUTION

ARIA v0.1 - STRUCTURE SOLUTION

NMR spectrometers:

Bruker DRX 500 MHz

PDB	1GH9
DBJ	BAM70325
GB	AAB85673
REF	WP_010876808 WP_048175749
SP	O27252
AlphaFold	O27252