BMRB Entry 7226

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PDB ID: 2hga
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: LACS
BMRB Entry DOI: doi:10.13018/BMR7226
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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 NMR Structure of Conserved protein MTH1368, Northeast Structural Genomics Consortium Target TT821A

Deposition date:

2006-07-14

Original release date:

2010-03-04

Authors:

Liu, G.; Lin, Y.; Parish, D.; Shen, Y.; Sukumaran, D.; Yee, A.; Semesi, A.; Arrowsmith, C.; Szyperski, T.

Citation:

Citation: Liu, G.; Lin, Y.; Parish, D.; Shen, Y.; Sukumaran, D.; Yee, A.; Semesi, A.; Arrowsmith, C.; Szyperski, T.. "Solution NMR Structure of Conserved protein MTH1368, Northeast Structural Genomics Consortium Target TT821A" .

Assembly members:

Assembly members:
Conserved protein MTH1368, polymer, 125 residues, Formula weight is not available

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Conserved protein MTH1368: MGSSHHHHHHSSGRENLYFQ GHQPDGVQIDSVVPGSPASK VLTPGLVIESINGMPTSNLT TYSAALKTISVGEVINITTD QGTFHLKTGRNPNNSSRAYM GIRTSNHLRVRDSVASVLGD TLPFA

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
13C chemical shifts	341
15N chemical shifts	106
1H chemical shifts	737

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Conserved protein MTH1368	1

Entities:

Entity 1, Conserved protein MTH1368 125 residues - Formula weight is not available

1

MET

GLY

SER

HIS

2

SER

GLY

ARG

GLU

ASN

LEU

TYR

PHE

GLN

3

GLY

HIS

GLN

PRO

ASP

GLY

VAL

GLN

ILE

ASP

4

SER

VAL

PRO

GLY

SER

PRO

ALA

SER

LYS

5

VAL

LEU

THR

PRO

GLY

LEU

VAL

ILE

GLU

SER

6

ILE

ASN

GLY

MET

PRO

THR

SER

ASN

LEU

THR

7

THR

TYR

SER

ALA

LEU

LYS

THR

ILE

SER

8

VAL

GLY

GLU

VAL

ILE

ASN

ILE

THR

ASP

9

GLN

GLY

THR

PHE

HIS

LEU

LYS

THR

GLY

ARG

10

ASN

PRO

ASN

SER

ARG

ALA

TYR

MET

11

GLY

ILE

ARG

THR

SER

ASN

HIS

LEU

ARG

VAL

12

ARG

ASP

SER

VAL

ALA

SER

VAL

LEU

GLY

ASP

13

THR

LEU

PRO

PHE

ALA

Samples:

sample_1: Conserved protein MTH1368, [U-15N; U-13C], 0.5 mM; TRIS BUFFER mM; NaCl2 200 mM; ZnSO4 10 uM; NaN3 0.01%; bezamidine 1 mM; inhibitor 1 x; H2O 93%; D2O 7%

sample_cond_1: pH: 7.0; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
SIMULTANEOUS HETERONUCLEAR RESOLVED [1H,1H]-NOESY	sample_1	not available	sample_cond_1
3D HNCACB	sample_1	not available	sample_cond_1
3D CBCACONH	sample_1	not available	sample_cond_1
GFT (4,3)D HABCAB(CO)NHN	sample_1	not available	sample_cond_1
GFT (4,3)D HCCH	sample_1	not available	sample_cond_1

Software:

VNMR v6.1C - collection

NMRPipe v2.3 - processing

AutoAssign v1.15.1 - data analysis

AutoStruct v2.0 - data analysis

CYANA v2.1 - structure solution

CNS v1.1 - refinement

NMR spectrometers:

Varian INOVA 600 MHz

PDB	2HGA
DBJ	BAM70490
GB	AAB85845
REF	NP_276484 WP_010876980