BMRB Entry 15172

Name: 1H, 13C and 15N chemical shift assignments for hypothetical protein TA0095 from Thermoplasma acidophilum
Published: 2007-09-27

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15172

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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:

1H, 13C and 15N chemical shift assignments for hypothetical protein TA0095 from Thermoplasma acidophilum

Deposition date:

2007-03-12

Original release date:

2007-09-27

Authors:

Jimenez, M. Angeles; Leon, Esther; Santoro, Jorge; Rico, Manuel; Yee, Adelinda

Citation:

Citation: Leon, Esther; Yee, Adelinda; Ortiz, A.R.; Santoro, Jorge; Rico, Manuel; Jimenez, M. Angeles. "Solution structure of the hypothetical protein TA0095 from Thermoplasma acidophilum: A novel superfamily with a 2-layer sandwich architecture" Protein Sci. 16, 2278-2286 (2007).
PubMed: 17766377

Assembly members:

Assembly members:
H6TA0095, polymer, 118 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Thermoplasma acidophilum Taxonomy ID: 2303 Superkingdom: Archaea Kingdom: not available Genus/species: Thermoplasma acidophilum

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-11b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
H6TA0095: MGTSHHHHHHSSGRENLYFQ GHMREYPVKKGFPTDYDSIK RKISELGFDVKSEGDLIIAS IPGISRIEIKPDKRKILVNT GDYDSDADKLAVVRTYNDFI EKLTGYSAKERKKMMTKD

Data sets:

assigned_chemical_shifts

Data type	Count
13C chemical shifts	283
15N chemical shifts	109
1H chemical shifts	1463

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	H6TA0095	1

Entities:

Entity 1, H6TA0095 118 residues - Formula weight is not available

1

MET

GLY

THR

SER

HIS

2

SER

GLY

ARG

GLU

ASN

LEU

TYR

PHE

GLN

3

GLY

HIS

MET

ARG

GLU

TYR

PRO

VAL

LYS

4

GLY

PHE

PRO

THR

ASP

TYR

ASP

SER

ILE

LYS

5

ARG

LYS

ILE

SER

GLU

LEU

GLY

PHE

ASP

VAL

6

LYS

SER

GLU

GLY

ASP

LEU

ILE

ALA

SER

7

ILE

PRO

GLY

ILE

SER

ARG

ILE

GLU

ILE

LYS

8

PRO

ASP

LYS

ARG

LYS

ILE

LEU

VAL

ASN

THR

9

GLY

ASP

TYR

ASP

SER

ASP

ALA

ASP

LYS

LEU

10

ALA

VAL

ARG

THR

TYR

ASN

ASP

PHE

ILE

11

GLU

LYS

LEU

THR

GLY

TYR

SER

ALA

LYS

GLU

12

ARG

LYS

MET

THR

LYS

ASP

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HACANH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_2
3D HNHA	sample_2	isotropic	sample_conditions_2
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_2
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_2
2D 1H-1H COSY	sample_3	isotropic	sample_conditions_2
2D 1H-1H TOCSY	sample_3	isotropic	sample_conditions_2
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_2
2D 1H-1H COSY	sample_4	isotropic	sample_conditions_2
2D 1H-1H TOCSY	sample_4	isotropic	sample_conditions_2
2D 1H-1H NOESY	sample_4	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_4	isotropic	sample_conditions_2

PDB	2JOI
EMBL	CAC11243
REF	WP_010900522

BMRB Entry 15172

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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