BMRB Entry 6318

Name: Solution structure of thioredoxin h1 from Arabidopsis thaliana
Published: 2005-09-08

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PDB ID: 1xfl
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR6318
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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 thioredoxin h1 from Arabidopsis thaliana

Deposition date:

2004-09-20

Original release date:

2005-09-08

Authors:

Peterson, F.; Lytle, B.; Sampath, S.; Vinarov, D.; Tyler, E.; Shahan, M.; Markley, J.; Volkman, B.

Citation:

Citation: Peterson, F.; Lytle, B.; Sampath, S.; Vinarov, D.; Tyler, E.; Shahan, M.; Markley, J.; Volkman, B.. "Solution structure of thioredoxin h1 from Arabidopsis thaliana" Protein Sci. 14, 2195-2200 (2005).
PubMed: 15987893

Assembly members:

Assembly members:
Thioredoxin h1, polymer, 124 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Triticum aestivum Vector: pEU(N)His6

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Thioredoxin h1: MGHHHHHHLEMASEEGQVIA CHTVETWNEQLQKANESKTL VVVDFTASWCGPCRFIAPFF ADLAKKLPNVLFLKVDTDEL KSVASDWAIQAMPTFMFLKE GKILDKVVGAKKDELQSTIA KHLA

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
1H chemical shifts	831
13C chemical shifts	512
15N chemical shifts	121

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AtTRXh1	1

Entities:

Entity 1, AtTRXh1 124 residues - Formula weight is not available

1

MET

GLY

HIS

LEU

GLU

2

MET

ALA

SER

GLU

GLY

GLN

VAL

ILE

ALA

3

CYS

HIS

THR

VAL

GLU

THR

TRP

ASN

GLU

GLN

4

LEU

GLN

LYS

ALA

ASN

GLU

SER

LYS

THR

LEU

5

VAL

ASP

PHE

THR

ALA

SER

TRP

CYS

6

GLY

PRO

CYS

ARG

PHE

ILE

ALA

PRO

PHE

7

ALA

ASP

LEU

ALA

LYS

LEU

PRO

ASN

VAL

8

LEU

PHE

LEU

LYS

VAL

ASP

THR

ASP

GLU

LEU

9

LYS

SER

VAL

ALA

SER

ASP

TRP

ALA

ILE

GLN

10

ALA

MET

PRO

THR

PHE

MET

PHE

LEU

LYS

GLU

11

GLY

LYS

ILE

LEU

ASP

LYS

VAL

GLY

ALA

12

LYS

ASP

GLU

LEU

GLN

SER

THR

ILE

ALA

13

LYS

HIS

LEU

ALA

Samples:

sample_1: Thioredoxin h1, [U-13C; U-15N], 0.5 mM; KCl 50 mM; potassium phosphate buffer 10 mM; H20 90%; D20 10%

sample_cond_1: pH: 5.5; temperature: 298 K; ionic strength: 50 mM

Experiments:

Name	Sample	Sample state	Sample conditions
1H-15N HSQC	sample_1	not available	sample_cond_1
HNCA	sample_1	not available	sample_cond_1
HNCO	sample_1	not available	sample_cond_1
HN(CO)CA	sample_1	not available	sample_cond_1
HNCACB	sample_1	not available	sample_cond_1
HN(CA)CO	sample_1	not available	sample_cond_1
C(CO)NH	sample_1	not available	sample_cond_1
HCCH-TOCSY	sample_1	not available	sample_cond_1
3D 15N-NOESY	sample_1	not available	sample_cond_1
3D 13C-NOESY-aliphatic	sample_1	not available	sample_cond_1
3D 13C-NOESY-aromatic	sample_1	not available	sample_cond_1

Software:

XWINNMR v3.1 - collection

NMRPipe v2.1 - processing

XEASY v1.3.1 - analysis

SPSCAN v1.1.0 - peak picking

GARANT v2.1 - automated backbone assignments

TALOS - generation of torsion angle restraints

CYANA v1.0.6 - refinement (torsion angle dynamics)

XPLOR-NIH v2.0.6 - refinement (cartesian MD in explicit solvent)

NMR spectrometers:

Bruker DRX 600 MHz

PDB	1XFL
EMBL	CAA78462 CAB62625
GB	AAC49354 AAM67008 AEE78739 EFH54044
REF	NP_190672 XP_002877785
SP	P29448
AlphaFold	P29448