BMRB Entry 30334

Name: H, 13C, and 15N Chemical Shift Assignments and structure of Thioredoxin from Mycobacterium thermoresistibile ATCC 19527 and NCTC 10409
Published: 2017-10-20

Click here to enlarge.

PDB ID: 6ap5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30334
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

H, 13C, and 15N Chemical Shift Assignments and structure of Thioredoxin from Mycobacterium thermoresistibile ATCC 19527 and NCTC 10409

Deposition date:

2017-08-17

Original release date:

2017-10-20

Authors:

Tang, C.; Yang, F.; Varani, G.; Seattle Structural Genomics Center for Infectious Disease (SSGCID), SSGCID

Citation:

Citation: Tang, C.; Yang, F.; Varani, G.. "1H, 13C, and 15N Chemical Shift Assignments and structure of Thioredoxin from Mycobacterium thermoresistibile ATCC 19527 and NCTC 10409" .

Assembly members:

Assembly members:
entity_1, polymer, 115 residues, 12508.391 Da.

Natural source:

Natural source: Common Name: Mycobacterium thermoresistibile Taxonomy ID: 1078020 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium thermoresistibile

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAHHHHHHMSGTVTVTDSTF KTDVLDSDTPVLVDFWADWC GPCKMVAPVLEEIANEKSGT LKVAKLDVDANPEAARDFQV VSIPTMILFKGGTPVKRIVG AKGKAALLREIEDAL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	443
15N chemical shifts	111
1H chemical shifts	672

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 115 residues - 12508.391 Da.

1

MET

ALA

HIS

MET

SER

2

GLY

THR

VAL

THR

VAL

THR

ASP

SER

THR

PHE

3

LYS

THR

ASP

VAL

LEU

ASP

SER

ASP

THR

PRO

4

VAL

LEU

VAL

ASP

PHE

TRP

ALA

ASP

TRP

CYS

5

GLY

PRO

CYS

LYS

MET

VAL

ALA

PRO

VAL

LEU

6

GLU

ILE

ALA

ASN

GLU

LYS

SER

GLY

THR

7

LEU

LYS

VAL

ALA

LYS

LEU

ASP

VAL

ASP

ALA

8

ASN

PRO

GLU

ALA

ARG

ASP

PHE

GLN

VAL

9

VAL

SER

ILE

PRO

THR

MET

ILE

LEU

PHE

LYS

10

GLY

THR

PRO

VAL

LYS

ARG

ILE

VAL

GLY

11

ALA

LYS

GLY

LYS

ALA

LEU

ARG

GLU

12

ILE

GLU

ASP

ALA

LEU

Samples:

sample_1: D20 10 % v/v; DTT 2 mM; Thioredoxin, [U-95% 13C; U-95% 15N], 1 mM; sodium chloride 100 mM; sodium phosphate 25 mM

sample_2: D2O 100 % v/v; DTT 2 mM; Thioredoxin, [U-95% 13C; U-95% 15N], 1 mM; sodium chloride 100 mM; sodium phosphate 25 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 Pa; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1

Software:

Analysis, CCPN - chemical shift assignment, peak picking, refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

Bruker Avance 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks