BMRB Entry 18495

Name: 1H chemical shifts of Thermolysin 205-316 fragment
Published: 2012-06-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18495

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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 chemical shifts of Thermolysin 205-316 fragment

Deposition date:

2012-05-31

Original release date:

2012-06-18

Authors:

Conejero-Lara, Francisco; Gonzalez, Carlos; Rico, Manuel; Jimenez, M Angeles

Citation:

Citation: Rico, Manuel; Jimenez, M Angeles; Gonzalez, Carlos; de Filippis, Vincenzo; Fontana, Angelo. "NMR solution structure of the C-terminal fragment 255-316 of Thermolysin: A dimer formed by subunits having native structure" Biochemistry 33, 14834-14847 (1994).
PubMed: 7993910

Assembly members:

Assembly members:
Th205-316, polymer, 112 residues, 11949.3 Da.

Natural source:

Natural source: Common Name: Bacillus thermoproteolyticus Taxonomy ID: 1427 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus thermoproteolyticus

Experimental source:

Experimental source: Production method: Limited proteolysis Host organism: Not applicable

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Th205-316: MSDPAKYGDPDHYSKRYTGT QDNGGVHINSGIINKAAYLI SQGGTHYGVSVVGIGRDKLG KIFYRALTQYLTPTSNFSQL RAAAVQSATDLYGSTSQEVA SVKQAFDAVGVK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	1
1H chemical shifts	750

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Th205-316, chain 1	1
2	Th205-316, chain 2	1

Entities:

Entity 1, Th205-316, chain 1 112 residues - 11949.3 Da.

1

MET

SER

ASP

PRO

ALA

LYS

TYR

GLY

ASP

PRO

2

ASP

HIS

TYR

SER

LYS

ARG

TYR

THR

GLY

THR

3

GLN

ASP

ASN

GLY

VAL

HIS

ILE

ASN

SER

4

GLY

ILE

ASN

LYS

ALA

TYR

LEU

ILE

5

SER

GLN

GLY

THR

HIS

TYR

GLY

VAL

SER

6

VAL

GLY

ILE

GLY

ARG

ASP

LYS

LEU

GLY

7

LYS

ILE

PHE

TYR

ARG

ALA

LEU

THR

GLN

TYR

8

LEU

THR

PRO

THR

SER

ASN

PHE

SER

GLN

LEU

9

ARG

ALA

VAL

GLN

SER

ALA

THR

ASP

10

LEU

TYR

GLY

SER

THR

SER

GLN

GLU

VAL

ALA

11

SER

VAL

LYS

GLN

ALA

PHE

ASP

ALA

VAL

GLY

12

VAL

LYS

Samples:

sample_1: Th205-316 1 mM; TSP 0.1 mM; H2O 90%; D2O 10%

sample_2: Th205-316 1 mM; TSP 0.1 mM; D2O 100%

sample_conditions_1: pH: 4.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1

Software:

UXNMR, Bruker Biospin - processing

XEASY, Bartels et al. - chemical shift assignment

NMR spectrometers:

Bruker AMX 600 MHz