BMRB Entry 15722

Name: 1H, 13C and 15N Resonance Assignments of Ca2+ bound collagen-binding domain derived from a clostridial collagenase
Published: 2008-08-08

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15722

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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 Resonance Assignments of Ca2+ bound collagen-binding domain derived from a clostridial collagenase

Deposition date:

2008-04-08

Original release date:

2008-08-08

Authors:

Philominathan, Sagaya T. Leena; Matsushita, Osamu; Jordan, J. Brad; Sakon, Joshua

Citation:

Citation: Philominathan, Sagaya Theresa Leena; Matsushita, Osamu; Jordan, John Brad; Sakon, Joshua. "1H, 13C and 15N resonance assignments of Ca2+ bound collagen-binding domain derived from a clostridial collagenase" Biomol. NMR Assignments 2, 127-129 (2008).
PubMed: 19636886

Assembly members:

Assembly members:
Collagen_binding_domain_derived_from_Clostridium_Histolyticum, polymer, 122 residues, 13786 Da.
CA, non-polymer, Formula weight is not available

Natural source:

Natural source: Common Name: Bacillus histolyticus Taxonomy ID: 1498 Superkingdom: Eubacteria Kingdom: not available Genus/species: Clostridium histolyticum

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-4T-2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Collagen_binding_domain_derived_from_Clostridium_Histolyticum: GSPGIPGNEKLKEKENNDSS DKATVIPNFNTTMQGSLLGD DSRDYYSFEVKEEGEVNIEL DKKDEFGVTWTLHPESNIND RITYGQVDGNKVSNKVKLRP GKYYLLVYKYSGSGNYELRV NK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	420
15N chemical shifts	105
1H chemical shifts	593

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Collagen binding domain derived from Clostridium Histolyticum	1
2	Calcium ion, 2+	2

Entities:

Entity 1, Collagen binding domain derived from Clostridium Histolyticum 122 residues - 13786 Da.

Residues 887-892 are introduced as clonging artifact

1

GLY

SER

PRO

GLY

ILE

PRO

GLY

ASN

GLU

LYS

2

LEU

LYS

GLU

LYS

GLU

ASN

ASP

SER

3

ASP

LYS

ALA

THR

VAL

ILE

PRO

ASN

PHE

ASN

4

THR

MET

GLN

GLY

SER

LEU

GLY

ASP

5

ASP

SER

ARG

ASP

TYR

SER

PHE

GLU

VAL

6

LYS

GLU

GLY

GLU

VAL

ASN

ILE

GLU

LEU

7

ASP

LYS

ASP

GLU

PHE

GLY

VAL

THR

TRP

8

THR

LEU

HIS

PRO

GLU

SER

ASN

ILE

ASN

ASP

9

ARG

ILE

THR

TYR

GLY

GLN

VAL

ASP

GLY

ASN

10

LYS

VAL

SER

ASN

LYS

VAL

LYS

LEU

ARG

PRO

11

GLY

LYS

TYR

LEU

VAL

TYR

LYS

TYR

12

SER

GLY

SER

GLY

ASN

TYR

GLU

LEU

ARG

VAL

13

ASN

LYS

Entity 2, Calcium ion, 2+ - Formula weight is not available

1

CA

Samples:

sample_1: Collagen binding domain derived from Clostridium Histolyticum, [U-100% 13C; U-100% 15N], 0.75 mM; Calcium Chloride 20 mM; TRIS, [U-100% 2H], 50 mM; sodium chloride 100 mM; sodium azide 0.3 mM

sample_2: Collagen binding domain derived from Clostridium Histolyticum, [U-99% 15N], 0.75 mM; Calcium Chloride 20 mM; TRIS, [U-100% 2H], 50 mM; sodium chloride 100 mM; sodium azide 0.3 mM

sample_3: Collagen binding domain derived from Clostridium Histolyticum, [U-100% 13C], 0.75 mM; Calcium Chloride 20 mM; TRIS, [U-100% 2H], 50 mM; sodium chloride 100 mM; sodium azide 0.3 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

xwinnmr, Bruker Biospin - processing

SPARKY, Goddard - data analysis

NMR spectrometers:

Bruker Avance 700 MHz