BMRB Entry 18083

Name: Solution structure of a THP type 1 alpha 1 collagen fragment (772-786)
Published: 2012-08-29

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PDB ID: 2llp
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18083
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of a THP type 1 alpha 1 collagen fragment (772-786)

Deposition date:

2011-11-15

Original release date:

2012-08-29

Authors:

Bertini, I.; Fragai, M.; Luchinat, C.; Melikian, M.; Toccafondi, M.; Lauer, J.; Fields, G.

Citation:

Citation: Bertini, Ivano; Fragai, Marco; Luchinat, Claudio; Melikian, Maxime; Toccafondi, Mirco; Lauer, Janelle; Fields, Gregg. "Structural basis for matrix metalloproteinase 1-catalyzed collagenolysis" J. Am. Chem. Soc. 134, 2100-2110 (2012).
PubMed: 22239621

Assembly members:

Assembly members:
entity_1, polymer, 18 residues, 1463.676 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: PPGPQGIAGQRGVVGLPG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	165
15N chemical shifts	45
1H chemical shifts	273

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	THP type 1 alpha 1 collagen fragment, 1	1
2	THP type 1 alpha 1 collagen fragment, 2	1
3	THP type 1 alpha 1 collagen fragment, 3	1

Entities:

Entity 1, THP type 1 alpha 1 collagen fragment, 1 18 residues - 1463.676 Da.

Corresponding to fragment G772-L785 of mature type 1 alpha 1 collagen

1

PRO

GLY

PRO

GLN

GLY

ILE

ALA

GLY

GLN

2

ARG

GLY

VAL

GLY

LEU

PRO

GLY

Samples:

sample: THP type I collagen, [U-98% 13C; U-98% 15N], 0.4 – 0.8 mM; sodium chloride 150 mM; calcium chloride 10 mM; zinc chloride 0.1 mM; tris buffer, [U-2H], 20 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D_15N-separated_NOESY	sample	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample	isotropic	sample_conditions_1
3D HNCA	sample	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample	isotropic	sample_conditions_1
3D HNCACB	sample	isotropic	sample_conditions_1

Software:

CYANA v2.0, Guntert P. - structure solution

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 900 MHz

PDB	2LLP
GB	AAD49346 EPQ08966 KQL74538