BMRB Entry 18083
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18083
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution structure of a THP type 1 alpha 1 collagen fragment (772-786) PubMed: 22239621
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: 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).
Assembly members:
entity_1, polymer, 18 residues, 1463.676 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity_1: PPGPQGIAGQRGVVGLPG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 165 |
| 15N chemical shifts | 45 |
| 1H chemical shifts | 273 |
Additional metadata:
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 | PRO | GLY | PRO | GLN | GLY | ILE | ALA | GLY | GLN | ||||
| 2 | ARG | GLY | VAL | 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
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts