BMRB Entry 30024
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30024
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: Structural basis for therapeutic inhibition of complement C5 PubMed: 27018802
Deposition date: 2016-02-25 Original release date: 2016-07-13
Authors: Sheppard, D.; Lea, S.
Citation: Jore, M.; Johnson, S.; Sheppard, D.; Barber, N.; Li, Y.; Nunn, M.; Elmlund, H.; Lea, S.. "Structural basis for therapeutic inhibition of complement C5." Nat. Struct. Mol. Biol. 23, 378-386 (2016).
Assembly members:
entity_1, polymer, 70 residues, 7476.488 Da.
Natural source: Common Name: mites & ticks Taxonomy ID: 34631 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rhipicephalus appendiculatus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: GPMEEANTTPISVKDQCANV
TCRRTVDNRGKRHIDGCPPG
CLCVLKGPDSKDNLDGTCYL
LATTPKSTTT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 203 |
| 15N chemical shifts | 62 |
| 1H chemical shifts | 405 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 70 residues - 7476.488 Da.
| 1 | GLY | PRO | MET | GLU | GLU | ALA | ASN | THR | THR | PRO | |
| 2 | ILE | SER | VAL | LYS | ASP | GLN | CYS | ALA | ASN | VAL | |
| 3 | THR | CYS | ARG | ARG | THR | VAL | ASP | ASN | ARG | GLY | |
| 4 | LYS | ARG | HIS | ILE | ASP | GLY | CYS | PRO | PRO | GLY | |
| 5 | CYS | LEU | CYS | VAL | LEU | LYS | GLY | PRO | ASP | SER | |
| 6 | LYS | ASP | ASN | LEU | ASP | GLY | THR | CYS | TYR | LEU | |
| 7 | LEU | ALA | THR | THR | PRO | LYS | SER | THR | THR | THR |
Samples:
sample_1: RaCI2, [U-100% 13C] [U-100% 15N], 330 uM
sample_conditions_1: ionic strength: 162.7 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCANH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CC(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
Software:
CS-Rosetta, Shen, Vernon, Baker and Bax - structure calculation
CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker AvanceII 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts