BMRB Entry 18604
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18604
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Title: Solution structure of CCP modules 10-11 of complement factor H PubMed: 23017427
Deposition date: 2012-07-20 Original release date: 2012-10-18
Authors: Makou, Elisavet; Mertens, H.; Maciejewski, M.; Soares, D.; Matis, I.; Schmidt, C.; Herbert, A.; Svergun, D.; Barlow, P.
Citation: Makou, Elisavet; Mertens, Haydyn; Maciejewski, Mateusz; Soares, Dinesh; Matis, Ilias; Schmidt, Christoph; Herbert, Andrew; Svergun, Dmitri; Barlow, Paul. "Solution structure of CCP modules 10-12 illuminates functional architecture of the complement regulator, factor H." J. Mol. Biol. 424, 295-312 (2012).
Assembly members:
COMPLEMENT_FACTOR_H, polymer, 126 residues, 14159.1579 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Pichia pastoris
Entity Sequences (FASTA):
COMPLEMENT_FACTOR_H: EAAGERECELPKIDVHLVPD
RKKDQYKVGEVLKFSCKPGF
TIVGPNSVQCYHFGLSPDLP
ICKEQVQSCGPPPELLNGNV
KEKTKEEYGHSEVVEYYCNP
RFLMKGPNKIQCVDGEWTTL
PVCIVE
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 568 |
15N chemical shifts | 123 |
1H chemical shifts | 876 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | COMPLEMENT FACTOR H | 1 |
Entities:
Entity 1, COMPLEMENT FACTOR H 126 residues - 14159.1579 Da.
1 | GLU | ALA | ALA | GLY | GLU | ARG | GLU | CYS | GLU | LEU | ||||
2 | PRO | LYS | ILE | ASP | VAL | HIS | LEU | VAL | PRO | ASP | ||||
3 | ARG | LYS | LYS | ASP | GLN | TYR | LYS | VAL | GLY | GLU | ||||
4 | VAL | LEU | LYS | PHE | SER | CYS | LYS | PRO | GLY | PHE | ||||
5 | THR | ILE | VAL | GLY | PRO | ASN | SER | VAL | GLN | CYS | ||||
6 | TYR | HIS | PHE | GLY | LEU | SER | PRO | ASP | LEU | PRO | ||||
7 | ILE | CYS | LYS | GLU | GLN | VAL | GLN | SER | CYS | GLY | ||||
8 | PRO | PRO | PRO | GLU | LEU | LEU | ASN | GLY | ASN | VAL | ||||
9 | LYS | GLU | LYS | THR | LYS | GLU | GLU | TYR | GLY | HIS | ||||
10 | SER | GLU | VAL | VAL | GLU | TYR | TYR | CYS | ASN | PRO | ||||
11 | ARG | PHE | LEU | MET | LYS | GLY | PRO | ASN | LYS | ILE | ||||
12 | GLN | CYS | VAL | ASP | GLY | GLU | TRP | THR | THR | LEU | ||||
13 | PRO | VAL | CYS | ILE | VAL | GLU |
Samples:
sample_1: COMPLEMENT FACTOR H, [U-13C; U-15N], 0.4 mM; potassium phosphate buffer 20 mM; H2O 90%; D2O 10%
sample_2: COMPLEMENT FACTOR H, [U-13C; U-15N], 0.54 mM; potassium phosphate buffer 20 mM; H2O 90%; D2O 10%
sample_3: COMPLEMENT FACTOR H, [U-13C; U-15N], 0.15 mM; potassium phosphate buffer 20 mM; H2O 90%; D2O 10%
sample_4: COMPLEMENT FACTOR H, [U-13C; U-15N], 0.5 mM; potassium phosphate buffer 20 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.020 mM; pH: 6.700; pressure: 1.000 atm; temperature: 298.000 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
CbCANH | sample_1 | solution | sample_conditions_1 |
CbCaCONH | sample_1 | solution | sample_conditions_1 |
HNCACO | sample_1 | solution | sample_conditions_1 |
HNCO | sample_1 | solution | sample_conditions_1 |
HbHaCONH | sample_1 | solution | sample_conditions_1 |
15N HSQC | sample_2 | solution | sample_conditions_1 |
c_cconh | sample_3 | solution | sample_conditions_1 |
h_cconh | sample_3 | solution | sample_conditions_1 |
hcch_tocsy | sample_3 | solution | sample_conditions_1 |
HSQC CH | sample_3 | solution | sample_conditions_1 |
15N_NOESY | sample_4 | solution | sample_conditions_1 |
CH_AROM_HSQC | sample_4 | solution | sample_conditions_1 |
HB_HD | sample_4 | solution | sample_conditions_1 |
HB_HE | sample_4 | solution | sample_conditions_1 |
13C_NOESY D2O | sample_4 | solution | sample_conditions_1 |
Software:
AZARA v2.0, Boucher - chemical shift assignment
AutoDep v4.3, PDBe - collection
CNS v1.2, BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- - chemical shift assignment
ANALYSIS v2.0, CCPN - data analysis
Molmol_2K. v2, Koradi, Billeter and Wuthrich - data analysis
ProcheckNMR v3.4.3, Laskowski and MacArthur - data analysis
TOPSPIN v1.3, Bruker Biospin - data analysis
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts