BMRB Entry 7420
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7420
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Title: STRUCTURE OF CCP MODULE 7 OF COMPLEMENT FACTOR H- THE AMD AT RISK VARIENT (402H) PubMed: 17360715
Deposition date: 2008-03-06 Original release date: 2008-08-08
Authors: Herbert, A.; Deakin, J.; Schmidt, C.; Blaum, B.; Egan, C.; Ferreira, V.; Pangburn, M.; Lyon, M.; Uhrin, D.; Barlow, P.
Citation: Herbert, A.; Deakin, J.; Schmidt, C.; Blaum, B.; Egan, C.; Ferreira, V.; Pangburn, M.; Lyon, M.; Uhrin, D.; Barlow, P.. "Structure Shows Glycosaminoglycan- and Protein-Recognition Site in Factor H is Perturbed by Age-Related Macular Degeneration-Linked single nucleotide polymorphism" J. Biol. Chem. 282, 18960-18968 (2007).
Assembly members:
COMPLEMENT_FACTOR_H, polymer, 65 residues, Formula weight is not available
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: EAAGLRKCYFPYLENGYNQN
HGRKFVQGKSIDVACHPGYA
LPKAQTTVTCMENGWSPTPR
CIRVK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 275 |
15N chemical shifts | 68 |
1H chemical shifts | 439 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | COMPLEMENT FACTOR H | 1 |
Entities:
Entity 1, COMPLEMENT FACTOR H 65 residues - Formula weight is not available
1 | GLU | ALA | ALA | GLY | LEU | ARG | LYS | CYS | TYR | PHE | ||||
2 | PRO | TYR | LEU | GLU | ASN | GLY | TYR | ASN | GLN | ASN | ||||
3 | HIS | GLY | ARG | LYS | PHE | VAL | GLN | GLY | LYS | SER | ||||
4 | ILE | ASP | VAL | ALA | CYS | HIS | PRO | GLY | TYR | ALA | ||||
5 | LEU | PRO | LYS | ALA | GLN | THR | THR | VAL | THR | CYS | ||||
6 | MET | GLU | ASN | GLY | TRP | SER | PRO | THR | PRO | ARG | ||||
7 | CYS | ILE | ARG | VAL | LYS |
Samples:
sample: COMPLEMENT FACTOR H mM
sample_conditions_1: ionic strength: 20 mM; pH: 5.2; pressure: 1.0 atm; temperature: 298.0 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
CBCACONH | sample | isotropic | sample_conditions_1 |
CBCANH | sample | isotropic | sample_conditions_1 |
H_CCONH TOCSY | sample | isotropic | sample_conditions_1 |
HCCH TOCSY | sample | isotropic | sample_conditions_1 |
HNCO | sample | isotropic | sample_conditions_1 |
15N EDITED TOCSY HSQC | sample | isotropic | sample_conditions_1 |
HBHACONH | sample | isotropic | sample_conditions_1 |
HBHANH | sample | isotropic | sample_conditions_1 |
C_CCONH TOCSY | sample | isotropic | sample_conditions_1 |
HBCBCGCDCEHE | sample | isotropic | sample_conditions_1 |
HBCBCGCDHD | sample | isotropic | sample_conditions_1 |
Software:
CNS v1.1, BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,SIMONSON,WARREN - refinement
ANALYSIS vANALYSIS - structure solution
NMR spectrometers:
- BRUKER OTHER 600 MHz
Related Database Links:
BMRB | 7421 |
PDB | |
EMBL | CAA30403 CAB41739 |
GB | AAA52013 AAH37285 AAI10644 ADZ15369 AHH32464 |
REF | NP_001014975 XP_004028137 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts