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
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:

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).
PubMed: 23017427

Assembly members:

Assembly members:
COMPLEMENT_FACTOR_H, polymer, 126 residues, 14159.1579 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: recombinant technology   Host organism: Pichia pastoris   Vector: pPICZaB

Entity Sequences (FASTA):

Entity Sequences (FASTA):
COMPLEMENT_FACTOR_H: EAAGERECELPKIDVHLVPD RKKDQYKVGEVLKFSCKPGF TIVGPNSVQCYHFGLSPDLP ICKEQVQSCGPPPELLNGNV KEKTKEEYGHSEVVEYYCNP RFLMKGPNKIQCVDGEWTTL PVCIVE

Data sets:
Data typeCount
13C chemical shifts568
15N chemical shifts123
1H chemical shifts876

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1COMPLEMENT FACTOR H1

Entities:

Entity 1, COMPLEMENT FACTOR H 126 residues - 14159.1579 Da.

1   GLUALAALAGLYGLUARGGLUCYSGLULEU
2   PROLYSILEASPVALHISLEUVALPROASP
3   ARGLYSLYSASPGLNTYRLYSVALGLYGLU
4   VALLEULYSPHESERCYSLYSPROGLYPHE
5   THRILEVALGLYPROASNSERVALGLNCYS
6   TYRHISPHEGLYLEUSERPROASPLEUPRO
7   ILECYSLYSGLUGLNVALGLNSERCYSGLY
8   PROPROPROGLULEULEUASNGLYASNVAL
9   LYSGLULYSTHRLYSGLUGLUTYRGLYHIS
10   SERGLUVALVALGLUTYRTYRCYSASNPRO
11   ARGPHELEUMETLYSGLYPROASNLYSILE
12   GLNCYSVALASPGLYGLUTRPTHRTHRLEU
13   PROVALCYSILEVALGLU

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:

NameSampleSample stateSample conditions
CbCANHsample_1solutionsample_conditions_1
CbCaCONHsample_1solutionsample_conditions_1
HNCACOsample_1solutionsample_conditions_1
HNCOsample_1solutionsample_conditions_1
HbHaCONHsample_1solutionsample_conditions_1
15N HSQCsample_2solutionsample_conditions_1
c_cconhsample_3solutionsample_conditions_1
h_cconhsample_3solutionsample_conditions_1
hcch_tocsysample_3solutionsample_conditions_1
HSQC CHsample_3solutionsample_conditions_1
15N_NOESYsample_4solutionsample_conditions_1
CH_AROM_HSQCsample_4solutionsample_conditions_1
HB_HDsample_4solutionsample_conditions_1
HB_HEsample_4solutionsample_conditions_1
13C_NOESY D2Osample_4solutionsample_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

Related Database Links:

UNP CFAH_HUMAN
PDB
AlphaFold Q9NU86

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks