BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18599

Title: Solution structure of CCP modules 11-12 of complement factor H   PubMed: 23017427

Authors: Makou, Elisavet; Mertens, Haydyn; Maciejewski, Mateusz; Soares, Dinesh; Matis, Ilias; Schmidt, Christoph; Herbert, Andrew; Svergun, Dmitri; Barlow, Paul; Herbert, C

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:
FH11-12, polymer, 127 residues, 14085.6893 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: KOMAGATAELLA PASTORIS

Entity Sequences (FASTA):
FH11-12: EAEAAGVQSCGPPPELLNGN VKEKTKEEYGHSEVVEYYCN PRFLMKGPNKIQCVDGEWTT LPVCIVEESTCGDIPELEHG WAQLSSPPYYYGDSVEFNCS ESFTMIGHRSITCIHGVWTQ LPQCVAI

Data sets:
Data typeCount
13C chemical shifts550
15N chemical shifts125
1H chemical shifts839

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FH11-121

Entities:

Entity 1, FH11-12 127 residues - 14085.6893 Da.

1   GLUALAGLUALAALAGLYVALGLNSERCYS
2   GLYPROPROPROGLULEULEUASNGLYASN
3   VALLYSGLULYSTHRLYSGLUGLUTYRGLY
4   HISSERGLUVALVALGLUTYRTYRCYSASN
5   PROARGPHELEUMETLYSGLYPROASNLYS
6   ILEGLNCYSVALASPGLYGLUTRPTHRTHR
7   LEUPROVALCYSILEVALGLUGLUSERTHR
8   CYSGLYASPILEPROGLULEUGLUHISGLY
9   TRPALAGLNLEUSERSERPROPROTYRTYR
10   TYRGLYASPSERVALGLUPHEASNCYSSER
11   GLUSERPHETHRMETILEGLYHISARGSER
12   ILETHRCYSILEHISGLYVALTRPTHRGLN
13   LEUPROGLNCYSVALALAILE

Samples:

13C15NFH11-12: FH11-12, [U-13C; U-15N], 0.65 mM; H2O 90%; D2O, [U-2H], 10%

sample_new_1: FH11-12, [U-13C; U-15N], 0.650 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0.020 M; pH: 6.300; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC/HMQC13C15NFH11-12isotropicsample_conditions_1
3D CBCA(CO)NH13C15NFH11-12isotropicsample_conditions_1
CbCaNH (h{CA|Cca}NH)13C15NFH11-12isotropicsample_conditions_1
3D HBHA(CO)NH13C15NFH11-12isotropicsample_conditions_1
HbHaNH (H{ca|cca}NH)13C15NFH11-12isotropicsample_conditions_1
hsqcCH_CT (ct.H[C[{c(2n)|c(2n+1)}]])13C15NFH11-12isotropicsample_conditions_1
3D HCCH-TOCSY13C15NFH11-12isotropicsample_conditions_1
3D H(CCO)NH13C15NFH11-12isotropicsample_conditions_1
c_cconh (hC_cacoNH.relayed)13C15NFH11-12isotropicsample_conditions_1
3D 1H-15N NOESY13C15NFH11-12isotropicsample_conditions_1
3D 1H-13C NOESY13C15NFH11-12isotropicsample_conditions_1
hsqcCH_arom (H[C[caro]])13C15NFH11-12isotropicsample_conditions_1
hbcbcgcdhd (hbCBcgcdHD)13C15NFH11-12isotropicsample_conditions_1
hbcbcgcdcehe (hbCBcgcdHD)13C15NFH11-12isotropicsample_conditions_1
3D HNCO13C15NFH11-12isotropicsample_conditions_1
HNCACO_CORRECT (H[N[ca[CO]]])13C15NFH11-12isotropicsample_conditions_1
CBCACONHsample_new_1solutionsample_conditions_1

Software:

AZARA v2.0, W. Boucher - Processing

AutoDep v4.3, PDBe - collection

CNS v1.2, BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,READ,RICE,SIMONSON,WARREN - Refinement

CYANA v2.1, P. Guntert, C. Mumenthaler and K. Wuthrich - Structure calculation

ANALYSIS v2.0, CCPN - Chemical shift assignment

Molmol v2K. 2, R. Koradi, M. Billeter and W. Wuthrich - Data analysis

ProcheckNMR v3.4.3, R.A. Laskowski, M.W. MacArthur, D.S. Moss and J.M. Thornton - Data analysis

TOPSPIN v1.3, Bruker Biospin - Collection

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UniProt CFAH_HUMAN
PDB