BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 18530

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18530

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Title: 1H, 13C and 15N resonance assignment of the pair of complement control protein modules of human C7   PubMed: 23054935

Deposition date: 2012-06-18 Original release date: 2012-11-02

Authors: Bramham, Janice; Clark, Carla; Barlow, Paul

Citation: Clark, Carla; Thai, Chuong-Thu; Phelan, Marie; Bella, Juraj; Uhrin, Duan; Ogata, Ronald; Barlow, Paul; Bramham, Janice. "1H, 13C and 15N resonance assignments of the complement control protein modules of the complement component C7."  Biomol. NMR Assignments 7, 285-288 (2013).

Assembly members:
C7_CCPs, polymer, 129 residues, 13990.1061 Da.

Natural source:   Common Name: Humans   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
C7_CCPs: GSHMTEFCPSPPALKDGFVQ DEGTMFPVGKNVVYTCNEGY SLIGNPVARCGEDLRWLVGE MHCQKIACVLPVLMDGIQSH PQKPFYTVGEKVTVSCSGGM SLEGPSAFLCGSSLKWSPEM KNARCVQKE

Data sets:
Data typeCount
13C chemical shifts569
15N chemical shifts132
1H chemical shifts880

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C7_CCPs1

Entities:

Entity 1, C7_CCPs 129 residues - 13990.1061 Da.

Residues 1-4 represent a cloning artefact

1   GLYSERHISMETTHRGLUPHECYSPROSER
2   PROPROALALEULYSASPGLYPHEVALGLN
3   ASPGLUGLYTHRMETPHEPROVALGLYLYS
4   ASNVALVALTYRTHRCYSASNGLUGLYTYR
5   SERLEUILEGLYASNPROVALALAARGCYS
6   GLYGLUASPLEUARGTRPLEUVALGLYGLU
7   METHISCYSGLNLYSILEALACYSVALLEU
8   PROVALLEUMETASPGLYILEGLNSERHIS
9   PROGLNLYSPROPHETYRTHRVALGLYGLU
10   LYSVALTHRVALSERCYSSERGLYGLYMET
11   SERLEUGLUGLYPROSERALAPHELEUCYS
12   GLYSERSERLEULYSTRPSERPROGLUMET
13   LYSASNALAARGCYSVALGLNLYSGLU

Samples:

sample_1: potassium phosphate 20 mM; EDTA 1 mM; sodium azide 0.02%; C7_CCPs 300 uM; H2O 90%; D2O 10%

sample_2: potassium phosphate 20 mM; EDTA 1 mM; sodium azide 0.02%; C7_CCPs, [U-15N], 300 uM; H2O 90%; D2O 10%

sample_3: potassium phosphate 20 mM; EDTA 1 mM; sodium azide 0.02%; C7_CCPs, [U-13C; U-15N], 300 uM; H2O 90%; D2O 10%

sample_conditions_1: pH: 5.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
2D hbCBcgcdHDsample_3isotropicsample_conditions_1
2D hbCBcgcdceHEsample_3isotropicsample_conditions_1
3D CBCANHsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HBHANHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1

Software:

ANALYSIS v2.2.2, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • spectrometer_1 Avance 800 MHz
  • spectrometer_2 Avance 600 MHz

Related Database Links:

SP P10643 P10643 Q5RAD0
DBJ BAF83038 BAG35608 BAJ20698
EMBL CAA60121 CAH91280
GB AAA51861 AAH63851 ADR82762 AIC48386 AKI71774
REF NP_000578 NP_001125756 XP_001138984 XP_003274433 XP_003811023

Download simulated HSQC data in one of the following formats:
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