BMRB Entry 30024

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30024
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Structural basis for therapeutic inhibition of complement C5
Deposition date:
2016-02-25
Original release date:
2016-07-13
Authors:
Sheppard, D.; Lea, S.
Citation:

Citation: Jore, M.; Johnson, S.; Sheppard, D.; Barber, N.; Li, Y.; Nunn, M.; Elmlund, H.; Lea, S.. "Structural basis for therapeutic inhibition of complement C5."  Nat. Struct. Mol. Biol. 23, 378-386 (2016).
PubMed: 27018802

Assembly members:

Assembly members:
entity_1, polymer, 70 residues, 7476.488 Da.

Natural source:

Natural source:   Common Name: mites & ticks   Taxonomy ID: 34631   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rhipicephalus appendiculatus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPMEEANTTPISVKDQCANV TCRRTVDNRGKRHIDGCPPG CLCVLKGPDSKDNLDGTCYL LATTPKSTTT

Data sets:
Data typeCount
13C chemical shifts203
15N chemical shifts62
1H chemical shifts405

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 70 residues - 7476.488 Da.

1   GLYPROMETGLUGLUALAASNTHRTHRPRO
2   ILESERVALLYSASPGLNCYSALAASNVAL
3   THRCYSARGARGTHRVALASPASNARGGLY
4   LYSARGHISILEASPGLYCYSPROPROGLY
5   CYSLEUCYSVALLEULYSGLYPROASPSER
6   LYSASPASNLEUASPGLYTHRCYSTYRLEU
7   LEUALATHRTHRPROLYSSERTHRTHRTHR

Samples:

sample_1: RaCI2, [U-100% 13C] [U-100% 15N], 330 uM

sample_conditions_1: ionic strength: 162.7 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1

Software:

CS-Rosetta, Shen, Vernon, Baker and Bax - structure calculation

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AvanceII 500 MHz

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