BMRB Entry 34488

Title:
Designing a Granulopoietic Protein by Topological Rescaffolding 2: Moevan
Deposition date:
2020-02-06
Original release date:
2020-03-16
Authors:
ElGamacy, M.; Coles, M.
Citation:

Citation: Alvarez, Birte; Skokowa, Julia; Coles, Murray; Mir, Perihan; Nasri, Masoud; Maksymenko, Kateryna; Weidmann, Laura; Rogers, Katherine; Welte, Karl; Lupas, Andrei; Muller, Patrick; ElGamacy, Mohammad. "Design of novel granulopoietic proteins by topological rescaffolding"  PLoS Biol. 18, e3000919-e3000919 (2020).
PubMed: 33351791

Assembly members:

Assembly members:
entity_1, polymer, 138 residues, 15645.854 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 32630   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts428
15N chemical shifts89
1H chemical shifts623

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 138 residues - 15645.854 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METGLUALAALAALAALAALAARGASPGLU
4   SERALATYRLEULYSLEUGLNGLUGLNMET
5   ARGLYSILEASPALAASPALAALAALALEU
6   SERGLUTHRARGTHRILEGLUGLULEUASP
7   THRPHELYSLEUASPVALALAASPPHEVAL
8   THRTHRVALVALGLNLEUALAGLUGLULEU
9   GLUHISARGPHEGLYARGASNARGARGGLY
10   ARGTHRGLUILETYRLYSILEVALLYSGLU
11   VALASPARGLYSLEULEUASPLEUTHRASP
12   ALAVALLEUALALYSGLULYSLYSGLYGLU
13   ASPILELEUASNMETVALALAGLUILELYS
14   ALALEULEUILEASNILETYRLYS

Samples:

sample_1: Moevan, [U-99% 13C; U-99% 15N], 600 uM; PBS 50 mM

sample_conditions_1: ionic strength: 125 mM; pH: 5.2; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 125 mM; pH: 5.2; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_2
3D HNCAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_2
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_2
3D (H)CC(CO)NHsample_1isotropicsample_conditions_1
3D (H)CC(CO)NHsample_1isotropicsample_conditions_2
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_2
2D NOESYsample_1isotropicsample_conditions_1
3D CNH-NOESYsample_1isotropicsample_conditions_1
3D CNH-NOESYsample_1isotropicsample_conditions_2
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

Sparky, Goddard - chemical shift assignment

Rosetta, Baker - structure calculation

CoMAND, in house - refinement

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 800 MHz

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