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 34489

Title: Designing a Granulopoietic Protein by Topological Rescaffolding 1: Sohair

Deposition date: 2020-02-06 Original release date: 2020-03-16

Authors: ElGamacy, M.; Coles, M.

Citation: ElGamacy, M.; Coles, M.. "Designing of novel granulopoietic proteins by topological rescaffolding"  . ., .-..

Assembly members:
entity_1, polymer, 175 residues, 20297.090 Da.

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

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

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MMTSDYIIEQIQRKQEEARL KVEEMERKLEAVKEASKRGV SSDQLLNLILDLADIITTLI QIIEESNEAIKELIKNQKGP TSDYIIEQIQRDQEEARKKV EEAEERLERVKEASKRGVSS DQLLDLIRELAEIIEELIRI IRRSNEAIKELIKNQ

Data sets:
Data typeCount
13C chemical shifts644
15N chemical shifts159
1H chemical shifts531

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 175 residues - 20297.090 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METMETTHRSERASPTYRILEILEGLUGLN
4   ILEGLNARGLYSGLNGLUGLUALAARGLEU
5   LYSVALGLUGLUMETGLUARGLYSLEUGLU
6   ALAVALLYSGLUALASERLYSARGGLYVAL
7   SERSERASPGLNLEULEUASNLEUILELEU
8   ASPLEUALAASPILEILETHRTHRLEUILE
9   GLNILEILEGLUGLUSERASNGLUALAILE
10   LYSGLULEUILELYSASNGLNLYSGLYPRO
11   THRSERASPTYRILEILEGLUGLNILEGLN
12   ARGASPGLNGLUGLUALAARGLYSLYSVAL
13   GLUGLUALAGLUGLUARGLEUGLUARGVAL
14   LYSGLUALASERLYSARGGLYVALSERSER
15   ASPGLNLEULEUASPLEUILEARGGLULEU
16   ALAGLUILEILEGLUGLULEUILEARGILE
17   ILEARGARGSERASNGLUALAILELYSGLU
18   LEUILELYSASNGLN

Samples:

sample_1: sohair, [U-99% 13C; U-99% 15N], 650 uM; PBS 50 mM

sample_conditions_1: ionic strength: 125 mM; pH: 5.2; pressure: 1 atm; temperature: 315 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D (H)CC(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
2D NOESYsample_1isotropicsample_conditions_1
3D CNH-NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D NNH-NOESYsample_1isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - data analysis

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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts