BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 51521

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51521
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Title: Backbone and side chain NMR assignments for the ribosome maturation factor P (RimP) from Staphylococcus aureus   PubMed: 36070063

Deposition date: 2022-07-20 Original release date: 2022-09-13

Authors: Garaeva, Nataliia; Bikmullin, Aydar; Fatkhullin, Bulat; Validov, Shamil; Kieffer, Bruno; Yusupov, Marat; Usachev, Konstantin

Citation: Garaeva, Nataliia; Bikmullin, Aydar; Fatkhullin, Bulat; Validov, Shamil; Kieffer, Bruno; Yusupov, Marat; Usachev, Konstantin. "Backbone and side chain NMR assignments for the ribosome maturation factor P (RimP) from Staphylococcus aureus"  Biomol. NMR Assignments 16, 373-377 (2022).

Assembly members:
entity_1, polymer, 156 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETGB1a

Entity Sequences (FASTA):
entity_1: MASKITEQVEVIVKPIMEDL NFELVDVEYVKEGRDHFLRI SIDKEGGVDLNDCTLASEKI SEAMDANDPIPEMYYLDVAS PGAERPIKKEQDFQNAITKP VFVSLYVPIEGEKEWLGILQ EVNNETIVVQVKIKARTKDI EIPRDKIAKARHAVMI

Data sets:
Data typeCount
13C chemical shifts502
15N chemical shifts137
1H chemical shifts570

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1RimP1

Entities:

Entity 1, RimP 156 residues - Formula weight is not available

1   METALASERLYSILETHRGLUGLNVALGLU
2   VALILEVALLYSPROILEMETGLUASPLEU
3   ASNPHEGLULEUVALASPVALGLUTYRVAL
4   LYSGLUGLYARGASPHISPHELEUARGILE
5   SERILEASPLYSGLUGLYGLYVALASPLEU
6   ASNASPCYSTHRLEUALASERGLULYSILE
7   SERGLUALAMETASPALAASNASPPROILE
8   PROGLUMETTYRTYRLEUASPVALALASER
9   PROGLYALAGLUARGPROILELYSLYSGLU
10   GLNASPPHEGLNASNALAILETHRLYSPRO
11   VALPHEVALSERLEUTYRVALPROILEGLU
12   GLYGLULYSGLUTRPLEUGLYILELEUGLN
13   GLUVALASNASNGLUTHRILEVALVALGLN
14   VALLYSILELYSALAARGTHRLYSASPILE
15   GLUILEPROARGASPLYSILEALALYSALA
16   ARGHISALAVALMETILE

Samples:

sample_1: RimP, [U-100% 13C; U-100% 15N], 0.7 mM; TrisHCl buffer 10 mM; NaCl 250 mM

sample_conditions_1: ionic strength: 0.25 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
1D 13Csample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HMQCsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CcpNMR - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

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