BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 50941

Title: NMR assignments and secondary structure determination of the N-terminal domain of ribosome maturation factor M from Staphylococcus aureus

Deposition date: 2021-05-14 Original release date: 2021-06-14

Authors: Natalia, Garaeva; Bikmullin, Aydar; Kuchaev, Evgeniy; Klochkova, Evelina; Validov, Shamil; Klochkov, Vladimir; Aganov, Albert; Yusupov, Marat; Usachev, Konstantin

Citation: Natalia, Garaeva; Bikmullin, Aydar; Kuchaev, Evgeniy; Klochkova, Evelina; Validov, Shamil; Klochkov, Vladimir; Aganov, Albert; Yusupov, Marat; Usachev, Konstantin. "NMR assignments and secondary structure determination of the N-terminal domain of ribosome maturation factor M from Staphylococcus aureus"  Russian Chemical Bulletin ., .-..

Assembly members:
entity_1, polymer, 172 residues, Formula weight is not available

Natural source:   Common Name: Staphylococcus aureus   Taxonomy ID: 1280   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETGB1_a

Entity Sequences (FASTA):
entity_1: MKHHHHHHPMKQYKLILNGK TLKGETTTEAVDAATAEKVF KQYANDNGVDGEWTYDDATK TFTVTEGSGSGSENLYFQGA GRVEVGQIVNTHGIKGEIKV KSNSDFTDVRFQPGQVLTVV HNNNDLEYTVKSHRVHKGLH MLTFEGINNINDIEHLKGSS IYQERDHEDIVL

Data sets:
Data typeCount
13C chemical shifts538
15N chemical shifts156
1H chemical shifts406

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Gb1-RimM_NTD1

Entities:

Entity 1, Gb1-RimM_NTD 172 residues - Formula weight is not available

1   METLYSHISHISHISHISHISHISPROMET
2   LYSGLNTYRLYSLEUILELEUASNGLYLYS
3   THRLEULYSGLYGLUTHRTHRTHRGLUALA
4   VALASPALAALATHRALAGLULYSVALPHE
5   LYSGLNTYRALAASNASPASNGLYVALASP
6   GLYGLUTRPTHRTYRASPASPALATHRLYS
7   THRPHETHRVALTHRGLUGLYSERGLYSER
8   GLYSERGLUASNLEUTYRPHEGLNGLYALA
9   GLYARGVALGLUVALGLYGLNILEVALASN
10   THRHISGLYILELYSGLYGLUILELYSVAL
11   LYSSERASNSERASPPHETHRASPVALARG
12   PHEGLNPROGLYGLNVALLEUTHRVALVAL
13   HISASNASNASNASPLEUGLUTYRTHRVAL
14   LYSSERHISARGVALHISLYSGLYLEUHIS
15   METLEUTHRPHEGLUGLYILEASNASNILE
16   ASNASPILEGLUHISLEULYSGLYSERSER
17   ILETYRGLNGLUARGASPHISGLUASPILE
18   VALLEU

Samples:

sample_1: GB1-RimM_NTD, [U-100% 13C; U-100% 15N], 0.68 mM; NaCl 200 mM; TRIS-HCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 8.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_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