BMRB Entry 34970

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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/BMR34970
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Title:
NMR solution structure of OrfM from ICESt3 of Streptococcus thermophilus
Deposition date:
2024-12-10
Original release date:
2025-10-31
Authors:
Tsan, P.; Cappele, J.; Laroussi, H.; Clement, E.; Favier, F.; Didierjean, C.; Soler, N.; Leblond-Bourget, N.
Citation:

Citation: Laroussi, H.; Maffo-Woulefack, R.; Cappele, J.; Sekkouri-Alaoui, H.; Lessure, L.; Zahaf, M.; Girardet, J.-M.; Clement, E.; Thiriet, L.; Bertin, S.; Roussel, Y.; Douzi, B.; Didierjean, C.; Favier, F.; Tsan, P.; Leblond-Bourget, N.; Soler, N.. "Two OB-fold proteins from a Gram-positive conjugative element engage in relaxosome assembly and DNA processing"  Nucleic Acids Res. ., .-. (2025).

Assembly members:

Assembly members:
entity_1, polymer, 98 residues, 10826.521 Da.

Natural source:

Natural source:   Common Name: Streptococcus thermophilus   Taxonomy ID: 1308   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus thermophilus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MIPETLVMKPDFIGPAYYEK LGNAPRFIFGKEGKYQRHIL NSEKHGAFHVITPASTTVFP EDALVEVVNPIFLSDTALNG NSVAPALNVFAEKLVLKK

Data sets:
Data typeCount
13C chemical shifts368
15N chemical shifts94
1H chemical shifts643

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 98 residues - 10826.521 Da.

1   METILEPROGLUTHRLEUVALMETLYSPRO
2   ASPPHEILEGLYPROALATYRTYRGLULYS
3   LEUGLYASNALAPROARGPHEILEPHEGLY
4   LYSGLUGLYLYSTYRGLNARGHISILELEU
5   ASNSERGLULYSHISGLYALAPHEHISVAL
6   ILETHRPROALASERTHRTHRVALPHEPRO
7   GLUASPALALEUVALGLUVALVALASNPRO
8   ILEPHELEUSERASPTHRALALEUASNGLY
9   ASNSERVALALAPROALALEUASNVALPHE
10   ALAGLULYSLEUVALLEULYSLYS

Samples:

sample_1: OrfM, [U-13C; U-15N], 0.545 mM; HEPES 20 mM; sodium chloride 100 mM

sample_2: OrfM, [U-15N], 0.15 mM; sodium chloride 200 mM; potassium phosphate 20 mM

sample_conditions_1: ionic strength: 100 mM; pH: 1; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_2
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_2
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1

Software:

CcpNmr Analysis, CCPN - chemical shift assignment, peak picking

ARIA, Linge, O'Donoghue and Nilges - refinement, structure calculation

NMR spectrometers:

  • Bruker DRX 600 MHz

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