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 34246

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34246
MolProbity Validation Chart

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Title: NMR structure of UB2H, regulatory domain of PBP1b from E. coli   PubMed: 30044025

Deposition date: 2018-03-15 Original release date: 2019-02-18

Authors: Simorre, J.; Maya Martinez, R.; Bougault, C.; Egan, A.; Vollmer, W.

Citation: Egan, A.; Maya-Martinez, R.; Ayala, I.; Bougault, C.; Banzhaf, M.; Breukink, E.; Vollmer, W.; Simorre, J.. "Induced conformational changes activate the peptidoglycan synthase PBP1B."  Mol. Microbiol. 110, 335-356 (2018).

Assembly members:
entity_1, polymer, 114 residues, 13183.969 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 83333   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MGRMVNLEPDMTISKNEMVK LLEATQYRQVSKMTRPGEFT VQANSIEMIRRPFDFPDSKE GQVRARLTFDGDHLATIVNM ENNRQFGFFRLDPR

Data sets:
Data typeCount
13C chemical shifts408
15N chemical shifts85
1H chemical shifts605

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 114 residues - 13183.969 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METGLYARGMETVALASNLEUGLUPROASP
4   METTHRILESERLYSASNGLUMETVALLYS
5   LEULEUGLUALATHRGLNTYRARGGLNVAL
6   SERLYSMETTHRARGPROGLYGLUPHETHR
7   VALGLNALAASNSERILEGLUMETILEARG
8   ARGPROPHEASPPHEPROASPSERLYSGLU
9   GLYGLNVALARGALAARGLEUTHRPHEASP
10   GLYASPHISLEUALATHRILEVALASNMET
11   GLUASNASNARGGLNPHEGLYPHEPHEARG
12   LEUASPPROARG

Samples:

sample_1: UB2H double label, [U-13C; U-15N], 500 ± 5 uM; UB2H single label, [U-99% 15N], 450 ± 5 uM; UB2H_Lys-Oxyl 100 ± 5 uM; Tris/HCl 10 mM; NaCl 200 mM

sample_conditions_1: ionic strength: 200 mM; pH: 7.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D BESTROSY-HNCACBsample_1isotropicsample_conditions_1
3D BESTROSY-HN(CO)CACBsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

Aria v2.3, Rieping W., Habeck M., Bardiaux B., Bernard A , Nilges M. - structure calculation

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CcpNmr_Analysis v2.4, CCPN - data analysis

Talos+, Yang Shen, Frank Delaglio, Gabriel Cornilescu, and Ad Bax - data analysis

Unio10 v2.0.2, Torsten Herrmann - structure calculation

nmrDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker AvanceIII 600 MHz
  • Bruker AvanceIII 700 MHz
  • Bruker AvanceIII 850 MHz
  • Bruker AvanceIII 950 MHz

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