BMRB Entry 34585

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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/BMR34585
MolProbity Validation Chart

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Title:
Solution Structure of RoxP
Deposition date:
2020-12-19
Original release date:
2021-11-19
Authors:
Stoedkilde, K.; Nielsen, J.; Mulder, F.; Andersen, C.
Citation:

Citation: Stoedkilde, K.; Nielsen, J.; Petersen, S.; Paetzold, B.; Brueggemann, H.; Mulder, F.; Andersen, C.. "Solution Structure of the Cutibacterium acnes-Specific Protein RoxP and Insights Into Its Antioxidant Activity"  Front. Cell Infect. Microbiol. 12, 803004-803004 (2022).
PubMed: 35223541

Assembly members:

Assembly members:
entity_1, polymer, 147 residues, 15977.760 Da.

Natural source:

Natural source:   Common Name: Cutibacterium acnes   Taxonomy ID: 267747   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Cutibacterium acnes

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pET22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MTPIDESQLPVGPQVSVTDS AQHTGPFAASSPLTITVKPG APCVRADGYQESMVTRVLDD KGHQVWTGTFDESKLIGGTG LGTATFHVGSPAAAFNFHGS ERTTYRTLSYCAYPHYVNGT RERLSQVSVKTFMVDPALNL EHHHHHH

Data sets:
Data typeCount
13C chemical shifts573
15N chemical shifts138
1H chemical shifts902

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 147 residues - 15977.760 Da.

1   METTHRPROILEASPGLUSERGLNLEUPRO
2   VALGLYPROGLNVALSERVALTHRASPSER
3   ALAGLNHISTHRGLYPROPHEALAALASER
4   SERPROLEUTHRILETHRVALLYSPROGLY
5   ALAPROCYSVALARGALAASPGLYTYRGLN
6   GLUSERMETVALTHRARGVALLEUASPASP
7   LYSGLYHISGLNVALTRPTHRGLYTHRPHE
8   ASPGLUSERLYSLEUILEGLYGLYTHRGLY
9   LEUGLYTHRALATHRPHEHISVALGLYSER
10   PROALAALAALAPHEASNPHEHISGLYSER
11   GLUARGTHRTHRTYRARGTHRLEUSERTYR
12   CYSALATYRPROHISTYRVALASNGLYTHR
13   ARGGLUARGLEUSERGLNVALSERVALLYS
14   THRPHEMETVALASPPROALALEUASNLEU
15   GLUHISHISHISHISHISHIS

Samples:

sample_1: RoxP, [U-98% 13C; U-98% 15N], 1.2 mM

sample_conditions_1: ionic strength: 0 M; pH: 5.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
2D HBCBCGCDHDsample_1isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 15N-separated NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
4D 13C-separated NOESYsample_1isotropicsample_conditions_1

Software:

TALOS-N, Shen Y, Bax A - chemical shift calculation

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

Sparky, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker AM 950 MHz

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