BMRB Entry 34487

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR34487
MolProbity Validation Chart

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

Title:
NMR solution structure of the Iron-Sulfur protein PioC from Rhodopseudomonas palustris TIE-1
Deposition date:
2020-01-31
Original release date:
2020-11-06
Authors:
Cantini, F.; Trindade, I.
Citation:

Citation: Trindade, I.; Invernici, M.; Cantini, F.; Louro, R.; Piccioli, M.. "PRE-driven protein NMR structures: an alternative approach in highly paramagnetic systems"  FEBS J. 288, 3010-3023 (2021).
PubMed: 33124176

Assembly members:

Assembly members:
entity_1, polymer, 54 residues, 5882.649 Da.
entity_SF4, non-polymer, 351.640 Da.

Natural source:

Natural source:   Common Name: Rhodopseudomonas palustris TIE-1   Taxonomy ID: 395960   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Rhodopseudomonas palustris

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: VTKKASHKDAGYQESPNGAK RCGTCRQFRPPSSCITVESP ISENGWCRLYAGKA

Data sets:
Data typeCount
13C chemical shifts231
15N chemical shifts60
1H chemical shifts324

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22

Entities:

Entity 1, unit_1 54 residues - 5882.649 Da.

1   VALTHRLYSLYSALASERHISLYSASPALA
2   GLYTYRGLNGLUSERPROASNGLYALALYS
3   ARGCYSGLYTHRCYSARGGLNPHEARGPRO
4   PROSERSERCYSILETHRVALGLUSERPRO
5   ILESERGLUASNGLYTRPCYSARGLEUTYR
6   ALAGLYLYSALA

Entity 2, unit_2 - Fe4 S4 - 351.640 Da.

1   SF4

Samples:

sample_1: PioC, [U-13C; U-15N], 500 ± 0.2 uM; potassium phosphate buffer 50 mM; NaCl 300 mM

sample_2: PioC 500 ± 0.2 uM; potassium phosphate buffer 50 mM; NaCl 300 mM

sample_3: PioC, [U-99% 15N], 150 ± 0.2 uM; potassium phosphate buffer 50 mM; NaCl 300 mM

sample_conditions_1: ionic strength: 300 mM; pH: 5.6; 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 CBCANHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D CONsample_1isotropicsample_conditions_1
2D relaxation experimentssample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

TopSpin v3.16, Bruker Biospin - collection, processing

Amber v16, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 900 MHz
  • Bruker AVANCE 500 MHz
  • Bruker AVANCE 950 MHz
  • Bruker AVANCE 700 MHz

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