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 50011

Title: rsFolder_off   PubMed: 31733726

Deposition date: 2019-09-10 Original release date: 2019-09-11

Authors: Christou, Nina-Eleni

Citation: Christou, Nina-Eleni; Ayala, Isabel; Giandoreggio-Barranco, Karine; Byrdin, Martin; Adam, Virgile; Bourgeois, Dominique; Brutscher, Bernhard. "NMR Reveals Light-Induced Changes in the Dynamics of a Photoswitchable Fluorescent Protein"  Biophys. J. 117, 2087-2100 (2019).

Assembly members:
entity_1, polymer, 249 residues, Formula weight is not available

Natural source:   Common Name: Aequorea victoria   Taxonomy ID: 6100   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Aequorea victoria

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

Entity Sequences (FASTA):
entity_1: GSHMATMVSKGEELFTGVVP ILVELDGDVNGHKFSVRGEG EGDATNGKLTLKFICTTGKL PVPWPTLVTTLAYGVLCFSR YPDHMKRHDFFKSAMPEGYV QERTISFKDDGTYKTRAEVK FEGDTLVNRIELKGIDFKED GNILGHKLEYNFNSHNVYIT ADKQKNGIKSNFKIRHNVED GSVQLADHYQQNTPIGDGPV LLPDNHYLSTQSKLSKDPNE KRDHMVLLEFVTAAGITHGM DELYKGSHGC

Data sets:
Data typeCount
13C chemical shifts671
15N chemical shifts201
1H chemical shifts471

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1rsFolder1

Entities:

Entity 1, rsFolder 249 residues - Formula weight is not available

1   GLYSERHISMETALATHRMETVALSERLYS
2   GLYGLUGLULEUPHETHRGLYVALVALPRO
3   ILELEUVALGLULEUASPGLYASPVALASN
4   GLYHISLYSPHESERVALARGGLYGLUGLY
5   GLUGLYASPALATHRASNGLYLYSLEUTHR
6   LEULYSPHEILECYSTHRTHRGLYLYSLEU
7   PROVALPROTRPPROTHRLEUVALTHRTHR
8   LEUALATYRGLYVALLEUCYSPHESERARG
9   TYRPROASPHISMETLYSARGHISASPPHE
10   PHELYSSERALAMETPROGLUGLYTYRVAL
11   GLNGLUARGTHRILESERPHELYSASPASP
12   GLYTHRTYRLYSTHRARGALAGLUVALLYS
13   PHEGLUGLYASPTHRLEUVALASNARGILE
14   GLULEULYSGLYILEASPPHELYSGLUASP
15   GLYASNILELEUGLYHISLYSLEUGLUTYR
16   ASNPHEASNSERHISASNVALTYRILETHR
17   ALAASPLYSGLNLYSASNGLYILELYSSER
18   ASNPHELYSILEARGHISASNVALGLUASP
19   GLYSERVALGLNLEUALAASPHISTYRGLN
20   GLNASNTHRPROILEGLYASPGLYPROVAL
21   LEULEUPROASPASNHISTYRLEUSERTHR
22   GLNSERLYSLEUSERLYSASPPROASNGLU
23   LYSARGASPHISMETVALLEULEUGLUPHE
24   VALTHRALAALAGLYILETHRHISGLYMET
25   ASPGLULEUTYRLYSGLYSERGLYCYS

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 200 ± 20 uM; HEPES 50 mM; NaCl 100 mM

sample_conditions_1: pH: 7.50; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D Laser-Driven EXSYsample_1isotropicsample_conditions_1
2D AminoAcid_Edited 1H-13C SOFAST HMQCsample_1isotropicsample_conditions_1
2D 1H-13C SOFAST HMQCsample_1isotropicsample_conditions_1

Software:

software_1 v2.4.2, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 850 MHz

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