BMRB Entry 50033

Title:
CDC25B - W550A
Deposition date:
2019-10-04
Original release date:
2019-10-29
Authors:
Reis, Andre
Citation:

Citation: Reis, Andre; Sayegh, Raphael; Marana, Sandro; Arantes, Guilherme. "Combining free energy simulations and NMR chemical-shift perturbation to identify transient cation-pi contacts in proteins"  J. Chem. Inf. Model. 60, 890-897 (2020).
PubMed: 31738549

Assembly members:

Assembly members:
entity_1, polymer, 218 residues, -4 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-28a

Data sets:
Data typeCount
15N chemical shifts144
1H chemical shifts144

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CDC25B - W550A1

Entities:

Entity 1, CDC25B - W550A 218 residues - -4 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METGLUPHEGLNSERASPHISARGGLULEU
4   ILEGLYASPTYRSERLYSALAPHELEULEU
5   GLNTHRVALASPGLYLYSHISGLNASPLEU
6   LYSTYRILESERPROGLUTHRMETVALALA
7   LEULEUTHRGLYLYSPHESERASNILEVAL
8   ASPLYSPHEVALILEVALASPCYSARGTYR
9   PROTYRGLUTYRGLUGLYGLYHISILELYS
10   THRALAVALASNLEUPROLEUGLUARGASP
11   ALAGLUSERPHELEULEULYSSERPROILE
12   ALAPROCYSSERLEUASPLYSARGVALILE
13   LEUILEPHEHISCYSGLUPHESERSERGLU
14   ARGGLYPROARGMETCYSARGPHEILEARG
15   GLUARGASPARGALAVALASNASPTYRPRO
16   SERLEUTYRTYRPROGLUMETTYRILELEU
17   LYSGLYGLYTYRLYSGLUPHEPHEPROGLN
18   HISPROASNPHECYSGLUPROGLNASPTYR
19   ARGPROMETASNHISGLUALAPHELYSASP
20   GLULEULYSTHRPHEARGLEULYSTHRARG
21   SERALAALAGLYGLUARGSERARGARGGLU
22   LEUCYSSERARGLEUGLNASPGLN

Samples:

sample_1: entity_1, [U-100% 15N], 0.2 mM; NaH2PO4 20 mM; NaCl 50 mM; BMER 5 mM; dithiotreitol 2 mM

sample_conditions_1: ionic strength: 0.075 M; pH: 6.7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Bruker AIII 800 MHz

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