BMRB Entry 26779

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26779

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Title:
Human Cdc25B complete catalytic domain: backbone assignments (1H, 13CA, 13CB, 13C', 15N), 15N relaxation times (T1 and T2), heteronuclear NOEs and residual dipolar couplings (NH)
Deposition date:
2016-04-14
Original release date:
2016-08-01
Authors:
Sayegh, Raphael; Tamaki, Fabio; Marana, Sandro; Salinas, Roberto; Arantes, Guilherme
Citation:

Citation: Sayegh, Raphael; Tamaki, Fabio; Marana, Sandro; Salinas, Roberto; Arantes, Guilherme. "Conformational flexibility of the complete catalytic domain of Cdc25B phosphatases"  Proteins 84, 1567-1575 (2016).
PubMed: 27410025

Assembly members:

Assembly members:
Cdc25B, polymer, 201 residues, Formula weight is not available

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: p28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Cdc25B: GSHMEFQSDHRELIGDYSKA FLLQTVDGKHQDLKYISPET MVALLTGKFSNIVDKFVIVD CRYPYEYEGGHIKTAVNLPL ERDAESFLLKSPIAPCSLDK RVILIFHCEFSSERGPRMCR FIRERDRAVNDYPSLYYPEM YILKGGYKEFFPQHPNFCEP QDYRPMNHEAFKDELKTFRL KTRSWAGERSRRELCSRLQD Q

Data sets:
Data typeCount
13C chemical shifts467
15N chemical shifts143
1H chemical shifts143
T1 relaxation values137
T2 relaxation values86
heteronuclear NOE values135
order parameters80
residual dipolar couplings144

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Cdc25B monomer1

Entities:

Entity 1, Cdc25B monomer 201 residues - Formula weight is not available

1   GLYSERHISMETGLUPHEGLNSERASPHIS
2   ARGGLULEUILEGLYASPTYRSERLYSALA
3   PHELEULEUGLNTHRVALASPGLYLYSHIS
4   GLNASPLEULYSTYRILESERPROGLUTHR
5   METVALALALEULEUTHRGLYLYSPHESER
6   ASNILEVALASPLYSPHEVALILEVALASP
7   CYSARGTYRPROTYRGLUTYRGLUGLYGLY
8   HISILELYSTHRALAVALASNLEUPROLEU
9   GLUARGASPALAGLUSERPHELEULEULYS
10   SERPROILEALAPROCYSSERLEUASPLYS
11   ARGVALILELEUILEPHEHISCYSGLUPHE
12   SERSERGLUARGGLYPROARGMETCYSARG
13   PHEILEARGGLUARGASPARGALAVALASN
14   ASPTYRPROSERLEUTYRTYRPROGLUMET
15   TYRILELEULYSGLYGLYTYRLYSGLUPHE
16   PHEPROGLNHISPROASNPHECYSGLUPRO
17   GLNASPTYRARGPROMETASNHISGLUALA
18   PHELYSASPGLULEULYSTHRPHEARGLEU
19   LYSTHRARGSERTRPALAGLYGLUARGSER
20   ARGARGGLULEUCYSSERARGLEUGLNASP
21   GLN

Samples:

sample_1: Cdc25B, [U-100% 13C; U-100% 15N], 0.15 mM; D2O, [U-2H], 5%; sodium phosphate 20 mM; DTT 2 mM; sodium chloride 50 mM; beta-mercaptoethanol 2 mM

sample_2: Cdc25B, [U-100% 13C; U-100% 15N], 0.1 mM; D2O, [U-2H], 5%; sodium phosphate 20 mM; DTT 2 mM; sodium chloride 50 mM; beta-mercaptoethanol 2 mM; n-hexanol 7.4 uL; PEG C12E5 5%

sample_conditions_1: ionic strength: 0.105 M; pH: 6.75; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-15N HSQC IPAPsample_2anisotropicsample_conditions_1

Software:

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

TOPSPIN, Bruker Biospin - collection, processing

ModelFree, Palmer - data analysis

AutoAssign, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz

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