BMRB Entry 19311

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19311
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:
Chemical shifts and structural restraints for Saccharomyces cerevisiae Est3 protein
Deposition date:
2013-06-21
Original release date:
2013-12-16
Authors:
Rao, Timsi; Armstrong, Geoffrey; Wuttke, Deborah
Citation:

Citation: Rao, Timsi; Lubin, Johnathan; Armstrong, Geoffrey; Tucey, Timothy; Lundblad, Victoria; Wuttke, Deborah. "Structure of Est3 reveals a bimodal surface with differential roles in telomere replication."  Proc. Natl. Acad. Sci. U.S.A. 111, 214-218 (2014).
PubMed: 24344315

Assembly members:

Assembly members:
entity, polymer, 170 residues, 19297.996 Da.

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: STDSVFLQPWIKALIEDNSE HDQYHPSGHVIPSLTKQDLA LPHMSPTILTNPCHFAKITK FYNVCDYKVYASIRDSSHQI LVEFSQECVSNFERTHNCRI TSETTNCLMIIGDADLVYVT NSRAMSHFKISLSNISSKEI VPVLNVNQATIFDIDQVGSL STFPFVYKYL

Data sets:
Data typeCount
13C chemical shifts568
15N chemical shifts151
1H chemical shifts352

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Est3 protein1

Entities:

Entity 1, Est3 protein 170 residues - 19297.996 Da.

Residues 1-12 were deleted from S. cerevisiae Est3 protein sequence. First serine was part of the cleaved affinity tag.

1   SERTHRASPSERVALPHELEUGLNPROTRP
2   ILELYSALALEUILEGLUASPASNSERGLU
3   HISASPGLNTYRHISPROSERGLYHISVAL
4   ILEPROSERLEUTHRLYSGLNASPLEUALA
5   LEUPROHISMETSERPROTHRILELEUTHR
6   ASNPROCYSHISPHEALALYSILETHRLYS
7   PHETYRASNVALCYSASPTYRLYSVALTYR
8   ALASERILEARGASPSERSERHISGLNILE
9   LEUVALGLUPHESERGLNGLUCYSVALSER
10   ASNPHEGLUARGTHRHISASNCYSARGILE
11   THRSERGLUTHRTHRASNCYSLEUMETILE
12   ILEGLYASPALAASPLEUVALTYRVALTHR
13   ASNSERARGALAMETSERHISPHELYSILE
14   SERLEUSERASNILESERSERLYSGLUILE
15   VALPROVALLEUASNVALASNGLNALATHR
16   ILEPHEASPILEASPGLNVALGLYSERLEU
17   SERTHRPHEPROPHEVALTYRLYSTYRLEU

Samples:

sample_1: Est3 protein, [U-13C; U-15N; U-2H], 280 uM; Bis tris propane 50 mM; MOPS 150 mM; sodium sulfate 50 mM; arginine 100 mM; glutamate 100 mM; NDSB-195 100 mM; DTT 2 mM; D2O 7%; H2O 93%; TSP 0.15 mM

sample_2: Est3 protein, [U-15N], 140 uM; Bis tris propane 50 mM; MOPS 150 mM; sodium sulfate 50 mM; arginine 100 mM; glutamate 100 mM; NDSB-195 100 mM; DTT 2 mM; D2O 10%; H2O 90%; Pf1 phage 9.6 mg/mL

sample_3: Est3 protein, [U-15N], 140 uM; Bis tris propane 50 mM; MOPS 150 mM; sodium sulfate 50 mM; arginine 100 mM; glutamate 100 mM; NDSB-195 100 mM; DTT 2 mM; D2O 10%; H2O 90%

sample_4: Est3 protein, [U-13C; U-15N; U-2H], 280 uM; Bis tris propane 50 mM; MOPS 150 mM; sodium sulfate 50 mM; arginine 100 mM; glutamate 100 mM; NDSB-195 100 mM; DTT 2 mM; D2O 7%; H2O 93%

sample_conditions_1: pH: 7.1; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC TROSYsample_1isotropicsample_conditions_1
3D HNCA TROSYsample_1isotropicsample_conditions_1
3D HN(CA)CB TROSYsample_1isotropicsample_conditions_1
3D HN(CO)CA TROSYsample_1isotropicsample_conditions_1
3D HN(COCA)CB TROSYsample_1isotropicsample_conditions_1
3D HNCO TROSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HMQCsample_4isotropicsample_conditions_1
3D HMCMCBCAsample_4isotropicsample_conditions_1
3D HMCMCGCBCAsample_4isotropicsample_conditions_1
3D methyl 1H-1H 13C HMQC NOESYsample_4isotropicsample_conditions_1
2D 1H-15N HSQCsample_2anisotropicsample_conditions_1
2D 1H-15N HSQC TROSYsample_2anisotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-15N HSQC TROSYsample_3isotropicsample_conditions_1

Software:

VNMRJ v3.1, Varian - collection

ANALYSIS v2.1.5, CCPN - chemical shift assignment, data analysis, peak picking

NMRPipe v2011, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - Constraints list generation for structure solution

Rosetta v3.4, David Baker - structure solution

CS-Rosetta_toolbox v1.3, David Baker - structure solution

X-PLOR NIH v2.29, Schwieters, Kuszewski, Tjandra and Clore - structure and constraints validation

NMR spectrometers:

  • Varian VNMRS 800 MHz
  • Agilent DD2 900 MHz

Related Database Links:

PDB
DBJ GAA24105
GB AHY75987 AJR36748 AJR36943 AJR37282 AJR37668
REF NP_012256
SP Q03096
TPG DAA08536
AlphaFold Q03096

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