BMRB Entry 25442
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25442
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Title: Snu17p-Bud13p structure intermediate during RES complex assembly PubMed: 26212312
Deposition date: 2015-01-19 Original release date: 2015-08-10
Authors: Wysoczanski, Piotr; Becker, Stefan; Zweckstetter, Markus
Citation: Wysoczanski, Piotr; Becker, Stefan; Zweckstetter, Markus. "Structures of intermediates during RES complex assembly" Sci. Rep. 5, 12545-12545 (2015).
Assembly members:
Snu17p, polymer, 118 residues, 13496.103 Da.
Bud13p, polymer, 41 residues, 4888.440 Da.
Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Snu17p: GAMGNEYKDNAYIYIGNLNR
ELTEGDILTVFSEYGVPVDV
ILSRDENTGESQGFAYLKYE
DQRSTILAVDNLNGFKIGGR
ALKIDHTFYRPKRSLQKYYE
AVKEELDRDIVSKNNAEK
Bud13p: YDKPAPENRFAIMPGSRWDG
VHRSNGFEEKWFAKQNEINE
K
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 527 |
15N chemical shifts | 148 |
1H chemical shifts | 1013 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity_1 | 1 |
2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 118 residues - 13496.103 Da.
as above
1 | GLY | ALA | MET | GLY | ASN | GLU | TYR | LYS | ASP | ASN | ||||
2 | ALA | TYR | ILE | TYR | ILE | GLY | ASN | LEU | ASN | ARG | ||||
3 | GLU | LEU | THR | GLU | GLY | ASP | ILE | LEU | THR | VAL | ||||
4 | PHE | SER | GLU | TYR | GLY | VAL | PRO | VAL | ASP | VAL | ||||
5 | ILE | LEU | SER | ARG | ASP | GLU | ASN | THR | GLY | GLU | ||||
6 | SER | GLN | GLY | PHE | ALA | TYR | LEU | LYS | TYR | GLU | ||||
7 | ASP | GLN | ARG | SER | THR | ILE | LEU | ALA | VAL | ASP | ||||
8 | ASN | LEU | ASN | GLY | PHE | LYS | ILE | GLY | GLY | ARG | ||||
9 | ALA | LEU | LYS | ILE | ASP | HIS | THR | PHE | TYR | ARG | ||||
10 | PRO | LYS | ARG | SER | LEU | GLN | LYS | TYR | TYR | GLU | ||||
11 | ALA | VAL | LYS | GLU | GLU | LEU | ASP | ARG | ASP | ILE | ||||
12 | VAL | SER | LYS | ASN | ASN | ALA | GLU | LYS |
Entity 2, entity_2 41 residues - 4888.440 Da.
as above
1 | TYR | ASP | LYS | PRO | ALA | PRO | GLU | ASN | ARG | PHE | ||||
2 | ALA | ILE | MET | PRO | GLY | SER | ARG | TRP | ASP | GLY | ||||
3 | VAL | HIS | ARG | SER | ASN | GLY | PHE | GLU | GLU | LYS | ||||
4 | TRP | PHE | ALA | LYS | GLN | ASN | GLU | ILE | ASN | GLU | ||||
5 | LYS |
Samples:
sample_1: sodium phosphate 25 mM; sodium chloride 250 mM; sodium azide 1 mM; entity_1, [U-13C; U-15N], 0.8 1 mM; entity_21.0 1.2 mM; H2O 90%; D2O 10%
sample_2: sodium phosphate 25 mM; sodium chloride 250 mM; sodium azide 1 mM; entity_11 1.2 mM; entity_2, [U-13C; U-15N], 0.8 1 mM; Snu17p 90%; Snu17p 10%
sample_3: sodium phosphate 25 mM; sodium chloride 250 mM; sodium azide 1 mM; entity_1, [U-13C; U-15N], 1 mM; entity_2, [U-13C; U-15N], 1 mM; H2O 90%; D2O 10%
sample_conditions: pH: 6.8; pressure: 1 atm; temperature: 308 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions |
3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions |
3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions |
3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions |
3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions |
3D HNCA | sample_1 | isotropic | sample_conditions |
3D HNCA | sample_2 | isotropic | sample_conditions |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions |
3D HN(CO)CA | sample_2 | isotropic | sample_conditions |
3D HNCO | sample_1 | isotropic | sample_conditions |
3D HNCO | sample_2 | isotropic | sample_conditions |
HCCH-TOCSY | sample_1 | isotropic | sample_conditions |
HCCH-TOCSY | sample_2 | isotropic | sample_conditions |
3D 1H-13C NOESY aliphatic | sample_3 | isotropic | sample_conditions |
3D 1H-13C NOESY aromatic | sample_3 | isotropic | sample_conditions |
Software:
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
X-PLOR_NIH v2.34, Schwieters, Kuszewski, Tjandra and Clore - refinment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
Analysis_CCPN, CCPN - chemical shift assignment
TOPSPIN, Bruker Biospin - processing
NMR spectrometers:
- Bruker Avance 900 MHz
- Bruker Avance 800 MHz
- Bruker Avance 700 MHz
- Bruker Avance 600 MHz
Related Database Links:
UNP | P40565 P46947 |
BMRB | 19766 25047 25443 |
PDB | |
DBJ | GAA24120 |
EMBL | CAA86207 CAY80517 |
GB | AAS56407 AEO21093 AHY76002 AJP39470 AJR36763 |
REF | NP_012270 |
SP | P40565 |
TPG | DAA08551 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts