BMRB Entry 25443
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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/BMR25443
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Title: Snu17p-Pml1p 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.
Pml1p, polymer, 23 residues, 2514.800 Da.
Natural source: Common Name: Baker's yeast Taxonomy ID: 559292 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
Pml1p: GSKSQYIDIMPDFSPSGLLE
LES
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 572 |
| 15N chemical shifts | 135 |
| 1H chemical shifts | 930 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Snu17p | 1 |
| 2 | Pml1p | 2 |
Entities:
Entity 1, Snu17p 118 residues - 13496.103 Da.
| 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, Pml1p 23 residues - 2514.800 Da.
| 1 | GLY | SER | LYS | SER | GLN | TYR | ILE | ASP | ILE | MET | ||||
| 2 | PRO | ASP | PHE | SER | PRO | SER | GLY | LEU | LEU | GLU | ||||
| 3 | LEU | GLU | SER |
Samples:
Snu17p_13C15N: sodium phosphate 25 mM; sodium chloride 250 mM; Snu17p, [U-13C; U-15N], 0.8 – 1 mM; Pml1p_Fmoc1.2 – 1.5 mM; sodium azide 1 mM; D2O 10%; H2O 90%
Pml1p_13C15N: sodium phosphate 25 mM; sodium chloride 250 mM; Snu17p1 – 1.2 mM; Pml1p, [U-13C; U-15N], 0.8 – 1 mM; sodium azide 1 mM; D2O 10%; H2O 90%
Standard_conditions: pH: 6.8; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | Snu17p_13C15N | isotropic | Standard_conditions |
| 2D 1H-15N HSQC | Pml1p_13C15N | isotropic | Standard_conditions |
| 2D 1H-15N HSQC | Snu17p_13C15N | isotropic | Standard_conditions |
| 2D 1H-15N HSQC | Pml1p_13C15N | isotropic | Standard_conditions |
| 2D 1H-15N HSQC | Snu17p_13C15N | isotropic | Standard_conditions |
| 2D 1H-15N HSQC | Pml1p_13C15N | isotropic | Standard_conditions |
| 2D 1H-15N HSQC | Snu17p_13C15N | isotropic | Standard_conditions |
| 2D 1H-15N HSQC | Pml1p_13C15N | isotropic | Standard_conditions |
| 2D 1H-13C HSQC aliphatic | Snu17p_13C15N | isotropic | Standard_conditions |
| 3D 1H-13C NOESY aromatic | Snu17p_13C15N | isotropic | Standard_conditions |
| 3D 1H-13C NOESY aromatic | Pml1p_13C15N | isotropic | Standard_conditions |
| 3D 1H-13C NOESY aliphatic | Pml1p_13C15N | isotropic | Standard_conditions |
| 3D HNCO | Snu17p_13C15N | isotropic | Standard_conditions |
| 3D HNCA | Snu17p_13C15N | isotropic | Standard_conditions |
| 3D HNCA | Pml1p_13C15N | isotropic | Standard_conditions |
| 3D HN(CO)CA | Snu17p_13C15N | isotropic | Standard_conditions |
| 3D HN(CO)CA | Pml1p_13C15N | isotropic | Standard_conditions |
| 3D HCCH-TOCSY | Snu17p_13C15N | isotropic | Standard_conditions |
| 3D 1H-15N NOESY | Snu17p_13C15N | isotropic | Standard_conditions |
| 3D 1H-15N NOESY | Pml1p_13C15N | isotropic | Standard_conditions |
| HBCBCGCDHD | Snu17p_13C15N | isotropic | Standard_conditions |
Software:
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
X-PLOR_NIH v2.34, Schwieters, Kuszewski, Tjandra and Clore - H2O 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:
| BMRB | 19766 25047 25442 |
| 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