Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19868
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NMR-STAR v3 text file.
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Citation: De Biasio, Alfredo; Ibanez de Opakua, Alain; Mortuza, Gulnehar B; Molina, Rafael; Cordeiro, Tiago N; Castillo, Francisco; Villate, Maider; Merino, Nekane; Delgado, Sandra; Gil, David; Diercks, Tammo; Luque, Irene; Bernado, Pau; Montoya, Guillermo; Blanco, Francisco J. "Structure of p15(PAF)-PCNA complex and implications for clamp sliding during DNA replication and repair" Nat. Commun. 6, 6439-6439 (2015).
PubMed: 25762514
Assembly members:
p15(PAF), polymer, 111 residues, Formula weight is not available
PCNA_trimer, polymer, 264 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet11d
Entity Sequences (FASTA):
p15(PAF): MVRTKADSVPGTYRKVVAAR
APRKVLGSSTSATNSTSVSS
RKAENKYAGGNPVCVRPTPK
WQKGIGEFFRLSPKDSEKEN
QIPEEAGSSGLGKAKRKACP
LQPDHTNDEKE
PCNA_trimer: GPHMFEARLVQGSILKKVLE
ALKDLINEACWDISSSGVNL
QSMDSSHVSLVQLTLRSEGF
DTYRCDRNLAMGVNLTSMSK
ILKCAGNEDIITLRAEDNAD
TLALVFEAPNQEKVSDYEMK
LMDLDVEQLGIPEQEYSCVV
KMPSGEFARICRDLSHIGDA
VVISCAKDGVKFSASGELGN
GNIKLSQTSNVDKEEEAVTI
EMNEPVQLTFALRYLNFFTK
ATPLSSTVTLSMSADVPLVV
EYKIADMGHLKYYLAPKIED
EEGS
Data type | Count |
13C chemical shifts | 232 |
15N chemical shifts | 78 |
1H chemical shifts | 78 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | p15(PAF) | 1 |
2 | PCNA trimer, 1 | 2 |
3 | PCNA trimer, 2 | 2 |
4 | PCNA trimer, 3 | 2 |
Entity 1, p15(PAF) 111 residues - Formula weight is not available
1 | MET | VAL | ARG | THR | LYS | ALA | ASP | SER | VAL | PRO | ||||
2 | GLY | THR | TYR | ARG | LYS | VAL | VAL | ALA | ALA | ARG | ||||
3 | ALA | PRO | ARG | LYS | VAL | LEU | GLY | SER | SER | THR | ||||
4 | SER | ALA | THR | ASN | SER | THR | SER | VAL | SER | SER | ||||
5 | ARG | LYS | ALA | GLU | ASN | LYS | TYR | ALA | GLY | GLY | ||||
6 | ASN | PRO | VAL | CYS | VAL | ARG | PRO | THR | PRO | LYS | ||||
7 | TRP | GLN | LYS | GLY | ILE | GLY | GLU | PHE | PHE | ARG | ||||
8 | LEU | SER | PRO | LYS | ASP | SER | GLU | LYS | GLU | ASN | ||||
9 | GLN | ILE | PRO | GLU | GLU | ALA | GLY | SER | SER | GLY | ||||
10 | LEU | GLY | LYS | ALA | LYS | ARG | LYS | ALA | CYS | PRO | ||||
11 | LEU | GLN | PRO | ASP | HIS | THR | ASN | ASP | GLU | LYS | ||||
12 | GLU |
Entity 2, PCNA trimer, 1 264 residues - Formula weight is not available
1 | GLY | PRO | HIS | MET | PHE | GLU | ALA | ARG | LEU | VAL | ||||
2 | GLN | GLY | SER | ILE | LEU | LYS | LYS | VAL | LEU | GLU | ||||
3 | ALA | LEU | LYS | ASP | LEU | ILE | ASN | GLU | ALA | CYS | ||||
4 | TRP | ASP | ILE | SER | SER | SER | GLY | VAL | ASN | LEU | ||||
5 | GLN | SER | MET | ASP | SER | SER | HIS | VAL | SER | LEU | ||||
6 | VAL | GLN | LEU | THR | LEU | ARG | SER | GLU | GLY | PHE | ||||
7 | ASP | THR | TYR | ARG | CYS | ASP | ARG | ASN | LEU | ALA | ||||
8 | MET | GLY | VAL | ASN | LEU | THR | SER | MET | SER | LYS | ||||
9 | ILE | LEU | LYS | CYS | ALA | GLY | ASN | GLU | ASP | ILE | ||||
10 | ILE | THR | LEU | ARG | ALA | GLU | ASP | ASN | ALA | ASP | ||||
11 | THR | LEU | ALA | LEU | VAL | PHE | GLU | ALA | PRO | ASN | ||||
12 | GLN | GLU | LYS | VAL | SER | ASP | TYR | GLU | MET | LYS | ||||
13 | LEU | MET | ASP | LEU | ASP | VAL | GLU | GLN | LEU | GLY | ||||
14 | ILE | PRO | GLU | GLN | GLU | TYR | SER | CYS | VAL | VAL | ||||
15 | LYS | MET | PRO | SER | GLY | GLU | PHE | ALA | ARG | ILE | ||||
16 | CYS | ARG | ASP | LEU | SER | HIS | ILE | GLY | ASP | ALA | ||||
17 | VAL | VAL | ILE | SER | CYS | ALA | LYS | ASP | GLY | VAL | ||||
18 | LYS | PHE | SER | ALA | SER | GLY | GLU | LEU | GLY | ASN | ||||
19 | GLY | ASN | ILE | LYS | LEU | SER | GLN | THR | SER | ASN | ||||
20 | VAL | ASP | LYS | GLU | GLU | GLU | ALA | VAL | THR | ILE | ||||
21 | GLU | MET | ASN | GLU | PRO | VAL | GLN | LEU | THR | PHE | ||||
22 | ALA | LEU | ARG | TYR | LEU | ASN | PHE | PHE | THR | LYS | ||||
23 | ALA | THR | PRO | LEU | SER | SER | THR | VAL | THR | LEU | ||||
24 | SER | MET | SER | ALA | ASP | VAL | PRO | LEU | VAL | VAL | ||||
25 | GLU | TYR | LYS | ILE | ALA | ASP | MET | GLY | HIS | LEU | ||||
26 | LYS | TYR | TYR | LEU | ALA | PRO | LYS | ILE | GLU | ASP | ||||
27 | GLU | GLU | GLY | SER |
sample_1: p15(PAF), [U-100% 13C; U-100% 15N], 400 uM; PCNA trimer, [U-100% 2H], 1.1 mM; DTT 2 mM; sodium azide 0.01 % w/v; sodium chloride 137 mM; potassium chloride 2.7 mM; sodium phosphate 10 mM; potassium phosphate 2 mM
sample_2: p15(PAF), [U-100% 13C; U-100% 15N], 150 uM; PCNA trimer, [U-100% 2H], 750 mM; DTT 2 mM; sodium azide 0.01 % w/v; sodium chloride 137 mM; potassium chloride 2.7 mM; sodium phosphate 10 mM; potassium phosphate 2 mM
sample_conditions_1: ionic strength: 0.150 M; pH: 7.0; pressure: 1 atm; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
3D HNCA | sample_2 | isotropic | sample_conditions_1 |
3D HN(CO)CACB | sample_2 | isotropic | sample_conditions_1 |
TOPSPIN, Bruker Biospin - collection, processing
SPARKY, Goddard - chemical shift assignment
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks