BMRB Entry 34940
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34940
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
Citation: Emmanouilidis, L.; Gaussmann, S.; Sattler, M.. "Humain complexn PEX5 TPR domain with PEX14 KIPSWQIPV peptide" .
Assembly members:
entity_1, polymer, 319 residues, 35246.699 Da.
entity_2, polymer, 9 residues, 1068.287 Da.
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
Entity Sequences (FASTA):
entity_1: DKGYQFEEENPLRDHPQPFE
EGLRRLQEGDLPNAVLLFEA
AVQQDPKHMEAWQYLGTTQA
ENEQELLAISALRRCLELKP
DNQTALMALAVSFTNESLQR
QACEILRDWLRYTPAYAHLV
TPAEEGAGGAGLGPSKRILG
SLLSDSLFLEVKELFLAAVR
LDPTSIDPDVQCGLGVLFNL
SGEYDKAVDCFTAALSVRPN
DYLLWNKLGATLANGNQSEE
AVAAYRRALELQPGYIRSRY
NLGISCINLGAHREAVEHFL
EALNMQRKSRGPRGEGGAMS
ENIWSTLRLALSMLGQSDAY
GAADARDLSTLLTMFGLPQ
entity_2: KIPSWQIPV
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 66 |
| 1H chemical shifts | 150 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
| 2 | unit_2 | 2 |
Entities:
Entity 1, unit_1 319 residues - 35246.699 Da.
| 1 | ASP | LYS | GLY | TYR | GLN | PHE | GLU | GLU | GLU | ASN | ||||
| 2 | PRO | LEU | ARG | ASP | HIS | PRO | GLN | PRO | PHE | GLU | ||||
| 3 | GLU | GLY | LEU | ARG | ARG | LEU | GLN | GLU | GLY | ASP | ||||
| 4 | LEU | PRO | ASN | ALA | VAL | LEU | LEU | PHE | GLU | ALA | ||||
| 5 | ALA | VAL | GLN | GLN | ASP | PRO | LYS | HIS | MET | GLU | ||||
| 6 | ALA | TRP | GLN | TYR | LEU | GLY | THR | THR | GLN | ALA | ||||
| 7 | GLU | ASN | GLU | GLN | GLU | LEU | LEU | ALA | ILE | SER | ||||
| 8 | ALA | LEU | ARG | ARG | CYS | LEU | GLU | LEU | LYS | PRO | ||||
| 9 | ASP | ASN | GLN | THR | ALA | LEU | MET | ALA | LEU | ALA | ||||
| 10 | VAL | SER | PHE | THR | ASN | GLU | SER | LEU | GLN | ARG | ||||
| 11 | GLN | ALA | CYS | GLU | ILE | LEU | ARG | ASP | TRP | LEU | ||||
| 12 | ARG | TYR | THR | PRO | ALA | TYR | ALA | HIS | LEU | VAL | ||||
| 13 | THR | PRO | ALA | GLU | GLU | GLY | ALA | GLY | GLY | ALA | ||||
| 14 | GLY | LEU | GLY | PRO | SER | LYS | ARG | ILE | LEU | GLY | ||||
| 15 | SER | LEU | LEU | SER | ASP | SER | LEU | PHE | LEU | GLU | ||||
| 16 | VAL | LYS | GLU | LEU | PHE | LEU | ALA | ALA | VAL | ARG | ||||
| 17 | LEU | ASP | PRO | THR | SER | ILE | ASP | PRO | ASP | VAL | ||||
| 18 | GLN | CYS | GLY | LEU | GLY | VAL | LEU | PHE | ASN | LEU | ||||
| 19 | SER | GLY | GLU | TYR | ASP | LYS | ALA | VAL | ASP | CYS | ||||
| 20 | PHE | THR | ALA | ALA | LEU | SER | VAL | ARG | PRO | ASN | ||||
| 21 | ASP | TYR | LEU | LEU | TRP | ASN | LYS | LEU | GLY | ALA | ||||
| 22 | THR | LEU | ALA | ASN | GLY | ASN | GLN | SER | GLU | GLU | ||||
| 23 | ALA | VAL | ALA | ALA | TYR | ARG | ARG | ALA | LEU | GLU | ||||
| 24 | LEU | GLN | PRO | GLY | TYR | ILE | ARG | SER | ARG | TYR | ||||
| 25 | ASN | LEU | GLY | ILE | SER | CYS | ILE | ASN | LEU | GLY | ||||
| 26 | ALA | HIS | ARG | GLU | ALA | VAL | GLU | HIS | PHE | LEU | ||||
| 27 | GLU | ALA | LEU | ASN | MET | GLN | ARG | LYS | SER | ARG | ||||
| 28 | GLY | PRO | ARG | GLY | GLU | GLY | GLY | ALA | MET | SER | ||||
| 29 | GLU | ASN | ILE | TRP | SER | THR | LEU | ARG | LEU | ALA | ||||
| 30 | LEU | SER | MET | LEU | GLY | GLN | SER | ASP | ALA | TYR | ||||
| 31 | GLY | ALA | ALA | ASP | ALA | ARG | ASP | LEU | SER | THR | ||||
| 32 | LEU | LEU | THR | MET | PHE | GLY | LEU | PRO | GLN |
Entity 2, unit_2 9 residues - 1068.287 Da.
| 1 | LYS | ILE | PRO | SER | TRP | GLN | ILE | PRO | VAL |
Samples:
sample_1: PEX14 1 mM; KIPSWQI 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM
sample_2: PEX14, [U-100% 13C; U-100% 15N; U-80% 2H], 0.4 mM; KIPSWQI 4 mM; sodium phosphate 20 mM; sodium chloride 50 mM; human PEX5 TPR domain, [U-100% 13C; U-100% 15N; U-80% 2H], 0.4 mM; DTT 1 mM
sample_conditions_1: ionic strength: 83 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 83 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TopSpin v3.6, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRFAM-SPARKY v3, SPARKY - peak picking
CcpNmr Analysis v2.4.2, CCPN - peak picking
NMRFAM-SPARKY, SPARKY - chemical shift assignment
CYANA v3.3, Guntert, Mumenthaler and Wuthrich - structure calculation
HADDOCK v2.4, Bonvin - refinement, structure calculation
NMR spectrometers:
- Bruker AVANCE III 900 MHz
- Bruker AVANCE III 500 MHz