BMRB Entry 50015
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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/BMR50015
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Title: Assignment of Titin domain I83 PubMed: 33811919
Deposition date: 2019-09-12 Original release date: 2021-04-11
Authors: Pfuhl, Mark
Citation: Kelly, Colleen; Pace, Nicola; Gage, Matthew; Pfuhl, Mark. "Solution NMR structure of titin N2A region Ig domain I83 and its interaction with metal ions" J. Mol. Biol. 433, 166977-166977 (2021).
Assembly members:
Titin, polymer, 106 residues, 11900 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 Vector: pET151/D-TOPO
Entity Sequences (FASTA):
Titin: GIDPFTAEPIQFTKRIQNIV
VSEHQSATFECEVSFDDAIV
TWYKGPTELTESQKYNFRND
GRCHYMTIHNVTPDDEGVYS
VIARLEPRGEARSTAELKGE
LRSGC*
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 452 |
15N chemical shifts | 107 |
1H chemical shifts | 711 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | I83 | 1 |
Entities:
Entity 1, I83 106 residues - 11900 Da.
1 | GLY | ILE | ASP | PRO | PHE | THR | ALA | GLU | PRO | ILE | ||||
2 | GLN | PHE | THR | LYS | ARG | ILE | GLN | ASN | ILE | VAL | ||||
3 | VAL | SER | GLU | HIS | GLN | SER | ALA | THR | PHE | GLU | ||||
4 | CYS | GLU | VAL | SER | PHE | ASP | ASP | ALA | ILE | VAL | ||||
5 | THR | TRP | TYR | LYS | GLY | PRO | THR | GLU | LEU | THR | ||||
6 | GLU | SER | GLN | LYS | TYR | ASN | PHE | ARG | ASN | ASP | ||||
7 | GLY | ARG | CYS | HIS | TYR | MET | THR | ILE | HIS | ASN | ||||
8 | VAL | THR | PRO | ASP | ASP | GLU | GLY | VAL | TYR | SER | ||||
9 | VAL | ILE | ALA | ARG | LEU | GLU | PRO | ARG | GLY | GLU | ||||
10 | ALA | ARG | SER | THR | ALA | GLU | LEU | LYS | GLY | GLU | ||||
11 | LEU | ARG | SER | GLY | CYS | X |
Samples:
sample_1: I83, [U-98% 15N], 0.6 mM
sample_2: I83, [U-95% 13C; U-95% 15N], 0.8 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 7.20; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | sample_2 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aromatic | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v4.0.6, Bruker Biospin - collection, processing
CcpNMR v2.4, CCPN - data analysis, peak picking
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 800 MHz
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts