BMRB Entry 18895
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18895
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Title: Backbone and partial sidechain assignment of the microtubule binding domain of the MAP1B light chain PubMed: 23339032
Deposition date: 2012-12-13 Original release date: 2013-01-29
Authors: Orban-Nemeth, Zsuzsanna; Propst, Friedrich; Henen, Morkos; Konrat, Robert; Kozminski, Wiktor; Zerko, Szymon; Saxena, Saurabh; Stanek, Jan; Geist, Leonhard
Citation: Orban-Nemeth, Zsuzsanna; Henen, Morkos; Geist, Leonhard; Zerko, Szymon; Saxena, Saurabh; Stanek, Jan; Komiski, Wiktor; Propst, Friedrich; Konrat, Robert. "Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain." Biomol. NMR Assignments ., .-. (2013).
Assembly members:
MAP1B, polymer, 150 residues, Formula weight is not available
Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
MAP1B: MGSSHHHHHHSSGLVPRGSH
MEFMVDPEALAIEQNLGKAL
KKDLKEKAKTKKPGTKTKSS
SPVKKGDGKSKPSAASPKPG
ALKESSDKVSRVASPKKKES
VEKAMKTTTTPEVKATRGEE
KDKETKNAANASASKSVKTA
TAGPGTTKTA
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 489 |
15N chemical shifts | 124 |
1H chemical shifts | 757 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | N-terminal MAP1B LC | 1 |
Entities:
Entity 1, N-terminal MAP1B LC 150 residues - Formula weight is not available
1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | |
2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | |
3 | MET | GLU | PHE | MET | VAL | ASP | PRO | GLU | ALA | LEU | |
4 | ALA | ILE | GLU | GLN | ASN | LEU | GLY | LYS | ALA | LEU | |
5 | LYS | LYS | ASP | LEU | LYS | GLU | LYS | ALA | LYS | THR | |
6 | LYS | LYS | PRO | GLY | THR | LYS | THR | LYS | SER | SER | |
7 | SER | PRO | VAL | LYS | LYS | GLY | ASP | GLY | LYS | SER | |
8 | LYS | PRO | SER | ALA | ALA | SER | PRO | LYS | PRO | GLY | |
9 | ALA | LEU | LYS | GLU | SER | SER | ASP | LYS | VAL | SER | |
10 | ARG | VAL | ALA | SER | PRO | LYS | LYS | LYS | GLU | SER | |
11 | VAL | GLU | LYS | ALA | MET | LYS | THR | THR | THR | THR | |
12 | PRO | GLU | VAL | LYS | ALA | THR | ARG | GLY | GLU | GLU | |
13 | LYS | ASP | LYS | GLU | THR | LYS | ASN | ALA | ALA | ASN | |
14 | ALA | SER | ALA | SER | LYS | SER | VAL | LYS | THR | ALA | |
15 | THR | ALA | GLY | PRO | GLY | THR | THR | LYS | THR | ALA |
Samples:
sample_1: MAP1B, [U-95% 13C; U-90% 15N], 0.6 1 mM; D2O, [U-100% 2H], 10%; sodium chloride 300 mM; sodium phosphate 50 mM
sample_conditions_1: pH: 5; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
5D HN(CA)CONH | sample_1 | isotropic | sample_conditions_1 |
5D (HACA)CON(CA)CONH | sample_1 | isotropic | sample_conditions_1 |
5D (H)NCO(NCA)CONH | sample_1 | isotropic | sample_conditions_1 |
4D HNCACO | sample_1 | isotropic | sample_conditions_1 |
5D HabCabCONH | sample_1 | isotropic | sample_conditions_1 |
5D H(CC-tocsy)CONH | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - data analysis
MFT, Wiktor Kozminski - processing
TSAR, Kozminski, Zawadzka, Kazimiurcuk - chemical shift assignment
NMR spectrometers:
- Agilent Direct Drive 700 MHz
Related Database Links:
RefSeq | NP_062090.1 |
EMBL | CAA34620 CAC16162 |
GB | EDM10176 |
PIR | S06017 |
REF | NP_062090 XP_008758883 |
SP | P15205 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts