BMRB Entry 11086
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                PDB ID: 
                
                
                Entry in NMR Restraints Grid
                Validation report in NRG-CING
            Chem Shift validation:  AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11086
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Title: Solution structure of the CH domain of human microtubule-associated protein RP/EB family member 3
Deposition date: 2009-12-28 Original release date: 2011-01-04
Authors: Tomizawa, T.; Kigawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.
Citation: Tomizawa, T.; Kigawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution structure of the CH domain of human microtubule-associated protein RP/EB family member 3" . ., .-..
Assembly members:
CH domain, polymer, 159 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: cell free synthesis Host organism: E. coli - cell free
Entity Sequences (FASTA):
CH domain: GSSGSSGMAVNVYSTSVTSE
NLSRHDMLAWVNDSLHLNYT
KIEQLCSGAAYCQFMDMLFP
GCVHLRKVKFQAKLEHEYIH
NFKVLQAAFKKMGVDKIIPV
EKLVKGKFQDNFEFIQWFKK
FFDANYDGKDYNPLLARQGQ
DVAPPPNPGDQIFSGPSSG
- assigned_chemical_shifts
| Data type | Count | 
| 13C chemical shifts | 711 | 
| 15N chemical shifts | 161 | 
| 1H chemical shifts | 1106 | 
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID | 
|---|---|---|
| 1 | CH domain | 1 | 
Entities:
Entity 1, CH domain 159 residues - Formula weight is not available
| 1 | GLY | SER | SER | GLY | SER | SER | GLY | MET | ALA | VAL | ||||
| 2 | ASN | VAL | TYR | SER | THR | SER | VAL | THR | SER | GLU | ||||
| 3 | ASN | LEU | SER | ARG | HIS | ASP | MET | LEU | ALA | TRP | ||||
| 4 | VAL | ASN | ASP | SER | LEU | HIS | LEU | ASN | TYR | THR | ||||
| 5 | LYS | ILE | GLU | GLN | LEU | CYS | SER | GLY | ALA | ALA | ||||
| 6 | TYR | CYS | GLN | PHE | MET | ASP | MET | LEU | PHE | PRO | ||||
| 7 | GLY | CYS | VAL | HIS | LEU | ARG | LYS | VAL | LYS | PHE | ||||
| 8 | GLN | ALA | LYS | LEU | GLU | HIS | GLU | TYR | ILE | HIS | ||||
| 9 | ASN | PHE | LYS | VAL | LEU | GLN | ALA | ALA | PHE | LYS | ||||
| 10 | LYS | MET | GLY | VAL | ASP | LYS | ILE | ILE | PRO | VAL | ||||
| 11 | GLU | LYS | LEU | VAL | LYS | GLY | LYS | PHE | GLN | ASP | ||||
| 12 | ASN | PHE | GLU | PHE | ILE | GLN | TRP | PHE | LYS | LYS | ||||
| 13 | PHE | PHE | ASP | ALA | ASN | TYR | ASP | GLY | LYS | ASP | ||||
| 14 | TYR | ASN | PRO | LEU | LEU | ALA | ARG | GLN | GLY | GLN | ||||
| 15 | ASP | VAL | ALA | PRO | PRO | PRO | ASN | PRO | GLY | ASP | ||||
| 16 | GLN | ILE | PHE | SER | GLY | PRO | SER | SER | GLY | 
Samples:
sample_1: CH domain, [U-100% 13C; U-100% 15N], 1.28 mM; TRIS, [U-100% 2H], 20 mM; sodium chloride 100 mM; DTT, [U-100% 2H], 1 mM; sodium azide 0.02%; D2O 10%; H2O 90%
condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K
Experiments:
| Name | Sample | Sample state | Sample conditions | 
|---|---|---|---|
| 3D 1H-15N-separated NOESY | sample_1 | isotropic | condition_1 | 
| 3D 1H-13C-separated NOESY | sample_1 | isotropic | condition_1 | 
Software:
xwinnmr v2.6, Bruker - collection
NMRPipe v20030801, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B.A. - data analysis
Kujira v0.9295, Kobayashi, N. - data analysis
CYANA v2.0.17, Guntert, P. - structure solution
NMR spectrometers:
- Bruker AVANCE 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAA82958 BAE87811 BAE88276 BAE90157 BAG35263 | 
| EMBL | CAA72060 CAG38760 CAG46643 | 
| GB | AAA96321 AAH11557 AAH57918 AAH83589 AAK07556 | 
| REF | NP_001007657 NP_001271740 NP_001289979 NP_036458 NP_579928 | 
| SP | Q5XIT1 Q6PER3 Q9UPY8 | 
Download simulated HSQC data in one of the following formats:
            
CSV: Backbone
            or all simulated shifts
            
SPARKY: Backbone
            or all simulated shifts
    
