BMRB Entry 18682
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18682
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Title: LIP5-CHMP5 PubMed: 23105106
Deposition date: 2012-08-29 Original release date: 2012-11-27
Authors: Skalicky, Jack; Sundquist, Wes
Citation: Skalicky, Jack; Arii, Jun; Wenzel, Dawn; Stubblefield, William-May; Katsuyama, Angela; Uter, Nathan; Bajorek, Monika; Myszka, David; Sundquist, Wesley. "Interactions of the human LIP5 regulatory protein with endosomal sorting complexes required for transport." J. Biol. Chem. 287, 43910-43926 (2012).
Assembly members:
LIP5(1-168), polymer, 168 residues, 18833.916 Da.
CHMP5(139-195), polymer, 59 residues, 3797.847 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):
LIP5(1-168): MAALAPLPPLPAQFKSIQHH
LRTAQEHDKRDPVVAYYCRL
YAMQTGMKIDSKTPECRKFL
SKLMDQLEALKKQLGDNEAI
TQEIVGCAHLENYALKMFLY
ADNEDRAGRFHKNMIKSFYT
ASLLIDVITVFGELTDENVK
HRKYARWKATYIHNCLKNGE
TPQAGPVG
CHMP5(139-195): GHMEDANEIQEALSRSYGTP
ELDEDDLEAELDALGDELLA
DEDSSYLDEAASAPAIPEG
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 651 |
15N chemical shifts | 228 |
1H chemical shifts | 1397 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | LIP5(1-168) | 1 |
2 | CHMP5(139-195) | 2 |
Entities:
Entity 1, LIP5(1-168) 168 residues - 18833.916 Da.
1 | MET | ALA | ALA | LEU | ALA | PRO | LEU | PRO | PRO | LEU | ||||
2 | PRO | ALA | GLN | PHE | LYS | SER | ILE | GLN | HIS | HIS | ||||
3 | LEU | ARG | THR | ALA | GLN | GLU | HIS | ASP | LYS | ARG | ||||
4 | ASP | PRO | VAL | VAL | ALA | TYR | TYR | CYS | ARG | LEU | ||||
5 | TYR | ALA | MET | GLN | THR | GLY | MET | LYS | ILE | ASP | ||||
6 | SER | LYS | THR | PRO | GLU | CYS | ARG | LYS | PHE | LEU | ||||
7 | SER | LYS | LEU | MET | ASP | GLN | LEU | GLU | ALA | LEU | ||||
8 | LYS | LYS | GLN | LEU | GLY | ASP | ASN | GLU | ALA | ILE | ||||
9 | THR | GLN | GLU | ILE | VAL | GLY | CYS | ALA | HIS | LEU | ||||
10 | GLU | ASN | TYR | ALA | LEU | LYS | MET | PHE | LEU | TYR | ||||
11 | ALA | ASP | ASN | GLU | ASP | ARG | ALA | GLY | ARG | PHE | ||||
12 | HIS | LYS | ASN | MET | ILE | LYS | SER | PHE | TYR | THR | ||||
13 | ALA | SER | LEU | LEU | ILE | ASP | VAL | ILE | THR | VAL | ||||
14 | PHE | GLY | GLU | LEU | THR | ASP | GLU | ASN | VAL | LYS | ||||
15 | HIS | ARG | LYS | TYR | ALA | ARG | TRP | LYS | ALA | THR | ||||
16 | TYR | ILE | HIS | ASN | CYS | LEU | LYS | ASN | GLY | GLU | ||||
17 | THR | PRO | GLN | ALA | GLY | PRO | VAL | GLY |
Entity 2, CHMP5(139-195) 59 residues - 3797.847 Da.
1 | GLY | HIS | MET | GLU | ASP | ALA | ASN | GLU | ILE | GLN | ||||
2 | GLU | ALA | LEU | SER | ARG | SER | TYR | GLY | THR | PRO | ||||
3 | GLU | LEU | ASP | GLU | ASP | ASP | LEU | GLU | ALA | GLU | ||||
4 | LEU | ASP | ALA | LEU | GLY | ASP | GLU | LEU | LEU | ALA | ||||
5 | ASP | GLU | ASP | SER | SER | TYR | LEU | ASP | GLU | ALA | ||||
6 | ALA | SER | ALA | PRO | ALA | ILE | PRO | GLU | GLY |
Samples:
sample_1: LIP5(1-168), [U-100% 13C; U-100% 15N], 0.5 mM; CHMP5(139-195), [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 25 mM; sodium chloride 50 mM; DTT 0.5 mM; EDTA 0.1 mM; H2O 92%; D2O 8%
sample_conditions_1: ionic strength: 75 mM; pH: 6.3; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HNHA | sample_1 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - data analysis
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian DirectDrive 900 MHz
Related Database Links:
BMRB | 18681 |
PDB | |
DBJ | BAA90909 BAB22228 BAB26150 BAE43171 BAG73861 BAB25962 BAE27642 BAG37842 BAI46888 |
EMBL | CAB66619 CAG33488 CAH92851 CAH90797 |
GB | AAF76210 AAG43125 AAH05937 AAH06989 AAH22536 AAD27743 AAF29140 AAF42917 AAG23821 AAH06947 |
REF | NP_001033134 NP_001126666 NP_001248449 NP_001273300 NP_057569 NP_001020581 NP_001029854 NP_001125453 NP_001231673 NP_001253497 |
SP | Q32L63 Q5R5W5 Q9CR26 Q9NP79 Q4QQV8 Q5RBR3 Q9D7S9 Q9NZZ3 |
TPG | DAA26071 DAA26641 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts