BMRB Entry 18595
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR18595
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Title: Solid-state NMR 13C and 15N resonance assignments of a seven-transmembrane helical protein Anabaena Sensory Rhodopsin PubMed: 22983928
Deposition date: 2012-07-16 Original release date: 2012-08-29
Authors: Wang, Shenlin; Shi, Lichi; Brown, Leonid; Ladizhansky, Vladimir
Citation: Wang, Shenlin; Shi, Lichi; Okitsu, Takashi; Wada, Akimori; Brown, Leonid; Ladizhansky, Vladimir. "Solid-state NMR 13C and 15N resonance assignments of a seven-transmembrane helical protein Anabaena Sensory Rhodopsin" Biomol. NMR Assign. 7, 253-256 (2013).
Assembly members:
ASR, polymer, 235 residues, Formula weight is not available
Natural source: Common Name: Cyanobacteria Taxonomy ID: 1172 Superkingdom: Bacteria Kingdom: not available Genus/species: Anabaena variabilis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
ASR: MNLESLLHWIYVAGMTIGAL
HFWSLSRNPRGVPQYEYLVA
MFIPIWSGLAYMAMAIDQGK
VEAAGQIAHYARYIDWMVTT
PLLLLSLSWTAMQFIKKDWT
LIGFLMSTQIVVITSGLIAD
LSERDWVRYLWYICGVCAFL
IILWGIWNPLRAKTRTQSSE
LANLYDKLVTYFTVLWIGYP
IVWIIGPSGFGWINQTIDTF
LFCLLPFFSKVGFSFLDLHG
LRNLNDSRQHHHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 963 |
15N chemical shifts | 223 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Anabeana sensory rhodopsin | 1 |
Entities:
Entity 1, Anabeana sensory rhodopsin 235 residues - Formula weight is not available
6X his-tagged C-terminal truncated at position 229 Anabeana sensory rhodospin
1 | MET | ASN | LEU | GLU | SER | LEU | LEU | HIS | TRP | ILE | ||||
2 | TYR | VAL | ALA | GLY | MET | THR | ILE | GLY | ALA | LEU | ||||
3 | HIS | PHE | TRP | SER | LEU | SER | ARG | ASN | PRO | ARG | ||||
4 | GLY | VAL | PRO | GLN | TYR | GLU | TYR | LEU | VAL | ALA | ||||
5 | MET | PHE | ILE | PRO | ILE | TRP | SER | GLY | LEU | ALA | ||||
6 | TYR | MET | ALA | MET | ALA | ILE | ASP | GLN | GLY | LYS | ||||
7 | VAL | GLU | ALA | ALA | GLY | GLN | ILE | ALA | HIS | TYR | ||||
8 | ALA | ARG | TYR | ILE | ASP | TRP | MET | VAL | THR | THR | ||||
9 | PRO | LEU | LEU | LEU | LEU | SER | LEU | SER | TRP | THR | ||||
10 | ALA | MET | GLN | PHE | ILE | LYS | LYS | ASP | TRP | THR | ||||
11 | LEU | ILE | GLY | PHE | LEU | MET | SER | THR | GLN | ILE | ||||
12 | VAL | VAL | ILE | THR | SER | GLY | LEU | ILE | ALA | ASP | ||||
13 | LEU | SER | GLU | ARG | ASP | TRP | VAL | ARG | TYR | LEU | ||||
14 | TRP | TYR | ILE | CYS | GLY | VAL | CYS | ALA | PHE | LEU | ||||
15 | ILE | ILE | LEU | TRP | GLY | ILE | TRP | ASN | PRO | LEU | ||||
16 | ARG | ALA | LYS | THR | ARG | THR | GLN | SER | SER | GLU | ||||
17 | LEU | ALA | ASN | LEU | TYR | ASP | LYS | LEU | VAL | THR | ||||
18 | TYR | PHE | THR | VAL | LEU | TRP | ILE | GLY | TYR | PRO | ||||
19 | ILE | VAL | TRP | ILE | ILE | GLY | PRO | SER | GLY | PHE | ||||
20 | GLY | TRP | ILE | ASN | GLN | THR | ILE | ASP | THR | PHE | ||||
21 | LEU | PHE | CYS | LEU | LEU | PRO | PHE | PHE | SER | LYS | ||||
22 | VAL | GLY | PHE | SER | PHE | LEU | ASP | LEU | HIS | GLY | ||||
23 | LEU | ARG | ASN | LEU | ASN | ASP | SER | ARG | GLN | HIS | ||||
24 | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: ASR, [U-100% 13C; U-100% 15N], w/w; DMPC, [U-100% 13C; U-100% 15N], w/w; DMPA, [U-100% 13C; U-100% 15N], w/w
sample_2: ASR, alternately labeled by 2-13C glycerol and U- 15N, w/w; DMPC, [U-100% 13C; U-100% 15N], w/w; DMPA, [U-100% 13C; U-100% 15N], w/w
sample_3: ASR, 1,3-C13-glycerol labeled and U-N15 labeled, w/w; DMPC, [U-100% 13C; U-100% 15N], w/w; DMPA, [U-100% 13C; U-100% 15N], w/w
sample_conditions_1: pH: 9.0; pressure: 1 atm; temperature: 278 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D NCA | sample_1 | solid | sample_conditions_1 |
2D NCO | sample_1 | solid | sample_conditions_1 |
3D CONCA | sample_1 | solid | sample_conditions_1 |
3D NCACX | sample_1 | solid | sample_conditions_1 |
3D NCOCX | sample_1 | solid | sample_conditions_1 |
2D CC (DARR) | sample_1 | solid | sample_conditions_1 |
2D NCA | sample_2 | solid | sample_conditions_1 |
2D NCO | sample_2 | solid | sample_conditions_1 |
3D NCACX | sample_2 | solid | sample_conditions_1 |
3D NCOCX | sample_2 | solid | sample_conditions_1 |
2D CC (DARR) | sample_2 | solid | sample_conditions_1 |
2D NCA | sample_3 | solid | sample_conditions_1 |
2D NCO | sample_3 | solid | sample_conditions_1 |
3D NCACX | sample_3 | solid | sample_conditions_1 |
3D NCOCX | sample_3 | solid | sample_conditions_1 |
2D CC (DARR) | sample_3 | solid | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Zhengrong and Bax - processing
CARA, Keller and Wuthrich - chemical shift assignment, data analysis
NMR spectrometers:
- Bruker Avance 800 MHz