BMRB Entry 34872
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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/BMR34872
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Title: Magic-angle spinning NMR Structure of Opa60 in Lipid Bilayers PubMed: 39010882
Deposition date: 2023-10-19 Original release date: 2024-07-17
Authors: Forster, M.; Andreas, L.
Citation: Forster, M.; Movellan, K.; Najbauer, E.; Becker, S.; Andreas, L.. "Magic-angle spinning NMR structure of Opa60 in lipid bilayers" J. Struct. Biol. X ., .-. (2024).
Assembly members:
entity_1, polymer, 252 residues, 28772.986 Da.
Natural source: Common Name: Neisseria gonorrhoeae Taxonomy ID: 485 Superkingdom: Bacteria Kingdom: not available Genus/species: Neisseria gonorrhoeae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
entity_1: MASEDGGRGPYVQADLAYAY
EHITHDYPEPTAPNKNKIST
VSDYFRNIRTRSVHPRVSVG
YDFGGWRIAADYARYRKWNN
NKYSVNIENVRIRKENGIRI
DRKTENQENGTFHAVSSLGL
SAIYDFQINDKFKPYIGARV
AYGHVRHSIDSTKKTIEVTT
VPSNAPNGAVTTYNTDPKTQ
NDYQSNSIRRVGLGVIAGVG
FDITPKLTLDAGYRYHNWGR
LENTRFKTHEASLGVRYRFK
LAAALEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 238 |
| 15N chemical shifts | 84 |
| 1H chemical shifts | 83 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 252 residues - 28772.986 Da.
| 1 | MET | ALA | SER | GLU | ASP | GLY | GLY | ARG | GLY | PRO | ||||
| 2 | TYR | VAL | GLN | ALA | ASP | LEU | ALA | TYR | ALA | TYR | ||||
| 3 | GLU | HIS | ILE | THR | HIS | ASP | TYR | PRO | GLU | PRO | ||||
| 4 | THR | ALA | PRO | ASN | LYS | ASN | LYS | ILE | SER | THR | ||||
| 5 | VAL | SER | ASP | TYR | PHE | ARG | ASN | ILE | ARG | THR | ||||
| 6 | ARG | SER | VAL | HIS | PRO | ARG | VAL | SER | VAL | GLY | ||||
| 7 | TYR | ASP | PHE | GLY | GLY | TRP | ARG | ILE | ALA | ALA | ||||
| 8 | ASP | TYR | ALA | ARG | TYR | ARG | LYS | TRP | ASN | ASN | ||||
| 9 | ASN | LYS | TYR | SER | VAL | ASN | ILE | GLU | ASN | VAL | ||||
| 10 | ARG | ILE | ARG | LYS | GLU | ASN | GLY | ILE | ARG | ILE | ||||
| 11 | ASP | ARG | LYS | THR | GLU | ASN | GLN | GLU | ASN | GLY | ||||
| 12 | THR | PHE | HIS | ALA | VAL | SER | SER | LEU | GLY | LEU | ||||
| 13 | SER | ALA | ILE | TYR | ASP | PHE | GLN | ILE | ASN | ASP | ||||
| 14 | LYS | PHE | LYS | PRO | TYR | ILE | GLY | ALA | ARG | VAL | ||||
| 15 | ALA | TYR | GLY | HIS | VAL | ARG | HIS | SER | ILE | ASP | ||||
| 16 | SER | THR | LYS | LYS | THR | ILE | GLU | VAL | THR | THR | ||||
| 17 | VAL | PRO | SER | ASN | ALA | PRO | ASN | GLY | ALA | VAL | ||||
| 18 | THR | THR | TYR | ASN | THR | ASP | PRO | LYS | THR | GLN | ||||
| 19 | ASN | ASP | TYR | GLN | SER | ASN | SER | ILE | ARG | ARG | ||||
| 20 | VAL | GLY | LEU | GLY | VAL | ILE | ALA | GLY | VAL | GLY | ||||
| 21 | PHE | ASP | ILE | THR | PRO | LYS | LEU | THR | LEU | ASP | ||||
| 22 | ALA | GLY | TYR | ARG | TYR | HIS | ASN | TRP | GLY | ARG | ||||
| 23 | LEU | GLU | ASN | THR | ARG | PHE | LYS | THR | HIS | GLU | ||||
| 24 | ALA | SER | LEU | GLY | VAL | ARG | TYR | ARG | PHE | LYS | ||||
| 25 | LEU | ALA | ALA | ALA | LEU | GLU | HIS | HIS | HIS | HIS | ||||
| 26 | HIS | HIS |
Samples:
sample_1: sodium phosphate 20 mM; sodium chloride 100 mM; magnesium chloride 20 mM; dimyristoyl-sn-glycero-3-phosphocholine 33 % w/w; protein, [U-99% 13C; U-99% 15N; U-98% 2H], 67 % w/w
sample_2: sodium phosphate 20 mM; sodium chloride 100 mM; magnesium chloride 20 mM; dimyristoyl-sn-glycero-3-phosphocholine, Acyl chain deuterated (d54), 33 % w/w; protein, [U-99% 13C; U-99% 15N; U-98% 2H], 67 % w/w
sample_conditions_1: ionic strength: 140 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| (H)CANH | sample_1 | isotropic | sample_conditions_1 |
| (H)(CO)CA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| (H)(CA)CB(CA)NH | sample_1 | isotropic | sample_conditions_1 |
| (H)(CA)CB(CA)(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| (H)CONH | sample_1 | isotropic | sample_conditions_1 |
| (H)CO(CA)NH | sample_1 | isotropic | sample_conditions_1 |
| (H)N(CA)(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| HN(H)(H)NH | sample_1 | isotropic | sample_conditions_1 |
| (H)CANH | sample_2 | isotropic | sample_conditions_1 |
| (H)NCAHA | sample_2 | isotropic | sample_conditions_1 |
| HC(H)(H)CH | sample_2 | isotropic | sample_conditions_1 |
| (H)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure calculation
NMRFAM-SPARKY, Lee W, Tonelli M, Markley JL - data analysis, peak picking
NMR spectrometers:
- Bruker AVANCE III HD 800 MHz
- Bruker AVANCE III HD 600 MHz
- Bruker AVANCE III HD 950 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts