mRojoA. Determined by X-ray diffraction at 1.7 Å resolution. Released 13 Oct 2010.
Explore 3NEZ in 3D Show helices and sheets RCSB PDB PDBe
3NEZ contains 31 α-helices and 53 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-22 | 11 | 1 |
| β-strand | 25-36 | 12 | 1 |
| β-strand | 41-50 | 10 | 1 |
| α-helix | 52 | 1 | |
| α-helix | 54 | 1 | |
| α-helix | 58-60 | 3 | |
| α-helix | 62-64 | 3 | |
| β-strand | 74 | 1 | 1 |
| α-helix | 82-85 | 4 | |
| β-strand | 91-99 | 9 | 1 |
| β-strand | 104-114 | 11 | 1 |
| β-strand | 117-127 | 11 | 1 |
| β-strand | 140-143 | 4 | 1 |
| α-helix | 144-145 | 2 | |
| β-strand | 146-153 | 8 | 1 |
| β-strand | 156-167 | 12 | 1 |
| β-strand | 172-183 | 12 | 1 |
| α-helix | 188-190 | 3 | |
| β-strand | 192 | 1 | 2 |
| β-strand | 193-204 | 12 | 1 |
| β-strand | 210-220 | 11 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-22 | 11 | 3 |
| β-strand | 25-36 | 12 | 3 |
| β-strand | 41-50 | 10 | 3 |
| α-helix | 52 | 1 | |
| α-helix | 54 | 1 | |
| α-helix | 58-60 | 3 | |
| α-helix | 62-64 | 3 | |
| α-helix | 70-72 | 3 | |
| β-strand | 74 | 1 | 3 |
| α-helix | 82-85 | 4 | |
| β-strand | 91-99 | 9 | 3 |
| β-strand | 104-114 | 11 | 3 |
| β-strand | 117-127 | 11 | 3 |
| β-strand | 143 | 1 | 3 |
| α-helix | 144-145 | 2 | |
| β-strand | 146-153 | 8 | 3 |
| β-strand | 156-166 | 11 | 3 |
| α-helix | 168-170 | 3 | |
| β-strand | 172-183 | 12 | 3 |
| α-helix | 188-190 | 3 | |
| β-strand | 193-204 | 12 | 3 |
| β-strand | 210-220 | 11 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-22 | 11 | 4 |
| β-strand | 25-36 | 12 | 4 |
| β-strand | 41-50 | 10 | 4 |
| α-helix | 52 | 1 | |
| α-helix | 54 | 1 | |
| α-helix | 58-60 | 3 | |
| α-helix | 62-64 | 3 | |
| α-helix | 70-72 | 3 | |
| β-strand | 74 | 1 | 4 |
| α-helix | 82-85 | 4 | |
| β-strand | 91-99 | 9 | 4 |
| β-strand | 104-114 | 11 | 4 |
| β-strand | 117-127 | 11 | 4 |
| β-strand | 140-143 | 4 | 4 |
| α-helix | 144-145 | 2 | |
| β-strand | 146-153 | 8 | 4 |
| β-strand | 156-167 | 12 | 4 |
| β-strand | 172-183 | 12 | 4 |
| α-helix | 188-192 | 5 | |
| β-strand | 193-204 | 12 | 4 |
| β-strand | 210-220 | 11 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-22 | 11 | 2 |
| β-strand | 25-36 | 12 | 2 |
| β-strand | 41-50 | 10 | 2 |
| α-helix | 52 | 1 | |
| α-helix | 54 | 1 | |
| α-helix | 58-60 | 3 | |
| α-helix | 62-64 | 3 | |
| β-strand | 74 | 1 | 2 |
| α-helix | 82-85 | 4 | |
| β-strand | 91-99 | 9 | 2 |
| β-strand | 104-114 | 11 | 2 |
| β-strand | 117-127 | 11 | 2 |
| β-strand | 140-143 | 4 | 2 |
| α-helix | 144-145 | 2 | |
| β-strand | 146-153 | 8 | 2 |
| β-strand | 156-167 | 12 | 2 |
| β-strand | 172-183 | 12 | 2 |
| α-helix | 188-190 | 3 | |
| β-strand | 193-204 | 12 | 2 |
| β-strand | 210-220 | 11 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| mRojoA | A, B, C, D | protein | 242 | Discosoma Sp. | D1MPT3 (AlphaFold model) |
>3NEZ_1 mRojoA (chains A, B, C, D) MGHHHHHHGVSKGEEDNMAIIKEFMRFKTHMEGSVNGHEFEIEGEGEGRPYEGTQTAKLK VTKGGPLPFAWDILSPQFXSKAYVKHPADIPDYLKLSFPEGFKWERVMNFEDGGVVTVTQ DSSLQDGEFIYKVKLHGTNFPSDGPVMQKKTMGWEASSERMYPEDGALKGEIKLRLKLKD GGHYDAEVKTTYKAKKPVQLPGAYNANYKLDITSHNEDYTIVEQYERCEGRHSTGGMDEL YK
Generation of longer emission wavelength red fluorescent proteins using computationally designed libraries. Chica, R.A., Moore, M.M., Allen, B.D. et al. Proc Natl Acad Sci U S A (2010) 107:20257-20262. DOI 10.1073/pnas.1013910107 · PubMed
Other PDB entries of the same protein (UniProt D1MPT3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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