Table 1 Methyl resonance assignment statistics
From: Automatic structure-based NMR methyl resonance assignment in large proteins
EIN | ATCase | MBP | MSG | α7α7 | |
|---|---|---|---|---|---|
Protein properties: | |||||
Residues per monomer | 259 | 153 | 370 | 731 | 233 |
Multimeric state | monomer | dimer | monomer | monomer | 14-mer |
Molecular mass of multimer (kDa) | 28.3 | 34.2 | 40.6 | 81.4 | 358.4 |
Experimental NMR data: | |||||
Labeled amino acids | AILV | ILV | ILV | ILV | ILV |
NOESY dimensions | HCCH | CCH | HCCH | HCCH | CCH |
Labeled methyl 1H-13C groups: | |||||
All | 146 | 66 | 123 | 276 | 97 |
With reference assignment | 133 | 62 | 123 | 268 | 93 |
With NOESY peaks | 116 | 54 | 118 | 236 | 88 |
Methyl resonances confidently assigned by MethylFLYA: | |||||
Alla | 101 | 45 | 86 | 176 | 80 |
Correct | 90 | 35 | 83 | 173 | 78 |
Erroneous | 0 | 4 | 2 | 0 | 0 |
Assigned by MethylFLYA using unfiltered peak lists: | |||||
Alla | 107 | 42 | 89 | 183 | 82 |
Correct | 98 | 35 | 87 | 174 | 80 |
Erroneous | 0 | 3 | 2 | 3 | 0 |
Assigned by MethylFLYA using a single distance cutoff: | |||||
Alla | 118 | 44 | 96 | 194 | 84 |
Correct | 101 | 35 | 85 | 176 | 80 |
Erroneous | 4 | 3 | 8 | 8 | 1 |
Methyl resonances assigned by MAGMA:32 | |||||
Correct | 56 | 18 | 78 | 97 | 84 |
Erroneous | 0 | 0 | 0 | 2 | 0 |
Methyl resonances assigned by MAP-XSII:29 | |||||
Correct | 64 | 24 | 16 | 33 | 79 |
Erroneous | 17 | 5 | 11 | 9 | 1 |
Methyl resonances assigned by FLAMEnGO2.0:31 | |||||
Correct | 0 | 8 | 35 | 0 | 70 |
Erroneous | 0 | 4 | 0 | 0 | 18 |
Methyl resonances assigned by MAGIC:33 | |||||
Correct | 71 | 39 | – | – | – |
Erroneous | 13 | 6 | – | – | – |
