Table 1.
Hydrogen-bond interactions of tryptophan residues in rRBP
| Trp 24 | Trp 91 | Trp 105 | |||||||
| Atom | H-Bonds Distance < 3.3 Å | Distance (Å) | Angle (°) | H-bonds Distance < 3.3 Å | Distance (Å) | Angle (°) | H-Bonds Distance < 3.3 Å | Distance (Å) | Angle (°) |
| Ala43 O | 2.84 | 154.9 | Val74 O | 2.95 | 157.4 | Tyr118 O | 2.71 | 165.5 | |
| Nɛ1 | Phe20 O | 2.76 | 145.2 | Wat | 3.17 | Wat | 2.87 | ||
| O | Ala43 N | 2.87 | 162.3 | Val74 N | 2.73 | 160.3 | Tyr118 N | 2.82 | 142.0 |
| Val74 O | 3.20 | 112.9 | |||||||
| Environment of trypotophan residues in rRBP | |||||||||
| Residue | van der Waals Interactions/ No. of contacts | Accessible protein surface, (Å2) | Temperature factor (Å2) | Comments | |||||
| van der Waals interactions were calculated using CCP4 (CCP4 1994). van der Waals distances are the maximum allowed values of C-C, 4.1 Å; C-N, 3.8 Å; C-O, 3.7 Å; O-O, 3.3 Å; O-N, 3.4 Å; and N-N, 3.4 Å. Accessible protein surface per atom for each tryptophan residue was calculated using DSSP (Kabsch and Sanders 1983). | |||||||||
| Trp24 | Phe20/15, Thr23/13, | 0.0 | 19.5 | well defined in the electron density map | |||||
| Tyr25/12, Ala43/1, Phe45/1, | |||||||||
| Thr109/1, Tyr111/6, | |||||||||
| Thr113/1, Tyr114/6, | |||||||||
| Ala115/5, Phe137/1, | |||||||||
| Ser138/3, Arg139/16 | |||||||||
| Trp67 | — | — | — | disordered well defined in the electron density map | |||||
| Trp91 | Met73/3, Val74/9, Thr76/2, | 77.0 | 28.3 | ||||||
| Lys89/5, Tyr90/18, | |||||||||
| Gly92/14, Lys99/2 | |||||||||
| Trp105 | Val6/5, Phe9/1, Val11/1, | 21.0 | 18.6 | well defined in the electron density map | |||||
| Ala84/2, Lys85/18, | |||||||||
| His104/17, Ile106/11, | |||||||||
| Val107/3, Gly117/4, | |||||||||
| Tyr118/5, Wat/6 | |||||||||