Relative Accessibility of ω+ Residues
|
|
LUP 1CDQ |
MUP 1MUP |
OBP 1OBP |
V2R 1EWK |
MHC M10 1BII |
||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Family structure (PDB) |
All |
ω+ |
All |
ω+ |
All |
ω+ |
All |
ω+ |
All |
ω+ |
|||||
| Total number of residues | 72 | 15 | 157 | 32 | 158 | 33 | 324 | 8 | 274 | 43 | |||||
| No. buried | 14 | 1 | 40 | 7 | 41 | 3 | 140 | 2 | 74 | 11 | |||||
| No. intermediate | 18 | 4 | 52 | 14 | 59 | 13 | 93 | 3 | 133 | 21 | |||||
| No. exposed | 40 | 10 | 65 | 11 | 58 | 17 | 91 | 3 | 67 | 11 | |||||
| % buried | 19.4 | 6.7 | 25.5 | 21.9 | 25.9 | 9.1 | 43.2 | 25.0 | 27.0 | 25.6 | |||||
| % intermediate | 25.0 | 26.7 | 33.5 | 43.8 | 37.3 | 39.4 | 28.7 | 37.5 | 48.5 | 48.8 | |||||
| % exposed
|
55.6
|
66.7
|
41.4
|
34.4
|
36.7
|
51.5
|
28.1
|
37.5
|
24.5
|
25.6
|
|||||
-
Protein structure information obtained from PDB (www.rcsb.org/pdb/) was selected, and residues corresponding to bound ligands were removed. The accessibility of individual amino acids was determined using DSSP (Kabsch and Sander 1983) and default parameters. Relative accessibility scores were calculated as: relative accessibility = (DSSP score/maximal accessibility of amino acid type) × 100. Results were fractionated into three states: buried (<9% relative accessibility), intermediate (9%—35% relative accessibility) and exposed (≥36% relative accessibility) (Rost and Sander 1994). The relative accessibility scores for all residues and ω+ residues are shown.











