4FBY
fs X-ray diffraction of Photosystem II
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0009523 | cellular_component | photosystem II |
| A | 0009635 | biological_process | response to herbicide |
| A | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| A | 0010242 | molecular_function | oxygen evolving activity |
| A | 0015979 | biological_process | photosynthesis |
| A | 0016168 | molecular_function | chlorophyll binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016682 | molecular_function | oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor |
| A | 0019684 | biological_process | photosynthesis, light reaction |
| A | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| A | 0042651 | cellular_component | thylakoid membrane |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0009521 | cellular_component | photosystem |
| B | 0009523 | cellular_component | photosystem II |
| B | 0009767 | biological_process | photosynthetic electron transport chain |
| B | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| B | 0015979 | biological_process | photosynthesis |
| B | 0016020 | cellular_component | membrane |
| B | 0016168 | molecular_function | chlorophyll binding |
| B | 0019684 | biological_process | photosynthesis, light reaction |
| B | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| B | 0042651 | cellular_component | thylakoid membrane |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009521 | cellular_component | photosystem |
| C | 0009523 | cellular_component | photosystem II |
| C | 0009767 | biological_process | photosynthetic electron transport chain |
| C | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| C | 0015979 | biological_process | photosynthesis |
| C | 0016020 | cellular_component | membrane |
| C | 0016168 | molecular_function | chlorophyll binding |
| C | 0019684 | biological_process | photosynthesis, light reaction |
| C | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| C | 0042651 | cellular_component | thylakoid membrane |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0009523 | cellular_component | photosystem II |
| D | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| D | 0010242 | molecular_function | oxygen evolving activity |
| D | 0015979 | biological_process | photosynthesis |
| D | 0016020 | cellular_component | membrane |
| D | 0016168 | molecular_function | chlorophyll binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019684 | biological_process | photosynthesis, light reaction |
| D | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| D | 0042651 | cellular_component | thylakoid membrane |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0009055 | molecular_function | electron transfer activity |
| E | 0009523 | cellular_component | photosystem II |
| E | 0009539 | cellular_component | photosystem II reaction center |
| E | 0009767 | biological_process | photosynthetic electron transport chain |
| E | 0015979 | biological_process | photosynthesis |
| E | 0016020 | cellular_component | membrane |
| E | 0019684 | biological_process | photosynthesis, light reaction |
| E | 0020037 | molecular_function | heme binding |
| E | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| E | 0042651 | cellular_component | thylakoid membrane |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0005506 | molecular_function | iron ion binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0009055 | molecular_function | electron transfer activity |
| F | 0009523 | cellular_component | photosystem II |
| F | 0009539 | cellular_component | photosystem II reaction center |
| F | 0009767 | biological_process | photosynthetic electron transport chain |
| F | 0015979 | biological_process | photosynthesis |
| F | 0016020 | cellular_component | membrane |
| F | 0019684 | biological_process | photosynthesis, light reaction |
| F | 0020037 | molecular_function | heme binding |
| F | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| F | 0042651 | cellular_component | thylakoid membrane |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0005506 | molecular_function | iron ion binding |
| G | 0009055 | molecular_function | electron transfer activity |
| G | 0009523 | cellular_component | photosystem II |
| G | 0009635 | biological_process | response to herbicide |
| G | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| G | 0010242 | molecular_function | oxygen evolving activity |
| G | 0015979 | biological_process | photosynthesis |
| G | 0016168 | molecular_function | chlorophyll binding |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016682 | molecular_function | oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor |
| G | 0019684 | biological_process | photosynthesis, light reaction |
| G | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| G | 0042651 | cellular_component | thylakoid membrane |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0009523 | cellular_component | photosystem II |
| H | 0015979 | biological_process | photosynthesis |
| H | 0016020 | cellular_component | membrane |
| H | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| H | 0042301 | molecular_function | phosphate ion binding |
| H | 0042651 | cellular_component | thylakoid membrane |
| H | 0050821 | biological_process | protein stabilization |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0009523 | cellular_component | photosystem II |
| I | 0009539 | cellular_component | photosystem II reaction center |
| I | 0015979 | biological_process | photosynthesis |
| I | 0016020 | cellular_component | membrane |
| I | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| I | 0042651 | cellular_component | thylakoid membrane |
| J | 0009523 | cellular_component | photosystem II |
| J | 0009539 | cellular_component | photosystem II reaction center |
| J | 0015979 | biological_process | photosynthesis |
| J | 0016020 | cellular_component | membrane |
| J | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| J | 0042651 | cellular_component | thylakoid membrane |
| K | 0009523 | cellular_component | photosystem II |
| K | 0009539 | cellular_component | photosystem II reaction center |
| K | 0015979 | biological_process | photosynthesis |
| L | 0005737 | cellular_component | cytoplasm |
| L | 0009523 | cellular_component | photosystem II |
| L | 0009539 | cellular_component | photosystem II reaction center |
| L | 0015979 | biological_process | photosynthesis |
| L | 0016020 | cellular_component | membrane |
| L | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| L | 0042651 | cellular_component | thylakoid membrane |
| M | 0005737 | cellular_component | cytoplasm |
| M | 0009523 | cellular_component | photosystem II |
| M | 0015979 | biological_process | photosynthesis |
| M | 0016020 | cellular_component | membrane |
| M | 0019684 | biological_process | photosynthesis, light reaction |
| M | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| M | 0042651 | cellular_component | thylakoid membrane |
| N | 0009521 | cellular_component | photosystem |
| N | 0009523 | cellular_component | photosystem II |
| N | 0009767 | biological_process | photosynthetic electron transport chain |
| N | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| N | 0015979 | biological_process | photosynthesis |
| N | 0016020 | cellular_component | membrane |
| N | 0016168 | molecular_function | chlorophyll binding |
| N | 0019684 | biological_process | photosynthesis, light reaction |
| N | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| N | 0042651 | cellular_component | thylakoid membrane |
| O | 0009523 | cellular_component | photosystem II |
| O | 0009654 | cellular_component | photosystem II oxygen evolving complex |
| O | 0010207 | biological_process | photosystem II assembly |
| O | 0010242 | molecular_function | oxygen evolving activity |
| O | 0015979 | biological_process | photosynthesis |
| O | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| O | 0042549 | biological_process | photosystem II stabilization |
| P | 0005737 | cellular_component | cytoplasm |
| P | 0009521 | cellular_component | photosystem |
| P | 0009523 | cellular_component | photosystem II |
| P | 0009767 | biological_process | photosynthetic electron transport chain |
| P | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| P | 0015979 | biological_process | photosynthesis |
| P | 0016020 | cellular_component | membrane |
| P | 0016168 | molecular_function | chlorophyll binding |
| P | 0019684 | biological_process | photosynthesis, light reaction |
| P | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| P | 0042651 | cellular_component | thylakoid membrane |
| P | 0046872 | molecular_function | metal ion binding |
| Q | 0005506 | molecular_function | iron ion binding |
| Q | 0005737 | cellular_component | cytoplasm |
| Q | 0009055 | molecular_function | electron transfer activity |
| Q | 0009523 | cellular_component | photosystem II |
| Q | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| Q | 0010242 | molecular_function | oxygen evolving activity |
| Q | 0015979 | biological_process | photosynthesis |
| Q | 0016020 | cellular_component | membrane |
| Q | 0016168 | molecular_function | chlorophyll binding |
| Q | 0016491 | molecular_function | oxidoreductase activity |
| Q | 0019684 | biological_process | photosynthesis, light reaction |
| Q | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| Q | 0042651 | cellular_component | thylakoid membrane |
| Q | 0046872 | molecular_function | metal ion binding |
| R | 0005506 | molecular_function | iron ion binding |
| R | 0005737 | cellular_component | cytoplasm |
| R | 0009055 | molecular_function | electron transfer activity |
| R | 0009523 | cellular_component | photosystem II |
| R | 0009539 | cellular_component | photosystem II reaction center |
| R | 0009767 | biological_process | photosynthetic electron transport chain |
| R | 0015979 | biological_process | photosynthesis |
| R | 0016020 | cellular_component | membrane |
| R | 0019684 | biological_process | photosynthesis, light reaction |
| R | 0020037 | molecular_function | heme binding |
| R | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| R | 0042651 | cellular_component | thylakoid membrane |
| R | 0046872 | molecular_function | metal ion binding |
| S | 0005506 | molecular_function | iron ion binding |
| S | 0005737 | cellular_component | cytoplasm |
| S | 0009055 | molecular_function | electron transfer activity |
| S | 0009523 | cellular_component | photosystem II |
| S | 0009539 | cellular_component | photosystem II reaction center |
| S | 0009767 | biological_process | photosynthetic electron transport chain |
| S | 0015979 | biological_process | photosynthesis |
| S | 0016020 | cellular_component | membrane |
| S | 0019684 | biological_process | photosynthesis, light reaction |
| S | 0020037 | molecular_function | heme binding |
| S | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| S | 0042651 | cellular_component | thylakoid membrane |
| S | 0046872 | molecular_function | metal ion binding |
| T | 0009523 | cellular_component | photosystem II |
| T | 0009539 | cellular_component | photosystem II reaction center |
| T | 0015979 | biological_process | photosynthesis |
| T | 0016020 | cellular_component | membrane |
| T | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| T | 0042651 | cellular_component | thylakoid membrane |
| U | 0009523 | cellular_component | photosystem II |
| U | 0009654 | cellular_component | photosystem II oxygen evolving complex |
| U | 0015979 | biological_process | photosynthesis |
| U | 0019898 | cellular_component | extrinsic component of membrane |
| U | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| U | 0042549 | biological_process | photosystem II stabilization |
| U | 0042651 | cellular_component | thylakoid membrane |
| V | 0005506 | molecular_function | iron ion binding |
| V | 0009055 | molecular_function | electron transfer activity |
| V | 0009523 | cellular_component | photosystem II |
| V | 0015979 | biological_process | photosynthesis |
| V | 0019684 | biological_process | photosynthesis, light reaction |
| V | 0020037 | molecular_function | heme binding |
| V | 0022904 | biological_process | respiratory electron transport chain |
| V | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| V | 0042651 | cellular_component | thylakoid membrane |
| V | 0046872 | molecular_function | metal ion binding |
| W | 0009523 | cellular_component | photosystem II |
| W | 0015979 | biological_process | photosynthesis |
| W | 0016020 | cellular_component | membrane |
| W | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| W | 0042301 | molecular_function | phosphate ion binding |
| W | 0042651 | cellular_component | thylakoid membrane |
| W | 0050821 | biological_process | protein stabilization |
| X | 0009523 | cellular_component | photosystem II |
| X | 0015979 | biological_process | photosynthesis |
| X | 0016020 | cellular_component | membrane |
| X | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| X | 0042651 | cellular_component | thylakoid membrane |
| Z | 0009523 | cellular_component | photosystem II |
| Z | 0009539 | cellular_component | photosystem II reaction center |
| Z | 0015979 | biological_process | photosynthesis |
| Z | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| Z | 0042549 | biological_process | photosystem II stabilization |
| Z | 0042651 | cellular_component | thylakoid membrane |
| a | 0005737 | cellular_component | cytoplasm |
| a | 0009523 | cellular_component | photosystem II |
| a | 0009539 | cellular_component | photosystem II reaction center |
| a | 0015979 | biological_process | photosynthesis |
| a | 0016020 | cellular_component | membrane |
| a | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| a | 0042651 | cellular_component | thylakoid membrane |
| b | 0009523 | cellular_component | photosystem II |
| b | 0009539 | cellular_component | photosystem II reaction center |
| b | 0015979 | biological_process | photosynthesis |
| b | 0016020 | cellular_component | membrane |
| b | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| b | 0042651 | cellular_component | thylakoid membrane |
| c | 0009523 | cellular_component | photosystem II |
| c | 0009539 | cellular_component | photosystem II reaction center |
| c | 0015979 | biological_process | photosynthesis |
| d | 0005737 | cellular_component | cytoplasm |
| d | 0009523 | cellular_component | photosystem II |
| d | 0009539 | cellular_component | photosystem II reaction center |
| d | 0015979 | biological_process | photosynthesis |
| d | 0016020 | cellular_component | membrane |
| d | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| d | 0042651 | cellular_component | thylakoid membrane |
| e | 0005737 | cellular_component | cytoplasm |
| e | 0009523 | cellular_component | photosystem II |
| e | 0015979 | biological_process | photosynthesis |
| e | 0016020 | cellular_component | membrane |
| e | 0019684 | biological_process | photosynthesis, light reaction |
| e | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| e | 0042651 | cellular_component | thylakoid membrane |
| f | 0009523 | cellular_component | photosystem II |
| f | 0009654 | cellular_component | photosystem II oxygen evolving complex |
| f | 0010207 | biological_process | photosystem II assembly |
| f | 0010242 | molecular_function | oxygen evolving activity |
| f | 0015979 | biological_process | photosynthesis |
| f | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| f | 0042549 | biological_process | photosystem II stabilization |
| g | 0009523 | cellular_component | photosystem II |
| g | 0009539 | cellular_component | photosystem II reaction center |
| g | 0015979 | biological_process | photosynthesis |
| g | 0016020 | cellular_component | membrane |
| g | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| g | 0042651 | cellular_component | thylakoid membrane |
| h | 0009523 | cellular_component | photosystem II |
| h | 0009654 | cellular_component | photosystem II oxygen evolving complex |
| h | 0015979 | biological_process | photosynthesis |
| h | 0019898 | cellular_component | extrinsic component of membrane |
| h | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| h | 0042549 | biological_process | photosystem II stabilization |
| h | 0042651 | cellular_component | thylakoid membrane |
| i | 0005506 | molecular_function | iron ion binding |
| i | 0009055 | molecular_function | electron transfer activity |
| i | 0009523 | cellular_component | photosystem II |
| i | 0015979 | biological_process | photosynthesis |
| i | 0019684 | biological_process | photosynthesis, light reaction |
| i | 0020037 | molecular_function | heme binding |
| i | 0022904 | biological_process | respiratory electron transport chain |
| i | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| i | 0042651 | cellular_component | thylakoid membrane |
| i | 0046872 | molecular_function | metal ion binding |
| j | 0009523 | cellular_component | photosystem II |
| j | 0015979 | biological_process | photosynthesis |
| j | 0016020 | cellular_component | membrane |
| j | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| j | 0042651 | cellular_component | thylakoid membrane |
| l | 0009523 | cellular_component | photosystem II |
| l | 0009539 | cellular_component | photosystem II reaction center |
| l | 0015979 | biological_process | photosynthesis |
| l | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| l | 0042549 | biological_process | photosystem II stabilization |
| l | 0042651 | cellular_component | thylakoid membrane |
| m | 0009523 | cellular_component | photosystem II |
| m | 0015979 | biological_process | photosynthesis |
| m | 0016020 | cellular_component | membrane |
| m | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| m | 0042651 | cellular_component | thylakoid membrane |
| y | 0009523 | cellular_component | photosystem II |
| y | 0015979 | biological_process | photosynthesis |
| y | 0016020 | cellular_component | membrane |
| y | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| y | 0042651 | cellular_component | thylakoid membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE CLA A 401 |
| Chain | Residue |
| A | PHE119 |
| A | HIS198 |
| A | GLY201 |
| A | VAL205 |
| A | THR286 |
| A | ILE290 |
| A | CLA402 |
| A | CLA403 |
| A | PHO404 |
| D | LEU182 |
| D | LEU205 |
| A | TYR147 |
| D | CLA401 |
| T | PHE17 |
| A | PRO150 |
| A | SER153 |
| A | VAL157 |
| A | MET183 |
| A | PHE186 |
| A | GLN187 |
| A | LEU193 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CLA A 402 |
| Chain | Residue |
| A | THR45 |
| A | VAL157 |
| A | PHE158 |
| A | MET172 |
| A | ILE176 |
| A | THR179 |
| A | PHE180 |
| A | MET183 |
| A | CLA401 |
| A | PHO404 |
| D | MET198 |
| D | VAL201 |
| D | GLY206 |
| D | CLA401 |
| D | PL9404 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CLA A 403 |
| Chain | Residue |
| A | GLN199 |
| A | VAL202 |
| A | ALA203 |
| A | LEU210 |
| A | TRP278 |
| A | CLA401 |
| C | DGD518 |
| D | PHE157 |
| D | VAL175 |
| D | ILE178 |
| D | PHE179 |
| D | PHE181 |
| D | LEU182 |
| D | CLA401 |
| D | PHO402 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PHO A 404 |
| Chain | Residue |
| A | LEU41 |
| A | ALA44 |
| A | THR45 |
| A | TYR126 |
| A | GLN130 |
| A | ALA146 |
| A | TYR147 |
| A | LEU174 |
| A | VAL283 |
| A | CLA401 |
| A | CLA402 |
| A | SQD414 |
| D | LEU205 |
| D | ALA208 |
| D | LEU209 |
| D | ILE213 |
| D | TRP253 |
| D | PHE257 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CLA A 405 |
| Chain | Residue |
| A | ILE36 |
| A | PRO39 |
| A | THR40 |
| A | PHE93 |
| A | PRO95 |
| A | ILE96 |
| A | TRP97 |
| A | LEU114 |
| A | HIS118 |
| A | LEU121 |
| A | DGD407 |
| A | SQD414 |
| I | TYR9 |
| I | VAL12 |
| I | BCR101 |
| I | LMG102 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PL9 A 406 |
| Chain | Residue |
| F | THR25 |
| J | PL9101 |
| A | PHE211 |
| A | HIS215 |
| A | LEU218 |
| A | HIS252 |
| A | PHE255 |
| A | SER264 |
| A | PHE265 |
| A | LEU271 |
| A | PHE274 |
| D | PHE38 |
| D | ALA41 |
| D | TYR42 |
| D | LEU45 |
| F | ALA22 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DGD A 407 |
| Chain | Residue |
| A | PHE93 |
| A | PRO95 |
| A | TRP97 |
| A | GLU98 |
| A | CLA405 |
| C | LEU214 |
| C | LYS215 |
| C | SER216 |
| C | PRO217 |
| C | TRP223 |
| C | PHE284 |
| I | LYS5 |
| I | TYR9 |
| O | GLY38 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE LHG A 408 |
| Chain | Residue |
| A | ARG140 |
| A | TRP142 |
| A | VAL145 |
| A | PHE273 |
| A | SQD409 |
| C | TRP36 |
| C | TRP443 |
| C | ARG447 |
| C | CLA504 |
| C | CLA508 |
| D | ASN220 |
| D | ALA229 |
| D | SER230 |
| D | THR231 |
| D | PHE232 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SQD A 409 |
| Chain | Residue |
| A | ASN267 |
| A | SER270 |
| A | PHE273 |
| A | PHE274 |
| A | LHG408 |
| A | LHG411 |
| C | TRP36 |
| C | CLA508 |
| C | DGD517 |
| C | DGD518 |
| D | PHE232 |
| D | ARG233 |
| J | PL9101 |
| K | PHE37 |
| site_id | BC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE LMG A 410 |
| Chain | Residue |
| A | SER232 |
| A | ASN234 |
| B | TRP5 |
| B | TYR6 |
| B | CLA611 |
| B | LMG622 |
| D | TRP266 |
| D | PHE273 |
| L | GLU11 |
| L | LEU12 |
| L | ASN13 |
| L | SER16 |
| L | LEU19 |
| L | GLY20 |
| L | LEU22 |
| L | ILE24 |
| L | VAL26 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE LHG A 411 |
| Chain | Residue |
| A | TYR262 |
| A | ASN266 |
| A | SQD409 |
| C | TRP35 |
| C | DGD517 |
| E | LMG102 |
| J | BCR102 |
| K | PHE45 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OEC A 412 |
| Chain | Residue |
| A | ASP170 |
| A | GLU189 |
| A | HIS332 |
| A | GLU333 |
| A | HIS337 |
| A | ASP342 |
| A | ALA344 |
| C | GLU354 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 A 413 |
| Chain | Residue |
| A | HIS215 |
| A | HIS272 |
| D | HIS214 |
| D | HIS268 |
| D | BCT410 |
| site_id | BC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE SQD A 414 |
| Chain | Residue |
| A | TRP20 |
| A | ASN26 |
| A | ARG27 |
| A | LEU28 |
| A | VAL30 |
| A | ILE38 |
| A | LEU41 |
| A | LEU42 |
| A | THR45 |
| A | PHO404 |
| A | CLA405 |
| I | BCR101 |
| N | TRP113 |
| N | TYR117 |
| N | CLA610 |
| N | CLA620 |
| T | BCR103 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CLA B 601 |
| Chain | Residue |
| B | TRP185 |
| B | PRO187 |
| B | PHE190 |
| B | ILE207 |
| B | VAL208 |
| B | CLA602 |
| H | PHE41 |
| H | ILE44 |
| H | BCR101 |
| site_id | BC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE CLA B 602 |
| Chain | Residue |
| B | GLU184 |
| B | GLY189 |
| B | GLY197 |
| B | ALA200 |
| B | HIS201 |
| B | ALA204 |
| B | ALA205 |
| B | VAL208 |
| B | PHE246 |
| B | PHE247 |
| B | CLA601 |
| B | CLA603 |
| B | DGD621 |
| D | VAL154 |
| H | PHE38 |
| H | PHE41 |
| H | ILE45 |
| H | TYR49 |
| site_id | BC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE CLA B 603 |
| Chain | Residue |
| B | ARG68 |
| B | LEU69 |
| B | ALA146 |
| B | LEU149 |
| B | CYS150 |
| B | PHE153 |
| B | VAL198 |
| B | HIS201 |
| B | HIS202 |
| B | PHE247 |
| B | VAL252 |
| B | THR262 |
| B | CLA602 |
| B | CLA604 |
| B | CLA605 |
| B | CLA606 |
| B | CLA609 |
| H | PHE38 |
| H | LEU42 |
| site_id | BC9 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE CLA B 604 |
| Chain | Residue |
| B | TRP33 |
| B | PHE61 |
| B | PHE65 |
| B | ARG68 |
| B | VAL245 |
| B | ALA248 |
| B | ALA249 |
| B | VAL252 |
| B | PHE451 |
| B | HIS455 |
| B | PHE458 |
| B | PHE462 |
| B | CLA603 |
| B | CLA605 |
| B | CLA607 |
| B | CLA612 |
| B | CLA613 |
| B | CLA615 |
| site_id | CC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE CLA B 605 |
| Chain | Residue |
| B | THR27 |
| B | VAL30 |
| B | ALA31 |
| B | TRP33 |
| B | ALA34 |
| B | VAL62 |
| B | PHE65 |
| B | MET66 |
| B | ARG68 |
| B | LEU69 |
| B | HIS100 |
| B | LEU103 |
| B | GLY147 |
| B | ALA205 |
| B | CLA603 |
| B | CLA604 |
| B | CLA606 |
| B | CLA610 |
| B | CLA612 |
| B | CLA615 |
| site_id | CC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE CLA B 606 |
| Chain | Residue |
| B | LEU69 |
| B | TRP91 |
| B | ALA99 |
| B | LEU103 |
| B | LEU106 |
| B | GLY152 |
| B | PHE153 |
| B | PHE156 |
| B | HIS157 |
| B | PHE162 |
| B | PRO164 |
| B | CLA603 |
| B | CLA605 |
| B | CLA616 |
| B | BCR620 |
| B | LMT625 |
| G | SQD401 |
| site_id | CC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE CLA B 607 |
| Chain | Residue |
| B | TRP33 |
| B | MET37 |
| B | TYR40 |
| B | GLN58 |
| B | GLY59 |
| B | PHE61 |
| B | GLY328 |
| B | PRO329 |
| B | TRP450 |
| B | ALA454 |
| B | CLA604 |
| B | BCR617 |
| B | BCR618 |
| B | BCR619 |
| B | LMG623 |
| D | MET281 |
| L | LEU27 |
| M | PHE14 |
| site_id | CC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE CLA B 608 |
| Chain | Residue |
| B | THR236 |
| B | SER239 |
| B | ALA243 |
| B | PHE246 |
| B | PHE463 |
| B | HIS466 |
| B | LEU474 |
| B | CLA609 |
| B | CLA610 |
| B | SQD624 |
| D | PHE120 |
| D | ILE123 |
| D | MET126 |
| D | LEU127 |
| D | PHE130 |
| D | CLA403 |
| H | LEU43 |
| site_id | CC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE CLA B 609 |
| Chain | Residue |
| B | PHE139 |
| B | LEU143 |
| B | VAL208 |
| B | ALA212 |
| B | PHE215 |
| B | HIS216 |
| B | PRO221 |
| B | PRO222 |
| B | LEU229 |
| B | CLA603 |
| B | CLA608 |
| B | CLA610 |
| H | THR27 |
| H | MET31 |
| H | PHE34 |
| H | LEU46 |
| H | BCR101 |
| site_id | CC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CLA B 610 |
| Chain | Residue |
| B | HIS23 |
| B | PHE139 |
| B | HIS142 |
| B | LEU143 |
| B | VAL237 |
| B | SER240 |
| B | CLA605 |
| B | CLA608 |
| B | CLA609 |
| B | CLA612 |
| B | CLA615 |
| H | BCR101 |
| site_id | CC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE CLA B 611 |
| Chain | Residue |
| A | LMG410 |
| B | TRP5 |
| B | TYR6 |
| B | ARG7 |
| B | VAL8 |
| B | HIS9 |
| B | LEU238 |
| B | ILE242 |
| B | PHE462 |
| B | PHE464 |
| B | GLY465 |
| B | TRP468 |
| B | HIS469 |
| B | ARG472 |
| B | CLA612 |
| B | CLA613 |
| B | CLA614 |
| B | LMG622 |
| site_id | CC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE CLA B 612 |
| Chain | Residue |
| B | HIS9 |
| B | LEU12 |
| B | LEU19 |
| B | ALA22 |
| B | HIS23 |
| B | HIS26 |
| B | THR27 |
| B | ILE234 |
| B | VAL237 |
| B | LEU238 |
| B | SER241 |
| B | VAL245 |
| B | CLA604 |
| B | CLA605 |
| B | CLA610 |
| B | CLA611 |
| B | CLA613 |
| B | CLA614 |
| B | CLA615 |
| site_id | CC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CLA B 613 |
| Chain | Residue |
| B | HIS9 |
| B | HIS26 |
| B | VAL30 |
| B | PHE462 |
| B | CLA604 |
| B | CLA611 |
| B | CLA612 |
| B | CLA614 |
| site_id | DC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CLA B 614 |
| Chain | Residue |
| B | VAL8 |
| B | HIS9 |
| B | TRP115 |
| B | CLA611 |
| B | CLA612 |
| B | CLA613 |
| B | BCR617 |
| B | SQD627 |
| L | VAL10 |
| e | LMG102 |
| g | PHE8 |
| site_id | DC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CLA B 615 |
| Chain | Residue |
| B | HIS23 |
| B | MET138 |
| B | ILE141 |
| B | HIS142 |
| B | LEU145 |
| B | CLA604 |
| B | CLA605 |
| B | CLA610 |
| B | CLA612 |
| B | CLA616 |
| H | LEU14 |
| H | ASN15 |
| site_id | DC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CLA B 616 |
| Chain | Residue |
| B | ILE20 |
| B | LEU24 |
| B | TRP113 |
| B | HIS114 |
| B | LEU120 |
| B | CLA606 |
| B | CLA615 |
| B | BCR620 |
| G | SQD401 |
| H | THR5 |
| site_id | DC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BCR B 617 |
| Chain | Residue |
| B | ALA21 |
| B | MET25 |
| B | LEU29 |
| B | TRP115 |
| B | CLA607 |
| B | CLA614 |
| B | BCR618 |
| B | BCR619 |
| B | LMG623 |
| B | SQD627 |
| M | ILE9 |
| M | ALA10 |
| M | LEU13 |
| M | LMT102 |
| g | PHE19 |
| site_id | DC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE BCR B 618 |
| Chain | Residue |
| B | TRP33 |
| B | SER36 |
| B | MET37 |
| B | TYR40 |
| B | CLA607 |
| B | BCR617 |
| B | BCR619 |
| B | LMT629 |
| Q | LMG407 |
| g | ILE4 |
| g | PHE8 |
| g | ALA11 |
| g | PHE17 |
| g | PHE22 |
| site_id | DC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BCR B 619 |
| Chain | Residue |
| B | LEU29 |
| B | GLY32 |
| B | TRP33 |
| B | ILE101 |
| B | GLY105 |
| B | CLA607 |
| B | BCR617 |
| B | BCR618 |
| B | DGD628 |
| site_id | DC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BCR B 620 |
| Chain | Residue |
| B | LEU109 |
| B | CYS112 |
| B | TRP113 |
| B | TYR117 |
| B | CLA606 |
| B | CLA616 |
| B | LMT625 |
| G | SQD401 |
| g | PHE22 |
| site_id | DC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DGD B 621 |
| Chain | Residue |
| B | TYR193 |
| B | PHE250 |
| B | TYR258 |
| B | TYR273 |
| B | SER277 |
| B | PHE463 |
| B | CLA602 |
| D | HIS87 |
| D | SER165 |
| H | TYR49 |
| H | ASN50 |
| H | VAL60 |
| H | SER61 |
| H | TRP62 |
| site_id | DC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE LMG B 622 |
| Chain | Residue |
| A | LMG410 |
| B | TRP5 |
| B | TYR6 |
| B | ARG7 |
| B | PHE464 |
| B | TRP468 |
| B | CLA611 |
| D | TYR141 |
| D | PHE269 |
| site_id | EC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE LMG B 623 |
| Chain | Residue |
| B | THR327 |
| B | GLY328 |
| B | PRO329 |
| B | LYS332 |
| B | PHE453 |
| B | CLA607 |
| B | BCR617 |
| D | ILE284 |
| L | PHE35 |
| M | LEU6 |
| M | LMT102 |
| site_id | EC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SQD B 624 |
| Chain | Residue |
| B | LYS227 |
| B | ALA228 |
| B | ARG230 |
| B | LEU474 |
| B | CLA608 |
| B | LMT626 |
| D | LYS23 |
| D | TRP32 |
| D | ARG134 |
| D | LEU135 |
| site_id | EC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE LMT B 625 |
| Chain | Residue |
| B | TRP91 |
| B | PHE162 |
| B | CLA606 |
| B | BCR620 |
| B | DGD628 |
| site_id | EC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE LMT B 626 |
| Chain | Residue |
| B | ARG224 |
| B | LEU225 |
| B | LYS227 |
| B | SQD624 |
| D | ASP16 |
| D | ASP19 |
| H | ALA32 |
| H | MET35 |
| site_id | EC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SQD B 627 |
| Chain | Residue |
| B | ARG18 |
| B | LEU29 |
| B | SER104 |
| B | TRP115 |
| B | CLA614 |
| B | BCR617 |
| L | ASN4 |
| d | ARG14 |
| d | TYR18 |
| e | TYR26 |
| e | LMG102 |
| g | PHE19 |
| g | PHE23 |
| site_id | EC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE DGD B 628 |
| Chain | Residue |
| B | TRP75 |
| B | ASP87 |
| B | GLY89 |
| B | PHE90 |
| B | TRP91 |
| B | VAL102 |
| B | BCR619 |
| B | LMT625 |
| B | LMT630 |
| a | LMG102 |
| site_id | EC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE LMT B 629 |
| Chain | Residue |
| B | SER36 |
| B | ALA43 |
| B | THR44 |
| B | BCR618 |
| G | LEU72 |
| g | VAL7 |
| site_id | EC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LMT B 630 |
| Chain | Residue |
| B | GLY85 |
| B | ASP87 |
| B | DGD628 |
| G | ALA100 |
| a | BCR101 |
| a | LMG102 |
| f | LYS95 |
| site_id | EC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CLA C 501 |
| Chain | Residue |
| C | LEU95 |
| C | LEU168 |
| C | GLY171 |
| C | ALA172 |
| C | ILE224 |
| C | VAL233 |
| C | HIS237 |
| C | ILE240 |
| C | ALA278 |
| C | MET282 |
| C | VAL296 |
| C | TYR297 |
| C | CLA502 |
| C | CLA503 |
| C | CLA507 |
| C | BCR515 |
| site_id | FC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CLA C 502 |
| Chain | Residue |
| C | TRP63 |
| C | HIS91 |
| C | TRP97 |
| C | LEU174 |
| C | LYS178 |
| C | PHE182 |
| C | LEU279 |
| C | MET282 |
| C | ALA286 |
| C | TYR297 |
| C | HIS430 |
| C | LEU433 |
| C | PHE437 |
| C | CLA501 |
| C | CLA503 |
| C | CLA510 |
| site_id | FC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CLA C 503 |
| Chain | Residue |
| C | ILE60 |
| C | VAL61 |
| C | ALA64 |
| C | THR68 |
| C | LEU88 |
| C | HIS91 |
| C | VAL114 |
| C | HIS118 |
| C | MET282 |
| C | CLA501 |
| C | CLA502 |
| C | CLA509 |
| C | CLA510 |
| C | CLA512 |
| C | LMG520 |
| site_id | FC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE CLA C 504 |
| Chain | Residue |
| A | PHE285 |
| A | LHG408 |
| C | TRP63 |
| C | MET67 |
| C | PHE70 |
| C | GLN84 |
| C | GLY85 |
| C | ILE87 |
| C | LEU404 |
| C | TRP425 |
| C | SER429 |
| C | CLA508 |
| C | CLA510 |
| C | DGD517 |
| C | DGD518 |
| C | LMG519 |
| K | PRO26 |
| site_id | FC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CLA C 505 |
| Chain | Residue |
| A | PHE33 |
| A | MET127 |
| A | TRP131 |
| C | ILE265 |
| C | TYR274 |
| C | GLY277 |
| C | ALA278 |
| C | LEU438 |
| C | HIS441 |
| C | LEU442 |
| C | ALA445 |
| C | ARG449 |
| C | CLA507 |
| C | BCR515 |
| I | PHE23 |
| site_id | FC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CLA C 506 |
| Chain | Residue |
| C | LEU161 |
| C | LEU165 |
| C | LEU213 |
| C | ILE243 |
| C | GLY247 |
| C | TRP250 |
| C | HIS251 |
| C | THR255 |
| C | PRO256 |
| C | PHE257 |
| C | TRP259 |
| C | ALA260 |
| C | PHE264 |
| C | CLA507 |
| C | BCR515 |
| site_id | FC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CLA C 507 |
| Chain | Residue |
| C | MET157 |
| C | LEU161 |
| C | HIS164 |
| C | ILE240 |
| C | PHE264 |
| C | TRP266 |
| C | TYR271 |
| C | TYR274 |
| C | SER275 |
| C | CLA501 |
| C | CLA505 |
| C | CLA506 |
| C | CLA509 |
| C | BCR515 |
| site_id | FC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE CLA C 508 |
| Chain | Residue |
| A | LHG408 |
| A | SQD409 |
| C | TRP36 |
| C | ALA37 |
| C | ASN39 |
| C | ALA40 |
| C | GLU269 |
| C | LEU276 |
| C | PHE436 |
| C | PHE437 |
| C | GLY440 |
| C | TRP443 |
| C | HIS444 |
| C | ARG447 |
| C | CLA504 |
| C | CLA509 |
| C | CLA510 |
| K | VAL30 |
| site_id | FC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE CLA C 509 |
| Chain | Residue |
| C | ASN39 |
| C | LEU42 |
| C | ILE43 |
| C | LEU49 |
| C | ALA52 |
| C | HIS53 |
| C | HIS56 |
| C | TYR149 |
| C | TRP151 |
| C | GLY268 |
| C | TYR271 |
| C | LEU272 |
| C | SER275 |
| C | LEU279 |
| C | CLA503 |
| C | CLA507 |
| C | CLA508 |
| C | CLA510 |
| C | CLA511 |
| C | CLA512 |
| site_id | FC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CLA C 510 |
| Chain | Residue |
| C | ASN39 |
| C | HIS56 |
| C | LEU59 |
| C | PHE436 |
| C | PHE437 |
| C | CLA502 |
| C | CLA503 |
| C | CLA504 |
| C | CLA508 |
| C | CLA509 |
| K | PRO29 |
| K | VAL30 |
| K | LEU33 |
| site_id | GC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE CLA C 511 |
| Chain | Residue |
| C | GLN28 |
| C | TRP35 |
| C | GLY38 |
| C | ASN39 |
| C | ARG41 |
| C | LEU42 |
| C | LYS48 |
| C | ALA52 |
| C | PHE127 |
| C | ILE134 |
| C | CLA509 |
| C | BCR514 |
| K | PHE32 |
| K | LEU33 |
| K | TRP39 |
| K | GLN40 |
| Z | MET19 |
| Z | VAL20 |
| Z | PRO24 |
| y | ILE35 |
| y | LEU46 |
| site_id | GC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CLA C 512 |
| Chain | Residue |
| C | LEU50 |
| C | HIS53 |
| C | ALA57 |
| C | PHE147 |
| C | PHE163 |
| C | HIS164 |
| C | VAL167 |
| C | ILE170 |
| C | GLY171 |
| C | LEU174 |
| C | CLA503 |
| C | CLA509 |
| C | CLA513 |
| Z | BCR101 |
| site_id | GC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CLA C 513 |
| Chain | Residue |
| C | VAL54 |
| C | GLY128 |
| C | TYR131 |
| C | HIS132 |
| C | PRO137 |
| C | LEU140 |
| C | PHE147 |
| C | CLA512 |
| Z | BCR101 |
| site_id | GC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE BCR C 514 |
| Chain | Residue |
| C | ALA55 |
| C | LEU59 |
| C | VAL116 |
| C | LEU119 |
| C | ILE120 |
| C | SER122 |
| C | ALA123 |
| C | CLA511 |
| K | PHE18 |
| K | PHE32 |
| K | BCR101 |
| Z | LEU9 |
| Z | VAL13 |
| Z | BCR101 |
| site_id | GC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BCR C 515 |
| Chain | Residue |
| C | ILE209 |
| C | PHE210 |
| C | TYR212 |
| C | LEU213 |
| C | VAL227 |
| C | ASP232 |
| C | VAL233 |
| C | ILE240 |
| C | PHE264 |
| C | CLA501 |
| C | CLA505 |
| C | CLA506 |
| C | CLA507 |
| I | VAL20 |
| I | LEU24 |
| site_id | GC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DGD C 516 |
| Chain | Residue |
| A | PHE155 |
| A | ILE163 |
| C | PRO217 |
| C | PHE218 |
| C | GLY219 |
| C | GLY220 |
| C | GLY222 |
| C | VAL225 |
| C | CYS288 |
| C | PHE292 |
| C | ASN294 |
| C | PRO307 |
| C | PHE361 |
| C | ARG362 |
| site_id | GC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE DGD C 517 |
| Chain | Residue |
| A | PHE197 |
| A | THR292 |
| A | SQD409 |
| A | LHG411 |
| C | TYR82 |
| C | GLU83 |
| C | GLN84 |
| C | GLY85 |
| C | LEU404 |
| C | SER406 |
| C | ASN418 |
| C | VAL420 |
| C | TRP425 |
| C | THR428 |
| C | SER429 |
| C | CLA504 |
| C | DGD518 |
| C | LMG519 |
| J | TYR33 |
| J | BCR102 |
| site_id | GC8 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE DGD C 518 |
| Chain | Residue |
| A | LEU200 |
| A | TRP278 |
| A | PHE300 |
| A | ASN301 |
| A | PHE302 |
| A | SER305 |
| A | CLA403 |
| A | SQD409 |
| C | ASN405 |
| C | ASN415 |
| C | SER416 |
| C | ASN418 |
| C | CLA504 |
| C | DGD517 |
| D | LMG406 |
| J | PHE29 |
| J | ALA32 |
| J | TYR33 |
| J | GLY37 |
| J | SER38 |
| J | SER39 |
| J | BCR102 |
| V | GLN60 |
| site_id | GC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LMG C 519 |
| Chain | Residue |
| C | HIS74 |
| C | CLA504 |
| C | DGD517 |
| K | ASP23 |
| K | VAL27 |
| K | VAL30 |
| y | ILE25 |
| site_id | HC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LMG C 520 |
| Chain | Residue |
| C | ASP107 |
| C | PHE109 |
| C | VAL114 |
| C | VAL117 |
| C | HIS118 |
| C | CLA503 |
| Z | PHE59 |
| site_id | HC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE CLA D 401 |
| Chain | Residue |
| A | PHE206 |
| A | CLA401 |
| A | CLA402 |
| A | CLA403 |
| D | TRP48 |
| D | LEU122 |
| D | PRO149 |
| D | VAL152 |
| D | VAL156 |
| D | LEU182 |
| D | PHE185 |
| D | GLN186 |
| D | TRP191 |
| D | THR192 |
| D | HIS197 |
| D | GLY200 |
| D | VAL201 |
| D | VAL204 |
| D | LEU279 |
| D | SER282 |
| D | ALA283 |
| D | PHO402 |
| site_id | HC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE PHO D 402 |
| Chain | Residue |
| A | PHE206 |
| A | ALA209 |
| A | LEU210 |
| A | MET214 |
| A | CLA403 |
| D | ALA41 |
| D | TRP48 |
| D | ILE114 |
| D | GLY118 |
| D | LEU122 |
| D | PHE125 |
| D | ASN142 |
| D | ALA145 |
| D | PHE146 |
| D | ALA148 |
| D | PRO149 |
| D | PHE153 |
| D | PRO275 |
| D | LEU279 |
| D | CLA401 |
| site_id | HC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CLA D 403 |
| Chain | Residue |
| B | CLA608 |
| D | PRO39 |
| D | LEU43 |
| D | LEU89 |
| D | LEU90 |
| D | LEU91 |
| D | LEU92 |
| D | TRP93 |
| D | THR112 |
| D | PHE113 |
| D | HIS117 |
| D | LMT409 |
| X | GLY22 |
| X | LEU23 |
| X | GLY26 |
| site_id | HC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PL9 D 404 |
| Chain | Residue |
| A | PHE52 |
| A | ILE53 |
| A | CLA402 |
| D | MET199 |
| D | ILE213 |
| D | HIS214 |
| D | THR217 |
| D | TRP253 |
| D | ALA260 |
| D | PHE261 |
| D | LEU267 |
| D | PHE273 |
| D | VAL274 |
| D | THR277 |
| D | LMG407 |
| L | LEU23 |
| L | VAL26 |
| L | LEU29 |
| T | PHE10 |
| site_id | HC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE BCR D 405 |
| Chain | Residue |
| D | TYR42 |
| D | GLY46 |
| D | GLY47 |
| D | LEU49 |
| D | THR50 |
| D | PHE101 |
| D | LMG406 |
| F | PRO29 |
| F | PHE33 |
| J | VAL21 |
| J | VAL25 |
| site_id | HC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE LMG D 406 |
| Chain | Residue |
| C | DGD518 |
| D | TYR67 |
| D | GLY70 |
| D | CYS71 |
| D | PHE73 |
| D | BCR405 |
| F | ILE37 |
| F | GLN41 |
| J | PHE28 |
| J | GLY31 |
| J | ALA32 |
| J | GLY37 |
| site_id | HC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE LMG D 407 |
| Chain | Residue |
| D | PHE257 |
| D | ALA260 |
| D | PHE261 |
| D | SER262 |
| D | ASN263 |
| D | TRP266 |
| D | PL9404 |
| L | THR15 |
| L | TYR18 |
| L | LEU19 |
| T | ALA20 |
| T | BCR102 |
| site_id | HC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DGD D 408 |
| Chain | Residue |
| E | LEU42 |
| E | ASP45 |
| E | VAL46 |
| D | ASP100 |
| D | PHE101 |
| D | LMT409 |
| site_id | IC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE LMT D 409 |
| Chain | Residue |
| D | LEU92 |
| D | TRP93 |
| D | GLY99 |
| D | CLA403 |
| D | DGD408 |
| X | ILE21 |
| X | SER25 |
| X | GLY26 |
| site_id | IC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BCT D 410 |
| Chain | Residue |
| A | HIS215 |
| A | GLU244 |
| A | TYR246 |
| A | HIS272 |
| A | FE2413 |
| D | HIS214 |
| D | TYR244 |
| D | LYS264 |
| D | HIS268 |
| site_id | IC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL D 411 |
| Chain | Residue |
| A | GLU333 |
| D | LYS317 |
| site_id | IC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE LMG D 412 |
| Chain | Residue |
| A | LEU72 |
| A | LEU102 |
| A | ASP103 |
| D | ARG304 |
| N | ALA43 |
| N | TRP75 |
| N | SER76 |
| N | LEU98 |
| O | GLY138 |
| site_id | IC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM E 101 |
| Chain | Residue |
| E | ARG8 |
| E | PHE10 |
| E | ILE13 |
| E | ARG18 |
| E | TYR19 |
| E | HIS23 |
| E | THR26 |
| E | LEU30 |
| F | ILE15 |
| F | ARG19 |
| F | TRP20 |
| F | HIS24 |
| F | ALA27 |
| F | ILE31 |
| site_id | IC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LMG E 102 |
| Chain | Residue |
| A | TYR262 |
| A | LHG411 |
| D | PHE27 |
| E | PRO9 |
| E | PHE10 |
| E | SER11 |
| J | PL9101 |
| site_id | IC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SQD F 101 |
| Chain | Residue |
| D | TRP21 |
| D | ARG26 |
| E | GLU7 |
| F | PHE16 |
| F | THR17 |
| F | VAL18 |
| X | THR33 |
| site_id | IC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BCR H 101 |
| Chain | Residue |
| B | CLA601 |
| B | CLA609 |
| B | CLA610 |
| H | MET35 |
| H | LEU37 |
| H | PHE38 |
| H | PHE41 |
| X | THR11 |
| X | LEU16 |
| site_id | IC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BCR I 101 |
| Chain | Residue |
| A | VAL35 |
| A | ILE38 |
| A | LEU42 |
| A | ALA43 |
| A | TRP105 |
| A | CLA405 |
| A | SQD414 |
| I | PHE15 |
| N | LMT604 |
| site_id | JC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LMG I 102 |
| Chain | Residue |
| A | CLA405 |
| I | MET1 |
| I | THR3 |
| I | LEU4 |
| I | LMT103 |
| N | DGD602 |
| N | LMT604 |
| site_id | JC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE LMT I 103 |
| Chain | Residue |
| I | THR3 |
| I | ILE6 |
| I | ILE10 |
| I | VAL11 |
| I | PHE14 |
| I | LMG102 |
| site_id | JC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PL9 J 101 |
| Chain | Residue |
| A | PL9406 |
| A | SQD409 |
| E | LMG102 |
| J | VAL16 |
| site_id | JC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BCR J 102 |
| Chain | Residue |
| A | LHG411 |
| C | DGD517 |
| C | DGD518 |
| J | PHE29 |
| J | TYR33 |
| site_id | JC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BCR K 101 |
| Chain | Residue |
| C | BCR514 |
| J | ALA14 |
| J | THR15 |
| J | GLY18 |
| J | MET19 |
| K | LEU21 |
| K | LEU31 |
| K | PHE37 |
| K | VAL38 |
| K | ALA41 |
| Z | SER16 |
| Z | PHE17 |
| y | ILE28 |
| y | GLY29 |
| y | GLY32 |
| site_id | JC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LMG M 101 |
| Chain | Residue |
| M | GLU30 |
| M | SER31 |
| N | CLA618 |
| d | PRO9 |
| d | VAL10 |
| e | LEU25 |
| e | GLN32 |
| site_id | JC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE LMT M 102 |
| Chain | Residue |
| B | TYR40 |
| B | BCR617 |
| B | LMG623 |
| M | GLN5 |
| e | MET1 |
| g | MET1 |
| site_id | JC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA O 301 |
| Chain | Residue |
| O | GLU81 |
| O | GLU140 |
| O | HIS257 |
| site_id | JC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE BCR T 101 |
| Chain | Residue |
| N | ALA21 |
| N | MET25 |
| N | LEU29 |
| N | TRP115 |
| N | SQD601 |
| N | CLA618 |
| N | BCR621 |
| N | LMG623 |
| T | PHE19 |
| T | BCR102 |
| e | ILE9 |
| e | ALA10 |
| e | LEU13 |
| e | LMT101 |
| site_id | KC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BCR T 102 |
| Chain | Residue |
| D | LMG407 |
| N | TRP33 |
| N | SER36 |
| N | MET37 |
| N | LMT603 |
| N | CLA611 |
| N | BCR621 |
| T | ILE4 |
| T | PHE8 |
| T | ALA11 |
| T | PHE17 |
| T | PHE18 |
| T | ILE21 |
| T | PHE22 |
| T | BCR101 |
| site_id | KC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BCR T 103 |
| Chain | Residue |
| A | SQD414 |
| N | LEU106 |
| N | LEU109 |
| N | CYS112 |
| N | TYR117 |
| N | CLA610 |
| N | CLA620 |
| T | PHE22 |
| site_id | KC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM V 201 |
| Chain | Residue |
| V | ALA62 |
| V | CYS63 |
| V | HIS67 |
| V | THR74 |
| V | LEU78 |
| V | ASP79 |
| V | THR84 |
| V | LEU85 |
| V | LEU98 |
| V | TYR101 |
| V | MET102 |
| V | TYR108 |
| V | HIS118 |
| V | PRO119 |
| site_id | KC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE BCR Z 101 |
| Chain | Residue |
| C | PHE112 |
| C | VAL116 |
| C | SER121 |
| C | VAL124 |
| C | CLA512 |
| C | CLA513 |
| C | BCR514 |
| K | TYR15 |
| Z | VAL54 |
| Z | GLY55 |
| Z | ASN58 |
| site_id | KC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE SQD G 401 |
| Chain | Residue |
| B | TRP113 |
| B | TYR117 |
| B | CLA606 |
| B | CLA616 |
| B | BCR620 |
| G | TRP20 |
| G | ASN26 |
| G | ARG27 |
| G | LEU28 |
| G | VAL30 |
| G | ILE38 |
| G | LEU41 |
| G | LEU42 |
| G | THR45 |
| G | PHO405 |
| G | CLA406 |
| a | BCR101 |
| site_id | KC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE CLA G 402 |
| Chain | Residue |
| G | PHE119 |
| G | TYR147 |
| G | PRO150 |
| G | SER153 |
| G | VAL157 |
| G | MET183 |
| G | PHE186 |
| G | GLN187 |
| G | LEU193 |
| G | HIS198 |
| G | VAL205 |
| G | THR286 |
| G | ILE290 |
| G | CLA403 |
| G | CLA404 |
| G | PHO405 |
| Q | LEU182 |
| Q | LEU205 |
| Q | CLA402 |
| g | PHE17 |
| site_id | KC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CLA G 403 |
| Chain | Residue |
| G | THR45 |
| G | VAL157 |
| G | PHE158 |
| G | MET172 |
| G | ILE176 |
| G | THR179 |
| G | MET183 |
| G | CLA402 |
| G | PHO405 |
| Q | MET198 |
| Q | VAL201 |
| Q | GLY206 |
| Q | CLA402 |
| Q | PL9405 |
| site_id | KC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CLA G 404 |
| Chain | Residue |
| G | GLN199 |
| G | VAL202 |
| G | ALA203 |
| G | LEU210 |
| G | TRP278 |
| G | CLA402 |
| P | DGD519 |
| Q | PHE157 |
| Q | VAL175 |
| Q | ILE178 |
| Q | PHE179 |
| Q | PHE181 |
| Q | LEU182 |
| Q | CLA402 |
| Q | PHO403 |
| b | PL9101 |
| site_id | KC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PHO G 405 |
| Chain | Residue |
| G | ALA44 |
| G | THR45 |
| G | ILE115 |
| G | TYR126 |
| G | GLN130 |
| G | ALA146 |
| G | TYR147 |
| G | PRO150 |
| G | LEU174 |
| G | VAL283 |
| G | SQD401 |
| G | CLA402 |
| G | CLA403 |
| Q | LEU205 |
| Q | ALA208 |
| Q | LEU209 |
| Q | ILE213 |
| Q | TRP253 |
| Q | PHE257 |
| site_id | LC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CLA G 406 |
| Chain | Residue |
| G | ILE36 |
| G | PRO39 |
| G | THR40 |
| G | PHE93 |
| G | PRO95 |
| G | ILE96 |
| G | TRP97 |
| G | LEU114 |
| G | HIS118 |
| G | LEU121 |
| G | SQD401 |
| G | DGD408 |
| a | TYR9 |
| a | VAL12 |
| a | LMG102 |
| site_id | LC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PL9 G 407 |
| Chain | Residue |
| G | PHE211 |
| G | HIS215 |
| G | LEU218 |
| G | HIS252 |
| G | PHE255 |
| G | SER264 |
| G | PHE265 |
| G | LEU271 |
| G | PHE274 |
| Q | PHE38 |
| Q | ALA41 |
| Q | TYR42 |
| Q | LEU45 |
| S | ALA22 |
| S | THR25 |
| b | PL9101 |
| site_id | LC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DGD G 408 |
| Chain | Residue |
| G | PHE93 |
| G | PRO95 |
| G | TRP97 |
| G | GLU98 |
| G | CLA406 |
| P | LEU214 |
| P | LYS215 |
| P | SER216 |
| P | PRO217 |
| P | TRP223 |
| P | PHE284 |
| a | LYS5 |
| a | TYR9 |
| f | GLY38 |
| site_id | LC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE LHG G 409 |
| Chain | Residue |
| G | ARG140 |
| G | TRP142 |
| G | PHE273 |
| G | SQD410 |
| P | TRP36 |
| P | ARG447 |
| P | CLA504 |
| P | CLA508 |
| P | CLA510 |
| Q | ASN220 |
| Q | ALA229 |
| Q | SER230 |
| Q | THR231 |
| Q | PHE232 |
| site_id | LC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SQD G 410 |
| Chain | Residue |
| G | ASN267 |
| G | SER270 |
| G | PHE273 |
| G | PHE274 |
| G | LHG409 |
| G | LHG412 |
| P | TRP36 |
| P | CLA508 |
| P | DGD518 |
| P | DGD519 |
| Q | ARG233 |
| b | PL9101 |
| c | PHE37 |
| site_id | LC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE LMG G 411 |
| Chain | Residue |
| G | SER232 |
| G | ASN234 |
| N | TRP5 |
| N | TYR6 |
| N | CLA615 |
| N | LMG622 |
| Q | TRP266 |
| Q | PHE270 |
| Q | PHE273 |
| Q | PL9405 |
| d | GLU11 |
| d | LEU12 |
| d | ASN13 |
| d | SER16 |
| d | GLY20 |
| d | ILE24 |
| d | VAL26 |
| site_id | LC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE LHG G 412 |
| Chain | Residue |
| G | TYR262 |
| G | ASN266 |
| G | SQD410 |
| P | TRP35 |
| P | DGD518 |
| R | LMG102 |
| b | BCR102 |
| c | PHE45 |
| site_id | LC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE OEC G 413 |
| Chain | Residue |
| G | ASP170 |
| G | GLU189 |
| G | HIS332 |
| G | GLU333 |
| G | ASP342 |
| G | ALA344 |
| P | GLU354 |
| site_id | LC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE2 G 414 |
| Chain | Residue |
| G | HIS215 |
| G | HIS272 |
| Q | HIS214 |
| Q | HIS268 |
| Q | BCT411 |
| site_id | MC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL G 415 |
| Chain | Residue |
| G | GLU333 |
| Q | LYS317 |
| site_id | MC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SQD N 601 |
| Chain | Residue |
| L | ARG14 |
| L | TYR18 |
| M | TYR26 |
| N | ARG18 |
| N | LEU29 |
| N | SER104 |
| N | TRP115 |
| N | CLA618 |
| T | PHE19 |
| T | PHE23 |
| T | BCR101 |
| d | ASN4 |
| site_id | MC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE DGD N 602 |
| Chain | Residue |
| I | LMG102 |
| N | TRP75 |
| N | ASP87 |
| N | GLY89 |
| N | PHE90 |
| N | TRP91 |
| N | LEU98 |
| N | VAL102 |
| N | LMT604 |
| N | LMT624 |
| site_id | MC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LMT N 603 |
| Chain | Residue |
| A | LEU72 |
| N | SER36 |
| N | ALA43 |
| N | LEU437 |
| T | ILE4 |
| T | VAL7 |
| T | BCR102 |
| site_id | MC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LMT N 604 |
| Chain | Residue |
| A | ALA100 |
| I | BCR101 |
| I | LMG102 |
| N | GLY85 |
| N | ASP87 |
| N | DGD602 |
| O | LYS95 |
| site_id | MC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CLA N 605 |
| Chain | Residue |
| N | TRP185 |
| N | PHE190 |
| N | ILE207 |
| N | VAL208 |
| N | CLA606 |
| W | PHE41 |
| W | ILE44 |
| W | BCR101 |
| site_id | MC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE CLA N 606 |
| Chain | Residue |
| N | GLU184 |
| N | GLY189 |
| N | GLY197 |
| N | ALA200 |
| N | HIS201 |
| N | ALA204 |
| N | ALA205 |
| N | VAL208 |
| N | PHE246 |
| N | PHE247 |
| N | CLA605 |
| N | CLA607 |
| Q | VAL154 |
| W | PHE38 |
| W | PHE41 |
| W | ILE45 |
| W | TYR49 |
| W | DGD102 |
| site_id | MC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE CLA N 607 |
| Chain | Residue |
| N | ARG68 |
| N | LEU69 |
| N | ALA146 |
| N | LEU149 |
| N | CYS150 |
| N | PHE153 |
| N | VAL198 |
| N | HIS201 |
| N | HIS202 |
| N | PHE247 |
| N | ALA248 |
| N | VAL252 |
| N | THR262 |
| N | CLA606 |
| N | CLA608 |
| N | CLA609 |
| N | CLA610 |
| N | CLA613 |
| W | PHE38 |
| W | LEU42 |
| site_id | MC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE CLA N 608 |
| Chain | Residue |
| N | TRP33 |
| N | PHE61 |
| N | PHE65 |
| N | ARG68 |
| N | VAL245 |
| N | ALA248 |
| N | ALA249 |
| N | VAL252 |
| N | PHE451 |
| N | HIS455 |
| N | PHE458 |
| N | PHE462 |
| N | CLA607 |
| N | CLA609 |
| N | CLA611 |
| N | CLA615 |
| N | CLA616 |
| N | CLA617 |
| N | CLA619 |
| site_id | NC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE CLA N 609 |
| Chain | Residue |
| N | THR27 |
| N | VAL30 |
| N | ALA31 |
| N | TRP33 |
| N | ALA34 |
| N | VAL62 |
| N | PHE65 |
| N | MET66 |
| N | ARG68 |
| N | LEU69 |
| N | HIS100 |
| N | LEU103 |
| N | GLY147 |
| N | ALA205 |
| N | CLA607 |
| N | CLA608 |
| N | CLA610 |
| N | CLA614 |
| N | CLA616 |
| N | CLA619 |
| site_id | NC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE CLA N 610 |
| Chain | Residue |
| A | SQD414 |
| N | LEU69 |
| N | TRP91 |
| N | ALA99 |
| N | LEU103 |
| N | LEU106 |
| N | GLY152 |
| N | PHE153 |
| N | PHE156 |
| N | HIS157 |
| N | PHE162 |
| N | PRO164 |
| N | CLA607 |
| N | CLA609 |
| N | CLA620 |
| N | LMT624 |
| T | BCR103 |
| site_id | NC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CLA N 611 |
| Chain | Residue |
| N | TRP33 |
| N | MET37 |
| N | TYR40 |
| N | GLN58 |
| N | GLY59 |
| N | PHE61 |
| N | GLY328 |
| N | PRO329 |
| N | TRP450 |
| N | ALA454 |
| N | CLA608 |
| N | BCR621 |
| N | LMG623 |
| Q | MET281 |
| T | BCR102 |
| e | PHE14 |
| site_id | NC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CLA N 612 |
| Chain | Residue |
| N | THR236 |
| N | SER239 |
| N | SER240 |
| N | ALA243 |
| N | PHE246 |
| N | PHE463 |
| N | HIS466 |
| N | LEU474 |
| N | CLA613 |
| N | CLA614 |
| Q | PHE120 |
| Q | ILE123 |
| Q | MET126 |
| Q | LEU127 |
| Q | PHE130 |
| site_id | NC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CLA N 613 |
| Chain | Residue |
| N | PHE139 |
| N | LEU143 |
| N | ALA212 |
| N | PHE215 |
| N | HIS216 |
| N | ARG220 |
| N | PRO221 |
| N | PRO222 |
| N | LEU229 |
| N | CLA607 |
| N | CLA612 |
| N | CLA614 |
| W | THR27 |
| W | MET31 |
| W | PHE34 |
| W | BCR101 |
| site_id | NC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CLA N 614 |
| Chain | Residue |
| N | PHE139 |
| N | HIS142 |
| N | LEU143 |
| N | THR236 |
| N | VAL237 |
| N | SER240 |
| N | CLA609 |
| N | CLA612 |
| N | CLA613 |
| N | CLA616 |
| N | CLA619 |
| site_id | NC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE CLA N 615 |
| Chain | Residue |
| G | LMG411 |
| N | TRP5 |
| N | TYR6 |
| N | ARG7 |
| N | VAL8 |
| N | HIS9 |
| N | LEU238 |
| N | ILE242 |
| N | LEU461 |
| N | PHE462 |
| N | PHE464 |
| N | GLY465 |
| N | TRP468 |
| N | HIS469 |
| N | ARG472 |
| N | CLA608 |
| N | CLA616 |
| N | CLA617 |
| N | CLA618 |
| N | LMG622 |
| site_id | NC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE CLA N 616 |
| Chain | Residue |
| N | HIS9 |
| N | LEU12 |
| N | LEU19 |
| N | ALA22 |
| N | HIS23 |
| N | HIS26 |
| N | THR27 |
| N | ILE234 |
| N | VAL237 |
| N | LEU238 |
| N | SER241 |
| N | VAL245 |
| N | CLA608 |
| N | CLA609 |
| N | CLA614 |
| N | CLA615 |
| N | CLA617 |
| N | CLA618 |
| N | CLA619 |
| site_id | NC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CLA N 617 |
| Chain | Residue |
| N | HIS9 |
| N | HIS26 |
| N | VAL30 |
| N | LEU461 |
| N | PHE462 |
| N | CLA608 |
| N | CLA615 |
| N | CLA616 |
| N | CLA618 |
| site_id | OC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CLA N 618 |
| Chain | Residue |
| M | LMG101 |
| N | VAL8 |
| N | HIS9 |
| N | ALA22 |
| N | TRP115 |
| N | SQD601 |
| N | CLA615 |
| N | CLA616 |
| N | CLA617 |
| T | PHE8 |
| T | BCR101 |
| d | VAL10 |
| site_id | OC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CLA N 619 |
| Chain | Residue |
| N | MET138 |
| N | ILE141 |
| N | HIS142 |
| N | LEU145 |
| N | CLA608 |
| N | CLA609 |
| N | CLA614 |
| N | CLA616 |
| N | CLA620 |
| W | LEU14 |
| site_id | OC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CLA N 620 |
| Chain | Residue |
| A | SQD414 |
| N | ILE20 |
| N | LEU24 |
| N | ALA110 |
| N | TRP113 |
| N | HIS114 |
| N | LEU120 |
| N | CLA610 |
| N | CLA619 |
| T | BCR103 |
| W | THR5 |
| site_id | OC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BCR N 621 |
| Chain | Residue |
| N | LEU29 |
| N | GLY32 |
| N | TRP33 |
| N | SER36 |
| N | ILE101 |
| N | CLA611 |
| T | BCR101 |
| T | BCR102 |
| site_id | OC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE LMG N 622 |
| Chain | Residue |
| G | LMG411 |
| N | TRP5 |
| N | TYR6 |
| N | ARG7 |
| N | PHE464 |
| N | TRP468 |
| N | CLA615 |
| Q | TYR141 |
| Q | PHE269 |
| site_id | OC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE LMG N 623 |
| Chain | Residue |
| N | THR327 |
| N | GLY328 |
| N | PRO329 |
| N | LYS332 |
| N | PHE453 |
| N | CLA611 |
| Q | ILE284 |
| T | BCR101 |
| d | PHE35 |
| e | LEU6 |
| e | LMT101 |
| site_id | OC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LMT N 624 |
| Chain | Residue |
| N | TRP91 |
| N | PHE162 |
| N | DGD602 |
| N | CLA610 |
| site_id | OC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE LMT N 625 |
| Chain | Residue |
| N | ARG224 |
| N | LEU225 |
| N | LYS227 |
| Q | ASP16 |
| Q | ASP19 |
| Q | SQD408 |
| W | ALA32 |
| W | MET35 |
| site_id | OC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CLA P 501 |
| Chain | Residue |
| P | LEU95 |
| P | LEU168 |
| P | GLY171 |
| P | ALA172 |
| P | ILE224 |
| P | VAL233 |
| P | HIS237 |
| P | ILE240 |
| P | MET282 |
| P | VAL296 |
| P | TYR297 |
| P | CLA502 |
| P | CLA503 |
| P | CLA507 |
| P | BCR516 |
| site_id | PC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CLA P 502 |
| Chain | Residue |
| P | TRP63 |
| P | HIS91 |
| P | TRP97 |
| P | LEU174 |
| P | LYS178 |
| P | LEU279 |
| P | MET282 |
| P | ALA286 |
| P | TYR297 |
| P | HIS430 |
| P | LEU433 |
| P | PHE437 |
| P | CLA501 |
| P | CLA503 |
| site_id | PC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CLA P 503 |
| Chain | Residue |
| P | ILE60 |
| P | VAL61 |
| P | ALA64 |
| P | THR68 |
| P | LEU88 |
| P | HIS91 |
| P | VAL114 |
| P | HIS118 |
| P | CLA501 |
| P | CLA502 |
| P | CLA510 |
| P | CLA512 |
| P | LMG521 |
| site_id | PC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE CLA P 504 |
| Chain | Residue |
| G | PHE285 |
| G | LHG409 |
| P | TRP63 |
| P | MET67 |
| P | PHE70 |
| P | GLN84 |
| P | GLY85 |
| P | ILE87 |
| P | LEU404 |
| P | TRP425 |
| P | SER429 |
| P | CLA508 |
| P | CLA510 |
| P | DGD518 |
| P | DGD519 |
| P | LMG520 |
| c | PRO26 |
| c | VAL30 |
| site_id | PC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CLA P 505 |
| Chain | Residue |
| G | PHE33 |
| G | MET127 |
| G | TRP131 |
| P | PHE264 |
| P | ILE265 |
| P | TYR274 |
| P | GLY277 |
| P | ALA278 |
| P | MET281 |
| P | HIS441 |
| P | LEU442 |
| P | ALA445 |
| P | ARG449 |
| P | CLA507 |
| P | BCR516 |
| a | PHE23 |
| site_id | PC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CLA P 506 |
| Chain | Residue |
| P | LEU161 |
| P | LEU165 |
| P | LEU213 |
| P | ILE243 |
| P | GLY247 |
| P | TRP250 |
| P | HIS251 |
| P | THR255 |
| P | PRO256 |
| P | PHE257 |
| P | TRP259 |
| P | ALA260 |
| P | PHE264 |
| P | CLA507 |
| site_id | PC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CLA P 507 |
| Chain | Residue |
| P | MET157 |
| P | LEU161 |
| P | HIS164 |
| P | PHE264 |
| P | TRP266 |
| P | TYR271 |
| P | TYR274 |
| P | SER275 |
| P | CLA501 |
| P | CLA505 |
| P | CLA506 |
| P | CLA509 |
| P | BCR516 |
| site_id | PC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE CLA P 508 |
| Chain | Residue |
| G | LHG409 |
| G | SQD410 |
| P | TRP36 |
| P | ALA37 |
| P | ASN39 |
| P | ALA40 |
| P | GLU269 |
| P | LEU272 |
| P | LEU276 |
| P | PHE436 |
| P | PHE437 |
| P | GLY440 |
| P | TRP443 |
| P | HIS444 |
| P | ARG447 |
| P | CLA504 |
| P | CLA509 |
| P | CLA510 |
| c | VAL30 |
| site_id | PC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE CLA P 509 |
| Chain | Residue |
| P | ASN39 |
| P | LEU42 |
| P | ILE43 |
| P | LEU49 |
| P | ALA52 |
| P | HIS53 |
| P | HIS56 |
| P | TYR149 |
| P | TRP151 |
| P | GLY268 |
| P | TYR271 |
| P | LEU272 |
| P | SER275 |
| P | LEU279 |
| P | CLA507 |
| P | CLA508 |
| P | CLA510 |
| P | CLA511 |
| P | CLA512 |
| site_id | PC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CLA P 510 |
| Chain | Residue |
| G | LHG409 |
| P | ASN39 |
| P | HIS56 |
| P | LEU59 |
| P | LEU279 |
| P | PHE436 |
| P | PHE437 |
| P | CLA503 |
| P | CLA504 |
| P | CLA508 |
| P | CLA509 |
| P | CLA511 |
| c | PRO29 |
| c | LEU33 |
| site_id | QC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE CLA P 511 |
| Chain | Residue |
| P | GLN28 |
| P | TRP35 |
| P | GLY38 |
| P | ASN39 |
| P | ARG41 |
| P | LEU42 |
| P | LYS48 |
| P | ALA52 |
| P | PHE127 |
| P | ILE134 |
| P | CLA509 |
| P | CLA510 |
| P | BCR514 |
| c | PHE32 |
| c | LEU33 |
| c | TRP39 |
| c | GLN40 |
| l | MET19 |
| l | VAL20 |
| l | PRO24 |
| m | ILE35 |
| m | ASN45 |
| m | LEU46 |
| site_id | QC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CLA P 512 |
| Chain | Residue |
| P | LEU50 |
| P | HIS53 |
| P | ALA57 |
| P | PHE147 |
| P | PHE163 |
| P | HIS164 |
| P | VAL167 |
| P | ILE170 |
| P | LEU174 |
| P | CLA503 |
| P | CLA509 |
| P | CLA513 |
| P | BCR515 |
| P | LMG521 |
| site_id | QC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CLA P 513 |
| Chain | Residue |
| P | LEU50 |
| P | VAL54 |
| P | GLY128 |
| P | TYR131 |
| P | HIS132 |
| P | PRO137 |
| P | LEU140 |
| P | TYR143 |
| P | PHE147 |
| P | ILE170 |
| P | CLA512 |
| P | BCR515 |
| site_id | QC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE BCR P 514 |
| Chain | Residue |
| P | ALA55 |
| P | LEU59 |
| P | VAL116 |
| P | LEU119 |
| P | ILE120 |
| P | SER122 |
| P | ALA123 |
| P | CLA511 |
| P | BCR515 |
| c | PHE32 |
| c | BCR101 |
| l | LEU9 |
| l | VAL13 |
| site_id | QC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE BCR P 515 |
| Chain | Residue |
| P | VAL116 |
| P | SER121 |
| P | VAL124 |
| P | CLA512 |
| P | CLA513 |
| P | BCR514 |
| c | TYR15 |
| l | VAL54 |
| l | GLY55 |
| l | ASN58 |
| site_id | QC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE BCR P 516 |
| Chain | Residue |
| P | ILE209 |
| P | TYR212 |
| P | LEU213 |
| P | VAL227 |
| P | ASP232 |
| P | VAL233 |
| P | ILE240 |
| P | PHE264 |
| P | CLA501 |
| P | CLA505 |
| P | CLA507 |
| a | VAL20 |
| site_id | QC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE DGD P 517 |
| Chain | Residue |
| G | LEU151 |
| G | PHE155 |
| G | ILE163 |
| P | PRO217 |
| P | PHE218 |
| P | GLY219 |
| P | GLY220 |
| P | GLY222 |
| P | VAL225 |
| P | PHE284 |
| P | CYS288 |
| P | PHE292 |
| P | ASN294 |
| P | PRO307 |
| P | PHE361 |
| P | ARG362 |
| site_id | QC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE DGD P 518 |
| Chain | Residue |
| G | PHE197 |
| G | THR292 |
| G | SQD410 |
| G | LHG412 |
| P | TYR82 |
| P | GLU83 |
| P | GLN84 |
| P | GLY85 |
| P | LEU404 |
| P | SER406 |
| P | ASN418 |
| P | VAL420 |
| P | TRP425 |
| P | THR428 |
| P | SER429 |
| P | CLA504 |
| P | DGD519 |
| P | LMG520 |
| b | TYR33 |
| b | BCR102 |
| site_id | QC9 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE DGD P 519 |
| Chain | Residue |
| G | LEU200 |
| G | TRP278 |
| G | PHE300 |
| G | ASN301 |
| G | PHE302 |
| G | SER305 |
| G | CLA404 |
| G | SQD410 |
| P | ASN405 |
| P | ASN415 |
| P | SER416 |
| P | ASN418 |
| P | CLA504 |
| P | DGD518 |
| Q | LMG406 |
| b | PHE29 |
| b | ALA32 |
| b | TYR33 |
| b | GLY37 |
| b | SER38 |
| b | SER39 |
| b | BCR102 |
| i | GLN60 |
| site_id | RC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE LMG P 520 |
| Chain | Residue |
| P | HIS74 |
| P | CLA504 |
| P | DGD518 |
| b | BCR102 |
| c | ASP23 |
| c | VAL27 |
| c | VAL30 |
| m | ILE25 |
| site_id | RC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE LMG P 521 |
| Chain | Residue |
| P | ASP107 |
| P | PHE109 |
| P | VAL114 |
| P | VAL117 |
| P | HIS118 |
| P | CLA503 |
| P | CLA512 |
| l | PHE59 |
| site_id | RC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE LMG Q 401 |
| Chain | Residue |
| B | ALA43 |
| B | TRP75 |
| B | SER76 |
| B | TRP78 |
| B | LEU98 |
| G | LEU102 |
| G | ASP103 |
| Q | ARG304 |
| f | GLY138 |
| site_id | RC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE CLA Q 402 |
| Chain | Residue |
| G | PHE206 |
| G | CLA402 |
| G | CLA403 |
| G | CLA404 |
| Q | TRP48 |
| Q | PRO149 |
| Q | VAL152 |
| Q | PHE153 |
| Q | VAL156 |
| Q | LEU182 |
| Q | PHE185 |
| Q | GLN186 |
| Q | TRP191 |
| Q | THR192 |
| Q | HIS197 |
| Q | GLY200 |
| Q | VAL201 |
| Q | VAL204 |
| Q | LEU279 |
| Q | SER282 |
| Q | ALA283 |
| Q | PHO403 |
| site_id | RC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PHO Q 403 |
| Chain | Residue |
| G | PHE206 |
| G | ALA209 |
| G | LEU210 |
| G | MET214 |
| G | CLA404 |
| Q | ALA41 |
| Q | TRP48 |
| Q | GLY118 |
| Q | LEU122 |
| Q | PHE125 |
| Q | ASN142 |
| Q | ALA145 |
| Q | PHE146 |
| Q | ALA148 |
| Q | PHE153 |
| Q | PRO275 |
| Q | LEU279 |
| Q | CLA402 |
| site_id | RC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CLA Q 404 |
| Chain | Residue |
| Q | LEU43 |
| Q | LEU89 |
| Q | LEU90 |
| Q | LEU91 |
| Q | LEU92 |
| Q | TRP93 |
| Q | TRP104 |
| Q | THR112 |
| Q | PHE113 |
| Q | HIS117 |
| Q | LMT410 |
| j | GLY22 |
| j | LEU23 |
| j | GLY26 |
| site_id | RC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE PL9 Q 405 |
| Chain | Residue |
| G | ILE53 |
| G | ILE77 |
| G | CLA403 |
| G | LMG411 |
| Q | MET199 |
| Q | HIS214 |
| Q | THR217 |
| Q | TRP253 |
| Q | ALA260 |
| Q | PHE261 |
| Q | LEU267 |
| Q | PHE273 |
| Q | VAL274 |
| Q | THR277 |
| Q | LMG407 |
| d | LEU23 |
| d | VAL26 |
| d | LEU27 |
| d | LEU29 |
| g | PHE10 |
| site_id | RC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE LMG Q 406 |
| Chain | Residue |
| P | DGD519 |
| Q | TYR67 |
| Q | GLY70 |
| Q | PHE73 |
| S | ILE37 |
| S | GLN41 |
| S | BCR101 |
| b | PHE28 |
| b | GLY31 |
| b | ALA32 |
| b | GLY37 |
| site_id | RC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE LMG Q 407 |
| Chain | Residue |
| B | BCR618 |
| Q | PHE257 |
| Q | ALA260 |
| Q | PHE261 |
| Q | SER262 |
| Q | ASN263 |
| Q | TRP266 |
| Q | PL9405 |
| d | THR15 |
| d | TYR18 |
| d | LEU19 |
| g | PHE10 |
| g | PHE17 |
| g | ALA20 |
| site_id | SC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SQD Q 408 |
| Chain | Residue |
| N | ALA228 |
| N | ARG230 |
| N | LEU474 |
| N | LMT625 |
| Q | LYS23 |
| Q | TRP32 |
| Q | ARG134 |
| Q | LEU135 |
| site_id | SC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DGD Q 409 |
| Chain | Residue |
| Q | ASP100 |
| Q | PHE101 |
| Q | LMT410 |
| R | LEU42 |
| R | ASP45 |
| R | VAL46 |
| site_id | SC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE LMT Q 410 |
| Chain | Residue |
| Q | LEU92 |
| Q | TRP93 |
| Q | GLY99 |
| Q | CLA404 |
| Q | DGD409 |
| j | ILE21 |
| j | SER25 |
| j | GLY26 |
| site_id | SC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BCT Q 411 |
| Chain | Residue |
| G | HIS215 |
| G | GLU244 |
| G | TYR246 |
| G | HIS272 |
| G | FE2414 |
| Q | HIS214 |
| Q | TYR244 |
| Q | LYS264 |
| Q | HIS268 |
| site_id | SC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM R 101 |
| Chain | Residue |
| R | ARG8 |
| R | PHE10 |
| R | ILE13 |
| R | ARG18 |
| R | TYR19 |
| R | HIS23 |
| R | THR26 |
| R | LEU30 |
| S | ILE15 |
| S | ARG19 |
| S | TRP20 |
| S | HIS24 |
| S | ALA27 |
| S | ILE31 |
| site_id | SC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LMG R 102 |
| Chain | Residue |
| G | TYR262 |
| G | LHG412 |
| Q | PHE27 |
| R | PRO9 |
| R | PHE10 |
| R | SER11 |
| b | PL9101 |
| site_id | SC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE BCR S 101 |
| Chain | Residue |
| Q | TYR42 |
| Q | GLY46 |
| Q | GLY47 |
| Q | LEU49 |
| Q | THR50 |
| Q | PHE101 |
| Q | LMG406 |
| S | PRO29 |
| S | PHE33 |
| b | VAL21 |
| b | VAL25 |
| site_id | SC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SQD S 102 |
| Chain | Residue |
| Q | ARG24 |
| Q | ARG26 |
| R | GLU7 |
| S | PHE16 |
| S | THR17 |
| S | VAL18 |
| j | LEU32 |
| j | THR33 |
| site_id | SC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BCR W 101 |
| Chain | Residue |
| N | CLA605 |
| N | CLA613 |
| W | MET35 |
| W | LEU37 |
| W | PHE38 |
| W | PHE41 |
| j | THR11 |
| j | ILE12 |
| j | LEU16 |
| site_id | TC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DGD W 102 |
| Chain | Residue |
| N | TYR193 |
| N | PHE250 |
| N | TYR258 |
| N | TYR273 |
| N | SER277 |
| N | PHE463 |
| N | CLA606 |
| Q | HIS87 |
| Q | SER165 |
| W | TYR49 |
| W | ASN50 |
| W | VAL60 |
| W | SER61 |
| W | TRP62 |
| site_id | TC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BCR a 101 |
| Chain | Residue |
| B | LMT630 |
| G | ILE38 |
| G | LEU42 |
| G | ALA43 |
| G | TRP105 |
| G | SQD401 |
| a | PHE15 |
| site_id | TC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LMG a 102 |
| Chain | Residue |
| B | DGD628 |
| B | LMT630 |
| G | CLA406 |
| a | MET1 |
| a | THR3 |
| a | LEU4 |
| a | LMT103 |
| site_id | TC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LMT a 103 |
| Chain | Residue |
| a | THR3 |
| a | ILE6 |
| a | ILE10 |
| a | LMG102 |
| site_id | TC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PL9 b 101 |
| Chain | Residue |
| G | CLA404 |
| G | PL9407 |
| G | SQD410 |
| R | LMG102 |
| b | VAL16 |
| b | GLY20 |
| site_id | TC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BCR b 102 |
| Chain | Residue |
| G | LHG412 |
| P | DGD518 |
| P | DGD519 |
| P | LMG520 |
| b | PHE29 |
| b | TYR33 |
| site_id | TC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE BCR c 101 |
| Chain | Residue |
| P | BCR514 |
| b | ALA14 |
| b | THR15 |
| b | GLY18 |
| b | MET19 |
| c | LEU21 |
| c | LEU31 |
| c | PHE32 |
| c | PHE37 |
| c | VAL38 |
| c | ALA41 |
| l | SER16 |
| l | PHE17 |
| m | ILE28 |
| m | GLY29 |
| m | GLY32 |
| site_id | TC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE LMT e 101 |
| Chain | Residue |
| M | MET1 |
| N | TYR40 |
| N | LMG623 |
| T | BCR101 |
| e | GLN5 |
| site_id | TC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LMG e 102 |
| Chain | Residue |
| B | CLA614 |
| B | SQD627 |
| L | PRO9 |
| L | VAL10 |
| M | GLN32 |
| e | GLU30 |
| e | SER31 |
| site_id | UC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA f 301 |
| Chain | Residue |
| f | GLU81 |
| f | GLU140 |
| f | HIS257 |
| site_id | UC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEM i 201 |
| Chain | Residue |
| i | ALA62 |
| i | CYS63 |
| i | HIS67 |
| i | THR74 |
| i | LEU78 |
| i | ASP79 |
| i | THR84 |
| i | LEU85 |
| i | TYR101 |
| i | MET102 |
| i | TYR108 |
| i | HIS118 |
| i | PRO119 |
Functional Information from PROSITE/UniProt
| site_id | PS00244 |
| Number of Residues | 27 |
| Details | REACTION_CENTER Photosynthetic reaction center proteins signature. NilmhPfHqlGvagvfggalfcAmHGS |
| Chain | Residue | Details |
| A | ASN191-SER217 | |
| D | ASN190-ALA216 |
| site_id | PS00537 |
| Number of Residues | 15 |
| Details | CYTOCHROME_B559 Cytochrome b559 subunits heme-binding site signature. ItSVRYwvIHSITIP |
| Chain | Residue | Details |
| E | ILE14-PRO28 | |
| F | ILE15-PRO29 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 470 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 840 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 216 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Site: {"description":"Tyrosine radical intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11217865","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Site: {"description":"Stabilizes free radical intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 258 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 452 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 92 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PDB","id":"7RF1","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01496","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 664 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 474 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 246 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI24 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI25 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI26 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI27 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI28 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_00642","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI29 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_00643","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16172937","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22665786","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23413188","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25006873","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgang K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/B406989G"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI30 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI31 |
| Number of Residues | 28 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI32 |
| Number of Residues | 26 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI33 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00808","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI34 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"12881497","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgangb K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/b406989g"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI35 |
| Number of Residues | 6 |
| Details | Topological domain: {"description":"Lumenal"} |
| Chain | Residue | Details |
