At2g05710.1/PDB

&&&&&&&&&&&&&&&&&&&& BEGIN /usr/local/www/html/proteins/Compiled_Programs/WYRM/PyMOL_highlight_conserved_residues &&&&&&&&&&&&&&&&&&&&
Successfully read 2 file paths from WYRM_file_paths.txt
generic_input /usr/local/www/html/proteins/workspace/
generic_output /usr/local/www/html/proteins/htdocs/results/
======================================================
Sequence file type = 3
Sequence type = 3
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Sequence 1
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Sequence 2
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Read 2 amino_acid sequences from PIR Sequence file /usr/local/www/html/proteins/workspace/At2g05710-2b3xA.pir.txt
======================================================
Assigned types to 990 residues in Sequence 2-05710, 0 remain unknown
Assigned types to 888 residues in Sequence 2b3xA, 102 remain unknown
======================================================
Successfully read 576 entries for residue match scoring matrix /usr/local/www/html/proteins/workspace/BLOSUM62.dat
Read the residue match scoring matrix /usr/local/www/html/proteins/workspace/BLOSUM62.dat
======================================================
Translated sequence file At2g05710-2b3xA.pir.txt into sequence alignment.
======================================================
>2B3X.pdb Made from 6928 ATOM records in 2B3X.pdb
SNPFAHLAEPLDPVQPGKKFFNLNKLEDSRYGRLPFSIRVLLEAAIRNCD
EFLVKKQDIENILHWNVTQHKNIEVPFKPARVILQDFTGVPAVVDFAAMR
DAVKKLGGDPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNR
ERFEFLKWGSQAFHNMRIIPPGSGIIHQVNLEYLARVVFDQDGYYYPDSL
VGTDSHTTMIDGLGILGWGVGGIEAEAVMLGQPISMVLPQVIGYRLMGKP
HPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCP
EYGATAAFFPVDEVSITYLVQTGRDEEKLKYIKKYLQAVGMFRDFNDPSQ
DPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSDMKKDFESCLGAKQGFKG
FQVAPEHHNDHKTFIYDNTEFTLAHGSVVIAAITSCTNTSNPSVMLGAGL
LAKKAVDAGLNVMPYIKTSLSPGSGVVTYYLQESGVMPYLSQLGFDVVGY
GCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYL
ASPPLVIAYAIAGTIRIDFEKEPLGVNAKGQQVFLKDIWPTRDEIQAVER
QYVIPGMFKEVYQKIETVNESWNALATPSDKLFFWNSKSTYIKSPPFFEN
LTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGL
TPREFNSYGSRRGNDAVMARGTFANIRLLNRFLNKQAPQTIHLPSGEILD
VFDAAERYQQAGLPLIVLAGKEYGAGSSRDWAAKGPFLLGIKAVLAESYE
RIHRSNLVGMGVIPLEYLPGENADALGLTGQERYTIIIPENLKPQMKVQV
KLDTGKTFQAVMRFDTDVELTYFLNGGILNYMIRKMAK
======================================================
Best alignment:
2B3X.pdb 19 KFFNLNKLEDSRYGRLPFSIRVLLEAAIRNCDEFLVKKQDIENILHWNVT 68
 KF++L L D R +LP+SIR+LLE+AIRNCD F V K+D+E I+ W T
2-05710 116 KFYSLPALNDPRVDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWEKT 165
2B3X.pdb 69 QHKNIEVPFKPARVILQDFTGVPAVVDFAAMRDAVKKLGGDPEKINPVCP 118
 K +E+PFKPARV+LQDFTGVPAVVD A MRDA+ KLG D KINP+ P
2-05710 166 SPKQVEIPFKPARVLLQDFTGVPAVVDLACMRDAMNKLGSDSNKINPLVP 215
2B3X.pdb 119 ADLVIDHSIQVDFNRRADSLQKNQDLEFERNRERFEFLKWGSQAFHNMRI 168
 DLVIDHS+QVD R +++Q N +LEF+RN+ERF FLKWGS AF NM +
2-05710 216 VDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSTAFQNMLV 265
2B3X.pdb 169 IPPGSGIIHQVNLEYLARVVFDQDGYYYPDSLVGTDSHTTMIDGLGILGW 218
 +PPGSGI+HQVNLEYL RVVF+ G YPDS+VGTDSHTTMIDGLG+ GW
2-05710 266 VPPGSGIVHQVNLEYLGRVVFNTKGLLYPDSVVGTDSHTTMIDGLGVAGW 315
2B3X.pdb 219 GVGGIEAEAVMLGQPISMVLPQVIGYRLMGKPHPLVTSTDIVLTITKHLR 268
 GVGGIEAEA MLGQP+SMVLP V+G++L GK VT+TD+VLT+T+ LR
2-05710 316 GVGGIEAEATMLGQPMSMVLPGVVGFKLAGKMRNGVTATDLVLTVTQMLR 365
2B3X.pdb 269 QVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSITY 318
 + GVVGKFVEF+G G++ LS+ADRATIANM PEYGAT FFPVD V++ Y
2-05710 366 KHGVVGKFVEFYGNGMSGLSLADRATIANMSPEYGATMGFFPVDHVTLQY 415
2B3X.pdb 319 LVQTGRDEEKLKYIKKYLQAVGMFRDFNDPSQDPDFTQVVELDLKTVVPC 368
 L TGR +E + I+ YL+A MF D+N+P QD ++ +EL+L V PC
2-05710 416 LKLTGRSDETVAMIEAYLRANNMFVDYNEPQQDRVYSSYLELNLDDVEPC 465
2B3X.pdb 369 CSGPKRPQDKVAVSDMKKDFESCLGAKQGFKGFQVAPEHHNDHKTFIYDN 418
 SGPKRP D+V + +MK D+ SCL +K GFKGF + E F +D 
2-05710 466 ISGPKRPHDRVTLKEMKADWHSCLDSKVGFKGFAIPKEAQEKVVNFSFDG 515
2B3X.pdb 419 TEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVDAGLNVMPYIKT 468
 L HGSVVIAAITSCTNTSNPSVMLGAGL+AKKA D GL V P+IKT
2-05710 516 QPAELKHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACDLGLQVKPWIKT 565
2B3X.pdb 469 SLSPGSGVVTYYLQESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVE 518
 SL+PGSGVVT YL +SG+ YL++ GF++VGYGC TCIGNSG + E V 
2-05710 566 SLAPGSGVVTKYLLKSGLQEYLNEQGFNIVGYGCTTCIGNSGEINESVGA 615
2B3X.pdb 519 AITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIAGTIRID 568
 AIT+ D+VA VLSGNRNFEGRVHP TRANYLASPPLV+AYA+AGT+ ID
2-05710 616 AITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTVNID 665
2B3X.pdb 569 FEKEPLGVNAKGQQVFLKDIWPTRDEIQAVERQYVIPGMFKEVYQKIETV 618
 FE EP+G G+ VFL+DIWPT +EI V + V+P MF+ Y+ I 
2-05710 666 FETEPIGKGKNGKDVFLRDIWPTTEEIAEVVQSSVLPDMFRATYESITKG 715
2B3X.pdb 619 NESWNALATPSDKLFFWNSKSTYIKSPPFFENLTLDLQPPKSIVDAYVLL 668
 N WN L+ P + L+ W+ STYI PP+F+++T+D P ++ DAY LL
2-05710 716 NPMWNKLSVPENTLYSWDPNSTYIHEPPYFKDMTMDPPGPHNVKDAYCLL 765
2B3X.pdb 669 NLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAVM 718
 N GDS+TTDHISPAGNI ++SPAA++L RG+ ++FNSYGSRRGND +M
2-05710 766 NFGDSITTDHISPAGNIQKDSPAAKFLMERGVDRKDFNSYGSRRGNDEIM 815
2B3X.pdb 719 ARGTFANIRLLNRFLNKQ-APQTIHLPSGEILDVFDAAERYQQAGLPLIV 767
 ARGTFANIR++N+ +N + P+T+H+PSGE L VFDAA RY+ +G I+
2-05710 816 ARGTFANIRIVNKLMNGEVGPKTVHIPSGEKLSVFDAAMRYKSSGEDTII 865
2B3X.pdb 768 LAGKEYGAGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEY 817
 LAG EYG+GSSRDWAAKGP L G+KAV+A+S+ERIHRSNLVGMG+IPL +
2-05710 866 LAGAEYGSGSSRDWAAKGPMLQGVKAVIAKSFERIHRSNLVGMGIIPLCF 915
2B3X.pdb 818 LPGENADALGLTGQERYTIIIP---ENLKPQMKVQVKLDTGKTFQAVMRF 864
 GE+AD LGLTG ERYTI +P ++P V V D GK+F +RF
2-05710 916 KSGEDADTLGLTGHERYTIHLPTDISEIRPGQDVTVTTDNGKSFTCTVRF 965
2B3X.pdb 865 DTDVELTYFLNGGILNYMIRKMAK 888
 DT+VEL YF +GGIL Y+IR ++K
2-05710 966 DTEVELAYFNHGGILPYVIRNLSK 989
======================================================
Highlighted IDENTICAL residue LYS 20 index1 19 path 116 %Seq 100.00
Highlighted IDENTICAL residue PHE 21 index1 20 path 117 %Seq 100.00
Highlighted IDENTICAL residue LEU 24 index1 23 path 120 %Seq 100.00
Highlighted IDENTICAL residue LEU 27 index1 26 path 123 %Seq 100.00
Highlighted IDENTICAL residue ASP 29 index1 28 path 125 %Seq 100.00
Highlighted IDENTICAL residue ARG 31 index1 30 path 127 %Seq 100.00
Highlighted IDENTICAL residue LEU 35 index1 34 path 131 %Seq 100.00
Highlighted IDENTICAL residue PRO 36 index1 35 path 132 %Seq 100.00
Highlighted IDENTICAL residue SER 38 index1 37 path 134 %Seq 100.00
Highlighted IDENTICAL residue ILE 39 index1 38 path 135 %Seq 100.00
Highlighted IDENTICAL residue ARG 40 index1 39 path 136 %Seq 100.00
Highlighted IDENTICAL residue LEU 42 index1 41 path 138 %Seq 100.00
Highlighted IDENTICAL residue LEU 43 index1 42 path 139 %Seq 100.00
Highlighted IDENTICAL residue GLU 44 index1 43 path 140 %Seq 100.00
Highlighted IDENTICAL residue ALA 46 index1 45 path 142 %Seq 100.00
Highlighted IDENTICAL residue ILE 47 index1 46 path 143 %Seq 100.00
Highlighted IDENTICAL residue ARG 48 index1 47 path 144 %Seq 100.00
Highlighted IDENTICAL residue ASN 49 index1 48 path 145 %Seq 100.00
Highlighted IDENTICAL residue CYS 50 index1 49 path 146 %Seq 100.00
Highlighted IDENTICAL residue ASP 51 index1 50 path 147 %Seq 100.00
Highlighted IDENTICAL residue PHE 53 index1 52 path 149 %Seq 100.00
Highlighted IDENTICAL residue VAL 55 index1 54 path 151 %Seq 100.00
Highlighted IDENTICAL residue LYS 57 index1 56 path 153 %Seq 100.00
Highlighted IDENTICAL residue ASP 59 index1 58 path 155 %Seq 100.00
Highlighted IDENTICAL residue GLU 61 index1 60 path 157 %Seq 100.00
Highlighted IDENTICAL residue ILE 63 index1 62 path 159 %Seq 100.00
Highlighted IDENTICAL residue TRP 66 index1 65 path 162 %Seq 100.00
Highlighted IDENTICAL residue THR 69 index1 68 path 165 %Seq 100.00
Highlighted IDENTICAL residue LYS 72 index1 71 path 168 %Seq 100.00
Highlighted IDENTICAL residue GLU 75 index1 74 path 171 %Seq 100.00
Highlighted IDENTICAL residue PRO 77 index1 76 path 173 %Seq 100.00
Highlighted IDENTICAL residue PHE 78 index1 77 path 174 %Seq 100.00
Highlighted IDENTICAL residue LYS 79 index1 78 path 175 %Seq 100.00
Highlighted IDENTICAL residue PRO 80 index1 79 path 176 %Seq 100.00
Highlighted IDENTICAL residue ALA 81 index1 80 path 177 %Seq 100.00
Highlighted IDENTICAL residue ARG 82 index1 81 path 178 %Seq 100.00
Highlighted IDENTICAL residue VAL 83 index1 82 path 179 %Seq 100.00
Highlighted IDENTICAL residue LEU 85 index1 84 path 181 %Seq 100.00
Highlighted IDENTICAL residue GLN 86 index1 85 path 182 %Seq 100.00
Highlighted IDENTICAL residue ASP 87 index1 86 path 183 %Seq 100.00
Highlighted IDENTICAL residue PHE 88 index1 87 path 184 %Seq 100.00
Highlighted IDENTICAL residue THR 89 index1 88 path 185 %Seq 100.00
Highlighted IDENTICAL residue GLY 90 index1 89 path 186 %Seq 100.00
Highlighted IDENTICAL residue VAL 91 index1 90 path 187 %Seq 100.00
Highlighted IDENTICAL residue PRO 92 index1 91 path 188 %Seq 100.00
Highlighted IDENTICAL residue ALA 93 index1 92 path 189 %Seq 100.00
Highlighted IDENTICAL residue VAL 94 index1 93 path 190 %Seq 100.00
Highlighted IDENTICAL residue VAL 95 index1 94 path 191 %Seq 100.00
Highlighted IDENTICAL residue ASP 96 index1 95 path 192 %Seq 100.00
Highlighted IDENTICAL residue ALA 98 index1 97 path 194 %Seq 100.00
Highlighted IDENTICAL residue MET 100 index1 99 path 196 %Seq 100.00
Highlighted IDENTICAL residue ARG 101 index1 100 path 197 %Seq 100.00
Highlighted IDENTICAL residue ASP 102 index1 101 path 198 %Seq 100.00
Highlighted IDENTICAL residue ALA 103 index1 102 path 199 %Seq 100.00
Highlighted IDENTICAL residue LYS 106 index1 105 path 202 %Seq 100.00
Highlighted IDENTICAL residue LEU 107 index1 106 path 203 %Seq 100.00
Highlighted IDENTICAL residue GLY 108 index1 107 path 204 %Seq 100.00
Highlighted IDENTICAL residue ASP 110 index1 109 path 206 %Seq 100.00
Highlighted IDENTICAL residue LYS 113 index1 112 path 209 %Seq 100.00
Highlighted IDENTICAL residue ILE 114 index1 113 path 210 %Seq 100.00
Highlighted IDENTICAL residue ASN 115 index1 114 path 211 %Seq 100.00
Highlighted IDENTICAL residue PRO 116 index1 115 path 212 %Seq 100.00
Highlighted IDENTICAL residue PRO 119 index1 118 path 215 %Seq 100.00
Highlighted IDENTICAL residue ASP 121 index1 120 path 217 %Seq 100.00
Highlighted IDENTICAL residue LEU 122 index1 121 path 218 %Seq 100.00
Highlighted IDENTICAL residue VAL 123 index1 122 path 219 %Seq 100.00
Highlighted IDENTICAL residue ILE 124 index1 123 path 220 %Seq 100.00
Highlighted IDENTICAL residue ASP 125 index1 124 path 221 %Seq 100.00
Highlighted IDENTICAL residue HIS 126 index1 125 path 222 %Seq 100.00
Highlighted IDENTICAL residue SER 127 index1 126 path 223 %Seq 100.00
Highlighted IDENTICAL residue GLN 129 index1 128 path 225 %Seq 100.00
Highlighted IDENTICAL residue VAL 130 index1 129 path 226 %Seq 100.00
Highlighted IDENTICAL residue ASP 131 index1 130 path 227 %Seq 100.00
Highlighted IDENTICAL residue ARG 134 index1 133 path 230 %Seq 100.00
Highlighted IDENTICAL residue GLN 140 index1 139 path 236 %Seq 100.00
Highlighted IDENTICAL residue ASN 142 index1 141 path 238 %Seq 100.00
Highlighted IDENTICAL residue LEU 145 index1 144 path 241 %Seq 100.00
Highlighted IDENTICAL residue GLU 146 index1 145 path 242 %Seq 100.00
Highlighted IDENTICAL residue PHE 147 index1 146 path 243 %Seq 100.00
Highlighted IDENTICAL residue ARG 149 index1 148 path 245 %Seq 100.00
Highlighted IDENTICAL residue ASN 150 index1 149 path 246 %Seq 100.00
Highlighted IDENTICAL residue GLU 152 index1 151 path 248 %Seq 100.00
Highlighted IDENTICAL residue ARG 153 index1 152 path 249 %Seq 100.00
Highlighted IDENTICAL residue PHE 154 index1 153 path 250 %Seq 100.00
Highlighted IDENTICAL residue PHE 156 index1 155 path 252 %Seq 100.00
Highlighted IDENTICAL residue LEU 157 index1 156 path 253 %Seq 100.00
Highlighted IDENTICAL residue LYS 158 index1 157 path 254 %Seq 100.00
Highlighted IDENTICAL residue TRP 159 index1 158 path 255 %Seq 100.00
Highlighted IDENTICAL residue GLY 160 index1 159 path 256 %Seq 100.00
Highlighted IDENTICAL residue SER 161 index1 160 path 257 %Seq 100.00
Highlighted IDENTICAL residue ALA 163 index1 162 path 259 %Seq 100.00
Highlighted IDENTICAL residue PHE 164 index1 163 path 260 %Seq 100.00
Highlighted IDENTICAL residue ASN 166 index1 165 path 262 %Seq 100.00
Highlighted IDENTICAL residue MET 167 index1 166 path 263 %Seq 100.00
Highlighted IDENTICAL residue PRO 171 index1 170 path 267 %Seq 100.00
Highlighted IDENTICAL residue PRO 172 index1 171 path 268 %Seq 100.00
Highlighted IDENTICAL residue GLY 173 index1 172 path 269 %Seq 100.00
Highlighted IDENTICAL residue SER 174 index1 173 path 270 %Seq 100.00
Highlighted IDENTICAL residue GLY 175 index1 174 path 271 %Seq 100.00
Highlighted IDENTICAL residue ILE 176 index1 175 path 272 %Seq 100.00
Highlighted IDENTICAL residue HIS 178 index1 177 path 274 %Seq 100.00
Highlighted IDENTICAL residue GLN 179 index1 178 path 275 %Seq 100.00
Highlighted IDENTICAL residue VAL 180 index1 179 path 276 %Seq 100.00
Highlighted IDENTICAL residue ASN 181 index1 180 path 277 %Seq 100.00
Highlighted IDENTICAL residue LEU 182 index1 181 path 278 %Seq 100.00
Highlighted IDENTICAL residue GLU 183 index1 182 path 279 %Seq 100.00
Highlighted IDENTICAL residue TYR 184 index1 183 path 280 %Seq 100.00
Highlighted IDENTICAL residue LEU 185 index1 184 path 281 %Seq 100.00
Highlighted IDENTICAL residue ARG 187 index1 186 path 283 %Seq 100.00
Highlighted IDENTICAL residue VAL 188 index1 187 path 284 %Seq 100.00
Highlighted IDENTICAL residue VAL 189 index1 188 path 285 %Seq 100.00
Highlighted IDENTICAL residue PHE 190 index1 189 path 286 %Seq 100.00
Highlighted IDENTICAL residue GLY 194 index1 193 path 290 %Seq 100.00
Highlighted IDENTICAL residue TYR 197 index1 196 path 293 %Seq 100.00
Highlighted IDENTICAL residue PRO 198 index1 197 path 294 %Seq 100.00
Highlighted IDENTICAL residue ASP 199 index1 198 path 295 %Seq 100.00
Highlighted IDENTICAL residue SER 200 index1 199 path 296 %Seq 100.00
Highlighted IDENTICAL residue VAL 202 index1 201 path 298 %Seq 100.00
Highlighted IDENTICAL residue GLY 203 index1 202 path 299 %Seq 100.00
Highlighted IDENTICAL residue THR 204 index1 203 path 300 %Seq 100.00
Highlighted IDENTICAL residue ASP 205 index1 204 path 301 %Seq 100.00
Highlighted IDENTICAL residue SER 206 index1 205 path 302 %Seq 100.00
Highlighted IDENTICAL residue HIS 207 index1 206 path 303 %Seq 100.00
Highlighted IDENTICAL residue THR 208 index1 207 path 304 %Seq 100.00
Highlighted IDENTICAL residue THR 209 index1 208 path 305 %Seq 100.00
Highlighted IDENTICAL residue MET 210 index1 209 path 306 %Seq 100.00
Highlighted IDENTICAL residue ILE 211 index1 210 path 307 %Seq 100.00
Highlighted IDENTICAL residue ASP 212 index1 211 path 308 %Seq 100.00
Highlighted IDENTICAL residue GLY 213 index1 212 path 309 %Seq 100.00
Highlighted IDENTICAL residue LEU 214 index1 213 path 310 %Seq 100.00
Highlighted IDENTICAL residue GLY 215 index1 214 path 311 %Seq 100.00
Highlighted IDENTICAL residue GLY 218 index1 217 path 314 %Seq 100.00
Highlighted IDENTICAL residue TRP 219 index1 218 path 315 %Seq 100.00
Highlighted IDENTICAL residue GLY 220 index1 219 path 316 %Seq 100.00
Highlighted IDENTICAL residue VAL 221 index1 220 path 317 %Seq 100.00
Highlighted IDENTICAL residue GLY 222 index1 221 path 318 %Seq 100.00
Highlighted IDENTICAL residue GLY 223 index1 222 path 319 %Seq 100.00
Highlighted IDENTICAL residue ILE 224 index1 223 path 320 %Seq 100.00
Highlighted IDENTICAL residue GLU 225 index1 224 path 321 %Seq 100.00
Highlighted IDENTICAL residue ALA 226 index1 225 path 322 %Seq 100.00
Highlighted IDENTICAL residue GLU 227 index1 226 path 323 %Seq 100.00
Highlighted IDENTICAL residue ALA 228 index1 227 path 324 %Seq 100.00
Highlighted IDENTICAL residue MET 230 index1 229 path 326 %Seq 100.00
Highlighted IDENTICAL residue LEU 231 index1 230 path 327 %Seq 100.00
Highlighted IDENTICAL residue GLY 232 index1 231 path 328 %Seq 100.00
Highlighted IDENTICAL residue GLN 233 index1 232 path 329 %Seq 100.00
Highlighted IDENTICAL residue PRO 234 index1 233 path 330 %Seq 100.00
Highlighted IDENTICAL residue SER 236 index1 235 path 332 %Seq 100.00
Highlighted IDENTICAL residue MET 237 index1 236 path 333 %Seq 100.00
Highlighted IDENTICAL residue VAL 238 index1 237 path 334 %Seq 100.00
Highlighted IDENTICAL residue LEU 239 index1 238 path 335 %Seq 100.00
Highlighted IDENTICAL residue PRO 240 index1 239 path 336 %Seq 100.00
Highlighted IDENTICAL residue VAL 242 index1 241 path 338 %Seq 100.00
Highlighted IDENTICAL residue GLY 244 index1 243 path 340 %Seq 100.00
Highlighted IDENTICAL residue LEU 247 index1 246 path 343 %Seq 100.00
Highlighted IDENTICAL residue GLY 249 index1 248 path 345 %Seq 100.00
Highlighted IDENTICAL residue LYS 250 index1 249 path 346 %Seq 100.00
Highlighted IDENTICAL residue VAL 255 index1 254 path 351 %Seq 100.00
Highlighted IDENTICAL residue THR 256 index1 255 path 352 %Seq 100.00
Highlighted IDENTICAL residue THR 258 index1 257 path 354 %Seq 100.00
Highlighted IDENTICAL residue ASP 259 index1 258 path 355 %Seq 100.00
Highlighted IDENTICAL residue VAL 261 index1 260 path 357 %Seq 100.00
Highlighted IDENTICAL residue LEU 262 index1 261 path 358 %Seq 100.00
Highlighted IDENTICAL residue THR 263 index1 262 path 359 %Seq 100.00
Highlighted IDENTICAL residue THR 265 index1 264 path 361 %Seq 100.00
Highlighted IDENTICAL residue LEU 268 index1 267 path 364 %Seq 100.00
Highlighted IDENTICAL residue ARG 269 index1 268 path 365 %Seq 100.00
Highlighted IDENTICAL residue GLY 272 index1 271 path 368 %Seq 100.00
Highlighted IDENTICAL residue VAL 273 index1 272 path 369 %Seq 100.00
Highlighted IDENTICAL residue VAL 274 index1 273 path 370 %Seq 100.00
Highlighted IDENTICAL residue GLY 275 index1 274 path 371 %Seq 100.00
Highlighted IDENTICAL residue LYS 276 index1 275 path 372 %Seq 100.00
Highlighted IDENTICAL residue PHE 277 index1 276 path 373 %Seq 100.00
Highlighted IDENTICAL residue VAL 278 index1 277 path 374 %Seq 100.00
Highlighted IDENTICAL residue GLU 279 index1 278 path 375 %Seq 100.00
Highlighted IDENTICAL residue PHE 280 index1 279 path 376 %Seq 100.00
Highlighted IDENTICAL residue GLY 282 index1 281 path 378 %Seq 100.00
Highlighted IDENTICAL residue GLY 284 index1 283 path 380 %Seq 100.00
Highlighted IDENTICAL residue LEU 288 index1 287 path 384 %Seq 100.00
Highlighted IDENTICAL residue SER 289 index1 288 path 385 %Seq 100.00
Highlighted IDENTICAL residue ALA 291 index1 290 path 387 %Seq 100.00
Highlighted IDENTICAL residue ASP 292 index1 291 path 388 %Seq 100.00
Highlighted IDENTICAL residue ARG 293 index1 292 path 389 %Seq 100.00
Highlighted IDENTICAL residue ALA 294 index1 293 path 390 %Seq 100.00
Highlighted IDENTICAL residue THR 295 index1 294 path 391 %Seq 100.00
Highlighted IDENTICAL residue ILE 296 index1 295 path 392 %Seq 100.00
Highlighted IDENTICAL residue ALA 297 index1 296 path 393 %Seq 100.00
Highlighted IDENTICAL residue ASN 298 index1 297 path 394 %Seq 100.00
Highlighted IDENTICAL residue MET 299 index1 298 path 395 %Seq 100.00
Highlighted IDENTICAL residue PRO 301 index1 300 path 397 %Seq 100.00
Highlighted IDENTICAL residue GLU 302 index1 301 path 398 %Seq 100.00
Highlighted IDENTICAL residue TYR 303 index1 302 path 399 %Seq 100.00
Highlighted IDENTICAL residue GLY 304 index1 303 path 400 %Seq 100.00
Highlighted IDENTICAL residue ALA 305 index1 304 path 401 %Seq 100.00
Highlighted IDENTICAL residue THR 306 index1 305 path 402 %Seq 100.00
Highlighted IDENTICAL residue PHE 309 index1 308 path 405 %Seq 100.00
Highlighted IDENTICAL residue PHE 310 index1 309 path 406 %Seq 100.00
Highlighted IDENTICAL residue PRO 311 index1 310 path 407 %Seq 100.00
Highlighted IDENTICAL residue VAL 312 index1 311 path 408 %Seq 100.00
Highlighted IDENTICAL residue ASP 313 index1 312 path 409 %Seq 100.00
Highlighted IDENTICAL residue VAL 315 index1 314 path 411 %Seq 100.00
Highlighted IDENTICAL residue TYR 319 index1 318 path 415 %Seq 100.00
Highlighted IDENTICAL residue LEU 320 index1 319 path 416 %Seq 100.00
Highlighted IDENTICAL residue THR 323 index1 322 path 419 %Seq 100.00
Highlighted IDENTICAL residue GLY 324 index1 323 path 420 %Seq 100.00
Highlighted IDENTICAL residue ARG 325 index1 324 path 421 %Seq 100.00
Highlighted IDENTICAL residue GLU 328 index1 327 path 424 %Seq 100.00
Highlighted IDENTICAL residue ILE 333 index1 332 path 429 %Seq 100.00
Highlighted IDENTICAL residue TYR 336 index1 335 path 432 %Seq 100.00
Highlighted IDENTICAL residue LEU 337 index1 336 path 433 %Seq 100.00
Highlighted IDENTICAL residue ALA 339 index1 338 path 435 %Seq 100.00
Highlighted IDENTICAL residue MET 342 index1 341 path 438 %Seq 100.00
Highlighted IDENTICAL residue PHE 343 index1 342 path 439 %Seq 100.00
Highlighted IDENTICAL residue ASP 345 index1 344 path 441 %Seq 100.00
Highlighted IDENTICAL residue ASN 347 index1 346 path 443 %Seq 100.00
Highlighted IDENTICAL residue PRO 349 index1 348 path 445 %Seq 100.00
Highlighted IDENTICAL residue GLN 351 index1 350 path 447 %Seq 100.00
Highlighted IDENTICAL residue ASP 352 index1 351 path 448 %Seq 100.00
Highlighted IDENTICAL residue GLU 360 index1 359 path 456 %Seq 100.00
Highlighted IDENTICAL residue LEU 361 index1 360 path 457 %Seq 100.00
Highlighted IDENTICAL residue LEU 363 index1 362 path 459 %Seq 100.00
Highlighted IDENTICAL residue VAL 366 index1 365 path 462 %Seq 100.00
Highlighted IDENTICAL residue PRO 368 index1 367 path 464 %Seq 100.00
Highlighted IDENTICAL residue CYS 369 index1 368 path 465 %Seq 100.00
Highlighted IDENTICAL residue SER 371 index1 370 path 467 %Seq 100.00
Highlighted IDENTICAL residue GLY 372 index1 371 path 468 %Seq 100.00
Highlighted IDENTICAL residue PRO 373 index1 372 path 469 %Seq 100.00
Highlighted IDENTICAL residue LYS 374 index1 373 path 470 %Seq 100.00
Highlighted IDENTICAL residue ARG 375 index1 374 path 471 %Seq 100.00
Highlighted IDENTICAL residue PRO 376 index1 375 path 472 %Seq 100.00
Highlighted IDENTICAL residue ASP 378 index1 377 path 474 %Seq 100.00
Highlighted IDENTICAL residue VAL 380 index1 379 path 476 %Seq 100.00
Highlighted IDENTICAL residue MET 385 index1 384 path 481 %Seq 100.00
Highlighted IDENTICAL residue LYS 386 index1 385 path 482 %Seq 100.00
Highlighted IDENTICAL residue ASP 388 index1 387 path 484 %Seq 100.00
Highlighted IDENTICAL residue SER 391 index1 390 path 487 %Seq 100.00
Highlighted IDENTICAL residue CYS 392 index1 391 path 488 %Seq 100.00
Highlighted IDENTICAL residue LEU 393 index1 392 path 489 %Seq 100.00
Highlighted IDENTICAL residue LYS 396 index1 395 path 492 %Seq 100.00
Highlighted IDENTICAL residue GLY 398 index1 397 path 494 %Seq 100.00
Highlighted IDENTICAL residue PHE 399 index1 398 path 495 %Seq 100.00
Highlighted IDENTICAL residue LYS 400 index1 399 path 496 %Seq 100.00
Highlighted IDENTICAL residue GLY 401 index1 400 path 497 %Seq 100.00
Highlighted IDENTICAL residue PHE 402 index1 401 path 498 %Seq 100.00
Highlighted IDENTICAL residue GLU 407 index1 406 path 503 %Seq 100.00
Highlighted IDENTICAL residue PHE 415 index1 414 path 511 %Seq 100.00
Highlighted IDENTICAL residue ASP 418 index1 417 path 514 %Seq 100.00
Highlighted IDENTICAL residue LEU 424 index1 423 path 520 %Seq 100.00
Highlighted IDENTICAL residue HIS 426 index1 425 path 522 %Seq 100.00
Highlighted IDENTICAL residue GLY 427 index1 426 path 523 %Seq 100.00
Highlighted IDENTICAL residue SER 428 index1 427 path 524 %Seq 100.00
Highlighted IDENTICAL residue VAL 429 index1 428 path 525 %Seq 100.00
Highlighted IDENTICAL residue VAL 430 index1 429 path 526 %Seq 100.00
Highlighted IDENTICAL residue ILE 431 index1 430 path 527 %Seq 100.00
Highlighted IDENTICAL residue ALA 432 index1 431 path 528 %Seq 100.00
Highlighted IDENTICAL residue ALA 433 index1 432 path 529 %Seq 100.00
Highlighted IDENTICAL residue ILE 434 index1 433 path 530 %Seq 100.00
Highlighted IDENTICAL residue THR 435 index1 434 path 531 %Seq 100.00
Highlighted IDENTICAL residue SER 436 index1 435 path 532 %Seq 100.00
Highlighted IDENTICAL residue CYS 437 index1 436 path 533 %Seq 100.00
Highlighted IDENTICAL residue THR 438 index1 437 path 534 %Seq 100.00
Highlighted IDENTICAL residue ASN 439 index1 438 path 535 %Seq 100.00
Highlighted IDENTICAL residue THR 440 index1 439 path 536 %Seq 100.00
Highlighted IDENTICAL residue SER 441 index1 440 path 537 %Seq 100.00
Highlighted IDENTICAL residue ASN 442 index1 441 path 538 %Seq 100.00
Highlighted IDENTICAL residue PRO 443 index1 442 path 539 %Seq 100.00
Highlighted IDENTICAL residue SER 444 index1 443 path 540 %Seq 100.00
Highlighted IDENTICAL residue VAL 445 index1 444 path 541 %Seq 100.00
Highlighted IDENTICAL residue MET 446 index1 445 path 542 %Seq 100.00
Highlighted IDENTICAL residue LEU 447 index1 446 path 543 %Seq 100.00
Highlighted IDENTICAL residue GLY 448 index1 447 path 544 %Seq 100.00
Highlighted IDENTICAL residue ALA 449 index1 448 path 545 %Seq 100.00
Highlighted IDENTICAL residue GLY 450 index1 449 path 546 %Seq 100.00
Highlighted IDENTICAL residue LEU 451 index1 450 path 547 %Seq 100.00
Highlighted IDENTICAL residue ALA 453 index1 452 path 549 %Seq 100.00
Highlighted IDENTICAL residue LYS 454 index1 453 path 550 %Seq 100.00
Highlighted IDENTICAL residue LYS 455 index1 454 path 551 %Seq 100.00
Highlighted IDENTICAL residue ALA 456 index1 455 path 552 %Seq 100.00
Highlighted IDENTICAL residue ASP 458 index1 457 path 554 %Seq 100.00
Highlighted IDENTICAL residue GLY 460 index1 459 path 556 %Seq 100.00
Highlighted IDENTICAL residue LEU 461 index1 460 path 557 %Seq 100.00
Highlighted IDENTICAL residue VAL 463 index1 462 path 559 %Seq 100.00
Highlighted IDENTICAL residue PRO 465 index1 464 path 561 %Seq 100.00
Highlighted IDENTICAL residue ILE 467 index1 466 path 563 %Seq 100.00
Highlighted IDENTICAL residue LYS 468 index1 467 path 564 %Seq 100.00
Highlighted IDENTICAL residue THR 469 index1 468 path 565 %Seq 100.00
Highlighted IDENTICAL residue SER 470 index1 469 path 566 %Seq 100.00
Highlighted IDENTICAL residue LEU 471 index1 470 path 567 %Seq 100.00
Highlighted IDENTICAL residue PRO 473 index1 472 path 569 %Seq 100.00
Highlighted IDENTICAL residue GLY 474 index1 473 path 570 %Seq 100.00
Highlighted IDENTICAL residue SER 475 index1 474 path 571 %Seq 100.00
Highlighted IDENTICAL residue GLY 476 index1 475 path 572 %Seq 100.00
Highlighted IDENTICAL residue VAL 477 index1 476 path 573 %Seq 100.00
Highlighted IDENTICAL residue VAL 478 index1 477 path 574 %Seq 100.00
Highlighted IDENTICAL residue THR 479 index1 478 path 575 %Seq 100.00
Highlighted IDENTICAL residue TYR 481 index1 480 path 577 %Seq 100.00
Highlighted IDENTICAL residue LEU 482 index1 481 path 578 %Seq 100.00
Highlighted IDENTICAL residue SER 485 index1 484 path 581 %Seq 100.00
Highlighted IDENTICAL residue GLY 486 index1 485 path 582 %Seq 100.00
Highlighted IDENTICAL residue TYR 490 index1 489 path 586 %Seq 100.00
Highlighted IDENTICAL residue LEU 491 index1 490 path 587 %Seq 100.00
Highlighted IDENTICAL residue GLY 495 index1 494 path 591 %Seq 100.00
Highlighted IDENTICAL residue PHE 496 index1 495 path 592 %Seq 100.00
Highlighted IDENTICAL residue VAL 499 index1 498 path 595 %Seq 100.00
Highlighted IDENTICAL residue GLY 500 index1 499 path 596 %Seq 100.00
Highlighted IDENTICAL residue TYR 501 index1 500 path 597 %Seq 100.00
Highlighted IDENTICAL residue GLY 502 index1 501 path 598 %Seq 100.00
Highlighted IDENTICAL residue CYS 503 index1 502 path 599 %Seq 100.00
Highlighted IDENTICAL residue THR 505 index1 504 path 601 %Seq 100.00
Highlighted IDENTICAL residue CYS 506 index1 505 path 602 %Seq 100.00
Highlighted IDENTICAL residue ILE 507 index1 506 path 603 %Seq 100.00
Highlighted IDENTICAL residue GLY 508 index1 507 path 604 %Seq 100.00
Highlighted IDENTICAL residue ASN 509 index1 508 path 605 %Seq 100.00
Highlighted IDENTICAL residue SER 510 index1 509 path 606 %Seq 100.00
Highlighted IDENTICAL residue GLY 511 index1 510 path 607 %Seq 100.00
Highlighted IDENTICAL residue GLU 515 index1 514 path 611 %Seq 100.00
Highlighted IDENTICAL residue VAL 517 index1 516 path 613 %Seq 100.00
Highlighted IDENTICAL residue ALA 520 index1 519 path 616 %Seq 100.00
Highlighted IDENTICAL residue ILE 521 index1 520 path 617 %Seq 100.00
Highlighted IDENTICAL residue THR 522 index1 521 path 618 %Seq 100.00
Highlighted IDENTICAL residue ASP 525 index1 524 path 621 %Seq 100.00
Highlighted IDENTICAL residue VAL 527 index1 526 path 623 %Seq 100.00
Highlighted IDENTICAL residue ALA 528 index1 527 path 624 %Seq 100.00
Highlighted IDENTICAL residue VAL 531 index1 530 path 627 %Seq 100.00
Highlighted IDENTICAL residue LEU 532 index1 531 path 628 %Seq 100.00
Highlighted IDENTICAL residue SER 533 index1 532 path 629 %Seq 100.00
Highlighted IDENTICAL residue GLY 534 index1 533 path 630 %Seq 100.00
Highlighted IDENTICAL residue ASN 535 index1 534 path 631 %Seq 100.00
Highlighted IDENTICAL residue ARG 536 index1 535 path 632 %Seq 100.00
Highlighted IDENTICAL residue ASN 537 index1 536 path 633 %Seq 100.00
Highlighted IDENTICAL residue PHE 538 index1 537 path 634 %Seq 100.00
Highlighted IDENTICAL residue GLU 539 index1 538 path 635 %Seq 100.00
Highlighted IDENTICAL residue GLY 540 index1 539 path 636 %Seq 100.00
Highlighted IDENTICAL residue ARG 541 index1 540 path 637 %Seq 100.00
Highlighted IDENTICAL residue VAL 542 index1 541 path 638 %Seq 100.00
Highlighted IDENTICAL residue HIS 543 index1 542 path 639 %Seq 100.00
Highlighted IDENTICAL residue PRO 544 index1 543 path 640 %Seq 100.00
Highlighted IDENTICAL residue THR 546 index1 545 path 642 %Seq 100.00
Highlighted IDENTICAL residue ARG 547 index1 546 path 643 %Seq 100.00
Highlighted IDENTICAL residue ALA 548 index1 547 path 644 %Seq 100.00
Highlighted IDENTICAL residue ASN 549 index1 548 path 645 %Seq 100.00
Highlighted IDENTICAL residue TYR 550 index1 549 path 646 %Seq 100.00
Highlighted IDENTICAL residue LEU 551 index1 550 path 647 %Seq 100.00
Highlighted IDENTICAL residue ALA 552 index1 551 path 648 %Seq 100.00
Highlighted IDENTICAL residue SER 553 index1 552 path 649 %Seq 100.00
Highlighted IDENTICAL residue PRO 554 index1 553 path 650 %Seq 100.00
Highlighted IDENTICAL residue PRO 555 index1 554 path 651 %Seq 100.00
Highlighted IDENTICAL residue LEU 556 index1 555 path 652 %Seq 100.00
Highlighted IDENTICAL residue VAL 557 index1 556 path 653 %Seq 100.00
Highlighted IDENTICAL residue ALA 559 index1 558 path 655 %Seq 100.00
Highlighted IDENTICAL residue TYR 560 index1 559 path 656 %Seq 100.00
Highlighted IDENTICAL residue ALA 561 index1 560 path 657 %Seq 100.00
Highlighted IDENTICAL residue ALA 563 index1 562 path 659 %Seq 100.00
Highlighted IDENTICAL residue GLY 564 index1 563 path 660 %Seq 100.00
Highlighted IDENTICAL residue THR 565 index1 564 path 661 %Seq 100.00
Highlighted IDENTICAL residue ILE 568 index1 567 path 664 %Seq 100.00
Highlighted IDENTICAL residue ASP 569 index1 568 path 665 %Seq 100.00
Highlighted IDENTICAL residue PHE 570 index1 569 path 666 %Seq 100.00
Highlighted IDENTICAL residue GLU 571 index1 570 path 667 %Seq 100.00
Highlighted IDENTICAL residue GLU 573 index1 572 path 669 %Seq 100.00
Highlighted IDENTICAL residue PRO 574 index1 573 path 670 %Seq 100.00
Highlighted IDENTICAL residue GLY 576 index1 575 path 672 %Seq 100.00
Highlighted IDENTICAL residue GLY 581 index1 580 path 677 %Seq 100.00
Highlighted IDENTICAL residue VAL 584 index1 583 path 680 %Seq 100.00
Highlighted IDENTICAL residue PHE 585 index1 584 path 681 %Seq 100.00
Highlighted IDENTICAL residue LEU 586 index1 585 path 682 %Seq 100.00
Highlighted IDENTICAL residue ASP 588 index1 587 path 684 %Seq 100.00
Highlighted IDENTICAL residue ILE 589 index1 588 path 685 %Seq 100.00
Highlighted IDENTICAL residue TRP 590 index1 589 path 686 %Seq 100.00
Highlighted IDENTICAL residue PRO 591 index1 590 path 687 %Seq 100.00
Highlighted IDENTICAL residue THR 592 index1 591 path 688 %Seq 100.00
Highlighted IDENTICAL residue GLU 595 index1 594 path 691 %Seq 100.00
Highlighted IDENTICAL residue ILE 596 index1 595 path 692 %Seq 100.00
Highlighted IDENTICAL residue VAL 599 index1 598 path 695 %Seq 100.00
Highlighted IDENTICAL residue VAL 604 index1 603 path 700 %Seq 100.00
Highlighted IDENTICAL residue PRO 606 index1 605 path 702 %Seq 100.00
Highlighted IDENTICAL residue MET 608 index1 607 path 704 %Seq 100.00
Highlighted IDENTICAL residue PHE 609 index1 608 path 705 %Seq 100.00
Highlighted IDENTICAL residue TYR 613 index1 612 path 709 %Seq 100.00
Highlighted IDENTICAL residue ILE 616 index1 615 path 712 %Seq 100.00
Highlighted IDENTICAL residue ASN 620 index1 619 path 716 %Seq 100.00
Highlighted IDENTICAL residue TRP 623 index1 622 path 719 %Seq 100.00
Highlighted IDENTICAL residue ASN 624 index1 623 path 720 %Seq 100.00
Highlighted IDENTICAL residue LEU 626 index1 625 path 722 %Seq 100.00
Highlighted IDENTICAL residue PRO 629 index1 628 path 725 %Seq 100.00
Highlighted IDENTICAL residue LEU 633 index1 632 path 729 %Seq 100.00
Highlighted IDENTICAL residue TRP 636 index1 635 path 732 %Seq 100.00
Highlighted IDENTICAL residue SER 640 index1 639 path 736 %Seq 100.00
Highlighted IDENTICAL residue THR 641 index1 640 path 737 %Seq 100.00
Highlighted IDENTICAL residue TYR 642 index1 641 path 738 %Seq 100.00
Highlighted IDENTICAL residue ILE 643 index1 642 path 739 %Seq 100.00
Highlighted IDENTICAL residue PRO 646 index1 645 path 742 %Seq 100.00
Highlighted IDENTICAL residue PRO 647 index1 646 path 743 %Seq 100.00
Highlighted IDENTICAL residue PHE 649 index1 648 path 745 %Seq 100.00
Highlighted IDENTICAL residue THR 653 index1 652 path 749 %Seq 100.00
Highlighted IDENTICAL residue ASP 655 index1 654 path 751 %Seq 100.00
Highlighted IDENTICAL residue PRO 659 index1 658 path 755 %Seq 100.00
Highlighted IDENTICAL residue ASP 664 index1 663 path 760 %Seq 100.00
Highlighted IDENTICAL residue ALA 665 index1 664 path 761 %Seq 100.00
Highlighted IDENTICAL residue TYR 666 index1 665 path 762 %Seq 100.00
Highlighted IDENTICAL residue LEU 668 index1 667 path 764 %Seq 100.00
Highlighted IDENTICAL residue LEU 669 index1 668 path 765 %Seq 100.00
Highlighted IDENTICAL residue ASN 670 index1 669 path 766 %Seq 100.00
Highlighted IDENTICAL residue GLY 672 index1 671 path 768 %Seq 100.00
Highlighted IDENTICAL residue ASP 673 index1 672 path 769 %Seq 100.00
Highlighted IDENTICAL residue SER 674 index1 673 path 770 %Seq 100.00
Highlighted IDENTICAL residue THR 676 index1 675 path 772 %Seq 100.00
Highlighted IDENTICAL residue THR 677 index1 676 path 773 %Seq 100.00
Highlighted IDENTICAL residue ASP 678 index1 677 path 774 %Seq 100.00
Highlighted IDENTICAL residue HIS 679 index1 678 path 775 %Seq 100.00
Highlighted IDENTICAL residue ILE 680 index1 679 path 776 %Seq 100.00
Highlighted IDENTICAL residue SER 681 index1 680 path 777 %Seq 100.00
Highlighted IDENTICAL residue PRO 682 index1 681 path 778 %Seq 100.00
Highlighted IDENTICAL residue ALA 683 index1 682 path 779 %Seq 100.00
Highlighted IDENTICAL residue GLY 684 index1 683 path 780 %Seq 100.00
Highlighted IDENTICAL residue ASN 685 index1 684 path 781 %Seq 100.00
Highlighted IDENTICAL residue ILE 686 index1 685 path 782 %Seq 100.00
Highlighted IDENTICAL residue SER 690 index1 689 path 786 %Seq 100.00
Highlighted IDENTICAL residue PRO 691 index1 690 path 787 %Seq 100.00
Highlighted IDENTICAL residue ALA 692 index1 691 path 788 %Seq 100.00
Highlighted IDENTICAL residue ALA 693 index1 692 path 789 %Seq 100.00
Highlighted IDENTICAL residue LEU 696 index1 695 path 792 %Seq 100.00
Highlighted IDENTICAL residue ARG 699 index1 698 path 795 %Seq 100.00
Highlighted IDENTICAL residue GLY 700 index1 699 path 796 %Seq 100.00
Highlighted IDENTICAL residue PHE 706 index1 705 path 802 %Seq 100.00
Highlighted IDENTICAL residue ASN 707 index1 706 path 803 %Seq 100.00
Highlighted IDENTICAL residue SER 708 index1 707 path 804 %Seq 100.00
Highlighted IDENTICAL residue TYR 709 index1 708 path 805 %Seq 100.00
Highlighted IDENTICAL residue GLY 710 index1 709 path 806 %Seq 100.00
Highlighted IDENTICAL residue SER 711 index1 710 path 807 %Seq 100.00
Highlighted IDENTICAL residue ARG 712 index1 711 path 808 %Seq 100.00
Highlighted IDENTICAL residue ARG 713 index1 712 path 809 %Seq 100.00
Highlighted IDENTICAL residue GLY 714 index1 713 path 810 %Seq 100.00
Highlighted IDENTICAL residue ASN 715 index1 714 path 811 %Seq 100.00
Highlighted IDENTICAL residue ASP 716 index1 715 path 812 %Seq 100.00
Highlighted IDENTICAL residue MET 719 index1 718 path 815 %Seq 100.00
Highlighted IDENTICAL residue ALA 720 index1 719 path 816 %Seq 100.00
Highlighted IDENTICAL residue ARG 721 index1 720 path 817 %Seq 100.00
Highlighted IDENTICAL residue GLY 722 index1 721 path 818 %Seq 100.00
Highlighted IDENTICAL residue THR 723 index1 722 path 819 %Seq 100.00
Highlighted IDENTICAL residue PHE 724 index1 723 path 820 %Seq 100.00
Highlighted IDENTICAL residue ALA 725 index1 724 path 821 %Seq 100.00
Highlighted IDENTICAL residue ASN 726 index1 725 path 822 %Seq 100.00
Highlighted IDENTICAL residue ILE 727 index1 726 path 823 %Seq 100.00
Highlighted IDENTICAL residue ARG 728 index1 727 path 824 %Seq 100.00
Highlighted IDENTICAL residue ASN 731 index1 730 path 827 %Seq 100.00
Highlighted IDENTICAL residue ASN 735 index1 734 path 831 %Seq 100.00
Highlighted IDENTICAL residue LYS 736 index1 735 path 832 %Seq 50.00
Highlighted IDENTICAL residue PRO 739 index1 738 path 836 %Seq 100.00
Highlighted IDENTICAL residue THR 741 index1 740 path 838 %Seq 100.00
Highlighted IDENTICAL residue HIS 743 index1 742 path 840 %Seq 100.00
Highlighted IDENTICAL residue PRO 745 index1 744 path 842 %Seq 100.00
Highlighted IDENTICAL residue SER 746 index1 745 path 843 %Seq 100.00
Highlighted IDENTICAL residue GLY 747 index1 746 path 844 %Seq 100.00
Highlighted IDENTICAL residue GLU 748 index1 747 path 845 %Seq 100.00
Highlighted IDENTICAL residue LEU 750 index1 749 path 847 %Seq 100.00
Highlighted IDENTICAL residue VAL 752 index1 751 path 849 %Seq 100.00
Highlighted IDENTICAL residue PHE 753 index1 752 path 850 %Seq 100.00
Highlighted IDENTICAL residue ASP 754 index1 753 path 851 %Seq 100.00
Highlighted IDENTICAL residue ALA 755 index1 754 path 852 %Seq 100.00
Highlighted IDENTICAL residue ALA 756 index1 755 path 853 %Seq 100.00
Highlighted IDENTICAL residue ARG 758 index1 757 path 855 %Seq 100.00
Highlighted IDENTICAL residue TYR 759 index1 758 path 856 %Seq 100.00
Highlighted IDENTICAL residue GLY 763 index1 762 path 860 %Seq 100.00
Highlighted IDENTICAL residue ILE 767 index1 766 path 864 %Seq 100.00
Highlighted IDENTICAL residue LEU 769 index1 768 path 866 %Seq 100.00
Highlighted IDENTICAL residue ALA 770 index1 769 path 867 %Seq 100.00
Highlighted IDENTICAL residue GLY 771 index1 770 path 868 %Seq 100.00
Highlighted IDENTICAL residue GLU 773 index1 772 path 870 %Seq 100.00
Highlighted IDENTICAL residue TYR 774 index1 773 path 871 %Seq 100.00
Highlighted IDENTICAL residue GLY 775 index1 774 path 872 %Seq 100.00
Highlighted IDENTICAL residue GLY 777 index1 776 path 874 %Seq 100.00
Highlighted IDENTICAL residue SER 778 index1 777 path 875 %Seq 100.00
Highlighted IDENTICAL residue SER 779 index1 778 path 876 %Seq 100.00
Highlighted IDENTICAL residue ARG 780 index1 779 path 877 %Seq 100.00
Highlighted IDENTICAL residue ASP 781 index1 780 path 878 %Seq 100.00
Highlighted IDENTICAL residue TRP 782 index1 781 path 879 %Seq 100.00
Highlighted IDENTICAL residue ALA 783 index1 782 path 880 %Seq 100.00
Highlighted IDENTICAL residue ALA 784 index1 783 path 881 %Seq 100.00
Highlighted IDENTICAL residue LYS 785 index1 784 path 882 %Seq 100.00
Highlighted IDENTICAL residue GLY 786 index1 785 path 883 %Seq 100.00
Highlighted IDENTICAL residue PRO 787 index1 786 path 884 %Seq 100.00
Highlighted IDENTICAL residue LEU 789 index1 788 path 886 %Seq 100.00
Highlighted IDENTICAL residue GLY 791 index1 790 path 888 %Seq 100.00
Highlighted IDENTICAL residue LYS 793 index1 792 path 890 %Seq 100.00
Highlighted IDENTICAL residue ALA 794 index1 793 path 891 %Seq 100.00
Highlighted IDENTICAL residue VAL 795 index1 794 path 892 %Seq 100.00
Highlighted IDENTICAL residue ALA 797 index1 796 path 894 %Seq 100.00
Highlighted IDENTICAL residue SER 799 index1 798 path 896 %Seq 100.00
Highlighted IDENTICAL residue GLU 801 index1 800 path 898 %Seq 100.00
Highlighted IDENTICAL residue ARG 802 index1 801 path 899 %Seq 100.00
Highlighted IDENTICAL residue ILE 803 index1 802 path 900 %Seq 100.00
Highlighted IDENTICAL residue HIS 804 index1 803 path 901 %Seq 100.00
Highlighted IDENTICAL residue ARG 805 index1 804 path 902 %Seq 100.00
Highlighted IDENTICAL residue SER 806 index1 805 path 903 %Seq 100.00
Highlighted IDENTICAL residue ASN 807 index1 806 path 904 %Seq 100.00
Highlighted IDENTICAL residue LEU 808 index1 807 path 905 %Seq 100.00
Highlighted IDENTICAL residue VAL 809 index1 808 path 906 %Seq 100.00
Highlighted IDENTICAL residue GLY 810 index1 809 path 907 %Seq 100.00
Highlighted IDENTICAL residue MET 811 index1 810 path 908 %Seq 100.00
Highlighted IDENTICAL residue GLY 812 index1 811 path 909 %Seq 100.00
Highlighted IDENTICAL residue ILE 814 index1 813 path 911 %Seq 100.00
Highlighted IDENTICAL residue PRO 815 index1 814 path 912 %Seq 100.00
Highlighted IDENTICAL residue LEU 816 index1 815 path 913 %Seq 100.00
Highlighted IDENTICAL residue GLY 821 index1 820 path 918 %Seq 100.00
Highlighted IDENTICAL residue GLU 822 index1 821 path 919 %Seq 100.00
Highlighted IDENTICAL residue ALA 824 index1 823 path 921 %Seq 100.00
Highlighted IDENTICAL residue ASP 825 index1 824 path 922 %Seq 100.00
Highlighted IDENTICAL residue LEU 827 index1 826 path 924 %Seq 100.00
Highlighted IDENTICAL residue GLY 828 index1 827 path 925 %Seq 100.00
Highlighted IDENTICAL residue LEU 829 index1 828 path 926 %Seq 100.00
Highlighted IDENTICAL residue THR 830 index1 829 path 927 %Seq 100.00
Highlighted IDENTICAL residue GLY 831 index1 830 path 928 %Seq 100.00
Highlighted IDENTICAL residue GLU 833 index1 832 path 930 %Seq 100.00
Highlighted IDENTICAL residue ARG 834 index1 833 path 931 %Seq 100.00
Highlighted IDENTICAL residue TYR 835 index1 834 path 932 %Seq 100.00
Highlighted IDENTICAL residue THR 836 index1 835 path 933 %Seq 100.00
Highlighted IDENTICAL residue ILE 837 index1 836 path 934 %Seq 100.00
Highlighted IDENTICAL residue PRO 840 index1 839 path 937 %Seq 100.00
Highlighted IDENTICAL residue GLU 841 index1 840 path 941 %Seq 50.00
Highlighted IDENTICAL residue ASN 842 index1 841 path 942 %Seq 50.00
Highlighted IDENTICAL residue PRO 845 index1 844 path 945 %Seq 100.00
Highlighted IDENTICAL residue VAL 849 index1 848 path 949 %Seq 100.00
Highlighted IDENTICAL residue VAL 851 index1 850 path 951 %Seq 100.00
Highlighted IDENTICAL residue ASP 854 index1 853 path 954 %Seq 100.00
Highlighted IDENTICAL residue GLY 856 index1 855 path 956 %Seq 100.00
Highlighted IDENTICAL residue LYS 857 index1 856 path 957 %Seq 100.00
Highlighted IDENTICAL residue PHE 859 index1 858 path 959 %Seq 100.00
Highlighted IDENTICAL residue ARG 864 index1 863 path 964 %Seq 100.00
Highlighted IDENTICAL residue PHE 865 index1 864 path 965 %Seq 100.00
Highlighted IDENTICAL residue ASP 866 index1 865 path 966 %Seq 100.00
Highlighted IDENTICAL residue THR 867 index1 866 path 967 %Seq 100.00
Highlighted IDENTICAL residue VAL 869 index1 868 path 969 %Seq 100.00
Highlighted IDENTICAL residue GLU 870 index1 869 path 970 %Seq 100.00
Highlighted IDENTICAL residue LEU 871 index1 870 path 971 %Seq 100.00
Highlighted IDENTICAL residue TYR 873 index1 872 path 973 %Seq 100.00
Highlighted IDENTICAL residue PHE 874 index1 873 path 974 %Seq 100.00
Highlighted IDENTICAL residue GLY 877 index1 876 path 977 %Seq 100.00
Highlighted IDENTICAL residue GLY 878 index1 877 path 978 %Seq 100.00
Highlighted IDENTICAL residue ILE 879 index1 878 path 979 %Seq 100.00
Highlighted IDENTICAL residue LEU 880 index1 879 path 980 %Seq 100.00
Highlighted IDENTICAL residue TYR 882 index1 881 path 982 %Seq 100.00
Highlighted IDENTICAL residue ILE 884 index1 883 path 984 %Seq 100.00
Highlighted IDENTICAL residue ARG 885 index1 884 path 985 %Seq 100.00
Highlighted IDENTICAL residue LYS 889 index1 888 path 989 %Seq 100.00
Highlighted 545 residues for visualization
Wrote PyMOL macro into file /usr/local/www/html/proteins/htdocs/results/At2g05710-2b3xA.pir.txt.2B3X.pdb.conservation.pml
===============================================================================
The program
/usr/local/www/html/proteins/Compiled_Programs/WYRM/PyMOL_highlight_conserved_residues At2g05710-2b3xA.pir.txt PIR amino_acid 2B3X.pdb _ 100.0 BLOSUM62.dat 
completed successfully.
@@@@@@@@@@@@@@@@@@@@ END /usr/local/www/html/proteins/Compiled_Programs/WYRM/PyMOL_highlight_conserved_residues @@@@@@@@@@@@@@@@@@@@