At2g02790.1/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
Got here 1
Got here 2
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Sequence 1
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Sequence 2
Got here 3
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Read 2 amino_acid sequences from PIR Sequence file /usr/local/www/html/proteins/workspace/At2g02790-2dfsA.pir.txt
======================================================
Assigned types to 636 residues in Sequence 2-02790, 23 remain unknown
Assigned types to 212 residues in Sequence 2dfsA, 447 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 At2g02790-2dfsA.pir.txt into sequence alignment.
======================================================
>2DFS.pdb Made from 29614 ATOM records in 2DFS.pdb
ELYTKYARVWIPDPEEVWKSAELLKDYKPGDKVLQLRLEEGKDLEYCLDP
KTKELPPLRNPDILVGENDLTALSYLHEPAVLHNLKVRFIDSKLIYTYCG
IVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDE
RNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIME
SIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAE
EERNYHIFYQLCASAALPEFKTLRLGNANYFHYTKQGGSPVIDGIDDAKE
MVNTRQACTLLGISDSYQMGIFRILAGILHLGNVEFASRDSDSCAIPPKH
DPLTIFCDLMGVDYEEMAHWLCHRKLATYIKPISKLHAINARDALAKHIY
ANLFNWIVDHVNKALHSTVKQHSFIGVLDIYGFETFEINSFEQFCINYAN
EKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIEAKMGVLDL
LDEECKMPKGSDDTWAQKLYNTHLNKCALFEKPRLSNKAFIIKHFADKVE
YQCEGFLEKNKDTVYEEQIKVLKSSKKFKLLPELFQHKKTVGHQFRNSLH
LLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISA
AGFPSRWTYQEFFSRYRVLMKQKDVLSDRKQTCKNVLEKLILDKDKYQFG
KTKIFFRAGQVAYLEKIRADKLRAACIRIQKTIRGWLMRKKYMRMRRAAI
TIQRYVRGHQARCYATFLRRTRAAIIIQKFQRMYVVRKRYQCMRDATIAL
QALLRGYLVRNKYQMMLREHKSIIIQKHVRGWLARVHYHRTLKAIVYLQC
CYRRMMAKRELKKLMNNLEITYSTETEKLRSDVERLRMSEEEAKNATNRV
LSLQEEIAKLRKELHQTQTEKKTIEEWADKYKHETEQLVSELKEQNTLLK
TEKEELNRRIHDQAKEITETMEKKLVEETKQLELDLNDERLRYQAEFKEA
FSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDF
PEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEK
LTDEEVDEMIREADIDGDGQVNYEEFVQMMTAKQIAEFKEAFSLFDKDGD
GTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMAR
KMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEM
IREADIDGDGQVNYEEFVQMMTAKAEFKEAFSLFDKDGDGTITTKELGTV
MRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEI
REAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQ
VNYEEFVQMMTAKQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPT
EAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDK
DGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQM
MTAKAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEV
DADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAEL
RHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAKQIAEFKE
AFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTID
FPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGE
KLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAKELYTKYARVWIPDPEE
VWKSAELLKDYKPGDKVLQLRLEEGKDLEYCLDPKTKELPPLRNPDILVG
ENDLTALSYLHEPAVLHNLKVRFIDSKLIYTYCGIVLVAINPYEQLPIYG
EDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKT
VSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRF
GKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAA
LPEFKTLRLGNANYFHYTKQGGSPVIDGIDDAKEMVNTRQACTLLGISDS
YQMGIFRILAGILHLGNVEFASRDSDSCAIPPKHDPLTIFCDLMGVDYEE
MAHWLCHRKLATYIKPISKLHAINARDALAKHIYANLFNWIVDHVNKALH
STVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ
EEYMKEQIPWTLIDFYDNQPCINLIEAKMGVLDLLDEECKMPKGSDDTWA
QKLYNTHLNKCALFEKPRLSNKAFIIKHFADKVEYQCEGFLEKNKDTVYE
EQIKVLKSSKKFKLLPELFQHKKTVGHQFRNSLHLLMETLNATTPHYVRC
IKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRY
RVLMKQKDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEK
IRADKLRAACIRIQKTIRGWLMRKKYMRMRRAAITIQRYVRGHQARCYAT
FLRRTRAAIIIQKFQRMYVVRKRYQCMRDATIALQALLRGYLVRNKYQMM
LREHKSIIIQKHVRGWLARVHYHRTLKAIVYLQCCYRRMMAKRELKKLMN
NLEITYSTETEKLRSDVERLRMSEEEAKNATNRVLSLQEEIAKLRKELHQ
TQTEKKTIEEWADKYKHETEQLVSELKEQNTLLKTEKEELNRRIHDQAKE
ITETMEKKLVEETKQLELDLNDERLRYQAEFKEAFSLFDKDGDGTITTKE
LGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDS
EEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADID
GDGQVNYEEFVQMMTAKQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLG
QNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFR
VFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEE
FVQMMTAKAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDM
INEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYIS
AAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAKQIA
EFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMT
NLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAKAEFKEAFSLFDK
DGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTM
MARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEV
DEMIREADIDGDGQVNYEEFVQMMTAKQIAEFKEAFSLFDKDGDGTITTK
ELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTD
SEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADI
DGDGQVNYEEFVQMMTAK
======================================================
Best alignment:
2DFS.pdb 880 RSDVERLRMSEEEAKNATNRVLSLQEEIAKLRKELHQTQTEKKTIEEWAD 929
 S R E+ K + +L +E++K+ + Q+ +K+ +
2-02790 293 NSSTSRSTADNEKPKRTVRKASTLGKELSKIEND-KSKQSSRKSTSAIKE 341
2DFS.pdb 930 KYKHETEQLVSELKEQNTLLKTEKEELNRRIHDQAKEITETMEKKL-VEE 978
 E + + + L + R+ ++ KEI + ++K+L +EE
2-02790 342 GSSVEVKDEKPRISHKKASLSNGIGKATRKSAEKKKEIADAVQKELPIEE 391
2DFS.pdb 979 TKQLELDL-NDERLRYQAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQN 1027
 +D DE++ S DKD + K +R+ + 
2-02790 392 VSVSLVDAPEDEKMNLIPVTISKESDLDKDEKSLVLDKPEQDELRT-AER 440
2DFS.pdb 1028 PTEAELQDMINEVDADGNGTIDFPE 1052
 +AE + E D I P+
2-02790 441 DDKAEEELKTAERDDSAEEKIQEPD 465
======================================================
Highlighted IDENTICAL residue ARG 966 index1 880 path 316 %Seq 50.00
Highlighted IDENTICAL residue SER 967 index1 881 path 317 %Seq 50.00
Highlighted IDENTICAL residue ASP 968 index1 882 path 318 %Seq 50.00
Highlighted IDENTICAL residue VAL 969 index1 883 path 319 %Seq 50.00
Highlighted IDENTICAL residue GLU 970 index1 884 path 320 %Seq 50.00
Highlighted IDENTICAL residue ARG 971 index1 885 path 321 %Seq 50.00
Highlighted IDENTICAL residue LEU 972 index1 886 path 322 %Seq 50.00
Highlighted IDENTICAL residue ARG 973 index1 887 path 323 %Seq 50.00
Highlighted IDENTICAL residue MET 974 index1 888 path 324 %Seq 50.00
Highlighted IDENTICAL residue SER 975 index1 889 path 325 %Seq 50.00
Highlighted IDENTICAL residue GLU 976 index1 890 path 326 %Seq 50.00
Highlighted IDENTICAL residue GLU 977 index1 891 path 327 %Seq 50.00
Highlighted IDENTICAL residue GLU 978 index1 892 path 328 %Seq 50.00
Highlighted IDENTICAL residue ALA 979 index1 893 path 329 %Seq 50.00
Highlighted IDENTICAL residue LYS 980 index1 894 path 330 %Seq 50.00
Highlighted IDENTICAL residue ASN 981 index1 895 path 331 %Seq 50.00
Highlighted IDENTICAL residue ALA 982 index1 896 path 332 %Seq 50.00
Highlighted IDENTICAL residue THR 983 index1 897 path 333 %Seq 50.00
Highlighted IDENTICAL residue ASN 984 index1 898 path 334 %Seq 50.00
Highlighted IDENTICAL residue ARG 985 index1 899 path 335 %Seq 50.00
Highlighted IDENTICAL residue VAL 986 index1 900 path 336 %Seq 50.00
Highlighted IDENTICAL residue LEU 987 index1 901 path 337 %Seq 50.00
Highlighted IDENTICAL residue SER 988 index1 902 path 338 %Seq 50.00
Highlighted IDENTICAL residue LEU 989 index1 903 path 339 %Seq 50.00
Highlighted IDENTICAL residue GLN 990 index1 904 path 340 %Seq 50.00
Highlighted IDENTICAL residue GLU 991 index1 905 path 341 %Seq 50.00
Highlighted IDENTICAL residue GLU 992 index1 906 path 342 %Seq 50.00
Highlighted IDENTICAL residue ILE 993 index1 907 path 343 %Seq 50.00
Highlighted IDENTICAL residue ALA 994 index1 908 path 344 %Seq 50.00
Highlighted IDENTICAL residue LYS 995 index1 909 path 345 %Seq 50.00
Highlighted IDENTICAL residue LEU 996 index1 910 path 346 %Seq 50.00
Highlighted IDENTICAL residue ARG 997 index1 911 path 347 %Seq 50.00
Highlighted IDENTICAL residue LYS 998 index1 912 path 348 %Seq 50.00
Highlighted IDENTICAL residue GLU 999 index1 913 path 349 %Seq 50.00
Highlighted IDENTICAL residue HIS 1001 index1 915 path 350 %Seq 50.00
Highlighted IDENTICAL residue GLN 1002 index1 916 path 351 %Seq 50.00
Highlighted IDENTICAL residue THR 1003 index1 917 path 352 %Seq 50.00
Highlighted IDENTICAL residue GLN 1004 index1 918 path 353 %Seq 50.00
Highlighted IDENTICAL residue THR 1005 index1 919 path 354 %Seq 50.00
Highlighted IDENTICAL residue GLU 1006 index1 920 path 355 %Seq 50.00
Highlighted IDENTICAL residue LYS 1007 index1 921 path 356 %Seq 50.00
Highlighted IDENTICAL residue LYS 1008 index1 922 path 357 %Seq 50.00
Highlighted IDENTICAL residue THR 1009 index1 923 path 358 %Seq 50.00
Highlighted IDENTICAL residue ILE 1010 index1 924 path 359 %Seq 50.00
Highlighted IDENTICAL residue GLU 1011 index1 925 path 360 %Seq 50.00
Highlighted IDENTICAL residue GLU 1012 index1 926 path 361 %Seq 50.00
Highlighted IDENTICAL residue TRP 1013 index1 927 path 362 %Seq 50.00
Highlighted IDENTICAL residue ALA 1014 index1 928 path 363 %Seq 50.00
Highlighted IDENTICAL residue ASP 1015 index1 929 path 364 %Seq 50.00
Highlighted IDENTICAL residue LYS 1016 index1 930 path 365 %Seq 50.00
Highlighted IDENTICAL residue TYR 1017 index1 931 path 366 %Seq 50.00
Highlighted IDENTICAL residue LYS 1018 index1 932 path 367 %Seq 50.00
Highlighted IDENTICAL residue HIS 1019 index1 933 path 368 %Seq 50.00
Highlighted IDENTICAL residue GLU 1020 index1 934 path 369 %Seq 50.00
Highlighted IDENTICAL residue THR 1021 index1 935 path 370 %Seq 50.00
Highlighted IDENTICAL residue GLU 1022 index1 936 path 371 %Seq 50.00
Highlighted IDENTICAL residue GLN 1023 index1 937 path 372 %Seq 50.00
Highlighted IDENTICAL residue LEU 1024 index1 938 path 373 %Seq 50.00
Highlighted IDENTICAL residue VAL 1025 index1 939 path 374 %Seq 50.00
Highlighted IDENTICAL residue SER 1026 index1 940 path 375 %Seq 50.00
Highlighted IDENTICAL residue GLU 1027 index1 941 path 376 %Seq 50.00
Highlighted IDENTICAL residue LEU 1028 index1 942 path 377 %Seq 50.00
Highlighted IDENTICAL residue LYS 1029 index1 943 path 378 %Seq 50.00
Highlighted IDENTICAL residue GLU 1030 index1 944 path 379 %Seq 50.00
Highlighted IDENTICAL residue GLN 1031 index1 945 path 380 %Seq 50.00
Highlighted IDENTICAL residue ASN 1032 index1 946 path 381 %Seq 50.00
Highlighted IDENTICAL residue THR 1033 index1 947 path 382 %Seq 50.00
Highlighted IDENTICAL residue LEU 1034 index1 948 path 383 %Seq 50.00
Highlighted IDENTICAL residue LEU 1035 index1 949 path 384 %Seq 50.00
Highlighted IDENTICAL residue LYS 1036 index1 950 path 385 %Seq 50.00
Highlighted IDENTICAL residue THR 1037 index1 951 path 386 %Seq 50.00
Highlighted IDENTICAL residue GLU 1038 index1 952 path 387 %Seq 50.00
Highlighted IDENTICAL residue LYS 1039 index1 953 path 388 %Seq 50.00
Highlighted IDENTICAL residue GLU 1040 index1 954 path 389 %Seq 50.00
Highlighted IDENTICAL residue GLU 1041 index1 955 path 390 %Seq 50.00
Highlighted IDENTICAL residue LEU 1042 index1 956 path 391 %Seq 50.00
Highlighted IDENTICAL residue ASN 1043 index1 957 path 392 %Seq 50.00
Highlighted IDENTICAL residue ARG 1044 index1 958 path 393 %Seq 50.00
Highlighted IDENTICAL residue ARG 1045 index1 959 path 394 %Seq 50.00
Highlighted IDENTICAL residue ILE 1046 index1 960 path 395 %Seq 50.00
Highlighted IDENTICAL residue HIS 1047 index1 961 path 396 %Seq 50.00
Highlighted IDENTICAL residue ASP 1048 index1 962 path 397 %Seq 50.00
Highlighted IDENTICAL residue GLN 1049 index1 963 path 398 %Seq 50.00
Highlighted IDENTICAL residue ALA 1050 index1 964 path 399 %Seq 50.00
Highlighted IDENTICAL residue LYS 1051 index1 965 path 400 %Seq 50.00
Highlighted IDENTICAL residue GLU 1052 index1 966 path 401 %Seq 50.00
Highlighted IDENTICAL residue ILE 1053 index1 967 path 402 %Seq 50.00
Highlighted IDENTICAL residue THR 1054 index1 968 path 403 %Seq 50.00
Highlighted IDENTICAL residue GLU 1055 index1 969 path 404 %Seq 50.00
Highlighted IDENTICAL residue THR 1056 index1 970 path 405 %Seq 50.00
Highlighted IDENTICAL residue MET 1057 index1 971 path 406 %Seq 50.00
Highlighted IDENTICAL residue GLU 1058 index1 972 path 407 %Seq 50.00
Highlighted IDENTICAL residue LYS 1059 index1 973 path 408 %Seq 50.00
Highlighted IDENTICAL residue LYS 1060 index1 974 path 409 %Seq 50.00
Highlighted IDENTICAL residue LEU 1061 index1 975 path 410 %Seq 50.00
Highlighted IDENTICAL residue VAL 1062 index1 976 path 412 %Seq 50.00
Highlighted IDENTICAL residue GLU 1063 index1 977 path 413 %Seq 50.00
Highlighted IDENTICAL residue GLU 1064 index1 978 path 414 %Seq 50.00
Highlighted IDENTICAL residue THR 1065 index1 979 path 415 %Seq 50.00
Highlighted IDENTICAL residue LYS 1066 index1 980 path 416 %Seq 50.00
Highlighted IDENTICAL residue GLN 1067 index1 981 path 417 %Seq 50.00
Highlighted IDENTICAL residue LEU 1068 index1 982 path 418 %Seq 50.00
Highlighted IDENTICAL residue GLU 1069 index1 983 path 419 %Seq 50.00
Highlighted IDENTICAL residue LEU 1070 index1 984 path 420 %Seq 50.00
Highlighted IDENTICAL residue ASP 1071 index1 985 path 421 %Seq 50.00
Highlighted IDENTICAL residue LEU 1072 index1 986 path 422 %Seq 50.00
Highlighted IDENTICAL residue ASN 1073 index1 987 path 424 %Seq 50.00
Highlighted IDENTICAL residue ASP 1074 index1 988 path 425 %Seq 50.00
Highlighted IDENTICAL residue GLU 1075 index1 989 path 426 %Seq 50.00
Highlighted IDENTICAL residue ARG 1076 index1 990 path 427 %Seq 50.00
Highlighted IDENTICAL residue LEU 1077 index1 991 path 428 %Seq 50.00
Highlighted IDENTICAL residue ARG 1078 index1 992 path 429 %Seq 50.00
Highlighted IDENTICAL residue TYR 1079 index1 993 path 430 %Seq 50.00
Highlighted IDENTICAL residue GLN 1080 index1 994 path 431 %Seq 50.00
Highlighted IDENTICAL residue ALA 10 index1 995 path 432 %Seq 50.00
Highlighted IDENTICAL residue GLU 11 index1 996 path 433 %Seq 50.00
Highlighted IDENTICAL residue PHE 12 index1 997 path 434 %Seq 50.00
Highlighted IDENTICAL residue LYS 13 index1 998 path 435 %Seq 50.00
Highlighted IDENTICAL residue GLU 14 index1 999 path 436 %Seq 50.00
Highlighted IDENTICAL residue ALA 15 index1 1000 path 437 %Seq 50.00
Highlighted IDENTICAL residue PHE 16 index1 1001 path 438 %Seq 50.00
Highlighted IDENTICAL residue SER 17 index1 1002 path 439 %Seq 50.00
Highlighted IDENTICAL residue LEU 18 index1 1003 path 440 %Seq 50.00
Highlighted IDENTICAL residue PHE 19 index1 1004 path 441 %Seq 50.00
Highlighted IDENTICAL residue ASP 20 index1 1005 path 442 %Seq 50.00
Highlighted IDENTICAL residue LYS 21 index1 1006 path 443 %Seq 50.00
Highlighted IDENTICAL residue ASP 22 index1 1007 path 444 %Seq 50.00
Highlighted IDENTICAL residue GLY 23 index1 1008 path 445 %Seq 50.00
Highlighted IDENTICAL residue ASP 24 index1 1009 path 446 %Seq 50.00
Highlighted IDENTICAL residue GLY 25 index1 1010 path 447 %Seq 50.00
Highlighted IDENTICAL residue THR 26 index1 1011 path 448 %Seq 50.00
Highlighted IDENTICAL residue ILE 27 index1 1012 path 449 %Seq 50.00
Highlighted IDENTICAL residue THR 28 index1 1013 path 450 %Seq 50.00
Highlighted IDENTICAL residue THR 29 index1 1014 path 451 %Seq 50.00
Highlighted IDENTICAL residue LYS 30 index1 1015 path 452 %Seq 50.00
Highlighted IDENTICAL residue GLU 31 index1 1016 path 453 %Seq 50.00
Highlighted IDENTICAL residue LEU 32 index1 1017 path 454 %Seq 50.00
Highlighted IDENTICAL residue GLY 33 index1 1018 path 455 %Seq 50.00
Highlighted IDENTICAL residue THR 34 index1 1019 path 456 %Seq 50.00
Highlighted IDENTICAL residue VAL 35 index1 1020 path 457 %Seq 50.00
Highlighted IDENTICAL residue MET 36 index1 1021 path 458 %Seq 50.00
Highlighted IDENTICAL residue ARG 37 index1 1022 path 459 %Seq 50.00
Highlighted IDENTICAL residue SER 38 index1 1023 path 460 %Seq 50.00
Highlighted IDENTICAL residue GLY 40 index1 1025 path 461 %Seq 50.00
Highlighted IDENTICAL residue GLN 41 index1 1026 path 462 %Seq 50.00
Highlighted IDENTICAL residue ASN 42 index1 1027 path 463 %Seq 50.00
Highlighted IDENTICAL residue PRO 43 index1 1028 path 464 %Seq 50.00
Highlighted IDENTICAL residue THR 44 index1 1029 path 465 %Seq 50.00
Highlighted IDENTICAL residue GLU 45 index1 1030 path 466 %Seq 50.00
Highlighted IDENTICAL residue ALA 46 index1 1031 path 467 %Seq 50.00
Highlighted IDENTICAL residue GLU 47 index1 1032 path 468 %Seq 50.00
Highlighted IDENTICAL residue LEU 48 index1 1033 path 469 %Seq 50.00
Highlighted IDENTICAL residue GLN 49 index1 1034 path 470 %Seq 50.00
Highlighted IDENTICAL residue ASP 50 index1 1035 path 471 %Seq 50.00
Highlighted IDENTICAL residue MET 51 index1 1036 path 472 %Seq 50.00
Highlighted IDENTICAL residue ILE 52 index1 1037 path 473 %Seq 50.00
Highlighted IDENTICAL residue ASN 53 index1 1038 path 474 %Seq 50.00
Highlighted IDENTICAL residue GLU 54 index1 1039 path 475 %Seq 50.00
Highlighted IDENTICAL residue VAL 55 index1 1040 path 476 %Seq 50.00
Highlighted IDENTICAL residue ASP 56 index1 1041 path 477 %Seq 50.00
Highlighted IDENTICAL residue ALA 57 index1 1042 path 478 %Seq 50.00
Highlighted IDENTICAL residue ASP 58 index1 1043 path 479 %Seq 50.00
Highlighted IDENTICAL residue GLY 59 index1 1044 path 480 %Seq 50.00
Highlighted IDENTICAL residue ASN 60 index1 1045 path 481 %Seq 50.00
Highlighted IDENTICAL residue GLY 61 index1 1046 path 482 %Seq 50.00
Highlighted IDENTICAL residue THR 62 index1 1047 path 483 %Seq 50.00
Highlighted IDENTICAL residue ILE 63 index1 1048 path 484 %Seq 50.00
Highlighted IDENTICAL residue ASP 64 index1 1049 path 485 %Seq 50.00
Highlighted IDENTICAL residue PHE 65 index1 1050 path 486 %Seq 50.00
Highlighted IDENTICAL residue PRO 66 index1 1051 path 487 %Seq 50.00
Highlighted IDENTICAL residue GLU 67 index1 1052 path 488 %Seq 50.00
Highlighted 171 residues for visualization
Wrote PyMOL macro into file /usr/local/www/html/proteins/htdocs/results/At2g02790-2dfsA.pir.txt.2DFS.pdb.conservation.pml
===============================================================================
The program
/usr/local/www/html/proteins/Compiled_Programs/WYRM/PyMOL_highlight_conserved_residues At2g02790-2dfsA.pir.txt PIR amino_acid 2DFS.pdb A 100.0 BLOSUM62.dat 
completed successfully.
@@@@@@@@@@@@@@@@@@@@ END /usr/local/www/html/proteins/Compiled_Programs/WYRM/PyMOL_highlight_conserved_residues @@@@@@@@@@@@@@@@@@@@