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/

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Sequence file type = 3

Sequence type = 3

Got here 1 Got here 2 Got here 3 Sequence 1 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Sequence 2 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Read 2 amino_acid sequences from PIR Sequence file /usr/local/www/html/proteins/workspace/At2g02790-2dfsA.pir.txt

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Assigned types to 636 residues in Sequence 2-02790, 23 remain unknown Assigned types to 212 residues in Sequence 2dfsA, 447 remain unknown

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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

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Translated sequence file At2g02790-2dfsA.pir.txt into sequence alignment.

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>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

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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

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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

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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.

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