FANDOM


&&&&&&&&&&&&&&&&&&&& 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
Got here 3
Sequence 1
Got here 3
Got here 4
Got here 3
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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

======================================================

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 @@@@@@@@@@@@@@@@@@@@

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