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At2g04030.2/PDB

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&&&&&&&&&&&&&&&&&&&& 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/At2g04030-2-2cg9A.pir.txt

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

Assigned types to 777 residues in Sequence 2-04030-2, 14 remain unknown
Assigned types to 655 residues in Sequence 2cg9A, 136 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 At2g04030-2-2cg9A.pir.txt into sequence alignment.

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

>2CG9.pdb  Made from 11844 ATOM records in 2CG9.pdb
ASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLS
DPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGT
KAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESN
AGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFV
AYPIQLVVTKEVEKEEEVQEIEELNKTKPLWTRNPSDITQEEYNAFYKSI
SNDWEDPLYVKHFSVEGQLEFRAILFIPKRAPFNNIKLYVRRVFITDEAE
DLIPEWLSFVKGVVDSEDLPLNLSREMLQQNKIMKVIRKNIVKKLIEAFN
EIAEDSEQFEKFYSAFSKNIKLGVHEDTQNRAALAKLLRYNSTKSVDELT
SLTDYVTRMPEHQKNIYYITGESLKAVEKSPFLDALKAKNFEVLFLTDPI
DEYAFTQLKEFEGKTLVDITKDFELEETDEEKAEREKEIKEYEPLTKALK
EILGDQVEKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQAKTFEISPK
SPIIKELKKRVDEGGAQDKTVKDLTKLLYETALLTSGFSLDEPTSFASRI
NRLISLGLNASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDAL
DKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINN
LGTIAKSGTKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSND
DEQYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKE
VIKRHSEFVAYPIQLVVTKEVEKEEEVQEIEELNKTKPLWTRNPSDITQE
EYNAFYKSISNDWEDPLYVKHFSVEGQLEFRAILFIPKRAPFDLFESKKK
KNNIKLYVRRVFITDEAEDLIPEWLSFVKGVVDSEDLPLNLSREMLQQNK
IMKVIRKNIVKKLIEAFNEIAEDSEQFEKFYSAFSKNIKLGVHEDTQNRA
ALAKLLRYNSTKSVDELTSLTDYVTRMPEHQKNIYYITGESLKAVEKSPF
LDALKAKNFEVLFLTDPIDEYAFTQLKEFEGKTLVDITKDFELEETDEEK
AEREKEIKEYEPLTKALKEILGDQVEKVVVSYKLLDAPAAIRTGQFGWSA
NMERIMKAQAKTFEISPKSPIIKELKKRVDEGGAQDKTVKDLTKLLYETA
LLTSGFSLDEPTSFASRINRLISLGLNWAQRSSTTDPERNYVLITVSIAD
CDAPELTIKPSYIELKAQSKVHHYQLHIDLYKEIIPEKTMHKVANGYFLK
LYKKDLESEYWPRLTKEKVKYPYIKTDFDKWVDADEQDEVEAWAQRSSTT
DPERNYVLITVSIADCDAPELTIKPSYIELKAQSKVHHYQLHIDLYKEII
PEKTMHKVANGYFLKLYKKDLESEYWPRLTKEKVKYPYIKTDFDKWVDAD
EQDEVEA

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

Best alignment:
2CG9.pdb   610  ASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLS   659
                ASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLS
2cg9A        1  ASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLS    50

2CG9.pdb   660  DPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGT   709
                DPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGT
2cg9A       51  DPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGT   100

2CG9.pdb   710  KAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESN   759
                KAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESN
2cg9A      101  KAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESN   150

2CG9.pdb   760  AGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFV   809
                AGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFV
2cg9A      151  AGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFV   200

2CG9.pdb   810  AYPIQLVVTKEVEK-----EEEVQEIEELNK-------------------   835
                AYPIQLVVTKEVEK     EEEVQEIEEL K                   
2cg9A      201  AYPIQLVVTKEVEKEVPIPXXXXXXXXXXPKLEEVDEEEEKKPKTKKVKE   250

2CG9.pdb   835  ----------TKPLWTRNPSDITQEEYNAFYKSISNDWEDPLYVKHFSVE   875
                          TKPLWTRNPSDITQEEYNAFYKSISNDWEDPLYVKHFSVE
2cg9A      251  EVQEIEELNKTKPLWTRNPSDITQEEYNAFYKSISNDWEDPLYVKHFSVE   300

2CG9.pdb   876  GQLEFRAILFIPKRAPFDLFESKKKKNNIKLYVRRVFITDEAEDLIPEWL   925
                GQLEFRAILFIPKRAPFDLFESKKKKNNIKLYVRRVFITDEAEDLIPEWL
2cg9A      301  GQLEFRAILFIPKRAPFDLFESKKKKNNIKLYVRRVFITDEAEDLIPEWL   350

2CG9.pdb   926  SFVKGVVDSEDLPLNLSREMLQQNKIMKVIRKNIVKKLIEAFNEIAEDSE   975
                SFVKGVVDSEDLPLNLSREMLQQNKIMKVIRKNIVKKLIEAFNEIAEDSE
2cg9A      351  SFVKGVVDSEDLPLNLSREMLQQNKIMKVIRKNIVKKLIEAFNEIAEDSE   400

2CG9.pdb   976  QFEKFYSAFSKNIKLGVHEDTQNRAALAKLLRYNSTKSVDELTSLTDYVT  1025
                QFEKFYSAFSKNIKLGVHEDTQNRAALAKLLRYNSTKSVDELTSLTDYVT
2cg9A      401  QFEKFYSAFSKNIKLGVHEDTQNRAALAKLLRYNSTKSVDELTSLTDYVT   450

2CG9.pdb  1026  RMPEHQKNIYYITGESLKAVEKSPFLDALKAKNFEVLFLTDPIDEYAFTQ  1075
                RMPEHQKNIYYITGESLKAVEKSPFLDALKAKNFEVLFLTDPIDEYAFTQ
2cg9A      451  RMPEHQKNIYYITGESLKAVEKSPFLDALKAKNFEVLFLTDPIDEYAFTQ   500

2CG9.pdb  1076  LKEFEGKTLVDITKDFELEETDEEKAEREKEIKEYEPLTKALKEILGDQV  1125
                LKEFEGKTLVDITKDFELEETDEEKAEREKEIKEYEPLTKALKEILGDQV
2cg9A      501  LKEFEGKTLVDITKDFELEETDEEKAEREKEIKEYEPLTKALKEILGDQV   550

2CG9.pdb  1126  EKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQA-------------KT  1162
                EKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQA             KT
2cg9A      551  EKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQALRDSSMSSYMSSKKT   600

2CG9.pdb  1163  FEISPKSPIIKELKKRVDEGGAQDKTVKDLTKLLYETALLTSGFSLDEPT  1212
                FEISPKSPIIKELKKRVDEGGAQDKTVKDLTKLLYETALLTSGFSLDEPT
2cg9A      601  FEISPKSPIIKELKKRVDEGGAQDKTVKDLTKLLYETALLTSGFSLDEPT   650

2CG9.pdb  1213  SFASRINRLISLGLN  1227
                SFASRINRLISLGLN
2cg9A      651  SFASRINRLISLGLN   665

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

Highlighted IDENTICAL residue GLU    4  index1  612  path   77  %Seq 100.00
Highlighted IDENTICAL residue PHE    6  index1  614  path   79  %Seq 100.00
Highlighted IDENTICAL residue GLU    7  index1  615  path   80  %Seq 100.00
Highlighted IDENTICAL residue GLN    9  index1  617  path   82  %Seq 100.00
Highlighted IDENTICAL residue ALA   10  index1  618  path   83  %Seq 100.00
Highlighted IDENTICAL residue GLU   11  index1  619  path   84  %Seq 100.00
Highlighted IDENTICAL residue LEU   15  index1  623  path   88  %Seq 100.00
Highlighted IDENTICAL residue LEU   18  index1  626  path   91  %Seq 100.00
Highlighted IDENTICAL residue ILE   19  index1  627  path   92  %Seq 100.00
Highlighted IDENTICAL residue TYR   24  index1  632  path   97  %Seq 100.00
Highlighted IDENTICAL residue SER   25  index1  633  path   98  %Seq 100.00
Highlighted IDENTICAL residue LYS   27  index1  635  path  100  %Seq 100.00
Highlighted IDENTICAL residue GLU   28  index1  636  path  101  %Seq 100.00
Highlighted IDENTICAL residue PHE   30  index1  638  path  103  %Seq 100.00
Highlighted IDENTICAL residue LEU   31  index1  639  path  104  %Seq 100.00
Highlighted IDENTICAL residue ARG   32  index1  640  path  105  %Seq 100.00
Highlighted IDENTICAL residue GLU   33  index1  641  path  106  %Seq 100.00
Highlighted IDENTICAL residue LEU   34  index1  642  path  107  %Seq 100.00
Highlighted IDENTICAL residue SER   36  index1  644  path  109  %Seq 100.00
Highlighted IDENTICAL residue ASN   37  index1  645  path  110  %Seq 100.00
Highlighted IDENTICAL residue ALA   38  index1  646  path  111  %Seq 100.00
Highlighted IDENTICAL residue SER   39  index1  647  path  112  %Seq 100.00
Highlighted IDENTICAL residue ASP   40  index1  648  path  113  %Seq 100.00
Highlighted IDENTICAL residue ALA   41  index1  649  path  114  %Seq 100.00
Highlighted IDENTICAL residue LEU   42  index1  650  path  115  %Seq 100.00
Highlighted IDENTICAL residue ASP   43  index1  651  path  116  %Seq 100.00
Highlighted IDENTICAL residue LYS   44  index1  652  path  117  %Seq 100.00
Highlighted IDENTICAL residue ARG   46  index1  654  path  119  %Seq 100.00
Highlighted IDENTICAL residue SER   49  index1  657  path  122  %Seq 100.00
Highlighted IDENTICAL residue PRO   53  index1  661  path  126  %Seq 100.00
Highlighted IDENTICAL residue LEU   56  index1  664  path  129  %Seq 100.00
Highlighted IDENTICAL residue ASP   61  index1  669  path  134  %Seq 100.00
Highlighted IDENTICAL residue LEU   62  index1  670  path  135  %Seq 100.00
Highlighted IDENTICAL residue ILE   64  index1  672  path  137  %Seq 100.00
Highlighted IDENTICAL residue ARG   65  index1  673  path  138  %Seq 100.00
Highlighted IDENTICAL residue ILE   66  index1  674  path  139  %Seq 100.00
Highlighted IDENTICAL residue PRO   68  index1  676  path  141  %Seq 100.00
Highlighted IDENTICAL residue PRO   70  index1  678  path  143  %Seq 100.00
Highlighted IDENTICAL residue ILE   77  index1  685  path  150  %Seq 100.00
Highlighted IDENTICAL residue ASP   79  index1  687  path  152  %Seq 100.00
Highlighted IDENTICAL residue GLY   81  index1  689  path  154  %Seq 100.00
Highlighted IDENTICAL residue ILE   82  index1  690  path  155  %Seq 100.00
Highlighted IDENTICAL residue GLY   83  index1  691  path  156  %Seq 100.00
Highlighted IDENTICAL residue MET   84  index1  692  path  157  %Seq 100.00
Highlighted IDENTICAL residue THR   85  index1  693  path  158  %Seq 100.00
Highlighted IDENTICAL residue LYS   86  index1  694  path  159  %Seq 100.00
Highlighted IDENTICAL residue GLU   88  index1  696  path  161  %Seq 100.00
Highlighted IDENTICAL residue LEU   89  index1  697  path  162  %Seq 100.00
Highlighted IDENTICAL residue ILE   90  index1  698  path  163  %Seq 100.00
Highlighted IDENTICAL residue LEU   93  index1  701  path  166  %Seq 100.00
Highlighted IDENTICAL residue GLY   94  index1  702  path  167  %Seq 100.00
Highlighted IDENTICAL residue THR   95  index1  703  path  168  %Seq 100.00
Highlighted IDENTICAL residue ILE   96  index1  704  path  169  %Seq 100.00
Highlighted IDENTICAL residue ALA   97  index1  705  path  170  %Seq 100.00
Highlighted IDENTICAL residue SER   99  index1  707  path  172  %Seq 100.00
Highlighted IDENTICAL residue GLY  100  index1  708  path  173  %Seq 100.00
Highlighted IDENTICAL residue THR  101  index1  709  path  174  %Seq 100.00
Highlighted IDENTICAL residue PHE  104  index1  712  path  177  %Seq 100.00
Highlighted IDENTICAL residue ALA  107  index1  715  path  180  %Seq 100.00
Highlighted IDENTICAL residue LEU  108  index1  716  path  181  %Seq 100.00
Highlighted IDENTICAL residue GLY  111  index1  719  path  188  %Seq 100.00
Highlighted IDENTICAL residue ALA  112  index1  720  path  189  %Seq 100.00
Highlighted IDENTICAL residue ASP  113  index1  721  path  190  %Seq 100.00
Highlighted IDENTICAL residue ILE  117  index1  725  path  194  %Seq 100.00
Highlighted IDENTICAL residue GLY  118  index1  726  path  195  %Seq 100.00
Highlighted IDENTICAL residue GLN  119  index1  727  path  196  %Seq 100.00
Highlighted IDENTICAL residue PHE  120  index1  728  path  197  %Seq 100.00
Highlighted IDENTICAL residue GLY  121  index1  729  path  198  %Seq 100.00
Highlighted IDENTICAL residue VAL  122  index1  730  path  199  %Seq 100.00
Highlighted IDENTICAL residue GLY  123  index1  731  path  200  %Seq 100.00
Highlighted IDENTICAL residue PHE  124  index1  732  path  201  %Seq 100.00
Highlighted IDENTICAL residue TYR  125  index1  733  path  202  %Seq 100.00
Highlighted IDENTICAL residue SER  126  index1  734  path  203  %Seq 100.00
Highlighted IDENTICAL residue PHE  128  index1  736  path  205  %Seq 100.00
Highlighted IDENTICAL residue LEU  129  index1  737  path  206  %Seq 100.00
Highlighted IDENTICAL residue VAL  130  index1  738  path  207  %Seq 100.00
Highlighted IDENTICAL residue ALA  131  index1  739  path  208  %Seq 100.00
Highlighted IDENTICAL residue VAL  134  index1  742  path  211  %Seq 100.00
Highlighted IDENTICAL residue VAL  136  index1  744  path  213  %Seq 100.00
Highlighted IDENTICAL residue LYS  139  index1  747  path  216  %Seq 100.00
Highlighted IDENTICAL residue SER  140  index1  748  path  217  %Seq 100.00
Highlighted IDENTICAL residue ASP  143  index1  751  path  221  %Seq 100.00
Highlighted IDENTICAL residue GLN  145  index1  753  path  223  %Seq 100.00
Highlighted IDENTICAL residue TYR  146  index1  754  path  224  %Seq 100.00
Highlighted IDENTICAL residue TRP  148  index1  756  path  226  %Seq 100.00
Highlighted IDENTICAL residue GLU  149  index1  757  path  227  %Seq 100.00
Highlighted IDENTICAL residue SER  150  index1  758  path  228  %Seq 100.00
Highlighted IDENTICAL residue ALA  152  index1  760  path  230  %Seq 100.00
Highlighted IDENTICAL residue SER  155  index1  763  path  233  %Seq 100.00
Highlighted IDENTICAL residue GLU  162  index1  770  path  240  %Seq 100.00
Highlighted IDENTICAL residue ARG  169  index1  777  path  249  %Seq 100.00
Highlighted IDENTICAL residue GLY  170  index1  778  path  250  %Seq 100.00
Highlighted IDENTICAL residue THR  171  index1  779  path  251  %Seq 100.00
Highlighted IDENTICAL residue LEU  175  index1  783  path  255  %Seq 100.00
Highlighted IDENTICAL residue LEU  177  index1  785  path  257  %Seq 100.00
Highlighted IDENTICAL residue ASP  179  index1  787  path  260  %Seq 100.00
Highlighted IDENTICAL residue ASP  180  index1  788  path  261  %Seq 100.00
Highlighted IDENTICAL residue GLU  183  index1  791  path  264  %Seq 100.00
Highlighted IDENTICAL residue GLU  186  index1  794  path  267  %Seq 100.00
Highlighted IDENTICAL residue ARG  189  index1  797  path  270  %Seq 100.00
Highlighted IDENTICAL residue ILE  190  index1  798  path  271  %Seq 100.00
Highlighted IDENTICAL residue LYS  191  index1  799  path  272  %Seq 100.00
Highlighted IDENTICAL residue LYS  195  index1  803  path  276  %Seq 100.00
Highlighted IDENTICAL residue SER  198  index1  806  path  279  %Seq 100.00
Highlighted IDENTICAL residue PHE  200  index1  808  path  281  %Seq 100.00
Highlighted IDENTICAL residue VAL  201  index1  809  path  282  %Seq 100.00
Highlighted IDENTICAL residue PRO  204  index1  812  path  285  %Seq 100.00
Highlighted IDENTICAL residue ILE  205  index1  813  path  286  %Seq 100.00
Highlighted IDENTICAL residue LYS  211  index1  819  path  292  %Seq 100.00
Highlighted IDENTICAL residue GLU  216  index1  824  path  302  %Seq  50.00
Highlighted IDENTICAL residue GLU  262  index1  825  path  303  %Seq  50.00
Highlighted IDENTICAL residue GLU  263  index1  826  path  304  %Seq  50.00
Highlighted IDENTICAL residue VAL  264  index1  827  path  305  %Seq  50.00
Highlighted IDENTICAL residue GLN  265  index1  828  path  306  %Seq  50.00
Highlighted IDENTICAL residue GLU  266  index1  829  path  307  %Seq  50.00
Highlighted IDENTICAL residue ILE  267  index1  830  path  308  %Seq  50.00
Highlighted IDENTICAL residue GLU  268  index1  831  path  309  %Seq  50.00
Highlighted IDENTICAL residue GLU  269  index1  832  path  310  %Seq  50.00
Highlighted IDENTICAL residue LEU  270  index1  833  path  311  %Seq  50.00
Highlighted IDENTICAL residue ASN  271  index1  834  path  312  %Seq 100.00
Highlighted IDENTICAL residue LYS  272  index1  835  path  313  %Seq 100.00
Highlighted IDENTICAL residue THR  273  index1  836  path  343  %Seq 100.00
Highlighted IDENTICAL residue LYS  274  index1  837  path  344  %Seq 100.00
Highlighted IDENTICAL residue PRO  275  index1  838  path  345  %Seq 100.00
Highlighted IDENTICAL residue LEU  276  index1  839  path  346  %Seq 100.00
Highlighted IDENTICAL residue TRP  277  index1  840  path  347  %Seq 100.00
Highlighted IDENTICAL residue ARG  279  index1  842  path  349  %Seq 100.00
Highlighted IDENTICAL residue ASN  280  index1  843  path  350  %Seq 100.00
Highlighted IDENTICAL residue GLU  288  index1  851  path  358  %Seq 100.00
Highlighted IDENTICAL residue TYR  289  index1  852  path  359  %Seq 100.00
Highlighted IDENTICAL residue ASN  290  index1  853  path  360  %Seq 100.00
Highlighted IDENTICAL residue PHE  292  index1  855  path  362  %Seq 100.00
Highlighted IDENTICAL residue TYR  293  index1  856  path  363  %Seq 100.00
Highlighted IDENTICAL residue LYS  294  index1  857  path  364  %Seq 100.00
Highlighted IDENTICAL residue ASN  298  index1  861  path  368  %Seq 100.00
Highlighted IDENTICAL residue ASP  302  index1  865  path  372  %Seq 100.00
Highlighted IDENTICAL residue PRO  303  index1  866  path  373  %Seq 100.00
Highlighted IDENTICAL residue LEU  304  index1  867  path  374  %Seq 100.00
Highlighted IDENTICAL residue HIS  308  index1  871  path  378  %Seq 100.00
Highlighted IDENTICAL residue PHE  309  index1  872  path  379  %Seq 100.00
Highlighted IDENTICAL residue GLU  312  index1  875  path  382  %Seq 100.00
Highlighted IDENTICAL residue GLY  313  index1  876  path  383  %Seq 100.00
Highlighted IDENTICAL residue GLU  316  index1  879  path  386  %Seq 100.00
Highlighted IDENTICAL residue PHE  317  index1  880  path  387  %Seq 100.00
Highlighted IDENTICAL residue ARG  318  index1  881  path  388  %Seq 100.00
Highlighted IDENTICAL residue ILE  320  index1  883  path  390  %Seq 100.00
Highlighted IDENTICAL residue LEU  321  index1  884  path  391  %Seq 100.00
Highlighted IDENTICAL residue ILE  323  index1  886  path  393  %Seq 100.00
Highlighted IDENTICAL residue PRO  324  index1  887  path  394  %Seq 100.00
Highlighted IDENTICAL residue PRO  328  index1  891  path  398  %Seq 100.00
Highlighted IDENTICAL residue LYS  337  index1  900  path  408  %Seq 100.00
Highlighted IDENTICAL residue ASN  340  index1  903  path  411  %Seq 100.00
Highlighted IDENTICAL residue ILE  341  index1  904  path  412  %Seq 100.00
Highlighted IDENTICAL residue LEU  343  index1  906  path  414  %Seq 100.00
Highlighted IDENTICAL residue TYR  344  index1  907  path  415  %Seq 100.00
Highlighted IDENTICAL residue VAL  345  index1  908  path  416  %Seq 100.00
Highlighted IDENTICAL residue ARG  347  index1  910  path  418  %Seq 100.00
Highlighted IDENTICAL residue VAL  348  index1  911  path  419  %Seq 100.00
Highlighted IDENTICAL residue PHE  349  index1  912  path  420  %Seq 100.00
Highlighted IDENTICAL residue ILE  350  index1  913  path  421  %Seq 100.00
Highlighted IDENTICAL residue ASP  352  index1  915  path  423  %Seq 100.00
Highlighted IDENTICAL residue LEU  357  index1  920  path  429  %Seq 100.00
Highlighted IDENTICAL residue PRO  359  index1  922  path  431  %Seq 100.00
Highlighted IDENTICAL residue LEU  362  index1  925  path  434  %Seq 100.00
Highlighted IDENTICAL residue SER  363  index1  926  path  435  %Seq 100.00
Highlighted IDENTICAL residue PHE  364  index1  927  path  436  %Seq 100.00
Highlighted IDENTICAL residue VAL  365  index1  928  path  437  %Seq 100.00
Highlighted IDENTICAL residue LYS  366  index1  929  path  438  %Seq 100.00
Highlighted IDENTICAL residue GLY  367  index1  930  path  439  %Seq 100.00
Highlighted IDENTICAL residue VAL  368  index1  931  path  440  %Seq 100.00
Highlighted IDENTICAL residue VAL  369  index1  932  path  441  %Seq 100.00
Highlighted IDENTICAL residue ASP  370  index1  933  path  442  %Seq 100.00
Highlighted IDENTICAL residue SER  371  index1  934  path  443  %Seq 100.00
Highlighted IDENTICAL residue ASP  373  index1  936  path  445  %Seq 100.00
Highlighted IDENTICAL residue LEU  374  index1  937  path  446  %Seq 100.00
Highlighted IDENTICAL residue PRO  375  index1  938  path  447  %Seq 100.00
Highlighted IDENTICAL residue LEU  376  index1  939  path  448  %Seq 100.00
Highlighted IDENTICAL residue ASN  377  index1  940  path  449  %Seq 100.00
Highlighted IDENTICAL residue SER  379  index1  942  path  451  %Seq 100.00
Highlighted IDENTICAL residue ARG  380  index1  943  path  452  %Seq 100.00
Highlighted IDENTICAL residue GLU  381  index1  944  path  453  %Seq 100.00
Highlighted IDENTICAL residue LEU  383  index1  946  path  455  %Seq 100.00
Highlighted IDENTICAL residue GLN  384  index1  947  path  456  %Seq 100.00
Highlighted IDENTICAL residue ILE  388  index1  951  path  460  %Seq 100.00
Highlighted IDENTICAL residue ARG  393  index1  956  path  465  %Seq 100.00
Highlighted IDENTICAL residue LYS  394  index1  957  path  466  %Seq 100.00
Highlighted IDENTICAL residue LYS  399  index1  962  path  471  %Seq 100.00
Highlighted IDENTICAL residue GLU  406  index1  969  path  478  %Seq 100.00
Highlighted IDENTICAL residue ILE  407  index1  970  path  479  %Seq 100.00
Highlighted IDENTICAL residue GLU  409  index1  972  path  481  %Seq 100.00
Highlighted IDENTICAL residue SER  411  index1  974  path  483  %Seq  50.00
Highlighted IDENTICAL residue GLU  412  index1  975  path  484  %Seq 100.00
Highlighted IDENTICAL residue GLU  415  index1  978  path  487  %Seq 100.00
Highlighted IDENTICAL residue LYS  416  index1  979  path  488  %Seq 100.00
Highlighted IDENTICAL residue PHE  417  index1  980  path  489  %Seq 100.00
Highlighted IDENTICAL residue PHE  421  index1  984  path  493  %Seq 100.00
Highlighted IDENTICAL residue LYS  426  index1  989  path  498  %Seq 100.00
Highlighted IDENTICAL residue LEU  427  index1  990  path  499  %Seq 100.00
Highlighted IDENTICAL residue GLY  428  index1  991  path  500  %Seq 100.00
Highlighted IDENTICAL residue GLU  431  index1  994  path  503  %Seq 100.00
Highlighted IDENTICAL residue ASP  432  index1  995  path  504  %Seq 100.00
Highlighted IDENTICAL residue THR  433  index1  996  path  505  %Seq 100.00
Highlighted IDENTICAL residue ASN  435  index1  998  path  507  %Seq 100.00
Highlighted IDENTICAL residue LEU  442  index1 1005  path  514  %Seq 100.00
Highlighted IDENTICAL residue LEU  443  index1 1006  path  515  %Seq 100.00
Highlighted IDENTICAL residue ARG  444  index1 1007  path  516  %Seq 100.00
Highlighted IDENTICAL residue SER  447  index1 1010  path  519  %Seq 100.00
Highlighted IDENTICAL residue LYS  449  index1 1012  path  521  %Seq 100.00
Highlighted IDENTICAL residue GLU  453  index1 1016  path  525  %Seq 100.00
Highlighted IDENTICAL residue LEU  454  index1 1017  path  526  %Seq 100.00
Highlighted IDENTICAL residue THR  455  index1 1018  path  527  %Seq 100.00
Highlighted IDENTICAL residue SER  456  index1 1019  path  528  %Seq 100.00
Highlighted IDENTICAL residue LEU  457  index1 1020  path  529  %Seq 100.00
Highlighted IDENTICAL residue ASP  459  index1 1022  path  531  %Seq 100.00
Highlighted IDENTICAL residue TYR  460  index1 1023  path  532  %Seq 100.00
Highlighted IDENTICAL residue MET  464  index1 1027  path  536  %Seq 100.00
Highlighted IDENTICAL residue GLU  466  index1 1029  path  538  %Seq 100.00
Highlighted IDENTICAL residue GLN  468  index1 1031  path  540  %Seq 100.00
Highlighted IDENTICAL residue LYS  469  index1 1032  path  541  %Seq 100.00
Highlighted IDENTICAL residue ILE  471  index1 1034  path  543  %Seq 100.00
Highlighted IDENTICAL residue TYR  472  index1 1035  path  544  %Seq 100.00
Highlighted IDENTICAL residue TYR  473  index1 1036  path  545  %Seq 100.00
Highlighted IDENTICAL residue SER  478  index1 1041  path  550  %Seq 100.00
Highlighted IDENTICAL residue LEU  479  index1 1042  path  551  %Seq 100.00
Highlighted IDENTICAL residue LYS  480  index1 1043  path  552  %Seq 100.00
Highlighted IDENTICAL residue PRO  486  index1 1049  path  558  %Seq 100.00
Highlighted IDENTICAL residue PHE  487  index1 1050  path  559  %Seq 100.00
Highlighted IDENTICAL residue LEU  488  index1 1051  path  560  %Seq 100.00
Highlighted IDENTICAL residue LEU  491  index1 1054  path  563  %Seq 100.00
Highlighted IDENTICAL residue LYS  494  index1 1057  path  566  %Seq 100.00
Highlighted IDENTICAL residue GLU  497  index1 1060  path  569  %Seq 100.00
Highlighted IDENTICAL residue VAL  498  index1 1061  path  570  %Seq 100.00
Highlighted IDENTICAL residue LEU  499  index1 1062  path  571  %Seq 100.00
Highlighted IDENTICAL residue LEU  501  index1 1064  path  573  %Seq 100.00
Highlighted IDENTICAL residue PRO  504  index1 1067  path  576  %Seq 100.00
Highlighted IDENTICAL residue ILE  505  index1 1068  path  577  %Seq 100.00
Highlighted IDENTICAL residue ASP  506  index1 1069  path  578  %Seq 100.00
Highlighted IDENTICAL residue GLU  507  index1 1070  path  579  %Seq 100.00
Highlighted IDENTICAL residue ALA  509  index1 1072  path  581  %Seq 100.00
Highlighted IDENTICAL residue LEU  513  index1 1076  path  585  %Seq 100.00
Highlighted IDENTICAL residue LYS  519  index1 1082  path  591  %Seq 100.00
Highlighted IDENTICAL residue VAL  522  index1 1085  path  594  %Seq 100.00
Highlighted IDENTICAL residue ASP  523  index1 1086  path  595  %Seq 100.00
Highlighted IDENTICAL residue ILE  524  index1 1087  path  596  %Seq 100.00
Highlighted IDENTICAL residue LYS  526  index1 1089  path  598  %Seq 100.00
Highlighted IDENTICAL residue PHE  528  index1 1091  path  600  %Seq  50.00
Highlighted IDENTICAL residue LEU  530  index1 1093  path  602  %Seq 100.00
Highlighted IDENTICAL residue GLU  531  index1 1094  path  603  %Seq 100.00
Highlighted IDENTICAL residue ASP  534  index1 1097  path  606  %Seq 100.00
Highlighted IDENTICAL residue GLU  535  index1 1098  path  607  %Seq 100.00
Highlighted IDENTICAL residue GLU  546  index1 1109  path  618  %Seq 100.00
Highlighted IDENTICAL residue LEU  550  index1 1113  path  622  %Seq 100.00
Highlighted IDENTICAL residue LYS  555  index1 1118  path  627  %Seq 100.00
Highlighted IDENTICAL residue LEU  558  index1 1121  path  630  %Seq 100.00
Highlighted IDENTICAL residue GLY  559  index1 1122  path  631  %Seq 100.00
Highlighted IDENTICAL residue ASP  560  index1 1123  path  632  %Seq 100.00
Highlighted IDENTICAL residue VAL  562  index1 1125  path  634  %Seq 100.00
Highlighted IDENTICAL residue LYS  564  index1 1127  path  636  %Seq 100.00
Highlighted IDENTICAL residue VAL  565  index1 1128  path  637  %Seq 100.00
Highlighted IDENTICAL residue VAL  567  index1 1130  path  639  %Seq 100.00
Highlighted IDENTICAL residue SER  568  index1 1131  path  640  %Seq 100.00
Highlighted IDENTICAL residue LEU  571  index1 1134  path  643  %Seq 100.00
Highlighted IDENTICAL residue PRO  575  index1 1138  path  647  %Seq 100.00
Highlighted IDENTICAL residue GLY  581  index1 1144  path  653  %Seq 100.00
Highlighted IDENTICAL residue PHE  583  index1 1146  path  655  %Seq 100.00
Highlighted IDENTICAL residue GLY  584  index1 1147  path  656  %Seq 100.00
Highlighted IDENTICAL residue TRP  585  index1 1148  path  657  %Seq 100.00
Highlighted IDENTICAL residue SER  586  index1 1149  path  658  %Seq 100.00
Highlighted IDENTICAL residue ALA  587  index1 1150  path  659  %Seq 100.00
Highlighted IDENTICAL residue ASN  588  index1 1151  path  660  %Seq 100.00
Highlighted IDENTICAL residue MET  589  index1 1152  path  661  %Seq 100.00
Highlighted IDENTICAL residue GLU  590  index1 1153  path  662  %Seq 100.00
Highlighted IDENTICAL residue ARG  591  index1 1154  path  663  %Seq 100.00
Highlighted IDENTICAL residue MET  593  index1 1156  path  665  %Seq 100.00
Highlighted IDENTICAL residue LYS  594  index1 1157  path  666  %Seq 100.00
Highlighted IDENTICAL residue ALA  595  index1 1158  path  667  %Seq 100.00
Highlighted IDENTICAL residue GLN  596  index1 1159  path  668  %Seq 100.00
Highlighted IDENTICAL residue ALA  597  index1 1160  path  669  %Seq 100.00
Highlighted IDENTICAL residue GLU  614  index1 1164  path  686  %Seq 100.00
Highlighted IDENTICAL residue ILE  615  index1 1165  path  687  %Seq 100.00
Highlighted IDENTICAL residue PRO  617  index1 1167  path  689  %Seq 100.00
Highlighted IDENTICAL residue PRO  620  index1 1170  path  692  %Seq 100.00
Highlighted IDENTICAL residue ILE  621  index1 1171  path  693  %Seq 100.00
Highlighted IDENTICAL residue ILE  622  index1 1172  path  694  %Seq 100.00
Highlighted IDENTICAL residue LYS  623  index1 1173  path  695  %Seq 100.00
Highlighted IDENTICAL residue LEU  625  index1 1175  path  697  %Seq 100.00
Highlighted IDENTICAL residue GLY  632  index1 1182  path  704  %Seq  50.00
Highlighted IDENTICAL residue LEU  645  index1 1195  path  717  %Seq 100.00
Highlighted IDENTICAL residue LEU  646  index1 1196  path  718  %Seq 100.00
Highlighted IDENTICAL residue TYR  647  index1 1197  path  719  %Seq 100.00
Highlighted IDENTICAL residue THR  649  index1 1199  path  721  %Seq 100.00
Highlighted IDENTICAL residue ALA  650  index1 1200  path  722  %Seq 100.00
Highlighted IDENTICAL residue SER  654  index1 1204  path  726  %Seq 100.00
Highlighted IDENTICAL residue GLY  655  index1 1205  path  727  %Seq 100.00
Highlighted IDENTICAL residue PHE  656  index1 1206  path  728  %Seq 100.00
Highlighted IDENTICAL residue ASP  659  index1 1209  path  731  %Seq 100.00
Highlighted IDENTICAL residue PRO  661  index1 1211  path  733  %Seq 100.00
Highlighted IDENTICAL residue ILE  668  index1 1218  path  740  %Seq 100.00
Highlighted 298 residues for visualization

Wrote PyMOL macro into file /usr/local/www/html/proteins/htdocs/results/At2g04030-2-2cg9A.pir.txt.2CG9.pdb.conservation.pml

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

The program

/usr/local/www/html/proteins/Compiled_Programs/WYRM/PyMOL_highlight_conserved_residues At2g04030-2-2cg9A.pir.txt PIR amino_acid 2CG9.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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