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At2g05990.2/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

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
Sequence 2
Got here 3
Got here 4
Got here 3
Got here 4
Got here 3
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Got here 3
Got here 4
Got here 3
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Got here 3
Got here 4
Read 2 amino_acid sequences from PIR Sequence file /usr/local/www/html/proteins/workspace/At2g05990-1eno_.pir.txt

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

Assigned types to 390 residues in Sequence 2-05990-390, 0 remain unknown
Assigned types to 312 residues in Sequence 1eno_, 78 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 At2g05990-1eno_.pir.txt into sequence alignment.

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

>1ENO.pdb  Made from 2181 ATOM records in 1ENO.pdb
LPIDLRGKRAFIAGIADDNGYGWAVAKSLAAAGAEILVGTWVPALNIFET
SLRRGKFDQSRVLPDGSLMEIKKVYPLDAVFDNPEDVPEDVKANKRYAGS
SNWTVQEAAECVRQDFGSIDILVHSLANGPEVSKPLLETSRKGYLAAISA
SSYSFVSLLSHFLPIMNPGGASISLTYIASERIIPGYGGGMSSAKAALES
DTRVLAFEAGRKQNIRVNTISAGPLGSRAAKAIGFIDTMIEYSYNNAPIQ
KTLTADEVGNAAAFLVSPLASAITGATIYVDNGLNSMGVALDSPVFK

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

Best alignment:
1ENO.pdb        1  LPIDLRGKRAFIAGIADDNGYGWAVAKSLAAAGAEILVGTWVPALNIFET    50
                   LPIDLRGKRAFIAGIADDNGYGWA+AKSLAAAGAEILVGTWVPALNIFET
2-05990-390    88  LPIDLRGKRAFIAGIADDNGYGWAIAKSLAAAGAEILVGTWVPALNIFET   137

1ENO.pdb       51  SLRRGKFDQSRVLPDGSLMEIKKVYPLDAVFDNPEDVPEDVKANKRYAGS   100
                   SLRRGKFDQSRVLPDGSLMEIKKVY LDAVFDNPEDVPEDVK NKRYAGS
2-05990-390   138  SLRRGKFDQSRVLPDGSLMEIKKVYALDAVFDNPEDVPEDVKTNKRYAGS   187

1ENO.pdb      101  SNWTVQEAAECVRQDFGSIDILVHSLANGPEVSKPLLETSRKGYLAAISA   150
                   SNWTVQEAAECV++DFGSIDILVHSLANGPEVSKPLLETSRKGYLAAISA
2-05990-390   188  SNWTVQEAAECVKKDFGSIDILVHSLANGPEVSKPLLETSRKGYLAAISA   237

1ENO.pdb      151  SSYSFVSLLSHFLPIMNPGGASISLTYIASERIIPGYGGGMSSAKAALES   200
                   SSYSFVSLL HFLPIMNPGGASISLTYIASERIIPGYGGGMSSAKAALES
2-05990-390   238  SSYSFVSLLRHFLPIMNPGGASISLTYIASERIIPGYGGGMSSAKAALES   287

1ENO.pdb      201  DTRVLAFEAGRKQNIRVNTISAGPLGSRAAKAIGFIDTMIEYSYNNAPIQ   250
                   DTRVLA+EAGRK NIRVNTISAGPLGSRAAKAIGFIDTMIEYSYNN PIQ
2-05990-390   288  DTRVLAYEAGRKSNIRVNTISAGPLGSRAAKAIGFIDTMIEYSYNNGPIQ   337

1ENO.pdb      251  KTLTADEVGNAAAFLVSPLASAITGATIYVDNGLNSMGVALDSPVFK   297
                   KTLTADEVGNAAAFL SPLASAITGATIYVDNGLN+MGVALDSPVFK
2-05990-390   338  KTLTADEVGNAAAFLASPLASAITGATIYVDNGLNAMGVALDSPVFK   384

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

Highlighted IDENTICAL residue LEU   12  index1    1  path   88  %Seq 100.00
Highlighted IDENTICAL residue PRO   13  index1    2  path   89  %Seq 100.00
Highlighted IDENTICAL residue ILE   14  index1    3  path   90  %Seq 100.00
Highlighted IDENTICAL residue ASP   15  index1    4  path   91  %Seq 100.00
Highlighted IDENTICAL residue LEU   16  index1    5  path   92  %Seq 100.00
Highlighted IDENTICAL residue ARG   17  index1    6  path   93  %Seq 100.00
Highlighted IDENTICAL residue GLY   18  index1    7  path   94  %Seq 100.00
Highlighted IDENTICAL residue LYS   19  index1    8  path   95  %Seq 100.00
Highlighted IDENTICAL residue ARG   20  index1    9  path   96  %Seq 100.00
Highlighted IDENTICAL residue ALA   21  index1   10  path   97  %Seq 100.00
Highlighted IDENTICAL residue PHE   22  index1   11  path   98  %Seq 100.00
Highlighted IDENTICAL residue ILE   23  index1   12  path   99  %Seq 100.00
Highlighted IDENTICAL residue ALA   24  index1   13  path  100  %Seq 100.00
Highlighted IDENTICAL residue GLY   25  index1   14  path  101  %Seq 100.00
Highlighted IDENTICAL residue ILE   26  index1   15  path  102  %Seq 100.00
Highlighted IDENTICAL residue ALA   27  index1   16  path  103  %Seq 100.00
Highlighted IDENTICAL residue ASP   28  index1   17  path  104  %Seq 100.00
Highlighted IDENTICAL residue ASP   29  index1   18  path  105  %Seq 100.00
Highlighted IDENTICAL residue ASN   30  index1   19  path  106  %Seq 100.00
Highlighted IDENTICAL residue GLY   31  index1   20  path  107  %Seq 100.00
Highlighted IDENTICAL residue TYR   32  index1   21  path  108  %Seq 100.00
Highlighted IDENTICAL residue GLY   33  index1   22  path  109  %Seq 100.00
Highlighted IDENTICAL residue TRP   34  index1   23  path  110  %Seq 100.00
Highlighted IDENTICAL residue ALA   35  index1   24  path  111  %Seq 100.00
Highlighted IDENTICAL residue ALA   37  index1   26  path  113  %Seq 100.00
Highlighted IDENTICAL residue LYS   38  index1   27  path  114  %Seq 100.00
Highlighted IDENTICAL residue SER   39  index1   28  path  115  %Seq 100.00
Highlighted IDENTICAL residue LEU   40  index1   29  path  116  %Seq 100.00
Highlighted IDENTICAL residue ALA   41  index1   30  path  117  %Seq 100.00
Highlighted IDENTICAL residue ALA   42  index1   31  path  118  %Seq 100.00
Highlighted IDENTICAL residue ALA   43  index1   32  path  119  %Seq 100.00
Highlighted IDENTICAL residue GLY   44  index1   33  path  120  %Seq 100.00
Highlighted IDENTICAL residue ALA   45  index1   34  path  121  %Seq 100.00
Highlighted IDENTICAL residue GLU   46  index1   35  path  122  %Seq 100.00
Highlighted IDENTICAL residue ILE   47  index1   36  path  123  %Seq 100.00
Highlighted IDENTICAL residue LEU   48  index1   37  path  124  %Seq 100.00
Highlighted IDENTICAL residue VAL   49  index1   38  path  125  %Seq 100.00
Highlighted IDENTICAL residue GLY   50  index1   39  path  126  %Seq 100.00
Highlighted IDENTICAL residue THR   51  index1   40  path  127  %Seq 100.00
Highlighted IDENTICAL residue TRP   52  index1   41  path  128  %Seq 100.00
Highlighted IDENTICAL residue VAL   53  index1   42  path  129  %Seq 100.00
Highlighted IDENTICAL residue PRO   54  index1   43  path  130  %Seq 100.00
Highlighted IDENTICAL residue ALA   55  index1   44  path  131  %Seq 100.00
Highlighted IDENTICAL residue LEU   56  index1   45  path  132  %Seq 100.00
Highlighted IDENTICAL residue ASN   57  index1   46  path  133  %Seq 100.00
Highlighted IDENTICAL residue ILE   58  index1   47  path  134  %Seq 100.00
Highlighted IDENTICAL residue PHE   59  index1   48  path  135  %Seq 100.00
Highlighted IDENTICAL residue GLU   60  index1   49  path  136  %Seq 100.00
Highlighted IDENTICAL residue THR   61  index1   50  path  137  %Seq 100.00
Highlighted IDENTICAL residue SER   62  index1   51  path  138  %Seq 100.00
Highlighted IDENTICAL residue LEU   63  index1   52  path  139  %Seq 100.00
Highlighted IDENTICAL residue ARG   64  index1   53  path  140  %Seq 100.00
Highlighted IDENTICAL residue ARG   65  index1   54  path  141  %Seq 100.00
Highlighted IDENTICAL residue GLY   66  index1   55  path  142  %Seq 100.00
Highlighted IDENTICAL residue LYS   67  index1   56  path  143  %Seq 100.00
Highlighted IDENTICAL residue PHE   68  index1   57  path  144  %Seq 100.00
Highlighted IDENTICAL residue ASP   69  index1   58  path  145  %Seq 100.00
Highlighted IDENTICAL residue GLN   70  index1   59  path  146  %Seq 100.00
Highlighted IDENTICAL residue SER   71  index1   60  path  147  %Seq 100.00
Highlighted IDENTICAL residue ARG   72  index1   61  path  148  %Seq 100.00
Highlighted IDENTICAL residue VAL   73  index1   62  path  149  %Seq 100.00
Highlighted IDENTICAL residue LEU   74  index1   63  path  150  %Seq 100.00
Highlighted IDENTICAL residue PRO   75  index1   64  path  151  %Seq 100.00
Highlighted IDENTICAL residue ASP   76  index1   65  path  152  %Seq 100.00
Highlighted IDENTICAL residue GLY   77  index1   66  path  153  %Seq 100.00
Highlighted IDENTICAL residue SER   78  index1   67  path  154  %Seq 100.00
Highlighted IDENTICAL residue LEU   79  index1   68  path  155  %Seq 100.00
Highlighted IDENTICAL residue MET   80  index1   69  path  156  %Seq 100.00
Highlighted IDENTICAL residue GLU   81  index1   70  path  157  %Seq 100.00
Highlighted IDENTICAL residue ILE   82  index1   71  path  158  %Seq 100.00
Highlighted IDENTICAL residue LYS   83  index1   72  path  159  %Seq 100.00
Highlighted IDENTICAL residue LYS   84  index1   73  path  160  %Seq 100.00
Highlighted IDENTICAL residue VAL   85  index1   74  path  161  %Seq 100.00
Highlighted IDENTICAL residue TYR   86  index1   75  path  162  %Seq 100.00
Highlighted IDENTICAL residue LEU   88  index1   77  path  164  %Seq 100.00
Highlighted IDENTICAL residue ASP   89  index1   78  path  165  %Seq 100.00
Highlighted IDENTICAL residue ALA   90  index1   79  path  166  %Seq 100.00
Highlighted IDENTICAL residue VAL   91  index1   80  path  167  %Seq 100.00
Highlighted IDENTICAL residue PHE   92  index1   81  path  168  %Seq 100.00
Highlighted IDENTICAL residue ASP   93  index1   82  path  169  %Seq 100.00
Highlighted IDENTICAL residue ASN   94  index1   83  path  170  %Seq 100.00
Highlighted IDENTICAL residue PRO   95  index1   84  path  171  %Seq 100.00
Highlighted IDENTICAL residue GLU   96  index1   85  path  172  %Seq 100.00
Highlighted IDENTICAL residue ASP   97  index1   86  path  173  %Seq 100.00
Highlighted IDENTICAL residue VAL   98  index1   87  path  174  %Seq 100.00
Highlighted IDENTICAL residue PRO   99  index1   88  path  175  %Seq 100.00
Highlighted IDENTICAL residue GLU  100  index1   89  path  176  %Seq 100.00
Highlighted IDENTICAL residue ASP  101  index1   90  path  177  %Seq 100.00
Highlighted IDENTICAL residue VAL  102  index1   91  path  178  %Seq 100.00
Highlighted IDENTICAL residue LYS  103  index1   92  path  179  %Seq 100.00
Highlighted IDENTICAL residue ASN  105  index1   94  path  181  %Seq 100.00
Highlighted IDENTICAL residue LYS  106  index1   95  path  182  %Seq 100.00
Highlighted IDENTICAL residue ARG  107  index1   96  path  183  %Seq 100.00
Highlighted IDENTICAL residue TYR  108  index1   97  path  184  %Seq 100.00
Highlighted IDENTICAL residue ALA  109  index1   98  path  185  %Seq 100.00
Highlighted IDENTICAL residue GLY  110  index1   99  path  186  %Seq 100.00
Highlighted IDENTICAL residue SER  111  index1  100  path  187  %Seq 100.00
Highlighted IDENTICAL residue SER  112  index1  101  path  188  %Seq 100.00
Highlighted IDENTICAL residue ASN  113  index1  102  path  189  %Seq 100.00
Highlighted IDENTICAL residue TRP  114  index1  103  path  190  %Seq 100.00
Highlighted IDENTICAL residue THR  115  index1  104  path  191  %Seq 100.00
Highlighted IDENTICAL residue VAL  116  index1  105  path  192  %Seq 100.00
Highlighted IDENTICAL residue GLN  117  index1  106  path  193  %Seq 100.00
Highlighted IDENTICAL residue GLU  118  index1  107  path  194  %Seq 100.00
Highlighted IDENTICAL residue ALA  119  index1  108  path  195  %Seq 100.00
Highlighted IDENTICAL residue ALA  120  index1  109  path  196  %Seq 100.00
Highlighted IDENTICAL residue GLU  121  index1  110  path  197  %Seq 100.00
Highlighted IDENTICAL residue CYS  122  index1  111  path  198  %Seq 100.00
Highlighted IDENTICAL residue VAL  123  index1  112  path  199  %Seq 100.00
Highlighted IDENTICAL residue ASP  126  index1  115  path  202  %Seq 100.00
Highlighted IDENTICAL residue PHE  127  index1  116  path  203  %Seq 100.00
Highlighted IDENTICAL residue GLY  128  index1  117  path  204  %Seq 100.00
Highlighted IDENTICAL residue SER  129  index1  118  path  205  %Seq 100.00
Highlighted IDENTICAL residue ILE  130  index1  119  path  206  %Seq 100.00
Highlighted IDENTICAL residue ASP  131  index1  120  path  207  %Seq 100.00
Highlighted IDENTICAL residue ILE  132  index1  121  path  208  %Seq 100.00
Highlighted IDENTICAL residue LEU  133  index1  122  path  209  %Seq 100.00
Highlighted IDENTICAL residue VAL  134  index1  123  path  210  %Seq 100.00
Highlighted IDENTICAL residue HIS  135  index1  124  path  211  %Seq 100.00
Highlighted IDENTICAL residue SER  136  index1  125  path  212  %Seq 100.00
Highlighted IDENTICAL residue LEU  137  index1  126  path  213  %Seq 100.00
Highlighted IDENTICAL residue ALA  138  index1  127  path  214  %Seq 100.00
Highlighted IDENTICAL residue ASN  139  index1  128  path  215  %Seq 100.00
Highlighted IDENTICAL residue GLY  140  index1  129  path  216  %Seq 100.00
Highlighted IDENTICAL residue PRO  141  index1  130  path  217  %Seq 100.00
Highlighted IDENTICAL residue GLU  142  index1  131  path  218  %Seq 100.00
Highlighted IDENTICAL residue VAL  143  index1  132  path  219  %Seq 100.00
Highlighted IDENTICAL residue SER  144  index1  133  path  220  %Seq 100.00
Highlighted IDENTICAL residue LYS  145  index1  134  path  221  %Seq 100.00
Highlighted IDENTICAL residue PRO  146  index1  135  path  222  %Seq 100.00
Highlighted IDENTICAL residue LEU  147  index1  136  path  223  %Seq 100.00
Highlighted IDENTICAL residue LEU  148  index1  137  path  224  %Seq 100.00
Highlighted IDENTICAL residue GLU  149  index1  138  path  225  %Seq 100.00
Highlighted IDENTICAL residue THR  150  index1  139  path  226  %Seq 100.00
Highlighted IDENTICAL residue SER  151  index1  140  path  227  %Seq 100.00
Highlighted IDENTICAL residue ARG  152  index1  141  path  228  %Seq 100.00
Highlighted IDENTICAL residue LYS  153  index1  142  path  229  %Seq 100.00
Highlighted IDENTICAL residue GLY  154  index1  143  path  230  %Seq 100.00
Highlighted IDENTICAL residue TYR  155  index1  144  path  231  %Seq 100.00
Highlighted IDENTICAL residue LEU  156  index1  145  path  232  %Seq 100.00
Highlighted IDENTICAL residue ALA  157  index1  146  path  233  %Seq 100.00
Highlighted IDENTICAL residue ALA  158  index1  147  path  234  %Seq 100.00
Highlighted IDENTICAL residue ILE  159  index1  148  path  235  %Seq 100.00
Highlighted IDENTICAL residue SER  160  index1  149  path  236  %Seq 100.00
Highlighted IDENTICAL residue ALA  161  index1  150  path  237  %Seq 100.00
Highlighted IDENTICAL residue SER  162  index1  151  path  238  %Seq 100.00
Highlighted IDENTICAL residue SER  163  index1  152  path  239  %Seq 100.00
Highlighted IDENTICAL residue TYR  164  index1  153  path  240  %Seq 100.00
Highlighted IDENTICAL residue SER  165  index1  154  path  241  %Seq 100.00
Highlighted IDENTICAL residue PHE  166  index1  155  path  242  %Seq 100.00
Highlighted IDENTICAL residue VAL  167  index1  156  path  243  %Seq 100.00
Highlighted IDENTICAL residue SER  168  index1  157  path  244  %Seq 100.00
Highlighted IDENTICAL residue LEU  169  index1  158  path  245  %Seq 100.00
Highlighted IDENTICAL residue LEU  170  index1  159  path  246  %Seq 100.00
Highlighted IDENTICAL residue HIS  172  index1  161  path  248  %Seq 100.00
Highlighted IDENTICAL residue PHE  173  index1  162  path  249  %Seq 100.00
Highlighted IDENTICAL residue LEU  174  index1  163  path  250  %Seq 100.00
Highlighted IDENTICAL residue PRO  175  index1  164  path  251  %Seq 100.00
Highlighted IDENTICAL residue ILE  176  index1  165  path  252  %Seq 100.00
Highlighted IDENTICAL residue MET  177  index1  166  path  253  %Seq 100.00
Highlighted IDENTICAL residue ASN  178  index1  167  path  254  %Seq 100.00
Highlighted IDENTICAL residue PRO  179  index1  168  path  255  %Seq 100.00
Highlighted IDENTICAL residue GLY  180  index1  169  path  256  %Seq 100.00
Highlighted IDENTICAL residue GLY  181  index1  170  path  257  %Seq 100.00
Highlighted IDENTICAL residue ALA  182  index1  171  path  258  %Seq 100.00
Highlighted IDENTICAL residue SER  183  index1  172  path  259  %Seq 100.00
Highlighted IDENTICAL residue ILE  184  index1  173  path  260  %Seq 100.00
Highlighted IDENTICAL residue SER  185  index1  174  path  261  %Seq 100.00
Highlighted IDENTICAL residue LEU  186  index1  175  path  262  %Seq 100.00
Highlighted IDENTICAL residue THR  187  index1  176  path  263  %Seq 100.00
Highlighted IDENTICAL residue TYR  188  index1  177  path  264  %Seq 100.00
Highlighted IDENTICAL residue ILE  189  index1  178  path  265  %Seq 100.00
Highlighted IDENTICAL residue ALA  190  index1  179  path  266  %Seq 100.00
Highlighted IDENTICAL residue SER  191  index1  180  path  267  %Seq 100.00
Highlighted IDENTICAL residue GLU  192  index1  181  path  268  %Seq 100.00
Highlighted IDENTICAL residue ARG  193  index1  182  path  269  %Seq 100.00
Highlighted IDENTICAL residue ILE  194  index1  183  path  270  %Seq 100.00
Highlighted IDENTICAL residue ILE  195  index1  184  path  271  %Seq 100.00
Highlighted IDENTICAL residue PRO  196  index1  185  path  272  %Seq 100.00
Highlighted IDENTICAL residue GLY  197  index1  186  path  273  %Seq 100.00
Highlighted IDENTICAL residue TYR  198  index1  187  path  274  %Seq 100.00
Highlighted IDENTICAL residue GLY  199  index1  188  path  275  %Seq 100.00
Highlighted IDENTICAL residue GLY  200  index1  189  path  276  %Seq 100.00
Highlighted IDENTICAL residue GLY  201  index1  190  path  277  %Seq 100.00
Highlighted IDENTICAL residue MET  202  index1  191  path  278  %Seq 100.00
Highlighted IDENTICAL residue SER  203  index1  192  path  279  %Seq 100.00
Highlighted IDENTICAL residue SER  204  index1  193  path  280  %Seq 100.00
Highlighted IDENTICAL residue ALA  205  index1  194  path  281  %Seq 100.00
Highlighted IDENTICAL residue LYS  206  index1  195  path  282  %Seq 100.00
Highlighted IDENTICAL residue ALA  207  index1  196  path  283  %Seq 100.00
Highlighted IDENTICAL residue ALA  208  index1  197  path  284  %Seq 100.00
Highlighted IDENTICAL residue LEU  209  index1  198  path  285  %Seq 100.00
Highlighted IDENTICAL residue GLU  210  index1  199  path  286  %Seq 100.00
Highlighted IDENTICAL residue SER  211  index1  200  path  287  %Seq 100.00
Highlighted IDENTICAL residue ASP  212  index1  201  path  288  %Seq 100.00
Highlighted IDENTICAL residue THR  213  index1  202  path  289  %Seq 100.00
Highlighted IDENTICAL residue ARG  214  index1  203  path  290  %Seq 100.00
Highlighted IDENTICAL residue VAL  215  index1  204  path  291  %Seq 100.00
Highlighted IDENTICAL residue LEU  216  index1  205  path  292  %Seq 100.00
Highlighted IDENTICAL residue ALA  217  index1  206  path  293  %Seq 100.00
Highlighted IDENTICAL residue GLU  219  index1  208  path  295  %Seq 100.00
Highlighted IDENTICAL residue ALA  220  index1  209  path  296  %Seq 100.00
Highlighted IDENTICAL residue GLY  221  index1  210  path  297  %Seq 100.00
Highlighted IDENTICAL residue ARG  222  index1  211  path  298  %Seq 100.00
Highlighted IDENTICAL residue LYS  223  index1  212  path  299  %Seq 100.00
Highlighted IDENTICAL residue ASN  225  index1  214  path  301  %Seq 100.00
Highlighted IDENTICAL residue ILE  226  index1  215  path  302  %Seq 100.00
Highlighted IDENTICAL residue ARG  227  index1  216  path  303  %Seq 100.00
Highlighted IDENTICAL residue VAL  228  index1  217  path  304  %Seq 100.00
Highlighted IDENTICAL residue ASN  229  index1  218  path  305  %Seq 100.00
Highlighted IDENTICAL residue THR  230  index1  219  path  306  %Seq 100.00
Highlighted IDENTICAL residue ILE  231  index1  220  path  307  %Seq 100.00
Highlighted IDENTICAL residue SER  232  index1  221  path  308  %Seq 100.00
Highlighted IDENTICAL residue ALA  233  index1  222  path  309  %Seq 100.00
Highlighted IDENTICAL residue GLY  234  index1  223  path  310  %Seq 100.00
Highlighted IDENTICAL residue PRO  235  index1  224  path  311  %Seq 100.00
Highlighted IDENTICAL residue LEU  236  index1  225  path  312  %Seq 100.00
Highlighted IDENTICAL residue GLY  237  index1  226  path  313  %Seq 100.00
Highlighted IDENTICAL residue SER  238  index1  227  path  314  %Seq 100.00
Highlighted IDENTICAL residue ARG  239  index1  228  path  315  %Seq 100.00
Highlighted IDENTICAL residue ALA  240  index1  229  path  316  %Seq 100.00
Highlighted IDENTICAL residue ALA  241  index1  230  path  317  %Seq 100.00
Highlighted IDENTICAL residue LYS  242  index1  231  path  318  %Seq 100.00
Highlighted IDENTICAL residue ALA  243  index1  232  path  319  %Seq 100.00
Highlighted IDENTICAL residue ILE  244  index1  233  path  320  %Seq 100.00
Highlighted IDENTICAL residue GLY  245  index1  234  path  321  %Seq 100.00
Highlighted IDENTICAL residue PHE  246  index1  235  path  322  %Seq 100.00
Highlighted IDENTICAL residue ILE  247  index1  236  path  323  %Seq 100.00
Highlighted IDENTICAL residue ASP  248  index1  237  path  324  %Seq 100.00
Highlighted IDENTICAL residue THR  249  index1  238  path  325  %Seq 100.00
Highlighted IDENTICAL residue MET  250  index1  239  path  326  %Seq 100.00
Highlighted IDENTICAL residue ILE  251  index1  240  path  327  %Seq 100.00
Highlighted IDENTICAL residue GLU  252  index1  241  path  328  %Seq 100.00
Highlighted IDENTICAL residue TYR  253  index1  242  path  329  %Seq 100.00
Highlighted IDENTICAL residue SER  254  index1  243  path  330  %Seq 100.00
Highlighted IDENTICAL residue TYR  255  index1  244  path  331  %Seq 100.00
Highlighted IDENTICAL residue ASN  256  index1  245  path  332  %Seq 100.00
Highlighted IDENTICAL residue ASN  257  index1  246  path  333  %Seq 100.00
Highlighted IDENTICAL residue PRO  259  index1  248  path  335  %Seq 100.00
Highlighted IDENTICAL residue ILE  260  index1  249  path  336  %Seq 100.00
Highlighted IDENTICAL residue GLN  261  index1  250  path  337  %Seq 100.00
Highlighted IDENTICAL residue LYS  262  index1  251  path  338  %Seq 100.00
Highlighted IDENTICAL residue THR  263  index1  252  path  339  %Seq 100.00
Highlighted IDENTICAL residue LEU  264  index1  253  path  340  %Seq 100.00
Highlighted IDENTICAL residue THR  265  index1  254  path  341  %Seq 100.00
Highlighted IDENTICAL residue ALA  266  index1  255  path  342  %Seq 100.00
Highlighted IDENTICAL residue ASP  267  index1  256  path  343  %Seq 100.00
Highlighted IDENTICAL residue GLU  268  index1  257  path  344  %Seq 100.00
Highlighted IDENTICAL residue VAL  269  index1  258  path  345  %Seq 100.00
Highlighted IDENTICAL residue GLY  270  index1  259  path  346  %Seq 100.00
Highlighted IDENTICAL residue ASN  271  index1  260  path  347  %Seq 100.00
Highlighted IDENTICAL residue ALA  272  index1  261  path  348  %Seq 100.00
Highlighted IDENTICAL residue ALA  273  index1  262  path  349  %Seq 100.00
Highlighted IDENTICAL residue ALA  274  index1  263  path  350  %Seq 100.00
Highlighted IDENTICAL residue PHE  275  index1  264  path  351  %Seq 100.00
Highlighted IDENTICAL residue LEU  276  index1  265  path  352  %Seq 100.00
Highlighted IDENTICAL residue SER  278  index1  267  path  354  %Seq 100.00
Highlighted IDENTICAL residue PRO  279  index1  268  path  355  %Seq 100.00
Highlighted IDENTICAL residue LEU  280  index1  269  path  356  %Seq 100.00
Highlighted IDENTICAL residue ALA  281  index1  270  path  357  %Seq 100.00
Highlighted IDENTICAL residue SER  282  index1  271  path  358  %Seq 100.00
Highlighted IDENTICAL residue ALA  283  index1  272  path  359  %Seq 100.00
Highlighted IDENTICAL residue ILE  284  index1  273  path  360  %Seq 100.00
Highlighted IDENTICAL residue THR  285  index1  274  path  361  %Seq 100.00
Highlighted IDENTICAL residue GLY  286  index1  275  path  362  %Seq 100.00
Highlighted IDENTICAL residue ALA  287  index1  276  path  363  %Seq 100.00
Highlighted IDENTICAL residue THR  288  index1  277  path  364  %Seq 100.00
Highlighted IDENTICAL residue ILE  289  index1  278  path  365  %Seq 100.00
Highlighted IDENTICAL residue TYR  290  index1  279  path  366  %Seq 100.00
Highlighted IDENTICAL residue VAL  291  index1  280  path  367  %Seq 100.00
Highlighted IDENTICAL residue ASP  292  index1  281  path  368  %Seq 100.00
Highlighted IDENTICAL residue ASN  293  index1  282  path  369  %Seq 100.00
Highlighted IDENTICAL residue GLY  294  index1  283  path  370  %Seq 100.00
Highlighted IDENTICAL residue LEU  295  index1  284  path  371  %Seq 100.00
Highlighted IDENTICAL residue ASN  296  index1  285  path  372  %Seq 100.00
Highlighted IDENTICAL residue MET  298  index1  287  path  374  %Seq 100.00
Highlighted IDENTICAL residue GLY  299  index1  288  path  375  %Seq 100.00
Highlighted IDENTICAL residue VAL  300  index1  289  path  376  %Seq 100.00
Highlighted IDENTICAL residue ALA  301  index1  290  path  377  %Seq 100.00
Highlighted IDENTICAL residue LEU  302  index1  291  path  378  %Seq 100.00
Highlighted IDENTICAL residue ASP  303  index1  292  path  379  %Seq 100.00
Highlighted IDENTICAL residue SER  304  index1  293  path  380  %Seq 100.00
Highlighted IDENTICAL residue PRO  305  index1  294  path  381  %Seq 100.00
Highlighted IDENTICAL residue VAL  306  index1  295  path  382  %Seq 100.00
Highlighted IDENTICAL residue PHE  307  index1  296  path  383  %Seq 100.00
Highlighted IDENTICAL residue LYS  308  index1  297  path  384  %Seq 100.00
Highlighted 286 residues for visualization

Wrote PyMOL macro into file /usr/local/www/html/proteins/htdocs/results/At2g05990-1eno_.pir.txt.1ENO.pdb.conservation.pml

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

The program

/usr/local/www/html/proteins/Compiled_Programs/WYRM/PyMOL_highlight_conserved_residues At2g05990-1eno_.pir.txt PIR amino_acid 1ENO.pdb _ 100.0 BLOSUM62.dat 

completed successfully.

@@@@@@@@@@@@@@@@@@@@ END  /usr/local/www/html/proteins/Compiled_Programs/WYRM/PyMOL_highlight_conserved_residues @@@@@@@@@@@@@@@@@@@@


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