At2g05100.1/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 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 Read 2 amino_acid sequences from PIR Sequence file /usr/local/www/html/proteins/workspace/At2g05100-c1rwta_.pir.txt

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Assigned types to 265 residues in Sequence 2-05100, 0 remain unknown Assigned types to 218 residues in Sequence c1rwta_, 47 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 At2g05100-c1rwta_.pir.txt into sequence alignment.

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>1RWT.pdb Made from 16619 ATOM records in 1RWT.pdb SPWYGPDRVKYLGPFSGESPSYLTGEFPGDYGWDTAGLSADPETFAKNRE LEVIHCRWAMLGALGCVFPELLARNGVKFGEAVWFKAGSQIFSEGGLDYL GNPSLVHAQSILAIWACQVILMGAVEGYRIAGGPLGEVVDPLYPGGSFDP LGLADDPEAFAELKVKEIKNGRLAMFSMFGFFVQAIVTGKGPLENLADHL ADPVNNNAWNFATNFVPGSPWYGPDRVKYLGPFSGESPSYLTGEFPGDYG WDTAGLSADPETFAKNRELEVIHCRWAMLGALGCVFPELLARNGVKFGEA VWFKAGSQIFSEGGLDYLGNPSLVHAQSILAIWACQVILMGAVEGYRIAG GPLGEVVDPLYPGGSFDPLGLADDPEAFAELKVKEIKNGRLAMFSMFGFF VQAIVTGKGPLENLADHLADPVNNNAWNFATNFVPGSPWYGPDRVKYLGP FSGESPSYLTGEFPGDYGWDTAGLSADPETFAKNRELEVIHCRWAMLGAL GCVFPELLARNGVKFGEAVWFKAGSQIFSEGGLDYLGNPSLVHAQSILAI WACQVILMGAVEGYRIAGGPLGEVVDPLYPGGSFDPLGLADDPEAFAELK VKEIKNGRLAMFSMFGFFVQAIVTGKGPLENLADHLADPVNNNAWNFATN FVPGSPWYGPDRVKYLGPFSGESPSYLTGEFPGDYGWDTAGLSADPETFA KNRELEVIHCRWAMLGALGCVFPELLARNGVKFGEAVWFKAGSQIFSEGG LDYLGNPSLVHAQSILAIWACQVILMGAVEGYRIAGGPLGEVVDPLYPGG SFDPLGLADDPEAFAELKVKEIKNGRLAMFSMFGFFVQAIVTGKGPLENL ADHLADPVNNNAWNFATNFVPGSPWYGPDRVKYLGPFSGESPSYLTGEFP GDYGWDTAGLSADPETFAKNRELEVIHCRWAMLGALGCVFPELLARNGVK FGEAVWFKAGSQIFSEGGLDYLGNPSLVHAQSILAIWACQVILMGAVEGY RIAGGPLGEVVDPLYPGGSFDPLGLADDPEAFAELKVKEIKNGRLAMFSM FGFFVQAIVTGKGPLENLADHLADPVNNNAWNFATNFVPGSPWYGPDRVK YLGPFSGESPSYLTGEFPGDYGWDTAGLSADPETFAKNRELEVIHCRWAM LGALGCVFPELLARNGVKFGEAVWFKAGSQIFSEGGLDYLGNPSLVHAQS ILAIWACQVILMGAVEGYRIAGGPLGEVVDPLYPGGSFDPLGLADDPEAF AELKVKEIKNGRLAMFSMFGFFVQAIVTGKGPLENLADHLADPVNNNAWN FATNFVPGKSPWYGPDRVKYLGPFSGESPSYLTGEFPGDYGWDTAGLSAD PETFAKNRELEVIHCRWAMLGALGCVFPELLARNGVKFGEAVWFKAGSQI FSEGGLDYLGNPSLVHAQSILAIWACQVILMGAVEGYRIAGGPLGEVVDP LYPGGSFDPLGLADDPEAFAELKVKEIKNGRLAMFSMFGFFVQAIVTGKG PLENLADHLADPVNNNAWNFATNFVPGSPWYGPDRVKYLGPFSGESPSYL TGEFPGDYGWDTAGLSADPETFAKNRELEVIHCRWAMLGALGCVFPELLA RNGVKFGEAVWFKAGSQIFSEGGLDYLGNPSLVHAQSILAIWACQVILMG AVEGYRIAGGPLGEVVDPLYPGGSFDPLGLADDPEAFAELKVKEIKNGRL AMFSMFGFFVQAIVTGKGPLENLADHLADPVNNNAWNFATNFVPGSPWYG PDRVKYLGPFSGESPSYLTGEFPGDYGWDTAGLSADPETFAKNRELEVIH CRWAMLGALGCVFPELLARNGVKFGEAVWFKAGSQIFSEGGLDYLGNPSL VHAQSILAIWACQVILMGAVEGYRIAGGPLGEVVDPLYPGGSFDPLGLAD DPEAFAELKVKEIKNGRLAMFSMFGFFVQAIVTGKGPLENLADHLADPVN NNAWNFATNFVPGSPWYGPDRVKYLGPFSGESPSYLTGEFPGDYGWDTAG LSADPETFAKNRELEVIHCRWAMLGALGCVFPELLARNGVKFGEAVWFKA GSQIFSEGGLDYLGNPSLVHAQSILAIWACQVILMGAVEGYRIAGGPLGE VVDPLYPGGSFDPLGLADDPEAFAELKVKEIKNGRLAMFSMFGFFVQAIV TGKGPLENLADHLADPVNNNAWNFATNFVPG

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Best alignment: 1RWT.pdb  216  VPGSPWYGPDRVKYLGPFSGESPSYLTGEFPGDYGWDTAGLSADPETFAK   265 P S WYGPDR KYLGPFS +PSYLTGE+PGDYGWDTAGLSADPETFAK 2-05100    44  TPQSIWYGPDRPKYLGPFSENTPSYLTGEYPGDYGWDTAGLSADPETFAK    93

1RWT.pdb  266  NRELEVIHCRWAMLGALGCVFPELLARNGVKFGEAVWFKAGSQIFSEGGL   315 NRELEVIH RWAMLGALGC FPE+L++NGVKFGEAVWFKAGSQIFSEGGL 2-05100    94  NRELEVIHSRWAMLGALGCTFPEILSKNGVKFGEAVWFKAGSQIFSEGGL   143

1RWT.pdb  316  DYLGNPSLVHAQSILAIWACQVILMGAVEGYRIAGGPLGEVVDPLYPGGS   365 DYLGNP+L+HAQSILAIWA QV+LMG +EGYRI GGPLGE +DPLYPGG+ 2-05100   144  DYLGNPNLIHAQSILAIWAVQVVLMGFIEGYRIGGGPLGEGLDPLYPGGA   193

1RWT.pdb  366  FDPLGLADDPEAFAELKVKEIKNGRLAMFSMFGFFVQAIVTGKGPLENLA   415 FDPL LA+DPEAF+ELKVKE+KNGRLAMFSMFGFFVQAIVTGKGP+ENL 2-05100   194  FDPLNLAEDPEAFSELKVKELKNGRLAMFSMFGFFVQAIVTGKGPIENLF   243

1RWT.pdb  416  DHLADPVNNNAWNFATNFVPGS   437 DHLADPV NNAW++ATNFVPG+ 2-05100   244  DHLADPVANNAWSYATNFVPGN   265

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Highlighted IDENTICAL residue VAL 229  index1  216  path   44  %Seq  50.00 Highlighted IDENTICAL residue PRO 230  index1  217  path   45  %Seq  50.00 Highlighted IDENTICAL residue GLY 231  index1  218  path   46  %Seq  50.00 Highlighted IDENTICAL residue SER  14  index1  219  path   47  %Seq 100.00 Highlighted IDENTICAL residue TRP  16  index1  221  path   49  %Seq 100.00 Highlighted IDENTICAL residue TYR  17  index1  222  path   50  %Seq 100.00 Highlighted IDENTICAL residue GLY  18  index1  223  path   51  %Seq 100.00 Highlighted IDENTICAL residue PRO  19  index1  224  path   52  %Seq 100.00 Highlighted IDENTICAL residue ASP  20  index1  225  path   53  %Seq 100.00 Highlighted IDENTICAL residue ARG  21  index1  226  path   54  %Seq 100.00 Highlighted IDENTICAL residue LYS  23  index1  228  path   56  %Seq 100.00 Highlighted IDENTICAL residue TYR  24  index1  229  path   57  %Seq 100.00 Highlighted IDENTICAL residue LEU  25  index1  230  path   58  %Seq 100.00 Highlighted IDENTICAL residue GLY  26  index1  231  path   59  %Seq 100.00 Highlighted IDENTICAL residue PRO  27  index1  232  path   60  %Seq 100.00 Highlighted IDENTICAL residue PHE  28  index1  233  path   61  %Seq 100.00 Highlighted IDENTICAL residue SER  29  index1  234  path   62  %Seq 100.00 Highlighted IDENTICAL residue PRO  33  index1  238  path   66  %Seq 100.00 Highlighted IDENTICAL residue SER  34  index1  239  path   67  %Seq 100.00 Highlighted IDENTICAL residue TYR  35  index1  240  path   68  %Seq 100.00 Highlighted IDENTICAL residue LEU  36  index1  241  path   69  %Seq 100.00 Highlighted IDENTICAL residue THR  37  index1  242  path   70  %Seq 100.00 Highlighted IDENTICAL residue GLY  38  index1  243  path   71  %Seq 100.00 Highlighted IDENTICAL residue GLU  39  index1  244  path   72  %Seq 100.00 Highlighted IDENTICAL residue PRO  41  index1  246  path   74  %Seq 100.00 Highlighted IDENTICAL residue GLY  42  index1  247  path   75  %Seq 100.00 Highlighted IDENTICAL residue ASP  43  index1  248  path   76  %Seq 100.00 Highlighted IDENTICAL residue TYR  44  index1  249  path   77  %Seq 100.00 Highlighted IDENTICAL residue GLY  45  index1  250  path   78  %Seq 100.00 Highlighted IDENTICAL residue TRP  46  index1  251  path   79  %Seq 100.00 Highlighted IDENTICAL residue ASP  47  index1  252  path   80  %Seq 100.00 Highlighted IDENTICAL residue THR  48  index1  253  path   81  %Seq 100.00 Highlighted IDENTICAL residue ALA  49  index1  254  path   82  %Seq 100.00 Highlighted IDENTICAL residue GLY  50  index1  255  path   83  %Seq 100.00 Highlighted IDENTICAL residue LEU  51  index1  256  path   84  %Seq 100.00 Highlighted IDENTICAL residue SER  52  index1  257  path   85  %Seq 100.00 Highlighted IDENTICAL residue ALA  53  index1  258  path   86  %Seq 100.00 Highlighted IDENTICAL residue ASP  54  index1  259  path   87  %Seq 100.00 Highlighted IDENTICAL residue PRO  55  index1  260  path   88  %Seq 100.00 Highlighted IDENTICAL residue GLU  56  index1  261  path   89  %Seq 100.00 Highlighted IDENTICAL residue THR  57  index1  262  path   90  %Seq 100.00 Highlighted IDENTICAL residue PHE  58  index1  263  path   91  %Seq 100.00 Highlighted IDENTICAL residue ALA  59  index1  264  path   92  %Seq 100.00 Highlighted IDENTICAL residue LYS  60  index1  265  path   93  %Seq 100.00 Highlighted IDENTICAL residue ASN  61  index1  266  path   94  %Seq 100.00 Highlighted IDENTICAL residue ARG  62  index1  267  path   95  %Seq 100.00 Highlighted IDENTICAL residue GLU  63  index1  268  path   96  %Seq 100.00 Highlighted IDENTICAL residue LEU  64  index1  269  path   97  %Seq 100.00 Highlighted IDENTICAL residue GLU  65  index1  270  path   98  %Seq 100.00 Highlighted IDENTICAL residue VAL  66  index1  271  path   99  %Seq 100.00 Highlighted IDENTICAL residue ILE  67  index1  272  path  100  %Seq 100.00 Highlighted IDENTICAL residue HIS  68  index1  273  path  101  %Seq 100.00 Highlighted IDENTICAL residue ARG  70  index1  275  path  103  %Seq 100.00 Highlighted IDENTICAL residue TRP  71  index1  276  path  104  %Seq 100.00 Highlighted IDENTICAL residue ALA  72  index1  277  path  105  %Seq 100.00 Highlighted IDENTICAL residue MET  73  index1  278  path  106  %Seq 100.00 Highlighted IDENTICAL residue LEU  74  index1  279  path  107  %Seq 100.00 Highlighted IDENTICAL residue GLY  75  index1  280  path  108  %Seq 100.00 Highlighted IDENTICAL residue ALA  76  index1  281  path  109  %Seq 100.00 Highlighted IDENTICAL residue LEU  77  index1  282  path  110  %Seq 100.00 Highlighted IDENTICAL residue GLY  78  index1  283  path  111  %Seq 100.00 Highlighted IDENTICAL residue CYS  79  index1  284  path  112  %Seq 100.00 Highlighted IDENTICAL residue PHE  81  index1  286  path  114  %Seq 100.00 Highlighted IDENTICAL residue PRO  82  index1  287  path  115  %Seq 100.00 Highlighted IDENTICAL residue GLU  83  index1  288  path  116  %Seq 100.00 Highlighted IDENTICAL residue LEU  85  index1  290  path  118  %Seq 100.00 Highlighted IDENTICAL residue ASN  88  index1  293  path  121  %Seq 100.00 Highlighted IDENTICAL residue GLY  89  index1  294  path  122  %Seq 100.00 Highlighted IDENTICAL residue VAL  90  index1  295  path  123  %Seq 100.00 Highlighted IDENTICAL residue LYS  91  index1  296  path  124  %Seq 100.00 Highlighted IDENTICAL residue PHE  92  index1  297  path  125  %Seq 100.00 Highlighted IDENTICAL residue GLY  93  index1  298  path  126  %Seq 100.00 Highlighted IDENTICAL residue GLU  94  index1  299  path  127  %Seq 100.00 Highlighted IDENTICAL residue ALA  95  index1  300  path  128  %Seq 100.00 Highlighted IDENTICAL residue VAL  96  index1  301  path  129  %Seq 100.00 Highlighted IDENTICAL residue TRP  97  index1  302  path  130  %Seq 100.00 Highlighted IDENTICAL residue PHE  98  index1  303  path  131  %Seq 100.00 Highlighted IDENTICAL residue LYS  99  index1  304  path  132  %Seq 100.00 Highlighted IDENTICAL residue ALA 100  index1  305  path  133  %Seq 100.00 Highlighted IDENTICAL residue GLY 101  index1  306  path  134  %Seq 100.00 Highlighted IDENTICAL residue SER 102  index1  307  path  135  %Seq 100.00 Highlighted IDENTICAL residue GLN 103  index1  308  path  136  %Seq 100.00 Highlighted IDENTICAL residue ILE 104  index1  309  path  137  %Seq 100.00 Highlighted IDENTICAL residue PHE 105  index1  310  path  138  %Seq 100.00 Highlighted IDENTICAL residue SER 106  index1  311  path  139  %Seq 100.00 Highlighted IDENTICAL residue GLU 107  index1  312  path  140  %Seq 100.00 Highlighted IDENTICAL residue GLY 108  index1  313  path  141  %Seq 100.00 Highlighted IDENTICAL residue GLY 109  index1  314  path  142  %Seq 100.00 Highlighted IDENTICAL residue LEU 110  index1  315  path  143  %Seq 100.00 Highlighted IDENTICAL residue ASP 111  index1  316  path  144  %Seq 100.00 Highlighted IDENTICAL residue TYR 112  index1  317  path  145  %Seq 100.00 Highlighted IDENTICAL residue LEU 113  index1  318  path  146  %Seq 100.00 Highlighted IDENTICAL residue GLY 114  index1  319  path  147  %Seq 100.00 Highlighted IDENTICAL residue ASN 115  index1  320  path  148  %Seq 100.00 Highlighted IDENTICAL residue PRO 116  index1  321  path  149  %Seq 100.00 Highlighted IDENTICAL residue LEU 118  index1  323  path  151  %Seq 100.00 Highlighted IDENTICAL residue HIS 120  index1  325  path  153  %Seq 100.00 Highlighted IDENTICAL residue ALA 121  index1  326  path  154  %Seq 100.00 Highlighted IDENTICAL residue GLN 122  index1  327  path  155  %Seq 100.00 Highlighted IDENTICAL residue SER 123  index1  328  path  156  %Seq 100.00 Highlighted IDENTICAL residue ILE 124  index1  329  path  157  %Seq 100.00 Highlighted IDENTICAL residue LEU 125  index1  330  path  158  %Seq 100.00 Highlighted IDENTICAL residue ALA 126  index1  331  path  159  %Seq 100.00 Highlighted IDENTICAL residue ILE 127  index1  332  path  160  %Seq 100.00 Highlighted IDENTICAL residue TRP 128  index1  333  path  161  %Seq 100.00 Highlighted IDENTICAL residue ALA 129  index1  334  path  162  %Seq 100.00 Highlighted IDENTICAL residue GLN 131  index1  336  path  164  %Seq 100.00 Highlighted IDENTICAL residue VAL 132  index1  337  path  165  %Seq 100.00 Highlighted IDENTICAL residue LEU 134  index1  339  path  167  %Seq 100.00 Highlighted IDENTICAL residue MET 135  index1  340  path  168  %Seq 100.00 Highlighted IDENTICAL residue GLY 136  index1  341  path  169  %Seq 100.00 Highlighted IDENTICAL residue GLU 139  index1  344  path  172  %Seq 100.00 Highlighted IDENTICAL residue GLY 140  index1  345  path  173  %Seq 100.00 Highlighted IDENTICAL residue TYR 141  index1  346  path  174  %Seq 100.00 Highlighted IDENTICAL residue ARG 142  index1  347  path  175  %Seq 100.00 Highlighted IDENTICAL residue ILE 143  index1  348  path  176  %Seq 100.00 Highlighted IDENTICAL residue GLY 145  index1  350  path  178  %Seq 100.00 Highlighted IDENTICAL residue GLY 146  index1  351  path  179  %Seq 100.00 Highlighted IDENTICAL residue PRO 147  index1  352  path  180  %Seq 100.00 Highlighted IDENTICAL residue LEU 148  index1  353  path  181  %Seq 100.00 Highlighted IDENTICAL residue GLY 149  index1  354  path  182  %Seq 100.00 Highlighted IDENTICAL residue GLU 150  index1  355  path  183  %Seq 100.00 Highlighted IDENTICAL residue ASP 153  index1  358  path  186  %Seq 100.00 Highlighted IDENTICAL residue PRO 154  index1  359  path  187  %Seq 100.00 Highlighted IDENTICAL residue LEU 155  index1  360  path  188  %Seq 100.00 Highlighted IDENTICAL residue TYR 156  index1  361  path  189  %Seq 100.00 Highlighted IDENTICAL residue PRO 157  index1  362  path  190  %Seq 100.00 Highlighted IDENTICAL residue GLY 158  index1  363  path  191  %Seq 100.00 Highlighted IDENTICAL residue GLY 159  index1  364  path  192  %Seq 100.00 Highlighted IDENTICAL residue PHE 161  index1  366  path  194  %Seq 100.00 Highlighted IDENTICAL residue ASP 162  index1  367  path  195  %Seq 100.00 Highlighted IDENTICAL residue PRO 163  index1  368  path  196  %Seq 100.00 Highlighted IDENTICAL residue LEU 164  index1  369  path  197  %Seq 100.00 Highlighted IDENTICAL residue LEU 166  index1  371  path  199  %Seq 100.00 Highlighted IDENTICAL residue ALA 167  index1  372  path  200  %Seq 100.00 Highlighted IDENTICAL residue ASP 169  index1  374  path  202  %Seq 100.00 Highlighted IDENTICAL residue PRO 170  index1  375  path  203  %Seq 100.00 Highlighted IDENTICAL residue GLU 171  index1  376  path  204  %Seq 100.00 Highlighted IDENTICAL residue ALA 172  index1  377  path  205  %Seq 100.00 Highlighted IDENTICAL residue PHE 173  index1  378  path  206  %Seq 100.00 Highlighted IDENTICAL residue GLU 175  index1  380  path  208  %Seq 100.00 Highlighted IDENTICAL residue LEU 176  index1  381  path  209  %Seq 100.00 Highlighted IDENTICAL residue LYS 177  index1  382  path  210  %Seq 100.00 Highlighted IDENTICAL residue VAL 178  index1  383  path  211  %Seq 100.00 Highlighted IDENTICAL residue LYS 179  index1  384  path  212  %Seq 100.00 Highlighted IDENTICAL residue GLU 180  index1  385  path  213  %Seq 100.00 Highlighted IDENTICAL residue LYS 182  index1  387  path  215  %Seq 100.00 Highlighted IDENTICAL residue ASN 183  index1  388  path  216  %Seq 100.00 Highlighted IDENTICAL residue GLY 184  index1  389  path  217  %Seq 100.00 Highlighted IDENTICAL residue ARG 185  index1  390  path  218  %Seq 100.00 Highlighted IDENTICAL residue LEU 186  index1  391  path  219  %Seq 100.00 Highlighted IDENTICAL residue ALA 187  index1  392  path  220  %Seq 100.00 Highlighted IDENTICAL residue MET 188  index1  393  path  221  %Seq 100.00 Highlighted IDENTICAL residue PHE 189  index1  394  path  222  %Seq 100.00 Highlighted IDENTICAL residue SER 190  index1  395  path  223  %Seq 100.00 Highlighted IDENTICAL residue MET 191  index1  396  path  224  %Seq 100.00 Highlighted IDENTICAL residue PHE 192  index1  397  path  225  %Seq 100.00 Highlighted IDENTICAL residue GLY 193  index1  398  path  226  %Seq 100.00 Highlighted IDENTICAL residue PHE 194  index1  399  path  227  %Seq 100.00 Highlighted IDENTICAL residue PHE 195  index1  400  path  228  %Seq 100.00 Highlighted IDENTICAL residue VAL 196  index1  401  path  229  %Seq 100.00 Highlighted IDENTICAL residue GLN 197  index1  402  path  230  %Seq 100.00 Highlighted IDENTICAL residue ALA 198  index1  403  path  231  %Seq 100.00 Highlighted IDENTICAL residue ILE 199  index1  404  path  232  %Seq 100.00 Highlighted IDENTICAL residue VAL 200  index1  405  path  233  %Seq 100.00 Highlighted IDENTICAL residue THR 201  index1  406  path  234  %Seq 100.00 Highlighted IDENTICAL residue GLY 202  index1  407  path  235  %Seq 100.00 Highlighted IDENTICAL residue LYS 203  index1  408  path  236  %Seq 100.00 Highlighted IDENTICAL residue GLY 204  index1  409  path  237  %Seq 100.00 Highlighted IDENTICAL residue PRO 205  index1  410  path  238  %Seq 100.00 Highlighted IDENTICAL residue GLU 207  index1  412  path  240  %Seq 100.00 Highlighted IDENTICAL residue ASN 208  index1  413  path  241  %Seq 100.00 Highlighted IDENTICAL residue LEU 209  index1  414  path  242  %Seq 100.00 Highlighted IDENTICAL residue ASP 211  index1  416  path  244  %Seq 100.00 Highlighted IDENTICAL residue HIS 212  index1  417  path  245  %Seq 100.00 Highlighted IDENTICAL residue LEU 213  index1  418  path  246  %Seq 100.00 Highlighted IDENTICAL residue ALA 214  index1  419  path  247  %Seq 100.00 Highlighted IDENTICAL residue ASP 215  index1  420  path  248  %Seq 100.00 Highlighted IDENTICAL residue PRO 216  index1  421  path  249  %Seq 100.00 Highlighted IDENTICAL residue VAL 217  index1  422  path  250  %Seq 100.00 Highlighted IDENTICAL residue ASN 219  index1  424  path  252  %Seq 100.00 Highlighted IDENTICAL residue ASN 220  index1  425  path  253  %Seq 100.00 Highlighted IDENTICAL residue ALA 221  index1  426  path  254  %Seq 100.00 Highlighted IDENTICAL residue TRP 222  index1  427  path  255  %Seq 100.00 Highlighted IDENTICAL residue ALA 225  index1  430  path  258  %Seq 100.00 Highlighted IDENTICAL residue THR 226  index1  431  path  259  %Seq 100.00 Highlighted IDENTICAL residue ASN 227  index1  432  path  260  %Seq 100.00 Highlighted IDENTICAL residue PHE 228  index1  433  path  261  %Seq 100.00 Highlighted IDENTICAL residue VAL 229  index1  434  path  262  %Seq 100.00 Highlighted IDENTICAL residue PRO 230  index1  435  path  263  %Seq 100.00 Highlighted IDENTICAL residue GLY 231  index1  436  path  264  %Seq 100.00 Highlighted IDENTICAL residue SER  14  index1  437  path  265  %Seq  50.00 Highlighted 192 residues for visualization

Wrote PyMOL macro into file /usr/local/www/html/proteins/htdocs/results/At2g05100-c1rwta_.pir.txt.1RWT.pdb.conservation.pml

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The program

/usr/local/www/html/proteins/Compiled_Programs/WYRM/PyMOL_highlight_conserved_residues At2g05100-c1rwta_.pir.txt PIR amino_acid 1RWT.pdb _ 100.0 BLOSUM62.dat

completed successfully.

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