At2g04030.2/PDB

&&&&&&&&&&&&&&&&&&&& BEGIN /usr/local/www/html/proteins/Compiled_Programs/WYRM/PyMOL_highlight_conserved_residues &&&&&&&&&&&&&&&&&&&&

Successfully read 2 file paths from WYRM_file_paths.txt

generic_input                                        /usr/local/www/html/proteins/workspace/ generic_output                                       /usr/local/www/html/proteins/htdocs/results/

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Sequence file type = 3

Sequence type = 3

Got here 1 Got here 2 Got here 3 Sequence 1 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 Got here 4 Got here 3 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 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/At2g04030-2-2cg9A.pir.txt

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

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>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

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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

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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.

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