FANDOM


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

Successfully read 2 file paths from WYRM_file_paths.txt

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

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

Sequence file type = 3

Sequence type = 3

Got here 1
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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/At2g05710-2b3xA.pir.txt

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

Assigned types to 990 residues in Sequence 2-05710, 0 remain unknown
Assigned types to 888 residues in Sequence 2b3xA, 102 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 At2g05710-2b3xA.pir.txt into sequence alignment.

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

>2B3X.pdb  Made from 6928 ATOM records in 2B3X.pdb
SNPFAHLAEPLDPVQPGKKFFNLNKLEDSRYGRLPFSIRVLLEAAIRNCD
EFLVKKQDIENILHWNVTQHKNIEVPFKPARVILQDFTGVPAVVDFAAMR
DAVKKLGGDPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNR
ERFEFLKWGSQAFHNMRIIPPGSGIIHQVNLEYLARVVFDQDGYYYPDSL
VGTDSHTTMIDGLGILGWGVGGIEAEAVMLGQPISMVLPQVIGYRLMGKP
HPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCP
EYGATAAFFPVDEVSITYLVQTGRDEEKLKYIKKYLQAVGMFRDFNDPSQ
DPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSDMKKDFESCLGAKQGFKG
FQVAPEHHNDHKTFIYDNTEFTLAHGSVVIAAITSCTNTSNPSVMLGAGL
LAKKAVDAGLNVMPYIKTSLSPGSGVVTYYLQESGVMPYLSQLGFDVVGY
GCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYL
ASPPLVIAYAIAGTIRIDFEKEPLGVNAKGQQVFLKDIWPTRDEIQAVER
QYVIPGMFKEVYQKIETVNESWNALATPSDKLFFWNSKSTYIKSPPFFEN
LTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGL
TPREFNSYGSRRGNDAVMARGTFANIRLLNRFLNKQAPQTIHLPSGEILD
VFDAAERYQQAGLPLIVLAGKEYGAGSSRDWAAKGPFLLGIKAVLAESYE
RIHRSNLVGMGVIPLEYLPGENADALGLTGQERYTIIIPENLKPQMKVQV
KLDTGKTFQAVMRFDTDVELTYFLNGGILNYMIRKMAK

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

Best alignment:
2B3X.pdb    19  KFFNLNKLEDSRYGRLPFSIRVLLEAAIRNCDEFLVKKQDIENILHWNVT    68
                KF++L  L D R  +LP+SIR+LLE+AIRNCD F V K+D+E I+ W  T
2-05710    116  KFYSLPALNDPRVDKLPYSIRILLESAIRNCDNFQVTKEDVEKIIDWEKT   165

2B3X.pdb    69  QHKNIEVPFKPARVILQDFTGVPAVVDFAAMRDAVKKLGGDPEKINPVCP   118
                  K +E+PFKPARV+LQDFTGVPAVVD A MRDA+ KLG D  KINP+ P
2-05710    166  SPKQVEIPFKPARVLLQDFTGVPAVVDLACMRDAMNKLGSDSNKINPLVP   215

2B3X.pdb   119  ADLVIDHSIQVDFNRRADSLQKNQDLEFERNRERFEFLKWGSQAFHNMRI   168
                 DLVIDHS+QVD  R  +++Q N +LEF+RN+ERF FLKWGS AF NM +
2-05710    216  VDLVIDHSVQVDVARSENAVQANMELEFQRNKERFAFLKWGSTAFQNMLV   265

2B3X.pdb   169  IPPGSGIIHQVNLEYLARVVFDQDGYYYPDSLVGTDSHTTMIDGLGILGW   218
                +PPGSGI+HQVNLEYL RVVF+  G  YPDS+VGTDSHTTMIDGLG+ GW
2-05710    266  VPPGSGIVHQVNLEYLGRVVFNTKGLLYPDSVVGTDSHTTMIDGLGVAGW   315

2B3X.pdb   219  GVGGIEAEAVMLGQPISMVLPQVIGYRLMGKPHPLVTSTDIVLTITKHLR   268
                GVGGIEAEA MLGQP+SMVLP V+G++L GK    VT+TD+VLT+T+ LR
2-05710    316  GVGGIEAEATMLGQPMSMVLPGVVGFKLAGKMRNGVTATDLVLTVTQMLR   365

2B3X.pdb   269  QVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSITY   318
                + GVVGKFVEF+G G++ LS+ADRATIANM PEYGAT  FFPVD V++ Y
2-05710    366  KHGVVGKFVEFYGNGMSGLSLADRATIANMSPEYGATMGFFPVDHVTLQY   415

2B3X.pdb   319  LVQTGRDEEKLKYIKKYLQAVGMFRDFNDPSQDPDFTQVVELDLKTVVPC   368
                L  TGR +E +  I+ YL+A  MF D+N+P QD  ++  +EL+L  V PC
2-05710    416  LKLTGRSDETVAMIEAYLRANNMFVDYNEPQQDRVYSSYLELNLDDVEPC   465

2B3X.pdb   369  CSGPKRPQDKVAVSDMKKDFESCLGAKQGFKGFQVAPEHHNDHKTFIYDN   418
                 SGPKRP D+V + +MK D+ SCL +K GFKGF +  E       F +D 
2-05710    466  ISGPKRPHDRVTLKEMKADWHSCLDSKVGFKGFAIPKEAQEKVVNFSFDG   515

2B3X.pdb   419  TEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVDAGLNVMPYIKT   468
                    L HGSVVIAAITSCTNTSNPSVMLGAGL+AKKA D GL V P+IKT
2-05710    516  QPAELKHGSVVIAAITSCTNTSNPSVMLGAGLVAKKACDLGLQVKPWIKT   565

2B3X.pdb   469  SLSPGSGVVTYYLQESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVE   518
                SL+PGSGVVT YL +SG+  YL++ GF++VGYGC TCIGNSG + E V  
2-05710    566  SLAPGSGVVTKYLLKSGLQEYLNEQGFNIVGYGCTTCIGNSGEINESVGA   615

2B3X.pdb   519  AITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIAGTIRID   568
                AIT+ D+VA  VLSGNRNFEGRVHP TRANYLASPPLV+AYA+AGT+ ID
2-05710    616  AITENDIVAAAVLSGNRNFEGRVHPLTRANYLASPPLVVAYALAGTVNID   665

2B3X.pdb   569  FEKEPLGVNAKGQQVFLKDIWPTRDEIQAVERQYVIPGMFKEVYQKIETV   618
                FE EP+G    G+ VFL+DIWPT +EI  V +  V+P MF+  Y+ I   
2-05710    666  FETEPIGKGKNGKDVFLRDIWPTTEEIAEVVQSSVLPDMFRATYESITKG   715

2B3X.pdb   619  NESWNALATPSDKLFFWNSKSTYIKSPPFFENLTLDLQPPKSIVDAYVLL   668
                N  WN L+ P + L+ W+  STYI  PP+F+++T+D   P ++ DAY LL
2-05710    716  NPMWNKLSVPENTLYSWDPNSTYIHEPPYFKDMTMDPPGPHNVKDAYCLL   765

2B3X.pdb   669  NLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAVM   718
                N GDS+TTDHISPAGNI ++SPAA++L  RG+  ++FNSYGSRRGND +M
2-05710    766  NFGDSITTDHISPAGNIQKDSPAAKFLMERGVDRKDFNSYGSRRGNDEIM   815

2B3X.pdb   719  ARGTFANIRLLNRFLNKQ-APQTIHLPSGEILDVFDAAERYQQAGLPLIV   767
                ARGTFANIR++N+ +N +  P+T+H+PSGE L VFDAA RY+ +G   I+
2-05710    816  ARGTFANIRIVNKLMNGEVGPKTVHIPSGEKLSVFDAAMRYKSSGEDTII   865

2B3X.pdb   768  LAGKEYGAGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEY   817
                LAG EYG+GSSRDWAAKGP L G+KAV+A+S+ERIHRSNLVGMG+IPL +
2-05710    866  LAGAEYGSGSSRDWAAKGPMLQGVKAVIAKSFERIHRSNLVGMGIIPLCF   915

2B3X.pdb   818  LPGENADALGLTGQERYTIIIP---ENLKPQMKVQVKLDTGKTFQAVMRF   864
                  GE+AD LGLTG ERYTI +P     ++P   V V  D GK+F   +RF
2-05710    916  KSGEDADTLGLTGHERYTIHLPTDISEIRPGQDVTVTTDNGKSFTCTVRF   965

2B3X.pdb   865  DTDVELTYFLNGGILNYMIRKMAK   888
                DT+VEL YF +GGIL Y+IR ++K
2-05710    966  DTEVELAYFNHGGILPYVIRNLSK   989

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

Highlighted IDENTICAL residue LYS   20  index1   19  path  116  %Seq 100.00
Highlighted IDENTICAL residue PHE   21  index1   20  path  117  %Seq 100.00
Highlighted IDENTICAL residue LEU   24  index1   23  path  120  %Seq 100.00
Highlighted IDENTICAL residue LEU   27  index1   26  path  123  %Seq 100.00
Highlighted IDENTICAL residue ASP   29  index1   28  path  125  %Seq 100.00
Highlighted IDENTICAL residue ARG   31  index1   30  path  127  %Seq 100.00
Highlighted IDENTICAL residue LEU   35  index1   34  path  131  %Seq 100.00
Highlighted IDENTICAL residue PRO   36  index1   35  path  132  %Seq 100.00
Highlighted IDENTICAL residue SER   38  index1   37  path  134  %Seq 100.00
Highlighted IDENTICAL residue ILE   39  index1   38  path  135  %Seq 100.00
Highlighted IDENTICAL residue ARG   40  index1   39  path  136  %Seq 100.00
Highlighted IDENTICAL residue LEU   42  index1   41  path  138  %Seq 100.00
Highlighted IDENTICAL residue LEU   43  index1   42  path  139  %Seq 100.00
Highlighted IDENTICAL residue GLU   44  index1   43  path  140  %Seq 100.00
Highlighted IDENTICAL residue ALA   46  index1   45  path  142  %Seq 100.00
Highlighted IDENTICAL residue ILE   47  index1   46  path  143  %Seq 100.00
Highlighted IDENTICAL residue ARG   48  index1   47  path  144  %Seq 100.00
Highlighted IDENTICAL residue ASN   49  index1   48  path  145  %Seq 100.00
Highlighted IDENTICAL residue CYS   50  index1   49  path  146  %Seq 100.00
Highlighted IDENTICAL residue ASP   51  index1   50  path  147  %Seq 100.00
Highlighted IDENTICAL residue PHE   53  index1   52  path  149  %Seq 100.00
Highlighted IDENTICAL residue VAL   55  index1   54  path  151  %Seq 100.00
Highlighted IDENTICAL residue LYS   57  index1   56  path  153  %Seq 100.00
Highlighted IDENTICAL residue ASP   59  index1   58  path  155  %Seq 100.00
Highlighted IDENTICAL residue GLU   61  index1   60  path  157  %Seq 100.00
Highlighted IDENTICAL residue ILE   63  index1   62  path  159  %Seq 100.00
Highlighted IDENTICAL residue TRP   66  index1   65  path  162  %Seq 100.00
Highlighted IDENTICAL residue THR   69  index1   68  path  165  %Seq 100.00
Highlighted IDENTICAL residue LYS   72  index1   71  path  168  %Seq 100.00
Highlighted IDENTICAL residue GLU   75  index1   74  path  171  %Seq 100.00
Highlighted IDENTICAL residue PRO   77  index1   76  path  173  %Seq 100.00
Highlighted IDENTICAL residue PHE   78  index1   77  path  174  %Seq 100.00
Highlighted IDENTICAL residue LYS   79  index1   78  path  175  %Seq 100.00
Highlighted IDENTICAL residue PRO   80  index1   79  path  176  %Seq 100.00
Highlighted IDENTICAL residue ALA   81  index1   80  path  177  %Seq 100.00
Highlighted IDENTICAL residue ARG   82  index1   81  path  178  %Seq 100.00
Highlighted IDENTICAL residue VAL   83  index1   82  path  179  %Seq 100.00
Highlighted IDENTICAL residue LEU   85  index1   84  path  181  %Seq 100.00
Highlighted IDENTICAL residue GLN   86  index1   85  path  182  %Seq 100.00
Highlighted IDENTICAL residue ASP   87  index1   86  path  183  %Seq 100.00
Highlighted IDENTICAL residue PHE   88  index1   87  path  184  %Seq 100.00
Highlighted IDENTICAL residue THR   89  index1   88  path  185  %Seq 100.00
Highlighted IDENTICAL residue GLY   90  index1   89  path  186  %Seq 100.00
Highlighted IDENTICAL residue VAL   91  index1   90  path  187  %Seq 100.00
Highlighted IDENTICAL residue PRO   92  index1   91  path  188  %Seq 100.00
Highlighted IDENTICAL residue ALA   93  index1   92  path  189  %Seq 100.00
Highlighted IDENTICAL residue VAL   94  index1   93  path  190  %Seq 100.00
Highlighted IDENTICAL residue VAL   95  index1   94  path  191  %Seq 100.00
Highlighted IDENTICAL residue ASP   96  index1   95  path  192  %Seq 100.00
Highlighted IDENTICAL residue ALA   98  index1   97  path  194  %Seq 100.00
Highlighted IDENTICAL residue MET  100  index1   99  path  196  %Seq 100.00
Highlighted IDENTICAL residue ARG  101  index1  100  path  197  %Seq 100.00
Highlighted IDENTICAL residue ASP  102  index1  101  path  198  %Seq 100.00
Highlighted IDENTICAL residue ALA  103  index1  102  path  199  %Seq 100.00
Highlighted IDENTICAL residue LYS  106  index1  105  path  202  %Seq 100.00
Highlighted IDENTICAL residue LEU  107  index1  106  path  203  %Seq 100.00
Highlighted IDENTICAL residue GLY  108  index1  107  path  204  %Seq 100.00
Highlighted IDENTICAL residue ASP  110  index1  109  path  206  %Seq 100.00
Highlighted IDENTICAL residue LYS  113  index1  112  path  209  %Seq 100.00
Highlighted IDENTICAL residue ILE  114  index1  113  path  210  %Seq 100.00
Highlighted IDENTICAL residue ASN  115  index1  114  path  211  %Seq 100.00
Highlighted IDENTICAL residue PRO  116  index1  115  path  212  %Seq 100.00
Highlighted IDENTICAL residue PRO  119  index1  118  path  215  %Seq 100.00
Highlighted IDENTICAL residue ASP  121  index1  120  path  217  %Seq 100.00
Highlighted IDENTICAL residue LEU  122  index1  121  path  218  %Seq 100.00
Highlighted IDENTICAL residue VAL  123  index1  122  path  219  %Seq 100.00
Highlighted IDENTICAL residue ILE  124  index1  123  path  220  %Seq 100.00
Highlighted IDENTICAL residue ASP  125  index1  124  path  221  %Seq 100.00
Highlighted IDENTICAL residue HIS  126  index1  125  path  222  %Seq 100.00
Highlighted IDENTICAL residue SER  127  index1  126  path  223  %Seq 100.00
Highlighted IDENTICAL residue GLN  129  index1  128  path  225  %Seq 100.00
Highlighted IDENTICAL residue VAL  130  index1  129  path  226  %Seq 100.00
Highlighted IDENTICAL residue ASP  131  index1  130  path  227  %Seq 100.00
Highlighted IDENTICAL residue ARG  134  index1  133  path  230  %Seq 100.00
Highlighted IDENTICAL residue GLN  140  index1  139  path  236  %Seq 100.00
Highlighted IDENTICAL residue ASN  142  index1  141  path  238  %Seq 100.00
Highlighted IDENTICAL residue LEU  145  index1  144  path  241  %Seq 100.00
Highlighted IDENTICAL residue GLU  146  index1  145  path  242  %Seq 100.00
Highlighted IDENTICAL residue PHE  147  index1  146  path  243  %Seq 100.00
Highlighted IDENTICAL residue ARG  149  index1  148  path  245  %Seq 100.00
Highlighted IDENTICAL residue ASN  150  index1  149  path  246  %Seq 100.00
Highlighted IDENTICAL residue GLU  152  index1  151  path  248  %Seq 100.00
Highlighted IDENTICAL residue ARG  153  index1  152  path  249  %Seq 100.00
Highlighted IDENTICAL residue PHE  154  index1  153  path  250  %Seq 100.00
Highlighted IDENTICAL residue PHE  156  index1  155  path  252  %Seq 100.00
Highlighted IDENTICAL residue LEU  157  index1  156  path  253  %Seq 100.00
Highlighted IDENTICAL residue LYS  158  index1  157  path  254  %Seq 100.00
Highlighted IDENTICAL residue TRP  159  index1  158  path  255  %Seq 100.00
Highlighted IDENTICAL residue GLY  160  index1  159  path  256  %Seq 100.00
Highlighted IDENTICAL residue SER  161  index1  160  path  257  %Seq 100.00
Highlighted IDENTICAL residue ALA  163  index1  162  path  259  %Seq 100.00
Highlighted IDENTICAL residue PHE  164  index1  163  path  260  %Seq 100.00
Highlighted IDENTICAL residue ASN  166  index1  165  path  262  %Seq 100.00
Highlighted IDENTICAL residue MET  167  index1  166  path  263  %Seq 100.00
Highlighted IDENTICAL residue PRO  171  index1  170  path  267  %Seq 100.00
Highlighted IDENTICAL residue PRO  172  index1  171  path  268  %Seq 100.00
Highlighted IDENTICAL residue GLY  173  index1  172  path  269  %Seq 100.00
Highlighted IDENTICAL residue SER  174  index1  173  path  270  %Seq 100.00
Highlighted IDENTICAL residue GLY  175  index1  174  path  271  %Seq 100.00
Highlighted IDENTICAL residue ILE  176  index1  175  path  272  %Seq 100.00
Highlighted IDENTICAL residue HIS  178  index1  177  path  274  %Seq 100.00
Highlighted IDENTICAL residue GLN  179  index1  178  path  275  %Seq 100.00
Highlighted IDENTICAL residue VAL  180  index1  179  path  276  %Seq 100.00
Highlighted IDENTICAL residue ASN  181  index1  180  path  277  %Seq 100.00
Highlighted IDENTICAL residue LEU  182  index1  181  path  278  %Seq 100.00
Highlighted IDENTICAL residue GLU  183  index1  182  path  279  %Seq 100.00
Highlighted IDENTICAL residue TYR  184  index1  183  path  280  %Seq 100.00
Highlighted IDENTICAL residue LEU  185  index1  184  path  281  %Seq 100.00
Highlighted IDENTICAL residue ARG  187  index1  186  path  283  %Seq 100.00
Highlighted IDENTICAL residue VAL  188  index1  187  path  284  %Seq 100.00
Highlighted IDENTICAL residue VAL  189  index1  188  path  285  %Seq 100.00
Highlighted IDENTICAL residue PHE  190  index1  189  path  286  %Seq 100.00
Highlighted IDENTICAL residue GLY  194  index1  193  path  290  %Seq 100.00
Highlighted IDENTICAL residue TYR  197  index1  196  path  293  %Seq 100.00
Highlighted IDENTICAL residue PRO  198  index1  197  path  294  %Seq 100.00
Highlighted IDENTICAL residue ASP  199  index1  198  path  295  %Seq 100.00
Highlighted IDENTICAL residue SER  200  index1  199  path  296  %Seq 100.00
Highlighted IDENTICAL residue VAL  202  index1  201  path  298  %Seq 100.00
Highlighted IDENTICAL residue GLY  203  index1  202  path  299  %Seq 100.00
Highlighted IDENTICAL residue THR  204  index1  203  path  300  %Seq 100.00
Highlighted IDENTICAL residue ASP  205  index1  204  path  301  %Seq 100.00
Highlighted IDENTICAL residue SER  206  index1  205  path  302  %Seq 100.00
Highlighted IDENTICAL residue HIS  207  index1  206  path  303  %Seq 100.00
Highlighted IDENTICAL residue THR  208  index1  207  path  304  %Seq 100.00
Highlighted IDENTICAL residue THR  209  index1  208  path  305  %Seq 100.00
Highlighted IDENTICAL residue MET  210  index1  209  path  306  %Seq 100.00
Highlighted IDENTICAL residue ILE  211  index1  210  path  307  %Seq 100.00
Highlighted IDENTICAL residue ASP  212  index1  211  path  308  %Seq 100.00
Highlighted IDENTICAL residue GLY  213  index1  212  path  309  %Seq 100.00
Highlighted IDENTICAL residue LEU  214  index1  213  path  310  %Seq 100.00
Highlighted IDENTICAL residue GLY  215  index1  214  path  311  %Seq 100.00
Highlighted IDENTICAL residue GLY  218  index1  217  path  314  %Seq 100.00
Highlighted IDENTICAL residue TRP  219  index1  218  path  315  %Seq 100.00
Highlighted IDENTICAL residue GLY  220  index1  219  path  316  %Seq 100.00
Highlighted IDENTICAL residue VAL  221  index1  220  path  317  %Seq 100.00
Highlighted IDENTICAL residue GLY  222  index1  221  path  318  %Seq 100.00
Highlighted IDENTICAL residue GLY  223  index1  222  path  319  %Seq 100.00
Highlighted IDENTICAL residue ILE  224  index1  223  path  320  %Seq 100.00
Highlighted IDENTICAL residue GLU  225  index1  224  path  321  %Seq 100.00
Highlighted IDENTICAL residue ALA  226  index1  225  path  322  %Seq 100.00
Highlighted IDENTICAL residue GLU  227  index1  226  path  323  %Seq 100.00
Highlighted IDENTICAL residue ALA  228  index1  227  path  324  %Seq 100.00
Highlighted IDENTICAL residue MET  230  index1  229  path  326  %Seq 100.00
Highlighted IDENTICAL residue LEU  231  index1  230  path  327  %Seq 100.00
Highlighted IDENTICAL residue GLY  232  index1  231  path  328  %Seq 100.00
Highlighted IDENTICAL residue GLN  233  index1  232  path  329  %Seq 100.00
Highlighted IDENTICAL residue PRO  234  index1  233  path  330  %Seq 100.00
Highlighted IDENTICAL residue SER  236  index1  235  path  332  %Seq 100.00
Highlighted IDENTICAL residue MET  237  index1  236  path  333  %Seq 100.00
Highlighted IDENTICAL residue VAL  238  index1  237  path  334  %Seq 100.00
Highlighted IDENTICAL residue LEU  239  index1  238  path  335  %Seq 100.00
Highlighted IDENTICAL residue PRO  240  index1  239  path  336  %Seq 100.00
Highlighted IDENTICAL residue VAL  242  index1  241  path  338  %Seq 100.00
Highlighted IDENTICAL residue GLY  244  index1  243  path  340  %Seq 100.00
Highlighted IDENTICAL residue LEU  247  index1  246  path  343  %Seq 100.00
Highlighted IDENTICAL residue GLY  249  index1  248  path  345  %Seq 100.00
Highlighted IDENTICAL residue LYS  250  index1  249  path  346  %Seq 100.00
Highlighted IDENTICAL residue VAL  255  index1  254  path  351  %Seq 100.00
Highlighted IDENTICAL residue THR  256  index1  255  path  352  %Seq 100.00
Highlighted IDENTICAL residue THR  258  index1  257  path  354  %Seq 100.00
Highlighted IDENTICAL residue ASP  259  index1  258  path  355  %Seq 100.00
Highlighted IDENTICAL residue VAL  261  index1  260  path  357  %Seq 100.00
Highlighted IDENTICAL residue LEU  262  index1  261  path  358  %Seq 100.00
Highlighted IDENTICAL residue THR  263  index1  262  path  359  %Seq 100.00
Highlighted IDENTICAL residue THR  265  index1  264  path  361  %Seq 100.00
Highlighted IDENTICAL residue LEU  268  index1  267  path  364  %Seq 100.00
Highlighted IDENTICAL residue ARG  269  index1  268  path  365  %Seq 100.00
Highlighted IDENTICAL residue GLY  272  index1  271  path  368  %Seq 100.00
Highlighted IDENTICAL residue VAL  273  index1  272  path  369  %Seq 100.00
Highlighted IDENTICAL residue VAL  274  index1  273  path  370  %Seq 100.00
Highlighted IDENTICAL residue GLY  275  index1  274  path  371  %Seq 100.00
Highlighted IDENTICAL residue LYS  276  index1  275  path  372  %Seq 100.00
Highlighted IDENTICAL residue PHE  277  index1  276  path  373  %Seq 100.00
Highlighted IDENTICAL residue VAL  278  index1  277  path  374  %Seq 100.00
Highlighted IDENTICAL residue GLU  279  index1  278  path  375  %Seq 100.00
Highlighted IDENTICAL residue PHE  280  index1  279  path  376  %Seq 100.00
Highlighted IDENTICAL residue GLY  282  index1  281  path  378  %Seq 100.00
Highlighted IDENTICAL residue GLY  284  index1  283  path  380  %Seq 100.00
Highlighted IDENTICAL residue LEU  288  index1  287  path  384  %Seq 100.00
Highlighted IDENTICAL residue SER  289  index1  288  path  385  %Seq 100.00
Highlighted IDENTICAL residue ALA  291  index1  290  path  387  %Seq 100.00
Highlighted IDENTICAL residue ASP  292  index1  291  path  388  %Seq 100.00
Highlighted IDENTICAL residue ARG  293  index1  292  path  389  %Seq 100.00
Highlighted IDENTICAL residue ALA  294  index1  293  path  390  %Seq 100.00
Highlighted IDENTICAL residue THR  295  index1  294  path  391  %Seq 100.00
Highlighted IDENTICAL residue ILE  296  index1  295  path  392  %Seq 100.00
Highlighted IDENTICAL residue ALA  297  index1  296  path  393  %Seq 100.00
Highlighted IDENTICAL residue ASN  298  index1  297  path  394  %Seq 100.00
Highlighted IDENTICAL residue MET  299  index1  298  path  395  %Seq 100.00
Highlighted IDENTICAL residue PRO  301  index1  300  path  397  %Seq 100.00
Highlighted IDENTICAL residue GLU  302  index1  301  path  398  %Seq 100.00
Highlighted IDENTICAL residue TYR  303  index1  302  path  399  %Seq 100.00
Highlighted IDENTICAL residue GLY  304  index1  303  path  400  %Seq 100.00
Highlighted IDENTICAL residue ALA  305  index1  304  path  401  %Seq 100.00
Highlighted IDENTICAL residue THR  306  index1  305  path  402  %Seq 100.00
Highlighted IDENTICAL residue PHE  309  index1  308  path  405  %Seq 100.00
Highlighted IDENTICAL residue PHE  310  index1  309  path  406  %Seq 100.00
Highlighted IDENTICAL residue PRO  311  index1  310  path  407  %Seq 100.00
Highlighted IDENTICAL residue VAL  312  index1  311  path  408  %Seq 100.00
Highlighted IDENTICAL residue ASP  313  index1  312  path  409  %Seq 100.00
Highlighted IDENTICAL residue VAL  315  index1  314  path  411  %Seq 100.00
Highlighted IDENTICAL residue TYR  319  index1  318  path  415  %Seq 100.00
Highlighted IDENTICAL residue LEU  320  index1  319  path  416  %Seq 100.00
Highlighted IDENTICAL residue THR  323  index1  322  path  419  %Seq 100.00
Highlighted IDENTICAL residue GLY  324  index1  323  path  420  %Seq 100.00
Highlighted IDENTICAL residue ARG  325  index1  324  path  421  %Seq 100.00
Highlighted IDENTICAL residue GLU  328  index1  327  path  424  %Seq 100.00
Highlighted IDENTICAL residue ILE  333  index1  332  path  429  %Seq 100.00
Highlighted IDENTICAL residue TYR  336  index1  335  path  432  %Seq 100.00
Highlighted IDENTICAL residue LEU  337  index1  336  path  433  %Seq 100.00
Highlighted IDENTICAL residue ALA  339  index1  338  path  435  %Seq 100.00
Highlighted IDENTICAL residue MET  342  index1  341  path  438  %Seq 100.00
Highlighted IDENTICAL residue PHE  343  index1  342  path  439  %Seq 100.00
Highlighted IDENTICAL residue ASP  345  index1  344  path  441  %Seq 100.00
Highlighted IDENTICAL residue ASN  347  index1  346  path  443  %Seq 100.00
Highlighted IDENTICAL residue PRO  349  index1  348  path  445  %Seq 100.00
Highlighted IDENTICAL residue GLN  351  index1  350  path  447  %Seq 100.00
Highlighted IDENTICAL residue ASP  352  index1  351  path  448  %Seq 100.00
Highlighted IDENTICAL residue GLU  360  index1  359  path  456  %Seq 100.00
Highlighted IDENTICAL residue LEU  361  index1  360  path  457  %Seq 100.00
Highlighted IDENTICAL residue LEU  363  index1  362  path  459  %Seq 100.00
Highlighted IDENTICAL residue VAL  366  index1  365  path  462  %Seq 100.00
Highlighted IDENTICAL residue PRO  368  index1  367  path  464  %Seq 100.00
Highlighted IDENTICAL residue CYS  369  index1  368  path  465  %Seq 100.00
Highlighted IDENTICAL residue SER  371  index1  370  path  467  %Seq 100.00
Highlighted IDENTICAL residue GLY  372  index1  371  path  468  %Seq 100.00
Highlighted IDENTICAL residue PRO  373  index1  372  path  469  %Seq 100.00
Highlighted IDENTICAL residue LYS  374  index1  373  path  470  %Seq 100.00
Highlighted IDENTICAL residue ARG  375  index1  374  path  471  %Seq 100.00
Highlighted IDENTICAL residue PRO  376  index1  375  path  472  %Seq 100.00
Highlighted IDENTICAL residue ASP  378  index1  377  path  474  %Seq 100.00
Highlighted IDENTICAL residue VAL  380  index1  379  path  476  %Seq 100.00
Highlighted IDENTICAL residue MET  385  index1  384  path  481  %Seq 100.00
Highlighted IDENTICAL residue LYS  386  index1  385  path  482  %Seq 100.00
Highlighted IDENTICAL residue ASP  388  index1  387  path  484  %Seq 100.00
Highlighted IDENTICAL residue SER  391  index1  390  path  487  %Seq 100.00
Highlighted IDENTICAL residue CYS  392  index1  391  path  488  %Seq 100.00
Highlighted IDENTICAL residue LEU  393  index1  392  path  489  %Seq 100.00
Highlighted IDENTICAL residue LYS  396  index1  395  path  492  %Seq 100.00
Highlighted IDENTICAL residue GLY  398  index1  397  path  494  %Seq 100.00
Highlighted IDENTICAL residue PHE  399  index1  398  path  495  %Seq 100.00
Highlighted IDENTICAL residue LYS  400  index1  399  path  496  %Seq 100.00
Highlighted IDENTICAL residue GLY  401  index1  400  path  497  %Seq 100.00
Highlighted IDENTICAL residue PHE  402  index1  401  path  498  %Seq 100.00
Highlighted IDENTICAL residue GLU  407  index1  406  path  503  %Seq 100.00
Highlighted IDENTICAL residue PHE  415  index1  414  path  511  %Seq 100.00
Highlighted IDENTICAL residue ASP  418  index1  417  path  514  %Seq 100.00
Highlighted IDENTICAL residue LEU  424  index1  423  path  520  %Seq 100.00
Highlighted IDENTICAL residue HIS  426  index1  425  path  522  %Seq 100.00
Highlighted IDENTICAL residue GLY  427  index1  426  path  523  %Seq 100.00
Highlighted IDENTICAL residue SER  428  index1  427  path  524  %Seq 100.00
Highlighted IDENTICAL residue VAL  429  index1  428  path  525  %Seq 100.00
Highlighted IDENTICAL residue VAL  430  index1  429  path  526  %Seq 100.00
Highlighted IDENTICAL residue ILE  431  index1  430  path  527  %Seq 100.00
Highlighted IDENTICAL residue ALA  432  index1  431  path  528  %Seq 100.00
Highlighted IDENTICAL residue ALA  433  index1  432  path  529  %Seq 100.00
Highlighted IDENTICAL residue ILE  434  index1  433  path  530  %Seq 100.00
Highlighted IDENTICAL residue THR  435  index1  434  path  531  %Seq 100.00
Highlighted IDENTICAL residue SER  436  index1  435  path  532  %Seq 100.00
Highlighted IDENTICAL residue CYS  437  index1  436  path  533  %Seq 100.00
Highlighted IDENTICAL residue THR  438  index1  437  path  534  %Seq 100.00
Highlighted IDENTICAL residue ASN  439  index1  438  path  535  %Seq 100.00
Highlighted IDENTICAL residue THR  440  index1  439  path  536  %Seq 100.00
Highlighted IDENTICAL residue SER  441  index1  440  path  537  %Seq 100.00
Highlighted IDENTICAL residue ASN  442  index1  441  path  538  %Seq 100.00
Highlighted IDENTICAL residue PRO  443  index1  442  path  539  %Seq 100.00
Highlighted IDENTICAL residue SER  444  index1  443  path  540  %Seq 100.00
Highlighted IDENTICAL residue VAL  445  index1  444  path  541  %Seq 100.00
Highlighted IDENTICAL residue MET  446  index1  445  path  542  %Seq 100.00
Highlighted IDENTICAL residue LEU  447  index1  446  path  543  %Seq 100.00
Highlighted IDENTICAL residue GLY  448  index1  447  path  544  %Seq 100.00
Highlighted IDENTICAL residue ALA  449  index1  448  path  545  %Seq 100.00
Highlighted IDENTICAL residue GLY  450  index1  449  path  546  %Seq 100.00
Highlighted IDENTICAL residue LEU  451  index1  450  path  547  %Seq 100.00
Highlighted IDENTICAL residue ALA  453  index1  452  path  549  %Seq 100.00
Highlighted IDENTICAL residue LYS  454  index1  453  path  550  %Seq 100.00
Highlighted IDENTICAL residue LYS  455  index1  454  path  551  %Seq 100.00
Highlighted IDENTICAL residue ALA  456  index1  455  path  552  %Seq 100.00
Highlighted IDENTICAL residue ASP  458  index1  457  path  554  %Seq 100.00
Highlighted IDENTICAL residue GLY  460  index1  459  path  556  %Seq 100.00
Highlighted IDENTICAL residue LEU  461  index1  460  path  557  %Seq 100.00
Highlighted IDENTICAL residue VAL  463  index1  462  path  559  %Seq 100.00
Highlighted IDENTICAL residue PRO  465  index1  464  path  561  %Seq 100.00
Highlighted IDENTICAL residue ILE  467  index1  466  path  563  %Seq 100.00
Highlighted IDENTICAL residue LYS  468  index1  467  path  564  %Seq 100.00
Highlighted IDENTICAL residue THR  469  index1  468  path  565  %Seq 100.00
Highlighted IDENTICAL residue SER  470  index1  469  path  566  %Seq 100.00
Highlighted IDENTICAL residue LEU  471  index1  470  path  567  %Seq 100.00
Highlighted IDENTICAL residue PRO  473  index1  472  path  569  %Seq 100.00
Highlighted IDENTICAL residue GLY  474  index1  473  path  570  %Seq 100.00
Highlighted IDENTICAL residue SER  475  index1  474  path  571  %Seq 100.00
Highlighted IDENTICAL residue GLY  476  index1  475  path  572  %Seq 100.00
Highlighted IDENTICAL residue VAL  477  index1  476  path  573  %Seq 100.00
Highlighted IDENTICAL residue VAL  478  index1  477  path  574  %Seq 100.00
Highlighted IDENTICAL residue THR  479  index1  478  path  575  %Seq 100.00
Highlighted IDENTICAL residue TYR  481  index1  480  path  577  %Seq 100.00
Highlighted IDENTICAL residue LEU  482  index1  481  path  578  %Seq 100.00
Highlighted IDENTICAL residue SER  485  index1  484  path  581  %Seq 100.00
Highlighted IDENTICAL residue GLY  486  index1  485  path  582  %Seq 100.00
Highlighted IDENTICAL residue TYR  490  index1  489  path  586  %Seq 100.00
Highlighted IDENTICAL residue LEU  491  index1  490  path  587  %Seq 100.00
Highlighted IDENTICAL residue GLY  495  index1  494  path  591  %Seq 100.00
Highlighted IDENTICAL residue PHE  496  index1  495  path  592  %Seq 100.00
Highlighted IDENTICAL residue VAL  499  index1  498  path  595  %Seq 100.00
Highlighted IDENTICAL residue GLY  500  index1  499  path  596  %Seq 100.00
Highlighted IDENTICAL residue TYR  501  index1  500  path  597  %Seq 100.00
Highlighted IDENTICAL residue GLY  502  index1  501  path  598  %Seq 100.00
Highlighted IDENTICAL residue CYS  503  index1  502  path  599  %Seq 100.00
Highlighted IDENTICAL residue THR  505  index1  504  path  601  %Seq 100.00
Highlighted IDENTICAL residue CYS  506  index1  505  path  602  %Seq 100.00
Highlighted IDENTICAL residue ILE  507  index1  506  path  603  %Seq 100.00
Highlighted IDENTICAL residue GLY  508  index1  507  path  604  %Seq 100.00
Highlighted IDENTICAL residue ASN  509  index1  508  path  605  %Seq 100.00
Highlighted IDENTICAL residue SER  510  index1  509  path  606  %Seq 100.00
Highlighted IDENTICAL residue GLY  511  index1  510  path  607  %Seq 100.00
Highlighted IDENTICAL residue GLU  515  index1  514  path  611  %Seq 100.00
Highlighted IDENTICAL residue VAL  517  index1  516  path  613  %Seq 100.00
Highlighted IDENTICAL residue ALA  520  index1  519  path  616  %Seq 100.00
Highlighted IDENTICAL residue ILE  521  index1  520  path  617  %Seq 100.00
Highlighted IDENTICAL residue THR  522  index1  521  path  618  %Seq 100.00
Highlighted IDENTICAL residue ASP  525  index1  524  path  621  %Seq 100.00
Highlighted IDENTICAL residue VAL  527  index1  526  path  623  %Seq 100.00
Highlighted IDENTICAL residue ALA  528  index1  527  path  624  %Seq 100.00
Highlighted IDENTICAL residue VAL  531  index1  530  path  627  %Seq 100.00
Highlighted IDENTICAL residue LEU  532  index1  531  path  628  %Seq 100.00
Highlighted IDENTICAL residue SER  533  index1  532  path  629  %Seq 100.00
Highlighted IDENTICAL residue GLY  534  index1  533  path  630  %Seq 100.00
Highlighted IDENTICAL residue ASN  535  index1  534  path  631  %Seq 100.00
Highlighted IDENTICAL residue ARG  536  index1  535  path  632  %Seq 100.00
Highlighted IDENTICAL residue ASN  537  index1  536  path  633  %Seq 100.00
Highlighted IDENTICAL residue PHE  538  index1  537  path  634  %Seq 100.00
Highlighted IDENTICAL residue GLU  539  index1  538  path  635  %Seq 100.00
Highlighted IDENTICAL residue GLY  540  index1  539  path  636  %Seq 100.00
Highlighted IDENTICAL residue ARG  541  index1  540  path  637  %Seq 100.00
Highlighted IDENTICAL residue VAL  542  index1  541  path  638  %Seq 100.00
Highlighted IDENTICAL residue HIS  543  index1  542  path  639  %Seq 100.00
Highlighted IDENTICAL residue PRO  544  index1  543  path  640  %Seq 100.00
Highlighted IDENTICAL residue THR  546  index1  545  path  642  %Seq 100.00
Highlighted IDENTICAL residue ARG  547  index1  546  path  643  %Seq 100.00
Highlighted IDENTICAL residue ALA  548  index1  547  path  644  %Seq 100.00
Highlighted IDENTICAL residue ASN  549  index1  548  path  645  %Seq 100.00
Highlighted IDENTICAL residue TYR  550  index1  549  path  646  %Seq 100.00
Highlighted IDENTICAL residue LEU  551  index1  550  path  647  %Seq 100.00
Highlighted IDENTICAL residue ALA  552  index1  551  path  648  %Seq 100.00
Highlighted IDENTICAL residue SER  553  index1  552  path  649  %Seq 100.00
Highlighted IDENTICAL residue PRO  554  index1  553  path  650  %Seq 100.00
Highlighted IDENTICAL residue PRO  555  index1  554  path  651  %Seq 100.00
Highlighted IDENTICAL residue LEU  556  index1  555  path  652  %Seq 100.00
Highlighted IDENTICAL residue VAL  557  index1  556  path  653  %Seq 100.00
Highlighted IDENTICAL residue ALA  559  index1  558  path  655  %Seq 100.00
Highlighted IDENTICAL residue TYR  560  index1  559  path  656  %Seq 100.00
Highlighted IDENTICAL residue ALA  561  index1  560  path  657  %Seq 100.00
Highlighted IDENTICAL residue ALA  563  index1  562  path  659  %Seq 100.00
Highlighted IDENTICAL residue GLY  564  index1  563  path  660  %Seq 100.00
Highlighted IDENTICAL residue THR  565  index1  564  path  661  %Seq 100.00
Highlighted IDENTICAL residue ILE  568  index1  567  path  664  %Seq 100.00
Highlighted IDENTICAL residue ASP  569  index1  568  path  665  %Seq 100.00
Highlighted IDENTICAL residue PHE  570  index1  569  path  666  %Seq 100.00
Highlighted IDENTICAL residue GLU  571  index1  570  path  667  %Seq 100.00
Highlighted IDENTICAL residue GLU  573  index1  572  path  669  %Seq 100.00
Highlighted IDENTICAL residue PRO  574  index1  573  path  670  %Seq 100.00
Highlighted IDENTICAL residue GLY  576  index1  575  path  672  %Seq 100.00
Highlighted IDENTICAL residue GLY  581  index1  580  path  677  %Seq 100.00
Highlighted IDENTICAL residue VAL  584  index1  583  path  680  %Seq 100.00
Highlighted IDENTICAL residue PHE  585  index1  584  path  681  %Seq 100.00
Highlighted IDENTICAL residue LEU  586  index1  585  path  682  %Seq 100.00
Highlighted IDENTICAL residue ASP  588  index1  587  path  684  %Seq 100.00
Highlighted IDENTICAL residue ILE  589  index1  588  path  685  %Seq 100.00
Highlighted IDENTICAL residue TRP  590  index1  589  path  686  %Seq 100.00
Highlighted IDENTICAL residue PRO  591  index1  590  path  687  %Seq 100.00
Highlighted IDENTICAL residue THR  592  index1  591  path  688  %Seq 100.00
Highlighted IDENTICAL residue GLU  595  index1  594  path  691  %Seq 100.00
Highlighted IDENTICAL residue ILE  596  index1  595  path  692  %Seq 100.00
Highlighted IDENTICAL residue VAL  599  index1  598  path  695  %Seq 100.00
Highlighted IDENTICAL residue VAL  604  index1  603  path  700  %Seq 100.00
Highlighted IDENTICAL residue PRO  606  index1  605  path  702  %Seq 100.00
Highlighted IDENTICAL residue MET  608  index1  607  path  704  %Seq 100.00
Highlighted IDENTICAL residue PHE  609  index1  608  path  705  %Seq 100.00
Highlighted IDENTICAL residue TYR  613  index1  612  path  709  %Seq 100.00
Highlighted IDENTICAL residue ILE  616  index1  615  path  712  %Seq 100.00
Highlighted IDENTICAL residue ASN  620  index1  619  path  716  %Seq 100.00
Highlighted IDENTICAL residue TRP  623  index1  622  path  719  %Seq 100.00
Highlighted IDENTICAL residue ASN  624  index1  623  path  720  %Seq 100.00
Highlighted IDENTICAL residue LEU  626  index1  625  path  722  %Seq 100.00
Highlighted IDENTICAL residue PRO  629  index1  628  path  725  %Seq 100.00
Highlighted IDENTICAL residue LEU  633  index1  632  path  729  %Seq 100.00
Highlighted IDENTICAL residue TRP  636  index1  635  path  732  %Seq 100.00
Highlighted IDENTICAL residue SER  640  index1  639  path  736  %Seq 100.00
Highlighted IDENTICAL residue THR  641  index1  640  path  737  %Seq 100.00
Highlighted IDENTICAL residue TYR  642  index1  641  path  738  %Seq 100.00
Highlighted IDENTICAL residue ILE  643  index1  642  path  739  %Seq 100.00
Highlighted IDENTICAL residue PRO  646  index1  645  path  742  %Seq 100.00
Highlighted IDENTICAL residue PRO  647  index1  646  path  743  %Seq 100.00
Highlighted IDENTICAL residue PHE  649  index1  648  path  745  %Seq 100.00
Highlighted IDENTICAL residue THR  653  index1  652  path  749  %Seq 100.00
Highlighted IDENTICAL residue ASP  655  index1  654  path  751  %Seq 100.00
Highlighted IDENTICAL residue PRO  659  index1  658  path  755  %Seq 100.00
Highlighted IDENTICAL residue ASP  664  index1  663  path  760  %Seq 100.00
Highlighted IDENTICAL residue ALA  665  index1  664  path  761  %Seq 100.00
Highlighted IDENTICAL residue TYR  666  index1  665  path  762  %Seq 100.00
Highlighted IDENTICAL residue LEU  668  index1  667  path  764  %Seq 100.00
Highlighted IDENTICAL residue LEU  669  index1  668  path  765  %Seq 100.00
Highlighted IDENTICAL residue ASN  670  index1  669  path  766  %Seq 100.00
Highlighted IDENTICAL residue GLY  672  index1  671  path  768  %Seq 100.00
Highlighted IDENTICAL residue ASP  673  index1  672  path  769  %Seq 100.00
Highlighted IDENTICAL residue SER  674  index1  673  path  770  %Seq 100.00
Highlighted IDENTICAL residue THR  676  index1  675  path  772  %Seq 100.00
Highlighted IDENTICAL residue THR  677  index1  676  path  773  %Seq 100.00
Highlighted IDENTICAL residue ASP  678  index1  677  path  774  %Seq 100.00
Highlighted IDENTICAL residue HIS  679  index1  678  path  775  %Seq 100.00
Highlighted IDENTICAL residue ILE  680  index1  679  path  776  %Seq 100.00
Highlighted IDENTICAL residue SER  681  index1  680  path  777  %Seq 100.00
Highlighted IDENTICAL residue PRO  682  index1  681  path  778  %Seq 100.00
Highlighted IDENTICAL residue ALA  683  index1  682  path  779  %Seq 100.00
Highlighted IDENTICAL residue GLY  684  index1  683  path  780  %Seq 100.00
Highlighted IDENTICAL residue ASN  685  index1  684  path  781  %Seq 100.00
Highlighted IDENTICAL residue ILE  686  index1  685  path  782  %Seq 100.00
Highlighted IDENTICAL residue SER  690  index1  689  path  786  %Seq 100.00
Highlighted IDENTICAL residue PRO  691  index1  690  path  787  %Seq 100.00
Highlighted IDENTICAL residue ALA  692  index1  691  path  788  %Seq 100.00
Highlighted IDENTICAL residue ALA  693  index1  692  path  789  %Seq 100.00
Highlighted IDENTICAL residue LEU  696  index1  695  path  792  %Seq 100.00
Highlighted IDENTICAL residue ARG  699  index1  698  path  795  %Seq 100.00
Highlighted IDENTICAL residue GLY  700  index1  699  path  796  %Seq 100.00
Highlighted IDENTICAL residue PHE  706  index1  705  path  802  %Seq 100.00
Highlighted IDENTICAL residue ASN  707  index1  706  path  803  %Seq 100.00
Highlighted IDENTICAL residue SER  708  index1  707  path  804  %Seq 100.00
Highlighted IDENTICAL residue TYR  709  index1  708  path  805  %Seq 100.00
Highlighted IDENTICAL residue GLY  710  index1  709  path  806  %Seq 100.00
Highlighted IDENTICAL residue SER  711  index1  710  path  807  %Seq 100.00
Highlighted IDENTICAL residue ARG  712  index1  711  path  808  %Seq 100.00
Highlighted IDENTICAL residue ARG  713  index1  712  path  809  %Seq 100.00
Highlighted IDENTICAL residue GLY  714  index1  713  path  810  %Seq 100.00
Highlighted IDENTICAL residue ASN  715  index1  714  path  811  %Seq 100.00
Highlighted IDENTICAL residue ASP  716  index1  715  path  812  %Seq 100.00
Highlighted IDENTICAL residue MET  719  index1  718  path  815  %Seq 100.00
Highlighted IDENTICAL residue ALA  720  index1  719  path  816  %Seq 100.00
Highlighted IDENTICAL residue ARG  721  index1  720  path  817  %Seq 100.00
Highlighted IDENTICAL residue GLY  722  index1  721  path  818  %Seq 100.00
Highlighted IDENTICAL residue THR  723  index1  722  path  819  %Seq 100.00
Highlighted IDENTICAL residue PHE  724  index1  723  path  820  %Seq 100.00
Highlighted IDENTICAL residue ALA  725  index1  724  path  821  %Seq 100.00
Highlighted IDENTICAL residue ASN  726  index1  725  path  822  %Seq 100.00
Highlighted IDENTICAL residue ILE  727  index1  726  path  823  %Seq 100.00
Highlighted IDENTICAL residue ARG  728  index1  727  path  824  %Seq 100.00
Highlighted IDENTICAL residue ASN  731  index1  730  path  827  %Seq 100.00
Highlighted IDENTICAL residue ASN  735  index1  734  path  831  %Seq 100.00
Highlighted IDENTICAL residue LYS  736  index1  735  path  832  %Seq  50.00
Highlighted IDENTICAL residue PRO  739  index1  738  path  836  %Seq 100.00
Highlighted IDENTICAL residue THR  741  index1  740  path  838  %Seq 100.00
Highlighted IDENTICAL residue HIS  743  index1  742  path  840  %Seq 100.00
Highlighted IDENTICAL residue PRO  745  index1  744  path  842  %Seq 100.00
Highlighted IDENTICAL residue SER  746  index1  745  path  843  %Seq 100.00
Highlighted IDENTICAL residue GLY  747  index1  746  path  844  %Seq 100.00
Highlighted IDENTICAL residue GLU  748  index1  747  path  845  %Seq 100.00
Highlighted IDENTICAL residue LEU  750  index1  749  path  847  %Seq 100.00
Highlighted IDENTICAL residue VAL  752  index1  751  path  849  %Seq 100.00
Highlighted IDENTICAL residue PHE  753  index1  752  path  850  %Seq 100.00
Highlighted IDENTICAL residue ASP  754  index1  753  path  851  %Seq 100.00
Highlighted IDENTICAL residue ALA  755  index1  754  path  852  %Seq 100.00
Highlighted IDENTICAL residue ALA  756  index1  755  path  853  %Seq 100.00
Highlighted IDENTICAL residue ARG  758  index1  757  path  855  %Seq 100.00
Highlighted IDENTICAL residue TYR  759  index1  758  path  856  %Seq 100.00
Highlighted IDENTICAL residue GLY  763  index1  762  path  860  %Seq 100.00
Highlighted IDENTICAL residue ILE  767  index1  766  path  864  %Seq 100.00
Highlighted IDENTICAL residue LEU  769  index1  768  path  866  %Seq 100.00
Highlighted IDENTICAL residue ALA  770  index1  769  path  867  %Seq 100.00
Highlighted IDENTICAL residue GLY  771  index1  770  path  868  %Seq 100.00
Highlighted IDENTICAL residue GLU  773  index1  772  path  870  %Seq 100.00
Highlighted IDENTICAL residue TYR  774  index1  773  path  871  %Seq 100.00
Highlighted IDENTICAL residue GLY  775  index1  774  path  872  %Seq 100.00
Highlighted IDENTICAL residue GLY  777  index1  776  path  874  %Seq 100.00
Highlighted IDENTICAL residue SER  778  index1  777  path  875  %Seq 100.00
Highlighted IDENTICAL residue SER  779  index1  778  path  876  %Seq 100.00
Highlighted IDENTICAL residue ARG  780  index1  779  path  877  %Seq 100.00
Highlighted IDENTICAL residue ASP  781  index1  780  path  878  %Seq 100.00
Highlighted IDENTICAL residue TRP  782  index1  781  path  879  %Seq 100.00
Highlighted IDENTICAL residue ALA  783  index1  782  path  880  %Seq 100.00
Highlighted IDENTICAL residue ALA  784  index1  783  path  881  %Seq 100.00
Highlighted IDENTICAL residue LYS  785  index1  784  path  882  %Seq 100.00
Highlighted IDENTICAL residue GLY  786  index1  785  path  883  %Seq 100.00
Highlighted IDENTICAL residue PRO  787  index1  786  path  884  %Seq 100.00
Highlighted IDENTICAL residue LEU  789  index1  788  path  886  %Seq 100.00
Highlighted IDENTICAL residue GLY  791  index1  790  path  888  %Seq 100.00
Highlighted IDENTICAL residue LYS  793  index1  792  path  890  %Seq 100.00
Highlighted IDENTICAL residue ALA  794  index1  793  path  891  %Seq 100.00
Highlighted IDENTICAL residue VAL  795  index1  794  path  892  %Seq 100.00
Highlighted IDENTICAL residue ALA  797  index1  796  path  894  %Seq 100.00
Highlighted IDENTICAL residue SER  799  index1  798  path  896  %Seq 100.00
Highlighted IDENTICAL residue GLU  801  index1  800  path  898  %Seq 100.00
Highlighted IDENTICAL residue ARG  802  index1  801  path  899  %Seq 100.00
Highlighted IDENTICAL residue ILE  803  index1  802  path  900  %Seq 100.00
Highlighted IDENTICAL residue HIS  804  index1  803  path  901  %Seq 100.00
Highlighted IDENTICAL residue ARG  805  index1  804  path  902  %Seq 100.00
Highlighted IDENTICAL residue SER  806  index1  805  path  903  %Seq 100.00
Highlighted IDENTICAL residue ASN  807  index1  806  path  904  %Seq 100.00
Highlighted IDENTICAL residue LEU  808  index1  807  path  905  %Seq 100.00
Highlighted IDENTICAL residue VAL  809  index1  808  path  906  %Seq 100.00
Highlighted IDENTICAL residue GLY  810  index1  809  path  907  %Seq 100.00
Highlighted IDENTICAL residue MET  811  index1  810  path  908  %Seq 100.00
Highlighted IDENTICAL residue GLY  812  index1  811  path  909  %Seq 100.00
Highlighted IDENTICAL residue ILE  814  index1  813  path  911  %Seq 100.00
Highlighted IDENTICAL residue PRO  815  index1  814  path  912  %Seq 100.00
Highlighted IDENTICAL residue LEU  816  index1  815  path  913  %Seq 100.00
Highlighted IDENTICAL residue GLY  821  index1  820  path  918  %Seq 100.00
Highlighted IDENTICAL residue GLU  822  index1  821  path  919  %Seq 100.00
Highlighted IDENTICAL residue ALA  824  index1  823  path  921  %Seq 100.00
Highlighted IDENTICAL residue ASP  825  index1  824  path  922  %Seq 100.00
Highlighted IDENTICAL residue LEU  827  index1  826  path  924  %Seq 100.00
Highlighted IDENTICAL residue GLY  828  index1  827  path  925  %Seq 100.00
Highlighted IDENTICAL residue LEU  829  index1  828  path  926  %Seq 100.00
Highlighted IDENTICAL residue THR  830  index1  829  path  927  %Seq 100.00
Highlighted IDENTICAL residue GLY  831  index1  830  path  928  %Seq 100.00
Highlighted IDENTICAL residue GLU  833  index1  832  path  930  %Seq 100.00
Highlighted IDENTICAL residue ARG  834  index1  833  path  931  %Seq 100.00
Highlighted IDENTICAL residue TYR  835  index1  834  path  932  %Seq 100.00
Highlighted IDENTICAL residue THR  836  index1  835  path  933  %Seq 100.00
Highlighted IDENTICAL residue ILE  837  index1  836  path  934  %Seq 100.00
Highlighted IDENTICAL residue PRO  840  index1  839  path  937  %Seq 100.00
Highlighted IDENTICAL residue GLU  841  index1  840  path  941  %Seq  50.00
Highlighted IDENTICAL residue ASN  842  index1  841  path  942  %Seq  50.00
Highlighted IDENTICAL residue PRO  845  index1  844  path  945  %Seq 100.00
Highlighted IDENTICAL residue VAL  849  index1  848  path  949  %Seq 100.00
Highlighted IDENTICAL residue VAL  851  index1  850  path  951  %Seq 100.00
Highlighted IDENTICAL residue ASP  854  index1  853  path  954  %Seq 100.00
Highlighted IDENTICAL residue GLY  856  index1  855  path  956  %Seq 100.00
Highlighted IDENTICAL residue LYS  857  index1  856  path  957  %Seq 100.00
Highlighted IDENTICAL residue PHE  859  index1  858  path  959  %Seq 100.00
Highlighted IDENTICAL residue ARG  864  index1  863  path  964  %Seq 100.00
Highlighted IDENTICAL residue PHE  865  index1  864  path  965  %Seq 100.00
Highlighted IDENTICAL residue ASP  866  index1  865  path  966  %Seq 100.00
Highlighted IDENTICAL residue THR  867  index1  866  path  967  %Seq 100.00
Highlighted IDENTICAL residue VAL  869  index1  868  path  969  %Seq 100.00
Highlighted IDENTICAL residue GLU  870  index1  869  path  970  %Seq 100.00
Highlighted IDENTICAL residue LEU  871  index1  870  path  971  %Seq 100.00
Highlighted IDENTICAL residue TYR  873  index1  872  path  973  %Seq 100.00
Highlighted IDENTICAL residue PHE  874  index1  873  path  974  %Seq 100.00
Highlighted IDENTICAL residue GLY  877  index1  876  path  977  %Seq 100.00
Highlighted IDENTICAL residue GLY  878  index1  877  path  978  %Seq 100.00
Highlighted IDENTICAL residue ILE  879  index1  878  path  979  %Seq 100.00
Highlighted IDENTICAL residue LEU  880  index1  879  path  980  %Seq 100.00
Highlighted IDENTICAL residue TYR  882  index1  881  path  982  %Seq 100.00
Highlighted IDENTICAL residue ILE  884  index1  883  path  984  %Seq 100.00
Highlighted IDENTICAL residue ARG  885  index1  884  path  985  %Seq 100.00
Highlighted IDENTICAL residue LYS  889  index1  888  path  989  %Seq 100.00
Highlighted 545 residues for visualization

Wrote PyMOL macro into file /usr/local/www/html/proteins/htdocs/results/At2g05710-2b3xA.pir.txt.2B3X.pdb.conservation.pml

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

The program

/usr/local/www/html/proteins/Compiled_Programs/WYRM/PyMOL_highlight_conserved_residues At2g05710-2b3xA.pir.txt PIR amino_acid 2B3X.pdb _ 100.0 BLOSUM62.dat 

completed successfully.

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


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