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At2g05070.1/PDB

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

Successfully read 2 file paths from WYRM_file_paths.txt

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

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

Sequence file type = 3

Sequence type = 3

Got here 1
Got here 2
Got here 3
Sequence 1
Got here 3
Got here 4
Got here 3
Got here 4
Got here 3
Got here 4
Got here 3
Got here 4
Got here 3
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/At2g05070-c1rwta_.pir.txt

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

Assigned types to 265 residues in Sequence 2-05070, 0 remain unknown
Assigned types to 218 residues in Sequence c1rwta_, 47 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 At2g05070-c1rwta_.pir.txt into sequence alignment.

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

>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

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

Best alignment:
1RWT.pdb  1088  VPGSPWYGPDRVKYLGPFSGESPSYLTGEFPGDYGWDTAGLSADPETFAK  1137
                 P S WYGPDR KYLGPFS  +PSYLTGE+PGDYGWDTAGLSADPETFAK
2-05070     44  TPQSIWYGPDRPKYLGPFSENTPSYLTGEYPGDYGWDTAGLSADPETFAK    93

1RWT.pdb  1138  NRELEVIHCRWAMLGALGCVFPELLARNGVKFGEAVWFKAGSQIFSEGGL  1187
                NRELEVIH RWAMLGALGC FPE+L++NGVKFGEAVWFKAGSQIFSEGGL
2-05070     94  NRELEVIHSRWAMLGALGCTFPEILSKNGVKFGEAVWFKAGSQIFSEGGL   143

1RWT.pdb  1188  DYLGNPSLVHAQSILAIWACQVILMGAVEGYRIAGGPLGEVVDPLYPGGS  1237
                DYLGNP+L+HAQSILAIWA QV+LMG +EGYRI GGPLGE +DPLYPGG+
2-05070    144  DYLGNPNLIHAQSILAIWAVQVVLMGFIEGYRIGGGPLGEGLDPLYPGGA   193

1RWT.pdb  1238  FDPLGLADDPEAFAELKVKEIKNGRLAMFSMFGFFVQAIVTGKGPLENLA  1287
                FDPL LA+DPEAF+ELKVKE+KNGRLAMFSMFGFFVQAIVTGKGP+ENL 
2-05070    194  FDPLNLAEDPEAFSELKVKELKNGRLAMFSMFGFFVQAIVTGKGPIENLF   243

1RWT.pdb  1288  DHLADPVNNNAWNFATNFVPGK  1309
                DHLADPV NNAW++ATNFVPGK
2-05070    244  DHLADPVANNAWSYATNFVPGK   265

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

Highlighted IDENTICAL residue VAL  229  index1 1088  path   44  %Seq  50.00
Highlighted IDENTICAL residue PRO  230  index1 1089  path   45  %Seq  50.00
Highlighted IDENTICAL residue GLY  231  index1 1090  path   46  %Seq  50.00
Highlighted IDENTICAL residue SER   14  index1 1091  path   47  %Seq 100.00
Highlighted IDENTICAL residue TRP   16  index1 1093  path   49  %Seq 100.00
Highlighted IDENTICAL residue TYR   17  index1 1094  path   50  %Seq 100.00
Highlighted IDENTICAL residue GLY   18  index1 1095  path   51  %Seq 100.00
Highlighted IDENTICAL residue PRO   19  index1 1096  path   52  %Seq 100.00
Highlighted IDENTICAL residue ASP   20  index1 1097  path   53  %Seq 100.00
Highlighted IDENTICAL residue ARG   21  index1 1098  path   54  %Seq 100.00
Highlighted IDENTICAL residue LYS   23  index1 1100  path   56  %Seq 100.00
Highlighted IDENTICAL residue TYR   24  index1 1101  path   57  %Seq 100.00
Highlighted IDENTICAL residue LEU   25  index1 1102  path   58  %Seq 100.00
Highlighted IDENTICAL residue GLY   26  index1 1103  path   59  %Seq 100.00
Highlighted IDENTICAL residue PRO   27  index1 1104  path   60  %Seq 100.00
Highlighted IDENTICAL residue PHE   28  index1 1105  path   61  %Seq 100.00
Highlighted IDENTICAL residue SER   29  index1 1106  path   62  %Seq 100.00
Highlighted IDENTICAL residue PRO   33  index1 1110  path   66  %Seq 100.00
Highlighted IDENTICAL residue SER   34  index1 1111  path   67  %Seq 100.00
Highlighted IDENTICAL residue TYR   35  index1 1112  path   68  %Seq 100.00
Highlighted IDENTICAL residue LEU   36  index1 1113  path   69  %Seq 100.00
Highlighted IDENTICAL residue THR   37  index1 1114  path   70  %Seq 100.00
Highlighted IDENTICAL residue GLY   38  index1 1115  path   71  %Seq 100.00
Highlighted IDENTICAL residue GLU   39  index1 1116  path   72  %Seq 100.00
Highlighted IDENTICAL residue PRO   41  index1 1118  path   74  %Seq 100.00
Highlighted IDENTICAL residue GLY   42  index1 1119  path   75  %Seq 100.00
Highlighted IDENTICAL residue ASP   43  index1 1120  path   76  %Seq 100.00
Highlighted IDENTICAL residue TYR   44  index1 1121  path   77  %Seq 100.00
Highlighted IDENTICAL residue GLY   45  index1 1122  path   78  %Seq 100.00
Highlighted IDENTICAL residue TRP   46  index1 1123  path   79  %Seq 100.00
Highlighted IDENTICAL residue ASP   47  index1 1124  path   80  %Seq 100.00
Highlighted IDENTICAL residue THR   48  index1 1125  path   81  %Seq 100.00
Highlighted IDENTICAL residue ALA   49  index1 1126  path   82  %Seq 100.00
Highlighted IDENTICAL residue GLY   50  index1 1127  path   83  %Seq 100.00
Highlighted IDENTICAL residue LEU   51  index1 1128  path   84  %Seq 100.00
Highlighted IDENTICAL residue SER   52  index1 1129  path   85  %Seq 100.00
Highlighted IDENTICAL residue ALA   53  index1 1130  path   86  %Seq 100.00
Highlighted IDENTICAL residue ASP   54  index1 1131  path   87  %Seq 100.00
Highlighted IDENTICAL residue PRO   55  index1 1132  path   88  %Seq 100.00
Highlighted IDENTICAL residue GLU   56  index1 1133  path   89  %Seq 100.00
Highlighted IDENTICAL residue THR   57  index1 1134  path   90  %Seq 100.00
Highlighted IDENTICAL residue PHE   58  index1 1135  path   91  %Seq 100.00
Highlighted IDENTICAL residue ALA   59  index1 1136  path   92  %Seq 100.00
Highlighted IDENTICAL residue LYS   60  index1 1137  path   93  %Seq 100.00
Highlighted IDENTICAL residue ASN   61  index1 1138  path   94  %Seq 100.00
Highlighted IDENTICAL residue ARG   62  index1 1139  path   95  %Seq 100.00
Highlighted IDENTICAL residue GLU   63  index1 1140  path   96  %Seq 100.00
Highlighted IDENTICAL residue LEU   64  index1 1141  path   97  %Seq 100.00
Highlighted IDENTICAL residue GLU   65  index1 1142  path   98  %Seq 100.00
Highlighted IDENTICAL residue VAL   66  index1 1143  path   99  %Seq 100.00
Highlighted IDENTICAL residue ILE   67  index1 1144  path  100  %Seq 100.00
Highlighted IDENTICAL residue HIS   68  index1 1145  path  101  %Seq 100.00
Highlighted IDENTICAL residue ARG   70  index1 1147  path  103  %Seq 100.00
Highlighted IDENTICAL residue TRP   71  index1 1148  path  104  %Seq 100.00
Highlighted IDENTICAL residue ALA   72  index1 1149  path  105  %Seq 100.00
Highlighted IDENTICAL residue MET   73  index1 1150  path  106  %Seq 100.00
Highlighted IDENTICAL residue LEU   74  index1 1151  path  107  %Seq 100.00
Highlighted IDENTICAL residue GLY   75  index1 1152  path  108  %Seq 100.00
Highlighted IDENTICAL residue ALA   76  index1 1153  path  109  %Seq 100.00
Highlighted IDENTICAL residue LEU   77  index1 1154  path  110  %Seq 100.00
Highlighted IDENTICAL residue GLY   78  index1 1155  path  111  %Seq 100.00
Highlighted IDENTICAL residue CYS   79  index1 1156  path  112  %Seq 100.00
Highlighted IDENTICAL residue PHE   81  index1 1158  path  114  %Seq 100.00
Highlighted IDENTICAL residue PRO   82  index1 1159  path  115  %Seq 100.00
Highlighted IDENTICAL residue GLU   83  index1 1160  path  116  %Seq 100.00
Highlighted IDENTICAL residue LEU   85  index1 1162  path  118  %Seq 100.00
Highlighted IDENTICAL residue ASN   88  index1 1165  path  121  %Seq 100.00
Highlighted IDENTICAL residue GLY   89  index1 1166  path  122  %Seq 100.00
Highlighted IDENTICAL residue VAL   90  index1 1167  path  123  %Seq 100.00
Highlighted IDENTICAL residue LYS   91  index1 1168  path  124  %Seq 100.00
Highlighted IDENTICAL residue PHE   92  index1 1169  path  125  %Seq 100.00
Highlighted IDENTICAL residue GLY   93  index1 1170  path  126  %Seq 100.00
Highlighted IDENTICAL residue GLU   94  index1 1171  path  127  %Seq 100.00
Highlighted IDENTICAL residue ALA   95  index1 1172  path  128  %Seq 100.00
Highlighted IDENTICAL residue VAL   96  index1 1173  path  129  %Seq 100.00
Highlighted IDENTICAL residue TRP   97  index1 1174  path  130  %Seq 100.00
Highlighted IDENTICAL residue PHE   98  index1 1175  path  131  %Seq 100.00
Highlighted IDENTICAL residue LYS   99  index1 1176  path  132  %Seq 100.00
Highlighted IDENTICAL residue ALA  100  index1 1177  path  133  %Seq 100.00
Highlighted IDENTICAL residue GLY  101  index1 1178  path  134  %Seq 100.00
Highlighted IDENTICAL residue SER  102  index1 1179  path  135  %Seq 100.00
Highlighted IDENTICAL residue GLN  103  index1 1180  path  136  %Seq 100.00
Highlighted IDENTICAL residue ILE  104  index1 1181  path  137  %Seq 100.00
Highlighted IDENTICAL residue PHE  105  index1 1182  path  138  %Seq 100.00
Highlighted IDENTICAL residue SER  106  index1 1183  path  139  %Seq 100.00
Highlighted IDENTICAL residue GLU  107  index1 1184  path  140  %Seq 100.00
Highlighted IDENTICAL residue GLY  108  index1 1185  path  141  %Seq 100.00
Highlighted IDENTICAL residue GLY  109  index1 1186  path  142  %Seq 100.00
Highlighted IDENTICAL residue LEU  110  index1 1187  path  143  %Seq 100.00
Highlighted IDENTICAL residue ASP  111  index1 1188  path  144  %Seq 100.00
Highlighted IDENTICAL residue TYR  112  index1 1189  path  145  %Seq 100.00
Highlighted IDENTICAL residue LEU  113  index1 1190  path  146  %Seq 100.00
Highlighted IDENTICAL residue GLY  114  index1 1191  path  147  %Seq 100.00
Highlighted IDENTICAL residue ASN  115  index1 1192  path  148  %Seq 100.00
Highlighted IDENTICAL residue PRO  116  index1 1193  path  149  %Seq 100.00
Highlighted IDENTICAL residue LEU  118  index1 1195  path  151  %Seq 100.00
Highlighted IDENTICAL residue HIS  120  index1 1197  path  153  %Seq 100.00
Highlighted IDENTICAL residue ALA  121  index1 1198  path  154  %Seq 100.00
Highlighted IDENTICAL residue GLN  122  index1 1199  path  155  %Seq 100.00
Highlighted IDENTICAL residue SER  123  index1 1200  path  156  %Seq 100.00
Highlighted IDENTICAL residue ILE  124  index1 1201  path  157  %Seq 100.00
Highlighted IDENTICAL residue LEU  125  index1 1202  path  158  %Seq 100.00
Highlighted IDENTICAL residue ALA  126  index1 1203  path  159  %Seq 100.00
Highlighted IDENTICAL residue ILE  127  index1 1204  path  160  %Seq 100.00
Highlighted IDENTICAL residue TRP  128  index1 1205  path  161  %Seq 100.00
Highlighted IDENTICAL residue ALA  129  index1 1206  path  162  %Seq 100.00
Highlighted IDENTICAL residue GLN  131  index1 1208  path  164  %Seq 100.00
Highlighted IDENTICAL residue VAL  132  index1 1209  path  165  %Seq 100.00
Highlighted IDENTICAL residue LEU  134  index1 1211  path  167  %Seq 100.00
Highlighted IDENTICAL residue MET  135  index1 1212  path  168  %Seq 100.00
Highlighted IDENTICAL residue GLY  136  index1 1213  path  169  %Seq 100.00
Highlighted IDENTICAL residue GLU  139  index1 1216  path  172  %Seq 100.00
Highlighted IDENTICAL residue GLY  140  index1 1217  path  173  %Seq 100.00
Highlighted IDENTICAL residue TYR  141  index1 1218  path  174  %Seq 100.00
Highlighted IDENTICAL residue ARG  142  index1 1219  path  175  %Seq 100.00
Highlighted IDENTICAL residue ILE  143  index1 1220  path  176  %Seq 100.00
Highlighted IDENTICAL residue GLY  145  index1 1222  path  178  %Seq 100.00
Highlighted IDENTICAL residue GLY  146  index1 1223  path  179  %Seq 100.00
Highlighted IDENTICAL residue PRO  147  index1 1224  path  180  %Seq 100.00
Highlighted IDENTICAL residue LEU  148  index1 1225  path  181  %Seq 100.00
Highlighted IDENTICAL residue GLY  149  index1 1226  path  182  %Seq 100.00
Highlighted IDENTICAL residue GLU  150  index1 1227  path  183  %Seq 100.00
Highlighted IDENTICAL residue ASP  153  index1 1230  path  186  %Seq 100.00
Highlighted IDENTICAL residue PRO  154  index1 1231  path  187  %Seq 100.00
Highlighted IDENTICAL residue LEU  155  index1 1232  path  188  %Seq 100.00
Highlighted IDENTICAL residue TYR  156  index1 1233  path  189  %Seq 100.00
Highlighted IDENTICAL residue PRO  157  index1 1234  path  190  %Seq 100.00
Highlighted IDENTICAL residue GLY  158  index1 1235  path  191  %Seq 100.00
Highlighted IDENTICAL residue GLY  159  index1 1236  path  192  %Seq 100.00
Highlighted IDENTICAL residue PHE  161  index1 1238  path  194  %Seq 100.00
Highlighted IDENTICAL residue ASP  162  index1 1239  path  195  %Seq 100.00
Highlighted IDENTICAL residue PRO  163  index1 1240  path  196  %Seq 100.00
Highlighted IDENTICAL residue LEU  164  index1 1241  path  197  %Seq 100.00
Highlighted IDENTICAL residue LEU  166  index1 1243  path  199  %Seq 100.00
Highlighted IDENTICAL residue ALA  167  index1 1244  path  200  %Seq 100.00
Highlighted IDENTICAL residue ASP  169  index1 1246  path  202  %Seq 100.00
Highlighted IDENTICAL residue PRO  170  index1 1247  path  203  %Seq 100.00
Highlighted IDENTICAL residue GLU  171  index1 1248  path  204  %Seq 100.00
Highlighted IDENTICAL residue ALA  172  index1 1249  path  205  %Seq 100.00
Highlighted IDENTICAL residue PHE  173  index1 1250  path  206  %Seq 100.00
Highlighted IDENTICAL residue GLU  175  index1 1252  path  208  %Seq 100.00
Highlighted IDENTICAL residue LEU  176  index1 1253  path  209  %Seq 100.00
Highlighted IDENTICAL residue LYS  177  index1 1254  path  210  %Seq 100.00
Highlighted IDENTICAL residue VAL  178  index1 1255  path  211  %Seq 100.00
Highlighted IDENTICAL residue LYS  179  index1 1256  path  212  %Seq 100.00
Highlighted IDENTICAL residue GLU  180  index1 1257  path  213  %Seq 100.00
Highlighted IDENTICAL residue LYS  182  index1 1259  path  215  %Seq 100.00
Highlighted IDENTICAL residue ASN  183  index1 1260  path  216  %Seq 100.00
Highlighted IDENTICAL residue GLY  184  index1 1261  path  217  %Seq 100.00
Highlighted IDENTICAL residue ARG  185  index1 1262  path  218  %Seq 100.00
Highlighted IDENTICAL residue LEU  186  index1 1263  path  219  %Seq 100.00
Highlighted IDENTICAL residue ALA  187  index1 1264  path  220  %Seq 100.00
Highlighted IDENTICAL residue MET  188  index1 1265  path  221  %Seq 100.00
Highlighted IDENTICAL residue PHE  189  index1 1266  path  222  %Seq 100.00
Highlighted IDENTICAL residue SER  190  index1 1267  path  223  %Seq 100.00
Highlighted IDENTICAL residue MET  191  index1 1268  path  224  %Seq 100.00
Highlighted IDENTICAL residue PHE  192  index1 1269  path  225  %Seq 100.00
Highlighted IDENTICAL residue GLY  193  index1 1270  path  226  %Seq 100.00
Highlighted IDENTICAL residue PHE  194  index1 1271  path  227  %Seq 100.00
Highlighted IDENTICAL residue PHE  195  index1 1272  path  228  %Seq 100.00
Highlighted IDENTICAL residue VAL  196  index1 1273  path  229  %Seq 100.00
Highlighted IDENTICAL residue GLN  197  index1 1274  path  230  %Seq 100.00
Highlighted IDENTICAL residue ALA  198  index1 1275  path  231  %Seq 100.00
Highlighted IDENTICAL residue ILE  199  index1 1276  path  232  %Seq 100.00
Highlighted IDENTICAL residue VAL  200  index1 1277  path  233  %Seq 100.00
Highlighted IDENTICAL residue THR  201  index1 1278  path  234  %Seq 100.00
Highlighted IDENTICAL residue GLY  202  index1 1279  path  235  %Seq 100.00
Highlighted IDENTICAL residue LYS  203  index1 1280  path  236  %Seq 100.00
Highlighted IDENTICAL residue GLY  204  index1 1281  path  237  %Seq 100.00
Highlighted IDENTICAL residue PRO  205  index1 1282  path  238  %Seq 100.00
Highlighted IDENTICAL residue GLU  207  index1 1284  path  240  %Seq 100.00
Highlighted IDENTICAL residue ASN  208  index1 1285  path  241  %Seq 100.00
Highlighted IDENTICAL residue LEU  209  index1 1286  path  242  %Seq 100.00
Highlighted IDENTICAL residue ASP  211  index1 1288  path  244  %Seq 100.00
Highlighted IDENTICAL residue HIS  212  index1 1289  path  245  %Seq 100.00
Highlighted IDENTICAL residue LEU  213  index1 1290  path  246  %Seq 100.00
Highlighted IDENTICAL residue ALA  214  index1 1291  path  247  %Seq 100.00
Highlighted IDENTICAL residue ASP  215  index1 1292  path  248  %Seq 100.00
Highlighted IDENTICAL residue PRO  216  index1 1293  path  249  %Seq 100.00
Highlighted IDENTICAL residue VAL  217  index1 1294  path  250  %Seq 100.00
Highlighted IDENTICAL residue ASN  219  index1 1296  path  252  %Seq 100.00
Highlighted IDENTICAL residue ASN  220  index1 1297  path  253  %Seq 100.00
Highlighted IDENTICAL residue ALA  221  index1 1298  path  254  %Seq 100.00
Highlighted IDENTICAL residue TRP  222  index1 1299  path  255  %Seq 100.00
Highlighted IDENTICAL residue ALA  225  index1 1302  path  258  %Seq 100.00
Highlighted IDENTICAL residue THR  226  index1 1303  path  259  %Seq 100.00
Highlighted IDENTICAL residue ASN  227  index1 1304  path  260  %Seq 100.00
Highlighted IDENTICAL residue PHE  228  index1 1305  path  261  %Seq 100.00
Highlighted IDENTICAL residue VAL  229  index1 1306  path  262  %Seq 100.00
Highlighted IDENTICAL residue PRO  230  index1 1307  path  263  %Seq 100.00
Highlighted IDENTICAL residue GLY  231  index1 1308  path  264  %Seq 100.00
Highlighted IDENTICAL residue LYS  232  index1 1309  path  265  %Seq  50.00
Highlighted 192 residues for visualization

Wrote PyMOL macro into file /usr/local/www/html/proteins/htdocs/results/At2g05070-c1rwta_.pir.txt.1RWT.pdb.conservation.pml

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

The program

/usr/local/www/html/proteins/Compiled_Programs/WYRM/PyMOL_highlight_conserved_residues At2g05070-c1rwta_.pir.txt PIR amino_acid 1RWT.pdb _ 100.0 BLOSUM62.dat 

completed successfully.

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

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