At2g14120.1/PDB

&&&&&&&&&&&&&&&&&&&& BEGIN /usr/local/www/html/proteins/Compiled_Programs/WYRM/PyMOL_highlight_conserved_residues &&&&&&&&&&&&&&&&&&&&
Successfully read 2 file paths from WYRM_file_paths.txt
generic_input /usr/local/www/html/proteins/workspace/
generic_output /usr/local/www/html/proteins/htdocs/results/
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Sequence file type = 3
Sequence type = 3
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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/At2g14120-1jwyB.pir.txt
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Assigned types to 780 residues in Sequence 2-14120, 0 remain unknown
Assigned types to 315 residues in Sequence 1jwyB, 465 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 At2g14120-1jwyB.pir.txt into sequence alignment.
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>1JWY.pdb Made from 8297 ATOM records in 1JWY.pdb
DPIHDRTSDYHKYLKVKQFKLTVSDKRYIWYNPDPKERDSYECGEIVSET
SDSFTFKTVDGQDRQVKKDDANQRNPIKFDGVEDMSELSYLNEPAVFHNL
RVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIF
AISDVAYRSMLDDRQNQSLLITGESGAGKTENTKKVIQYLASVAGSGVLE
QQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQSYL
LEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGC
VDIKGVSDSEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEKG
AGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVE
KSSSSRDALVKALYGRLFLWLVKKINNVLCQERKAYFIGVLDISGFEIFK
VNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLKEKINWTFIDFGLDSQA
TIDLIDGRQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPR
FSKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLF
NDPNIASRAKKGANFITVAAQYKEQLASLMATLETTNPHFVRCIIPNNKQ
LPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNV
PRDAEDSQKATDAVLKHLNIDPEQYRFGITKIFFRAGQLARIEEAREQRI
SEIDQLIPVINKLQDVFNTLGSDPLDLPQIVVVGSQSSGKSSVLENIVGR
DFLPRPLILQLTHLPIADDGSQTQEWGEFLHKPNDMFYDFSEIREEIIRD
TDISAQPINLKIYSPHVVNLTLVDLPGITDIEQQIRRMVMAYIKKQNAII
VAVTPANTDLANSDALQLAKEVDPEGKRTIGVITKLDLMDKGTDAMEVLT
GRVIPLTLGFIGVINRSQEDIIAKKSIRESLKSEILYFKNHPIYKSIANR
SGTAYLSKTLNKLLMFHIRDTLPDLKVKVSKMLSTRGLV
======================================================
Best alignment:
1JWY.pdb 754 DQLIPVINKLQDVFNTLGS-DPLDLPQIVVVGSQSSGKSSVLENIVGRDF 802
 +IP++NKLQD+F LGS + LPQ+ VVGSQSSGKSSVLE +VGRDF
2-14120 19 SSVIPIVNKLQDIFAQLGSQSTIALPQVAVVGSQSSGKSSVLEALVGRDF 68
1JWY.pdb 803 LP--------RPLILQLTHLPIADDGSQTQEWGEFL-HKPNDMFYDFSEI 843
 LP RPL LQL + DG +EWGEFL H P YDFSEI
2-14120 69 LPRGNDICTRRPLRLQLVQTKPSSDGGSDEEWGEFLHHDPVRRIYDFSEI 118
1JWY.pdb 844 REEIIRDTD-ISAQ-------PINLKIYSPHVVNLTLVDLPGIT------ 879
 R EI +T+ +S + PI LKI+SP+V++++LVDLPGIT 
2-14120 119 RREIEAETNRVSGENKGVSDIPIGLKIFSPNVLDISLVDLPGITKVPVGD 168
1JWY.pdb 879 ---DIEQQIRRMVMAYIKKQNAIIVAVTPANTDLANSDALQLAKEVDPEG 926
 DIE +IR M++ YIK+ + +I+AV+PANTDLANSDALQ+A DP+G
2-14120 169 QPSDIEARIRTMILTYIKEPSCLILAVSPANTDLANSDALQIAGNADPDG 218
1JWY.pdb 927 KRTIGVITKLDLMDKGTDAMEVLTGRVIPLTLGFIGVINRSQEDIIAKKS 976
 RTIGVITKLD+MD+GTDA L G+ IPL LG++GV+NRSQEDI+ +S
2-14120 219 HRTIGVITKLDIMDRGTDARNHLLGKTIPLRLGYVGVVNRSQEDILMNRS 268
1JWY.pdb 977 IRESLKSEILYFKNHPIYKSIANRSGTAYLSKTLNKLLMFHIRDTLPDLK 1026
 I+++L +E +F++ P+Y + +R G L+K LN++L+ HI+ LP LK
2-14120 269 IKDALVAEEKFFRSRPVYSGLTDRLGVPQLAKKLNQVLVQHIKALLPSLK 318
1JWY.pdb 1027 VKVSKML 1033
 +++ L
2-14120 319 SRINNAL 325
======================================================
Highlighted IDENTICAL residue ILE 5 index1 757 path 22 %Seq 100.00
Highlighted IDENTICAL residue PRO 6 index1 758 path 23 %Seq 100.00
Highlighted IDENTICAL residue ASN 9 index1 761 path 26 %Seq 100.00
Highlighted IDENTICAL residue LYS 10 index1 762 path 27 %Seq 100.00
Highlighted IDENTICAL residue LEU 11 index1 763 path 28 %Seq 100.00
Highlighted IDENTICAL residue GLN 12 index1 764 path 29 %Seq 100.00
Highlighted IDENTICAL residue ASP 13 index1 765 path 30 %Seq 100.00
Highlighted IDENTICAL residue PHE 15 index1 767 path 32 %Seq 100.00
Highlighted IDENTICAL residue LEU 18 index1 770 path 35 %Seq 100.00
Highlighted IDENTICAL residue GLY 19 index1 771 path 36 %Seq 100.00
Highlighted IDENTICAL residue SER 20 index1 772 path 37 %Seq 50.00
Highlighted IDENTICAL residue LEU 25 index1 777 path 43 %Seq 100.00
Highlighted IDENTICAL residue PRO 26 index1 778 path 44 %Seq 100.00
Highlighted IDENTICAL residue GLN 27 index1 779 path 45 %Seq 100.00
Highlighted IDENTICAL residue VAL 30 index1 782 path 48 %Seq 100.00
Highlighted IDENTICAL residue VAL 31 index1 783 path 49 %Seq 100.00
Highlighted IDENTICAL residue GLY 32 index1 784 path 50 %Seq 100.00
Highlighted IDENTICAL residue SER 33 index1 785 path 51 %Seq 100.00
Highlighted IDENTICAL residue GLN 34 index1 786 path 52 %Seq 100.00
Highlighted IDENTICAL residue SER 35 index1 787 path 53 %Seq 100.00
Highlighted IDENTICAL residue SER 36 index1 788 path 54 %Seq 100.00
Highlighted IDENTICAL residue GLY 37 index1 789 path 55 %Seq 100.00
Highlighted IDENTICAL residue LYS 38 index1 790 path 56 %Seq 100.00
Highlighted IDENTICAL residue SER 39 index1 791 path 57 %Seq 100.00
Highlighted IDENTICAL residue SER 40 index1 792 path 58 %Seq 100.00
Highlighted IDENTICAL residue VAL 41 index1 793 path 59 %Seq 100.00
Highlighted IDENTICAL residue LEU 42 index1 794 path 60 %Seq 100.00
Highlighted IDENTICAL residue GLU 43 index1 795 path 61 %Seq 100.00
Highlighted IDENTICAL residue VAL 46 index1 798 path 64 %Seq 100.00
Highlighted IDENTICAL residue GLY 47 index1 799 path 65 %Seq 100.00
Highlighted IDENTICAL residue ARG 48 index1 800 path 66 %Seq 100.00
Highlighted IDENTICAL residue ASP 49 index1 801 path 67 %Seq 100.00
Highlighted IDENTICAL residue PHE 50 index1 802 path 68 %Seq 100.00
Highlighted IDENTICAL residue LEU 51 index1 803 path 69 %Seq 100.00
Highlighted IDENTICAL residue PRO 52 index1 804 path 70 %Seq 100.00
Highlighted IDENTICAL residue ARG 61 index1 805 path 79 %Seq 100.00
Highlighted IDENTICAL residue PRO 62 index1 806 path 80 %Seq 100.00
Highlighted IDENTICAL residue LEU 63 index1 807 path 81 %Seq 100.00
Highlighted IDENTICAL residue LEU 65 index1 809 path 83 %Seq 100.00
Highlighted IDENTICAL residue GLN 66 index1 810 path 84 %Seq 100.00
Highlighted IDENTICAL residue LEU 67 index1 811 path 85 %Seq 100.00
Highlighted IDENTICAL residue ASP 75 index1 819 path 93 %Seq 100.00
Highlighted IDENTICAL residue GLY 76 index1 820 path 94 %Seq 100.00
Highlighted IDENTICAL residue GLU 81 index1 825 path 99 %Seq 100.00
Highlighted IDENTICAL residue TRP 82 index1 826 path 100 %Seq 100.00
Highlighted IDENTICAL residue GLY 83 index1 827 path 101 %Seq 100.00
Highlighted IDENTICAL residue GLU 84 index1 828 path 102 %Seq 100.00
Highlighted IDENTICAL residue PHE 85 index1 829 path 103 %Seq 100.00
Highlighted IDENTICAL residue LEU 86 index1 830 path 104 %Seq 100.00
Highlighted IDENTICAL residue HIS 87 index1 831 path 106 %Seq 50.00
Highlighted IDENTICAL residue PRO 89 index1 833 path 108 %Seq 100.00
Highlighted IDENTICAL residue TYR 94 index1 838 path 113 %Seq 100.00
Highlighted IDENTICAL residue ASP 95 index1 839 path 114 %Seq 100.00
Highlighted IDENTICAL residue PHE 96 index1 840 path 115 %Seq 100.00
Highlighted IDENTICAL residue SER 97 index1 841 path 116 %Seq 100.00
Highlighted IDENTICAL residue GLU 98 index1 842 path 117 %Seq 100.00
Highlighted IDENTICAL residue ILE 99 index1 843 path 118 %Seq 100.00
Highlighted IDENTICAL residue ARG 100 index1 844 path 119 %Seq 100.00
Highlighted IDENTICAL residue GLU 102 index1 846 path 121 %Seq 100.00
Highlighted IDENTICAL residue ILE 103 index1 847 path 122 %Seq 100.00
Highlighted IDENTICAL residue THR 107 index1 851 path 126 %Seq 100.00
Highlighted IDENTICAL residue ALA 119 index1 855 path 131 %Seq 100.00
Highlighted IDENTICAL residue PRO 121 index1 857 path 140 %Seq 100.00
Highlighted IDENTICAL residue ILE 122 index1 858 path 141 %Seq 100.00
Highlighted IDENTICAL residue LEU 124 index1 860 path 143 %Seq 100.00
Highlighted IDENTICAL residue LYS 125 index1 861 path 144 %Seq 100.00
Highlighted IDENTICAL residue ILE 126 index1 862 path 145 %Seq 100.00
Highlighted IDENTICAL residue SER 128 index1 864 path 147 %Seq 100.00
Highlighted IDENTICAL residue PRO 129 index1 865 path 148 %Seq 100.00
Highlighted IDENTICAL residue VAL 131 index1 867 path 150 %Seq 100.00
Highlighted IDENTICAL residue LEU 136 index1 872 path 155 %Seq 100.00
Highlighted IDENTICAL residue VAL 137 index1 873 path 156 %Seq 100.00
Highlighted IDENTICAL residue ASP 138 index1 874 path 157 %Seq 100.00
Highlighted IDENTICAL residue LEU 139 index1 875 path 158 %Seq 100.00
Highlighted IDENTICAL residue PRO 140 index1 876 path 159 %Seq 100.00
Highlighted IDENTICAL residue GLY 141 index1 877 path 160 %Seq 100.00
Highlighted IDENTICAL residue ILE 142 index1 878 path 161 %Seq 100.00
Highlighted IDENTICAL residue THR 152 index1 879 path 162 %Seq 100.00
Highlighted IDENTICAL residue ASP 153 index1 880 path 172 %Seq 100.00
Highlighted IDENTICAL residue ILE 154 index1 881 path 173 %Seq 100.00
Highlighted IDENTICAL residue GLU 155 index1 882 path 174 %Seq 100.00
Highlighted IDENTICAL residue ILE 158 index1 885 path 177 %Seq 100.00
Highlighted IDENTICAL residue ARG 159 index1 886 path 178 %Seq 100.00
Highlighted IDENTICAL residue MET 161 index1 888 path 180 %Seq 100.00
Highlighted IDENTICAL residue TYR 165 index1 892 path 184 %Seq 100.00
Highlighted IDENTICAL residue ILE 166 index1 893 path 185 %Seq 100.00
Highlighted IDENTICAL residue LYS 167 index1 894 path 186 %Seq 100.00
Highlighted IDENTICAL residue ILE 173 index1 900 path 192 %Seq 100.00
Highlighted IDENTICAL residue ALA 175 index1 902 path 194 %Seq 100.00
Highlighted IDENTICAL residue VAL 176 index1 903 path 195 %Seq 100.00
Highlighted IDENTICAL residue PRO 178 index1 905 path 197 %Seq 100.00
Highlighted IDENTICAL residue ALA 179 index1 906 path 198 %Seq 100.00
Highlighted IDENTICAL residue ASN 180 index1 907 path 199 %Seq 100.00
Highlighted IDENTICAL residue THR 181 index1 908 path 200 %Seq 100.00
Highlighted IDENTICAL residue ASP 182 index1 909 path 201 %Seq 100.00
Highlighted IDENTICAL residue LEU 183 index1 910 path 202 %Seq 100.00
Highlighted IDENTICAL residue ALA 184 index1 911 path 203 %Seq 100.00
Highlighted IDENTICAL residue ASN 185 index1 912 path 204 %Seq 100.00
Highlighted IDENTICAL residue SER 186 index1 913 path 205 %Seq 100.00
Highlighted IDENTICAL residue ASP 187 index1 914 path 206 %Seq 100.00
Highlighted IDENTICAL residue ALA 188 index1 915 path 207 %Seq 100.00
Highlighted IDENTICAL residue LEU 189 index1 916 path 208 %Seq 100.00
Highlighted IDENTICAL residue GLN 190 index1 917 path 209 %Seq 100.00
Highlighted IDENTICAL residue ALA 192 index1 919 path 211 %Seq 100.00
Highlighted IDENTICAL residue ASP 196 index1 923 path 215 %Seq 100.00
Highlighted IDENTICAL residue PRO 197 index1 924 path 216 %Seq 100.00
Highlighted IDENTICAL residue GLY 199 index1 926 path 218 %Seq 100.00
Highlighted IDENTICAL residue ARG 201 index1 928 path 220 %Seq 100.00
Highlighted IDENTICAL residue THR 202 index1 929 path 221 %Seq 100.00
Highlighted IDENTICAL residue ILE 203 index1 930 path 222 %Seq 100.00
Highlighted IDENTICAL residue GLY 204 index1 931 path 223 %Seq 100.00
Highlighted IDENTICAL residue VAL 205 index1 932 path 224 %Seq 100.00
Highlighted IDENTICAL residue ILE 206 index1 933 path 225 %Seq 100.00
Highlighted IDENTICAL residue THR 207 index1 934 path 226 %Seq 100.00
Highlighted IDENTICAL residue LYS 208 index1 935 path 227 %Seq 100.00
Highlighted IDENTICAL residue LEU 209 index1 936 path 228 %Seq 100.00
Highlighted IDENTICAL residue ASP 210 index1 937 path 229 %Seq 100.00
Highlighted IDENTICAL residue MET 212 index1 939 path 231 %Seq 100.00
Highlighted IDENTICAL residue ASP 213 index1 940 path 232 %Seq 100.00
Highlighted IDENTICAL residue GLY 215 index1 942 path 234 %Seq 100.00
Highlighted IDENTICAL residue THR 216 index1 943 path 235 %Seq 100.00
Highlighted IDENTICAL residue ASP 217 index1 944 path 236 %Seq 100.00
Highlighted IDENTICAL residue ALA 218 index1 945 path 237 %Seq 100.00
Highlighted IDENTICAL residue LEU 222 index1 949 path 241 %Seq 100.00
Highlighted IDENTICAL residue GLY 224 index1 951 path 243 %Seq 100.00
Highlighted IDENTICAL residue ILE 227 index1 954 path 246 %Seq 100.00
Highlighted IDENTICAL residue PRO 228 index1 955 path 247 %Seq 100.00
Highlighted IDENTICAL residue LEU 229 index1 956 path 248 %Seq 100.00
Highlighted IDENTICAL residue LEU 231 index1 958 path 250 %Seq 100.00
Highlighted IDENTICAL residue GLY 232 index1 959 path 251 %Seq 100.00
Highlighted IDENTICAL residue GLY 235 index1 962 path 254 %Seq 100.00
Highlighted IDENTICAL residue VAL 236 index1 963 path 255 %Seq 100.00
Highlighted IDENTICAL residue ASN 238 index1 965 path 257 %Seq 100.00
Highlighted IDENTICAL residue ARG 239 index1 966 path 258 %Seq 100.00
Highlighted IDENTICAL residue SER 240 index1 967 path 259 %Seq 100.00
Highlighted IDENTICAL residue GLN 241 index1 968 path 260 %Seq 100.00
Highlighted IDENTICAL residue GLU 242 index1 969 path 261 %Seq 100.00
Highlighted IDENTICAL residue ASP 243 index1 970 path 262 %Seq 100.00
Highlighted IDENTICAL residue ILE 244 index1 971 path 263 %Seq 100.00
Highlighted IDENTICAL residue SER 249 index1 976 path 268 %Seq 100.00
Highlighted IDENTICAL residue ILE 250 index1 977 path 269 %Seq 100.00
Highlighted IDENTICAL residue LEU 254 index1 981 path 273 %Seq 100.00
Highlighted IDENTICAL residue GLU 257 index1 984 path 276 %Seq 100.00
Highlighted IDENTICAL residue PHE 261 index1 988 path 280 %Seq 100.00
Highlighted IDENTICAL residue PRO 265 index1 992 path 284 %Seq 100.00
Highlighted IDENTICAL residue TYR 267 index1 994 path 286 %Seq 100.00
Highlighted IDENTICAL residue ARG 273 index1 1000 path 292 %Seq 100.00
Highlighted IDENTICAL residue GLY 275 index1 1002 path 294 %Seq 100.00
Highlighted IDENTICAL residue LEU 279 index1 1006 path 298 %Seq 100.00
Highlighted IDENTICAL residue LYS 281 index1 1008 path 300 %Seq 100.00
Highlighted IDENTICAL residue LEU 283 index1 1010 path 302 %Seq 100.00
Highlighted IDENTICAL residue ASN 284 index1 1011 path 303 %Seq 100.00
Highlighted IDENTICAL residue LEU 287 index1 1014 path 306 %Seq 100.00
Highlighted IDENTICAL residue HIS 290 index1 1017 path 309 %Seq 100.00
Highlighted IDENTICAL residue ILE 291 index1 1018 path 310 %Seq 100.00
Highlighted IDENTICAL residue LEU 295 index1 1022 path 314 %Seq 100.00
Highlighted IDENTICAL residue PRO 296 index1 1023 path 315 %Seq 100.00
Highlighted IDENTICAL residue LEU 298 index1 1025 path 317 %Seq 100.00
Highlighted IDENTICAL residue LYS 299 index1 1026 path 318 %Seq 100.00
Highlighted IDENTICAL residue LEU 306 index1 1033 path 325 %Seq 100.00
Highlighted 160 residues for visualization
Wrote PyMOL macro into file /usr/local/www/html/proteins/htdocs/results/At2g14120-1jwyB.pir.txt.1JWY.pdb.conservation.pml
===============================================================================
The program
/usr/local/www/html/proteins/Compiled_Programs/WYRM/PyMOL_highlight_conserved_residues At2g14120-1jwyB.pir.txt PIR amino_acid 1JWY.pdb _ 100.0 BLOSUM62.dat 
completed successfully.
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