############################################################### ############################################################### ############################################################### ### CCP4 6.0: CHAINSAW version 6.0 : ## ############################################################### User: pjx Run date: 5/ 2/2006 Run time: 17:33:08 Please reference: Collaborative Computational Project, Number 4. 1994. "The CCP4 Suite: Programs for Protein Crystallography". Acta Cryst. D50, 760-763. as well as any specific reference in the program write-up. Data line--- END PDB file /home/pjx/CCP4_REMOTE/ccp4/examples/data/1a80_A.pdb has been read in. *** input filename /home/pjx/CCP4_REMOTE/ccp4/examples/data/1mzr_1a80.pir target_seq = MANPTVIKLQDGNVMPQLGLGVWQASNEEVITAIQKALEVGYRSIDTAAAYKNEEGVGKALKNASVNREELFITTKLWNDDH--KRPREALLDSLKKLQLDYIDLYLMHWPVPAIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGKGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVWDFRLDKDELGEIAKLDQGK---RLGPDPDQFGG model_seq = -TVPSIV-LNDGNSIPQLGYGVFKVPPADTQRAVEEALEVGYRHIDTAAIYGNEEGVGAAIAASGIARDDLFITTKLWNDRHDGDEPAAAIAESLAKLALDQVDLYLVHWPTPAADNYVHAWEKMIELRAAGLTRSIGVSNHLVPHLERIVAATGVVPAVNQIELHPAYQQREITDWAAAHDVKIESWGPLGQGKYDLFGAEPVTAAAAAHGKTPAQAVLRWHLQKGFVVFPKSVRRERLEENLDVFDFDLTDTEIAAIDAMDPGDGSGRVSAHPDEVD- itarget = 280 imodel = 280 Target MANPTVIKLQ DGNVMPQLGL GVWQASNEEV ITAIQKALEV GYRSIDTAAA YKNEEGVGKA 60 * * *** **** ** * **** *** ***** * ****** * Model -TVPSIV-LN DGNSIPQLGY GVFKVPPADT QRAVEEALEV GYRHIDTAAI YGNEEGVGAA Target LKNASVNREE LFITTKLWND DH--KRPREA LLDSLKKLQL DYIDLYLMHW PVPAIDHYVE 120 * ********** * * * ** ** * * **** ** * ** * ** Model IAASGIARDD LFITTKLWND RHDGDEPAAA IAESLAKLAL DQVDLYLVHW PTPAADNYVH Target AWKGMIELQK EGLIKSIGVC NFQIHHLQRL IDETGVTPVI NQIELHPLMQ QRQLHAWNAT 180 ** **** ** **** * ** * *** * ******* * ** * * Model AWEKMIELRA AGLTRSIGVS NHLVPHLERI VAATGVVPAV NQIELHPAYQ QREITDWAAA Target HKIQTESWSP LAQGGKGVFD QKVIRDLADK YGKTPAQIVI RWHLDSGLVV IPKSVTPSRI 240 * *** * * ** * * ****** * **** * ** **** * Model HDVKIESWGP LGQGKYDLFG AEPVTAAAAA HGKTPAQAVL RWHLQKGFVV FPKSVRRERL Target AENFDVWDFR LDKDELGEIA KLDQGK---R LGPDPDQFGG 280 ** ** ** * * * * * * ** Model EENLDVFDFD LTDTEIAAID AMDPGDGSGR VSAHPDEVD- Target sequence in pdb format: SEQRES 1 A 275 MET ALA ASN PRO THR VAL ILE LYS LEU GLN ASP GLY ASN SEQRES 2 A 275 VAL MET PRO GLN LEU GLY LEU GLY VAL TRP GLN ALA SER SEQRES 3 A 275 ASN GLU GLU VAL ILE THR ALA ILE GLN LYS ALA LEU GLU SEQRES 4 A 275 VAL GLY TYR ARG SER ILE ASP THR ALA ALA ALA TYR LYS SEQRES 5 A 275 ASN GLU GLU GLY VAL GLY LYS ALA LEU LYS ASN ALA SER SEQRES 6 A 275 VAL ASN ARG GLU GLU LEU PHE ILE THR THR LYS LEU TRP SEQRES 7 A 275 ASN ASP ASP HIS LYS ARG PRO ARG GLU ALA LEU LEU ASP SEQRES 8 A 275 SER LEU LYS LYS LEU GLN LEU ASP TYR ILE ASP LEU TYR SEQRES 9 A 275 LEU MET HIS TRP PRO VAL PRO ALA ILE ASP HIS TYR VAL SEQRES 10 A 275 GLU ALA TRP LYS GLY MET ILE GLU LEU GLN LYS GLU GLY SEQRES 11 A 275 LEU ILE LYS SER ILE GLY VAL CYS ASN PHE GLN ILE HIS SEQRES 12 A 275 HIS LEU GLN ARG LEU ILE ASP GLU THR GLY VAL THR PRO SEQRES 13 A 275 VAL ILE ASN GLN ILE GLU LEU HIS PRO LEU MET GLN GLN SEQRES 14 A 275 ARG GLN LEU HIS ALA TRP ASN ALA THR HIS LYS ILE GLN SEQRES 15 A 275 THR GLU SER TRP SER PRO LEU ALA GLN GLY GLY LYS GLY SEQRES 16 A 275 VAL PHE ASP GLN LYS VAL ILE ARG ASP LEU ALA ASP LYS SEQRES 17 A 275 TYR GLY LYS THR PRO ALA GLN ILE VAL ILE ARG TRP HIS SEQRES 18 A 275 LEU ASP SER GLY LEU VAL VAL ILE PRO LYS SER VAL THR SEQRES 19 A 275 PRO SER ARG ILE ALA GLU ASN PHE ASP VAL TRP ASP PHE SEQRES 20 A 275 ARG LEU ASP LYS ASP GLU LEU GLY GLU ILE ALA LYS LEU SEQRES 21 A 275 ASP GLN GLY LYS ARG LEU GLY PRO ASP PRO ASP GLN PHE SEQRES 22 A 275 GLY GLY Number of models = 1. Number of chains in model 1 = 1. Number of residues in chain A = 277. pdb_seq = -TVPSIV-LNDGNSIPQLGYGVFKVPPADTQRAVEEALEVGYRHIDTAAIYGNEEGVGAAIAASGIARDDLFITTKLWNDRHDGDEPAAAIAESLAKLALDQVDLYLVHWPTPAADNYVHAWEKMIELRAAGLTRSIGVSNHLVPHLERIVAATGVVPAVNQIELHPAYQQREITDWAAAHDVKIESWGPLGQGKYDLFGAEPVTAAAAAHGKTPAQAVLRWHLQKGFVVFPKSVRRERLEENLDVFDFDLTDTEIAAIDAMDPGDGSGRVSAHPDEVD- Mutating residue T at position 1 to A. Mutating residue V at position 2 to N. Residue P at position 3 conserved. Mutating residue S at position 4 to T. Mutating residue I at position 5 to V. Mutating residue V at position 6 to I. Residue L at position 7 conserved. Mutating residue N at position 8 to Q. Residue D at position 9 conserved. Residue G at position 10 conserved. Residue N at position 11 conserved. Mutating residue S at position 12 to V. Mutating residue I at position 13 to M. Residue P at position 14 conserved. Residue Q at position 15 conserved. Residue L at position 16 conserved. Residue G at position 17 conserved. Mutating residue Y at position 18 to L. Residue G at position 19 conserved. Residue V at position 20 conserved. Mutating residue F at position 21 to W. Mutating residue K at position 22 to Q. Mutating residue V at position 23 to A. Mutating residue P at position 24 to S. Mutating residue P at position 25 to N. Mutating residue A at position 26 to E. Mutating residue D at position 27 to E. Mutating residue T at position 28 to V. Mutating residue Q at position 29 to I. Mutating residue R at position 30 to T. Residue A at position 31 conserved. Mutating residue V at position 32 to I. Mutating residue E at position 33 to Q. Mutating residue E at position 34 to K. Residue A at position 35 conserved. Residue L at position 36 conserved. Residue E at position 37 conserved. Residue V at position 38 conserved. Residue G at position 39 conserved. Residue Y at position 40 conserved. Residue R at position 41 conserved. Mutating residue H at position 42 to S. Residue I at position 43 conserved. Residue D at position 44 conserved. Residue T at position 45 conserved. Residue A at position 46 conserved. Residue A at position 47 conserved. Mutating residue I at position 48 to A. Residue Y at position 49 conserved. Mutating residue G at position 50 to K. Residue N at position 51 conserved. Residue E at position 52 conserved. Residue E at position 53 conserved. Residue G at position 54 conserved. Residue V at position 55 conserved. Residue G at position 56 conserved. Mutating residue A at position 57 to K. Residue A at position 58 conserved. Mutating residue I at position 59 to L. Mutating residue A at position 60 to K. Mutating residue A at position 61 to N. Mutating residue S at position 62 to A. Mutating residue G at position 63 to S. Mutating residue I at position 64 to V. Mutating residue A at position 65 to N. Residue R at position 66 conserved. Mutating residue D at position 67 to E. Mutating residue D at position 68 to E. Residue L at position 69 conserved. Residue F at position 70 conserved. Residue I at position 71 conserved. Residue T at position 72 conserved. Residue T at position 73 conserved. Residue K at position 74 conserved. Residue L at position 75 conserved. Residue W at position 76 conserved. Residue N at position 77 conserved. Residue D at position 78 conserved. Mutating residue R at position 79 to D. Residue H at position 80 conserved. Deleting residue D at position 81. Deleting residue G at position 82. Mutating residue D at position 83 to K. Mutating residue E at position 84 to R. Residue P at position 85 conserved. Mutating residue A at position 86 to R. Mutating residue A at position 87 to E. Residue A at position 88 conserved. Mutating residue I at position 89 to L. Mutating residue A at position 90 to L. Mutating residue E at position 91 to D. Residue S at position 92 conserved. Residue L at position 93 conserved. Mutating residue A at position 94 to K. Residue K at position 95 conserved. Residue L at position 96 conserved. Mutating residue A at position 97 to Q. Residue L at position 98 conserved. Residue D at position 99 conserved. Mutating residue Q at position 100 to Y. Mutating residue V at position 101 to I. Residue D at position 102 conserved. Residue L at position 103 conserved. Residue Y at position 104 conserved. Residue L at position 105 conserved. Mutating residue V at position 106 to M. Residue H at position 107 conserved. Residue W at position 108 conserved. Residue P at position 109 conserved. Mutating residue T at position 110 to V. Residue P at position 111 conserved. Residue A at position 112 conserved. Mutating residue A at position 113 to I. Residue D at position 114 conserved. Mutating residue N at position 115 to H. Residue Y at position 116 conserved. Residue V at position 117 conserved. Mutating residue H at position 118 to E. Residue A at position 119 conserved. Residue W at position 120 conserved. Mutating residue E at position 121 to K. Mutating residue K at position 122 to G. Residue M at position 123 conserved. Residue I at position 124 conserved. Residue E at position 125 conserved. Residue L at position 126 conserved. Mutating residue R at position 127 to Q. Mutating residue A at position 128 to K. Mutating residue A at position 129 to E. Residue G at position 130 conserved. Residue L at position 131 conserved. Mutating residue T at position 132 to I. Mutating residue R at position 133 to K. Residue S at position 134 conserved. Residue I at position 135 conserved. Residue G at position 136 conserved. Residue V at position 137 conserved. Mutating residue S at position 138 to C. Residue N at position 139 conserved. Mutating residue H at position 140 to F. Mutating residue L at position 141 to Q. Mutating residue V at position 142 to I. Mutating residue P at position 143 to H. Residue H at position 144 conserved. Residue L at position 145 conserved. Mutating residue E at position 146 to Q. Residue R at position 147 conserved. Mutating residue I at position 148 to L. Mutating residue V at position 149 to I. Mutating residue A at position 150 to D. Mutating residue A at position 151 to E. Residue T at position 152 conserved. Residue G at position 153 conserved. Residue V at position 154 conserved. Mutating residue V at position 155 to T. Residue P at position 156 conserved. Mutating residue A at position 157 to V. Mutating residue V at position 158 to I. Residue N at position 159 conserved. Residue Q at position 160 conserved. Residue I at position 161 conserved. Residue E at position 162 conserved. Residue L at position 163 conserved. Residue H at position 164 conserved. Residue P at position 165 conserved. Mutating residue A at position 166 to L. Mutating residue Y at position 167 to M. Residue Q at position 168 conserved. Residue Q at position 169 conserved. Residue R at position 170 conserved. Mutating residue E at position 171 to Q. Mutating residue I at position 172 to L. Mutating residue T at position 173 to H. Mutating residue D at position 174 to A. Residue W at position 175 conserved. Mutating residue A at position 176 to N. Residue A at position 177 conserved. Mutating residue A at position 178 to T. Residue H at position 179 conserved. Mutating residue D at position 180 to K. Mutating residue V at position 181 to I. Mutating residue K at position 182 to Q. Mutating residue I at position 183 to T. Residue E at position 184 conserved. Residue S at position 185 conserved. Residue W at position 186 conserved. Mutating residue G at position 187 to S. Residue P at position 188 conserved. Residue L at position 189 conserved. Mutating residue G at position 190 to A. Residue Q at position 191 conserved. Residue G at position 192 conserved. Mutating residue K at position 193 to G. Mutating residue Y at position 194 to K. Mutating residue D at position 195 to G. Mutating residue L at position 196 to V. Residue F at position 197 conserved. Mutating residue G at position 198 to D. Mutating residue A at position 199 to Q. Mutating residue E at position 200 to K. Mutating residue P at position 201 to V. Mutating residue V at position 202 to I. Mutating residue T at position 203 to R. Mutating residue A at position 204 to D. Mutating residue A at position 205 to L. Residue A at position 206 conserved. Mutating residue A at position 207 to D. Mutating residue A at position 208 to K. Mutating residue H at position 209 to Y. Residue G at position 210 conserved. Residue K at position 211 conserved. Residue T at position 212 conserved. Residue P at position 213 conserved. Residue A at position 214 conserved. Residue Q at position 215 conserved. Mutating residue A at position 216 to I. Residue V at position 217 conserved. Mutating residue L at position 218 to I. Residue R at position 219 conserved. Residue W at position 220 conserved. Residue H at position 221 conserved. Residue L at position 222 conserved. Mutating residue Q at position 223 to D. Mutating residue K at position 224 to S. Residue G at position 225 conserved. Mutating residue F at position 226 to L. Residue V at position 227 conserved. Residue V at position 228 conserved. Mutating residue F at position 229 to I. Residue P at position 230 conserved. Residue K at position 231 conserved. Residue S at position 232 conserved. Residue V at position 233 conserved. Mutating residue R at position 234 to T. Mutating residue R at position 235 to P. Mutating residue E at position 236 to S. Residue R at position 237 conserved. Mutating residue L at position 238 to I. Mutating residue E at position 239 to A. Residue E at position 240 conserved. Residue N at position 241 conserved. Mutating residue L at position 242 to F. Residue D at position 243 conserved. Residue V at position 244 conserved. Mutating residue F at position 245 to W. Residue D at position 246 conserved. Residue F at position 247 conserved. Mutating residue D at position 248 to R. Residue L at position 249 conserved. Mutating residue T at position 250 to D. Mutating residue D at position 251 to K. Mutating residue T at position 252 to D. Residue E at position 253 conserved. Mutating residue I at position 254 to L. Mutating residue A at position 255 to G. Mutating residue A at position 256 to E. Residue I at position 257 conserved. Mutating residue D at position 258 to A. Mutating residue A at position 259 to K. Mutating residue M at position 260 to L. Residue D at position 261 conserved. Mutating residue P at position 262 to Q. Residue G at position 263 conserved. Mutating residue D at position 264 to K. Deleting residue G at position 265. Deleting residue S at position 266. Deleting residue G at position 267. Residue R at position 268 conserved. Mutating residue V at position 269 to L. Mutating residue S at position 270 to G. Mutating residue A at position 271 to P. Mutating residue H at position 272 to D. Residue P at position 273 conserved. Residue D at position 274 conserved. Mutating residue E at position 275 to Q. Mutating residue V at position 276 to F. Mutating residue D at position 277 to G. 5 deleted, 139 conserved, 133 mutated Estimated sequence identity: 0.50 ...writing PDB file /tmp/pjx/1mzr_model.pdb CHAINSAW: Normal termination Times: User: 0.0s System: 0.0s Elapsed: 0:00