data_19835 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of E. coli Trigger Factor in complex with unfolded PhoA220-310 ; _BMRB_accession_number 19835 _BMRB_flat_file_name bmr19835.str _Entry_type original _Submission_date 2014-03-05 _Accession_date 2014-03-05 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Saio Tomohide . . 2 Guan Xiao . . 3 Rossi Paolo . . 4 Economou Anastassios . . 5 Kalodimos Charalampos G. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 1065 "13C chemical shifts" 481 "15N chemical shifts" 444 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-05-20 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 19836 'E. coli Trigger Factor in complex with unfolded PhoA1-150' 19837 'E. coli Trigger Factor in complex with unfolded PhoA365-471' stop_ _Original_release_date 2014-05-20 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural basis for protein antiaggregation activity of the trigger factor chaperone' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24812405 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Saio Tomohide . . 2 Guan Xiao . . 3 Rossi Paolo . . 4 Economou Anastassios . . 5 Kalodimos Charalampos G. . stop_ _Journal_abbreviation Science _Journal_volume 344 _Journal_issue 6184 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1250494 _Page_last 1250494 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'E. coli Trigger Factor in complex with unfolded PhoA220-310' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $entity_1 entity_2 $entity_2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 9596.792 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 93 _Mol_residue_sequence ; HMARADVTLGGGAKTFAETA TAGEWQGKTLREQAQARGYQ LVSDAASLNSVTEANQQKPL LGLFADGNMPVRWLGPKATY HGNIDKPAVTCTP ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1218 HIS 2 1219 MET 3 1220 ALA 4 1221 ARG 5 1222 ALA 6 1223 ASP 7 1224 VAL 8 1225 THR 9 1226 LEU 10 1227 GLY 11 1228 GLY 12 1229 GLY 13 1230 ALA 14 1231 LYS 15 1232 THR 16 1233 PHE 17 1234 ALA 18 1235 GLU 19 1236 THR 20 1237 ALA 21 1238 THR 22 1239 ALA 23 1240 GLY 24 1241 GLU 25 1242 TRP 26 1243 GLN 27 1244 GLY 28 1245 LYS 29 1246 THR 30 1247 LEU 31 1248 ARG 32 1249 GLU 33 1250 GLN 34 1251 ALA 35 1252 GLN 36 1253 ALA 37 1254 ARG 38 1255 GLY 39 1256 TYR 40 1257 GLN 41 1258 LEU 42 1259 VAL 43 1260 SER 44 1261 ASP 45 1262 ALA 46 1263 ALA 47 1264 SER 48 1265 LEU 49 1266 ASN 50 1267 SER 51 1268 VAL 52 1269 THR 53 1270 GLU 54 1271 ALA 55 1272 ASN 56 1273 GLN 57 1274 GLN 58 1275 LYS 59 1276 PRO 60 1277 LEU 61 1278 LEU 62 1279 GLY 63 1280 LEU 64 1281 PHE 65 1282 ALA 66 1283 ASP 67 1284 GLY 68 1285 ASN 69 1286 MET 70 1287 PRO 71 1288 VAL 72 1289 ARG 73 1290 TRP 74 1291 LEU 75 1292 GLY 76 1293 PRO 77 1294 LYS 78 1295 ALA 79 1296 THR 80 1297 TYR 81 1298 HIS 82 1299 GLY 83 1300 ASN 84 1301 ILE 85 1302 ASP 86 1303 LYS 87 1304 PRO 88 1305 ALA 89 1306 VAL 90 1307 THR 91 1308 CYS 92 1309 THR 93 1310 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-05 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1AJA "Three-Dimensional Structure Of The D153g Mutant Of E. Coli Alkaline Phosphatase: A Mutant With Weaker Magnesium Binding And Inc" 97.85 449 98.90 100.00 1.18e-55 PDB 1AJB "Three-Dimensional Structure Of The D153g Mutant Of E. Coli Alkaline Phosphatase: A Mutant With Weaker Magnesium Binding And Inc" 97.85 449 98.90 100.00 1.18e-55 PDB 1AJC "Three-Dimensional Structure Of The D153g Mutant Of E. Coli Alkaline Phosphatase: A Mutant With Weaker Magnesium Binding And Inc" 97.85 449 98.90 100.00 1.18e-55 PDB 1AJD "Three-Dimensional Structure Of The D153g Mutant Of E. Coli Alkaline Phosphatase: A Mutant With Weaker Magnesium Binding And Inc" 97.85 449 98.90 100.00 1.18e-55 PDB 1ALH "Kinetics And Crystal Structure Of A Mutant E. Coli Alkaline Phosphatase (Asp-369-->asn): A Mechanism Involving One Zinc Per Act" 97.85 446 98.90 100.00 1.15e-55 PDB 1ALI "Alkaline Phosphatase Mutant (H412n)" 97.85 449 100.00 100.00 3.65e-56 PDB 1ALJ "Alkaline Phosphatase Mutant (H412n)" 97.85 449 100.00 100.00 3.65e-56 PDB 1ALK "Reaction Mechanism Of Alkaline Phosphatase Based On Crystal Structures. Two Metal Ion Catalysis" 97.85 449 97.80 100.00 3.37e-55 PDB 1ANI "Alkaline Phosphatase (D153h, K328h)" 97.85 446 100.00 100.00 4.03e-56 PDB 1ANJ "Alkaline Phosphatase (K328h)" 97.85 446 100.00 100.00 4.03e-56 PDB 1B8J "Alkaline Phosphatase Complexed With Vanadate" 97.85 449 100.00 100.00 4.61e-56 PDB 1ED8 "Structure Of E. Coli Alkaline Phosphatase Inhibited By The Inorganic Phosphate At 1.75a Resolution" 97.85 449 100.00 100.00 3.65e-56 PDB 1ED9 "Structure Of E. Coli Alkaline Phosphatase Without The Inorganic Phosphate At 1.75a Resolution" 97.85 449 100.00 100.00 3.65e-56 PDB 1ELX "E. Coli Alkaline Phosphatase Mutant (S102a)" 97.85 449 100.00 100.00 3.69e-56 PDB 1ELY "E. Coli Alkaline Phosphatase Mutant (S102c)" 97.85 449 100.00 100.00 5.18e-56 PDB 1ELZ "E. Coli Alkaline Phosphatase Mutant (S102g)" 97.85 449 100.00 100.00 4.56e-56 PDB 1EW8 "Alkaline Phosphatase (e.c. 3.1.3.1) Complex With Phosphonoacetic Acid" 97.85 449 100.00 100.00 3.65e-56 PDB 1EW9 "Alkaline Phosphatase (E.C. 3.1.3.1) Complex With Mercaptomethyl Phosphonate" 97.85 449 100.00 100.00 3.65e-56 PDB 1HJK "Alkaline Phosphatase Mutant H331q" 97.85 449 100.00 100.00 4.42e-56 PDB 1HQA "Alkaline Phosphatase (H412q)" 97.85 449 100.00 100.00 3.73e-56 PDB 1KH4 "E. Coli Alkaline Phosphatase Mutant (d330n) In Complex With Phosphate" 97.85 449 97.80 100.00 3.20e-55 PDB 1KH5 "E. Coli Alkaline Phosphatase Mutant (d330n) Mimic Of The Transition States With Aluminium Fluoride" 97.85 449 97.80 100.00 3.20e-55 PDB 1KH7 "E. Coli Alkaline Phosphatase Mutant (d153gd330n)" 97.85 449 97.80 100.00 3.87e-55 PDB 1KH9 "E. Coli Alkaline Phosphatase Mutant (d153gd330n) Complex With Phosphate" 97.85 449 97.80 100.00 3.20e-55 PDB 1KHJ "E. Coli Alkaline Phosphatase Mutant (d153hd330n) Mimic Of The Transition States With Aluminium Fluoride" 97.85 449 97.80 100.00 3.41e-55 PDB 1KHK "E. Coli Alkaline Phosphatase Mutant (d153hd330n)" 97.85 449 97.80 100.00 3.41e-55 PDB 1KHL "E. Coli Alkaline Phosphatase Mutant (d153hd330n) Complex With Phosphate" 97.85 449 97.80 100.00 3.41e-55 PDB 1KHN "E. Coli Alkaline Phosphatase Mutant (d153hd330n) Zinc Form" 97.85 449 97.80 100.00 3.41e-55 PDB 1URA "Alkaline Phosphatase (D51zn)" 97.85 446 100.00 100.00 3.82e-56 PDB 1URB "Alkaline Phosphatase (N51mg)" 97.85 446 100.00 100.00 3.82e-56 PDB 1Y6V "Structure Of E. Coli Alkaline Phosphatase In Presence Of Cobalt At 1.60 A Resolution" 97.85 449 100.00 100.00 3.65e-56 PDB 1Y7A "Structure Of D153hK328W E. COLI ALKALINE PHOSPHATASE IN Presence Of Cobalt At 1.77 A Resolution" 97.85 449 100.00 100.00 6.89e-56 PDB 2ANH "Alkaline Phosphatase (D153h)" 97.85 446 100.00 100.00 3.86e-56 PDB 2G9Y "Structure Of S102t E. Coli Alkaline Phosphatase In Presence Of Phosphate At 2.00 A Resolution" 97.85 449 100.00 100.00 4.06e-56 PDB 2GA3 "Structure Of S102t E. Coli Alkaline Phosphatase-Phosphate Intermediate At 2.20a Resolution" 97.85 449 100.00 100.00 4.61e-56 PDB 2MLX "Nmr Structure Of E. Coli Trigger Factor In Complex With Unfolded Phoa220-310" 100.00 93 100.00 100.00 3.25e-61 PDB 3BDF "Crystal Structure Of Metal-Free E. Coli Alkaline Phosphatase (T155v)" 97.85 458 100.00 100.00 5.64e-56 PDB 3BDG "Crystal Structure Of Wild-TypeT155V MIXED DIMER OF E. COLI ALKALINE Phosphatase" 97.85 458 100.00 100.00 4.61e-56 PDB 3BDH "Crystal Structure Of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase" 97.85 458 100.00 100.00 5.41e-56 PDB 3CMR "E. Coli Alkaline Phosphatase Mutant R166s In Complex With Phosphate" 97.85 449 100.00 100.00 3.54e-56 PDB 3DPC "Structure Of E.coli Alkaline Phosphatase Mutant In Complex With A Phosphorylated Peptide" 97.85 455 100.00 100.00 5.43e-56 PDB 3DYC "Structure Of E322y Alkaline Phosphatase In Complex With Inorganic Phosphate" 97.85 449 100.00 100.00 4.10e-56 PDB 3TG0 "E. Coli Alkaline Phosphatase With Bound Inorganic Phosphate" 97.85 449 100.00 100.00 3.65e-56 PDB 4KM4 "E. Coli Alkaline Phosphatase Mutant S102g/r166s In Complex With Inorganic Phosphate" 97.85 445 100.00 100.00 3.66e-56 PDB 4YR1 "Crystal Structure Of E. Coli Alkaline Phosphatase D101a/d153a In Complex With Inorganic Phosphate" 97.85 443 100.00 100.00 2.84e-56 DBJ BAB33856 "alkaline phosphatase [Escherichia coli O157:H7 str. Sakai]" 97.85 494 100.00 100.00 9.05e-56 DBJ BAE76164 "alkaline phosphatase [Escherichia coli str. K12 substr. W3110]" 97.85 471 100.00 100.00 6.54e-56 DBJ BAG75928 "alkaline phosphatase [Escherichia coli SE11]" 97.85 494 98.90 100.00 3.03e-55 DBJ BAI23756 "bacterial alkaline phosphatase PhoA [Escherichia coli O26:H11 str. 11368]" 97.85 471 100.00 100.00 5.08e-56 DBJ BAI29227 "bacterial alkaline phosphatase PhoA [Escherichia coli O103:H2 str. 12009]" 97.85 471 98.90 100.00 1.74e-55 EMBL CAA28257 "alkaline phosphatase [Escherichia coli]" 97.85 471 100.00 100.00 6.54e-56 EMBL CAP74918 "alkaline phosphatase [Escherichia coli LF82]" 97.85 471 97.80 97.80 3.13e-54 EMBL CAQ30851 "alkaline phosphatase [Escherichia coli BL21(DE3)]" 97.85 471 97.80 98.90 2.17e-54 EMBL CAQ97255 "bacterial alkaline phosphatase [Escherichia coli IAI1]" 97.85 471 100.00 100.00 6.54e-56 EMBL CAR01727 "bacterial alkaline phosphatase [Escherichia coli S88]" 97.85 471 97.80 97.80 3.13e-54 GB AAA24363 "alkaline phosphatase precursor (EC 3.1.3.1) [Escherichia coli]" 97.85 471 97.80 100.00 7.63e-55 GB AAA24364 "alkaline phosphatase precursor (EC 3.1.3.1) [Escherichia coli]" 97.85 471 100.00 100.00 6.54e-56 GB AAA24365 "alkaline phosphatase precursor (EC 3.1.3.1) [Escherichia coli]" 97.85 471 100.00 100.00 6.54e-56 GB AAA24366 "alkaline phosphatase precursor (EC 3.1.3.1) [Escherichia coli]" 97.85 471 97.80 100.00 6.87e-55 GB AAA24367 "alkaline phosphatase precursor (EC 3.1.3.1) [Escherichia coli]" 97.85 471 98.90 100.00 2.07e-55 REF NP_308460 "alkaline phosphatase [Escherichia coli O157:H7 str. Sakai]" 97.85 494 100.00 100.00 9.05e-56 REF NP_414917 "bacterial alkaline phosphatase [Escherichia coli str. K-12 substr. MG1655]" 97.85 471 100.00 100.00 6.54e-56 REF NP_706185 "alkaline phosphatase [Shigella flexneri 2a str. 301]" 97.85 494 97.80 98.90 1.55e-53 REF WP_000089619 "alkaline phosphatase [Escherichia coli]" 97.85 494 100.00 100.00 9.05e-56 REF WP_000089625 "alkaline phosphatase [Shigella flexneri]" 97.85 494 97.80 98.90 1.55e-53 SP P00634 "RecName: Full=Alkaline phosphatase; Short=APase; Flags: Precursor" 97.85 471 100.00 100.00 6.54e-56 stop_ save_ save_entity_2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_2 _Molecular_mass 48256.020 _Mol_thiol_state 'not present' _Details . _Residue_count 443 _Mol_residue_sequence ; MNHKVHHHHHHMQVSVETTQ GLGRRVTITIAADSIETAVK SELVNVAKKVRIDGFRKGKV PMNIVAQRYGASVRQDVLGD LMSRNFIDAIIKEKINPAGA PTYVPGEYKLGEDFTYSVEF EVYPEVELQGLEAIEVEKPI VEVTDADVDGMLDTLRKQQA TWKEKDGAVEAEDRVTIDFT GSVDGEEFEGGKASDFVLAM GQGRMIPGFEDGIKGHKAGE EFTIDVTFPEEYHAENLKGK AAKFAINLKKVEERELPELT AEFIKRFGVEDGSVEGLRAE VRKNMERELKSAIRNRVKSQ AIEGLVKANDIDVPAALIDS EIDVLRRQAAQRFGGNEKQA LELPRELFEEQAKRRVVVGL LLGEVIRTNELKADEERVKG LIEEMASAYEDPKEVIEFYS KNKELMDNMRNVALEEQAVE AVLAKAKVTEKETTFNELMN QQA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -10 MET 2 -9 ASN 3 -8 HIS 4 -7 LYS 5 -6 VAL 6 -5 HIS 7 -4 HIS 8 -3 HIS 9 -2 HIS 10 -1 HIS 11 0 HIS 12 1 MET 13 2 GLN 14 3 VAL 15 4 SER 16 5 VAL 17 6 GLU 18 7 THR 19 8 THR 20 9 GLN 21 10 GLY 22 11 LEU 23 12 GLY 24 13 ARG 25 14 ARG 26 15 VAL 27 16 THR 28 17 ILE 29 18 THR 30 19 ILE 31 20 ALA 32 21 ALA 33 22 ASP 34 23 SER 35 24 ILE 36 25 GLU 37 26 THR 38 27 ALA 39 28 VAL 40 29 LYS 41 30 SER 42 31 GLU 43 32 LEU 44 33 VAL 45 34 ASN 46 35 VAL 47 36 ALA 48 37 LYS 49 38 LYS 50 39 VAL 51 40 ARG 52 41 ILE 53 42 ASP 54 43 GLY 55 44 PHE 56 45 ARG 57 46 LYS 58 47 GLY 59 48 LYS 60 49 VAL 61 50 PRO 62 51 MET 63 52 ASN 64 53 ILE 65 54 VAL 66 55 ALA 67 56 GLN 68 57 ARG 69 58 TYR 70 59 GLY 71 60 ALA 72 61 SER 73 62 VAL 74 63 ARG 75 64 GLN 76 65 ASP 77 66 VAL 78 67 LEU 79 68 GLY 80 69 ASP 81 70 LEU 82 71 MET 83 72 SER 84 73 ARG 85 74 ASN 86 75 PHE 87 76 ILE 88 77 ASP 89 78 ALA 90 79 ILE 91 80 ILE 92 81 LYS 93 82 GLU 94 83 LYS 95 84 ILE 96 85 ASN 97 86 PRO 98 87 ALA 99 88 GLY 100 89 ALA 101 90 PRO 102 91 THR 103 92 TYR 104 93 VAL 105 94 PRO 106 95 GLY 107 96 GLU 108 97 TYR 109 98 LYS 110 99 LEU 111 100 GLY 112 101 GLU 113 102 ASP 114 103 PHE 115 104 THR 116 105 TYR 117 106 SER 118 107 VAL 119 108 GLU 120 109 PHE 121 110 GLU 122 111 VAL 123 112 TYR 124 113 PRO 125 114 GLU 126 115 VAL 127 116 GLU 128 117 LEU 129 118 GLN 130 119 GLY 131 120 LEU 132 121 GLU 133 122 ALA 134 123 ILE 135 124 GLU 136 125 VAL 137 126 GLU 138 127 LYS 139 128 PRO 140 129 ILE 141 130 VAL 142 131 GLU 143 132 VAL 144 133 THR 145 134 ASP 146 135 ALA 147 136 ASP 148 137 VAL 149 138 ASP 150 139 GLY 151 140 MET 152 141 LEU 153 142 ASP 154 143 THR 155 144 LEU 156 145 ARG 157 146 LYS 158 147 GLN 159 148 GLN 160 149 ALA 161 150 THR 162 151 TRP 163 152 LYS 164 153 GLU 165 154 LYS 166 155 ASP 167 156 GLY 168 157 ALA 169 158 VAL 170 159 GLU 171 160 ALA 172 161 GLU 173 162 ASP 174 163 ARG 175 164 VAL 176 165 THR 177 166 ILE 178 167 ASP 179 168 PHE 180 169 THR 181 170 GLY 182 171 SER 183 172 VAL 184 173 ASP 185 174 GLY 186 175 GLU 187 176 GLU 188 177 PHE 189 178 GLU 190 179 GLY 191 180 GLY 192 181 LYS 193 182 ALA 194 183 SER 195 184 ASP 196 185 PHE 197 186 VAL 198 187 LEU 199 188 ALA 200 189 MET 201 190 GLY 202 191 GLN 203 192 GLY 204 193 ARG 205 194 MET 206 195 ILE 207 196 PRO 208 197 GLY 209 198 PHE 210 199 GLU 211 200 ASP 212 201 GLY 213 202 ILE 214 203 LYS 215 204 GLY 216 205 HIS 217 206 LYS 218 207 ALA 219 208 GLY 220 209 GLU 221 210 GLU 222 211 PHE 223 212 THR 224 213 ILE 225 214 ASP 226 215 VAL 227 216 THR 228 217 PHE 229 218 PRO 230 219 GLU 231 220 GLU 232 221 TYR 233 222 HIS 234 223 ALA 235 224 GLU 236 225 ASN 237 226 LEU 238 227 LYS 239 228 GLY 240 229 LYS 241 230 ALA 242 231 ALA 243 232 LYS 244 233 PHE 245 234 ALA 246 235 ILE 247 236 ASN 248 237 LEU 249 238 LYS 250 239 LYS 251 240 VAL 252 241 GLU 253 242 GLU 254 243 ARG 255 244 GLU 256 245 LEU 257 246 PRO 258 247 GLU 259 248 LEU 260 249 THR 261 250 ALA 262 251 GLU 263 252 PHE 264 253 ILE 265 254 LYS 266 255 ARG 267 256 PHE 268 257 GLY 269 258 VAL 270 259 GLU 271 260 ASP 272 261 GLY 273 262 SER 274 263 VAL 275 264 GLU 276 265 GLY 277 266 LEU 278 267 ARG 279 268 ALA 280 269 GLU 281 270 VAL 282 271 ARG 283 272 LYS 284 273 ASN 285 274 MET 286 275 GLU 287 276 ARG 288 277 GLU 289 278 LEU 290 279 LYS 291 280 SER 292 281 ALA 293 282 ILE 294 283 ARG 295 284 ASN 296 285 ARG 297 286 VAL 298 287 LYS 299 288 SER 300 289 GLN 301 290 ALA 302 291 ILE 303 292 GLU 304 293 GLY 305 294 LEU 306 295 VAL 307 296 LYS 308 297 ALA 309 298 ASN 310 299 ASP 311 300 ILE 312 301 ASP 313 302 VAL 314 303 PRO 315 304 ALA 316 305 ALA 317 306 LEU 318 307 ILE 319 308 ASP 320 309 SER 321 310 GLU 322 311 ILE 323 312 ASP 324 313 VAL 325 314 LEU 326 315 ARG 327 316 ARG 328 317 GLN 329 318 ALA 330 319 ALA 331 320 GLN 332 321 ARG 333 322 PHE 334 323 GLY 335 324 GLY 336 325 ASN 337 326 GLU 338 327 LYS 339 328 GLN 340 329 ALA 341 330 LEU 342 331 GLU 343 332 LEU 344 333 PRO 345 334 ARG 346 335 GLU 347 336 LEU 348 337 PHE 349 338 GLU 350 339 GLU 351 340 GLN 352 341 ALA 353 342 LYS 354 343 ARG 355 344 ARG 356 345 VAL 357 346 VAL 358 347 VAL 359 348 GLY 360 349 LEU 361 350 LEU 362 351 LEU 363 352 GLY 364 353 GLU 365 354 VAL 366 355 ILE 367 356 ARG 368 357 THR 369 358 ASN 370 359 GLU 371 360 LEU 372 361 LYS 373 362 ALA 374 363 ASP 375 364 GLU 376 365 GLU 377 366 ARG 378 367 VAL 379 368 LYS 380 369 GLY 381 370 LEU 382 371 ILE 383 372 GLU 384 373 GLU 385 374 MET 386 375 ALA 387 376 SER 388 377 ALA 389 378 TYR 390 379 GLU 391 380 ASP 392 381 PRO 393 382 LYS 394 383 GLU 395 384 VAL 396 385 ILE 397 386 GLU 398 387 PHE 399 388 TYR 400 389 SER 401 390 LYS 402 391 ASN 403 392 LYS 404 393 GLU 405 394 LEU 406 395 MET 407 396 ASP 408 397 ASN 409 398 MET 410 399 ARG 411 400 ASN 412 401 VAL 413 402 ALA 414 403 LEU 415 404 GLU 416 405 GLU 417 406 GLN 418 407 ALA 419 408 VAL 420 409 GLU 421 410 ALA 422 411 VAL 423 412 LEU 424 413 ALA 425 414 LYS 426 415 ALA 427 416 LYS 428 417 VAL 429 418 THR 430 419 GLU 431 420 LYS 432 421 GLU 433 422 THR 434 423 THR 435 424 PHE 436 425 ASN 437 426 GLU 438 427 LEU 439 428 MET 440 429 ASN 441 430 GLN 442 431 GLN 443 432 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 19836 entity_2 100.00 443 100.00 100.00 0.00e+00 BMRB 19837 entity_2 100.00 443 100.00 100.00 0.00e+00 PDB 1W26 "Trigger Factor In Complex With The Ribosome Forms A Molecular Cradle For Nascent Proteins" 97.29 432 97.68 97.68 0.00e+00 PDB 2MLX "Nmr Structure Of E. Coli Trigger Factor In Complex With Unfolded Phoa220-310" 100.00 443 100.00 100.00 0.00e+00 PDB 2MLY "Nmr Structure Of E. Coli Trigger Factor In Complex With Unfolded Phoa1-150" 100.00 443 100.00 100.00 0.00e+00 PDB 2MLZ "Nmr Structure Of E. Coli Trigger Factor In Complex With Unfolded Phoa365-471" 100.00 443 100.00 100.00 0.00e+00 PDB 2VRH "Structure Of The E. Coli Trigger Factor Bound To A Translating Ribosome" 97.29 432 97.68 97.68 0.00e+00 DBJ BAB33913 "trigger factor [Escherichia coli O157:H7 str. Sakai]" 97.52 432 100.00 100.00 0.00e+00 DBJ BAD98926 "trigger factor tag [Expression vector pColdTF]" 100.00 489 100.00 100.00 0.00e+00 DBJ BAE76216 "peptidyl-prolyl cis/trans isomerase [Escherichia coli str. K-12 substr. W3110]" 97.52 432 100.00 100.00 0.00e+00 DBJ BAG75986 "trigger factor [Escherichia coli SE11]" 97.52 432 99.77 100.00 0.00e+00 DBJ BAI23810 "peptidyl-prolyl cis/trans isomerase [Escherichia coli O26:H11 str. 11368]" 97.52 432 99.77 99.77 0.00e+00 EMBL CAP74970 "Trigger factor [Escherichia coli LF82]" 97.52 432 99.77 99.77 0.00e+00 EMBL CAQ30908 "trigger factor; a molecular chaperone involved in cell division [Escherichia coli BL21(DE3)]" 97.52 432 100.00 100.00 0.00e+00 EMBL CAQ97312 "peptidyl-prolyl cis/trans isomerase (trigger factor) [Escherichia coli IAI1]" 97.52 432 100.00 100.00 0.00e+00 EMBL CAR01780 "peptidyl-prolyl cis/trans isomerase (trigger factor) [Escherichia coli S88]" 96.84 429 100.00 100.00 0.00e+00 EMBL CAR06670 "peptidyl-prolyl cis/trans isomerase (trigger factor) [Escherichia coli ED1a]" 97.52 432 100.00 100.00 0.00e+00 GB AAA62791 "trigger factor [Escherichia coli]" 97.52 432 97.69 98.61 0.00e+00 GB AAB40192 "trigger factor [Escherichia coli]" 97.52 432 100.00 100.00 0.00e+00 GB AAC73539 "peptidyl-prolyl cis/trans isomerase (trigger factor) [Escherichia coli str. K-12 substr. MG1655]" 97.52 432 100.00 100.00 0.00e+00 GB AAG54786 "trigger factor; a molecular chaperone involved in cell division [Escherichia coli O157:H7 str. EDL933]" 97.52 432 100.00 100.00 0.00e+00 GB AAN42037 "trigger factor [Shigella flexneri 2a str. 301]" 97.52 432 100.00 100.00 0.00e+00 REF NP_286178 "trigger factor [Escherichia coli O157:H7 str. EDL933]" 97.52 432 100.00 100.00 0.00e+00 REF NP_308517 "trigger factor [Escherichia coli O157:H7 str. Sakai]" 97.52 432 100.00 100.00 0.00e+00 REF NP_414970 "peptidyl-prolyl cis/trans isomerase (trigger factor) [Escherichia coli str. K-12 substr. MG1655]" 97.52 432 100.00 100.00 0.00e+00 REF NP_706330 "trigger factor [Shigella flexneri 2a str. 301]" 97.52 432 100.00 100.00 0.00e+00 REF NP_752485 "trigger factor [Escherichia coli CFT073]" 97.52 432 99.77 99.77 0.00e+00 SP A1A8A5 "RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase [Escherichia coli APEC O1]" 96.84 429 100.00 100.00 0.00e+00 SP A7ZIJ4 "RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase [Escherichia coli E24377A]" 97.52 432 99.77 100.00 0.00e+00 SP A7ZX94 "RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase [Escherichia coli HS]" 97.52 432 100.00 100.00 0.00e+00 SP B1J012 "RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase [Escherichia coli ATCC 8739]" 97.52 432 100.00 100.00 0.00e+00 SP B1LJJ3 "RecName: Full=Trigger factor; Short=TF; AltName: Full=PPIase [Escherichia coli SMS-3-5]" 97.52 432 100.00 100.00 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 'E. coli' 469008 Bacteria . Escherichia coli $entity_2 'E. coli' 469008 Bacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $entity_1 'recombinant technology' . Escherichia coli BL21(DE3) pET16b $entity_2 'recombinant technology' . Escherichia coli BL21(DE3) pCold stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 0.5 mM '[U-100% 13C; U-100% 15N]' $entity_2 0.5 mM '[U-100% 13C; U-100% 15N]' 'potassium chloride' 100 mM 'natural abundance' BME 3 mM 'natural abundance' 'potassium phosphate' 20 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.113 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_CNS _Saveframe_category software _Name CNS _Version . loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_OLIVIA _Saveframe_category software _Name OLIVIA _Version 1.16 loop_ _Vendor _Address _Electronic_address 'Olivia, Yokochi Masashi' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version 3.0 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ save_X-PLOR_NIH _Saveframe_category software _Name X-PLOR_NIH _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_TALOSN _Saveframe_category software _Name TALOSN _Version . loop_ _Vendor _Address _Electronic_address 'Shen and Bax' . . stop_ loop_ _Task 'geometry optimization' stop_ _Details . save_ save_PSVS _Saveframe_category software _Name PSVS _Version 1.5 loop_ _Vendor _Address _Electronic_address 'Bhattacharya and Montelione' . . stop_ loop_ _Task validation stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_1H-13C_HMQC-NOESY_HMQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C HMQC-NOESY_HMQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HMQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HMQC' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 7 . pH pressure 1 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name entity_2 _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 12 MET HE H 2.108 0.02 1 2 1 12 MET CE C 17.403 0.20 1 3 3 14 VAL H H 8.321 0.02 1 4 3 14 VAL HG1 H 0.840 0.02 2 5 3 14 VAL HG2 H 0.858 0.02 2 6 3 14 VAL CG1 C 21.584 0.20 2 7 3 14 VAL CG2 C 17.303 0.20 2 8 3 14 VAL N N 122.686 0.20 1 9 4 15 SER H H 8.689 0.02 1 10 4 15 SER N N 121.236 0.20 1 11 5 16 VAL H H 8.806 0.02 1 12 5 16 VAL HG1 H 0.765 0.02 2 13 5 16 VAL HG2 H 1.056 0.02 2 14 5 16 VAL CG1 C 20.086 0.20 2 15 5 16 VAL CG2 C 21.484 0.20 2 16 5 16 VAL N N 125.511 0.20 1 17 6 17 GLU H H 8.922 0.02 1 18 6 17 GLU N N 126.142 0.20 1 19 7 18 THR H H 8.711 0.02 1 20 7 18 THR N N 118.421 0.20 1 21 8 19 THR H H 7.708 0.02 1 22 8 19 THR N N 117.503 0.20 1 23 9 20 GLN H H 8.239 0.02 1 24 9 20 GLN N N 119.524 0.20 1 25 11 22 LEU H H 8.990 0.02 1 26 11 22 LEU HD1 H 0.733 0.02 2 27 11 22 LEU HD2 H 0.934 0.02 2 28 11 22 LEU CD1 C 22.234 0.20 2 29 11 22 LEU CD2 C 25.718 0.20 2 30 11 22 LEU N N 129.153 0.20 1 31 12 23 GLY H H 8.537 0.02 1 32 12 23 GLY N N 106.953 0.20 1 33 13 24 ARG H H 8.919 0.02 1 34 13 24 ARG N N 124.485 0.20 1 35 14 25 ARG H H 8.684 0.02 1 36 14 25 ARG N N 120.539 0.20 1 37 15 26 VAL H H 9.312 0.02 1 38 15 26 VAL HG1 H 1.158 0.02 2 39 15 26 VAL HG2 H 1.054 0.02 2 40 15 26 VAL CG1 C 22.607 0.20 2 41 15 26 VAL CG2 C 21.443 0.20 2 42 15 26 VAL N N 126.770 0.20 1 43 16 27 THR H H 8.945 0.02 1 44 16 27 THR N N 125.094 0.20 1 45 17 28 ILE H H 8.563 0.02 1 46 17 28 ILE HD1 H 0.827 0.02 1 47 17 28 ILE CD1 C 13.908 0.20 1 48 17 28 ILE N N 129.070 0.20 1 49 18 29 THR H H 8.357 0.02 1 50 18 29 THR N N 121.479 0.20 1 51 19 30 ILE H H 9.912 0.02 1 52 19 30 ILE HD1 H 0.930 0.02 1 53 19 30 ILE CD1 C 14.412 0.20 1 54 19 30 ILE N N 127.534 0.20 1 55 20 31 ALA H H 8.690 0.02 1 56 20 31 ALA HB H 1.553 0.02 1 57 20 31 ALA CB C 19.542 0.20 1 58 20 31 ALA N N 129.247 0.20 1 59 21 32 ALA H H 9.376 0.02 1 60 21 32 ALA HB H 1.334 0.02 1 61 21 32 ALA CB C 18.742 0.20 1 62 21 32 ALA N N 126.228 0.20 1 63 22 33 ASP H H 8.927 0.02 1 64 22 33 ASP N N 115.111 0.20 1 65 23 34 SER H H 7.597 0.02 1 66 23 34 SER N N 116.495 0.20 1 67 24 35 ILE H H 7.390 0.02 1 68 24 35 ILE HD1 H 0.890 0.02 1 69 24 35 ILE CD1 C 14.923 0.20 1 70 24 35 ILE N N 122.361 0.20 1 71 25 36 GLU H H 8.233 0.02 1 72 25 36 GLU N N 117.692 0.20 1 73 26 37 THR H H 8.264 0.02 1 74 26 37 THR N N 115.095 0.20 1 75 27 38 ALA H H 7.328 0.02 1 76 27 38 ALA HB H 1.523 0.02 1 77 27 38 ALA CB C 18.985 0.20 1 78 27 38 ALA N N 125.189 0.20 1 79 28 39 VAL H H 8.607 0.02 1 80 28 39 VAL HG1 H 0.907 0.02 2 81 28 39 VAL HG2 H 0.823 0.02 2 82 28 39 VAL CG1 C 23.815 0.20 2 83 28 39 VAL CG2 C 20.965 0.20 2 84 28 39 VAL N N 119.922 0.20 1 85 29 40 LYS H H 8.102 0.02 1 86 29 40 LYS N N 118.843 0.20 1 87 30 41 SER H H 7.896 0.02 1 88 30 41 SER N N 112.454 0.20 1 89 31 42 GLU H H 7.871 0.02 1 90 31 42 GLU N N 121.930 0.20 1 91 32 43 LEU H H 8.664 0.02 1 92 32 43 LEU HD1 H 0.793 0.02 2 93 32 43 LEU HD2 H 0.679 0.02 2 94 32 43 LEU CD1 C 26.207 0.20 2 95 32 43 LEU CD2 C 23.471 0.20 2 96 32 43 LEU N N 121.004 0.20 1 97 33 44 VAL H H 7.683 0.02 1 98 33 44 VAL HG1 H 1.056 0.02 2 99 33 44 VAL HG2 H 0.655 0.02 2 100 33 44 VAL CG1 C 22.846 0.20 2 101 33 44 VAL CG2 C 21.438 0.20 2 102 33 44 VAL N N 118.838 0.20 1 103 34 45 ASN H H 7.241 0.02 1 104 34 45 ASN N N 118.030 0.20 1 105 35 46 VAL H H 8.445 0.02 1 106 35 46 VAL HG1 H 0.873 0.02 2 107 35 46 VAL HG2 H 0.872 0.02 2 108 35 46 VAL CG1 C 23.633 0.20 2 109 35 46 VAL CG2 C 22.866 0.20 2 110 35 46 VAL N N 121.777 0.20 1 111 36 47 ALA H H 8.311 0.02 1 112 36 47 ALA HB H 1.491 0.02 1 113 36 47 ALA CB C 18.907 0.20 1 114 36 47 ALA N N 120.267 0.20 1 115 37 48 LYS H H 7.351 0.02 1 116 37 48 LYS N N 114.141 0.20 1 117 38 49 LYS H H 7.606 0.02 1 118 38 49 LYS N N 115.473 0.20 1 119 39 50 VAL H H 7.419 0.02 1 120 39 50 VAL HG1 H 0.903 0.02 2 121 39 50 VAL HG2 H 0.718 0.02 2 122 39 50 VAL CG1 C 20.483 0.20 2 123 39 50 VAL CG2 C 21.327 0.20 2 124 39 50 VAL N N 116.433 0.20 1 125 40 51 ARG H H 8.368 0.02 1 126 40 51 ARG N N 124.277 0.20 1 127 41 52 ILE H H 8.073 0.02 1 128 41 52 ILE HD1 H 0.796 0.02 1 129 41 52 ILE CD1 C 13.971 0.20 1 130 41 52 ILE N N 124.148 0.20 1 131 42 53 ASP H H 8.573 0.02 1 132 42 53 ASP N N 124.954 0.20 1 133 43 54 GLY H H 8.475 0.02 1 134 43 54 GLY N N 110.101 0.20 1 135 44 55 PHE H H 8.085 0.02 1 136 44 55 PHE N N 118.593 0.20 1 137 45 56 ARG H H 8.721 0.02 1 138 45 56 ARG N N 122.232 0.20 1 139 46 57 LYS H H 8.634 0.02 1 140 46 57 LYS N N 122.694 0.20 1 141 47 58 GLY H H 8.924 0.02 1 142 47 58 GLY N N 113.989 0.20 1 143 48 59 LYS H H 8.093 0.02 1 144 48 59 LYS N N 119.432 0.20 1 145 49 60 VAL H H 8.061 0.02 1 146 49 60 VAL HG1 H 0.819 0.02 2 147 49 60 VAL HG2 H 0.654 0.02 2 148 49 60 VAL CG1 C 22.264 0.20 2 149 49 60 VAL CG2 C 21.368 0.20 2 150 49 60 VAL N N 123.619 0.20 1 151 51 62 MET HE H 1.939 0.02 1 152 51 62 MET CE C 16.268 0.20 1 153 52 63 ASN H H 8.833 0.02 1 154 52 63 ASN N N 123.474 0.20 1 155 53 64 ILE H H 7.208 0.02 1 156 53 64 ILE HD1 H 0.791 0.02 1 157 53 64 ILE CD1 C 11.563 0.20 1 158 53 64 ILE N N 121.514 0.20 1 159 54 65 VAL H H 7.494 0.02 1 160 54 65 VAL HG1 H 0.894 0.02 2 161 54 65 VAL HG2 H 0.893 0.02 2 162 54 65 VAL CG1 C 21.755 0.20 2 163 54 65 VAL CG2 C 21.202 0.20 2 164 54 65 VAL N N 120.799 0.20 1 165 55 66 ALA H H 8.869 0.02 1 166 55 66 ALA HB H 1.425 0.02 1 167 55 66 ALA CB C 17.841 0.20 1 168 55 66 ALA N N 120.856 0.20 1 169 56 67 GLN H H 7.666 0.02 1 170 56 67 GLN N N 118.538 0.20 1 171 57 68 ARG H H 8.020 0.02 1 172 57 68 ARG N N 116.667 0.20 1 173 58 69 TYR H H 8.619 0.02 1 174 58 69 TYR N N 114.284 0.20 1 175 59 70 GLY H H 8.158 0.02 1 176 59 70 GLY N N 109.105 0.20 1 177 60 71 ALA H H 8.507 0.02 1 178 60 71 ALA HB H 1.418 0.02 1 179 60 71 ALA CB C 17.878 0.20 1 180 60 71 ALA N N 122.730 0.20 1 181 61 72 SER H H 8.059 0.02 1 182 61 72 SER N N 115.187 0.20 1 183 62 73 VAL H H 8.399 0.02 1 184 62 73 VAL HG1 H 1.052 0.02 2 185 62 73 VAL HG2 H 0.902 0.02 2 186 62 73 VAL CG1 C 23.761 0.20 2 187 62 73 VAL CG2 C 22.741 0.20 2 188 62 73 VAL N N 122.495 0.20 1 189 63 74 ARG H H 8.300 0.02 1 190 63 74 ARG N N 118.635 0.20 1 191 64 75 GLN H H 7.481 0.02 1 192 64 75 GLN N N 116.268 0.20 1 193 65 76 ASP H H 7.847 0.02 1 194 65 76 ASP N N 121.702 0.20 1 195 66 77 VAL H H 8.728 0.02 1 196 66 77 VAL HG1 H 0.903 0.02 2 197 66 77 VAL CG1 C 23.133 0.20 2 198 66 77 VAL N N 121.548 0.20 1 199 67 78 LEU H H 8.284 0.02 1 200 67 78 LEU HD1 H 0.027 0.02 2 201 67 78 LEU HD2 H -0.120 0.02 2 202 67 78 LEU CD1 C 24.067 0.20 2 203 67 78 LEU CD2 C 22.218 0.20 2 204 67 78 LEU N N 119.779 0.20 1 205 68 79 GLY H H 7.660 0.02 1 206 68 79 GLY N N 104.928 0.20 1 207 69 80 ASP H H 7.723 0.02 1 208 69 80 ASP N N 123.146 0.20 1 209 70 81 LEU H H 8.948 0.02 1 210 70 81 LEU HD1 H 0.681 0.02 2 211 70 81 LEU HD2 H 0.738 0.02 2 212 70 81 LEU CD1 C 26.787 0.20 2 213 70 81 LEU CD2 C 22.399 0.20 2 214 70 81 LEU N N 118.632 0.20 1 215 71 82 MET H H 8.725 0.02 1 216 71 82 MET HE H 1.803 0.02 1 217 71 82 MET CE C 16.413 0.20 1 218 71 82 MET N N 120.051 0.20 1 219 72 83 SER H H 7.451 0.02 1 220 72 83 SER N N 115.745 0.20 1 221 73 84 ARG H H 8.634 0.02 1 222 73 84 ARG N N 121.209 0.20 1 223 74 85 ASN H H 8.347 0.02 1 224 74 85 ASN N N 114.087 0.20 1 225 75 86 PHE H H 7.738 0.02 1 226 75 86 PHE N N 121.314 0.20 1 227 76 87 ILE H H 8.218 0.02 1 228 76 87 ILE N N 119.891 0.20 1 229 77 88 ASP H H 7.666 0.02 1 230 77 88 ASP N N 116.921 0.20 1 231 78 89 ALA H H 7.513 0.02 1 232 78 89 ALA HB H 1.457 0.02 1 233 78 89 ALA CB C 18.752 0.20 1 234 78 89 ALA N N 120.884 0.20 1 235 79 90 ILE H H 8.030 0.02 1 236 79 90 ILE HD1 H 0.325 0.02 1 237 79 90 ILE CD1 C 13.436 0.20 1 238 79 90 ILE N N 113.413 0.20 1 239 80 91 ILE H H 7.892 0.02 1 240 80 91 ILE HD1 H 0.777 0.02 1 241 80 91 ILE CD1 C 13.166 0.20 1 242 80 91 ILE N N 122.547 0.20 1 243 81 92 LYS H H 7.821 0.02 1 244 81 92 LYS N N 121.440 0.20 1 245 82 93 GLU H H 8.011 0.02 1 246 82 93 GLU N N 114.760 0.20 1 247 83 94 LYS H H 7.737 0.02 1 248 83 94 LYS N N 117.012 0.20 1 249 84 95 ILE H H 7.948 0.02 1 250 84 95 ILE HD1 H 0.808 0.02 1 251 84 95 ILE CD1 C 13.491 0.20 1 252 84 95 ILE N N 119.229 0.20 1 253 85 96 ASN H H 8.653 0.02 1 254 85 96 ASN N N 124.286 0.20 1 255 87 98 ALA H H 9.209 0.02 1 256 87 98 ALA HB H 0.502 0.02 1 257 87 98 ALA CB C 18.741 0.20 1 258 87 98 ALA N N 125.524 0.20 1 259 88 99 GLY H H 7.554 0.02 1 260 88 99 GLY N N 107.014 0.20 1 261 89 100 ALA H H 8.411 0.02 1 262 89 100 ALA HB H 1.367 0.02 1 263 89 100 ALA CB C 18.461 0.20 1 264 89 100 ALA N N 124.058 0.20 1 265 91 102 THR H H 8.853 0.02 1 266 91 102 THR N N 117.682 0.20 1 267 92 103 TYR H H 9.054 0.02 1 268 92 103 TYR N N 126.639 0.20 1 269 93 104 VAL H H 9.523 0.02 1 270 93 104 VAL HG1 H 0.832 0.02 2 271 93 104 VAL HG2 H 0.729 0.02 2 272 93 104 VAL CG1 C 21.971 0.20 2 273 93 104 VAL CG2 C 19.213 0.20 2 274 93 104 VAL N N 124.611 0.20 1 275 95 106 GLY H H 6.857 0.02 1 276 95 106 GLY N N 109.037 0.20 1 277 96 107 GLU H H 8.389 0.02 1 278 96 107 GLU N N 119.656 0.20 1 279 97 108 TYR H H 8.911 0.02 1 280 97 108 TYR N N 126.986 0.20 1 281 98 109 LYS H H 8.380 0.02 1 282 98 109 LYS N N 131.055 0.20 1 283 99 110 LEU H H 7.947 0.02 1 284 99 110 LEU HD1 H 0.923 0.02 2 285 99 110 LEU HD2 H 0.849 0.02 2 286 99 110 LEU CD1 C 24.344 0.20 2 287 99 110 LEU CD2 C 24.891 0.20 2 288 99 110 LEU N N 124.566 0.20 1 289 100 111 GLY H H 8.274 0.02 1 290 100 111 GLY N N 113.138 0.20 1 291 101 112 GLU H H 7.884 0.02 1 292 101 112 GLU N N 119.234 0.20 1 293 102 113 ASP H H 8.627 0.02 1 294 102 113 ASP N N 121.919 0.20 1 295 103 114 PHE H H 8.923 0.02 1 296 103 114 PHE N N 123.333 0.20 1 297 104 115 THR H H 8.414 0.02 1 298 104 115 THR N N 126.257 0.20 1 299 105 116 TYR H H 8.945 0.02 1 300 105 116 TYR N N 122.193 0.20 1 301 106 117 SER H H 8.175 0.02 1 302 106 117 SER N N 112.325 0.20 1 303 107 118 VAL H H 9.037 0.02 1 304 107 118 VAL HG1 H 0.625 0.02 2 305 107 118 VAL HG2 H -0.553 0.02 2 306 107 118 VAL CG1 C 22.513 0.20 2 307 107 118 VAL CG2 C 21.989 0.20 2 308 107 118 VAL N N 121.772 0.20 1 309 108 119 GLU H H 8.971 0.02 1 310 108 119 GLU N N 125.633 0.20 1 311 109 120 PHE H H 7.865 0.02 1 312 109 120 PHE N N 117.269 0.20 1 313 110 121 GLU H H 8.612 0.02 1 314 110 121 GLU N N 118.490 0.20 1 315 111 122 VAL H H 8.113 0.02 1 316 111 122 VAL HG1 H 0.962 0.02 2 317 111 122 VAL HG2 H 0.866 0.02 2 318 111 122 VAL CG1 C 23.529 0.20 2 319 111 122 VAL CG2 C 17.936 0.20 2 320 111 122 VAL N N 113.925 0.20 1 321 112 123 TYR H H 8.124 0.02 1 322 112 123 TYR N N 118.544 0.20 1 323 114 125 GLU H H 8.361 0.02 1 324 114 125 GLU N N 121.276 0.20 1 325 115 126 VAL H H 8.288 0.02 1 326 115 126 VAL HG1 H 0.778 0.02 2 327 115 126 VAL HG2 H 0.843 0.02 2 328 115 126 VAL CG1 C 21.020 0.20 2 329 115 126 VAL CG2 C 20.870 0.20 2 330 115 126 VAL N N 123.600 0.20 1 331 116 127 GLU H H 8.321 0.02 1 332 116 127 GLU N N 126.838 0.20 1 333 117 128 LEU H H 8.599 0.02 1 334 117 128 LEU HD1 H 0.852 0.02 2 335 117 128 LEU HD2 H 0.775 0.02 2 336 117 128 LEU CD1 C 25.991 0.20 2 337 117 128 LEU CD2 C 23.839 0.20 2 338 117 128 LEU N N 125.363 0.20 1 339 118 129 GLN H H 9.378 0.02 1 340 118 129 GLN N N 122.903 0.20 1 341 119 130 GLY H H 8.462 0.02 1 342 119 130 GLY N N 105.397 0.20 1 343 120 131 LEU H H 8.120 0.02 1 344 120 131 LEU HD1 H 0.844 0.02 2 345 120 131 LEU HD2 H 0.786 0.02 2 346 120 131 LEU CD1 C 25.302 0.20 2 347 120 131 LEU CD2 C 23.954 0.20 2 348 120 131 LEU N N 121.598 0.20 1 349 121 132 GLU H H 8.642 0.02 1 350 121 132 GLU N N 113.497 0.20 1 351 122 133 ALA H H 7.264 0.02 1 352 122 133 ALA HB H 1.342 0.02 1 353 122 133 ALA CB C 19.071 0.20 1 354 122 133 ALA N N 120.333 0.20 1 355 123 134 ILE H H 7.080 0.02 1 356 123 134 ILE HD1 H 0.808 0.02 1 357 123 134 ILE CD1 C 13.841 0.20 1 358 123 134 ILE N N 122.862 0.20 1 359 124 135 GLU H H 8.268 0.02 1 360 124 135 GLU N N 127.435 0.20 1 361 125 136 VAL H H 8.406 0.02 1 362 125 136 VAL HG1 H 0.913 0.02 2 363 125 136 VAL HG2 H 0.911 0.02 2 364 125 136 VAL CG1 C 21.068 0.20 2 365 125 136 VAL CG2 C 20.331 0.20 2 366 125 136 VAL N N 123.447 0.20 1 367 126 137 GLU H H 9.109 0.02 1 368 126 137 GLU N N 128.145 0.20 1 369 127 138 LYS H H 9.222 0.02 1 370 127 138 LYS N N 131.418 0.20 1 371 129 140 ILE H H 8.074 0.02 1 372 129 140 ILE HD1 H 0.662 0.02 1 373 129 140 ILE CD1 C 10.838 0.20 1 374 129 140 ILE N N 125.127 0.20 1 375 130 141 VAL H H 8.035 0.02 1 376 130 141 VAL HG1 H 0.812 0.02 2 377 130 141 VAL HG2 H 0.801 0.02 2 378 130 141 VAL CG1 C 20.387 0.20 2 379 130 141 VAL CG2 C 21.581 0.20 2 380 130 141 VAL N N 126.200 0.20 1 381 131 142 GLU H H 8.527 0.02 1 382 131 142 GLU N N 125.767 0.20 1 383 132 143 VAL H H 8.638 0.02 1 384 132 143 VAL HG1 H 0.899 0.02 2 385 132 143 VAL HG2 H 0.840 0.02 2 386 132 143 VAL CG1 C 24.877 0.20 2 387 132 143 VAL CG2 C 23.252 0.20 2 388 132 143 VAL N N 122.041 0.20 1 389 133 144 THR H H 9.654 0.02 1 390 133 144 THR N N 123.411 0.20 1 391 134 145 ASP H H 8.791 0.02 1 392 134 145 ASP N N 121.107 0.20 1 393 135 146 ALA H H 8.032 0.02 1 394 135 146 ALA HB H 1.386 0.02 1 395 135 146 ALA CB C 17.808 0.20 1 396 135 146 ALA N N 121.613 0.20 1 397 136 147 ASP H H 7.844 0.02 1 398 136 147 ASP N N 121.656 0.20 1 399 137 148 VAL H H 7.600 0.02 1 400 137 148 VAL HG2 H 0.767 0.02 2 401 137 148 VAL CG2 C 22.596 0.20 2 402 137 148 VAL N N 123.143 0.20 1 403 138 149 ASP H H 8.630 0.02 1 404 138 149 ASP N N 120.658 0.20 1 405 139 150 GLY H H 8.122 0.02 1 406 139 150 GLY N N 107.803 0.20 1 407 141 152 LEU H H 8.510 0.02 1 408 141 152 LEU HD1 H 0.840 0.02 2 409 141 152 LEU HD2 H 0.772 0.02 2 410 141 152 LEU CD1 C 25.401 0.20 2 411 141 152 LEU CD2 C 24.046 0.20 2 412 141 152 LEU N N 121.553 0.20 1 413 142 153 ASP H H 7.930 0.02 1 414 142 153 ASP N N 119.398 0.20 1 415 143 154 THR H H 7.966 0.02 1 416 143 154 THR N N 118.184 0.20 1 417 144 155 LEU H H 8.280 0.02 1 418 144 155 LEU HD1 H 1.004 0.02 2 419 144 155 LEU HD2 H 0.758 0.02 2 420 144 155 LEU CD1 C 26.437 0.20 2 421 144 155 LEU CD2 C 22.456 0.20 2 422 144 155 LEU N N 122.453 0.20 1 423 145 156 ARG H H 8.207 0.02 1 424 145 156 ARG N N 119.426 0.20 1 425 146 157 LYS H H 7.851 0.02 1 426 146 157 LYS N N 119.318 0.20 1 427 147 158 GLN H H 7.836 0.02 1 428 147 158 GLN N N 118.688 0.20 1 429 148 159 GLN H H 7.744 0.02 1 430 148 159 GLN N N 118.632 0.20 1 431 149 160 ALA H H 7.992 0.02 1 432 149 160 ALA HB H 1.408 0.02 1 433 149 160 ALA CB C 18.744 0.20 1 434 149 160 ALA N N 123.979 0.20 1 435 150 161 THR H H 8.174 0.02 1 436 150 161 THR HA H 4.426 0.02 1 437 150 161 THR HB H 4.132 0.02 1 438 150 161 THR HG2 H 1.116 0.02 1 439 150 161 THR CA C 61.563 0.20 1 440 150 161 THR CB C 70.337 0.20 1 441 150 161 THR CG2 C 21.984 0.20 1 442 150 161 THR N N 115.091 0.20 1 443 151 162 TRP H H 8.430 0.02 1 444 151 162 TRP HA H 5.038 0.02 1 445 151 162 TRP HB2 H 2.886 0.02 2 446 151 162 TRP HB3 H 2.731 0.02 2 447 151 162 TRP HD1 H 7.058 0.02 1 448 151 162 TRP HE1 H 9.891 0.02 1 449 151 162 TRP HE3 H 7.194 0.02 1 450 151 162 TRP HZ2 H 7.366 0.02 1 451 151 162 TRP HH2 H 7.179 0.02 1 452 151 162 TRP CA C 56.277 0.20 1 453 151 162 TRP CB C 32.513 0.20 1 454 151 162 TRP CD1 C 127.468 0.20 1 455 151 162 TRP CE3 C 124.200 0.20 1 456 151 162 TRP CZ2 C 113.835 0.20 1 457 151 162 TRP CH2 C 123.284 0.20 1 458 151 162 TRP N N 123.279 0.20 1 459 151 162 TRP NE1 N 128.918 0.20 1 460 152 163 LYS HD2 H 1.680 0.02 1 461 152 163 LYS HD3 H 1.680 0.02 1 462 152 163 LYS H H 9.563 0.02 1 463 152 163 LYS HA H 4.942 0.02 1 464 152 163 LYS HB2 H 1.837 0.02 2 465 152 163 LYS HG2 H 1.394 0.02 1 466 152 163 LYS HG3 H 1.394 0.02 1 467 152 163 LYS HE2 H 2.938 0.02 1 468 152 163 LYS HE3 H 2.938 0.02 1 469 152 163 LYS CA C 54.221 0.20 1 470 152 163 LYS CB C 35.893 0.20 1 471 152 163 LYS CG C 23.804 0.20 1 472 152 163 LYS CD C 29.422 0.20 1 473 152 163 LYS CE C 42.111 0.20 1 474 152 163 LYS N N 121.584 0.20 1 475 153 164 GLU H H 8.902 0.02 1 476 153 164 GLU HB2 H 1.826 0.02 1 477 153 164 GLU HB3 H 1.826 0.02 1 478 153 164 GLU HG2 H 2.437 0.02 2 479 153 164 GLU HG3 H 2.250 0.02 2 480 153 164 GLU CB C 30.207 0.20 1 481 153 164 GLU CG C 37.209 0.20 1 482 153 164 GLU N N 124.044 0.20 1 483 154 165 LYS H H 8.844 0.02 1 484 154 165 LYS HA H 4.700 0.02 1 485 154 165 LYS HB2 H 1.697 0.02 1 486 154 165 LYS HB3 H 1.697 0.02 1 487 154 165 LYS HD2 H 1.765 0.02 2 488 154 165 LYS HD3 H 1.447 0.02 2 489 154 165 LYS HE2 H 2.861 0.02 2 490 154 165 LYS HE3 H 2.531 0.02 2 491 154 165 LYS CA C 54.553 0.20 1 492 154 165 LYS CB C 36.184 0.20 1 493 154 165 LYS CD C 29.860 0.20 1 494 154 165 LYS CE C 42.165 0.20 1 495 154 165 LYS N N 123.890 0.20 1 496 155 166 ASP H H 8.735 0.02 1 497 155 166 ASP HA H 4.876 0.02 1 498 155 166 ASP HB2 H 2.716 0.02 2 499 155 166 ASP HB3 H 2.666 0.02 2 500 155 166 ASP CA C 53.307 0.20 1 501 155 166 ASP CB C 40.585 0.20 1 502 155 166 ASP N N 123.701 0.20 1 503 156 167 GLY H H 7.288 0.02 1 504 156 167 GLY HA2 H 4.176 0.02 2 505 156 167 GLY HA3 H 3.888 0.02 2 506 156 167 GLY CA C 44.028 0.20 1 507 156 167 GLY N N 106.428 0.20 1 508 157 168 ALA H H 8.255 0.02 1 509 157 168 ALA HA H 4.181 0.02 1 510 157 168 ALA HB H 1.095 0.02 1 511 157 168 ALA CA C 51.228 0.20 1 512 157 168 ALA CB C 20.178 0.20 1 513 157 168 ALA N N 119.804 0.20 1 514 158 169 VAL H H 8.762 0.02 1 515 158 169 VAL HA H 3.851 0.02 1 516 158 169 VAL HB H 2.090 0.02 1 517 158 169 VAL HG1 H 1.004 0.02 2 518 158 169 VAL HG2 H 1.199 0.02 2 519 158 169 VAL CA C 64.308 0.20 1 520 158 169 VAL CB C 32.875 0.20 1 521 158 169 VAL CG1 C 23.868 0.20 2 522 158 169 VAL CG2 C 25.860 0.20 2 523 158 169 VAL N N 119.306 0.20 1 524 159 170 GLU H H 9.645 0.02 1 525 159 170 GLU N N 132.141 0.20 1 526 160 171 ALA HA H 3.849 0.02 1 527 160 171 ALA HB H 1.471 0.02 1 528 160 171 ALA CA C 55.417 0.20 1 529 160 171 ALA CB C 19.997 0.20 1 530 161 172 GLU H H 8.129 0.02 1 531 161 172 GLU HA H 4.652 0.02 1 532 161 172 GLU HB2 H 1.958 0.02 1 533 161 172 GLU HB3 H 1.958 0.02 1 534 161 172 GLU HG2 H 2.195 0.02 1 535 161 172 GLU HG3 H 2.195 0.02 1 536 161 172 GLU CA C 55.964 0.20 1 537 161 172 GLU CB C 29.455 0.20 1 538 161 172 GLU CG C 37.193 0.20 1 539 161 172 GLU N N 111.916 0.20 1 540 162 173 ASP H H 7.279 0.02 1 541 162 173 ASP HA H 5.213 0.02 1 542 162 173 ASP CA C 55.272 0.20 1 543 162 173 ASP N N 122.877 0.20 1 544 163 174 ARG HD2 H 2.361 0.02 1 545 163 174 ARG HD3 H 2.361 0.02 1 546 163 174 ARG H H 8.884 0.02 1 547 163 174 ARG HA H 5.242 0.02 1 548 163 174 ARG HB2 H 1.027 0.02 2 549 163 174 ARG HB3 H 0.143 0.02 2 550 163 174 ARG HG2 H 0.732 0.02 1 551 163 174 ARG HG3 H 0.732 0.02 1 552 163 174 ARG CA C 54.707 0.20 1 553 163 174 ARG CB C 34.051 0.20 1 554 163 174 ARG CG C 25.979 0.20 1 555 163 174 ARG CD C 43.719 0.20 1 556 163 174 ARG N N 118.553 0.20 1 557 164 175 VAL H H 9.067 0.02 1 558 164 175 VAL HA H 5.366 0.02 1 559 164 175 VAL HB H 2.151 0.02 1 560 164 175 VAL HG1 H 1.108 0.02 2 561 164 175 VAL HG2 H 1.116 0.02 2 562 164 175 VAL CA C 58.104 0.20 1 563 164 175 VAL CB C 34.377 0.20 1 564 164 175 VAL CG1 C 19.590 0.20 2 565 164 175 VAL CG2 C 24.217 0.20 2 566 164 175 VAL N N 119.608 0.20 1 567 165 176 THR H H 8.470 0.02 1 568 165 176 THR HA H 5.219 0.02 1 569 165 176 THR HB H 3.866 0.02 1 570 165 176 THR HG2 H 0.900 0.02 1 571 165 176 THR CA C 61.962 0.20 1 572 165 176 THR CB C 69.257 0.20 1 573 165 176 THR CG2 C 19.783 0.20 1 574 165 176 THR N N 119.207 0.20 1 575 166 177 ILE H H 9.580 0.02 1 576 166 177 ILE HA H 5.738 0.02 1 577 166 177 ILE HB H 2.070 0.02 1 578 166 177 ILE HG2 H 0.995 0.02 1 579 166 177 ILE HD1 H 1.012 0.02 1 580 166 177 ILE CA C 58.446 0.20 1 581 166 177 ILE CB C 42.775 0.20 1 582 166 177 ILE CG2 C 19.202 0.20 1 583 166 177 ILE CD1 C 14.562 0.20 1 584 166 177 ILE N N 119.726 0.20 1 585 167 178 ASP H H 8.537 0.02 1 586 167 178 ASP HA H 5.340 0.02 1 587 167 178 ASP HB3 H 2.600 0.02 2 588 167 178 ASP CA C 52.577 0.20 1 589 167 178 ASP CB C 42.446 0.20 1 590 167 178 ASP N N 119.082 0.20 1 591 168 179 PHE H H 8.585 0.02 1 592 168 179 PHE HA H 6.089 0.02 1 593 168 179 PHE HB2 H 2.985 0.02 2 594 168 179 PHE HB3 H 2.943 0.02 2 595 168 179 PHE HD1 H 6.967 0.02 3 596 168 179 PHE HD2 H 6.950 0.02 3 597 168 179 PHE HE1 H 6.346 0.02 1 598 168 179 PHE HE2 H 6.346 0.02 1 599 168 179 PHE HZ H 6.626 0.02 1 600 168 179 PHE CA C 55.736 0.20 1 601 168 179 PHE CB C 43.785 0.20 1 602 168 179 PHE CD1 C 132.418 0.20 1 603 168 179 PHE CD2 C 132.418 0.20 1 604 168 179 PHE CE1 C 130.471 0.20 1 605 168 179 PHE CE2 C 130.471 0.20 1 606 168 179 PHE CZ C 130.449 0.20 1 607 168 179 PHE N N 114.697 0.20 1 608 169 180 THR H H 8.514 0.02 1 609 169 180 THR HA H 4.789 0.02 1 610 169 180 THR HB H 4.012 0.02 1 611 169 180 THR HG2 H 1.054 0.02 1 612 169 180 THR CA C 62.633 0.20 1 613 169 180 THR CB C 71.640 0.20 1 614 169 180 THR CG2 C 21.489 0.20 1 615 169 180 THR N N 114.778 0.20 1 616 170 181 GLY H H 9.368 0.02 1 617 170 181 GLY HA2 H 4.580 0.02 2 618 170 181 GLY HA3 H 2.543 0.02 2 619 170 181 GLY CA C 45.123 0.20 1 620 170 181 GLY N N 119.427 0.20 1 621 171 182 SER H H 9.047 0.02 1 622 171 182 SER HA H 5.034 0.02 1 623 171 182 SER HB2 H 3.517 0.02 2 624 171 182 SER HB3 H 3.275 0.02 2 625 171 182 SER CA C 57.502 0.20 1 626 171 182 SER CB C 66.208 0.20 1 627 171 182 SER N N 115.665 0.20 1 628 172 183 VAL H H 8.866 0.02 1 629 172 183 VAL HA H 4.456 0.02 1 630 172 183 VAL HB H 1.871 0.02 1 631 172 183 VAL HG1 H 0.791 0.02 2 632 172 183 VAL HG2 H 0.879 0.02 2 633 172 183 VAL CA C 61.498 0.20 1 634 172 183 VAL CB C 34.830 0.20 1 635 172 183 VAL CG1 C 21.442 0.20 2 636 172 183 VAL CG2 C 21.551 0.20 2 637 172 183 VAL N N 120.269 0.20 1 638 173 184 ASP H H 9.626 0.02 1 639 173 184 ASP HA H 4.292 0.02 1 640 173 184 ASP HB2 H 2.985 0.02 2 641 173 184 ASP HB3 H 2.700 0.02 2 642 173 184 ASP CA C 55.536 0.20 1 643 173 184 ASP CB C 39.603 0.20 1 644 173 184 ASP N N 129.180 0.20 1 645 174 185 GLY H H 8.660 0.02 1 646 174 185 GLY HA2 H 4.195 0.02 2 647 174 185 GLY HA3 H 3.571 0.02 2 648 174 185 GLY CA C 45.253 0.20 1 649 174 185 GLY N N 102.270 0.20 1 650 175 186 GLU H H 7.909 0.02 1 651 175 186 GLU HA H 4.696 0.02 1 652 175 186 GLU HB2 H 2.120 0.02 2 653 175 186 GLU HB3 H 1.965 0.02 2 654 175 186 GLU CA C 54.780 0.20 1 655 175 186 GLU CB C 32.028 0.20 1 656 175 186 GLU N N 120.489 0.20 1 657 176 187 GLU H H 8.861 0.02 1 658 176 187 GLU HA H 4.458 0.02 1 659 176 187 GLU HG2 H 2.262 0.02 1 660 176 187 GLU HG3 H 2.262 0.02 1 661 176 187 GLU CA C 56.876 0.20 1 662 176 187 GLU CG C 36.541 0.20 1 663 176 187 GLU N N 125.338 0.20 1 664 177 188 PHE HD1 H 7.105 0.02 1 665 177 188 PHE HD2 H 7.105 0.02 1 666 177 188 PHE H H 7.139 0.02 1 667 177 188 PHE HA H 5.085 0.02 1 668 177 188 PHE HB2 H 3.123 0.02 2 669 177 188 PHE HB3 H 2.982 0.02 2 670 177 188 PHE HE1 H 7.006 0.02 1 671 177 188 PHE HE2 H 7.006 0.02 1 672 177 188 PHE HZ H 7.149 0.02 1 673 177 188 PHE CA C 54.147 0.20 1 674 177 188 PHE CB C 41.300 0.20 1 675 177 188 PHE CD1 C 133.648 0.20 1 676 177 188 PHE CD2 C 133.648 0.20 1 677 177 188 PHE CE1 C 130.480 0.20 1 678 177 188 PHE CE2 C 130.480 0.20 1 679 177 188 PHE CZ C 128.650 0.20 1 680 177 188 PHE N N 117.023 0.20 1 681 178 189 GLU H H 9.052 0.02 1 682 178 189 GLU HA H 4.175 0.02 1 683 178 189 GLU HG2 H 2.355 0.02 1 684 178 189 GLU HG3 H 2.355 0.02 1 685 178 189 GLU CA C 57.933 0.20 1 686 178 189 GLU CG C 36.067 0.20 1 687 178 189 GLU N N 124.724 0.20 1 688 179 190 GLY H H 9.017 0.02 1 689 179 190 GLY HA2 H 4.419 0.02 2 690 179 190 GLY HA3 H 3.986 0.02 2 691 179 190 GLY CA C 45.675 0.20 1 692 179 190 GLY N N 113.761 0.20 1 693 180 191 GLY H H 7.877 0.02 1 694 180 191 GLY HA2 H 4.217 0.02 2 695 180 191 GLY HA3 H 2.875 0.02 2 696 180 191 GLY CA C 46.354 0.20 1 697 180 191 GLY N N 106.863 0.20 1 698 181 192 LYS HD2 H 1.590 0.02 1 699 181 192 LYS HD3 H 1.590 0.02 1 700 181 192 LYS H H 7.540 0.02 1 701 181 192 LYS HA H 5.314 0.02 1 702 181 192 LYS HG2 H 1.524 0.02 2 703 181 192 LYS HG3 H 1.212 0.02 2 704 181 192 LYS CA C 54.297 0.20 1 705 181 192 LYS CG C 24.677 0.20 1 706 181 192 LYS CD C 29.519 0.20 1 707 181 192 LYS N N 119.060 0.20 1 708 182 193 ALA H H 8.096 0.02 1 709 182 193 ALA HA H 4.300 0.02 1 710 182 193 ALA HB H 0.608 0.02 1 711 182 193 ALA CA C 51.721 0.20 1 712 182 193 ALA CB C 23.150 0.20 1 713 182 193 ALA N N 125.253 0.20 1 714 183 194 SER H H 8.419 0.02 1 715 183 194 SER HA H 5.090 0.02 1 716 183 194 SER HB2 H 3.645 0.02 2 717 183 194 SER HB3 H 3.516 0.02 2 718 183 194 SER CA C 56.382 0.20 1 719 183 194 SER CB C 65.393 0.20 1 720 183 194 SER N N 115.543 0.20 1 721 184 195 ASP H H 9.621 0.02 1 722 184 195 ASP HA H 3.766 0.02 1 723 184 195 ASP HB2 H 2.593 0.02 2 724 184 195 ASP HB3 H 2.533 0.02 2 725 184 195 ASP CA C 56.142 0.20 1 726 184 195 ASP CB C 39.526 0.20 1 727 184 195 ASP N N 123.358 0.20 1 728 185 196 PHE HD1 H 7.154 0.02 1 729 185 196 PHE HD2 H 7.154 0.02 1 730 185 196 PHE H H 9.174 0.02 1 731 185 196 PHE HA H 4.370 0.02 1 732 185 196 PHE HB2 H 3.295 0.02 2 733 185 196 PHE HB3 H 2.602 0.02 2 734 185 196 PHE HE1 H 7.306 0.02 3 735 185 196 PHE HZ H 7.260 0.02 1 736 185 196 PHE CA C 57.863 0.20 1 737 185 196 PHE CB C 40.167 0.20 1 738 185 196 PHE CD1 C 131.703 0.20 1 739 185 196 PHE CD2 C 131.703 0.20 1 740 185 196 PHE CE1 C 131.550 0.20 3 741 185 196 PHE CZ C 129.885 0.20 1 742 185 196 PHE N N 121.553 0.20 1 743 186 197 VAL H H 7.926 0.02 1 744 186 197 VAL HA H 4.466 0.02 1 745 186 197 VAL HB H 1.634 0.02 1 746 186 197 VAL HG1 H 0.407 0.02 2 747 186 197 VAL HG2 H 0.789 0.02 2 748 186 197 VAL CA C 62.177 0.20 1 749 186 197 VAL CB C 31.369 0.20 1 750 186 197 VAL CG1 C 20.660 0.20 2 751 186 197 VAL CG2 C 20.945 0.20 2 752 186 197 VAL N N 129.442 0.20 1 753 187 198 LEU H H 9.345 0.02 1 754 187 198 LEU HA H 4.394 0.02 1 755 187 198 LEU HB2 H 1.933 0.02 2 756 187 198 LEU HB3 H 1.201 0.02 2 757 187 198 LEU HG H 1.304 0.02 1 758 187 198 LEU HD1 H 0.915 0.02 2 759 187 198 LEU HD2 H 0.965 0.02 2 760 187 198 LEU CA C 52.932 0.20 1 761 187 198 LEU CB C 44.649 0.20 1 762 187 198 LEU CG C 27.653 0.20 1 763 187 198 LEU CD1 C 25.908 0.20 2 764 187 198 LEU CD2 C 22.955 0.20 2 765 187 198 LEU N N 131.275 0.20 1 766 188 199 ALA H H 8.648 0.02 1 767 188 199 ALA HA H 4.260 0.02 1 768 188 199 ALA HB H 1.244 0.02 1 769 188 199 ALA CA C 51.846 0.20 1 770 188 199 ALA CB C 16.812 0.20 1 771 188 199 ALA N N 132.524 0.20 1 772 189 200 MET H H 8.607 0.02 1 773 189 200 MET HA H 4.171 0.02 1 774 189 200 MET HG2 H 2.611 0.02 2 775 189 200 MET HG3 H 2.238 0.02 2 776 189 200 MET HE H 1.978 0.02 1 777 189 200 MET CA C 56.785 0.20 1 778 189 200 MET CG C 32.430 0.20 1 779 189 200 MET CE C 16.961 0.20 1 780 189 200 MET N N 125.180 0.20 1 781 190 201 GLY H H 10.223 0.02 1 782 190 201 GLY HA2 H 4.255 0.02 2 783 190 201 GLY HA3 H 3.901 0.02 2 784 190 201 GLY CA C 46.382 0.20 1 785 190 201 GLY N N 109.534 0.20 1 786 191 202 GLN H H 9.089 0.02 1 787 191 202 GLN HA H 4.607 0.02 1 788 191 202 GLN HG2 H 2.270 0.02 2 789 191 202 GLN HG3 H 2.206 0.02 2 790 191 202 GLN CA C 54.097 0.20 1 791 191 202 GLN CG C 33.318 0.20 1 792 191 202 GLN N N 118.762 0.20 1 793 192 203 GLY H H 9.158 0.02 1 794 192 203 GLY HA2 H 4.018 0.02 1 795 192 203 GLY HA3 H 4.018 0.02 1 796 192 203 GLY CA C 46.341 0.20 1 797 192 203 GLY N N 110.921 0.20 1 798 193 204 ARG H H 8.308 0.02 1 799 193 204 ARG N N 117.360 0.20 1 800 194 205 MET H H 8.087 0.02 1 801 194 205 MET HB2 H 2.403 0.02 1 802 194 205 MET HB3 H 2.403 0.02 1 803 194 205 MET HG2 H 1.997 0.02 1 804 194 205 MET HG3 H 1.997 0.02 1 805 194 205 MET HE H 0.569 0.02 1 806 194 205 MET CB C 37.068 0.20 1 807 194 205 MET CG C 33.560 0.20 1 808 194 205 MET CE C 15.974 0.20 1 809 194 205 MET N N 115.009 0.20 1 810 195 206 ILE H H 7.639 0.02 1 811 195 206 ILE HB H 1.839 0.02 1 812 195 206 ILE HG12 H 1.235 0.02 1 813 195 206 ILE HG13 H 1.235 0.02 1 814 195 206 ILE HG2 H 0.914 0.02 1 815 195 206 ILE HD1 H 0.234 0.02 1 816 195 206 ILE CB C 36.941 0.20 1 817 195 206 ILE CG1 C 25.298 0.20 1 818 195 206 ILE CG2 C 18.513 0.20 1 819 195 206 ILE CD1 C 13.787 0.20 1 820 195 206 ILE N N 115.145 0.20 1 821 197 208 GLY H H 8.500 0.02 1 822 197 208 GLY HA2 H 4.385 0.02 2 823 197 208 GLY HA3 H 3.731 0.02 2 824 197 208 GLY CA C 45.721 0.20 1 825 197 208 GLY N N 111.261 0.20 1 826 198 209 PHE HD1 H 6.214 0.02 1 827 198 209 PHE HD2 H 6.214 0.02 1 828 198 209 PHE H H 7.788 0.02 1 829 198 209 PHE HB2 H 3.090 0.02 2 830 198 209 PHE HB3 H 2.469 0.02 2 831 198 209 PHE HE1 H 5.758 0.02 3 832 198 209 PHE HE2 H 5.735 0.02 3 833 198 209 PHE HZ H 5.744 0.02 1 834 198 209 PHE CB C 40.805 0.20 1 835 198 209 PHE CD1 C 130.640 0.20 1 836 198 209 PHE CD2 C 130.640 0.20 1 837 198 209 PHE CE1 C 130.566 0.20 1 838 198 209 PHE CE2 C 130.566 0.20 1 839 198 209 PHE CZ C 128.573 0.20 1 840 198 209 PHE N N 122.915 0.20 1 841 200 211 ASP HA H 4.194 0.02 1 842 200 211 ASP HB2 H 2.637 0.02 2 843 200 211 ASP HB3 H 2.499 0.02 2 844 200 211 ASP CA C 57.168 0.20 1 845 200 211 ASP CB C 40.276 0.20 1 846 201 212 GLY H H 7.406 0.02 1 847 201 212 GLY HA2 H 4.120 0.02 2 848 201 212 GLY HA3 H 3.589 0.02 2 849 201 212 GLY CA C 46.091 0.20 1 850 201 212 GLY N N 103.210 0.20 1 851 202 213 ILE H H 7.345 0.02 1 852 202 213 ILE HA H 3.854 0.02 1 853 202 213 ILE HB H 1.941 0.02 1 854 202 213 ILE HG12 H 0.919 0.02 1 855 202 213 ILE HG13 H 0.919 0.02 1 856 202 213 ILE HG2 H 1.151 0.02 1 857 202 213 ILE HD1 H 0.773 0.02 1 858 202 213 ILE CA C 63.145 0.20 1 859 202 213 ILE CB C 38.754 0.20 1 860 202 213 ILE CG1 C 29.081 0.20 1 861 202 213 ILE CG2 C 18.870 0.20 1 862 202 213 ILE CD1 C 14.077 0.20 1 863 202 213 ILE N N 118.982 0.20 1 864 203 214 LYS HD2 H 1.747 0.02 1 865 203 214 LYS HD3 H 1.747 0.02 1 866 203 214 LYS H H 7.029 0.02 1 867 203 214 LYS HA H 3.549 0.02 1 868 203 214 LYS HB2 H 1.704 0.02 1 869 203 214 LYS HB3 H 1.704 0.02 1 870 203 214 LYS HG2 H 1.596 0.02 2 871 203 214 LYS HG3 H 1.093 0.02 2 872 203 214 LYS HE2 H 2.894 0.02 1 873 203 214 LYS HE3 H 2.894 0.02 1 874 203 214 LYS CA C 58.588 0.20 1 875 203 214 LYS CB C 32.441 0.20 1 876 203 214 LYS CG C 25.986 0.20 1 877 203 214 LYS CD C 29.601 0.20 1 878 203 214 LYS CE C 42.095 0.20 1 879 203 214 LYS N N 117.503 0.20 1 880 204 215 GLY H H 8.912 0.02 1 881 204 215 GLY HA2 H 4.167 0.02 2 882 204 215 GLY HA3 H 3.471 0.02 2 883 204 215 GLY CA C 45.123 0.20 1 884 204 215 GLY N N 109.228 0.20 1 885 205 216 HIS H H 7.514 0.02 1 886 205 216 HIS HB2 H 2.861 0.02 1 887 205 216 HIS HB3 H 2.861 0.02 1 888 205 216 HIS HD2 H 6.599 0.02 1 889 205 216 HIS CB C 30.247 0.20 1 890 205 216 HIS CD2 C 120.697 0.20 1 891 205 216 HIS N N 117.831 0.20 1 892 206 217 LYS HD2 H 1.671 0.02 1 893 206 217 LYS HD3 H 1.671 0.02 1 894 206 217 LYS H H 8.611 0.02 1 895 206 217 LYS HA H 4.668 0.02 1 896 206 217 LYS HB2 H 1.761 0.02 2 897 206 217 LYS HB3 H 1.623 0.02 2 898 206 217 LYS HG2 H 1.320 0.02 2 899 206 217 LYS HG3 H 1.123 0.02 2 900 206 217 LYS HE2 H 2.929 0.02 1 901 206 217 LYS HE3 H 2.929 0.02 1 902 206 217 LYS CA C 54.699 0.20 1 903 206 217 LYS CB C 36.271 0.20 1 904 206 217 LYS CG C 24.799 0.20 1 905 206 217 LYS CD C 29.327 0.20 1 906 206 217 LYS CE C 42.212 0.20 1 907 206 217 LYS N N 118.051 0.20 1 908 207 218 ALA H H 8.772 0.02 1 909 207 218 ALA HB H 1.376 0.02 1 910 207 218 ALA CB C 18.009 0.20 1 911 207 218 ALA N N 121.092 0.20 1 912 208 219 GLY H H 9.199 0.02 1 913 208 219 GLY HA2 H 4.451 0.02 2 914 208 219 GLY HA3 H 3.811 0.02 2 915 208 219 GLY CA C 44.747 0.20 1 916 208 219 GLY N N 110.704 0.20 1 917 209 220 GLU H H 7.927 0.02 1 918 209 220 GLU HA H 4.598 0.02 1 919 209 220 GLU HB2 H 2.539 0.02 2 920 209 220 GLU HB3 H 2.292 0.02 2 921 209 220 GLU HG2 H 2.589 0.02 2 922 209 220 GLU HG3 H 2.352 0.02 2 923 209 220 GLU CA C 57.159 0.20 1 924 209 220 GLU CB C 32.679 0.20 1 925 209 220 GLU CG C 38.226 0.20 1 926 209 220 GLU N N 119.828 0.20 1 927 210 221 GLU H H 8.299 0.02 1 928 210 221 GLU HA H 5.364 0.02 1 929 210 221 GLU HG2 H 2.182 0.02 2 930 210 221 GLU HG3 H 2.104 0.02 2 931 210 221 GLU CA C 54.694 0.20 1 932 210 221 GLU CG C 36.784 0.20 1 933 210 221 GLU N N 119.706 0.20 1 934 211 222 PHE HD1 H 6.523 0.02 1 935 211 222 PHE HD2 H 6.523 0.02 1 936 211 222 PHE H H 8.265 0.02 1 937 211 222 PHE HA H 4.982 0.02 1 938 211 222 PHE HB2 H 3.168 0.02 2 939 211 222 PHE HB3 H 2.930 0.02 2 940 211 222 PHE HE1 H 6.804 0.02 1 941 211 222 PHE HE2 H 6.804 0.02 1 942 211 222 PHE HZ H 6.752 0.02 1 943 211 222 PHE CA C 55.687 0.20 1 944 211 222 PHE CB C 38.983 0.20 1 945 211 222 PHE CD1 C 132.439 0.20 1 946 211 222 PHE CD2 C 132.439 0.20 1 947 211 222 PHE CE1 C 130.124 0.20 1 948 211 222 PHE CE2 C 130.124 0.20 1 949 211 222 PHE CZ C 127.473 0.20 1 950 211 222 PHE N N 120.145 0.20 1 951 212 223 THR H H 8.752 0.02 1 952 212 223 THR HA H 5.478 0.02 1 953 212 223 THR HB H 3.921 0.02 1 954 212 223 THR HG2 H 1.084 0.02 1 955 212 223 THR CA C 60.788 0.20 1 956 212 223 THR CB C 71.011 0.20 1 957 212 223 THR CG2 C 21.987 0.20 1 958 212 223 THR N N 115.311 0.20 1 959 213 224 ILE H H 8.974 0.02 1 960 213 224 ILE HA H 4.831 0.02 1 961 213 224 ILE HB H 1.862 0.02 1 962 213 224 ILE HG12 H 1.317 0.02 1 963 213 224 ILE HG13 H 1.317 0.02 1 964 213 224 ILE HG2 H 0.847 0.02 1 965 213 224 ILE HD1 H 0.179 0.02 1 966 213 224 ILE CA C 59.406 0.20 1 967 213 224 ILE CB C 41.195 0.20 1 968 213 224 ILE CG1 C 26.318 0.20 1 969 213 224 ILE CG2 C 18.272 0.20 1 970 213 224 ILE CD1 C 14.516 0.20 1 971 213 224 ILE N N 119.752 0.20 1 972 214 225 ASP H H 8.497 0.02 1 973 214 225 ASP HA H 5.414 0.02 1 974 214 225 ASP HB2 H 2.608 0.02 1 975 214 225 ASP HB3 H 2.608 0.02 1 976 214 225 ASP CA C 53.820 0.20 1 977 214 225 ASP CB C 42.990 0.20 1 978 214 225 ASP N N 122.985 0.20 1 979 215 226 VAL H H 8.598 0.02 1 980 215 226 VAL HA H 4.515 0.02 1 981 215 226 VAL HB H 1.870 0.02 1 982 215 226 VAL HG1 H 0.594 0.02 2 983 215 226 VAL HG2 H 0.623 0.02 2 984 215 226 VAL CA C 59.752 0.20 1 985 215 226 VAL CB C 36.360 0.20 1 986 215 226 VAL CG1 C 21.737 0.20 2 987 215 226 VAL CG2 C 20.701 0.20 2 988 215 226 VAL N N 118.422 0.20 1 989 216 227 THR H H 8.627 0.02 1 990 216 227 THR HA H 4.948 0.02 1 991 216 227 THR HB H 3.781 0.02 1 992 216 227 THR HG2 H 0.997 0.02 1 993 216 227 THR CA C 61.183 0.20 1 994 216 227 THR CB C 70.155 0.20 1 995 216 227 THR CG2 C 21.337 0.20 1 996 216 227 THR N N 120.119 0.20 1 997 217 228 PHE HD1 H 6.466 0.02 1 998 217 228 PHE HD2 H 6.466 0.02 1 999 217 228 PHE H H 8.953 0.02 1 1000 217 228 PHE HA H 4.064 0.02 1 1001 217 228 PHE HB2 H 3.245 0.02 2 1002 217 228 PHE HB3 H 2.239 0.02 2 1003 217 228 PHE HE1 H 6.854 0.02 1 1004 217 228 PHE HE2 H 6.854 0.02 1 1005 217 228 PHE HZ H 7.048 0.02 1 1006 217 228 PHE CA C 58.135 0.20 1 1007 217 228 PHE CB C 39.567 0.20 1 1008 217 228 PHE CD1 C 131.216 0.20 1 1009 217 228 PHE CD2 C 131.216 0.20 1 1010 217 228 PHE CE1 C 131.148 0.20 1 1011 217 228 PHE CE2 C 131.148 0.20 1 1012 217 228 PHE CZ C 128.781 0.20 1 1013 217 228 PHE N N 127.504 0.20 1 1014 218 229 PRO HA H 4.499 0.02 1 1015 218 229 PRO HB2 H 2.605 0.02 2 1016 218 229 PRO HB3 H 2.102 0.02 2 1017 218 229 PRO HG2 H 2.277 0.02 2 1018 218 229 PRO HG3 H 2.174 0.02 2 1019 218 229 PRO HD2 H 3.953 0.02 2 1020 218 229 PRO HD3 H 3.369 0.02 2 1021 218 229 PRO CA C 62.614 0.20 1 1022 218 229 PRO CB C 32.684 0.20 1 1023 218 229 PRO CG C 27.738 0.20 1 1024 218 229 PRO CD C 50.604 0.20 1 1025 219 230 GLU H H 8.981 0.02 1 1026 219 230 GLU HA H 3.866 0.02 1 1027 219 230 GLU HG2 H 2.402 0.02 2 1028 219 230 GLU HG3 H 2.335 0.02 2 1029 219 230 GLU CA C 59.388 0.20 1 1030 219 230 GLU CG C 36.433 0.20 1 1031 219 230 GLU N N 123.400 0.20 1 1032 220 231 GLU H H 8.264 0.02 1 1033 220 231 GLU HA H 4.487 0.02 1 1034 220 231 GLU HB2 H 2.179 0.02 2 1035 220 231 GLU HB3 H 1.930 0.02 2 1036 220 231 GLU HG2 H 2.240 0.02 1 1037 220 231 GLU HG3 H 2.240 0.02 1 1038 220 231 GLU CA C 54.922 0.20 1 1039 220 231 GLU CB C 28.517 0.20 1 1040 220 231 GLU CG C 36.125 0.20 1 1041 220 231 GLU N N 114.616 0.20 1 1042 221 232 TYR HD1 H 7.106 0.02 1 1043 221 232 TYR HD2 H 7.106 0.02 1 1044 221 232 TYR H H 7.434 0.02 1 1045 221 232 TYR HA H 4.428 0.02 1 1046 221 232 TYR HB2 H 3.398 0.02 2 1047 221 232 TYR HB3 H 2.383 0.02 2 1048 221 232 TYR HE1 H 6.740 0.02 1 1049 221 232 TYR HE2 H 6.740 0.02 1 1050 221 232 TYR CA C 59.417 0.20 1 1051 221 232 TYR CB C 40.332 0.20 1 1052 221 232 TYR CD1 C 132.234 0.20 1 1053 221 232 TYR CD2 C 132.234 0.20 1 1054 221 232 TYR CE1 C 119.843 0.20 1 1055 221 232 TYR CE2 C 119.843 0.20 1 1056 221 232 TYR N N 121.989 0.20 1 1057 222 233 HIS H H 6.945 0.02 1 1058 222 233 HIS HA H 4.120 0.02 1 1059 222 233 HIS HB2 H 3.028 0.02 2 1060 222 233 HIS HB3 H 2.868 0.02 2 1061 222 233 HIS HD2 H 6.742 0.02 1 1062 222 233 HIS CA C 58.174 0.20 1 1063 222 233 HIS CB C 29.464 0.20 1 1064 222 233 HIS CD2 C 118.965 0.20 1 1065 222 233 HIS N N 120.655 0.20 1 1066 223 234 ALA H H 5.655 0.02 1 1067 223 234 ALA HA H 4.481 0.02 1 1068 223 234 ALA HB H 1.042 0.02 1 1069 223 234 ALA CA C 50.882 0.20 1 1070 223 234 ALA CB C 18.457 0.20 1 1071 223 234 ALA N N 122.538 0.20 1 1072 224 235 GLU H H 8.964 0.02 1 1073 224 235 GLU HA H 3.745 0.02 1 1074 224 235 GLU HB2 H 2.022 0.02 1 1075 224 235 GLU HB3 H 2.022 0.02 1 1076 224 235 GLU HG3 H 2.301 0.02 2 1077 224 235 GLU CA C 59.650 0.20 1 1078 224 235 GLU CB C 29.593 0.20 1 1079 224 235 GLU CG C 35.836 0.20 1 1080 224 235 GLU N N 126.929 0.20 1 1081 225 236 ASN H H 8.741 0.02 1 1082 225 236 ASN HA H 4.405 0.02 1 1083 225 236 ASN HB2 H 2.749 0.02 2 1084 225 236 ASN HB3 H 2.706 0.02 2 1085 225 236 ASN CA C 54.430 0.20 1 1086 225 236 ASN CB C 36.798 0.20 1 1087 225 236 ASN N N 112.685 0.20 1 1088 226 237 LEU H H 7.021 0.02 1 1089 226 237 LEU HA H 4.003 0.02 1 1090 226 237 LEU HD1 H 0.023 0.02 2 1091 226 237 LEU HD2 H -0.325 0.02 2 1092 226 237 LEU CA C 54.067 0.20 1 1093 226 237 LEU CD1 C 25.200 0.20 2 1094 226 237 LEU CD2 C 21.061 0.20 2 1095 226 237 LEU N N 117.277 0.20 1 1096 227 238 LYS H H 7.018 0.02 1 1097 227 238 LYS HA H 3.804 0.02 1 1098 227 238 LYS HB2 H 1.809 0.02 1 1099 227 238 LYS HB3 H 1.809 0.02 1 1100 227 238 LYS HG2 H 1.547 0.02 2 1101 227 238 LYS HG3 H 1.459 0.02 2 1102 227 238 LYS HE2 H 3.049 0.02 2 1103 227 238 LYS HE3 H 3.011 0.02 2 1104 227 238 LYS CA C 58.163 0.20 1 1105 227 238 LYS CB C 32.434 0.20 1 1106 227 238 LYS CG C 23.883 0.20 1 1107 227 238 LYS CE C 42.360 0.20 1 1108 227 238 LYS N N 117.380 0.20 1 1109 228 239 GLY H H 7.139 0.02 1 1110 228 239 GLY HA2 H 3.995 0.02 2 1111 228 239 GLY HA3 H 3.681 0.02 2 1112 228 239 GLY CA C 46.069 0.20 1 1113 228 239 GLY N N 111.088 0.20 1 1114 229 240 LYS H H 7.884 0.02 1 1115 229 240 LYS HA H 4.352 0.02 1 1116 229 240 LYS HB2 H 1.879 0.02 1 1117 229 240 LYS HB3 H 1.879 0.02 1 1118 229 240 LYS HG2 H 1.306 0.02 2 1119 229 240 LYS HG3 H 1.134 0.02 2 1120 229 240 LYS HD2 H 1.604 0.02 2 1121 229 240 LYS HD3 H 1.533 0.02 2 1122 229 240 LYS HE2 H 2.910 0.02 1 1123 229 240 LYS HE3 H 2.910 0.02 1 1124 229 240 LYS CA C 55.407 0.20 1 1125 229 240 LYS CB C 33.165 0.20 1 1126 229 240 LYS CG C 25.209 0.20 1 1127 229 240 LYS CD C 28.644 0.20 1 1128 229 240 LYS CE C 42.457 0.20 1 1129 229 240 LYS N N 119.325 0.20 1 1130 230 241 ALA H H 8.353 0.02 1 1131 230 241 ALA HB H 1.406 0.02 1 1132 230 241 ALA CB C 18.810 0.20 1 1133 230 241 ALA N N 123.792 0.20 1 1134 231 242 ALA H H 9.298 0.02 1 1135 231 242 ALA HA H 5.210 0.02 1 1136 231 242 ALA HB H 1.258 0.02 1 1137 231 242 ALA CA C 50.365 0.20 1 1138 231 242 ALA CB C 24.287 0.20 1 1139 231 242 ALA N N 126.588 0.20 1 1140 232 243 LYS H H 8.677 0.02 1 1141 232 243 LYS HA H 5.444 0.02 1 1142 232 243 LYS HB2 H 1.552 0.02 2 1143 232 243 LYS HB3 H 1.524 0.02 2 1144 232 243 LYS HG2 H 1.451 0.02 2 1145 232 243 LYS HG3 H 1.378 0.02 2 1146 232 243 LYS HE2 H 2.902 0.02 1 1147 232 243 LYS HE3 H 2.902 0.02 1 1148 232 243 LYS CA C 54.358 0.20 1 1149 232 243 LYS CB C 36.166 0.20 1 1150 232 243 LYS CG C 25.081 0.20 1 1151 232 243 LYS CE C 41.983 0.20 1 1152 232 243 LYS N N 120.189 0.20 1 1153 233 244 PHE HD1 H 6.980 0.02 1 1154 233 244 PHE HD2 H 6.980 0.02 1 1155 233 244 PHE H H 9.102 0.02 1 1156 233 244 PHE HA H 5.218 0.02 1 1157 233 244 PHE HB2 H 2.608 0.02 2 1158 233 244 PHE HB3 H 2.417 0.02 2 1159 233 244 PHE HE1 H 7.166 0.02 1 1160 233 244 PHE HE2 H 7.166 0.02 1 1161 233 244 PHE HZ H 7.395 0.02 1 1162 233 244 PHE CA C 56.809 0.20 1 1163 233 244 PHE CB C 42.213 0.20 1 1164 233 244 PHE CD1 C 131.542 0.20 1 1165 233 244 PHE CD2 C 131.542 0.20 1 1166 233 244 PHE CE1 C 131.420 0.20 1 1167 233 244 PHE CE2 C 131.420 0.20 1 1168 233 244 PHE CZ C 129.408 0.20 1 1169 233 244 PHE N N 118.854 0.20 1 1170 234 245 ALA H H 8.609 0.02 1 1171 234 245 ALA HA H 4.616 0.02 1 1172 234 245 ALA HB H 1.328 0.02 1 1173 234 245 ALA CA C 51.750 0.20 1 1174 234 245 ALA CB C 18.746 0.20 1 1175 234 245 ALA N N 127.743 0.20 1 1176 235 246 ILE H H 9.141 0.02 1 1177 235 246 ILE HB H 0.523 0.02 1 1178 235 246 ILE HG12 H 1.030 0.02 2 1179 235 246 ILE HG13 H 0.855 0.02 2 1180 235 246 ILE HG2 H 0.472 0.02 1 1181 235 246 ILE CB C 38.314 0.20 1 1182 235 246 ILE CG1 C 27.344 0.20 1 1183 235 246 ILE CG2 C 17.866 0.20 1 1184 235 246 ILE N N 126.182 0.20 1 1185 236 247 ASN H H 8.568 0.02 1 1186 236 247 ASN HA H 4.982 0.02 1 1187 236 247 ASN HB2 H 2.839 0.02 1 1188 236 247 ASN HB3 H 2.839 0.02 1 1189 236 247 ASN CA C 51.970 0.20 1 1190 236 247 ASN CB C 40.149 0.20 1 1191 236 247 ASN N N 124.179 0.20 1 1192 237 248 LEU H H 8.602 0.02 1 1193 237 248 LEU HA H 4.693 0.02 1 1194 237 248 LEU HB2 H 1.258 0.02 1 1195 237 248 LEU HB3 H 1.258 0.02 1 1196 237 248 LEU HG H 1.343 0.02 1 1197 237 248 LEU HD1 H 0.825 0.02 2 1198 237 248 LEU HD2 H 0.922 0.02 2 1199 237 248 LEU CA C 54.619 0.20 1 1200 237 248 LEU CB C 42.846 0.20 1 1201 237 248 LEU CG C 28.054 0.20 1 1202 237 248 LEU CD1 C 27.140 0.20 2 1203 237 248 LEU CD2 C 24.974 0.20 2 1204 237 248 LEU N N 127.294 0.20 1 1205 238 249 LYS H H 8.677 0.02 1 1206 238 249 LYS HA H 4.342 0.02 1 1207 238 249 LYS HB2 H 1.829 0.02 2 1208 238 249 LYS HB3 H 1.430 0.02 2 1209 238 249 LYS CA C 58.280 0.20 1 1210 238 249 LYS CB C 33.519 0.20 1 1211 238 249 LYS N N 127.363 0.20 1 1212 239 250 LYS HD2 H 1.524 0.02 1 1213 239 250 LYS HD3 H 1.524 0.02 1 1214 239 250 LYS H H 7.618 0.02 1 1215 239 250 LYS HA H 4.457 0.02 1 1216 239 250 LYS HE2 H 2.764 0.02 1 1217 239 250 LYS HE3 H 2.764 0.02 1 1218 239 250 LYS CA C 56.660 0.20 1 1219 239 250 LYS CD C 29.327 0.20 1 1220 239 250 LYS CE C 41.608 0.20 1 1221 239 250 LYS N N 117.789 0.20 1 1222 240 251 VAL H H 9.153 0.02 1 1223 240 251 VAL HA H 4.602 0.02 1 1224 240 251 VAL HB H 2.275 0.02 1 1225 240 251 VAL HG1 H 1.038 0.02 2 1226 240 251 VAL HG2 H 1.007 0.02 2 1227 240 251 VAL CA C 62.207 0.20 1 1228 240 251 VAL CB C 34.569 0.20 1 1229 240 251 VAL CG1 C 22.846 0.20 2 1230 240 251 VAL CG2 C 22.995 0.20 2 1231 240 251 VAL N N 126.238 0.20 1 1232 241 252 GLU H H 9.364 0.02 1 1233 241 252 GLU HA H 5.324 0.02 1 1234 241 252 GLU CA C 54.212 0.20 1 1235 241 252 GLU N N 124.926 0.20 1 1236 242 253 GLU H H 9.512 0.02 1 1237 242 253 GLU HA H 5.489 0.02 1 1238 242 253 GLU HG2 H 2.094 0.02 1 1239 242 253 GLU HG3 H 2.094 0.02 1 1240 242 253 GLU CA C 52.867 0.20 1 1241 242 253 GLU CG C 34.755 0.20 1 1242 242 253 GLU N N 117.520 0.20 1 1243 243 254 ARG HD2 H 2.571 0.02 1 1244 243 254 ARG HD3 H 2.571 0.02 1 1245 243 254 ARG H H 8.490 0.02 1 1246 243 254 ARG HA H 3.742 0.02 1 1247 243 254 ARG HB2 H 1.157 0.02 2 1248 243 254 ARG HB3 H 1.021 0.02 2 1249 243 254 ARG HG2 H 0.740 0.02 2 1250 243 254 ARG HG3 H 0.562 0.02 2 1251 243 254 ARG CA C 55.965 0.20 1 1252 243 254 ARG CB C 30.307 0.20 1 1253 243 254 ARG CG C 26.868 0.20 1 1254 243 254 ARG CD C 43.007 0.20 1 1255 243 254 ARG N N 123.424 0.20 1 1256 244 255 GLU H H 8.211 0.02 1 1257 244 255 GLU HA H 4.208 0.02 1 1258 244 255 GLU HG2 H 2.085 0.02 2 1259 244 255 GLU HG3 H 1.965 0.02 2 1260 244 255 GLU CA C 56.092 0.20 1 1261 244 255 GLU CG C 36.661 0.20 1 1262 244 255 GLU N N 124.080 0.20 1 1263 245 256 LEU H H 8.493 0.02 1 1264 245 256 LEU HA H 4.574 0.02 1 1265 245 256 LEU HB2 H 1.540 0.02 1 1266 245 256 LEU HB3 H 1.540 0.02 1 1267 245 256 LEU HG H 1.557 0.02 1 1268 245 256 LEU HD1 H 0.809 0.02 2 1269 245 256 LEU CA C 52.651 0.20 1 1270 245 256 LEU CB C 41.728 0.20 1 1271 245 256 LEU CG C 26.975 0.20 1 1272 245 256 LEU CD1 C 23.404 0.20 2 1273 245 256 LEU N N 126.373 0.20 1 1274 246 257 PRO HA H 4.323 0.02 1 1275 246 257 PRO HB2 H 2.215 0.02 2 1276 246 257 PRO HB3 H 1.843 0.02 2 1277 246 257 PRO HG2 H 1.944 0.02 1 1278 246 257 PRO HG3 H 1.944 0.02 1 1279 246 257 PRO HD2 H 3.718 0.02 2 1280 246 257 PRO HD3 H 3.618 0.02 2 1281 246 257 PRO CA C 63.152 0.20 1 1282 246 257 PRO CB C 32.038 0.20 1 1283 246 257 PRO CG C 27.331 0.20 1 1284 246 257 PRO CD C 50.539 0.20 1 1285 247 258 GLU H H 8.552 0.02 1 1286 247 258 GLU HA H 4.135 0.02 1 1287 247 258 GLU CA C 56.788 0.20 1 1288 247 258 GLU N N 120.616 0.20 1 1289 248 259 LEU HD1 H 0.786 0.02 2 1290 248 259 LEU HD2 H 0.503 0.02 2 1291 248 259 LEU CD1 C 25.408 0.20 2 1292 248 259 LEU CD2 C 22.910 0.20 2 1293 249 260 THR H H 7.893 0.02 1 1294 249 260 THR N N 114.269 0.20 1 1295 250 261 ALA H H 8.582 0.02 1 1296 250 261 ALA HB H 1.480 0.02 1 1297 250 261 ALA CB C 18.300 0.20 1 1298 250 261 ALA N N 123.770 0.20 1 1299 251 262 GLU H H 8.289 0.02 1 1300 251 262 GLU N N 117.064 0.20 1 1301 252 263 PHE H H 7.903 0.02 1 1302 252 263 PHE N N 121.871 0.20 1 1303 253 264 ILE H H 8.200 0.02 1 1304 253 264 ILE HD1 H 0.681 0.02 1 1305 253 264 ILE CD1 C 13.058 0.20 1 1306 253 264 ILE N N 120.642 0.20 1 1307 257 268 GLY H H 7.691 0.02 1 1308 257 268 GLY N N 105.519 0.20 1 1309 258 269 VAL H H 7.427 0.02 1 1310 258 269 VAL HG1 H 0.936 0.02 2 1311 258 269 VAL HG2 H 0.798 0.02 2 1312 258 269 VAL CG1 C 21.137 0.20 2 1313 258 269 VAL CG2 C 20.269 0.20 2 1314 258 269 VAL N N 120.477 0.20 1 1315 259 270 GLU H H 8.542 0.02 1 1316 259 270 GLU N N 127.169 0.20 1 1317 260 271 ASP H H 8.197 0.02 1 1318 260 271 ASP N N 116.940 0.20 1 1319 261 272 GLY H H 8.087 0.02 1 1320 261 272 GLY N N 108.316 0.20 1 1321 262 273 SER H H 8.144 0.02 1 1322 262 273 SER N N 115.804 0.20 1 1323 263 274 VAL H H 8.567 0.02 1 1324 263 274 VAL HG1 H 0.930 0.02 2 1325 263 274 VAL HG2 H 1.019 0.02 2 1326 263 274 VAL CG1 C 21.133 0.20 2 1327 263 274 VAL CG2 C 22.176 0.20 2 1328 263 274 VAL N N 123.717 0.20 1 1329 264 275 GLU H H 8.749 0.02 1 1330 264 275 GLU N N 121.376 0.20 1 1331 265 276 GLY H H 8.322 0.02 1 1332 265 276 GLY N N 110.393 0.20 1 1333 266 277 LEU H H 8.016 0.02 1 1334 266 277 LEU HD2 H 0.778 0.02 2 1335 266 277 LEU CD2 C 26.143 0.20 2 1336 266 277 LEU N N 124.735 0.20 1 1337 267 278 ARG H H 8.482 0.02 1 1338 267 278 ARG N N 118.788 0.20 1 1339 268 279 ALA H H 7.672 0.02 1 1340 268 279 ALA HB H 1.514 0.02 1 1341 268 279 ALA CB C 18.024 0.20 1 1342 268 279 ALA N N 119.860 0.20 1 1343 269 280 GLU H H 7.872 0.02 1 1344 269 280 GLU N N 121.102 0.20 1 1345 270 281 VAL H H 8.313 0.02 1 1346 270 281 VAL HG1 H 0.878 0.02 2 1347 270 281 VAL HG2 H 1.027 0.02 2 1348 270 281 VAL CG1 C 22.691 0.20 2 1349 270 281 VAL CG2 C 22.221 0.20 2 1350 270 281 VAL N N 119.894 0.20 1 1351 271 282 ARG H H 7.607 0.02 1 1352 271 282 ARG N N 123.426 0.20 1 1353 274 285 MET HE H 2.086 0.02 1 1354 274 285 MET CE C 17.337 0.20 1 1355 277 288 GLU H H 8.164 0.02 1 1356 277 288 GLU N N 120.426 0.20 1 1357 278 289 LEU H H 8.862 0.02 1 1358 278 289 LEU HD1 H 0.714 0.02 2 1359 278 289 LEU HD2 H 0.772 0.02 2 1360 278 289 LEU CD1 C 26.668 0.20 2 1361 278 289 LEU CD2 C 24.046 0.20 2 1362 278 289 LEU N N 122.603 0.20 1 1363 279 290 LYS H H 7.965 0.02 1 1364 279 290 LYS N N 119.055 0.20 1 1365 280 291 SER H H 7.550 0.02 1 1366 280 291 SER N N 114.321 0.20 1 1367 281 292 ALA H H 8.104 0.02 1 1368 281 292 ALA HB H 1.460 0.02 1 1369 281 292 ALA CB C 18.766 0.20 1 1370 281 292 ALA N N 125.431 0.20 1 1371 282 293 ILE H H 8.742 0.02 1 1372 282 293 ILE HD1 H 0.841 0.02 1 1373 282 293 ILE CD1 C 14.098 0.20 1 1374 282 293 ILE N N 120.785 0.20 1 1375 283 294 ARG H H 7.616 0.02 1 1376 283 294 ARG N N 119.160 0.20 1 1377 284 295 ASN H H 8.330 0.02 1 1378 284 295 ASN N N 117.500 0.20 1 1379 285 296 ARG H H 8.204 0.02 1 1380 285 296 ARG N N 123.385 0.20 1 1381 286 297 VAL H H 8.321 0.02 1 1382 286 297 VAL HG1 H 1.109 0.02 2 1383 286 297 VAL CG1 C 22.168 0.20 2 1384 286 297 VAL N N 120.175 0.20 1 1385 287 298 LYS H H 8.272 0.02 1 1386 287 298 LYS N N 120.714 0.20 1 1387 288 299 SER H H 8.297 0.02 1 1388 288 299 SER N N 112.588 0.20 1 1389 289 300 GLN H H 7.369 0.02 1 1390 289 300 GLN N N 119.499 0.20 1 1391 290 301 ALA H H 8.176 0.02 1 1392 290 301 ALA HB H 1.400 0.02 1 1393 290 301 ALA CB C 17.654 0.20 1 1394 290 301 ALA N N 124.394 0.20 1 1395 291 302 ILE H H 8.353 0.02 1 1396 291 302 ILE HD1 H 0.798 0.02 1 1397 291 302 ILE CD1 C 12.093 0.20 1 1398 291 302 ILE N N 116.525 0.20 1 1399 292 303 GLU H H 8.227 0.02 1 1400 292 303 GLU N N 119.557 0.20 1 1401 293 304 GLY H H 8.025 0.02 1 1402 293 304 GLY N N 105.174 0.20 1 1403 294 305 LEU HD1 H 0.775 0.02 2 1404 294 305 LEU HD2 H 0.779 0.02 2 1405 294 305 LEU CD1 C 23.839 0.20 2 1406 294 305 LEU CD2 C 24.148 0.20 2 1407 295 306 VAL H H 8.349 0.02 1 1408 295 306 VAL N N 119.423 0.20 1 1409 296 307 LYS H H 8.175 0.02 1 1410 296 307 LYS N N 119.010 0.20 1 1411 297 308 ALA H H 7.160 0.02 1 1412 297 308 ALA HB H 1.439 0.02 1 1413 297 308 ALA CB C 20.368 0.20 1 1414 297 308 ALA N N 117.049 0.20 1 1415 298 309 ASN H H 7.279 0.02 1 1416 298 309 ASN N N 118.409 0.20 1 1417 299 310 ASP H H 8.301 0.02 1 1418 299 310 ASP N N 122.930 0.20 1 1419 300 311 ILE H H 7.687 0.02 1 1420 300 311 ILE HD1 H 0.825 0.02 1 1421 300 311 ILE CD1 C 14.225 0.20 1 1422 300 311 ILE N N 120.282 0.20 1 1423 301 312 ASP H H 8.388 0.02 1 1424 301 312 ASP N N 124.119 0.20 1 1425 302 313 VAL H H 8.098 0.02 1 1426 302 313 VAL HG1 H 1.106 0.02 2 1427 302 313 VAL HG2 H 0.860 0.02 2 1428 302 313 VAL CG1 C 23.933 0.20 2 1429 302 313 VAL CG2 C 21.206 0.20 2 1430 302 313 VAL N N 122.085 0.20 1 1431 304 315 ALA H H 8.661 0.02 1 1432 304 315 ALA HB H 1.464 0.02 1 1433 304 315 ALA CB C 18.288 0.20 1 1434 304 315 ALA N N 128.663 0.20 1 1435 305 316 ALA H H 8.743 0.02 1 1436 305 316 ALA HB H 1.402 0.02 1 1437 305 316 ALA CB C 18.402 0.20 1 1438 305 316 ALA N N 117.597 0.20 1 1439 306 317 LEU H H 7.182 0.02 1 1440 306 317 LEU HD1 H 0.954 0.02 2 1441 306 317 LEU HD2 H 0.887 0.02 2 1442 306 317 LEU CD1 C 25.023 0.20 2 1443 306 317 LEU CD2 C 22.549 0.20 2 1444 306 317 LEU N N 115.482 0.20 1 1445 307 318 ILE H H 7.126 0.02 1 1446 307 318 ILE HD1 H 0.829 0.02 1 1447 307 318 ILE CD1 C 12.893 0.20 1 1448 307 318 ILE N N 121.075 0.20 1 1449 308 319 ASP H H 8.473 0.02 1 1450 308 319 ASP N N 120.455 0.20 1 1451 309 320 SER H H 7.624 0.02 1 1452 309 320 SER N N 114.500 0.20 1 1453 310 321 GLU H H 7.492 0.02 1 1454 310 321 GLU N N 124.076 0.20 1 1455 311 322 ILE H H 8.663 0.02 1 1456 311 322 ILE HD1 H 0.892 0.02 1 1457 311 322 ILE CD1 C 14.139 0.20 1 1458 311 322 ILE N N 121.488 0.20 1 1459 312 323 ASP H H 7.315 0.02 1 1460 312 323 ASP N N 119.378 0.20 1 1461 313 324 VAL H H 7.331 0.02 1 1462 313 324 VAL N N 121.341 0.20 1 1463 314 325 LEU H H 8.034 0.02 1 1464 314 325 LEU HD1 H 0.826 0.02 2 1465 314 325 LEU HD2 H 0.966 0.02 2 1466 314 325 LEU CD1 C 21.789 0.20 2 1467 314 325 LEU CD2 C 26.568 0.20 2 1468 314 325 LEU N N 125.153 0.20 1 1469 315 326 ARG H H 8.638 0.02 1 1470 315 326 ARG N N 122.041 0.20 1 1471 318 329 ALA H H 7.976 0.02 1 1472 318 329 ALA HB H 1.656 0.02 1 1473 318 329 ALA CB C 18.070 0.20 1 1474 318 329 ALA N N 123.121 0.20 1 1475 319 330 ALA H H 8.013 0.02 1 1476 319 330 ALA HB H 1.276 0.02 1 1477 319 330 ALA CB C 17.962 0.20 1 1478 319 330 ALA N N 120.066 0.20 1 1479 320 331 GLN H H 7.673 0.02 1 1480 320 331 GLN N N 117.530 0.20 1 1481 321 332 ARG H H 7.519 0.02 1 1482 321 332 ARG N N 118.993 0.20 1 1483 322 333 PHE H H 7.572 0.02 1 1484 322 333 PHE N N 116.853 0.20 1 1485 323 334 GLY H H 7.875 0.02 1 1486 323 334 GLY N N 110.692 0.20 1 1487 324 335 GLY H H 8.079 0.02 1 1488 324 335 GLY N N 108.586 0.20 1 1489 325 336 ASN H H 8.134 0.02 1 1490 325 336 ASN N N 119.492 0.20 1 1491 326 337 GLU H H 8.530 0.02 1 1492 326 337 GLU N N 121.828 0.20 1 1493 327 338 LYS H H 8.013 0.02 1 1494 327 338 LYS N N 120.066 0.20 1 1495 328 339 GLN H H 7.879 0.02 1 1496 328 339 GLN N N 118.346 0.20 1 1497 329 340 ALA H H 7.955 0.02 1 1498 329 340 ALA HB H 1.342 0.02 1 1499 329 340 ALA CB C 18.454 0.20 1 1500 329 340 ALA N N 122.967 0.20 1 1501 330 341 LEU H H 7.698 0.02 1 1502 330 341 LEU HD1 H 0.855 0.02 2 1503 330 341 LEU HD2 H 0.774 0.02 2 1504 330 341 LEU CD1 C 24.876 0.20 2 1505 330 341 LEU CD2 C 22.629 0.20 2 1506 330 341 LEU N N 116.656 0.20 1 1507 331 342 GLU H H 7.520 0.02 1 1508 331 342 GLU N N 117.624 0.20 1 1509 332 343 LEU HD1 H 1.137 0.02 2 1510 332 343 LEU HD2 H 0.978 0.02 2 1511 332 343 LEU CD1 C 26.459 0.20 2 1512 332 343 LEU CD2 C 22.648 0.20 2 1513 334 345 ARG H H 8.691 0.02 1 1514 334 345 ARG N N 123.171 0.20 1 1515 335 346 GLU H H 9.488 0.02 1 1516 335 346 GLU N N 117.939 0.20 1 1517 336 347 LEU H H 7.429 0.02 1 1518 336 347 LEU HD1 H 0.711 0.02 2 1519 336 347 LEU HD2 H 0.828 0.02 2 1520 336 347 LEU CD1 C 22.597 0.20 2 1521 336 347 LEU CD2 C 25.046 0.20 2 1522 336 347 LEU N N 119.286 0.20 1 1523 337 348 PHE H H 7.628 0.02 1 1524 337 348 PHE N N 114.263 0.20 1 1525 338 349 GLU H H 7.332 0.02 1 1526 338 349 GLU N N 120.019 0.20 1 1527 339 350 GLU H H 8.628 0.02 1 1528 339 350 GLU N N 120.148 0.20 1 1529 340 351 GLN H H 8.566 0.02 1 1530 340 351 GLN N N 121.107 0.20 1 1531 341 352 ALA H H 8.644 0.02 1 1532 341 352 ALA HB H 1.490 0.02 1 1533 341 352 ALA CB C 20.397 0.20 1 1534 341 352 ALA N N 122.221 0.20 1 1535 342 353 LYS H H 8.231 0.02 1 1536 342 353 LYS N N 117.543 0.20 1 1537 343 354 ARG H H 7.629 0.02 1 1538 343 354 ARG N N 117.923 0.20 1 1539 344 355 ARG H H 7.912 0.02 1 1540 344 355 ARG N N 117.633 0.20 1 1541 345 356 VAL H H 8.129 0.02 1 1542 345 356 VAL HG1 H 0.979 0.02 2 1543 345 356 VAL HG2 H 0.902 0.02 2 1544 345 356 VAL CG1 C 22.914 0.20 2 1545 345 356 VAL CG2 C 23.018 0.20 2 1546 345 356 VAL N N 119.987 0.20 1 1547 346 357 VAL H H 8.552 0.02 1 1548 346 357 VAL N N 121.244 0.20 1 1549 347 358 VAL H H 8.427 0.02 1 1550 347 358 VAL HG1 H 0.812 0.02 2 1551 347 358 VAL HG2 H 0.903 0.02 2 1552 347 358 VAL CG1 C 25.978 0.20 2 1553 347 358 VAL CG2 C 21.587 0.20 2 1554 347 358 VAL N N 120.048 0.20 1 1555 348 359 GLY H H 7.758 0.02 1 1556 348 359 GLY N N 105.224 0.20 1 1557 349 360 LEU H H 8.161 0.02 1 1558 349 360 LEU HD1 H 0.823 0.02 2 1559 349 360 LEU HD2 H 0.873 0.02 2 1560 349 360 LEU CD1 C 26.437 0.20 2 1561 349 360 LEU CD2 C 22.822 0.20 2 1562 349 360 LEU N N 123.311 0.20 1 1563 350 361 LEU H H 8.607 0.02 1 1564 350 361 LEU N N 120.469 0.20 1 1565 351 362 LEU H H 9.025 0.02 1 1566 351 362 LEU HD1 H 1.077 0.02 2 1567 351 362 LEU HD2 H 0.634 0.02 2 1568 351 362 LEU CD1 C 23.780 0.20 2 1569 351 362 LEU CD2 C 21.346 0.20 2 1570 351 362 LEU N N 118.327 0.20 1 1571 352 363 GLY H H 8.035 0.02 1 1572 352 363 GLY N N 107.011 0.20 1 1573 353 364 GLU H H 7.673 0.02 1 1574 353 364 GLU N N 123.882 0.20 1 1575 354 365 VAL H H 8.063 0.02 1 1576 354 365 VAL HG1 H 0.940 0.02 2 1577 354 365 VAL CG1 C 22.280 0.20 2 1578 354 365 VAL N N 125.201 0.20 1 1579 355 366 ILE H H 8.440 0.02 1 1580 355 366 ILE HD1 H 0.776 0.02 1 1581 355 366 ILE CD1 C 13.828 0.20 1 1582 355 366 ILE N N 121.731 0.20 1 1583 356 367 ARG H H 8.030 0.02 1 1584 356 367 ARG N N 119.300 0.20 1 1585 357 368 THR H H 8.637 0.02 1 1586 357 368 THR N N 112.438 0.20 1 1587 358 369 ASN H H 7.374 0.02 1 1588 358 369 ASN N N 116.627 0.20 1 1589 359 370 GLU H H 7.669 0.02 1 1590 359 370 GLU N N 118.937 0.20 1 1591 360 371 LEU H H 7.952 0.02 1 1592 360 371 LEU HD1 H 0.691 0.02 2 1593 360 371 LEU HD2 H 0.812 0.02 2 1594 360 371 LEU CD1 C 25.210 0.20 2 1595 360 371 LEU CD2 C 22.340 0.20 2 1596 360 371 LEU N N 116.264 0.20 1 1597 361 372 LYS H H 8.275 0.02 1 1598 361 372 LYS N N 121.035 0.20 1 1599 362 373 ALA H H 8.904 0.02 1 1600 362 373 ALA HB H 1.273 0.02 1 1601 362 373 ALA CB C 18.314 0.20 1 1602 362 373 ALA N N 126.883 0.20 1 1603 363 374 ASP H H 8.898 0.02 1 1604 363 374 ASP N N 125.163 0.20 1 1605 364 375 GLU H H 8.978 0.02 1 1606 364 375 GLU N N 127.932 0.20 1 1607 367 378 VAL H H 7.957 0.02 1 1608 367 378 VAL HG1 H 0.915 0.02 2 1609 367 378 VAL HG2 H 0.842 0.02 2 1610 367 378 VAL CG1 C 23.967 0.20 2 1611 367 378 VAL CG2 C 21.640 0.20 2 1612 367 378 VAL N N 120.675 0.20 1 1613 368 379 LYS H H 7.698 0.02 1 1614 368 379 LYS N N 118.694 0.20 1 1615 369 380 GLY H H 7.829 0.02 1 1616 369 380 GLY N N 106.885 0.20 1 1617 370 381 LEU H H 8.210 0.02 1 1618 370 381 LEU HD1 H 0.835 0.02 2 1619 370 381 LEU HD2 H 0.873 0.02 2 1620 370 381 LEU CD1 C 26.051 0.20 2 1621 370 381 LEU CD2 C 22.866 0.20 2 1622 370 381 LEU N N 124.546 0.20 1 1623 371 382 ILE H H 7.963 0.02 1 1624 371 382 ILE HD1 H 0.801 0.02 1 1625 371 382 ILE CD1 C 14.176 0.20 1 1626 371 382 ILE N N 121.561 0.20 1 1627 372 383 GLU H H 8.216 0.02 1 1628 372 383 GLU N N 120.412 0.20 1 1629 373 384 GLU H H 8.040 0.02 1 1630 373 384 GLU N N 119.684 0.20 1 1631 374 385 MET H H 7.836 0.02 1 1632 374 385 MET HE H 1.742 0.02 1 1633 374 385 MET CE C 16.531 0.20 1 1634 374 385 MET N N 121.537 0.20 1 1635 375 386 ALA H H 8.386 0.02 1 1636 375 386 ALA HB H 1.519 0.02 1 1637 375 386 ALA CB C 19.176 0.20 1 1638 375 386 ALA N N 120.994 0.20 1 1639 377 388 ALA H H 7.359 0.02 1 1640 377 388 ALA HB H 1.213 0.02 1 1641 377 388 ALA CB C 19.076 0.20 1 1642 377 388 ALA N N 122.867 0.20 1 1643 378 389 TYR H H 7.779 0.02 1 1644 378 389 TYR N N 118.447 0.20 1 1645 380 391 ASP H H 8.114 0.02 1 1646 380 391 ASP N N 117.249 0.20 1 1647 382 393 LYS H H 7.851 0.02 1 1648 382 393 LYS N N 115.812 0.20 1 1649 383 394 GLU H H 7.459 0.02 1 1650 383 394 GLU N N 119.553 0.20 1 1651 384 395 VAL H H 7.203 0.02 1 1652 384 395 VAL HG1 H 0.687 0.02 2 1653 384 395 VAL HG2 H 0.591 0.02 2 1654 384 395 VAL CG1 C 21.020 0.20 2 1655 384 395 VAL CG2 C 21.648 0.20 2 1656 384 395 VAL N N 121.261 0.20 1 1657 385 396 ILE H H 8.144 0.02 1 1658 385 396 ILE HD1 H 0.804 0.02 1 1659 385 396 ILE CD1 C 13.552 0.20 1 1660 385 396 ILE N N 120.973 0.20 1 1661 386 397 GLU H H 7.912 0.02 1 1662 386 397 GLU N N 120.824 0.20 1 1663 387 398 PHE H H 7.971 0.02 1 1664 387 398 PHE N N 121.133 0.20 1 1665 388 399 TYR H H 8.581 0.02 1 1666 388 399 TYR N N 119.603 0.20 1 1667 389 400 SER H H 7.875 0.02 1 1668 389 400 SER N N 110.692 0.20 1 1669 390 401 LYS H H 7.161 0.02 1 1670 390 401 LYS N N 118.547 0.20 1 1671 391 402 ASN H H 7.447 0.02 1 1672 391 402 ASN N N 121.662 0.20 1 1673 392 403 LYS H H 8.485 0.02 1 1674 392 403 LYS N N 127.162 0.20 1 1675 393 404 GLU H H 8.249 0.02 1 1676 393 404 GLU N N 118.463 0.20 1 1677 394 405 LEU H H 7.570 0.02 1 1678 394 405 LEU HD1 H 0.375 0.02 2 1679 394 405 LEU HD2 H 0.633 0.02 2 1680 394 405 LEU CD1 C 24.977 0.20 2 1681 394 405 LEU CD2 C 22.599 0.20 2 1682 394 405 LEU N N 120.510 0.20 1 1683 395 406 MET H H 8.060 0.02 1 1684 395 406 MET HE H 1.923 0.02 1 1685 395 406 MET CE C 15.857 0.20 1 1686 395 406 MET N N 119.320 0.20 1 1687 396 407 ASP H H 8.686 0.02 1 1688 396 407 ASP N N 120.989 0.20 1 1689 397 408 ASN H H 7.883 0.02 1 1690 397 408 ASN N N 119.470 0.20 1 1691 398 409 MET H H 8.128 0.02 1 1692 398 409 MET HE H 1.964 0.02 1 1693 398 409 MET CE C 17.440 0.20 1 1694 398 409 MET N N 119.248 0.20 1 1695 399 410 ARG H H 8.562 0.02 1 1696 399 410 ARG N N 120.989 0.20 1 1697 400 411 ASN H H 7.655 0.02 1 1698 400 411 ASN N N 117.911 0.20 1 1699 401 412 VAL H H 7.875 0.02 1 1700 401 412 VAL HG1 H 1.105 0.02 2 1701 401 412 VAL HG2 H 0.962 0.02 2 1702 401 412 VAL CG1 C 22.287 0.20 2 1703 401 412 VAL CG2 C 21.784 0.20 2 1704 401 412 VAL N N 123.544 0.20 1 1705 402 413 ALA H H 8.136 0.02 1 1706 402 413 ALA HB H 1.448 0.02 1 1707 402 413 ALA CB C 18.109 0.20 1 1708 402 413 ALA N N 123.151 0.20 1 1709 403 414 LEU H H 8.315 0.02 1 1710 403 414 LEU HD1 H 0.795 0.02 2 1711 403 414 LEU HD2 H 0.746 0.02 2 1712 403 414 LEU CD1 C 24.372 0.20 2 1713 403 414 LEU CD2 C 24.507 0.20 2 1714 403 414 LEU N N 118.858 0.20 1 1715 404 415 GLU H H 7.956 0.02 1 1716 404 415 GLU N N 120.035 0.20 1 1717 406 417 GLN H H 8.553 0.02 1 1718 406 417 GLN N N 119.750 0.20 1 1719 407 418 ALA H H 8.791 0.02 1 1720 407 418 ALA HB H 1.487 0.02 1 1721 407 418 ALA CB C 18.473 0.20 1 1722 407 418 ALA N N 125.631 0.20 1 1723 408 419 VAL H H 8.119 0.02 1 1724 408 419 VAL HG1 H 0.954 0.02 2 1725 408 419 VAL HG2 H 0.886 0.02 2 1726 408 419 VAL CG1 C 23.182 0.20 2 1727 408 419 VAL CG2 C 21.282 0.20 2 1728 408 419 VAL N N 119.190 0.20 1 1729 409 420 GLU H H 8.030 0.02 1 1730 409 420 GLU N N 119.300 0.20 1 1731 410 421 ALA H H 7.831 0.02 1 1732 410 421 ALA HB H 1.401 0.02 1 1733 410 421 ALA CB C 17.206 0.20 1 1734 410 421 ALA N N 123.453 0.20 1 1735 411 422 VAL H H 7.701 0.02 1 1736 411 422 VAL HG1 H 0.763 0.02 2 1737 411 422 VAL HG2 H 1.017 0.02 2 1738 411 422 VAL CG1 C 25.816 0.20 2 1739 411 422 VAL CG2 C 23.294 0.20 2 1740 411 422 VAL N N 120.582 0.20 1 1741 412 423 LEU H H 8.429 0.02 1 1742 412 423 LEU HD1 H 0.763 0.02 2 1743 412 423 LEU HD2 H 0.722 0.02 2 1744 412 423 LEU CD1 C 25.667 0.20 2 1745 412 423 LEU CD2 C 24.057 0.20 2 1746 412 423 LEU N N 120.037 0.20 1 1747 413 424 ALA H H 7.569 0.02 1 1748 413 424 ALA HB H 1.492 0.02 1 1749 413 424 ALA CB C 18.340 0.20 1 1750 413 424 ALA N N 118.506 0.20 1 1751 414 425 LYS H H 7.091 0.02 1 1752 414 425 LYS N N 115.412 0.20 1 1753 415 426 ALA H H 7.113 0.02 1 1754 415 426 ALA HB H 1.246 0.02 1 1755 415 426 ALA CB C 19.715 0.20 1 1756 415 426 ALA N N 121.749 0.20 1 1757 416 427 LYS H H 8.642 0.02 1 1758 416 427 LYS N N 121.412 0.20 1 1759 417 428 VAL H H 8.375 0.02 1 1760 417 428 VAL HG1 H 0.778 0.02 2 1761 417 428 VAL HG2 H 0.810 0.02 2 1762 417 428 VAL CG1 C 21.020 0.20 2 1763 417 428 VAL CG2 C 21.758 0.20 2 1764 417 428 VAL N N 129.549 0.20 1 1765 418 429 THR H H 8.892 0.02 1 1766 418 429 THR N N 124.178 0.20 1 1767 419 430 GLU H H 8.720 0.02 1 1768 419 430 GLU N N 124.474 0.20 1 1769 420 431 LYS H H 8.231 0.02 1 1770 420 431 LYS N N 124.589 0.20 1 1771 421 432 GLU H H 9.106 0.02 1 1772 421 432 GLU N N 130.895 0.20 1 1773 422 433 THR H H 8.373 0.02 1 1774 422 433 THR N N 120.713 0.20 1 1775 423 434 THR H H 8.453 0.02 1 1776 423 434 THR N N 112.737 0.20 1 1777 424 435 PHE H H 9.794 0.02 1 1778 424 435 PHE N N 124.760 0.20 1 1779 425 436 ASN H H 9.342 0.02 1 1780 425 436 ASN N N 116.073 0.20 1 1781 426 437 GLU H H 7.619 0.02 1 1782 426 437 GLU N N 118.920 0.20 1 1783 427 438 LEU H H 7.868 0.02 1 1784 427 438 LEU HD1 H 1.004 0.02 2 1785 427 438 LEU HD2 H 0.897 0.02 2 1786 427 438 LEU CD1 C 26.437 0.20 2 1787 427 438 LEU CD2 C 24.249 0.20 2 1788 427 438 LEU N N 120.092 0.20 1 1789 428 439 MET H H 7.930 0.02 1 1790 428 439 MET HE H 1.739 0.02 1 1791 428 439 MET CE C 16.713 0.20 1 1792 428 439 MET N N 115.030 0.20 1 1793 429 440 ASN H H 7.524 0.02 1 1794 429 440 ASN N N 117.622 0.20 1 1795 430 441 GLN H H 7.752 0.02 1 1796 430 441 GLN N N 119.813 0.20 1 1797 431 442 GLN H H 8.084 0.02 1 1798 431 442 GLN N N 121.474 0.20 1 1799 432 443 ALA H H 7.871 0.02 1 1800 432 443 ALA HB H 1.311 0.02 1 1801 432 443 ALA CB C 19.948 0.20 1 1802 432 443 ALA N N 131.624 0.20 1 stop_ save_ save_assigned_chem_shift_list_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $OLIVIA stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name entity_1 _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1221 4 ARG H H 8.232 0.02 1 2 1221 4 ARG N N 119.836 0.20 1 3 1222 5 ALA H H 8.302 0.02 1 4 1222 5 ALA N N 125.122 0.20 1 5 1223 6 ASP H H 8.369 0.02 1 6 1223 6 ASP N N 119.611 0.20 1 7 1224 7 VAL H H 8.139 0.02 1 8 1224 7 VAL N N 120.562 0.20 1 9 1225 8 THR H H 8.387 0.02 1 10 1225 8 THR N N 117.894 0.20 1 11 1226 9 LEU H H 8.282 0.02 1 12 1226 9 LEU N N 124.736 0.20 1 13 1227 10 GLY H H 8.487 0.02 1 14 1227 10 GLY N N 109.947 0.20 1 15 1228 11 GLY H H 8.319 0.02 1 16 1228 11 GLY N N 108.825 0.20 1 17 1232 15 THR H H 8.117 0.02 1 18 1232 15 THR HA H 4.344 0.02 1 19 1232 15 THR HB H 4.328 0.02 1 20 1232 15 THR HG2 H 1.218 0.02 1 21 1232 15 THR N N 115.658 0.20 1 22 1233 16 PHE HD1 H 7.259 0.02 1 23 1233 16 PHE HD2 H 7.259 0.02 1 24 1233 16 PHE H H 8.377 0.02 1 25 1233 16 PHE HA H 4.527 0.02 1 26 1233 16 PHE HB2 H 3.131 0.02 2 27 1233 16 PHE HB3 H 3.019 0.02 2 28 1233 16 PHE HE1 H 7.440 0.02 1 29 1233 16 PHE HE2 H 7.440 0.02 1 30 1233 16 PHE HZ H 6.855 0.02 1 31 1233 16 PHE N N 122.343 0.20 1 32 1234 17 ALA H H 8.280 0.02 1 33 1234 17 ALA HA H 4.351 0.02 1 34 1234 17 ALA HB H 1.393 0.02 1 35 1234 17 ALA N N 125.064 0.20 1 36 1235 18 GLU H H 8.354 0.02 1 37 1235 18 GLU HA H 4.287 0.02 1 38 1235 18 GLU HB2 H 1.904 0.02 1 39 1235 18 GLU HB3 H 1.904 0.02 1 40 1235 18 GLU HG2 H 2.187 0.02 1 41 1235 18 GLU HG3 H 2.187 0.02 1 42 1235 18 GLU N N 120.198 0.20 1 43 1236 19 THR H H 8.156 0.02 1 44 1236 19 THR HA H 4.256 0.02 1 45 1236 19 THR HB H 4.209 0.02 1 46 1236 19 THR HG2 H 1.179 0.02 1 47 1236 19 THR N N 115.024 0.20 1 48 1237 20 ALA H H 8.368 0.02 1 49 1237 20 ALA HA H 4.289 0.02 1 50 1237 20 ALA HB H 1.432 0.02 1 51 1237 20 ALA N N 126.720 0.20 1 52 1238 21 THR H H 8.186 0.02 1 53 1238 21 THR HA H 4.338 0.02 1 54 1238 21 THR HB H 4.287 0.02 1 55 1238 21 THR HG2 H 1.256 0.02 1 56 1238 21 THR N N 113.893 0.20 1 57 1240 23 GLY H H 8.271 0.02 1 58 1240 23 GLY N N 108.207 0.20 1 59 1241 24 GLU H H 8.191 0.02 1 60 1241 24 GLU HA H 4.179 0.02 1 61 1241 24 GLU HB2 H 1.965 0.02 1 62 1241 24 GLU HB3 H 1.965 0.02 1 63 1241 24 GLU HG2 H 2.162 0.02 2 64 1241 24 GLU HG3 H 2.065 0.02 2 65 1241 24 GLU N N 120.291 0.20 1 66 1242 25 TRP H H 8.132 0.02 1 67 1242 25 TRP HA H 4.648 0.02 1 68 1242 25 TRP HB2 H 3.275 0.02 1 69 1242 25 TRP HB3 H 3.275 0.02 1 70 1242 25 TRP HD1 H 7.213 0.02 1 71 1242 25 TRP HE1 H 10.212 0.02 1 72 1242 25 TRP HE3 H 7.612 0.02 1 73 1242 25 TRP HZ2 H 7.455 0.02 1 74 1242 25 TRP HZ3 H 7.123 0.02 1 75 1242 25 TRP HH2 H 7.198 0.02 1 76 1242 25 TRP N N 121.548 0.20 1 77 1245 28 LYS H H 8.061 0.02 1 78 1245 28 LYS N N 120.799 0.20 1 79 1246 29 THR H H 8.369 0.02 1 80 1246 29 THR N N 115.046 0.20 1 81 1247 30 LEU H H 8.418 0.02 1 82 1247 30 LEU N N 123.719 0.20 1 83 1248 31 ARG H H 8.313 0.02 1 84 1248 31 ARG N N 121.035 0.20 1 85 1249 32 GLU H H 8.208 0.02 1 86 1249 32 GLU N N 120.921 0.20 1 87 1250 33 GLN H H 8.391 0.02 1 88 1250 33 GLN N N 120.798 0.20 1 89 1251 34 ALA H H 8.177 0.02 1 90 1251 34 ALA N N 123.600 0.20 1 91 1252 35 GLN H H 8.179 0.02 1 92 1252 35 GLN N N 118.734 0.20 1 93 1253 36 ALA H H 8.108 0.02 1 94 1253 36 ALA N N 123.995 0.20 1 95 1254 37 ARG H H 8.126 0.02 1 96 1254 37 ARG N N 119.192 0.20 1 97 1255 38 GLY H H 8.206 0.02 1 98 1255 38 GLY N N 108.855 0.20 1 99 1258 41 LEU H H 8.272 0.02 1 100 1258 41 LEU N N 123.707 0.20 1 101 1259 42 VAL H H 8.219 0.02 1 102 1259 42 VAL N N 121.695 0.20 1 103 1260 43 SER H H 8.410 0.02 1 104 1260 43 SER N N 119.499 0.20 1 105 1261 44 ASP H H 8.392 0.02 1 106 1261 44 ASP N N 123.002 0.20 1 107 1262 45 ALA H H 8.280 0.02 1 108 1262 45 ALA N N 124.542 0.20 1 109 1263 46 ALA H H 8.272 0.02 1 110 1263 46 ALA N N 121.829 0.20 1 111 1264 47 SER H H 8.126 0.02 1 112 1264 47 SER N N 114.580 0.20 1 113 1265 48 LEU H H 8.140 0.02 1 114 1265 48 LEU N N 123.649 0.20 1 115 1266 49 ASN H H 8.338 0.02 1 116 1266 49 ASN N N 118.540 0.20 1 117 1267 50 SER H H 8.211 0.02 1 118 1267 50 SER N N 116.068 0.20 1 119 1268 51 VAL H H 8.213 0.02 1 120 1268 51 VAL N N 122.288 0.20 1 121 1269 52 THR H H 8.255 0.02 1 122 1269 52 THR N N 117.924 0.20 1 123 1270 53 GLU H H 8.436 0.02 1 124 1270 53 GLU N N 123.462 0.20 1 125 1271 54 ALA H H 8.327 0.02 1 126 1271 54 ALA N N 124.345 0.20 1 127 1272 55 ASN H H 8.361 0.02 1 128 1272 55 ASN N N 117.073 0.20 1 129 1273 56 GLN H H 8.217 0.02 1 130 1273 56 GLN N N 120.178 0.20 1 131 1274 57 GLN H H 8.393 0.02 1 132 1274 57 GLN N N 121.527 0.20 1 133 1277 60 LEU HD1 H 0.928 0.02 1 134 1277 60 LEU HD2 H 0.870 0.02 1 135 1277 60 LEU CD1 C 24.834 0.20 2 136 1277 60 LEU CD2 C 23.459 0.20 2 137 1278 61 LEU HD1 H 0.925 0.02 1 138 1278 61 LEU HD2 H 0.880 0.02 1 139 1278 61 LEU CD1 C 24.944 0.20 2 140 1278 61 LEU CD2 C 23.479 0.20 2 141 1280 63 LEU HD1 H 0.881 0.02 1 142 1280 63 LEU HD2 H 0.853 0.02 1 143 1280 63 LEU CD1 C 23.550 0.20 2 144 1280 63 LEU CD2 C 24.834 0.20 2 145 1281 64 PHE HD1 H 7.258 0.02 1 146 1281 64 PHE HD2 H 7.258 0.02 1 147 1281 64 PHE CD1 C 131.001 0.20 1 148 1281 64 PHE CD2 C 131.001 0.20 1 149 1282 65 ALA HB H 1.357 0.02 1 150 1282 65 ALA CB C 19.286 0.20 1 151 1286 69 MET HE H 2.001 0.02 1 152 1286 69 MET CE C 17.244 0.20 1 153 1288 71 VAL HG2 H 1.238 0.02 1 154 1288 71 VAL HG1 H 0.922 0.02 1 155 1288 71 VAL CG1 C 20.805 0.20 2 156 1288 71 VAL CG2 C 21.688 0.20 2 157 1290 73 TRP HD1 H 7.549 0.02 1 158 1290 73 TRP HE3 H 7.208 0.02 1 159 1290 73 TRP HZ2 H 7.430 0.02 1 160 1290 73 TRP HZ3 H 7.087 0.02 1 161 1290 73 TRP HH2 H 7.172 0.02 1 162 1290 73 TRP CD1 C 120.729 0.20 1 163 1290 73 TRP CE3 C 127.145 0.20 1 164 1290 73 TRP CZ2 C 114.500 0.20 1 165 1290 73 TRP CZ3 C 122.106 0.20 1 166 1290 73 TRP CH2 C 124.516 0.20 1 167 1291 74 LEU HD1 H 0.849 0.02 1 168 1291 74 LEU HD2 H 0.865 0.02 1 169 1291 74 LEU CD1 C 24.923 0.20 2 170 1291 74 LEU CD2 C 23.333 0.20 2 171 1295 78 ALA HB H 1.360 0.02 1 172 1295 78 ALA CB C 19.300 0.20 1 173 1296 79 THR HG2 H 1.097 0.02 1 174 1296 79 THR CG2 C 21.541 0.20 1 175 1297 80 TYR HD1 H 7.236 0.02 3 176 1297 80 TYR CD1 C 133.175 0.20 3 177 1298 81 HIS HD2 H 7.186 0.02 1 178 1298 81 HIS HE1 H 7.639 0.02 1 179 1298 81 HIS CD2 C 119.586 0.20 1 180 1298 81 HIS CE1 C 137.032 0.20 1 181 1301 84 ILE HD1 H 0.887 0.02 1 182 1301 84 ILE CD1 C 17.485 0.20 1 183 1305 88 ALA H H 8.507 0.02 1 184 1305 88 ALA N N 124.939 0.20 1 185 1306 89 VAL H H 8.272 0.02 1 186 1306 89 VAL N N 119.997 0.20 1 187 1307 90 THR H H 8.360 0.02 1 188 1307 90 THR N N 118.752 0.20 1 stop_ save_