data_19740 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The delicate conformational balance of a redox enzyme: Cytochrome P450cam does not open but remains closed when its partner putidaredoxin binds. ; _BMRB_accession_number 19740 _BMRB_flat_file_name bmr19740.str _Entry_type original _Submission_date 2014-01-19 _Accession_date 2014-01-19 _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 Skinner Simon P. . 2 Ubbink Marcellus . . 3 Hiruma Yoshitaka . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 306 "13C chemical shifts" 960 "15N chemical shifts" 297 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-06-22 original BMRB . stop_ _Original_release_date 2015-06-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Delicate conformational balance of the redox enzyme cytochrome P450cam ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Skinner Simon P. . 2 Liu Wei-Min . . 3 Hiruma Yoshitaka . . 4 Timmer Monika . . 5 Blok Anneloes . . 6 Hass Mathias A.S. . 7 Ubbink Marcellus . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. USA' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name CYP101 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CYP101 $CYP101 'PROTOPORPHYRIN IX CONTAINING FE' $entity_HEM CAMPHOR $entity_CAM 'CYANIDE ION' $entity_CYN stop_ _System_molecular_weight 46633.007 _System_physical_state native _System_oligomer_state ? _System_paramagnetic yes _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CYP101 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CYP101 _Molecular_mass 46633.007 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 414 _Mol_residue_sequence ; TTETIQSNANLAPLPPHVPE HLVFDFDMYNPSNLSAGVQE AWAVLQESNVPDLVWTRCNG GHWIATRGQLIREAYEDYRH FSSECPFIPREAGEAYDFIP TSMDPPEQRQFRALANQVVG MPVVDKLENRIQELACSLIE SLRPQGQCNFTEDYAEPFPI RIFMLLAGLPEEDIPHLKYL TDQMTRPDGSMTFAEAKEAL YDYLIPIIEQRRQKPGTDAI SIVANGQVNGRPITSDEAKR MCGLLLVGGLDTVVNFLSFS MEFLAKSPEHRQELIERPER IPAACEELLRRFSLVADGRI LTSDYEFHGVQLKKGDQILL PQMLSGLDERENAAPMHVDF SRQKVSHTTFGHGSHLCLGQ HLARREIIVTLKEWLTRIPD FSIAPGAQIQHKSGIVSGVQ ALPLVWDPATTKAV ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 2 THR 2 3 THR 3 4 GLU 4 5 THR 5 6 ILE 6 7 GLN 7 8 SER 8 9 ASN 9 10 ALA 10 11 ASN 11 12 LEU 12 13 ALA 13 14 PRO 14 15 LEU 15 16 PRO 16 17 PRO 17 18 HIS 18 19 VAL 19 20 PRO 20 21 GLU 21 22 HIS 22 23 LEU 23 24 VAL 24 25 PHE 25 26 ASP 26 27 PHE 27 28 ASP 28 29 MET 29 30 TYR 30 31 ASN 31 32 PRO 32 33 SER 33 34 ASN 34 35 LEU 35 36 SER 36 37 ALA 37 38 GLY 38 39 VAL 39 40 GLN 40 41 GLU 41 42 ALA 42 43 TRP 43 44 ALA 44 45 VAL 45 46 LEU 46 47 GLN 47 48 GLU 48 49 SER 49 50 ASN 50 51 VAL 51 52 PRO 52 53 ASP 53 54 LEU 54 55 VAL 55 56 TRP 56 57 THR 57 58 ARG 58 59 CYS 59 60 ASN 60 61 GLY 61 62 GLY 62 63 HIS 63 64 TRP 64 65 ILE 65 66 ALA 66 67 THR 67 68 ARG 68 69 GLY 69 70 GLN 70 71 LEU 71 72 ILE 72 73 ARG 73 74 GLU 74 75 ALA 75 76 TYR 76 77 GLU 77 78 ASP 78 79 TYR 79 80 ARG 80 81 HIS 81 82 PHE 82 83 SER 83 84 SER 84 85 GLU 85 86 CYS 86 87 PRO 87 88 PHE 88 89 ILE 89 90 PRO 90 91 ARG 91 92 GLU 92 93 ALA 93 94 GLY 94 95 GLU 95 96 ALA 96 97 TYR 97 98 ASP 98 99 PHE 99 100 ILE 100 101 PRO 101 102 THR 102 103 SER 103 104 MET 104 105 ASP 105 106 PRO 106 107 PRO 107 108 GLU 108 109 GLN 109 110 ARG 110 111 GLN 111 112 PHE 112 113 ARG 113 114 ALA 114 115 LEU 115 116 ALA 116 117 ASN 117 118 GLN 118 119 VAL 119 120 VAL 120 121 GLY 121 122 MET 122 123 PRO 123 124 VAL 124 125 VAL 125 126 ASP 126 127 LYS 127 128 LEU 128 129 GLU 129 130 ASN 130 131 ARG 131 132 ILE 132 133 GLN 133 134 GLU 134 135 LEU 135 136 ALA 136 137 CYS 137 138 SER 138 139 LEU 139 140 ILE 140 141 GLU 141 142 SER 142 143 LEU 143 144 ARG 144 145 PRO 145 146 GLN 146 147 GLY 147 148 GLN 148 149 CYS 149 150 ASN 150 151 PHE 151 152 THR 152 153 GLU 153 154 ASP 154 155 TYR 155 156 ALA 156 157 GLU 157 158 PRO 158 159 PHE 159 160 PRO 160 161 ILE 161 162 ARG 162 163 ILE 163 164 PHE 164 165 MET 165 166 LEU 166 167 LEU 167 168 ALA 168 169 GLY 169 170 LEU 170 171 PRO 171 172 GLU 172 173 GLU 173 174 ASP 174 175 ILE 175 176 PRO 176 177 HIS 177 178 LEU 178 179 LYS 179 180 TYR 180 181 LEU 181 182 THR 182 183 ASP 183 184 GLN 184 185 MET 185 186 THR 186 187 ARG 187 188 PRO 188 189 ASP 189 190 GLY 190 191 SER 191 192 MET 192 193 THR 193 194 PHE 194 195 ALA 195 196 GLU 196 197 ALA 197 198 LYS 198 199 GLU 199 200 ALA 200 201 LEU 201 202 TYR 202 203 ASP 203 204 TYR 204 205 LEU 205 206 ILE 206 207 PRO 207 208 ILE 208 209 ILE 209 210 GLU 210 211 GLN 211 212 ARG 212 213 ARG 213 214 GLN 214 215 LYS 215 216 PRO 216 217 GLY 217 218 THR 218 219 ASP 219 220 ALA 220 221 ILE 221 222 SER 222 223 ILE 223 224 VAL 224 225 ALA 225 226 ASN 226 227 GLY 227 228 GLN 228 229 VAL 229 230 ASN 230 231 GLY 231 232 ARG 232 233 PRO 233 234 ILE 234 235 THR 235 236 SER 236 237 ASP 237 238 GLU 238 239 ALA 239 240 LYS 240 241 ARG 241 242 MET 242 243 CYS 243 244 GLY 244 245 LEU 245 246 LEU 246 247 LEU 247 248 VAL 248 249 GLY 249 250 GLY 250 251 LEU 251 252 ASP 252 253 THR 253 254 VAL 254 255 VAL 255 256 ASN 256 257 PHE 257 258 LEU 258 259 SER 259 260 PHE 260 261 SER 261 262 MET 262 263 GLU 263 264 PHE 264 265 LEU 265 266 ALA 266 267 LYS 267 268 SER 268 269 PRO 269 270 GLU 270 271 HIS 271 272 ARG 272 273 GLN 273 274 GLU 274 275 LEU 275 276 ILE 276 277 GLU 277 278 ARG 278 279 PRO 279 280 GLU 280 281 ARG 281 282 ILE 282 283 PRO 283 284 ALA 284 285 ALA 285 286 CYS 286 287 GLU 287 288 GLU 288 289 LEU 289 290 LEU 290 291 ARG 291 292 ARG 292 293 PHE 293 294 SER 294 295 LEU 295 296 VAL 296 297 ALA 297 298 ASP 298 299 GLY 299 300 ARG 300 301 ILE 301 302 LEU 302 303 THR 303 304 SER 304 305 ASP 305 306 TYR 306 307 GLU 307 308 PHE 308 309 HIS 309 310 GLY 310 311 VAL 311 312 GLN 312 313 LEU 313 314 LYS 314 315 LYS 315 316 GLY 316 317 ASP 317 318 GLN 318 319 ILE 319 320 LEU 320 321 LEU 321 322 PRO 322 323 GLN 323 324 MET 324 325 LEU 325 326 SER 326 327 GLY 327 328 LEU 328 329 ASP 329 330 GLU 330 331 ARG 331 332 GLU 332 333 ASN 333 334 ALA 334 335 ALA 335 336 PRO 336 337 MET 337 338 HIS 338 339 VAL 339 340 ASP 340 341 PHE 341 342 SER 342 343 ARG 343 344 GLN 344 345 LYS 345 346 VAL 346 347 SER 347 348 HIS 348 349 THR 349 350 THR 350 351 PHE 351 352 GLY 352 353 HIS 353 354 GLY 354 355 SER 355 356 HIS 356 357 LEU 357 358 CYS 358 359 LEU 359 360 GLY 360 361 GLN 361 362 HIS 362 363 LEU 363 364 ALA 364 365 ARG 365 366 ARG 366 367 GLU 367 368 ILE 368 369 ILE 369 370 VAL 370 371 THR 371 372 LEU 372 373 LYS 373 374 GLU 374 375 TRP 375 376 LEU 376 377 THR 377 378 ARG 378 379 ILE 379 380 PRO 380 381 ASP 381 382 PHE 382 383 SER 383 384 ILE 384 385 ALA 385 386 PRO 386 387 GLY 387 388 ALA 388 389 GLN 389 390 ILE 390 391 GLN 391 392 HIS 392 393 LYS 393 394 SER 394 395 GLY 395 396 ILE 396 397 VAL 397 398 SER 398 399 GLY 399 400 VAL 400 401 GLN 401 402 ALA 402 403 LEU 403 404 PRO 404 405 LEU 405 406 VAL 406 407 TRP 407 408 ASP 408 409 PRO 409 410 ALA 410 411 THR 411 412 THR 412 413 LYS 413 414 ALA 414 415 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 16753 P450cam 100.00 414 99.52 99.76 0.00e+00 BMRB 17415 entity_1 99.76 413 99.76 99.76 0.00e+00 BMRB 19038 entity_1 97.58 404 99.50 99.75 0.00e+00 BMRB 19763 CYP101 100.00 414 100.00 100.00 0.00e+00 PDB 1AKD "Cytochrome P450cam From Pseudomonas Putida, Complexed With 1s-Camphor" 100.00 414 99.52 99.76 0.00e+00 PDB 1C8J "Crystal Structure Of Cytochrome P450cam Mutant (F87wY96F)" 100.00 414 99.28 99.76 0.00e+00 PDB 1CP4 "Formation, Crystal Structure, And Rearrangement Of A Cytochrome P450-Cam Iron-Phenyl Complex" 100.00 414 99.76 99.76 0.00e+00 PDB 1DZ4 "Ferric P450cam From Pseudomonas Putida" 100.00 414 99.52 99.76 0.00e+00 PDB 1DZ6 "Ferrous P450cam From Pseudomonas Putida" 100.00 414 99.52 99.76 0.00e+00 PDB 1DZ8 "Oxygen Complex Of P450cam From Pseudomonas Putida" 100.00 414 99.52 99.76 0.00e+00 PDB 1DZ9 "Putative Oxo Complex Of P450cam From Pseudomonas Putida" 100.00 414 99.52 99.76 0.00e+00 PDB 1GEB "X-Ray Crystal Structure And Catalytic Properties Of Thr252ile Mutant Of Cytochrome P450cam" 100.00 415 99.52 99.52 0.00e+00 PDB 1GEK "Structural Characterization Of N-Butyl-Isocyanide Complexes Of Cytochromes P450nor And P450cam" 100.00 415 99.76 99.76 0.00e+00 PDB 1GEM "Structural Characterization Of N-Butyl-Isocyanide Complexes Of Cytochromes P450nor And P450cam" 100.00 415 99.76 99.76 0.00e+00 PDB 1GJM "Covalent Attachment Of An Electroactive Sulphydryl Reagent In The Active Site Of Cytochrome P450cam" 100.00 414 100.00 100.00 0.00e+00 PDB 1IWI "Putidaredoxin-Binding Stablilizes An Active Conformer Of Cytochrome P450cam In Its Reduced State; Crystal Structure Of Cytochro" 100.00 415 99.76 99.76 0.00e+00 PDB 1IWJ "Putidaredoxin-Binding Stablilizes An Active Conformer Of Cytochrome P450cam In Its Reduced State; Crystal Structure Of Mutant(1" 100.00 415 99.52 99.76 0.00e+00 PDB 1IWK "Putidaredoxin-Binding Stablilizes An Active Conformer Of Cytochrome P450cam In Its Reduced State; Crystal Structure Of Mutant(1" 100.00 415 99.52 99.76 0.00e+00 PDB 1J51 "Crystal Structure Of Cytochrome P450cam Mutant (F87wY96FV247LC334A) WITH 1,3,5-Trichlorobenzene" 100.00 414 99.28 100.00 0.00e+00 PDB 1K2O "Cytochrome P450cam With Bound Bis(2,2'-Bipyridine)-(5-Methyl-2-2'- Bipyridine)-C2-Adamantane Ruthenium (Ii)" 100.00 414 100.00 100.00 0.00e+00 PDB 1LWL "Crystal Structure Of Cytochrome P450-Cam With A Fluorescent Probe D-8-Ad (Adamantane-1-Carboxylic Acid-5-Dimethylamino- Naphtha" 100.00 417 99.76 99.76 0.00e+00 PDB 1MPW "Molecular Recognition In (+)-a-pinene Oxidation By Cytochrome P450cam" 100.00 414 99.28 100.00 0.00e+00 PDB 1NOO "Cytochrome P450-Cam Complexed With 5-Exo-Hydroxycamphor" 100.00 414 99.76 99.76 0.00e+00 PDB 1O76 "Cyanide Complex Of P450cam From Pseudomonas Putida" 100.00 414 99.52 99.76 0.00e+00 PDB 1P2Y "Crystal Structure Of Cytochrome P450cam In Complex With (S)- (-)-Nicotine" 100.00 420 99.76 99.76 0.00e+00 PDB 1P7R "Crystal Structure Of Reduced, Co-Exposed Complex Of Cytochrome P450cam With (S)-(-)-Nicotine" 100.00 420 99.76 99.76 0.00e+00 PDB 1PHA "Inhibitor-Induced Conformational Change In Cytochrome P450- Cam" 100.00 414 99.76 99.76 0.00e+00 PDB 1PHB "Inhibitor-Induced Conformational Change In Cytochrome P450- Cam" 100.00 414 99.76 99.76 0.00e+00 PDB 1PHC "Crystal Structure Of Substrate-free Pseudomonas Putida Cytochrome P450" 100.00 414 99.76 99.76 0.00e+00 PDB 1PHD "Crystal Structures Of Metyrapone-And Phenylimidazole-Inhibited Complexes Of Cytochrome P450-Cam" 100.00 414 99.76 99.76 0.00e+00 PDB 1PHE "Crystal Structures Of Metyrapone-And Phenylimidazole-Inhibited Complexes Of Cytochrome P450-Cam" 100.00 414 99.76 99.76 0.00e+00 PDB 1PHF "Crystal Structures Of Metyrapone-And Phenylimidazole- Inhibited Complexes Of Cytochrome P450-Cam" 100.00 414 99.76 99.76 0.00e+00 PDB 1PHG "Crystal Structures Of Metyrapone-And Phenylimidazole- Inhibited Complexes Of Cytochrome P450-Cam" 100.00 414 99.76 99.76 0.00e+00 PDB 1QMQ "Optical Detection Of Cytochrome P450 By Sensitizer-Linked Substrates" 100.00 414 100.00 100.00 0.00e+00 PDB 1RE9 "Crystal Structure Of Cytochrome P450-cam With A Fluorescent Probe D-8-ad (adamantane-1-carboxylic Acid-5-dimethylamino- Naphtha" 100.00 414 99.76 99.76 0.00e+00 PDB 1RF9 "Crystal Structure Of Cytochrome P450-Cam With A Fluorescent Probe D-4-Ad (Adamantane-1-Carboxylic Acid-5-Dimethylamino- Naphtha" 100.00 417 99.76 99.76 0.00e+00 PDB 1T85 "Crystal Structure Of The Ferrous Co-Bound Cytochrome P450cam Mutant (L358pC334A)" 100.00 414 99.76 99.76 0.00e+00 PDB 1T86 "Crystal Structure Of The Ferrous Cytochrome P450cam Mutant (L358pC334A)" 100.00 414 99.76 99.76 0.00e+00 PDB 1T87 "Crystal Structure Of The Ferrous Co-Bound Cytochrome P450cam (C334a)" 100.00 414 100.00 100.00 0.00e+00 PDB 1T88 "Crystal Structure Of The Ferrous Cytochrome P450cam (C334a)" 100.00 414 100.00 100.00 0.00e+00 PDB 1UYU "Xenon Complex Of Wildtype P450cam From Pseudomonas Putida" 100.00 414 99.52 99.76 0.00e+00 PDB 1YRC "X-ray Crystal Structure Of Hydrogenated Cytochrome P450cam" 100.00 414 99.76 99.76 0.00e+00 PDB 1YRD "X-Ray Crystal Structure Of Perdeuterated Cytochrome P450cam" 100.00 414 99.76 99.76 0.00e+00 PDB 2A1M "Crystal Structure Of Ferrous Dioxygen Complex Of Wild-Type Cytochrome P450cam" 100.00 415 100.00 100.00 0.00e+00 PDB 2A1N "Crystal Structure Of Ferrous Dioxygen Complex Of D251n Cytochrome P450cam" 100.00 415 99.76 100.00 0.00e+00 PDB 2A1O "Crystal Structure Of Ferrous Dioxygen Complex Of T252a Cytochrome P450cam" 100.00 415 99.76 99.76 0.00e+00 PDB 2CP4 "Crystal Structure Of The Cytochrome P450-Cam Active Site Mutant Thr252ala" 100.00 414 99.52 99.52 0.00e+00 PDB 2CPP "High-Resolution Crystal Structure Of Cytochrome P450-Cam" 100.00 414 99.76 99.76 0.00e+00 PDB 2FE6 "P450cam From Pseudomonas Putida Reconstituted With Manganic Protoporphyrin Ix" 100.00 421 99.76 99.76 0.00e+00 PDB 2FER "P450cam From Pseudomonas Putida Reconstituted With Manganic Protoporphyrin Ix" 97.83 411 99.75 99.75 0.00e+00 PDB 2FEU "P450cam From Pseudomonas Putida Reconstituted With Manganic Protoporphyrin Ix" 97.83 411 99.75 99.75 0.00e+00 PDB 2FRZ "Crystal Structure Of Cytochrome P450cam Mutant (F87wY96FV247LC334A)" 100.00 414 99.28 100.00 0.00e+00 PDB 2GQX "Crystal Structure Of Cytochrome P450cam Mutant (F87wY96FL244AV247LC334A) WITH PENTACHLOROBENZENE" 97.83 405 99.01 99.75 0.00e+00 PDB 2GR6 "Crystal Structure Of Cytochrome P450cam Mutant (F87wY96FL244AV247LC334A)" 97.83 405 99.01 99.75 0.00e+00 PDB 2H7Q "Cytochrome P450cam Complexed With Imidazole" 100.00 414 99.76 99.76 0.00e+00 PDB 2H7R "L244a Mutant Of Cytochrome P450cam Complexed With Imidazole" 100.00 414 99.76 99.76 0.00e+00 PDB 2H7S "L244a Mutant Of Cytochrome P450cam" 100.00 414 99.76 99.76 0.00e+00 PDB 2L8M "Reduced And Co-Bound Cytochrome P450cam (Cyp101a1)" 100.00 415 99.76 99.76 0.00e+00 PDB 2LQD "Reduced And Co-Bound Cytochrome P450cam (Cyp101a1)" 97.83 405 99.75 99.75 0.00e+00 PDB 2M56 "The Structure Of The Complex Of Cytochrome P450cam And Its Electron Donor Putidaredoxin Determined By Paramagnetic Nmr Spectros" 97.58 404 99.50 99.75 0.00e+00 PDB 2QBL "Crystal Structure Of Ferric G248t Cytochrome P450cam" 100.00 421 99.52 99.52 0.00e+00 PDB 2QBM "Crystal Structure Of The P450cam G248t Mutant In The Cyanide Bound State" 100.00 421 99.52 99.52 0.00e+00 PDB 2QBN "Crystal Structure Of Ferric G248v Cytochrome P450cam" 100.00 421 99.52 99.52 0.00e+00 PDB 2QBO "Crystal Structure Of The P450cam G248v Mutant In The Cyanide Bound State" 100.00 421 99.52 99.52 0.00e+00 PDB 2Z97 "Crystal Structure Of Ferric Cytochrome P450cam Reconstituted With 7- Methyl-7-Depropionated Hemin" 100.00 415 99.76 99.76 0.00e+00 PDB 2ZAW "Crystal Structure Of Ferric Cytochrome P450cam Reconstituted With 6- Methyl-6-Depropionated Hemin" 100.00 415 99.76 99.76 0.00e+00 PDB 2ZAX "Crystal Structure Of Ferric Cytochrome P450cam" 100.00 415 99.76 99.76 0.00e+00 PDB 2ZUH "Crystal Structure Of Camphor-Soaked Ferric Cytochrome P450cam Mutant (D297a)" 100.00 415 99.52 99.52 0.00e+00 PDB 2ZUI "Crystal Structure Of Camphor-Soaked Ferric Cytochrome P450cam Mutant (D297n)" 100.00 415 99.52 99.76 0.00e+00 PDB 2ZUJ "Crystal Structure Of Camphor-Soaked Ferric Cytochrome P450cam Mutant(D297l)" 100.00 415 99.52 99.52 0.00e+00 PDB 2ZWT "Crystal Structure Of Ferric Cytochrome P450cam" 100.00 415 99.76 99.76 0.00e+00 PDB 2ZWU "Crystal Structure Of Camphor Soaked Ferric Cytochrome P450cam" 100.00 415 99.76 99.76 0.00e+00 PDB 3CP4 "Crystal Structure Of The Cytochrome P450-Cam Active Site Mutant Thr252ala" 100.00 414 99.76 99.76 0.00e+00 PDB 3CPP "Crystal Structure Of The Carbon Monoxy-Substrate-Cytochrome P450-Cam Ternary Complex" 100.00 414 99.76 99.76 0.00e+00 PDB 3FWF "Ferric Camphor Bound Cytochrome P450cam Containing A Selenocysteine As The 5th Heme Ligand, Monoclinic Crystal Form" 97.83 405 98.77 99.26 0.00e+00 PDB 3FWG "Ferric Camphor Bound Cytochrome P450cam, Arg365leu, Glu366gln, Monoclinic Crystal Form" 97.83 405 99.01 99.51 0.00e+00 PDB 3FWI "Ferric Camphor Bound Cytochrome P450cam Containing A Selenocysteine As The 5th Heme Ligand, Tetragonal Crystal Form" 97.83 405 99.01 99.26 0.00e+00 PDB 3FWJ "Ferric Camphor Bound Cytochrome P450cam Containing A Selenocysteine As The 5th Heme Ligand, Orthorombic Crystal Form" 97.83 405 99.01 99.26 0.00e+00 PDB 3L61 "Crystal Structure Of Substrate-Free P450cam At 200 Mm [k+]" 100.00 414 100.00 100.00 0.00e+00 PDB 3L62 "Crystal Structure Of Substrate-Free P450cam At Low [k+]" 100.00 414 100.00 100.00 0.00e+00 PDB 3L63 "Crystal Structure Of Camphor-Bound P450cam At Low [k+]" 100.00 414 100.00 100.00 0.00e+00 PDB 3OIA "Crystal Structure Of Cytochrome P450cam Crystallized In The Presence Of A Tethered Substrate Analog Adac1-C8gluetg-Bio" 100.00 414 100.00 100.00 0.00e+00 PDB 3OL5 "Crystal Structure Of Cytochrome P450cam Crystallized With A Tethered Substrate Analog 3oh-Adac1-C8-Dans" 100.00 414 100.00 100.00 0.00e+00 PDB 3P6M "Crystal Structure Of Cytochrome P450cam Crystallized In The Presence Of A Tethered Substrate Analog Adac1-C8-Dans" 100.00 414 100.00 100.00 0.00e+00 PDB 3P6N "Crystal Structure Of Cytochrome P450cam Crystallized In The Presence Of A Tethered Substrate Analog Adac1-C8-Dans" 100.00 414 100.00 100.00 0.00e+00 PDB 3P6O "Crystal Structure Of Cytochrome P450cam Crystallized In The Presence Of A Tethered Substrate Analog Adac1-Etg-Dans" 100.00 414 100.00 100.00 0.00e+00 PDB 3P6P "Crystal Structure Of Cytochrome P450cam Crystallized In The Presence Of A Tethered Substrate Analog Adac1-C6-Bio" 100.00 414 100.00 100.00 0.00e+00 PDB 3P6Q "Crystal Structure Of Cytochrome P450cam Crystallized In The Presence Of A Tethered Substrate Analog Adac2-Etg-Boc" 100.00 414 100.00 100.00 0.00e+00 PDB 3P6R "Crystal Structure Of Cytochrome P450cam Crystallized In The Presence Of A Tethered Substrate Analog 3oh-Adac1-Etg-Boc" 100.00 414 100.00 100.00 0.00e+00 PDB 3P6S "Crystal Structure Of Cytochrome P450cam Crystallized In The Presence Of A Tethered Substrate Analog Adac2-C8-Dans" 100.00 414 100.00 100.00 0.00e+00 PDB 3P6T "Crystal Structure Of Cytochrome P450cam Crystallized In The Presence Of A Tethered Substrate Analog Adac2-C8-Dans" 100.00 414 100.00 100.00 0.00e+00 PDB 3P6U "Crystal Structure Of Cytochrome P450cam Crystallized In The Presence Of A Tethered Substrate Analog Adac3-C6-Dans" 100.00 414 100.00 100.00 0.00e+00 PDB 3P6V "Crystal Structure Of Cytochrome P450cam Crystallized In The Presence Of A Tethered Substrate Analog 3et-Adac1-Etg-Boc" 100.00 414 100.00 100.00 0.00e+00 PDB 3P6W "Crystal Structure Of Cytochrome P450cam Crystallized In The Presence Of A Tethered Substrate Analog Adac3-Etg-Boc" 100.00 414 100.00 100.00 0.00e+00 PDB 3P6X "Crystal Structure Of Cytochrome P450cam Crystallized In The Presence Of A Tethered Substrate Analog Adac3-C8-Dans" 100.00 414 100.00 100.00 0.00e+00 PDB 3W9C "Crystal Structure Of The Electron Transfer Complex Of Cytochrome P450cam With Putidaredoxin" 100.00 416 99.52 99.52 0.00e+00 PDB 3WRH "Crystal Structure Of P450cam" 100.00 421 99.76 99.76 0.00e+00 PDB 3WRI "Crystal Structure Of P450cam" 100.00 421 99.76 99.76 0.00e+00 PDB 3WRJ "Crystal Structure Of P450cam" 100.00 421 99.76 99.76 0.00e+00 PDB 3WRK "Crystal Structure Of P450cam" 100.00 421 99.76 99.76 0.00e+00 PDB 3WRL "Crystal Structure Of P450cam" 100.00 421 99.76 99.76 0.00e+00 PDB 3WRM "Crystal Structure Of P450cam" 100.00 421 99.76 99.76 0.00e+00 PDB 4CP4 "Crystal Structure Of The Cytochrome P450-Cam Active Site Mutant Thr252ala" 100.00 414 99.76 99.76 0.00e+00 PDB 4CPP "Crystal Structures Of Cytochrome P450-Cam Complexed With Camphane, Thiocamphor, And Adamantane: Factors Controlling P450 Substr" 100.00 414 99.76 99.76 0.00e+00 PDB 4EK1 "Crystal Structure Of Electron-Spin Labeled Cytochrome P450cam" 100.00 414 98.55 98.55 0.00e+00 PDB 4G3R "Crystal Structure Of Nitrosyl Cytochrome P450cam" 100.00 414 100.00 100.00 0.00e+00 PDB 4JWS "Crystal Structure Of Cytochrome P450cam-putidaredoxin Complex" 100.00 415 98.79 98.79 0.00e+00 PDB 4JWU "Crystal Structure Of Cytochrome P450cam-putidaredoxin Complex" 100.00 415 98.79 98.79 0.00e+00 PDB 4JX1 "Crystal Structure Of Reduced Cytochrome P450cam-putidaredoxin Complex Bound To Camphor And 5-exo-hydroxycamphor" 100.00 415 98.79 98.79 0.00e+00 PDB 4KKY "Crystal Structure Of N-(1-pyrene)acetamide Labeled P450cam In Substrate Bound Form" 99.76 413 98.55 98.55 0.00e+00 PDB 4L49 "Structure Of L358a Mutant Of P450cam Bound To Camphor" 100.00 415 99.76 99.76 0.00e+00 PDB 4L4A "Structure Of L358a/k178g Mutant Of P450cam Bound To Camphor" 100.00 415 99.52 99.52 0.00e+00 PDB 4L4B "Structure Of L358a/k178g/d182n Mutant Of P450cam Bound To Camphor" 100.00 415 99.28 99.52 0.00e+00 PDB 4L4C "Structure Of L358p/k178g Mutant Of P450cam Bound To Camphor" 100.00 415 99.52 99.52 0.00e+00 PDB 4L4D "Structure Of Cyanide And Camphor Bound P450cam Mutant L358a" 100.00 415 99.76 99.76 0.00e+00 PDB 4L4E "Structure Of Cyanide And Camphor Bound P450cam Mutant L358a/k178g" 100.00 415 99.52 99.52 0.00e+00 PDB 4L4F "Structure Of Cyanide And Camphor Bound P450cam Mutant L358a/k178g/d182n" 100.00 415 99.28 99.52 0.00e+00 PDB 4L4G "Structure Of Cyanide And Camphor Bound P450cam Mutant L358p/k178g" 100.00 415 99.52 99.52 0.00e+00 PDB 5CP4 "Cryogenic Structure Of P450cam" 100.00 414 99.76 99.76 0.00e+00 PDB 5CPP "The Structural Basis For Substrate-Induced Changes In Redox Potential And Spin Equilibrium In Cytochrome P-450(Cam)" 100.00 414 99.76 99.76 0.00e+00 PDB 6CP4 "P450cam D251n Mutant" 100.00 414 99.52 99.76 0.00e+00 PDB 6CPP "Crystal Structures Of Cytochrome P450-Cam Complexed With Camphane, Thiocamphor, And Adamantane: Factors Controlling P450 Substr" 100.00 414 99.76 99.76 0.00e+00 PDB 7CPP "The Structural Basis For Substrate-Induced Changes In Redox Potential And Spin Equilibrium In Cytochrome P450(Cam)" 100.00 414 99.76 99.76 0.00e+00 PDB 8CPP "Crystal Structures Of Cytochrome P450-Cam Complexed With Camphane, Thiocamphor, And Adamantane: Factors Controlling P450 Substr" 100.00 414 99.76 99.76 0.00e+00 DBJ BAN13286 "cytochrome P-450cam [Pseudomonas putida]" 100.00 415 99.76 99.76 0.00e+00 GB AAA25760 "cytochrome P-450-cam [Pseudomonas putida]" 100.00 415 99.76 99.76 0.00e+00 REF WP_032492633 "camphor 5-monooxygenase [Pseudomonas putida]" 100.00 415 99.76 99.76 0.00e+00 REF YP_009083112 "cytochrome P-450cam [Pseudomonas putida]" 100.00 415 99.76 99.76 0.00e+00 SP P00183 "RecName: Full=Camphor 5-monooxygenase; AltName: Full=Cytochrome P450-cam; Short=Cytochrome P450cam" 100.00 415 99.76 99.76 0.00e+00 stop_ save_ ############# # Ligands # ############# save_HEM _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "entity_HEM (PROTOPORPHYRIN IX CONTAINING FE)" _BMRB_code HEM _PDB_code HEM _Molecular_mass 616.487 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CHA CHA C . 0 . ? CHB CHB C . 0 . ? CHC CHC C . 0 . ? CHD CHD C . 0 . ? C1A C1A C . 0 . ? C2A C2A C . 0 . ? C3A C3A C . 0 . ? C4A C4A C . 0 . ? CMA CMA C . 0 . ? CAA CAA C . 0 . ? CBA CBA C . 0 . ? CGA CGA C . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? C1B C1B C . 0 . ? C2B C2B C . 0 . ? C3B C3B C . 0 . ? C4B C4B C . 0 . ? CMB CMB C . 0 . ? CAB CAB C . 0 . ? CBB CBB C . 0 . ? C1C C1C C . 0 . ? C2C C2C C . 0 . ? C3C C3C C . 0 . ? C4C C4C C . 0 . ? CMC CMC C . 0 . ? CAC CAC C . 0 . ? CBC CBC C . 0 . ? C1D C1D C . 0 . ? C2D C2D C . 0 . ? C3D C3D C . 0 . ? C4D C4D C . 0 . ? CMD CMD C . 0 . ? CAD CAD C . 0 . ? CBD CBD C . 0 . ? CGD CGD C . 0 . ? O1D O1D O . 0 . ? O2D O2D O . 0 . ? NA NA N . 0 . ? NB NB N . 0 . ? NC NC N . 0 . ? ND ND N . 0 . ? FE FE FE . 0 . ? HHB HHB H . 0 . ? HHC HHC H . 0 . ? HHD HHD H . 0 . ? HMA HMA H . 0 . ? HMAA HMAA H . 0 . ? HMAB HMAB H . 0 . ? HAA HAA H . 0 . ? HAAA HAAA H . 0 . ? HBA HBA H . 0 . ? HBAA HBAA H . 0 . ? HMB HMB H . 0 . ? HMBA HMBA H . 0 . ? HMBB HMBB H . 0 . ? HAB HAB H . 0 . ? HBB HBB H . 0 . ? HBBA HBBA H . 0 . ? HMC HMC H . 0 . ? HMCA HMCA H . 0 . ? HMCB HMCB H . 0 . ? HAC HAC H . 0 . ? HBC HBC H . 0 . ? HBCA HBCA H . 0 . ? HMD HMD H . 0 . ? HMDA HMDA H . 0 . ? HMDB HMDB H . 0 . ? HAD HAD H . 0 . ? HADA HADA H . 0 . ? HBD HBD H . 0 . ? HBDA HBDA H . 0 . ? H2A H2A H . 0 . ? H2D H2D H . 0 . ? HHA HHA H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING CHA C1A ? ? DOUB CHA C4D ? ? SING CHA HHA ? ? SING CHB C4A ? ? DOUB CHB C1B ? ? SING CHB HHB ? ? SING CHC C4B ? ? DOUB CHC C1C ? ? SING CHC HHC ? ? DOUB CHD C4C ? ? SING CHD C1D ? ? SING CHD HHD ? ? DOUB C1A C2A ? ? SING C1A NA ? ? SING C2A C3A ? ? SING C2A CAA ? ? DOUB C3A C4A ? ? SING C3A CMA ? ? SING C4A NA ? ? SING CMA HMA ? ? SING CMA HMAA ? ? SING CMA HMAB ? ? SING CAA CBA ? ? SING CAA HAA ? ? SING CAA HAAA ? ? SING CBA CGA ? ? SING CBA HBA ? ? SING CBA HBAA ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING C1B C2B ? ? SING C1B NB ? ? DOUB C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? SING C3B CAB ? ? DOUB C4B NB ? ? SING CMB HMB ? ? SING CMB HMBA ? ? SING CMB HMBB ? ? DOUB CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB ? ? SING CBB HBBA ? ? SING C1C C2C ? ? SING C1C NC ? ? DOUB C2C C3C ? ? SING C2C CMC ? ? SING C3C C4C ? ? SING C3C CAC ? ? SING C4C NC ? ? SING CMC HMC ? ? SING CMC HMCA ? ? SING CMC HMCB ? ? DOUB CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC ? ? SING CBC HBCA ? ? SING C1D C2D ? ? DOUB C1D ND ? ? DOUB C2D C3D ? ? SING C2D CMD ? ? SING C3D C4D ? ? SING C3D CAD ? ? SING C4D ND ? ? SING CMD HMD ? ? SING CMD HMDA ? ? SING CMD HMDB ? ? SING CAD CBD ? ? SING CAD HAD ? ? SING CAD HADA ? ? SING CBD CGD ? ? SING CBD HBD ? ? SING CBD HBDA ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2A H2A ? ? SING O2D H2D ? ? SING FE NA ? ? SING FE NB ? ? SING FE NC ? ? SING FE ND ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_CAM _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "entity_CAM (CAMPHOR)" _BMRB_code CAM _PDB_code CAM _Molecular_mass 152.233 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C2 C2 C . 0 . ? O O O . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? C8 C8 C . 0 . ? C9 C9 C . 0 . ? C10 C10 C . 0 . ? H31 H31 H . 0 . ? H32 H32 H . 0 . ? H4 H4 H . 0 . ? H51 H51 H . 0 . ? H52 H52 H . 0 . ? H61 H61 H . 0 . ? H62 H62 H . 0 . ? H81 H81 H . 0 . ? H82 H82 H . 0 . ? H83 H83 H . 0 . ? H91 H91 H . 0 . ? H92 H92 H . 0 . ? H93 H93 H . 0 . ? H101 H101 H . 0 . ? H102 H102 H . 0 . ? H103 H103 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING C1 C2 ? ? SING C1 C6 ? ? SING C1 C7 ? ? SING C1 C10 ? ? DOUB C2 O ? ? SING C2 C3 ? ? SING C3 C4 ? ? SING C3 H31 ? ? SING C3 H32 ? ? SING C4 C5 ? ? SING C4 C7 ? ? SING C4 H4 ? ? SING C5 C6 ? ? SING C5 H51 ? ? SING C5 H52 ? ? SING C6 H61 ? ? SING C6 H62 ? ? SING C7 C8 ? ? SING C7 C9 ? ? SING C8 H81 ? ? SING C8 H82 ? ? SING C8 H83 ? ? SING C9 H91 ? ? SING C9 H92 ? ? SING C9 H93 ? ? SING C10 H101 ? ? SING C10 H102 ? ? SING C10 H103 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_CYN _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'CYANIDE ION' _BMRB_code CYN _PDB_code CYN _Molecular_mass 26.017 _Mol_charge -1 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . -1 . ? N N N . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name TRIP C N ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CYP101 'Pseudomonas putida' 303 Bacteria . Pseudomonas putida 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 _Details $CYP101 'recombinant technology' 'Escherichia coli' Escherichia coli 'BL21 DE3' pLysS 'pET28a Xho1/Nco1 restriction sites, Kanamycin resistance' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '1 % methanol, 6 % D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CYP101 0.53 mM '[U-13C; U-15N; U-2H]' HEPES 20 mM 'natural abundance' NaCN 100 mM 'natural abundance' camphor 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CcpNmr_Analysis _Saveframe_category software _Name CcpNmr_Analysis _Version 2.1 loop_ _Vendor _Address _Electronic_address CCPN 'Department of Biochemistry, Cambridge CB2 1GA, UK' http://www.ccpn.ac.uk stop_ loop_ _Task 'Spectrum analysis' stop_ _Details 'The CCPN NMR assignment and data analysis application' save_ save_Topspin _Saveframe_category software _Name Topspin _Version 2.1 loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task 'Data acquisition' 'Spectrum processing' stop_ _Details . save_ save_nmrPipe _Saveframe_category software _Name nmrPipe _Version any loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'Spectrum processing' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_Bruker_AVANCE_I_800 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_Bruker_AVANCE_III_950 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 950 _Details . save_ ############################# # NMR applied experiments # ############################# save_TROSY-HNcoCACB_(H[N[co[{CA|ca[C]}]]])_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY-HNcoCACB (H[N[co[{CA|ca[C]}]]])' _Sample_label $sample_1 save_ save_3D_TROSY-HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCACB' _Sample_label $sample_1 save_ save_2D_1H-15N_TROSY-HSQC/HMQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY-HSQC/HMQC' _Sample_label $sample_1 save_ save_TROSY-HNCACO_(H[N[ca[CO]]])_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY-HNCACO (H[N[ca[CO]]])' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC/HMQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC/HMQC' _Sample_label $sample_1 save_ save_3D_TROSY-HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCO' _Sample_label $sample_1 save_ save_2D_1H-15N_TROSY-HSQC/HMQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY-HSQC/HMQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_p450camcn _Saveframe_category sample_conditions _Details 'buffer; 20 mM HEPES, pH=7.4, 100 mM NaCN, 1 mM camphor, 1 % methanol, 6 % D2O' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100.000 . mM pH 7.400 . pH pressure 1.000 . atm temperature 298.000 . 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 4.76 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D TROSY-HNCACB' '2D 1H-15N TROSY-HSQC/HMQC' 'TROSY-HNcoCACB (H[N[co[{CA|ca[C]}]]])' 'TROSY-HNCACO (H[N[ca[CO]]])' '3D TROSY-HNCO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $p450camcn _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name CYP101 _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 4 3 GLU H H 8.437 0.002 . 2 4 3 GLU C C 176.543 0.008 . 3 4 3 GLU CA C 56.316 0.029 . 4 4 3 GLU CB C 29.462 0.024 . 5 4 3 GLU N N 123.877 0.039 . 6 5 4 THR H H 8.191 0.003 . 7 5 4 THR C C 174.471 0.005 . 8 5 4 THR CA C 61.650 0.024 . 9 5 4 THR CB C 69.249 0.001 . 10 5 4 THR N N 116.427 0.118 . 11 6 5 ILE H H 8.143 0.002 . 12 6 5 ILE C C 176.208 0.005 . 13 6 5 ILE CA C 60.741 0.015 . 14 6 5 ILE CB C 37.670 0.006 . 15 6 5 ILE N N 124.164 0.038 . 16 7 6 GLN H H 8.408 0.002 . 17 7 6 GLN HE21 H 6.864 0.009 . 18 7 6 GLN HE22 H 6.772 0.001 . 19 7 6 GLN C C 175.952 0.000 . 20 7 6 GLN CA C 55.330 0.015 . 21 7 6 GLN CB C 28.652 0.029 . 22 7 6 GLN CG C 32.917 0.002 . 23 7 6 GLN CD C 180.581 0.051 . 24 7 6 GLN N N 125.009 0.037 . 25 7 6 GLN NE2 N 113.537 0.057 . 26 8 7 SER H H 8.307 0.002 . 27 8 7 SER C C 174.319 0.000 . 28 8 7 SER CA C 57.972 0.013 . 29 8 7 SER CB C 63.006 0.063 . 30 8 7 SER N N 117.770 0.035 . 31 9 8 ASN H H 8.364 0.002 . 32 9 8 ASN C C 174.971 0.000 . 33 9 8 ASN CA C 52.760 0.000 . 34 9 8 ASN CB C 38.264 0.000 . 35 9 8 ASN N N 121.167 0.043 . 36 12 11 LEU H H 10.272 0.004 . 37 12 11 LEU CA C 62.071 0.000 . 38 12 11 LEU CB C 40.985 0.016 . 39 12 11 LEU N N 125.334 0.048 . 40 13 12 ALA H H 7.650 0.002 . 41 13 12 ALA C C 176.724 0.000 . 42 13 12 ALA CA C 50.225 0.000 . 43 13 12 ALA CB C 20.506 0.000 . 44 13 12 ALA N N 128.171 0.037 . 45 17 16 PRO C C 176.991 0.002 . 46 17 16 PRO CA C 64.094 0.000 . 47 17 16 PRO CB C 31.176 0.000 . 48 18 17 HIS H H 7.662 0.002 . 49 18 17 HIS CA C 55.826 0.023 . 50 18 17 HIS CB C 30.137 0.000 . 51 18 17 HIS N N 111.373 0.041 . 52 19 18 VAL H H 6.827 0.002 . 53 19 18 VAL C C 172.689 0.000 . 54 19 18 VAL CA C 59.833 0.000 . 55 19 18 VAL CB C 31.151 0.000 . 56 19 18 VAL N N 127.218 0.039 . 57 20 19 PRO C C 178.378 0.000 . 58 20 19 PRO CA C 61.234 0.025 . 59 20 19 PRO CB C 31.630 0.000 . 60 21 20 GLU H H 8.629 0.002 . 61 21 20 GLU C C 178.662 0.034 . 62 21 20 GLU CA C 59.179 0.006 . 63 21 20 GLU CB C 28.658 0.045 . 64 21 20 GLU N N 121.026 0.039 . 65 22 21 HIS H H 7.874 0.001 . 66 22 21 HIS CA C 57.789 0.001 . 67 22 21 HIS CB C 28.615 0.000 . 68 22 21 HIS N N 113.708 0.036 . 69 23 22 LEU H H 7.192 0.002 . 70 23 22 LEU C C 175.657 0.018 . 71 23 22 LEU CA C 53.488 0.019 . 72 23 22 LEU CB C 40.287 0.037 . 73 23 22 LEU N N 119.247 0.039 . 74 24 23 VAL H H 7.104 0.002 . 75 24 23 VAL C C 177.015 0.027 . 76 24 23 VAL CA C 62.856 0.026 . 77 24 23 VAL CB C 30.756 0.013 . 78 24 23 VAL N N 120.407 0.037 . 79 25 24 PHE H H 9.192 0.002 . 80 25 24 PHE C C 174.597 0.018 . 81 25 24 PHE CA C 57.732 0.021 . 82 25 24 PHE CB C 39.763 0.089 . 83 25 24 PHE N N 133.220 0.037 . 84 26 25 ASP H H 8.161 0.002 . 85 26 25 ASP C C 174.891 0.022 . 86 26 25 ASP CA C 55.227 0.013 . 87 26 25 ASP CB C 39.491 0.000 . 88 26 25 ASP N N 126.037 0.039 . 89 27 26 PHE H H 8.278 0.002 . 90 27 26 PHE C C 175.169 0.019 . 91 27 26 PHE CA C 57.482 0.005 . 92 27 26 PHE CB C 40.832 0.022 . 93 27 26 PHE N N 124.841 0.039 . 94 28 27 ASP H H 8.163 0.002 . 95 28 27 ASP C C 174.813 0.000 . 96 28 27 ASP CA C 51.373 0.000 . 97 28 27 ASP CB C 40.190 0.000 . 98 28 27 ASP N N 133.025 0.038 . 99 30 29 TYR H H 7.953 0.002 . 100 30 29 TYR C C 175.632 0.018 . 101 30 29 TYR CA C 59.183 0.038 . 102 30 29 TYR CB C 38.139 0.019 . 103 30 29 TYR N N 118.066 0.043 . 104 31 30 ASN H H 6.854 0.002 . 105 31 30 ASN C C 169.334 0.000 . 106 31 30 ASN CA C 51.609 0.000 . 107 31 30 ASN CB C 38.372 0.000 . 108 31 30 ASN N N 116.348 0.044 . 109 32 31 PRO C C 178.509 0.000 . 110 32 31 PRO CA C 62.481 0.000 . 111 32 31 PRO CB C 30.815 0.000 . 112 33 32 SER H H 7.885 0.002 . 113 33 32 SER C C 175.152 0.002 . 114 33 32 SER CA C 59.841 0.005 . 115 33 32 SER CB C 62.364 0.014 . 116 33 32 SER N N 118.009 0.040 . 117 34 33 ASN H H 8.777 0.002 . 118 34 33 ASN C C 175.265 0.002 . 119 34 33 ASN CA C 53.206 0.023 . 120 34 33 ASN CB C 37.177 0.038 . 121 34 33 ASN N N 117.918 0.041 . 122 35 34 LEU H H 7.299 0.002 . 123 35 34 LEU C C 178.321 0.003 . 124 35 34 LEU CA C 57.114 0.032 . 125 35 34 LEU CB C 41.267 0.032 . 126 35 34 LEU N N 119.879 0.039 . 127 36 35 SER H H 8.572 0.002 . 128 36 35 SER C C 174.744 0.012 . 129 36 35 SER CA C 60.262 0.030 . 130 36 35 SER CB C 61.945 0.003 . 131 36 35 SER N N 114.317 0.041 . 132 37 36 ALA H H 7.799 0.002 . 133 37 36 ALA C C 176.882 0.006 . 134 37 36 ALA CA C 52.443 0.009 . 135 37 36 ALA CB C 18.328 0.013 . 136 37 36 ALA N N 124.311 0.039 . 137 38 37 GLY H H 7.429 0.002 . 138 38 37 GLY C C 175.838 0.000 . 139 38 37 GLY CA C 42.741 0.000 . 140 38 37 GLY N N 109.422 0.041 . 141 39 38 VAL C C 176.587 0.000 . 142 39 38 VAL CA C 66.683 0.000 . 143 39 38 VAL CB C 31.302 0.000 . 144 40 39 GLN H H 7.632 0.002 . 145 40 39 GLN C C 177.605 0.018 . 146 40 39 GLN CA C 61.749 0.035 . 147 40 39 GLN CB C 24.359 0.000 . 148 40 39 GLN N N 122.165 0.044 . 149 41 40 GLU H H 9.655 0.001 . 150 41 40 GLU C C 179.368 0.006 . 151 41 40 GLU CA C 60.796 0.019 . 152 41 40 GLU CB C 27.227 0.006 . 153 41 40 GLU N N 120.325 0.039 . 154 42 41 ALA H H 8.531 0.002 . 155 42 41 ALA C C 181.017 0.019 . 156 42 41 ALA CA C 54.436 0.009 . 157 42 41 ALA CB C 17.032 0.012 . 158 42 41 ALA N N 122.816 0.036 . 159 43 42 TRP H H 8.374 0.002 . 160 43 42 TRP C C 177.635 0.000 . 161 43 42 TRP CA C 60.540 0.000 . 162 43 42 TRP CB C 27.347 0.030 . 163 43 42 TRP N N 120.138 0.038 . 164 44 43 ALA H H 8.242 0.001 . 165 44 43 ALA C C 179.634 0.006 . 166 44 43 ALA CA C 53.645 0.040 . 167 44 43 ALA CB C 16.581 0.000 . 168 44 43 ALA N N 120.178 0.040 . 169 45 44 VAL H H 7.058 0.002 . 170 45 44 VAL C C 177.409 0.000 . 171 45 44 VAL CA C 64.205 0.031 . 172 45 44 VAL CB C 30.088 0.021 . 173 45 44 VAL N N 119.413 0.039 . 174 46 45 LEU H H 7.496 0.002 . 175 46 45 LEU C C 174.557 0.001 . 176 46 45 LEU CA C 55.387 0.016 . 177 46 45 LEU CB C 40.607 0.017 . 178 46 45 LEU N N 119.104 0.068 . 179 47 46 GLN H H 7.426 0.002 . 180 47 46 GLN C C 176.509 0.048 . 181 47 46 GLN CA C 53.383 0.065 . 182 47 46 GLN CB C 27.673 0.037 . 183 47 46 GLN N N 111.894 0.039 . 184 48 47 GLU H H 6.840 0.000 . 185 48 47 GLU C C 177.982 0.003 . 186 48 47 GLU CA C 56.872 0.008 . 187 48 47 GLU CB C 29.557 0.014 . 188 48 47 GLU N N 120.978 0.038 . 189 49 48 SER H H 8.623 0.002 . 190 49 48 SER C C 174.603 0.060 . 191 49 48 SER CA C 60.911 0.061 . 192 49 48 SER CB C 62.610 0.008 . 193 49 48 SER N N 115.518 0.039 . 194 50 49 ASN H H 8.292 0.002 . 195 50 49 ASN C C 174.569 0.008 . 196 50 49 ASN CA C 53.078 0.015 . 197 50 49 ASN CB C 37.225 0.005 . 198 50 49 ASN N N 116.369 0.039 . 199 51 50 VAL H H 7.701 0.001 . 200 51 50 VAL C C 175.093 0.000 . 201 51 50 VAL CA C 60.510 0.000 . 202 51 50 VAL CB C 31.587 0.000 . 203 51 50 VAL N N 125.740 0.036 . 204 56 55 TRP H H 8.888 0.002 . 205 56 55 TRP C C 175.164 0.009 . 206 56 55 TRP CA C 55.025 0.000 . 207 56 55 TRP CB C 31.075 0.025 . 208 56 55 TRP N N 122.774 0.045 . 209 57 56 THR H H 7.882 0.002 . 210 57 56 THR C C 171.830 0.014 . 211 57 56 THR CA C 55.132 0.000 . 212 57 56 THR CB C 69.457 0.014 . 213 57 56 THR N N 119.890 0.040 . 214 58 57 ARG H H 7.951 0.002 . 215 58 57 ARG C C 176.748 0.026 . 216 58 57 ARG CA C 55.493 0.000 . 217 58 57 ARG CB C 29.809 0.024 . 218 58 57 ARG N N 122.469 0.044 . 219 59 58 CYS H H 8.046 0.002 . 220 59 58 CYS C C 174.591 0.039 . 221 59 58 CYS CA C 58.662 0.008 . 222 59 58 CYS CB C 28.638 0.003 . 223 59 58 CYS N N 119.021 0.039 . 224 60 59 ASN H H 9.325 0.002 . 225 60 59 ASN C C 174.465 0.023 . 226 60 59 ASN CA C 55.361 0.013 . 227 60 59 ASN CB C 37.651 0.025 . 228 60 59 ASN N N 114.825 0.038 . 229 61 60 GLY H H 8.864 0.002 . 230 61 60 GLY C C 174.404 0.001 . 231 61 60 GLY CA C 44.885 0.000 . 232 61 60 GLY N N 103.823 0.041 . 233 62 61 GLY H H 7.487 0.002 . 234 62 61 GLY C C 172.936 0.008 . 235 62 61 GLY CA C 43.719 0.005 . 236 62 61 GLY N N 111.867 0.072 . 237 63 62 HIS H H 7.119 0.001 . 238 63 62 HIS CA C 55.019 0.026 . 239 63 62 HIS CB C 28.473 0.002 . 240 63 62 HIS N N 121.487 0.028 . 241 64 63 TRP H H 8.278 0.002 . 242 64 63 TRP C C 179.952 0.000 . 243 64 63 TRP CA C 56.013 0.000 . 244 64 63 TRP CB C 32.107 0.000 . 245 64 63 TRP N N 118.159 0.038 . 246 67 66 THR C C 173.432 0.000 . 247 67 66 THR CA C 61.611 0.027 . 248 67 66 THR CB C 68.099 0.000 . 249 68 67 ARG H H 6.260 0.004 . 250 68 67 ARG C C 177.203 0.005 . 251 68 67 ARG CA C 51.427 0.024 . 252 68 67 ARG CB C 32.759 0.031 . 253 68 67 ARG N N 114.389 0.037 . 254 69 68 GLY H H 10.170 0.001 . 255 69 68 GLY C C 174.684 0.008 . 256 69 68 GLY CA C 46.684 0.013 . 257 69 68 GLY N N 111.721 0.042 . 258 70 69 GLN H H 8.773 0.003 . 259 70 69 GLN C C 177.730 0.005 . 260 70 69 GLN CA C 58.644 0.014 . 261 70 69 GLN CB C 27.602 0.009 . 262 70 69 GLN N N 119.390 0.036 . 263 71 70 LEU H H 6.267 0.002 . 264 71 70 LEU C C 177.550 0.002 . 265 71 70 LEU CA C 58.620 0.000 . 266 71 70 LEU CB C 42.610 0.080 . 267 71 70 LEU N N 116.541 0.038 . 268 72 71 ILE H H 7.462 0.002 . 269 72 71 ILE C C 176.884 0.006 . 270 72 71 ILE CA C 65.466 0.036 . 271 72 71 ILE CB C 37.905 0.002 . 272 72 71 ILE N N 120.318 0.034 . 273 73 72 ARG H H 7.945 0.001 . 274 73 72 ARG C C 178.311 0.008 . 275 73 72 ARG CA C 59.632 0.006 . 276 73 72 ARG CB C 29.563 0.004 . 277 73 72 ARG N N 115.307 0.038 . 278 74 73 GLU H H 7.441 0.002 . 279 74 73 GLU C C 180.305 0.028 . 280 74 73 GLU CA C 59.103 0.017 . 281 74 73 GLU CB C 29.686 0.013 . 282 74 73 GLU N N 116.935 0.041 . 283 75 74 ALA H H 8.062 0.002 . 284 75 74 ALA C C 179.709 0.008 . 285 75 74 ALA CA C 54.140 0.001 . 286 75 74 ALA CB C 17.236 0.015 . 287 75 74 ALA N N 120.890 0.037 . 288 76 75 TYR H H 7.641 0.002 . 289 76 75 TYR C C 178.220 0.014 . 290 76 75 TYR CA C 60.907 0.009 . 291 76 75 TYR CB C 36.861 0.028 . 292 76 75 TYR N N 114.934 0.036 . 293 77 76 GLU H H 7.772 0.002 . 294 77 76 GLU C C 177.450 0.011 . 295 77 76 GLU CA C 58.111 0.016 . 296 77 76 GLU CB C 29.394 0.001 . 297 77 76 GLU N N 116.412 0.069 . 298 78 77 ASP H H 7.559 0.002 . 299 78 77 ASP C C 175.529 0.033 . 300 78 77 ASP CA C 51.503 0.006 . 301 78 77 ASP CB C 38.548 0.012 . 302 78 77 ASP N N 119.827 0.044 . 303 79 78 TYR H H 7.334 0.002 . 304 79 78 TYR C C 175.916 0.006 . 305 79 78 TYR CA C 57.208 0.010 . 306 79 78 TYR CB C 36.431 0.020 . 307 79 78 TYR N N 121.481 0.035 . 308 80 79 ARG H H 7.231 0.002 . 309 80 79 ARG C C 178.462 0.010 . 310 80 79 ARG CA C 57.876 0.058 . 311 80 79 ARG CB C 27.802 0.019 . 312 80 79 ARG N N 120.987 0.042 . 313 81 80 HIS H H 6.803 0.001 . 314 81 80 HIS CA C 58.589 0.004 . 315 81 80 HIS CB C 28.417 0.062 . 316 81 80 HIS N N 112.844 0.045 . 317 82 81 PHE H H 7.873 0.002 . 318 82 81 PHE C C 174.454 0.016 . 319 82 81 PHE CA C 55.277 0.005 . 320 82 81 PHE CB C 36.473 0.001 . 321 82 81 PHE N N 118.898 0.036 . 322 83 82 SER H H 8.876 0.002 . 323 83 82 SER C C 176.849 0.000 . 324 83 82 SER CA C 56.403 0.010 . 325 83 82 SER CB C 63.323 0.031 . 326 83 82 SER N N 117.232 0.041 . 327 84 83 SER H H 9.702 0.002 . 328 84 83 SER C C 172.335 0.000 . 329 84 83 SER CA C 59.192 0.063 . 330 84 83 SER CB C 61.087 0.005 . 331 84 83 SER N N 126.446 0.037 . 332 85 84 GLU H H 8.078 0.001 . 333 85 84 GLU C C 175.055 0.000 . 334 85 84 GLU CA C 58.478 0.000 . 335 85 84 GLU CB C 28.992 0.000 . 336 85 84 GLU N N 119.196 0.039 . 337 90 89 PRO C C 176.345 0.000 . 338 90 89 PRO CA C 61.534 0.002 . 339 90 89 PRO CB C 34.962 0.000 . 340 91 90 ARG H H 9.445 0.001 . 341 91 90 ARG C C 177.056 0.021 . 342 91 90 ARG CA C 60.132 0.010 . 343 91 90 ARG CB C 29.826 0.041 . 344 91 90 ARG N N 124.045 0.039 . 345 92 91 GLU H H 9.439 0.002 . 346 92 91 GLU C C 179.573 0.014 . 347 92 91 GLU CA C 59.588 0.009 . 348 92 91 GLU CB C 27.785 0.002 . 349 92 91 GLU N N 115.833 0.038 . 350 93 92 ALA H H 7.387 0.002 . 351 93 92 ALA C C 178.013 0.014 . 352 93 92 ALA CA C 53.824 0.036 . 353 93 92 ALA CB C 17.055 0.003 . 354 93 92 ALA N N 123.207 0.038 . 355 94 93 GLY H H 7.495 0.002 . 356 94 93 GLY C C 176.034 0.005 . 357 94 93 GLY CA C 48.770 0.009 . 358 94 93 GLY N N 104.297 0.039 . 359 95 94 GLU H H 9.075 0.002 . 360 95 94 GLU C C 178.677 0.016 . 361 95 94 GLU CA C 58.761 0.007 . 362 95 94 GLU CB C 28.518 0.024 . 363 95 94 GLU N N 120.667 0.029 . 364 96 95 ALA H H 7.038 0.002 . 365 96 95 ALA C C 176.988 0.000 . 366 96 95 ALA CA C 52.391 0.033 . 367 96 95 ALA CB C 18.328 0.017 . 368 96 95 ALA N N 120.300 0.037 . 369 97 96 TYR H H 8.352 0.001 . 370 97 96 TYR C C 174.372 0.003 . 371 97 96 TYR CA C 52.938 0.028 . 372 97 96 TYR CB C 37.819 0.006 . 373 97 96 TYR N N 117.402 0.039 . 374 98 97 ASP H H 7.758 0.002 . 375 98 97 ASP C C 176.000 0.007 . 376 98 97 ASP CA C 52.978 0.003 . 377 98 97 ASP CB C 40.740 0.014 . 378 98 97 ASP N N 121.920 0.038 . 379 99 98 PHE H H 8.709 0.002 . 380 99 98 PHE C C 176.251 0.000 . 381 99 98 PHE CA C 50.018 0.000 . 382 99 98 PHE N N 129.707 0.038 . 383 101 100 PRO C C 178.546 0.000 . 384 101 100 PRO CA C 62.591 0.000 . 385 101 100 PRO CB C 34.268 0.000 . 386 102 101 THR H H 7.269 0.002 . 387 102 101 THR C C 173.221 0.000 . 388 102 101 THR CA C 66.211 0.012 . 389 102 101 THR CB C 67.749 0.003 . 390 102 101 THR N N 115.684 0.040 . 391 103 102 SER H H 8.092 0.003 . 392 103 102 SER C C 172.370 0.000 . 393 103 102 SER CA C 58.716 0.078 . 394 103 102 SER CB C 63.453 0.010 . 395 103 102 SER N N 110.905 0.045 . 396 104 103 MET H H 7.594 0.002 . 397 104 103 MET C C 174.078 0.004 . 398 104 103 MET CA C 54.219 0.020 . 399 104 103 MET CB C 35.198 0.010 . 400 104 103 MET N N 119.372 0.038 . 401 105 104 ASP H H 8.712 0.002 . 402 105 104 ASP C C 175.359 0.000 . 403 105 104 ASP CA C 51.821 0.000 . 404 105 104 ASP CB C 41.440 0.000 . 405 105 104 ASP N N 119.642 0.035 . 406 107 106 PRO C C 178.790 0.005 . 407 107 106 PRO CA C 64.885 0.030 . 408 107 106 PRO CB C 31.160 0.000 . 409 108 107 GLU H H 9.004 0.002 . 410 108 107 GLU C C 179.578 0.010 . 411 108 107 GLU CA C 59.567 0.017 . 412 108 107 GLU CB C 27.991 0.037 . 413 108 107 GLU N N 117.067 0.037 . 414 109 108 GLN H H 7.514 0.003 . 415 109 108 GLN C C 177.914 0.043 . 416 109 108 GLN CA C 61.679 0.018 . 417 109 108 GLN CB C 30.656 0.007 . 418 109 108 GLN N N 119.456 0.037 . 419 110 109 ARG H H 7.569 0.002 . 420 110 109 ARG C C 177.990 0.020 . 421 110 109 ARG CA C 60.514 0.045 . 422 110 109 ARG CB C 29.581 0.004 . 423 110 109 ARG N N 117.142 0.038 . 424 111 110 GLN H H 8.330 0.001 . 425 111 110 GLN HE21 H 7.633 0.001 . 426 111 110 GLN HE22 H 7.732 0.001 . 427 111 110 GLN C C 178.045 0.000 . 428 111 110 GLN CA C 58.040 0.017 . 429 111 110 GLN CB C 27.076 0.042 . 430 111 110 GLN CG C 32.653 0.016 . 431 111 110 GLN N N 116.605 0.033 . 432 111 110 GLN NE2 N 112.507 0.016 . 433 112 111 PHE H H 7.056 0.002 . 434 112 111 PHE C C 177.743 0.017 . 435 112 111 PHE CA C 61.337 0.001 . 436 112 111 PHE CB C 39.191 0.001 . 437 112 111 PHE N N 117.825 0.040 . 438 113 112 ARG H H 8.674 0.005 . 439 113 112 ARG C C 177.127 0.003 . 440 113 112 ARG CA C 59.962 0.006 . 441 113 112 ARG CB C 29.654 0.000 . 442 113 112 ARG N N 121.081 0.039 . 443 114 113 ALA H H 7.814 0.002 . 444 114 113 ALA C C 180.048 0.008 . 445 114 113 ALA CA C 54.767 0.019 . 446 114 113 ALA CB C 17.099 0.010 . 447 114 113 ALA N N 119.934 0.037 . 448 115 114 LEU H H 7.014 0.002 . 449 115 114 LEU C C 178.057 0.008 . 450 115 114 LEU CA C 57.162 0.044 . 451 115 114 LEU CB C 40.610 0.020 . 452 115 114 LEU N N 119.823 0.039 . 453 116 115 ALA H H 7.934 0.002 . 454 116 115 ALA C C 179.790 0.013 . 455 116 115 ALA CA C 54.543 0.057 . 456 116 115 ALA CB C 16.698 0.003 . 457 116 115 ALA N N 119.876 0.035 . 458 117 116 ASN H H 8.759 0.038 . 459 117 116 ASN C C 177.301 0.005 . 460 117 116 ASN CA C 55.785 0.019 . 461 117 116 ASN CB C 38.668 0.003 . 462 117 116 ASN N N 116.325 0.088 . 463 118 117 GLN H H 7.601 0.002 . 464 118 117 GLN HE21 H 7.231 0.001 . 465 118 117 GLN HE22 H 6.736 0.004 . 466 118 117 GLN C C 176.770 0.007 . 467 118 117 GLN CA C 57.821 0.017 . 468 118 117 GLN CB C 27.975 0.022 . 469 118 117 GLN CG C 33.231 0.025 . 470 118 117 GLN CD C 179.780 0.013 . 471 118 117 GLN N N 116.298 0.040 . 472 118 117 GLN NE2 N 111.946 0.038 . 473 119 118 VAL H H 7.191 0.002 . 474 119 118 VAL C C 175.560 0.000 . 475 119 118 VAL CA C 61.611 0.000 . 476 119 118 VAL CB C 31.562 0.000 . 477 119 118 VAL N N 108.753 0.041 . 478 120 119 VAL C C 178.435 0.000 . 479 120 119 VAL CA C 63.398 0.024 . 480 120 119 VAL CB C 30.612 0.000 . 481 121 120 GLY H H 8.682 0.002 . 482 121 120 GLY C C 174.100 0.000 . 483 121 120 GLY CA C 44.974 0.030 . 484 121 120 GLY N N 112.896 0.044 . 485 122 121 MET H H 8.214 0.001 . 486 122 121 MET C C 175.181 0.000 . 487 122 121 MET CA C 54.022 0.000 . 488 122 121 MET CB C 31.010 0.000 . 489 122 121 MET N N 118.278 0.026 . 490 123 122 PRO C C 179.357 0.014 . 491 123 122 PRO CA C 65.583 0.008 . 492 123 122 PRO CB C 30.221 0.000 . 493 124 123 VAL H H 7.178 0.003 . 494 124 123 VAL C C 177.555 0.003 . 495 124 123 VAL CA C 64.183 0.011 . 496 124 123 VAL CB C 30.852 0.031 . 497 124 123 VAL N N 116.570 0.038 . 498 125 124 VAL H H 7.305 0.003 . 499 125 124 VAL C C 178.042 0.009 . 500 125 124 VAL CA C 66.570 0.046 . 501 125 124 VAL CB C 29.774 0.027 . 502 125 124 VAL N N 121.386 0.040 . 503 126 125 ASP H H 8.122 0.002 . 504 126 125 ASP C C 179.209 0.011 . 505 126 125 ASP CA C 56.918 0.060 . 506 126 125 ASP CB C 39.503 0.004 . 507 126 125 ASP N N 117.481 0.040 . 508 127 126 LYS H H 7.139 0.002 . 509 127 126 LYS C C 178.270 0.010 . 510 127 126 LYS CA C 57.884 0.010 . 511 127 126 LYS CB C 31.393 0.009 . 512 127 126 LYS N N 118.587 0.041 . 513 128 127 LEU H H 7.680 0.002 . 514 128 127 LEU C C 177.415 0.010 . 515 128 127 LEU CA C 54.280 0.020 . 516 128 127 LEU CB C 42.558 0.017 . 517 128 127 LEU N N 119.261 0.042 . 518 129 128 GLU H H 7.410 0.002 . 519 129 128 GLU C C 177.238 0.058 . 520 129 128 GLU CA C 60.499 0.004 . 521 129 128 GLU CB C 28.663 0.024 . 522 129 128 GLU N N 121.056 0.038 . 523 130 129 ASN H H 8.537 0.002 . 524 130 129 ASN C C 177.357 0.004 . 525 130 129 ASN CA C 56.297 0.036 . 526 130 129 ASN CB C 36.951 0.023 . 527 130 129 ASN N N 116.228 0.040 . 528 131 130 ARG H H 7.789 0.002 . 529 131 130 ARG C C 178.767 0.007 . 530 131 130 ARG CA C 57.409 0.006 . 531 131 130 ARG CB C 28.381 0.007 . 532 131 130 ARG N N 121.266 0.039 . 533 132 131 ILE H H 8.263 0.002 . 534 132 131 ILE C C 177.023 0.013 . 535 132 131 ILE CA C 65.653 0.005 . 536 132 131 ILE CB C 37.144 0.020 . 537 132 131 ILE N N 120.408 0.041 . 538 133 132 GLN H H 7.985 0.157 . 539 133 132 GLN HE21 H 6.658 0.001 . 540 133 132 GLN HE22 H 7.488 0.002 . 541 133 132 GLN C C 177.918 0.011 . 542 133 132 GLN CA C 59.191 0.000 . 543 133 132 GLN CB C 27.400 0.019 . 544 133 132 GLN CG C 32.654 0.019 . 545 133 132 GLN CD C 179.440 0.015 . 546 133 132 GLN N N 117.707 1.667 . 547 133 132 GLN NE2 N 112.528 0.041 . 548 134 133 GLU H H 8.295 0.001 . 549 134 133 GLU C C 179.661 0.018 . 550 134 133 GLU CA C 59.016 0.020 . 551 134 133 GLU CB C 29.310 0.027 . 552 134 133 GLU N N 118.837 0.038 . 553 135 134 LEU H H 8.266 0.002 . 554 135 134 LEU C C 178.394 0.000 . 555 135 134 LEU CA C 57.426 0.000 . 556 135 134 LEU CB C 40.499 0.000 . 557 135 134 LEU N N 121.088 0.036 . 558 137 136 CYS C C 176.697 0.002 . 559 137 136 CYS CA C 64.128 0.000 . 560 137 136 CYS CB C 26.288 0.000 . 561 138 137 SER H H 8.173 0.002 . 562 138 137 SER C C 178.156 0.000 . 563 138 137 SER CA C 61.072 0.009 . 564 138 137 SER CB C 62.157 0.022 . 565 138 137 SER N N 115.117 0.042 . 566 139 138 LEU H H 8.455 0.003 . 567 139 138 LEU C C 180.191 0.000 . 568 139 138 LEU CA C 57.556 0.000 . 569 139 138 LEU CB C 41.786 0.000 . 570 139 138 LEU N N 122.525 0.073 . 571 140 139 ILE C C 177.980 0.004 . 572 140 139 ILE CA C 65.914 0.000 . 573 140 139 ILE CB C 37.065 0.000 . 574 141 140 GLU H H 8.506 0.002 . 575 141 140 GLU C C 178.431 0.010 . 576 141 140 GLU CA C 57.808 0.027 . 577 141 140 GLU CB C 27.739 0.002 . 578 141 140 GLU N N 119.519 0.045 . 579 142 141 SER H H 7.445 0.002 . 580 142 141 SER C C 176.195 0.000 . 581 142 141 SER CA C 60.925 0.010 . 582 142 141 SER CB C 62.360 0.031 . 583 142 141 SER N N 112.422 0.044 . 584 143 142 LEU H H 7.373 0.002 . 585 143 142 LEU C C 178.888 0.000 . 586 143 142 LEU CA C 56.287 0.000 . 587 143 142 LEU CB C 42.024 0.000 . 588 143 142 LEU N N 119.685 0.039 . 589 145 144 PRO C C 177.230 0.005 . 590 145 144 PRO CA C 64.459 0.013 . 591 145 144 PRO CB C 30.647 0.000 . 592 146 145 GLN H H 8.369 0.002 . 593 146 145 GLN HE21 H 7.438 0.001 . 594 146 145 GLN HE22 H 6.774 0.001 . 595 146 145 GLN C C 178.497 0.009 . 596 146 145 GLN CA C 57.336 0.015 . 597 146 145 GLN CB C 28.869 0.005 . 598 146 145 GLN CG C 32.915 0.000 . 599 146 145 GLN N N 113.795 0.037 . 600 146 145 GLN NE2 N 112.547 0.044 . 601 147 146 GLY H H 6.508 0.002 . 602 147 146 GLY C C 170.529 0.018 . 603 147 146 GLY CA C 44.191 0.009 . 604 147 146 GLY N N 101.566 0.042 . 605 148 147 GLN H H 5.899 0.002 . 606 148 147 GLN HE21 H 7.336 0.001 . 607 148 147 GLN HE22 H 6.621 0.001 . 608 148 147 GLN C C 174.464 0.014 . 609 148 147 GLN CA C 53.683 0.015 . 610 148 147 GLN CB C 29.170 0.038 . 611 148 147 GLN CG C 30.868 0.003 . 612 148 147 GLN CD C 181.000 0.000 . 613 148 147 GLN N N 111.069 0.032 . 614 148 147 GLN NE2 N 112.292 0.033 . 615 149 148 CYS H H 8.291 0.002 . 616 149 148 CYS C C 171.782 0.009 . 617 149 148 CYS CA C 56.430 0.027 . 618 149 148 CYS CB C 30.117 0.008 . 619 149 148 CYS N N 110.383 0.037 . 620 150 149 ASN H H 9.159 0.001 . 621 150 149 ASN C C 176.110 0.009 . 622 150 149 ASN CA C 51.610 0.009 . 623 150 149 ASN CB C 36.730 0.035 . 624 150 149 ASN N N 119.637 0.036 . 625 151 150 PHE H H 9.406 0.002 . 626 151 150 PHE C C 176.705 0.009 . 627 151 150 PHE CA C 62.828 0.025 . 628 151 150 PHE CB C 39.568 0.027 . 629 151 150 PHE N N 123.876 0.038 . 630 152 151 THR H H 7.294 0.002 . 631 152 151 THR C C 173.985 0.000 . 632 152 151 THR CA C 64.567 0.009 . 633 152 151 THR CB C 66.756 0.013 . 634 152 151 THR N N 109.400 0.039 . 635 153 152 GLU H H 6.244 0.003 . 636 153 152 GLU C C 177.705 0.000 . 637 153 152 GLU CA C 57.289 0.000 . 638 153 152 GLU CB C 30.646 0.000 . 639 153 152 GLU N N 118.339 0.037 . 640 163 162 ILE C C 176.438 0.000 . 641 163 162 ILE CA C 62.531 0.000 . 642 163 162 ILE CB C 34.696 0.000 . 643 164 163 PHE H H 7.839 0.002 . 644 164 163 PHE C C 176.793 0.012 . 645 164 163 PHE CA C 62.371 0.017 . 646 164 163 PHE CB C 37.828 0.010 . 647 164 163 PHE N N 121.151 0.036 . 648 165 164 MET H H 8.926 0.002 . 649 165 164 MET C C 178.782 0.008 . 650 165 164 MET CA C 57.506 0.451 . 651 165 164 MET CB C 29.181 0.309 . 652 165 164 MET N N 116.339 0.036 . 653 166 165 LEU H H 7.321 0.002 . 654 166 165 LEU C C 180.052 0.028 . 655 166 165 LEU CA C 57.229 0.029 . 656 166 165 LEU CB C 40.358 0.000 . 657 166 165 LEU N N 120.454 0.036 . 658 167 166 LEU H H 7.718 0.002 . 659 167 166 LEU C C 178.236 0.022 . 660 167 166 LEU CA C 57.162 0.055 . 661 167 166 LEU CB C 40.704 0.037 . 662 167 166 LEU N N 123.014 0.040 . 663 168 167 ALA H H 8.279 0.003 . 664 168 167 ALA C C 174.912 0.000 . 665 168 167 ALA CA C 52.140 0.036 . 666 168 167 ALA CB C 17.517 0.031 . 667 168 167 ALA N N 118.671 0.037 . 668 169 168 GLY H H 7.651 0.002 . 669 169 168 GLY C C 175.253 0.008 . 670 169 168 GLY CA C 46.856 0.014 . 671 169 168 GLY N N 108.312 0.043 . 672 170 169 LEU H H 8.311 0.002 . 673 170 169 LEU C C 173.709 0.000 . 674 170 169 LEU CA C 50.860 0.000 . 675 170 169 LEU CB C 41.454 0.000 . 676 170 169 LEU N N 122.191 0.029 . 677 171 170 PRO C C 178.237 0.004 . 678 171 170 PRO CA C 62.111 0.028 . 679 171 170 PRO CB C 31.516 0.000 . 680 172 171 GLU H H 8.722 0.003 . 681 172 171 GLU C C 179.571 0.018 . 682 172 171 GLU CA C 58.962 0.006 . 683 172 171 GLU CB C 28.489 0.061 . 684 172 171 GLU N N 122.920 0.037 . 685 173 172 GLU H H 9.409 0.002 . 686 173 172 GLU C C 177.021 0.007 . 687 173 172 GLU CA C 58.564 0.034 . 688 173 172 GLU CB C 27.792 0.002 . 689 173 172 GLU N N 119.655 0.042 . 690 174 173 ASP H H 7.575 0.002 . 691 174 173 ASP C C 176.011 0.008 . 692 174 173 ASP CA C 54.742 0.009 . 693 174 173 ASP CB C 39.730 0.018 . 694 174 173 ASP N N 118.873 0.038 . 695 175 174 ILE H H 7.587 0.002 . 696 175 174 ILE C C 173.567 0.000 . 697 175 174 ILE CA C 67.508 0.000 . 698 175 174 ILE N N 119.055 0.038 . 699 180 179 TYR C C 173.882 0.009 . 700 180 179 TYR CA C 62.449 0.037 . 701 180 179 TYR CB C 31.879 0.000 . 702 181 180 LEU H H 8.006 0.002 . 703 181 180 LEU C C 174.471 0.000 . 704 181 180 LEU CA C 55.579 0.013 . 705 181 180 LEU CB C 40.206 0.145 . 706 181 180 LEU N N 117.474 0.054 . 707 182 181 THR H H 6.933 0.003 . 708 182 181 THR C C 177.393 0.000 . 709 182 181 THR CA C 62.597 0.147 . 710 182 181 THR CB C 61.124 0.005 . 711 182 181 THR N N 115.744 0.044 . 712 183 182 ASP H H 8.236 0.014 . 713 183 182 ASP C C 178.040 0.021 . 714 183 182 ASP CA C 56.513 0.002 . 715 183 182 ASP CB C 39.540 0.064 . 716 183 182 ASP N N 122.630 0.038 . 717 184 183 GLN H H 7.341 0.002 . 718 184 183 GLN C C 177.313 0.007 . 719 184 183 GLN CA C 55.991 0.032 . 720 184 183 GLN CB C 26.870 0.009 . 721 184 183 GLN N N 114.108 0.039 . 722 185 184 MET H H 7.708 0.002 . 723 185 184 MET C C 176.691 0.000 . 724 185 184 MET CA C 58.751 0.009 . 725 185 184 MET CB C 33.501 0.010 . 726 185 184 MET N N 115.639 0.045 . 727 186 185 THR H H 7.841 0.004 . 728 186 185 THR C C 176.024 0.004 . 729 186 185 THR CA C 62.748 0.011 . 730 186 185 THR CB C 69.663 0.013 . 731 186 185 THR N N 106.972 0.040 . 732 187 186 ARG H H 8.775 0.000 . 733 187 186 ARG C C 172.682 0.000 . 734 187 186 ARG CA C 53.960 0.000 . 735 187 186 ARG CB C 31.213 0.000 . 736 187 186 ARG N N 122.751 0.044 . 737 189 188 ASP C C 177.977 0.000 . 738 189 188 ASP CA C 52.704 0.013 . 739 189 188 ASP CB C 40.446 0.000 . 740 190 189 GLY H H 8.762 0.001 . 741 190 189 GLY C C 175.406 0.002 . 742 190 189 GLY CA C 44.593 0.004 . 743 190 189 GLY N N 110.336 0.045 . 744 191 190 SER H H 8.833 0.002 . 745 191 190 SER C C 174.528 0.055 . 746 191 190 SER CA C 60.550 0.020 . 747 191 190 SER CB C 62.709 0.023 . 748 191 190 SER N N 119.500 0.031 . 749 192 191 MET H H 8.380 0.002 . 750 192 191 MET C C 176.304 0.005 . 751 192 191 MET CA C 55.087 0.014 . 752 192 191 MET CB C 36.815 0.002 . 753 192 191 MET N N 120.941 0.043 . 754 193 192 THR H H 8.933 0.002 . 755 193 192 THR C C 174.563 0.014 . 756 193 192 THR CA C 60.874 0.021 . 757 193 192 THR CB C 70.301 0.038 . 758 193 192 THR N N 116.671 0.039 . 759 194 193 PHE H H 8.747 0.080 . 760 194 193 PHE C C 178.136 1.372 . 761 194 193 PHE CA C 58.676 3.663 . 762 194 193 PHE CB C 37.750 0.013 . 763 194 193 PHE N N 121.364 2.190 . 764 196 195 GLU H H 7.667 0.002 . 765 196 195 GLU C C 179.502 0.010 . 766 196 195 GLU CA C 58.511 0.003 . 767 196 195 GLU CB C 29.404 0.009 . 768 196 195 GLU N N 117.772 0.033 . 769 197 196 ALA H H 8.022 0.002 . 770 197 196 ALA C C 178.310 0.007 . 771 197 196 ALA CA C 54.884 0.017 . 772 197 196 ALA CB C 17.178 0.011 . 773 197 196 ALA N N 125.282 0.035 . 774 198 197 LYS H H 8.415 0.002 . 775 198 197 LYS C C 177.440 0.009 . 776 198 197 LYS CA C 58.899 0.000 . 777 198 197 LYS CB C 29.874 0.011 . 778 198 197 LYS N N 119.033 0.035 . 779 199 198 GLU H H 7.939 0.001 . 780 199 198 GLU C C 178.796 0.000 . 781 199 198 GLU CA C 58.846 0.058 . 782 199 198 GLU CB C 28.149 0.000 . 783 199 198 GLU N N 117.109 0.041 . 784 202 201 TYR H H 7.649 0.001 . 785 202 201 TYR C C 176.354 0.004 . 786 202 201 TYR CA C 58.261 0.001 . 787 202 201 TYR CB C 30.011 0.000 . 788 202 201 TYR N N 116.961 0.047 . 789 203 202 ASP H H 7.567 0.002 . 790 203 202 ASP C C 179.095 0.009 . 791 203 202 ASP CA C 57.079 0.014 . 792 203 202 ASP CB C 41.404 0.045 . 793 203 202 ASP N N 117.394 0.039 . 794 204 203 TYR H H 9.047 0.002 . 795 204 203 TYR C C 177.165 0.007 . 796 204 203 TYR CA C 57.103 0.000 . 797 204 203 TYR CB C 31.132 0.005 . 798 204 203 TYR N N 120.421 0.046 . 799 205 204 LEU H H 7.529 0.002 . 800 205 204 LEU C C 177.553 0.016 . 801 205 204 LEU CA C 61.288 0.018 . 802 205 204 LEU CB C 37.199 0.011 . 803 205 204 LEU N N 118.983 0.043 . 804 206 205 ILE H H 7.383 0.002 . 805 206 205 ILE C C 178.808 0.012 . 806 206 205 ILE CA C 57.400 0.026 . 807 206 205 ILE CB C 40.950 0.025 . 808 206 205 ILE N N 116.571 0.042 . 809 207 206 PRO C C 179.450 0.017 . 810 207 206 PRO CA C 64.905 0.022 . 811 207 206 PRO CB C 30.172 0.000 . 812 208 207 ILE H H 6.628 0.002 . 813 208 207 ILE C C 177.915 0.025 . 814 208 207 ILE CA C 63.986 0.017 . 815 208 207 ILE CB C 37.481 0.004 . 816 208 207 ILE N N 119.857 0.040 . 817 209 208 ILE H H 8.306 0.002 . 818 209 208 ILE C C 177.319 0.007 . 819 209 208 ILE CA C 64.908 0.010 . 820 209 208 ILE CB C 36.445 0.008 . 821 209 208 ILE N N 120.759 0.036 . 822 210 209 GLU H H 7.705 0.002 . 823 210 209 GLU C C 179.745 0.000 . 824 210 209 GLU CA C 58.817 0.006 . 825 210 209 GLU CB C 28.134 0.013 . 826 210 209 GLU N N 117.003 0.036 . 827 211 210 GLN H H 7.737 0.002 . 828 211 210 GLN C C 179.129 0.003 . 829 211 210 GLN CA C 58.569 0.012 . 830 211 210 GLN CB C 27.632 0.000 . 831 211 210 GLN N N 118.742 0.042 . 832 212 211 ARG H H 8.093 0.002 . 833 212 211 ARG C C 177.087 0.005 . 834 212 211 ARG CA C 57.221 0.027 . 835 212 211 ARG CB C 27.990 0.000 . 836 212 211 ARG N N 118.382 0.041 . 837 213 212 ARG H H 7.615 0.001 . 838 213 212 ARG C C 177.690 0.012 . 839 213 212 ARG CA C 57.608 0.053 . 840 213 212 ARG CB C 29.904 0.035 . 841 213 212 ARG N N 118.664 0.046 . 842 214 213 GLN H H 7.328 0.220 . 843 214 213 GLN HE21 H 7.535 0.002 . 844 214 213 GLN HE22 H 6.847 0.000 . 845 214 213 GLN C C 176.938 0.012 . 846 214 213 GLN CA C 57.165 0.009 . 847 214 213 GLN CB C 28.150 0.040 . 848 214 213 GLN CG C 33.087 0.068 . 849 214 213 GLN CD C 180.307 0.004 . 850 214 213 GLN N N 116.719 2.004 . 851 214 213 GLN NE2 N 113.196 0.052 . 852 215 214 LYS H H 7.897 0.002 . 853 215 214 LYS C C 171.696 0.000 . 854 215 214 LYS CA C 52.903 0.000 . 855 215 214 LYS CB C 32.161 0.000 . 856 215 214 LYS N N 119.018 0.041 . 857 216 215 PRO C C 178.737 0.000 . 858 216 215 PRO CA C 63.407 0.000 . 859 216 215 PRO CB C 31.908 0.000 . 860 217 216 GLY H H 8.491 0.002 . 861 217 216 GLY C C 173.548 0.012 . 862 217 216 GLY CA C 43.266 0.060 . 863 217 216 GLY N N 110.951 0.052 . 864 218 217 THR H H 8.545 0.001 . 865 218 217 THR C C 173.774 0.000 . 866 218 217 THR CA C 60.576 0.016 . 867 218 217 THR CB C 68.142 0.016 . 868 218 217 THR N N 109.879 0.032 . 869 219 218 ASP H H 8.100 0.002 . 870 219 218 ASP C C 174.682 0.007 . 871 219 218 ASP CA C 52.288 0.018 . 872 219 218 ASP CB C 42.227 0.004 . 873 219 218 ASP N N 118.973 0.040 . 874 220 219 ALA H H 8.507 0.002 . 875 220 219 ALA C C 179.015 0.011 . 876 220 219 ALA CA C 54.866 0.020 . 877 220 219 ALA CB C 18.801 0.009 . 878 220 219 ALA N N 117.880 0.035 . 879 221 220 ILE H H 7.506 0.002 . 880 221 220 ILE C C 177.685 0.000 . 881 221 220 ILE CA C 64.363 0.000 . 882 221 220 ILE CB C 35.109 0.000 . 883 221 220 ILE N N 114.426 0.040 . 884 225 224 ALA H H 8.917 0.001 . 885 225 224 ALA C C 176.464 0.000 . 886 225 224 ALA CA C 53.708 0.000 . 887 225 224 ALA CB C 18.043 0.011 . 888 225 224 ALA N N 116.118 0.014 . 889 226 225 ASN H H 7.162 0.002 . 890 226 225 ASN C C 174.721 0.004 . 891 226 225 ASN CA C 52.460 0.022 . 892 226 225 ASN CB C 39.713 0.001 . 893 226 225 ASN N N 112.570 0.041 . 894 227 226 GLY H H 7.618 0.003 . 895 227 226 GLY C C 171.691 0.005 . 896 227 226 GLY CA C 44.842 0.003 . 897 227 226 GLY N N 109.705 0.046 . 898 228 227 GLN H H 8.101 0.002 . 899 228 227 GLN C C 175.121 0.006 . 900 228 227 GLN CA C 53.981 0.014 . 901 228 227 GLN CB C 30.934 0.004 . 902 228 227 GLN N N 117.956 0.035 . 903 229 228 VAL H H 8.906 0.002 . 904 229 228 VAL C C 174.830 0.012 . 905 229 228 VAL CA C 59.320 0.016 . 906 229 228 VAL CB C 33.506 0.004 . 907 229 228 VAL N N 117.321 0.035 . 908 230 229 ASN H H 8.916 0.002 . 909 230 229 ASN C C 175.704 0.004 . 910 230 229 ASN CA C 53.611 0.017 . 911 230 229 ASN CB C 37.378 0.015 . 912 230 229 ASN N N 121.367 0.033 . 913 231 230 GLY H H 8.596 0.002 . 914 231 230 GLY C C 173.106 0.001 . 915 231 230 GLY CA C 45.334 0.047 . 916 231 230 GLY N N 103.213 0.040 . 917 232 231 ARG H H 7.981 0.023 . 918 232 231 ARG C C 172.828 0.000 . 919 232 231 ARG CA C 52.141 0.023 . 920 232 231 ARG CB C 29.366 0.000 . 921 232 231 ARG N N 118.943 0.046 . 922 234 233 ILE H H 8.248 0.002 . 923 234 233 ILE CA C 61.587 0.012 . 924 234 233 ILE CB C 38.662 0.008 . 925 234 233 ILE N N 126.862 0.037 . 926 235 234 THR H H 9.059 0.002 . 927 235 234 THR C C 176.066 0.026 . 928 235 234 THR CA C 60.598 0.015 . 929 235 234 THR CB C 70.586 0.034 . 930 235 234 THR N N 119.722 0.040 . 931 236 235 SER H H 9.058 0.002 . 932 236 235 SER CA C 62.590 0.000 . 933 236 235 SER CB C 61.079 0.000 . 934 236 235 SER N N 118.176 0.043 . 935 238 237 GLU C C 178.962 0.015 . 936 238 237 GLU CA C 58.553 0.007 . 937 238 237 GLU CB C 29.172 0.000 . 938 239 238 ALA H H 8.606 0.002 . 939 239 238 ALA C C 179.732 0.009 . 940 239 238 ALA CA C 54.650 0.036 . 941 239 238 ALA CB C 17.072 0.015 . 942 239 238 ALA N N 119.276 0.043 . 943 240 239 LYS H H 8.116 0.002 . 944 240 239 LYS C C 176.821 0.036 . 945 240 239 LYS CA C 59.634 0.002 . 946 240 239 LYS CB C 30.270 0.051 . 947 240 239 LYS N N 121.644 0.037 . 948 241 240 ARG H H 7.484 0.003 . 949 241 240 ARG C C 179.766 0.000 . 950 241 240 ARG CA C 58.330 0.000 . 951 241 240 ARG CB C 40.579 0.000 . 952 241 240 ARG N N 118.929 0.036 . 953 242 241 MET H H 8.158 0.002 . 954 242 241 MET C C 178.731 0.000 . 955 242 241 MET CA C 56.992 0.000 . 956 242 241 MET CB C 33.263 0.000 . 957 242 241 MET N N 119.789 0.035 . 958 243 242 CYS C C 176.675 0.000 . 959 243 242 CYS CA C 64.779 0.010 . 960 243 242 CYS CB C 26.632 0.000 . 961 244 243 GLY H H 8.792 0.002 . 962 244 243 GLY C C 171.851 0.018 . 963 244 243 GLY CA C 47.448 0.014 . 964 244 243 GLY N N 105.522 0.048 . 965 245 244 LEU H H 6.194 0.002 . 966 245 244 LEU C C 178.485 0.000 . 967 245 244 LEU CA C 55.832 0.000 . 968 245 244 LEU CB C 39.542 0.000 . 969 245 244 LEU N N 121.230 0.032 . 970 250 249 GLY C C 176.052 0.000 . 971 250 249 GLY CA C 44.795 0.008 . 972 251 250 LEU H H 7.677 0.002 . 973 251 250 LEU C C 176.802 0.000 . 974 251 250 LEU CA C 56.205 0.000 . 975 251 250 LEU CB C 41.757 0.000 . 976 251 250 LEU N N 118.938 0.035 . 977 254 253 VAL C C 177.067 0.009 . 978 254 253 VAL CA C 67.620 0.036 . 979 254 253 VAL CB C 31.116 0.000 . 980 255 254 VAL H H 7.055 0.003 . 981 255 254 VAL C C 178.390 0.008 . 982 255 254 VAL CA C 64.269 0.019 . 983 255 254 VAL CB C 32.517 0.006 . 984 255 254 VAL N N 118.432 0.034 . 985 256 255 ASN H H 7.928 0.003 . 986 256 255 ASN C C 176.546 0.008 . 987 256 255 ASN CA C 56.778 0.005 . 988 256 255 ASN CB C 40.467 0.014 . 989 256 255 ASN N N 115.216 0.045 . 990 257 256 PHE H H 9.114 0.002 . 991 257 256 PHE C C 178.487 0.035 . 992 257 256 PHE CA C 63.840 0.044 . 993 257 256 PHE CB C 39.891 0.001 . 994 257 256 PHE N N 121.456 0.038 . 995 258 257 LEU H H 9.047 0.002 . 996 258 257 LEU C C 179.049 0.005 . 997 258 257 LEU CA C 58.000 0.013 . 998 258 257 LEU CB C 41.425 0.028 . 999 258 257 LEU N N 118.570 0.039 . 1000 259 258 SER H H 7.330 0.002 . 1001 259 258 SER CA C 63.017 0.000 . 1002 259 258 SER CB C 62.010 0.000 . 1003 259 258 SER N N 115.070 0.039 . 1004 260 259 PHE C C 177.774 0.006 . 1005 260 259 PHE CA C 57.042 0.000 . 1006 260 259 PHE CB C 39.714 0.000 . 1007 261 260 SER H H 7.030 0.002 . 1008 261 260 SER C C 173.968 0.004 . 1009 261 260 SER CA C 64.624 0.021 . 1010 261 260 SER CB C 69.125 0.010 . 1011 261 260 SER N N 108.257 0.043 . 1012 262 261 MET H H 6.485 0.002 . 1013 262 261 MET C C 175.136 0.000 . 1014 262 261 MET CA C 56.960 0.000 . 1015 262 261 MET CB C 32.552 0.000 . 1016 262 261 MET N N 118.377 0.041 . 1017 266 265 ALA C C 178.458 0.008 . 1018 266 265 ALA CA C 53.504 0.013 . 1019 266 265 ALA CB C 18.269 0.000 . 1020 267 266 LYS H H 7.282 0.002 . 1021 267 266 LYS C C 176.571 0.013 . 1022 267 266 LYS CA C 56.502 0.035 . 1023 267 266 LYS CB C 33.112 0.022 . 1024 267 266 LYS N N 115.960 0.045 . 1025 268 267 SER H H 7.184 0.003 . 1026 268 267 SER CA C 53.739 0.000 . 1027 268 267 SER CB C 60.811 0.000 . 1028 268 267 SER N N 114.461 0.042 . 1029 269 268 PRO C C 178.918 0.014 . 1030 269 268 PRO CA C 63.842 0.006 . 1031 269 268 PRO CB C 33.911 0.000 . 1032 270 269 GLU H H 8.759 0.001 . 1033 270 269 GLU C C 177.794 0.009 . 1034 270 269 GLU CA C 59.972 0.039 . 1035 270 269 GLU CB C 28.734 0.051 . 1036 270 269 GLU N N 127.659 0.042 . 1037 271 270 HIS H H 7.668 0.002 . 1038 271 270 HIS CA C 57.471 0.009 . 1039 271 270 HIS CB C 26.801 0.029 . 1040 271 270 HIS N N 113.269 0.032 . 1041 272 271 ARG H H 7.432 0.002 . 1042 272 271 ARG C C 179.402 0.000 . 1043 272 271 ARG CA C 60.452 0.000 . 1044 272 271 ARG CB C 29.137 0.000 . 1045 272 271 ARG N N 117.664 0.042 . 1046 274 273 GLU C C 178.385 0.000 . 1047 274 273 GLU CA C 58.039 0.000 . 1048 274 273 GLU CB C 31.602 0.000 . 1049 275 274 LEU H H 7.910 0.002 . 1050 275 274 LEU C C 178.763 0.068 . 1051 275 274 LEU CA C 54.493 0.036 . 1052 275 274 LEU CB C 43.012 0.011 . 1053 275 274 LEU N N 119.455 0.045 . 1054 276 275 ILE H H 7.639 0.004 . 1055 276 275 ILE C C 180.851 0.000 . 1056 276 275 ILE CA C 63.708 0.032 . 1057 276 275 ILE CB C 36.077 0.004 . 1058 276 275 ILE N N 121.410 0.041 . 1059 277 276 GLU H H 7.660 0.002 . 1060 277 276 GLU C C 177.686 0.000 . 1061 277 276 GLU CA C 66.352 0.019 . 1062 277 276 GLU CB C 30.797 0.045 . 1063 277 276 GLU N N 118.302 0.036 . 1064 278 277 ARG H H 8.921 0.002 . 1065 278 277 ARG C C 178.793 0.000 . 1066 278 277 ARG CA C 57.142 0.000 . 1067 278 277 ARG CB C 28.960 0.000 . 1068 278 277 ARG N N 116.156 0.038 . 1069 279 278 PRO C C 179.693 0.003 . 1070 279 278 PRO CA C 64.179 0.011 . 1071 279 278 PRO CB C 30.476 0.000 . 1072 280 279 GLU H H 10.043 0.002 . 1073 280 279 GLU C C 177.586 0.007 . 1074 280 279 GLU CA C 57.800 0.021 . 1075 280 279 GLU CB C 26.412 0.021 . 1076 280 279 GLU N N 121.864 0.041 . 1077 281 280 ARG H H 8.573 0.002 . 1078 281 280 ARG C C 176.308 0.007 . 1079 281 280 ARG CA C 56.025 0.015 . 1080 281 280 ARG CB C 29.520 0.005 . 1081 281 280 ARG N N 120.765 0.039 . 1082 282 281 ILE H H 7.858 0.002 . 1083 282 281 ILE C C 174.709 0.000 . 1084 282 281 ILE CA C 67.671 0.000 . 1085 282 281 ILE CB C 34.927 0.000 . 1086 282 281 ILE N N 119.824 0.037 . 1087 283 282 PRO C C 178.997 0.011 . 1088 283 282 PRO CA C 66.833 0.017 . 1089 283 282 PRO CB C 29.759 0.000 . 1090 284 283 ALA H H 7.808 0.001 . 1091 284 283 ALA C C 180.983 0.015 . 1092 284 283 ALA CA C 54.514 0.049 . 1093 284 283 ALA CB C 17.390 0.021 . 1094 284 283 ALA N N 122.324 0.034 . 1095 285 284 ALA H H 8.579 0.002 . 1096 285 284 ALA C C 178.979 0.000 . 1097 285 284 ALA CB C 16.980 0.000 . 1098 285 284 ALA N N 122.657 0.042 . 1099 288 287 GLU C C 174.347 0.000 . 1100 288 287 GLU CA C 63.816 0.000 . 1101 288 287 GLU CB C 31.137 0.000 . 1102 289 288 LEU H H 5.739 0.001 . 1103 289 288 LEU C C 172.387 0.004 . 1104 289 288 LEU CA C 53.498 0.014 . 1105 289 288 LEU CB C 39.469 0.009 . 1106 289 288 LEU N N 116.903 0.014 . 1107 290 289 LEU H H 5.929 0.002 . 1108 290 289 LEU C C 174.501 0.000 . 1109 290 289 LEU CA C 57.044 0.007 . 1110 290 289 LEU CB C 40.699 0.064 . 1111 290 289 LEU N N 121.413 0.039 . 1112 291 290 ARG H H 7.476 0.002 . 1113 291 290 ARG C C 177.361 0.003 . 1114 291 290 ARG CA C 58.442 0.067 . 1115 291 290 ARG CB C 28.352 0.011 . 1116 291 290 ARG N N 120.465 0.042 . 1117 292 291 ARG H H 8.210 0.002 . 1118 292 291 ARG C C 175.042 0.011 . 1119 292 291 ARG CA C 56.414 0.065 . 1120 292 291 ARG CB C 28.411 0.000 . 1121 292 291 ARG N N 119.201 0.041 . 1122 293 292 PHE H H 8.383 0.002 . 1123 293 292 PHE C C 171.364 0.003 . 1124 293 292 PHE CB C 35.929 0.000 . 1125 293 292 PHE N N 114.991 0.037 . 1126 294 293 SER H H 5.568 0.002 . 1127 294 293 SER C C 175.142 0.000 . 1128 294 293 SER CA C 60.070 0.000 . 1129 294 293 SER CB C 63.076 0.000 . 1130 294 293 SER N N 109.625 0.017 . 1131 296 295 VAL C C 172.388 0.044 . 1132 296 295 VAL CA C 61.191 0.013 . 1133 296 295 VAL CB C 30.877 0.000 . 1134 297 296 ALA H H 8.708 0.002 . 1135 297 296 ALA C C 172.460 0.005 . 1136 297 296 ALA CA C 51.710 0.017 . 1137 297 296 ALA CB C 21.458 0.002 . 1138 297 296 ALA N N 127.298 0.038 . 1139 298 297 ASP H H 7.469 0.002 . 1140 298 297 ASP C C 173.083 0.014 . 1141 298 297 ASP CA C 49.976 0.031 . 1142 298 297 ASP CB C 37.153 0.012 . 1143 298 297 ASP N N 119.657 0.036 . 1144 299 298 GLY H H 7.540 0.002 . 1145 299 298 GLY C C 172.623 0.011 . 1146 299 298 GLY CA C 44.939 0.006 . 1147 299 298 GLY N N 102.302 0.039 . 1148 300 299 ARG H H 8.417 0.002 . 1149 300 299 ARG C C 173.905 0.017 . 1150 300 299 ARG CA C 51.962 0.009 . 1151 300 299 ARG CB C 36.142 0.018 . 1152 300 299 ARG N N 117.315 0.035 . 1153 301 300 ILE H H 9.425 0.003 . 1154 301 300 ILE C C 172.748 0.007 . 1155 301 300 ILE CA C 58.564 0.008 . 1156 301 300 ILE CB C 41.275 0.012 . 1157 301 300 ILE N N 121.238 0.036 . 1158 302 301 LEU H H 8.730 0.002 . 1159 302 301 LEU C C 181.268 0.010 . 1160 302 301 LEU CA C 51.624 0.043 . 1161 302 301 LEU CB C 39.248 0.059 . 1162 302 301 LEU N N 131.026 0.040 . 1163 303 302 THR H H 8.603 0.002 . 1164 303 302 THR C C 174.023 0.004 . 1165 303 302 THR CA C 61.838 0.011 . 1166 303 302 THR CB C 69.002 0.033 . 1167 303 302 THR N N 116.235 0.039 . 1168 304 303 SER H H 7.565 0.003 . 1169 304 303 SER C C 171.389 0.007 . 1170 304 303 SER CA C 55.955 0.009 . 1171 304 303 SER CB C 64.885 0.027 . 1172 304 303 SER N N 112.651 0.038 . 1173 305 304 ASP H H 8.486 0.002 . 1174 305 304 ASP C C 177.148 0.020 . 1175 305 304 ASP CA C 54.535 0.006 . 1176 305 304 ASP CB C 38.727 0.020 . 1177 305 304 ASP N N 120.948 0.036 . 1178 306 305 TYR C C 171.963 0.008 . 1179 306 305 TYR CA C 56.029 0.000 . 1180 306 305 TYR CB C 40.749 0.000 . 1181 307 306 GLU H H 8.004 0.342 . 1182 307 306 GLU C C 172.676 0.407 . 1183 307 306 GLU CA C 54.415 0.002 . 1184 307 306 GLU CB C 28.888 0.003 . 1185 307 306 GLU N N 128.208 1.936 . 1186 308 307 PHE H H 8.459 0.002 . 1187 308 307 PHE C C 173.545 0.040 . 1188 308 307 PHE CA C 54.054 0.030 . 1189 308 307 PHE CB C 41.708 0.008 . 1190 308 307 PHE N N 129.492 0.038 . 1191 309 308 HIS H H 9.058 0.001 . 1192 309 308 HIS CA C 56.555 0.033 . 1193 309 308 HIS CB C 25.623 0.042 . 1194 309 308 HIS N N 123.396 0.035 . 1195 310 309 GLY H H 8.365 0.002 . 1196 310 309 GLY C C 173.425 0.004 . 1197 310 309 GLY CA C 44.688 0.013 . 1198 310 309 GLY N N 102.489 0.037 . 1199 311 310 VAL H H 7.454 0.002 . 1200 311 310 VAL C C 174.626 0.005 . 1201 311 310 VAL CA C 60.825 0.013 . 1202 311 310 VAL CB C 32.223 0.000 . 1203 311 310 VAL N N 123.635 0.040 . 1204 312 311 GLN H H 8.394 0.002 . 1205 312 311 GLN C C 173.508 0.021 . 1206 312 311 GLN CA C 55.550 0.028 . 1207 312 311 GLN CB C 27.246 0.023 . 1208 312 311 GLN N N 125.671 0.035 . 1209 313 312 LEU H H 8.595 0.001 . 1210 313 312 LEU C C 177.344 0.012 . 1211 313 312 LEU CA C 53.177 0.043 . 1212 313 312 LEU CB C 40.503 0.031 . 1213 313 312 LEU N N 128.152 0.037 . 1214 314 313 LYS H H 8.542 0.003 . 1215 314 313 LYS C C 175.461 0.003 . 1216 314 313 LYS CA C 53.058 0.002 . 1217 314 313 LYS CB C 33.414 0.000 . 1218 314 313 LYS N N 124.588 0.038 . 1219 315 314 LYS H H 8.719 0.002 . 1220 315 314 LYS C C 177.471 0.005 . 1221 315 314 LYS CA C 58.303 0.019 . 1222 315 314 LYS CB C 31.639 0.008 . 1223 315 314 LYS N N 121.618 0.036 . 1224 316 315 GLY H H 8.565 0.002 . 1225 316 315 GLY C C 174.178 0.021 . 1226 316 315 GLY CA C 44.626 0.017 . 1227 316 315 GLY N N 117.102 0.041 . 1228 317 316 ASP H H 8.953 0.001 . 1229 317 316 ASP C C 176.008 0.004 . 1230 317 316 ASP CA C 55.106 0.010 . 1231 317 316 ASP CB C 41.060 0.080 . 1232 317 316 ASP N N 122.597 0.031 . 1233 318 317 GLN H H 9.445 0.002 . 1234 318 317 GLN C C 174.880 0.029 . 1235 318 317 GLN CA C 55.314 0.042 . 1236 318 317 GLN CB C 32.599 0.059 . 1237 318 317 GLN N N 118.781 0.036 . 1238 319 318 ILE H H 8.814 0.002 . 1239 319 318 ILE C C 171.933 0.000 . 1240 319 318 ILE CA C 57.309 0.000 . 1241 319 318 ILE CB C 41.729 0.000 . 1242 322 321 PRO C C 175.477 0.004 . 1243 322 321 PRO CA C 63.097 0.000 . 1244 322 321 PRO CB C 30.642 0.000 . 1245 323 322 GLN H H 9.670 0.001 . 1246 323 322 GLN C C 178.327 0.008 . 1247 323 322 GLN CA C 61.929 0.025 . 1248 323 322 GLN CB C 23.423 0.003 . 1249 323 322 GLN N N 134.731 0.041 . 1250 324 323 MET H H 7.686 0.002 . 1251 324 323 MET C C 176.750 0.007 . 1252 324 323 MET CA C 55.935 0.000 . 1253 324 323 MET CB C 34.212 0.008 . 1254 324 323 MET N N 113.492 0.041 . 1255 325 324 LEU H H 7.231 0.002 . 1256 325 324 LEU C C 180.173 0.000 . 1257 325 324 LEU CA C 55.839 0.093 . 1258 325 324 LEU CB C 40.264 0.000 . 1259 325 324 LEU N N 113.700 0.037 . 1260 327 326 GLY C C 175.142 0.000 . 1261 327 326 GLY CA C 45.742 0.013 . 1262 328 327 LEU H H 6.743 0.002 . 1263 328 327 LEU C C 173.482 0.009 . 1264 328 327 LEU CA C 53.193 0.047 . 1265 328 327 LEU CB C 39.899 0.027 . 1266 328 327 LEU N N 119.426 0.027 . 1267 329 328 ASP H H 6.679 0.002 . 1268 329 328 ASP C C 178.603 0.009 . 1269 329 328 ASP CA C 53.216 0.014 . 1270 329 328 ASP CB C 42.206 0.006 . 1271 329 328 ASP N N 118.536 0.047 . 1272 330 329 GLU H H 9.457 0.001 . 1273 330 329 GLU C C 177.017 0.015 . 1274 330 329 GLU CA C 56.828 0.011 . 1275 330 329 GLU CB C 27.657 0.017 . 1276 330 329 GLU N N 131.722 0.038 . 1277 331 330 ARG H H 8.698 0.002 . 1278 331 330 ARG C C 177.784 0.000 . 1279 331 330 ARG CA C 57.312 0.000 . 1280 331 330 ARG CB C 29.010 0.000 . 1281 331 330 ARG N N 118.660 0.040 . 1282 332 331 GLU C C 176.341 0.002 . 1283 332 331 GLU CA C 56.520 0.001 . 1284 332 331 GLU CB C 30.875 0.000 . 1285 333 332 ASN H H 7.819 0.002 . 1286 333 332 ASN C C 171.521 0.006 . 1287 333 332 ASN CA C 51.818 0.047 . 1288 333 332 ASN CB C 42.450 0.001 . 1289 333 332 ASN N N 116.332 0.042 . 1290 334 333 ALA H H 8.525 0.002 . 1291 334 333 ALA C C 178.264 0.010 . 1292 334 333 ALA CA C 51.950 0.009 . 1293 334 333 ALA CB C 17.824 0.016 . 1294 334 333 ALA N N 124.027 0.040 . 1295 335 334 ALA H H 9.212 0.001 . 1296 335 334 ALA C C 176.551 0.000 . 1297 335 334 ALA CB C 16.258 0.000 . 1298 335 334 ALA N N 122.700 0.038 . 1299 336 335 PRO C C 179.793 0.012 . 1300 336 335 PRO CA C 63.670 0.041 . 1301 336 335 PRO CB C 32.401 0.000 . 1302 337 336 MET H H 8.727 0.002 . 1303 337 336 MET CA C 53.743 0.013 . 1304 337 336 MET CB C 29.375 0.006 . 1305 337 336 MET N N 115.613 0.039 . 1306 338 337 HIS H H 8.104 0.002 . 1307 338 337 HIS CA C 54.966 0.012 . 1308 338 337 HIS CB C 29.996 0.051 . 1309 338 337 HIS N N 123.313 0.043 . 1310 339 338 VAL H H 8.129 0.002 . 1311 339 338 VAL C C 174.825 0.004 . 1312 339 338 VAL CA C 61.354 0.013 . 1313 339 338 VAL CB C 29.424 0.042 . 1314 339 338 VAL N N 126.720 0.037 . 1315 340 339 ASP H H 10.179 0.002 . 1316 340 339 ASP C C 176.622 0.016 . 1317 340 339 ASP CA C 51.329 0.033 . 1318 340 339 ASP CB C 41.517 0.046 . 1319 340 339 ASP N N 131.244 0.038 . 1320 341 340 PHE H H 9.591 0.001 . 1321 341 340 PHE C C 177.135 0.005 . 1322 341 340 PHE CA C 55.471 0.011 . 1323 341 340 PHE CB C 35.153 0.005 . 1324 341 340 PHE N N 124.258 0.037 . 1325 342 341 SER H H 8.734 0.002 . 1326 342 341 SER C C 173.932 0.000 . 1327 342 341 SER CA C 57.512 0.008 . 1328 342 341 SER CB C 62.707 0.002 . 1329 342 341 SER N N 116.007 0.036 . 1330 343 342 ARG H H 7.239 0.002 . 1331 343 342 ARG C C 177.080 0.000 . 1332 343 342 ARG CB C 30.436 0.000 . 1333 343 342 ARG N N 124.119 0.040 . 1334 344 343 GLN C C 176.227 0.000 . 1335 344 343 GLN CA C 57.370 0.000 . 1336 344 343 GLN CB C 28.412 0.000 . 1337 345 344 LYS H H 8.377 0.010 . 1338 345 344 LYS C C 174.627 0.009 . 1339 345 344 LYS CA C 54.937 0.007 . 1340 345 344 LYS CB C 31.959 0.060 . 1341 345 344 LYS N N 120.552 0.047 . 1342 346 345 VAL H H 8.668 0.014 . 1343 346 345 VAL C C 175.164 0.006 . 1344 346 345 VAL CA C 62.407 0.020 . 1345 346 345 VAL CB C 30.867 0.014 . 1346 346 345 VAL N N 126.763 0.109 . 1347 347 346 SER H H 8.079 0.002 . 1348 347 346 SER C C 174.154 0.000 . 1349 347 346 SER CA C 56.118 0.015 . 1350 347 346 SER CB C 62.855 0.016 . 1351 347 346 SER N N 123.309 0.041 . 1352 348 347 HIS H H 8.216 0.002 . 1353 348 347 HIS CA C 55.564 0.000 . 1354 348 347 HIS CB C 31.656 0.000 . 1355 348 347 HIS N N 121.526 0.036 . 1356 349 348 THR C C 177.734 0.000 . 1357 349 348 THR CA C 59.370 0.000 . 1358 349 348 THR CB C 68.468 0.000 . 1359 350 349 THR H H 11.774 0.002 . 1360 350 349 THR C C 173.385 0.000 . 1361 350 349 THR CA C 66.359 0.006 . 1362 350 349 THR CB C 67.094 0.006 . 1363 350 349 THR N N 128.900 0.038 . 1364 351 350 PHE H H 8.097 0.003 . 1365 351 350 PHE C C 172.203 0.000 . 1366 351 350 PHE CA C 57.102 0.007 . 1367 351 350 PHE CB C 40.939 0.037 . 1368 351 350 PHE N N 114.561 0.038 . 1369 352 351 GLY H H 6.901 0.001 . 1370 352 351 GLY C C 172.203 0.000 . 1371 352 351 GLY CA C 42.915 0.000 . 1372 352 351 GLY N N 104.481 0.043 . 1373 353 352 HIS H H 7.829 0.001 . 1374 353 352 HIS CA C 56.640 0.020 . 1375 353 352 HIS CB C 33.235 0.010 . 1376 353 352 HIS N N 118.002 0.014 . 1377 354 353 GLY H H 8.060 0.002 . 1378 354 353 GLY C C 175.781 0.000 . 1379 354 353 GLY CA C 43.846 0.043 . 1380 354 353 GLY N N 114.413 0.039 . 1381 355 354 SER H H 9.414 0.001 . 1382 355 354 SER C C 176.672 0.000 . 1383 355 354 SER CA C 61.455 0.033 . 1384 355 354 SER CB C 62.571 0.021 . 1385 355 354 SER N N 119.930 0.029 . 1386 356 355 HIS H H 8.549 0.002 . 1387 356 355 HIS CA C 55.374 0.023 . 1388 356 355 HIS CB C 27.097 0.009 . 1389 356 355 HIS N N 119.295 0.039 . 1390 357 356 LEU H H 6.949 0.003 . 1391 357 356 LEU CA C 61.669 0.000 . 1392 357 356 LEU CB C 42.732 0.000 . 1393 357 356 LEU N N 119.091 0.044 . 1394 359 358 LEU CA C 59.208 0.000 . 1395 359 358 LEU CB C 32.118 0.000 . 1396 360 359 GLY H H 7.073 0.002 . 1397 360 359 GLY C C 173.604 0.012 . 1398 360 359 GLY CA C 43.645 0.007 . 1399 360 359 GLY N N 105.808 0.049 . 1400 361 360 GLN H H 8.683 0.001 . 1401 361 360 GLN C C 178.207 0.009 . 1402 361 360 GLN CA C 59.373 0.050 . 1403 361 360 GLN CB C 29.136 0.013 . 1404 361 360 GLN N N 118.107 0.030 . 1405 362 361 HIS H H 7.040 0.003 . 1406 362 361 HIS CA C 55.519 0.009 . 1407 362 361 HIS CB C 40.042 0.064 . 1408 362 361 HIS N N 115.340 0.051 . 1409 363 362 LEU H H 7.088 0.002 . 1410 363 362 LEU C C 175.158 0.000 . 1411 363 362 LEU CA C 54.062 0.000 . 1412 363 362 LEU CB C 44.221 0.000 . 1413 363 362 LEU N N 118.733 0.039 . 1414 370 369 VAL H H 8.827 0.002 . 1415 370 369 VAL C C 174.266 0.015 . 1416 370 369 VAL CA C 54.590 0.004 . 1417 370 369 VAL CB C 34.919 0.000 . 1418 370 369 VAL N N 118.790 0.042 . 1419 371 370 THR H H 8.823 0.002 . 1420 371 370 THR C C 173.475 0.000 . 1421 371 370 THR CA C 54.920 0.000 . 1422 371 370 THR CB C 65.390 0.000 . 1423 371 370 THR N N 117.207 0.044 . 1424 375 374 TRP C C 178.235 0.003 . 1425 375 374 TRP CA C 63.025 0.009 . 1426 375 374 TRP CB C 31.046 0.000 . 1427 381 380 ASP H H 8.170 0.002 . 1428 381 380 ASP C C 174.341 0.016 . 1429 381 380 ASP CA C 52.862 0.018 . 1430 381 380 ASP CB C 42.618 0.007 . 1431 381 380 ASP N N 116.360 0.044 . 1432 382 381 PHE H H 6.652 0.002 . 1433 382 381 PHE C C 172.010 0.000 . 1434 382 381 PHE CA C 54.958 0.000 . 1435 382 381 PHE CB C 39.264 0.000 . 1436 382 381 PHE N N 118.871 0.042 . 1437 383 382 SER C C 173.486 0.000 . 1438 383 382 SER CA C 56.544 0.000 . 1439 383 382 SER CB C 66.537 0.000 . 1440 384 383 ILE H H 8.556 0.002 . 1441 384 383 ILE C C 177.020 0.014 . 1442 384 383 ILE CA C 60.321 0.030 . 1443 384 383 ILE CB C 35.935 0.021 . 1444 384 383 ILE N N 122.352 0.040 . 1445 385 384 ALA H H 8.224 0.002 . 1446 385 384 ALA C C 175.119 0.000 . 1447 385 384 ALA CA C 50.750 0.000 . 1448 385 384 ALA CB C 17.012 0.000 . 1449 385 384 ALA N N 131.446 0.039 . 1450 387 386 GLY C C 174.089 0.005 . 1451 387 386 GLY CA C 44.907 0.000 . 1452 388 387 ALA H H 7.669 0.002 . 1453 388 387 ALA C C 177.067 0.009 . 1454 388 387 ALA CA C 52.187 0.009 . 1455 388 387 ALA CB C 18.977 0.002 . 1456 388 387 ALA N N 123.632 0.030 . 1457 389 388 GLN H H 8.489 0.004 . 1458 389 388 GLN C C 174.984 0.005 . 1459 389 388 GLN CA C 53.852 0.057 . 1460 389 388 GLN CB C 29.008 0.019 . 1461 389 388 GLN N N 122.285 0.039 . 1462 390 389 ILE H H 8.628 0.001 . 1463 390 389 ILE C C 175.996 0.010 . 1464 390 389 ILE CA C 58.933 0.007 . 1465 390 389 ILE CB C 34.511 0.008 . 1466 390 389 ILE N N 126.412 0.037 . 1467 391 390 GLN H H 9.617 0.002 . 1468 391 390 GLN C C 174.773 0.036 . 1469 391 390 GLN CA C 54.121 0.035 . 1470 391 390 GLN CB C 30.426 0.025 . 1471 391 390 GLN N N 129.519 0.039 . 1472 392 391 HIS H H 8.938 0.001 . 1473 392 391 HIS CA C 52.566 0.009 . 1474 392 391 HIS CB C 34.412 0.008 . 1475 392 391 HIS N N 124.876 0.043 . 1476 393 392 LYS H H 8.976 0.002 . 1477 393 392 LYS C C 174.490 0.005 . 1478 393 392 LYS CA C 54.798 0.016 . 1479 393 392 LYS CB C 35.459 0.019 . 1480 393 392 LYS N N 119.385 0.048 . 1481 394 393 SER H H 8.966 0.002 . 1482 394 393 SER C C 173.683 0.001 . 1483 394 393 SER CA C 55.218 0.054 . 1484 394 393 SER CB C 65.326 0.003 . 1485 394 393 SER N N 117.586 0.037 . 1486 395 394 GLY H H 7.085 0.002 . 1487 395 394 GLY C C 171.749 0.006 . 1488 395 394 GLY CA C 45.732 0.004 . 1489 395 394 GLY N N 110.613 0.044 . 1490 396 395 ILE H H 8.374 0.002 . 1491 396 395 ILE C C 176.454 0.002 . 1492 396 395 ILE CA C 61.691 0.037 . 1493 396 395 ILE CB C 36.471 0.017 . 1494 396 395 ILE N N 124.829 0.024 . 1495 397 396 VAL H H 6.366 0.002 . 1496 397 396 VAL C C 177.416 0.007 . 1497 397 396 VAL CA C 60.849 0.012 . 1498 397 396 VAL CB C 34.334 0.025 . 1499 397 396 VAL N N 113.401 0.036 . 1500 398 397 SER H H 8.673 0.002 . 1501 398 397 SER C C 172.413 0.002 . 1502 398 397 SER CA C 61.243 0.067 . 1503 398 397 SER CB C 63.791 0.010 . 1504 398 397 SER N N 125.931 0.042 . 1505 399 398 GLY H H 8.957 0.002 . 1506 399 398 GLY C C 171.572 0.013 . 1507 399 398 GLY CA C 44.997 0.009 . 1508 399 398 GLY N N 102.308 0.043 . 1509 400 399 VAL H H 7.092 0.002 . 1510 400 399 VAL C C 176.433 0.007 . 1511 400 399 VAL CA C 60.681 0.033 . 1512 400 399 VAL CB C 33.039 0.005 . 1513 400 399 VAL N N 118.006 0.026 . 1514 401 400 GLN H H 8.827 0.378 . 1515 401 400 GLN HE21 H 6.900 0.000 . 1516 401 400 GLN HE22 H 7.460 0.000 . 1517 401 400 GLN C C 175.470 0.018 . 1518 401 400 GLN CA C 59.070 0.002 . 1519 401 400 GLN CB C 28.678 0.012 . 1520 401 400 GLN N N 125.604 0.038 . 1521 401 400 GLN NE2 N 112.938 0.139 . 1522 402 401 ALA H H 7.378 0.002 . 1523 402 401 ALA C C 175.449 0.000 . 1524 402 401 ALA CA C 51.807 0.037 . 1525 402 401 ALA CB C 20.839 0.003 . 1526 402 401 ALA N N 117.417 0.038 . 1527 403 402 LEU H H 8.725 0.002 . 1528 403 402 LEU C C 170.507 0.000 . 1529 403 402 LEU CB C 43.034 0.000 . 1530 403 402 LEU N N 119.784 0.038 . 1531 409 408 PRO C C 178.259 0.020 . 1532 409 408 PRO CA C 64.734 0.017 . 1533 409 408 PRO CB C 31.883 0.000 . 1534 410 409 ALA H H 8.687 0.002 . 1535 410 409 ALA C C 178.726 0.020 . 1536 410 409 ALA CA C 54.021 0.010 . 1537 410 409 ALA CB C 17.621 0.024 . 1538 410 409 ALA N N 121.400 0.038 . 1539 411 410 THR H H 8.161 0.003 . 1540 411 410 THR C C 174.676 0.004 . 1541 411 410 THR CA C 61.509 0.023 . 1542 411 410 THR CB C 69.807 0.017 . 1543 411 410 THR N N 108.153 0.038 . 1544 412 411 THR H H 7.318 0.002 . 1545 412 411 THR C C 174.004 0.058 . 1546 412 411 THR CA C 60.434 0.003 . 1547 412 411 THR CB C 70.888 0.014 . 1548 412 411 THR N N 112.844 0.034 . 1549 413 412 LYS H H 8.985 0.002 . 1550 413 412 LYS C C 173.916 0.002 . 1551 413 412 LYS CA C 54.839 0.006 . 1552 413 412 LYS CB C 33.887 0.005 . 1553 413 412 LYS N N 120.839 0.039 . 1554 414 413 ALA H H 8.068 0.002 . 1555 414 413 ALA C C 177.211 0.005 . 1556 414 413 ALA CA C 50.995 0.011 . 1557 414 413 ALA CB C 18.316 0.007 . 1558 414 413 ALA N N 125.210 0.036 . 1559 415 414 VAL H H 7.992 0.002 . 1560 415 414 VAL C C 181.092 0.000 . 1561 415 414 VAL CA C 63.640 0.000 . 1562 415 414 VAL CB C 32.650 0.000 . 1563 415 414 VAL N N 126.887 0.038 . stop_ save_