data_17415 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Reduced and CO-bound cytochrome P450cam (CYP101A1) ; _BMRB_accession_number 17415 _BMRB_flat_file_name bmr17415.str _Entry_type original _Submission_date 2011-01-19 _Accession_date 2011-01-19 _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 Pochapsky Thomas C. . 2 Pochapsky Susan S. . 3 Dang Marina . . 4 Asciutto Eliana . . 5 Madura Jeffry . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 298 "13C chemical shifts" 596 "15N chemical shifts" 295 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-04-01 update BMRB 'update audit loop' 2011-03-24 update BMRB 'update entry citation' 2011-02-23 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 5759 'oxidized CYP101A1' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Experimentally Restrained Molecular Dynamics Simulations for Characterizing the Open States of Cytochrome P450(cam).' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21265500 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Asciutto Eliana K. . 2 Dang Marina . . 3 Pochapsky 'Susan Sondej' . . 4 Madura Jeffry D. . 5 Pochapsky Thomas C. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 50 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1664 _Page_last 1671 _Year 2011 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'cytochrome P450cam' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'cytochrome P450cam' $entity_1 CAM $CAM 'PROTOPORPHYRIN IX CONTAINING FE' $HEM 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 45643.371 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 413 _Mol_residue_sequence ; TETIQSNANLAPLPPHVPEH LVFDFDMYNPSNLSAGVQEA WAVLQESNVPDLVWTRCNGG HWIATRGQLIREAYEDYRHF SSECPFIPREAGEAYDFIPT SMDPPEQRQFRALANQVVGM PVVDKLENRIQELACSLIES LRPQGQCNFTEDYAEPFPIR IFMLLAGLPEEDIPHLKYLT DQMTRPDGSMTFAEAKEALY DYLIPIIEQRRQKPGTDAIS IVANGQVNGRPITSDEAKRM CGLLLVGGLDTVVNFLSFSM EFLAKSPEHRQELIERPERI PAACEELLRRFSLVADGRIL TSDYEFHGVQLKKGDQILLP QMLSGLDERENACPMHVDFS RQKVSHTTFGHGSHLCLGQH LARREIIVTLKEWLTRIPDF SIAPGAQIQHKSGIVSGVQA LPLVWDPATTKAV ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 2 THR 2 3 GLU 3 4 THR 4 5 ILE 5 6 GLN 6 7 SER 7 8 ASN 8 9 ALA 9 10 ASN 10 11 LEU 11 12 ALA 12 13 PRO 13 14 LEU 14 15 PRO 15 16 PRO 16 17 HIS 17 18 VAL 18 19 PRO 19 20 GLU 20 21 HIS 21 22 LEU 22 23 VAL 23 24 PHE 24 25 ASP 25 26 PHE 26 27 ASP 27 28 MET 28 29 TYR 29 30 ASN 30 31 PRO 31 32 SER 32 33 ASN 33 34 LEU 34 35 SER 35 36 ALA 36 37 GLY 37 38 VAL 38 39 GLN 39 40 GLU 40 41 ALA 41 42 TRP 42 43 ALA 43 44 VAL 44 45 LEU 45 46 GLN 46 47 GLU 47 48 SER 48 49 ASN 49 50 VAL 50 51 PRO 51 52 ASP 52 53 LEU 53 54 VAL 54 55 TRP 55 56 THR 56 57 ARG 57 58 CYS 58 59 ASN 59 60 GLY 60 61 GLY 61 62 HIS 62 63 TRP 63 64 ILE 64 65 ALA 65 66 THR 66 67 ARG 67 68 GLY 68 69 GLN 69 70 LEU 70 71 ILE 71 72 ARG 72 73 GLU 73 74 ALA 74 75 TYR 75 76 GLU 76 77 ASP 77 78 TYR 78 79 ARG 79 80 HIS 80 81 PHE 81 82 SER 82 83 SER 83 84 GLU 84 85 CYS 85 86 PRO 86 87 PHE 87 88 ILE 88 89 PRO 89 90 ARG 90 91 GLU 91 92 ALA 92 93 GLY 93 94 GLU 94 95 ALA 95 96 TYR 96 97 ASP 97 98 PHE 98 99 ILE 99 100 PRO 100 101 THR 101 102 SER 102 103 MET 103 104 ASP 104 105 PRO 105 106 PRO 106 107 GLU 107 108 GLN 108 109 ARG 109 110 GLN 110 111 PHE 111 112 ARG 112 113 ALA 113 114 LEU 114 115 ALA 115 116 ASN 116 117 GLN 117 118 VAL 118 119 VAL 119 120 GLY 120 121 MET 121 122 PRO 122 123 VAL 123 124 VAL 124 125 ASP 125 126 LYS 126 127 LEU 127 128 GLU 128 129 ASN 129 130 ARG 130 131 ILE 131 132 GLN 132 133 GLU 133 134 LEU 134 135 ALA 135 136 CYS 136 137 SER 137 138 LEU 138 139 ILE 139 140 GLU 140 141 SER 141 142 LEU 142 143 ARG 143 144 PRO 144 145 GLN 145 146 GLY 146 147 GLN 147 148 CYS 148 149 ASN 149 150 PHE 150 151 THR 151 152 GLU 152 153 ASP 153 154 TYR 154 155 ALA 155 156 GLU 156 157 PRO 157 158 PHE 158 159 PRO 159 160 ILE 160 161 ARG 161 162 ILE 162 163 PHE 163 164 MET 164 165 LEU 165 166 LEU 166 167 ALA 167 168 GLY 168 169 LEU 169 170 PRO 170 171 GLU 171 172 GLU 172 173 ASP 173 174 ILE 174 175 PRO 175 176 HIS 176 177 LEU 177 178 LYS 178 179 TYR 179 180 LEU 180 181 THR 181 182 ASP 182 183 GLN 183 184 MET 184 185 THR 185 186 ARG 186 187 PRO 187 188 ASP 188 189 GLY 189 190 SER 190 191 MET 191 192 THR 192 193 PHE 193 194 ALA 194 195 GLU 195 196 ALA 196 197 LYS 197 198 GLU 198 199 ALA 199 200 LEU 200 201 TYR 201 202 ASP 202 203 TYR 203 204 LEU 204 205 ILE 205 206 PRO 206 207 ILE 207 208 ILE 208 209 GLU 209 210 GLN 210 211 ARG 211 212 ARG 212 213 GLN 213 214 LYS 214 215 PRO 215 216 GLY 216 217 THR 217 218 ASP 218 219 ALA 219 220 ILE 220 221 SER 221 222 ILE 222 223 VAL 223 224 ALA 224 225 ASN 225 226 GLY 226 227 GLN 227 228 VAL 228 229 ASN 229 230 GLY 230 231 ARG 231 232 PRO 232 233 ILE 233 234 THR 234 235 SER 235 236 ASP 236 237 GLU 237 238 ALA 238 239 LYS 239 240 ARG 240 241 MET 241 242 CYS 242 243 GLY 243 244 LEU 244 245 LEU 245 246 LEU 246 247 VAL 247 248 GLY 248 249 GLY 249 250 LEU 250 251 ASP 251 252 THR 252 253 VAL 253 254 VAL 254 255 ASN 255 256 PHE 256 257 LEU 257 258 SER 258 259 PHE 259 260 SER 260 261 MET 261 262 GLU 262 263 PHE 263 264 LEU 264 265 ALA 265 266 LYS 266 267 SER 267 268 PRO 268 269 GLU 269 270 HIS 270 271 ARG 271 272 GLN 272 273 GLU 273 274 LEU 274 275 ILE 275 276 GLU 276 277 ARG 277 278 PRO 278 279 GLU 279 280 ARG 280 281 ILE 281 282 PRO 282 283 ALA 283 284 ALA 284 285 CYS 285 286 GLU 286 287 GLU 287 288 LEU 288 289 LEU 289 290 ARG 290 291 ARG 291 292 PHE 292 293 SER 293 294 LEU 294 295 VAL 295 296 ALA 296 297 ASP 297 298 GLY 298 299 ARG 299 300 ILE 300 301 LEU 301 302 THR 302 303 SER 303 304 ASP 304 305 TYR 305 306 GLU 306 307 PHE 307 308 HIS 308 309 GLY 309 310 VAL 310 311 GLN 311 312 LEU 312 313 LYS 313 314 LYS 314 315 GLY 315 316 ASP 316 317 GLN 317 318 ILE 318 319 LEU 319 320 LEU 320 321 PRO 321 322 GLN 322 323 MET 323 324 LEU 324 325 SER 325 326 GLY 326 327 LEU 327 328 ASP 328 329 GLU 329 330 ARG 330 331 GLU 331 332 ASN 332 333 ALA 333 334 CYS 334 335 PRO 335 336 MET 336 337 HIS 337 338 VAL 338 339 ASP 339 340 PHE 340 341 SER 341 342 ARG 342 343 GLN 343 344 LYS 344 345 VAL 345 346 SER 346 347 HIS 347 348 THR 348 349 THR 349 350 PHE 350 351 GLY 351 352 HIS 352 353 GLY 353 354 SER 354 355 HIS 355 356 LEU 356 357 CYS 357 358 LEU 358 359 GLY 359 360 GLN 360 361 HIS 361 362 LEU 362 363 ALA 363 364 ARG 364 365 ARG 365 366 GLU 366 367 ILE 367 368 ILE 368 369 VAL 369 370 THR 370 371 LEU 371 372 LYS 372 373 GLU 373 374 TRP 374 375 LEU 375 376 THR 376 377 ARG 377 378 ILE 378 379 PRO 379 380 ASP 380 381 PHE 381 382 SER 382 383 ILE 383 384 ALA 384 385 PRO 385 386 GLY 386 387 ALA 387 388 GLN 388 389 ILE 389 390 GLN 390 391 HIS 391 392 LYS 392 393 SER 393 394 GLY 394 395 ILE 395 396 VAL 396 397 SER 397 398 GLY 398 399 VAL 399 400 GLN 400 401 ALA 401 402 LEU 402 403 PRO 403 404 LEU 404 405 VAL 405 406 TRP 406 407 ASP 407 408 PRO 408 409 ALA 409 410 THR 410 411 THR 411 412 LYS 412 413 ALA 413 414 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-18 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 99.76 100.00 0.00e+00 BMRB 19038 entity_1 97.82 404 99.75 100.00 0.00e+00 BMRB 19740 CYP101 100.00 414 99.76 99.76 0.00e+00 BMRB 19763 CYP101 100.00 414 99.76 99.76 0.00e+00 PDB 1AKD "Cytochrome P450cam From Pseudomonas Putida, Complexed With 1s-Camphor" 100.00 414 99.76 100.00 0.00e+00 PDB 1C8J "Crystal Structure Of Cytochrome P450cam Mutant (F87wY96F)" 100.00 414 99.52 100.00 0.00e+00 PDB 1CP4 "Formation, Crystal Structure, And Rearrangement Of A Cytochrome P450-Cam Iron-Phenyl Complex" 100.00 414 100.00 100.00 0.00e+00 PDB 1DZ4 "Ferric P450cam From Pseudomonas Putida" 100.00 414 99.76 100.00 0.00e+00 PDB 1DZ6 "Ferrous P450cam From Pseudomonas Putida" 100.00 414 99.76 100.00 0.00e+00 PDB 1DZ8 "Oxygen Complex Of P450cam From Pseudomonas Putida" 100.00 414 99.76 100.00 0.00e+00 PDB 1DZ9 "Putative Oxo Complex Of P450cam From Pseudomonas Putida" 100.00 414 99.76 100.00 0.00e+00 PDB 1GEB "X-Ray Crystal Structure And Catalytic Properties Of Thr252ile Mutant Of Cytochrome P450cam" 100.00 415 99.76 99.76 0.00e+00 PDB 1GEK "Structural Characterization Of N-Butyl-Isocyanide Complexes Of Cytochromes P450nor And P450cam" 100.00 415 100.00 100.00 0.00e+00 PDB 1GEM "Structural Characterization Of N-Butyl-Isocyanide Complexes Of Cytochromes P450nor And P450cam" 100.00 415 100.00 100.00 0.00e+00 PDB 1GJM "Covalent Attachment Of An Electroactive Sulphydryl Reagent In The Active Site Of Cytochrome P450cam" 100.00 414 99.76 99.76 0.00e+00 PDB 1IWI "Putidaredoxin-Binding Stablilizes An Active Conformer Of Cytochrome P450cam In Its Reduced State; Crystal Structure Of Cytochro" 100.00 415 100.00 100.00 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 99.76 100.00 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 99.76 100.00 0.00e+00 PDB 1J51 "Crystal Structure Of Cytochrome P450cam Mutant (F87wY96FV247LC334A) WITH 1,3,5-Trichlorobenzene" 100.00 414 99.03 99.76 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 99.76 99.76 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" 100.00 417 100.00 100.00 0.00e+00 PDB 1MPW "Molecular Recognition In (+)-a-pinene Oxidation By Cytochrome P450cam" 100.00 414 99.03 99.76 0.00e+00 PDB 1NOO "Cytochrome P450-Cam Complexed With 5-Exo-Hydroxycamphor" 100.00 414 100.00 100.00 0.00e+00 PDB 1O76 "Cyanide Complex Of P450cam From Pseudomonas Putida" 100.00 414 99.76 100.00 0.00e+00 PDB 1P2Y "Crystal Structure Of Cytochrome P450cam In Complex With (S)- (-)-Nicotine" 100.00 420 100.00 100.00 0.00e+00 PDB 1P7R "Crystal Structure Of Reduced, Co-Exposed Complex Of Cytochrome P450cam With (S)-(-)-Nicotine" 100.00 420 100.00 100.00 0.00e+00 PDB 1PHA "Inhibitor-Induced Conformational Change In Cytochrome P450- Cam" 100.00 414 100.00 100.00 0.00e+00 PDB 1PHB "Inhibitor-Induced Conformational Change In Cytochrome P450- Cam" 100.00 414 100.00 100.00 0.00e+00 PDB 1PHC "Crystal Structure Of Substrate-free Pseudomonas Putida Cytochrome P450" 100.00 414 100.00 100.00 0.00e+00 PDB 1PHD "Crystal Structures Of Metyrapone-And Phenylimidazole-Inhibited Complexes Of Cytochrome P450-Cam" 100.00 414 100.00 100.00 0.00e+00 PDB 1PHE "Crystal Structures Of Metyrapone-And Phenylimidazole-Inhibited Complexes Of Cytochrome P450-Cam" 100.00 414 100.00 100.00 0.00e+00 PDB 1PHF "Crystal Structures Of Metyrapone-And Phenylimidazole- Inhibited Complexes Of Cytochrome P450-Cam" 100.00 414 100.00 100.00 0.00e+00 PDB 1PHG "Crystal Structures Of Metyrapone-And Phenylimidazole- Inhibited Complexes Of Cytochrome P450-Cam" 100.00 414 100.00 100.00 0.00e+00 PDB 1QMQ "Optical Detection Of Cytochrome P450 By Sensitizer-Linked Substrates" 100.00 414 99.76 99.76 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" 100.00 414 100.00 100.00 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" 100.00 417 100.00 100.00 0.00e+00 PDB 1T85 "Crystal Structure Of The Ferrous Co-Bound Cytochrome P450cam Mutant (L358pC334A)" 100.00 414 99.52 99.52 0.00e+00 PDB 1T86 "Crystal Structure Of The Ferrous Cytochrome P450cam Mutant (L358pC334A)" 100.00 414 99.52 99.52 0.00e+00 PDB 1T87 "Crystal Structure Of The Ferrous Co-Bound Cytochrome P450cam (C334a)" 100.00 414 99.76 99.76 0.00e+00 PDB 1T88 "Crystal Structure Of The Ferrous Cytochrome P450cam (C334a)" 100.00 414 99.76 99.76 0.00e+00 PDB 1UYU "Xenon Complex Of Wildtype P450cam From Pseudomonas Putida" 100.00 414 99.76 100.00 0.00e+00 PDB 1YRC "X-ray Crystal Structure Of Hydrogenated Cytochrome P450cam" 100.00 414 100.00 100.00 0.00e+00 PDB 1YRD "X-Ray Crystal Structure Of Perdeuterated Cytochrome P450cam" 100.00 414 100.00 100.00 0.00e+00 PDB 2A1M "Crystal Structure Of Ferrous Dioxygen Complex Of Wild-Type Cytochrome P450cam" 100.00 415 99.76 99.76 0.00e+00 PDB 2A1N "Crystal Structure Of Ferrous Dioxygen Complex Of D251n Cytochrome P450cam" 100.00 415 99.52 99.76 0.00e+00 PDB 2A1O "Crystal Structure Of Ferrous Dioxygen Complex Of T252a Cytochrome P450cam" 100.00 415 99.52 99.52 0.00e+00 PDB 2CP4 "Crystal Structure Of The Cytochrome P450-Cam Active Site Mutant Thr252ala" 100.00 414 99.76 99.76 0.00e+00 PDB 2CPP "High-Resolution Crystal Structure Of Cytochrome P450-Cam" 100.00 414 100.00 100.00 0.00e+00 PDB 2FE6 "P450cam From Pseudomonas Putida Reconstituted With Manganic Protoporphyrin Ix" 100.00 421 100.00 100.00 0.00e+00 PDB 2FER "P450cam From Pseudomonas Putida Reconstituted With Manganic Protoporphyrin Ix" 98.06 411 100.00 100.00 0.00e+00 PDB 2FEU "P450cam From Pseudomonas Putida Reconstituted With Manganic Protoporphyrin Ix" 98.06 411 100.00 100.00 0.00e+00 PDB 2FRZ "Crystal Structure Of Cytochrome P450cam Mutant (F87wY96FV247LC334A)" 100.00 414 99.03 99.76 0.00e+00 PDB 2GQX "Crystal Structure Of Cytochrome P450cam Mutant (F87wY96FL244AV247LC334A) WITH PENTACHLOROBENZENE" 98.06 405 98.77 99.51 0.00e+00 PDB 2GR6 "Crystal Structure Of Cytochrome P450cam Mutant (F87wY96FL244AV247LC334A)" 98.06 405 98.77 99.51 0.00e+00 PDB 2H7Q "Cytochrome P450cam Complexed With Imidazole" 100.00 414 100.00 100.00 0.00e+00 PDB 2H7R "L244a Mutant Of Cytochrome P450cam Complexed With Imidazole" 100.00 414 99.52 99.52 0.00e+00 PDB 2H7S "L244a Mutant Of Cytochrome P450cam" 100.00 414 99.52 99.52 0.00e+00 PDB 2L8M "Reduced And Co-Bound Cytochrome P450cam (Cyp101a1)" 100.00 415 100.00 100.00 0.00e+00 PDB 2LQD "Reduced And Co-Bound Cytochrome P450cam (Cyp101a1)" 98.06 405 100.00 100.00 0.00e+00 PDB 2M56 "The Structure Of The Complex Of Cytochrome P450cam And Its Electron Donor Putidaredoxin Determined By Paramagnetic Nmr Spectros" 97.82 404 99.75 100.00 0.00e+00 PDB 2QBL "Crystal Structure Of Ferric G248t Cytochrome P450cam" 100.00 421 99.76 99.76 0.00e+00 PDB 2QBM "Crystal Structure Of The P450cam G248t Mutant In The Cyanide Bound State" 100.00 421 99.76 99.76 0.00e+00 PDB 2QBN "Crystal Structure Of Ferric G248v Cytochrome P450cam" 100.00 421 99.76 99.76 0.00e+00 PDB 2QBO "Crystal Structure Of The P450cam G248v Mutant In The Cyanide Bound State" 100.00 421 99.76 99.76 0.00e+00 PDB 2Z97 "Crystal Structure Of Ferric Cytochrome P450cam Reconstituted With 7- Methyl-7-Depropionated Hemin" 100.00 415 100.00 100.00 0.00e+00 PDB 2ZAW "Crystal Structure Of Ferric Cytochrome P450cam Reconstituted With 6- Methyl-6-Depropionated Hemin" 100.00 415 100.00 100.00 0.00e+00 PDB 2ZAX "Crystal Structure Of Ferric Cytochrome P450cam" 100.00 415 100.00 100.00 0.00e+00 PDB 2ZUH "Crystal Structure Of Camphor-Soaked Ferric Cytochrome P450cam Mutant (D297a)" 100.00 415 99.76 99.76 0.00e+00 PDB 2ZUI "Crystal Structure Of Camphor-Soaked Ferric Cytochrome P450cam Mutant (D297n)" 100.00 415 99.76 100.00 0.00e+00 PDB 2ZUJ "Crystal Structure Of Camphor-Soaked Ferric Cytochrome P450cam Mutant(D297l)" 100.00 415 99.76 99.76 0.00e+00 PDB 2ZWT "Crystal Structure Of Ferric Cytochrome P450cam" 100.00 415 100.00 100.00 0.00e+00 PDB 2ZWU "Crystal Structure Of Camphor Soaked Ferric Cytochrome P450cam" 100.00 415 100.00 100.00 0.00e+00 PDB 3CP4 "Crystal Structure Of The Cytochrome P450-Cam Active Site Mutant Thr252ala" 100.00 414 100.00 100.00 0.00e+00 PDB 3CPP "Crystal Structure Of The Carbon Monoxy-Substrate-Cytochrome P450-Cam Ternary Complex" 100.00 414 100.00 100.00 0.00e+00 PDB 3FWF "Ferric Camphor Bound Cytochrome P450cam Containing A Selenocysteine As The 5th Heme Ligand, Monoclinic Crystal Form" 98.06 405 99.01 99.51 0.00e+00 PDB 3FWG "Ferric Camphor Bound Cytochrome P450cam, Arg365leu, Glu366gln, Monoclinic Crystal Form" 98.06 405 99.26 99.75 0.00e+00 PDB 3FWI "Ferric Camphor Bound Cytochrome P450cam Containing A Selenocysteine As The 5th Heme Ligand, Tetragonal Crystal Form" 98.06 405 99.26 99.51 0.00e+00 PDB 3FWJ "Ferric Camphor Bound Cytochrome P450cam Containing A Selenocysteine As The 5th Heme Ligand, Orthorombic Crystal Form" 98.06 405 99.26 99.51 0.00e+00 PDB 3L61 "Crystal Structure Of Substrate-Free P450cam At 200 Mm [k+]" 100.00 414 99.76 99.76 0.00e+00 PDB 3L62 "Crystal Structure Of Substrate-Free P450cam At Low [k+]" 100.00 414 99.76 99.76 0.00e+00 PDB 3L63 "Crystal Structure Of Camphor-Bound P450cam At Low [k+]" 100.00 414 99.76 99.76 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 99.76 99.76 0.00e+00 PDB 3OL5 "Crystal Structure Of Cytochrome P450cam Crystallized With A Tethered Substrate Analog 3oh-Adac1-C8-Dans" 100.00 414 99.76 99.76 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 99.76 99.76 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 99.76 99.76 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 99.76 99.76 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 99.76 99.76 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 99.76 99.76 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 99.76 99.76 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 99.76 99.76 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 99.76 99.76 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 99.76 99.76 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 99.76 99.76 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 99.76 99.76 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 99.76 99.76 0.00e+00 PDB 3W9C "Crystal Structure Of The Electron Transfer Complex Of Cytochrome P450cam With Putidaredoxin" 100.00 416 99.27 99.27 0.00e+00 PDB 3WRH "Crystal Structure Of P450cam" 100.00 421 100.00 100.00 0.00e+00 PDB 3WRI "Crystal Structure Of P450cam" 100.00 421 100.00 100.00 0.00e+00 PDB 3WRJ "Crystal Structure Of P450cam" 100.00 421 100.00 100.00 0.00e+00 PDB 3WRK "Crystal Structure Of P450cam" 100.00 421 100.00 100.00 0.00e+00 PDB 3WRL "Crystal Structure Of P450cam" 100.00 421 100.00 100.00 0.00e+00 PDB 3WRM "Crystal Structure Of P450cam" 100.00 421 100.00 100.00 0.00e+00 PDB 4CP4 "Crystal Structure Of The Cytochrome P450-Cam Active Site Mutant Thr252ala" 100.00 414 100.00 100.00 0.00e+00 PDB 4CPP "Crystal Structures Of Cytochrome P450-Cam Complexed With Camphane, Thiocamphor, And Adamantane: Factors Controlling P450 Substr" 100.00 414 100.00 100.00 0.00e+00 PDB 4EK1 "Crystal Structure Of Electron-Spin Labeled Cytochrome P450cam" 100.00 414 98.31 98.31 0.00e+00 PDB 4G3R "Crystal Structure Of Nitrosyl Cytochrome P450cam" 100.00 414 99.76 99.76 0.00e+00 PDB 4JWS "Crystal Structure Of Cytochrome P450cam-putidaredoxin Complex" 100.00 415 98.55 98.55 0.00e+00 PDB 4JWU "Crystal Structure Of Cytochrome P450cam-putidaredoxin Complex" 100.00 415 98.55 98.55 0.00e+00 PDB 4JX1 "Crystal Structure Of Reduced Cytochrome P450cam-putidaredoxin Complex Bound To Camphor And 5-exo-hydroxycamphor" 100.00 415 98.55 98.55 0.00e+00 PDB 4KKY "Crystal Structure Of N-(1-pyrene)acetamide Labeled P450cam In Substrate Bound Form" 99.76 413 98.54 98.54 0.00e+00 PDB 4L49 "Structure Of L358a Mutant Of P450cam Bound To Camphor" 100.00 415 99.52 99.52 0.00e+00 PDB 4L4A "Structure Of L358a/k178g Mutant Of P450cam Bound To Camphor" 100.00 415 99.27 99.27 0.00e+00 PDB 4L4B "Structure Of L358a/k178g/d182n Mutant Of P450cam Bound To Camphor" 100.00 415 99.03 99.27 0.00e+00 PDB 4L4C "Structure Of L358p/k178g Mutant Of P450cam Bound To Camphor" 100.00 415 99.27 99.27 0.00e+00 PDB 4L4D "Structure Of Cyanide And Camphor Bound P450cam Mutant L358a" 100.00 415 99.52 99.52 0.00e+00 PDB 4L4E "Structure Of Cyanide And Camphor Bound P450cam Mutant L358a/k178g" 100.00 415 99.27 99.27 0.00e+00 PDB 4L4F "Structure Of Cyanide And Camphor Bound P450cam Mutant L358a/k178g/d182n" 100.00 415 99.03 99.27 0.00e+00 PDB 4L4G "Structure Of Cyanide And Camphor Bound P450cam Mutant L358p/k178g" 100.00 415 99.27 99.27 0.00e+00 PDB 5CP4 "Cryogenic Structure Of P450cam" 100.00 414 100.00 100.00 0.00e+00 PDB 5CPP "The Structural Basis For Substrate-Induced Changes In Redox Potential And Spin Equilibrium In Cytochrome P-450(Cam)" 100.00 414 100.00 100.00 0.00e+00 PDB 6CP4 "P450cam D251n Mutant" 100.00 414 99.76 100.00 0.00e+00 PDB 6CPP "Crystal Structures Of Cytochrome P450-Cam Complexed With Camphane, Thiocamphor, And Adamantane: Factors Controlling P450 Substr" 100.00 414 100.00 100.00 0.00e+00 PDB 7CPP "The Structural Basis For Substrate-Induced Changes In Redox Potential And Spin Equilibrium In Cytochrome P450(Cam)" 100.00 414 100.00 100.00 0.00e+00 PDB 8CPP "Crystal Structures Of Cytochrome P450-Cam Complexed With Camphane, Thiocamphor, And Adamantane: Factors Controlling P450 Substr" 100.00 414 100.00 100.00 0.00e+00 DBJ BAN13286 "cytochrome P-450cam [Pseudomonas putida]" 100.00 415 100.00 100.00 0.00e+00 GB AAA25760 "cytochrome P-450-cam [Pseudomonas putida]" 100.00 415 100.00 100.00 0.00e+00 REF WP_032492633 "camphor 5-monooxygenase [Pseudomonas putida]" 100.00 415 100.00 100.00 0.00e+00 REF YP_009083112 "cytochrome P-450cam [Pseudomonas putida]" 100.00 415 100.00 100.00 0.00e+00 SP P00183 "RecName: Full=Camphor 5-monooxygenase; AltName: Full=Cytochrome P450-cam; Short=Cytochrome P450cam" 100.00 415 100.00 100.00 0.00e+00 stop_ save_ ############# # Ligands # ############# save_HEM _Saveframe_category ligand _Mol_type non-polymer _Name_common "HEM (PROTOPORPHYRIN IX CONTAINING FE)" _BMRB_code . _PDB_code HEM _Molecular_mass 616.487 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Feb 10 12:38:22 2011 ; 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 _Name_common CAM _BMRB_code . _PDB_code CAM _Molecular_mass 152.233 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Feb 10 12:46:41 2011 ; 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_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 '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 $entity_1 'recombinant technology' . Escherichia coli . N/A stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; 0.4 mM reduced-CO-bound CYP101A1, 3 mM CAM, pH 7.4 TrisHCl buffer, 100 mM KCl ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 0.4 mM '[U-100% 13C; U-100% 15N; U-80% 2H]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' $HEM 0.4 mM 'natural abundance' $CAM 3 mM 'natural abundance' KCl 100 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type bicelle _Details 'Same as sample_1, except 5% nematic phase C12E5/hexanol added for alignment' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 0.4 mM [U-15N] H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' $HEM 0.4 mM 'natural abundance' $CAM 3 mM 'natural abundance' KCl 100 mM 'natural abundance' C12E5/hexanol 5 % 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type 'filamentous virus' _Details 'Same as sample_1, except 8 mg/mL pf1 phage added' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 0.4 mM [U-15N] H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' $HEM 0.4 mM 'natural abundance' $CAM 3 mM 'natural abundance' KCl 100 mM 'natural abundance' pf1 8 mg/mL 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_AMBER _Saveframe_category software _Name AMBER _Version 10 loop_ _Vendor _Address _Electronic_address 'Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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_2D_1H-15N_TROSY-semiTROSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY-semiTROSY' _Sample_label $sample_2 save_ save_2D_1H-15N_TROSY-semiTROSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY-semiTROSY' _Sample_label $sample_3 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 7.4 0.1 pH pressure 1 . atm temperature 298 0.1 K stop_ save_ save_sample_conditions_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 0.1 mM pH 7.4 0.1 pH pressure 1 . atm temperature 298 0.1 K stop_ save_ save_sample_conditions_3 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 0.1 mM pH 7.4 0.1 pH pressure 1 . atm temperature 298 0.1 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 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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 '3D HNCA' '3D HN(CO)CA' '3D HNCACB' '3D 1H-15N NOESY' 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 'cytochrome P450cam' _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 2 1 THR H H 8.20 0.02 1 2 2 1 THR CA C 60.7 0.1 1 3 2 1 THR CB C 68.4 0.1 1 4 2 1 THR N N 117.1 0.1 1 5 3 2 GLU H H 8.16 0.02 1 6 3 2 GLU CA C 55.2 0.1 1 7 3 2 GLU CB C 28.6 0.1 1 8 3 2 GLU N N 116.9 0.1 1 9 4 3 THR H H 8.12 0.02 1 10 4 3 THR CA C 60.7 0.1 1 11 4 3 THR CB C 68.4 0.1 1 12 4 3 THR N N 120.5 0.1 1 13 5 4 ILE H H 8.15 0.02 1 14 5 4 ILE CA C 60.2 0.1 1 15 5 4 ILE CB C 36.8 0.1 1 16 5 4 ILE N N 124.9 0.1 1 17 6 5 GLN H H 8.39 0.02 1 18 6 5 GLN CA C 54.5 0.1 1 19 6 5 GLN CB C 28.0 0.1 1 20 6 5 GLN N N 125.5 0.1 1 21 7 6 SER H H 8.29 0.02 1 22 7 6 SER CA C 57.2 0.1 1 23 7 6 SER CB C 62.7 0.1 1 24 7 6 SER N N 118.4 0.1 1 25 8 7 ASN H H 8.35 0.02 1 26 8 7 ASN CA C 51.9 0.1 1 27 8 7 ASN CB C 37.3 0.1 1 28 8 7 ASN N N 121.7 0.1 1 29 9 8 ALA H H 8.10 0.02 1 30 9 8 ALA CA C 51.1 0.1 1 31 9 8 ALA CB C 17.1 0.1 1 32 9 8 ALA N N 124.3 0.1 1 33 10 9 ASN H H 8.32 0.02 1 34 10 9 ASN CA C 51.9 0.1 1 35 10 9 ASN CB C 36.9 0.1 1 36 10 9 ASN N N 117.8 0.1 1 37 11 10 LEU H H 7.74 0.02 1 38 11 10 LEU CA C 52.2 0.1 1 39 11 10 LEU CB C 39.7 0.1 1 40 11 10 LEU N N 122.0 0.1 1 41 12 11 ALA H H 8.70 0.02 1 42 12 11 ALA CA C 49.1 0.1 1 43 12 11 ALA CB C 15.9 0.1 1 44 12 11 ALA N N 129.9 0.1 1 45 16 15 PRO CA C 63.2 0.1 1 46 16 15 PRO CB C 30.8 0.1 1 47 17 16 HIS H H 7.64 0.02 1 48 17 16 HIS CA C 55.0 0.1 1 49 17 16 HIS CB C 29.2 0.1 1 50 17 16 HIS N N 111.6 0.1 1 51 18 17 VAL H H 6.84 0.02 1 52 18 17 VAL CA C 59.1 0.1 1 53 18 17 VAL CB C 30.3 0.1 1 54 18 17 VAL N N 127.6 0.02 1 55 19 18 PRO CA C 63.2 0.1 1 56 19 18 PRO CB C 30.8 0.1 1 57 20 19 GLU H H 8.62 0.02 1 58 20 19 GLU CA C 58.3 0.1 1 59 20 19 GLU CB C 27.5 0.1 1 60 20 19 GLU N N 122.3 0.1 1 61 21 20 HIS H H 8.08 0.02 1 62 21 20 HIS CA C 56.8 0.1 1 63 21 20 HIS CB C 27.2 0.1 1 64 21 20 HIS N N 113.9 0.1 1 65 22 21 LEU H H 7.30 0.02 1 66 22 21 LEU CA C 52.7 0.1 1 67 22 21 LEU CB C 40.3 0.1 1 68 22 21 LEU N N 119.3 0.1 1 69 23 22 VAL H H 7.15 0.02 1 70 23 22 VAL CA C 61.7 0.1 1 71 23 22 VAL CB C 29.9 0.1 1 72 23 22 VAL N N 120.5 0.1 1 73 24 23 PHE H H 9.20 0.02 1 74 24 23 PHE CA C 56.8 0.1 1 75 24 23 PHE CB C 39.1 0.1 1 76 24 23 PHE N N 133.7 0.1 1 77 25 24 ASP H H 8.13 0.02 1 78 25 24 ASP CA C 54.3 0.1 1 79 25 24 ASP CB C 38.9 0.1 1 80 25 24 ASP N N 126.3 0.1 1 81 26 25 PHE H H 8.33 0.02 1 82 26 25 PHE CA C 60.0 0.1 1 83 26 25 PHE CB C 36.5 0.1 1 84 26 25 PHE N N 125.5 0.1 1 85 28 27 MET CA C 56.3 0.1 1 86 28 27 MET CB C 28.1 0.1 1 87 29 28 TYR H H 7.90 0.02 1 88 29 28 TYR CA C 57.3 0.1 1 89 29 28 TYR CB C 31.2 0.1 1 90 29 28 TYR N N 119.6 0.1 1 91 31 30 PRO CA C 61.6 0.1 1 92 31 30 PRO CB C 30.0 0.1 1 93 32 31 SER H H 7.91 0.02 1 94 32 31 SER CA C 59.1 0.1 1 95 32 31 SER CB C 61.5 0.1 1 96 32 31 SER N N 118.7 0.1 1 97 33 32 ASN H H 8.75 0.02 1 98 33 32 ASN CA C 52.3 0.1 1 99 33 32 ASN CB C 36.6 0.1 1 100 33 32 ASN N N 118.1 0.1 1 101 34 33 LEU H H 7.26 0.02 1 102 34 33 LEU CA C 56.2 0.1 1 103 34 33 LEU CB C 40.8 0.1 1 104 34 33 LEU N N 120.2 0.1 1 105 35 34 SER H H 8.60 0.02 1 106 35 34 SER CA C 59.5 0.1 1 107 35 34 SER CB C 61.3 0.1 1 108 35 34 SER N N 115.1 0.1 1 109 36 35 ALA H H 7.75 0.02 1 110 36 35 ALA CA C 51.5 0.1 1 111 36 35 ALA CB C 17.5 0.1 1 112 36 35 ALA N N 124.6 0.1 1 113 37 36 GLY H H 7.38 0.02 1 114 37 36 GLY CA C 41.9 0.1 1 115 37 36 GLY N N 109.8 0.1 1 116 38 37 VAL H H 7.51 0.02 1 117 38 37 VAL CA C 66.1 0.1 1 118 38 37 VAL CB C 28.1 0.1 1 119 38 37 VAL N N 124.3 0.1 1 120 39 38 GLN H H 7.56 0.02 1 121 39 38 GLN CA C 60.8 0.1 1 122 39 38 GLN CB C 23.6 0.1 1 123 39 38 GLN N N 121.7 0.1 1 124 40 39 GLU H H 9.81 0.02 1 125 40 39 GLU CA C 59.8 0.1 1 126 40 39 GLU CB C 26.4 0.1 1 127 40 39 GLU N N 120.8 0.1 1 128 41 40 ALA H H 8.53 0.02 1 129 41 40 ALA CA C 53.6 0.1 1 130 41 40 ALA CB C 16.6 0.1 1 131 41 40 ALA N N 122.8 0.1 1 132 42 41 TRP H H 7.75 0.02 1 133 42 41 TRP HE1 H 9.81 0.02 1 134 42 41 TRP CA C 55.5 0.1 1 135 42 41 TRP N N 122.3 0.1 1 136 42 41 TRP NE1 N 128.7 0.1 1 137 43 42 ALA CA C 50.5 0.1 1 138 44 43 VAL H H 6.08 0.02 1 139 44 43 VAL CA C 62.2 0.1 1 140 44 43 VAL N N 115.1 0.1 1 141 45 44 LEU H H 7.07 0.02 1 142 45 44 LEU CA C 54.2 0.1 1 143 45 44 LEU N N 119.3 0.1 1 144 46 45 GLN H H 7.43 0.02 1 145 46 45 GLN CA C 52.4 0.1 1 146 46 45 GLN CB C 26.6 0.1 1 147 46 45 GLN N N 112.2 0.1 1 148 47 46 GLU H H 6.72 0.02 1 149 47 46 GLU CA C 55.9 0.1 1 150 47 46 GLU CB C 28.6 0.1 1 151 47 46 GLU N N 121.1 0.1 1 152 48 47 SER H H 8.56 0.02 1 153 48 47 SER CA C 60.0 0.1 1 154 48 47 SER CB C 61.8 0.1 1 155 48 47 SER N N 115.7 0.1 1 156 49 48 ASN H H 8.28 0.02 1 157 49 48 ASN CA C 52.1 0.1 1 158 49 48 ASN CB C 36.3 0.1 1 159 49 48 ASN N N 116.6 0.1 1 160 50 49 VAL H H 7.69 0.02 1 161 50 49 VAL CA C 59.6 0.1 1 162 50 49 VAL CB C 30.9 0.1 1 163 50 49 VAL N N 125.8 0.1 1 164 51 50 PRO CA C 61.6 0.1 1 165 51 50 PRO CB C 30.9 0.1 1 166 52 51 ASP H H 8.04 0.02 1 167 52 51 ASP CA C 54.7 0.1 1 168 52 51 ASP CB C 39.2 0.1 1 169 52 51 ASP N N 117.8 0.1 1 170 53 52 LEU H H 7.10 0.02 1 171 53 52 LEU CA C 53.2 0.1 1 172 53 52 LEU CB C 43.9 0.1 1 173 53 52 LEU N N 119.0 0.1 1 174 54 53 VAL H H 8.50 0.02 1 175 54 53 VAL CA C 57.1 0.1 1 176 54 53 VAL N N 113.6 0.1 1 177 55 54 TRP H H 8.98 0.02 1 178 55 54 TRP HE1 H 9.00 0.02 1 179 55 54 TRP CA C 54.2 0.1 1 180 55 54 TRP N N 122.8 0.1 1 181 55 54 TRP NE1 N 130.7 0.1 1 182 56 55 THR H H 7.90 0.02 1 183 56 55 THR CA C 57.4 0.1 1 184 56 55 THR CB C 64.5 0.1 1 185 56 55 THR N N 120.2 0.1 1 186 57 56 ARG H H 7.89 0.02 1 187 57 56 ARG CA C 54.6 0.1 1 188 57 56 ARG CB C 28.0 0.1 1 189 57 56 ARG N N 119.0 0.1 1 190 58 57 CYS H H 8.04 0.02 1 191 58 57 CYS CA C 57.7 0.1 1 192 58 57 CYS CB C 27.9 0.1 1 193 58 57 CYS N N 119.3 0.1 1 194 59 58 ASN H H 9.32 0.02 1 195 59 58 ASN CA C 54.4 0.1 1 196 59 58 ASN CB C 36.9 0.1 1 197 59 58 ASN N N 114.8 1.0 1 198 60 59 GLY H H 8.88 0.02 1 199 60 59 GLY CA C 43.9 0.1 1 200 60 59 GLY N N 104.1 0.1 1 201 61 60 GLY H H 7.48 0.02 1 202 61 60 GLY CA C 43.0 0.1 1 203 61 60 GLY N N 111.9 0.1 1 204 62 61 HIS H H 7.14 0.02 1 205 62 61 HIS CA C 54.2 0.1 1 206 62 61 HIS CB C 27.8 0.1 1 207 62 61 HIS N N 122.0 0.1 1 208 63 62 TRP H H 8.31 0.02 1 209 63 62 TRP HE1 H 10.35 0.02 1 210 63 62 TRP CA C 56.9 0.1 1 211 63 62 TRP N N 118.3 0.1 1 212 63 62 TRP NE1 N 129.0 0.1 1 213 64 63 ILE H H 10.29 0.02 1 214 64 63 ILE CA C 61.2 0.1 1 215 64 63 ILE N N 125.4 0.1 1 216 65 64 ALA H H 7.76 0.02 1 217 65 64 ALA CA C 49.4 0.1 1 218 65 64 ALA CB C 20.2 0.1 1 219 65 64 ALA N N 128.4 0.1 1 220 67 66 ARG CA C 50.6 0.1 1 221 67 66 ARG CB C 31.9 0.1 1 222 68 67 GLY H H 10.25 0.02 1 223 68 67 GLY CA C 46.0 0.1 1 224 68 67 GLY N N 112.2 0.1 1 225 69 68 GLN H H 8.83 0.02 1 226 69 68 GLN CA C 50.6 0.1 1 227 69 68 GLN CB C 26.8 0.1 1 228 69 68 GLN N N 119.6 0.1 1 229 70 69 LEU H H 6.36 0.02 1 230 70 69 LEU CA C 54.5 0.1 1 231 70 69 LEU CB C 41.5 0.1 1 232 70 69 LEU N N 116.6 0.1 1 233 71 70 ILE H H 7.55 0.02 1 234 71 70 ILE CA C 60.3 0.1 1 235 71 70 ILE N N 121.4 0.1 1 236 72 71 ARG H H 8.06 0.02 1 237 72 71 ARG N N 115.4 0.1 1 238 75 74 TYR H H 7.89 0.02 1 239 75 74 TYR N N 117.8 0.1 1 240 77 76 ASP H H 7.61 0.02 1 241 77 76 ASP CA C 50.6 0.1 1 242 77 76 ASP CB C 37.6 0.1 1 243 77 76 ASP N N 119.9 0.1 1 244 78 77 TYR H H 7.32 0.02 1 245 78 77 TYR CA C 56.4 0.1 1 246 78 77 TYR CB C 35.6 0.1 1 247 78 77 TYR N N 121.7 0.1 1 248 79 78 ARG H H 7.24 0.02 1 249 79 78 ARG CA C 57.1 0.1 1 250 79 78 ARG CB C 26.9 0.1 1 251 79 78 ARG N N 121.4 0.02 1 252 80 79 HIS H H 6.85 0.02 1 253 80 79 HIS CA C 57.6 0.1 1 254 80 79 HIS CB C 28.3 0.1 1 255 80 79 HIS N N 113.1 0.1 1 256 81 80 PHE H H 7.92 0.02 1 257 81 80 PHE CA C 54.2 0.1 1 258 81 80 PHE N N 119.0 0.1 1 259 82 81 SER H H 8.97 0.02 1 260 82 81 SER CA C 55.6 0.1 1 261 82 81 SER CB C 62.5 0.1 1 262 82 81 SER N N 117.5 0.1 1 263 83 82 SER H H 9.91 0.02 1 264 83 82 SER CA C 59.4 0.1 1 265 83 82 SER CB C 60.6 0.1 1 266 83 82 SER N N 127.6 0.1 1 267 84 83 GLU H H 8.19 0.02 1 268 84 83 GLU CA C 57.9 0.1 1 269 84 83 GLU N N 119.0 0.1 1 270 85 84 CYS H H 5.66 0.02 1 271 85 84 CYS CA C 53.0 0.1 1 272 85 84 CYS CB C 25.9 0.1 1 273 85 84 CYS N N 111.6 0.1 1 274 86 85 PRO CA C 60.7 0.1 1 275 87 86 PHE H H 5.90 0.02 1 276 87 86 PHE CA C 52.7 0.1 1 277 87 86 PHE CB C 39.0 0.1 1 278 87 86 PHE N N 117.5 0.1 1 279 88 87 ILE H H 6.01 0.02 1 280 88 87 ILE CA C 56.2 0.1 1 281 88 87 ILE CB C 39.3 0.1 1 282 88 87 ILE N N 121.4 0.1 1 283 89 88 PRO CA C 60.7 0.1 1 284 89 88 PRO CB C 29.1 0.1 1 285 90 89 ARG H H 9.45 0.02 1 286 90 89 ARG CA C 59.3 0.1 1 287 90 89 ARG CB C 34.0 0.1 1 288 90 89 ARG N N 124.3 0.1 1 289 91 90 GLU H H 9.39 0.02 1 290 91 90 GLU CA C 58.8 0.1 1 291 91 90 GLU CB C 26.7 0.1 1 292 91 90 GLU N N 116.0 0.1 1 293 92 91 ALA H H 7.30 0.02 1 294 92 91 ALA CA C 52.8 0.1 1 295 92 91 ALA CB C 16.5 0.1 1 296 92 91 ALA N N 123.4 0.1 1 297 93 92 GLY H H 7.49 0.02 1 298 93 92 GLY CA C 48.0 0.1 1 299 93 92 GLY N N 104.7 0.1 1 300 94 93 GLU H H 8.99 0.02 1 301 94 93 GLU CA C 57.7 0.1 1 302 94 93 GLU CB C 28.3 0.1 1 303 94 93 GLU N N 121.1 0.1 1 304 95 94 ALA H H 6.99 0.02 1 305 95 94 ALA CA C 51.3 0.1 1 306 95 94 ALA CB C 17.4 0.1 1 307 95 94 ALA N N 120.5 0.1 1 308 96 95 TYR H H 7.45 0.02 1 309 96 95 TYR CA C 58.8 0.1 1 310 96 95 TYR CB C 36.0 0.1 1 311 96 95 TYR N N 121.7 0.1 1 312 97 96 ASP H H 7.28 0.02 1 313 97 96 ASP CA C 51.1 0.1 1 314 97 96 ASP CB C 39.1 0.1 1 315 97 96 ASP N N 126.4 0.1 1 316 98 97 PHE H H 5.57 0.02 1 317 98 97 PHE CA C 54.8 0.1 1 318 98 97 PHE CB C 36.6 0.1 1 319 98 97 PHE N N 121.7 0.1 1 320 99 98 ILE H H 7.28 0.02 1 321 99 98 ILE CA C 56.4 0.1 1 322 99 98 ILE N N 123.4 0.1 1 323 100 99 PRO CA C 62.0 0.1 1 324 100 99 PRO CB C 26.9 0.1 1 325 101 100 THR H H 7.34 0.02 1 326 101 100 THR CA C 64.2 0.1 1 327 101 100 THR CB C 67.1 0.1 1 328 101 100 THR N N 112.7 0.1 1 329 102 101 SER H H 8.00 0.02 1 330 102 101 SER CA C 57.5 0.1 1 331 102 101 SER CB C 62.7 0.1 1 332 102 101 SER N N 112.2 0.1 1 333 103 102 MET H H 7.63 0.02 1 334 103 102 MET CA C 53.3 0.1 1 335 103 102 MET CB C 34.7 0.1 1 336 103 102 MET N N 119.3 0.1 1 337 104 103 ASP H H 8.80 0.02 1 338 104 103 ASP CA C 50.6 0.1 1 339 104 103 ASP CB C 40.7 0.1 1 340 104 103 ASP N N 119.6 0.1 1 341 106 105 PRO CA C 63.0 0.1 1 342 106 105 PRO CB C 33.3 0.1 1 343 107 106 GLU H H 8.69 0.02 1 344 107 106 GLU CA C 59.0 0.1 1 345 107 106 GLU CB C 28.1 0.1 1 346 107 106 GLU N N 127.9 0.1 1 347 108 107 GLN H H 7.60 0.02 1 348 108 107 GLN CA C 56.8 0.1 1 349 108 107 GLN CB C 26.1 0.1 1 350 108 107 GLN N N 113.6 0.1 1 351 109 108 ARG H H 7.54 0.02 1 352 109 108 ARG CA C 57.7 0.1 1 353 109 108 ARG CB C 27.1 0.1 1 354 109 108 ARG N N 118.1 0.1 1 355 111 110 PHE H H 6.97 0.02 1 356 111 110 PHE CA C 60.3 0.1 1 357 111 110 PHE CB C 38.4 0.1 1 358 111 110 PHE N N 117.8 0.1 1 359 112 111 ARG H H 8.48 0.02 1 360 112 111 ARG CA C 59.1 0.1 1 361 112 111 ARG CB C 28.4 0.1 1 362 112 111 ARG N N 122.0 0.1 1 363 113 112 ALA H H 7.57 0.02 1 364 113 112 ALA CA C 53.7 0.1 1 365 113 112 ALA CB C 16.5 0.1 1 366 113 112 ALA N N 119.9 0.1 1 367 114 113 LEU H H 6.92 0.02 1 368 114 113 LEU CA C 56.3 0.1 1 369 114 113 LEU CB C 39.9 0.1 1 370 114 113 LEU N N 120.2 0.1 1 371 115 114 ALA H H 7.92 0.02 1 372 115 114 ALA CA C 53.9 0.1 1 373 115 114 ALA CB C 15.6 0.1 1 374 115 114 ALA N N 120.2 0.1 1 375 116 115 ASN H H 8.55 0.02 1 376 116 115 ASN CA C 54.7 0.1 1 377 116 115 ASN CB C 37.8 0.1 1 378 116 115 ASN N N 116.0 0.1 1 379 117 116 GLN H H 7.62 0.02 1 380 117 116 GLN CA C 57.0 0.1 1 381 117 116 GLN CB C 27.0 0.1 1 382 117 116 GLN N N 116.9 0.1 1 383 118 117 VAL H H 7.34 0.02 1 384 118 117 VAL CA C 61.5 0.1 1 385 118 117 VAL CB C 31.0 0.1 1 386 118 117 VAL N N 110.1 0.1 1 387 119 118 VAL H H 6.99 0.02 1 388 119 118 VAL CA C 59.0 0.1 1 389 119 118 VAL CB C 32.3 0.1 1 390 119 118 VAL N N 106.8 0.1 1 391 120 119 GLY H H 7.26 0.02 1 392 120 119 GLY CA C 43.0 0.1 1 393 120 119 GLY N N 105.9 0.1 1 394 121 120 MET H H 8.52 0.02 1 395 121 120 MET CA C 58.4 0.1 1 396 121 120 MET CB C 28.1 0.1 1 397 121 120 MET N N 118.1 0.1 1 398 122 121 PRO CA C 64.8 0.1 1 399 123 122 VAL H H 7.30 0.02 1 400 123 122 VAL CA C 64.0 0.1 1 401 123 122 VAL CB C 29.9 0.1 1 402 123 122 VAL N N 117.8 0.1 1 403 124 123 VAL H H 7.48 0.02 1 404 124 123 VAL CA C 65.9 0.1 1 405 124 123 VAL CB C 29.6 0.1 1 406 124 123 VAL N N 121.7 0.1 1 407 125 124 ASP H H 8.26 0.02 1 408 125 124 ASP CA C 55.8 0.1 1 409 125 124 ASP N N 117.8 0.1 1 410 126 125 LYS H H 7.25 0.02 1 411 126 125 LYS CA C 57.3 0.1 1 412 126 125 LYS CB C 30.7 0.1 1 413 126 125 LYS N N 119.0 0.1 1 414 127 126 LEU H H 7.84 0.02 1 415 127 126 LEU CA C 53.5 0.1 1 416 127 126 LEU CB C 42.1 0.1 1 417 127 126 LEU N N 119.9 0.1 1 418 128 127 GLU H H 7.50 0.02 1 419 128 127 GLU CA C 53.4 0.1 1 420 128 127 GLU CB C 27.8 0.1 1 421 128 127 GLU N N 121.1 0.1 1 422 129 128 ASN H H 8.61 0.02 1 423 129 128 ASN CA C 56.5 0.1 1 424 129 128 ASN N N 116.4 0.1 1 425 130 129 ARG H H 7.89 0.02 1 426 141 140 SER CA C 60.2 0.1 1 427 141 140 SER CB C 61.7 0.1 1 428 142 141 LEU H H 7.34 0.02 1 429 142 141 LEU CA C 55.4 0.1 1 430 142 141 LEU N N 120.1 0.1 1 431 143 142 ARG H H 8.88 0.02 1 432 143 142 ARG CA C 56.0 0.1 1 433 143 142 ARG N N 120.8 0.1 1 434 144 143 PRO CA C 63.6 0.1 1 435 144 143 PRO CB C 29.8 0.1 1 436 145 144 GLN H H 8.33 0.02 1 437 145 144 GLN CA C 56.5 0.1 1 438 145 144 GLN CB C 28.0 0.1 1 439 145 144 GLN N N 113.9 0.1 1 440 146 145 GLY H H 6.46 0.02 1 441 146 145 GLY CA C 43.1 0.1 1 442 146 145 GLY N N 101.5 0.1 1 443 147 146 GLN H H 5.85 0.02 1 444 147 146 GLN CA C 52.8 0.1 1 445 147 146 GLN N N 111.3 0.1 1 446 148 147 CYS H H 8.24 0.02 1 447 148 147 CYS CA C 55.5 0.1 1 448 148 147 CYS CB C 29.5 0.1 1 449 148 147 CYS N N 110.7 0.1 1 450 149 148 ASN H H 9.10 0.02 1 451 149 148 ASN CA C 50.6 0.1 1 452 149 148 ASN CB C 35.9 0.1 1 453 149 148 ASN N N 119.9 0.1 1 454 150 149 PHE H H 9.31 0.02 1 455 150 149 PHE CA C 62.0 0.1 1 456 150 149 PHE CB C 38.8 0.1 1 457 150 149 PHE N N 124.0 0.1 1 458 151 150 THR H H 7.19 0.02 1 459 151 150 THR CA C 63.5 0.1 1 460 151 150 THR CB C 65.6 0.1 1 461 151 150 THR N N 109.2 0.1 1 462 152 151 GLU H H 6.20 0.02 1 463 152 151 GLU CA C 56.4 0.1 1 464 152 151 GLU CB C 29.8 0.1 1 465 152 151 GLU N N 118.4 0.1 1 466 153 152 ASP H H 6.96 0.02 1 467 153 152 ASP CA C 51.9 0.1 1 468 154 153 TYR H H 6.57 0.02 1 469 154 153 TYR CA C 54.1 0.1 1 470 154 153 TYR CB C 38.4 0.1 1 471 154 153 TYR N N 119.0 0.1 1 472 155 154 ALA H H 8.34 0.02 1 473 155 154 ALA CA C 52.0 0.1 1 474 155 154 ALA CB C 16.1 0.1 1 475 155 154 ALA N N 119.0 0.1 1 476 159 158 PRO CA C 63.2 0.1 1 477 159 158 PRO CB C 29.3 0.1 1 478 160 159 ILE H H 7.38 0.02 1 479 160 159 ILE CA C 65.5 0.1 1 480 160 159 ILE CB C 34.9 0.1 1 481 160 159 ILE N N 116.0 0.1 1 482 161 160 ARG H H 7.51 0.02 1 483 161 160 ARG CA C 58.7 0.1 1 484 161 160 ARG N N 117.5 0.1 1 485 162 161 ILE H H 8.27 0.02 1 486 162 161 ILE CA C 56.2 0.1 1 487 162 161 ILE N N 121.4 0.1 1 488 163 162 PHE H H 7.08 0.02 1 489 163 162 PHE CA C 61.6 0.1 1 490 163 162 PHE CB C 40.1 0.1 1 491 163 162 PHE N N 116.0 0.1 1 492 164 163 MET H H 7.85 0.02 1 493 164 163 MET CA C 56.5 0.1 1 494 164 163 MET CB C 26.8 0.1 1 495 164 163 MET N N 126.1 0.1 1 496 165 164 LEU H H 7.28 0.02 1 497 165 164 LEU CA C 52.7 0.1 1 498 165 164 LEU CB C 39.4 0.1 1 499 165 164 LEU N N 118.7 0.1 1 500 167 166 ALA CA C 51.2 0.1 1 501 167 166 ALA CB C 16.9 0.1 1 502 168 167 GLY H H 7.72 0.02 1 503 168 167 GLY CA C 46.2 0.1 1 504 168 167 GLY N N 108.9 0.1 1 505 169 168 LEU H H 8.45 0.02 1 506 169 168 LEU CA C 50.4 0.1 1 507 169 168 LEU CB C 40.9 0.1 1 508 169 168 LEU N N 122.3 0.1 1 509 170 169 PRO CA C 61.3 0.1 1 510 170 169 PRO CB C 30.8 0.1 1 511 171 170 GLU H H 8.73 0.02 1 512 171 170 GLU CA C 58.1 0.1 1 513 171 170 GLU CB C 27.8 0.1 1 514 171 170 GLU N N 123.1 0.1 1 515 172 171 GLU H H 9.36 0.02 1 516 172 171 GLU CA C 57.8 0.1 1 517 172 171 GLU CB C 26.9 0.1 1 518 172 171 GLU N N 119.9 0.1 1 519 173 172 ASP H H 6.31 0.02 1 520 173 172 ASP CA C 54.8 0.1 1 521 173 172 ASP CB C 42.0 0.1 1 522 173 172 ASP N N 117.2 0.1 1 523 175 174 PRO CA C 60.4 0.1 1 524 175 174 PRO CB C 29.1 0.1 1 525 176 175 HIS H H 7.58 0.02 1 526 176 175 HIS CA C 56.0 0.1 1 527 176 175 HIS CB C 27.3 0.1 1 528 176 175 HIS N N 117.5 0.1 1 529 177 176 LEU H H 7.70 0.02 1 530 177 176 LEU CA C 56.5 0.1 1 531 177 176 LEU CB C 39.0 0.1 1 532 177 176 LEU N N 125.2 0.1 1 533 178 177 LYS H H 8.08 0.02 1 534 178 177 LYS CA C 59.7 0.1 1 535 178 177 LYS N N 120.2 0.1 1 536 179 178 TYR CA C 54.1 0.1 1 537 180 179 LEU H H 7.11 0.02 1 538 180 179 LEU CA C 56.3 0.1 1 539 180 179 LEU CB C 40.7 0.1 1 540 180 179 LEU N N 114.9 0.1 1 541 181 180 THR H H 7.93 0.02 1 542 181 180 THR CA C 65.3 0.1 1 543 181 180 THR CB C 66.8 0.1 1 544 181 180 THR N N 111.8 0.1 1 545 184 183 MET CA C 56.4 0.1 1 546 184 183 MET CB C 39.4 0.1 1 547 185 184 THR H H 6.99 0.02 1 548 185 184 THR CA C 63.7 0.1 1 549 185 184 THR CB C 68.3 0.1 1 550 185 184 THR N N 108.6 0.1 1 551 186 185 ARG H H 6.47 0.02 1 552 186 185 ARG CA C 56.2 0.1 1 553 186 185 ARG CB C 31.7 0.1 1 554 186 185 ARG N N 118.7 0.1 1 555 187 186 PRO CA C 61.4 0.1 1 556 187 186 PRO CB C 30.4 0.1 1 557 188 187 ASP H H 8.43 0.02 1 558 188 187 ASP CA C 51.8 0.1 1 559 188 187 ASP CB C 41.7 0.1 1 560 188 187 ASP N N 126.7 0.1 1 561 189 188 GLY H H 8.64 0.02 1 562 189 188 GLY CA C 43.5 0.1 1 563 189 188 GLY N N 110.4 0.1 1 564 190 189 SER H H 8.71 0.02 1 565 190 189 SER CA C 59.5 0.1 1 566 190 189 SER CB C 61.8 0.1 1 567 190 189 SER N N 119.6 0.1 1 568 191 190 MET H H 8.29 0.02 1 569 191 190 MET CA C 54.2 0.1 1 570 191 190 MET CB C 35.9 0.1 1 571 191 190 MET N N 121.1 0.1 1 572 192 191 THR H H 8.81 0.02 1 573 192 191 THR CA C 60.0 0.1 1 574 192 191 THR CB C 69.5 0.1 1 575 192 191 THR N N 117.2 0.1 1 576 193 192 PHE H H 8.72 0.02 1 577 193 192 PHE CA C 61.4 0.1 1 578 193 192 PHE CB C 36.8 0.1 1 579 193 192 PHE N N 123.7 0.1 1 580 194 193 ALA H H 8.61 0.02 1 581 194 193 ALA CA C 54.1 0.1 1 582 194 193 ALA CB C 16.5 0.1 1 583 194 193 ALA N N 119.3 0.1 1 584 195 194 GLU H H 7.57 0.02 1 585 195 194 GLU CA C 57.2 0.1 1 586 195 194 GLU CB C 28.6 0.1 1 587 195 194 GLU N N 117.8 0.1 1 588 196 195 ALA H H 7.87 0.02 1 589 196 195 ALA CA C 53.8 0.1 1 590 196 195 ALA CB C 16.0 0.1 1 591 196 195 ALA N N 125.2 0.1 1 592 197 196 LYS H H 8.25 0.02 1 593 197 196 LYS CA C 58.1 0.1 1 594 197 196 LYS CB C 29.0 0.1 1 595 197 196 LYS N N 119.0 0.1 1 596 198 197 GLU CA C 58.7 0.1 1 597 198 197 GLU CB C 29.6 0.1 1 598 199 198 ALA H H 8.07 0.02 1 599 199 198 ALA CA C 53.5 0.1 1 600 199 198 ALA CB C 16.5 0.1 1 601 199 198 ALA N N 121.7 0.1 1 602 206 205 PRO CA C 64.0 0.1 1 603 206 205 PRO CB C 29.3 0.1 1 604 207 206 ILE H H 6.53 0.02 1 605 207 206 ILE CA C 63.1 0.1 1 606 207 206 ILE CB C 36.8 0.1 1 607 207 206 ILE N N 119.9 0.1 1 608 208 207 ILE H H 8.24 0.02 1 609 208 207 ILE CA C 64.0 0.1 1 610 208 207 ILE CB C 35.9 0.1 1 611 208 207 ILE N N 121.1 0.1 1 612 209 208 GLU H H 7.68 0.02 1 613 209 208 GLU CA C 57.8 0.1 1 614 209 208 GLU CB C 27.2 0.1 1 615 209 208 GLU N N 117.5 0.1 1 616 215 214 PRO CA C 62.6 0.1 1 617 215 214 PRO CB C 30.6 0.1 1 618 216 215 GLY H H 8.49 0.02 1 619 216 215 GLY CA C 42.4 0.1 1 620 216 215 GLY N N 111.3 0.1 1 621 217 216 THR H H 8.59 0.02 1 622 217 216 THR CA C 59.8 0.1 1 623 217 216 THR CB C 67.3 0.1 1 624 217 216 THR N N 109.8 0.1 1 625 218 217 ASP H H 8.15 0.02 1 626 218 217 ASP CA C 51.5 0.1 1 627 218 217 ASP CB C 41.7 0.1 1 628 218 217 ASP N N 119.3 0.1 1 629 219 218 ALA H H 8.61 0.02 1 630 219 218 ALA CA C 54.1 0.1 1 631 219 218 ALA CB C 18.1 0.1 1 632 219 218 ALA N N 118.1 0.1 1 633 220 219 ILE H H 7.61 0.02 1 634 220 219 ILE CA C 63.4 0.1 1 635 220 219 ILE N N 114.8 0.1 1 636 224 223 ALA CA C 52.5 0.1 1 637 224 223 ALA CB C 17.1 0.1 1 638 225 224 ASN H H 7.20 0.02 1 639 225 224 ASN CA C 51.6 0.1 1 640 225 224 ASN CB C 39.1 0.1 1 641 225 224 ASN N N 113.0 0.1 1 642 226 225 GLY H H 7.63 0.02 1 643 226 225 GLY CA C 44.1 0.1 1 644 226 225 GLY N N 110.1 0.1 1 645 227 226 GLN H H 8.10 0.02 1 646 227 226 GLN CA C 53.0 0.1 1 647 227 226 GLN CB C 30.2 0.1 1 648 227 226 GLN N N 118.4 0.1 1 649 228 227 VAL H H 8.88 0.02 1 650 228 227 VAL CA C 58.3 0.1 1 651 228 227 VAL CB C 32.4 0.1 1 652 228 227 VAL N N 117.8 0.1 1 653 229 228 ASN H H 8.89 0.02 1 654 229 228 ASN CA C 52.6 0.1 1 655 229 228 ASN CB C 36.6 0.1 1 656 229 228 ASN N N 121.7 0.1 1 657 230 229 GLY H H 8.55 0.02 1 658 230 229 GLY CA C 44.4 0.1 1 659 230 229 GLY N N 103.5 0.1 1 660 231 230 ARG H H 7.93 0.02 1 661 231 230 ARG CA C 51.3 0.1 1 662 231 230 ARG CB C 28.6 0.1 1 663 231 230 ARG N N 119.3 0.1 1 664 232 231 PRO CA C 62.0 0.1 1 665 232 231 PRO CB C 30.1 0.1 1 666 233 232 ILE H H 8.23 0.02 1 667 233 232 ILE CA C 60.6 0.1 1 668 233 232 ILE CB C 38.0 0.1 1 669 233 232 ILE N N 127.0 0.1 1 670 234 233 THR H H 9.03 0.02 1 671 234 233 THR CA C 59.8 0.1 1 672 234 233 THR CB C 69.8 0.1 1 673 234 233 THR N N 119.9 0.1 1 674 235 234 SER H H 9.03 0.02 1 675 235 234 SER CA C 61.7 0.1 1 676 235 234 SER CB C 59.9 0.1 1 677 235 234 SER N N 118.4 0.1 1 678 236 235 ASP H H 8.23 0.02 1 679 236 235 ASP CA C 56.4 0.1 1 680 236 235 ASP CB C 40.8 0.1 1 681 236 235 ASP N N 122.8 0.1 1 682 237 236 GLU H H 7.58 0.02 1 683 237 236 GLU CA C 57.1 0.1 1 684 237 236 GLU CB C 28.9 0.1 1 685 237 236 GLU N N 118.7 0.1 1 686 241 240 MET CA C 55.5 0.1 1 687 241 240 MET CB C 30.3 0.1 1 688 242 241 CYS H H 8.88 0.02 1 689 242 241 CYS CA C 48.9 0.1 1 690 242 241 CYS CB C 40.6 0.1 1 691 242 241 CYS N N 118.7 0.1 1 692 243 242 GLY H H 8.18 0.02 1 693 243 242 GLY CA C 45.2 0.1 1 694 243 242 GLY N N 103.5 0.1 1 695 244 243 LEU H H 6.83 0.02 1 696 244 243 LEU CA C 52.4 0.1 1 697 244 243 LEU CB C 39.3 0.1 1 698 244 243 LEU N N 119.6 0.1 1 699 245 244 LEU H H 6.76 0.02 1 700 245 244 LEU CA C 52.5 0.1 1 701 245 244 LEU CB C 39.3 0.1 1 702 245 244 LEU N N 119.2 0.1 1 703 246 245 LEU H H 6.99 0.02 1 704 247 246 VAL H H 6.88 0.02 1 705 247 246 VAL CA C 64.9 0.1 1 706 247 246 VAL CB C 28.9 0.1 1 707 247 246 VAL N N 118.2 0.1 1 708 248 247 GLY H H 7.40 0.02 1 709 248 247 GLY CA C 43.8 0.1 1 710 248 247 GLY N N 104.7 0.1 1 711 249 248 GLY H H 7.92 0.02 1 712 249 248 GLY CA C 45.0 0.1 1 713 249 248 GLY N N 108.6 0.1 1 714 250 249 LEU H H 7.41 0.02 1 715 250 249 LEU CA C 55.4 0.1 1 716 250 249 LEU CB C 40.4 0.1 1 717 250 249 LEU N N 120.3 0.1 1 718 251 250 ASP H H 7.51 0.02 1 719 251 250 ASP CA C 53.4 0.1 1 720 251 250 ASP CB C 43.4 0.1 1 721 251 250 ASP N N 119.3 0.1 1 722 252 251 THR H H 7.40 0.02 1 723 252 251 THR CA C 60.5 0.1 1 724 252 251 THR CB C 67.2 0.1 1 725 252 251 THR N N 105.6 0.1 1 726 253 252 VAL H H 9.38 0.02 1 727 253 252 VAL CA C 65.8 0.1 1 728 253 252 VAL CB C 31.3 0.1 1 729 253 252 VAL N N 126.1 0.1 1 730 254 253 VAL H H 6.97 0.02 1 731 254 253 VAL CA C 62.3 0.1 1 732 254 253 VAL CB C 32.5 0.1 1 733 254 253 VAL N N 114.8 0.1 1 734 255 254 ASN H H 6.82 0.02 1 735 255 254 ASN CA C 54.4 0.1 1 736 255 254 ASN CB C 39.4 0.1 1 737 255 254 ASN N N 115.4 0.1 1 738 256 255 PHE H H 8.27 0.02 1 739 256 255 PHE CA C 56.6 0.1 1 740 256 255 PHE CB C 40.4 0.1 1 741 256 255 PHE N N 124.9 0.1 1 742 257 256 LEU H H 7.44 0.02 1 743 257 256 LEU CA C 57.0 0.1 1 744 257 256 LEU CB C 40.1 0.1 1 745 257 256 LEU N N 120.8 0.1 1 746 258 257 SER H H 7.43 0.02 1 747 258 257 SER CA C 59.9 0.1 1 748 258 257 SER CB C 61.7 0.1 1 749 258 257 SER N N 112.5 0.1 1 750 259 258 PHE H H 8.48 0.02 1 751 259 258 PHE CA C 56.6 0.1 1 752 259 258 PHE CB C 41.0 0.1 1 753 259 258 PHE N N 122.8 0.1 1 754 260 259 SER H H 6.93 0.02 1 755 260 259 SER CA C 62.0 0.1 1 756 260 259 SER CB C 63.9 0.1 1 757 260 259 SER N N 115.1 0.1 1 758 261 260 MET H H 7.95 0.02 1 759 261 260 MET CA C 55.6 0.1 1 760 261 260 MET CB C 36.0 0.1 1 761 261 260 MET N N 124.9 0.1 1 762 262 261 GLU H H 7.90 0.02 1 763 262 261 GLU CA C 56.6 0.1 1 764 262 261 GLU CB C 28.2 0.1 1 765 262 261 GLU N N 121.9 0.1 1 766 263 262 PHE H H 8.38 0.02 1 767 263 262 PHE CA C 65.0 0.1 1 768 263 262 PHE N N 121.1 0.1 1 769 264 263 LEU H H 8.18 0.02 1 770 264 263 LEU CA C 58.0 0.1 1 771 264 263 LEU N N 118.7 0.1 1 772 265 264 ALA CA C 52.6 0.1 1 773 265 264 ALA CB C 15.7 0.1 1 774 266 265 LYS H H 7.20 0.02 1 775 266 265 LYS CA C 55.7 0.1 1 776 266 265 LYS CB C 32.5 0.1 1 777 266 265 LYS N N 116.3 0.1 1 778 267 266 SER H H 7.07 0.02 1 779 267 266 SER CA C 53.2 0.1 1 780 267 266 SER CB C 60.2 0.1 1 781 267 266 SER N N 114.5 0.1 1 782 268 267 PRO CA C 62.5 0.1 1 783 268 267 PRO CB C 30.3 0.1 1 784 269 268 GLU H H 10.26 0.02 1 785 269 268 GLU CA C 61.8 0.1 1 786 269 268 GLU CB C 24.0 0.1 1 787 269 268 GLU N N 135.5 0.1 1 788 270 269 HIS H H 8.04 0.02 1 789 270 269 HIS CA C 55.4 0.1 1 790 270 269 HIS CB C 33.6 0.1 1 791 270 269 HIS N N 113.3 0.1 1 792 271 270 ARG H H 7.50 0.02 1 793 271 270 ARG CA C 56.2 0.1 1 794 271 270 ARG CB C 28.6 0.1 1 795 271 270 ARG N N 117.5 0.1 1 796 272 271 GLN H H 8.33 0.02 1 797 272 271 GLN CA C 57.2 0.1 1 798 272 271 GLN CB C 26.1 0.1 1 799 272 271 GLN N N 116.9 0.1 1 800 273 272 GLU H H 7.46 0.02 1 801 273 272 GLU CA C 58.4 0.1 1 802 273 272 GLU CB C 28.2 0.1 1 803 273 272 GLU N N 118.4 0.1 1 804 274 273 LEU H H 6.96 0.02 1 805 274 273 LEU CA C 54.6 0.1 1 806 274 273 LEU CB C 40.8 0.1 1 807 274 273 LEU N N 115.4 0.1 1 808 278 277 PRO CA C 63.4 0.1 1 809 279 278 GLU H H 10.01 0.02 1 810 279 278 GLU CA C 57.0 0.1 1 811 279 278 GLU CB C 25.5 0.1 1 812 279 278 GLU N N 122.3 0.1 1 813 280 279 ARG H H 8.51 0.02 1 814 280 279 ARG CA C 55.1 0.1 1 815 280 279 ARG CB C 28.9 0.1 1 816 280 279 ARG N N 120.8 0.1 1 817 281 280 ILE H H 7.82 0.02 1 818 281 280 ILE CA C 66.9 0.1 1 819 281 280 ILE CB C 34.0 0.1 1 820 281 280 ILE N N 120.2 0.1 1 821 282 281 PRO CA C 65.9 0.1 1 822 282 281 PRO CB C 29.0 0.1 1 823 283 282 ALA H H 7.79 0.02 1 824 283 282 ALA CA C 54.4 0.1 1 825 283 282 ALA CB C 17.0 0.1 1 826 283 282 ALA N N 122.6 0.1 1 827 284 283 ALA H H 8.11 0.02 1 828 284 283 ALA CA C 51.6 0.1 1 829 284 283 ALA CB C 17.5 0.1 1 830 284 283 ALA N N 124.9 0.1 1 831 294 293 LEU H H 7.50 0.02 1 832 294 293 LEU CA C 56.0 0.1 1 833 294 293 LEU N N 117.2 0.1 1 834 295 294 VAL H H 7.30 0.02 1 835 295 294 VAL CA C 60.3 0.1 1 836 295 294 VAL CB C 31.5 0.1 1 837 295 294 VAL N N 117.2 0.1 1 838 296 295 ALA H H 8.90 0.02 1 839 296 295 ALA CA C 51.4 0.1 1 840 296 295 ALA CB C 21.1 0.1 1 841 296 295 ALA N N 126.7 0.1 1 842 297 296 ASP H H 8.26 0.02 1 843 297 296 ASP CA C 49.8 0.1 1 844 297 296 ASP CB C 36.8 0.1 1 845 297 296 ASP N N 120.5 0.1 1 846 298 297 GLY H H 7.97 0.02 1 847 298 297 GLY CA C 44.4 0.1 1 848 298 297 GLY N N 103.2 0.1 1 849 299 298 ARG H H 7.93 0.02 1 850 299 298 ARG CA C 51.5 0.1 1 851 299 298 ARG N N 119.0 0.1 1 852 300 299 ILE H H 9.47 0.02 1 853 300 299 ILE CA C 57.9 0.1 1 854 300 299 ILE N N 121.7 0.1 1 855 301 300 LEU H H 8.81 0.02 1 856 301 300 LEU CA C 59.9 0.1 1 857 301 300 LEU CB C 38.7 0.1 1 858 301 300 LEU N N 131.8 0.1 1 859 302 301 THR H H 8.62 0.02 1 860 302 301 THR CA C 61.2 0.1 1 861 302 301 THR CB C 68.3 0.1 1 862 302 301 THR N N 116.3 0.1 1 863 303 302 SER H H 7.58 0.02 1 864 303 302 SER CA C 55.0 0.1 1 865 303 302 SER CB C 64.4 0.1 1 866 303 302 SER N N 112.7 0.1 1 867 304 303 ASP H H 8.50 0.02 1 868 304 303 ASP CA C 53.6 0.1 1 869 304 303 ASP CB C 38.1 0.1 1 870 304 303 ASP N N 121.4 0.1 1 871 305 304 TYR H H 8.40 0.02 1 872 305 304 TYR CA C 55.1 0.1 1 873 305 304 TYR CB C 41.0 0.1 1 874 305 304 TYR N N 126.1 0.1 1 875 306 305 GLU H H 7.74 0.02 1 876 306 305 GLU CA C 53.4 0.1 1 877 306 305 GLU CB C 28.0 0.1 1 878 306 305 GLU N N 130.0 0.1 1 879 307 306 PHE H H 8.47 0.02 1 880 307 306 PHE CA C 53.2 0.1 1 881 307 306 PHE CB C 40.8 0.1 1 882 307 306 PHE N N 129.7 0.1 1 883 308 307 HIS H H 9.00 0.02 1 884 308 307 HIS CA C 55.8 0.1 1 885 308 307 HIS CB C 24.4 0.1 1 886 308 307 HIS N N 123.4 0.1 1 887 309 308 GLY H H 8.39 0.02 1 888 309 308 GLY CA C 43.8 0.1 1 889 309 308 GLY N N 102.6 0.1 1 890 310 309 VAL H H 7.44 0.02 1 891 310 309 VAL CA C 60.0 0.1 1 892 310 309 VAL CB C 31.5 0.1 1 893 310 309 VAL N N 123.7 0.1 1 894 311 310 GLN H H 8.40 0.02 1 895 311 310 GLN CA C 54.8 0.1 1 896 311 310 GLN CB C 26.5 0.1 1 897 311 310 GLN N N 126.1 0.1 1 898 312 311 LEU H H 8.61 0.02 1 899 312 311 LEU CA C 52.4 0.1 1 900 312 311 LEU CB C 39.5 0.1 1 901 312 311 LEU N N 128.5 0.1 1 902 313 312 LYS CA C 52.2 0.1 1 903 313 312 LYS CB C 32.7 0.1 1 904 314 313 LYS H H 8.73 0.02 1 905 314 313 LYS CA C 57.5 0.1 1 906 314 313 LYS CB C 31.2 0.1 1 907 314 313 LYS N N 122.0 0.1 1 908 315 314 GLY H H 8.57 0.02 1 909 315 314 GLY CA C 43.8 0.1 1 910 315 314 GLY N N 117.2 0.1 1 911 320 319 LEU H H 7.50 0.02 1 912 320 319 LEU N N 114.1 0.1 1 913 321 320 PRO CA C 64.2 0.1 1 914 321 320 PRO CB C 30.0 0.1 1 915 322 321 GLN H H 8.98 0.02 1 916 322 321 GLN CA C 58.5 0.1 1 917 322 321 GLN CB C 27.0 0.1 1 918 322 321 GLN N N 117.2 0.1 1 919 323 322 MET H H 7.47 0.02 1 920 323 322 MET CA C 60.6 0.1 1 921 323 322 MET CB C 29.0 0.1 1 922 323 322 MET N N 118.9 0.1 1 923 324 323 LEU H H 7.48 0.02 1 924 324 323 LEU CA C 55.1 0.1 1 925 324 323 LEU N N 114.5 0.1 1 926 325 324 SER H H 5.75 0.02 1 927 325 324 SER N N 121.3 0.1 1 928 326 325 GLY H H 8.56 0.02 1 929 326 325 GLY N N 105.8 0.1 1 930 327 326 LEU H H 6.77 0.02 1 931 327 326 LEU CB C 39.4 0.1 1 932 327 326 LEU N N 119.3 0.1 1 933 328 327 ASP CA C 52.6 0.1 1 934 328 327 ASP CB C 41.9 0.1 1 935 329 328 GLU H H 9.45 0.02 1 936 329 328 GLU CA C 56.0 0.1 1 937 329 328 GLU CB C 26.9 0.1 1 938 329 328 GLU N N 131.8 0.1 1 939 330 329 ARG H H 8.70 0.02 1 940 330 329 ARG CA C 56.5 0.1 1 941 330 329 ARG CB C 27.7 0.1 1 942 330 329 ARG N N 119.0 0.1 1 943 331 330 GLU H H 7.77 0.02 1 944 331 330 GLU CA C 56.6 0.1 1 945 331 330 GLU CB C 28.4 0.1 1 946 331 330 GLU N N 116.6 0.1 1 947 332 331 ASN H H 7.80 0.02 1 948 332 331 ASN CA C 51.0 0.1 1 949 332 331 ASN CB C 42.0 0.1 1 950 332 331 ASN N N 116.6 0.1 1 951 333 332 ALA H H 8.52 0.02 1 952 333 332 ALA CA C 50.9 0.1 1 953 333 332 ALA CB C 16.9 0.1 1 954 333 332 ALA N N 124.0 0.1 1 955 335 334 PRO CA C 62.9 0.1 1 956 335 334 PRO CB C 31.3 0.1 1 957 336 335 MET H H 8.74 0.02 1 958 336 335 MET CA C 52.8 0.1 1 959 336 335 MET N N 115.7 0.1 1 960 337 336 HIS H H 8.07 0.02 1 961 337 336 HIS CA C 54.0 0.1 1 962 337 336 HIS CB C 28.6 0.1 1 963 337 336 HIS N N 123.7 0.1 1 964 338 337 VAL H H 8.07 0.02 1 965 338 337 VAL CA C 60.6 0.1 1 966 338 337 VAL CB C 28.8 0.1 1 967 338 337 VAL N N 126.4 0.1 1 968 339 338 ASP H H 10.17 0.02 1 969 339 338 ASP CA C 50.4 0.1 1 970 339 338 ASP CB C 41.0 0.1 1 971 339 338 ASP N N 131.5 0.1 1 972 340 339 PHE H H 9.53 0.02 1 973 340 339 PHE CA C 54.7 0.1 1 974 340 339 PHE CB C 34.5 0.1 1 975 340 339 PHE N N 124.3 0.1 1 976 341 340 SER H H 8.66 0.02 1 977 341 340 SER CA C 56.6 0.1 1 978 341 340 SER CB C 61.8 0.1 1 979 341 340 SER N N 116.0 0.1 1 980 342 341 ARG H H 7.18 0.02 1 981 342 341 ARG CA C 56.5 0.1 1 982 342 341 ARG CB C 29.4 0.1 1 983 342 341 ARG N N 124.3 0.1 1 984 344 343 LYS CA C 54.0 0.1 1 985 344 343 LYS CB C 33.7 0.1 1 986 345 344 VAL H H 8.60 0.02 1 987 345 344 VAL CA C 61.4 0.1 1 988 345 344 VAL CB C 30.3 0.1 1 989 345 344 VAL N N 127.0 0.1 1 990 346 345 SER H H 8.03 0.02 1 991 346 345 SER CA C 55.1 0.1 1 992 346 345 SER CB C 62.5 0.1 1 993 346 345 SER N N 123.1 0.1 1 994 347 346 HIS H H 8.17 0.02 1 995 347 346 HIS CA C 54.9 0.1 1 996 347 346 HIS CB C 30.9 0.1 1 997 347 346 HIS N N 121.7 0.1 1 998 348 347 THR H H 9.44 0.02 1 999 348 347 THR CA C 58.7 0.1 1 1000 348 347 THR CB C 67.8 0.1 1 1001 348 347 THR N N 113.3 0.1 1 1002 349 348 THR H H 11.82 0.02 1 1003 349 348 THR CA C 66.1 0.1 1 1004 349 348 THR CB C 67.2 0.1 1 1005 349 348 THR N N 128.8 0.1 1 1006 350 349 PHE H H 8.11 0.02 1 1007 350 349 PHE CA C 55.8 0.1 1 1008 350 349 PHE CB C 36.6 0.1 1 1009 350 349 PHE N N 115.7 0.1 1 1010 351 350 GLY H H 7.78 0.02 1 1011 351 350 GLY CA C 43.1 0.1 1 1012 351 350 GLY N N 104.4 0.1 1 1013 352 351 HIS H H 8.24 0.02 1 1014 352 351 HIS CA C 55.8 0.1 1 1015 352 351 HIS CB C 31.5 0.1 1 1016 352 351 HIS N N 117.8 0.1 1 1017 353 352 GLY H H 8.04 0.02 1 1018 353 352 GLY CA C 42.8 0.1 1 1019 353 352 GLY N N 115.1 0.1 1 1020 354 353 SER H H 9.41 0.02 1 1021 354 353 SER CA C 60.5 0.1 1 1022 354 353 SER CB C 61.9 0.1 1 1023 354 353 SER N N 120.2 0.1 1 1024 355 354 HIS H H 7.74 0.02 1 1025 355 354 HIS CA C 56.6 0.1 1 1026 355 354 HIS CB C 26.2 0.1 1 1027 355 354 HIS N N 125.2 0.1 1 1028 356 355 LEU H H 5.63 0.02 1 1029 356 355 LEU CA C 56.6 0.1 1 1030 356 355 LEU CB C 41.2 0.1 1 1031 356 355 LEU N N 121.1 0.1 1 1032 357 356 CYS H H 4.04 0.02 1 1033 357 356 CYS CA C 59.4 0.1 1 1034 357 356 CYS CB C 59.1 0.1 1 1035 357 356 CYS N N 117.8 0.1 1 1036 358 357 LEU H H 2.74 0.02 1 1037 358 357 LEU CA C 52.6 0.1 1 1038 358 357 LEU CB C 43.4 0.1 1 1039 358 357 LEU N N 125.8 0.1 1 1040 359 358 GLY H H 6.55 0.02 1 1041 359 358 GLY CA C 41.1 0.1 1 1042 359 358 GLY N N 118.7 0.1 1 1043 360 359 GLN H H 6.98 0.02 1 1044 360 359 GLN CA C 48.8 0.1 1 1045 360 359 GLN N N 123.2 0.1 1 1046 363 362 ALA CA C 53.7 0.1 1 1047 363 362 ALA CB C 17.4 0.1 1 1048 364 363 ARG H H 7.51 0.02 1 1049 364 363 ARG CA C 59.6 0.1 1 1050 364 363 ARG CB C 27.8 0.1 1 1051 364 363 ARG N N 121.7 0.1 1 1052 365 364 ARG H H 8.49 0.02 1 1053 365 364 ARG CA C 57.1 0.1 1 1054 365 364 ARG CB C 26.1 0.1 1 1055 365 364 ARG N N 117.2 0.1 1 1056 366 365 GLU H H 7.35 0.02 1 1057 366 365 GLU CA C 59.5 0.1 1 1058 366 365 GLU CB C 27.9 0.1 1 1059 366 365 GLU N N 117.8 0.1 1 1060 367 366 ILE CA C 61.2 0.1 1 1061 368 367 ILE H H 7.95 0.02 1 1062 368 367 ILE CA C 62.6 0.1 1 1063 368 367 ILE CB C 37.5 0.1 1 1064 368 367 ILE N N 121.1 0.1 1 1065 369 368 VAL H H 9.03 0.02 1 1066 369 368 VAL CA C 61.9 0.1 1 1067 369 368 VAL CB C 28.6 0.1 1 1068 369 368 VAL N N 117.2 0.1 1 1069 374 373 TRP CA C 60.1 0.1 1 1070 375 374 LEU H H 7.81 0.02 1 1071 375 374 LEU CA C 57.4 0.1 1 1072 375 374 LEU CB C 43.4 0.1 1 1073 375 374 LEU N N 116.6 0.1 1 1074 376 375 THR H H 7.23 0.02 1 1075 376 375 THR CA C 61.5 0.1 1 1076 376 375 THR CB C 68.5 0.1 1 1077 376 375 THR N N 106.5 0.1 1 1078 377 376 ARG H H 8.15 0.02 1 1079 377 376 ARG CA C 53.1 0.1 1 1080 377 376 ARG CB C 29.9 0.1 1 1081 377 376 ARG N N 122.8 0.1 1 1082 378 377 ILE H H 7.65 0.02 1 1083 378 377 ILE CA C 62.0 0.1 1 1084 378 377 ILE N N 125.2 0.1 1 1085 379 378 PRO CA C 62.4 0.1 1 1086 380 379 ASP H H 8.44 0.02 1 1087 380 379 ASP CA C 51.7 0.1 1 1088 380 379 ASP CB C 39.4 0.1 1 1089 380 379 ASP N N 121.1 0.1 1 1090 381 380 PHE CB C 30.8 0.1 1 1091 382 381 SER CA C 55.6 0.1 1 1092 382 381 SER CB C 66.0 0.1 1 1093 383 382 ILE H H 8.51 0.02 1 1094 383 382 ILE CA C 59.4 0.1 1 1095 383 382 ILE CB C 35.4 0.1 1 1096 383 382 ILE N N 122.3 0.1 1 1097 384 383 ALA H H 8.17 0.02 1 1098 384 383 ALA CA C 49.8 0.1 1 1099 384 383 ALA CB C 16.2 0.1 1 1100 384 383 ALA N N 131.5 0.1 1 1101 385 384 PRO CA C 62.6 0.1 1 1102 385 384 PRO CB C 29.6 0.1 1 1103 386 385 GLY H H 8.66 0.02 1 1104 386 385 GLY CA C 44.0 0.1 1 1105 386 385 GLY N N 113.3 0.1 1 1106 387 386 ALA H H 7.59 0.02 1 1107 387 386 ALA CA C 51.2 0.1 1 1108 387 386 ALA CB C 18.3 0.1 1 1109 387 386 ALA N N 123.1 0.1 1 1110 388 387 GLN H H 8.43 0.02 1 1111 388 387 GLN CA C 53.0 0.1 1 1112 388 387 GLN CB C 28.2 0.1 1 1113 388 387 GLN N N 122.6 0.1 1 1114 389 388 ILE H H 8.61 0.02 1 1115 389 388 ILE CA C 57.8 0.1 1 1116 389 388 ILE CB C 33.7 0.1 1 1117 389 388 ILE N N 126.7 0.1 1 1118 390 389 GLN H H 9.52 0.02 1 1119 390 389 GLN CA C 53.0 0.1 1 1120 390 389 GLN CB C 29.6 0.1 1 1121 390 389 GLN N N 129.4 0.1 1 1122 391 390 HIS H H 8.98 0.02 1 1123 391 390 HIS CA C 51.6 0.1 1 1124 391 390 HIS N N 125.2 0.1 1 1125 392 391 LYS H H 8.85 0.02 1 1126 392 391 LYS CA C 53.6 0.1 1 1127 392 391 LYS N N 119.3 0.1 1 1128 393 392 SER H H 8.79 0.02 1 1129 393 392 SER CA C 54.0 0.1 1 1130 393 392 SER CB C 64.5 0.1 1 1131 393 392 SER N N 117.1 0.1 1 1132 394 393 GLY H H 6.95 0.02 1 1133 394 393 GLY CA C 44.6 0.1 1 1134 394 393 GLY N N 110.1 0.1 1 1135 395 394 ILE H H 8.25 0.02 1 1136 395 394 ILE CA C 61.0 0.1 1 1137 395 394 ILE N N 124.9 0.1 1 1138 396 395 VAL H H 6.11 0.02 1 1139 396 395 VAL CA C 59.9 0.1 1 1140 396 395 VAL CB C 35.3 0.1 1 1141 396 395 VAL N N 112.5 0.1 1 1142 397 396 SER CA C 60.2 0.1 1 1143 398 397 GLY H H 8.71 0.02 1 1144 398 397 GLY CA C 43.7 0.1 1 1145 398 397 GLY N N 102.4 0.1 1 1146 399 398 VAL H H 8.09 0.02 1 1147 399 398 VAL CA C 59.9 0.1 1 1148 399 398 VAL CB C 32.2 0.1 1 1149 399 398 VAL N N 119.6 0.1 1 1150 400 399 GLN H H 8.78 0.02 1 1151 400 399 GLN CA C 58.0 0.1 1 1152 400 399 GLN CB C 27.8 0.1 1 1153 400 399 GLN N N 125.2 0.1 1 1154 401 400 ALA H H 7.23 0.02 1 1155 401 400 ALA CA C 50.8 0.1 1 1156 401 400 ALA CB C 19.9 0.1 1 1157 401 400 ALA N N 117.5 0.1 1 1158 402 401 LEU H H 8.67 0.02 1 1159 402 401 LEU CA C 51.1 0.1 1 1160 402 401 LEU CB C 42.2 0.1 1 1161 402 401 LEU N N 120.2 0.1 1 1162 404 403 LEU H H 8.92 0.02 1 1163 404 403 LEU N N 125.9 0.1 1 1164 408 407 PRO CA C 63.8 0.1 1 1165 408 407 PRO CB C 30.8 0.1 1 1166 409 408 ALA H H 8.63 0.02 1 1167 409 408 ALA CA C 53.1 0.1 1 1168 409 408 ALA CB C 17.0 0.1 1 1169 409 408 ALA N N 121.7 0.1 1 1170 410 409 THR H H 8.13 0.02 1 1171 410 409 THR CA C 60.5 0.1 1 1172 410 409 THR CB C 69.1 0.1 1 1173 410 409 THR N N 108.3 0.1 1 1174 411 410 THR H H 7.29 0.02 1 1175 411 410 THR CA C 59.5 0.1 1 1176 411 410 THR CB C 69.9 0.1 1 1177 411 410 THR N N 113.0 0.1 1 1178 412 411 LYS H H 8.95 0.02 1 1179 412 411 LYS CA C 53.9 0.1 1 1180 412 411 LYS CB C 33.1 0.1 1 1181 412 411 LYS N N 121.1 0.1 1 1182 413 412 ALA H H 8.06 0.02 1 1183 413 412 ALA CA C 50.2 0.1 1 1184 413 412 ALA CB C 17.4 0.1 1 1185 413 412 ALA N N 125.5 0.1 1 1186 414 413 VAL H H 7.98 0.02 1 1187 414 413 VAL CA C 62.9 0.1 1 1188 414 413 VAL CB C 32.0 0.1 1 1189 414 413 VAL N N 127.3 0.1 1 stop_ save_