data_5759 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; A model for effector activity in a highly specific biological electron transfer complex: The cytochrome P450cam-putidaredoxin couple ; _BMRB_accession_number 5759 _BMRB_flat_file_name bmr5759.str _Entry_type original _Submission_date 2003-03-31 _Accession_date 2003-04-07 _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 Susan Sondej . 2 Pochapsky Thomas C. . 3 Wei Julie W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 143 "13C chemical shifts" 404 "15N chemical shifts" 143 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-04-07 original author . stop_ _Original_release_date 2004-04-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; A Model for Effector Activity in a Highly Specific Biological Electron Transfer Complex: The Cytochrome P450cam-Putidaredoxin Couple ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22627434 _PubMed_ID 12741821 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pochapsky Susan Sondej . 2 Pochapsky Thomas C. . 3 Wei Julie W. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 42 _Journal_issue 19 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5649 _Page_last 5656 _Year 2003 _Details . loop_ _Keyword 'electron transfer' NMR TROSY 'protein dynamics' 'molecular recognition' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Nickerson, D.P. & Wong, L.L. (1997) Protein Engineering 10, 1357-1361. ; _Citation_title 'The dimerization of Pseudomonas putida cytochrome P450cam: practical consequences and engineering of a monomeric enzyme.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9542996 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nickerson 'D. P.' P. . 2 Wong 'L. L.' L. . stop_ _Journal_abbreviation 'Protein Eng.' _Journal_name_full 'Protein engineering' _Journal_volume 10 _Journal_issue 12 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 1357 _Page_last 1361 _Year 1997 _Details ; Cytochrome P450cam dimerizes via the formation of an intermolecular disulfide bond, complicating the storage and handling of the enzyme, particularly at higher concentrations. The dimeric enzyme is 14% less active than the monomer and forms at a slow but significant rate even at 4 degrees C [k = 1.09 x 10(-3) mM(-1) h(-1)]. To eliminate any ambiguity introduced by dimer formation and to simplify handling and storage of the enzyme, site-directed mutagenesis was used to identify C334 as the single cysteine residue responsible for the formation of the disulfide linkage and to engineer a monomeric enzyme by substituting an alanine in its place. The C334A mutant is identical with the wild-type P450cam monomer in terms of optical spectra, camphor binding and turnover activity, but shows no evidence of dimerization and aggregation even at millimolar concentrations. Preliminary 1H NMR investigations also indicate a significant improvement in the quality of spectra obtained with this mutant. (C334A)P450cam is therefore proposed as an alternative to the wild-type enzyme-a base mutant otherwise identical with the wild-type but with improved handling characteristics. ; save_ ################################## # Molecular system description # ################################## save_system_CYP101 _Saveframe_category molecular_system _Mol_system_name 'cytochrome P450cam' _Abbreviation_common CYP101 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'cytochrome P450cam' $CYP101 Heme $HEM stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic yes _System_thiol_state 'all free' loop_ _Biological_function 'camphor hydroxylase' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CYP101 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'cytochrome P450cam' _Name_variant C334A _Abbreviation_common CYP101 _Molecular_mass . _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_label 1 THR 2 THR 3 GLU 4 THR 5 ILE 6 GLN 7 SER 8 ASN 9 ALA 10 ASN 11 LEU 12 ALA 13 PRO 14 LEU 15 PRO 16 PRO 17 HIS 18 VAL 19 PRO 20 GLU 21 HIS 22 LEU 23 VAL 24 PHE 25 ASP 26 PHE 27 ASP 28 MET 29 TYR 30 ASN 31 PRO 32 SER 33 ASN 34 LEU 35 SER 36 ALA 37 GLY 38 VAL 39 GLN 40 GLU 41 ALA 42 TRP 43 ALA 44 VAL 45 LEU 46 GLN 47 GLU 48 SER 49 ASN 50 VAL 51 PRO 52 ASP 53 LEU 54 VAL 55 TRP 56 THR 57 ARG 58 CYS 59 ASN 60 GLY 61 GLY 62 HIS 63 TRP 64 ILE 65 ALA 66 THR 67 ARG 68 GLY 69 GLN 70 LEU 71 ILE 72 ARG 73 GLU 74 ALA 75 TYR 76 GLU 77 ASP 78 TYR 79 ARG 80 HIS 81 PHE 82 SER 83 SER 84 GLU 85 CYS 86 PRO 87 PHE 88 ILE 89 PRO 90 ARG 91 GLU 92 ALA 93 GLY 94 GLU 95 ALA 96 TYR 97 ASP 98 PHE 99 ILE 100 PRO 101 THR 102 SER 103 MET 104 ASP 105 PRO 106 PRO 107 GLU 108 GLN 109 ARG 110 GLN 111 PHE 112 ARG 113 ALA 114 LEU 115 ALA 116 ASN 117 GLN 118 VAL 119 VAL 120 GLY 121 MET 122 PRO 123 VAL 124 VAL 125 ASP 126 LYS 127 LEU 128 GLU 129 ASN 130 ARG 131 ILE 132 GLN 133 GLU 134 LEU 135 ALA 136 CYS 137 SER 138 LEU 139 ILE 140 GLU 141 SER 142 LEU 143 ARG 144 PRO 145 GLN 146 GLY 147 GLN 148 CYS 149 ASN 150 PHE 151 THR 152 GLU 153 ASP 154 TYR 155 ALA 156 GLU 157 PRO 158 PHE 159 PRO 160 ILE 161 ARG 162 ILE 163 PHE 164 MET 165 LEU 166 LEU 167 ALA 168 GLY 169 LEU 170 PRO 171 GLU 172 GLU 173 ASP 174 ILE 175 PRO 176 HIS 177 LEU 178 LYS 179 TYR 180 LEU 181 THR 182 ASP 183 GLN 184 MET 185 THR 186 ARG 187 PRO 188 ASP 189 GLY 190 SER 191 MET 192 THR 193 PHE 194 ALA 195 GLU 196 ALA 197 LYS 198 GLU 199 ALA 200 LEU 201 TYR 202 ASP 203 TYR 204 LEU 205 ILE 206 PRO 207 ILE 208 ILE 209 GLU 210 GLN 211 ARG 212 ARG 213 GLN 214 LYS 215 PRO 216 GLY 217 THR 218 ASP 219 ALA 220 ILE 221 SER 222 ILE 223 VAL 224 ALA 225 ASN 226 GLY 227 GLN 228 VAL 229 ASN 230 GLY 231 ARG 232 PRO 233 ILE 234 THR 235 SER 236 ASP 237 GLU 238 ALA 239 LYS 240 ARG 241 MET 242 CYS 243 GLY 244 LEU 245 LEU 246 LEU 247 VAL 248 GLY 249 GLY 250 LEU 251 ASP 252 THR 253 VAL 254 VAL 255 ASN 256 PHE 257 LEU 258 SER 259 PHE 260 SER 261 MET 262 GLU 263 PHE 264 LEU 265 ALA 266 LYS 267 SER 268 PRO 269 GLU 270 HIS 271 ARG 272 GLN 273 GLU 274 LEU 275 ILE 276 GLU 277 ARG 278 PRO 279 GLU 280 ARG 281 ILE 282 PRO 283 ALA 284 ALA 285 CYS 286 GLU 287 GLU 288 LEU 289 LEU 290 ARG 291 ARG 292 PHE 293 SER 294 LEU 295 VAL 296 ALA 297 ASP 298 GLY 299 ARG 300 ILE 301 LEU 302 THR 303 SER 304 ASP 305 TYR 306 GLU 307 PHE 308 HIS 309 GLY 310 VAL 311 GLN 312 LEU 313 LYS 314 LYS 315 GLY 316 ASP 317 GLN 318 ILE 319 LEU 320 LEU 321 PRO 322 GLN 323 MET 324 LEU 325 SER 326 GLY 327 LEU 328 ASP 329 GLU 330 ARG 331 GLU 332 ASN 333 ALA 334 ALA 335 PRO 336 MET 337 HIS 338 VAL 339 ASP 340 PHE 341 SER 342 ARG 343 GLN 344 LYS 345 VAL 346 SER 347 HIS 348 THR 349 THR 350 PHE 351 GLY 352 HIS 353 GLY 354 SER 355 HIS 356 LEU 357 CYS 358 LEU 359 GLY 360 GLN 361 HIS 362 LEU 363 ALA 364 ARG 365 ARG 366 GLU 367 ILE 368 ILE 369 VAL 370 THR 371 LEU 372 LYS 373 GLU 374 TRP 375 LEU 376 THR 377 ARG 378 ILE 379 PRO 380 ASP 381 PHE 382 SER 383 ILE 384 ALA 385 PRO 386 GLY 387 ALA 388 GLN 389 ILE 390 GLN 391 HIS 392 LYS 393 SER 394 GLY 395 ILE 396 VAL 397 SER 398 GLY 399 VAL 400 GLN 401 ALA 402 LEU 403 PRO 404 LEU 405 VAL 406 TRP 407 ASP 408 PRO 409 ALA 410 THR 411 THR 412 LYS 413 ALA 414 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 97.83 405 99.75 99.75 0.00e+00 BMRB 19038 entity_1 97.58 404 99.50 99.75 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 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 "cytochrome P-450cam [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 [Pseudomonas putida]" 100.00 415 99.76 99.76 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 Wed Jul 27 11:45:31 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_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $CYP101 'Pseudomonas putida' 303 Eubacteria . Pseudomonas putida 'Originally cloned from naturally-occurring CAM plasmid.' 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' 'E. coli' Escherichia coli NCM533 . ; Clone for C334A mutation of CYP101 which suppresses dimerization obtained from Prof. L. Wong and Dr. D. Nickerson, Nickerson, D.P. & Wong, L.L. (1997) Protein Engineering 10, 1357-1361. ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CYP101 . mM 0.2 0.6 '[U-15N; U-13C, U-85% 2H]' TrisCl 50 mM . . [U-2H] KCl 150 mM . . . camphor 1 mM . . [U-2H] H2O 90 % . . . D2O 10 % . . . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY-INOVA _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY-INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_Experiments_were_run_with_16_scans_per_t1_point,_512_(1H)_x_32_(13C)_x_32_(15N)_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'Experiments were run with 16 scans per t1 point, 512 (1H) x 32 (13C) x 32 (15N)' _Sample_label $sample_1 save_ save_complex_points,_and_1_second_recycle_delays._Spectral_widths_were_10000_Hz_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'complex points, and 1 second recycle delays. Spectral widths were 10000 Hz' _Sample_label $sample_1 save_ save_(1H)_and_2600_Hz_(15N)._13C_spectral_widths_were_4524_Hz_(HNCA_and_HN(CO)CA),_3 _Saveframe_category NMR_applied_experiment _Experiment_name '(1H) and 2600 Hz (15N). 13C spectral widths were 4524 Hz (HNCA and HN(CO)CA),' _Sample_label $sample_1 save_ save_12064_Hz_(HNCACB)_and_3000_Hz_(HNCO)._The_implementations_of_triple_resonance_4 _Saveframe_category NMR_applied_experiment _Experiment_name '12064 Hz (HNCACB) and 3000 Hz (HNCO). The implementations of triple resonance' _Sample_label $sample_1 save_ save_experiments_used_were_TROSY_versions_of_the_sensitivity-enhanced_gradient_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'experiments used were TROSY versions of the sensitivity-enhanced gradient' _Sample_label $sample_1 save_ save_coherence_selection_experiments_as_described_by_Muhandiram_&_Kay_(J._Magn._6 _Saveframe_category NMR_applied_experiment _Experiment_name 'coherence selection experiments as described by Muhandiram & Kay (J. Magn.' _Sample_label $sample_1 save_ save_Reson._Series_B,_vol.103,_203-216,_1994)._7 _Saveframe_category NMR_applied_experiment _Experiment_name 'Reson. Series B, vol.103, 203-216, 1994).' _Sample_label $sample_1 save_ save_A_3D_1H,_15N-TROSY-NOESY_spectrum_and_2D_1H,_15N-TROSY-HSQC_spectrum_were_8 _Saveframe_category NMR_applied_experiment _Experiment_name 'A 3D 1H, 15N-TROSY-NOESY spectrum and 2D 1H, 15N-TROSY-HSQC spectrum were' _Sample_label $sample_1 save_ save_acquired_with_a_2H,_15N-labeled_mos_sample._The_HSQC_was_acquired_with_9 _Saveframe_category NMR_applied_experiment _Experiment_name 'acquired with a 2H, 15N-labeled mos sample. The HSQC was acquired with' _Sample_label $sample_1 save_ save_spectral_widths_of_8000_Hz_(1H)_and_2200_Hz_(15N),_640_x_128_complex_points,_8_10 _Saveframe_category NMR_applied_experiment _Experiment_name 'spectral widths of 8000 Hz (1H) and 2200 Hz (15N), 640 x 128 complex points, 8' _Sample_label $sample_1 save_ save_scans_per_t1_point_and_a_1_second_recycle_delay._The_spectral_widths_for_the_11 _Saveframe_category NMR_applied_experiment _Experiment_name 'scans per t1 point and a 1 second recycle delay. The spectral widths for the' _Sample_label $sample_1 save_ save_3D_NOESY_experiment_were_10000_Hz_(1H),_10000_Hz_(1H)_and_2000_Hz_(15N),_with_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NOESY experiment were 10000 Hz (1H), 10000 Hz (1H) and 2000 Hz (15N), with' _Sample_label $sample_1 save_ save_512_x_128_x_32_complex_points,_respectively._The_mixing_time_was_150_ms,_13 _Saveframe_category NMR_applied_experiment _Experiment_name '512 x 128 x 32 complex points, respectively. The mixing time was 150 ms,' _Sample_label $sample_1 save_ save_recycle_delay_was_1_sec_and_16_scans_per_t1_point_were_acquired._14 _Saveframe_category NMR_applied_experiment _Experiment_name 'recycle delay was 1 sec and 16 scans per t1 point were acquired.' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.4 0.2 n/a temperature 308 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_oxidized_CYP101 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _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 . 10 ASN CA C 54.421 . 1 2 . 10 ASN C C 174.283 . 1 3 . 11 LEU H H 7.657 . 1 4 . 11 LEU N N 122.011 . 1 5 . 11 LEU CA C 53.047 . 1 6 . 11 LEU C C 175.947 . 1 7 . 12 ALA H H 8.603 . 1 8 . 12 ALA N N 129.521 . 1 9 . 12 ALA CA C 50.026 . 1 10 . 16 PRO CA C 63.939 . 1 11 . 16 PRO C C 176.950 . 1 12 . 17 HIS H H 7.69 . 1 13 . 17 HIS N N 111.703 . 1 14 . 17 HIS CA C 55.908 . 1 15 . 17 HIS C C 175.344 . 1 16 . 17 HIS CB C 30.352 . 1 17 . 18 VAL H H 6.799 . 1 18 . 18 VAL N N 127.188 . 1 19 . 18 VAL CA C 59.884 . 1 20 . 18 VAL CB C 31.304 . 1 21 . 19 PRO CA C 61.21 . 1 22 . 19 PRO C C 178.326 . 1 23 . 19 PRO CB C 31.777 . 1 24 . 20 GLU H H 8.591 . 1 25 . 20 GLU N N 121.284 . 1 26 . 20 GLU CA C 59.210 . 1 27 . 20 GLU C C 178.533 . 1 28 . 20 GLU CB C 28.784 . 1 29 . 21 HIS H H 7.846 . 1 30 . 21 HIS N N 113.824 . 1 31 . 21 HIS CA C 57.700 . 1 32 . 21 HIS C C 175.977 . 1 33 . 21 HIS CB C 28.942 . 1 34 . 22 LEU H H 7.202 . 1 35 . 22 LEU N N 119.375 . 1 36 . 22 LEU CA C 53.462 . 1 37 . 22 LEU C C 175.647 . 1 38 . 22 LEU CB C 40.439 . 1 39 . 23 VAL H H 7.097 . 1 40 . 23 VAL N N 120.577 . 1 41 . 23 VAL CA C 62.808 . 1 42 . 23 VAL C C 177.009 . 1 43 . 23 VAL CB C 30.989 . 1 44 . 24 PHE H H 9.181 . 1 45 . 24 PHE N N 133.34 . 1 46 . 24 PHE CA C 57.727 . 1 47 . 24 PHE CB C 40.281 . 1 48 . 35 SER CA C 60.189 . 1 49 . 35 SER C C 174.699 . 1 50 . 36 ALA H H 7.779 . 1 51 . 36 ALA N N 124.536 . 1 52 . 36 ALA CA C 52.472 . 1 53 . 36 ALA C C 176.837 . 1 54 . 36 ALA CB C 18.390 . 1 55 . 37 GLY H H 7.387 . 1 56 . 37 GLY N N 109.476 . 1 57 . 37 GLY CA C 42.824 . 1 58 . 45 LEU CA C 55.48 . 1 59 . 45 LEU C C 174.606 . 1 60 . 46 GLN H H 7.478 . 1 61 . 46 GLN N N 112.056 . 1 62 . 46 GLN CA C 53.498 . 1 63 . 46 GLN C C 176.510 . 1 64 . 46 GLN CB C 31.304 . 1 65 . 47 GLU H H 6.813 . 1 66 . 47 GLU N N 121.213 . 1 67 . 47 GLU CA C 56.879 . 1 68 . 47 GLU C C 177.910 . 1 69 . 47 GLU CB C 29.572 . 1 70 . 48 SER H H 8.531 . 1 71 . 48 SER N N 115.663 . 1 72 . 48 SER CA C 60.949 . 1 73 . 48 SER C C 174.631 . 1 74 . 48 SER CB C 62.961 . 1 75 . 49 ASN H H 8.251 . 1 76 . 49 ASN N N 116.476 . 1 77 . 49 ASN CA C 53.135 . 1 78 . 49 ASN C C 174.517 . 1 79 . 49 ASN CB C 37.447 . 1 80 . 50 VAL H H 7.726 . 1 81 . 50 VAL N N 125.845 . 1 82 . 50 VAL CA C 60.486 . 1 83 . 50 VAL CB C 31.619 . 1 84 . 51 PRO CA C 62.456 . 1 85 . 51 PRO C C 174.006 . 1 86 . 51 PRO CB C 31.934 . 1 87 . 52 ASP H H 7.979 . 1 88 . 52 ASP N N 117.784 . 1 89 . 52 ASP CA C 55.684 . 1 90 . 52 ASP C C 174.624 . 1 91 . 52 ASP CB C 40.439 . 1 92 . 53 LEU H H 7.167 . 1 93 . 53 LEU N N 118.668 . 1 94 . 53 LEU CA C 54.141 . 1 95 . 53 LEU C C 175.273 . 1 96 . 53 LEU CB C 44.534 . 1 97 . 54 VAL H H 8.536 . 1 98 . 54 VAL N N 113.343 . 1 99 . 54 VAL CA C 57.885 . 1 100 . 54 VAL C C 174.288 . 1 101 . 54 VAL CB C 35.242 . 1 102 . 55 TRP H H 8.911 . 1 103 . 55 TRP N N 123.348 . 1 104 . 55 TRP CA C 55.116 . 1 105 . 55 TRP CB C 31.304 . 1 106 . 57 ARG H H 7.173 . 1 107 . 57 ARG N N 121.016 . 1 108 . 57 ARG CA C 57.638 . 1 109 . 57 ARG C C 176.767 . 1 110 . 58 CYS H H 6.952 . 1 111 . 58 CYS N N 113.188 . 1 112 . 58 CYS CA C 58.593 . 1 113 . 58 CYS C C 174.560 . 1 114 . 58 CYS CB C 28.312 . 1 115 . 59 ASN H H 9.202 . 1 116 . 59 ASN N N 114.92 . 1 117 . 59 ASN CA C 55.325 . 1 118 . 59 ASN C C 174.426 . 1 119 . 59 ASN CB C 37.762 . 1 120 . 60 GLY H H 8.764 . 1 121 . 60 GLY N N 103.996 . 1 122 . 60 GLY CA C 44.854 . 1 123 . 60 GLY C C 174.335 . 1 124 . 61 GLY H H 7.431 . 1 125 . 61 GLY N N 111.88 . 1 126 . 61 GLY CA C 43.716 . 1 127 . 62 HIS H H 7.106 . 1 128 . 62 HIS N N 121.457 . 1 129 . 62 HIS CA C 55.130 . 1 130 . 62 HIS CB C 28.469 . 1 131 . 63 TRP CA C 56.185 . 1 132 . 63 TRP C C 180.122 . 1 133 . 64 ILE H H 10.375 . 1 134 . 64 ILE N N 125.813 . 1 135 . 64 ILE CA C 62.178 . 1 136 . 64 ILE C C 175.267 . 1 137 . 65 ALA H H 7.865 . 1 138 . 65 ALA N N 128.444 . 1 139 . 65 ALA CA C 50.359 . 1 140 . 65 ALA CB C 20.910 . 1 141 . 66 THR H H 8.595 . 1 142 . 66 THR N N 108.99 . 1 143 . 66 THR CA C 61.862 . 1 144 . 66 THR C C 173.583 . 1 145 . 66 THR CB C 68.316 . 1 146 . 67 ARG H H 6.449 . 1 147 . 67 ARG N N 114.714 . 1 148 . 67 ARG CA C 51.643 . 1 149 . 67 ARG C C 177.452 . 1 150 . 67 ARG CB C 32.879 . 1 151 . 68 GLY H H 10.36 . 1 152 . 68 GLY N N 112.339 . 1 153 . 68 GLY CA C 47.047 . 1 154 . 68 GLY C C 174.900 . 1 155 . 69 GLN H H 8.884 . 1 156 . 69 GLN N N 119.693 . 1 157 . 69 GLN CA C 58.775 . 1 158 . 69 GLN C C 177.812 . 1 159 . 69 GLN CB C 27.839 . 1 160 . 70 LEU H H 6.443 . 1 161 . 70 LEU N N 116.935 . 1 162 . 70 LEU CA C 58.731 . 1 163 . 70 LEU CB C 42.801 . 1 164 . 90 ARG C C 177.097 . 1 165 . 91 GLU H H 9.337 . 1 166 . 91 GLU N N 115.981 . 1 167 . 91 GLU CA C 59.505 . 1 168 . 91 GLU C C 179.265 . 1 169 . 92 ALA H H 7.2 . 1 170 . 92 ALA N N 123.193 . 1 171 . 92 ALA CA C 53.541 . 1 172 . 92 ALA C C 177.809 . 1 173 . 93 GLY H H 7.394 . 1 174 . 93 GLY N N 104.349 . 1 175 . 93 GLY CA C 48.367 . 1 176 . 93 GLY C C 175.748 . 1 177 . 94 GLU H H 9.04 . 1 178 . 94 GLU N N 120.005 . 1 179 . 94 GLU CA C 55.135 . 1 180 . 95 ALA H H 6.920 . 1 181 . 95 ALA N N 120.082 . 1 182 . 95 ALA CA C 52.368 . 1 183 . 95 ALA C C 176.833 . 1 184 . 96 TYR H H 7.317 . 1 185 . 96 TYR N N 121.496 . 1 186 . 96 TYR CA C 59.264 . 1 187 . 96 TYR CB C 36.502 . 1 188 . 100 PRO CA C 65.729 . 1 189 . 100 PRO C C 175.993 . 1 190 . 101 THR H H 7.706 . 1 191 . 101 THR N N 120.718 . 1 192 . 101 THR CA C 62.872 . 1 193 . 101 THR CB C 70.101 . 1 194 . 106 PRO C C 178.893 . 1 195 . 107 GLU H H 8.795 . 1 196 . 107 GLU N N 127.506 . 1 197 . 107 GLU CA C 59.964 . 1 198 . 107 GLU C C 177.732 . 1 199 . 108 GLN H H 7.706 . 1 200 . 108 GLN N N 113.860 . 1 201 . 108 GLN CA C 57.521 . 1 202 . 108 GLN C C 177.111 . 1 203 . 109 ARG H H 7.573 . 1 204 . 109 ARG N N 119.003 . 1 205 . 109 ARG CA C 62.557 . 1 206 . 112 ARG CA C 58.346 . 1 207 . 112 ARG C C 177.515 . 1 208 . 113 ALA H H 7.768 . 1 209 . 113 ALA N N 120.259 . 1 210 . 113 ALA CA C 51.798 . 1 211 . 122 PRO CA C 65.601 . 1 212 . 122 PRO C C 179.361 . 1 213 . 123 VAL H H 7.199 . 1 214 . 123 VAL N N 116.723 . 1 215 . 123 VAL CA C 64.466 . 1 216 . 123 VAL C C 177.843 . 1 217 . 123 VAL CB C 31.147 . 1 218 . 124 VAL H H 7.473 . 1 219 . 124 VAL N N 121.461 . 1 220 . 124 VAL CA C 66.578 . 1 221 . 124 VAL C C 178.167 . 1 222 . 124 VAL CB C 30.044 . 1 223 . 125 ASP H H 8.21 . 1 224 . 125 ASP N N 118.279 . 1 225 . 125 ASP CA C 57.061 . 1 226 . 125 ASP C C 179.330 . 1 227 . 125 ASP CB C 39.494 . 1 228 . 126 LYS H H 7.25 . 1 229 . 126 LYS N N 118.668 . 1 230 . 126 LYS CA C 58.014 . 1 231 . 126 LYS CB C 31.619 . 1 232 . 144 PRO CA C 64.437 . 1 233 . 144 PRO C C 177.108 . 1 234 . 145 GLN H H 8.318 . 1 235 . 145 GLN N N 113.93 . 1 236 . 145 GLN CA C 57.251 . 1 237 . 145 GLN CB C 28.784 . 1 238 . 146 GLY H H 6.502 . 1 239 . 146 GLY N N 101.768 . 1 240 . 146 GLY CA C 44.111 . 1 241 . 147 GLN H H 5.898 . 1 242 . 147 GLN N N 111.385 . 1 243 . 147 GLN CA C 53.661 . 1 244 . 147 GLN C C 174.502 . 1 245 . 147 GLN CB C 29.572 . 1 246 . 148 CYS H H 8.276 . 1 247 . 148 CYS N N 110.713 . 1 248 . 148 CYS CA C 56.463 . 1 249 . 148 CYS C C 171.836 . 1 250 . 148 CYS CB C 30.359 . 1 251 . 149 ASN H H 9.139 . 1 252 . 149 ASN N N 119.671 . 1 253 . 149 ASN CA C 51.562 . 1 254 . 149 ASN C C 176.163 . 1 255 . 149 ASN CB C 36.817 . 1 256 . 150 PHE H H 9.343 . 1 257 . 150 PHE N N 124.148 . 1 258 . 150 PHE CA C 62.865 . 1 259 . 150 PHE C C 170.000 . 1 260 . 150 PHE CB C 39.470 . 1 261 . 151 THR H H 7.173 . 1 262 . 151 THR N N 109.122 . 1 263 . 151 THR CA C 64.326 . 1 264 . 152 GLU H H 6.230 . 1 265 . 152 GLU N N 118.456 . 1 266 . 152 GLU CA C 57.282 . 1 267 . 152 GLU CB C 30.897 . 1 268 . 164 MET C C 178.921 . 1 269 . 165 LEU H H 7.671 . 1 270 . 165 LEU N N 120.674 . 1 271 . 165 LEU CA C 57.574 . 1 272 . 165 LEU C C 180.189 . 1 273 . 166 LEU H H 8.177 . 1 274 . 166 LEU N N 123.405 . 1 275 . 166 LEU CA C 57.552 . 1 276 . 166 LEU C C 178.330 . 1 277 . 166 LEU CB C 41.413 . 1 278 . 167 ALA H H 8.644 . 1 279 . 167 ALA N N 119.021 . 1 280 . 167 ALA CA C 52.327 . 1 281 . 167 ALA C C 175.086 . 1 282 . 167 ALA CB C 17.753 . 1 283 . 168 GLY H H 7.885 . 1 284 . 168 GLY N N 108.981 . 1 285 . 168 GLY CA C 47.134 . 1 286 . 168 GLY C C 175.298 . 1 287 . 169 LEU H H 8.538 . 1 288 . 169 LEU N N 122.344 . 1 289 . 169 LEU CA C 50.977 . 1 290 . 169 LEU CB C 41.641 . 1 291 . 170 PRO CA C 62.170 . 1 292 . 170 PRO C C 178.249 . 1 293 . 170 PRO CB C 31.583 . 1 294 . 171 GLU H H 8.734 . 1 295 . 171 GLU N N 123.158 . 1 296 . 171 GLU CA C 59.049 . 1 297 . 171 GLU C C 179.458 . 1 298 . 171 GLU CB C 28.497 . 1 299 . 172 GLU H H 9.380 . 1 300 . 172 GLU N N 119.671 . 1 301 . 172 GLU CA C 58.571 . 1 302 . 172 GLU C C 176.985 . 1 303 . 172 GLU CB C 27.926 . 1 304 . 173 ASP H H 7.515 . 1 305 . 173 ASP N N 119.003 . 1 306 . 173 ASP CA C 54.593 . 1 307 . 173 ASP CB C 39.927 . 1 308 . 178 LYS CA C 56.832 . 1 309 . 178 LYS C C 176.481 . 1 310 . 179 TYR H H 7.151 . 1 311 . 179 TYR N N 118.334 . 1 312 . 179 TYR CA C 60.899 . 1 313 . 179 TYR CB C 44.613 . 1 314 . 184 MET CA C 56.993 . 1 315 . 184 MET C C 177.732 . 1 316 . 185 THR H H 7.041 . 1 317 . 185 THR N N 108.45 . 1 318 . 185 THR CA C 64.639 . 1 319 . 185 THR CB C 68.958 . 1 320 . 186 ARG H H 6.526 . 1 321 . 186 ARG N N 118.47 . 1 322 . 186 ARG CA C 56.961 . 1 323 . 186 ARG CB C 32.383 . 1 324 . 187 PRO CA C 62.121 . 1 325 . 187 PRO C C 177.142 . 1 326 . 187 PRO CB C 31.240 . 1 327 . 188 ASP H H 8.344 . 1 328 . 188 ASP N N 126.446 . 1 329 . 188 ASP CA C 52.632 . 1 330 . 188 ASP C C 177.659 . 1 331 . 188 ASP CB C 42.099 . 1 332 . 189 GLY H H 8.465 . 1 333 . 189 GLY N N 110.112 . 1 334 . 189 GLY CA C 44.433 . 1 335 . 193 PHE C C 176.855 . 1 336 . 194 ALA H H 8.405 . 1 337 . 194 ALA N N 119.003 . 1 338 . 194 ALA CA C 54.895 . 1 339 . 194 ALA C C 179.472 . 1 340 . 194 ALA CB C 17.411 . 1 341 . 195 GLU H H 7.412 . 1 342 . 195 GLU N N 117.784 . 1 343 . 195 GLU CA C 58.287 . 1 344 . 195 GLU C C 179.2 . 1 345 . 196 ALA H H 7.699 . 1 346 . 196 ALA N N 124.685 . 1 347 . 196 ALA CA C 54.548 . 1 348 . 196 ALA C C 179.103 . 1 349 . 197 LYS H H 8.097 . 1 350 . 197 LYS N N 118.668 . 1 351 . 197 LYS CA C 58.576 . 1 352 . 197 LYS C C 177.142 . 1 353 . 197 LYS CB C 30.897 . 1 354 . 198 GLU H H 7.757 . 1 355 . 198 GLU N N 117.183 . 1 356 . 198 GLU CA C 58.600 . 1 357 . 198 GLU C C 178.635 . 1 358 . 198 GLU CB C 28.040 . 1 359 . 199 ALA H H 7.393 . 1 360 . 199 ALA N N 121.39 . 1 361 . 199 ALA CA C 54.176 . 1 362 . 199 ALA C C 180.654 . 1 363 . 199 ALA CB C 17.525 . 1 364 . 200 LEU H H 7.872 . 1 365 . 200 LEU N N 123.829 . 1 366 . 200 LEU CA C 57.19 . 1 367 . 200 LEU CB C 40.384 . 1 368 . 206 PRO CA C 64.963 . 1 369 . 207 ILE H H 6.593 . 1 370 . 207 ILE N N 119.552 . 1 371 . 207 ILE CA C 63.969 . 1 372 . 207 ILE CB C 37.412 . 1 373 . 208 ILE CA C 65.153 . 1 374 . 208 ILE C C 177.289 . 1 375 . 209 GLU H H 7.827 . 1 376 . 209 GLU N N 117.147 . 1 377 . 209 GLU CA C 58.883 . 1 378 . 209 GLU CB C 28.269 . 1 379 . 222 ILE CA C 63.77 . 1 380 . 222 ILE C C 178.803 . 1 381 . 223 VAL H H 7.819 . 1 382 . 223 VAL N N 118.632 . 1 383 . 223 VAL CA C 66.525 . 1 384 . 223 VAL C C 177.732 . 1 385 . 224 ALA H H 9.008 . 1 386 . 224 ALA N N 116.617 . 1 387 . 224 ALA CA C 53.781 . 1 388 . 224 ALA C C 179.815 . 1 389 . 224 ALA CB C 18.554 . 1 390 . 225 ASN H H 7.26 . 1 391 . 225 ASN N N 112.764 . 1 392 . 225 ASN CA C 52.613 . 1 393 . 225 ASN C C 174.728 . 1 394 . 225 ASN CB C 39.584 . 1 395 . 226 GLY H H 7.702 . 1 396 . 226 GLY N N 109.758 . 1 397 . 226 GLY CA C 44.978 . 1 398 . 226 GLY C C 171.796 . 1 399 . 227 GLN H H 8.112 . 1 400 . 227 GLN N N 118.279 . 1 401 . 227 GLN CA C 54.018 . 1 402 . 227 GLN C C 175.103 . 1 403 . 227 GLN CB C 30.897 . 1 404 . 228 VAL H H 8.895 . 1 405 . 228 VAL N N 117.819 . 1 406 . 228 VAL CA C 59.374 . 1 407 . 228 VAL C C 174.800 . 1 408 . 228 VAL CB C 33.526 . 1 409 . 229 ASN H H 8.877 . 1 410 . 229 ASN N N 121.677 . 1 411 . 229 ASN CA C 53.651 . 1 412 . 229 ASN C C 175.619 . 1 413 . 229 ASN CB C 37.298 . 1 414 . 230 GLY H H 8.52 . 1 415 . 230 GLY N N 103.324 . 1 416 . 230 GLY CA C 45.322 . 1 417 . 230 GLY C C 173.109 . 1 418 . 231 ARG H H 7.951 . 1 419 . 231 ARG N N 119.375 . 1 420 . 231 ARG CA C 52.082 . 1 421 . 231 ARG CB C 29.183 . 1 422 . 236 ASP CA C 57.341 . 1 423 . 236 ASP C C 177.927 . 1 424 . 237 GLU H H 7.896 . 1 425 . 237 GLU N N 120.011 . 1 426 . 237 GLU CA C 58.540 . 1 427 . 237 GLU C C 179.018 . 1 428 . 237 GLU CB C 29.183 . 1 429 . 238 ALA H H 8.635 . 1 430 . 238 ALA N N 119.671 . 1 431 . 238 ALA CA C 54.791 . 1 432 . 238 ALA C C 180.011 . 1 433 . 238 ALA CB C 17.182 . 1 434 . 239 LYS H H 8.248 . 1 435 . 239 LYS N N 121.991 . 1 436 . 239 LYS CA C 59.649 . 1 437 . 239 LYS C C 175.993 . 1 438 . 239 LYS CB C 29.755 . 1 439 . 240 ARG H H 7.411 . 1 440 . 240 ARG N N 120.005 . 1 441 . 240 ARG CA C 58.231 . 1 442 . 243 GLY C C 175.143 . 1 443 . 244 LEU H H 7.025 . 1 444 . 244 LEU N N 119.728 . 1 445 . 244 LEU CA C 53.297 . 1 446 . 244 LEU C C 173.569 . 1 447 . 244 LEU CB C 40.384 . 1 448 . 245 LEU H H 6.851 . 1 449 . 245 LEU N N 118.88 . 1 450 . 245 LEU CA C 53.36 . 1 451 . 245 LEU CB C 42.213 . 1 452 . 264 LEU C C 170.000 . 1 453 . 265 ALA H H 7.011 . 1 454 . 265 ALA N N 113.32 . 1 455 . 265 ALA CA C 53.503 . 1 456 . 265 ALA C C 178.559 . 1 457 . 266 LYS H H 7.298 . 1 458 . 266 LYS N N 116.299 . 1 459 . 266 LYS CA C 56.541 . 1 460 . 266 LYS C C 176.481 . 1 461 . 266 LYS CB C 32.955 . 1 462 . 267 SER H H 7.139 . 1 463 . 267 SER N N 114.461 . 1 464 . 267 SER CA C 53.758 . 1 465 . 267 SER CB C 61.072 . 1 466 . 270 HIS CA C 61.502 . 1 467 . 270 HIS C C 177.803 . 1 468 . 271 ARG H H 7.576 . 1 469 . 271 ARG N N 117.508 . 1 470 . 271 ARG CA C 60.385 . 1 471 . 271 ARG C C 177.928 . 1 472 . 271 ARG CB C 29.526 . 1 473 . 272 GLN H H 8.34 . 1 474 . 272 GLN N N 116.794 . 1 475 . 272 GLN CA C 58.126 . 1 476 . 272 GLN CB C 27.011 . 1 477 . 273 GLU H H 7.474 . 1 478 . 273 GLU N N 119.003 . 1 479 . 273 GLU CA C 59.492 . 1 480 . 273 GLU C C 178.149 . 1 481 . 273 GLU CB C 30.097 . 1 482 . 274 LEU H H 7.019 . 1 483 . 274 LEU N N 115.557 . 1 484 . 274 LEU CA C 55.485 . 1 485 . 274 LEU CB C 40.270 . 1 486 . 278 PRO CA C 64.168 . 1 487 . 278 PRO C C 179.583 . 1 488 . 279 GLU H H 9.953 . 1 489 . 279 GLU N N 121.814 . 1 490 . 279 GLU CA C 57.812 . 1 491 . 279 GLU C C 177.507 . 1 492 . 279 GLU CB C 26.554 . 1 493 . 280 ARG H H 8.504 . 1 494 . 280 ARG N N 120.647 . 1 495 . 280 ARG CA C 55.825 . 1 496 . 280 ARG C C 176.343 . 1 497 . 280 ARG CB C 29.412 . 1 498 . 281 ILE H H 7.819 . 1 499 . 281 ILE N N 119.905 . 1 500 . 281 ILE CA C 67.629 . 1 501 . 302 THR H H 8.665 . 1 502 . 302 THR N N 116.44 . 1 503 . 302 THR CA C 61.950 . 1 504 . 302 THR C C 174.078 . 1 505 . 302 THR CB C 69.758 . 1 506 . 303 SER H H 7.608 . 1 507 . 303 SER N N 113.046 . 1 508 . 303 SER CA C 56.107 . 1 509 . 303 SER C C 171.463 . 1 510 . 303 SER CB C 65.072 . 1 511 . 304 ASP H H 8.452 . 1 512 . 304 ASP N N 121.342 . 1 513 . 304 ASP CA C 54.631 . 1 514 . 304 ASP C C 177.110 . 1 515 . 304 ASP CB C 38.784 . 1 516 . 305 TYR H H 8.43 . 1 517 . 305 TYR N N 126.198 . 1 518 . 305 TYR CA C 56.242 . 1 519 . 305 TYR C C 172.054 . 1 520 . 305 TYR CB C 40.841 . 1 521 . 306 GLU H H 7.674 . 1 522 . 306 GLU N N 129.663 . 1 523 . 306 GLU CA C 54.476 . 1 524 . 306 GLU C C 172.958 . 1 525 . 306 GLU CB C 29.183 . 1 526 . 307 PHE H H 8.491 . 1 527 . 307 PHE N N 129.804 . 1 528 . 307 PHE CA C 53.988 . 1 529 . 307 PHE C C 173.518 . 1 530 . 307 PHE CB C 41.984 . 1 531 . 308 HIS H H 8.948 . 1 532 . 308 HIS N N 123.348 . 1 533 . 308 HIS CA C 56.596 . 1 534 . 308 HIS C C 174.971 . 1 535 . 308 HIS CB C 25.640 . 1 536 . 309 GLY H H 8.334 . 1 537 . 309 GLY N N 102.582 . 1 538 . 309 GLY CA C 44.688 . 1 539 . 309 GLY C C 173.487 . 1 540 . 310 VAL H H 7.477 . 1 541 . 310 VAL N N 123.723 . 1 542 . 310 VAL CA C 60.875 . 1 543 . 310 VAL C C 174.625 . 1 544 . 310 VAL CB C 32.269 . 1 545 . 311 GLN H H 8.358 . 1 546 . 311 GLN N N 125.986 . 1 547 . 311 GLN CA C 55.652 . 1 548 . 311 GLN C C 173.524 . 1 549 . 311 GLN CB C 27.240 . 1 550 . 312 LEU H H 8.621 . 1 551 . 312 LEU N N 128.602 . 1 552 . 312 LEU CA C 53.330 . 1 553 . 312 LEU C C 177.351 . 1 554 . 312 LEU CB C 40.727 . 1 555 . 313 LYS H H 8.538 . 1 556 . 313 LYS N N 124.607 . 1 557 . 313 LYS CA C 53.190 . 1 558 . 313 LYS C C 175.508 . 1 559 . 313 LYS CB C 33.526 . 1 560 . 314 LYS H H 8.713 . 1 561 . 314 LYS N N 121.814 . 1 562 . 314 LYS CA C 58.295 . 1 563 . 314 LYS C C 177.484 . 1 564 . 314 LYS CB C 31.926 . 1 565 . 315 GLY H H 8.6 . 1 566 . 315 GLY N N 117.183 . 1 567 . 315 GLY CA C 44.686 . 1 568 . 328 ASP H H 9.445 . 1 569 . 328 ASP N N 124.289 . 1 570 . 328 ASP CA C 57.147 . 1 571 . 328 ASP C C 176.894 . 1 572 . 329 GLU H H 8.716 . 1 573 . 329 GLU N N 116.016 . 1 574 . 329 GLU CA C 57.516 . 1 575 . 330 ARG H H 7.161 . 1 576 . 330 ARG N N 123.971 . 1 577 . 330 ARG CA C 54.603 . 1 578 . 335 PRO CA C 63.653 . 1 579 . 335 PRO C C 179.799 . 1 580 . 336 MET H H 8.723 . 1 581 . 336 MET N N 115.945 . 1 582 . 336 MET CA C 53.822 . 1 583 . 336 MET CB C 29.412 . 1 584 . 337 HIS H H 8.133 . 1 585 . 337 HIS N N 123.759 . 1 586 . 337 HIS CA C 55.04 . 1 587 . 337 HIS C C 174.224 . 1 588 . 338 VAL H H 8.088 . 1 589 . 338 VAL N N 126.552 . 1 590 . 338 VAL CA C 61.386 . 1 591 . 338 VAL C C 174.805 . 1 592 . 338 VAL CB C 29.869 . 1 593 . 339 ASP H H 10.117 . 1 594 . 339 ASP N N 131.289 . 1 595 . 339 ASP CA C 51.369 . 1 596 . 339 ASP C C 176.507 . 1 597 . 339 ASP CB C 41.641 . 1 598 . 340 PHE H H 9.445 . 1 599 . 340 PHE N N 124.289 . 1 600 . 340 PHE CA C 55.406 . 1 601 . 340 PHE C C 176.894 . 1 602 . 340 PHE CB C 35.355 . 1 603 . 341 SER H H 8.716 . 1 604 . 341 SER N N 116.016 . 1 605 . 341 SER CA C 57.516 . 1 606 . 341 SER C C 173.943 . 1 607 . 342 ARG H H 7.16 . 1 608 . 342 ARG N N 123.971 . 1 609 . 342 ARG CA C 57.488 . 1 610 . 342 ARG CB C 30.212 . 1 611 . 386 GLY CA C 44.9 . 1 612 . 386 GLY C C 174.006 . 1 613 . 387 ALA H H 7.606 . 1 614 . 387 ALA N N 123.688 . 1 615 . 387 ALA CA C 52.152 . 1 616 . 387 ALA C C 176.982 . 1 617 . 387 ALA CB C 19.011 . 1 618 . 388 GLN H H 8.360 . 1 619 . 388 GLN N N 122.415 . 1 620 . 388 GLN CA C 53.892 . 1 621 . 388 GLN C C 174.833 . 1 622 . 388 GLN CB C 28.954 . 1 623 . 389 ILE H H 8.536 . 1 624 . 389 ILE N N 126.764 . 1 625 . 389 ILE CA C 58.702 . 1 626 . 389 ILE C C 175.830 . 1 627 . 389 ILE CB C 34.441 . 1 628 . 390 GLN H H 9.455 . 1 629 . 390 GLN N N 129.345 . 1 630 . 390 GLN CA C 54.015 . 1 631 . 390 GLN C C 174.774 . 1 632 . 390 GLN CB C 30.555 . 1 633 . 391 HIS H H 8.926 . 1 634 . 391 HIS N N 125.354 . 1 635 . 391 HIS CA C 52.650 . 1 636 . 391 HIS C C 174.610 . 1 637 . 391 HIS CB C 34.212 . 1 638 . 392 LYS H H 8.778 . 1 639 . 392 LYS N N 118.986 . 1 640 . 392 LYS CA C 54.513 . 1 641 . 392 LYS CB C 34.898 . 1 642 . 397 SER CA C 60.652 . 1 643 . 397 SER C C 172.009 . 1 644 . 398 GLY H H 8.537 . 1 645 . 398 GLY N N 102.652 . 1 646 . 398 GLY CA C 44.662 . 1 647 . 399 VAL CA C 60.541 . 1 648 . 399 VAL C C 175.972 . 1 649 . 400 GLN H H 8.819 . 1 650 . 400 GLN N N 125.019 . 1 651 . 400 GLN CA C 59.054 . 1 652 . 400 GLN C C 175.411 . 1 653 . 400 GLN CB C 28.497 . 1 654 . 401 ALA H H 7.314 . 1 655 . 401 ALA N N 117.466 . 1 656 . 401 ALA CA C 51.734 . 1 657 . 401 ALA CB C 21.068 . 1 658 . 402 LEU H H 8.585 . 1 659 . 402 LEU N N 119.622 . 1 660 . 408 PRO CA C 64.631 . 1 661 . 408 PRO C C 178.121 . 1 662 . 409 ALA H H 8.650 . 1 663 . 409 ALA N N 121.673 . 1 664 . 409 ALA CA C 53.939 . 1 665 . 409 ALA C C 178.641 . 1 666 . 409 ALA CB C 17.868 . 1 667 . 410 THR H H 8.127 . 1 668 . 410 THR N N 108.309 . 1 669 . 410 THR CA C 61.525 . 1 670 . 410 THR C C 175.738 . 1 671 . 410 THR CB C 69.415 . 1 672 . 411 THR H H 9.043 . 1 673 . 411 THR N N 119.658 . 1 674 . 411 THR CA C 60.551 . 1 675 . 411 THR C C 173.973 . 1 676 . 411 THR CB C 70.444 . 1 677 . 412 LYS H H 8.942 . 1 678 . 412 LYS N N 120.93 . 1 679 . 412 LYS CA C 54.790 . 1 680 . 412 LYS C C 174.015 . 1 681 . 412 LYS CB C 33.869 . 1 682 . 413 ALA H H 8.013 . 1 683 . 413 ALA N N 125.031 . 1 684 . 413 ALA CA C 51.034 . 1 685 . 413 ALA C C 177.108 . 1 686 . 413 ALA CB C 18.325 . 1 687 . 414 VAL H H 7.889 . 1 688 . 414 VAL N N 126.693 . 1 689 . 414 VAL CA C 63.558 . 1 690 . 414 VAL CB C 32.612 . 1 stop_ save_