data_6183 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for cAMP-dependent protein kinase ; _BMRB_accession_number 6183 _BMRB_flat_file_name bmr6183.str _Entry_type original _Submission_date 2004-04-20 _Accession_date 2004-04-20 _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 Thomas Langer . . 2 Martin Vogtherr . . 3 Bettina Elshorst . . 4 Marco Betz . . 5 Ulrich Schieborr . . 6 Krishna Saxena . . 7 Harald Schwalbe . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 191 "13C chemical shifts" 579 "15N chemical shifts" 191 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-04-20 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR backbone assignment of a protein kinase catalytic domain by a combination of several approaches: Application to the catalytic subunit of cAMP-dependent protein kinase ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15481030 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Langer Thomas . . 2 Vogtherr Martin . . 3 Elshorst Bettina . . 4 Betz Marco . . 5 Schieborr Ulrich . . 6 Saxena Krishna . . 7 Schwalbe Harald . . stop_ _Journal_abbreviation Chembiochem _Journal_volume 5 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1508 _Page_last 1516 _Year 2004 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref-1 _Saveframe_category citation _Citation_full ; Ch. Bartels, T.-H. Xia, M. Billeter, P. Guntert, K. Wuthrich (1995). J. Biomol. NMR 5, 1-10 ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _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 . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_cAPK_PKA _Saveframe_category molecular_system _Mol_system_name 'cAMP-dependent protein kinase' _Abbreviation_common 'cAPK, PKA' _Enzyme_commission_number 2.7.1.37 loop_ _Mol_system_component_name _Mol_label 'cAMP dependent protein kinase catalytic domain' $cAPK_PKA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'protein kinase catalytic domain' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cAPK_PKA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'protein kinase catalytic domain' _Abbreviation_common 'cAPK, PKA' _Molecular_mass . _Mol_thiol_state 'all free' _Details 'First amino acid=Gly -3' ############################## # Polymer residue sequence # ############################## _Residue_count 353 _Mol_residue_sequence ; GHMGNAAAAKKGSEQESVKE FLAKAKEEFLKKWESPSQNT AQLDHFDRIKTLGTGSFGRV MLVKHKETGNHYAMKILDKQ KVVKLKQIEHTLNEKRILQA VNFPFLVKLEFSFKDNSNLY MVMEYVPGGEMFSHLRRIGR FSEPHARFYAAQIVLTFEYL HSLDLIYRDLKPENLLIDQQ GYIQVTDFGFAKRVKGRTWT LCGTPEYLAPEIILSKGYNK AVDWWALGVLIYEMAAGYPP FFADQPIQIYEKIVSGKVRF PSHFSSDLKDLLRNLLQVDL TKRFGNLKNGVNDIKNHKWF ATTDWIAIYQRKVEAPFIPK FKGPGDTSNFDDYEEEEIRV SINEKCGKEFTEF ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -3 GLY 2 -2 HIS 3 -1 MET 4 1 GLY 5 2 ASN 6 3 ALA 7 4 ALA 8 5 ALA 9 6 ALA 10 7 LYS 11 8 LYS 12 9 GLY 13 10 SER 14 11 GLU 15 12 GLN 16 13 GLU 17 14 SER 18 15 VAL 19 16 LYS 20 17 GLU 21 18 PHE 22 19 LEU 23 20 ALA 24 21 LYS 25 22 ALA 26 23 LYS 27 24 GLU 28 25 GLU 29 26 PHE 30 27 LEU 31 28 LYS 32 29 LYS 33 30 TRP 34 31 GLU 35 32 SER 36 33 PRO 37 34 SER 38 35 GLN 39 36 ASN 40 37 THR 41 38 ALA 42 39 GLN 43 40 LEU 44 41 ASP 45 42 HIS 46 43 PHE 47 44 ASP 48 45 ARG 49 46 ILE 50 47 LYS 51 48 THR 52 49 LEU 53 50 GLY 54 51 THR 55 52 GLY 56 53 SER 57 54 PHE 58 55 GLY 59 56 ARG 60 57 VAL 61 58 MET 62 59 LEU 63 60 VAL 64 61 LYS 65 62 HIS 66 63 LYS 67 64 GLU 68 65 THR 69 66 GLY 70 67 ASN 71 68 HIS 72 69 TYR 73 70 ALA 74 71 MET 75 72 LYS 76 73 ILE 77 74 LEU 78 75 ASP 79 76 LYS 80 77 GLN 81 78 LYS 82 79 VAL 83 80 VAL 84 81 LYS 85 82 LEU 86 83 LYS 87 84 GLN 88 85 ILE 89 86 GLU 90 87 HIS 91 88 THR 92 89 LEU 93 90 ASN 94 91 GLU 95 92 LYS 96 93 ARG 97 94 ILE 98 95 LEU 99 96 GLN 100 97 ALA 101 98 VAL 102 99 ASN 103 100 PHE 104 101 PRO 105 102 PHE 106 103 LEU 107 104 VAL 108 105 LYS 109 106 LEU 110 107 GLU 111 108 PHE 112 109 SER 113 110 PHE 114 111 LYS 115 112 ASP 116 113 ASN 117 114 SER 118 115 ASN 119 116 LEU 120 117 TYR 121 118 MET 122 119 VAL 123 120 MET 124 121 GLU 125 122 TYR 126 123 VAL 127 124 PRO 128 125 GLY 129 126 GLY 130 127 GLU 131 128 MET 132 129 PHE 133 130 SER 134 131 HIS 135 132 LEU 136 133 ARG 137 134 ARG 138 135 ILE 139 136 GLY 140 137 ARG 141 138 PHE 142 139 SER 143 140 GLU 144 141 PRO 145 142 HIS 146 143 ALA 147 144 ARG 148 145 PHE 149 146 TYR 150 147 ALA 151 148 ALA 152 149 GLN 153 150 ILE 154 151 VAL 155 152 LEU 156 153 THR 157 154 PHE 158 155 GLU 159 156 TYR 160 157 LEU 161 158 HIS 162 159 SER 163 160 LEU 164 161 ASP 165 162 LEU 166 163 ILE 167 164 TYR 168 165 ARG 169 166 ASP 170 167 LEU 171 168 LYS 172 169 PRO 173 170 GLU 174 171 ASN 175 172 LEU 176 173 LEU 177 174 ILE 178 175 ASP 179 176 GLN 180 177 GLN 181 178 GLY 182 179 TYR 183 180 ILE 184 181 GLN 185 182 VAL 186 183 THR 187 184 ASP 188 185 PHE 189 186 GLY 190 187 PHE 191 188 ALA 192 189 LYS 193 190 ARG 194 191 VAL 195 192 LYS 196 193 GLY 197 194 ARG 198 195 THR 199 196 TRP 200 197 THR 201 198 LEU 202 199 CYS 203 200 GLY 204 201 THR 205 202 PRO 206 203 GLU 207 204 TYR 208 205 LEU 209 206 ALA 210 207 PRO 211 208 GLU 212 209 ILE 213 210 ILE 214 211 LEU 215 212 SER 216 213 LYS 217 214 GLY 218 215 TYR 219 216 ASN 220 217 LYS 221 218 ALA 222 219 VAL 223 220 ASP 224 221 TRP 225 222 TRP 226 223 ALA 227 224 LEU 228 225 GLY 229 226 VAL 230 227 LEU 231 228 ILE 232 229 TYR 233 230 GLU 234 231 MET 235 232 ALA 236 233 ALA 237 234 GLY 238 235 TYR 239 236 PRO 240 237 PRO 241 238 PHE 242 239 PHE 243 240 ALA 244 241 ASP 245 242 GLN 246 243 PRO 247 244 ILE 248 245 GLN 249 246 ILE 250 247 TYR 251 248 GLU 252 249 LYS 253 250 ILE 254 251 VAL 255 252 SER 256 253 GLY 257 254 LYS 258 255 VAL 259 256 ARG 260 257 PHE 261 258 PRO 262 259 SER 263 260 HIS 264 261 PHE 265 262 SER 266 263 SER 267 264 ASP 268 265 LEU 269 266 LYS 270 267 ASP 271 268 LEU 272 269 LEU 273 270 ARG 274 271 ASN 275 272 LEU 276 273 LEU 277 274 GLN 278 275 VAL 279 276 ASP 280 277 LEU 281 278 THR 282 279 LYS 283 280 ARG 284 281 PHE 285 282 GLY 286 283 ASN 287 284 LEU 288 285 LYS 289 286 ASN 290 287 GLY 291 288 VAL 292 289 ASN 293 290 ASP 294 291 ILE 295 292 LYS 296 293 ASN 297 294 HIS 298 295 LYS 299 296 TRP 300 297 PHE 301 298 ALA 302 299 THR 303 300 THR 304 301 ASP 305 302 TRP 306 303 ILE 307 304 ALA 308 305 ILE 309 306 TYR 310 307 GLN 311 308 ARG 312 309 LYS 313 310 VAL 314 311 GLU 315 312 ALA 316 313 PRO 317 314 PHE 318 315 ILE 319 316 PRO 320 317 LYS 321 318 PHE 322 319 LYS 323 320 GLY 324 321 PRO 325 322 GLY 326 323 ASP 327 324 THR 328 325 SER 329 326 ASN 330 327 PHE 331 328 ASP 332 329 ASP 333 330 TYR 334 331 GLU 335 332 GLU 336 333 GLU 337 334 GLU 338 335 ILE 339 336 ARG 340 337 VAL 341 338 SER 342 339 ILE 343 340 ASN 344 341 GLU 345 342 LYS 346 343 CYS 347 344 GLY 348 345 LYS 349 346 GLU 350 347 PHE 351 348 THR 352 349 GLU 353 350 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1APM "2.0 Angstrom Refined Crystal Structure Of The Catalytic Subunit Of Camp-Dependent Protein Kinase Complexed With A Peptide Inhib" 99.15 350 97.43 98.57 0.00e+00 PDB 1ATP "2.2 Angstrom Refined Crystal Structure Of The Catalytic Subunit Of Camp-Dependent Protein Kinase Complexed With Mnatp And A Pep" 99.15 350 98.00 98.86 0.00e+00 PDB 1BKX "A Binary Complex Of The Catalytic Subunit Of Camp-Dependent Protein Kinase And Adenosine Further Defines Conformational Flexibi" 99.15 350 97.71 98.57 0.00e+00 PDB 1BX6 "Crystal Structure Of The Potent Natural Product Inhibitor Balanol In Complex With The Catalytic Subunit Of Camp- Dependent Prot" 99.15 350 97.71 98.57 0.00e+00 PDB 1CTP "Structure Of The Mammalian Catalytic Subunit Of Camp-Dependent Protein Kinase And An Inhibitor Peptide Displays An Open Conform" 99.15 350 97.14 99.14 0.00e+00 PDB 1FMO "Crystal Structure Of A Polyhistidine-Tagged Recombinant Catalytic Subunit Of Camp-Dependent Protein Kinase Complexed With The P" 99.15 350 98.00 98.86 0.00e+00 PDB 1J3H "Crystal Structure Of Apoenzyme Camp-Dependent Protein Kinase Catalytic Subunit" 99.15 350 97.71 98.57 0.00e+00 PDB 1JBP "Crystal Structure Of The Catalytic Subunit Of Camp- Dependent Protein Kinase Complexed With A Substrate Peptide, Adp And Deterg" 99.15 350 97.43 98.57 0.00e+00 PDB 1JLU "Crystal Structure Of The Catalytic Subunit Of Camp-dependent Protein Kinase Complexed With A Phosphorylated Substrate Peptide A" 99.15 350 98.00 98.86 0.00e+00 PDB 1L3R "Crystal Structure Of A Transition State Mimic Of The Catalytic Subunit Of Camp-Dependent Protein Kinase" 99.15 350 97.43 98.29 0.00e+00 PDB 1RDQ "Hydrolysis Of Atp In The Crystal Of Y204a Mutant Of Camp-dependent Protein Kinase" 99.15 350 97.71 98.57 0.00e+00 PDB 1RE8 "Crystal Structure Of Camp-Dependent Protein Kinase Complexed With Balanol Analog 2" 99.15 350 98.00 98.86 0.00e+00 PDB 1REJ "Crystal Structure Of Camp-Dependent Protein Kinase Complexed With Balanol Analog 1" 99.15 350 98.00 98.86 0.00e+00 PDB 1REK "Crystal Structure Of Camp-Dependent Protein Kinase Complexed With Balanol Analog 8" 99.15 350 98.00 98.86 0.00e+00 PDB 1SVH "Crystal Structure Of Protein Kinase A In Complex With Azepane Derivative 8" 99.15 350 97.14 98.57 0.00e+00 PDB 1SYK "Crystal Structure Of E230q Mutant Of Camp-Dependent Protein Kinase Reveals Unexpected Apoenzyme Conformation" 99.15 350 97.71 98.86 0.00e+00 PDB 1XH5 "Crystal Structures Of Protein Kinase B Selective Inhibitors In Complex With Protein Kinase A And Mutants" 99.15 350 97.14 98.57 0.00e+00 PDB 1XH6 "Crystal Structures Of Protein Kinase B Selective Inhibitors In Complex With Protein Kinase A And Mutants" 99.15 350 97.14 98.57 0.00e+00 PDB 1XH8 "Crystal Structures Of Protein Kinase B Selective Inhibitors In Complex With Protein Kinase A And Mutants" 99.15 350 97.14 98.57 0.00e+00 PDB 2C1A "Structure Of Camp-Dependent Protein Kinase Complexed With Isoquinoline-5-Sulfonic Acid (2-(2-(4-Chlorobenzyloxy) Ethylamino)eth" 99.43 351 97.15 98.58 0.00e+00 PDB 2C1B "Structure Of Camp-Dependent Protein Kinase Complexed With (4r,2s)-5'-(4-(4-Chlorobenzyloxy)pyrrolidin-2- Ylmethanesulfonyl)isoq" 99.43 351 97.15 98.58 0.00e+00 PDB 2CPK "Crystal Structure Of The Catalytic Subunit Of Cyclic Adenosine Monophosphate-Dependent Protein Kinase" 99.15 350 97.71 98.57 0.00e+00 PDB 2ERZ "Crystal Structure Of C-amp Dependent Kinase (pka) Bound To Hydroxyfasudil" 99.43 351 98.01 98.86 0.00e+00 PDB 2F7E "Pka Complexed With (S)-2-(1h-Indol-3-Yl)-1-(5-Isoquinolin-6- Yl-Pyridin-3-Yloxymethyl-Etylamine" 99.43 351 97.72 99.15 0.00e+00 PDB 2F7X "Protein Kinase A Bound To (s)-2-(1h-indol-3-yl)-1-[5-((e)-2- Pyridin-4-yl-vinyl)-pyridin-3-yloxymethyl]-ethylamine" 99.43 351 97.72 99.15 0.00e+00 PDB 2F7Z "Protein Kinase A Bound To (R)-1-(1h-Indol-3-Ylmethyl)-2-(2- Pyridin-4-Yl-[1,7]naphtyridin-5-Yloxy)-Ehylamine" 99.43 351 97.72 99.15 0.00e+00 PDB 2GFC "Camp-Dependent Protein Kinase Pka Catalytic Subunit With Pki-5-24" 99.15 350 97.14 98.57 0.00e+00 PDB 2GU8 "Discovery Of 2-pyrimidyl-5-amidothiophenes As Novel And Potent Inhibitors For Akt: Synthesis And Sar Studies" 95.47 337 97.63 98.81 0.00e+00 PDB 2OH0 "Crystal Structure Of Protein Kinase A In Complex With Pyridine-Pyrazolopyridine Based Inhibitors" 99.43 351 97.72 99.15 0.00e+00 PDB 2OJF "Crystal Structure Of Protein Kinase A In Complex With Pyridine-Pyrazolopyridine Based Inhibitors" 99.43 351 97.72 99.15 0.00e+00 PDB 2QCS "A Complex Structure Between The Catalytic And Regulatory Subunit Of Protein Kinase A That Represents The Inhibited State" 99.15 350 97.71 98.57 0.00e+00 PDB 2QUR "Crystal Structure Of F327aK285P MUTANT OF CAMP-Dependent Protein Kinase" 99.15 350 97.43 98.29 0.00e+00 PDB 2QVS "Crystal Structure Of Type Iia Holoenzyme Of Camp-Dependent Protein Kinase" 99.15 350 98.00 98.86 0.00e+00 PDB 2UZT "Pka Structures Of Akt, Indazole-Pyridine Inhibitors" 95.18 336 97.32 99.11 0.00e+00 PDB 2UZU "Pka Structures Of Indazole-Pyridine Series Of Akt Inhibitors" 95.18 336 97.32 99.11 0.00e+00 PDB 2UZV "Pka Structures Of Indazole-pyridine Series Of Akt Inhibitors" 95.18 336 97.32 99.11 0.00e+00 PDB 2UZW "Pka Structures Of Indazole-Pyridine Series Of Akt Inhibitors" 95.18 336 97.32 99.11 0.00e+00 PDB 2VO7 "Structure Of Pka Complexed With 4-(4-Chlorobenzyl)-1-(7h- Pyrrolo(2,3-D)pyrimidin-4-Yl)piperidin-4-Ylamine" 99.43 351 97.15 98.58 0.00e+00 PDB 3AG9 "Complex Of Pka With The Bisubstrate Protein Kinase Inhibitor Arc-1012" 99.43 351 97.15 98.58 0.00e+00 PDB 3AGL "Complex Of Pka With The Bisubstrate Protein Kinase Inhibitor Arc-1039" 99.43 351 97.44 98.58 0.00e+00 PDB 3AGM "Complex Of Pka With The Bisubstrate Protein Kinase Inhibitor Arc-670" 99.43 351 97.72 98.86 0.00e+00 PDB 3FHI "Crystal Structure Of A Complex Between The Catalytic And Regulatory (Ri{alpha}) Subunits Of Pka" 99.15 350 97.71 98.57 0.00e+00 PDB 3FJQ "Crystal Structure Of Camp-Dependent Protein Kinase Catalytic Subunit Alpha In Complex With Peptide Inhibitor Pki Alpha (6-25)" 99.15 350 98.00 98.86 0.00e+00 PDB 3IDB "Crystal Structure Of (108-268)riib:c Holoenzyme Of Camp- Dependent Protein Kinase" 99.15 350 98.00 98.86 0.00e+00 PDB 3IDC "Crystal Structure Of (102-265)riib:c Holoenzyme Of Camp- Dependent Protein Kinase" 99.15 350 98.00 98.86 0.00e+00 PDB 3J4Q "Pseudo-atomic Model Of The Akap18-pka Complex In A Bent Conformation Derived From Electron Microscopy" 99.43 351 98.58 99.43 0.00e+00 PDB 3J4R "Pseudo-atomic Model Of The Akap18-pka Complex In A Linear Conformation Derived From Electron Microscopy" 99.43 351 98.58 99.43 0.00e+00 PDB 3L9L "Crystal Structure Of Pka With Compound 36" 99.43 351 97.72 98.86 0.00e+00 PDB 3MVJ "Human Cyclic Amp-Dependent Protein Kinase Pka Inhibitor Complex" 99.72 371 97.73 98.86 0.00e+00 PDB 3NX8 "Human Camp Dependent Protein Kinase In Complex With Phenol" 99.43 351 97.44 98.58 0.00e+00 PDB 3O7L "Crystal Structure Of Phospholamban (1-19):pka C-Subunit:amp-Pnp:mg2+ Complex" 99.15 350 98.00 98.86 0.00e+00 PDB 3OOG "Human Camp-Dependent Protein Kinase In Complex With A Small Fragment" 99.43 351 97.72 98.86 0.00e+00 PDB 3OVV "Human Camp-Dependent Protein Kinase In Complex With An Inhibitor" 99.43 351 97.72 98.86 0.00e+00 PDB 3OW3 "Discovery Of Dihydrothieno- And Dihydrofuropyrimidines As Potent Pan Akt Inhibitors" 99.15 350 98.00 98.86 0.00e+00 PDB 3OWP "Human Camp-Dependent Protein Kinase In Complex With An Inhibitor" 99.43 351 97.72 98.86 0.00e+00 PDB 3OXT "Human Camp-Dependent Protein Kinase In Complex With An Inhibitor" 99.43 351 97.72 98.86 0.00e+00 PDB 3P0M "Human Camp-Dependent Protein Kinase In Complex With An Inhibitor" 99.43 351 97.72 98.86 0.00e+00 PDB 3POO "Human Camp-Dependent Protein Kinase In Complex With An Inhibitor" 99.43 351 97.72 98.86 0.00e+00 PDB 3PVB "Crystal Structure Of (73-244)ria:c Holoenzyme Of Camp-dependent Protein Kinase" 97.73 345 97.39 98.26 0.00e+00 PDB 3QAL "Crystal Structure Of Arg280ala Mutant Of Catalytic Subunit Of Camp- Dependent Protein Kinase" 99.15 350 97.71 98.57 0.00e+00 PDB 3QAM "Crystal Structure Of Glu208ala Mutant Of Catalytic Subunit Of Camp- Dependent Protein Kinase" 99.15 350 97.71 98.57 0.00e+00 PDB 3TNP "Structure And Allostery Of The Pka Riib Tetrameric Holoenzyme" 99.15 350 97.43 98.29 0.00e+00 PDB 3TNQ "Structure And Allostery Of The Pka Riib Tetrameric Holoenzyme" 99.15 350 97.43 98.29 0.00e+00 PDB 3VQH "Bromine Sad Partially Resolves Multiple Binding Modes For Pka Inhibitor H-89" 99.43 351 97.44 98.58 0.00e+00 PDB 3ZO4 "The Synthesis And Evaluation Of Diazaspirocyclic Protein Kinase Inhibitors" 99.43 351 97.15 98.58 0.00e+00 PDB 4DFX "Crystal Structure Of Myristoylated K7c Catalytic Subunit Of Camp- Dependent Protein Kinase In Complex With Sp20 And Amp-Pnp" 99.15 350 97.43 98.29 0.00e+00 PDB 4DFY "Crystal Structure Of R194a Mutant Of Camp-Dependent Protein Kinase With Unphosphorylated Activation Loop" 99.72 371 98.01 98.86 0.00e+00 PDB 4DFZ "Crystal Structure Of Myristoylated K7c Catalytic Subunit Of Camp- Dependent Protein Kinase In Complex With Sp20" 99.15 350 97.43 98.29 0.00e+00 PDB 4DG0 "Crystal Structure Of Myristoylated Wt Catalytic Subunit Of Camp- Dependent Protein Kinase In Complex With Sp20 And Amp-Pnp" 99.15 350 97.71 98.57 0.00e+00 PDB 4DG2 "Crystal Structure Of Myristoylated Wt Catalytic Subunit Of Camp- Dependent Protein Kinase In Complex With Sp20" 99.15 350 97.71 98.57 0.00e+00 PDB 4DG3 "Crystal Structure Of R336a Mutant Of Camp-dependent Protein Kinase With Unphosphorylated Turn Motif" 99.72 371 97.73 98.58 0.00e+00 PDB 4DH1 "Low Temperature X-ray Structure Of Camp Dependent Protein Kinase A Catalytic Subunit With Low Mg2+, Atp And Ip20" 99.15 350 97.71 98.57 0.00e+00 PDB 4DH3 "Low Temperature X-ray Structure Of Camp Dependent Protein Kinase A Catalytic Subunit With High Mg2+, Atp And Ip20" 99.15 350 97.71 98.57 0.00e+00 PDB 4DH5 "Room Temperature X-ray Structure Of Camp Dependent Protein Kinase A Catalytic Subunit With High Mg2+, Adp, Phosphate, And Ip20" 99.15 350 97.71 98.57 0.00e+00 PDB 4DH7 "Low Temperature X-ray Structure Of Camp Dependent Protein Kinase A Catalytic Subunit With High Mg2+, Amp-pnp And Ip20'" 99.15 350 97.71 98.57 0.00e+00 PDB 4DH8 "Room Temperature X-ray Structure Of Camp Dependent Protein Kinase A Catalytic Subunit With High Mg2+, Amp-pnp And Ip20" 99.15 350 97.71 98.57 0.00e+00 PDB 4DIN "Novel Localization And Quaternary Structure Of The Pka Ri Beta Holoenzyme" 99.15 350 98.00 98.86 0.00e+00 PDB 4HPT "Crystal Structure Of The Catalytic Subunit Of Camp-dependent Protein Kinase Displaying Complete Phosphoryl Transfer Of Amp-pnp " 99.15 350 98.00 98.86 0.00e+00 PDB 4HPU "Crystal Structure Of The Catalytic Subunit Of Camp-dependent Protein Kinase Displaying Partial Phosphoryl Transfer Of Amp-pnp O" 99.15 350 97.71 98.57 0.00e+00 PDB 4IAC "X-ray Structure Of Camp Dependent Protein Kinase A In Compelx With High Mg2+ Concentration, Amp-pcp And Pseudo-substrate Peptid" 99.72 356 97.44 98.30 0.00e+00 PDB 4IAD "Low Temperature X-ray Structure Of Camp Dependent Protein Kinase A In Compelx With High Mg2+ Concentration, Adp And Phosphoryla" 99.72 356 97.44 98.30 0.00e+00 PDB 4IAF "Room Temperature X-ray Structure Of Camp Dependent Protein Kinase A In Complex With High Mg2+ Concentration, Adp And Phosphoryl" 99.72 356 97.44 98.30 0.00e+00 PDB 4IAI "X-ray Structure Of Camp Dependent Protein Kinase A In Complex With High Ca2+ Concentration, Adp And Phosphorylated Peptide Psp2" 99.72 356 97.44 98.30 0.00e+00 PDB 4IAK "Low Temperature X-ray Structure Of Camp Dependent Protein Kinase A In Complex With High Sr2+ Concentration, Adp And Phosphoryla" 99.72 356 97.44 98.30 0.00e+00 PDB 4IAY "Room Temperature X-ray Structure Of Camp Dependent Protein Kinase A In Complex With High Sr2+ Concentration, Adp And Phosphoryl" 99.72 356 97.44 98.30 0.00e+00 PDB 4IAZ "Structure Of Camp Dependent Protein Kinase A In Complex With High Ba2+ Concentration, Adp And Phosphorylated Peptide Psp20" 99.72 356 97.44 98.30 0.00e+00 PDB 4IB0 "X-ray Structure Of Camp Dependent Protein Kinase A In Complex With High Na+ Concentration, Adp And Phosphorylated Peptide Psp20" 99.72 356 97.44 98.30 0.00e+00 PDB 4IB1 "Structure Of Camp Dependent Protein Kinase A In Complex With High K+ Concentration, Adp And Phosphorylated Peptide Psp20" 99.72 356 97.44 98.30 0.00e+00 PDB 4IB3 "Structure Of Camp Dependent Protein Kinase A In Complex With Adp, Phosphorylated Peptide Psp20, And No Metal" 99.72 356 97.44 98.30 0.00e+00 PDB 4IE9 "Bovine Pka C-alpha In Complex With 3-pyridylmethyl-5-methyl-1h- Pyrazole-3-carboxylate" 99.43 351 97.15 98.58 0.00e+00 PDB 4IJ9 "Bovine Pka C-alpha In Complex With 2-[[5-(4-pyridyl)-1h-1,2,4-triazol- 3-yl]sulfanyl]-1-(2-thiophenyl)ethanone" 99.15 350 97.14 98.57 0.00e+00 PDB 4NTS "Apo Structure Of The Catalytic Subunit Of Camp-dependent Protein Kinase" 99.15 350 97.71 98.57 0.00e+00 PDB 4NTT "Structure Of The Catalytic Subunit Of Camp-dependent Protein Kinase Bound To Adp And One Magnesium Ion" 99.15 350 97.71 98.57 0.00e+00 PDB 4O21 "Product Complex Of Metal-free Pkac, Atp-gamma-s And Sp20." 95.18 342 97.62 98.51 0.00e+00 PDB 4O22 "Binary Complex Of Metal-free Pkac With Sp20" 95.18 342 97.62 98.51 0.00e+00 PDB 4WIH "Crystal Structure Of Camp-dependent Protein Kinase A From Cricetulus Griseus" 100.00 353 99.15 99.15 0.00e+00 DBJ BAF82836 "unnamed protein product [Homo sapiens]" 99.43 351 98.29 99.43 0.00e+00 DBJ BAH13444 "unnamed protein product [Homo sapiens]" 56.37 230 100.00 100.00 3.17e-142 DBJ BAI46794 "protein kinase, cAMP-dependent, catalytic, alpha [synthetic construct]" 99.43 351 98.29 99.43 0.00e+00 EMBL CAA30597 "unnamed protein product [Homo sapiens]" 99.43 351 98.29 99.43 0.00e+00 EMBL CAA41052 "cAMP-dependent protein kinase subunit C alpha [Rattus rattus]" 99.43 351 99.15 99.72 0.00e+00 EMBL CAA47627 "protein kinase [Bos taurus]" 99.43 351 97.72 99.15 0.00e+00 GB AAA37010 "cAMP-dependent protein kinase alpha-catalytic subunit [Cricetulus sp.]" 99.43 351 100.00 100.00 0.00e+00 GB AAA39936 "cAMP-dependent protein kinase catalytic subunit [Mus musculus domesticus]" 99.43 351 98.29 99.15 0.00e+00 GB AAA39937 "cAMP-dependent protein kinase alpha subunit, partial [Mus musculus]" 99.43 351 98.58 99.43 0.00e+00 GB AAA60094 "protein kinase A-alpha, partial [Homo sapiens]" 55.81 207 97.46 98.98 2.63e-136 GB AAF76423 "cAMP-dependent protein kinase catalytic subunit Calpha1 [Ovis aries]" 99.43 351 97.72 99.15 0.00e+00 REF NP_001003032 "cAMP-dependent protein kinase catalytic subunit alpha [Canis lupus familiaris]" 99.43 350 97.44 98.86 0.00e+00 REF NP_001009234 "cAMP-dependent protein kinase catalytic subunit alpha [Ovis aries]" 99.43 351 97.72 99.15 0.00e+00 REF NP_001094392 "cAMP-dependent protein kinase catalytic subunit alpha [Rattus norvegicus]" 99.43 351 99.15 100.00 0.00e+00 REF NP_001264827 "cAMP-dependent protein kinase catalytic subunit alpha isoform 2 [Mus musculus]" 96.88 343 97.08 97.95 0.00e+00 REF NP_001291278 "cAMP-dependent protein kinase catalytic subunit alpha isoform 3 [Homo sapiens]" 95.18 427 98.21 99.40 0.00e+00 SP P00517 "RecName: Full=cAMP-dependent protein kinase catalytic subunit alpha; Short=PKA C-alpha [Bos taurus]" 99.43 351 97.72 99.15 0.00e+00 SP P05132 "RecName: Full=cAMP-dependent protein kinase catalytic subunit alpha; Short=PKA C-alpha [Mus musculus]" 99.43 351 98.58 99.43 0.00e+00 SP P17612 "RecName: Full=cAMP-dependent protein kinase catalytic subunit alpha; Short=PKA C-alpha [Homo sapiens]" 99.43 351 98.29 99.43 0.00e+00 SP P25321 "RecName: Full=cAMP-dependent protein kinase catalytic subunit alpha; Short=PKA C-alpha [Cricetulus griseus]" 99.43 351 100.00 100.00 0.00e+00 SP P27791 "RecName: Full=cAMP-dependent protein kinase catalytic subunit alpha; Short=PKA C-alpha [Rattus norvegicus]" 99.43 351 99.15 99.72 0.00e+00 TPG DAA28080 "TPA: cAMP-dependent protein kinase catalytic subunit alpha [Bos taurus]" 99.43 351 97.72 99.15 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $cAPK_PKA 'Chinese hamster' 10029 Eukaryota Metazoa Cricetulus griseus 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 $cAPK_PKA 'recombinant technology' . . . . . 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 $cAPK_PKA . mM 0.4 0.6 '[U-100% 13C; U-100% 15N; U-100% 2H]' NaCl 300 mM . . . Hepes 50 mM . . . Dithiotheithrol 5 mM . . . stop_ save_ ############################ # Computer software used # ############################ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.14 loop_ _Task assignment stop_ _Details . _Citation_label $ref-1 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label $sample_1 save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label $sample_1 save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_HN(CO)CACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _Sample_label $sample_1 save_ save_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.1 pH temperature 298 1 K 'ionic strength' 0.3 . M 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 . . . 1.0 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'cAMP dependent protein kinase catalytic domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 -1 3 MET C C 176.459 0.5 1 2 1 4 GLY H H 8.246 0.01 1 3 1 4 GLY N N 109.984 0.2 1 4 1 4 GLY CA C 44.877 0.5 1 5 1 4 GLY C C 173.712 0.5 1 6 2 5 ASN H H 8.166 0.01 1 7 2 5 ASN N N 118.96 0.2 1 8 2 5 ASN CA C 51.91 0.5 1 9 2 5 ASN C C 175.21 0.5 1 10 3 6 ALA H H 8.162 0.01 1 11 3 6 ALA N N 124.514 0.2 1 12 3 6 ALA CA C 52.784 0.5 1 13 3 6 ALA C C 177.643 0.5 1 14 3 6 ALA CB C 18.161 0.5 1 15 4 7 ALA H H 7.872 0.01 1 16 4 7 ALA N N 122.396 0.2 1 17 4 7 ALA CA C 52.079 0.5 1 18 4 7 ALA C C 177.424 0.5 1 19 4 7 ALA CB C 18.086 0.5 1 20 5 8 ALA H H 7.921 0.01 1 21 5 8 ALA N N 122.821 0.2 1 22 5 8 ALA CA C 51.923 0.5 1 23 5 8 ALA C C 177.643 0.5 1 24 5 8 ALA CB C 18.236 0.5 1 25 6 9 ALA H H 8.003 0.01 1 26 6 9 ALA N N 122.359 0.2 1 27 6 9 ALA CA C 52.392 0.5 1 28 6 9 ALA C C 177.599 0.5 1 29 6 9 ALA CB C 18.086 0.5 1 30 7 10 LYS H H 8.016 0.01 1 31 7 10 LYS N N 120.715 0.2 1 32 7 10 LYS CA C 55.603 0.5 1 33 7 10 LYS C C 176.394 0.5 1 34 7 10 LYS CB C 32.009 0.5 1 35 8 11 LYS H H 8.268 0.01 1 36 8 11 LYS N N 123.286 0.2 1 37 8 11 LYS CA C 55.446 0.5 1 38 8 11 LYS C C 176.985 0.5 1 39 8 11 LYS CB C 32.009 0.5 1 40 9 12 GLY H H 8.307 0.01 1 41 9 12 GLY N N 110.411 0.2 1 42 9 12 GLY CA C 44.954 0.5 1 43 9 12 GLY C C 174.312 0.5 1 44 10 13 SER H H 8.726 0.01 1 45 10 13 SER N N 117.423 0.2 1 46 10 13 SER CA C 57.482 0.5 1 47 10 13 SER C C 174.859 0.5 1 48 10 13 SER CB C 65.17 0.5 1 49 11 14 GLU H H 8.519 0.01 1 50 11 14 GLU N N 122.833 0.2 1 51 11 14 GLU CA C 56.934 0.5 1 52 11 14 GLU C C 176.744 0.5 1 53 11 14 GLU CB C 29.015 0.5 1 54 12 15 GLN H H 8.218 0.01 1 55 12 15 GLN N N 120.494 0.2 1 56 12 15 GLN CA C 56.307 0.5 1 57 12 15 GLN C C 176.459 0.5 1 58 12 15 GLN CB C 28.79 0.5 1 59 13 16 GLU H H 8.254 0.01 1 60 13 16 GLU N N 122.132 0.2 1 61 13 16 GLU CA C 56.542 0.5 1 62 13 16 GLU C C 176.76 0.5 1 63 13 16 GLU CB C 29.239 0.5 1 64 14 17 SER H H 8.16 0.01 1 65 14 17 SER N N 116.791 0.2 1 66 14 17 SER CA C 58.108 0.5 1 67 14 17 SER C C 175.521 0.5 1 68 14 17 SER CB C 63.149 0.5 1 69 15 18 VAL H H 8.036 0.01 1 70 15 18 VAL N N 123.033 0.2 1 71 15 18 VAL CA C 64.842 0.5 1 72 15 18 VAL C C 177.065 0.5 1 73 15 18 VAL CB C 30.662 0.5 1 74 16 19 LYS H H 7.857 0.01 1 75 16 19 LYS N N 120.209 0.2 1 76 16 19 LYS CA C 58.656 0.5 1 77 16 19 LYS C C 178.441 0.5 1 78 16 19 LYS CB C 31.26 0.5 1 79 17 20 GLU H H 7.88 0.01 1 80 17 20 GLU N N 119.8 0.2 1 81 17 20 GLU CA C 58.634 0.5 1 82 17 20 GLU C C 176.882 0.5 1 83 17 20 GLU CB C 28.715 0.5 1 84 18 21 PHE H H 7.045 0.01 1 85 18 21 PHE N N 119.872 0.2 1 86 18 21 PHE CA C 60.047 0.5 1 87 18 21 PHE C C 178.334 0.5 1 88 18 21 PHE CB C 37.698 0.5 1 89 19 22 LEU H H 8.54 0.01 1 90 19 22 LEU N N 119.699 0.2 1 91 19 22 LEU CA C 56.691 0.5 1 92 19 22 LEU C C 179.442 0.5 1 93 19 22 LEU CB C 39.944 0.5 1 94 20 23 ALA H H 7.859 0.01 1 95 20 23 ALA N N 123.304 0.2 1 96 20 23 ALA CA C 54.863 0.5 1 97 20 23 ALA C C 180.704 0.5 1 98 20 23 ALA CB C 16.963 0.5 1 99 21 24 LYS H H 7.681 0.01 1 100 21 24 LYS N N 119.187 0.2 1 101 21 24 LYS CA C 57.862 0.5 1 102 21 24 LYS C C 178.557 0.5 1 103 21 24 LYS CB C 31.036 0.5 1 104 22 25 ALA H H 8.112 0.01 1 105 22 25 ALA N N 121.868 0.2 1 106 22 25 ALA CA C 54.141 0.5 1 107 22 25 ALA C C 181.252 0.5 1 108 22 25 ALA CB C 17.337 0.5 1 109 23 26 LYS H H 8.072 0.01 1 110 23 26 LYS N N 120.762 0.2 1 111 23 26 LYS CA C 58.891 0.5 1 112 23 26 LYS C C 177.456 0.5 1 113 23 26 LYS CB C 30.662 0.5 1 114 24 27 GLU H H 7.505 0.01 1 115 24 27 GLU N N 118.616 0.2 1 116 24 27 GLU CA C 59.111 0.5 1 117 24 27 GLU C C 179.523 0.5 1 118 24 27 GLU CB C 28.491 0.5 1 119 25 28 GLU H H 7.877 0.01 1 120 25 28 GLU N N 118.149 0.2 1 121 25 28 GLU CA C 58.875 0.5 1 122 25 28 GLU C C 177.27 0.5 1 123 25 28 GLU CB C 28.79 0.5 1 124 26 29 PHE H H 7.574 0.01 1 125 26 29 PHE N N 120.066 0.2 1 126 26 29 PHE CA C 60.005 0.5 1 127 26 29 PHE CB C 37.623 0.5 1 128 37 40 THR CA C 61.581 0.5 1 129 37 40 THR C C 173.825 0.5 1 130 37 40 THR CB C 69.468 0.5 1 131 38 41 ALA H H 7.55 0.01 1 132 38 41 ALA N N 119.638 0.2 1 133 38 41 ALA CA C 50.591 0.5 1 134 38 41 ALA C C 172.25 0.5 1 135 38 41 ALA CB C 19.957 0.5 1 136 39 42 GLN H H 5.995 0.01 1 137 39 42 GLN N N 112.377 0.2 1 138 39 42 GLN CA C 52.392 0.5 1 139 39 42 GLN C C 175.002 0.5 1 140 39 42 GLN CB C 30.287 0.5 1 141 40 43 LEU H H 8.486 0.01 1 142 40 43 LEU N N 123.392 0.2 1 143 40 43 LEU CA C 57.873 0.5 1 144 40 43 LEU C C 178.101 0.5 1 145 40 43 LEU CB C 40.842 0.5 1 146 41 44 ASP H H 7.939 0.01 1 147 41 44 ASP N N 112.724 0.2 1 148 41 44 ASP CA C 54.428 0.5 1 149 41 44 ASP C C 176.389 0.5 1 150 41 44 ASP CB C 38.896 0.5 1 151 42 45 HIS H H 7.281 0.01 1 152 42 45 HIS N N 116.466 0.2 1 153 42 45 HIS CA C 54.35 0.5 1 154 42 45 HIS C C 174.439 0.5 1 155 42 45 HIS CB C 30.362 0.5 1 156 43 46 PHE H H 7.717 0.01 1 157 43 46 PHE N N 115.311 0.2 1 158 43 46 PHE CA C 55.838 0.5 1 159 43 46 PHE C C 174.937 0.5 1 160 43 46 PHE CB C 41.066 0.5 1 161 44 47 ASP H H 9.289 0.01 1 162 44 47 ASP N N 123.149 0.2 1 163 44 47 ASP CA C 52.894 0.5 1 164 44 47 ASP C C 176.152 0.5 1 165 44 47 ASP CB C 41.965 0.5 1 166 45 48 ARG H H 8.991 0.01 1 167 45 48 ARG N N 123.764 0.2 1 168 45 48 ARG CA C 56.855 0.5 1 169 45 48 ARG C C 175.247 0.5 1 170 45 48 ARG CB C 28.865 0.5 1 171 46 49 ILE H H 8.626 0.01 1 172 46 49 ILE N N 123.863 0.2 1 173 46 49 ILE CA C 62.023 0.5 1 174 46 49 ILE C C 177.379 0.5 1 175 46 49 ILE CB C 37.024 0.5 1 176 47 50 LYS H H 8.029 0.01 1 177 47 50 LYS N N 117.338 0.2 1 178 47 50 LYS CA C 57.35 0.5 1 179 47 50 LYS CB C 35.377 0.5 1 180 49 52 LEU C C 176.542 0.5 1 181 50 53 GLY H H 7.375 0.01 1 182 50 53 GLY N N 105.868 0.2 1 183 50 53 GLY CA C 44.797 0.5 1 184 50 53 GLY C C 171.13 0.5 1 185 51 54 THR H H 8.038 0.01 1 186 51 54 THR N N 112.202 0.2 1 187 51 54 THR CA C 60.066 0.5 1 188 51 54 THR C C 173.221 0.5 1 189 51 54 THR CB C 70.709 0.5 1 190 52 55 GLY H H 7.931 0.01 1 191 52 55 GLY N N 110.271 0.2 1 192 52 55 GLY CA C 43.779 0.5 1 193 52 55 GLY C C 177.27 0.5 1 194 53 56 SER H H 8.415 0.01 1 195 53 56 SER N N 115.947 0.2 1 196 53 56 SER CA C 62.27 0.5 1 197 53 56 SER C C 174.641 0.5 1 198 54 57 PHE C C 173.911 0.5 1 199 55 58 GLY H H 6.766 0.01 1 200 55 58 GLY N N 107.254 0.2 1 201 55 58 GLY CA C 45.11 0.5 1 202 55 58 GLY C C 171.957 0.5 1 203 56 59 ARG H H 8.131 0.01 1 204 56 59 ARG N N 118.588 0.2 1 205 56 59 ARG CA C 54.428 0.5 1 206 56 59 ARG C C 173.331 0.5 1 207 56 59 ARG CB C 32.832 0.5 1 208 57 60 VAL H H 8.339 0.01 1 209 57 60 VAL N N 119.731 0.2 1 210 57 60 VAL CA C 60.144 0.5 1 211 57 60 VAL C C 175.693 0.5 1 212 57 60 VAL CB C 32.683 0.5 1 213 58 61 MET H H 9.359 0.01 1 214 58 61 MET N N 124.91 0.2 1 215 58 61 MET CA C 53.723 0.5 1 216 58 61 MET C C 174.448 0.5 1 217 58 61 MET CB C 35.377 0.5 1 218 59 62 LEU H H 9.26 0.01 1 219 59 62 LEU N N 125.413 0.2 1 220 59 62 LEU CA C 53.88 0.5 1 221 59 62 LEU C C 175.5 0.5 1 222 59 62 LEU CB C 41.59 0.5 1 223 60 63 VAL H H 9.057 0.01 1 224 60 63 VAL N N 119.932 0.2 1 225 60 63 VAL CA C 57.717 0.5 1 226 60 63 VAL C C 173.374 0.5 1 227 60 63 VAL CB C 35.228 0.5 1 228 61 64 LYS H H 8.931 0.01 1 229 61 64 LYS N N 120.178 0.2 1 230 61 64 LYS CA C 53.489 0.5 1 231 61 64 LYS C C 176.273 0.5 1 232 61 64 LYS CB C 35.303 0.5 1 233 62 65 HIS H H 9.351 0.01 1 234 62 65 HIS N N 129.321 0.2 1 235 62 65 HIS CA C 57.404 0.5 1 236 62 65 HIS C C 176.874 0.5 1 237 62 65 HIS CB C 31.934 0.5 1 238 63 66 LYS H H 8.069 0.01 1 239 63 66 LYS N N 128.809 0.2 1 240 63 66 LYS CA C 59.518 0.5 1 241 63 66 LYS C C 178.205 0.5 1 242 63 66 LYS CB C 31.71 0.5 1 243 64 67 GLU H H 8.364 0.01 1 244 64 67 GLU N N 117.158 0.2 1 245 64 67 GLU CA C 57.482 0.5 1 246 64 67 GLU C C 178.012 0.5 1 247 64 67 GLU CB C 29.913 0.5 1 248 65 68 THR H H 7.858 0.01 1 249 65 68 THR N N 106.619 0.2 1 250 65 68 THR CA C 61.553 0.5 1 251 65 68 THR C C 176.531 0.5 1 252 65 68 THR CB C 70.709 0.5 1 253 66 69 GLY H H 8.106 0.01 1 254 66 69 GLY N N 109.931 0.2 1 255 66 69 GLY CA C 44.876 0.5 1 256 66 69 GLY C C 173.331 0.5 1 257 67 70 ASN H H 7.608 0.01 1 258 67 70 ASN N N 117.678 0.2 1 259 67 70 ASN CA C 52.94 0.5 1 260 67 70 ASN C C 174.276 0.5 1 261 67 70 ASN CB C 38.596 0.5 1 262 68 71 HIS H H 8.361 0.01 1 263 68 71 HIS N N 119.153 0.2 1 264 68 71 HIS CA C 56.151 0.5 1 265 68 71 HIS C C 174.147 0.5 1 266 68 71 HIS CB C 30.287 0.5 1 267 69 72 TYR H H 8.823 0.01 1 268 69 72 TYR N N 115.907 0.2 1 269 69 72 TYR CA C 56.934 0.5 1 270 69 72 TYR C C 173.098 0.5 1 271 69 72 TYR CB C 43.387 0.5 1 272 70 73 ALA H H 8.828 0.01 1 273 70 73 ALA N N 123.467 0.2 1 274 70 73 ALA CA C 49.965 0.5 1 275 70 73 ALA C C 175.055 0.5 1 276 70 73 ALA CB C 18.909 0.5 1 277 71 74 MET H H 9.643 0.01 1 278 71 74 MET N N 124.902 0.2 1 279 71 74 MET CA C 53.175 0.5 1 280 71 74 MET C C 173.672 0.5 1 281 71 74 MET CB C 36.875 0.5 1 282 72 75 LYS H H 9.255 0.01 1 283 72 75 LYS N N 130.209 0.2 1 284 72 75 LYS CA C 55.524 0.5 1 285 72 75 LYS C C 174.183 0.5 1 286 72 75 LYS CB C 32.608 0.5 1 287 73 76 ILE H H 8.672 0.01 1 288 73 76 ILE N N 125.914 0.2 1 289 73 76 ILE CA C 60.301 0.5 1 290 73 76 ILE C C 175.459 0.5 1 291 73 76 ILE CB C 38.671 0.5 1 292 74 77 LEU H H 8.833 0.01 1 293 74 77 LEU N N 126.85 0.2 1 294 74 77 LEU CA C 52.94 0.5 1 295 74 77 LEU C C 174.587 0.5 1 296 74 77 LEU CB C 41.516 0.5 1 297 75 78 ASP H H 8.287 0.01 1 298 75 78 ASP N N 124.241 0.2 1 299 75 78 ASP CA C 52.627 0.5 1 300 75 78 ASP C C 176.714 0.5 1 301 75 78 ASP CB C 41.74 0.5 1 302 76 79 LYS H H 8.022 0.01 1 303 76 79 LYS N N 125.739 0.2 1 304 76 79 LYS CA C 60.536 0.5 1 305 76 79 LYS C C 177.544 0.5 1 306 76 79 LYS CB C 33.656 0.5 1 307 77 80 GLN H H 7.971 0.01 1 308 77 80 GLN N N 113.603 0.2 1 309 77 80 GLN CA C 59.048 0.5 1 310 77 80 GLN CB C 28.341 0.5 1 311 79 82 VAL C C 178.097 0.5 1 312 80 83 VAL H H 7.797 0.01 1 313 80 83 VAL N N 117.444 0.2 1 314 80 83 VAL CA C 66.173 0.5 1 315 80 83 VAL C C 180.351 0.5 1 316 80 83 VAL CB C 30.811 0.5 1 317 81 84 LYS H H 8.149 0.01 1 318 81 84 LYS N N 122.877 0.2 1 319 81 84 LYS CA C 58.891 0.5 1 320 81 84 LYS C C 178.309 0.5 1 321 81 84 LYS CB C 31.635 0.5 1 322 82 85 LEU H H 7.87 0.01 1 323 82 85 LEU N N 116.249 0.2 1 324 82 85 LEU CA C 53.958 0.5 1 325 82 85 LEU C C 175.863 0.5 1 326 82 85 LEU CB C 39.644 0.5 1 327 83 86 LYS H H 7.919 0.01 1 328 83 86 LYS N N 116.522 0.2 1 329 83 86 LYS CA C 56.855 0.5 1 330 83 86 LYS C C 177.27 0.5 1 331 83 86 LYS CB C 27.293 0.5 1 332 84 87 GLN H H 8.017 0.01 1 333 84 87 GLN N N 114.472 0.2 1 334 84 87 GLN CA C 53.417 0.5 1 335 84 87 GLN C C 177.27 0.5 1 336 84 87 GLN CB C 27.518 0.5 1 337 85 88 ILE H H 8.061 0.01 1 338 85 88 ILE N N 123.661 0.2 1 339 85 88 ILE CA C 66.292 0.5 1 340 85 88 ILE CB C 37.623 0.5 1 341 95 98 LEU C C 179.134 0.5 1 342 96 99 GLN H H 8.003 0.01 1 343 96 99 GLN N N 112.514 0.2 1 344 96 99 GLN CA C 56.307 0.5 1 345 96 99 GLN C C 175.31 0.5 1 346 96 99 GLN CB C 26.021 0.5 1 347 97 100 ALA H H 7.622 0.01 1 348 97 100 ALA N N 121.981 0.2 1 349 97 100 ALA CA C 52.236 0.5 1 350 97 100 ALA C C 176.82 0.5 1 351 97 100 ALA CB C 20.781 0.5 1 352 98 101 VAL H H 7.326 0.01 1 353 98 101 VAL N N 109.376 0.2 1 354 98 101 VAL CA C 60.222 0.5 1 355 98 101 VAL C C 175.97 0.5 1 356 98 101 VAL CB C 33.806 0.5 1 357 99 102 ASN H H 7.932 0.01 1 358 99 102 ASN N N 116.043 0.2 1 359 99 102 ASN CA C 54.016 0.5 1 360 99 102 ASN C C 172.205 0.5 1 361 99 102 ASN CB C 39.869 0.5 1 362 100 103 PHE H H 8.507 0.01 1 363 100 103 PHE N N 126.143 0.2 1 364 100 103 PHE CA C 56.855 0.5 1 365 100 103 PHE CB C 42.938 0.5 1 366 102 105 PHE C C 173.785 0.5 1 367 103 106 LEU H H 7.285 0.01 1 368 103 106 LEU N N 117.185 0.2 1 369 103 106 LEU CA C 52.788 0.5 1 370 103 106 LEU C C 175.828 0.5 1 371 103 106 LEU CB C 43.013 0.5 1 372 104 107 VAL H H 7.641 0.01 1 373 104 107 VAL N N 121.348 0.2 1 374 104 107 VAL CA C 62.27 0.5 1 375 104 107 VAL CB C 31.111 0.5 1 376 107 110 GLU C C 176.161 0.5 1 377 108 111 PHE H H 7.732 0.01 1 378 108 111 PHE N N 110.755 0.2 1 379 108 111 PHE CA C 55.133 0.5 1 380 108 111 PHE C C 173.949 0.5 1 381 108 111 PHE CB C 43.162 0.5 1 382 109 112 SER H H 8.203 0.01 1 383 109 112 SER N N 113.459 0.2 1 384 109 112 SER CA C 58.108 0.5 1 385 109 112 SER C C 171.609 0.5 1 386 109 112 SER CB C 65.544 0.5 1 387 110 113 PHE H H 8.424 0.01 1 388 110 113 PHE N N 114.88 0.2 1 389 110 113 PHE CA C 56.386 0.5 1 390 110 113 PHE C C 172.077 0.5 1 391 110 113 PHE CB C 38.372 0.5 1 392 111 114 LYS H H 8.858 0.01 1 393 111 114 LYS N N 115.317 0.2 1 394 111 114 LYS CA C 54.115 0.5 1 395 111 114 LYS C C 174.119 0.5 1 396 111 114 LYS CB C 36.425 0.5 1 397 112 115 ASP H H 8.97 0.01 1 398 112 115 ASP N N 123.075 0.2 1 399 112 115 ASP CA C 52.079 0.5 1 400 112 115 ASP C C 176.523 0.5 1 401 112 115 ASP CB C 42.713 0.5 1 402 113 116 ASN H H 8.281 0.01 1 403 113 116 ASN N N 114.098 0.2 1 404 113 116 ASN CA C 56.112 0.5 1 405 113 116 ASN CB C 37.099 0.5 1 406 122 125 TYR C C 174.295 0.5 1 407 123 126 VAL H H 8.055 0.01 1 408 123 126 VAL N N 131.68 0.2 1 409 123 126 VAL CA C 62.08 0.5 1 410 123 126 VAL C C 174.21 0.5 1 411 123 126 VAL CB C 37.18 0.5 1 412 128 131 MET CA C 60.23 0.5 1 413 128 131 MET C C 177.807 0.5 1 414 129 132 PHE H H 6.751 0.01 1 415 129 132 PHE N N 110.177 0.2 1 416 129 132 PHE CA C 56.708 0.5 1 417 129 132 PHE C C 175.737 0.5 1 418 129 132 PHE CB C 37.923 0.5 1 419 130 133 SER H H 7.296 0.01 1 420 130 133 SER N N 119.363 0.2 1 421 130 133 SER CA C 66.408 0.5 1 422 130 133 SER C C 174.642 0.5 1 423 130 133 SER CB C 68.538 0.5 1 424 131 134 HIS H H 8.6 0.01 1 425 131 134 HIS N N 116.01 0.2 1 426 131 134 HIS CA C 56.386 0.5 1 427 131 134 HIS C C 176.222 0.5 1 428 131 134 HIS CB C 29.239 0.5 1 429 132 135 LEU H H 7.599 0.01 1 430 132 135 LEU N N 125.09 0.2 1 431 132 135 LEU CA C 61.553 0.5 1 432 132 135 LEU CB C 39.569 0.5 1 433 149 152 GLN CA C 59.03 0.5 1 434 149 152 GLN C C 179.24 0.5 1 435 150 153 ILE H H 7.411 0.01 1 436 150 153 ILE N N 121.429 0.2 1 437 150 153 ILE CA C 62.571 0.5 1 438 150 153 ILE C C 176.786 0.5 1 439 150 153 ILE CB C 34.061 0.5 1 440 151 154 VAL H H 8.661 0.01 1 441 151 154 VAL N N 120.96 0.2 1 442 151 154 VAL CA C 67.462 0.5 1 443 151 154 VAL C C 177.838 0.5 1 444 151 154 VAL CB C 30.259 0.5 1 445 187 190 PHE C C 174.78 0.5 1 446 188 191 ALA H H 7.107 0.01 1 447 188 191 ALA N N 126.455 0.2 1 448 188 191 ALA CA C 52.236 0.5 1 449 188 191 ALA C C 176.901 0.5 1 450 188 191 ALA CB C 18.984 0.5 1 451 189 192 LYS H H 8.169 0.01 1 452 189 192 LYS N N 119.553 0.2 1 453 189 192 LYS CA C 55.055 0.5 1 454 189 192 LYS C C 174.038 0.5 1 455 189 192 LYS CB C 36.351 0.5 1 456 190 193 ARG H H 8.77 0.01 1 457 190 193 ARG N N 127.54 0.2 1 458 190 193 ARG CA C 55.055 0.5 1 459 190 193 ARG C C 175.035 0.5 1 460 190 193 ARG CB C 28.266 0.5 1 461 191 194 VAL H H 8.677 0.01 1 462 191 194 VAL N N 127.499 0.2 1 463 191 194 VAL CA C 60.222 0.5 1 464 191 194 VAL C C 173.105 0.5 1 465 191 194 VAL CB C 33.656 0.5 1 466 192 195 LYS H H 8.356 0.01 1 467 192 195 LYS N N 126.487 0.2 1 468 192 195 LYS CA C 55.524 0.5 1 469 192 195 LYS C C 176.371 0.5 1 470 192 195 LYS CB C 31.485 0.5 1 471 193 196 GLY H H 7.841 0.01 1 472 193 196 GLY N N 110.903 0.2 1 473 193 196 GLY CA C 44.954 0.5 1 474 193 196 GLY C C 172.214 0.5 1 475 194 197 ARG H H 7.823 0.01 1 476 194 197 ARG N N 122.818 0.2 1 477 194 197 ARG CA C 54.193 0.5 1 478 194 197 ARG C C 174.505 0.5 1 479 194 197 ARG CB C 32.009 0.5 1 480 195 198 THR H H 7.998 0.01 1 481 195 198 THR N N 116.071 0.2 1 482 195 198 THR CA C 60.849 0.5 1 483 195 198 THR CB C 70.11 0.5 1 484 199 202 CYS CA C 55.28 0.5 1 485 199 202 CYS C C 171.164 0.5 1 486 200 203 GLY H H 6.99 0.01 1 487 200 203 GLY N N 105.077 0.2 1 488 200 203 GLY CA C 43.31 0.5 1 489 200 203 GLY C C 173.515 0.5 1 490 201 204 THR H H 8.873 0.01 1 491 201 204 THR N N 119.473 0.2 1 492 201 204 THR CA C 60.614 0.5 1 493 201 204 THR CB C 69.661 0.5 1 494 203 206 GLU C C 177.609 0.5 1 495 204 207 TYR H H 7.98 0.01 1 496 204 207 TYR N N 117.108 0.2 1 497 204 207 TYR CA C 58.393 0.5 1 498 204 207 TYR C C 175.479 0.5 1 499 204 207 TYR CB C 39.794 0.5 1 500 205 208 LEU H H 7.196 0.01 1 501 205 208 LEU N N 119.302 0.2 1 502 205 208 LEU CA C 55.052 0.5 1 503 205 208 LEU C C 174.797 0.5 1 504 205 208 LEU CB C 41.74 0.5 1 505 206 209 ALA H H 6.361 0.01 1 506 206 209 ALA N N 121.413 0.2 1 507 206 209 ALA CA C 47.949 0.5 1 508 206 209 ALA CB C 16.739 0.5 1 509 212 215 SER CA C 59.12 0.5 1 510 212 215 SER C C 177.566 0.5 1 511 212 215 SER CB C 61.27 0.5 1 512 213 216 LYS H H 7.421 0.01 1 513 213 216 LYS N N 116.122 0.2 1 514 213 216 LYS CA C 55.104 0.5 1 515 213 216 LYS C C 176.955 0.5 1 516 213 216 LYS CB C 32.084 0.5 1 517 214 217 GLY H H 8.496 0.01 1 518 214 217 GLY N N 112.235 0.2 1 519 214 217 GLY CA C 42.918 0.5 1 520 214 217 GLY C C 172.597 0.5 1 521 215 218 TYR H H 8.04 0.01 1 522 215 218 TYR N N 117.444 0.2 1 523 215 218 TYR CA C 55.588 0.5 1 524 215 218 TYR C C 171.796 0.5 1 525 215 218 TYR CB C 39.42 0.5 1 526 216 219 ASN H H 8.585 0.01 1 527 216 219 ASN N N 118.84 0.2 1 528 216 219 ASN CA C 50.648 0.5 1 529 216 219 ASN C C 175.538 0.5 1 530 216 219 ASN CB C 39.794 0.5 1 531 217 220 LYS H H 7.664 0.01 1 532 217 220 LYS N N 114.796 0.2 1 533 217 220 LYS CA C 57.94 0.5 1 534 217 220 LYS C C 176.018 0.5 1 535 217 220 LYS CB C 29.464 0.5 1 536 218 221 ALA H H 8.071 0.01 1 537 218 221 ALA N N 120.725 0.2 1 538 218 221 ALA CA C 54.302 0.5 1 539 218 221 ALA C C 181.176 0.5 1 540 218 221 ALA CB C 17.637 0.5 1 541 219 222 VAL H H 8.103 0.01 1 542 219 222 VAL N N 114.162 0.2 1 543 219 222 VAL CA C 64.216 0.5 1 544 219 222 VAL C C 177.156 0.5 1 545 219 222 VAL CB C 29.689 0.5 1 546 220 223 ASP H H 9.638 0.01 1 547 220 223 ASP N N 111.818 0.2 1 548 220 223 ASP CA C 57.862 0.5 1 549 220 223 ASP CB C 42.189 0.5 1 550 222 225 TRP C C 176.883 0.5 1 551 223 226 ALA H H 9.213 0.01 1 552 223 226 ALA N N 120.331 0.2 1 553 223 226 ALA CA C 54.943 0.5 1 554 223 226 ALA C C 176.241 0.5 1 555 223 226 ALA CB C 17.712 0.5 1 556 224 227 LEU H H 8.303 0.01 1 557 224 227 LEU N N 117.742 0.2 1 558 224 227 LEU CA C 57.511 0.5 1 559 224 227 LEU C C 177.982 0.5 1 560 224 227 LEU CB C 39.794 0.5 1 561 225 228 GLY H H 7.885 0.01 1 562 225 228 GLY N N 107.431 0.2 1 563 225 228 GLY CA C 47.642 0.5 1 564 225 228 GLY C C 173.968 0.5 1 565 226 229 VAL H H 7.738 0.01 1 566 226 229 VAL N N 122.41 0.2 1 567 226 229 VAL CA C 66.898 0.5 1 568 226 229 VAL C C 177.064 0.5 1 569 226 229 VAL CB C 29.988 0.5 1 570 227 230 LEU H H 8.608 0.01 1 571 227 230 LEU N N 119.284 0.2 1 572 227 230 LEU CA C 57.029 0.5 1 573 227 230 LEU CB C 41.291 0.5 1 574 237 240 PRO C C 178.445 0.5 1 575 238 241 PHE H H 7.902 0.01 1 576 238 241 PHE N N 119.583 0.2 1 577 238 241 PHE CA C 59.987 0.5 1 578 238 241 PHE C C 177.131 0.5 1 579 238 241 PHE CB C 39.045 0.5 1 580 239 242 PHE H H 8.531 0.01 1 581 239 242 PHE N N 119.058 0.2 1 582 239 242 PHE CA C 57.09 0.5 1 583 239 242 PHE C C 172.655 0.5 1 584 239 242 PHE CB C 40.168 0.5 1 585 240 243 ALA H H 6.882 0.01 1 586 240 243 ALA N N 123.17 0.2 1 587 240 243 ALA CA C 50.826 0.5 1 588 240 243 ALA C C 175.007 0.5 1 589 240 243 ALA CB C 21.08 0.5 1 590 241 244 ASP H H 8.125 0.01 1 591 241 244 ASP N N 116.168 0.2 1 592 241 244 ASP CA C 55.888 0.5 1 593 241 244 ASP C C 175.791 0.5 1 594 241 244 ASP CB C 40.692 0.5 1 595 242 245 GLN H H 7.068 0.01 1 596 242 245 GLN N N 114.186 0.2 1 597 242 245 GLN CA C 51.844 0.5 1 598 242 245 GLN CB C 29.838 0.5 1 599 243 246 PRO CA C 65.362 0.5 1 600 243 246 PRO C C 176.728 0.5 1 601 243 246 PRO CB C 30.972 0.5 1 602 244 247 ILE H H 7.86 0.01 1 603 244 247 ILE N N 112.804 0.2 1 604 244 247 ILE CA C 63.119 0.5 1 605 244 247 ILE C C 177.478 0.5 1 606 244 247 ILE CB C 36.425 0.5 1 607 245 248 GLN H H 6.797 0.01 1 608 245 248 GLN N N 117.877 0.2 1 609 245 248 GLN CA C 57.09 0.5 1 610 245 248 GLN C C 179.033 0.5 1 611 245 248 GLN CB C 28.566 0.5 1 612 246 249 ILE H H 7.201 0.01 1 613 246 249 ILE N N 121.57 0.2 1 614 246 249 ILE CA C 65.625 0.5 1 615 246 249 ILE CB C 36.351 0.5 1 616 247 250 TYR CA C 58.07 0.5 1 617 247 250 TYR C C 177.722 0.5 1 618 247 250 TYR CB C 35.72 0.5 1 619 248 251 GLU H H 7.323 0.01 1 620 248 251 GLU N N 116.221 0.2 1 621 248 251 GLU CA C 58.486 0.5 1 622 248 251 GLU C C 179.072 0.5 1 623 248 251 GLU CB C 28.715 0.5 1 624 249 252 LYS H H 7.26 0.01 1 625 249 252 LYS N N 118.647 0.2 1 626 249 252 LYS CA C 58.33 0.5 1 627 249 252 LYS C C 179.132 0.5 1 628 249 252 LYS CB C 32.234 0.5 1 629 250 253 ILE H H 7.936 0.01 1 630 250 253 ILE N N 122.132 0.2 1 631 250 253 ILE CA C 65.087 0.5 1 632 250 253 ILE C C 177.431 0.5 1 633 250 253 ILE CB C 37.324 0.5 1 634 251 254 VAL H H 7.391 0.01 1 635 251 254 VAL N N 110.378 0.2 1 636 251 254 VAL CA C 63.902 0.5 1 637 251 254 VAL C C 177.406 0.5 1 638 251 254 VAL CB C 30.287 0.5 1 639 252 255 SER H H 7.219 0.01 1 640 252 255 SER N N 113.194 0.2 1 641 252 255 SER CA C 59.674 0.5 1 642 252 255 SER C C 176.277 0.5 1 643 252 255 SER CB C 63.373 0.5 1 644 253 256 GLY H H 7.597 0.01 1 645 253 256 GLY N N 109.185 0.2 1 646 253 256 GLY CA C 45.972 0.5 1 647 253 256 GLY C C 173.448 0.5 1 648 254 257 LYS H H 7.772 0.01 1 649 254 257 LYS N N 120.719 0.2 1 650 254 257 LYS CA C 55.211 0.5 1 651 254 257 LYS C C 175.016 0.5 1 652 254 257 LYS CB C 31.41 0.5 1 653 255 258 VAL H H 7.88 0.01 1 654 255 258 VAL N N 123.158 0.2 1 655 255 258 VAL CA C 60.144 0.5 1 656 255 258 VAL C C 173.348 0.5 1 657 255 258 VAL CB C 33.132 0.5 1 658 256 259 ARG H H 7.952 0.01 1 659 256 259 ARG N N 125.818 0.2 1 660 256 259 ARG CA C 53.332 0.5 1 661 256 259 ARG C C 174.991 0.5 1 662 256 259 ARG CB C 30.362 0.5 1 663 257 260 PHE H H 8.886 0.01 1 664 257 260 PHE N N 124.79 0.2 1 665 257 260 PHE CA C 54.84 0.5 1 666 257 260 PHE CB C 38.372 0.5 1 667 260 263 HIS C C 175.638 0.5 1 668 261 264 PHE H H 6.828 0.01 1 669 261 264 PHE N N 121.306 0.2 1 670 261 264 PHE CA C 55.208 0.5 1 671 261 264 PHE C C 176.633 0.5 1 672 261 264 PHE CB C 36.949 0.5 1 673 262 265 SER H H 9.987 0.01 1 674 262 265 SER N N 120.955 0.2 1 675 262 265 SER CA C 57.912 0.5 1 676 262 265 SER C C 175.165 0.5 1 677 262 265 SER CB C 63.074 0.5 1 678 263 266 SER H H 8.879 0.01 1 679 263 266 SER N N 116.916 0.2 1 680 263 266 SER CA C 61.53 0.5 1 681 263 266 SER CB C 62.999 0.5 1 682 273 276 LEU CA C 52.359 0.5 1 683 273 276 LEU C C 176.388 0.5 1 684 273 276 LEU CB C 37.388 0.5 1 685 274 277 GLN H H 6.636 0.01 1 686 274 277 GLN N N 118.316 0.2 1 687 274 277 GLN CA C 52.784 0.5 1 688 274 277 GLN C C 176.956 0.5 1 689 274 277 GLN CB C 29.389 0.5 1 690 275 278 VAL H H 8.973 0.01 1 691 275 278 VAL N N 127.974 0.2 1 692 275 278 VAL CA C 65.155 0.5 1 693 275 278 VAL C C 175.393 0.5 1 694 275 278 VAL CB C 30.886 0.5 1 695 276 279 ASP H H 8.432 0.01 1 696 276 279 ASP N N 118.626 0.2 1 697 276 279 ASP CA C 52.627 0.5 1 698 276 279 ASP C C 177.27 0.5 1 699 276 279 ASP CB C 39.794 0.5 1 700 277 280 LEU H H 8.31 0.01 1 701 277 280 LEU N N 128.857 0.2 1 702 277 280 LEU CA C 57.873 0.5 1 703 277 280 LEU C C 178.566 0.5 1 704 277 280 LEU CB C 40.468 0.5 1 705 278 281 THR H H 8.432 0.01 1 706 278 281 THR N N 109.643 0.2 1 707 278 281 THR CA C 62.885 0.5 1 708 278 281 THR C C 174.739 0.5 1 709 278 281 THR CB C 68.613 0.5 1 710 279 282 LYS H H 7.62 0.01 1 711 279 282 LYS N N 118.339 0.2 1 712 279 282 LYS CA C 55.055 0.5 1 713 279 282 LYS C C 175.35 0.5 1 714 279 282 LYS CB C 33.806 0.5 1 715 280 283 ARG H H 6.929 0.01 1 716 280 283 ARG N N 122.371 0.2 1 717 280 283 ARG CA C 56.072 0.5 1 718 280 283 ARG C C 175.373 0.5 1 719 280 283 ARG CB C 30.961 0.5 1 720 281 284 PHE H H 8.225 0.01 1 721 281 284 PHE N N 127.764 0.2 1 722 281 284 PHE CA C 57.795 0.5 1 723 281 284 PHE CB C 37.099 0.5 1 724 282 285 GLY CA C 44.755 0.5 1 725 282 285 GLY C C 175.146 0.5 1 726 283 286 ASN H H 8.274 0.01 1 727 283 286 ASN N N 118.25 0.2 1 728 283 286 ASN CA C 51.493 0.5 1 729 283 286 ASN C C 175.162 0.5 1 730 283 286 ASN CB C 42.564 0.5 1 731 284 287 LEU H H 7.778 0.01 1 732 284 287 LEU N N 118.125 0.2 1 733 284 287 LEU CA C 52.701 0.5 1 734 284 287 LEU C C 178.895 0.5 1 735 284 287 LEU CB C 39.869 0.5 1 736 285 288 LYS H H 8.086 0.01 1 737 285 288 LYS N N 122.414 0.2 1 738 285 288 LYS CA C 59.299 0.5 1 739 285 288 LYS C C 177.979 0.5 1 740 285 288 LYS CB C 31.111 0.5 1 741 286 289 ASN H H 8.318 0.01 1 742 286 289 ASN N N 113.181 0.2 1 743 286 289 ASN CA C 52.623 0.5 1 744 286 289 ASN C C 176.031 0.5 1 745 286 289 ASN CB C 37.399 0.5 1 746 287 290 GLY H H 7.775 0.01 1 747 287 290 GLY N N 108.014 0.2 1 748 287 290 GLY CA C 45.632 0.5 1 749 290 293 ASP CA C 57.32 0.5 1 750 290 293 ASP C C 176.403 0.5 1 751 291 294 ILE H H 6.377 0.01 1 752 291 294 ILE N N 114.776 0.2 1 753 291 294 ILE CA C 64.09 0.5 1 754 291 294 ILE C C 176.683 0.5 1 755 291 294 ILE CB C 37.473 0.5 1 756 292 295 LYS H H 7.266 0.01 1 757 292 295 LYS N N 113.828 0.2 1 758 292 295 LYS CA C 58.828 0.5 1 759 292 295 LYS C C 177.591 0.5 1 760 292 295 LYS CB C 31.335 0.5 1 761 293 296 ASN H H 7.493 0.01 1 762 293 296 ASN N N 110.706 0.2 1 763 293 296 ASN CA C 52.78 0.5 1 764 293 296 ASN C C 174.681 0.5 1 765 293 296 ASN CB C 37.848 0.5 1 766 294 297 HIS H H 7.662 0.01 1 767 294 297 HIS N N 122.921 0.2 1 768 294 297 HIS CA C 59.22 0.5 1 769 294 297 HIS C C 177.963 0.5 1 770 294 297 HIS CB C 31.335 0.5 1 771 295 298 LYS H H 8.076 0.01 1 772 295 298 LYS N N 130.255 0.2 1 773 295 298 LYS CA C 59.299 0.5 1 774 295 298 LYS CB C 31.56 0.5 1 775 296 299 TRP CA C 62.961 0.5 1 776 296 299 TRP C C 178.089 0.5 1 777 297 300 PHE H H 8.188 0.01 1 778 297 300 PHE N N 112.466 0.2 1 779 297 300 PHE CA C 57.751 0.5 1 780 297 300 PHE C C 176.716 0.5 1 781 297 300 PHE CB C 39.794 0.5 1 782 298 301 ALA H H 7.692 0.01 1 783 298 301 ALA N N 124.587 0.2 1 784 298 301 ALA CA C 55.607 0.5 1 785 298 301 ALA C C 179.293 0.5 1 786 298 301 ALA CB C 18.236 0.5 1 787 299 302 THR H H 8.102 0.01 1 788 299 302 THR N N 104.415 0.2 1 789 299 302 THR CA C 61.027 0.5 1 790 299 302 THR C C 174.886 0.5 1 791 299 302 THR CB C 68.463 0.5 1 792 300 303 THR H H 7.839 0.01 1 793 300 303 THR N N 123.218 0.2 1 794 300 303 THR CA C 63.776 0.5 1 795 300 303 THR C C 172.623 0.5 1 796 300 303 THR CB C 68.089 0.5 1 797 301 304 ASP H H 8.4 0.01 1 798 301 304 ASP N N 128.643 0.2 1 799 301 304 ASP CA C 51.253 0.5 1 800 301 304 ASP C C 174.983 0.5 1 801 301 304 ASP CB C 39.569 0.5 1 802 302 305 TRP H H 7.291 0.01 1 803 302 305 TRP N N 124.552 0.2 1 804 302 305 TRP CA C 59.63 0.5 1 805 302 305 TRP C C 178.329 0.5 1 806 302 305 TRP CB C 29.763 0.5 1 807 303 306 ILE H H 7.851 0.01 1 808 303 306 ILE N N 118.01 0.2 1 809 303 306 ILE CA C 63.047 0.5 1 810 303 306 ILE C C 177.107 0.5 1 811 303 306 ILE CB C 35.677 0.5 1 812 304 307 ALA H H 7.419 0.01 1 813 304 307 ALA N N 122.739 0.2 1 814 304 307 ALA CA C 54.115 0.5 1 815 304 307 ALA C C 180.199 0.5 1 816 304 307 ALA CB C 17.637 0.5 1 817 305 308 ILE H H 7.908 0.01 1 818 305 308 ILE N N 117.298 0.2 1 819 305 308 ILE CA C 63.207 0.5 1 820 305 308 ILE C C 178.418 0.5 1 821 305 308 ILE CB C 35.153 0.5 1 822 306 309 TYR H H 7.652 0.01 1 823 306 309 TYR N N 120.374 0.2 1 824 306 309 TYR CA C 61.602 0.5 1 825 306 309 TYR CB C 37.698 0.5 1 826 307 310 GLN C C 174.441 0.5 1 827 308 311 ARG H H 8.066 0.01 1 828 308 311 ARG N N 117.444 0.2 1 829 308 311 ARG CA C 55.988 0.5 1 830 308 311 ARG C C 176.679 0.5 1 831 308 311 ARG CB C 25.572 0.5 1 832 309 312 LYS H H 8.419 0.01 1 833 309 312 LYS N N 113.991 0.2 1 834 309 312 LYS CA C 55.442 0.5 1 835 309 312 LYS C C 177.164 0.5 1 836 309 312 LYS CB C 32.758 0.5 1 837 310 313 VAL H H 6.768 0.01 1 838 310 313 VAL N N 119.191 0.2 1 839 310 313 VAL CA C 61.218 0.5 1 840 310 313 VAL C C 176.933 0.5 1 841 310 313 VAL CB C 32.383 0.5 1 842 311 314 GLU H H 8.696 0.01 1 843 311 314 GLU N N 129.878 0.2 1 844 311 314 GLU CA C 56.223 0.5 1 845 311 314 GLU C C 174.487 0.5 1 846 311 314 GLU CB C 28.416 0.5 1 847 312 315 ALA H H 8.454 0.01 1 848 312 315 ALA N N 129.901 0.2 1 849 312 315 ALA CA C 49.354 0.5 1 850 312 315 ALA CB C 18.909 0.5 1 851 321 324 PRO CA C 63.29 0.5 1 852 321 324 PRO C C 177.27 0.5 1 853 321 324 PRO CB C 31.209 0.5 1 854 322 325 GLY H H 8.385 0.01 1 855 322 325 GLY N N 107.924 0.2 1 856 322 325 GLY CA C 44.358 0.5 1 857 322 325 GLY C C 173.449 0.5 1 858 323 326 ASP H H 7.556 0.01 1 859 323 326 ASP N N 119.413 0.2 1 860 323 326 ASP CA C 54.427 0.5 1 861 323 326 ASP C C 176.679 0.5 1 862 323 326 ASP CB C 41.216 0.5 1 863 324 327 THR H H 7.259 0.01 1 864 324 327 THR N N 109.529 0.2 1 865 324 327 THR CA C 59.033 0.5 1 866 324 327 THR C C 174.372 0.5 1 867 324 327 THR CB C 60.978 0.5 1 868 325 328 SER H H 7.422 0.01 1 869 325 328 SER N N 116.549 0.2 1 870 325 328 SER CA C 55.052 0.5 1 871 325 328 SER CB C 60.978 0.5 1 872 327 330 PHE C C 173.088 0.5 1 873 328 331 ASP H H 9.146 0.01 1 874 328 331 ASP N N 121.663 0.2 1 875 328 331 ASP CA C 52.086 0.5 1 876 328 331 ASP C C 172.481 0.5 1 877 328 331 ASP CB C 41.89 0.5 1 878 329 332 ASP H H 8.401 0.01 1 879 329 332 ASP N N 116.232 0.2 1 880 329 332 ASP CA C 51.93 0.5 1 881 329 332 ASP C C 174.86 0.5 1 882 329 332 ASP CB C 41.441 0.5 1 883 330 333 TYR H H 8.459 0.01 1 884 330 333 TYR N N 116.18 0.2 1 885 330 333 TYR CA C 55.524 0.5 1 886 330 333 TYR C C 175.973 0.5 1 887 330 333 TYR CB C 38.521 0.5 1 888 331 334 GLU H H 8.423 0.01 1 889 331 334 GLU N N 119.457 0.2 1 890 331 334 GLU CA C 54.427 0.5 1 891 331 334 GLU C C 173.634 0.5 1 892 331 334 GLU CB C 35.677 0.5 1 893 332 335 GLU H H 8.785 0.01 1 894 332 335 GLU N N 124.103 0.2 1 895 332 335 GLU CA C 54.622 0.5 1 896 332 335 GLU CB C 35.602 0.5 1 897 333 336 GLU C C 176.264 0.5 1 898 334 337 GLU H H 8.455 0.01 1 899 334 337 GLU N N 123.304 0.2 1 900 334 337 GLU CA C 55.746 0.5 1 901 334 337 GLU C C 176.371 0.5 1 902 334 337 GLU CB C 29.614 0.5 1 903 335 338 ILE H H 8.251 0.01 1 904 335 338 ILE N N 124.288 0.2 1 905 335 338 ILE CA C 60.516 0.5 1 906 335 338 ILE C C 174.651 0.5 1 907 335 338 ILE CB C 37.099 0.5 1 908 336 339 ARG H H 8.464 0.01 1 909 336 339 ARG N N 129.055 0.2 1 910 336 339 ARG CA C 55.286 0.5 1 911 336 339 ARG C C 175.153 0.5 1 912 336 339 ARG CB C 29.614 0.5 1 913 337 340 VAL H H 8.41 0.01 1 914 337 340 VAL N N 128.073 0.2 1 915 337 340 VAL CA C 61.218 0.5 1 916 337 340 VAL C C 175.535 0.5 1 917 337 340 VAL CB C 32.308 0.5 1 918 338 341 SER H H 8.384 0.01 1 919 338 341 SER N N 120.095 0.2 1 920 338 341 SER CA C 55.264 0.5 1 921 338 341 SER C C 175.322 0.5 1 922 338 341 SER CB C 64.646 0.5 1 923 339 342 ILE H H 9.276 0.01 1 924 339 342 ILE N N 123.327 0.2 1 925 339 342 ILE CA C 61.921 0.5 1 926 339 342 ILE C C 175.209 0.5 1 927 339 342 ILE CB C 36.949 0.5 1 928 340 343 ASN H H 7.955 0.01 1 929 340 343 ASN N N 119.531 0.2 1 930 340 343 ASN CA C 51.539 0.5 1 931 340 343 ASN C C 173.378 0.5 1 932 340 343 ASN CB C 41.441 0.5 1 933 341 344 GLU H H 8.469 0.01 1 934 341 344 GLU N N 121.429 0.2 1 935 341 344 GLU CA C 57.549 0.5 1 936 341 344 GLU C C 176.078 0.5 1 937 341 344 GLU CB C 29.389 0.5 1 938 342 345 LYS H H 8.938 0.01 1 939 342 345 LYS N N 127.301 0.2 1 940 342 345 LYS CA C 52.164 0.5 1 941 342 345 LYS C C 176.899 0.5 1 942 342 345 LYS CB C 31.335 0.5 1 943 343 346 CYS H H 9.392 0.01 1 944 343 346 CYS N N 118.548 0.2 1 945 343 346 CYS CA C 58.018 0.5 1 946 343 346 CYS C C 175.702 0.5 1 947 343 346 CYS CB C 26.32 0.5 1 948 344 347 GLY H H 8.504 0.01 1 949 344 347 GLY N N 105.846 0.2 1 950 344 347 GLY CA C 46.622 0.5 1 951 344 347 GLY C C 177.486 0.5 1 952 345 348 LYS H H 8.274 0.01 1 953 345 348 LYS N N 120.757 0.2 1 954 345 348 LYS CA C 58.018 0.5 1 955 345 348 LYS C C 179.693 0.5 1 956 345 348 LYS CB C 30.886 0.5 1 957 346 349 GLU H H 9.564 0.01 1 958 346 349 GLU N N 120.372 0.2 1 959 346 349 GLU CA C 60.047 0.5 1 960 346 349 GLU CB C 27.892 0.5 1 961 350 353 PHE C C 179.422 0.5 1 stop_ save_