data_11028 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solid-state NMR assignment of the rigid core of the HET-s(218-289) prion protein in its amyloid conformation. ; _BMRB_accession_number 11028 _BMRB_flat_file_name bmr11028.str _Entry_type original _Submission_date 2008-01-25 _Accession_date 2008-01-27 _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 Siemer Ansgar . . 2 Wasmer Christian . . 3 Lange Adam . . 4 'Van Melckebeke' Helene . . 5 Ernst Matthias . . 6 Ritter Christiane H. . 7 Steinmetz Michel O. . 8 Riek Roland . . 9 Meier Beat H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 217 "15N chemical shifts" 56 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-03-31 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 11064 'A more extended version of 11028' stop_ _Original_release_date 2009-03-31 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Amyloid fibrils of the HET-s(218-289) prion form a beta-solenoid with a triangular hydrophobic core. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18339938 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wasmer Christian . . 2 Lange Adam . . 3 'Van Melckebeke' Helene . . 4 Siemer Ansgar . . 5 Riek Roland . . 6 Meier Beat H. . stop_ _Journal_abbreviation Science _Journal_volume 319 _Journal_issue 5869 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1523 _Page_last 1526 _Year 2008 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_reference_citation _Saveframe_category citation _Citation_full . _Citation_title ; 13C, 15N Resonance assignment of parts of the HET-s prion protein in its amyloid form. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16518695 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Siemer Ansgar . . 2 Ritter Christiane . . 3 Steinmetz Michel O. . 4 Ernst Matthias . . 5 Riek Roland . . 6 Meier Beat H. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full . _Journal_volume 34 _Journal_issue 2 _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 75 _Page_last 87 _Year 2006 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name HET-s(218-289) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label HET-s(218-289) $entity_1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'amyloid fibrils' 'heterokaryon incompatibility' 'prion protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HET-s(218-289) _Molecular_mass 8667.732 _Mol_thiol_state 'not present' loop_ _Biological_function 'heterokaryon incompatibility' 'prion protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 79 _Mol_residue_sequence ; MKIDAIVGRNSAKDIRTEER ARVQLGNVVTAAALHGGIRI SDQTTNSVETVVGKGESRVL IGNEYGGKGFWDNHHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 217 MET 2 218 LYS 3 219 ILE 4 220 ASP 5 221 ALA 6 222 ILE 7 223 VAL 8 224 GLY 9 225 ARG 10 226 ASN 11 227 SER 12 228 ALA 13 229 LYS 14 230 ASP 15 231 ILE 16 232 ARG 17 233 THR 18 234 GLU 19 235 GLU 20 236 ARG 21 237 ALA 22 238 ARG 23 239 VAL 24 240 GLN 25 241 LEU 26 242 GLY 27 243 ASN 28 244 VAL 29 245 VAL 30 246 THR 31 247 ALA 32 248 ALA 33 249 ALA 34 250 LEU 35 251 HIS 36 252 GLY 37 253 GLY 38 254 ILE 39 255 ARG 40 256 ILE 41 257 SER 42 258 ASP 43 259 GLN 44 260 THR 45 261 THR 46 262 ASN 47 263 SER 48 264 VAL 49 265 GLU 50 266 THR 51 267 VAL 52 268 VAL 53 269 GLY 54 270 LYS 55 271 GLY 56 272 GLU 57 273 SER 58 274 ARG 59 275 VAL 60 276 LEU 61 277 ILE 62 278 GLY 63 279 ASN 64 280 GLU 65 281 TYR 66 282 GLY 67 283 GLY 68 284 LYS 69 285 GLY 70 286 PHE 71 287 TRP 72 288 ASP 73 289 ASN 74 290 HIS 75 291 HIS 76 292 HIS 77 293 HIS 78 294 HIS 79 295 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-01 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 11064 HET-s(218-289) 100.00 79 100.00 100.00 3.37e-48 PDB 2KJ3 "High-Resolution Structure Of The Het-S(218-289) Prion In Its Amyloid Form Obtained By Solid-State Nmr" 100.00 79 100.00 100.00 3.37e-48 PDB 2LBU "Haddock Calculated Model Of Congo Red Bound To The Het-S Amyloid" 100.00 79 100.00 100.00 3.37e-48 PDB 2RNM "Structure Of The Het-s(218-289) Prion In Its Amyloid Form Obtained By Solid-state Nmr" 100.00 79 100.00 100.00 3.37e-48 GB AAB19707 "s gene 30 kDa polypeptide [Podospora anserina=fungus, Peptide, 289 aa]" 91.14 289 100.00 100.00 4.93e-40 GB AAB94631 "small s protein [Podospora anserina]" 91.14 289 100.00 100.00 3.05e-40 PRF 1718317A "vegetative incompatibility gene s" 91.14 289 100.00 100.00 2.47e-40 SP Q03689 "RecName: Full=Heterokaryon incompatibility protein s; AltName: Full=Small s protein; AltName: Full=Vegetative incompatibility p" 91.14 289 100.00 100.00 3.05e-40 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 'Podospora anserina' 5145 Eukaryota Fungi Podospora anserina stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $entity_1 'recombinant technology' . Escherichia coli BL21(DE3) . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type 'fibrous protein' _Details ; "Wet" fibrils sample: the total amount of water in the sample is at least 60% (weight). Below, the concentration is given with respect to the total protein concentration. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $entity_1 . mg 5 40 '[U-100% 13C; U-100% 15N]' H2O . % 7.5 . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Rochus Keller' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 850 _Details . save_ ############################# # NMR applied experiments # ############################# save_DREAM_1 _Saveframe_category NMR_applied_experiment _Experiment_name DREAM _Sample_label $sample_1 save_ save_TOBSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOBSY _Sample_label $sample_1 save_ save_PDSD_3 _Saveframe_category NMR_applied_experiment _Experiment_name PDSD _Sample_label $sample_1 save_ save_NCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name NCA _Sample_label $sample_1 save_ save_NCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name NCO _Sample_label $sample_1 save_ save_N(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name N(CO)CA _Sample_label $sample_1 save_ save_N(CO)CB_7 _Saveframe_category NMR_applied_experiment _Experiment_name N(CO)CB _Sample_label $sample_1 save_ save_N(CA)CO_8 _Saveframe_category NMR_applied_experiment _Experiment_name N(CA)CO _Sample_label $sample_1 save_ save_CA-CA_9 _Saveframe_category NMR_applied_experiment _Experiment_name CA-CA _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0 . M pH 7.5 . pH pressure 1 . atm temperature 278 2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio adamantan C 13 'methine carbon' ppm 31.47 external direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.10132912 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label DREAM TOBSY PDSD NCA NCO N(CO)CA N(CO)CB N(CA)CO CA-CA stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name HET-s(218-289) _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 1 226 10 ASN C C 174.7 0.2 1 2 226 10 ASN CA C 52.1 0.2 1 3 226 10 ASN CB C 39.9 0.2 1 4 226 10 ASN CG C 177.4 0.2 1 5 226 10 ASN N N 125.9 0.2 1 6 226 10 ASN ND2 N 115.4 0.2 1 7 227 11 SER C C 171.9 0.2 1 8 227 11 SER CA C 56.8 0.2 1 9 227 11 SER CB C 67.2 0.2 1 10 227 11 SER N N 119.3 0.2 1 11 228 12 ALA C C 176.9 0.2 1 12 228 12 ALA CA C 49.5 0.2 1 13 228 12 ALA CB C 23.9 0.2 1 14 228 12 ALA N N 122.9 0.2 1 15 229 13 LYS C C 175.2 0.2 1 16 229 13 LYS CA C 59.9 0.2 1 17 229 13 LYS CB C 32.7 0.2 1 18 229 13 LYS CG C 25.5 0.2 1 19 229 13 LYS CD C 29.7 0.2 1 20 229 13 LYS CE C 42.2 0.2 1 21 229 13 LYS N N 123.4 0.2 1 22 230 14 ASP C C 174.4 0.2 1 23 230 14 ASP CA C 53.2 0.2 1 24 230 14 ASP CB C 45.1 0.2 1 25 230 14 ASP CG C 179.7 0.2 1 26 230 14 ASP N N 118 0.2 1 27 231 15 ILE C C 174.6 0.2 1 28 231 15 ILE CA C 60.9 0.2 1 29 231 15 ILE CB C 41.8 0.2 1 30 231 15 ILE CG1 C 27.6 0.2 1 31 231 15 ILE CG2 C 17.7 0.2 1 32 231 15 ILE CD1 C 14.2 0.2 1 33 231 15 ILE N N 122.9 0.2 1 34 232 16 ARG C C 175.5 0.2 1 35 232 16 ARG CA C 54.3 0.2 1 36 232 16 ARG CB C 33.1 0.2 1 37 232 16 ARG N N 130.1 0.2 1 38 233 17 THR C C 174.5 0.2 1 39 233 17 THR CA C 59.6 0.2 1 40 233 17 THR CB C 71.8 0.2 1 41 233 17 THR CG2 C 23.8 0.2 1 42 233 17 THR N N 113.6 0.2 1 43 234 18 GLU C C 173.8 0.2 1 44 234 18 GLU CA C 53.8 0.2 1 45 234 18 GLU CB C 33.9 0.2 1 46 234 18 GLU CG C 35.9 0.2 1 47 234 18 GLU CD C 182.9 0.2 1 48 234 18 GLU N N 120.3 0.2 1 49 235 19 GLU C C 174.2 0.2 1 50 235 19 GLU CA C 58.7 0.2 1 51 235 19 GLU CB C 27.5 0.2 1 52 235 19 GLU CG C 38.5 0.2 1 53 235 19 GLU CD C 184.8 0.2 1 54 235 19 GLU N N 117.5 0.2 1 55 236 20 ARG C C 176.3 0.2 1 56 236 20 ARG CA C 54.8 0.2 1 57 236 20 ARG CB C 30.7 0.2 1 58 236 20 ARG CG C 28.4 0.2 1 59 236 20 ARG CD C 43.9 0.2 1 60 236 20 ARG N N 123 0.2 1 61 236 20 ARG NE N 85.2 0.2 1 62 237 21 ALA C C 176.1 0.2 1 63 237 21 ALA CA C 53.2 0.2 1 64 237 21 ALA CB C 19.9 0.2 1 65 237 21 ALA N N 126 0.2 1 66 238 22 ARG C C 174.7 0.2 1 67 238 22 ARG CA C 54.7 0.2 1 68 238 22 ARG CB C 35.4 0.2 1 69 238 22 ARG CG C 26.1 0.2 1 70 238 22 ARG CD C 41.2 0.2 1 71 238 22 ARG N N 118.4 0.2 1 72 239 23 VAL C C 173.2 0.2 1 73 239 23 VAL CA C 60 0.2 1 74 239 23 VAL CB C 37 0.2 1 75 239 23 VAL CG1 C 20.9 0.2 2 76 239 23 VAL CG2 C 22.4 0.2 2 77 239 23 VAL N N 123 0.2 1 78 240 24 GLN C C 173.2 0.2 1 79 240 24 GLN CA C 52.8 0.2 1 80 240 24 GLN CB C 33 0.2 1 81 240 24 GLN CG C 31.6 0.2 1 82 240 24 GLN CD C 175.7 0.2 1 83 240 24 GLN N N 126.9 0.2 1 84 240 24 GLN NE2 N 104.6 0.2 1 85 241 25 LEU C C 172.7 0.2 1 86 241 25 LEU CA C 52.8 0.2 1 87 241 25 LEU CB C 44.8 0.2 1 88 241 25 LEU CG C 27.7 0.2 1 89 241 25 LEU CD1 C 27.1 0.2 2 90 241 25 LEU CD2 C 28.1 0.2 2 91 241 25 LEU N N 131.6 0.2 1 92 242 26 GLY C C 170.8 0.2 1 93 242 26 GLY CA C 43.8 0.2 1 94 242 26 GLY N N 113.9 0.2 1 95 243 27 ASN C C 176.1 0.2 1 96 243 27 ASN CA C 51.3 0.2 1 97 243 27 ASN CB C 40.1 0.2 1 98 243 27 ASN CG C 176.1 0.2 1 99 243 27 ASN N N 110.2 0.2 1 100 244 28 VAL C C 174.5 0.2 1 101 244 28 VAL CA C 62.1 0.2 1 102 244 28 VAL CB C 34.4 0.2 1 103 244 28 VAL CG1 C 22.1 0.2 2 104 244 28 VAL CG2 C 24.7 0.2 2 105 244 28 VAL N N 123.1 0.2 1 106 245 29 VAL C C 175.2 0.2 1 107 245 29 VAL CA C 61.1 0.2 1 108 245 29 VAL CB C 32.2 0.2 1 109 245 29 VAL CG1 C 22.5 0.2 2 110 245 29 VAL CG2 C 20.3 0.2 2 111 245 29 VAL N N 129.2 0.2 1 112 246 30 THR C C 175.3 0.2 1 113 246 30 THR CA C 62.4 0.2 1 114 246 30 THR CB C 70.9 0.2 1 115 246 30 THR CG2 C 20.8 0.2 1 116 246 30 THR N N 116.7 0.2 1 117 247 31 ALA C C 179.2 0.2 1 118 247 31 ALA CA C 56.2 0.2 1 119 247 31 ALA CB C 17.1 0.2 1 120 247 31 ALA N N 121.4 0.2 1 121 248 32 ALA C C 179.3 0.2 1 122 248 32 ALA CA C 55.1 0.2 1 123 248 32 ALA CB C 18.4 0.2 1 124 248 32 ALA N N 119.5 0.2 1 125 260 44 THR C C 175.2 0.2 1 126 260 44 THR CA C 66.2 0.2 1 127 260 44 THR CB C 69.9 0.2 1 128 260 44 THR CG2 C 22.1 0.2 1 129 260 44 THR N N 122.8 0.2 1 130 261 45 THR C C 172.4 0.2 1 131 261 45 THR CA C 61.2 0.2 1 132 261 45 THR CB C 70.8 0.2 1 133 261 45 THR CG2 C 21.2 0.2 1 134 261 45 THR N N 124.1 0.2 1 135 262 46 ASN C C 174.7 0.2 1 136 262 46 ASN CA C 52.4 0.2 1 137 262 46 ASN CB C 41 0.2 1 138 262 46 ASN CG C 176.5 0.2 1 139 262 46 ASN N N 128.1 0.2 1 140 262 46 ASN ND2 N 113.5 0.2 1 141 263 47 SER C C 171.6 0.2 1 142 263 47 SER CA C 56.5 0.2 1 143 263 47 SER CB C 66.1 0.2 1 144 263 47 SER N N 117.7 0.2 1 145 264 48 VAL C C 174.5 0.2 1 146 264 48 VAL CA C 57.1 0.2 1 147 264 48 VAL CB C 35.6 0.2 1 148 264 48 VAL CG1 C 20.7 0.2 2 149 264 48 VAL CG2 C 23.1 0.2 2 150 264 48 VAL N N 125.5 0.2 1 151 265 49 GLU C C 175.9 0.2 1 152 265 49 GLU CA C 59.5 0.2 1 153 265 49 GLU CB C 29.5 0.2 1 154 265 49 GLU CG C 37.2 0.2 1 155 265 49 GLU CD C 183.6 0.2 1 156 265 49 GLU N N 127.4 0.2 1 157 266 50 THR C C 172.9 0.2 1 158 266 50 THR CA C 60.9 0.2 1 159 266 50 THR CB C 71.6 0.2 1 160 266 50 THR CG2 C 22.3 0.2 1 161 266 50 THR N N 113.1 0.2 1 162 267 51 VAL C C 175.3 0.2 1 163 267 51 VAL CA C 60.7 0.2 1 164 267 51 VAL CB C 35.6 0.2 1 165 267 51 VAL CG1 C 21.4 0.2 2 166 267 51 VAL CG2 C 22.8 0.2 2 167 267 51 VAL N N 124.3 0.2 1 168 268 52 VAL C C 175.1 0.2 1 169 268 52 VAL CA C 61.2 0.2 1 170 268 52 VAL CB C 34.2 0.2 1 171 268 52 VAL CG1 C 20.9 0.2 2 172 268 52 VAL CG2 C 20.9 0.2 2 173 268 52 VAL N N 128.7 0.2 1 174 269 53 GLY C C 172.1 0.2 1 175 269 53 GLY CA C 44.6 0.2 1 176 269 53 GLY N N 113.6 0.2 1 177 270 54 LYS C C 176.7 0.2 1 178 270 54 LYS CA C 54.3 0.2 1 179 270 54 LYS CB C 35.3 0.2 1 180 270 54 LYS CG C 24.3 0.2 1 181 270 54 LYS CD C 29.7 0.2 1 182 270 54 LYS CE C 41.7 0.2 1 183 270 54 LYS N N 121.8 0.2 1 184 270 54 LYS NZ N 33.9 0.2 1 185 271 55 GLY C C 172.1 0.2 1 186 271 55 GLY CA C 48.5 0.2 1 187 271 55 GLY N N 115.8 0.2 1 188 272 56 GLU C C 176.4 0.2 1 189 272 56 GLU CA C 54.2 0.2 1 190 272 56 GLU CB C 30 0.2 1 191 272 56 GLU CG C 37.3 0.2 1 192 272 56 GLU CD C 184.9 0.2 1 193 272 56 GLU N N 128.8 0.2 1 194 273 57 SER C C 173.5 0.2 1 195 273 57 SER CA C 59.3 0.2 1 196 273 57 SER CB C 66.8 0.2 1 197 273 57 SER N N 116.6 0.2 1 198 274 58 ARG C C 175.6 0.2 1 199 274 58 ARG CA C 54.9 0.2 1 200 274 58 ARG CB C 32.9 0.2 1 201 274 58 ARG CG C 27.9 0.2 1 202 274 58 ARG CD C 43.8 0.2 1 203 274 58 ARG N N 118.1 0.2 1 204 274 58 ARG NE N 86.8 0.2 1 205 275 59 VAL C C 172.9 0.2 1 206 275 59 VAL CA C 60.3 0.2 1 207 275 59 VAL CB C 36.1 0.2 1 208 275 59 VAL CG1 C 21.8 0.2 2 209 275 59 VAL CG2 C 22.8 0.2 2 210 275 59 VAL N N 123 0.2 1 211 276 60 LEU C C 173.8 0.2 1 212 276 60 LEU CA C 52.7 0.2 1 213 276 60 LEU CB C 43.6 0.2 1 214 276 60 LEU CG C 26.9 0.2 1 215 276 60 LEU CD1 C 24.2 0.2 2 216 276 60 LEU CD2 C 26.3 0.2 2 217 276 60 LEU N N 130.6 0.2 1 218 277 61 ILE C C 173.3 0.2 1 219 277 61 ILE CA C 58.7 0.2 1 220 277 61 ILE CB C 35.7 0.2 1 221 277 61 ILE CG1 C 26.3 0.2 1 222 277 61 ILE CG2 C 18.8 0.2 1 223 277 61 ILE CD1 C 14.6 0.2 1 224 277 61 ILE N N 130.4 0.2 1 225 278 62 GLY C C 172.1 0.2 1 226 278 62 GLY CA C 44 0.2 1 227 278 62 GLY N N 111.6 0.2 1 228 279 63 ASN C C 173 0.2 1 229 279 63 ASN CA C 51.9 0.2 1 230 279 63 ASN CB C 40.5 0.2 1 231 279 63 ASN CG C 176.3 0.2 1 232 279 63 ASN N N 114.8 0.2 1 233 279 63 ASN ND2 N 115.4 0.2 1 234 280 64 GLU C C 174.9 0.2 1 235 280 64 GLU CA C 54.6 0.2 1 236 280 64 GLU CB C 33.4 0.2 1 237 280 64 GLU CG C 37.8 0.2 1 238 280 64 GLU CD C 181.8 0.2 1 239 280 64 GLU N N 120.6 0.2 1 240 281 65 TYR C C 176.4 0.2 1 241 281 65 TYR CA C 56.1 0.2 1 242 281 65 TYR CB C 40.4 0.2 1 243 281 65 TYR CG C 127.6 0.2 1 244 281 65 TYR CD1 C 132.8 0.2 3 245 281 65 TYR CD2 C 132.8 0.2 3 246 281 65 TYR CE1 C 117.6 0.2 3 247 281 65 TYR CE2 C 117.6 0.2 3 248 281 65 TYR N N 129.1 0.2 1 249 282 66 GLY C C 174.3 0.2 1 250 282 66 GLY CA C 46.1 0.2 1 251 282 66 GLY N N 110.3 0.2 1 252 286 70 PHE C C 175.1 0.2 1 253 286 70 PHE CA C 59.7 0.2 1 254 286 70 PHE CB C 41.3 0.2 1 255 286 70 PHE CG C 136.5 0.2 1 256 286 70 PHE CD1 C 130.9 0.2 3 257 286 70 PHE CD2 C 130.9 0.2 3 258 286 70 PHE CE1 C 129.3 0.2 3 259 286 70 PHE CE2 C 129.3 0.2 3 260 286 70 PHE CZ C 132.1 0.2 1 261 286 70 PHE N N 127.6 0.2 1 262 287 71 TRP C C 175.5 0.2 1 263 287 71 TRP CA C 57.4 0.2 1 264 287 71 TRP CB C 29.5 0.2 1 265 287 71 TRP CG C 112.1 0.2 1 266 287 71 TRP CD1 C 128.4 0.2 1 267 287 71 TRP CD2 C 129.3 0.2 1 268 287 71 TRP CE3 C 121 0.2 1 269 287 71 TRP CZ2 C 117.7 0.2 1 270 287 71 TRP CZ3 C 119.8 0.2 1 271 287 71 TRP CH2 C 124.1 0.2 1 272 287 71 TRP N N 118.2 0.2 1 273 287 71 TRP NE1 N 133.4 0.2 1 stop_ save_