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. ; 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_ _BMRB_accession_number 11028 _BMRB_flat_file_name bmr11028.str _Entry_type new _Submission_date 2008-01-25 _Accession_date 2008-01-27 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '13C chemical shifts' 218 '15N chemical shifts' 56 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _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 _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 _Page_first 1523 _Page_last 1526 _Year 2008 save_ ####################################### # Cited references within the entry # ####################################### save_reference_citation _Saveframe_category citation _Citation_title ; 13C, 15N Resonance assignment of parts of the HET-s prion protein in its amyloid form. ; _Citation_status published _Citation_type journal _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_volume 34 _Journal_issue 2 _Page_first 75 _Page_last 87 _Year 2006 save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name HET-s(218-289) loop_ _Mol_system_component_name _Mol_label HET-s(218-289) $HET-s(218-289) stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no loop_ _Biological_function 'amyloid fibrils' 'heterokaryon incompatibility' 'prion protein' stop_ save_ ######################## # Monomeric polymers # ######################## save_HET-s(218-289) _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_ ############################## # Polymer residue sequence # ############################## _Residue_count 79 _Mol_residue_sequence ; MKIDAIVGRNSAKDIRTEER ARVQLGNVVTAAALHGGIRI SDQTTNSVETVVGKGESRVL IGNEYGGKGFWDNHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 ILE 4 ASP 5 ALA 6 ILE 7 VAL 8 GLY 9 ARG 10 ASN 11 SER 12 ALA 13 LYS 14 ASP 15 ILE 16 ARG 17 THR 18 GLU 19 GLU 20 ARG 21 ALA 22 ARG 23 VAL 24 GLN 25 LEU 26 GLY 27 ASN 28 VAL 29 VAL 30 THR 31 ALA 32 ALA 33 ALA 34 LEU 35 HIS 36 GLY 37 GLY 38 ILE 39 ARG 40 ILE 41 SER 42 ASP 43 GLN 44 THR 45 THR 46 ASN 47 SER 48 VAL 49 GLU 50 THR 51 VAL 52 VAL 53 GLY 54 LYS 55 GLY 56 GLU 57 SER 58 ARG 59 VAL 60 LEU 61 ILE 62 GLY 63 ASN 64 GLU 65 TYR 66 GLY 67 GLY 68 LYS 69 GLY 70 PHE 71 TRP 72 ASP 73 ASN 74 HIS 75 HIS 76 HIS 77 HIS 78 HIS 79 HIS stop_ _Sequence_homology_query_date 2009-11-21 _Sequence_homology_query_revised_last_date 2009-10-07 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 1.33e-37 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 1.33e-37 GB AAB19707 "s gene 30 kDa polypeptide [Podospora anserina=fungus, Peptide, 289 aa]" 91.14 289 100.00 100.00 3.25e-33 GB AAB94631 "small s protein [Podospora anserina]" 91.14 289 100.00 100.00 2.23e-33 PRF 1718317A "vegetative incompatibility gene s" 91.14 289 100.00 100.00 1.89e-33 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HET-s(218-289) '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 $HET-s(218-289) '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 $HET-s(218-289) . mg 5 40 '[U-100% 13C; U-100% 15N]' H2O 100 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing stop_ save_ save_SPARKY _Saveframe_category software _Name SPARKY loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ save_ save_CARA _Saveframe_category software _Name CARA loop_ _Vendor _Address _Electronic_address 'Rochus Keller' . . stop_ loop_ _Task 'data analysis' stop_ save_ save_xwinnmr _Saveframe_category software _Name xwinnmr loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing stop_ save_ save_NMRPipe _Saveframe_category software _Name NMRPipe loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 850 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 loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 278 2 K pH 7.5 . pH pressure 1 . atm 'ionic strength' 0 . M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference 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 adamantan N 15 'methine carbon' ppm 31.47 external 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 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) 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 10 ASN C C 174.7 0.2 1 2 10 10 ASN CA C 52.1 0.2 1 3 10 10 ASN CB C 39.9 0.2 1 4 10 10 ASN CG C 177.4 0.2 1 5 10 10 ASN N N 125.9 0.2 1 6 10 10 ASN ND2 N 115.4 0.2 1 7 11 11 SER C C 171.9 0.2 1 8 11 11 SER CA C 56.8 0.2 1 9 11 11 SER CB C 67.2 0.2 1 10 11 11 SER N N 119.3 0.2 1 11 12 12 ALA C C 176.9 0.2 1 12 12 12 ALA CA C 49.5 0.2 1 13 12 12 ALA CB C 23.9 0.2 1 14 12 12 ALA N N 122.9 0.2 1 15 13 13 LYS C C 175.2 0.2 1 16 13 13 LYS CA C 59.9 0.2 1 17 13 13 LYS CB C 32.7 0.2 1 18 13 13 LYS CG C 25.5 0.2 1 19 13 13 LYS CD C 29.7 0.2 1 20 13 13 LYS CE C 42.2 0.2 1 21 13 13 LYS N N 123.4 0.2 1 22 14 14 ASP C C 174.4 0.2 1 23 14 14 ASP CA C 53.2 0.2 1 24 14 14 ASP CB C 45.1 0.2 1 25 14 14 ASP CG C 179.7 0.2 1 26 14 14 ASP N N 118.0 0.2 1 27 15 15 ILE C C 174.6 0.2 1 28 15 15 ILE CA C 60.9 0.2 1 29 15 15 ILE CB C 41.8 0.2 1 30 15 15 ILE CG1 C 27.6 0.2 1 31 15 15 ILE CG2 C 17.7 0.2 1 32 15 15 ILE CD1 C 14.2 0.2 1 33 15 15 ILE N N 122.9 0.2 1 34 16 16 ARG C C 175.5 0.2 1 35 16 16 ARG CA C 54.3 0.2 1 36 16 16 ARG CB C 33.1 0.2 1 37 16 16 ARG N N 130.1 0.2 1 38 17 17 THR C C 174.5 0.2 1 39 17 17 THR CA C 59.6 0.2 1 40 17 17 THR CB C 71.8 0.2 1 41 17 17 THR CG2 C 23.8 0.2 1 42 17 17 THR N N 113.6 0.2 1 43 18 18 GLU C C 173.8 0.2 1 44 18 18 GLU CA C 53.8 0.2 1 45 18 18 GLU CB C 33.9 0.2 1 46 18 18 GLU CG C 35.9 0.2 1 47 18 18 GLU CD C 182.9 0.2 1 48 18 18 GLU N N 120.3 0.2 1 49 19 19 GLU C C 174.2 0.2 1 50 19 19 GLU CA C 58.7 0.2 1 51 19 19 GLU CB C 27.5 0.2 1 52 19 19 GLU CG C 38.5 0.2 1 53 19 19 GLU CD C 184.8 0.2 1 54 19 19 GLU N N 117.5 0.2 1 55 20 20 ARG C C 176.3 0.2 1 56 20 20 ARG CA C 54.8 0.2 1 57 20 20 ARG CB C 30.7 0.2 1 58 20 20 ARG CG C 28.4 0.2 1 59 20 20 ARG CD C 43.9 0.2 1 60 20 20 ARG N N 123.0 0.2 1 61 20 20 ARG NE N 85.2 0.2 1 62 21 21 ALA C C 176.1 0.2 1 63 21 21 ALA CA C 53.2 0.2 1 64 21 21 ALA CB C 19.9 0.2 1 65 21 21 ALA N N 126.0 0.2 1 66 22 22 ARG C C 174.7 0.2 1 67 22 22 ARG CA C 54.7 0.2 1 68 22 22 ARG CB C 35.4 0.2 1 69 22 22 ARG CG C 26.1 0.2 1 70 22 22 ARG CD C 41.2 0.2 1 71 22 22 ARG N N 118.4 0.2 1 72 23 23 VAL C C 173.2 0.2 1 73 23 23 VAL CA C 60.0 0.2 1 74 23 23 VAL CB C 37.0 0.2 1 75 23 23 VAL CG1 C 20.9 0.2 2 76 23 23 VAL CG2 C 22.4 0.2 2 77 23 23 VAL N N 123.0 0.2 1 78 24 24 GLN C C 173.2 0.2 1 79 24 24 GLN CA C 52.8 0.2 1 80 24 24 GLN CB C 33.0 0.2 1 81 24 24 GLN CG C 31.6 0.2 1 82 24 24 GLN CD C 175.7 0.2 1 83 24 24 GLN N N 126.9 0.2 1 84 24 24 GLN NE2 N 104.6 0.2 1 85 25 25 LEU C C 172.7 0.2 1 86 25 25 LEU CA C 52.8 0.2 1 87 25 25 LEU CB C 44.8 0.2 1 88 25 25 LEU CG C 27.7 0.2 1 89 25 25 LEU CD1 C 27.1 0.2 2 90 25 25 LEU CD2 C 28.1 0.2 2 91 25 25 LEU N N 131.6 0.2 1 92 26 26 GLY C C 170.8 0.2 1 93 26 26 GLY CA C 43.8 0.2 1 94 26 26 GLY N N 113.9 0.2 1 95 27 27 ASN C C 176.1 0.2 1 96 27 27 ASN CA C 51.3 0.2 1 97 27 27 ASN CB C 40.1 0.2 1 98 27 27 ASN CG C 176.1 0.2 1 99 27 27 ASN N N 110.2 0.2 1 100 28 28 VAL C C 174.5 0.2 1 101 28 28 VAL CA C 62.1 0.2 1 102 28 28 VAL CB C 34.4 0.2 1 103 28 28 VAL CG1 C 22.1 0.2 2 104 28 28 VAL CG2 C 24.7 0.2 2 105 28 28 VAL N N 123.1 0.2 1 106 29 29 VAL C C 175.2 0.2 1 107 29 29 VAL CA C 61.1 0.2 1 108 29 29 VAL CB C 32.2 0.2 1 109 29 29 VAL CG1 C 22.5 0.2 2 110 29 29 VAL CG2 C 20.3 0.2 2 111 29 29 VAL N N 129.2 0.2 1 112 30 30 THR C C 175.3 0.2 1 113 30 30 THR CA C 62.4 0.2 1 114 30 30 THR CB C 70.9 0.2 1 115 30 30 THR CG2 C 20.8 0.2 1 116 30 30 THR N N 116.7 0.2 1 117 31 31 ALA C C 179.2 0.2 1 118 31 31 ALA CA C 56.2 0.2 1 119 31 31 ALA CB C 17.1 0.2 1 120 31 31 ALA N N 121.4 0.2 1 121 32 32 ALA C C 179.3 0.2 1 122 32 32 ALA CA C 55.1 0.2 1 123 32 32 ALA CB C 18.4 0.2 1 124 32 32 ALA N N 119.5 0.2 1 125 44 44 THR C C 175.2 0.2 1 126 44 44 THR CA C 66.2 0.2 1 127 44 44 THR CB C 69.9 0.2 1 128 44 44 THR CG2 C 22.1 0.2 1 129 44 44 THR N N 122.8 0.2 1 130 45 45 THR C C 172.4 0.2 1 131 45 45 THR CA C 61.2 0.2 1 132 45 45 THR CB C 70.8 0.2 1 133 45 45 THR CG2 C 21.2 0.2 1 134 45 45 THR N N 124.1 0.2 1 135 46 46 ASN C C 174.7 0.2 1 136 46 46 ASN CA C 52.4 0.2 1 137 46 46 ASN CB C 41.0 0.2 1 138 46 46 ASN CG C 176.5 0.2 1 139 46 46 ASN N N 128.1 0.2 1 140 46 46 ASN ND2 N 113.5 0.2 1 141 47 47 SER C C 171.6 0.2 1 142 47 47 SER CA C 56.5 0.2 1 143 47 47 SER CB C 66.1 0.2 1 144 47 47 SER N N 117.7 0.2 1 145 48 48 VAL C C 174.5 0.2 1 146 48 48 VAL CA C 57.1 0.2 1 147 48 48 VAL CB C 35.6 0.2 1 148 48 48 VAL CG1 C 20.7 0.2 2 149 48 48 VAL CG2 C 23.1 0.2 2 150 48 48 VAL N N 125.5 0.2 1 151 49 49 GLU C C 175.9 0.2 1 152 49 49 GLU CA C 59.5 0.2 1 153 49 49 GLU CB C 29.5 0.2 1 154 49 49 GLU CG C 37.2 0.2 1 155 49 49 GLU CD C 183.6 0.2 1 156 49 49 GLU N N 127.4 0.2 1 157 50 50 THR C C 172.9 0.2 1 158 50 50 THR CA C 60.9 0.2 1 159 50 50 THR CB C 71.6 0.2 1 160 50 50 THR CG2 C 22.3 0.2 1 161 50 50 THR N N 113.1 0.2 1 162 51 51 VAL C C 175.3 0.2 1 163 51 51 VAL CA C 60.7 0.2 1 164 51 51 VAL CB C 35.6 0.2 1 165 51 51 VAL CG1 C 21.4 0.2 2 166 51 51 VAL CG2 C 22.8 0.2 2 167 51 51 VAL N N 124.3 0.2 1 168 52 52 VAL C C 175.1 0.2 1 169 52 52 VAL CA C 61.2 0.2 1 170 52 52 VAL CB C 34.2 0.2 1 171 52 52 VAL CG1 C 20.9 0.2 2 172 52 52 VAL CG2 C 20.9 0.2 2 173 52 52 VAL N N 128.7 0.2 1 174 53 53 GLY C C 172.1 0.2 1 175 53 53 GLY CA C 44.6 0.2 1 176 53 53 GLY N N 113.6 0.2 1 177 54 54 LYS C C 176.7 0.2 1 178 54 54 LYS CA C 54.3 0.2 1 179 54 54 LYS CB C 35.3 0.2 1 180 54 54 LYS CG C 24.3 0.2 1 181 54 54 LYS CD C 29.7 0.2 1 182 54 54 LYS CE C 41.7 0.2 1 183 54 54 LYS N N 121.8 0.2 1 184 54 54 LYS NZ N 33.9 0.2 1 185 55 55 GLY C C 172.1 0.2 1 186 55 55 GLY CA C 48.5 0.2 1 187 55 55 GLY N N 115.8 0.2 1 188 56 56 GLU C C 176.4 0.2 1 189 56 56 GLU CA C 54.2 0.2 1 190 56 56 GLU CB C 30.0 0.2 1 191 56 56 GLU CG C 37.3 0.2 1 192 56 56 GLU CD C 184.9 0.2 1 193 56 56 GLU N N 128.8 0.2 1 194 57 57 SER C C 173.5 0.2 1 195 57 57 SER CA C 59.3 0.2 1 196 57 57 SER CB C 66.8 0.2 1 197 57 57 SER N N 116.6 0.2 1 198 58 58 ARG C C 175.6 0.2 1 199 58 58 ARG CA C 54.9 0.2 1 200 58 58 ARG CB C 32.9 0.2 1 201 58 58 ARG CG C 27.9 0.2 1 202 58 58 ARG CD C 43.8 0.2 1 203 58 58 ARG N N 118.1 0.2 1 204 58 58 ARG NE N 86.8 0.2 1 205 59 59 VAL C C 172.9 0.2 1 206 59 59 VAL CA C 60.3 0.2 1 207 59 59 VAL CB C 36.1 0.2 1 208 59 59 VAL CG1 C 21.8 0.2 2 209 59 59 VAL CG2 C 22.8 0.2 2 210 59 59 VAL N N 123.0 0.2 1 211 60 60 LEU C C 173.8 0.2 1 212 60 60 LEU CA C 52.7 0.2 1 213 60 60 LEU CB C 43.6 0.2 1 214 60 60 LEU CG C 26.9 0.2 1 215 60 60 LEU CD1 C 24.2 0.2 2 216 60 60 LEU CD2 C 26.3 0.2 2 217 60 60 LEU N N 130.6 0.2 1 218 61 61 ILE C C 173.3 0.2 1 219 61 61 ILE CA C 58.7 0.2 1 220 61 61 ILE CB C 35.7 0.2 1 221 61 61 ILE CG1 C 26.3 0.2 1 222 61 61 ILE CG2 C 18.8 0.2 1 223 61 61 ILE CD1 C 14.6 0.2 1 224 61 61 ILE N N 130.4 0.2 1 225 62 62 GLY C C 172.1 0.2 1 226 62 62 GLY CA C 44.0 0.2 1 227 62 62 GLY N N 111.6 0.2 1 228 63 63 ASN C C 173.0 0.2 1 229 63 63 ASN CA C 51.9 0.2 1 230 63 63 ASN CB C 40.5 0.2 1 231 63 63 ASN CG C 176.3 0.2 1 232 63 63 ASN N N 114.8 0.2 1 233 63 63 ASN ND2 N 115.4 0.2 1 234 64 64 GLU C C 174.9 0.2 1 235 64 64 GLU CA C 54.6 0.2 1 236 64 64 GLU CB C 33.4 0.2 1 237 64 64 GLU CG C 37.8 0.2 1 238 64 64 GLU CD C 181.8 0.2 1 239 64 64 GLU N N 120.6 0.2 1 240 65 65 TYR C C 176.4 0.2 1 241 65 65 TYR CA C 56.1 0.2 1 242 65 65 TYR CB C 40.4 0.2 1 243 65 65 TYR CG C 127.6 0.2 1 244 65 65 TYR CD1 C 132.8 0.2 3 245 65 65 TYR CD2 C 132.8 0.2 3 246 65 65 TYR CE1 C 117.6 0.2 3 247 65 65 TYR CE2 C 117.6 0.2 3 248 65 65 TYR N N 129.1 0.2 1 249 66 66 GLY C C 174.3 0.2 1 250 66 66 GLY CA C 46.1 0.2 1 251 66 66 GLY N N 110.3 0.2 1 252 70 70 PHE C C 175.1 0.2 1 253 70 70 PHE CA C 59.7 0.2 1 254 70 70 PHE CB C 41.3 0.2 1 255 70 70 PHE CG C 136.5 0.2 1 256 70 70 PHE CD1 C 130.9 0.2 3 257 70 70 PHE CD2 C 130.9 0.2 3 258 70 70 PHE CE1 C 129.3 0.2 3 259 70 70 PHE CE2 C 129.3 0.2 3 260 70 70 PHE CZ C 132.1 0.2 1 261 70 70 PHE N N 127.6 0.2 1 262 71 71 TRP C C 175.5 0.2 1 263 71 71 TRP CA C 57.4 0.2 1 264 71 71 TRP CB C 29.5 0.2 1 265 71 71 TRP CG C 112.1 0.2 1 266 71 71 TRP CD1 C 128.4 0.2 1 267 71 71 TRP CD2 C 129.3 0.2 1 268 71 71 TRP CE3 C 121.0 0.2 1 269 71 71 TRP CZ2 C 117.7 0.2 1 270 71 71 TRP CZ3 C 119.8 0.2 1 271 71 71 TRP CH2 C 124.1 0.2 1 272 71 71 TRP N N 118.2 0.2 1 273 71 71 TRP NE1 N 133.4 0.2 1 stop_ save_