data_27025 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Ascl1 fragment C ; _BMRB_accession_number 27025 _BMRB_flat_file_name bmr27025.str _Entry_type original _Submission_date 2017-02-06 _Accession_date 2017-02-06 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Fragment C of Ascl1 protein' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Baronti Lorenzo . . 2 Hosek Tomas . . 3 Gil-Caballero Sergio . . 4 Raveh-Amit Hadas . . 5 Calcada Eduardo O. . 6 Ayala Isabel . . 7 Dinnyes Andras . . 8 Felli Isabella C. . 9 Pierattelli Roberta . . 10 Brutscher Bernhard . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 67 "13C chemical shifts" 208 "15N chemical shifts" 67 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-04-21 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 27023 'Ascl1 fragment A' 27024 'Ascl1 fragment B' 27026 'Ascl1 fragment D' stop_ _Original_release_date 2017-02-06 save_ ############################# # Citation for this entry # ############################# save_Baronti_et_al. _Saveframe_category entry_citation _Citation_full . _Citation_title ; Fragment-Based NMR Study of the Conformational Dynamics in the bHLH Transcription Factor Ascl1' ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 28402879 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Baronti Lorenzo . . 2 Hosek Tomas . . 3 Gil-Caballero Sergio . . 4 Raveh-Amit Hadas . . 5 Calcada Eduardo O. . 6 Ayala Isabel . . 7 Dinnyes Andras . . 8 Felli Isabella C. . 9 Pierattelli Roberta . . 10 Brutscher Bernhard . . stop_ _Journal_abbreviation 'Biophys. J.' _Journal_name_full 'Biophysical journal' _Journal_volume 112 _Journal_issue 7 _Journal_ISSN 1542-0086 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1366 _Page_last 1373 _Year 2017 _Details . loop_ _Keyword Ascl1 HASH1 IDP 'Intrinsically disordered protein' bHLH stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Ascl1 trascription factor' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Ascl1 trascription factor, Fragment C' $Ascl1_fragment_C stop_ _System_molecular_weight . _System_physical_state 'partially disordered' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details ; Ascl1 human bHLH transcription factor. Ascl1 was studied by generating different overlapping fragments (A,B,C and D) that represent different functional motifs on the Ascl1 polypeptide chain. Fragment C is composed of a 9 aa tag at the N-terminus followed by residues 114-183 of the full length sequence. ; save_ ######################## # Monomeric polymers # ######################## save_Ascl1_fragment_C _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Ascl1_fragment_C _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'Basic Helix-Loop-Helix (bHLH) DNA binding domain of Ascl1. Fragment 114-183 of the full length sequence.' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 79 _Mol_residue_sequence ; MASHHHHHHQQQPAAVARRN ERERNRVKLVNLGFATLREH VPNGAANKKMSKVETLRSAV EYIRALQQLLDEHDAVSAA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -8 MET 2 -7 ALA 3 -6 SER 4 -5 HIS 5 -4 HIS 6 -3 HIS 7 -2 HIS 8 -1 HIS 9 0 HIS 10 114 GLN 11 115 GLN 12 116 GLN 13 117 PRO 14 118 ALA 15 119 ALA 16 120 VAL 17 121 ALA 18 122 ARG 19 123 ARG 20 124 ASN 21 125 GLU 22 126 ARG 23 127 GLU 24 128 ARG 25 129 ASN 26 130 ARG 27 131 VAL 28 132 LYS 29 133 LEU 30 134 VAL 31 135 ASN 32 136 LEU 33 137 GLY 34 138 PHE 35 139 ALA 36 140 THR 37 141 LEU 38 142 ARG 39 143 GLU 40 144 HIS 41 145 VAL 42 146 PRO 43 147 ASN 44 148 GLY 45 149 ALA 46 150 ALA 47 151 ASN 48 152 LYS 49 153 LYS 50 154 MET 51 155 SER 52 156 LYS 53 157 VAL 54 158 GLU 55 159 THR 56 160 LEU 57 161 ARG 58 162 SER 59 163 ALA 60 164 VAL 61 165 GLU 62 166 TYR 63 167 ILE 64 168 ARG 65 169 ALA 66 170 LEU 67 171 GLN 68 172 GLN 69 173 LEU 70 174 LEU 71 175 ASP 72 176 GLU 73 177 HIS 74 178 ASP 75 179 ALA 76 180 VAL 77 181 SER 78 182 ALA 79 183 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Ascl1_fragment_C Human 9606 Eukaryota Metazoa Homo sapiens 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 $Ascl1_fragment_C 'recombinant technology' . Escherichia coli . pET21a 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 $Ascl1_fragment_C 250 uM 100 400 '[U-100% 13C; U-100% 15N]' TRIS 50 mM . . 'natural abundance' DTT 5 mM . . 'natural abundance' SDS 2 mM . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CCPNMR _Saveframe_category software _Name CCPNMR _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 950 _Details 'Equipped with cryogenically cooled triple-resonance probeheads (TCI)' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 850 _Details 'Equipped with cryogenically cooled triple-resonance probeheads (TCI)' save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details 'Equipped with cryogenically cooled triple-resonance probeheads (TCI)' save_ save_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'Equipped with cryogenically cooled triple-resonance probeheads (TCI)' save_ ############################# # NMR applied experiments # ############################# save_3D_BEST-TROSY_HCNs_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D BEST-TROSY HCNs' _Sample_label $sample_1 save_ save_3D_BEST-TROSY_HNNs_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D BEST-TROSY HNNs' _Sample_label $sample_1 save_ save_HADAMAC_3 _Saveframe_category NMR_applied_experiment _Experiment_name HADAMAC _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 pH 6.5 . pH pressure 1 . atm temperature 323 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details ; The reported chemical shift assignment is numbered according to "Baronti_et_al.". All assigned chemical shifts of Ascl1 fragments deposited start from the first biologically relevant aminoacid and do not take into account the artificial tag at the N-terminus (see "Baronti_et_al."). ; loop_ _Software_label $CCPNMR stop_ loop_ _Experiment_label '3D BEST-TROSY HCNs' '3D BEST-TROSY HNNs' HADAMAC 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 'Ascl1 trascription factor, Fragment C' _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 1 114 10 GLN C C 175.7 . 1 2 114 10 GLN CA C 56.5 . 1 3 114 10 GLN CB C 29.6 . 1 4 115 11 GLN H H 8.15 . 1 5 115 11 GLN C C 175.4 . 1 6 115 11 GLN CA C 56.2 . 1 7 115 11 GLN CB C 29.7 . 1 8 115 11 GLN N N 120.2 . 1 9 116 12 GLN H H 8.18 . 1 10 116 12 GLN C C 174.1 . 1 11 116 12 GLN CA C 54 . 1 12 116 12 GLN CB C 29.2 . 1 13 116 12 GLN N N 121.5 . 1 14 117 13 PRO C C 177 . 1 15 117 13 PRO CA C 64 . 1 16 117 13 PRO CB C 32.1 . 1 17 118 14 ALA H H 8.23 . 1 18 118 14 ALA C C 177.9 . 1 19 118 14 ALA CA C 53.5 . 1 20 118 14 ALA CB C 19.2 . 1 21 118 14 ALA N N 123.3 . 1 22 119 15 ALA H H 7.91 . 1 23 119 15 ALA C C 178.2 . 1 24 119 15 ALA CA C 53.7 . 1 25 119 15 ALA CB C 19.3 . 1 26 119 15 ALA N N 121.1 . 1 27 120 16 VAL H H 7.54 . 1 28 120 16 VAL C C 176.2 . 1 29 120 16 VAL CA C 63.3 . 1 30 120 16 VAL CB C 32.5 . 1 31 120 16 VAL N N 116.8 . 1 32 121 17 ALA H H 7.81 . 1 33 121 17 ALA C C 178.1 . 1 34 121 17 ALA CA C 53.3 . 1 35 121 17 ALA CB C 19.3 . 1 36 121 17 ALA N N 124.8 . 1 37 122 18 ARG H H 7.84 . 1 38 122 18 ARG C C 177.1 . 1 39 122 18 ARG CA C 56.9 . 1 40 122 18 ARG CB C 30.6 . 1 41 122 18 ARG N N 118.1 . 1 42 123 19 ARG H H 7.91 . 1 43 123 19 ARG C C 176.7 . 1 44 123 19 ARG CA C 57.5 . 1 45 123 19 ARG CB C 30.5 . 1 46 123 19 ARG N N 120 . 1 47 124 20 ASN H H 8.08 . 1 48 124 20 ASN C C 175.4 . 1 49 124 20 ASN CA C 54.1 . 1 50 124 20 ASN CB C 39.3 . 1 51 124 20 ASN N N 117.9 . 1 52 125 21 GLU H H 8.05 . 1 53 125 21 GLU C C 176.1 . 1 54 125 21 GLU CA C 56.8 . 1 55 125 21 GLU CB C 29.9 . 1 56 125 21 GLU N N 119.7 . 1 57 126 22 ARG H H 7.79 . 1 58 126 22 ARG C C 176 . 1 59 126 22 ARG CA C 56.2 . 1 60 126 22 ARG CB C 31.2 . 1 61 126 22 ARG N N 120.9 . 1 62 127 23 GLU H H 8.3 . 1 63 127 23 GLU C C 176.3 . 1 64 127 23 GLU CA C 56.8 . 1 65 127 23 GLU CB C 30.2 . 1 66 127 23 GLU N N 122.5 . 1 67 128 24 ARG H H 8.12 . 1 68 128 24 ARG C C 176 . 1 69 128 24 ARG CA C 56.1 . 1 70 128 24 ARG CB C 30.6 . 1 71 128 24 ARG N N 121.7 . 1 72 129 25 ASN H H 8.26 . 1 73 129 25 ASN C C 175.3 . 1 74 129 25 ASN CA C 53.8 . 1 75 129 25 ASN CB C 39.2 . 1 76 129 25 ASN N N 119.9 . 1 77 130 26 ARG H H 8.06 . 1 78 130 26 ARG C C 176.6 . 1 79 130 26 ARG CA C 57.5 . 1 80 130 26 ARG CB C 30.7 . 1 81 130 26 ARG N N 120.9 . 1 82 131 27 VAL H H 7.75 . 1 83 131 27 VAL C C 175.8 . 1 84 131 27 VAL CA C 63.6 . 1 85 131 27 VAL CB C 32.4 . 1 86 131 27 VAL N N 119.4 . 1 87 132 28 LYS H H 7.8 . 1 88 132 28 LYS C C 177.4 . 1 89 132 28 LYS CA C 57 . 1 90 132 28 LYS CB C 32.8 . 1 91 132 28 LYS N N 122 . 1 92 133 29 LEU H H 8.01 . 1 93 133 29 LEU C C 178 . 1 94 133 29 LEU CA C 57.2 . 1 95 133 29 LEU CB C 42.2 . 1 96 133 29 LEU N N 121.7 . 1 97 134 30 VAL H H 7.65 . 1 98 134 30 VAL C C 176.3 . 1 99 134 30 VAL CA C 64.1 . 1 100 134 30 VAL CB C 32.1 . 1 101 134 30 VAL N N 115.4 . 1 102 135 31 ASN H H 7.88 . 1 103 135 31 ASN C C 176.1 . 1 104 135 31 ASN CA C 54.7 . 1 105 135 31 ASN CB C 39 . 1 106 135 31 ASN N N 118.9 . 1 107 136 32 LEU H H 7.76 . 1 108 136 32 LEU C C 178 . 1 109 136 32 LEU CA C 56.5 . 1 110 136 32 LEU CB C 42.6 . 1 111 136 32 LEU N N 121.2 . 1 112 137 33 GLY H H 8.04 . 1 113 137 33 GLY C C 174.6 . 1 114 137 33 GLY CA C 46.4 . 1 115 137 33 GLY N N 107.8 . 1 116 138 34 PHE H H 8.21 . 1 117 138 34 PHE C C 176.9 . 1 118 138 34 PHE CA C 60.5 . 1 119 138 34 PHE CB C 39.1 . 1 120 138 34 PHE N N 120.9 . 1 121 139 35 ALA H H 8.27 . 1 122 139 35 ALA C C 179.7 . 1 123 139 35 ALA CA C 55.2 . 1 124 139 35 ALA CB C 18.6 . 1 125 139 35 ALA N N 121.2 . 1 126 140 36 THR H H 7.76 . 1 127 140 36 THR C C 176.7 . 1 128 140 36 THR CA C 65.2 . 1 129 140 36 THR CB C 69 . 1 130 140 36 THR N N 112.9 . 1 131 141 37 LEU H H 7.86 . 1 132 141 37 LEU C C 178.6 . 1 133 141 37 LEU CA C 58.5 . 1 134 141 37 LEU CB C 42 . 1 135 141 37 LEU N N 122.8 . 1 136 142 38 ARG H H 8.04 . 1 137 142 38 ARG C C 177.7 . 1 138 142 38 ARG CA C 59.1 . 1 139 142 38 ARG CB C 30 . 1 140 142 38 ARG N N 116.9 . 1 141 143 39 GLU H H 7.55 . 1 142 143 39 GLU C C 176.9 . 1 143 143 39 GLU CA C 57.6 . 1 144 143 39 GLU CB C 29.7 . 1 145 143 39 GLU N N 116.5 . 1 146 144 40 HIS H H 7.81 . 1 147 144 40 HIS C C 173.6 . 1 148 144 40 HIS CA C 56.1 . 1 149 144 40 HIS CB C 29.7 . 1 150 144 40 HIS N N 115.9 . 1 151 145 41 VAL H H 7.44 . 1 152 145 41 VAL C C 174.4 . 1 153 145 41 VAL CA C 61 . 1 154 145 41 VAL CB C 32.5 . 1 155 145 41 VAL N N 120.5 . 1 156 146 42 PRO C C 176.6 . 1 157 146 42 PRO CA C 63.6 . 1 158 146 42 PRO CB C 32.1 . 1 159 147 43 ASN H H 8.27 . 1 160 147 43 ASN C C 176.3 . 1 161 147 43 ASN CA C 54.1 . 1 162 147 43 ASN CB C 39.3 . 1 163 147 43 ASN N N 118.7 . 1 164 148 44 GLY H H 8.24 . 1 165 148 44 GLY C C 174.5 . 1 166 148 44 GLY CA C 46.1 . 1 167 148 44 GLY N N 109.6 . 1 168 149 45 ALA H H 7.92 . 1 169 149 45 ALA C C 177.8 . 1 170 149 45 ALA CA C 53.6 . 1 171 149 45 ALA CB C 19.3 . 1 172 149 45 ALA N N 123.3 . 1 173 150 46 ALA H H 7.98 . 1 174 150 46 ALA C C 177.9 . 1 175 150 46 ALA CA C 53.6 . 1 176 150 46 ALA CB C 19 . 1 177 150 46 ALA N N 120.7 . 1 178 151 47 ASN H H 7.98 . 1 179 151 47 ASN C C 175.5 . 1 180 151 47 ASN CA C 53.9 . 1 181 151 47 ASN CB C 39.1 . 1 182 151 47 ASN N N 116.4 . 1 183 152 48 LYS H H 7.88 . 1 184 152 48 LYS C C 176.7 . 1 185 152 48 LYS CA C 56.8 . 1 186 152 48 LYS CB C 32.8 . 1 187 152 48 LYS N N 120.3 . 1 188 153 49 LYS H H 8.04 . 1 189 153 49 LYS C C 176.9 . 1 190 153 49 LYS CA C 57.1 . 1 191 153 49 LYS CB C 32.8 . 1 192 153 49 LYS N N 121 . 1 193 154 50 MET H H 8.1 . 1 194 154 50 MET C C 176.8 . 1 195 154 50 MET CA C 56.3 . 1 196 154 50 MET CB C 33 . 1 197 154 50 MET N N 119.5 . 1 198 155 51 SER H H 8.13 . 1 199 155 51 SER C C 176.1 . 1 200 155 51 SER CA C 59.6 . 1 201 155 51 SER CB C 63.8 . 1 202 155 51 SER N N 116.2 . 1 203 156 52 LYS H H 8.23 . 1 204 156 52 LYS C C 177.9 . 1 205 156 52 LYS CA C 58.8 . 1 206 156 52 LYS CB C 32.5 . 1 207 156 52 LYS N N 122.4 . 1 208 157 53 VAL H H 7.72 . 1 209 157 53 VAL C C 177.2 . 1 210 157 53 VAL CA C 65.9 . 1 211 157 53 VAL CB C 31.7 . 1 212 157 53 VAL N N 118.3 . 1 213 158 54 GLU H H 7.99 . 1 214 158 54 GLU C C 179.1 . 1 215 158 54 GLU CA C 59.4 . 1 216 158 54 GLU CB C 29.4 . 1 217 158 54 GLU N N 120.4 . 1 218 159 55 THR H H 7.89 . 1 219 159 55 THR C C 176 . 1 220 159 55 THR CA C 66.3 . 1 221 159 55 THR CB C 69 . 1 222 159 55 THR N N 117.2 . 1 223 160 56 LEU H H 7.9 . 1 224 160 56 LEU C C 178.2 . 1 225 160 56 LEU CA C 58.1 . 1 226 160 56 LEU CB C 41.7 . 1 227 160 56 LEU N N 122.1 . 1 228 161 57 ARG H H 8.24 . 1 229 161 57 ARG C C 178.9 . 1 230 161 57 ARG CA C 59.8 . 1 231 161 57 ARG CB C 30 . 1 232 161 57 ARG N N 118 . 1 233 162 58 SER H H 8.04 . 1 234 162 58 SER C C 176 . 1 235 162 58 SER CA C 61.6 . 1 236 162 58 SER CB C 63.2 . 1 237 162 58 SER N N 115.5 . 1 238 163 59 ALA H H 8.13 . 1 239 163 59 ALA C C 179 . 1 240 163 59 ALA CA C 55.5 . 1 241 163 59 ALA CB C 18.4 . 1 242 163 59 ALA N N 124.5 . 1 243 164 60 VAL H H 7.97 . 1 244 164 60 VAL C C 177.6 . 1 245 164 60 VAL CA C 66.9 . 1 246 164 60 VAL CB C 31.8 . 1 247 164 60 VAL N N 116.9 . 1 248 165 61 GLU H H 7.86 . 1 249 165 61 GLU C C 179.6 . 1 250 165 61 GLU CA C 59.5 . 1 251 165 61 GLU CB C 29 . 1 252 165 61 GLU N N 119.1 . 1 253 166 62 TYR H H 7.94 . 1 254 166 62 TYR C C 177.9 . 1 255 166 62 TYR CA C 61.6 . 1 256 166 62 TYR CB C 38.4 . 1 257 166 62 TYR N N 120.1 . 1 258 167 63 ILE H H 8.13 . 1 259 167 63 ILE C C 178.1 . 1 260 167 63 ILE CA C 65 . 1 261 167 63 ILE CB C 37.4 . 1 262 167 63 ILE N N 120.1 . 1 263 168 64 ARG H H 8.37 . 1 264 168 64 ARG C C 179.2 . 1 265 168 64 ARG CA C 59.5 . 1 266 168 64 ARG CB C 29.9 . 1 267 168 64 ARG N N 119.6 . 1 268 169 65 ALA H H 7.83 . 1 269 169 65 ALA C C 180.4 . 1 270 169 65 ALA CA C 55.1 . 1 271 169 65 ALA CB C 18.2 . 1 272 169 65 ALA N N 122.4 . 1 273 170 66 LEU H H 8.01 . 1 274 170 66 LEU C C 178.6 . 1 275 170 66 LEU CA C 57.8 . 1 276 170 66 LEU CB C 41.9 . 1 277 170 66 LEU N N 120.8 . 1 278 171 67 GLN H H 8.28 . 1 279 171 67 GLN C C 178.2 . 1 280 171 67 GLN CA C 59.5 . 1 281 171 67 GLN CB C 28.8 . 1 282 171 67 GLN N N 117.9 . 1 283 172 68 GLN H H 7.72 . 1 284 172 68 GLN C C 178 . 1 285 172 68 GLN CA C 58.5 . 1 286 172 68 GLN CB C 28.6 . 1 287 172 68 GLN N N 117.6 . 1 288 173 69 LEU H H 7.78 . 1 289 173 69 LEU C C 179.2 . 1 290 173 69 LEU CA C 57.6 . 1 291 173 69 LEU CB C 42.5 . 1 292 173 69 LEU N N 120.9 . 1 293 174 70 LEU H H 7.93 . 1 294 174 70 LEU C C 178.5 . 1 295 174 70 LEU CA C 56.8 . 1 296 174 70 LEU CB C 41.8 . 1 297 174 70 LEU N N 119.5 . 1 298 175 71 ASP H H 7.89 . 1 299 175 71 ASP C C 177.3 . 1 300 175 71 ASP CA C 55.7 . 1 301 175 71 ASP CB C 41.1 . 1 302 175 71 ASP N N 120 . 1 303 176 72 GLU H H 7.99 . 1 304 176 72 GLU C C 177.1 . 1 305 176 72 GLU CA C 57.4 . 1 306 176 72 GLU CB C 29.7 . 1 307 176 72 GLU N N 119.9 . 1 308 177 73 HIS H H 8.1 . 1 309 177 73 HIS C C 174.6 . 1 310 177 73 HIS CA C 56.5 . 1 311 177 73 HIS CB C 29 . 1 312 177 73 HIS N N 118.9 . 1 313 178 74 ASP H H 8.21 . 1 314 178 74 ASP C C 175.9 . 1 315 178 74 ASP CA C 54.8 . 1 316 178 74 ASP CB C 41.2 . 1 317 178 74 ASP N N 121.3 . 1 318 179 75 ALA H H 8 . 1 319 179 75 ALA C C 178 . 1 320 179 75 ALA CA C 53 . 1 321 179 75 ALA CB C 19.4 . 1 322 179 75 ALA N N 124.3 . 1 323 180 76 VAL H H 7.89 . 1 324 180 76 VAL C C 176.4 . 1 325 180 76 VAL CA C 62.7 . 1 326 180 76 VAL CB C 32.8 . 1 327 180 76 VAL N N 118.7 . 1 328 181 77 SER H H 8.09 . 1 329 181 77 SER C C 174.2 . 1 330 181 77 SER CA C 58.4 . 1 331 181 77 SER CB C 64.1 . 1 332 181 77 SER N N 119.1 . 1 333 182 78 ALA H H 8.09 . 1 334 182 78 ALA C C 176.3 . 1 335 182 78 ALA CA C 52.5 . 1 336 182 78 ALA CB C 19.8 . 1 337 182 78 ALA N N 127.1 . 1 338 183 79 ALA H H 7.74 . 1 339 183 79 ALA C C 182.5 . 1 340 183 79 ALA CA C 53.8 . 1 341 183 79 ALA CB C 20.3 . 1 342 183 79 ALA N N 129.2 . 1 stop_ save_