data_27026 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Ascl1 fragment D ; _BMRB_accession_number 27026 _BMRB_flat_file_name bmr27026.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 D 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" 83 "13C chemical shifts" 237 "15N chemical shifts" 83 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' 27025 'Ascl1 fragment C' 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 D' $Ascl1_fragment_D 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 D is composed of a 44 aa tag at the N-terminus followed by residues 118-236 of the full length sequence. ; save_ ######################## # Monomeric polymers # ######################## save_Ascl1_fragment_D _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Ascl1_fragment_D _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function ; Basic Helix-Loop-Helix (bHLH) DNA binding domain and disordered C-terminal domain of Ascl1. Fragment 118-236 of the full length sequence. ; stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 163 _Mol_residue_sequence ; MSYYHHHHHHLESTSLYKKA GLYKKAGSAAAVLEENLYFQ GSFTAAVARRNERERNRVKL VNLGFATLREHVPNGAANKK MSKVETLRSAVEYIRALQQL LDEHDAVSAAFQAGVLSPTI SPNYSNDLNSMAGSPVSSYS SDEGSYDPLSPEEQELLDFT NWF ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -43 MET 2 -42 SER 3 -41 TYR 4 -40 TYR 5 -39 HIS 6 -38 HIS 7 -37 HIS 8 -36 HIS 9 -35 HIS 10 -34 HIS 11 -33 LEU 12 -32 GLU 13 -31 SER 14 -30 THR 15 -29 SER 16 -28 LEU 17 -27 TYR 18 -26 LYS 19 -25 LYS 20 -24 ALA 21 -23 GLY 22 -22 LEU 23 -21 TYR 24 -20 LYS 25 -19 LYS 26 -18 ALA 27 -17 GLY 28 -16 SER 29 -15 ALA 30 -14 ALA 31 -13 ALA 32 -12 VAL 33 -11 LEU 34 -10 GLU 35 -9 GLU 36 -8 ASN 37 -7 LEU 38 -6 TYR 39 -5 PHE 40 -4 GLN 41 -3 GLY 42 -2 SER 43 -1 PHE 44 0 THR 45 118 ALA 46 119 ALA 47 120 VAL 48 121 ALA 49 122 ARG 50 123 ARG 51 124 ASN 52 125 GLU 53 126 ARG 54 127 GLU 55 128 ARG 56 129 ASN 57 130 ARG 58 131 VAL 59 132 LYS 60 133 LEU 61 134 VAL 62 135 ASN 63 136 LEU 64 137 GLY 65 138 PHE 66 139 ALA 67 140 THR 68 141 LEU 69 142 ARG 70 143 GLU 71 144 HIS 72 145 VAL 73 146 PRO 74 147 ASN 75 148 GLY 76 149 ALA 77 150 ALA 78 151 ASN 79 152 LYS 80 153 LYS 81 154 MET 82 155 SER 83 156 LYS 84 157 VAL 85 158 GLU 86 159 THR 87 160 LEU 88 161 ARG 89 162 SER 90 163 ALA 91 164 VAL 92 165 GLU 93 166 TYR 94 167 ILE 95 168 ARG 96 169 ALA 97 170 LEU 98 171 GLN 99 172 GLN 100 173 LEU 101 174 LEU 102 175 ASP 103 176 GLU 104 177 HIS 105 178 ASP 106 179 ALA 107 180 VAL 108 181 SER 109 182 ALA 110 183 ALA 111 184 PHE 112 185 GLN 113 186 ALA 114 187 GLY 115 188 VAL 116 189 LEU 117 190 SER 118 191 PRO 119 192 THR 120 193 ILE 121 194 SER 122 195 PRO 123 196 ASN 124 197 TYR 125 198 SER 126 199 ASN 127 200 ASP 128 201 LEU 129 202 ASN 130 203 SER 131 204 MET 132 205 ALA 133 206 GLY 134 207 SER 135 208 PRO 136 209 VAL 137 210 SER 138 211 SER 139 212 TYR 140 213 SER 141 214 SER 142 215 ASP 143 216 GLU 144 217 GLY 145 218 SER 146 219 TYR 147 220 ASP 148 221 PRO 149 222 LEU 150 223 SER 151 224 PRO 152 225 GLU 153 226 GLU 154 227 GLN 155 228 GLU 156 229 LEU 157 230 LEU 158 231 ASP 159 232 PHE 160 233 THR 161 234 ASN 162 235 TRP 163 236 PHE 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_D 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_D '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_D 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 298 . 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 D' _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 1 118 45 ALA H H 7.74 . 1 2 118 45 ALA C C 179.42 . 1 3 118 45 ALA CA C 54.50 . 1 4 118 45 ALA CB C 18.27 . 1 5 118 45 ALA N N 124.31 . 1 6 119 46 ALA H H 7.72 . 1 7 119 46 ALA C C 179.46 . 1 8 119 46 ALA CA C 54.80 . 1 9 119 46 ALA CB C 18.38 . 1 10 119 46 ALA N N 122.11 . 1 11 120 47 VAL H H 7.77 . 1 12 120 47 VAL C C 177.79 . 1 13 120 47 VAL CA C 65.70 . 1 14 120 47 VAL N N 117.63 . 1 15 121 48 ALA H H 7.63 . 1 16 121 48 ALA C C 179.60 . 1 17 121 48 ALA CA C 54.40 . 1 18 121 48 ALA CB C 18.24 . 1 19 121 48 ALA N N 122.45 . 1 20 122 49 ARG H H 7.68 . 1 21 122 49 ARG C C 178.19 . 1 22 122 49 ARG CA C 57.81 . 1 23 122 49 ARG CB C 30.33 . 1 24 122 49 ARG N N 117.88 . 1 25 123 50 ARG H H 7.80 . 1 26 123 50 ARG C C 177.49 . 1 27 123 50 ARG CA C 58.20 . 1 28 123 50 ARG CB C 29.66 . 1 29 123 50 ARG N N 120.35 . 1 30 124 51 ASN H H 8.05 . 1 31 124 51 ASN C C 175.99 . 1 32 124 51 ASN CA C 54.54 . 1 33 124 51 ASN CB C 38.72 . 1 34 124 51 ASN N N 117.46 . 1 35 125 52 GLU H H 7.81 . 1 36 125 52 GLU C C 176.36 . 1 37 125 52 GLU CB C 29.89 . 1 38 125 52 GLU N N 119.31 . 1 39 126 53 ARG H H 7.54 . 1 40 126 53 ARG C C 175.87 . 1 41 126 53 ARG CB C 30.93 . 1 42 126 53 ARG N N 120.46 . 1 43 127 54 GLU H H 8.32 . 1 44 127 54 GLU C C 176.15 . 1 45 127 54 GLU CA C 56.50 . 1 46 127 54 GLU CB C 29.98 . 1 47 127 54 GLU N N 122.57 . 1 48 128 55 ARG H H 8.17 . 1 49 128 55 ARG C C 175.86 . 1 50 128 55 ARG CA C 55.90 . 1 51 128 55 ARG CB C 30.43 . 1 52 128 55 ARG N N 122.22 . 1 53 129 56 ASN H H 8.28 . 1 54 129 56 ASN C C 174.98 . 1 55 129 56 ASN CB C 39.09 . 1 56 129 56 ASN N N 120.53 . 1 57 130 57 ARG H H 8.05 . 1 58 130 57 ARG C C 176.42 . 1 59 130 57 ARG CA C 56.80 . 1 60 130 57 ARG N N 121.09 . 1 61 131 58 VAL H H 7.80 . 1 62 131 58 VAL C C 175.74 . 1 63 131 58 VAL CB C 32.36 . 1 64 131 58 VAL N N 120.36 . 1 65 132 59 LYS H H 7.85 . 1 66 132 59 LYS C C 176.81 . 1 67 132 59 LYS CB C 32.46 . 1 68 132 59 LYS N N 122.52 . 1 69 133 60 LEU H H 8.08 . 1 70 133 60 LEU C C 176.53 . 1 71 133 60 LEU N N 119.77 . 1 72 137 64 GLY H H 8.07 . 1 73 137 64 GLY N N 108.08 . 1 74 138 65 PHE H H 8.19 . 1 75 138 65 PHE C C 176.83 . 1 76 138 65 PHE CB C 38.83 . 1 77 138 65 PHE N N 120.86 . 1 78 139 66 ALA H H 8.24 . 1 79 139 66 ALA C C 179.81 . 1 80 139 66 ALA CA C 55.10 . 1 81 139 66 ALA CB C 18.32 . 1 82 139 66 ALA N N 121.26 . 1 83 140 67 THR H H 7.76 . 1 84 140 67 THR C C 176.59 . 1 85 140 67 THR CA C 65.00 . 1 86 140 67 THR CB C 68.75 . 1 87 140 67 THR N N 113.21 . 1 88 141 68 LEU H H 7.83 . 1 89 141 68 LEU C C 178.53 . 1 90 141 68 LEU CB C 41.66 . 1 91 141 68 LEU N N 123.06 . 1 92 142 69 ARG H H 8.04 . 1 93 142 69 ARG C C 177.74 . 1 94 142 69 ARG CA C 58.80 . 1 95 142 69 ARG CB C 29.94 . 1 96 142 69 ARG N N 116.92 . 1 97 143 70 GLU H H 7.52 . 1 98 143 70 GLU C C 176.89 . 1 99 143 70 GLU CA C 57.40 . 1 100 143 70 GLU CB C 29.39 . 1 101 143 70 GLU N N 116.82 . 1 102 144 71 HIS H H 7.76 . 1 103 144 71 HIS C C 173.50 . 1 104 144 71 HIS CA C 55.90 . 1 105 144 71 HIS N N 115.82 . 1 106 145 72 VAL H H 7.44 . 1 107 145 72 VAL C C 174.16 . 1 108 145 72 VAL CA C 60.80 . 1 109 145 72 VAL N N 120.81 . 1 110 146 73 PRO C C 176.53 . 1 111 146 73 PRO CA C 63.50 . 1 112 146 73 PRO CB C 31.94 . 1 113 147 74 ASN H H 8.31 . 1 114 147 74 ASN C C 176.26 . 1 115 147 74 ASN CA C 53.90 . 1 116 147 74 ASN CB C 38.97 . 1 117 147 74 ASN N N 118.92 . 1 118 148 75 GLY H H 8.23 . 1 119 148 75 GLY C C 174.46 . 1 120 148 75 GLY CA C 45.90 . 1 121 148 75 GLY N N 109.88 . 1 122 149 76 ALA H H 7.91 . 1 123 149 76 ALA C C 177.81 . 1 124 149 76 ALA CA C 53.30 . 1 125 149 76 ALA CB C 18.77 . 1 126 149 76 ALA N N 123.37 . 1 127 151 78 ASN H H 7.96 . 1 128 151 78 ASN C C 175.48 . 1 129 151 78 ASN CA C 53.80 . 1 130 151 78 ASN N N 116.37 . 1 131 152 79 LYS H H 7.86 . 1 132 152 79 LYS C C 176.69 . 1 133 152 79 LYS CA C 56.70 . 1 134 152 79 LYS N N 120.56 . 1 135 179 106 ALA H H 8.19 . 1 136 179 106 ALA C C 179.33 . 1 137 179 106 ALA CA C 54.50 . 1 138 179 106 ALA N N 122.86 . 1 139 180 107 VAL H H 7.85 . 1 140 180 107 VAL C C 177.08 . 1 141 180 107 VAL CA C 65.60 . 1 142 180 107 VAL CB C 18.97 . 1 143 180 107 VAL N N 118.23 . 1 144 181 108 SER H H 7.96 . 1 145 181 108 SER C C 176.48 . 1 146 181 108 SER CA C 60.90 . 1 147 181 108 SER N N 115.10 . 1 148 182 109 ALA H H 7.89 . 1 149 182 109 ALA C C 179.57 . 1 150 182 109 ALA CA C 54.50 . 1 151 182 109 ALA CB C 18.41 . 1 152 182 109 ALA N N 123.69 . 1 153 183 110 ALA H H 7.79 . 1 154 183 110 ALA C C 179.03 . 1 155 183 110 ALA CA C 54.40 . 1 156 183 110 ALA CB C 18.47 . 1 157 183 110 ALA N N 121.63 . 1 158 184 111 PHE H H 7.97 . 1 159 184 111 PHE C C 177.82 . 1 160 184 111 PHE CA C 59.80 . 1 161 184 111 PHE CB C 39.17 . 1 162 184 111 PHE N N 117.61 . 1 163 185 112 GLN H H 8.12 . 1 164 185 112 GLN C C 176.74 . 1 165 185 112 GLN CA C 57.40 . 1 166 185 112 GLN CB C 28.92 . 1 167 185 112 GLN N N 119.44 . 1 168 186 113 ALA H H 7.79 . 1 169 186 113 ALA C C 178.34 . 1 170 186 113 ALA CA C 53.10 . 1 171 186 113 ALA CB C 19.00 . 1 172 186 113 ALA N N 121.38 . 1 173 187 114 GLY H H 7.85 . 1 174 187 114 GLY C C 174.73 . 1 175 187 114 GLY CA C 45.90 . 1 176 187 114 GLY N N 107.22 . 1 177 188 115 VAL H H 7.63 . 1 178 188 115 VAL C C 175.60 . 1 179 188 115 VAL CA C 63.20 . 1 180 188 115 VAL CB C 32.41 . 1 181 188 115 VAL N N 117.96 . 1 182 189 116 LEU H H 7.66 . 1 183 189 116 LEU C C 176.28 . 1 184 189 116 LEU CA C 54.60 . 1 185 189 116 LEU CB C 42.24 . 1 186 189 116 LEU N N 120.25 . 1 187 190 117 SER H H 7.78 . 1 188 190 117 SER C C 172.92 . 1 189 190 117 SER CA C 56.50 . 1 190 190 117 SER N N 116.01 . 1 191 191 118 PRO C C 176.92 . 1 192 191 118 PRO CA C 63.60 . 1 193 191 118 PRO CB C 31.93 . 1 194 192 119 THR H H 7.91 . 1 195 192 119 THR C C 174.38 . 1 196 192 119 THR CA C 62.50 . 1 197 192 119 THR CB C 69.44 . 1 198 192 119 THR N N 113.49 . 1 199 193 120 ILE H H 7.70 . 1 200 193 120 ILE C C 175.42 . 1 201 193 120 ILE CA C 60.90 . 1 202 193 120 ILE CB C 38.74 . 1 203 193 120 ILE N N 121.89 . 1 204 194 121 SER H H 8.03 . 1 205 194 121 SER C C 173.04 . 1 206 194 121 SER CA C 55.90 . 1 207 194 121 SER N N 119.42 . 1 208 195 122 PRO C C 176.49 . 1 209 195 122 PRO CA C 63.40 . 1 210 195 122 PRO CB C 31.94 . 1 211 196 123 ASN H H 8.15 . 1 212 196 123 ASN C C 174.97 . 1 213 196 123 ASN CA C 53.10 . 1 214 196 123 ASN CB C 38.76 . 1 215 196 123 ASN N N 118.10 . 1 216 197 124 TYR H H 7.81 . 1 217 197 124 TYR C C 175.82 . 1 218 197 124 TYR CA C 58.40 . 1 219 197 124 TYR CB C 38.65 . 1 220 197 124 TYR N N 121.37 . 1 221 198 125 SER H H 7.94 . 1 222 198 125 SER C C 174.10 . 1 223 198 125 SER CA C 58.20 . 1 224 198 125 SER CB C 63.83 . 1 225 198 125 SER N N 117.33 . 1 226 199 126 ASN H H 8.13 . 1 227 199 126 ASN C C 174.96 . 1 228 199 126 ASN CA C 53.40 . 1 229 199 126 ASN CB C 38.98 . 1 230 199 126 ASN N N 121.37 . 1 231 200 127 ASP H H 8.14 . 1 232 200 127 ASP C C 176.58 . 1 233 200 127 ASP CA C 54.50 . 1 234 200 127 ASP CB C 40.91 . 1 235 200 127 ASP N N 120.97 . 1 236 201 128 LEU H H 8.05 . 1 237 201 128 LEU C C 177.75 . 1 238 201 128 LEU CA C 56.00 . 1 239 201 128 LEU CB C 41.86 . 1 240 201 128 LEU N N 122.72 . 1 241 202 129 ASN H H 8.21 . 1 242 202 129 ASN C C 175.70 . 1 243 202 129 ASN CA C 53.70 . 1 244 202 129 ASN CB C 38.77 . 1 245 202 129 ASN N N 118.55 . 1 246 203 130 SER H H 7.97 . 1 247 203 130 SER C C 174.85 . 1 248 203 130 SER CA C 58.90 . 1 249 203 130 SER CB C 63.58 . 1 250 203 130 SER N N 116.16 . 1 251 204 131 MET H H 8.10 . 1 252 204 131 MET C C 176.10 . 1 253 204 131 MET CA C 55.62 . 1 254 204 131 MET CB C 32.59 . 1 255 204 131 MET N N 122.10 . 1 256 205 132 ALA H H 8.01 . 1 257 205 132 ALA C C 178.04 . 1 258 205 132 ALA CA C 52.74 . 1 259 205 132 ALA CB C 19.08 . 1 260 205 132 ALA N N 124.96 . 1 261 206 133 GLY H H 8.14 . 1 262 206 133 GLY C C 173.80 . 1 263 206 133 GLY CA C 44.95 . 1 264 206 133 GLY N N 108.37 . 1 265 207 134 SER H H 8.01 . 1 266 207 134 SER C C 172.66 . 1 267 207 134 SER CA C 56.37 . 1 268 207 134 SER N N 117.21 . 1 269 208 135 PRO C C 176.94 . 1 270 208 135 PRO CA C 63.16 . 1 271 208 135 PRO CB C 31.99 . 1 272 209 136 VAL H H 8.08 . 1 273 209 136 VAL C C 176.29 . 1 274 209 136 VAL CA C 62.28 . 1 275 209 136 VAL CB C 32.67 . 1 276 209 136 VAL N N 120.57 . 1 277 210 137 SER H H 8.22 . 1 278 210 137 SER C C 174.32 . 1 279 210 137 SER CA C 58.09 . 1 280 210 137 SER CB C 63.88 . 1 281 210 137 SER N N 119.78 . 1 282 211 138 SER H H 8.15 . 1 283 211 138 SER C C 173.84 . 1 284 211 138 SER CA C 58.14 . 1 285 211 138 SER CB C 63.78 . 1 286 211 138 SER N N 118.36 . 1 287 212 139 TYR H H 8.05 . 1 288 212 139 TYR C C 175.56 . 1 289 212 139 TYR CA C 57.91 . 1 290 212 139 TYR CB C 38.87 . 1 291 212 139 TYR N N 122.62 . 1 292 213 140 SER H H 8.06 . 1 293 213 140 SER C C 174.12 . 1 294 213 140 SER CA C 57.77 . 1 295 213 140 SER CB C 64.00 . 1 296 213 140 SER N N 118.42 . 1 297 214 141 SER H H 8.24 . 1 298 214 141 SER C C 174.24 . 1 299 214 141 SER CA C 58.26 . 1 300 214 141 SER CB C 63.85 . 1 301 214 141 SER N N 118.60 . 1 302 215 142 ASP H H 8.24 . 1 303 215 142 ASP C C 176.33 . 1 304 215 142 ASP CA C 54.39 . 1 305 215 142 ASP CB C 41.13 . 1 306 215 142 ASP N N 122.86 . 1 307 216 143 GLU H H 8.25 . 1 308 216 143 GLU C C 177.03 . 1 309 216 143 GLU CA C 56.95 . 1 310 216 143 GLU CB C 30.04 . 1 311 216 143 GLU N N 121.91 . 1 312 217 144 GLY H H 8.28 . 1 313 217 144 GLY C C 173.95 . 1 314 217 144 GLY CA C 45.28 . 1 315 217 144 GLY N N 110.15 . 1 316 218 145 SER H H 7.91 . 1 317 218 145 SER C C 173.78 . 1 318 218 145 SER CA C 57.97 . 1 319 218 145 SER CB C 63.88 . 1 320 218 145 SER N N 115.78 . 1 321 219 146 TYR H H 8.04 . 1 322 219 146 TYR C C 174.64 . 1 323 219 146 TYR CA C 57.37 . 1 324 219 146 TYR CB C 38.94 . 1 325 219 146 TYR N N 122.95 . 1 326 220 147 ASP H H 8.17 . 1 327 220 147 ASP C C 174.04 . 1 328 220 147 ASP CA C 51.58 . 1 329 220 147 ASP N N 125.32 . 1 330 221 148 PRO C C 176.85 . 1 331 221 148 PRO CA C 63.05 . 1 332 221 148 PRO CB C 32.09 . 1 333 222 149 LEU H H 8.13 . 1 334 222 149 LEU C C 177.39 . 1 335 222 149 LEU CA C 54.75 . 1 336 222 149 LEU CB C 42.09 . 1 337 222 149 LEU N N 121.53 . 1 338 223 150 SER H H 8.14 . 1 339 223 150 SER C C 172.91 . 1 340 223 150 SER CA C 56.40 . 1 341 223 150 SER N N 118.76 . 1 342 224 151 PRO C C 177.67 . 1 343 224 151 PRO CA C 64.01 . 1 344 224 151 PRO CB C 31.91 . 1 345 225 152 GLU H H 8.44 . 1 346 225 152 GLU C C 177.33 . 1 347 225 152 GLU CA C 57.65 . 1 348 225 152 GLU CB C 29.71 . 1 349 225 152 GLU N N 120.08 . 1 350 226 153 GLU H H 8.05 . 1 351 226 153 GLU C C 177.11 . 1 352 226 153 GLU CA C 57.08 . 1 353 226 153 GLU CB C 30.19 . 1 354 226 153 GLU N N 121.61 . 1 355 227 154 GLN H H 8.20 . 1 356 227 154 GLN C C 176.33 . 1 357 227 154 GLN CA C 56.50 . 1 358 227 154 GLN CB C 29.39 . 1 359 227 154 GLN N N 121.20 . 1 360 228 155 GLU H H 8.17 . 1 361 228 155 GLU C C 176.62 . 1 362 228 155 GLU CA C 57.11 . 1 363 228 155 GLU CB C 30.03 . 1 364 228 155 GLU N N 121.73 . 1 365 229 156 LEU H H 7.90 . 1 366 229 156 LEU C C 177.40 . 1 367 229 156 LEU CA C 55.35 . 1 368 229 156 LEU CB C 42.06 . 1 369 229 156 LEU N N 122.74 . 1 370 230 157 LEU H H 7.86 . 1 371 230 157 LEU C C 176.86 . 1 372 230 157 LEU CA C 55.19 . 1 373 230 157 LEU CB C 42.35 . 1 374 230 157 LEU N N 122.88 . 1 375 231 158 ASP H H 7.98 . 1 376 231 158 ASP C C 176.07 . 1 377 231 158 ASP CA C 54.13 . 1 378 231 158 ASP CB C 41.10 . 1 379 231 158 ASP N N 120.80 . 1 380 232 159 PHE H H 7.98 . 1 381 232 159 PHE C C 176.07 . 1 382 232 159 PHE CA C 57.97 . 1 383 232 159 PHE CB C 39.10 . 1 384 232 159 PHE N N 121.35 . 1 385 233 160 THR H H 7.92 . 1 386 233 160 THR C C 174.13 . 1 387 233 160 THR CA C 62.77 . 1 388 233 160 THR CB C 69.55 . 1 389 233 160 THR N N 115.53 . 1 390 234 161 ASN H H 7.97 . 1 391 234 161 ASN C C 174.40 . 1 392 234 161 ASN CA C 53.06 . 1 393 234 161 ASN CB C 38.91 . 1 394 234 161 ASN N N 120.82 . 1 395 235 162 TRP H H 7.70 . 1 396 235 162 TRP C C 174.72 . 1 397 235 162 TRP CA C 56.99 . 1 398 235 162 TRP CB C 29.67 . 1 399 235 162 TRP N N 121.74 . 1 400 236 163 PHE H H 7.34 . 1 401 236 163 PHE C C 179.93 . 1 402 236 163 PHE CA C 58.79 . 1 403 236 163 PHE N N 125.85 . 1 stop_ save_