data_27023 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Ascl1_fragment_A ; _BMRB_accession_number 27023 _BMRB_flat_file_name bmr27023.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 A 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" 212 "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 27024 'Ascl1 fragment B' 27025 'Ascl1 fragment C' 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 A' $Ascl1_fragment_A 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 A is composed of a 9 aa tag at the N-terminus followed by residues 1-78 of the full length sequence. ; save_ ######################## # Monomeric polymers # ######################## save_Ascl1_fragment_A _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Ascl1_fragment_A _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'N-terminal polyA/polyQ region of the bHLH transcription factor Ascl1' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 87 _Mol_residue_sequence ; MASHHHHHHMESSAKMESGG AGQQPQPQPQQPFLPPAACF FATAAAAAAAAAAAAAQSAQ QQQQQQQQQQQAPQLRPAAD GQPSGGG ; 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 1 MET 11 2 GLU 12 3 SER 13 4 SER 14 5 ALA 15 6 LYS 16 7 MET 17 8 GLU 18 9 SER 19 10 GLY 20 11 GLY 21 12 ALA 22 13 GLY 23 14 GLN 24 15 GLN 25 16 PRO 26 17 GLN 27 18 PRO 28 19 GLN 29 20 PRO 30 21 GLN 31 22 GLN 32 23 PRO 33 24 PHE 34 25 LEU 35 26 PRO 36 27 PRO 37 28 ALA 38 29 ALA 39 30 CYS 40 31 PHE 41 32 PHE 42 33 ALA 43 34 THR 44 35 ALA 45 36 ALA 46 37 ALA 47 38 ALA 48 39 ALA 49 40 ALA 50 41 ALA 51 42 ALA 52 43 ALA 53 44 ALA 54 45 ALA 55 46 ALA 56 47 ALA 57 48 GLN 58 49 SER 59 50 ALA 60 51 GLN 61 52 GLN 62 53 GLN 63 54 GLN 64 55 GLN 65 56 GLN 66 57 GLN 67 58 GLN 68 59 GLN 69 60 GLN 70 61 GLN 71 62 GLN 72 63 ALA 73 64 PRO 74 65 GLN 75 66 LEU 76 67 ARG 77 68 PRO 78 69 ALA 79 70 ALA 80 71 ASP 81 72 GLY 82 73 GLN 83 74 PRO 84 75 SER 85 76 GLY 86 77 GLY 87 78 GLY 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_A 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_A '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_A 250 uM 100 400 '[U-100% 13C; U-100% 15N]' TRIS 50 mM . . 'natural abundance' TCEP 5 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 288 . 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 "entry_citation". 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 "entry_citation". ; 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 A' _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 10 MET H H 8.43 . 1 2 1 10 MET C C 177.13 . 1 3 1 10 MET CA C 55.38 . 1 4 1 10 MET CB C 32.83 . 1 5 1 10 MET N N 122.35 . 1 6 2 11 GLU H H 8.58 . 1 7 2 11 GLU C C 176.57 . 1 8 2 11 GLU CA C 56.62 . 1 9 2 11 GLU CB C 30.19 . 1 10 2 11 GLU N N 122.7 . 1 11 3 12 SER H H 8.46 . 1 12 3 12 SER C C 178.44 . 1 13 3 12 SER CA C 58.45 . 1 14 3 12 SER CB C 63.78 . 1 15 3 12 SER N N 117.01 . 1 16 4 13 SER H H 8.38 . 1 17 4 13 SER C C 178.88 . 1 18 4 13 SER CA C 58.52 . 1 19 4 13 SER CB C 63.67 . 1 20 4 13 SER N N 118.07 . 1 21 5 14 ALA H H 8.27 . 1 22 5 14 ALA C C 175.53 . 1 23 5 14 ALA CA C 52.65 . 1 24 5 14 ALA CB C 19.1 . 1 25 5 14 ALA N N 125.85 . 1 26 6 15 LYS H H 8.25 . 1 27 6 15 LYS C C 176.58 . 1 28 6 15 LYS CA C 56.24 . 1 29 6 15 LYS CB C 32.83 . 1 30 6 15 LYS N N 120.53 . 1 31 7 16 MET H H 8.4 . 1 32 7 16 MET C C 176.86 . 1 33 7 16 MET CA C 55.48 . 1 34 7 16 MET CB C 32.8 . 1 35 7 16 MET N N 122.05 . 1 36 8 17 GLU H H 8.55 . 1 37 8 17 GLU C C 176.6 . 1 38 8 17 GLU CA C 56.51 . 1 39 8 17 GLU CB C 30.24 . 1 40 8 17 GLU N N 122.75 . 1 41 9 18 SER H H 8.46 . 1 42 9 18 SER C C 178.02 . 1 43 9 18 SER CA C 58.49 . 1 44 9 18 SER CB C 63.74 . 1 45 9 18 SER N N 117.04 . 1 46 10 19 GLY H H 8.51 . 1 47 10 19 GLY C C 178.47 . 1 48 10 19 GLY CA C 45.41 . 1 49 10 19 GLY N N 110.98 . 1 50 11 20 GLY H H 8.3 . 1 51 11 20 GLY C C 179.11 . 1 52 11 20 GLY CA C 45.13 . 1 53 11 20 GLY N N 108.8 . 1 54 12 21 ALA H H 8.34 . 1 55 12 21 ALA C C 174.73 . 1 56 12 21 ALA CA C 52.72 . 1 57 12 21 ALA CB C 19.05 . 1 58 12 21 ALA N N 123.86 . 1 59 13 22 GLY H H 8.48 . 1 60 13 22 GLY C C 179.07 . 1 61 13 22 GLY CA C 45.2 . 1 62 13 22 GLY N N 108.18 . 1 63 14 23 GLN H H 8.18 . 1 64 14 23 GLN C C 177.29 . 1 65 14 23 GLN CA C 55.59 . 1 66 14 23 GLN CB C 29.54 . 1 67 14 23 GLN N N 119.57 . 1 68 15 24 GLN H H 8.52 . 1 69 15 24 GLN C C 179.26 . 1 70 15 24 GLN CA C 53.6 . 1 71 15 24 GLN CB C 28.84 . 1 72 15 24 GLN N N 123.1 . 1 73 20 29 PRO C C 176.43 . 1 74 20 29 PRO CA C 63.01 . 1 75 20 29 PRO CB C 32.03 . 1 76 21 30 GLN H H 8.56 . 1 77 21 30 GLN C C 177.36 . 1 78 21 30 GLN CA C 55.74 . 1 79 21 30 GLN CB C 29.62 . 1 80 21 30 GLN N N 120.88 . 1 81 22 31 GLN H H 8.47 . 1 82 22 31 GLN C C 179.29 . 1 83 22 31 GLN CA C 53.58 . 1 84 22 31 GLN CB C 29.03 . 1 85 22 31 GLN N N 122.97 . 1 86 23 32 PRO C C 177.02 . 1 87 23 32 PRO CA C 63.06 . 1 88 23 32 PRO CB C 31.97 . 1 89 24 33 PHE H H 8.29 . 1 90 24 33 PHE C C 178.27 . 1 91 24 33 PHE CA C 57.47 . 1 92 24 33 PHE CB C 39.41 . 1 93 24 33 PHE N N 120.59 . 1 94 25 34 LEU H H 8.07 . 1 95 25 34 LEU C C 179.41 . 1 96 25 34 LEU CA C 52.08 . 1 97 25 34 LEU CB C 42.24 . 1 98 25 34 LEU N N 126.89 . 1 99 27 36 PRO C C 176.38 . 1 100 27 36 PRO CA C 63.09 . 1 101 27 36 PRO CB C 32 . 1 102 28 37 ALA H H 8.37 . 1 103 28 37 ALA C C 175.41 . 1 104 28 37 ALA CA C 52.53 . 1 105 28 37 ALA CB C 19.18 . 1 106 28 37 ALA N N 123.74 . 1 107 29 38 ALA H H 8.29 . 1 108 29 38 ALA C C 175.34 . 1 109 29 38 ALA CA C 52.8 . 1 110 29 38 ALA CB C 19.03 . 1 111 29 38 ALA N N 122.7 . 1 112 30 39 CYS H H 8.15 . 1 113 30 39 CYS C C 178.91 . 1 114 30 39 CYS CA C 58.52 . 1 115 30 39 CYS CB C 27.94 . 1 116 30 39 CYS N N 117.78 . 1 117 31 40 PHE H H 8.17 . 1 118 31 40 PHE C C 177.76 . 1 119 31 40 PHE CA C 58.31 . 1 120 31 40 PHE CB C 39.59 . 1 121 31 40 PHE N N 122.91 . 1 122 32 41 PHE H H 8.1 . 1 123 32 41 PHE C C 177.3 . 1 124 32 41 PHE CA C 57.98 . 1 125 32 41 PHE CB C 40.05 . 1 126 32 41 PHE N N 121.08 . 1 127 33 42 ALA H H 8.47 . 1 128 33 42 ALA C C 174.68 . 1 129 33 42 ALA CA C 53.49 . 1 130 33 42 ALA CB C 19.1 . 1 131 33 42 ALA N N 124.58 . 1 132 34 43 THR H H 7.79 . 1 133 34 43 THR C C 177.83 . 1 134 34 43 THR CA C 61.9 . 1 135 34 43 THR CB C 70.72 . 1 136 34 43 THR N N 110.31 . 1 137 35 44 ALA H H 8.52 . 1 138 35 44 ALA C C 173.01 . 1 139 35 44 ALA CA C 54.5 . 1 140 35 44 ALA CB C 17.99 . 1 141 35 44 ALA N N 125.54 . 1 142 36 45 ALA H H 8.36 . 1 143 36 45 ALA C C 172.96 . 1 144 36 45 ALA CA C 54.56 . 1 145 36 45 ALA CB C 18.08 . 1 146 36 45 ALA N N 122.12 . 1 147 37 46 ALA H H 8.1 . 1 148 37 46 ALA C C 172.89 . 1 149 37 46 ALA CA C 54.46 . 1 150 37 46 ALA CB C 18.11 . 1 151 37 46 ALA N N 122.71 . 1 152 38 47 ALA H H 7.97 . 1 153 38 47 ALA C C 172.93 . 1 154 38 47 ALA CA C 54.51 . 1 155 38 47 ALA CB C 17.98 . 1 156 38 47 ALA N N 122.7 . 1 157 39 48 ALA H H 8.15 . 1 158 39 48 ALA C C 172.73 . 1 159 39 48 ALA CA C 54.58 . 1 160 39 48 ALA CB C 17.79 . 1 161 39 48 ALA N N 122.34 . 1 162 40 49 ALA H H 8.08 . 1 163 40 49 ALA C C 172.76 . 1 164 40 49 ALA CA C 54.62 . 1 165 40 49 ALA CB C 17.95 . 1 166 40 49 ALA N N 122.5 . 1 167 41 50 ALA H H 7.96 . 1 168 41 50 ALA C C 172.8 . 1 169 41 50 ALA CA C 54.57 . 1 170 41 50 ALA CB C 18.11 . 1 171 41 50 ALA N N 122.37 . 1 172 42 51 ALA H H 8.02 . 1 173 42 51 ALA C C 172.85 . 1 174 42 51 ALA CA C 54.54 . 1 175 42 51 ALA CB C 17.9 . 1 176 42 51 ALA N N 122.37 . 1 177 43 52 ALA H H 8.07 . 1 178 43 52 ALA C C 172.94 . 1 179 43 52 ALA CA C 54.5 . 1 180 43 52 ALA CB C 17.74 . 1 181 43 52 ALA N N 122.17 . 1 182 44 53 ALA H H 8.02 . 1 183 44 53 ALA C C 173.28 . 1 184 44 53 ALA CA C 54.42 . 1 185 44 53 ALA CB C 17.98 . 1 186 44 53 ALA N N 122.2 . 1 187 45 54 ALA H H 7.97 . 1 188 45 54 ALA C C 173.29 . 1 189 45 54 ALA CA C 54.28 . 1 190 45 54 ALA CB C 18.08 . 1 191 45 54 ALA N N 121.58 . 1 192 46 55 ALA H H 7.97 . 1 193 46 55 ALA C C 173.62 . 1 194 46 55 ALA CA C 54.08 . 1 195 46 55 ALA CB C 18.2 . 1 196 46 55 ALA N N 121.62 . 1 197 47 56 ALA H H 7.92 . 1 198 47 56 ALA C C 173.7 . 1 199 47 56 ALA CA C 54.05 . 1 200 47 56 ALA CB C 18.05 . 1 201 47 56 ALA N N 121.68 . 1 202 48 57 GLN H H 8.02 . 1 203 48 57 GLN C C 175.52 . 1 204 48 57 GLN CA C 57.57 . 1 205 48 57 GLN CB C 28.78 . 1 206 48 57 GLN N N 118.61 . 1 207 49 58 SER H H 8.19 . 1 208 49 58 SER C C 177.41 . 1 209 49 58 SER CA C 60.06 . 1 210 49 58 SER CB C 63.23 . 1 211 49 58 SER N N 115.8 . 1 212 50 59 ALA H H 8.13 . 1 213 50 59 ALA C C 173.97 . 1 214 50 59 ALA CA C 54.08 . 1 215 50 59 ALA CB C 18.28 . 1 216 50 59 ALA N N 124.41 . 1 217 51 60 GLN H H 8.07 . 1 218 51 60 GLN C C 175.78 . 1 219 51 60 GLN CA C 57.44 . 1 220 51 60 GLN CB C 28.78 . 1 221 51 60 GLN N N 118.39 . 1 222 52 61 GLN H H 8.18 . 1 223 52 61 GLN C C 175.84 . 1 224 52 61 GLN CA C 57.34 . 1 225 52 61 GLN CB C 28.82 . 1 226 52 61 GLN N N 120.12 . 1 227 53 62 GLN H H 8.26 . 1 228 53 62 GLN C C 176.03 . 1 229 53 62 GLN CA C 57.18 . 1 230 53 62 GLN CB C 28.87 . 1 231 53 62 GLN N N 120.05 . 1 232 54 63 GLN H H 8.22 . 1 233 54 63 GLN C C 176.12 . 1 234 54 63 GLN CA C 57.07 . 1 235 54 63 GLN CB C 28.9 . 1 236 54 63 GLN N N 120.28 . 1 237 55 64 GLN H H 8.29 . 1 238 55 64 GLN C C 176.22 . 1 239 55 64 GLN CA C 56.89 . 1 240 55 64 GLN CB C 28.92 . 1 241 55 64 GLN N N 120.34 . 1 242 56 65 GLN H H 8.3 . 1 243 56 65 GLN C C 176.36 . 1 244 56 65 GLN CA C 56.78 . 1 245 56 65 GLN CB C 28.95 . 1 246 56 65 GLN N N 120.44 . 1 247 57 66 GLN H H 8.31 . 1 248 57 66 GLN C C 176.49 . 1 249 57 66 GLN CA C 56.68 . 1 250 57 66 GLN CB C 28.97 . 1 251 57 66 GLN N N 120.53 . 1 252 58 67 GLN H H 8.33 . 1 253 58 67 GLN C C 176.63 . 1 254 58 67 GLN CA C 56.57 . 1 255 58 67 GLN CB C 29.01 . 1 256 58 67 GLN N N 120.64 . 1 257 59 68 GLN H H 8.35 . 1 258 59 68 GLN C C 176.79 . 1 259 59 68 GLN CA C 56.37 . 1 260 59 68 GLN CB C 29.11 . 1 261 59 68 GLN N N 120.78 . 1 262 60 69 GLN H H 8.37 . 1 263 60 69 GLN C C 177.03 . 1 264 60 69 GLN CA C 56.14 . 1 265 60 69 GLN CB C 29.24 . 1 266 60 69 GLN N N 121 . 1 267 61 70 GLN H H 8.39 . 1 268 61 70 GLN C C 177.29 . 1 269 61 70 GLN CA C 55.87 . 1 270 61 70 GLN CB C 29.35 . 1 271 61 70 GLN N N 121.25 . 1 272 62 71 GLN H H 8.39 . 1 273 62 71 GLN C C 177.86 . 1 274 62 71 GLN CA C 55.5 . 1 275 62 71 GLN CB C 29.65 . 1 276 62 71 GLN N N 121.52 . 1 277 63 72 ALA H H 8.41 . 1 278 63 72 ALA C C 177.72 . 1 279 63 72 ALA CA C 50.67 . 1 280 63 72 ALA CB C 17.87 . 1 281 63 72 ALA N N 127.07 . 1 282 64 73 PRO C C 176.36 . 1 283 64 73 PRO CA C 63.09 . 1 284 64 73 PRO CB C 31.92 . 1 285 65 74 GLN H H 8.53 . 1 286 65 74 GLN C C 177.35 . 1 287 65 74 GLN CA C 55.64 . 1 288 65 74 GLN CB C 29.48 . 1 289 65 74 GLN N N 120.61 . 1 290 66 75 LEU H H 8.34 . 1 291 66 75 LEU C C 176.25 . 1 292 66 75 LEU CA C 54.99 . 1 293 66 75 LEU CB C 42.29 . 1 294 66 75 LEU N N 124.13 . 1 295 67 76 ARG H H 8.37 . 1 296 67 76 ARG C C 179.26 . 1 297 67 76 ARG CA C 53.69 . 1 298 67 76 ARG CB C 30.12 . 1 299 67 76 ARG N N 123.31 . 1 300 68 77 PRO C C 176.57 . 1 301 68 77 PRO CA C 62.95 . 1 302 68 77 PRO CB C 32.11 . 1 303 69 78 ALA H H 8.49 . 1 304 69 78 ALA C C 175.4 . 1 305 69 78 ALA CA C 52.43 . 1 306 69 78 ALA CB C 19.17 . 1 307 69 78 ALA N N 124.88 . 1 308 70 79 ALA H H 8.4 . 1 309 70 79 ALA C C 175.68 . 1 310 70 79 ALA CA C 52.51 . 1 311 70 79 ALA CB C 19.08 . 1 312 70 79 ALA N N 123.52 . 1 313 71 80 ASP H H 8.26 . 1 314 71 80 ASP C C 176.36 . 1 315 71 80 ASP CA C 54.34 . 1 316 71 80 ASP CB C 41.06 . 1 317 71 80 ASP N N 119.25 . 1 318 72 81 GLY H H 8.3 . 1 319 72 81 GLY C C 179.19 . 1 320 72 81 GLY CA C 45.27 . 1 321 72 81 GLY N N 108.98 . 1 322 73 82 GLN H H 8.2 . 1 323 73 82 GLN C C 179.03 . 1 324 73 82 GLN CA C 53.61 . 1 325 73 82 GLN CB C 28.73 . 1 326 73 82 GLN N N 120.59 . 1 327 74 83 PRO C C 176.04 . 1 328 74 83 PRO CA C 63 . 1 329 74 83 PRO CB C 32.01 . 1 330 75 84 SER H H 8.57 . 1 331 75 84 SER C C 177.83 . 1 332 75 84 SER CA C 58.48 . 1 333 75 84 SER CB C 63.85 . 1 334 75 84 SER N N 116.54 . 1 335 76 85 GLY H H 8.54 . 1 336 76 85 GLY C C 178.41 . 1 337 76 85 GLY CA C 45.41 . 1 338 76 85 GLY N N 111.16 . 1 339 77 86 GLY H H 8.35 . 1 340 77 86 GLY C C 178.49 . 1 341 77 86 GLY CA C 45.22 . 1 342 77 86 GLY N N 108.6 . 1 343 78 87 GLY H H 8.35 . 1 344 78 87 GLY C C 179.21 . 1 345 78 87 GLY CA C 45.14 . 1 346 78 87 GLY N N 108.59 . 1 stop_ save_