data_27024 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Ascl1 fragment B ; _BMRB_accession_number 27024 _BMRB_flat_file_name bmr27024.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 B 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" 97 "13C chemical shifts" 315 "15N chemical shifts" 97 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' 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 B' $Ascl1_fragment_B 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 B is composed of a 9 aa tag at the N-terminus followed by residues 1-117 of the full length sequence. ; save_ ######################## # Monomeric polymers # ######################## save_Ascl1_fragment_B _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Ascl1_fragment_B _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'N-terminal domain of Ascl1 bHLH transcription factor, containing a polyA/polyQ stretch and a disordered region.' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 126 _Mol_residue_sequence ; MASHHHHHHMESSAKMESGG AGQQPQPQPQQPFLPPAACF FATAAAAAAAAAAAAAQSAQ QQQQQQQQQQQAPQLRPAAD GQPSGGGHKSAPKQVKRQRS SSPELMRCKRRLNFSGFGYS LPQQQP ; 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 88 79 HIS 89 80 LYS 90 81 SER 91 82 ALA 92 83 PRO 93 84 LYS 94 85 GLN 95 86 VAL 96 87 LYS 97 88 ARG 98 89 GLN 99 90 ARG 100 91 SER 101 92 SER 102 93 SER 103 94 PRO 104 95 GLU 105 96 LEU 106 97 MET 107 98 ARG 108 99 CYS 109 100 LYS 110 101 ARG 111 102 ARG 112 103 LEU 113 104 ASN 114 105 PHE 115 106 SER 116 107 GLY 117 108 PHE 118 109 GLY 119 110 TYR 120 111 SER 121 112 LEU 122 113 PRO 123 114 GLN 124 115 GLN 125 116 GLN 126 117 PRO 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_B 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_B '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_B 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 "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 B' _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 . 1 347 79 88 HIS H H 8.28 . 1 348 79 88 HIS C C 177.86 . 1 349 79 88 HIS CA C 56.08 . 1 350 79 88 HIS CB C 30.44 . 1 351 79 88 HIS N N 119.26 . 1 352 80 89 LYS H H 8.4 . 1 353 80 89 LYS C C 176.8 . 1 354 80 89 LYS CA C 56.23 . 1 355 80 89 LYS CB C 33.04 . 1 356 80 89 LYS N N 123.31 . 1 357 81 90 SER H H 8.38 . 1 358 81 90 SER C C 179.52 . 1 359 81 90 SER CA C 58.06 . 1 360 81 90 SER CB C 63.89 . 1 361 81 90 SER N N 117.54 . 1 362 82 91 ALA H H 8.39 . 1 363 82 91 ALA C C 177.83 . 1 364 82 91 ALA CA C 50.55 . 1 365 82 91 ALA CB C 18.09 . 1 366 82 91 ALA N N 127.4 . 1 367 83 92 PRO C C 176.31 . 1 368 83 92 PRO CA C 62.94 . 1 369 83 92 PRO CB C 32.22 . 1 370 84 93 LYS H H 8.48 . 1 371 84 93 LYS C C 176.6 . 1 372 84 93 LYS CA C 56.23 . 1 373 84 93 LYS CB C 33.01 . 1 374 84 93 LYS N N 121.88 . 1 375 85 94 GLN H H 8.47 . 1 376 85 94 GLN C C 177.43 . 1 377 85 94 GLN CA C 55.53 . 1 378 85 94 GLN CB C 29.56 . 1 379 85 94 GLN N N 122.24 . 1 380 86 95 VAL H H 8.34 . 1 381 86 95 VAL C C 177.24 . 1 382 86 95 VAL CA C 62.24 . 1 383 86 95 VAL CB C 32.92 . 1 384 86 95 VAL N N 123.02 . 1 385 87 96 LYS H H 8.49 . 1 386 87 96 LYS C C 176.94 . 1 387 87 96 LYS CA C 56.21 . 1 388 87 96 LYS CB C 33.08 . 1 389 87 96 LYS N N 126.1 . 1 390 88 97 ARG H H 8.48 . 1 391 88 97 ARG C C 177.1 . 1 392 88 97 ARG CA C 55.72 . 1 393 88 97 ARG CB C 30.9 . 1 394 88 97 ARG N N 123.64 . 1 395 89 98 GLN H H 8.56 . 1 396 89 98 GLN C C 177.32 . 1 397 89 98 GLN CA C 56.02 . 1 398 89 98 GLN CB C 29.61 . 1 399 89 98 GLN N N 122.71 . 1 400 90 99 ARG H H 8.58 . 1 401 90 99 ARG C C 176.87 . 1 402 90 99 ARG CA C 56.14 . 1 403 90 99 ARG CB C 30.94 . 1 404 90 99 ARG N N 123.37 . 1 405 91 100 SER H H 8.5 . 1 406 91 100 SER C C 178.77 . 1 407 91 100 SER CA C 58.29 . 1 408 91 100 SER CB C 63.87 . 1 409 91 100 SER N N 117.61 . 1 410 92 101 SER H H 8.44 . 1 411 92 101 SER C C 179.16 . 1 412 92 101 SER CA C 58.07 . 1 413 92 101 SER CB C 63.66 . 1 414 92 101 SER N N 117.93 . 1 415 93 102 SER H H 8.35 . 1 416 93 102 SER C C 180.19 . 1 417 93 102 SER CA C 56.5 . 1 418 93 102 SER CB C 63.26 . 1 419 93 102 SER N N 118.71 . 1 420 94 103 PRO C C 175.81 . 1 421 94 103 PRO CA C 63.84 . 1 422 94 103 PRO CB C 32 . 1 423 95 104 GLU H H 8.61 . 1 424 95 104 GLU C C 176.22 . 1 425 95 104 GLU CA C 57.2 . 1 426 95 104 GLU CB C 29.78 . 1 427 95 104 GLU N N 120.45 . 1 428 96 105 LEU H H 8.11 . 1 429 96 105 LEU C C 175.44 . 1 430 96 105 LEU CA C 55.31 . 1 431 96 105 LEU CB C 42.14 . 1 432 96 105 LEU N N 122.52 . 1 433 97 106 MET H H 8.2 . 1 434 97 106 MET C C 176.69 . 1 435 97 106 MET CA C 55.9 . 1 436 97 106 MET CB C 32.53 . 1 437 97 106 MET N N 120.15 . 1 438 98 107 ARG H H 8.23 . 1 439 98 107 ARG C C 176.88 . 1 440 98 107 ARG CA C 56.49 . 1 441 98 107 ARG CB C 30.59 . 1 442 98 107 ARG N N 121.7 . 1 443 100 109 LYS C C 176.84 . 1 444 100 109 LYS CA C 56.3 . 1 445 100 109 LYS CB C 32.85 . 1 446 101 110 ARG H H 8.31 . 1 447 101 110 ARG C C 177.31 . 1 448 101 110 ARG CA C 56.15 . 1 449 101 110 ARG CB C 30.86 . 1 450 101 110 ARG N N 122.63 . 1 451 102 111 ARG H H 8.45 . 1 452 102 111 ARG C C 177.19 . 1 453 102 111 ARG CA C 55.92 . 1 454 102 111 ARG CB C 30.88 . 1 455 102 111 ARG N N 123.32 . 1 456 103 112 LEU H H 8.46 . 1 457 103 112 LEU C C 177.03 . 1 458 103 112 LEU CA C 55.21 . 1 459 103 112 LEU CB C 42.43 . 1 460 103 112 LEU N N 124.49 . 1 461 104 113 ASN H H 7.96 . 1 462 104 113 ASN C C 173.81 . 1 463 104 113 ASN CA C 54.52 . 1 464 104 113 ASN CB C 40.2 . 1 465 104 113 ASN N N 123.94 . 1 466 107 116 GLY C C 179.53 . 1 467 107 116 GLY CA C 45.11 . 1 468 108 117 PHE H H 8.14 . 1 469 108 117 PHE C C 176.98 . 1 470 108 117 PHE CA C 58.04 . 1 471 108 117 PHE CB C 39.68 . 1 472 108 117 PHE N N 119.87 . 1 473 109 118 GLY H H 8.35 . 1 474 109 118 GLY C C 179.7 . 1 475 109 118 GLY CA C 45.16 . 1 476 109 118 GLY N N 110.58 . 1 477 110 119 TYR H H 7.95 . 1 478 110 119 TYR C C 177.59 . 1 479 110 119 TYR CA C 57.75 . 1 480 110 119 TYR CB C 39.09 . 1 481 110 119 TYR N N 119.75 . 1 482 111 120 SER H H 8.22 . 1 483 111 120 SER C C 179.65 . 1 484 111 120 SER CA C 57.82 . 1 485 111 120 SER CB C 63.99 . 1 486 111 120 SER N N 117.76 . 1 487 112 121 LEU H H 8.24 . 1 488 112 121 LEU C C 177.93 . 1 489 112 121 LEU CA C 53.18 . 1 490 112 121 LEU CB C 41.66 . 1 491 112 121 LEU N N 125.12 . 1 492 113 122 PRO C C 176.38 . 1 493 113 122 PRO CA C 63.15 . 1 494 113 122 PRO CB C 31.85 . 1 495 114 123 GLN H H 8.49 . 1 496 114 123 GLN C C 177.29 . 1 497 114 123 GLN CA C 55.78 . 1 498 114 123 GLN CB C 29.64 . 1 499 114 123 GLN N N 120.46 . 1 500 115 124 GLN H H 8.45 . 1 501 115 124 GLN C C 177.68 . 1 502 115 124 GLN CA C 55.6 . 1 503 115 124 GLN CB C 29.36 . 1 504 115 124 GLN N N 122.1 . 1 505 116 125 GLN H H 8.49 . 1 506 116 125 GLN C C 180.08 . 1 507 116 125 GLN CA C 53.53 . 1 508 116 125 GLN CB C 28.86 . 1 509 116 125 GLN N N 123.66 . 1 stop_ save_