data_34163 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of DNA-binding HU protein from micoplasma Spiroplasma melliferum ; _BMRB_accession_number 34163 _BMRB_flat_file_name bmr34163.str _Entry_type original _Submission_date 2017-07-13 _Accession_date 2017-07-13 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Altukhov D. A. . 2 Talyzina A. A. . 3 Agapova Y. K. . 4 Vlaskina A. V. . 5 Korzhenevskiy D. A. . 6 Bocharov E. V. . 7 Rakitina T. V. . 8 Timofeev V. I. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 123 "13C chemical shifts" 119 "15N chemical shifts" 78 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-08-23 update BMRB 'update entry citation' 2017-08-18 original author 'original release' stop_ _Original_release_date 2017-07-24 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural plasticity and thermal stability of the histone-like protein from Spiroplasma melliferum are due to phenylalanine insertions into the conservative scaffold ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29283021 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Timofeev Vladimir I. . 2 Altukhov Dmitry A. . 3 Talyzina Anna A. . 4 Agapova Yulia K. . 5 Vlaskina Anna V. . 6 Korzhenevskiy Dmitry A. . 7 Kleymenov 'Sergey Yu' Y. . 8 Bocharov Eduard V. . 9 Rakitina Tatiana V. . stop_ _Journal_abbreviation 'J. Biomol. Struct. Dyn.' _Journal_name_full 'Journal of biomolecular structure & dynamics' _Journal_volume 36 _Journal_issue 16 _Journal_ISSN 1538-0254 _Journal_CSD 0353 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4392 _Page_last 4404 _Year 2018 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'DNA-binding protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'entity_1, chain 1' $entity_1 'entity_1, chain 2' $entity_1 stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'DNA-binding protein' _Molecular_mass 10291.794 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 95 _Mol_residue_sequence ; GHMSKKELAAQIAEKFTDVL SKTHAEEITNFVFDHIKKAL VAGKEVSIAGFGKFAVTERA ARDGRNPSTGETIKIPASKS AKFKAGKQLKTDLNN ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -1 GLY 2 0 HIS 3 1 MET 4 2 SER 5 3 LYS 6 4 LYS 7 5 GLU 8 6 LEU 9 7 ALA 10 8 ALA 11 9 GLN 12 10 ILE 13 11 ALA 14 12 GLU 15 13 LYS 16 14 PHE 17 15 THR 18 16 ASP 19 17 VAL 20 18 LEU 21 19 SER 22 20 LYS 23 21 THR 24 22 HIS 25 23 ALA 26 24 GLU 27 25 GLU 28 26 ILE 29 27 THR 30 28 ASN 31 29 PHE 32 30 VAL 33 31 PHE 34 32 ASP 35 33 HIS 36 34 ILE 37 35 LYS 38 36 LYS 39 37 ALA 40 38 LEU 41 39 VAL 42 40 ALA 43 41 GLY 44 42 LYS 45 43 GLU 46 44 VAL 47 45 SER 48 46 ILE 49 47 ALA 50 48 GLY 51 49 PHE 52 50 GLY 53 51 LYS 54 52 PHE 55 53 ALA 56 54 VAL 57 55 THR 58 56 GLU 59 57 ARG 60 58 ALA 61 59 ALA 62 60 ARG 63 61 ASP 64 62 GLY 65 63 ARG 66 64 ASN 67 65 PRO 68 66 SER 69 67 THR 70 68 GLY 71 69 GLU 72 70 THR 73 71 ILE 74 72 LYS 75 73 ILE 76 74 PRO 77 75 ALA 78 76 SER 79 77 LYS 80 78 SER 81 79 ALA 82 80 LYS 83 81 PHE 84 82 LYS 85 83 ALA 86 84 GLY 87 85 LYS 88 86 GLN 89 87 LEU 90 88 LYS 91 89 THR 92 90 ASP 93 91 LEU 94 92 ASN 95 93 ASN 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 _Gene_mnemonic $entity_1 'Spiroplasma melliferum KC3' 570509 Bacteria . Spiroplasma Melliferum SPM_000560 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 $entity_1 'recombinant technology' . Escherichia coli . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '5 % [U-2H] D2O, 95% H2O/5% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 . mM na D2O 5 % [U-2H] stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name GROMACS _Version . loop_ _Vendor _Address _Electronic_address "Herman Berendsen's group, department of Biophysical Chemistry of Groningen University" . . stop_ loop_ _Task refinement stop_ _Details . save_ save_software_2 _Saveframe_category software _Name TALOS++ _Version . loop_ _Vendor _Address _Electronic_address 'Cornilescu, Delaglio and Bax' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Agilent _Model 'Uniform NMR System' _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _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 'ionic strength' 0.375 . M pH 6.7 . pH pressure 1 . atm temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 0.000 internal indirect . . . 0.25144953 DSS H 1 'methyl protons' ppm 0.000 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.000 internal 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name 'entity_1, chain 1' _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 4 6 LYS H H 8.194 0.020 . 2 4 6 LYS HA H 3.577 0.020 . 3 4 6 LYS CA C 59.001 0.400 . 4 4 6 LYS CB C 31.762 0.400 . 5 4 6 LYS N N 118.812 0.400 . 6 5 7 GLU H H 7.841 0.020 . 7 5 7 GLU HA H 4.09 0.020 . 8 5 7 GLU CA C 58.575 0.400 . 9 5 7 GLU CB C 29.324 0.400 . 10 5 7 GLU N N 119.921 0.400 . 11 6 8 LEU H H 7.816 0.020 . 12 6 8 LEU HA H 4.04 0.020 . 13 6 8 LEU CA C 57.703 0.400 . 14 6 8 LEU CB C 40.55 0.400 . 15 6 8 LEU N N 120.555 0.400 . 16 7 9 ALA H H 8.471 0.020 . 17 7 9 ALA CA C 55.148 0.400 . 18 7 9 ALA CB C 17.649 0.400 . 19 7 9 ALA N N 120.485 0.400 . 20 8 10 ALA H H 7.718 0.020 . 21 8 10 ALA HA H 4.007 0.020 . 22 8 10 ALA CA C 54.587 0.400 . 23 8 10 ALA CB C 17.456 0.400 . 24 8 10 ALA N N 119.352 0.400 . 25 9 11 GLN H H 8.013 0.020 . 26 9 11 GLN HA H 4.073 0.020 . 27 9 11 GLN CA C 58.637 0.400 . 28 9 11 GLN CB C 27.848 0.400 . 29 9 11 GLN N N 118.09 0.400 . 30 10 12 ILE H H 8.589 0.020 . 31 10 12 ILE HA H 3.462 0.020 . 32 10 12 ILE CA C 65.368 0.400 . 33 10 12 ILE CB C 37.471 0.400 . 34 10 12 ILE N N 120.382 0.400 . 35 11 13 ALA H H 8.361 0.020 . 36 11 13 ALA HA H 3.652 0.020 . 37 11 13 ALA CA C 54.709 0.400 . 38 11 13 ALA CB C 17.52 0.400 . 39 11 13 ALA N N 120.561 0.400 . 40 12 14 GLU H H 7.595 0.020 . 41 12 14 GLU HA H 3.974 0.020 . 42 12 14 GLU CA C 58.201 0.400 . 43 12 14 GLU CB C 29.581 0.400 . 44 12 14 GLU N N 114.766 0.400 . 45 13 15 LYS H H 7.856 0.020 . 46 13 15 LYS HA H 3.834 0.020 . 47 13 15 LYS CA C 57.204 0.400 . 48 13 15 LYS CB C 31.569 0.400 . 49 13 15 LYS N N 119.235 0.400 . 50 14 16 PHE H H 7.864 0.020 . 51 14 16 PHE HA H 4.685 0.020 . 52 14 16 PHE CA C 56.612 0.400 . 53 14 16 PHE CB C 36.637 0.400 . 54 14 16 PHE N N 114.764 0.400 . 55 15 17 THR H H 6.798 0.020 . 56 15 17 THR HA H 4.296 0.020 . 57 15 17 THR CA C 64.184 0.400 . 58 15 17 THR CB C 68.904 0.400 . 59 15 17 THR N N 115.568 0.400 . 60 16 18 ASP H H 8.713 0.020 . 61 16 18 ASP HA H 4.47 0.020 . 62 16 18 ASP CA C 55.366 0.400 . 63 16 18 ASP CB C 39.844 0.400 . 64 16 18 ASP N N 117.676 0.400 . 65 17 19 VAL H H 7.831 0.020 . 66 17 19 VAL HA H 4.181 0.020 . 67 17 19 VAL CA C 62.189 0.400 . 68 17 19 VAL CB C 34.007 0.400 . 69 17 19 VAL N N 114.619 0.400 . 70 18 20 LEU H H 8.087 0.020 . 71 18 20 LEU HA H 4.858 0.020 . 72 18 20 LEU CA C 53.122 0.400 . 73 18 20 LEU CB C 44.271 0.400 . 74 18 20 LEU N N 118.232 0.400 . 75 19 21 SER H H 9.491 0.020 . 76 19 21 SER HA H 4.619 0.020 . 77 19 21 SER CA C 56.363 0.400 . 78 19 21 SER CB C 65.44 0.400 . 79 19 21 SER N N 119.583 0.400 . 80 20 22 LYS H H 8.837 0.020 . 81 20 22 LYS HA H 3.42 0.020 . 82 20 22 LYS CA C 59.915 0.400 . 83 20 22 LYS N N 121.334 0.400 . 84 21 23 THR H H 7.882 0.020 . 85 21 23 THR CA C 65.523 0.400 . 86 21 23 THR CB C 68.125 0.400 . 87 21 23 THR N N 113.627 0.400 . 88 22 24 HIS H H 7.646 0.020 . 89 22 24 HIS HA H 4.363 0.020 . 90 22 24 HIS CA C 59.35 0.400 . 91 22 24 HIS CB C 31.234 0.400 . 92 22 24 HIS N N 121.681 0.400 . 93 23 25 ALA H H 8.515 0.020 . 94 23 25 ALA HA H 3.726 0.020 . 95 23 25 ALA CA C 55.49 0.400 . 96 23 25 ALA CB C 17.898 0.400 . 97 23 25 ALA N N 120.852 0.400 . 98 24 26 GLU H H 8.178 0.020 . 99 24 26 GLU HA H 3.792 0.020 . 100 24 26 GLU CA C 59.65 0.400 . 101 24 26 GLU CB C 28.679 0.400 . 102 24 26 GLU N N 120.616 0.400 . 103 25 27 GLU H H 8.165 0.020 . 104 25 27 GLU HA H 4.148 0.020 . 105 25 27 GLU CA C 59.742 0.400 . 106 25 27 GLU CB C 29.489 0.400 . 107 25 27 GLU N N 120.668 0.400 . 108 26 28 ILE H H 8.811 0.020 . 109 26 28 ILE HA H 4.671 0.020 . 110 26 28 ILE CA C 65.149 0.400 . 111 26 28 ILE CB C 37.599 0.400 . 112 26 28 ILE N N 121.133 0.400 . 113 27 29 THR H H 7.941 0.020 . 114 27 29 THR HA H 3.528 0.020 . 115 27 29 THR CA C 68.546 0.400 . 116 27 29 THR CB C 67.429 0.400 . 117 27 29 THR N N 117.254 0.400 . 118 28 30 ASN H H 8.346 0.020 . 119 28 30 ASN HA H 4.39 0.020 . 120 28 30 ASN CA C 56.207 0.400 . 121 28 30 ASN CB C 37.278 0.400 . 122 28 30 ASN N N 119.921 0.400 . 123 29 31 PHE H H 8.199 0.020 . 124 29 31 PHE HA H 4.418 0.020 . 125 29 31 PHE CA C 61.255 0.400 . 126 29 31 PHE CB C 39.01 0.400 . 127 29 31 PHE N N 121.308 0.400 . 128 30 32 VAL H H 8.781 0.020 . 129 30 32 VAL HA H 3.419 0.020 . 130 30 32 VAL CA C 66.707 0.400 . 131 30 32 VAL CB C 31.056 0.400 . 132 30 32 VAL N N 119.361 0.400 . 133 31 33 PHE H H 8.503 0.020 . 134 31 33 PHE CA C 62.407 0.400 . 135 31 33 PHE CB C 38.241 0.400 . 136 31 33 PHE N N 118.678 0.400 . 137 32 34 ASP H H 8.314 0.020 . 138 32 34 ASP HA H 4.384 0.020 . 139 32 34 ASP CA C 57.266 0.400 . 140 32 34 ASP CB C 40.037 0.400 . 141 32 34 ASP N N 120.383 0.400 . 142 33 35 HIS H H 8.084 0.020 . 143 33 35 HIS HA H 3.843 0.020 . 144 33 35 HIS CA C 60.201 0.400 . 145 33 35 HIS CB C 29.709 0.400 . 146 33 35 HIS N N 120.359 0.400 . 147 34 36 ILE H H 8.166 0.020 . 148 34 36 ILE HA H 3.487 0.020 . 149 34 36 ILE CA C 60.149 0.400 . 150 34 36 ILE N N 119.379 0.400 . 151 35 37 LYS H H 7.838 0.020 . 152 35 37 LYS CA C 59.058 0.400 . 153 35 37 LYS CB C 31.826 0.400 . 154 35 37 LYS N N 116.828 0.400 . 155 36 38 LYS H H 7.728 0.020 . 156 36 38 LYS CA C 58.533 0.400 . 157 36 38 LYS CB C 32.018 0.400 . 158 36 38 LYS N N 116.975 0.400 . 159 37 39 ALA H H 7.582 0.020 . 160 37 39 ALA HA H 3.973 0.020 . 161 37 39 ALA CA C 53.932 0.400 . 162 37 39 ALA CB C 17.713 0.400 . 163 37 39 ALA N N 121.609 0.400 . 164 38 40 LEU H H 7.912 0.020 . 165 38 40 LEU HA H 4.089 0.020 . 166 38 40 LEU CA C 56.269 0.400 . 167 38 40 LEU CB C 41.576 0.400 . 168 38 40 LEU N N 117.963 0.400 . 169 39 41 VAL H H 8.047 0.020 . 170 39 41 VAL CA C 64.011 0.400 . 171 39 41 VAL N N 118.45 0.400 . 172 40 42 ALA H H 7.716 0.020 . 173 40 42 ALA CA C 52.312 0.400 . 174 40 42 ALA N N 122.524 0.400 . 175 41 43 GLY H H 8 0.020 . 176 41 43 GLY CA C 45.146 0.400 . 177 41 43 GLY N N 106.899 0.400 . 178 42 44 LYS H H 7.765 0.020 . 179 42 44 LYS CA C 57.058 0.400 . 180 42 44 LYS CB C 30.799 0.400 . 181 42 44 LYS N N 125.548 0.400 . 182 49 51 PHE H H 8.482 0.020 . 183 49 51 PHE HA H 4.801 0.020 . 184 49 51 PHE CA C 59.546 0.400 . 185 49 51 PHE N N 120.904 0.400 . 186 50 52 GLY H H 8.517 0.020 . 187 50 52 GLY HA3 H 3.664 0.020 . 188 50 52 GLY CA C 45.894 0.400 . 189 50 52 GLY N N 107.823 0.400 . 190 51 53 LYS H H 7.842 0.020 . 191 51 53 LYS CA C 53.678 0.400 . 192 51 53 LYS N N 118.713 0.400 . 193 52 54 PHE H H 9.767 0.020 . 194 52 54 PHE CA C 55.74 0.400 . 195 52 54 PHE N N 121.447 0.400 . 196 53 55 ALA H H 8.848 0.020 . 197 53 55 ALA HA H 4.801 0.020 . 198 53 55 ALA CA C 50.661 0.400 . 199 53 55 ALA CB C 22.396 0.400 . 200 53 55 ALA N N 122.62 0.400 . 201 54 56 VAL H H 9.048 0.020 . 202 54 56 VAL HA H 4.743 0.020 . 203 54 56 VAL CA C 61.784 0.400 . 204 54 56 VAL N N 121.714 0.400 . 205 55 57 THR H H 8.005 0.020 . 206 55 57 THR HA H 4.038 0.020 . 207 55 57 THR CA C 58.108 0.400 . 208 55 57 THR N N 121.329 0.400 . 209 56 58 GLU H H 8.526 0.020 . 210 56 58 GLU CA C 54.929 0.400 . 211 56 58 GLU N N 119.799 0.400 . 212 57 59 ARG H H 7.881 0.020 . 213 57 59 ARG CA C 54.618 0.400 . 214 57 59 ARG N N 119.652 0.400 . 215 58 60 ALA H H 8.362 0.020 . 216 58 60 ALA CA C 51.627 0.400 . 217 58 60 ALA N N 126.199 0.400 . 218 59 61 ALA H H 8.534 0.020 . 219 59 61 ALA CA C 52.298 0.400 . 220 59 61 ALA N N 123.487 0.400 . 221 60 62 ARG H H 8.589 0.020 . 222 60 62 ARG CA C 54.524 0.400 . 223 60 62 ARG N N 118.882 0.400 . 224 61 63 ASP H H 8.405 0.020 . 225 61 63 ASP CA C 53.532 0.400 . 226 61 63 ASP N N 120.711 0.400 . 227 62 64 GLY H H 8.841 0.020 . 228 62 64 GLY CA C 44.18 0.400 . 229 62 64 GLY N N 110.169 0.400 . 230 66 68 SER H H 8.342 0.020 . 231 66 68 SER CA C 59.759 0.400 . 232 66 68 SER N N 113.013 0.400 . 233 67 69 THR H H 7.432 0.020 . 234 67 69 THR CA C 61.068 0.400 . 235 67 69 THR N N 108.578 0.400 . 236 68 70 GLY H H 8.484 0.020 . 237 68 70 GLY CA C 45.177 0.400 . 238 68 70 GLY N N 110.926 0.400 . 239 69 71 GLU H H 7.876 0.020 . 240 69 71 GLU CA C 55.989 0.400 . 241 69 71 GLU CB C 30.797 0.400 . 242 69 71 GLU N N 120.233 0.400 . 243 70 72 THR H H 8.658 0.020 . 244 70 72 THR CA C 62.906 0.400 . 245 70 72 THR CB C 69.097 0.400 . 246 70 72 THR N N 118.721 0.400 . 247 71 73 ILE H H 8.285 0.020 . 248 71 73 ILE HA H 4.412 0.020 . 249 71 73 ILE CA C 59.229 0.400 . 250 71 73 ILE CB C 40.871 0.400 . 251 71 73 ILE N N 123.579 0.400 . 252 72 74 LYS H H 8.469 0.020 . 253 72 74 LYS CA C 54.805 0.400 . 254 72 74 LYS CB C 31.826 0.400 . 255 72 74 LYS N N 124.258 0.400 . 256 73 75 ILE H H 8.971 0.020 . 257 73 75 ILE HA H 4.437 0.020 . 258 73 75 ILE CA C 57.827 0.400 . 259 73 75 ILE N N 129.081 0.400 . 260 75 77 ALA H H 8.533 0.020 . 261 75 77 ALA CA C 52.25 0.400 . 262 75 77 ALA CB C 18.941 0.400 . 263 75 77 ALA N N 123.467 0.400 . 264 76 78 SER H H 8.406 0.020 . 265 76 78 SER CA C 57.329 0.400 . 266 76 78 SER CB C 65.312 0.400 . 267 76 78 SER N N 113.829 0.400 . 268 77 79 LYS H H 9.462 0.020 . 269 77 79 LYS CA C 55.21 0.400 . 270 77 79 LYS N N 123.183 0.400 . 271 78 80 SER H H 8.782 0.020 . 272 78 80 SER HA H 4.462 0.020 . 273 78 80 SER CA C 55.895 0.400 . 274 78 80 SER N N 115.882 0.400 . 275 79 81 ALA H H 8.631 0.020 . 276 79 81 ALA CA C 50.38 0.400 . 277 79 81 ALA N N 123.253 0.400 . 278 80 82 LYS H H 9.303 0.020 . 279 80 82 LYS HA H 4.933 0.020 . 280 80 82 LYS CA C 53.839 0.400 . 281 80 82 LYS N N 122.005 0.400 . 282 81 83 PHE H H 8.716 0.020 . 283 81 83 PHE CA C 60.538 0.400 . 284 81 83 PHE N N 122.856 0.400 . 285 82 84 LYS H H 8.972 0.020 . 286 82 84 LYS HA H 4.825 0.020 . 287 82 84 LYS CA C 56.456 0.400 . 288 82 84 LYS N N 123.113 0.400 . 289 83 85 ALA H H 8.771 0.020 . 290 83 85 ALA HA H 4.313 0.020 . 291 83 85 ALA CA C 56.674 0.400 . 292 83 85 ALA N N 124.788 0.400 . 293 86 88 GLN H H 7.754 0.020 . 294 86 88 GLN CA C 58.619 0.400 . 295 86 88 GLN N N 125.943 0.400 . 296 87 89 LEU H H 7.955 0.020 . 297 87 89 LEU CA C 57.703 0.400 . 298 87 89 LEU N N 120.641 0.400 . 299 88 90 LYS H H 8.036 0.020 . 300 88 90 LYS CA C 60.538 0.400 . 301 88 90 LYS N N 116.758 0.400 . 302 89 91 THR H H 8.327 0.020 . 303 89 91 THR HA H 3.883 0.020 . 304 89 91 THR CA C 66.458 0.400 . 305 89 91 THR N N 116.89 0.400 . 306 90 92 ASP H H 8.473 0.020 . 307 90 92 ASP HA H 4.296 0.020 . 308 90 92 ASP CA C 57.079 0.400 . 309 90 92 ASP N N 122.96 0.400 . 310 91 93 LEU H H 8.121 0.020 . 311 91 93 LEU HA H 4.115 0.020 . 312 91 93 LEU CA C 56.269 0.400 . 313 91 93 LEU N N 116.85 0.400 . 314 92 94 ASN H H 7.482 0.020 . 315 92 94 ASN HA H 4.834 0.020 . 316 92 94 ASN CA C 53.714 0.400 . 317 92 94 ASN N N 114.733 0.400 . 318 93 95 ASN H H 7.783 0.020 . 319 93 95 ASN CA C 53.091 0.400 . 320 93 95 ASN N N 119.154 0.400 . stop_ save_