data_26068 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of DNA-binding HU protein from micoplasma Mycoplasma gallisepticum ; _BMRB_accession_number 26068 _BMRB_flat_file_name bmr26068.str _Entry_type original _Submission_date 2016-09-13 _Accession_date 2016-09-13 _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 Dmitry A. . 2 Talyzina Anna A. . 3 Agapova Yulia K. . 4 Vlaskina Anna V. . 5 Korzhenevskiy Dmitry A. . 6 Bocharov Eduard V. . 7 Rakitina Tatiana V. . 8 Timofeev Vladimir I. . 9 Popov Vladimir O. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 163 "13C chemical shifts" 251 "15N chemical shifts" 94 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-11-03 original BMRB . stop_ _Original_release_date 2016-11-03 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure of DNA-binding HU protein from micoplasma Mycoplasma gallisepticum ; _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Altukhov Dmitry A. . 2 Talyzina Anna A. . 3 Agapova Yulia K. . 4 Vlaskina Anna V. . 5 Korzhenevskiy Dmitry A. . 6 Bocharov Eduard V. . 7 Rakitina Tatiana V. . 8 Timofeev Vladimir I. . 9 Popov Vladimir O. . stop_ _Journal_abbreviation 'Biochem. Biophys. Res. Commun.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'DNA-binding HU protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $entity entity_2 $entity stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass 10983.192 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 99 _Mol_residue_sequence ; MAKIKSLSAAEYLKEMADET NIKVQDIRLVVTSLQKVLAK ELATTGEVRLFDIGKFKLVT TKPRTGINPKTKQKIQIPAG KKIKLTVSKILTDAVDSHK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 LYS 4 ILE 5 LYS 6 SER 7 LEU 8 SER 9 ALA 10 ALA 11 GLU 12 TYR 13 LEU 14 LYS 15 GLU 16 MET 17 ALA 18 ASP 19 GLU 20 THR 21 ASN 22 ILE 23 LYS 24 VAL 25 GLN 26 ASP 27 ILE 28 ARG 29 LEU 30 VAL 31 VAL 32 THR 33 SER 34 LEU 35 GLN 36 LYS 37 VAL 38 LEU 39 ALA 40 LYS 41 GLU 42 LEU 43 ALA 44 THR 45 THR 46 GLY 47 GLU 48 VAL 49 ARG 50 LEU 51 PHE 52 ASP 53 ILE 54 GLY 55 LYS 56 PHE 57 LYS 58 LEU 59 VAL 60 THR 61 THR 62 LYS 63 PRO 64 ARG 65 THR 66 GLY 67 ILE 68 ASN 69 PRO 70 LYS 71 THR 72 LYS 73 GLN 74 LYS 75 ILE 76 GLN 77 ILE 78 PRO 79 ALA 80 GLY 81 LYS 82 LYS 83 ILE 84 LYS 85 LEU 86 THR 87 VAL 88 SER 89 LYS 90 ILE 91 LEU 92 THR 93 ASP 94 ALA 95 VAL 96 ASP 97 SER 98 HIS 99 LYS 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 $entity 'Mycoplasma gallisepticum' 2096 Bacteria . Mycoplasma gallisepticum 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 'recombinant technology' . Escherichia coli . pHisTEV 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 _Isotopic_labeling $entity 1 mM '[U-13C; U-15N]' D2O 5 % [U-2H] 'sodium phosphate' 50 mM 'natural abundance' 'sodium azide' 0.1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TALOS++ _Saveframe_category software _Name TALOS++ _Version . loop_ _Vendor _Address _Electronic_address 'Cornilescu, Delaglio and Bax' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_GROMACS _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_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_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 308 . 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_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 $chemical_shift_reference_1 _Mol_system_component_name entity_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 1 1 MET C C 175.01 0.400 . 2 2 2 ALA H H 8.25 0.020 . 3 2 2 ALA C C 176.53 0.400 . 4 2 2 ALA CA C 51.73 0.400 . 5 2 2 ALA N N 125.69 0.400 . 6 3 3 LYS H H 8.21 0.020 . 7 3 3 LYS C C 175.52 0.400 . 8 3 3 LYS CA C 55.23 0.400 . 9 3 3 LYS N N 121.04 0.400 . 10 4 4 ILE H H 8.17 0.020 . 11 4 4 ILE HA H 4.18 0.020 . 12 4 4 ILE C C 174.95 0.400 . 13 4 4 ILE CA C 59.87 0.400 . 14 4 4 ILE N N 122.49 0.400 . 15 5 5 LYS H H 8.32 0.020 . 16 5 5 LYS C C 174.33 0.400 . 17 5 5 LYS CA C 55.06 0.400 . 18 5 5 LYS N N 126.6 0.400 . 19 6 6 SER H H 8.2 0.020 . 20 6 6 SER C C 174.22 0.400 . 21 6 6 SER CA C 56.3 0.400 . 22 6 6 SER N N 118.4 0.400 . 23 7 7 LEU H H 9.05 0.020 . 24 7 7 LEU C C 177.73 0.400 . 25 7 7 LEU CA C 54.95 0.400 . 26 7 7 LEU CB C 42 0.400 . 27 7 7 LEU N N 125.4 0.400 . 28 8 8 SER H H 9.14 0.020 . 29 8 8 SER HA H 4.51 0.020 . 30 8 8 SER C C 173.81 0.400 . 31 8 8 SER CA C 56.74 0.400 . 32 8 8 SER CB C 64.39 0.400 . 33 8 8 SER N N 124.87 0.400 . 34 9 9 ALA H H 8.71 0.020 . 35 9 9 ALA HA H 4.4 0.020 . 36 9 9 ALA C C 178.94 0.400 . 37 9 9 ALA CA C 54.94 0.400 . 38 9 9 ALA N N 124.34 0.400 . 39 10 10 ALA H H 8.38 0.020 . 40 10 10 ALA C C 180.6 0.400 . 41 10 10 ALA CA C 54.38 0.400 . 42 10 10 ALA CB C 17.24 0.400 . 43 10 10 ALA N N 117.99 0.400 . 44 11 11 GLU H H 7.78 0.020 . 45 11 11 GLU HA H 4.04 0.020 . 46 11 11 GLU C C 177.77 0.400 . 47 11 11 GLU CA C 58.21 0.400 . 48 11 11 GLU CB C 29.31 0.400 . 49 11 11 GLU N N 118.9 0.400 . 50 12 12 TYR H H 8.8 0.020 . 51 12 12 TYR C C 179.28 0.400 . 52 12 12 TYR CA C 59.69 0.400 . 53 12 12 TYR CB C 37.53 0.400 . 54 12 12 TYR N N 125.59 0.400 . 55 13 13 LEU H H 8.77 0.020 . 56 13 13 LEU HA H 4.13 0.020 . 57 13 13 LEU C C 177.79 0.400 . 58 13 13 LEU CA C 58.18 0.400 . 59 13 13 LEU CB C 41.29 0.400 . 60 13 13 LEU N N 118.24 0.400 . 61 14 14 LYS H H 7.79 0.020 . 62 14 14 LYS HA H 3.98 0.020 . 63 14 14 LYS C C 177.09 0.400 . 64 14 14 LYS CA C 58.61 0.400 . 65 14 14 LYS CB C 31.22 0.400 . 66 14 14 LYS N N 118.87 0.400 . 67 15 15 GLU H H 8.33 0.020 . 68 15 15 GLU HA H 4.05 0.020 . 69 15 15 GLU C C 179.66 0.400 . 70 15 15 GLU CA C 59.26 0.400 . 71 15 15 GLU CB C 28.01 0.400 . 72 15 15 GLU N N 119.56 0.400 . 73 16 16 MET H H 7.94 0.020 . 74 16 16 MET HA H 4.42 0.020 . 75 16 16 MET C C 178.96 0.400 . 76 16 16 MET CA C 58.2 0.400 . 77 16 16 MET CB C 34.37 0.400 . 78 16 16 MET N N 116.76 0.400 . 79 17 17 ALA H H 8.82 0.020 . 80 17 17 ALA HA H 4.21 0.020 . 81 17 17 ALA C C 179.62 0.400 . 82 17 17 ALA CA C 54.76 0.400 . 83 17 17 ALA CB C 17.75 0.400 . 84 17 17 ALA N N 128 0.400 . 85 18 18 ASP H H 8.77 0.020 . 86 18 18 ASP HA H 4.42 0.020 . 87 18 18 ASP C C 177.75 0.400 . 88 18 18 ASP CA C 55.79 0.400 . 89 18 18 ASP CB C 38.98 0.400 . 90 18 18 ASP N N 119.66 0.400 . 91 19 19 GLU H H 7.62 0.020 . 92 19 19 GLU HA H 4.19 0.020 . 93 19 19 GLU C C 177.54 0.400 . 94 19 19 GLU CA C 57.75 0.400 . 95 19 19 GLU CB C 29.36 0.400 . 96 19 19 GLU N N 117.15 0.400 . 97 20 20 THR H H 7.9 0.020 . 98 20 20 THR HA H 4.12 0.020 . 99 20 20 THR C C 174.8 0.400 . 100 20 20 THR CA C 62.2 0.400 . 101 20 20 THR CB C 70.87 0.400 . 102 20 20 THR N N 105.73 0.400 . 103 21 21 ASN H H 8.46 0.020 . 104 21 21 ASN HA H 4.39 0.020 . 105 21 21 ASN HD21 H 7.46 0.020 . 106 21 21 ASN HD22 H 6.78 0.020 . 107 21 21 ASN C C 173.06 0.400 . 108 21 21 ASN CA C 54.21 0.400 . 109 21 21 ASN CB C 36.87 0.400 . 110 21 21 ASN N N 116.95 0.400 . 111 21 21 ASN ND2 N 112.2 0.400 . 112 22 22 ILE H H 7.68 0.020 . 113 22 22 ILE HA H 4.14 0.020 . 114 22 22 ILE C C 174.78 0.400 . 115 22 22 ILE CA C 59.1 0.400 . 116 22 22 ILE CB C 37.06 0.400 . 117 22 22 ILE N N 121.83 0.400 . 118 23 23 LYS H H 8.51 0.020 . 119 23 23 LYS HA H 4.14 0.020 . 120 23 23 LYS C C 178.55 0.400 . 121 23 23 LYS CA C 55.94 0.400 . 122 23 23 LYS CB C 31.67 0.400 . 123 23 23 LYS N N 124.75 0.400 . 124 24 24 VAL H H 8.8 0.020 . 125 24 24 VAL C C 176.35 0.400 . 126 24 24 VAL CA C 66.09 0.400 . 127 24 24 VAL CB C 30.64 0.400 . 128 24 24 VAL N N 122.57 0.400 . 129 25 25 GLN H H 8.95 0.020 . 130 25 25 GLN C C 177.42 0.400 . 131 25 25 GLN CA C 58.5 0.400 . 132 25 25 GLN CB C 26.8 0.400 . 133 25 25 GLN N N 117.73 0.400 . 134 26 26 ASP H H 7.1 0.020 . 135 26 26 ASP HA H 4.61 0.020 . 136 26 26 ASP C C 177.32 0.400 . 137 26 26 ASP CA C 55.98 0.400 . 138 26 26 ASP CB C 39.24 0.400 . 139 26 26 ASP N N 120.36 0.400 . 140 27 27 ILE H H 7.95 0.020 . 141 27 27 ILE C C 177.47 0.400 . 142 27 27 ILE CA C 65.11 0.400 . 143 27 27 ILE CB C 35.84 0.400 . 144 27 27 ILE N N 120.73 0.400 . 145 28 28 ARG H H 8.64 0.020 . 146 28 28 ARG C C 178.15 0.400 . 147 28 28 ARG CA C 59.04 0.400 . 148 28 28 ARG CB C 28.91 0.400 . 149 28 28 ARG N N 118.34 0.400 . 150 29 29 LEU H H 7.34 0.020 . 151 29 29 LEU HA H 4.05 0.020 . 152 29 29 LEU C C 178.97 0.400 . 153 29 29 LEU CA C 57.15 0.400 . 154 29 29 LEU CB C 40.84 0.400 . 155 29 29 LEU N N 119.8 0.400 . 156 30 30 VAL H H 7.93 0.020 . 157 30 30 VAL HA H 3.41 0.020 . 158 30 30 VAL C C 176.58 0.400 . 159 30 30 VAL CA C 66.49 0.400 . 160 30 30 VAL CB C 30.39 0.400 . 161 30 30 VAL N N 120.2 0.400 . 162 31 31 VAL H H 8.52 0.020 . 163 31 31 VAL HA H 3.21 0.020 . 164 31 31 VAL C C 177.75 0.400 . 165 31 31 VAL CA C 66.04 0.400 . 166 31 31 VAL CB C 29.87 0.400 . 167 31 31 VAL N N 119.11 0.400 . 168 32 32 THR H H 8.22 0.020 . 169 32 32 THR C C 175.68 0.400 . 170 32 32 THR CA C 66.44 0.400 . 171 32 32 THR CB C 67.47 0.400 . 172 32 32 THR N N 118.4 0.400 . 173 33 33 SER H H 7.82 0.020 . 174 33 33 SER HA H 4.33 0.020 . 175 33 33 SER C C 175.56 0.400 . 176 33 33 SER CA C 60.86 0.400 . 177 33 33 SER CB C 62.72 0.400 . 178 33 33 SER N N 118.47 0.400 . 179 34 34 LEU H H 8.94 0.020 . 180 34 34 LEU C C 180.12 0.400 . 181 34 34 LEU CA C 58.68 0.400 . 182 34 34 LEU CB C 41.87 0.400 . 183 34 34 LEU N N 120.79 0.400 . 184 35 35 GLN H H 7.67 0.020 . 185 35 35 GLN HA H 3.8 0.020 . 186 35 35 GLN HE21 H 7.2 0.020 . 187 35 35 GLN HE22 H 6.54 0.020 . 188 35 35 GLN C C 176.16 0.400 . 189 35 35 GLN CA C 58.91 0.400 . 190 35 35 GLN CB C 29.04 0.400 . 191 35 35 GLN N N 117.68 0.400 . 192 35 35 GLN NE2 N 107.5 0.400 . 193 36 36 LYS H H 8.1 0.020 . 194 36 36 LYS HA H 4 0.020 . 195 36 36 LYS C C 178.72 0.400 . 196 36 36 LYS CA C 59.1 0.400 . 197 36 36 LYS CB C 31.48 0.400 . 198 36 36 LYS N N 124.07 0.400 . 199 37 37 VAL H H 8.56 0.020 . 200 37 37 VAL HA H 3.42 0.020 . 201 37 37 VAL C C 176.25 0.400 . 202 37 37 VAL CA C 65.61 0.400 . 203 37 37 VAL N N 120.47 0.400 . 204 38 38 LEU H H 7.12 0.020 . 205 38 38 LEU C C 176.92 0.400 . 206 38 38 LEU CA C 57.72 0.400 . 207 38 38 LEU CB C 41.04 0.400 . 208 38 38 LEU N N 119.99 0.400 . 209 39 39 ALA H H 7.54 0.020 . 210 39 39 ALA HA H 3.78 0.020 . 211 39 39 ALA C C 177.77 0.400 . 212 39 39 ALA CA C 53.91 0.400 . 213 39 39 ALA CB C 17.37 0.400 . 214 39 39 ALA N N 117.87 0.400 . 215 40 40 LYS H H 7.76 0.020 . 216 40 40 LYS HA H 3.22 0.020 . 217 40 40 LYS C C 179.39 0.400 . 218 40 40 LYS CA C 58.17 0.400 . 219 40 40 LYS CB C 29.75 0.400 . 220 40 40 LYS N N 117.34 0.400 . 221 41 41 GLU H H 8.81 0.020 . 222 41 41 GLU HA H 3.9 0.020 . 223 41 41 GLU C C 179.39 0.400 . 224 41 41 GLU CA C 57.85 0.400 . 225 41 41 GLU CB C 28.72 0.400 . 226 41 41 GLU N N 119.51 0.400 . 227 42 42 LEU H H 8.2 0.020 . 228 42 42 LEU HA H 3.67 0.020 . 229 42 42 LEU C C 176.37 0.400 . 230 42 42 LEU CA C 57.65 0.400 . 231 42 42 LEU CB C 41.04 0.400 . 232 42 42 LEU N N 120.43 0.400 . 233 43 43 ALA H H 7.85 0.020 . 234 43 43 ALA HA H 4.03 0.020 . 235 43 43 ALA C C 177.51 0.400 . 236 43 43 ALA CA C 53.13 0.400 . 237 43 43 ALA CB C 19.23 0.400 . 238 43 43 ALA N N 117 0.400 . 239 44 44 THR H H 7.57 0.020 . 240 44 44 THR HA H 4.37 0.020 . 241 44 44 THR C C 174.16 0.400 . 242 44 44 THR CA C 61.03 0.400 . 243 44 44 THR CB C 69.2 0.400 . 244 44 44 THR N N 107.52 0.400 . 245 45 45 THR H H 8.69 0.020 . 246 45 45 THR HA H 4.17 0.020 . 247 45 45 THR C C 175.16 0.400 . 248 45 45 THR CA C 63.16 0.400 . 249 45 45 THR CB C 68.75 0.400 . 250 45 45 THR N N 120.02 0.400 . 251 46 46 GLY H H 8.3 0.020 . 252 46 46 GLY HA2 H 4.14 0.020 . 253 46 46 GLY HA3 H 4.45 0.020 . 254 46 46 GLY C C 171.89 0.400 . 255 46 46 GLY CA C 44.6 0.400 . 256 46 46 GLY N N 108.11 0.400 . 257 47 47 GLU H H 7.21 0.020 . 258 47 47 GLU HA H 5.33 0.020 . 259 47 47 GLU C C 173.28 0.400 . 260 47 47 GLU CA C 54.06 0.400 . 261 47 47 GLU CB C 32.28 0.400 . 262 47 47 GLU N N 115.32 0.400 . 263 48 48 VAL H H 8.81 0.020 . 264 48 48 VAL HA H 4.45 0.020 . 265 48 48 VAL C C 171.5 0.400 . 266 48 48 VAL CA C 60.08 0.400 . 267 48 48 VAL CB C 32.51 0.400 . 268 48 48 VAL N N 118.46 0.400 . 269 49 49 ARG H H 9.51 0.020 . 270 49 49 ARG HA H 4.7 0.020 . 271 49 49 ARG C C 173.52 0.400 . 272 49 49 ARG CA C 54.96 0.400 . 273 49 49 ARG CB C 29.17 0.400 . 274 49 49 ARG N N 129.96 0.400 . 275 50 50 LEU H H 8.96 0.020 . 276 50 50 LEU HA H 4.44 0.020 . 277 50 50 LEU C C 171.89 0.400 . 278 50 50 LEU CA C 51.1 0.400 . 279 50 50 LEU CB C 41.74 0.400 . 280 50 50 LEU N N 129.55 0.400 . 281 51 51 PHE H H 7.96 0.020 . 282 51 51 PHE HA H 3.75 0.020 . 283 51 51 PHE C C 173.52 0.400 . 284 51 51 PHE CA C 59.75 0.400 . 285 51 51 PHE CB C 36.61 0.400 . 286 51 51 PHE N N 122.72 0.400 . 287 52 52 ASP H H 8.69 0.020 . 288 52 52 ASP HA H 5.07 0.020 . 289 52 52 ASP C C 175.16 0.400 . 290 52 52 ASP CA C 53.38 0.400 . 291 52 52 ASP CB C 39.95 0.400 . 292 52 52 ASP N N 122.67 0.400 . 293 53 53 ILE H H 8.71 0.020 . 294 53 53 ILE HA H 3.98 0.020 . 295 53 53 ILE C C 174.95 0.400 . 296 53 53 ILE CA C 63.53 0.400 . 297 53 53 ILE CB C 37 0.400 . 298 53 53 ILE N N 121.19 0.400 . 299 54 54 GLY H H 6.69 0.020 . 300 54 54 GLY HA2 H 4.63 0.020 . 301 54 54 GLY HA3 H 4.73 0.020 . 302 54 54 GLY C C 169.84 0.400 . 303 54 54 GLY CA C 43.74 0.400 . 304 54 54 GLY N N 101.4 0.400 . 305 55 55 LYS H H 8.11 0.020 . 306 55 55 LYS HA H 4.93 0.020 . 307 55 55 LYS C C 174.34 0.400 . 308 55 55 LYS CA C 54.19 0.400 . 309 55 55 LYS CB C 33.66 0.400 . 310 55 55 LYS N N 119.44 0.400 . 311 56 56 PHE H H 9.42 0.020 . 312 56 56 PHE HA H 5.17 0.020 . 313 56 56 PHE C C 174.04 0.400 . 314 56 56 PHE CA C 56.14 0.400 . 315 56 56 PHE CB C 41.1 0.400 . 316 56 56 PHE N N 128.54 0.400 . 317 57 57 LYS H H 9.06 0.020 . 318 57 57 LYS HA H 5.03 0.020 . 319 57 57 LYS C C 173.28 0.400 . 320 57 57 LYS CA C 54.19 0.400 . 321 57 57 LYS CB C 36.42 0.400 . 322 57 57 LYS N N 120.82 0.400 . 323 58 58 LEU H H 8.42 0.020 . 324 58 58 LEU HA H 4.95 0.020 . 325 58 58 LEU C C 175.18 0.400 . 326 58 58 LEU CA C 52.89 0.400 . 327 58 58 LEU CB C 42.32 0.400 . 328 58 58 LEU N N 125.69 0.400 . 329 59 59 VAL H H 9.26 0.020 . 330 59 59 VAL HA H 4.54 0.020 . 331 59 59 VAL C C 174.69 0.400 . 332 59 59 VAL CA C 59.78 0.400 . 333 59 59 VAL CB C 32.95 0.400 . 334 59 59 VAL N N 125.77 0.400 . 335 60 60 THR H H 8.48 0.020 . 336 60 60 THR C C 174.25 0.400 . 337 60 60 THR CA C 60.74 0.400 . 338 60 60 THR CB C 65.26 0.400 . 339 60 60 THR N N 119.18 0.400 . 340 61 61 THR H H 8.61 0.020 . 341 61 61 THR C C 173.55 0.400 . 342 61 61 THR CA C 59.29 0.400 . 343 61 61 THR N N 117.84 0.400 . 344 62 62 LYS H H 8.38 0.020 . 345 62 62 LYS HA H 4.48 0.020 . 346 62 62 LYS CA C 53.75 0.400 . 347 62 62 LYS N N 122.61 0.400 . 348 63 63 PRO C C 176.78 0.400 . 349 64 64 ARG H H 8.13 0.020 . 350 64 64 ARG C C 177.07 0.400 . 351 64 64 ARG CA C 57.23 0.400 . 352 64 64 ARG N N 116.83 0.400 . 353 65 65 THR H H 7.37 0.020 . 354 65 65 THR C C 173.78 0.400 . 355 65 65 THR CA C 60.68 0.400 . 356 65 65 THR N N 127.24 0.400 . 357 66 66 GLY H H 8.76 0.020 . 358 66 66 GLY C C 171.63 0.400 . 359 66 66 GLY CA C 43.61 0.400 . 360 66 66 GLY N N 112.84 0.400 . 361 67 67 ILE H H 8.31 0.020 . 362 67 67 ILE C C 175.11 0.400 . 363 67 67 ILE CA C 58.22 0.400 . 364 67 67 ILE N N 119.56 0.400 . 365 68 68 ASN H H 8.75 0.020 . 366 68 68 ASN CA C 49.84 0.400 . 367 68 68 ASN N N 127.19 0.400 . 368 70 70 LYS H H 8.87 0.020 . 369 70 70 LYS HA H 4.53 0.020 . 370 70 70 LYS CA C 57.27 0.400 . 371 70 70 LYS N N 128.54 0.400 . 372 71 71 THR C C 174.77 0.400 . 373 71 71 THR CA C 60.65 0.400 . 374 72 72 LYS H H 8.45 0.020 . 375 72 72 LYS C C 174.5 0.400 . 376 72 72 LYS CA C 56.71 0.400 . 377 72 72 LYS N N 116.54 0.400 . 378 73 73 GLN H H 7.6 0.020 . 379 73 73 GLN HA H 4.2 0.020 . 380 73 73 GLN C C 174.7 0.400 . 381 73 73 GLN CA C 54.25 0.400 . 382 73 73 GLN N N 117.62 0.400 . 383 74 74 LYS H H 8.5 0.020 . 384 74 74 LYS C C 175.84 0.400 . 385 74 74 LYS CA C 55.9 0.400 . 386 74 74 LYS N N 122.53 0.400 . 387 75 75 ILE H H 8.48 0.020 . 388 75 75 ILE HA H 4.44 0.020 . 389 75 75 ILE C C 174 0.400 . 390 75 75 ILE CA C 58.75 0.400 . 391 75 75 ILE N N 121.12 0.400 . 392 76 76 GLN H H 8.51 0.020 . 393 76 76 GLN C C 174 0.400 . 394 76 76 GLN CA C 54.22 0.400 . 395 76 76 GLN N N 123.28 0.400 . 396 77 77 ILE H H 8.42 0.020 . 397 77 77 ILE CA C 60.71 0.400 . 398 77 77 ILE N N 115.59 0.400 . 399 78 78 PRO C C 176.07 0.400 . 400 79 79 ALA H H 8.49 0.020 . 401 79 79 ALA HA H 3.99 0.020 . 402 79 79 ALA C C 176.74 0.400 . 403 79 79 ALA CA C 51.67 0.400 . 404 79 79 ALA CB C 18.71 0.400 . 405 79 79 ALA N N 123.15 0.400 . 406 80 80 GLY H H 7.96 0.020 . 407 80 80 GLY C C 172.35 0.400 . 408 80 80 GLY CA C 43.65 0.400 . 409 80 80 GLY N N 109.54 0.400 . 410 81 81 LYS H H 8.33 0.020 . 411 81 81 LYS C C 174.92 0.400 . 412 81 81 LYS CA C 54.33 0.400 . 413 81 81 LYS N N 120.31 0.400 . 414 82 82 LYS H H 8.97 0.020 . 415 82 82 LYS HA H 4.67 0.020 . 416 82 82 LYS C C 173.36 0.400 . 417 82 82 LYS CA C 53.91 0.400 . 418 82 82 LYS CB C 35.2 0.400 . 419 82 82 LYS N N 121.71 0.400 . 420 83 83 ILE H H 8.47 0.020 . 421 83 83 ILE HA H 4.7 0.020 . 422 83 83 ILE C C 173.82 0.400 . 423 83 83 ILE CA C 60.2 0.400 . 424 83 83 ILE CB C 37.96 0.400 . 425 83 83 ILE N N 123.31 0.400 . 426 84 84 LYS H H 9.16 0.020 . 427 84 84 LYS HA H 4.7 0.020 . 428 84 84 LYS C C 173.77 0.400 . 429 84 84 LYS CA C 53.26 0.400 . 430 84 84 LYS CB C 35.07 0.400 . 431 84 84 LYS N N 127.19 0.400 . 432 85 85 LEU H H 8.62 0.020 . 433 85 85 LEU HA H 4.69 0.020 . 434 85 85 LEU C C 175.52 0.400 . 435 85 85 LEU CA C 52.08 0.400 . 436 85 85 LEU CB C 43.67 0.400 . 437 85 85 LEU N N 125.12 0.400 . 438 86 86 THR H H 8.77 0.020 . 439 86 86 THR HA H 4.55 0.020 . 440 86 86 THR C C 174.77 0.400 . 441 86 86 THR CA C 60.44 0.400 . 442 86 86 THR CB C 68.04 0.400 . 443 86 86 THR N N 124.61 0.400 . 444 87 87 VAL C C 174.81 0.400 . 445 87 87 VAL CA C 63.17 0.400 . 446 88 88 SER H H 8.33 0.020 . 447 88 88 SER HA H 4.47 0.020 . 448 88 88 SER CA C 56.79 0.400 . 449 88 88 SER N N 122.64 0.400 . 450 89 89 LYS C C 176.56 0.400 . 451 90 90 ILE H H 7.93 0.020 . 452 90 90 ILE HA H 3.7 0.020 . 453 90 90 ILE C C 178.25 0.400 . 454 90 90 ILE CA C 63.2 0.400 . 455 90 90 ILE CB C 36.23 0.400 . 456 90 90 ILE N N 117.64 0.400 . 457 91 91 LEU H H 7.38 0.020 . 458 91 91 LEU HA H 4.21 0.020 . 459 91 91 LEU C C 177.41 0.400 . 460 91 91 LEU CA C 56.75 0.400 . 461 91 91 LEU CB C 39.561 0.400 . 462 91 91 LEU N N 121.35 0.400 . 463 92 92 THR H H 7.78 0.020 . 464 92 92 THR HA H 3.67 0.020 . 465 92 92 THR C C 176.17 0.400 . 466 92 92 THR CA C 66.15 0.400 . 467 92 92 THR CB C 66.95 0.400 . 468 92 92 THR N N 113.94 0.400 . 469 93 93 ASP H H 8.79 0.020 . 470 93 93 ASP HA H 4.36 0.020 . 471 93 93 ASP C C 178.02 0.400 . 472 93 93 ASP CA C 56.14 0.400 . 473 93 93 ASP CB C 38.73 0.400 . 474 93 93 ASP N N 121.58 0.400 . 475 94 94 ALA H H 8.05 0.020 . 476 94 94 ALA HA H 4.13 0.020 . 477 94 94 ALA C C 180.08 0.400 . 478 94 94 ALA CA C 54.12 0.400 . 479 94 94 ALA CB C 17.11 0.400 . 480 94 94 ALA N N 124.61 0.400 . 481 95 95 VAL H H 8.11 0.020 . 482 95 95 VAL HA H 3.65 0.020 . 483 95 95 VAL C C 177.26 0.400 . 484 95 95 VAL CA C 65.35 0.400 . 485 95 95 VAL CB C 30.64 0.400 . 486 95 95 VAL N N 119.04 0.400 . 487 96 96 ASP H H 7.97 0.020 . 488 96 96 ASP HA H 4.46 0.020 . 489 96 96 ASP C C 176.71 0.400 . 490 96 96 ASP CA C 55.79 0.400 . 491 96 96 ASP CB C 40.14 0.400 . 492 96 96 ASP N N 119.55 0.400 . 493 97 97 SER H H 7.87 0.020 . 494 97 97 SER HA H 4.42 0.020 . 495 97 97 SER CA C 58.29 0.400 . 496 97 97 SER CB C 62.72 0.400 . 497 97 97 SER N N 112.6 0.400 . 498 98 98 HIS H H 7.34 0.020 . 499 98 98 HIS HA H 4.09 0.020 . 500 98 98 HIS C C 173.4 0.400 . 501 98 98 HIS CA C 57.4 0.400 . 502 98 98 HIS CB C 29.81 0.400 . 503 98 98 HIS N N 122.58 0.400 . 504 99 99 LYS H H 7.33 0.020 . 505 99 99 LYS HA H 4.03 0.020 . 506 99 99 LYS CA C 56.57 0.400 . 507 99 99 LYS CB C 32.87 0.400 . 508 99 99 LYS N N 128.65 0.400 . stop_ save_