data_50228 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N resonance assignments for the microtubule binding region of the kinetoplastid kinetochore protein KKT4 145-232 ; _BMRB_accession_number 50228 _BMRB_flat_file_name bmr50228.str _Entry_type original _Submission_date 2020-04-09 _Accession_date 2020-04-09 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details '1H, 13C and 15N resonance assignments for the microtubule binding region of the kinetoplastid kinetochore protein KKT4 145-232' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ludzia Patryk . . 2 Akiyoshi Bungo . . 3 Redfield Christina . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 100 "13C chemical shifts" 249 "15N chemical shifts" 92 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-11-18 update BMRB 'update entry citation' 2020-07-24 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 50215 'kinetoplastid kinetochore protein KKT4 115-174' 50229 'kinetoplastid kinetochore protein KKT4 115-343' stop_ _Original_release_date 2020-04-09 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; 1 H, 13 C and 15 N resonance assignments for the microtubule-binding domain of the kinetoplastid kinetochore protein KKT4 from Trypanosoma brucei ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32696260 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ludzia Patryk . . 2 Akiyoshi Bungo . . 3 Redfield Christina . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_volume 14 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 309 _Page_last 315 _Year 2020 _Details . loop_ _Keyword KKT4 'NMR resonance assignments' Trypanosome kinetochore kinetoplastids stop_ save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name KKT4_145_232 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'KKT4 145-232' $entity_1 stop_ _System_molecular_weight 20671.42 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'kinetochore protein' microtubule-binding stop_ _Database_query_date . _Details '20671.42 is molecular mass of a dimer' save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 10335.71 _Mol_thiol_state 'not present' loop_ _Biological_function 'kinetoplastid kinetochore protein' microtubule-binding stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 90 _Mol_residue_sequence ; SMRSEPVVDTQRVLDLEEEV ARLKRTIGHLQGVVEEKESA LEKHATQHNLEVHEMKKNYE LKIKSLTQTHEAAVRKLVSA QELVTAARNY ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 143 SER 2 144 MET 3 145 ARG 4 146 SER 5 147 GLU 6 148 PRO 7 149 VAL 8 150 VAL 9 151 ASP 10 152 THR 11 153 GLN 12 154 ARG 13 155 VAL 14 156 LEU 15 157 ASP 16 158 LEU 17 159 GLU 18 160 GLU 19 161 GLU 20 162 VAL 21 163 ALA 22 164 ARG 23 165 LEU 24 166 LYS 25 167 ARG 26 168 THR 27 169 ILE 28 170 GLY 29 171 HIS 30 172 LEU 31 173 GLN 32 174 GLY 33 175 VAL 34 176 VAL 35 177 GLU 36 178 GLU 37 179 LYS 38 180 GLU 39 181 SER 40 182 ALA 41 183 LEU 42 184 GLU 43 185 LYS 44 186 HIS 45 187 ALA 46 188 THR 47 189 GLN 48 190 HIS 49 191 ASN 50 192 LEU 51 193 GLU 52 194 VAL 53 195 HIS 54 196 GLU 55 197 MET 56 198 LYS 57 199 LYS 58 200 ASN 59 201 TYR 60 202 GLU 61 203 LEU 62 204 LYS 63 205 ILE 64 206 LYS 65 207 SER 66 208 LEU 67 209 THR 68 210 GLN 69 211 THR 70 212 HIS 71 213 GLU 72 214 ALA 73 215 ALA 74 216 VAL 75 217 ARG 76 218 LYS 77 219 LEU 78 220 VAL 79 221 SER 80 222 ALA 81 223 GLN 82 224 GLU 83 225 LEU 84 226 VAL 85 227 THR 86 228 ALA 87 229 ALA 88 230 ARG 89 231 ASN 90 232 TYR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value UniProt A0A3L6L4L8 KKT4 . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source_1 _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Gene_mnemonic $entity_1 'Trypanosoma brucei brucei' 5691 Eukaryota . Trypanosoma brucei TREU927 Tb927.8.3680 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_1 _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $entity_1 'recombinant technology' . Escherichia coli BL21(DE3) plasmid pRSF_Duet-1 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 0.35 mM '[U-13C; U-15N; U-2H]' HEPES 25 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' TCEP 0.5 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 0.35 mM '[U-13C; U-15N]' HEPES 25 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' TCEP 0.5 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name 'CcpNmr Analysis' _Version 2.4.2 loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_software_2 _Saveframe_category software _Name NMRPipe _Version 9.7 loop_ _Task processing stop_ _Details . save_ save_software_4 _Saveframe_category software _Name hmsIST _Version v211_64b loop_ _Task processing stop_ _Details . save_ save_software_3 _Saveframe_category software _Name TOPSPIN _Version 3.2 loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'Avance III HD' _Field_strength 750 _Details 'with TCI 5mm cryoprobe' save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'Avance III HD' _Field_strength 950 _Details 'with TCI 5mm cryoprobe' save_ ############################# # NMR applied experiments # ############################# save_2D_BEST_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D BEST TROSY' _Sample_label $sample_2 save_ save_2D_BEST_TROSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D BEST TROSY' _Sample_label $sample_1 save_ save_2D_BEST_TROSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D BEST TROSY' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_2 save_ save_3D_1H-15N_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_2 save_ save_3D_BT_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D BT HNCA' _Sample_label $sample_1 save_ save_3D_BT_HN(CO)CACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D BT HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_BT_HNCACB_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D BT HNCACB' _Sample_label $sample_1 save_ save_3D_BT_HNCO_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D BT HNCO' _Sample_label $sample_1 save_ save_3D_BT_HN(CA)CO_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D BT HN(CA)CO' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_aliphatic_11 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _Sample_label $sample_2 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' 150 . mM pH 7.2 0.1 pH pressure 1 . atm temperature 303.15 0.5 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 carbons' ppm 0.0 internal direct . . . 1 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0.0 na indirect . . . 0.101329 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_ _Software_label $software_1 stop_ loop_ _Experiment_label '2D BEST TROSY' '3D 1H-15N TOCSY' '3D 1H-15N NOESY' '3D BT HNCA' '3D BT HN(CO)CACB' '3D BT HNCACB' '3D BT HNCO' '3D BT HN(CA)CO' '2D 1H-13C HSQC aliphatic' stop_ loop_ _Sample_label $sample_2 $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name 'KKT4 145-232' _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 1 145 3 ARG H H 8.417 0.002 1 2 145 3 ARG N N 122.510 0.020 1 3 146 4 SER H H 8.366 0.002 1 4 146 4 SER C C 174.004 0.020 1 5 146 4 SER CA C 57.770 0.020 1 6 146 4 SER CB C 63.523 0.016 1 7 146 4 SER N N 117.665 0.020 1 8 147 5 GLU H H 8.326 0.001 1 9 147 5 GLU C C 174.458 0.020 1 10 147 5 GLU CA C 53.970 0.020 1 11 147 5 GLU CB C 29.016 0.020 1 12 147 5 GLU N N 123.860 0.018 1 13 148 6 PRO C C 176.690 0.020 1 14 148 6 PRO CA C 62.720 0.020 1 15 148 6 PRO CB C 31.204 0.020 1 16 149 7 VAL H H 8.236 0.001 1 17 149 7 VAL C C 176.230 0.016 1 18 149 7 VAL CA C 61.782 0.046 1 19 149 7 VAL CB C 32.001 0.020 1 20 149 7 VAL N N 120.786 0.014 1 21 150 8 VAL H H 8.231 0.001 1 22 150 8 VAL C C 175.528 0.008 1 23 150 8 VAL CA C 61.714 0.022 1 24 150 8 VAL CB C 32.059 0.005 1 25 150 8 VAL N N 123.721 0.007 1 26 151 9 ASP H H 8.255 0.001 1 27 151 9 ASP C C 176.511 0.001 1 28 151 9 ASP CA C 53.730 0.005 1 29 151 9 ASP CB C 40.826 0.030 1 30 151 9 ASP N N 124.423 0.036 1 31 152 10 THR H H 8.062 0.001 1 32 152 10 THR C C 175.888 0.013 1 33 152 10 THR CA C 64.060 0.013 1 34 152 10 THR CB C 68.636 0.015 1 35 152 10 THR N N 115.005 0.028 1 36 153 11 GLN H H 8.297 0.001 1 37 153 11 GLN HE21 H 7.913 0.005 1 38 153 11 GLN HE22 H 6.869 0.005 1 39 153 11 GLN C C 176.892 0.005 1 40 153 11 GLN CA C 57.477 0.012 1 41 153 11 GLN CB C 27.740 0.012 1 42 153 11 GLN N N 121.548 0.021 1 43 153 11 GLN NE2 N 115.993 0.020 1 44 154 12 ARG H H 7.915 0.002 1 45 154 12 ARG C C 178.541 0.007 1 46 154 12 ARG CA C 58.065 0.009 1 47 154 12 ARG CB C 29.037 0.007 1 48 154 12 ARG N N 118.971 0.038 1 49 155 13 VAL H H 7.501 0.002 1 50 155 13 VAL C C 177.109 0.012 1 51 155 13 VAL CA C 66.419 0.010 1 52 155 13 VAL CB C 30.856 0.065 1 53 155 13 VAL N N 117.278 0.026 1 54 156 14 LEU H H 7.682 0.001 1 55 156 14 LEU C C 180.335 0.013 1 56 156 14 LEU CA C 57.725 0.038 1 57 156 14 LEU CB C 40.248 0.031 1 58 156 14 LEU N N 119.563 0.033 1 59 157 15 ASP H H 8.608 0.001 1 60 157 15 ASP C C 180.279 0.020 1 61 157 15 ASP CA C 56.934 0.039 1 62 157 15 ASP CB C 39.549 0.088 1 63 157 15 ASP N N 119.927 0.016 1 64 158 16 LEU H H 8.251 0.003 1 65 158 16 LEU C C 178.887 0.020 1 66 158 16 LEU CA C 57.606 0.034 1 67 158 16 LEU CB C 42.872 0.010 1 68 158 16 LEU N N 122.957 0.066 1 69 159 17 GLU H H 8.853 0.001 1 70 159 17 GLU C C 180.823 0.010 1 71 159 17 GLU CA C 59.831 0.014 1 72 159 17 GLU CB C 28.593 0.020 1 73 159 17 GLU N N 119.555 0.022 1 74 160 18 GLU H H 8.183 0.002 1 75 160 18 GLU C C 178.648 0.023 1 76 160 18 GLU CA C 58.716 0.062 1 77 160 18 GLU CB C 29.564 0.020 1 78 160 18 GLU N N 120.597 0.016 1 79 161 19 GLU H H 8.030 0.003 1 80 161 19 GLU C C 178.532 0.020 1 81 161 19 GLU CA C 59.196 0.007 1 82 161 19 GLU CB C 28.469 0.028 1 83 161 19 GLU N N 123.005 0.026 1 84 162 20 VAL H H 8.742 0.001 1 85 162 20 VAL C C 177.629 0.020 1 86 162 20 VAL CA C 67.126 0.017 1 87 162 20 VAL CB C 30.856 0.085 1 88 162 20 VAL N N 119.229 0.035 1 89 163 21 ALA H H 7.641 0.001 1 90 163 21 ALA C C 181.040 0.007 1 91 163 21 ALA CA C 55.044 0.040 1 92 163 21 ALA CB C 17.172 0.020 1 93 163 21 ALA N N 119.750 0.041 1 94 164 22 ARG H H 8.235 0.003 1 95 164 22 ARG C C 179.924 0.013 1 96 164 22 ARG CA C 59.401 0.016 1 97 164 22 ARG CB C 29.653 0.020 1 98 164 22 ARG N N 120.081 0.127 1 99 165 23 LEU H H 8.911 0.002 1 100 165 23 LEU C C 179.923 0.020 1 101 165 23 LEU CA C 57.636 0.020 1 102 165 23 LEU CB C 40.904 0.009 1 103 165 23 LEU N N 122.036 0.029 1 104 166 24 LYS H H 8.678 0.001 1 105 166 24 LYS C C 180.532 0.008 1 106 166 24 LYS CA C 60.504 0.009 1 107 166 24 LYS CB C 31.595 0.020 1 108 166 24 LYS N N 118.576 0.028 1 109 167 25 ARG H H 7.856 0.002 1 110 167 25 ARG C C 179.674 0.030 1 111 167 25 ARG CA C 59.270 0.011 1 112 167 25 ARG CB C 28.860 0.020 1 113 167 25 ARG N N 120.808 0.028 1 114 168 26 THR H H 8.195 0.004 1 115 168 26 THR C C 176.186 0.005 1 116 168 26 THR CA C 66.796 0.030 1 117 168 26 THR CB C 67.934 0.002 1 118 168 26 THR N N 120.002 0.083 1 119 169 27 ILE H H 8.406 0.002 1 120 169 27 ILE C C 177.273 0.002 1 121 169 27 ILE CA C 66.294 0.021 1 122 169 27 ILE CB C 37.294 0.068 1 123 169 27 ILE N N 122.908 0.032 1 124 170 28 GLY H H 7.965 0.002 1 125 170 28 GLY CA C 46.844 0.016 1 126 170 28 GLY N N 105.563 0.024 1 127 171 29 HIS H H 8.062 0.002 1 128 171 29 HIS C C 178.520 0.045 1 129 171 29 HIS CA C 59.203 0.102 1 130 171 29 HIS CB C 29.785 0.020 1 131 171 29 HIS N N 121.976 0.063 1 132 172 30 LEU H H 8.726 0.002 1 133 172 30 LEU C C 179.004 0.005 1 134 172 30 LEU CA C 57.604 0.014 1 135 172 30 LEU CB C 42.423 0.056 1 136 172 30 LEU N N 120.483 0.026 1 137 173 31 GLN H H 8.899 0.001 1 138 173 31 GLN HE21 H 7.415 0.005 1 139 173 31 GLN HE22 H 6.697 0.005 1 140 173 31 GLN C C 179.453 0.004 1 141 173 31 GLN CA C 58.933 0.001 1 142 173 31 GLN CB C 27.171 0.033 1 143 173 31 GLN N N 118.068 0.027 1 144 173 31 GLN NE2 N 110.651 0.020 1 145 174 32 GLY H H 7.657 0.001 1 146 174 32 GLY C C 176.552 0.021 1 147 174 32 GLY CA C 46.570 0.001 1 148 174 32 GLY N N 106.687 0.024 1 149 175 33 VAL H H 7.874 0.002 1 150 175 33 VAL C C 178.538 0.010 1 151 175 33 VAL CA C 65.948 0.040 1 152 175 33 VAL CB C 30.813 0.020 1 153 175 33 VAL N N 124.836 0.022 1 154 176 34 VAL H H 8.436 0.002 1 155 176 34 VAL C C 177.891 0.006 1 156 176 34 VAL CA C 67.982 0.005 1 157 176 34 VAL CB C 30.866 0.094 1 158 176 34 VAL N N 120.097 0.033 1 159 177 35 GLU H H 7.639 0.002 1 160 177 35 GLU C C 179.693 0.004 1 161 177 35 GLU CA C 59.090 0.044 1 162 177 35 GLU CB C 28.477 0.054 1 163 177 35 GLU N N 117.296 0.029 1 164 178 36 GLU H H 8.198 0.004 1 165 178 36 GLU C C 180.146 0.020 1 166 178 36 GLU CA C 59.159 0.025 1 167 178 36 GLU CB C 28.709 0.020 1 168 178 36 GLU N N 121.384 0.085 1 169 179 37 LYS H H 8.663 0.003 1 170 179 37 LYS C C 179.504 0.018 1 171 179 37 LYS CA C 57.687 0.015 1 172 179 37 LYS CB C 30.970 0.116 1 173 179 37 LYS N N 119.373 0.049 1 174 180 38 GLU H H 8.714 0.003 1 175 180 38 GLU C C 179.712 0.046 1 176 180 38 GLU CA C 59.261 0.014 1 177 180 38 GLU CB C 28.933 0.020 1 178 180 38 GLU N N 120.480 0.018 1 179 181 39 SER H H 8.331 0.002 1 180 181 39 SER C C 177.060 0.002 1 181 181 39 SER CA C 61.039 0.127 1 182 181 39 SER CB C 62.207 0.020 1 183 181 39 SER N N 115.653 0.041 1 184 182 40 ALA H H 8.183 0.002 1 185 182 40 ALA C C 179.933 0.009 1 186 182 40 ALA CA C 54.682 0.001 1 187 182 40 ALA CB C 17.644 0.081 1 188 182 40 ALA N N 124.134 0.041 1 189 183 41 LEU H H 7.962 0.002 1 190 183 41 LEU C C 179.318 0.005 1 191 183 41 LEU CA C 58.193 0.045 1 192 183 41 LEU CB C 40.832 0.020 1 193 183 41 LEU N N 120.016 0.042 1 194 184 42 GLU H H 7.720 0.002 1 195 184 42 GLU C C 179.247 0.011 1 196 184 42 GLU CA C 58.862 0.020 1 197 184 42 GLU CB C 28.826 0.020 1 198 184 42 GLU N N 119.808 0.069 1 199 185 43 LYS H H 8.332 0.001 1 200 185 43 LYS C C 179.636 0.026 1 201 185 43 LYS CA C 59.075 0.061 1 202 185 43 LYS CB C 31.486 0.081 1 203 185 43 LYS N N 120.611 0.022 1 204 186 44 HIS H H 8.520 0.001 1 205 186 44 HIS C C 177.571 0.006 1 206 186 44 HIS CA C 59.052 0.005 1 207 186 44 HIS CB C 29.185 0.063 1 208 186 44 HIS N N 118.649 0.012 1 209 187 45 ALA H H 8.148 0.002 1 210 187 45 ALA C C 180.339 0.012 1 211 187 45 ALA CA C 55.195 0.009 1 212 187 45 ALA CB C 17.130 0.020 1 213 187 45 ALA N N 121.961 0.061 1 214 188 46 THR H H 8.186 0.001 1 215 188 46 THR C C 176.702 0.020 1 216 188 46 THR CA C 66.019 0.004 1 217 188 46 THR CB C 68.360 0.074 1 218 188 46 THR N N 115.382 0.028 1 219 189 47 GLN H H 8.130 0.002 1 220 189 47 GLN HE21 H 7.733 0.005 1 221 189 47 GLN HE22 H 6.796 0.005 1 222 189 47 GLN C C 178.368 0.011 1 223 189 47 GLN CA C 58.446 0.037 1 224 189 47 GLN CB C 27.149 0.001 1 225 189 47 GLN N N 121.778 0.023 1 226 189 47 GLN NE2 N 111.901 0.020 1 227 190 48 HIS H H 8.568 0.001 1 228 190 48 HIS C C 176.563 0.020 1 229 190 48 HIS CA C 58.483 0.020 1 230 190 48 HIS CB C 28.896 0.020 1 231 190 48 HIS N N 119.356 0.042 1 232 191 49 ASN HD21 H 7.643 0.005 1 233 191 49 ASN HD22 H 6.962 0.005 1 234 191 49 ASN C C 178.229 0.020 1 235 191 49 ASN CA C 55.869 0.020 1 236 191 49 ASN ND2 N 112.423 0.020 1 237 192 50 LEU H H 7.897 0.002 1 238 192 50 LEU C C 179.200 0.020 1 239 192 50 LEU CA C 57.816 0.003 1 240 192 50 LEU N N 120.992 0.055 1 241 193 51 GLU H H 8.310 0.003 1 242 193 51 GLU C C 180.193 0.033 1 243 193 51 GLU CA C 59.280 0.001 1 244 193 51 GLU CB C 29.148 0.061 1 245 193 51 GLU N N 120.404 0.052 1 246 194 52 VAL H H 8.366 0.003 1 247 194 52 VAL C C 177.761 0.020 1 248 194 52 VAL CA C 66.474 0.010 1 249 194 52 VAL N N 118.759 0.030 1 250 195 53 HIS H H 7.988 0.002 1 251 195 53 HIS C C 178.287 0.020 1 252 195 53 HIS CA C 60.003 0.013 1 253 195 53 HIS CB C 29.489 0.049 1 254 195 53 HIS N N 119.467 0.017 1 255 196 54 GLU H H 8.409 0.001 1 256 196 54 GLU C C 178.536 0.020 1 257 196 54 GLU CA C 58.700 0.020 1 258 196 54 GLU CB C 28.647 0.020 1 259 196 54 GLU N N 118.947 0.029 1 260 197 55 MET H H 8.219 0.002 1 261 197 55 MET C C 178.367 0.020 1 262 197 55 MET CA C 58.743 0.020 1 263 197 55 MET N N 119.769 0.002 1 264 198 56 LYS H H 8.333 0.002 1 265 198 56 LYS C C 178.187 0.011 1 266 198 56 LYS CA C 59.925 0.021 1 267 198 56 LYS N N 119.813 0.055 1 268 199 57 LYS H H 7.907 0.002 1 269 199 57 LYS C C 179.273 0.035 1 270 199 57 LYS CA C 58.778 0.034 1 271 199 57 LYS CB C 31.186 0.037 1 272 199 57 LYS N N 118.312 0.049 1 273 200 58 ASN H H 8.117 0.002 1 274 200 58 ASN HD21 H 7.280 0.005 1 275 200 58 ASN HD22 H 6.921 0.005 1 276 200 58 ASN C C 178.723 0.009 1 277 200 58 ASN CA C 55.917 0.011 1 278 200 58 ASN CB C 37.806 0.020 1 279 200 58 ASN N N 117.225 0.018 1 280 200 58 ASN ND2 N 112.551 0.020 1 281 201 59 TYR H H 8.270 0.003 1 282 201 59 TYR C C 178.321 0.010 1 283 201 59 TYR CA C 62.079 0.068 1 284 201 59 TYR N N 120.157 0.036 1 285 202 60 GLU H H 8.583 0.001 1 286 202 60 GLU C C 180.332 0.014 1 287 202 60 GLU CA C 59.384 0.035 1 288 202 60 GLU N N 118.791 0.024 1 289 203 61 LEU H H 8.037 0.004 1 290 203 61 LEU C C 179.725 0.027 1 291 203 61 LEU CA C 57.545 0.021 1 292 203 61 LEU CB C 40.647 0.020 1 293 203 61 LEU N N 120.882 0.055 1 294 204 62 LYS H H 7.836 0.002 1 295 204 62 LYS C C 179.403 0.008 1 296 204 62 LYS CA C 58.941 0.020 1 297 204 62 LYS CB C 31.223 0.088 1 298 204 62 LYS N N 121.878 0.052 1 299 205 63 ILE H H 8.421 0.002 1 300 205 63 ILE C C 178.642 0.030 1 301 205 63 ILE CA C 65.150 0.021 1 302 205 63 ILE CB C 36.823 0.020 1 303 205 63 ILE N N 120.059 0.068 1 304 206 64 LYS H H 8.216 0.007 1 305 206 64 LYS C C 178.924 0.025 1 306 206 64 LYS CA C 59.375 0.010 1 307 206 64 LYS CB C 31.472 0.046 1 308 206 64 LYS N N 122.600 0.047 1 309 207 65 SER H H 8.295 0.003 1 310 207 65 SER C C 177.358 0.001 1 311 207 65 SER CA C 61.189 0.003 1 312 207 65 SER CB C 62.209 0.032 1 313 207 65 SER N N 114.834 0.042 1 314 208 66 LEU H H 8.393 0.001 1 315 208 66 LEU C C 179.225 0.011 1 316 208 66 LEU CA C 57.464 0.007 1 317 208 66 LEU CB C 41.723 0.020 1 318 208 66 LEU N N 123.264 0.059 1 319 209 67 THR H H 8.311 0.001 1 320 209 67 THR CA C 66.376 0.020 1 321 209 67 THR N N 114.449 0.054 1 322 210 68 GLN H H 8.229 0.004 1 323 210 68 GLN HE21 H 7.482 0.005 1 324 210 68 GLN HE22 H 6.841 0.005 1 325 210 68 GLN C C 179.160 0.020 1 326 210 68 GLN CA C 58.604 0.006 1 327 210 68 GLN CB C 27.898 0.020 1 328 210 68 GLN N N 121.481 0.033 1 329 210 68 GLN NE2 N 111.411 0.020 1 330 211 69 THR H H 8.279 0.002 1 331 211 69 THR C C 176.759 0.020 1 332 211 69 THR CA C 65.758 0.020 1 333 211 69 THR CB C 68.258 0.020 1 334 211 69 THR N N 117.467 0.040 1 335 212 70 HIS C C 176.908 0.020 1 336 212 70 HIS CA C 58.285 0.020 1 337 212 70 HIS CB C 29.527 0.020 1 338 213 71 GLU H H 8.371 0.001 1 339 213 71 GLU C C 179.249 0.008 1 340 213 71 GLU CA C 58.882 0.012 1 341 213 71 GLU CB C 28.675 0.020 1 342 213 71 GLU N N 118.489 0.034 1 343 214 72 ALA H H 7.860 0.001 1 344 214 72 ALA C C 179.821 0.002 1 345 214 72 ALA CA C 54.212 0.020 1 346 214 72 ALA CB C 17.524 0.063 1 347 214 72 ALA N N 120.777 0.026 1 348 215 73 ALA H H 7.956 0.001 1 349 215 73 ALA C C 180.766 0.024 1 350 215 73 ALA CA C 54.352 0.020 1 351 215 73 ALA CB C 17.346 0.020 1 352 215 73 ALA N N 122.024 0.052 1 353 216 74 VAL H H 8.206 0.001 1 354 216 74 VAL C C 177.696 0.003 1 355 216 74 VAL CA C 65.844 0.022 1 356 216 74 VAL CB C 30.987 0.020 1 357 216 74 VAL N N 118.034 0.025 1 358 217 75 ARG H H 7.921 0.003 1 359 217 75 ARG C C 178.850 0.015 1 360 217 75 ARG CA C 58.615 0.018 1 361 217 75 ARG CB C 29.106 0.047 1 362 217 75 ARG N N 119.006 0.014 1 363 218 76 LYS H H 7.700 0.003 1 364 218 76 LYS C C 178.443 0.015 1 365 218 76 LYS CA C 58.183 0.015 1 366 218 76 LYS CB C 31.743 0.014 1 367 218 76 LYS N N 118.633 0.026 1 368 219 77 LEU H H 7.758 0.001 1 369 219 77 LEU C C 178.970 0.009 1 370 219 77 LEU CA C 56.709 0.002 1 371 219 77 LEU CB C 41.912 0.060 1 372 219 77 LEU N N 120.533 0.022 1 373 220 78 VAL H H 8.252 0.005 1 374 220 78 VAL C C 177.797 0.009 1 375 220 78 VAL CA C 63.912 0.069 1 376 220 78 VAL CB C 31.272 0.020 1 377 220 78 VAL N N 118.006 0.033 1 378 221 79 SER H H 8.069 0.001 1 379 221 79 SER C C 175.360 0.001 1 380 221 79 SER CA C 59.629 0.012 1 381 221 79 SER CB C 63.046 0.020 1 382 221 79 SER N N 116.313 0.069 1 383 222 80 ALA H H 7.949 0.005 1 384 222 80 ALA C C 178.713 0.013 1 385 222 80 ALA CA C 53.241 0.002 1 386 222 80 ALA CB C 17.989 0.028 1 387 222 80 ALA N N 124.149 0.057 1 388 223 81 GLN H H 8.032 0.003 1 389 223 81 GLN HE21 H 7.486 0.005 1 390 223 81 GLN HE22 H 6.743 0.005 1 391 223 81 GLN C C 176.952 0.014 1 392 223 81 GLN CA C 56.505 0.024 1 393 223 81 GLN CB C 28.258 0.011 1 394 223 81 GLN N N 117.866 0.034 1 395 223 81 GLN NE2 N 111.273 0.020 1 396 224 82 GLU H H 8.174 0.002 1 397 224 82 GLU C C 177.066 0.020 1 398 224 82 GLU CA C 56.954 0.005 1 399 224 82 GLU CB C 29.175 0.032 1 400 224 82 GLU N N 120.457 0.011 1 401 225 83 LEU H H 7.959 0.002 1 402 225 83 LEU C C 177.929 0.009 1 403 225 83 LEU CA C 55.453 0.001 1 404 225 83 LEU CB C 41.270 0.003 1 405 225 83 LEU N N 121.424 0.009 1 406 226 84 VAL H H 7.928 0.002 1 407 226 84 VAL C C 176.866 0.020 1 408 226 84 VAL CA C 62.752 0.035 1 409 226 84 VAL CB C 31.541 0.026 1 410 226 84 VAL N N 120.128 0.010 1 411 227 85 THR H H 8.061 0.001 1 412 227 85 THR C C 174.596 0.016 1 413 227 85 THR CA C 62.049 0.002 1 414 227 85 THR CB C 69.104 0.044 1 415 227 85 THR N N 116.571 0.027 1 416 228 86 ALA H H 8.088 0.001 1 417 228 86 ALA C C 177.504 0.014 1 418 228 86 ALA CA C 52.242 0.086 1 419 228 86 ALA CB C 18.401 0.004 1 420 228 86 ALA N N 125.583 0.016 1 421 229 87 ALA H H 8.058 0.002 1 422 229 87 ALA C C 177.571 0.020 1 423 229 87 ALA CA C 52.133 0.024 1 424 229 87 ALA CB C 18.351 0.015 1 425 229 87 ALA N N 122.448 0.015 1 426 230 88 ARG H H 8.066 0.001 1 427 230 88 ARG C C 175.658 0.020 1 428 230 88 ARG CA C 55.462 0.020 1 429 230 88 ARG CB C 30.047 0.020 1 430 230 88 ARG N N 119.479 0.014 1 431 231 89 ASN HD21 H 7.513 0.005 1 432 231 89 ASN HD22 H 6.831 0.005 1 433 231 89 ASN C C 173.646 0.020 1 434 231 89 ASN CA C 52.753 0.020 1 435 231 89 ASN CB C 38.567 0.040 1 436 231 89 ASN ND2 N 112.505 0.020 1 437 232 90 TYR H H 7.550 0.001 1 438 232 90 TYR C C 180.112 0.020 1 439 232 90 TYR CA C 58.637 0.020 1 440 232 90 TYR CB C 38.606 0.020 1 441 232 90 TYR N N 124.639 0.015 1 stop_ save_