data_28077 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, 15N chemical shift assignments for BRCT_S3R_V63A ; _BMRB_accession_number 28077 _BMRB_flat_file_name bmr28077.str _Entry_type original _Submission_date 2020-02-09 _Accession_date 2020-02-09 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Part of the anti Tuberculosis drug discovery program' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ampapathi Ravi S. . 2 Vaishnav Jayanti . . 3 Alam Faiyaz . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 72 "13C chemical shifts" 220 "15N chemical shifts" 72 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-03-09 original BMRB . stop_ _Original_release_date 2020-02-10 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; 'Backbone 1H, 13C, 15N chemical shift assignments of BRCT' ; _Citation_status na _Citation_type 'BMRB only' _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ampapathi Ravi S. . 2 Vaishnav Jayanti . . 3 Alam Faiyaz . . stop_ _Journal_abbreviation . _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 BRCT _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label BRCT $BRCA1_C-terminal_(BRCT)_domain 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_BRCA1_C-terminal_(BRCT)_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common BRCA1_C-terminal_(BRCT)_domain _Molecular_mass 12167.65 _Mol_thiol_state 'not present' loop_ _Biological_function 'Catalytic activity' stop_ _Details ; BRCT domain is a quite flexible domain, and we have observed at least more than 50% of the residues exist in two distinct populations, which are in the slow exchange regime, and we were able to assign the peaks corresponding to second population as well. ; ############################## # Polymer residue sequence # ############################## _Residue_count 116 _Mol_residue_sequence ; MASMTGGQQMGRGSEFDERV PRTLAGLTIVVTGSLTGFSR DDAKEAIVARGGKAAGSVSK KTNYVVAGDSPGSKYDKAAE LGVPILDEDGFRRLLADGPA SRTKLAAALEHHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -15 MET 2 -14 ALA 3 -13 SER 4 -12 MET 5 -11 THR 6 -10 GLY 7 -9 GLY 8 -8 GLN 9 -7 GLN 10 -6 MET 11 -5 GLY 12 -4 ARG 13 -3 GLY 14 -2 SER 15 -1 GLU 16 0 PHE 17 1 ASP 18 2 GLU 19 3 ARG 20 4 VAL 21 5 PRO 22 6 ARG 23 7 THR 24 8 LEU 25 9 ALA 26 10 GLY 27 11 LEU 28 12 THR 29 13 ILE 30 14 VAL 31 15 VAL 32 16 THR 33 17 GLY 34 18 SER 35 19 LEU 36 20 THR 37 21 GLY 38 22 PHE 39 23 SER 40 24 ARG 41 25 ASP 42 26 ASP 43 27 ALA 44 28 LYS 45 29 GLU 46 30 ALA 47 31 ILE 48 32 VAL 49 33 ALA 50 34 ARG 51 35 GLY 52 36 GLY 53 37 LYS 54 38 ALA 55 39 ALA 56 40 GLY 57 41 SER 58 42 VAL 59 43 SER 60 44 LYS 61 45 LYS 62 46 THR 63 47 ASN 64 48 TYR 65 49 VAL 66 50 VAL 67 51 ALA 68 52 GLY 69 53 ASP 70 54 SER 71 55 PRO 72 56 GLY 73 57 SER 74 58 LYS 75 59 TYR 76 60 ASP 77 61 LYS 78 62 ALA 79 63 ALA 80 64 GLU 81 65 LEU 82 66 GLY 83 67 VAL 84 68 PRO 85 69 ILE 86 70 LEU 87 71 ASP 88 72 GLU 89 73 ASP 90 74 GLY 91 75 PHE 92 76 ARG 93 77 ARG 94 78 LEU 95 79 LEU 96 80 ALA 97 81 ASP 98 82 GLY 99 83 PRO 100 84 ALA 101 85 SER 102 86 ARG 103 87 THR 104 88 LYS 105 89 LEU 106 90 ALA 107 91 ALA 108 92 ALA 109 93 LEU 110 94 GLU 111 95 HIS 112 96 HIS 113 97 HIS 114 98 HIS 115 99 HIS 116 100 HIS 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 $BRCA1_C-terminal_(BRCT)_domain . 1773 Bacteria . Mycobacterium tuberculosis 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 $BRCA1_C-terminal_(BRCT)_domain 'recombinant technology' . Escherichia coli . pET21d 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 $BRCA1_C-terminal_(BRCT)_domain 0.5 mM '[U-99% 13C; U-99% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.113 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Agilent _Model DD2 _Field_strength 700 _Details 'Agilent DD2-700 MHz Spectrometer, four channel console, triple resonance cold probe with 13C signal enhancement' 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_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _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' 200 . mM pH 8.0 . pH pressure 1 . atm temperature 293 . 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 . 'separate tube (no insert) similar to the experimental sample tube' . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . 'separate tube (no insert) similar to the experimental sample tube' . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . 'separate tube (no insert) similar to the experimental sample tube' . 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 . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D CBCA(CO)NH' '3D HNCO' 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 BRCT _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 17 ASP H H 8.124 0.02 1 2 1 17 ASP C C 176.23 0.2 1 3 1 17 ASP CA C 54.19 0.2 1 4 1 17 ASP CB C 41.18 0.2 1 5 1 17 ASP N N 122.24 0.2 1 6 2 18 GLU H H 8.430 0.02 1 7 2 18 GLU C C 176.54 0.2 1 8 2 18 GLU CA C 56.58 0.2 1 9 2 18 GLU CB C 30.02 0.2 1 10 2 18 GLU N N 122.06 0.2 1 11 3 19 ARG H H 8.370 0.02 1 12 3 19 ARG C C 176.40 0.2 1 13 3 19 ARG CA C 56.30 0.2 1 14 3 19 ARG CB C 30.43 0.2 1 15 3 19 ARG N N 121.72 0.2 1 16 4 20 VAL H H 8.109 0.02 1 17 4 20 VAL CA C 59.73 0.2 1 18 4 20 VAL CB C 32.40 0.2 1 19 4 20 VAL N N 121.66 0.2 1 20 5 21 PRO C C 177.13 0.2 1 21 5 21 PRO CA C 62.82 0.2 1 22 5 21 PRO CB C 32.08 0.2 1 23 6 22 ARG H H 8.677 0.02 1 24 6 22 ARG C C 178.41 0.2 1 25 6 22 ARG CA C 54.81 0.2 1 26 6 22 ARG CB C 28.22 0.2 1 27 6 22 ARG N N 124.04 0.2 1 28 7 23 THR H H 8.064 0.02 1 29 7 23 THR C C 176.22 0.2 1 30 7 23 THR CA C 63.25 0.2 1 31 7 23 THR CB C 69.11 0.2 1 32 7 23 THR N N 112.60 0.2 1 33 8 24 LEU H H 8.338 0.02 1 34 8 24 LEU C C 174.93 0.2 1 35 8 24 LEU CA C 52.51 0.2 1 36 8 24 LEU CB C 40.14 0.2 1 37 8 24 LEU N N 117.57 0.2 1 38 9 25 ALA H H 7.032 0.02 1 39 9 25 ALA C C 179.05 0.2 1 40 9 25 ALA CA C 53.69 0.2 1 41 9 25 ALA CB C 18.33 0.2 1 42 9 25 ALA N N 120.75 0.2 1 43 10 26 GLY H H 8.262 0.02 1 44 10 26 GLY C C 174.52 0.2 1 45 10 26 GLY CA C 45.61 0.2 1 46 10 26 GLY N N 110.87 0.2 1 47 11 27 LEU H H 8.309 0.02 1 48 11 27 LEU C C 176.65 0.2 1 49 11 27 LEU CA C 53.81 0.2 1 50 11 27 LEU CB C 44.20 0.2 1 51 11 27 LEU N N 120.11 0.2 1 52 12 28 THR H H 9.712 0.02 1 53 12 28 THR C C 174.23 0.2 1 54 12 28 THR CA C 62.59 0.2 1 55 12 28 THR CB C 69.57 0.2 1 56 12 28 THR N N 119.97 0.2 1 57 13 29 ILE H H 9.298 0.02 1 58 13 29 ILE C C 174.35 0.2 1 59 13 29 ILE CA C 58.88 0.2 1 60 13 29 ILE CB C 41.88 0.2 1 61 13 29 ILE N N 128.73 0.2 1 62 14 30 VAL H H 8.110 0.02 1 63 14 30 VAL C C 174.07 0.2 1 64 14 30 VAL CA C 60.14 0.2 1 65 14 30 VAL CB C 34.48 0.2 1 66 14 30 VAL N N 126.72 0.2 1 67 15 31 VAL H H 8.840 0.02 1 68 15 31 VAL C C 175.09 0.2 1 69 15 31 VAL CA C 61.07 0.2 1 70 15 31 VAL CB C 32.15 0.2 1 71 15 31 VAL N N 128.24 0.2 1 72 16 32 THR H H 9.032 0.02 1 73 16 32 THR C C 172.46 0.2 1 74 16 32 THR CA C 60.09 0.2 1 75 16 32 THR CB C 70.19 0.2 1 76 16 32 THR N N 121.06 0.2 1 77 17 33 GLY H H 8.234 0.02 1 78 17 33 GLY C C 172.19 0.2 1 79 17 33 GLY CA C 44.48 0.2 1 80 17 33 GLY N N 112.29 0.2 1 81 18 34 SER H H 8.753 0.02 1 82 18 34 SER C C 174.17 0.2 1 83 18 34 SER CA C 57.71 0.2 1 84 18 34 SER CB C 64.02 0.2 1 85 18 34 SER N N 113.77 0.2 1 86 19 35 LEU H H 9.143 0.02 1 87 19 35 LEU C C 176.53 0.2 1 88 19 35 LEU CA C 53.58 0.2 1 89 19 35 LEU CB C 42.11 0.2 1 90 19 35 LEU N N 127.91 0.2 1 91 20 36 THR H H 10.304 0.02 1 92 20 36 THR C C 177.34 0.2 1 93 20 36 THR CA C 65.06 0.2 1 94 20 36 THR CB C 69.11 0.2 1 95 20 36 THR N N 119.6 0.2 1 96 21 37 GLY H H 10.48 0.02 1 97 21 37 GLY C C 173.24 0.2 1 98 21 37 GLY CA C 44.57 0.2 1 99 21 37 GLY N N 111.63 0.2 1 100 22 38 PHE H H 6.910 0.02 1 101 22 38 PHE C C 175.44 0.2 1 102 22 38 PHE CA C 56.56 0.2 1 103 22 38 PHE CB C 43.93 0.2 1 104 22 38 PHE N N 115.07 0.2 1 105 23 39 SER H H 9.380 0.02 1 106 23 39 SER CA C 57.39 0.2 1 107 23 39 SER CB C 64.63 0.2 1 108 23 39 SER N N 119.47 0.2 1 109 24 40 ARG C C 179.00 0.2 1 110 24 40 ARG CA C 59.47 0.2 1 111 24 40 ARG CB C 28.84 0.2 1 112 25 41 ASP H H 8.448 0.02 1 113 25 41 ASP C C 178.42 0.2 1 114 25 41 ASP CA C 57.19 0.2 1 115 25 41 ASP CB C 40.28 0.2 1 116 25 41 ASP N N 118.01 0.2 1 117 26 42 ASP H H 8.340 0.02 1 118 26 42 ASP C C 179.84 0.2 1 119 26 42 ASP CA C 56.93 0.2 1 120 26 42 ASP CB C 40.70 0.2 1 121 26 42 ASP N N 121.29 0.2 1 122 27 43 ALA H H 8.635 0.02 1 123 27 43 ALA C C 178.30 0.2 1 124 27 43 ALA CA C 53.41 0.2 1 125 27 43 ALA CB C 17.65 0.2 1 126 27 43 ALA N N 123.37 0.2 1 127 28 44 LYS H H 7.730 0.02 1 128 28 44 LYS C C 178.25 0.2 1 129 28 44 LYS CA C 60.47 0.2 1 130 28 44 LYS CB C 31.78 0.2 1 131 28 44 LYS N N 116.62 0.2 1 132 29 45 GLU H H 8.388 0.02 1 133 29 45 GLU C C 178.86 0.2 1 134 29 45 GLU CA C 59.11 0.2 1 135 29 45 GLU CB C 29.16 0.2 1 136 29 45 GLU N N 117.84 0.2 1 137 30 46 ALA H H 8.092 0.02 1 138 30 46 ALA C C 179.99 0.2 1 139 30 46 ALA CA C 54.58 0.2 1 140 30 46 ALA CB C 17.87 0.2 1 141 30 46 ALA N N 121.67 0.2 1 142 31 47 ILE H H 7.618 0.02 1 143 31 47 ILE C C 177.54 0.2 1 144 31 47 ILE CA C 64.36 0.2 1 145 31 47 ILE CB C 38.68 0.2 1 146 31 47 ILE N N 117.52 0.2 1 147 32 48 VAL H H 8.275 0.02 1 148 32 48 VAL C C 181.29 0.2 1 149 32 48 VAL CA C 65.12 0.2 1 150 32 48 VAL CB C 32.00 0.2 1 151 32 48 VAL N N 121.18 0.2 1 152 33 49 ALA H H 8.779 0.02 1 153 33 49 ALA C C 178.84 0.2 1 154 33 49 ALA CA C 54.60 0.2 1 155 33 49 ALA CB C 18.38 0.2 1 156 33 49 ALA N N 124.18 0.2 1 157 34 50 ARG H H 6.923 0.02 1 158 34 50 ARG CA C 54.79 0.2 1 159 34 50 ARG CB C 30.00 0.2 1 160 34 50 ARG N N 112.84 0.2 1 161 35 51 GLY C C 174.34 0.2 1 162 35 51 GLY CA C 44.99 0.2 1 163 36 52 GLY H H 8.082 0.02 1 164 36 52 GLY C C 171.90 0.2 1 165 36 52 GLY CA C 44.47 0.2 1 166 36 52 GLY N N 108.57 0.2 1 167 37 53 LYS H H 8.520 0.02 1 168 37 53 LYS C C 174.55 0.2 1 169 37 53 LYS CA C 54.77 0.2 1 170 37 53 LYS CB C 34.30 0.2 1 171 37 53 LYS N N 118.57 0.2 1 172 38 54 ALA H H 8.583 0.02 1 173 38 54 ALA C C 176.35 0.2 1 174 38 54 ALA CA C 49.73 0.2 1 175 38 54 ALA CB C 18.99 0.2 1 176 38 54 ALA N N 128.80 0.2 1 177 39 55 ALA H H 8.183 0.02 1 178 39 55 ALA C C 177.01 0.2 1 179 39 55 ALA CA C 50.70 0.2 1 180 39 55 ALA CB C 22.25 0.2 1 181 39 55 ALA N N 126.44 0.2 1 182 40 56 GLY H H 7.946 0.02 1 183 40 56 GLY C C 173.80 0.2 1 184 40 56 GLY CA C 45.92 0.2 1 185 40 56 GLY N N 114.66 0.2 1 186 41 57 SER H H 7.415 0.02 1 187 41 57 SER CA C 56.34 0.2 1 188 41 57 SER CB C 64.94 0.2 1 189 41 57 SER N N 112.83 0.2 1 190 42 58 VAL C C 174.37 0.2 1 191 42 58 VAL CA C 62.10 0.2 1 192 42 58 VAL CB C 32.32 0.2 1 193 43 59 SER H H 9.354 0.02 1 194 43 59 SER CA C 56.84 0.2 1 195 43 59 SER CB C 67.24 0.2 1 196 43 59 SER N N 124.15 0.2 1 197 44 60 LYS C C 176.37 0.2 1 198 44 60 LYS CA C 56.24 0.2 1 199 44 60 LYS CB C 30.39 0.2 1 200 45 61 LYS H H 8.187 0.02 1 201 45 61 LYS C C 176.63 0.2 1 202 45 61 LYS CA C 59.58 0.2 1 203 45 61 LYS CB C 32.47 0.2 1 204 45 61 LYS N N 122.07 0.2 1 205 46 62 THR H H 7.689 0.02 1 206 46 62 THR C C 172.89 0.2 1 207 46 62 THR CA C 65.05 0.2 1 208 46 62 THR CB C 68.47 0.2 1 209 46 62 THR N N 118.27 0.2 1 210 47 63 ASN H H 8.869 0.02 1 211 47 63 ASN C C 173.57 0.2 1 212 47 63 ASN CA C 57.20 0.2 1 213 47 63 ASN CB C 41.5 0.2 1 214 47 63 ASN N N 122.88 0.2 1 215 48 64 TYR H H 7.255 0.02 1 216 48 64 TYR C C 174.02 0.2 1 217 48 64 TYR CA C 57.24 0.2 1 218 48 64 TYR CB C 44.24 0.2 1 219 48 64 TYR N N 109.43 0.2 1 220 49 65 VAL H H 8.747 0.02 1 221 49 65 VAL C C 174.07 0.2 1 222 49 65 VAL CA C 60.17 0.2 1 223 49 65 VAL CB C 33.86 0.2 1 224 49 65 VAL N N 121.88 0.2 1 225 50 66 VAL H H 9.133 0.02 1 226 50 66 VAL C C 173.39 0.2 1 227 50 66 VAL CA C 60.56 0.2 1 228 50 66 VAL CB C 32.46 0.2 1 229 50 66 VAL N N 128.20 0.2 1 230 51 67 ALA H H 8.938 0.02 1 231 51 67 ALA C C 176.94 0.2 1 232 51 67 ALA CA C 49.97 0.2 1 233 51 67 ALA CB C 21.16 0.2 1 234 51 67 ALA N N 130.09 0.2 1 235 52 68 GLY H H 8.498 0.02 1 236 52 68 GLY C C 173.05 0.2 1 237 52 68 GLY CA C 43.38 0.2 1 238 52 68 GLY N N 110.01 0.2 1 239 53 69 ASP H H 8.573 0.02 1 240 53 69 ASP C C 176.84 0.2 1 241 53 69 ASP CA C 55.14 0.2 1 242 53 69 ASP CB C 42.04 0.2 1 243 53 69 ASP N N 121.05 0.2 1 244 54 70 SER H H 8.960 0.02 1 245 54 70 SER CA C 57.71 0.2 1 246 54 70 SER CB C 61.78 0.2 1 247 54 70 SER N N 114.57 0.2 1 248 58 74 LYS C C 177.99 0.2 1 249 59 75 TYR H H 7.587 0.02 1 250 59 75 TYR C C 175.76 0.2 1 251 59 75 TYR CA C 60.67 0.2 1 252 59 75 TYR CB C 38.94 0.2 1 253 59 75 TYR N N 118.24 0.2 1 254 60 76 ASP H H 7.353 0.02 1 255 60 76 ASP C C 178.78 0.2 1 256 60 76 ASP CA C 56.83 0.2 1 257 60 76 ASP CB C 40.11 0.2 1 258 60 76 ASP N N 118.97 0.2 1 259 61 77 LYS H H 8.285 0.02 1 260 61 77 LYS C C 177.95 0.2 1 261 61 77 LYS CA C 57.65 0.2 1 262 61 77 LYS CB C 31.49 0.2 1 263 61 77 LYS N N 120.38 0.2 1 264 62 78 ALA H H 7.837 0.02 1 265 62 78 ALA C C 178.92 0.2 1 266 62 78 ALA CA C 55.27 0.2 1 267 62 78 ALA CB C 17.92 0.2 1 268 62 78 ALA N N 120.93 0.2 1 269 63 79 ALA H H 7.993 0.02 1 270 63 79 ALA C C 181.10 0.2 1 271 63 79 ALA CA C 54.50 0.2 1 272 63 79 ALA CB C 17.41 0.2 1 273 63 79 ALA N N 119.43 0.2 1 274 64 80 GLU H H 8.063 0.02 1 275 64 80 GLU C C 178.45 0.2 1 276 64 80 GLU CA C 58.73 0.2 1 277 64 80 GLU CB C 29.72 0.2 1 278 64 80 GLU N N 119.73 0.2 1 279 65 81 LEU H H 7.856 0.02 1 280 65 81 LEU C C 177.33 0.2 1 281 65 81 LEU CA C 54.93 0.2 1 282 65 81 LEU CB C 43.33 0.2 1 283 65 81 LEU N N 116.64 0.2 1 284 66 82 GLY H H 7.854 0.02 1 285 66 82 GLY C C 174.83 0.2 1 286 66 82 GLY CA C 45.94 0.2 1 287 66 82 GLY N N 109.05 0.2 1 288 67 83 VAL H H 8.045 0.02 1 289 67 83 VAL CA C 59.73 0.2 1 290 67 83 VAL CB C 33.26 0.2 1 291 67 83 VAL N N 124.43 0.2 1 292 68 84 PRO C C 174.97 0.2 1 293 68 84 PRO CA C 63.72 0.2 1 294 68 84 PRO CB C 32.46 0.2 1 295 69 85 ILE H H 8.093 0.02 1 296 69 85 ILE C C 176.92 0.2 1 297 69 85 ILE CA C 59.49 0.2 1 298 69 85 ILE CB C 40.11 0.2 1 299 69 85 ILE N N 122.46 0.2 1 300 70 86 LEU H H 9.634 0.02 1 301 70 86 LEU C C 176.24 0.2 1 302 70 86 LEU CA C 52.72 0.2 1 303 70 86 LEU CB C 45.26 0.2 1 304 70 86 LEU N N 128.63 0.2 1 305 71 87 ASP H H 7.955 0.02 1 306 71 87 ASP C C 176.40 0.2 1 307 71 87 ASP CA C 51.07 0.2 1 308 71 87 ASP CB C 41.06 0.2 1 309 71 87 ASP N N 119.23 0.2 1 310 72 88 GLU H H 8.926 0.02 1 311 72 88 GLU C C 178.27 0.2 1 312 72 88 GLU CA C 61.37 0.2 1 313 72 88 GLU CB C 29.10 0.2 1 314 72 88 GLU N N 120.25 0.2 1 315 73 89 ASP H H 8.322 0.02 1 316 73 89 ASP C C 179.16 0.2 1 317 73 89 ASP CA C 57.76 0.2 1 318 73 89 ASP CB C 40.64 0.2 1 319 73 89 ASP N N 118.90 0.2 1 320 74 90 GLY H H 8.824 0.02 1 321 74 90 GLY C C 177.02 0.2 1 322 74 90 GLY CA C 47.05 0.2 1 323 74 90 GLY N N 109.85 0.2 1 324 75 91 PHE H H 9.096 0.02 1 325 75 91 PHE C C 176.06 0.2 1 326 75 91 PHE CA C 58.30 0.2 1 327 75 91 PHE CB C 39.14 0.2 1 328 75 91 PHE N N 124.83 0.2 1 329 76 92 ARG H H 8.590 0.02 1 330 76 92 ARG C C 179.95 0.2 1 331 76 92 ARG CA C 60.60 0.2 1 332 76 92 ARG CB C 30.05 0.2 1 333 76 92 ARG N N 118.67 0.2 1 334 77 93 ARG H H 7.933 0.02 1 335 77 93 ARG C C 177.46 0.2 1 336 77 93 ARG CA C 59.43 0.2 1 337 77 93 ARG CB C 29.80 0.2 1 338 77 93 ARG N N 119.11 0.2 1 339 78 94 LEU H H 7.886 0.02 1 340 78 94 LEU C C 179.08 0.2 1 341 78 94 LEU CA C 57.72 0.2 1 342 78 94 LEU CB C 41.67 0.2 1 343 78 94 LEU N N 122.21 0.2 1 344 79 95 LEU H H 8.091 0.02 1 345 79 95 LEU C C 178.71 0.2 1 346 79 95 LEU CA C 57.42 0.2 1 347 79 95 LEU CB C 41.86 0.2 1 348 79 95 LEU N N 115.56 0.2 1 349 80 96 ALA H H 7.301 0.02 1 350 80 96 ALA C C 179.04 0.2 1 351 80 96 ALA CA C 54.34 0.2 1 352 80 96 ALA CB C 19.37 0.2 1 353 80 96 ALA N N 118.74 0.2 1 354 81 97 ASP H H 8.542 0.02 1 355 81 97 ASP C C 178.23 0.2 1 356 81 97 ASP CA C 54.79 0.2 1 357 81 97 ASP CB C 42.80 0.2 1 358 81 97 ASP N N 114.84 0.2 1 359 82 98 GLY H H 8.398 0.02 1 360 82 98 GLY CA C 44.87 0.2 1 361 82 98 GLY N N 110.09 0.2 1 362 87 103 THR C C 173.72 0.2 1 363 87 103 THR CA C 61.86 0.2 1 364 87 103 THR CB C 69.65 0.2 1 stop_ save_