data_50078 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C assignment of BRCA2 53-131 ; _BMRB_accession_number 50078 _BMRB_flat_file_name bmr50078.str _Entry_type original _Submission_date 2019-10-23 _Accession_date 2019-10-23 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'BRCA2 fragment from aa 53 to 131' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Julien Manon H.F. . 2 Miron Simona . . 3 Carreira Aura . . 4 Theillet Francois-Xavier . . 5 Zinn-Justin Sophie . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 68 "13C chemical shifts" 215 "15N chemical shifts" 68 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-04-21 update BMRB 'update entry citation' 2019-10-29 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 50077 'BRCA2 48-218(C4A)' 50079 'BRCA2 190-284' stop_ _Original_release_date 2019-10-23 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; 1H, 13C and 15N backbone resonance assignment of the human BRCA2 N-terminal region ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 31900740 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Julien Manon . . 2 Miron Simona . . 3 Carreira Aura . . 4 Theillet Francois-Xavier . . 5 Zinn-Justin Sophie . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_volume 14 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 79 _Page_last 85 _Year 2020 _Details . loop_ _Keyword BRCA2 NMR 'breast cancer' 'intrinsically disordered protein' mitosis phosphorylation stop_ save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name 'BRCA2 53-131' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'BRCA2 53-131' $entity_1 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_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'genome stability, mitosis' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 85 _Mol_residue_sequence ; GEESEHKNNNYEPNLFKTPQ RKPSYNQLASTPIIFKEQGL TLPLYQSPVKELDKFKLDLG RNVPNSRHKSLRTVKTKMDQ ADDVS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 47 GLY 2 48 GLU 3 49 GLU 4 50 SER 5 51 GLU 6 52 HIS 7 53 LYS 8 54 ASN 9 55 ASN 10 56 ASN 11 57 TYR 12 58 GLU 13 59 PRO 14 60 ASN 15 61 LEU 16 62 PHE 17 63 LYS 18 64 THR 19 65 PRO 20 66 GLN 21 67 ARG 22 68 LYS 23 69 PRO 24 70 SER 25 71 TYR 26 72 ASN 27 73 GLN 28 74 LEU 29 75 ALA 30 76 SER 31 77 THR 32 78 PRO 33 79 ILE 34 80 ILE 35 81 PHE 36 82 LYS 37 83 GLU 38 84 GLN 39 85 GLY 40 86 LEU 41 87 THR 42 88 LEU 43 89 PRO 44 90 LEU 45 91 TYR 46 92 GLN 47 93 SER 48 94 PRO 49 95 VAL 50 96 LYS 51 97 GLU 52 98 LEU 53 99 ASP 54 100 LYS 55 101 PHE 56 102 LYS 57 103 LEU 58 104 ASP 59 105 LEU 60 106 GLY 61 107 ARG 62 108 ASN 63 109 VAL 64 110 PRO 65 111 ASN 66 112 SER 67 113 ARG 68 114 HIS 69 115 LYS 70 116 SER 71 117 LEU 72 118 ARG 73 119 THR 74 120 VAL 75 121 LYS 76 122 THR 77 123 LYS 78 124 MET 79 125 ASP 80 126 GLN 81 127 ALA 82 128 ASP 83 129 ASP 84 130 VAL 85 131 SER 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 UNP P51587 BRCA2 . . . . . 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 _Gene_mnemonic $entity_1 Human 9606 Eukaryota Metazoa Homo sapiens BRCA2 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 plasmid pET-41b 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 0.2 mM '[U-95% 13C; U-95% 15N]' HEPES 50 mM 'natural abundance' EDTA 1 mM 'natural abundance' DTT 2 mM 'natural abundance' DSS 50 uM 'natural abundance' D2O 10 % '[U-99% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name CcpNMR _Version 2.4 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . CCPN . . stop_ loop_ _Task 'chemical shift assignment' collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details '600 MHz Bruker Advance II' save_ ############################# # NMR applied experiments # ############################# save_3D_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _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_2D_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '50 mM Hepes, 1 mM EDTA, 2 mM DTT, pH 7.0, 10 % D2O, 50 uM DSS' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0 . M pH 7.0 . pH pressure 1 . atm temperature 283 . 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 0.244 internal indirect . . . . DSS H 1 'methyl protons' ppm 0.22 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0.244 internal indirect . . . . 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 '3D HNCACB' '2D 1H-15N HSQC' '3D CBCA(CO)NH' '2D 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 'BRCA2 53-131' _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 55 9 ASN C C 174.32 . 1 2 55 9 ASN CA C 53.15 . 1 3 55 9 ASN CB C 38.37 . 1 4 56 10 ASN H H 7.97 . 1 5 56 10 ASN C C 174.18 . 1 6 56 10 ASN CA C 52.83 . 1 7 56 10 ASN CB C 38.21 . 1 8 56 10 ASN N N 118.43 . 1 9 57 11 TYR H H 7.76 . 1 10 57 11 TYR C C 174.7 . 1 11 57 11 TYR CA C 57.44 . 1 12 57 11 TYR CB C 38.17 . 1 13 57 11 TYR N N 120.48 . 1 14 58 12 GLU H H 7.77 . 1 15 58 12 GLU C C 173.54 . 1 16 58 12 GLU CA C 53.35 . 1 17 58 12 GLU CB C 29.71 . 1 18 58 12 GLU N N 125.08 . 1 19 59 13 PRO C C 176.33 . 1 20 59 13 PRO CA C 62.93 . 1 21 59 13 PRO CB C 31.5 . 1 22 60 14 ASN H H 8.18 . 1 23 60 14 ASN C C 174.86 . 1 24 60 14 ASN CA C 52.92 . 1 25 60 14 ASN CB C 37.88 . 1 26 60 14 ASN N N 117.65 . 1 27 61 15 LEU H H 7.69 . 1 28 61 15 LEU C C 176.67 . 1 29 61 15 LEU CA C 54.98 . 1 30 61 15 LEU CB C 41.65 . 1 31 61 15 LEU N N 122.06 . 1 32 62 16 PHE H H 7.72 . 1 33 62 16 PHE C C 175.13 . 1 34 62 16 PHE CA C 57.17 . 1 35 62 16 PHE CB C 38.81 . 1 36 62 16 PHE N N 119.51 . 1 37 63 17 LYS H H 7.68 . 1 38 63 17 LYS C C 175.65 . 1 39 63 17 LYS CA C 55.46 . 1 40 63 17 LYS CB C 32.63 . 1 41 63 17 LYS N N 122.21 . 1 42 64 18 THR H H 7.76 . 1 43 64 18 THR C C 172.36 . 1 44 64 18 THR CA C 59.66 . 1 45 64 18 THR CB C 68.97 . 1 46 64 18 THR N N 117.66 . 1 47 65 19 PRO C C 176.35 . 1 48 65 19 PRO CA C 62.64 . 1 49 65 19 PRO CB C 31.57 . 1 50 66 20 GLN H H 8.13 . 1 51 66 20 GLN C C 175.49 . 1 52 66 20 GLN CA C 55.25 . 1 53 66 20 GLN CB C 29.05 . 1 54 66 20 GLN N N 120.84 . 1 55 67 21 ARG H H 8.05 . 1 56 67 21 ARG C C 175.6 . 1 57 67 21 ARG CA C 55.26 . 1 58 67 21 ARG CB C 30.39 . 1 59 67 21 ARG N N 122.93 . 1 60 68 22 LYS H H 8.09 . 1 61 68 22 LYS C C 174.06 . 1 62 68 22 LYS CA C 53.87 . 1 63 68 22 LYS CB C 32.01 . 1 64 68 22 LYS N N 124.37 . 1 65 69 23 PRO C C 176.16 . 1 66 69 23 PRO CB C 31.36 . 1 67 70 24 SER H H 7.94 . 1 68 70 24 SER C C 173.78 . 1 69 70 24 SER CA C 57.64 . 1 70 70 24 SER CB C 63.43 . 1 71 70 24 SER N N 115.35 . 1 72 71 25 TYR H H 7.84 . 1 73 71 25 TYR C C 175.03 . 1 74 71 25 TYR CA C 57.6 . 1 75 71 25 TYR CB C 38.33 . 1 76 71 25 TYR N N 121.82 . 1 77 72 26 ASN H H 7.93 . 1 78 72 26 ASN C C 174.41 . 1 79 72 26 ASN CA C 52.63 . 1 80 72 26 ASN CB C 38.16 . 1 81 72 26 ASN N N 120.2 . 1 82 73 27 GLN H H 7.88 . 1 83 73 27 GLN C C 175.55 . 1 84 73 27 GLN CA C 55.7 . 1 85 73 27 GLN CB C 28.66 . 1 86 73 27 GLN N N 120.79 . 1 87 74 28 LEU H H 7.83 . 1 88 74 28 LEU C C 176.9 . 1 89 74 28 LEU CA C 54.56 . 1 90 74 28 LEU CB C 41.66 . 1 91 74 28 LEU N N 122.73 . 1 92 75 29 ALA H H 7.84 . 1 93 75 29 ALA C C 177.23 . 1 94 75 29 ALA CA C 52.07 . 1 95 75 29 ALA CB C 18.78 . 1 96 75 29 ALA N N 124.26 . 1 97 76 30 SER H H 7.82 . 1 98 76 30 SER C C 173.81 . 1 99 76 30 SER CA C 57.81 . 1 100 76 30 SER CB C 63.29 . 1 101 76 30 SER N N 114.52 . 1 102 77 31 THR H H 7.74 . 1 103 77 31 THR C C 172.19 . 1 104 77 31 THR CA C 59.57 . 1 105 77 31 THR CB C 69.14 . 1 106 77 31 THR N N 118.25 . 1 107 78 32 PRO C C 176.11 . 1 108 78 32 PRO CA C 62.73 . 1 109 78 32 PRO CB C 31.71 . 1 110 79 33 ILE H H 7.89 . 1 111 79 33 ILE C C 175.56 . 1 112 79 33 ILE CA C 60.8 . 1 113 79 33 ILE CB C 37.91 . 1 114 79 33 ILE N N 121.94 . 1 115 80 34 ILE H H 7.77 . 1 116 80 34 ILE C C 175.31 . 1 117 80 34 ILE CA C 60.22 . 1 118 80 34 ILE CB C 38.02 . 1 119 80 34 ILE N N 125.36 . 1 120 81 35 PHE H H 8.05 . 1 121 81 35 PHE C C 174.95 . 1 122 81 35 PHE CA C 57.38 . 1 123 81 35 PHE CB C 38.81 . 1 124 81 35 PHE N N 125.63 . 1 125 82 36 LYS H H 7.82 . 1 126 82 36 LYS C C 175.47 . 1 127 82 36 LYS CA C 55.74 . 1 128 82 36 LYS CB C 32.91 . 1 129 82 36 LYS N N 123.92 . 1 130 83 37 GLU H H 8.04 . 1 131 83 37 GLU C C 176.07 . 1 132 83 37 GLU CA C 56.21 . 1 133 83 37 GLU CB C 29.52 . 1 134 83 37 GLU N N 122.24 . 1 135 84 38 GLN H H 8.11 . 1 136 84 38 GLN C C 176.04 . 1 137 84 38 GLN CA C 55.76 . 1 138 84 38 GLN CB C 29.07 . 1 139 84 38 GLN N N 121.46 . 1 140 85 39 GLY H H 8.09 . 1 141 85 39 GLY C C 173.5 . 1 142 85 39 GLY CA C 44.85 . 1 143 85 39 GLY N N 109.53 . 1 144 86 40 LEU H H 7.73 . 1 145 86 40 LEU C C 177.11 . 1 146 86 40 LEU CA C 54.56 . 1 147 86 40 LEU CB C 42.01 . 1 148 86 40 LEU N N 121.08 . 1 149 87 41 THR H H 7.84 . 1 150 87 41 THR C C 173.68 . 1 151 87 41 THR CA C 61.38 . 1 152 87 41 THR CB C 69.26 . 1 153 87 41 THR N N 115.92 . 1 154 88 42 LEU H H 7.91 . 1 155 88 42 LEU C C 174.6 . 1 156 88 42 LEU CA C 52.6 . 1 157 88 42 LEU CB C 41.07 . 1 158 88 42 LEU N N 126.35 . 1 159 89 43 PRO C C 176.08 . 1 160 89 43 PRO CA C 62.31 . 1 161 89 43 PRO CB C 31.43 . 1 162 90 44 LEU H H 7.84 . 1 163 90 44 LEU C C 176.72 . 1 164 90 44 LEU CA C 54.78 . 1 165 90 44 LEU CB C 41.79 . 1 166 90 44 LEU N N 121.52 . 1 167 91 45 TYR H H 7.75 . 1 168 91 45 TYR C C 174.82 . 1 169 91 45 TYR CA C 57.4 . 1 170 91 45 TYR CB C 38.21 . 1 171 91 45 TYR N N 120.51 . 1 172 92 46 GLN H H 7.69 . 1 173 92 46 GLN C C 174.46 . 1 174 92 46 GLN CA C 54.5 . 1 175 92 46 GLN CB C 29.55 . 1 176 92 46 GLN N N 122.77 . 1 177 93 47 SER H H 7.99 . 1 178 93 47 SER C C 172.42 . 1 179 93 47 SER CA C 56.17 . 1 180 93 47 SER CB C 62.59 . 1 181 93 47 SER N N 119.06 . 1 182 94 48 PRO C C 176.4 . 1 183 95 49 VAL H H 7.8 . 1 184 95 49 VAL C C 175.82 . 1 185 95 49 VAL N N 120.6 . 1 186 96 50 LYS H H 8.02 . 1 187 96 50 LYS C C 176.1 . 1 188 96 50 LYS CA C 55.98 . 1 189 96 50 LYS CB C 32.31 . 1 190 96 50 LYS N N 125.31 . 1 191 97 51 GLU H H 8.08 . 1 192 97 51 GLU C C 176.19 . 1 193 97 51 GLU CA C 56.34 . 1 194 97 51 GLU CB C 29.61 . 1 195 97 51 GLU N N 122.49 . 1 196 98 52 LEU H H 7.91 . 1 197 98 52 LEU C C 177.04 . 1 198 98 52 LEU CA C 55.13 . 1 199 98 52 LEU CB C 41.8 . 1 200 98 52 LEU N N 122.48 . 1 201 99 53 ASP H H 7.91 . 1 202 99 53 ASP C C 176.35 . 1 203 99 53 ASP CA C 54.1 . 1 204 99 53 ASP CB C 40.5 . 1 205 99 53 ASP N N 120.53 . 1 206 100 54 LYS H H 7.73 . 1 207 100 54 LYS C C 176.36 . 1 208 100 54 LYS CA C 56.8 . 1 209 100 54 LYS CB C 31.91 . 1 210 100 54 LYS N N 121.04 . 1 211 101 55 PHE H H 7.72 . 1 212 101 55 PHE C C 175.58 . 1 213 101 55 PHE CA C 57.55 . 1 214 101 55 PHE CB C 38.46 . 1 215 101 55 PHE N N 119.05 . 1 216 102 56 LYS H H 7.5 . 1 217 102 56 LYS C C 176.04 . 1 218 102 56 LYS CA C 56.22 . 1 219 102 56 LYS CB C 32.43 . 1 220 102 56 LYS N N 121.37 . 1 221 103 57 LEU H H 7.73 . 1 222 103 57 LEU C C 176.64 . 1 223 103 57 LEU CA C 54.98 . 1 224 103 57 LEU CB C 41.86 . 1 225 103 57 LEU N N 122.46 . 1 226 104 58 ASP H H 7.94 . 1 227 104 58 ASP C C 176.12 . 1 228 104 58 ASP CA C 53.73 . 1 229 104 58 ASP CB C 40.45 . 1 230 104 58 ASP N N 121 . 1 231 105 59 LEU H H 7.87 . 1 232 105 59 LEU C C 177.93 . 1 233 105 59 LEU CA C 55.3 . 1 234 105 59 LEU CB C 40.47 . 1 235 105 59 LEU N N 122.88 . 1 236 106 60 GLY H H 8.06 . 1 237 106 60 GLY C C 174.01 . 1 238 106 60 GLY CA C 45.12 . 1 239 106 60 GLY N N 108.14 . 1 240 107 61 ARG H H 7.57 . 1 241 107 61 ARG C C 175.63 . 1 242 107 61 ARG CA C 55.78 . 1 243 107 61 ARG CB C 30.05 . 1 244 107 61 ARG N N 119.37 . 1 245 108 62 ASN H H 8.08 . 1 246 108 62 ASN C C 174.28 . 1 247 108 62 ASN CA C 52.83 . 1 248 108 62 ASN CB C 38.23 . 1 249 108 62 ASN N N 119.17 . 1 250 109 63 VAL H H 7.69 . 1 251 109 63 VAL C C 174.09 . 1 252 109 63 VAL CA C 59.55 . 1 253 109 63 VAL CB C 32 . 1 254 109 63 VAL N N 121.45 . 1 255 110 64 PRO C C 176.35 . 1 256 111 65 ASN H H 8.23 . 1 257 111 65 ASN C C 175.07 . 1 258 111 65 ASN CA C 53.09 . 1 259 111 65 ASN CB C 38.16 . 1 260 111 65 ASN N N 118.62 . 1 261 112 66 SER H H 7.92 . 1 262 112 66 SER C C 174.43 . 1 263 112 66 SER CA C 58.37 . 1 264 112 66 SER CB C 62.95 . 1 265 112 66 SER N N 115.85 . 1 266 113 67 ARG H H 7.96 . 1 267 113 67 ARG C C 175.85 . 1 268 113 67 ARG CB C 29.64 . 1 269 113 67 ARG N N 122.19 . 1 270 114 68 HIS H H 7.79 . 1 271 114 68 HIS C C 175.21 . 1 272 114 68 HIS CB C 30.35 . 1 273 114 68 HIS N N 120.08 . 1 274 116 70 SER H H 8.06 . 1 275 116 70 SER C C 174.12 . 1 276 116 70 SER CA C 58.14 . 1 277 116 70 SER CB C 63.14 . 1 278 116 70 SER N N 116.79 . 1 279 117 71 LEU H H 7.93 . 1 280 117 71 LEU C C 176.9 . 1 281 117 71 LEU CA C 54.79 . 1 282 117 71 LEU CB C 41.64 . 1 283 117 71 LEU N N 123.97 . 1 284 118 72 ARG H H 7.9 . 1 285 118 72 ARG C C 175.91 . 1 286 118 72 ARG CA C 55.72 . 1 287 118 72 ARG CB C 30.16 . 1 288 118 72 ARG N N 121.41 . 1 289 119 73 THR H H 7.84 . 1 290 119 73 THR C C 173.97 . 1 291 119 73 THR CA C 61.37 . 1 292 119 73 THR CB C 69.28 . 1 293 119 73 THR N N 115.82 . 1 294 120 74 VAL H H 7.8 . 1 295 120 74 VAL C C 175.52 . 1 296 120 74 VAL CA C 61.71 . 1 297 120 74 VAL CB C 32.31 . 1 298 120 74 VAL N N 122.6 . 1 299 121 75 LYS H H 8.1 . 1 300 121 75 LYS C C 176.24 . 1 301 121 75 LYS CA C 55.85 . 1 302 121 75 LYS CB C 32.68 . 1 303 121 75 LYS N N 125.3 . 1 304 122 76 THR H H 7.91 . 1 305 122 76 THR C C 174.07 . 1 306 122 76 THR CA C 61.45 . 1 307 122 76 THR CB C 69.59 . 1 308 122 76 THR N N 115.45 . 1 309 123 77 LYS H H 7.96 . 1 310 123 77 LYS C C 176.17 . 1 311 123 77 LYS N N 122.54 . 1 312 124 78 MET H H 8.04 . 1 313 124 78 MET C C 175.67 . 1 314 124 78 MET CA C 55.27 . 1 315 124 78 MET CB C 32.04 . 1 316 124 78 MET N N 120.86 . 1 317 125 79 ASP H H 7.9 . 1 318 125 79 ASP C C 175.59 . 1 319 125 79 ASP CA C 54.07 . 1 320 125 79 ASP CB C 40.51 . 1 321 125 79 ASP N N 120.49 . 1 322 126 80 GLN H H 7.82 . 1 323 126 80 GLN C C 175.23 . 1 324 126 80 GLN CA C 55.46 . 1 325 126 80 GLN CB C 29.05 . 1 326 126 80 GLN N N 119.63 . 1 327 127 81 ALA H H 8 . 1 328 127 81 ALA C C 177.12 . 1 329 127 81 ALA CA C 52.25 . 1 330 127 81 ALA CB C 18.9 . 1 331 127 81 ALA N N 124.84 . 1 332 128 82 ASP H H 7.9 . 1 333 128 82 ASP C C 175.52 . 1 334 128 82 ASP CA C 53.96 . 1 335 128 82 ASP CB C 40.69 . 1 336 128 82 ASP N N 118.81 . 1 337 129 83 ASP H H 7.85 . 1 338 129 83 ASP C C 175.69 . 1 339 129 83 ASP CA C 53.9 . 1 340 129 83 ASP CB C 40.62 . 1 341 129 83 ASP N N 120.11 . 1 342 130 84 VAL H H 7.68 . 1 343 130 84 VAL C C 175.11 . 1 344 130 84 VAL CA C 61.55 . 1 345 130 84 VAL CB C 32.18 . 1 346 130 84 VAL N N 119.41 . 1 347 131 85 SER H H 7.64 . 1 348 131 85 SER C C 178.27 . 1 349 131 85 SER CA C 59.84 . 1 350 131 85 SER CB C 64.28 . 1 351 131 85 SER N N 124.83 . 1 stop_ save_