data_26655 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N resonance assignments of the intrinsically disordered region of the nuclear envelope protein emerin ; _BMRB_accession_number 26655 _BMRB_flat_file_name bmr26655.str _Entry_type original _Submission_date 2015-09-11 _Accession_date 2015-09-11 _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 Samson Camille . . 2 Herrada Isaline . . 3 Celli Florian . . 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" 96 "13C chemical shifts" 202 "15N chemical shifts" 96 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-07-08 update BMRB 'update entry citation' 2016-02-12 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 26654 'emerin 67-170 (0 Mc)' stop_ _Original_release_date 2016-02-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation2 _Saveframe_category entry_citation _Citation_full . _Citation_title ; 1H, 13C and 15N backbone resonance assignment of the intrinsically disordered region of the nuclear envelope protein emerin ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26725056 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Samson Camille . . 2 Herrada Isaline . . 3 Celli Florian . . 4 Theillet Francois-Xavier . . 5 Zinn-Justin Sophie . . stop_ _Journal_abbreviation 'Biomol. NMR Assign.' _Journal_volume 10 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 179 _Page_last 182 _Year 2016 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'emerin 67-170' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'emerin 67-170' $emerin_67-170 stop_ _System_molecular_weight . _System_physical_state denatured _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_emerin_67-170 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common emerin_67-170 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 105 _Mol_residue_sequence ; GTRGDADMYDLPKKEDALLY QSKGYNDDYYEESYFTTRTY GEPESAGPSRAVRQSVTSFP DADAFHHQVHDDDLLSSSEE ECKDRERPMYGRDSAYQSIT HYRPV ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 66 GLY 2 67 THR 3 68 ARG 4 69 GLY 5 70 ASP 6 71 ALA 7 72 ASP 8 73 MET 9 74 TYR 10 75 ASP 11 76 LEU 12 77 PRO 13 78 LYS 14 79 LYS 15 80 GLU 16 81 ASP 17 82 ALA 18 83 LEU 19 84 LEU 20 85 TYR 21 86 GLN 22 87 SER 23 88 LYS 24 89 GLY 25 90 TYR 26 91 ASN 27 92 ASP 28 93 ASP 29 94 TYR 30 95 TYR 31 96 GLU 32 97 GLU 33 98 SER 34 99 TYR 35 100 PHE 36 101 THR 37 102 THR 38 103 ARG 39 104 THR 40 105 TYR 41 106 GLY 42 107 GLU 43 108 PRO 44 109 GLU 45 110 SER 46 111 ALA 47 112 GLY 48 113 PRO 49 114 SER 50 115 ARG 51 116 ALA 52 117 VAL 53 118 ARG 54 119 GLN 55 120 SER 56 121 VAL 57 122 THR 58 123 SER 59 124 PHE 60 125 PRO 61 126 ASP 62 127 ALA 63 128 ASP 64 129 ALA 65 130 PHE 66 131 HIS 67 132 HIS 68 133 GLN 69 134 VAL 70 135 HIS 71 136 ASP 72 137 ASP 73 138 ASP 74 139 LEU 75 140 LEU 76 141 SER 77 142 SER 78 143 SER 79 144 GLU 80 145 GLU 81 146 GLU 82 147 CYS 83 148 LYS 84 149 ASP 85 150 ARG 86 151 GLU 87 152 ARG 88 153 PRO 89 154 MET 90 155 TYR 91 156 GLY 92 157 ARG 93 158 ASP 94 159 SER 95 160 ALA 96 161 TYR 97 162 GLN 98 163 SER 99 164 ILE 100 165 THR 101 166 HIS 102 167 TYR 103 168 ARG 104 169 PRO 105 170 VAL 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 $emerin_67-170 human 9606 Eukaryota Metazoa Homo sapiens 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 $emerin_67-170 'recombinant technology' . Escherichia coli . pETM-13 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 $emerin_67-170 500 uM '[U-100% 13C; U-100% 15N]' urea 8 M 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 750 _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_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HCACO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCACO' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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' 30 . mM pH 6.5 . pH pressure 1 . atm temperature 303 . 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 DSS P 31 'methyl protons' ppm 0.00 na indirect . . . 0.404808636 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 HNCO' '3D HCACO' '3D CBCA(CO)NH' '3D HNCACB' 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 'emerin 67-170' _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 66 1 GLY H H 7.99 . 1 2 66 1 GLY CA C 45.38 . 1 3 66 1 GLY N N 109.47 . 1 4 67 2 THR H H 8.27 . 1 5 67 2 THR CA C 61.94 . 1 6 67 2 THR CB C 70.31 . 1 7 67 2 THR N N 113.66 . 1 8 68 3 ARG H H 8.61 . 1 9 68 3 ARG CA C 56.51 . 1 10 68 3 ARG CB C 31.13 . 1 11 68 3 ARG N N 123.42 . 1 12 69 4 GLY H H 8.54 . 1 13 69 4 GLY CA C 45.47 . 1 14 69 4 GLY N N 110.15 . 1 15 70 5 ASP CA C 54.58 . 1 16 70 5 ASP CB C 41.49 . 1 17 71 6 ALA H H 8.32 . 1 18 71 6 ALA CA C 53 . 1 19 71 6 ALA CB C 19.39 . 1 20 71 6 ALA N N 123.56 . 1 21 72 7 ASP H H 8.37 . 1 22 72 7 ASP CA C 54.67 . 1 23 72 7 ASP CB C 41.52 . 1 24 72 7 ASP N N 118.97 . 1 25 73 8 MET H H 8.19 . 1 26 73 8 MET CA C 56.03 . 1 27 73 8 MET CB C 33.01 . 1 28 73 8 MET N N 119.9 . 1 29 74 9 TYR H H 8.2 . 1 30 74 9 TYR CA C 58.25 . 1 31 74 9 TYR CB C 39.05 . 1 32 74 9 TYR N N 120.18 . 1 33 75 10 ASP H H 8.36 . 1 34 75 10 ASP CA C 54.45 . 1 35 75 10 ASP CB C 41.66 . 1 36 75 10 ASP N N 121.6 . 1 37 76 11 LEU H H 8.14 . 1 38 76 11 LEU CA C 53.02 . 1 39 76 11 LEU CB C 41.96 . 1 40 76 11 LEU N N 123.28 . 1 41 77 12 PRO CA C 63.21 . 1 42 77 12 PRO CB C 32.52 . 1 43 78 13 LYS H H 8.57 . 1 44 78 13 LYS CA C 56.35 . 1 45 78 13 LYS CB C 33.37 . 1 46 78 13 LYS N N 122.4 . 1 47 79 14 LYS H H 8.64 . 1 48 79 14 LYS CA C 56.64 . 1 49 79 14 LYS CB C 33.33 . 1 50 79 14 LYS N N 124 . 1 51 80 15 GLU H H 8.78 . 1 52 80 15 GLU CA C 56.91 . 1 53 80 15 GLU CB C 30.45 . 1 54 80 15 GLU N N 122.85 . 1 55 81 16 ASP H H 8.46 . 1 56 81 16 ASP CA C 54.58 . 1 57 81 16 ASP CB C 41.62 . 1 58 81 16 ASP N N 121.96 . 1 59 82 17 ALA H H 8.32 . 1 60 82 17 ALA CA C 53.02 . 1 61 82 17 ALA CB C 19.36 . 1 62 82 17 ALA N N 124.2 . 1 63 83 18 LEU H H 8.26 . 1 64 83 18 LEU CA C 55.36 . 1 65 83 18 LEU CB C 42.16 . 1 66 83 18 LEU N N 120.64 . 1 67 84 19 LEU H H 8.16 . 1 68 84 19 LEU CA C 55.45 . 1 69 84 19 LEU CB C 42.49 . 1 70 84 19 LEU N N 122.36 . 1 71 85 20 TYR H H 8.21 . 1 72 85 20 TYR CA C 57.96 . 1 73 85 20 TYR CB C 38.88 . 1 74 85 20 TYR N N 120.44 . 1 75 86 21 GLN H H 8.3 . 1 76 86 21 GLN CA C 55.42 . 1 77 86 21 GLN CB C 29.95 . 1 78 86 21 GLN N N 122.06 . 1 79 87 22 SER H H 8.4 . 1 80 87 22 SER CA C 58.54 . 1 81 87 22 SER CB C 64.02 . 1 82 87 22 SER N N 117.39 . 1 83 88 23 LYS H H 8.53 . 1 84 88 23 LYS CA C 56.78 . 1 85 88 23 LYS CB C 33.33 . 1 86 88 23 LYS N N 123.32 . 1 87 89 24 GLY H H 8.48 . 1 88 89 24 GLY CA C 45.32 . 1 89 89 24 GLY N N 109.76 . 1 90 90 25 TYR H H 8.16 . 1 91 90 25 TYR CA C 58.13 . 1 92 90 25 TYR CB C 39.14 . 1 93 90 25 TYR N N 119.99 . 1 94 91 26 ASN H H 8.55 . 1 95 91 26 ASN CA C 53.27 . 1 96 91 26 ASN CB C 39.27 . 1 97 91 26 ASN N N 120.36 . 1 98 92 27 ASP H H 8.34 . 1 99 92 27 ASP CA C 54.65 . 1 100 92 27 ASP CB C 41.47 . 1 101 92 27 ASP N N 120.66 . 1 102 93 28 ASP H H 8.36 . 1 103 93 28 ASP CA C 54.73 . 1 104 93 28 ASP CB C 41.45 . 1 105 93 28 ASP N N 120.14 . 1 106 94 29 TYR H H 8.12 . 1 107 94 29 TYR CA C 58.33 . 1 108 94 29 TYR CB C 39.15 . 1 109 94 29 TYR N N 120.61 . 1 110 95 30 TYR H H 8.07 . 1 111 95 30 TYR CA C 57.95 . 1 112 95 30 TYR CB C 39.4 . 1 113 95 30 TYR N N 122.61 . 1 114 96 31 GLU H H 8.25 . 1 115 96 31 GLU CA C 56.35 . 1 116 96 31 GLU CB C 30.99 . 1 117 96 31 GLU N N 123.28 . 1 118 97 32 GLU H H 8.56 . 1 119 97 32 GLU CA C 56.94 . 1 120 97 32 GLU CB C 30.42 . 1 121 97 32 GLU N N 122.83 . 1 122 98 33 SER H H 8.41 . 1 123 98 33 SER CA C 58.58 . 1 124 98 33 SER CB C 64.17 . 1 125 98 33 SER N N 116.47 . 1 126 99 34 TYR H H 8.22 . 1 127 99 34 TYR CA C 58.53 . 1 128 99 34 TYR CB C 39.05 . 1 129 99 34 TYR N N 122.3 . 1 130 100 35 PHE H H 8.18 . 1 131 100 35 PHE CA C 57.98 . 1 132 100 35 PHE CB C 39.96 . 1 133 100 35 PHE N N 120.54 . 1 134 101 36 THR H H 8.15 . 1 135 101 36 THR CA C 61.93 . 1 136 101 36 THR CB C 70.13 . 1 137 101 36 THR N N 115.31 . 1 138 102 37 THR H H 8.26 . 1 139 102 37 THR CA C 62.04 . 1 140 102 37 THR CB C 70.1 . 1 141 102 37 THR N N 116.38 . 1 142 103 38 ARG H H 8.46 . 1 143 103 38 ARG CA C 56.22 . 1 144 103 38 ARG CB C 31.21 . 1 145 103 38 ARG N N 123.85 . 1 146 104 39 THR H H 8.31 . 1 147 104 39 THR CA C 61.85 . 1 148 104 39 THR CB C 70.17 . 1 149 104 39 THR N N 115.67 . 1 150 105 40 TYR H H 8.42 . 1 151 105 40 TYR CA C 58.07 . 1 152 105 40 TYR CB C 39.31 . 1 153 105 40 TYR N N 122.56 . 1 154 106 41 GLY H H 8.38 . 1 155 106 41 GLY CA C 45.15 . 1 156 106 41 GLY N N 110.63 . 1 157 107 42 GLU H H 8.36 . 1 158 107 42 GLU CA C 54.43 . 1 159 107 42 GLU CB C 29.82 . 1 160 107 42 GLU N N 121.6 . 1 161 108 43 PRO CA C 63.48 . 1 162 108 43 PRO CB C 32.25 . 1 163 109 44 GLU H H 8.72 . 1 164 109 44 GLU CA C 57.16 . 1 165 109 44 GLU CB C 30.39 . 1 166 109 44 GLU N N 121.29 . 1 167 110 45 SER H H 8.41 . 1 168 110 45 SER CA C 58.51 . 1 169 110 45 SER CB C 64.08 . 1 170 110 45 SER N N 116.59 . 1 171 111 46 ALA H H 8.41 . 1 172 111 46 ALA CA C 52.69 . 1 173 111 46 ALA CB C 19.51 . 1 174 111 46 ALA N N 125.97 . 1 175 112 47 GLY H H 8.24 . 1 176 112 47 GLY CA C 44.65 . 1 177 112 47 GLY N N 107.93 . 1 178 113 48 PRO CA C 63.3 . 1 179 113 48 PRO CB C 32.36 . 1 180 114 49 SER H H 8.55 . 1 181 114 49 SER CA C 58.67 . 1 182 114 49 SER CB C 63.9 . 1 183 114 49 SER N N 116.34 . 1 184 115 50 ARG H H 8.52 . 1 185 115 50 ARG CA C 56.23 . 1 186 115 50 ARG CB C 31.01 . 1 187 115 50 ARG N N 123.41 . 1 188 116 51 ALA H H 8.38 . 1 189 116 51 ALA CA C 52.54 . 1 190 116 51 ALA CB C 19.36 . 1 191 116 51 ALA N N 125.2 . 1 192 117 52 VAL H H 8.22 . 1 193 117 52 VAL CA C 62.38 . 1 194 117 52 VAL CB C 33.06 . 1 195 117 52 VAL N N 120.05 . 1 196 118 53 ARG H H 8.55 . 1 197 118 53 ARG CA C 56.16 . 1 198 118 53 ARG CB C 31.1 . 1 199 118 53 ARG N N 125.33 . 1 200 119 54 GLN H H 8.64 . 1 201 119 54 GLN CA C 56 . 1 202 119 54 GLN CB C 29.91 . 1 203 119 54 GLN N N 122.68 . 1 204 120 55 SER H H 8.59 . 1 205 120 55 SER CA C 58.51 . 1 206 120 55 SER CB C 64.11 . 1 207 120 55 SER N N 117.97 . 1 208 121 56 VAL H H 8.37 . 1 209 121 56 VAL CA C 62.38 . 1 210 121 56 VAL CB C 33.17 . 1 211 121 56 VAL N N 121.67 . 1 212 122 57 THR H H 8.31 . 1 213 122 57 THR CA C 61.82 . 1 214 122 57 THR CB C 70.05 . 1 215 122 57 THR N N 117.25 . 1 216 123 58 SER H H 8.27 . 1 217 123 58 SER CA C 58.17 . 1 218 123 58 SER CB C 64.18 . 1 219 123 58 SER N N 118.22 . 1 220 124 59 PHE H H 8.42 . 1 221 124 59 PHE CA C 55.85 . 1 222 124 59 PHE CB C 39.31 . 1 223 124 59 PHE N N 122.56 . 1 224 125 60 PRO CA C 63.66 . 1 225 125 60 PRO CB C 32.25 . 1 226 126 61 ASP H H 8.42 . 1 227 126 61 ASP CA C 54.63 . 1 228 126 61 ASP CB C 41.5 . 1 229 126 61 ASP N N 120.33 . 1 230 127 62 ALA H H 8.32 . 1 231 127 62 ALA CA C 53.15 . 1 232 127 62 ALA CB C 19.36 . 1 233 127 62 ALA N N 124.19 . 1 234 128 63 ASP H H 8.39 . 1 235 128 63 ASP CA C 54.68 . 1 236 128 63 ASP CB C 41.56 . 1 237 128 63 ASP N N 118.84 . 1 238 129 64 ALA H H 8.1 . 1 239 129 64 ALA CA C 53.05 . 1 240 129 64 ALA CB C 19.3 . 1 241 129 64 ALA N N 123.6 . 1 242 130 65 PHE H H 8.17 . 1 243 130 65 PHE CA C 57.97 . 1 244 130 65 PHE CB C 39.53 . 1 245 130 65 PHE N N 117.92 . 1 246 131 66 HIS H H 8.27 . 1 247 131 66 HIS CA C 55.9 . 1 248 131 66 HIS CB C 29.7 . 1 249 131 66 HIS N N 119.91 . 1 250 132 67 HIS H H 8.5 . 1 251 132 67 HIS CA C 56.05 . 1 252 132 67 HIS N N 122.64 . 1 253 133 68 GLN CA C 56.1 . 1 254 133 68 GLN CB C 29.96 . 1 255 134 69 VAL H H 8.39 . 1 256 134 69 VAL CA C 62.46 . 1 257 134 69 VAL CB C 33.14 . 1 258 134 69 VAL N N 121.87 . 1 259 135 70 HIS H H 8.71 . 1 260 135 70 HIS CA C 55.55 . 1 261 135 70 HIS CB C 30.13 . 1 262 135 70 HIS N N 122.73 . 1 263 136 71 ASP H H 8.57 . 1 264 136 71 ASP CA C 54.99 . 1 265 136 71 ASP N N 122.86 . 1 266 137 72 ASP H H 8.6 . 1 267 137 72 ASP CA C 55.06 . 1 268 137 72 ASP CB C 41.53 . 1 269 137 72 ASP N N 120.5 . 1 270 138 73 ASP H H 8.35 . 1 271 138 73 ASP CA C 54.64 . 1 272 138 73 ASP CB C 41.68 . 1 273 138 73 ASP N N 120.9 . 1 274 139 74 LEU H H 8.19 . 1 275 139 74 LEU CA C 55.57 . 1 276 139 74 LEU CB C 42.42 . 1 277 139 74 LEU N N 121.91 . 1 278 140 75 LEU H H 8.32 . 1 279 140 75 LEU CA C 55.42 . 1 280 140 75 LEU CB C 42.59 . 1 281 140 75 LEU N N 122.51 . 1 282 141 76 SER H H 8.4 . 1 283 141 76 SER CA C 58.57 . 1 284 141 76 SER CB C 64.1 . 1 285 141 76 SER N N 116.67 . 1 286 142 77 SER H H 8.49 . 1 287 142 77 SER CA C 58.58 . 1 288 142 77 SER CB C 64.08 . 1 289 142 77 SER N N 117.77 . 1 290 143 78 SER H H 8.52 . 1 291 143 78 SER CA C 58.75 . 1 292 143 78 SER CB C 64.24 . 1 293 143 78 SER N N 117.95 . 1 294 144 79 GLU H H 8.54 . 1 295 144 79 GLU CA C 57.06 . 1 296 144 79 GLU CB C 30.46 . 1 297 144 79 GLU N N 122.71 . 1 298 145 80 GLU H H 8.45 . 1 299 145 80 GLU CA C 56.78 . 1 300 145 80 GLU CB C 30.49 . 1 301 145 80 GLU N N 121.18 . 1 302 146 81 GLU H H 8.45 . 1 303 146 81 GLU CA C 57.05 . 1 304 146 81 GLU CB C 29.96 . 1 305 146 81 GLU N N 121.75 . 1 306 147 82 CYS H H 8.52 . 1 307 147 82 CYS CA C 59.05 . 1 308 147 82 CYS CB C 27.83 . 1 309 147 82 CYS N N 120.74 . 1 310 148 83 LYS H H 8.55 . 1 311 148 83 LYS CA C 56.99 . 1 312 148 83 LYS CB C 33.21 . 1 313 148 83 LYS N N 124.5 . 1 314 149 84 ASP H H 8.4 . 1 315 149 84 ASP CA C 54.78 . 1 316 149 84 ASP CB C 41.4 . 1 317 149 84 ASP N N 120.43 . 1 318 150 85 ARG H H 8.23 . 1 319 150 85 ARG CA C 56.54 . 1 320 150 85 ARG CB C 31.16 . 1 321 150 85 ARG N N 120.76 . 1 322 151 86 GLU H H 8.48 . 1 323 151 86 GLU CA C 56.66 . 1 324 151 86 GLU CB C 30.64 . 1 325 151 86 GLU N N 121.16 . 1 326 152 87 ARG H H 8.41 . 1 327 152 87 ARG CA C 54.11 . 1 328 152 87 ARG CB C 30.44 . 1 329 152 87 ARG N N 123.17 . 1 330 153 88 PRO CA C 63.28 . 1 331 153 88 PRO CB C 32.33 . 1 332 154 89 MET H H 8.55 . 1 333 154 89 MET CA C 54.13 . 1 334 154 89 MET CB C 30.42 . 1 335 154 89 MET N N 121.16 . 1 336 155 90 TYR H H 8.27 . 1 337 155 90 TYR CA C 57.81 . 1 338 155 90 TYR CB C 39.13 . 1 339 155 90 TYR N N 120.88 . 1 340 156 91 GLY H H 8.49 . 1 341 156 91 GLY CA C 45.37 . 1 342 156 91 GLY N N 110.46 . 1 343 157 92 ARG H H 8.35 . 1 344 157 92 ARG CA C 56.52 . 1 345 157 92 ARG CB C 31.22 . 1 346 157 92 ARG N N 120.64 . 1 347 158 93 ASP H H 8.59 . 1 348 158 93 ASP CA C 54.6 . 1 349 158 93 ASP CB C 41.58 . 1 350 158 93 ASP N N 121.08 . 1 351 159 94 SER H H 8.32 . 1 352 159 94 SER CA C 58.88 . 1 353 159 94 SER CB C 64.08 . 1 354 159 94 SER N N 116.22 . 1 355 160 95 ALA H H 8.42 . 1 356 160 95 ALA CA C 52.89 . 1 357 160 95 ALA CB C 19.1 . 1 358 160 95 ALA N N 125.67 . 1 359 161 96 TYR H H 8.12 . 1 360 161 96 TYR CA C 58.2 . 1 361 161 96 TYR CB C 38.88 . 1 362 161 96 TYR N N 119.06 . 1 363 162 97 GLN H H 8.25 . 1 364 162 97 GLN CA C 55.74 . 1 365 162 97 GLN CB C 29.91 . 1 366 162 97 GLN N N 121.98 . 1 367 163 98 SER H H 8.45 . 1 368 163 98 SER CA C 58.59 . 1 369 163 98 SER CB C 64.1 . 1 370 163 98 SER N N 117.71 . 1 371 164 99 ILE H H 8.28 . 1 372 164 99 ILE CA C 61.4 . 1 373 164 99 ILE CB C 39.11 . 1 374 164 99 ILE N N 122.6 . 1 375 165 100 THR H H 8.26 . 1 376 165 100 THR CA C 61.58 . 1 377 165 100 THR CB C 70.03 . 1 378 165 100 THR N N 117.87 . 1 379 166 101 HIS CA C 56.14 . 1 380 166 101 HIS CB C 30.4 . 1 381 167 102 TYR H H 8.39 . 1 382 167 102 TYR CA C 58.12 . 1 383 167 102 TYR CB C 39.17 . 1 384 167 102 TYR N N 122.51 . 1 385 168 103 ARG H H 8.41 . 1 386 168 103 ARG CA C 52.69 . 1 387 168 103 ARG CB C 31.02 . 1 388 168 103 ARG N N 125.42 . 1 389 169 104 PRO CA C 63.23 . 1 390 169 104 PRO CB C 32.36 . 1 391 170 105 VAL H H 7.86 . 1 392 170 105 VAL CA C 63.75 . 1 393 170 105 VAL CB C 32.12 . 1 394 170 105 VAL N N 124.13 . 1 stop_ save_