data_26654 ####################### # 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 26654 _BMRB_flat_file_name bmr26654.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" 95 "13C chemical shifts" 304 "15N chemical shifts" 95 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 26655 'emerin 67-170 (8M urea)' stop_ _Original_release_date 2016-02-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _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 native _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]' 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_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _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 'Use of DSS as an internal reference (aqueous solution).' 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HCACO' '3D HNCACB' '3D CBCA(CO)NH' 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 67 2 THR CA C 62.02 . 1 2 67 2 THR CB C 70.02 . 1 3 68 3 ARG H H 8.55 . 1 4 68 3 ARG C C 176.83 . 1 5 68 3 ARG CA C 56.49 . 1 6 68 3 ARG CB C 30.79 . 1 7 68 3 ARG N N 123.36 . 1 8 69 4 GLY H H 8.48 . 1 9 69 4 GLY C C 174.12 . 1 10 69 4 GLY CA C 45.36 . 1 11 69 4 GLY N N 110.66 . 1 12 70 5 ASP H H 8.247 . 1 13 70 5 ASP C C 176.42 . 1 14 70 5 ASP CA C 54.72 . 1 15 70 5 ASP CB C 41.02 . 1 16 70 5 ASP N N 120.73 . 1 17 71 6 ALA H H 8.18 . 1 18 71 6 ALA C C 177.66 . 1 19 71 6 ALA CA C 52.88 . 1 20 71 6 ALA CB C 19.28 . 1 21 71 6 ALA N N 122.96 . 1 22 72 7 ASP H H 8.17 . 1 23 72 7 ASP C C 176.43 . 1 24 72 7 ASP CA C 54.6 . 1 25 72 7 ASP CB C 41.13 . 1 26 72 7 ASP N N 118.76 . 1 27 73 8 MET H H 8 . 1 28 73 8 MET C C 175.94 . 1 29 73 8 MET CA C 55.95 . 1 30 73 8 MET CB C 32.77 . 1 31 73 8 MET N N 119.49 . 1 32 74 9 TYR H H 8.016 . 1 33 74 9 TYR C C 175.33 . 1 34 74 9 TYR CA C 57.73 . 1 35 74 9 TYR CB C 38.79 . 1 36 74 9 TYR N N 119.92 . 1 37 75 10 ASP H H 8.163 . 1 38 75 10 ASP C C 175.49 . 1 39 75 10 ASP CA C 54.1 . 1 40 75 10 ASP CB C 41.28 . 1 41 75 10 ASP N N 121.36 . 1 42 76 11 LEU H H 7.97 . 1 43 76 11 LEU C C 175.2 . 1 44 76 11 LEU CA C 53.15 . 1 45 76 11 LEU CB C 42.03 . 1 46 76 11 LEU N N 123.31 . 1 47 77 12 PRO C C 176.87 . 1 48 77 12 PRO CA C 63.18 . 1 49 77 12 PRO CB C 32.16 . 1 50 78 13 LYS H H 8.37 . 1 51 78 13 LYS C C 176.92 . 1 52 78 13 LYS CA C 55.94 . 1 53 78 13 LYS CB C 33.23 . 1 54 78 13 LYS N N 121.77 . 1 55 79 14 LYS H H 8.42 . 1 56 79 14 LYS C C 176.88 . 1 57 79 14 LYS CA C 56.77 . 1 58 79 14 LYS CB C 33.04 . 1 59 79 14 LYS N N 123.6 . 1 60 80 15 GLU H H 8.66 . 1 61 80 15 GLU C C 176.45 . 1 62 80 15 GLU CA C 56.97 . 1 63 80 15 GLU CB C 30.03 . 1 64 80 15 GLU N N 121.79 . 1 65 81 16 ASP H H 8.22 . 1 66 81 16 ASP C C 176.42 . 1 67 81 16 ASP CA C 54.72 . 1 68 81 16 ASP CB C 41.27 . 1 69 81 16 ASP N N 121.33 . 1 70 82 17 ALA H H 8.115 . 1 71 82 17 ALA C C 178.22 . 1 72 82 17 ALA CA C 53.22 . 1 73 82 17 ALA CB C 19.15 . 1 74 82 17 ALA N N 123.85 . 1 75 83 18 LEU H H 8.07 . 1 76 83 18 LEU C C 177.82 . 1 77 83 18 LEU CA C 55.67 . 1 78 83 18 LEU CB C 41.94 . 1 79 83 18 LEU N N 119.48 . 1 80 84 19 LEU H H 7.86 . 1 81 84 19 LEU C C 177.4 . 1 82 84 19 LEU CA C 55.62 . 1 83 84 19 LEU CB C 42.19 . 1 84 84 19 LEU N N 121.22 . 1 85 85 20 TYR H H 7.91 . 1 86 85 20 TYR C C 175.88 . 1 87 85 20 TYR CA C 58.02 . 1 88 85 20 TYR CB C 38.52 . 1 89 85 20 TYR N N 119.27 . 1 90 86 21 GLN H H 8.03 . 1 91 86 21 GLN C C 175.82 . 1 92 86 21 GLN CA C 55.82 . 1 93 86 21 GLN CB C 29.6 . 1 94 86 21 GLN N N 121.26 . 1 95 87 22 SER H H 8.23 . 1 96 87 22 SER C C 174.67 . 1 97 87 22 SER CA C 58.65 . 1 98 87 22 SER CB C 63.74 . 1 99 87 22 SER N N 116.86 . 1 100 88 23 LYS H H 8.3 . 1 101 88 23 LYS C C 176.85 . 1 102 88 23 LYS CA C 56.42 . 1 103 88 23 LYS CB C 33.07 . 1 104 88 23 LYS N N 122.96 . 1 105 89 24 GLY H H 8.34 . 1 106 89 24 GLY C C 173.77 . 1 107 89 24 GLY CA C 45.17 . 1 108 89 24 GLY N N 109.55 . 1 109 90 25 TYR H H 7.941 . 1 110 90 25 TYR C C 175.5 . 1 111 90 25 TYR CA C 58.01 . 1 112 90 25 TYR CB C 38.88 . 1 113 90 25 TYR N N 119.63 . 1 114 91 26 ASN H H 8.35 . 1 115 91 26 ASN C C 174.7 . 1 116 91 26 ASN CA C 53.16 . 1 117 91 26 ASN CB C 39.16 . 1 118 91 26 ASN N N 119.93 . 1 119 92 27 ASP H H 8.18 . 1 120 92 27 ASP C C 175.94 . 1 121 92 27 ASP CA C 54.82 . 1 122 92 27 ASP CB C 41.22 . 1 123 92 27 ASP N N 120.46 . 1 124 93 28 ASP H H 8.21 . 1 125 93 28 ASP C C 175.85 . 1 126 93 28 ASP CA C 54.61 . 1 127 93 28 ASP CB C 41.01 . 1 128 93 28 ASP N N 119.66 . 1 129 94 29 TYR H H 7.95 . 1 130 94 29 TYR C C 175.29 . 1 131 94 29 TYR CA C 58.27 . 1 132 94 29 TYR CB C 38.88 . 1 133 94 29 TYR N N 120.14 . 1 134 95 30 TYR H H 7.85 . 1 135 95 30 TYR C C 175.21 . 1 136 95 30 TYR CA C 57.98 . 1 137 95 30 TYR CB C 39.17 . 1 138 95 30 TYR N N 122.06 . 1 139 96 31 GLU H H 8.05 . 1 140 96 31 GLU C C 176.26 . 1 141 96 31 GLU CA C 56.43 . 1 142 96 31 GLU CB C 30.49 . 1 143 96 31 GLU N N 122.62 . 1 144 97 32 GLU H H 8.37 . 1 145 97 32 GLU C C 176.89 . 1 146 97 32 GLU CA C 57.37 . 1 147 97 32 GLU CB C 30.12 . 1 148 97 32 GLU N N 121.95 . 1 149 98 33 SER H H 8.23 . 1 150 98 33 SER C C 174.6 . 1 151 98 33 SER CA C 58.85 . 1 152 98 33 SER CB C 63.67 . 1 153 98 33 SER N N 115.76 . 1 154 99 34 TYR H H 8.01 . 1 155 99 34 TYR C C 175.76 . 1 156 99 34 TYR CA C 58.62 . 1 157 99 34 TYR CB C 38.65 . 1 158 99 34 TYR N N 121.87 . 1 159 100 35 PHE H H 7.948 . 1 160 100 35 PHE C C 175.99 . 1 161 100 35 PHE CA C 58.04 . 1 162 100 35 PHE CB C 39.55 . 1 163 100 35 PHE N N 119.58 . 1 164 101 36 THR H H 7.94 . 1 165 101 36 THR C C 174.58 . 1 166 101 36 THR CA C 62.12 . 1 167 101 36 THR CB C 69.86 . 1 168 101 36 THR N N 114.6 . 1 169 102 37 THR H H 8.04 . 1 170 102 37 THR C C 174.45 . 1 171 102 37 THR CA C 62.12 . 1 172 102 37 THR CB C 69.81 . 1 173 102 37 THR N N 115.96 . 1 174 103 38 ARG H H 8.22 . 1 175 103 38 ARG C C 176.1 . 1 176 103 38 ARG CA C 56.06 . 1 177 103 38 ARG CB C 30.93 . 1 178 103 38 ARG N N 123.5 . 1 179 104 39 THR H H 8.11 . 1 180 104 39 THR C C 174.11 . 1 181 104 39 THR CA C 61.82 . 1 182 104 39 THR CB C 69.84 . 1 183 104 39 THR N N 115.49 . 1 184 105 40 TYR H H 8.24 . 1 185 105 40 TYR C C 176.1 . 1 186 105 40 TYR CA C 58.07 . 1 187 105 40 TYR CB C 38.99 . 1 188 105 40 TYR N N 122.46 . 1 189 106 41 GLY H H 8.23 . 1 190 106 41 GLY C C 173.6 . 1 191 106 41 GLY CA C 44.96 . 1 192 106 41 GLY N N 110.69 . 1 193 107 42 GLU H H 8.15 . 1 194 107 42 GLU C C 174.81 . 1 195 107 42 GLU CA C 54.46 . 1 196 107 42 GLU CB C 29.68 . 1 197 107 42 GLU N N 121.61 . 1 198 108 43 PRO C C 177.19 . 1 199 108 43 PRO CA C 63.4 . 1 200 108 43 PRO CB C 32.1 . 1 201 109 44 GLU H H 8.6 . 1 202 109 44 GLU C C 176.79 . 1 203 109 44 GLU CA C 57.03 . 1 204 109 44 GLU CB C 30.12 . 1 205 109 44 GLU N N 120.87 . 1 206 110 45 SER H H 8.25 . 1 207 110 45 SER C C 174.23 . 1 208 110 45 SER CA C 58.35 . 1 209 110 45 SER CB C 63.85 . 1 210 110 45 SER N N 116.35 . 1 211 111 46 ALA H H 8.28 . 1 212 111 46 ALA C C 177.75 . 1 213 111 46 ALA CA C 52.5 . 1 214 111 46 ALA CB C 19.54 . 1 215 111 46 ALA N N 125.78 . 1 216 112 47 GLY H H 8.12 . 1 217 112 47 GLY C C 178.02 . 1 218 112 47 GLY CA C 44.66 . 1 219 112 47 GLY N N 108.06 . 1 220 113 48 PRO C C 177.36 . 1 221 113 48 PRO CA C 63.36 . 1 222 113 48 PRO CB C 32.18 . 1 223 114 49 SER H H 8.38 . 1 224 114 49 SER C C 174.8 . 1 225 114 49 SER CA C 58.62 . 1 226 114 49 SER CB C 63.77 . 1 227 114 49 SER N N 115.83 . 1 228 115 50 ARG H H 8.299 . 1 229 115 50 ARG C C 175.9 . 1 230 115 50 ARG CA C 56.32 . 1 231 115 50 ARG CB C 30.8 . 1 232 115 50 ARG N N 122.93 . 1 233 116 51 ALA H H 8.2 . 1 234 116 51 ALA C C 177.65 . 1 235 116 51 ALA CA C 52.44 . 1 236 116 51 ALA CB C 19.3 . 1 237 116 51 ALA N N 124.76 . 1 238 117 52 VAL H H 8.045 . 1 239 117 52 VAL C C 176.2 . 1 240 117 52 VAL CA C 62.31 . 1 241 117 52 VAL CB C 32.83 . 1 242 117 52 VAL N N 119.57 . 1 243 118 53 ARG H H 8.36 . 1 244 118 53 ARG C C 176.1 . 1 245 118 53 ARG CA C 56.06 . 1 246 118 53 ARG CB C 30.91 . 1 247 118 53 ARG N N 124.75 . 1 248 119 54 GLN H H 8.44 . 1 249 119 54 GLN C C 175.86 . 1 250 119 54 GLN CA C 55.86 . 1 251 119 54 GLN CB C 29.64 . 1 252 119 54 GLN N N 122.04 . 1 253 120 55 SER H H 8.38 . 1 254 120 55 SER C C 174.47 . 1 255 120 55 SER CA C 58.33 . 1 256 120 55 SER CB C 63.8 . 1 257 120 55 SER N N 117.47 . 1 258 121 56 VAL H H 8.2 . 1 259 121 56 VAL C C 176.29 . 1 260 121 56 VAL CA C 62.4 . 1 261 121 56 VAL CB C 32.86 . 1 262 121 56 VAL N N 121.49 . 1 263 122 57 THR H H 8.17 . 1 264 122 57 THR C C 174.2 . 1 265 122 57 THR CA C 61.79 . 1 266 122 57 THR CB C 69.65 . 1 267 122 57 THR N N 117.06 . 1 268 123 58 SER H H 8.08 . 1 269 123 58 SER C C 173.35 . 1 270 123 58 SER CA C 58.03 . 1 271 123 58 SER CB C 63.9 . 1 272 123 58 SER N N 118.13 . 1 273 124 59 PHE H H 8.24 . 1 274 124 59 PHE C C 174.01 . 1 275 124 59 PHE CA C 55.57 . 1 276 124 59 PHE CB C 38.82 . 1 277 124 59 PHE N N 122.59 . 1 278 125 60 PRO C C 176.63 . 1 279 125 60 PRO CA C 63.56 . 1 280 125 60 PRO CB C 31.94 . 1 281 126 61 ASP H H 8.26 . 1 282 126 61 ASP C C 176.35 . 1 283 126 61 ASP CA C 54.37 . 1 284 126 61 ASP CB C 41.17 . 1 285 126 61 ASP N N 119.9 . 1 286 127 62 ALA H H 8.19 . 1 287 127 62 ALA C C 177.93 . 1 288 127 62 ALA CA C 53.15 . 1 289 127 62 ALA CB C 19.29 . 1 290 127 62 ALA N N 123.92 . 1 291 128 63 ASP H H 8.25 . 1 292 128 63 ASP C C 176.47 . 1 293 128 63 ASP CA C 54.63 . 1 294 128 63 ASP CB C 41.17 . 1 295 128 63 ASP N N 118.75 . 1 296 129 64 ALA H H 7.97 . 1 297 129 64 ALA C C 177.85 . 1 298 129 64 ALA CA C 53.16 . 1 299 129 64 ALA CB C 19.01 . 1 300 129 64 ALA N N 123.33 . 1 301 130 65 PHE H H 8.02 . 1 302 130 65 PHE C C 175.81 . 1 303 130 65 PHE CA C 58.04 . 1 304 130 65 PHE CB C 39.25 . 1 305 130 65 PHE N N 117.56 . 1 306 131 66 HIS H H 8.01 . 1 307 131 66 HIS C C 174.62 . 1 308 131 66 HIS CA C 55.89 . 1 309 131 66 HIS CB C 29.91 . 1 310 131 66 HIS N N 119.3 . 1 311 132 67 HIS H H 8.36 . 1 312 132 67 HIS CA C 55.85 . 1 313 132 67 HIS N N 121.96 . 1 314 133 68 GLN C C 175.61 . 1 315 133 68 GLN CA C 55.82 . 1 316 133 68 GLN CB C 29.72 . 1 317 134 69 VAL H H 8.18 . 1 318 134 69 VAL C C 175.49 . 1 319 134 69 VAL CA C 62.42 . 1 320 134 69 VAL CB C 32.77 . 1 321 134 69 VAL N N 121.46 . 1 322 135 70 HIS H H 8.54 . 1 323 135 70 HIS C C 174.56 . 1 324 135 70 HIS CA C 55.46 . 1 325 135 70 HIS CB C 30.05 . 1 326 135 70 HIS N N 122.66 . 1 327 136 71 ASP H H 8.38 . 1 328 136 71 ASP C C 176.15 . 1 329 136 71 ASP CA C 54.95 . 1 330 136 71 ASP CB C 41.2 . 1 331 136 71 ASP N N 122.46 . 1 332 137 72 ASP H H 8.44 . 1 333 137 72 ASP C C 176.58 . 1 334 137 72 ASP CA C 54.82 . 1 335 137 72 ASP CB C 41.15 . 1 336 137 72 ASP N N 120.31 . 1 337 138 73 ASP H H 8.25 . 1 338 138 73 ASP C C 176.56 . 1 339 138 73 ASP CA C 54.82 . 1 340 138 73 ASP CB C 41.12 . 1 341 138 73 ASP N N 120.36 . 1 342 139 74 LEU H H 8.07 . 1 343 139 74 LEU C C 177.72 . 1 344 139 74 LEU CA C 55.62 . 1 345 139 74 LEU CB C 42.18 . 1 346 139 74 LEU N N 121.6 . 1 347 140 75 LEU H H 8.11 . 1 348 140 75 LEU C C 177.72 . 1 349 140 75 LEU CA C 55.47 . 1 350 140 75 LEU CB C 42.12 . 1 351 140 75 LEU N N 121.86 . 1 352 141 76 SER H H 8.18 . 1 353 141 76 SER C C 174.75 . 1 354 141 76 SER CA C 58.53 . 1 355 141 76 SER CB C 63.79 . 1 356 141 76 SER N N 116.25 . 1 357 142 77 SER H H 8.3 . 1 358 142 77 SER C C 174.78 . 1 359 142 77 SER CA C 58.47 . 1 360 142 77 SER CB C 63.92 . 1 361 142 77 SER N N 117.56 . 1 362 143 78 SER H H 8.36 . 1 363 143 78 SER C C 174.9 . 1 364 143 78 SER CA C 58.67 . 1 365 143 78 SER CB C 63.87 . 1 366 143 78 SER N N 117.86 . 1 367 144 79 GLU H H 8.44 . 1 368 144 79 GLU C C 176.92 . 1 369 144 79 GLU CA C 57.22 . 1 370 144 79 GLU CB C 30.12 . 1 371 144 79 GLU N N 122.66 . 1 372 145 80 GLU H H 8.32 . 1 373 145 80 GLU C C 176.92 . 1 374 145 80 GLU CA C 57.17 . 1 375 145 80 GLU CB C 30.24 . 1 376 145 80 GLU N N 120.96 . 1 377 146 81 GLU H H 8.29 . 1 378 146 81 GLU C C 176.72 . 1 379 146 81 GLU CA C 57.22 . 1 380 146 81 GLU CB C 30.22 . 1 381 146 81 GLU N N 121.26 . 1 382 147 82 CYS H H 8.31 . 1 383 147 82 CYS C C 175.12 . 1 384 147 82 CYS CA C 59.02 . 1 385 147 82 CYS CB C 27.62 . 1 386 147 82 CYS N N 120.06 . 1 387 148 83 LYS H H 8.34 . 1 388 148 83 LYS C C 176.62 . 1 389 148 83 LYS CA C 56.92 . 1 390 148 83 LYS CB C 32.82 . 1 391 148 83 LYS N N 123.86 . 1 392 149 84 ASP H H 8.24 . 1 393 149 84 ASP C C 176.32 . 1 394 149 84 ASP CA C 54.82 . 1 395 149 84 ASP CB C 40.92 . 1 396 149 84 ASP N N 120.21 . 1 397 150 85 ARG H H 8.05 . 1 398 150 85 ARG C C 176.32 . 1 399 150 85 ARG CA C 56.33 . 1 400 150 85 ARG CB C 30.89 . 1 401 150 85 ARG N N 120.26 . 1 402 151 86 GLU H H 8.29 . 1 403 151 86 GLU C C 176.22 . 1 404 151 86 GLU CA C 56.52 . 1 405 151 86 GLU CB C 30.32 . 1 406 151 86 GLU N N 120.56 . 1 407 152 87 ARG H H 8.14 . 1 408 152 87 ARG C C 174.05 . 1 409 152 87 ARG CA C 54.01 . 1 410 152 87 ARG CB C 30.29 . 1 411 152 87 ARG N N 122.66 . 1 412 153 88 PRO C C 176.84 . 1 413 153 88 PRO CA C 63.14 . 1 414 153 88 PRO CB C 32.05 . 1 415 154 89 MET H H 8.37 . 1 416 154 89 MET C C 175.94 . 1 417 154 89 MET CA C 55.52 . 1 418 154 89 MET CB C 32.96 . 1 419 154 89 MET N N 120.22 . 1 420 155 90 TYR H H 8.07 . 1 421 155 90 TYR C C 176.36 . 1 422 155 90 TYR CA C 57.86 . 1 423 155 90 TYR CB C 38.81 . 1 424 155 90 TYR N N 120.43 . 1 425 156 91 GLY H H 8.34 . 1 426 156 91 GLY C C 174.28 . 1 427 156 91 GLY CA C 45.38 . 1 428 156 91 GLY N N 110.37 . 1 429 157 92 ARG H H 8.14 . 1 430 157 92 ARG C C 176.21 . 1 431 157 92 ARG CA C 56.33 . 1 432 157 92 ARG CB C 30.88 . 1 433 157 92 ARG N N 120.32 . 1 434 158 93 ASP H H 8.41 . 1 435 158 93 ASP C C 176.55 . 1 436 158 93 ASP CA C 54.53 . 1 437 158 93 ASP CB C 41.29 . 1 438 158 93 ASP N N 120.54 . 1 439 159 94 SER H H 8.17 . 1 440 159 94 SER C C 174.73 . 1 441 159 94 SER CA C 58.79 . 1 442 159 94 SER CB C 63.78 . 1 443 159 94 SER N N 116.1 . 1 444 160 95 ALA H H 8.29 . 1 445 160 95 ALA C C 177.77 . 1 446 160 95 ALA CA C 52.93 . 1 447 160 95 ALA CB C 18.98 . 1 448 160 95 ALA N N 125.33 . 1 449 161 96 TYR H H 7.95 . 1 450 161 96 TYR C C 175.88 . 1 451 161 96 TYR CA C 58.28 . 1 452 161 96 TYR CB C 38.57 . 1 453 161 96 TYR N N 118.56 . 1 454 162 97 GLN H H 8.03 . 1 455 162 97 GLN C C 175.6 . 1 456 162 97 GLN CA C 55.84 . 1 457 162 97 GLN CB C 29.6 . 1 458 162 97 GLN N N 121.15 . 1 459 163 98 SER H H 8.2 . 1 460 163 98 SER C C 174.76 . 1 461 163 98 SER CA C 58.52 . 1 462 163 98 SER CB C 63.77 . 1 463 163 98 SER N N 116.56 . 1 464 164 99 ILE H H 8.08 . 1 465 164 99 ILE C C 176.35 . 1 466 164 99 ILE CA C 61.46 . 1 467 164 99 ILE CB C 38.78 . 1 468 164 99 ILE N N 122.07 . 1 469 165 100 THR H H 8.07 . 1 470 165 100 THR C C 174.15 . 1 471 165 100 THR CA C 61.9 . 1 472 165 100 THR CB C 69.66 . 1 473 165 100 THR N N 117.21 . 1 474 166 101 HIS C C 174.45 . 1 475 166 101 HIS CA C 55.86 . 1 476 166 101 HIS CB C 30.2 . 1 477 167 102 TYR H H 8.16 . 1 478 167 102 TYR C C 174.98 . 1 479 167 102 TYR CA C 57.97 . 1 480 167 102 TYR CB C 38.82 . 1 481 167 102 TYR N N 121.96 . 1 482 168 103 ARG H H 8.06 . 1 483 168 103 ARG C C 173.29 . 1 484 168 103 ARG CA C 53.33 . 1 485 168 103 ARG CB C 30.85 . 1 486 168 103 ARG N N 125.31 . 1 487 169 104 PRO C C 176.06 . 1 488 169 104 PRO CA C 63.25 . 1 489 169 104 PRO CB C 31.89 . 1 490 170 105 VAL H H 7.64 . 1 491 170 105 VAL C C 175.12 . 1 492 170 105 VAL CA C 63.46 . 1 493 170 105 VAL CB C 33.33 . 1 494 170 105 VAL N N 123.86 . 1 stop_ save_