data_30021 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the pore-forming region of C. elegans Mitochondrial Calcium Uniporter (MCU) ; _BMRB_accession_number 30021 _BMRB_flat_file_name bmr30021.str _Entry_type original _Submission_date 2016-02-23 _Accession_date 2016-02-23 _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 Oxenoid K. . . 2 Dong Y. . . 3 Cao C. . . 4 Cui T. . . 5 Sancak Y. . . 6 Markhard A. L. . 7 Grabarek Z. . . 8 Kong L. . . 9 Liu Z. . . 10 Ouyang B. . . 11 Cong Y. . . 12 Mootha V. K. . 13 Chou J. J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 136 "13C chemical shifts" 385 "15N chemical shifts" 136 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-05-23 original BMRB . stop_ _Original_release_date 2016-05-23 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Architecture of the Mitochondrial Calcium Uniporter ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 27135929 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Oxenoid K. . . 2 Dong Y. . . 3 Cao C. . . 4 Cui T. . . 5 Sancak Y. . . 6 Markhard A. L. . 7 Grabarek Z. . . 8 Kong L. . . 9 Liu Z. . . 10 Ouyang B. . . 11 Cong Y. . . 12 Mootha V. K. . 13 Chou J. J. . stop_ _Journal_abbreviation Nature _Journal_volume 533 _Journal_issue . _Journal_CSD 0353 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 269 _Page_last 273 _Year 2016 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Mitochondrial Calcium Uniporter' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'entity 1' $entity_1 'entity 2' $entity_1 'entity 3' $entity_1 'entity 4' $entity_1 'entity 5' $entity_1 stop_ _System_molecular_weight . _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 'Mitochondrial Calcium Uniporter' _Molecular_mass 18927.207 _Mol_thiol_state . _Details ; Start Residues Number: 166 C-terminal 6His Tag ; ############################## # Polymer residue sequence # ############################## _Residue_count 159 _Mol_residue_sequence ; MAALSVDEYKLSREKKLLLQ LENAETLLAPLHDAKRKIEQ EAEAHTDRVAWAGFAASGVQ TGLFARLTWWEYSWDIVEPV TYFATYSTVAATFGYYLYTQ QSFEYPSARERVYTKQFYRR AQKQNFDIEKYNRLVTEVDE LRNQLKRLRDPLEHHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 166 MET 2 167 ALA 3 168 ALA 4 169 LEU 5 170 SER 6 171 VAL 7 172 ASP 8 173 GLU 9 174 TYR 10 175 LYS 11 176 LEU 12 177 SER 13 178 ARG 14 179 GLU 15 180 LYS 16 181 LYS 17 182 LEU 18 183 LEU 19 184 LEU 20 185 GLN 21 186 LEU 22 187 GLU 23 188 ASN 24 189 ALA 25 190 GLU 26 191 THR 27 192 LEU 28 193 LEU 29 194 ALA 30 195 PRO 31 196 LEU 32 197 HIS 33 198 ASP 34 199 ALA 35 200 LYS 36 201 ARG 37 202 LYS 38 203 ILE 39 204 GLU 40 205 GLN 41 206 GLU 42 207 ALA 43 208 GLU 44 209 ALA 45 210 HIS 46 211 THR 47 212 ASP 48 213 ARG 49 214 VAL 50 215 ALA 51 216 TRP 52 217 ALA 53 218 GLY 54 219 PHE 55 220 ALA 56 221 ALA 57 222 SER 58 223 GLY 59 224 VAL 60 225 GLN 61 226 THR 62 227 GLY 63 228 LEU 64 229 PHE 65 230 ALA 66 231 ARG 67 232 LEU 68 233 THR 69 234 TRP 70 235 TRP 71 236 GLU 72 237 TYR 73 238 SER 74 239 TRP 75 240 ASP 76 241 ILE 77 242 VAL 78 243 GLU 79 244 PRO 80 245 VAL 81 246 THR 82 247 TYR 83 248 PHE 84 249 ALA 85 250 THR 86 251 TYR 87 252 SER 88 253 THR 89 254 VAL 90 255 ALA 91 256 ALA 92 257 THR 93 258 PHE 94 259 GLY 95 260 TYR 96 261 TYR 97 262 LEU 98 263 TYR 99 264 THR 100 265 GLN 101 266 GLN 102 267 SER 103 268 PHE 104 269 GLU 105 270 TYR 106 271 PRO 107 272 SER 108 273 ALA 109 274 ARG 110 275 GLU 111 276 ARG 112 277 VAL 113 278 TYR 114 279 THR 115 280 LYS 116 281 GLN 117 282 PHE 118 283 TYR 119 284 ARG 120 285 ARG 121 286 ALA 122 287 GLN 123 288 LYS 124 289 GLN 125 290 ASN 126 291 PHE 127 292 ASP 128 293 ILE 129 294 GLU 130 295 LYS 131 296 TYR 132 297 ASN 133 298 ARG 134 299 LEU 135 300 VAL 136 301 THR 137 302 GLU 138 303 VAL 139 304 ASP 140 305 GLU 141 306 LEU 142 307 ARG 143 308 ASN 144 309 GLN 145 310 LEU 146 311 LYS 147 312 ARG 148 313 LEU 149 314 ARG 150 315 ASP 151 316 PRO 152 317 LEU 153 318 GLU 154 . HIS 155 . HIS 156 . HIS 157 . HIS 158 . HIS 159 . 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 _Gene_mnemonic $entity_1 nematodes 6239 Eukaryota Metazoa Caenorhabditis elegans 'mcu-1, CELE_K02B2.3, K02B2.3' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _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) pET21a . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type micelle _Details '0.8 mM [100% 13C; 100% 15N; 85% 2H] MCU-dNTD, 27 mM Foscholine-14, 20 mM MES, 75 mM NaCl, 2 mM EDTA, 0.3 mM NaN3, 95% H2O/5% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling EDTA 2 mM 'natural abundance' Foscholine-14 27 mM 'natural abundance' $entity_1 0.8 mM '[100% 13C; 100% 15N; 85% 2H]' MES 20 mM 'natural abundance' NaCl 75 mM 'natural abundance' NaN3 0.3 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type micelle _Details ; 0.8 mM [100% 13C; 100% 15N] MCU-dNTD, 27 mM [100% 2H at acyl chain] Foscholine-14, 20 mM MES, 75 mM NaCl, 2 mM EDTA, 0.3 mM NaN3, 95% H2O/5% D2O ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling EDTA 2 mM 'natural abundance' Foscholine-14 27 mM '[100% 2H at acyl chain]' $entity_1 0.8 mM '[100% 13C; 100% 15N]' MES 20 mM 'natural abundance' NaCl 75 mM 'natural abundance' NaN3 0.3 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type micelle _Details ; 0.4 mM [100% 15N; 100% 2H] MCU-dNTD, 0.4 mM [15% 13C] MCU-dNTD, 27 mM [100% 2H at acyl chain] Foscholine-14, 20 mM MES, 75 mM NaCl, 2 mM EDTA, 0.3 mM NaN3, 95% H2O/5% D2O ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling EDTA 2 mM 'natural abundance' Foscholine-14 27 mM '[100% 2H at acyl chain]' $entity_1 0.4 mM '[100% 15N; 100% 2H]' $entity_1 0.4 mM '[15% 13C]' MES 20 mM 'natural abundance' NaCl 75 mM 'natural abundance' NaN3 0.3 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name CcpNMR _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_software_2 _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_software_3 _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_software_4 _Saveframe_category software _Name TALOS _Version . loop_ _Vendor _Address _Electronic_address 'Cornilescu, Delaglio and Bax' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_software_5 _Saveframe_category software _Name XEASY _Version . loop_ _Vendor _Address _Electronic_address 'Bartels et al.' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_software_6 _Saveframe_category software _Name XPLOR-NIH _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters et al' . . stop_ loop_ _Task 'structure calculation' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AvanceII _Field_strength 600 _Details 'cryogenic probe' save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AvanceIII _Field_strength 900 _Details 'cryogenic probe' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $sample_1 save_ save_3D_tr-HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D tr-HNCA' _Sample_label $sample_1 save_ save_3D_tr-HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D tr-HN(CO)CA' _Sample_label $sample_1 save_ save_3D_tr-HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D tr-HN(CA)CO' _Sample_label $sample_1 save_ save_3D_tr-HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D tr-HNCO' _Sample_label $sample_1 save_ save_3D_tr-HN(CA)CB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D tr-HN(CA)CB' _Sample_label $sample_1 save_ save_3D_15N-15N_HSQC-NOESY-TROSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-15N HSQC-NOESY-TROSY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY-TROSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY-TROSY' _Sample_label $sample_2 save_ save_3D_1H-15N_NOESY-TROSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY-TROSY' _Sample_label $sample_2 save_ save_3D_1H-13C_Methyl_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C Methyl NOESY' _Sample_label $sample_2 save_ save_3D_1H-13C_Methyl_NOESY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C Methyl NOESY' _Sample_label $sample_2 save_ save_3D_1H-15N_NOESY-TROSY_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY-TROSY' _Sample_label $sample_3 save_ save_3D_1H-15N_NOESY-TROSY_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY-TROSY' _Sample_label $sample_3 save_ save_2D_1H-13C_HSQC_aliphatic_14 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _Sample_label $sample_2 save_ save_2D_1H-13C_HSQC_aliphatic_15 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _Sample_label $sample_3 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' 100 10 mM pH 6.5 0.1 pH pressure 1 0.01 atm temperature 306 0.2 K stop_ save_ save_sample_conditions_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 10 mM pH 6.5 0.1 pH pressure 1 0.01 atm temperature 306 0.2 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 0.000 internal indirect . . . 0.25144953 DSS H 1 'methyl protons' ppm 0.000 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.000 internal indirect . . . 0.10132912 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_2 $software_5 stop_ loop_ _Experiment_label '3D tr-HNCA' '3D tr-HN(CO)CA' '3D tr-HN(CA)CO' '3D tr-HNCO' '3D tr-HN(CA)CB' '3D 15N-15N HSQC-NOESY-TROSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_2 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name 'entity 1' _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 1 167 2 ALA H H 8.15 0.002 1 2 167 2 ALA C C 178.21 0.001 1 3 167 2 ALA CA C 52.49 0.002 1 4 167 2 ALA CB C 21.75 0.005 1 5 167 2 ALA N N 106.83 0.010 1 6 168 3 ALA H H 8.23 0.002 1 7 168 3 ALA C C 177.93 0.001 1 8 168 3 ALA CA C 52.31 0.002 1 9 168 3 ALA CB C 21.59 0.005 1 10 168 3 ALA N N 123.25 0.010 1 11 169 4 LEU H H 8.05 0.002 1 12 169 4 LEU C C 177.43 0.001 1 13 169 4 LEU CA C 55.00 0.002 1 14 169 4 LEU CB C 44.65 0.005 1 15 169 4 LEU N N 121.60 0.010 1 16 170 5 SER H H 8.25 0.002 1 17 170 5 SER C C 175.13 0.001 1 18 170 5 SER CA C 57.90 0.002 1 19 170 5 SER CB C 67.02 0.005 1 20 170 5 SER N N 117.65 0.010 1 21 171 6 VAL H H 8.16 0.002 1 22 171 6 VAL C C 176.44 0.001 1 23 171 6 VAL CA C 62.93 0.002 1 24 171 6 VAL CB C 34.25 0.005 1 25 171 6 VAL N N 122.70 0.010 1 26 172 7 ASP H H 8.16 0.002 1 27 172 7 ASP C C 177.06 0.001 1 28 172 7 ASP CA C 55.00 0.002 1 29 172 7 ASP CB C 43.95 0.005 1 30 172 7 ASP N N 122.70 0.010 1 31 173 8 GLU H H 8.11 0.002 1 32 173 8 GLU C C 177.29 0.001 1 33 173 8 GLU CA C 57.49 0.002 1 34 173 8 GLU CB C 31.99 0.005 1 35 173 8 GLU N N 121.32 0.010 1 36 174 9 TYR H H 8.07 0.002 1 37 174 9 TYR C C 176.41 0.001 1 38 174 9 TYR CA C 58.83 0.002 1 39 174 9 TYR CB C 40.35 0.005 1 40 174 9 TYR N N 120.77 0.010 1 41 175 10 LYS H H 7.89 0.002 1 42 175 10 LYS C C 177.04 0.001 1 43 175 10 LYS CA C 57.07 0.002 1 44 175 10 LYS CB C 34.26 0.005 1 45 175 10 LYS N N 121.87 0.010 1 46 176 11 LEU H H 7.96 0.002 1 47 176 11 LEU C C 177.74 0.001 1 48 176 11 LEU CA C 55.42 0.002 1 49 176 11 LEU CB C 44.82 0.005 1 50 176 11 LEU N N 121.69 0.010 1 51 177 12 SER H H 8.04 0.002 1 52 177 12 SER C C 175.67 0.001 1 53 177 12 SER CA C 58.96 0.002 1 54 177 12 SER CB C 67.02 0.005 1 55 177 12 SER N N 116.83 0.010 1 56 178 13 ARG H H 8.45 0.002 1 57 178 13 ARG C C 177.92 0.001 1 58 178 13 ARG CA C 58.41 0.002 1 59 178 13 ARG CB C 32.10 0.005 1 60 178 13 ARG N N 122.70 0.010 1 61 179 14 GLU H H 8.66 0.002 1 62 179 14 GLU C C 177.96 0.001 1 63 179 14 GLU CA C 58.99 0.002 1 64 179 14 GLU CB C 31.45 0.005 1 65 179 14 GLU N N 119.76 0.010 1 66 180 15 LYS H H 7.90 0.002 1 67 180 15 LYS C C 178.29 0.001 1 68 180 15 LYS CA C 58.31 0.002 1 69 180 15 LYS CB C 33.77 0.005 1 70 180 15 LYS N N 120.40 0.010 1 71 181 16 LYS H H 8.05 0.002 1 72 181 16 LYS C C 178.67 0.001 1 73 181 16 LYS CA C 58.63 0.002 1 74 181 16 LYS CB C 34.01 0.005 1 75 181 16 LYS N N 120.13 0.010 1 76 182 17 LEU H H 7.95 0.002 1 77 182 17 LEU C C 178.74 0.001 1 78 182 17 LEU CA C 57.18 0.002 1 79 182 17 LEU CB C 44.16 0.005 1 80 182 17 LEU N N 120.96 0.010 1 81 183 18 LEU H H 7.96 0.002 1 82 183 18 LEU C C 178.85 0.001 1 83 183 18 LEU CA C 57.33 0.002 1 84 183 18 LEU CB C 44.08 0.005 1 85 183 18 LEU N N 119.58 0.010 1 86 184 19 LEU H H 7.79 0.002 1 87 184 19 LEU C C 178.68 0.001 1 88 184 19 LEU CA C 56.50 0.002 1 89 184 19 LEU CB C 43.74 0.005 1 90 184 19 LEU N N 119.12 0.010 1 91 185 20 GLN H H 7.78 0.002 1 92 185 20 GLN C C 177.74 0.001 1 93 185 20 GLN CA C 56.97 0.002 1 94 185 20 GLN CB C 31.13 0.005 1 95 185 20 GLN N N 118.57 0.010 1 96 186 21 LEU H H 8.02 0.002 1 97 186 21 LEU C C 178.09 0.001 1 98 186 21 LEU CA C 56.66 0.002 1 99 186 21 LEU CB C 43.95 0.005 1 100 186 21 LEU N N 121.05 0.010 1 101 187 22 GLU H H 8.21 0.002 1 102 187 22 GLU C C 177.67 0.001 1 103 187 22 GLU CA C 58.49 0.002 1 104 187 22 GLU CB C 31.68 0.005 1 105 187 22 GLU N N 119.40 0.010 1 106 188 23 ASN H H 7.99 0.002 1 107 188 23 ASN C C 176.38 0.001 1 108 188 23 ASN CA C 53.85 0.002 1 109 188 23 ASN CB C 41.37 0.005 1 110 188 23 ASN N N 116.92 0.010 1 111 189 24 ALA H H 8.12 0.002 1 112 189 24 ALA C C 178.51 0.001 1 113 189 24 ALA CA C 54.38 0.002 1 114 189 24 ALA CB C 20.89 0.005 1 115 189 24 ALA N N 123.80 0.010 1 116 190 25 GLU H H 8.46 0.002 1 117 190 25 GLU C C 178.63 0.001 1 118 190 25 GLU CA C 59.35 0.002 1 119 190 25 GLU CB C 31.45 0.005 1 120 190 25 GLU N N 118.20 0.010 1 121 191 26 THR H H 7.81 0.002 1 122 191 26 THR C C 176.01 0.001 1 123 191 26 THR CA C 64.52 0.002 1 124 191 26 THR CB C 71.98 0.005 1 125 191 26 THR N N 113.25 0.010 1 126 192 27 LEU H H 7.68 0.002 1 127 192 27 LEU C C 177.08 0.001 1 128 192 27 LEU CA C 56.43 0.002 1 129 192 27 LEU CB C 44.82 0.005 1 130 192 27 LEU N N 121.23 0.010 1 131 193 28 LEU H H 7.62 0.002 1 132 193 28 LEU C C 178.29 0.001 1 133 193 28 LEU CA C 55.84 0.002 1 134 193 28 LEU CB C 44.26 0.005 1 135 193 28 LEU N N 114.81 0.010 1 136 194 29 ALA H H 7.77 0.002 1 137 194 29 ALA CA C 56.14 0.002 1 138 194 29 ALA N N 123.16 0.010 1 139 195 30 PRO C C 179.02 0.001 1 140 195 30 PRO CA C 65.27 0.002 1 141 196 31 LEU H H 7.55 0.002 1 142 196 31 LEU C C 178.32 0.001 1 143 196 31 LEU CA C 57.36 0.002 1 144 196 31 LEU N N 117.47 0.010 1 145 197 32 HIS H H 8.10 0.002 1 146 197 32 HIS C C 177.76 0.001 1 147 197 32 HIS CA C 58.94 0.002 1 148 197 32 HIS N N 119.12 0.010 1 149 198 33 ASP H H 8.26 0.002 1 150 198 33 ASP C C 178.40 0.001 1 151 198 33 ASP CA C 56.97 0.002 1 152 198 33 ASP CB C 42.23 0.005 1 153 198 33 ASP N N 120.68 0.010 1 154 199 34 ALA H H 8.06 0.002 1 155 199 34 ALA C C 178.82 0.001 1 156 199 34 ALA CA C 55.00 0.002 1 157 199 34 ALA CB C 20.89 0.005 1 158 199 34 ALA N N 123.34 0.010 1 159 200 35 LYS H H 8.10 0.002 1 160 200 35 LYS C C 177.80 0.001 1 161 200 35 LYS CA C 59.66 0.002 1 162 200 35 LYS N N 118.66 0.010 1 163 201 36 ARG H H 7.82 0.002 1 164 201 36 ARG C C 177.37 0.001 1 165 201 36 ARG CA C 58.30 0.002 1 166 201 36 ARG CB C 31.44 0.005 1 167 201 36 ARG N N 118.66 0.010 1 168 202 37 LYS H H 7.99 0.002 1 169 202 37 LYS C C 175.26 0.001 1 170 202 37 LYS CA C 58.07 0.002 1 171 202 37 LYS N N 118.57 0.010 1 172 203 38 ILE H H 7.64 0.002 1 173 203 38 ILE N N 115.27 0.010 1 174 206 41 GLU C C 178.51 0.001 1 175 206 41 GLU CA C 57.79 0.002 1 176 207 42 ALA H H 8.32 0.002 1 177 207 42 ALA C C 179.33 0.001 1 178 207 42 ALA CA C 54.38 0.002 1 179 207 42 ALA N N 122.70 0.010 1 180 208 43 GLU H H 7.87 0.002 1 181 208 43 GLU C C 178.39 0.001 1 182 208 43 GLU CA C 57.83 0.002 1 183 208 43 GLU N N 118.02 0.010 1 184 209 44 ALA H H 8.01 0.002 1 185 209 44 ALA CA C 54.07 0.002 1 186 209 44 ALA CB C 20.03 0.005 1 187 209 44 ALA N N 122.97 0.010 1 188 210 45 HIS C C 175.38 0.001 1 189 210 45 HIS CA C 55.73 0.002 1 190 211 46 THR H H 7.87 0.002 1 191 211 46 THR C C 174.94 0.001 1 192 211 46 THR CA C 63.28 0.002 1 193 211 46 THR N N 114.44 0.010 1 194 212 47 ASP H H 8.35 0.002 1 195 212 47 ASP C C 177.08 0.001 1 196 212 47 ASP CA C 54.80 0.002 1 197 212 47 ASP CB C 43.03 0.005 1 198 212 47 ASP N N 121.87 0.010 1 199 213 48 ARG H H 8.17 0.002 1 200 213 48 ARG C C 177.26 0.001 1 201 213 48 ARG CA C 57.49 0.002 1 202 213 48 ARG CB C 32.08 0.005 1 203 213 48 ARG N N 120.96 0.010 1 204 214 49 VAL H H 7.87 0.002 1 205 214 49 VAL C C 177.06 0.001 1 206 214 49 VAL CA C 63.80 0.002 1 207 214 49 VAL N N 119.40 0.010 1 208 215 50 ALA H H 8.02 0.002 1 209 215 50 ALA C C 179.24 0.001 1 210 215 50 ALA CA C 53.43 0.002 1 211 215 50 ALA N N 125.45 0.010 1 212 216 51 TRP H H 8.05 0.002 1 213 216 51 TRP C C 177.36 0.001 1 214 216 51 TRP CA C 59.04 0.002 1 215 216 51 TRP CB C 31.88 0.005 1 216 216 51 TRP N N 119.86 0.010 1 217 217 52 ALA H H 8.08 0.002 1 218 217 52 ALA C C 179.08 0.001 1 219 217 52 ALA CA C 54.28 0.002 1 220 217 52 ALA CB C 20.67 0.005 1 221 217 52 ALA N N 122.61 0.010 1 222 218 53 GLY H H 7.79 0.002 1 223 218 53 GLY C C 175.81 0.001 1 224 218 53 GLY CA C 48.80 0.002 1 225 218 53 GLY N N 105.64 0.010 1 226 219 54 PHE H H 7.93 0.002 1 227 219 54 PHE C C 177.29 0.001 1 228 219 54 PHE CA C 59.76 0.002 1 229 219 54 PHE CB C 41.37 0.005 1 230 219 54 PHE N N 121.60 0.010 1 231 220 55 ALA H H 8.19 0.002 1 232 220 55 ALA C C 178.38 0.001 1 233 220 55 ALA CA C 53.76 0.002 1 234 220 55 ALA CB C 21.10 0.005 1 235 220 55 ALA N N 122.97 0.010 1 236 221 56 ALA H H 8.02 0.002 1 237 221 56 ALA C C 178.96 0.001 1 238 221 56 ALA CA C 53.82 0.002 1 239 221 56 ALA CB C 21.36 0.005 1 240 221 56 ALA N N 120.31 0.010 1 241 222 57 SER H H 7.91 0.002 1 242 222 57 SER C C 176.22 0.001 1 243 222 57 SER CA C 60.28 0.002 1 244 222 57 SER CB C 66.23 0.005 1 245 222 57 SER N N 113.53 0.010 1 246 223 58 GLY H H 8.13 0.002 1 247 223 58 GLY C C 175.24 0.001 1 248 223 58 GLY CA C 48.49 0.002 1 249 223 58 GLY N N 110.32 0.010 1 250 224 59 VAL H H 7.84 0.002 1 251 224 59 VAL C C 176.61 0.001 1 252 224 59 VAL CA C 64.01 0.002 1 253 224 59 VAL CB C 33.79 0.005 1 254 224 59 VAL N N 119.95 0.010 1 255 225 60 GLN H H 8.17 0.002 1 256 225 60 GLN C C 176.87 0.001 1 257 225 60 GLN CA C 57.42 0.002 1 258 225 60 GLN CB C 31.36 0.005 1 259 225 60 GLN N N 121.14 0.010 1 260 226 61 THR H H 8.02 0.002 1 261 226 61 THR C C 176.28 0.001 1 262 226 61 THR CA C 63.59 0.002 1 263 226 61 THR CB C 72.19 0.005 1 264 226 61 THR N N 113.07 0.010 1 265 227 62 GLY H H 8.27 0.002 1 266 227 62 GLY C C 175.54 0.001 1 267 227 62 GLY CA C 48.56 0.002 1 268 227 62 GLY N N 110.96 0.010 1 269 228 63 LEU H H 8.07 0.002 1 270 228 63 LEU C C 178.06 0.001 1 271 228 63 LEU CA C 57.56 0.002 1 272 228 63 LEU CB C 44.73 0.005 1 273 228 63 LEU N N 122.15 0.010 1 274 229 64 PHE H H 8.05 0.002 1 275 229 64 PHE C C 177.45 0.001 1 276 229 64 PHE CA C 59.66 0.002 1 277 229 64 PHE CB C 40.29 0.005 1 278 229 64 PHE N N 116.19 0.010 1 279 230 65 ALA H H 7.78 0.002 1 280 230 65 ALA C C 179.03 0.001 1 281 230 65 ALA CA C 53.97 0.002 1 282 230 65 ALA CB C 21.28 0.005 1 283 230 65 ALA N N 121.05 0.010 1 284 231 66 ARG H H 7.66 0.002 1 285 231 66 ARG C C 176.93 0.001 1 286 231 66 ARG CA C 56.66 0.002 1 287 231 66 ARG CB C 32.31 0.005 1 288 231 66 ARG N N 116.37 0.010 1 289 232 67 LEU H H 7.60 0.002 1 290 232 67 LEU C C 177.32 0.001 1 291 232 67 LEU CA C 55.31 0.002 1 292 232 67 LEU CB C 43.95 0.005 1 293 232 67 LEU N N 119.58 0.010 1 294 233 68 THR H H 7.66 0.002 1 295 233 68 THR C C 175.30 0.001 1 296 233 68 THR CA C 62.23 0.002 1 297 233 68 THR CB C 71.55 0.005 1 298 233 68 THR N N 112.33 0.010 1 299 234 69 TRP H H 7.42 0.002 1 300 234 69 TRP C C 176.41 0.001 1 301 234 69 TRP CA C 57.60 0.002 1 302 234 69 TRP N N 120.77 0.010 1 303 235 70 TRP H H 7.21 0.002 1 304 235 70 TRP C C 176.00 0.001 1 305 235 70 TRP CA C 58.11 0.002 1 306 235 70 TRP CB C 31.76 0.005 1 307 235 70 TRP N N 120.50 0.010 1 308 236 71 GLU H H 7.67 0.002 1 309 236 71 GLU C C 176.34 0.001 1 310 236 71 GLU CA C 56.39 0.002 1 311 236 71 GLU CB C 31.02 0.005 1 312 236 71 GLU N N 120.59 0.010 1 313 237 72 TYR H H 7.39 0.002 1 314 237 72 TYR C C 175.30 0.001 1 315 237 72 TYR CA C 57.87 0.002 1 316 237 72 TYR CB C 40.98 0.005 1 317 237 72 TYR N N 120.04 0.010 1 318 238 73 SER H H 7.70 0.002 1 319 238 73 SER C C 174.87 0.001 1 320 238 73 SER CA C 58.53 0.002 1 321 238 73 SER N N 115.36 0.010 1 322 239 74 TRP H H 8.23 0.002 1 323 239 74 TRP C C 176.61 0.001 1 324 239 74 TRP CA C 58.37 0.002 1 325 239 74 TRP CB C 31.79 0.005 1 326 239 74 TRP N N 122.51 0.010 1 327 240 75 ASP H H 8.20 0.002 1 328 240 75 ASP C C 177.33 0.001 1 329 240 75 ASP CA C 55.57 0.002 1 330 240 75 ASP CB C 43.20 0.005 1 331 240 75 ASP N N 119.12 0.010 1 332 241 76 ILE H H 7.60 0.002 1 333 241 76 ILE C C 175.70 0.001 1 334 241 76 ILE CA C 62.04 0.002 1 335 241 76 ILE CB C 40.72 0.005 1 336 241 76 ILE N N 117.56 0.010 1 337 242 77 VAL H H 7.53 0.002 1 338 242 77 VAL C C 176.90 0.001 1 339 242 77 VAL CA C 63.66 0.002 1 340 242 77 VAL N N 117.03 0.010 1 341 243 78 GLU H H 8.11 0.002 1 342 243 78 GLU CA C 59.45 0.002 1 343 243 78 GLU N N 121.96 0.010 1 344 244 79 PRO C C 178.30 0.001 1 345 245 80 VAL H H 7.81 0.002 1 346 245 80 VAL C C 177.75 0.001 1 347 245 80 VAL CA C 65.88 0.002 1 348 245 80 VAL N N 115.36 0.010 1 349 246 81 THR H H 8.00 0.002 1 350 246 81 THR C C 176.94 0.001 1 351 246 81 THR CA C 65.62 0.002 1 352 246 81 THR N N 114.26 0.010 1 353 247 82 TYR H H 7.82 0.002 1 354 247 82 TYR C C 177.63 0.001 1 355 247 82 TYR CA C 60.60 0.002 1 356 247 82 TYR N N 122.15 0.010 1 357 248 83 PHE H H 8.08 0.002 1 358 248 83 PHE C C 177.62 0.001 1 359 248 83 PHE CA C 60.18 0.002 1 360 248 83 PHE CB C 40.72 0.005 1 361 248 83 PHE N N 118.30 0.010 1 362 249 84 ALA H H 8.25 0.002 1 363 249 84 ALA C C 179.25 0.001 1 364 249 84 ALA CA C 54.94 0.002 1 365 249 84 ALA CB C 21.53 0.005 1 366 249 84 ALA N N 121.96 0.010 1 367 250 85 THR H H 7.88 0.002 1 368 250 85 THR CA C 64.53 0.002 1 369 250 85 THR N N 112.79 0.010 1 370 251 86 TYR C C 177.26 0.001 1 371 251 86 TYR CA C 60.67 0.002 1 372 252 87 SER H H 8.13 0.002 1 373 252 87 SER C C 176.55 0.001 1 374 252 87 SER CA C 62.39 0.002 1 375 252 87 SER N N 115.82 0.010 1 376 253 88 THR H H 7.79 0.002 1 377 253 88 THR C C 177.49 0.001 1 378 253 88 THR CA C 66.21 0.002 1 379 253 88 THR N N 118.11 0.010 1 380 254 89 VAL H H 7.81 0.002 1 381 254 89 VAL C C 178.06 0.001 1 382 254 89 VAL CA C 66.08 0.002 1 383 254 89 VAL CB C 33.32 0.005 1 384 254 89 VAL N N 123.89 0.010 1 385 255 90 ALA H H 8.15 0.002 1 386 255 90 ALA C C 179.48 0.001 1 387 255 90 ALA CA C 55.45 0.002 1 388 255 90 ALA CB C 20.73 0.005 1 389 255 90 ALA N N 122.33 0.010 1 390 256 91 ALA H H 8.17 0.002 1 391 256 91 ALA C C 179.91 0.001 1 392 256 91 ALA CA C 55.06 0.002 1 393 256 91 ALA CB C 20.73 0.005 1 394 256 91 ALA N N 119.21 0.010 1 395 257 92 THR H H 8.05 0.002 1 396 257 92 THR C C 176.82 0.001 1 397 257 92 THR CA C 66.90 0.002 1 398 257 92 THR CB C 71.62 0.005 1 399 257 92 THR N N 114.99 0.010 1 400 258 93 PHE H H 8.34 0.002 1 401 258 93 PHE C C 177.98 0.001 1 402 258 93 PHE CA C 61.11 0.002 1 403 258 93 PHE CB C 41.58 0.005 1 404 258 93 PHE N N 122.42 0.010 1 405 259 94 GLY H H 8.74 0.002 1 406 259 94 GLY C C 174.82 0.001 1 407 259 94 GLY CA C 49.97 0.002 1 408 259 94 GLY N N 106.83 0.010 1 409 260 95 TYR H H 8.29 0.002 1 410 260 95 TYR C C 178.28 0.001 1 411 260 95 TYR CA C 61.92 0.002 1 412 260 95 TYR N N 121.78 0.010 1 413 261 96 TYR H H 7.98 0.002 1 414 261 96 TYR C C 177.80 0.001 1 415 261 96 TYR CA C 61.42 0.002 1 416 261 96 TYR CB C 40.20 0.005 1 417 261 96 TYR N N 120.31 0.010 1 418 262 97 LEU H H 8.06 0.002 1 419 262 97 LEU C C 178.51 0.001 1 420 262 97 LEU CA C 57.59 0.002 1 421 262 97 LEU CB C 44.17 0.005 1 422 262 97 LEU N N 119.30 0.010 1 423 263 98 TYR H H 7.99 0.002 1 424 263 98 TYR C C 176.90 0.001 1 425 263 98 TYR CA C 60.59 0.002 1 426 263 98 TYR N N 117.38 0.010 1 427 264 99 THR C C 175.92 0.001 1 428 264 99 THR CA C 63.18 0.002 1 429 265 100 GLN H H 7.67 0.002 1 430 265 100 GLN C C 176.16 0.001 1 431 265 100 GLN CA C 56.04 0.002 1 432 265 100 GLN CB C 31.13 0.005 1 433 265 100 GLN N N 120.50 0.010 1 434 266 101 GLN H H 7.87 0.002 1 435 266 101 GLN C C 175.70 0.001 1 436 266 101 GLN CA C 55.76 0.002 1 437 266 101 GLN CB C 31.21 0.005 1 438 266 101 GLN N N 118.85 0.010 1 439 267 102 SER H H 7.91 0.002 1 440 267 102 SER C C 174.12 0.001 1 441 267 102 SER CA C 58.50 0.002 1 442 267 102 SER CB C 66.91 0.005 1 443 267 102 SER N N 115.36 0.010 1 444 268 103 PHE H H 8.26 0.002 1 445 268 103 PHE C C 174.77 0.001 1 446 268 103 PHE CA C 57.49 0.002 1 447 268 103 PHE CB C 42.01 0.005 1 448 268 103 PHE N N 121.96 0.010 1 449 269 104 GLU H H 7.94 0.002 1 450 269 104 GLU C C 175.60 0.001 1 451 269 104 GLU CA C 55.33 0.002 1 452 269 104 GLU CB C 33.11 0.005 1 453 269 104 GLU N N 121.96 0.010 1 454 270 105 TYR H H 8.36 0.002 1 455 270 105 TYR CA C 57.18 0.002 1 456 270 105 TYR N N 122.61 0.010 1 457 271 106 PRO C C 177.10 0.001 1 458 271 106 PRO CA C 63.77 0.002 1 459 272 107 SER H H 8.19 0.002 1 460 272 107 SER C C 175.53 0.001 1 461 272 107 SER CA C 58.80 0.002 1 462 272 107 SER N N 115.27 0.010 1 463 273 108 ALA H H 8.30 0.002 1 464 273 108 ALA C C 178.90 0.001 1 465 273 108 ALA CA C 54.18 0.002 1 466 273 108 ALA N N 125.45 0.010 1 467 274 109 ARG H H 8.17 0.002 1 468 274 109 ARG C C 178.38 0.001 1 469 274 109 ARG CA C 58.17 0.002 1 470 274 109 ARG N N 118.20 0.010 1 471 275 110 GLU H H 8.17 0.002 1 472 275 110 GLU C C 178.47 0.001 1 473 275 110 GLU CA C 60.71 0.002 1 474 275 110 GLU CB C 32.33 0.005 1 475 275 110 GLU N N 120.22 0.010 1 476 276 111 ARG H H 8.12 0.002 1 477 276 111 ARG C C 176.83 0.001 1 478 276 111 ARG CA C 56.56 0.002 1 479 276 111 ARG CB C 35.33 0.005 1 480 276 111 ARG N N 126.55 0.010 1 481 277 112 VAL H H 7.97 0.002 1 482 277 112 VAL CA C 68.13 0.002 1 483 277 112 VAL CB C 32.53 0.005 1 484 277 112 VAL N N 122.61 0.010 1 485 278 113 TYR C C 175.87 0.001 1 486 278 113 TYR CA C 57.79 0.002 1 487 279 114 THR H H 7.89 0.002 1 488 279 114 THR C C 174.18 0.001 1 489 279 114 THR CA C 61.72 0.002 1 490 279 114 THR CB C 72.63 0.005 1 491 279 114 THR N N 117.01 0.010 1 492 280 115 LYS H H 8.18 0.002 1 493 280 115 LYS C C 175.73 0.001 1 494 280 115 LYS CA C 56.45 0.002 1 495 280 115 LYS CB C 35.12 0.005 1 496 280 115 LYS N N 125.08 0.010 1 497 281 116 GLN H H 7.94 0.002 1 498 281 116 GLN C C 180.78 0.001 1 499 281 116 GLN CA C 57.28 0.002 1 500 281 116 GLN CB C 32.74 0.005 1 501 281 116 GLN N N 104.54 0.010 1 502 285 120 ARG C C 175.22 0.001 1 503 286 121 ALA H H 8.19 0.002 1 504 286 121 ALA C C 173.65 0.001 1 505 286 121 ALA CA C 52.15 0.002 1 506 286 121 ALA N N 125.82 0.010 1 507 287 122 GLN H H 8.29 0.002 1 508 287 122 GLN N N 125.72 0.010 1 509 288 123 LYS C C 177.10 0.001 1 510 288 123 LYS CA C 56.86 0.002 1 511 289 124 GLN H H 7.67 0.002 1 512 289 124 GLN C C 175.32 0.001 1 513 289 124 GLN CA C 55.52 0.002 1 514 289 124 GLN CB C 30.95 0.005 1 515 289 124 GLN N N 118.39 0.010 1 516 290 125 ASN H H 8.11 0.002 1 517 290 125 ASN C C 174.77 0.001 1 518 290 125 ASN CA C 53.38 0.002 1 519 290 125 ASN CB C 40.96 0.005 1 520 290 125 ASN N N 118.48 0.010 1 521 291 126 PHE H H 8.23 0.002 1 522 291 126 PHE C C 174.63 0.001 1 523 291 126 PHE CA C 57.80 0.002 1 524 291 126 PHE CB C 42.08 0.005 1 525 291 126 PHE N N 120.77 0.010 1 526 292 127 ASP H H 8.07 0.002 1 527 292 127 ASP C C 176.53 0.001 1 528 292 127 ASP CA C 53.24 0.002 1 529 292 127 ASP CB C 44.23 0.005 1 530 292 127 ASP N N 123.71 0.010 1 531 293 128 ILE H H 8.35 0.002 1 532 293 128 ILE C C 177.09 0.001 1 533 293 128 ILE CA C 62.39 0.002 1 534 293 128 ILE CB C 40.53 0.005 1 535 293 128 ILE N N 123.52 0.010 1 536 294 129 GLU H H 8.21 0.002 1 537 294 129 GLU C C 179.64 0.001 1 538 294 129 GLU CA C 59.18 0.002 1 539 294 129 GLU CB C 31.02 0.005 1 540 294 129 GLU N N 122.06 0.010 1 541 295 130 LYS H H 7.74 0.002 1 542 295 130 LYS C C 178.39 0.001 1 543 295 130 LYS CA C 58.94 0.002 1 544 295 130 LYS CB C 34.47 0.005 1 545 295 130 LYS N N 119.58 0.010 1 546 296 131 TYR H H 7.61 0.002 1 547 296 131 TYR C C 176.63 0.001 1 548 296 131 TYR CA C 60.69 0.002 1 549 296 131 TYR CB C 40.29 0.005 1 550 296 131 TYR N N 119.12 0.010 1 551 297 132 ASN H H 8.34 0.002 1 552 297 132 ASN C C 178.43 0.001 1 553 297 132 ASN CA C 56.08 0.002 1 554 297 132 ASN CB C 40.35 0.005 1 555 297 132 ASN N N 118.48 0.010 1 556 298 133 ARG H H 8.02 0.002 1 557 298 133 ARG C C 178.47 0.001 1 558 298 133 ARG CA C 58.80 0.002 1 559 298 133 ARG CB C 31.90 0.005 1 560 298 133 ARG N N 120.59 0.010 1 561 299 134 LEU H H 7.75 0.002 1 562 299 134 LEU C C 178.49 0.001 1 563 299 134 LEU CA C 58.06 0.002 1 564 299 134 LEU CB C 43.95 0.005 1 565 299 134 LEU N N 120.86 0.010 1 566 300 135 VAL H H 7.92 0.002 1 567 300 135 VAL C C 178.33 0.001 1 568 300 135 VAL CA C 66.54 0.002 1 569 300 135 VAL CB C 33.20 0.005 1 570 300 135 VAL N N 117.29 0.010 1 571 301 136 THR H H 7.77 0.002 1 572 301 136 THR C C 176.93 0.001 1 573 301 136 THR CA C 66.18 0.002 1 574 301 136 THR CB C 71.76 0.005 1 575 301 136 THR N N 115.36 0.010 1 576 302 137 GLU H H 7.94 0.002 1 577 302 137 GLU C C 179.17 0.001 1 578 302 137 GLU CA C 58.32 0.002 1 579 302 137 GLU CB C 30.80 0.005 1 580 302 137 GLU N N 121.87 0.010 1 581 303 138 VAL H H 8.22 0.002 1 582 303 138 VAL C C 177.62 0.001 1 583 303 138 VAL CA C 66.59 0.002 1 584 303 138 VAL CB C 33.20 0.005 1 585 303 138 VAL N N 120.22 0.010 1 586 304 139 ASP H H 8.16 0.002 1 587 304 139 ASP C C 178.74 0.001 1 588 304 139 ASP CA C 57.68 0.002 1 589 304 139 ASP CB C 43.95 0.005 1 590 304 139 ASP N N 121.14 0.010 1 591 305 140 GLU H H 7.95 0.002 1 592 305 140 GLU C C 179.85 0.001 1 593 305 140 GLU CA C 58.91 0.002 1 594 305 140 GLU CB C 31.02 0.005 1 595 305 140 GLU N N 119.58 0.010 1 596 306 141 LEU H H 8.02 0.002 1 597 306 141 LEU C C 179.14 0.001 1 598 306 141 LEU CA C 58.11 0.002 1 599 306 141 LEU CB C 44.60 0.005 1 600 306 141 LEU N N 121.60 0.010 1 601 307 142 ARG H H 8.44 0.002 1 602 307 142 ARG C C 178.99 0.001 1 603 307 142 ARG CA C 60.18 0.002 1 604 307 142 ARG CB C 31.88 0.005 1 605 307 142 ARG N N 119.40 0.010 1 606 308 143 ASN H H 8.07 0.002 1 607 308 143 ASN C C 178.33 0.001 1 608 308 143 ASN CA C 56.15 0.002 1 609 308 143 ASN CB C 40.61 0.005 1 610 308 143 ASN N N 118.39 0.010 1 611 309 144 GLN H H 8.19 0.002 1 612 309 144 GLN C C 178.92 0.001 1 613 309 144 GLN CA C 58.47 0.002 1 614 309 144 GLN CB C 30.37 0.005 1 615 309 144 GLN N N 120.59 0.010 1 616 310 145 LEU H H 8.13 0.002 1 617 310 145 LEU C C 178.95 0.001 1 618 310 145 LEU CA C 57.61 0.002 1 619 310 145 LEU CB C 43.95 0.005 1 620 310 145 LEU N N 119.67 0.010 1 621 311 146 LYS H H 7.76 0.002 1 622 311 146 LYS C C 178.88 0.001 1 623 311 146 LYS CA C 59.35 0.002 1 624 311 146 LYS CB C 34.15 0.005 1 625 311 146 LYS N N 118.39 0.010 1 626 312 147 ARG H H 7.55 0.002 1 627 312 147 ARG C C 178.08 0.001 1 628 312 147 ARG CA C 58.01 0.002 1 629 312 147 ARG CB C 32.53 0.005 1 630 312 147 ARG N N 118.02 0.010 1 631 313 148 LEU H H 7.57 0.002 1 632 313 148 LEU C C 177.43 0.001 1 633 313 148 LEU CA C 56.45 0.002 1 634 313 148 LEU CB C 44.60 0.005 1 635 313 148 LEU N N 118.66 0.010 1 636 314 149 ARG H H 7.53 0.002 1 637 314 149 ARG C C 176.28 0.001 1 638 314 149 ARG CA C 56.56 0.002 1 639 314 149 ARG N N 116.37 0.010 1 640 315 150 ASP H H 7.89 0.002 1 641 315 150 ASP C C 175.10 0.001 1 642 315 150 ASP CA C 53.35 0.002 1 643 315 150 ASP CB C 32.94 0.005 1 644 315 150 ASP N N 120.96 0.010 1 645 316 151 PRO C C 177.76 0.001 1 646 316 151 PRO CA C 63.90 0.002 1 647 316 151 PRO CB C 34.04 0.005 1 648 317 152 LEU H H 8.09 0.002 1 649 317 152 LEU C C 177.87 0.001 1 650 317 152 LEU CA C 55.42 0.002 1 651 317 152 LEU CB C 43.95 0.005 1 652 317 152 LEU N N 120.13 0.010 1 653 318 153 GLU H H 7.91 0.002 1 654 318 153 GLU C C 176.81 0.001 1 655 318 153 GLU CA C 56.87 0.002 1 656 318 153 GLU CB C 32.10 0.005 1 657 318 153 GLU N N 120.59 0.010 1 stop_ save_