data_18779 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance assignments of FrpD from Neisseria meningitidis ; _BMRB_accession_number 18779 _BMRB_flat_file_name bmr18779.str _Entry_type original _Submission_date 2012-10-11 _Accession_date 2012-10-11 _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 Bumba Ladislav . . 2 Sviridova Ekaterina . . 3 'Kuta Smatanova' Ivana . . 4 Rezacova Pavlina . . 5 Veverka Vaclav . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 217 "13C chemical shifts" 687 "15N chemical shifts" 217 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-01-29 original author . stop_ _Original_release_date 2013-01-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone resonance assignments of the outer membrane lipoprotein FrpD from Neisseria meningitidis.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23225222 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bumba Ladislav . . 2 Sviridova Ekaterina . . 3 'Kuta Smatanova' Ivana . . 4 Rezaova Pavlina . . 5 Veverka Vaclav . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name FrpD_protein _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label FrpD_protein $FrpD 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_FrpD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FrpD _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 237 _Mol_residue_sequence ; MAKEQTSFNNPEPMTGFEHT VTFDFQGTKMVIPYGYLARY TQDNATKWLSDTPGQDAYSI NLIEISVYYKKTDQGWVLEP YNQQNKAHFIQFLRDGLDSV DDIVIRKDACSLSTTMGERL LTYGVKKMPSAYPEYEAYED KRHIPENPYFHEFYYIKKGE NPAIITHRNNRINQTEEDSY STSVGSCINGFTVQYYPFIR EKQQLTQQELVGYHQQVEQL VQSFVNNSNKKENLYFQ ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 41 MET 2 42 ALA 3 43 LYS 4 44 GLU 5 45 GLN 6 46 THR 7 47 SER 8 48 PHE 9 49 ASN 10 50 ASN 11 51 PRO 12 52 GLU 13 53 PRO 14 54 MET 15 55 THR 16 56 GLY 17 57 PHE 18 58 GLU 19 59 HIS 20 60 THR 21 61 VAL 22 62 THR 23 63 PHE 24 64 ASP 25 65 PHE 26 66 GLN 27 67 GLY 28 68 THR 29 69 LYS 30 70 MET 31 71 VAL 32 72 ILE 33 73 PRO 34 74 TYR 35 75 GLY 36 76 TYR 37 77 LEU 38 78 ALA 39 79 ARG 40 80 TYR 41 81 THR 42 82 GLN 43 83 ASP 44 84 ASN 45 85 ALA 46 86 THR 47 87 LYS 48 88 TRP 49 89 LEU 50 90 SER 51 91 ASP 52 92 THR 53 93 PRO 54 94 GLY 55 95 GLN 56 96 ASP 57 97 ALA 58 98 TYR 59 99 SER 60 100 ILE 61 101 ASN 62 102 LEU 63 103 ILE 64 104 GLU 65 105 ILE 66 106 SER 67 107 VAL 68 108 TYR 69 109 TYR 70 110 LYS 71 111 LYS 72 112 THR 73 113 ASP 74 114 GLN 75 115 GLY 76 116 TRP 77 117 VAL 78 118 LEU 79 119 GLU 80 120 PRO 81 121 TYR 82 122 ASN 83 123 GLN 84 124 GLN 85 125 ASN 86 126 LYS 87 127 ALA 88 128 HIS 89 129 PHE 90 130 ILE 91 131 GLN 92 132 PHE 93 133 LEU 94 134 ARG 95 135 ASP 96 136 GLY 97 137 LEU 98 138 ASP 99 139 SER 100 140 VAL 101 141 ASP 102 142 ASP 103 143 ILE 104 144 VAL 105 145 ILE 106 146 ARG 107 147 LYS 108 148 ASP 109 149 ALA 110 150 CYS 111 151 SER 112 152 LEU 113 153 SER 114 154 THR 115 155 THR 116 156 MET 117 157 GLY 118 158 GLU 119 159 ARG 120 160 LEU 121 161 LEU 122 162 THR 123 163 TYR 124 164 GLY 125 165 VAL 126 166 LYS 127 167 LYS 128 168 MET 129 169 PRO 130 170 SER 131 171 ALA 132 172 TYR 133 173 PRO 134 174 GLU 135 175 TYR 136 176 GLU 137 177 ALA 138 178 TYR 139 179 GLU 140 180 ASP 141 181 LYS 142 182 ARG 143 183 HIS 144 184 ILE 145 185 PRO 146 186 GLU 147 187 ASN 148 188 PRO 149 189 TYR 150 190 PHE 151 191 HIS 152 192 GLU 153 193 PHE 154 194 TYR 155 195 TYR 156 196 ILE 157 197 LYS 158 198 LYS 159 199 GLY 160 200 GLU 161 201 ASN 162 202 PRO 163 203 ALA 164 204 ILE 165 205 ILE 166 206 THR 167 207 HIS 168 208 ARG 169 209 ASN 170 210 ASN 171 211 ARG 172 212 ILE 173 213 ASN 174 214 GLN 175 215 THR 176 216 GLU 177 217 GLU 178 218 ASP 179 219 SER 180 220 TYR 181 221 SER 182 222 THR 183 223 SER 184 224 VAL 185 225 GLY 186 226 SER 187 227 CYS 188 228 ILE 189 229 ASN 190 230 GLY 191 231 PHE 192 232 THR 193 233 VAL 194 234 GLN 195 235 TYR 196 236 TYR 197 237 PRO 198 238 PHE 199 239 ILE 200 240 ARG 201 241 GLU 202 242 LYS 203 243 GLN 204 244 GLN 205 245 LEU 206 246 THR 207 247 GLN 208 248 GLN 209 249 GLU 210 250 LEU 211 251 VAL 212 252 GLY 213 253 TYR 214 254 HIS 215 255 GLN 216 256 GLN 217 257 VAL 218 258 GLU 219 259 GLN 220 260 LEU 221 261 VAL 222 262 GLN 223 263 SER 224 264 PHE 225 265 VAL 226 266 ASN 227 267 ASN 228 268 SER 229 269 ASN 230 270 LYS 231 271 LYS 232 272 GLU 233 273 ASN 234 274 LEU 235 275 TYR 236 276 PHE 237 277 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-04-23 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 EMBL CAM09823 "putative outer membrane protein [Neisseria meningitidis FAM18]" 97.05 271 100.00 100.00 5.91e-171 EMBL CAM10568 "putative rtx iron-regulated frpc protein outer membrane [Neisseria meningitidis FAM18]" 97.05 271 100.00 100.00 5.91e-171 EMBL CBA03514 "FrpC operon protein [Neisseria meningitidis alpha153]" 97.05 250 97.83 99.13 1.87e-167 EMBL CBA04365 "FrpC operon protein [Neisseria meningitidis alpha14]" 97.05 250 97.83 99.13 1.85e-167 EMBL CBA08292 "FrpC operon protein [Neisseria meningitidis alpha275]" 70.04 176 96.99 98.80 6.00e-115 GB AAA99901 "ORF1 [Neisseria meningitidis]" 97.05 271 100.00 100.00 5.91e-171 GB AAF40807 "FrpC operon protein [Neisseria meningitidis MC58]" 96.20 257 98.68 100.00 7.68e-167 GB AAF41012 "FrpC operon protein [Neisseria meningitidis MC58]" 97.05 271 97.83 99.13 4.59e-167 GB AAF41775 "FrpC operon protein [Neisseria meningitidis MC58]" 96.20 257 97.81 99.12 2.87e-165 GB ABX73920 "FrpC operon protein [Neisseria meningitidis 053442]" 96.20 236 97.37 98.68 1.27e-164 REF NP_273413 "outer membrane protein FrpC [Neisseria meningitidis MC58]" 96.20 257 98.68 100.00 7.68e-167 REF NP_273628 "outer membrane protein FrpC [Neisseria meningitidis MC58]" 97.05 271 97.83 99.13 4.59e-167 REF NP_274426 "outer membrane protein FrpC [Neisseria meningitidis MC58]" 96.20 257 97.81 99.12 2.87e-165 REF WP_002218733 "FrpC operon protein [Neisseria meningitidis]" 96.20 257 97.37 98.68 3.40e-164 REF WP_002221985 "FrpC operon protein [Neisseria meningitidis]" 97.05 271 97.39 99.13 1.56e-166 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $FrpD 'Neisseria meningitidis' 487 Bacteria . Neisseria meningitidis 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 $FrpD 'recombinant technology' . Escherichia coli . pET28b 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 $FrpD 0.250 mM '[U-100% 13C; U-100% 15N]' 'sodium phosphate' 6 mM 'natural abundance' NaCl 50 mM '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_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _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_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . 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' 50 . mM pH 7.4 . pH pressure 1 . atm temperature 308 . 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 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 FrpD_protein _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 43 3 LYS C C 176.403 0.064 1 2 43 3 LYS CA C 56.661 0.088 1 3 43 3 LYS CB C 32.900 0.125 1 4 44 4 GLU H H 8.638 0.005 1 5 44 4 GLU C C 176.380 0.064 1 6 44 4 GLU CA C 56.805 0.088 1 7 44 4 GLU CB C 30.393 0.125 1 8 44 4 GLU N N 122.352 0.051 1 9 45 5 GLN H H 8.681 0.003 1 10 45 5 GLN C C 175.691 0.064 1 11 45 5 GLN CA C 55.560 0.088 1 12 45 5 GLN CB C 30.253 0.125 1 13 45 5 GLN N N 121.657 0.031 1 14 46 6 THR H H 8.159 0.005 1 15 46 6 THR C C 173.682 0.064 1 16 46 6 THR CA C 61.781 0.088 1 17 46 6 THR CB C 70.118 0.125 1 18 46 6 THR N N 115.689 0.049 1 19 47 7 SER H H 7.494 0.007 1 20 47 7 SER C C 171.459 0.064 1 21 47 7 SER CA C 57.725 0.088 1 22 47 7 SER CB C 65.137 0.125 1 23 47 7 SER N N 117.695 0.037 1 24 48 8 PHE H H 8.576 0.005 1 25 48 8 PHE C C 176.498 0.064 1 26 48 8 PHE CA C 55.721 0.088 1 27 48 8 PHE CB C 38.785 0.125 1 28 48 8 PHE N N 122.285 0.020 1 29 49 9 ASN H H 7.780 0.003 1 30 49 9 ASN C C 176.279 0.064 1 31 49 9 ASN CA C 53.229 0.088 1 32 49 9 ASN CB C 39.173 0.125 1 33 49 9 ASN N N 113.210 0.021 1 34 50 10 ASN H H 8.378 0.009 1 35 50 10 ASN C C 173.724 0.064 1 36 50 10 ASN CA C 50.209 0.088 1 37 50 10 ASN CB C 39.088 0.125 1 38 50 10 ASN N N 118.912 0.023 1 39 51 11 PRO C C 175.518 0.064 1 40 51 11 PRO CA C 61.340 0.088 1 41 51 11 PRO CB C 32.938 0.125 1 42 52 12 GLU H H 8.637 0.004 1 43 52 12 GLU C C 174.089 0.064 1 44 52 12 GLU CA C 54.173 0.088 1 45 52 12 GLU CB C 30.771 0.125 1 46 52 12 GLU N N 122.727 0.029 1 47 53 13 PRO C C 176.587 0.064 1 48 53 13 PRO CA C 63.692 0.088 1 49 53 13 PRO CB C 32.405 0.125 1 50 54 14 MET H H 8.830 0.009 1 51 54 14 MET C C 178.909 0.064 1 52 54 14 MET CA C 56.707 0.088 1 53 54 14 MET CB C 33.234 0.125 1 54 54 14 MET N N 119.650 0.042 1 55 55 15 THR H H 10.835 0.010 1 56 55 15 THR C C 174.863 0.064 1 57 55 15 THR CA C 61.923 0.088 1 58 55 15 THR CB C 70.999 0.125 1 59 55 15 THR N N 113.716 0.093 1 60 56 16 GLY H H 8.581 0.008 1 61 56 16 GLY C C 173.147 0.064 1 62 56 16 GLY CA C 45.475 0.088 1 63 56 16 GLY N N 110.122 0.053 1 64 57 17 PHE H H 7.924 0.007 1 65 57 17 PHE C C 177.451 0.064 1 66 57 17 PHE CA C 57.304 0.088 1 67 57 17 PHE CB C 40.214 0.125 1 68 57 17 PHE N N 114.968 0.020 1 69 58 18 GLU H H 10.523 0.008 1 70 58 18 GLU C C 175.158 0.064 1 71 58 18 GLU CA C 61.801 0.088 1 72 58 18 GLU CB C 29.191 0.125 1 73 58 18 GLU N N 121.286 0.028 1 74 59 19 HIS H H 6.870 0.006 1 75 59 19 HIS C C 173.962 0.064 1 76 59 19 HIS CA C 53.373 0.088 1 77 59 19 HIS CB C 33.810 0.125 1 78 59 19 HIS N N 109.509 0.029 1 79 60 20 THR H H 8.602 0.004 1 80 60 20 THR C C 172.529 0.064 1 81 60 20 THR CA C 59.292 0.088 1 82 60 20 THR CB C 72.181 0.125 1 83 60 20 THR N N 111.734 0.056 1 84 61 21 VAL H H 8.289 0.011 1 85 61 21 VAL C C 175.022 0.064 1 86 61 21 VAL CA C 60.918 0.088 1 87 61 21 VAL CB C 34.623 0.125 1 88 61 21 VAL N N 118.964 0.042 1 89 62 22 THR H H 8.810 0.010 1 90 62 22 THR C C 173.669 0.064 1 91 62 22 THR CA C 62.821 0.088 1 92 62 22 THR CB C 68.958 0.125 1 93 62 22 THR N N 123.259 0.054 1 94 63 23 PHE H H 9.472 0.010 1 95 63 23 PHE C C 173.854 0.064 1 96 63 23 PHE CA C 56.870 0.088 1 97 63 23 PHE CB C 43.333 0.125 1 98 63 23 PHE N N 126.293 0.025 1 99 64 24 ASP H H 9.136 0.009 1 100 64 24 ASP C C 174.735 0.064 1 101 64 24 ASP CA C 53.489 0.088 1 102 64 24 ASP CB C 44.576 0.125 1 103 64 24 ASP N N 121.389 0.027 1 104 65 25 PHE H H 9.245 0.012 1 105 65 25 PHE C C 175.599 0.064 1 106 65 25 PHE CA C 55.074 0.088 1 107 65 25 PHE CB C 38.973 0.125 1 108 65 25 PHE N N 126.677 0.026 1 109 66 26 GLN H H 8.834 0.004 1 110 66 26 GLN C C 175.892 0.064 1 111 66 26 GLN CA C 56.527 0.088 1 112 66 26 GLN CB C 27.900 0.125 1 113 66 26 GLN N N 120.571 0.025 1 114 67 27 GLY H H 9.423 0.008 1 115 67 27 GLY C C 175.358 0.064 1 116 67 27 GLY CA C 45.373 0.088 1 117 67 27 GLY N N 108.471 0.020 1 118 68 28 THR H H 7.733 0.005 1 119 68 28 THR C C 173.615 0.064 1 120 68 28 THR CA C 62.444 0.100 1 121 68 28 THR CB C 69.991 0.125 1 122 68 28 THR N N 118.480 0.032 1 123 69 29 LYS H H 8.819 0.008 1 124 69 29 LYS C C 176.704 0.064 1 125 69 29 LYS CA C 55.730 0.088 1 126 69 29 LYS CB C 34.272 0.125 1 127 69 29 LYS N N 127.886 0.062 1 128 70 30 MET H H 9.085 0.009 1 129 70 30 MET C C 174.172 0.064 1 130 70 30 MET CA C 55.544 0.098 1 131 70 30 MET CB C 38.252 0.125 1 132 70 30 MET N N 119.884 0.041 1 133 71 31 VAL H H 8.791 0.008 1 134 71 31 VAL C C 175.452 0.064 1 135 71 31 VAL CA C 62.223 0.088 1 136 71 31 VAL CB C 33.090 0.125 1 137 71 31 VAL N N 125.447 0.034 1 138 72 32 ILE H H 8.739 0.010 1 139 72 32 ILE C C 175.018 0.064 1 140 72 32 ILE CA C 58.789 0.088 1 141 72 32 ILE CB C 41.807 0.125 1 142 72 32 ILE N N 127.358 0.038 1 143 73 33 PRO C C 179.435 0.064 1 144 73 33 PRO CA C 63.234 0.088 1 145 73 33 PRO CB C 32.138 0.125 1 146 74 34 TYR H H 9.535 0.010 1 147 74 34 TYR C C 175.501 0.064 1 148 74 34 TYR CA C 59.351 0.088 1 149 74 34 TYR CB C 37.548 0.125 1 150 74 34 TYR N N 126.430 0.064 1 151 75 35 GLY H H 8.591 0.005 1 152 75 35 GLY C C 175.499 0.064 1 153 75 35 GLY CA C 46.317 0.088 1 154 75 35 GLY N N 107.473 0.020 1 155 76 36 TYR H H 8.026 0.009 1 156 76 36 TYR C C 174.593 0.064 1 157 76 36 TYR CA C 61.377 0.088 1 158 76 36 TYR CB C 37.853 0.125 1 159 76 36 TYR N N 119.422 0.029 1 160 77 37 LEU H H 7.858 0.010 1 161 77 37 LEU C C 177.991 0.064 1 162 77 37 LEU CA C 53.078 0.092 1 163 77 37 LEU CB C 40.858 0.125 1 164 77 37 LEU N N 119.381 0.025 1 165 78 38 ALA H H 9.203 0.007 1 166 78 38 ALA C C 177.981 0.064 1 167 78 38 ALA CA C 55.457 0.088 1 168 78 38 ALA CB C 19.640 0.125 1 169 78 38 ALA N N 122.162 0.050 1 170 79 39 ARG H H 9.023 0.009 1 171 79 39 ARG C C 177.862 0.064 1 172 79 39 ARG CA C 58.286 0.088 1 173 79 39 ARG CB C 29.534 0.125 1 174 79 39 ARG N N 111.751 0.054 1 175 80 40 TYR H H 8.647 0.005 1 176 80 40 TYR C C 173.961 0.064 1 177 80 40 TYR CA C 55.616 0.088 1 178 80 40 TYR CB C 37.554 0.125 1 179 80 40 TYR N N 123.685 0.040 1 180 81 41 THR H H 6.659 0.008 1 181 81 41 THR C C 174.441 0.064 1 182 81 41 THR CA C 58.470 0.088 1 183 81 41 THR CB C 74.381 0.125 1 184 81 41 THR N N 105.012 0.030 1 185 82 42 GLN H H 8.677 0.006 1 186 82 42 GLN C C 175.367 0.064 1 187 82 42 GLN CA C 53.621 0.088 1 188 82 42 GLN CB C 33.027 0.128 1 189 82 42 GLN N N 115.965 0.023 1 190 83 43 ASP H H 8.582 0.006 1 191 83 43 ASP C C 176.936 0.064 1 192 83 43 ASP CA C 54.027 0.088 1 193 83 43 ASP CB C 38.351 0.125 1 194 83 43 ASP N N 117.775 0.047 1 195 84 44 ASN H H 9.102 0.008 1 196 84 44 ASN C C 173.425 0.064 1 197 84 44 ASN CA C 54.497 0.088 1 198 84 44 ASN CB C 37.228 0.125 1 199 84 44 ASN N N 120.481 0.020 1 200 85 45 ALA H H 8.570 0.005 1 201 85 45 ALA C C 176.926 0.064 1 202 85 45 ALA CA C 53.128 0.088 1 203 85 45 ALA CB C 16.171 0.125 1 204 85 45 ALA N N 113.767 0.020 1 205 86 46 THR H H 7.734 0.008 1 206 86 46 THR C C 175.190 0.064 1 207 86 46 THR CA C 63.085 0.088 1 208 86 46 THR CB C 70.797 0.125 1 209 86 46 THR N N 106.852 0.053 1 210 87 47 LYS H H 7.688 0.006 1 211 87 47 LYS C C 174.813 0.064 1 212 87 47 LYS CA C 56.024 0.088 1 213 87 47 LYS CB C 34.252 0.125 1 214 87 47 LYS N N 121.691 0.027 1 215 88 48 TRP H H 8.786 0.008 1 216 88 48 TRP C C 174.821 0.064 1 217 88 48 TRP CA C 57.349 0.088 1 218 88 48 TRP CB C 30.834 0.125 1 219 88 48 TRP N N 123.843 0.020 1 220 89 49 LEU H H 7.725 0.010 1 221 89 49 LEU C C 173.502 0.064 1 222 89 49 LEU CA C 56.161 0.088 1 223 89 49 LEU CB C 42.790 0.125 1 224 89 49 LEU N N 123.140 0.033 1 225 90 50 SER H H 8.308 0.009 1 226 90 50 SER C C 174.290 0.064 1 227 90 50 SER CA C 54.754 0.088 1 228 90 50 SER CB C 68.332 0.125 1 229 90 50 SER N N 115.264 0.038 1 230 91 51 ASP H H 8.981 0.008 1 231 91 51 ASP C C 176.659 0.064 1 232 91 51 ASP CA C 55.811 0.088 1 233 91 51 ASP CB C 41.076 0.125 1 234 91 51 ASP N N 122.478 0.034 1 235 92 52 THR H H 9.151 0.008 1 236 92 52 THR C C 172.326 0.064 1 237 92 52 THR CA C 60.127 0.088 1 238 92 52 THR CB C 70.605 0.125 1 239 92 52 THR N N 123.574 0.054 1 240 93 53 PRO C C 178.207 0.064 1 241 94 54 GLY H H 8.038 0.006 1 242 94 54 GLY C C 173.225 0.064 1 243 94 54 GLY CA C 45.234 0.088 1 244 94 54 GLY N N 104.963 0.022 1 245 95 55 GLN H H 7.834 0.007 1 246 95 55 GLN C C 175.303 0.064 1 247 95 55 GLN CA C 53.948 0.088 1 248 95 55 GLN CB C 31.287 0.125 1 249 95 55 GLN N N 120.233 0.026 1 250 96 56 ASP H H 8.664 0.007 1 251 96 56 ASP C C 175.496 0.064 1 252 96 56 ASP CA C 56.520 0.088 1 253 96 56 ASP CB C 41.023 0.125 1 254 96 56 ASP N N 125.357 0.068 1 255 97 57 ALA H H 7.422 0.009 1 256 97 57 ALA C C 176.686 0.064 1 257 97 57 ALA CA C 51.092 0.088 1 258 97 57 ALA CB C 22.813 0.125 1 259 97 57 ALA N N 116.224 0.045 1 260 98 58 TYR H H 7.407 0.006 1 261 98 58 TYR C C 176.076 0.064 1 262 98 58 TYR CA C 58.140 0.088 1 263 98 58 TYR CB C 38.958 0.125 1 264 98 58 TYR N N 117.842 0.034 1 265 99 59 SER H H 9.290 0.008 1 266 99 59 SER C C 174.766 0.064 1 267 99 59 SER CA C 58.336 0.088 1 268 99 59 SER CB C 62.718 0.125 1 269 99 59 SER N N 123.176 0.044 1 270 100 60 ILE H H 8.248 0.012 1 271 100 60 ILE C C 174.229 0.064 1 272 100 60 ILE CA C 59.816 0.088 1 273 100 60 ILE CB C 43.620 0.125 1 274 100 60 ILE N N 122.960 0.020 1 275 101 61 ASN C C 174.712 0.064 1 276 101 61 ASN CA C 53.404 0.088 1 277 101 61 ASN CB C 40.513 0.125 1 278 102 62 LEU H H 7.510 0.005 1 279 102 62 LEU C C 174.079 0.064 1 280 102 62 LEU CA C 55.353 0.088 1 281 102 62 LEU CB C 44.882 0.125 1 282 102 62 LEU N N 120.840 0.024 1 283 103 63 ILE H H 9.088 0.008 1 284 103 63 ILE C C 171.857 0.064 1 285 103 63 ILE CA C 59.216 0.088 1 286 103 63 ILE CB C 42.729 0.125 1 287 103 63 ILE N N 122.291 0.049 1 288 104 64 GLU H H 7.779 0.007 1 289 104 64 GLU C C 175.867 0.064 1 290 104 64 GLU CA C 54.591 0.088 1 291 104 64 GLU CB C 31.304 0.125 1 292 104 64 GLU N N 125.943 0.042 1 293 105 65 ILE H H 8.814 0.012 1 294 105 65 ILE C C 175.843 0.064 1 295 105 65 ILE CA C 59.127 0.088 1 296 105 65 ILE CB C 39.981 0.125 1 297 105 65 ILE N N 119.090 0.044 1 298 106 66 SER H H 8.655 0.009 1 299 106 66 SER C C 174.154 0.064 1 300 106 66 SER CA C 57.850 0.088 1 301 106 66 SER CB C 64.593 0.125 1 302 106 66 SER N N 118.407 0.058 1 303 107 67 VAL H H 9.054 0.007 1 304 107 67 VAL C C 173.331 0.064 1 305 107 67 VAL CA C 58.077 0.095 1 306 107 67 VAL CB C 34.735 0.125 1 307 107 67 VAL N N 115.991 0.020 1 308 108 68 TYR H H 9.068 0.010 1 309 108 68 TYR C C 174.171 0.064 1 310 108 68 TYR CA C 55.552 0.088 1 311 108 68 TYR CB C 40.358 0.125 1 312 108 68 TYR N N 125.184 0.048 1 313 109 69 TYR H H 7.143 0.006 1 314 109 69 TYR C C 172.586 0.064 1 315 109 69 TYR CA C 53.766 0.088 1 316 109 69 TYR CB C 41.646 0.125 1 317 109 69 TYR N N 123.934 0.025 1 318 110 70 LYS H H 8.531 0.007 1 319 110 70 LYS C C 174.263 0.064 1 320 110 70 LYS CA C 54.272 0.088 1 321 110 70 LYS CB C 35.455 0.125 1 322 110 70 LYS N N 117.676 0.048 1 323 111 71 LYS H H 8.692 0.004 1 324 111 71 LYS C C 176.322 0.064 1 325 111 71 LYS CA C 56.504 0.088 1 326 111 71 LYS CB C 32.028 0.125 1 327 111 71 LYS N N 126.714 0.031 1 328 112 72 THR H H 7.835 0.012 1 329 112 72 THR C C 175.252 0.064 1 330 112 72 THR CA C 59.811 0.088 1 331 112 72 THR CB C 72.459 0.125 1 332 112 72 THR N N 118.080 0.020 1 333 113 73 ASP C C 176.833 0.064 1 334 113 73 ASP CA C 56.541 0.088 1 335 113 73 ASP CB C 39.923 0.125 1 336 114 74 GLN H H 7.887 0.008 1 337 114 74 GLN C C 175.204 0.064 1 338 114 74 GLN CA C 55.233 0.115 1 339 114 74 GLN CB C 29.288 0.125 1 340 114 74 GLN N N 115.918 0.038 1 341 115 75 GLY H H 7.353 0.006 1 342 115 75 GLY C C 173.805 0.064 1 343 115 75 GLY CA C 44.226 0.088 1 344 115 75 GLY N N 108.222 0.035 1 345 116 76 TRP H H 8.490 0.006 1 346 116 76 TRP C C 176.820 0.064 1 347 116 76 TRP CA C 57.136 0.088 1 348 116 76 TRP CB C 29.709 0.125 1 349 116 76 TRP N N 123.366 0.020 1 350 117 77 VAL H H 9.475 0.006 1 351 117 77 VAL C C 173.607 0.064 1 352 117 77 VAL CA C 60.567 0.088 1 353 117 77 VAL CB C 35.560 0.125 1 354 117 77 VAL N N 121.239 0.033 1 355 118 78 LEU H H 7.542 0.010 1 356 118 78 LEU C C 178.655 0.064 1 357 118 78 LEU CA C 53.289 0.088 1 358 118 78 LEU CB C 43.083 0.125 1 359 118 78 LEU N N 121.403 0.036 1 360 119 79 GLU H H 9.898 0.005 1 361 119 79 GLU C C 173.988 0.064 1 362 119 79 GLU CA C 53.518 0.088 1 363 119 79 GLU CB C 34.052 0.125 1 364 119 79 GLU N N 122.764 0.020 1 365 120 80 PRO C C 173.177 0.064 1 366 120 80 PRO CA C 61.357 0.113 1 367 120 80 PRO CB C 30.907 0.125 1 368 121 81 TYR H H 7.187 0.006 1 369 121 81 TYR C C 173.150 0.064 1 370 121 81 TYR CA C 58.632 0.088 1 371 121 81 TYR CB C 39.396 0.125 1 372 121 81 TYR N N 119.305 0.021 1 373 122 82 ASN H H 8.530 0.011 1 374 122 82 ASN C C 174.692 0.064 1 375 122 82 ASN CA C 51.036 0.088 1 376 122 82 ASN CB C 40.211 0.125 1 377 122 82 ASN N N 120.960 0.033 1 378 123 83 GLN H H 8.096 0.007 1 379 123 83 GLN C C 177.040 0.064 1 380 123 83 GLN CA C 57.977 0.088 1 381 123 83 GLN CB C 29.066 0.125 1 382 123 83 GLN N N 111.862 0.024 1 383 124 84 GLN H H 8.082 0.011 1 384 124 84 GLN C C 178.253 0.064 1 385 124 84 GLN CA C 58.136 0.088 1 386 124 84 GLN CB C 28.902 0.125 1 387 124 84 GLN N N 115.817 0.020 1 388 125 85 ASN H H 8.065 0.008 1 389 125 85 ASN C C 179.565 0.064 1 390 125 85 ASN CA C 52.515 0.088 1 391 125 85 ASN CB C 39.262 0.125 1 392 125 85 ASN N N 117.809 0.050 1 393 126 86 LYS H H 7.251 0.008 1 394 126 86 LYS C C 177.350 0.064 1 395 126 86 LYS CA C 60.466 0.088 1 396 126 86 LYS CB C 31.653 0.125 1 397 126 86 LYS N N 118.319 0.023 1 398 127 87 ALA H H 8.513 0.005 1 399 127 87 ALA C C 181.189 0.064 1 400 127 87 ALA CA C 55.241 0.088 1 401 127 87 ALA CB C 18.259 0.125 1 402 127 87 ALA N N 121.470 0.028 1 403 128 88 HIS H H 8.011 0.007 1 404 128 88 HIS C C 177.466 0.064 1 405 128 88 HIS CA C 57.211 0.088 1 406 128 88 HIS CB C 28.066 0.125 1 407 128 88 HIS N N 114.719 0.036 1 408 129 89 PHE H H 7.141 0.009 1 409 129 89 PHE C C 178.272 0.064 1 410 129 89 PHE CA C 63.056 0.088 1 411 129 89 PHE CB C 41.330 0.125 1 412 129 89 PHE N N 117.504 0.048 1 413 130 90 ILE H H 8.734 0.007 1 414 130 90 ILE C C 178.595 0.064 1 415 130 90 ILE CA C 64.295 0.088 1 416 130 90 ILE CB C 36.812 0.125 1 417 130 90 ILE N N 119.825 0.027 1 418 131 91 GLN H H 7.613 0.005 1 419 131 91 GLN C C 178.100 0.064 1 420 131 91 GLN CA C 58.941 0.120 1 421 131 91 GLN CB C 28.620 0.125 1 422 131 91 GLN N N 118.875 0.020 1 423 132 92 PHE H H 8.104 0.010 1 424 132 92 PHE C C 178.013 0.064 1 425 132 92 PHE CA C 60.545 0.101 1 426 132 92 PHE CB C 39.369 0.125 1 427 132 92 PHE N N 120.467 0.034 1 428 133 93 LEU H H 8.745 0.008 1 429 133 93 LEU C C 178.175 0.064 1 430 133 93 LEU CA C 56.967 0.088 1 431 133 93 LEU CB C 41.890 0.125 1 432 133 93 LEU N N 120.758 0.023 1 433 134 94 ARG H H 7.754 0.011 1 434 134 94 ARG C C 177.403 0.064 1 435 134 94 ARG CA C 58.566 0.099 1 436 134 94 ARG CB C 30.370 0.125 1 437 134 94 ARG N N 119.326 0.034 1 438 135 95 ASP H H 8.125 0.011 1 439 135 95 ASP C C 176.875 0.064 1 440 135 95 ASP CA C 53.931 0.088 1 441 135 95 ASP CB C 41.976 0.125 1 442 135 95 ASP N N 114.532 0.037 1 443 136 96 GLY H H 8.263 0.009 1 444 136 96 GLY C C 174.850 0.064 1 445 136 96 GLY CA C 45.834 0.088 1 446 136 96 GLY N N 108.146 0.057 1 447 137 97 LEU H H 8.081 0.005 1 448 137 97 LEU C C 175.588 0.064 1 449 137 97 LEU CA C 54.015 0.088 1 450 137 97 LEU CB C 40.299 0.125 1 451 137 97 LEU N N 122.594 0.033 1 452 138 98 ASP H H 8.507 0.007 1 453 138 98 ASP C C 176.020 0.064 1 454 138 98 ASP CA C 52.876 0.088 1 455 138 98 ASP CB C 45.364 0.125 1 456 138 98 ASP N N 120.819 0.028 1 457 139 99 SER H H 11.001 0.008 1 458 139 99 SER C C 172.584 0.064 1 459 139 99 SER CA C 56.776 0.088 1 460 139 99 SER CB C 62.582 0.125 1 461 139 99 SER N N 121.034 0.038 1 462 140 100 VAL H H 7.509 0.006 1 463 140 100 VAL C C 173.878 0.064 1 464 140 100 VAL CA C 59.352 0.088 1 465 140 100 VAL CB C 35.261 0.125 1 466 140 100 VAL N N 121.200 0.042 1 467 141 101 ASP H H 8.972 0.010 1 468 141 101 ASP C C 175.830 0.064 1 469 141 101 ASP CA C 52.674 0.088 1 470 141 101 ASP CB C 44.065 0.125 1 471 141 101 ASP N N 125.032 0.035 1 472 142 102 ASP H H 7.911 0.012 1 473 142 102 ASP C C 176.315 0.064 1 474 142 102 ASP CA C 53.091 0.088 1 475 142 102 ASP CB C 45.106 0.125 1 476 142 102 ASP N N 117.377 0.025 1 477 143 103 ILE H H 9.703 0.008 1 478 143 103 ILE C C 174.697 0.064 1 479 143 103 ILE CA C 61.066 0.088 1 480 143 103 ILE CB C 39.982 0.156 1 481 143 103 ILE N N 123.509 0.034 1 482 144 104 VAL H H 8.137 0.012 1 483 144 104 VAL C C 175.630 0.064 1 484 144 104 VAL CA C 62.922 0.088 1 485 144 104 VAL CB C 32.638 0.129 1 486 144 104 VAL N N 126.490 0.052 1 487 145 105 ILE H H 8.993 0.008 1 488 145 105 ILE C C 174.674 0.064 1 489 145 105 ILE CA C 60.979 0.088 1 490 145 105 ILE CB C 40.404 0.125 1 491 145 105 ILE N N 129.098 0.027 1 492 146 106 ARG H H 8.970 0.011 1 493 146 106 ARG C C 174.726 0.064 1 494 146 106 ARG CA C 54.669 0.088 1 495 146 106 ARG CB C 35.041 0.125 1 496 146 106 ARG N N 123.394 0.050 1 497 147 107 LYS H H 8.835 0.005 1 498 147 107 LYS C C 174.305 0.064 1 499 147 107 LYS CA C 55.767 0.088 1 500 147 107 LYS CB C 33.179 0.125 1 501 147 107 LYS N N 124.580 0.030 1 502 148 108 ASP H H 7.647 0.013 1 503 148 108 ASP C C 174.483 0.064 1 504 148 108 ASP CA C 53.090 0.088 1 505 148 108 ASP CB C 42.837 0.125 1 506 148 108 ASP N N 123.976 0.020 1 507 149 109 ALA H H 8.380 0.009 1 508 149 109 ALA C C 177.066 0.064 1 509 149 109 ALA CA C 52.082 0.088 1 510 149 109 ALA CB C 18.654 0.125 1 511 149 109 ALA N N 123.035 0.033 1 512 150 110 CYS C C 174.086 0.064 1 513 150 110 CYS CA C 53.408 0.088 1 514 150 110 CYS CB C 38.931 0.125 1 515 151 111 SER H H 7.806 0.003 1 516 151 111 SER C C 174.214 0.064 1 517 151 111 SER CA C 57.710 0.088 1 518 151 111 SER CB C 63.705 0.125 1 519 151 111 SER N N 126.078 0.047 1 520 152 112 LEU H H 7.356 0.010 1 521 152 112 LEU C C 177.256 0.064 1 522 152 112 LEU CA C 55.160 0.088 1 523 152 112 LEU CB C 42.750 0.125 1 524 152 112 LEU N N 122.735 0.032 1 525 153 113 SER H H 8.468 0.004 1 526 153 113 SER CA C 57.692 0.088 1 527 153 113 SER CB C 63.548 0.125 1 528 153 113 SER N N 117.152 0.055 1 529 155 115 THR C C 175.360 0.064 1 530 155 115 THR CA C 61.158 0.088 1 531 155 115 THR CB C 68.650 0.125 1 532 156 116 MET H H 7.555 0.010 1 533 156 116 MET C C 177.113 0.064 1 534 156 116 MET CA C 58.489 0.093 1 535 156 116 MET CB C 32.791 0.125 1 536 156 116 MET N N 120.761 0.051 1 537 157 117 GLY H H 8.664 0.005 1 538 157 117 GLY C C 174.568 0.064 1 539 157 117 GLY CA C 46.694 0.088 1 540 157 117 GLY N N 107.009 0.023 1 541 158 118 GLU H H 7.871 0.007 1 542 158 118 GLU C C 179.384 0.064 1 543 158 118 GLU CA C 59.389 0.088 1 544 158 118 GLU CB C 29.190 0.125 1 545 158 118 GLU N N 119.311 0.031 1 546 159 119 ARG H H 7.618 0.002 1 547 159 119 ARG C C 178.630 0.064 1 548 159 119 ARG CA C 58.686 0.135 1 549 159 119 ARG CB C 29.624 0.125 1 550 159 119 ARG N N 119.520 0.043 1 551 160 120 LEU H H 7.940 0.005 1 552 160 120 LEU C C 179.138 0.064 1 553 160 120 LEU CA C 57.437 0.088 1 554 160 120 LEU CB C 40.255 0.125 1 555 160 120 LEU N N 119.093 0.053 1 556 161 121 LEU H H 7.769 0.004 1 557 161 121 LEU C C 181.308 0.064 1 558 161 121 LEU CA C 57.415 0.088 1 559 161 121 LEU CB C 41.535 0.125 1 560 161 121 LEU N N 117.984 0.036 1 561 162 122 THR H H 7.784 0.004 1 562 162 122 THR C C 175.573 0.064 1 563 162 122 THR CA C 65.053 0.088 1 564 162 122 THR CB C 69.094 0.125 1 565 162 122 THR N N 114.558 0.047 1 566 163 123 TYR H H 7.673 0.006 1 567 163 123 TYR C C 176.517 0.064 1 568 163 123 TYR CA C 57.223 0.088 1 569 163 123 TYR CB C 37.933 0.125 1 570 163 123 TYR N N 119.602 0.033 1 571 164 124 GLY H H 7.841 0.006 1 572 164 124 GLY C C 174.976 0.064 1 573 164 124 GLY CA C 45.516 0.088 1 574 164 124 GLY N N 106.840 0.022 1 575 165 125 VAL H H 7.527 0.006 1 576 165 125 VAL C C 174.438 0.064 1 577 165 125 VAL CA C 63.627 0.088 1 578 165 125 VAL CB C 31.243 0.125 1 579 165 125 VAL N N 121.311 0.061 1 580 166 126 LYS H H 8.053 0.014 1 581 166 126 LYS C C 176.149 0.064 1 582 166 126 LYS CA C 55.529 0.088 1 583 166 126 LYS CB C 34.455 0.125 1 584 166 126 LYS N N 124.736 0.036 1 585 167 127 LYS H H 8.615 0.007 1 586 167 127 LYS C C 176.208 0.064 1 587 167 127 LYS CA C 56.606 0.088 1 588 167 127 LYS CB C 33.748 0.125 1 589 167 127 LYS N N 124.413 0.020 1 590 168 128 MET H H 8.646 0.005 1 591 168 128 MET C C 173.262 0.064 1 592 168 128 MET CA C 52.214 0.088 1 593 168 128 MET CB C 33.581 0.125 1 594 168 128 MET N N 126.572 0.025 1 595 169 129 PRO C C 176.227 0.064 1 596 169 129 PRO CA C 63.182 0.088 1 597 169 129 PRO CB C 31.567 0.125 1 598 170 130 SER H H 8.621 0.003 1 599 170 130 SER C C 175.768 0.064 1 600 170 130 SER CA C 54.769 0.088 1 601 170 130 SER CB C 65.686 0.125 1 602 170 130 SER N N 115.323 0.043 1 603 171 131 ALA H H 8.600 0.008 1 604 171 131 ALA C C 175.522 0.064 1 605 171 131 ALA CA C 52.533 0.088 1 606 171 131 ALA CB C 18.635 0.125 1 607 171 131 ALA N N 129.469 0.038 1 608 172 132 TYR H H 7.888 0.010 1 609 172 132 TYR C C 175.206 0.064 1 610 172 132 TYR CA C 54.745 0.088 1 611 172 132 TYR CB C 41.620 0.125 1 612 172 132 TYR N N 115.817 0.043 1 613 173 133 PRO C C 177.712 0.064 1 614 173 133 PRO CA C 64.894 0.088 1 615 173 133 PRO CB C 32.076 0.125 1 616 174 134 GLU H H 9.875 0.006 1 617 174 134 GLU C C 175.444 0.064 1 618 174 134 GLU CA C 57.532 0.088 1 619 174 134 GLU CB C 29.174 0.125 1 620 174 134 GLU N N 116.101 0.044 1 621 175 135 TYR H H 8.134 0.010 1 622 175 135 TYR C C 176.894 0.064 1 623 175 135 TYR CA C 57.348 0.088 1 624 175 135 TYR CB C 41.733 0.125 1 625 175 135 TYR N N 116.668 0.036 1 626 176 136 GLU H H 9.527 0.008 1 627 176 136 GLU C C 174.984 0.064 1 628 176 136 GLU CA C 55.222 0.088 1 629 176 136 GLU CB C 33.291 0.125 1 630 176 136 GLU N N 121.882 0.029 1 631 177 137 ALA H H 8.960 0.007 1 632 177 137 ALA C C 174.875 0.064 1 633 177 137 ALA CA C 51.000 0.088 1 634 177 137 ALA CB C 23.392 0.125 1 635 177 137 ALA N N 125.599 0.020 1 636 178 138 TYR H H 9.005 0.008 1 637 178 138 TYR C C 174.669 0.064 1 638 178 138 TYR CA C 56.320 0.088 1 639 178 138 TYR CB C 42.823 0.125 1 640 178 138 TYR N N 118.717 0.031 1 641 179 139 GLU H H 9.226 0.008 1 642 179 139 GLU C C 174.187 0.064 1 643 179 139 GLU CA C 55.114 0.088 1 644 179 139 GLU CB C 33.984 0.125 1 645 179 139 GLU N N 121.663 0.042 1 646 180 140 ASP H H 9.702 0.008 1 647 180 140 ASP C C 174.533 0.064 1 648 180 140 ASP CA C 52.685 0.088 1 649 180 140 ASP CB C 43.954 0.125 1 650 180 140 ASP N N 128.062 0.046 1 651 181 141 LYS H H 8.719 0.006 1 652 181 141 LYS C C 176.162 0.064 1 653 181 141 LYS CA C 54.353 0.088 1 654 181 141 LYS CB C 33.789 0.125 1 655 181 141 LYS N N 127.142 0.071 1 656 182 142 ARG H H 7.793 0.008 1 657 182 142 ARG C C 174.748 0.064 1 658 182 142 ARG CA C 56.559 0.088 1 659 182 142 ARG CB C 31.450 0.125 1 660 182 142 ARG N N 121.435 0.020 1 661 183 143 HIS H H 8.280 0.006 1 662 183 143 HIS C C 174.695 0.064 1 663 183 143 HIS CA C 56.034 0.106 1 664 183 143 HIS CB C 29.790 0.125 1 665 183 143 HIS N N 118.945 0.045 1 666 184 144 ILE H H 8.581 0.006 1 667 184 144 ILE C C 174.712 0.064 1 668 184 144 ILE CA C 57.408 0.088 1 669 184 144 ILE CB C 38.172 0.125 1 670 184 144 ILE N N 127.800 0.030 1 671 185 145 PRO C C 178.013 0.064 1 672 185 145 PRO CA C 65.466 0.088 1 673 185 145 PRO CB C 31.567 0.125 1 674 186 146 GLU H H 8.714 0.005 1 675 186 146 GLU C C 176.304 0.064 1 676 186 146 GLU CA C 57.578 0.088 1 677 186 146 GLU CB C 28.912 0.125 1 678 186 146 GLU N N 112.701 0.028 1 679 187 147 ASN H H 7.741 0.009 1 680 187 147 ASN C C 172.869 0.064 1 681 187 147 ASN CA C 51.002 0.088 1 682 187 147 ASN CB C 38.825 0.125 1 683 187 147 ASN N N 113.515 0.040 1 684 188 148 PRO C C 175.849 0.064 1 685 188 148 PRO CA C 63.489 0.096 1 686 188 148 PRO CB C 31.876 0.125 1 687 189 149 TYR H H 7.566 0.009 1 688 189 149 TYR C C 174.639 0.064 1 689 189 149 TYR CA C 56.663 0.088 1 690 189 149 TYR CB C 37.358 0.125 1 691 189 149 TYR N N 117.023 0.020 1 692 190 150 PHE H H 6.735 0.012 1 693 190 150 PHE C C 176.052 0.064 1 694 190 150 PHE CA C 59.362 0.088 1 695 190 150 PHE CB C 39.962 0.125 1 696 190 150 PHE N N 120.453 0.042 1 697 191 151 HIS H H 8.767 0.010 1 698 191 151 HIS C C 172.919 0.064 1 699 191 151 HIS CA C 54.987 0.088 1 700 191 151 HIS CB C 32.198 0.125 1 701 191 151 HIS N N 128.542 0.030 1 702 192 152 GLU H H 8.513 0.010 1 703 192 152 GLU C C 173.551 0.064 1 704 192 152 GLU CA C 54.953 0.088 1 705 192 152 GLU CB C 34.269 0.125 1 706 192 152 GLU N N 123.695 0.031 1 707 193 153 PHE H H 9.200 0.006 1 708 193 153 PHE C C 174.700 0.064 1 709 193 153 PHE CA C 56.222 0.088 1 710 193 153 PHE CB C 42.959 0.125 1 711 193 153 PHE N N 119.043 0.048 1 712 194 154 TYR H H 8.616 0.008 1 713 194 154 TYR C C 174.773 0.064 1 714 194 154 TYR CA C 55.792 0.102 1 715 194 154 TYR CB C 42.019 0.127 1 716 194 154 TYR N N 116.850 0.027 1 717 195 155 TYR H H 9.440 0.007 1 718 195 155 TYR C C 175.360 0.064 1 719 195 155 TYR CA C 56.128 0.088 1 720 195 155 TYR CB C 40.270 0.125 1 721 195 155 TYR N N 120.143 0.021 1 722 196 156 ILE H H 9.349 0.007 1 723 196 156 ILE C C 174.281 0.064 1 724 196 156 ILE CA C 60.537 0.088 1 725 196 156 ILE CB C 42.309 0.218 1 726 196 156 ILE N N 123.622 0.030 1 727 197 157 LYS H H 9.531 0.005 1 728 197 157 LYS C C 175.726 0.064 1 729 197 157 LYS CA C 55.129 0.088 1 730 197 157 LYS CB C 35.223 0.125 1 731 197 157 LYS N N 132.345 0.022 1 732 198 158 LYS H H 8.447 0.004 1 733 198 158 LYS C C 176.054 0.064 1 734 198 158 LYS CA C 55.198 0.088 1 735 198 158 LYS CB C 33.062 0.125 1 736 198 158 LYS N N 125.924 0.044 1 737 199 159 GLY H H 8.184 0.007 1 738 199 159 GLY C C 173.522 0.064 1 739 199 159 GLY CA C 44.772 0.088 1 740 199 159 GLY N N 107.582 0.020 1 741 200 160 GLU H H 8.401 0.004 1 742 200 160 GLU C C 176.305 0.064 1 743 200 160 GLU CA C 58.118 0.088 1 744 200 160 GLU CB C 30.073 0.125 1 745 200 160 GLU N N 120.892 0.027 1 746 201 161 ASN H H 8.597 0.005 1 747 201 161 ASN C C 172.601 0.064 1 748 201 161 ASN CA C 51.774 0.088 1 749 201 161 ASN CB C 38.665 0.125 1 750 201 161 ASN N N 117.052 0.039 1 751 202 162 PRO C C 175.011 0.064 1 752 202 162 PRO CA C 63.243 0.088 1 753 202 162 PRO CB C 34.122 0.125 1 754 203 163 ALA H H 8.239 0.009 1 755 203 163 ALA C C 175.801 0.064 1 756 203 163 ALA CA C 51.834 0.088 1 757 203 163 ALA CB C 23.223 0.125 1 758 203 163 ALA N N 116.874 0.020 1 759 204 164 ILE H H 9.189 0.008 1 760 204 164 ILE C C 174.790 0.064 1 761 204 164 ILE CA C 61.382 0.088 1 762 204 164 ILE CB C 40.886 0.125 1 763 204 164 ILE N N 118.712 0.030 1 764 205 165 ILE H H 9.503 0.008 1 765 205 165 ILE C C 175.217 0.064 1 766 205 165 ILE CA C 60.578 0.110 1 767 205 165 ILE CB C 40.504 0.125 1 768 205 165 ILE N N 130.606 0.030 1 769 206 166 THR H H 9.141 0.008 1 770 206 166 THR C C 173.387 0.064 1 771 206 166 THR CA C 61.127 0.088 1 772 206 166 THR CB C 70.226 0.125 1 773 206 166 THR N N 121.695 0.089 1 774 207 167 HIS H H 9.036 0.010 1 775 207 167 HIS C C 173.517 0.064 1 776 207 167 HIS CA C 54.502 0.088 1 777 207 167 HIS CB C 33.221 0.130 1 778 207 167 HIS N N 128.718 0.022 1 779 208 168 ARG H H 9.002 0.009 1 780 208 168 ARG C C 173.066 0.064 1 781 208 168 ARG CA C 53.507 0.088 1 782 208 168 ARG CB C 34.921 0.125 1 783 208 168 ARG N N 123.133 0.020 1 784 209 169 ASN H H 7.913 0.009 1 785 209 169 ASN C C 176.446 0.064 1 786 209 169 ASN CA C 51.500 0.088 1 787 209 169 ASN CB C 38.148 0.125 1 788 209 169 ASN N N 118.286 0.040 1 789 210 170 ASN H H 9.059 0.008 1 790 210 170 ASN C C 174.918 0.064 1 791 210 170 ASN CA C 53.449 0.088 1 792 210 170 ASN CB C 40.072 0.125 1 793 210 170 ASN N N 124.845 0.029 1 794 211 171 ARG H H 7.262 0.010 1 795 211 171 ARG C C 174.845 0.064 1 796 211 171 ARG CA C 57.136 0.088 1 797 211 171 ARG CB C 32.389 0.125 1 798 211 171 ARG N N 123.010 0.022 1 799 212 172 ILE H H 8.781 0.002 1 800 212 172 ILE C C 175.543 0.064 1 801 212 172 ILE CA C 60.608 0.088 1 802 212 172 ILE CB C 41.076 0.125 1 803 212 172 ILE N N 120.660 0.027 1 804 213 173 ASN H H 7.950 0.012 1 805 213 173 ASN C C 175.814 0.064 1 806 213 173 ASN CA C 52.188 0.088 1 807 213 173 ASN CB C 41.759 0.125 1 808 213 173 ASN N N 118.204 0.020 1 809 214 174 GLN C C 177.488 0.064 1 810 214 174 GLN CA C 58.594 0.088 1 811 214 174 GLN CB C 28.876 0.125 1 812 215 175 THR H H 7.908 0.010 1 813 215 175 THR C C 174.594 0.064 1 814 215 175 THR CA C 62.277 0.088 1 815 215 175 THR CB C 68.611 0.125 1 816 215 175 THR N N 107.195 0.034 1 817 216 176 GLU H H 7.038 0.009 1 818 216 176 GLU C C 175.270 0.064 1 819 216 176 GLU CA C 54.971 0.088 1 820 216 176 GLU CB C 32.324 0.125 1 821 216 176 GLU N N 120.994 0.060 1 822 217 177 GLU H H 7.956 0.006 1 823 217 177 GLU C C 177.101 0.064 1 824 217 177 GLU CA C 54.869 0.088 1 825 217 177 GLU CB C 31.329 0.125 1 826 217 177 GLU N N 116.787 0.026 1 827 218 178 ASP H H 8.529 0.003 1 828 218 178 ASP C C 175.798 0.064 1 829 218 178 ASP CA C 56.904 0.088 1 830 218 178 ASP CB C 41.474 0.125 1 831 218 178 ASP N N 119.696 0.020 1 832 219 179 SER H H 7.845 0.006 1 833 219 179 SER C C 173.409 0.064 1 834 219 179 SER CA C 56.579 0.138 1 835 219 179 SER CB C 63.749 0.125 1 836 219 179 SER N N 115.651 0.020 1 837 220 180 TYR H H 9.597 0.005 1 838 220 180 TYR C C 176.627 0.064 1 839 220 180 TYR CA C 57.657 0.088 1 840 220 180 TYR CB C 39.990 0.125 1 841 220 180 TYR N N 129.402 0.029 1 842 221 181 SER H H 8.781 0.008 1 843 221 181 SER C C 173.808 0.064 1 844 221 181 SER CA C 57.270 0.088 1 845 221 181 SER CB C 66.159 0.125 1 846 221 181 SER N N 114.441 0.023 1 847 222 182 THR H H 8.902 0.007 1 848 222 182 THR C C 173.726 0.064 1 849 222 182 THR CA C 62.276 0.088 1 850 222 182 THR CB C 70.849 0.125 1 851 222 182 THR N N 118.323 0.026 1 852 223 183 SER H H 9.046 0.008 1 853 223 183 SER C C 172.775 0.064 1 854 223 183 SER CA C 56.463 0.126 1 855 223 183 SER CB C 66.313 0.125 1 856 223 183 SER N N 119.747 0.020 1 857 224 184 VAL H H 8.583 0.008 1 858 224 184 VAL C C 175.386 0.064 1 859 224 184 VAL CA C 61.854 0.088 1 860 224 184 VAL CB C 33.364 0.125 1 861 224 184 VAL N N 124.538 0.046 1 862 225 185 GLY H H 8.294 0.011 1 863 225 185 GLY C C 171.832 0.064 1 864 225 185 GLY CA C 44.874 0.088 1 865 225 185 GLY N N 113.971 0.023 1 866 226 186 SER H H 8.419 0.013 1 867 226 186 SER C C 173.726 0.064 1 868 226 186 SER CA C 57.924 0.088 1 869 226 186 SER CB C 67.471 0.125 1 870 226 186 SER N N 116.534 0.028 1 871 227 187 CYS H H 8.771 0.006 1 872 227 187 CYS C C 172.344 0.064 1 873 227 187 CYS CA C 53.511 0.088 1 874 227 187 CYS CB C 45.044 0.125 1 875 227 187 CYS N N 122.944 0.030 1 876 228 188 ILE H H 8.812 0.007 1 877 228 188 ILE C C 175.576 0.064 1 878 228 188 ILE CA C 59.972 0.194 1 879 228 188 ILE CB C 41.480 0.125 1 880 228 188 ILE N N 120.670 0.031 1 881 229 189 ASN H H 8.921 0.007 1 882 229 189 ASN C C 174.292 0.064 1 883 229 189 ASN CA C 54.511 0.088 1 884 229 189 ASN CB C 37.966 0.125 1 885 229 189 ASN N N 124.721 0.026 1 886 230 190 GLY H H 8.593 0.005 1 887 230 190 GLY C C 173.680 0.064 1 888 230 190 GLY CA C 45.260 0.088 1 889 230 190 GLY N N 102.700 0.020 1 890 231 191 PHE H H 8.196 0.012 1 891 231 191 PHE C C 177.104 0.064 1 892 231 191 PHE CA C 57.309 0.088 1 893 231 191 PHE CB C 39.608 0.125 1 894 231 191 PHE N N 118.404 0.036 1 895 232 192 THR H H 9.407 0.007 1 896 232 192 THR C C 173.936 0.064 1 897 232 192 THR CA C 61.948 0.088 1 898 232 192 THR CB C 69.857 0.125 1 899 232 192 THR N N 117.763 0.069 1 900 233 193 VAL H H 8.579 0.013 1 901 233 193 VAL C C 175.471 0.064 1 902 233 193 VAL CA C 61.739 0.088 1 903 233 193 VAL CB C 33.218 0.125 1 904 233 193 VAL N N 127.394 0.024 1 905 234 194 GLN H H 8.816 0.009 1 906 234 194 GLN C C 174.509 0.064 1 907 234 194 GLN CA C 53.942 0.100 1 908 234 194 GLN CB C 32.447 0.125 1 909 234 194 GLN N N 127.843 0.036 1 910 235 195 TYR H H 8.438 0.009 1 911 235 195 TYR C C 171.676 0.064 1 912 235 195 TYR CA C 56.694 0.088 1 913 235 195 TYR CB C 40.849 0.125 1 914 235 195 TYR N N 119.711 0.054 1 915 236 196 TYR H H 8.982 0.011 1 916 236 196 TYR C C 172.521 0.064 1 917 236 196 TYR CA C 53.997 0.088 1 918 236 196 TYR CB C 37.995 0.125 1 919 236 196 TYR N N 121.481 0.021 1 920 237 197 PRO C C 176.734 0.064 1 921 237 197 PRO CA C 61.850 0.088 1 922 237 197 PRO CB C 32.015 0.125 1 923 238 198 PHE H H 10.204 0.008 1 924 238 198 PHE C C 181.254 0.064 1 925 238 198 PHE CA C 56.898 0.088 1 926 238 198 PHE CB C 34.996 0.125 1 927 238 198 PHE N N 116.767 0.025 1 928 239 199 ILE H H 9.079 0.008 1 929 239 199 ILE C C 177.127 0.064 1 930 239 199 ILE CA C 63.733 0.088 1 931 239 199 ILE CB C 38.428 0.125 1 932 239 199 ILE N N 120.095 0.067 1 933 240 200 ARG H H 7.973 0.008 1 934 240 200 ARG C C 177.105 0.064 1 935 240 200 ARG CA C 54.645 0.088 1 936 240 200 ARG CB C 29.905 0.125 1 937 240 200 ARG N N 116.784 0.020 1 938 241 201 GLU H H 8.279 0.007 1 939 241 201 GLU C C 176.147 0.064 1 940 241 201 GLU CA C 55.386 0.088 1 941 241 201 GLU CB C 28.996 0.125 1 942 241 201 GLU N N 119.912 0.022 1 943 242 202 LYS H H 8.342 0.008 1 944 242 202 LYS C C 177.494 0.064 1 945 242 202 LYS CA C 55.877 0.091 1 946 242 202 LYS CB C 34.696 0.125 1 947 242 202 LYS N N 119.572 0.039 1 948 243 203 GLN H H 8.729 0.009 1 949 243 203 GLN C C 174.109 0.064 1 950 243 203 GLN CA C 55.227 0.088 1 951 243 203 GLN CB C 28.824 0.125 1 952 243 203 GLN N N 120.338 0.030 1 953 244 204 GLN H H 8.057 0.010 1 954 244 204 GLN C C 176.123 0.064 1 955 244 204 GLN CA C 55.802 0.089 1 956 244 204 GLN CB C 28.855 0.125 1 957 244 204 GLN N N 120.764 0.028 1 958 245 205 LEU H H 10.502 0.005 1 959 245 205 LEU C C 177.072 0.064 1 960 245 205 LEU CA C 53.160 0.088 1 961 245 205 LEU CB C 43.194 0.125 1 962 245 205 LEU N N 132.950 0.048 1 963 246 206 THR H H 8.681 0.008 1 964 246 206 THR C C 175.579 0.064 1 965 246 206 THR CA C 60.210 0.088 1 966 246 206 THR CB C 72.084 0.125 1 967 246 206 THR N N 111.281 0.027 1 968 247 207 GLN H H 8.956 0.009 1 969 247 207 GLN C C 177.206 0.064 1 970 247 207 GLN CA C 59.540 0.134 1 971 247 207 GLN CB C 26.858 0.125 1 972 247 207 GLN N N 119.649 0.041 1 973 248 208 GLN H H 8.833 0.005 1 974 248 208 GLN C C 179.727 0.064 1 975 248 208 GLN CA C 59.587 0.088 1 976 248 208 GLN CB C 27.684 0.125 1 977 248 208 GLN N N 115.740 0.020 1 978 249 209 GLU H H 7.521 0.006 1 979 249 209 GLU C C 178.171 0.064 1 980 249 209 GLU CA C 59.492 0.088 1 981 249 209 GLU CB C 30.575 0.125 1 982 249 209 GLU N N 119.998 0.025 1 983 250 210 LEU H H 7.490 0.008 1 984 250 210 LEU C C 178.696 0.064 1 985 250 210 LEU CA C 57.953 0.088 1 986 250 210 LEU CB C 42.994 0.125 1 987 250 210 LEU N N 118.385 0.020 1 988 251 211 VAL H H 8.769 0.007 1 989 251 211 VAL C C 177.950 0.064 1 990 251 211 VAL CA C 65.993 0.088 1 991 251 211 VAL CB C 30.362 0.125 1 992 251 211 VAL N N 118.724 0.026 1 993 252 212 GLY H H 7.743 0.005 1 994 252 212 GLY C C 177.169 0.064 1 995 252 212 GLY CA C 47.240 0.088 1 996 252 212 GLY N N 106.159 0.029 1 997 253 213 TYR H H 7.544 0.008 1 998 253 213 TYR C C 178.373 0.064 1 999 253 213 TYR CA C 61.546 0.088 1 1000 253 213 TYR CB C 38.727 0.125 1 1001 253 213 TYR N N 123.338 0.052 1 1002 254 214 HIS H H 8.090 0.011 1 1003 254 214 HIS C C 177.748 0.064 1 1004 254 214 HIS CA C 60.775 0.110 1 1005 254 214 HIS CB C 30.539 0.125 1 1006 254 214 HIS N N 119.295 0.023 1 1007 255 215 GLN H H 9.280 0.008 1 1008 255 215 GLN C C 180.210 0.064 1 1009 255 215 GLN CA C 59.089 0.088 1 1010 255 215 GLN CB C 28.467 0.125 1 1011 255 215 GLN N N 116.783 0.020 1 1012 256 216 GLN H H 7.367 0.007 1 1013 256 216 GLN C C 178.742 0.064 1 1014 256 216 GLN CA C 59.016 0.088 1 1015 256 216 GLN CB C 29.991 0.125 1 1016 256 216 GLN N N 117.335 0.054 1 1017 257 217 VAL H H 7.793 0.009 1 1018 257 217 VAL C C 177.376 0.064 1 1019 257 217 VAL CA C 67.572 0.088 1 1020 257 217 VAL CB C 30.864 0.141 1 1021 257 217 VAL N N 123.618 0.024 1 1022 258 218 GLU H H 8.677 0.007 1 1023 258 218 GLU C C 178.607 0.064 1 1024 258 218 GLU CA C 60.224 0.088 1 1025 258 218 GLU CB C 30.055 0.125 1 1026 258 218 GLU N N 118.453 0.020 1 1027 259 219 GLN H H 7.517 0.005 1 1028 259 219 GLN C C 178.733 0.064 1 1029 259 219 GLN CA C 58.669 0.088 1 1030 259 219 GLN CB C 28.387 0.125 1 1031 259 219 GLN N N 115.830 0.020 1 1032 260 220 LEU H H 7.990 0.009 1 1033 260 220 LEU C C 178.496 0.064 1 1034 260 220 LEU CA C 57.367 0.088 1 1035 260 220 LEU CB C 41.960 0.125 1 1036 260 220 LEU N N 121.956 0.020 1 1037 261 221 VAL H H 8.205 0.013 1 1038 261 221 VAL C C 178.092 0.064 1 1039 261 221 VAL CA C 66.824 0.088 1 1040 261 221 VAL CB C 31.169 0.125 1 1041 261 221 VAL N N 117.971 0.020 1 1042 262 222 GLN H H 7.879 0.007 1 1043 262 222 GLN C C 178.817 0.064 1 1044 262 222 GLN CA C 59.474 0.088 1 1045 262 222 GLN CB C 28.224 0.125 1 1046 262 222 GLN N N 114.713 0.043 1 1047 263 223 SER H H 7.946 0.008 1 1048 263 223 SER C C 176.190 0.064 1 1049 263 223 SER CA C 61.293 0.088 1 1050 263 223 SER CB C 62.583 0.125 1 1051 263 223 SER N N 115.998 0.037 1 1052 264 224 PHE H H 7.649 0.005 1 1053 264 224 PHE C C 178.745 0.064 1 1054 264 224 PHE CA C 55.589 0.088 1 1055 264 224 PHE CB C 38.206 0.125 1 1056 264 224 PHE N N 121.304 0.020 1 1057 265 225 VAL H H 7.567 0.005 1 1058 265 225 VAL C C 177.314 0.064 1 1059 265 225 VAL CA C 63.513 0.088 1 1060 265 225 VAL CB C 32.829 0.125 1 1061 265 225 VAL N N 115.946 0.027 1 1062 266 226 ASN H H 8.419 0.011 1 1063 266 226 ASN C C 175.989 0.064 1 1064 266 226 ASN CA C 54.111 0.088 1 1065 266 226 ASN CB C 38.861 0.125 1 1066 266 226 ASN N N 120.996 0.021 1 1067 267 227 ASN H H 8.481 0.011 1 1068 267 227 ASN C C 175.828 0.064 1 1069 267 227 ASN CA C 53.643 0.088 1 1070 267 227 ASN CB C 39.006 0.125 1 1071 267 227 ASN N N 119.002 0.020 1 1072 268 228 SER H H 8.206 0.010 1 1073 268 228 SER C C 177.105 0.064 1 1074 268 228 SER CA C 59.019 0.088 1 1075 268 228 SER CB C 63.729 0.125 1 1076 268 228 SER N N 115.121 0.083 1 1077 269 229 ASN H H 8.278 0.014 1 1078 269 229 ASN C C 175.125 0.064 1 1079 269 229 ASN CA C 53.413 0.088 1 1080 269 229 ASN CB C 38.928 0.125 1 1081 269 229 ASN N N 119.882 0.022 1 1082 270 230 LYS H H 8.109 0.011 1 1083 270 230 LYS C C 176.468 0.064 1 1084 270 230 LYS CA C 56.418 0.088 1 1085 270 230 LYS CB C 32.992 0.125 1 1086 270 230 LYS N N 121.228 0.055 1 1087 271 231 LYS H H 8.293 0.008 1 1088 271 231 LYS C C 176.496 0.064 1 1089 271 231 LYS CA C 56.347 0.088 1 1090 271 231 LYS CB C 33.035 0.125 1 1091 271 231 LYS N N 122.641 0.020 1 1092 272 232 GLU H H 8.413 0.008 1 1093 272 232 GLU C C 176.003 0.064 1 1094 272 232 GLU CA C 56.498 0.088 1 1095 272 232 GLU CB C 30.488 0.125 1 1096 272 232 GLU N N 121.239 0.041 1 1097 273 233 ASN H H 8.401 0.010 1 1098 273 233 ASN C C 174.692 0.064 1 1099 273 233 ASN CA C 53.194 0.088 1 1100 273 233 ASN CB C 38.977 0.125 1 1101 273 233 ASN N N 119.030 0.035 1 1102 274 234 LEU H H 8.075 0.006 1 1103 274 234 LEU C C 175.965 0.064 1 1104 274 234 LEU CA C 55.304 0.088 1 1105 274 234 LEU CB C 42.520 0.125 1 1106 274 234 LEU N N 122.263 0.031 1 1107 275 235 TYR H H 7.546 0.004 1 1108 275 235 TYR C C 180.413 0.064 1 1109 275 235 TYR CA C 58.839 0.088 1 1110 275 235 TYR CB C 39.511 0.125 1 1111 275 235 TYR N N 124.237 0.020 1 1112 276 236 PHE H H 8.076 0.003 1 1113 276 236 PHE C C 174.486 0.064 1 1114 276 236 PHE CA C 57.395 0.088 1 1115 276 236 PHE CB C 39.591 0.125 1 1116 276 236 PHE N N 122.264 0.020 1 1117 277 237 GLN H H 7.721 0.005 1 1118 277 237 GLN C C 180.162 0.064 1 1119 277 237 GLN CA C 57.445 0.088 1 1120 277 237 GLN CB C 30.975 0.125 1 1121 277 237 GLN N N 125.881 0.032 1 stop_ save_