data_18730 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignment of West Nile Virus NS2B-NS3 protease in a complex with 4-phenyl-phenyl-KKR-aldehyde. ; _BMRB_accession_number 18730 _BMRB_flat_file_name bmr18730.str _Entry_type original _Submission_date 2012-09-20 _Accession_date 2012-09-20 _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 Gayen Shovanlal . . 2 Chen Angela Shuyi . 3 Kang Congbao . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 189 "13C chemical shifts" 557 "15N chemical shifts" 187 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-12 original author . stop_ _Original_release_date 2013-02-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Exploring the binding of peptidic West Nile virus NS2B-NS3 protease inhibitors by NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23211132 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kang Congbao . . 2 Gayen Shovanlal . . 3 Wang Weiling . . 4 Severin Rene . . 5 Chen 'Angela Shuyi' . . 6 Lim 'Huichang Annie' . . 7 Chia 'Cheng San Brian' . . 8 Schuller Andreas . . 9 Doan 'Danny Ngoc Phouc' . . 10 Poulsen Anders . . 11 Hill Jeffrey . . 12 Vasudevan Subhash G. . 13 Keller Thomas H. . stop_ _Journal_abbreviation 'Antiviral Res.' _Journal_name_full 'Antiviral research' _Journal_volume 97 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 137 _Page_last 144 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name West_nile_protease _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label West_nile_protease $West_nile_protease 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_West_nile_protease _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common West_nile_protease _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 248 _Mol_residue_sequence ; MAGSHHHHHHGSTDMWIERT ADISWESDAEITGSSERVDV RLDDDGNFQLMNDPGAGGGG SGGGGGVLWDTPSPKEYKKG DTTTGVYRIMTRGLLGSYQA GAGVMVEGVFHTLWHTTKGA ALMSGEGRLDPYWGSVKEDR LCYGGPWKLQHKWNGQDEVQ MIVVEPGKNVKNVQTKPGVF KTPEGEIGAVTLDFPTGTSG SPIVDKNGDVIGLYGNGVIM PNGSYISAIVQGERMDEPIP AGFEPEML ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 ALA 3 3 GLY 4 4 SER 5 5 HIS 6 6 HIS 7 7 HIS 8 8 HIS 9 9 HIS 10 10 HIS 11 11 GLY 12 12 SER 13 13 THR 14 14 ASP 15 15 MET 16 16 TRP 17 17 ILE 18 18 GLU 19 19 ARG 20 20 THR 21 21 ALA 22 22 ASP 23 23 ILE 24 24 SER 25 25 TRP 26 26 GLU 27 27 SER 28 28 ASP 29 29 ALA 30 30 GLU 31 31 ILE 32 32 THR 33 33 GLY 34 34 SER 35 35 SER 36 36 GLU 37 37 ARG 38 38 VAL 39 39 ASP 40 40 VAL 41 41 ARG 42 42 LEU 43 43 ASP 44 44 ASP 45 45 ASP 46 46 GLY 47 47 ASN 48 48 PHE 49 49 GLN 50 50 LEU 51 51 MET 52 52 ASN 53 53 ASP 54 54 PRO 55 55 GLY 56 56 ALA 57 57 GLY 58 58 GLY 59 59 GLY 60 60 GLY 61 61 SER 62 62 GLY 63 63 GLY 64 64 GLY 65 65 GLY 66 66 GLY 67 67 VAL 68 68 LEU 69 69 TRP 70 70 ASP 71 71 THR 72 72 PRO 73 73 SER 74 74 PRO 75 75 LYS 76 76 GLU 77 77 TYR 78 78 LYS 79 79 LYS 80 80 GLY 81 81 ASP 82 82 THR 83 83 THR 84 84 THR 85 85 GLY 86 86 VAL 87 87 TYR 88 88 ARG 89 89 ILE 90 90 MET 91 91 THR 92 92 ARG 93 93 GLY 94 94 LEU 95 95 LEU 96 96 GLY 97 97 SER 98 98 TYR 99 99 GLN 100 100 ALA 101 101 GLY 102 102 ALA 103 103 GLY 104 104 VAL 105 105 MET 106 106 VAL 107 107 GLU 108 108 GLY 109 109 VAL 110 110 PHE 111 111 HIS 112 112 THR 113 113 LEU 114 114 TRP 115 115 HIS 116 116 THR 117 117 THR 118 118 LYS 119 119 GLY 120 120 ALA 121 121 ALA 122 122 LEU 123 123 MET 124 124 SER 125 125 GLY 126 126 GLU 127 127 GLY 128 128 ARG 129 129 LEU 130 130 ASP 131 131 PRO 132 132 TYR 133 133 TRP 134 134 GLY 135 135 SER 136 136 VAL 137 137 LYS 138 138 GLU 139 139 ASP 140 140 ARG 141 141 LEU 142 142 CYS 143 143 TYR 144 144 GLY 145 145 GLY 146 146 PRO 147 147 TRP 148 148 LYS 149 149 LEU 150 150 GLN 151 151 HIS 152 152 LYS 153 153 TRP 154 154 ASN 155 155 GLY 156 156 GLN 157 157 ASP 158 158 GLU 159 159 VAL 160 160 GLN 161 161 MET 162 162 ILE 163 163 VAL 164 164 VAL 165 165 GLU 166 166 PRO 167 167 GLY 168 168 LYS 169 169 ASN 170 170 VAL 171 171 LYS 172 172 ASN 173 173 VAL 174 174 GLN 175 175 THR 176 176 LYS 177 177 PRO 178 178 GLY 179 179 VAL 180 180 PHE 181 181 LYS 182 182 THR 183 183 PRO 184 184 GLU 185 185 GLY 186 186 GLU 187 187 ILE 188 188 GLY 189 189 ALA 190 190 VAL 191 191 THR 192 192 LEU 193 193 ASP 194 194 PHE 195 195 PRO 196 196 THR 197 197 GLY 198 198 THR 199 199 SER 200 200 GLY 201 201 SER 202 202 PRO 203 203 ILE 204 204 VAL 205 205 ASP 206 206 LYS 207 207 ASN 208 208 GLY 209 209 ASP 210 210 VAL 211 211 ILE 212 212 GLY 213 213 LEU 214 214 TYR 215 215 GLY 216 216 ASN 217 217 GLY 218 218 VAL 219 219 ILE 220 220 MET 221 221 PRO 222 222 ASN 223 223 GLY 224 224 SER 225 225 TYR 226 226 ILE 227 227 SER 228 228 ALA 229 229 ILE 230 230 VAL 231 231 GLN 232 232 GLY 233 233 GLU 234 234 ARG 235 235 MET 236 236 ASP 237 237 GLU 238 238 PRO 239 239 ILE 240 240 PRO 241 241 ALA 242 242 GLY 243 243 PHE 244 244 GLU 245 245 PRO 246 246 GLU 247 247 MET 248 248 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-12 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 PDB 2FP7 "West Nile Virus Ns2b/ns3protease In Complex With Bz-nle-lys-arg-arg-h" 68.15 172 97.63 98.82 2.18e-114 PDB 2GGV "Crystal Structure Of The West Nile Virus Ns2b-Ns3 Protease, His51ala Mutant" 71.37 185 98.31 99.44 1.19e-120 PDB 2IJO "Crystal Structure Of The West Nile Virus Ns2b-Ns3 Protease Complexed With Bovine Pancreatic Trypsin Inhibitor" 74.19 192 98.91 100.00 1.57e-127 PDB 3E90 "West Nile Vi Rus Ns2b-Ns3protease In Complexed With Inhibitor Naph-Kkr-H" 75.81 198 98.94 100.00 9.92e-130 GB ADX89821 "polyprotein, partial [West Nile virus]" 74.19 1920 100.00 100.00 1.46e-118 GB ADX89822 "polyprotein, partial [West Nile virus]" 74.19 1920 100.00 100.00 1.50e-118 GB ADX89823 "polyprotein, partial [West Nile virus]" 74.19 1920 100.00 100.00 1.46e-118 GB ADX89824 "polyprotein, partial [West Nile virus]" 74.19 1920 100.00 100.00 1.46e-118 GB ADX89825 "polyprotein, partial [West Nile virus]" 74.19 1920 100.00 100.00 1.46e-118 REF NP_776018 "unnamed protein product [West Nile virus]" 74.19 619 97.83 98.91 5.03e-123 REF YP_001527884 "unnamed protein product [West Nile virus]" 74.19 619 100.00 100.00 8.93e-126 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $West_nile_protease 'Escherichia coli' 562 Bacteria . Escherichia coli 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 $West_nile_protease 'recombinant technology' . Escherichia coli . pET21 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'Sample is dissolved in 20mM HEPES, pH 7.3, 1mM DTT, and 10% D2O, as well as 2mM peptide inhibitor.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $West_nile_protease 0.8 mM '[U-13C; U-15N]' '4-Phenyl-phenylacetyl-KKR aldehyde' 2 mM 'natural abundance' HEPES 20 mM 'natural abundance' DTT 1 mM 'natural abundance' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 1.3 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_ save_NMRPipe _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_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _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_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details 'Sample is dissolved in 20mM HEPES, pH 7.3, 1mM DTT, and 10% D2O.' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0 . M pH 7.3 . pH pressure 1 . atm temperature 298 . 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 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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 HNCACB' '3D CBCA(CO)NH' '3D HNCA' '3D HNCO' '3D HN(CO)CA' 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 West_nile_protease _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 10 10 HIS CA C 56.66 0.02 1 2 10 10 HIS CB C 30.46 0.2 1 3 11 11 GLY H H 8.294 0.02 1 4 11 11 GLY C C 171.43 0.2 1 5 11 11 GLY CA C 45.37 0.2 1 6 11 11 GLY N N 110.069 0.2 1 7 12 12 SER H H 8.151 0.02 1 8 12 12 SER C C 171.83 0.2 1 9 12 12 SER CA C 58.74 0.2 1 10 12 12 SER CB C 64.36 0.2 1 11 12 12 SER N N 115.468 0.2 1 12 13 13 THR H H 8.057 0.02 1 13 13 13 THR C C 171.03 0.2 1 14 13 13 THR CA C 61.03 0.2 1 15 13 13 THR CB C 69.53 0.2 1 16 13 13 THR N N 114.994 0.2 1 17 14 14 ASP H H 8.334 0.02 1 18 14 14 ASP C C 172.93 0.2 1 19 14 14 ASP CA C 55.11 0.2 1 20 14 14 ASP CB C 41.89 0.2 1 21 14 14 ASP N N 122.236 0.2 1 22 15 15 MET H H 8.214 0.02 1 23 15 15 MET C C 172.43 0.2 1 24 15 15 MET CA C 55.71 0.2 1 25 15 15 MET N N 119.316 0.2 1 26 16 16 TRP C C 169.93 0.2 1 27 16 16 TRP CA C 56.56 0.2 1 28 16 16 TRP CB C 33.5 0.2 1 29 17 17 ILE H H 8.071 0.02 1 30 17 17 ILE C C 172.83 0.2 1 31 17 17 ILE CA C 58.2 0.2 1 32 17 17 ILE CB C 41.03 0.2 1 33 17 17 ILE N N 109.281 0.2 1 34 18 18 GLU C C 172.33 0.2 1 35 18 18 GLU CA C 54.34 0.2 1 36 18 18 GLU CB C 33.03 0.2 1 37 19 19 ARG H H 9.22 0.02 1 38 19 19 ARG C C 173.53 0.2 1 39 19 19 ARG CA C 58.1 0.2 1 40 19 19 ARG CB C 28.36 0.2 1 41 19 19 ARG N N 129.707 0.2 1 42 20 20 THR H H 9.03 0.02 1 43 20 20 THR C C 169.83 0.2 1 44 20 20 THR CA C 60.41 0.2 1 45 20 20 THR CB C 71.54 0.2 1 46 20 20 THR N N 119.156 0.2 1 47 21 21 ALA H H 7.421 0.02 1 48 21 21 ALA C C 172.43 0.2 1 49 21 21 ALA CA C 52.37 0.2 1 50 21 21 ALA CB C 22.36 0.2 1 51 21 21 ALA N N 121.1 0.2 1 52 22 22 ASP C C 172.63 0.2 1 53 22 22 ASP CA C 53.63 0.2 1 54 22 22 ASP CB C 41.7 0.2 1 55 23 23 ILE H H 8.766 0.02 1 56 23 23 ILE C C 172.43 0.2 1 57 23 23 ILE CA C 62.19 0.2 1 58 23 23 ILE CB C 37.23 0.2 1 59 23 23 ILE N N 119.77 0.2 1 60 24 24 SER H H 6.854 0.02 1 61 24 24 SER C C 168.53 0.2 1 62 24 24 SER CA C 57.69 0.2 1 63 24 24 SER CB C 65.32 0.2 1 64 24 24 SER N N 120.332 0.2 1 65 25 25 TRP H H 8.325 0.02 1 66 25 25 TRP C C 173.33 0.2 1 67 25 25 TRP CA C 56.55 0.2 1 68 25 25 TRP CB C 30.03 0.2 1 69 25 25 TRP N N 122.044 0.2 1 70 26 26 GLU H H 8.815 0.02 1 71 26 26 GLU C C 174.13 0.2 1 72 26 26 GLU CA C 54.48 0.2 1 73 26 26 GLU CB C 31.08 0.2 1 74 26 26 GLU N N 129.244 0.2 1 75 27 27 SER H H 8.884 0.02 1 76 27 27 SER C C 171.73 0.2 1 77 27 27 SER CA C 60.9 0.2 1 78 27 27 SER CB C 63.41 0.2 1 79 27 27 SER N N 120.971 0.2 1 80 28 28 ASP H H 8.4 0.02 1 81 28 28 ASP C C 172.23 0.2 1 82 28 28 ASP CA C 53.78 0.2 1 83 28 28 ASP CB C 39.56 0.2 1 84 28 28 ASP N N 119.346 0.2 1 85 29 29 ALA H H 6.854 0.02 1 86 29 29 ALA C C 174.23 0.2 1 87 29 29 ALA CA C 52.37 0.2 1 88 29 29 ALA CB C 19.46 0.2 1 89 29 29 ALA N N 121.711 0.2 1 90 30 30 GLU H H 8.102 0.02 1 91 30 30 GLU C C 171.93 0.2 1 92 30 30 GLU CA C 56.61 0.2 1 93 30 30 GLU CB C 30.22 0.2 1 94 30 30 GLU N N 121.798 0.2 1 95 31 31 ILE H H 8.215 0.02 1 96 31 31 ILE C C 174.13 0.2 1 97 31 31 ILE CA C 60.23 0.2 1 98 31 31 ILE CB C 38.16 0.2 1 99 31 31 ILE N N 124.807 0.2 1 100 32 32 THR H H 8.762 0.02 1 101 32 32 THR C C 170.83 0.2 1 102 32 32 THR CA C 60.81 0.2 1 103 32 32 THR CB C 69.36 0.2 1 104 32 32 THR N N 122.117 0.2 1 105 33 33 GLY H H 8.202 0.02 1 106 33 33 GLY C C 169.73 0.2 1 107 33 33 GLY CA C 44.74 0.2 1 108 33 33 GLY N N 110.863 0.2 1 109 34 34 SER H H 7.672 0.02 1 110 34 34 SER C C 170.93 0.2 1 111 34 34 SER CA C 57.8 0.2 1 112 34 34 SER CB C 64.9 0.2 1 113 34 34 SER N N 113.488 0.2 1 114 35 35 SER H H 8.458 0.02 1 115 35 35 SER C C 171.33 0.2 1 116 35 35 SER CA C 56.89 0.2 1 117 35 35 SER CB C 63.26 0.2 1 118 35 35 SER N N 117.45 0.2 1 119 36 36 GLU H H 7.99 0.02 1 120 36 36 GLU C C 172.23 0.2 1 121 36 36 GLU CA C 55.15 0.2 1 122 36 36 GLU CB C 30.92 0.2 1 123 36 36 GLU N N 124.71 0.2 1 124 37 37 ARG H H 8.468 0.02 1 125 37 37 ARG C C 173.03 0.2 1 126 37 37 ARG CA C 55.36 0.2 1 127 37 37 ARG CB C 31.13 0.2 1 128 37 37 ARG N N 121.05 0.2 1 129 38 38 VAL H H 8.593 0.02 1 130 38 38 VAL C C 171.33 0.2 1 131 38 38 VAL CA C 60.83 0.2 1 132 38 38 VAL CB C 35.63 0.2 1 133 38 38 VAL N N 123.942 0.2 1 134 39 39 ASP H H 8.413 0.02 1 135 39 39 ASP C C 172.93 0.2 1 136 39 39 ASP CA C 54.46 0.2 1 137 39 39 ASP CB C 41.23 0.2 1 138 39 39 ASP N N 127.438 0.2 1 139 40 40 VAL H H 8.127 0.02 1 140 40 40 VAL C C 170.23 0.2 1 141 40 40 VAL CA C 60.18 0.2 1 142 40 40 VAL CB C 36.95 0.2 1 143 40 40 VAL N N 117.432 0.2 1 144 41 41 ARG H H 8.523 0.02 1 145 41 41 ARG C C 170.83 0.2 1 146 41 41 ARG CA C 54.31 0.2 1 147 41 41 ARG CB C 32.79 0.2 1 148 41 41 ARG N N 115.006 0.2 1 149 42 42 LEU H H 9.076 0.02 1 150 42 42 LEU C C 173.53 0.2 1 151 42 42 LEU CA C 54.03 0.2 1 152 42 42 LEU CB C 42.99 0.2 1 153 42 42 LEU N N 126.301 0.2 1 154 43 43 ASP H H 8.412 0.02 1 155 43 43 ASP CA C 53.04 0.2 1 156 43 43 ASP CB C 41.61 0.2 1 157 43 43 ASP N N 127.299 0.2 1 158 44 44 ASP H H 8.062 0.02 1 159 44 44 ASP C C 173.33 0.2 1 160 44 44 ASP CA C 56.88 0.2 1 161 44 44 ASP CB C 40.31 0.2 1 162 44 44 ASP N N 114.851 0.2 1 163 45 45 ASP H H 7.958 0.02 1 164 45 45 ASP C C 173.33 0.2 1 165 45 45 ASP CA C 53.89 0.2 1 166 45 45 ASP CB C 41.54 0.2 1 167 45 45 ASP N N 116.938 0.2 1 168 46 46 GLY H H 7.938 0.02 1 169 46 46 GLY C C 171.73 0.2 1 170 46 46 GLY CA C 47.35 0.2 1 171 46 46 GLY N N 108.086 0.2 1 172 47 47 ASN H H 8.131 0.02 1 173 47 47 ASN C C 172.93 0.2 1 174 47 47 ASN CA C 51.56 0.2 1 175 47 47 ASN CB C 39.76 0.2 1 176 47 47 ASN N N 118.238 0.2 1 177 48 48 PHE H H 9.943 0.02 1 178 48 48 PHE C C 173.53 0.2 1 179 48 48 PHE CA C 59.59 0.2 1 180 48 48 PHE CB C 40.36 0.2 1 181 48 48 PHE N N 124.611 0.2 1 182 49 49 GLN H H 9.059 0.02 1 183 49 49 GLN C C 173.53 0.2 1 184 49 49 GLN CA C 53.21 0.2 1 185 49 49 GLN CB C 29.88 0.2 1 186 49 49 GLN N N 118.716 0.2 1 187 50 50 LEU H H 8.667 0.02 1 188 50 50 LEU C C 175.63 0.2 1 189 50 50 LEU CA C 55.84 0.2 1 190 50 50 LEU N N 122.697 0.2 1 191 52 52 ASN H H 8.258 0.02 1 192 52 52 ASN N N 115.911 0.2 1 193 53 53 ASP H H 7.566 0.02 1 194 53 53 ASP N N 120.31 0.2 1 195 54 54 PRO C C 174.93 0.2 1 196 54 54 PRO CA C 64 0.2 1 197 54 54 PRO CB C 31.5 0.2 1 198 55 55 GLY H H 8.434 0.02 1 199 55 55 GLY C C 171.43 0.2 1 200 55 55 GLY CA C 45.29 0.2 1 201 55 55 GLY N N 107.906 0.2 1 202 56 56 ALA H H 7.893 0.02 1 203 56 56 ALA C C 175.53 0.2 1 204 56 56 ALA CA C 52.73 0.2 1 205 56 56 ALA N N 123.405 0.2 1 206 57 57 GLY H H 8.337 0.02 1 207 57 57 GLY N N 108.698 0.2 1 208 58 58 GLY H H 7.284 0.02 1 209 58 58 GLY C C 178.73 0.2 1 210 58 58 GLY CA C 43.15 0.2 1 211 58 58 GLY N N 121.322 0.2 1 212 59 59 GLY H H 7.326 0.02 1 213 59 59 GLY N N 120.737 0.2 1 214 60 60 GLY H H 6.762 0.02 1 215 60 60 GLY N N 118.247 0.2 1 216 61 61 SER H H 8.455 0.02 1 217 61 61 SER N N 115.701 0.2 1 218 77 77 TYR CA C 57.15 0.2 1 219 77 77 TYR CB C 39.95 0.2 1 220 78 78 LYS H H 8.283 0.02 1 221 78 78 LYS C C 172.73 0.2 1 222 78 78 LYS CA C 55.68 0.2 1 223 78 78 LYS CB C 32.54 0.2 1 224 78 78 LYS N N 123.419 0.2 1 225 79 79 LYS H H 8.4 0.02 1 226 79 79 LYS C C 175.23 0.2 1 227 79 79 LYS CA C 57.15 0.2 1 228 79 79 LYS CB C 32.05 0.2 1 229 79 79 LYS N N 125.483 0.2 1 230 80 80 GLY H H 7.973 0.02 1 231 80 80 GLY C C 168.13 0.2 1 232 80 80 GLY CA C 44.69 0.2 1 233 80 80 GLY N N 110.725 0.2 1 234 81 81 ASP H H 7.385 0.02 1 235 81 81 ASP C C 175.03 0.2 1 236 81 81 ASP CA C 55.43 0.2 1 237 81 81 ASP CB C 41.11 0.2 1 238 81 81 ASP N N 119.406 0.2 1 239 82 82 THR H H 8.343 0.02 1 240 82 82 THR C C 171.43 0.2 1 241 82 82 THR CA C 59.48 0.2 1 242 82 82 THR N N 113.823 0.2 1 243 83 83 THR C C 173.23 0.2 1 244 83 83 THR CA C 65.09 0.2 1 245 83 83 THR CB C 68.67 0.2 1 246 84 84 THR H H 9.049 0.02 1 247 84 84 THR C C 172.03 0.2 1 248 84 84 THR CA C 64.15 0.2 1 249 84 84 THR CB C 70 0.2 1 250 84 84 THR N N 127.479 0.2 1 251 85 85 GLY H H 8.934 0.02 1 252 85 85 GLY C C 167.33 0.2 1 253 85 85 GLY CA C 45.11 0.2 1 254 85 85 GLY N N 111.915 0.2 1 255 86 86 VAL H H 8.9 0.02 1 256 86 86 VAL C C 172.73 0.2 1 257 86 86 VAL CA C 62.53 0.2 1 258 86 86 VAL CB C 32.89 0.2 1 259 86 86 VAL N N 120.69 0.2 1 260 87 87 TYR H H 9.014 0.02 1 261 87 87 TYR C C 172.53 0.2 1 262 87 87 TYR CA C 57.16 0.2 1 263 87 87 TYR CB C 42.77 0.2 1 264 87 87 TYR N N 125.724 0.2 1 265 88 88 ARG H H 8.7 0.02 1 266 88 88 ARG C C 172.33 0.2 1 267 88 88 ARG CA C 55.3 0.2 1 268 88 88 ARG CB C 32.34 0.2 1 269 88 88 ARG N N 116.097 0.2 1 270 89 89 ILE H H 8.707 0.02 1 271 89 89 ILE C C 171.43 0.2 1 272 89 89 ILE CA C 61.13 0.2 1 273 89 89 ILE N N 121.697 0.2 1 274 90 90 MET H H 8.874 0.02 1 275 90 90 MET C C 171.43 0.2 1 276 90 90 MET CA C 51.63 0.2 1 277 90 90 MET CB C 31.12 0.2 1 278 90 90 MET N N 125.989 0.2 1 279 91 91 THR H H 8.051 0.02 1 280 91 91 THR C C 169.03 0.2 1 281 91 91 THR CA C 59.4 0.2 1 282 91 91 THR CB C 70.22 0.2 1 283 91 91 THR N N 111.76 0.2 1 284 92 92 ARG H H 7.961 0.02 1 285 92 92 ARG C C 173.23 0.2 1 286 92 92 ARG CA C 56.09 0.2 1 287 92 92 ARG CB C 31.58 0.2 1 288 92 92 ARG N N 121.594 0.2 1 289 93 93 GLY H H 8.083 0.02 1 290 93 93 GLY C C 171.83 0.2 1 291 93 93 GLY CA C 44.53 0.2 1 292 93 93 GLY N N 111.799 0.2 1 293 94 94 LEU H H 8.597 0.02 1 294 94 94 LEU C C 176.03 0.2 1 295 94 94 LEU CA C 58.04 0.2 1 296 94 94 LEU CB C 41.88 0.2 1 297 94 94 LEU N N 122.097 0.2 1 298 95 95 LEU H H 8.386 0.02 1 299 95 95 LEU C C 174.23 0.2 1 300 95 95 LEU CA C 54.41 0.2 1 301 95 95 LEU CB C 41.21 0.2 1 302 95 95 LEU N N 116.215 0.2 1 303 96 96 GLY H H 7.426 0.02 1 304 96 96 GLY C C 171.03 0.2 1 305 96 96 GLY CA C 44.61 0.2 1 306 96 96 GLY N N 107.317 0.2 1 307 97 97 SER H H 8.642 0.02 1 308 97 97 SER C C 171.23 0.2 1 309 97 97 SER CA C 58.26 0.2 1 310 97 97 SER CB C 65.09 0.2 1 311 97 97 SER N N 117.108 0.2 1 312 98 98 TYR H H 8.77 0.02 1 313 98 98 TYR C C 169.33 0.2 1 314 98 98 TYR CA C 56.57 0.2 1 315 98 98 TYR CB C 39.96 0.2 1 316 98 98 TYR N N 119.459 0.2 1 317 99 99 GLN H H 8.629 0.02 1 318 99 99 GLN C C 172.13 0.2 1 319 99 99 GLN CA C 55.39 0.2 1 320 99 99 GLN N N 121.294 0.2 1 321 100 100 ALA H H 8.758 0.02 1 322 100 100 ALA CA C 52.42 0.2 1 323 100 100 ALA N N 131.046 0.2 1 324 101 101 GLY H H 7.854 0.02 1 325 101 101 GLY C C 166.43 0.2 1 326 101 101 GLY CA C 46.45 0.2 1 327 101 101 GLY N N 104.947 0.2 1 328 102 102 ALA H H 8.907 0.02 1 329 102 102 ALA C C 171.83 0.2 1 330 102 102 ALA CA C 50.8 0.2 1 331 102 102 ALA CB C 21.96 0.2 1 332 102 102 ALA N N 123.664 0.2 1 333 103 103 GLY H H 8.432 0.02 1 334 103 103 GLY C C 169.73 0.2 1 335 103 103 GLY CA C 46.89 0.2 1 336 103 103 GLY N N 103.906 0.2 1 337 104 104 VAL C C 169.43 0.2 1 338 104 104 VAL CA C 58.88 0.2 1 339 105 105 MET H H 9.747 0.02 1 340 105 105 MET CA C 53.52 0.2 1 341 105 105 MET N N 134.916 0.2 1 342 106 106 VAL H H 8.884 0.02 1 343 106 106 VAL CA C 62.4 0.2 1 344 106 106 VAL CB C 37.68 0.2 1 345 106 106 VAL N N 125.818 0.2 1 346 107 107 GLU H H 9.413 0.02 1 347 107 107 GLU C C 172.83 0.2 1 348 107 107 GLU CA C 57.48 0.2 1 349 107 107 GLU CB C 27.69 0.2 1 350 107 107 GLU N N 123.666 0.2 1 351 108 108 GLY H H 9.092 0.02 1 352 108 108 GLY C C 169.53 0.2 1 353 108 108 GLY CA C 45.42 0.2 1 354 108 108 GLY N N 103.058 0.2 1 355 109 109 VAL H H 7.498 0.02 1 356 109 109 VAL CA C 61.09 0.2 1 357 109 109 VAL CB C 34.78 0.2 1 358 109 109 VAL N N 119.617 0.2 1 359 110 110 PHE H H 8.311 0.02 1 360 110 110 PHE C C 171.63 0.2 1 361 110 110 PHE CA C 57.39 0.2 1 362 110 110 PHE CB C 40.39 0.2 1 363 110 110 PHE N N 126.353 0.2 1 364 111 111 HIS H H 8.494 0.02 1 365 111 111 HIS C C 170.23 0.2 1 366 111 111 HIS CA C 55.86 0.2 1 367 111 111 HIS CB C 30.22 0.2 1 368 111 111 HIS N N 125.97 0.2 1 369 112 112 THR H H 8.985 0.02 1 370 112 112 THR C C 170.43 0.2 1 371 112 112 THR CA C 60.61 0.2 1 372 112 112 THR N N 116.094 0.2 1 373 113 113 LEU C C 175.03 0.2 1 374 113 113 LEU CA C 54.35 0.2 1 375 113 113 LEU CB C 41.68 0.2 1 376 114 114 TRP H H 6.871 0.02 1 377 114 114 TRP CA C 61.08 0.2 1 378 114 114 TRP N N 122.726 0.2 1 379 115 115 HIS C C 173.43 0.2 1 380 115 115 HIS CA C 59.86 0.2 1 381 115 115 HIS CB C 27.03 0.2 1 382 116 116 THR H H 7.115 0.02 1 383 116 116 THR C C 173.63 0.2 1 384 116 116 THR CA C 64.6 0.2 1 385 116 116 THR CB C 68.37 0.2 1 386 116 116 THR N N 111.898 0.2 1 387 117 117 THR H H 6.347 0.02 1 388 117 117 THR C C 173.23 0.2 1 389 117 117 THR CA C 60.39 0.2 1 390 117 117 THR N N 105.937 0.2 1 391 118 118 LYS C C 172.73 0.2 1 392 118 118 LYS CA C 56.5 0.2 1 393 119 119 GLY H H 6.797 0.02 1 394 119 119 GLY C C 170.03 0.2 1 395 119 119 GLY CA C 44.71 0.2 1 396 120 120 ALA H H 6.921 0.02 1 397 120 120 ALA C C 174.83 0.2 1 398 120 120 ALA CA C 52.52 0.2 1 399 120 120 ALA CB C 18.76 0.2 1 400 120 120 ALA N N 120.716 0.2 1 401 121 121 ALA H H 8.497 0.02 1 402 121 121 ALA C C 172.83 0.2 1 403 121 121 ALA CA C 53.46 0.2 1 404 121 121 ALA CB C 18.7 0.2 1 405 121 121 ALA N N 123.671 0.2 1 406 122 122 LEU H H 8.007 0.02 1 407 122 122 LEU CA C 52.46 0.2 1 408 122 122 LEU N N 116.198 0.2 1 409 123 123 MET C C 173.03 0.2 1 410 123 123 MET CA C 54.7 0.2 1 411 123 123 MET CB C 29.65 0.2 1 412 124 124 SER H H 8.36 0.02 1 413 124 124 SER C C 172.93 0.2 1 414 124 124 SER CA C 56.08 0.2 1 415 124 124 SER CB C 62.98 0.2 1 416 124 124 SER N N 115.133 0.2 1 417 125 125 GLY H H 9.349 0.02 1 418 125 125 GLY C C 172.43 0.2 1 419 125 125 GLY CA C 47.02 0.2 1 420 125 125 GLY N N 120.194 0.2 1 421 126 126 GLU H H 9.044 0.02 1 422 126 126 GLU C C 173.23 0.2 1 423 126 126 GLU CA C 56.51 0.2 1 424 126 126 GLU CB C 29.7 0.2 1 425 126 126 GLU N N 125.223 0.2 1 426 127 127 GLY H H 7.367 0.02 1 427 127 127 GLY C C 168.03 0.2 1 428 127 127 GLY CA C 44.44 0.2 1 429 127 127 GLY N N 105.325 0.2 1 430 128 128 ARG C C 172.73 0.2 1 431 128 128 ARG CA C 55.01 0.2 1 432 128 128 ARG CB C 34.95 0.2 1 433 129 129 LEU H H 9.376 0.02 1 434 129 129 LEU C C 171.73 0.2 1 435 129 129 LEU CA C 53.7 0.2 1 436 129 129 LEU CB C 43.81 0.2 1 437 129 129 LEU N N 124.881 0.2 1 438 130 130 ASP H H 8.938 0.02 1 439 130 130 ASP C C 123.047 0.2 1 440 130 130 ASP CA C 52.06 0.2 1 441 130 130 ASP N N 123.017 0.2 1 442 131 131 PRO C C 172.83 0.2 1 443 131 131 PRO CA C 54.83 0.2 1 444 131 131 PRO CB C 35.94 0.2 1 445 132 132 TYR H H 8.938 0.02 1 446 132 132 TYR CA C 53.5 0.2 1 447 132 132 TYR N N 126.519 0.2 1 448 133 133 TRP C C 175.23 0.2 1 449 133 133 TRP CA C 57.29 0.2 1 450 133 133 TRP CB C 31.94 0.2 1 451 134 134 GLY H H 7.696 0.02 1 452 134 134 GLY C C 167.93 0.2 1 453 134 134 GLY CA C 44.85 0.2 1 454 134 134 GLY N N 110.751 0.2 1 455 135 135 SER H H 8.095 0.02 1 456 135 135 SER C C 171.83 0.2 1 457 135 135 SER CA C 55.47 0.2 1 458 135 135 SER CB C 65.83 0.2 1 459 135 135 SER N N 111.089 0.2 1 460 136 136 VAL H H 7.934 0.02 1 461 136 136 VAL C C 175.33 0.2 1 462 136 136 VAL CA C 65.87 0.2 1 463 136 136 VAL CB C 31.03 0.2 1 464 136 136 VAL N N 129.986 0.2 1 465 137 137 LYS H H 7.718 0.02 1 466 137 137 LYS C C 172.13 0.2 1 467 137 137 LYS CA C 59.33 0.2 1 468 137 137 LYS CB C 31.83 0.2 1 469 137 137 LYS N N 119.887 0.2 1 470 138 138 GLU H H 7.167 0.02 1 471 138 138 GLU C C 173.23 0.2 1 472 138 138 GLU CA C 56.04 0.2 1 473 138 138 GLU CB C 29.67 0.2 1 474 138 138 GLU N N 108.557 0.2 1 475 139 139 ASP H H 7.75 0.02 1 476 139 139 ASP C C 172.03 0.2 1 477 139 139 ASP CA C 54.5 0.2 1 478 139 139 ASP CB C 40.34 0.2 1 479 139 139 ASP N N 120.896 0.2 1 480 140 140 ARG H H 7.669 0.02 1 481 140 140 ARG C C 172.03 0.2 1 482 140 140 ARG CA C 56.25 0.2 1 483 140 140 ARG CB C 34.91 0.2 1 484 140 140 ARG N N 111.861 0.2 1 485 141 141 LEU H H 8.412 0.02 1 486 141 141 LEU C C 170.63 0.2 1 487 141 141 LEU CA C 55.42 0.2 1 488 141 141 LEU CB C 45.89 0.2 1 489 141 141 LEU N N 122.623 0.2 1 490 142 142 CYS H H 9.744 0.02 1 491 142 142 CYS C C 170.83 0.2 1 492 142 142 CYS CA C 55.01 0.2 1 493 142 142 CYS CB C 31.5 0.2 1 494 142 142 CYS N N 119.797 0.2 1 495 143 143 TYR H H 9.292 0.02 1 496 143 143 TYR C C 173.53 0.2 1 497 143 143 TYR CA C 57.46 0.2 1 498 143 143 TYR N N 118.668 0.2 1 499 144 144 GLY H H 8.135 0.02 1 500 144 144 GLY C C 169.73 0.2 1 501 144 144 GLY CA C 45.52 0.2 1 502 144 144 GLY N N 108.39 0.2 1 503 145 145 GLY H H 6.986 0.02 1 504 145 145 GLY CA C 44.22 0.2 1 505 145 145 GLY N N 107.612 0.2 1 506 146 146 PRO C C 170.43 0.2 1 507 146 146 PRO CA C 62.17 0.2 1 508 146 146 PRO CB C 32.05 0.2 1 509 147 147 TRP H H 7.134 0.02 1 510 147 147 TRP C C 174.53 0.2 1 511 147 147 TRP CA C 59.95 0.2 1 512 147 147 TRP CB C 30.13 0.2 1 513 147 147 TRP N N 119.567 0.2 1 514 148 148 LYS H H 10.711 0.02 1 515 148 148 LYS C C 175.63 0.2 1 516 148 148 LYS CA C 54.6 0.2 1 517 148 148 LYS CB C 34.64 0.2 1 518 148 148 LYS N N 128.114 0.2 1 519 149 149 LEU CA C 55.11 0.2 1 520 149 149 LEU CB C 40.12 0.2 1 521 150 150 GLN H H 8.17 0.02 1 522 150 150 GLN C C 172.53 0.2 1 523 150 150 GLN CA C 55.8 0.2 1 524 150 150 GLN N N 116.598 0.2 1 525 151 151 HIS C C 170.33 0.2 1 526 151 151 HIS CA C 57 0.2 1 527 151 151 HIS CB C 31.19 0.2 1 528 152 152 LYS H H 8.433 0.02 1 529 152 152 LYS C C 174.43 0.2 1 530 152 152 LYS CA C 54.19 0.2 1 531 152 152 LYS CB C 35.96 0.2 1 532 152 152 LYS N N 117.601 0.2 1 533 153 153 TRP H H 9.697 0.02 1 534 153 153 TRP C C 174.63 0.2 1 535 153 153 TRP CA C 57.45 0.2 1 536 153 153 TRP CB C 28.14 0.2 1 537 153 153 TRP N N 123.493 0.2 1 538 154 154 ASN H H 9.069 0.02 1 539 154 154 ASN C C 172.93 0.2 1 540 154 154 ASN CA C 53.03 0.2 1 541 154 154 ASN N N 128.319 0.2 1 542 155 155 GLY C C 170.63 0.2 1 543 155 155 GLY CA C 44.26 0.2 1 544 156 156 GLN H H 7.483 0.02 1 545 156 156 GLN C C 172.83 0.2 1 546 156 156 GLN CA C 56.46 0.2 1 547 156 156 GLN N N 115.744 0.2 1 548 157 157 ASP H H 8.161 0.02 1 549 157 157 ASP C C 174.63 0.2 1 550 157 157 ASP CA C 55.55 0.2 1 551 157 157 ASP CB C 43.48 0.2 1 552 157 157 ASP N N 119.042 0.2 1 553 158 158 GLU H H 8.618 0.02 1 554 158 158 GLU C C 172.43 0.2 1 555 158 158 GLU CA C 57.88 0.2 1 556 158 158 GLU CB C 30.67 0.2 1 557 158 158 GLU N N 115.991 0.2 1 558 159 159 VAL H H 8.738 0.02 1 559 159 159 VAL C C 171.63 0.2 1 560 159 159 VAL CA C 58.99 0.2 1 561 159 159 VAL CB C 34.15 0.2 1 562 159 159 VAL N N 110.543 0.2 1 563 160 160 GLN H H 8.725 0.02 1 564 160 160 GLN C C 172.03 0.2 1 565 160 160 GLN CA C 53.52 0.2 1 566 160 160 GLN CB C 30.71 0.2 1 567 160 160 GLN N N 115.65 0.2 1 568 161 161 MET H H 8.804 0.02 1 569 161 161 MET C C 171.43 0.2 1 570 161 161 MET CA C 54.15 0.2 1 571 161 161 MET CB C 35.36 0.2 1 572 161 161 MET N N 120.506 0.2 1 573 162 162 ILE H H 8.313 0.02 1 574 162 162 ILE C C 171.53 0.2 1 575 162 162 ILE CA C 54.14 0.2 1 576 162 162 ILE CB C 35.6 0.2 1 577 162 162 ILE N N 129.086 0.2 1 578 163 163 VAL H H 8.626 0.02 1 579 163 163 VAL C C 174.03 0.2 1 580 163 163 VAL CA C 63.92 0.2 1 581 163 163 VAL N N 123.705 0.2 1 582 164 164 VAL CA C 59.58 0.2 1 583 164 164 VAL CB C 28.37 0.2 1 584 165 165 GLU H H 7.415 0.02 1 585 165 165 GLU C C 172.63 0.2 1 586 165 165 GLU CA C 54.24 0.2 1 587 165 165 GLU N N 123.908 0.2 1 588 166 166 PRO C C 174.83 0.2 1 589 166 166 PRO CA C 63.54 0.2 1 590 166 166 PRO CB C 31.2 0.2 1 591 167 167 GLY H H 8.674 0.02 1 592 167 167 GLY C C 170.53 0.2 1 593 167 167 GLY CA C 46.07 0.2 1 594 167 167 GLY N N 110.611 0.2 1 595 168 168 LYS H H 7.352 0.02 1 596 168 168 LYS C C 173.43 0.2 1 597 168 168 LYS CA C 53.77 0.2 1 598 168 168 LYS CB C 35.61 0.2 1 599 168 168 LYS N N 117.551 0.2 1 600 169 169 ASN H H 8.493 0.02 1 601 169 169 ASN C C 173.93 0.2 1 602 169 169 ASN CA C 53.25 0.2 1 603 169 169 ASN CB C 37.86 0.2 1 604 169 169 ASN N N 119.048 0.2 1 605 170 170 VAL H H 8.537 0.02 1 606 170 170 VAL C C 171.83 0.2 1 607 170 170 VAL CA C 63.92 0.2 1 608 170 170 VAL CB C 31.58 0.2 1 609 170 170 VAL N N 122.99 0.2 1 610 171 171 LYS H H 7.388 0.02 1 611 171 171 LYS C C 169.73 0.2 1 612 171 171 LYS CA C 54.65 0.2 1 613 171 171 LYS CB C 35.11 0.2 1 614 171 171 LYS N N 122.329 0.2 1 615 172 172 ASN H H 8.543 0.02 1 616 172 172 ASN C C 172.53 0.2 1 617 172 172 ASN CA C 51.71 0.2 1 618 172 172 ASN CB C 38.13 0.2 1 619 172 172 ASN N N 121.428 0.2 1 620 173 173 VAL H H 8.303 0.02 1 621 173 173 VAL C C 170.13 0.2 1 622 173 173 VAL CA C 60.23 0.2 1 623 173 173 VAL CB C 34.78 0.2 1 624 173 173 VAL N N 114.738 0.2 1 625 174 174 GLN H H 9.196 0.02 1 626 174 174 GLN C C 170.43 0.2 1 627 174 174 GLN CA C 54.06 0.2 1 628 174 174 GLN CB C 31.61 0.2 1 629 174 174 GLN N N 127.061 0.2 1 630 175 175 THR H H 8.726 0.02 1 631 175 175 THR C C 168.13 0.2 1 632 175 175 THR CA C 60.53 0.2 1 633 175 175 THR CB C 70.31 0.2 1 634 175 175 THR N N 116.968 0.2 1 635 176 176 LYS H H 7.989 0.02 1 636 176 176 LYS C C 170.73 0.2 1 637 176 176 LYS CA C 52.75 0.2 1 638 176 176 LYS N N 128.248 0.2 1 639 177 177 PRO C C 174.73 0.2 1 640 177 177 PRO CA C 63.53 0.2 1 641 177 177 PRO CB C 30.38 0.2 1 642 178 178 GLY H H 8.129 0.02 1 643 178 178 GLY C C 170.03 0.2 1 644 178 178 GLY CA C 43.97 0.2 1 645 178 178 GLY N N 109.104 0.2 1 646 179 179 VAL H H 8.208 0.02 1 647 179 179 VAL C C 173.03 0.2 1 648 179 179 VAL CA C 60.74 0.2 1 649 179 179 VAL N N 113.839 0.2 1 650 180 180 PHE H H 9.394 0.02 1 651 180 180 PHE C C 172.33 0.2 1 652 180 180 PHE CA C 51.98 0.2 1 653 180 180 PHE CB C 37.79 0.2 1 654 180 180 PHE N N 123.52 0.2 1 655 181 181 LYS H H 9.1 0.02 1 656 181 181 LYS C C 172.83 0.2 1 657 181 181 LYS CA C 55.95 0.2 1 658 181 181 LYS CB C 31.43 0.2 1 659 181 181 LYS N N 126.279 0.2 1 660 182 182 THR H H 7.991 0.02 1 661 182 182 THR C C 172.43 0.2 1 662 182 182 THR CA C 59.57 0.2 1 663 182 182 THR N N 118.931 0.2 1 664 183 183 PRO C C 174.43 0.2 1 665 183 183 PRO CA C 65.02 0.2 1 666 183 183 PRO CB C 31.43 0.2 1 667 184 184 GLU H H 7.779 0.02 1 668 184 184 GLU C C 173.23 0.2 1 669 184 184 GLU CA C 56.48 0.2 1 670 184 184 GLU CB C 29.63 0.2 1 671 184 184 GLU N N 112.987 0.2 1 672 185 185 GLY H H 7.542 0.02 1 673 185 185 GLY C C 170.83 0.2 1 674 185 185 GLY CA C 44.74 0.2 1 675 185 185 GLY N N 108.101 0.2 1 676 186 186 GLU H H 8.595 0.02 1 677 186 186 GLU C C 174.03 0.2 1 678 186 186 GLU CA C 56.11 0.2 1 679 186 186 GLU CB C 31.27 0.2 1 680 186 186 GLU N N 120.543 0.2 1 681 187 187 ILE H H 9.145 0.02 1 682 187 187 ILE C C 172.63 0.2 1 683 187 187 ILE CA C 60.38 0.2 1 684 187 187 ILE CB C 42.23 0.2 1 685 187 187 ILE N N 122.923 0.2 1 686 188 188 GLY H H 9.857 0.02 1 687 188 188 GLY C C 168.93 0.2 1 688 188 188 GLY CA C 47.11 0.2 1 689 188 188 GLY N N 112.98 0.2 1 690 189 189 ALA H H 7.344 0.02 1 691 189 189 ALA C C 173.93 0.2 1 692 189 189 ALA CA C 51.02 0.2 1 693 189 189 ALA CB C 20.89 0.2 1 694 189 189 ALA N N 123.522 0.2 1 695 190 190 VAL H H 9.151 0.02 1 696 190 190 VAL C C 172.43 0.2 1 697 190 190 VAL CA C 57.72 0.2 1 698 190 190 VAL CB C 34.13 0.2 1 699 190 190 VAL N N 112.151 0.2 1 700 191 191 THR H H 9.333 0.02 1 701 191 191 THR C C 171.43 0.2 1 702 191 191 THR CA C 59.58 0.2 1 703 191 191 THR CB C 67.49 0.2 1 704 191 191 THR N N 124.608 0.2 1 705 192 192 LEU H H 6.838 0.02 1 706 192 192 LEU C C 172.73 0.2 1 707 192 192 LEU CA C 53.18 0.2 1 708 192 192 LEU CB C 45.09 0.2 1 709 192 192 LEU N N 120.949 0.2 1 710 193 193 ASP H H 8.781 0.02 1 711 193 193 ASP C C 172.63 0.2 1 712 193 193 ASP CA C 53.82 0.2 1 713 193 193 ASP CB C 41.89 0.2 1 714 193 193 ASP N N 127.848 0.2 1 715 194 194 PHE H H 7.331 0.02 1 716 194 194 PHE CA C 56.2 0.2 1 717 194 194 PHE N N 121.456 0.2 1 718 199 199 SER C C 169.73 0.2 1 719 199 199 SER CA C 62.49 0.2 1 720 199 199 SER CB C 64.79 0.2 1 721 200 200 GLY H H 10.056 0.02 1 722 200 200 GLY C C 169.53 0.2 1 723 200 200 GLY CA C 44.58 0.2 1 724 200 200 GLY N N 111.151 0.2 1 725 202 202 PRO C C 170.63 0.2 1 726 202 202 PRO CA C 62.65 0.2 1 727 202 202 PRO CB C 32.19 0.2 1 728 203 203 ILE H H 8.57 0.02 1 729 203 203 ILE C C 172.63 0.2 1 730 203 203 ILE CA C 59.05 0.2 1 731 203 203 ILE CB C 38.34 0.2 1 732 203 203 ILE N N 120.549 0.2 1 733 204 204 VAL H H 9.717 0.02 1 734 204 204 VAL C C 172.43 0.2 1 735 204 204 VAL CA C 58.66 0.2 1 736 204 204 VAL CB C 36.14 0.2 1 737 204 204 VAL N N 120.177 0.2 1 738 205 205 ASP H H 8.348 0.02 1 739 205 205 ASP C C 175.83 0.2 1 740 205 205 ASP CA C 51.7 0.2 1 741 205 205 ASP CB C 42.8 0.2 1 742 205 205 ASP N N 119.43 0.2 1 743 206 206 LYS H H 7.763 0.02 1 744 206 206 LYS C C 174.73 0.2 1 745 206 206 LYS CA C 57.73 0.2 1 746 206 206 LYS CB C 30.54 0.2 1 747 206 206 LYS N N 114.99 0.2 1 748 207 207 ASN H H 7.751 0.02 1 749 207 207 ASN C C 173.13 0.2 1 750 207 207 ASN CA C 53.21 0.2 1 751 207 207 ASN CB C 38.66 0.2 1 752 207 207 ASN N N 116.895 0.2 1 753 208 208 GLY H H 8.734 0.02 1 754 208 208 GLY C C 170.23 0.2 1 755 208 208 GLY CA C 45.05 0.2 1 756 208 208 GLY N N 109.372 0.2 1 757 209 209 ASP H H 7.786 0.02 1 758 209 209 ASP C C 172.83 0.2 1 759 209 209 ASP CA C 54.31 0.2 1 760 209 209 ASP CB C 40.92 0.2 1 761 209 209 ASP N N 118.68 0.2 1 762 210 210 VAL H H 8.552 0.02 1 763 210 210 VAL C C 173.83 0.2 1 764 210 210 VAL CA C 63.22 0.2 1 765 210 210 VAL CB C 31.13 0.2 1 766 210 210 VAL N N 119.397 0.2 1 767 211 211 ILE H H 8.884 0.02 1 768 211 211 ILE C C 172.03 0.2 1 769 211 211 ILE CA C 60.91 0.2 1 770 211 211 ILE CB C 37.71 0.2 1 771 211 211 ILE N N 120.795 0.2 1 772 212 212 GLY H H 7.421 0.02 1 773 212 212 GLY C C 167.53 0.2 1 774 212 212 GLY CA C 45.21 0.2 1 775 212 212 GLY N N 105.257 0.2 1 776 213 213 LEU H H 9.277 0.02 1 777 213 213 LEU C C 172.53 0.2 1 778 213 213 LEU CA C 53.49 0.2 1 779 213 213 LEU CB C 45.75 0.2 1 780 213 213 LEU N N 118.426 0.2 1 781 214 214 TYR H H 8.59 0.02 1 782 214 214 TYR C C 174.23 0.2 1 783 214 214 TYR CA C 58.38 0.2 1 784 214 214 TYR CB C 42.93 0.2 1 785 214 214 TYR N N 117.94 0.2 1 786 215 215 GLY H H 8.246 0.02 1 787 215 215 GLY C C 169.83 0.2 1 788 215 215 GLY CA C 46.76 0.2 1 789 215 215 GLY N N 110.819 0.2 1 790 216 216 ASN H H 6.931 0.02 1 791 216 216 ASN C C 172.33 0.2 1 792 216 216 ASN CA C 53.59 0.2 1 793 216 216 ASN CB C 39.87 0.2 1 794 216 216 ASN N N 116.367 0.2 1 795 217 217 GLY H H 8.347 0.02 1 796 217 217 GLY C C 169.23 0.2 1 797 217 217 GLY CA C 46.79 0.2 1 798 217 217 GLY N N 112.794 0.2 1 799 218 218 VAL H H 8.475 0.02 1 800 218 218 VAL C C 169.23 0.2 1 801 218 218 VAL CA C 59.67 0.2 1 802 218 218 VAL CB C 36.33 0.2 1 803 218 218 VAL N N 113.973 0.2 1 804 219 219 ILE H H 7.532 0.02 1 805 219 219 ILE C C 174.43 0.2 1 806 219 219 ILE CA C 59.66 0.2 1 807 219 219 ILE CB C 37.33 0.2 1 808 219 219 ILE N N 119.759 0.2 1 809 220 220 MET H H 8.899 0.02 1 810 220 220 MET C C 174.33 0.2 1 811 220 220 MET CA C 53.9 0.2 1 812 220 220 MET N N 126.401 0.2 1 813 221 221 PRO C C 174.23 0.2 1 814 221 221 PRO CA C 65.76 0.2 1 815 221 221 PRO CB C 31.12 0.2 1 816 222 222 ASN H H 7.579 0.02 1 817 222 222 ASN C C 173.73 0.2 1 818 222 222 ASN CA C 52.71 0.2 1 819 222 222 ASN CB C 37 0.2 1 820 222 222 ASN N N 111.663 0.2 1 821 223 223 GLY H H 8.528 0.02 1 822 223 223 GLY C C 171.53 0.2 1 823 223 223 GLY CA C 45.03 0.2 1 824 223 223 GLY N N 109.291 0.2 1 825 224 224 SER H H 7.614 0.02 1 826 224 224 SER C C 169.33 0.2 1 827 224 224 SER CA C 59.37 0.2 1 828 224 224 SER N N 116.158 0.2 1 829 225 225 TYR H H 7.951 0.02 1 830 225 225 TYR C C 171.23 0.2 1 831 225 225 TYR CA C 57.24 0.2 1 832 225 225 TYR CB C 40.96 0.2 1 833 225 225 TYR N N 123.054 0.2 1 834 226 226 ILE H H 7.504 0.02 1 835 226 226 ILE C C 171.73 0.2 1 836 226 226 ILE CA C 59.54 0.2 1 837 226 226 ILE N N 124.132 0.2 1 838 227 227 SER H H 8.113 0.02 1 839 227 227 SER C C 172.33 0.2 1 840 227 227 SER CA C 55.52 0.2 1 841 227 227 SER CB C 66.35 0.2 1 842 227 227 SER N N 115.759 0.2 1 843 228 228 ALA H H 8.767 0.02 1 844 228 228 ALA C C 175.53 0.2 1 845 228 228 ALA CA C 53.76 0.2 1 846 228 228 ALA CB C 18.7 0.2 1 847 229 229 ILE H H 8.014 0.02 1 848 229 229 ILE C C 172.73 0.2 1 849 229 229 ILE CA C 62.57 0.2 1 850 229 229 ILE CB C 35.6 0.2 1 851 229 229 ILE N N 121.335 0.2 1 852 230 230 VAL H H 8.98 0.02 1 853 230 230 VAL C C 172.73 0.2 1 854 230 230 VAL CA C 65.6 0.2 1 855 230 230 VAL CB C 31.56 0.2 1 856 230 230 VAL N N 130.964 0.2 1 857 231 231 GLN H H 8.462 0.02 1 858 231 231 GLN C C 171.83 0.2 1 859 231 231 GLN CA C 54.05 0.2 1 860 231 231 GLN CB C 32.74 0.2 1 861 231 231 GLN N N 127.029 0.2 1 862 232 232 GLY H H 8.766 0.02 1 863 232 232 GLY C C 168.93 0.2 1 864 232 232 GLY CA C 44.31 0.2 1 865 232 232 GLY N N 112.27 0.2 1 866 233 233 GLU H H 7.837 0.02 1 867 233 233 GLU C C 173.53 0.2 1 868 233 233 GLU CA C 55.59 0.2 1 869 233 233 GLU N N 117.347 0.2 1 870 234 234 ARG H H 7.951 0.02 1 871 234 234 ARG C C 173.73 0.2 1 872 234 234 ARG CA C 56.4 0.2 1 873 234 234 ARG CB C 29.86 0.2 1 874 234 234 ARG N N 120.837 0.2 1 875 235 235 MET H H 8.569 0.02 1 876 235 235 MET C C 172.03 0.2 1 877 235 235 MET CA C 55 0.2 1 878 235 235 MET CB C 34.64 0.2 1 879 235 235 MET N N 126.625 0.2 1 880 236 236 ASP H H 8.231 0.02 1 881 236 236 ASP C C 173.03 0.2 1 882 236 236 ASP CA C 54.14 0.2 1 883 236 236 ASP CB C 41.91 0.2 1 884 236 236 ASP N N 121.21 0.2 1 885 237 237 GLU H H 8.296 0.02 1 886 237 237 GLU C C 171.73 0.2 1 887 237 237 GLU CA C 54.61 0.2 1 888 237 237 GLU N N 121.191 0.2 1 889 238 238 PRO C C 173.83 0.2 1 890 238 238 PRO CA C 62.97 0.2 1 891 238 238 PRO CB C 31.45 0.2 1 892 239 239 ILE H H 8.161 0.02 1 893 239 239 ILE C C 172.13 0.2 1 894 239 239 ILE CA C 58.77 0.2 1 895 239 239 ILE N N 122.547 0.2 1 896 240 240 PRO C C 173.83 0.2 1 897 240 240 PRO CA C 63.23 0.2 1 898 240 240 PRO CB C 31.51 0.2 1 899 241 241 ALA H H 8.275 0.02 1 900 241 241 ALA C C 175.63 0.2 1 901 241 241 ALA CA C 52.82 0.2 1 902 241 241 ALA CB C 18.92 0.2 1 903 241 241 ALA N N 124.229 0.2 1 904 242 242 GLY H H 8.3 0.02 1 905 242 242 GLY C C 170.93 0.2 1 906 242 242 GLY CA C 45.27 0.2 1 907 242 242 GLY N N 108.033 0.2 1 908 243 243 PHE H H 7.89 0.02 1 909 243 243 PHE C C 172.43 0.2 1 910 243 243 PHE CA C 57.75 0.2 1 911 243 243 PHE CB C 39.54 0.2 1 912 243 243 PHE N N 119.596 0.2 1 913 244 244 GLU H H 8.189 0.02 1 914 244 244 GLU C C 171.23 0.2 1 915 244 244 GLU CA C 54.13 0.2 1 916 244 244 GLU N N 124.245 0.2 1 917 245 245 PRO C C 174.13 0.2 1 918 245 245 PRO CA C 63.26 0.2 1 919 245 245 PRO CB C 31.57 0.2 1 920 246 246 GLU H H 8.401 0.02 1 921 246 246 GLU C C 173.63 0.2 1 922 246 246 GLU CA C 56.82 0.2 1 923 246 246 GLU CB C 29.74 0.2 1 924 246 246 GLU N N 120.156 0.2 1 925 247 247 MET H H 8.243 0.02 1 926 247 247 MET C C 172.23 0.2 1 927 247 247 MET CA C 55.38 0.2 1 928 247 247 MET CB C 32.43 0.2 1 929 247 247 MET N N 121.869 0.2 1 930 248 248 LEU H H 7.754 0.02 1 931 248 248 LEU C C 179.63 0.2 1 932 248 248 LEU CA C 56.82 0.2 1 933 248 248 LEU N N 129.251 0.2 1 stop_ save_