data_50387 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N backbone chemical shift assignments of the macrodomain of SARS-CoV-2 non-structural protein 3b ; _BMRB_accession_number 50387 _BMRB_flat_file_name bmr50387.str _Entry_type original _Submission_date 2020-07-13 _Accession_date 2020-07-13 _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 Schwalbe Harald . . 2 Sreeramulu Sridhar . . 3 Banci Lucia . . 4 Cantini Francesca . . 5 Richter Christian . . 6 Lohr Frank . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 166 "13C chemical shifts" 502 "15N chemical shifts" 166 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-12-23 update BMRB 'update entry citation' 2020-08-19 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 50388 'macrodomain of SARS-CoV-2 non-structural protein 3b bound to ADPr' stop_ _Original_release_date 2020-07-13 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; 1H, 13C, and 15N backbone chemical shift assignments of the apo and the ADP-ribose bound forms of the macrodomain of SARS-CoV-2 non-structural protein 3b ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32803496 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cantini Francesca . . 2 Banco Lucia . . 3 Altincekic Nadide . . 4 Bains Jasleen K. . 5 Dhamotharan Karthikeyan . . 6 Fuks Christin . . 7 Gande Santosh L. . 8 Hargittay Bruno . . 9 Hutchison Marie T. . 10 Korn Sophie M. . 11 Kubatova Nina . . 12 Kutz Felicitas . . 13 Meiser Nathalie . . 14 Linhardt Verena . . 15 Pyper Dennis J. . 16 Furtig Boris . . 17 Hengesbach Martin . . 18 Lohr Frank . . 19 Qureshi Nusrat S. . 20 Richter Christian . . 21 Saxena Krishna . . 22 Schlundt Andreas . . 23 Schwalbe Harald . . 24 Sreeramulu Sridhar . . 25 Tants Jan-Niklas . . 26 Wacker Anna . . 27 Weigand Julia E. . 28 Wohnert Jens . . 29 Tsika Aikaterini C. . 30 Fourkiotis Nikolaos K. . 31 Spyroulias Georgios A. . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_volume 14 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 339 _Page_last 346 _Year 2020 _Details . loop_ _Keyword COVID19-NMR Macrodomain 'Non-structural protein' 'Protein drugability' SARS-CoV-2 'Solution NMR-spectroscopy' stop_ save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name Nsp3b _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Nsp3b $entity_1 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_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 173 _Mol_residue_sequence ; GHMVNSFSGYLKLTDNVYIK NADIVEEAKKVKPTVVVNAA NVYLKHGGGVAGALNKATNN AMQVESDDYIATNGPLKVGG SCVLSGHNLAKHCLHVVGPN VNKGEDIQLLKSAYENFNQH EVLLAPLLSAGIFGADPIHS LRVCVDTVRTNVYLAVFDKN LYDKLVSSFLEMK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 GLY 2 -1 HIS 3 0 MET 4 1 VAL 5 2 ASN 6 3 SER 7 4 PHE 8 5 SER 9 6 GLY 10 7 TYR 11 8 LEU 12 9 LYS 13 10 LEU 14 11 THR 15 12 ASP 16 13 ASN 17 14 VAL 18 15 TYR 19 16 ILE 20 17 LYS 21 18 ASN 22 19 ALA 23 20 ASP 24 21 ILE 25 22 VAL 26 23 GLU 27 24 GLU 28 25 ALA 29 26 LYS 30 27 LYS 31 28 VAL 32 29 LYS 33 30 PRO 34 31 THR 35 32 VAL 36 33 VAL 37 34 VAL 38 35 ASN 39 36 ALA 40 37 ALA 41 38 ASN 42 39 VAL 43 40 TYR 44 41 LEU 45 42 LYS 46 43 HIS 47 44 GLY 48 45 GLY 49 46 GLY 50 47 VAL 51 48 ALA 52 49 GLY 53 50 ALA 54 51 LEU 55 52 ASN 56 53 LYS 57 54 ALA 58 55 THR 59 56 ASN 60 57 ASN 61 58 ALA 62 59 MET 63 60 GLN 64 61 VAL 65 62 GLU 66 63 SER 67 64 ASP 68 65 ASP 69 66 TYR 70 67 ILE 71 68 ALA 72 69 THR 73 70 ASN 74 71 GLY 75 72 PRO 76 73 LEU 77 74 LYS 78 75 VAL 79 76 GLY 80 77 GLY 81 78 SER 82 79 CYS 83 80 VAL 84 81 LEU 85 82 SER 86 83 GLY 87 84 HIS 88 85 ASN 89 86 LEU 90 87 ALA 91 88 LYS 92 89 HIS 93 90 CYS 94 91 LEU 95 92 HIS 96 93 VAL 97 94 VAL 98 95 GLY 99 96 PRO 100 97 ASN 101 98 VAL 102 99 ASN 103 100 LYS 104 101 GLY 105 102 GLU 106 103 ASP 107 104 ILE 108 105 GLN 109 106 LEU 110 107 LEU 111 108 LYS 112 109 SER 113 110 ALA 114 111 TYR 115 112 GLU 116 113 ASN 117 114 PHE 118 115 ASN 119 116 GLN 120 117 HIS 121 118 GLU 122 119 VAL 123 120 LEU 124 121 LEU 125 122 ALA 126 123 PRO 127 124 LEU 128 125 LEU 129 126 SER 130 127 ALA 131 128 GLY 132 129 ILE 133 130 PHE 134 131 GLY 135 132 ALA 136 133 ASP 137 134 PRO 138 135 ILE 139 136 HIS 140 137 SER 141 138 LEU 142 139 ARG 143 140 VAL 144 141 CYS 145 142 VAL 146 143 ASP 147 144 THR 148 145 VAL 149 146 ARG 150 147 THR 151 148 ASN 152 149 VAL 153 150 TYR 154 151 LEU 155 152 ALA 156 153 VAL 157 154 PHE 158 155 ASP 159 156 LYS 160 157 ASN 161 158 LEU 162 159 TYR 163 160 ASP 164 161 LYS 165 162 LEU 166 163 VAL 167 164 SER 168 165 SER 169 166 PHE 170 167 LEU 171 168 GLU 172 169 MET 173 170 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 GB MN908947.3 . . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source_1 _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $entity_1 SARS-CoV-2 2697049 Viruses . Betacoronavirus HCoV-SARS SARS-CoV-2 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_1 _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $entity_1 'recombinant technology' . Escherichia coli . plasmid pET28a(+) 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 $entity_1 650 uM '[U-13C; U-15N]' Bis-Tris 25 mM 'natural abundance' NaCl 150 mM 'natural abundance' TCEP 3 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name LOGS _Version 2.2 loop_ _Task collection stop_ _Details . save_ save_software_2 _Saveframe_category software _Name CARA _Version . loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_software_3 _Saveframe_category software _Name TOPSPIN _Version 4.0.6 loop_ _Task 'acquisition and processing' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'Bruker Avance neo 1200 MHz' _Field_strength 1200 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_HSQC_HN_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D HSQC HN' _Sample_label $sample_1 save_ save_3D_best-TROSY_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D best-TROSY HNCACB' _Sample_label $sample_1 save_ save_3D_best-TROSY_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D best-TROSY HNCO' _Sample_label $sample_1 save_ save_2D_best-TROSY_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D best-TROSY HSQC' _Sample_label $sample_1 save_ save_3D_best-TROSY_HN(CO)CACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D best-TROSY HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_best-TROSY_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D best-TROSY HN(CA)CO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 178 . mM pH 6.5 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $software_1 $software_2 stop_ loop_ _Experiment_label '2D HSQC HN' '3D best-TROSY HNCACB' '3D best-TROSY HNCO' '2D best-TROSY HSQC' '3D best-TROSY HN(CO)CACB' '3D best-TROSY HN(CA)CO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name Nsp3b _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 -1 2 HIS C C 175.04 0.300 1 2 -1 2 HIS CA C 56.06 0.300 1 3 -1 2 HIS CB C 30.96 0.300 1 4 0 3 MET H H 8.42 0.020 1 5 0 3 MET C C 175.53 0.300 1 6 0 3 MET CA C 55.21 0.300 1 7 0 3 MET CB C 32.73 0.300 1 8 0 3 MET N N 122.30 0.300 1 9 1 4 VAL H H 7.95 0.020 1 10 1 4 VAL C C 175.49 0.300 1 11 1 4 VAL CA C 61.02 0.300 1 12 1 4 VAL CB C 33.17 0.300 1 13 1 4 VAL N N 119.25 0.300 1 14 2 5 ASN H H 8.24 0.020 1 15 2 5 ASN C C 174.73 0.300 1 16 2 5 ASN CA C 53.58 0.300 1 17 2 5 ASN CB C 37.54 0.300 1 18 2 5 ASN N N 119.52 0.300 1 19 3 6 SER H H 8.30 0.020 1 20 3 6 SER C C 173.87 0.300 1 21 3 6 SER CA C 56.69 0.300 1 22 3 6 SER CB C 62.36 0.300 1 23 3 6 SER N N 115.59 0.300 1 24 4 7 PHE H H 7.47 0.020 1 25 4 7 PHE C C 176.41 0.300 1 26 4 7 PHE CA C 58.39 0.300 1 27 4 7 PHE CB C 39.32 0.300 1 28 4 7 PHE N N 122.16 0.300 1 29 5 8 SER H H 9.50 0.020 1 30 5 8 SER C C 174.06 0.300 1 31 5 8 SER CA C 57.48 0.300 1 32 5 8 SER CB C 65.13 0.300 1 33 5 8 SER N N 119.26 0.300 1 34 6 9 GLY H H 9.02 0.020 1 35 6 9 GLY C C 174.95 0.300 1 36 6 9 GLY CA C 46.32 0.300 1 37 6 9 GLY N N 111.75 0.300 1 38 7 10 TYR H H 8.50 0.020 1 39 7 10 TYR C C 175.44 0.300 1 40 7 10 TYR CA C 58.54 0.300 1 41 7 10 TYR CB C 39.54 0.300 1 42 7 10 TYR N N 118.49 0.300 1 43 8 11 LEU H H 9.64 0.020 1 44 8 11 LEU C C 175.72 0.300 1 45 8 11 LEU CA C 53.94 0.300 1 46 8 11 LEU CB C 43.52 0.300 1 47 8 11 LEU N N 125.78 0.300 1 48 9 12 LYS H H 8.72 0.020 1 49 9 12 LYS C C 175.38 0.300 1 50 9 12 LYS CA C 57.19 0.300 1 51 9 12 LYS CB C 33.02 0.300 1 52 9 12 LYS N N 128.55 0.300 1 53 10 13 LEU H H 8.68 0.020 1 54 10 13 LEU C C 177.04 0.300 1 55 10 13 LEU CA C 55.99 0.300 1 56 10 13 LEU CB C 42.09 0.300 1 57 10 13 LEU N N 128.29 0.300 1 58 11 14 THR H H 7.68 0.020 1 59 11 14 THR C C 172.94 0.300 1 60 11 14 THR CA C 58.41 0.300 1 61 11 14 THR CB C 71.36 0.300 1 62 11 14 THR N N 109.14 0.300 1 63 12 15 ASP H H 8.30 0.020 1 64 12 15 ASP C C 175.89 0.300 1 65 12 15 ASP CA C 57.32 0.300 1 66 12 15 ASP CB C 40.57 0.300 1 67 12 15 ASP N N 113.28 0.300 1 68 13 16 ASN H H 7.82 0.020 1 69 13 16 ASN C C 170.84 0.300 1 70 13 16 ASN CA C 53.05 0.300 1 71 13 16 ASN CB C 40.03 0.300 1 72 13 16 ASN N N 111.22 0.300 1 73 14 17 VAL H H 6.72 0.020 1 74 14 17 VAL C C 172.47 0.300 1 75 14 17 VAL CA C 61.97 0.300 1 76 14 17 VAL CB C 32.02 0.300 1 77 14 17 VAL N N 119.26 0.300 1 78 15 18 TYR H H 8.70 0.020 1 79 15 18 TYR C C 174.91 0.300 1 80 15 18 TYR CA C 55.45 0.300 1 81 15 18 TYR CB C 42.06 0.300 1 82 15 18 TYR N N 127.44 0.300 1 83 16 19 ILE H H 9.75 0.020 1 84 16 19 ILE C C 172.28 0.300 1 85 16 19 ILE CA C 59.87 0.300 1 86 16 19 ILE CB C 44.07 0.300 1 87 16 19 ILE N N 120.38 0.300 1 88 17 20 LYS H H 8.94 0.020 1 89 17 20 LYS C C 173.34 0.300 1 90 17 20 LYS CA C 55.56 0.300 1 91 17 20 LYS CB C 38.73 0.300 1 92 17 20 LYS N N 127.50 0.300 1 93 18 21 ASN H H 8.33 0.020 1 94 18 21 ASN C C 172.23 0.300 1 95 18 21 ASN CA C 49.97 0.300 1 96 18 21 ASN CB C 36.50 0.300 1 97 18 21 ASN N N 125.19 0.300 1 98 19 22 ALA H H 7.63 0.020 1 99 19 22 ALA C C 174.04 0.300 1 100 19 22 ALA CA C 50.83 0.300 1 101 19 22 ALA CB C 22.30 0.300 1 102 19 22 ALA N N 127.68 0.300 1 103 20 23 ASP H H 8.78 0.020 1 104 20 23 ASP C C 176.84 0.300 1 105 20 23 ASP CA C 52.58 0.300 1 106 20 23 ASP CB C 42.77 0.300 1 107 20 23 ASP N N 119.86 0.300 1 108 21 24 ILE H H 8.96 0.020 1 109 21 24 ILE C C 174.48 0.300 1 110 21 24 ILE CA C 65.56 0.300 1 111 21 24 ILE CB C 38.27 0.300 1 112 21 24 ILE N N 128.01 0.300 1 113 22 25 VAL H H 7.86 0.020 1 114 22 25 VAL C C 177.41 0.300 1 115 22 25 VAL CA C 67.01 0.300 1 116 22 25 VAL CB C 30.72 0.300 1 117 22 25 VAL N N 122.21 0.300 1 118 23 26 GLU H H 7.22 0.020 1 119 23 26 GLU C C 180.14 0.300 1 120 23 26 GLU CA C 58.53 0.300 1 121 23 26 GLU CB C 29.21 0.300 1 122 23 26 GLU N N 118.10 0.300 1 123 24 27 GLU H H 8.57 0.020 1 124 24 27 GLU C C 177.52 0.300 1 125 24 27 GLU CA C 58.53 0.300 1 126 24 27 GLU CB C 30.52 0.300 1 127 24 27 GLU N N 118.19 0.300 1 128 25 28 ALA H H 8.51 0.020 1 129 25 28 ALA C C 179.46 0.300 1 130 25 28 ALA CA C 55.76 0.300 1 131 25 28 ALA CB C 16.61 0.300 1 132 25 28 ALA N N 122.46 0.300 1 133 26 29 LYS H H 7.89 0.020 1 134 26 29 LYS C C 178.11 0.300 1 135 26 29 LYS CA C 59.68 0.300 1 136 26 29 LYS CB C 32.65 0.300 1 137 26 29 LYS N N 114.46 0.300 1 138 27 30 LYS H H 7.48 0.020 1 139 27 30 LYS C C 177.91 0.300 1 140 27 30 LYS CA C 58.25 0.300 1 141 27 30 LYS CB C 33.60 0.300 1 142 27 30 LYS N N 116.64 0.300 1 143 28 31 VAL H H 8.57 0.020 1 144 28 31 VAL C C 175.90 0.300 1 145 28 31 VAL CA C 63.50 0.300 1 146 28 31 VAL CB C 33.05 0.300 1 147 28 31 VAL N N 117.74 0.300 1 148 29 32 LYS H H 8.23 0.020 1 149 29 32 LYS C C 173.68 0.300 1 150 29 32 LYS CA C 55.66 0.300 1 151 29 32 LYS CB C 29.36 0.300 1 152 29 32 LYS N N 114.09 0.300 1 153 30 33 PRO C C 176.69 0.300 1 154 30 33 PRO CA C 61.79 0.300 1 155 30 33 PRO CB C 31.96 0.300 1 156 31 34 THR H H 8.57 0.020 1 157 31 34 THR C C 174.93 0.300 1 158 31 34 THR CA C 66.12 0.300 1 159 31 34 THR CB C 68.74 0.300 1 160 31 34 THR N N 115.54 0.300 1 161 32 35 VAL H H 8.46 0.020 1 162 32 35 VAL C C 174.01 0.300 1 163 32 35 VAL CA C 61.18 0.300 1 164 32 35 VAL CB C 35.68 0.300 1 165 32 35 VAL N N 118.08 0.300 1 166 33 36 VAL H H 7.94 0.020 1 167 33 36 VAL C C 172.21 0.300 1 168 33 36 VAL CA C 57.37 0.300 1 169 33 36 VAL CB C 35.28 0.300 1 170 33 36 VAL N N 125.08 0.300 1 171 34 37 VAL H H 8.70 0.020 1 172 34 37 VAL C C 172.85 0.300 1 173 34 37 VAL CA C 60.64 0.300 1 174 34 37 VAL CB C 33.00 0.300 1 175 34 37 VAL N N 129.68 0.300 1 176 35 38 ASN H H 8.21 0.020 1 177 35 38 ASN C C 175.35 0.300 1 178 35 38 ASN CA C 49.78 0.300 1 179 35 38 ASN CB C 41.80 0.300 1 180 35 38 ASN N N 118.29 0.300 1 181 36 39 ALA H H 6.39 0.020 1 182 36 39 ALA C C 174.32 0.300 1 183 36 39 ALA CA C 50.11 0.300 1 184 36 39 ALA CB C 17.84 0.300 1 185 36 39 ALA N N 131.59 0.300 1 186 37 40 ALA H H 7.70 0.020 1 187 37 40 ALA C C 176.46 0.300 1 188 37 40 ALA CA C 51.21 0.300 1 189 37 40 ALA CB C 22.36 0.300 1 190 37 40 ALA N N 126.06 0.300 1 191 38 41 ASN H H 7.48 0.020 1 192 38 41 ASN C C 177.73 0.300 1 193 38 41 ASN CA C 51.13 0.300 1 194 38 41 ASN CB C 42.01 0.300 1 195 38 41 ASN N N 112.73 0.300 1 196 39 42 VAL H H 8.54 0.020 1 197 39 42 VAL C C 175.29 0.300 1 198 39 42 VAL CA C 65.23 0.300 1 199 39 42 VAL CB C 30.99 0.300 1 200 39 42 VAL N N 110.02 0.300 1 201 40 43 TYR H H 6.97 0.020 1 202 40 43 TYR C C 173.01 0.300 1 203 40 43 TYR CA C 58.03 0.300 1 204 40 43 TYR CB C 38.41 0.300 1 205 40 43 TYR N N 113.31 0.300 1 206 41 44 LEU H H 8.12 0.020 1 207 41 44 LEU C C 173.58 0.300 1 208 41 44 LEU CA C 54.45 0.300 1 209 41 44 LEU CB C 40.00 0.300 1 210 41 44 LEU N N 114.24 0.300 1 211 42 45 LYS H H 7.92 0.020 1 212 42 45 LYS C C 176.86 0.300 1 213 42 45 LYS CA C 53.83 0.300 1 214 42 45 LYS CB C 31.53 0.300 1 215 42 45 LYS N N 115.09 0.300 1 216 43 46 HIS H H 9.21 0.020 1 217 43 46 HIS C C 174.69 0.300 1 218 43 46 HIS CA C 53.88 0.300 1 219 43 46 HIS CB C 28.40 0.300 1 220 43 46 HIS N N 130.21 0.300 1 221 44 47 GLY H H 7.96 0.020 1 222 44 47 GLY C C 174.36 0.300 1 223 44 47 GLY CA C 45.88 0.300 1 224 44 47 GLY N N 109.02 0.300 1 225 45 48 GLY H H 8.09 0.020 1 226 45 48 GLY C C 173.98 0.300 1 227 45 48 GLY CA C 44.13 0.300 1 228 45 48 GLY N N 108.20 0.300 1 229 46 49 GLY H H 8.79 0.020 1 230 46 49 GLY C C 175.09 0.300 1 231 46 49 GLY CA C 46.22 0.300 1 232 46 49 GLY N N 108.07 0.300 1 233 47 50 VAL H H 8.56 0.020 1 234 47 50 VAL C C 176.45 0.300 1 235 47 50 VAL CA C 65.72 0.300 1 236 47 50 VAL CB C 32.45 0.300 1 237 47 50 VAL N N 126.04 0.300 1 238 48 51 ALA H H 8.89 0.020 1 239 48 51 ALA C C 180.75 0.300 1 240 48 51 ALA CA C 55.28 0.300 1 241 48 51 ALA CB C 18.99 0.300 1 242 48 51 ALA N N 122.94 0.300 1 243 49 52 GLY H H 7.75 0.020 1 244 49 52 GLY C C 176.30 0.300 1 245 49 52 GLY CA C 46.50 0.300 1 246 49 52 GLY N N 104.04 0.300 1 247 50 53 ALA H H 7.65 0.020 1 248 50 53 ALA C C 181.28 0.300 1 249 50 53 ALA CA C 54.83 0.300 1 250 50 53 ALA CB C 18.13 0.300 1 251 50 53 ALA N N 125.73 0.300 1 252 51 54 LEU H H 8.96 0.020 1 253 51 54 LEU C C 178.46 0.300 1 254 51 54 LEU CA C 58.07 0.300 1 255 51 54 LEU CB C 41.33 0.300 1 256 51 54 LEU N N 120.66 0.300 1 257 52 55 ASN H H 8.57 0.020 1 258 52 55 ASN C C 181.17 0.300 1 259 52 55 ASN CA C 57.73 0.300 1 260 52 55 ASN CB C 39.85 0.300 1 261 52 55 ASN N N 114.52 0.300 1 262 53 56 LYS H H 8.74 0.020 1 263 53 56 LYS C C 180.12 0.300 1 264 53 56 LYS CA C 59.65 0.300 1 265 53 56 LYS CB C 31.99 0.300 1 266 53 56 LYS N N 123.53 0.300 1 267 54 57 ALA H H 7.81 0.020 1 268 54 57 ALA C C 178.63 0.300 1 269 54 57 ALA CA C 54.52 0.300 1 270 54 57 ALA CB C 19.29 0.300 1 271 54 57 ALA N N 122.33 0.300 1 272 55 58 THR H H 7.63 0.020 1 273 55 58 THR C C 175.99 0.300 1 274 55 58 THR CA C 61.06 0.300 1 275 55 58 THR CB C 70.81 0.300 1 276 55 58 THR N N 107.40 0.300 1 277 56 59 ASN H H 8.58 0.020 1 278 56 59 ASN C C 175.45 0.300 1 279 56 59 ASN CA C 54.48 0.300 1 280 56 59 ASN CB C 36.59 0.300 1 281 56 59 ASN N N 122.01 0.300 1 282 57 60 ASN H H 7.55 0.020 1 283 57 60 ASN C C 174.37 0.300 1 284 57 60 ASN CA C 54.66 0.300 1 285 57 60 ASN CB C 39.90 0.300 1 286 57 60 ASN N N 109.96 0.300 1 287 58 61 ALA H H 7.62 0.020 1 288 58 61 ALA C C 180.72 0.300 1 289 58 61 ALA CA C 54.89 0.300 1 290 58 61 ALA CB C 18.28 0.300 1 291 58 61 ALA N N 124.23 0.300 1 292 59 62 MET H H 8.16 0.020 1 293 59 62 MET C C 179.18 0.300 1 294 59 62 MET CA C 59.09 0.300 1 295 59 62 MET CB C 33.36 0.300 1 296 59 62 MET N N 116.24 0.300 1 297 60 63 GLN H H 8.14 0.020 1 298 60 63 GLN C C 176.98 0.300 1 299 60 63 GLN CA C 57.78 0.300 1 300 60 63 GLN CB C 29.85 0.300 1 301 60 63 GLN N N 124.98 0.300 1 302 61 64 VAL H H 7.81 0.020 1 303 61 64 VAL C C 178.82 0.300 1 304 61 64 VAL CA C 66.60 0.300 1 305 61 64 VAL CB C 31.91 0.300 1 306 61 64 VAL N N 120.83 0.300 1 307 62 65 GLU H H 7.89 0.020 1 308 62 65 GLU C C 180.10 0.300 1 309 62 65 GLU CA C 58.62 0.300 1 310 62 65 GLU CB C 30.55 0.300 1 311 62 65 GLU N N 120.22 0.300 1 312 63 66 SER H H 8.48 0.020 1 313 63 66 SER C C 174.24 0.300 1 314 63 66 SER CA C 61.94 0.300 1 315 63 66 SER CB C 62.95 0.300 1 316 63 66 SER N N 117.34 0.300 1 317 64 67 ASP H H 8.89 0.020 1 318 64 67 ASP C C 179.65 0.300 1 319 64 67 ASP CA C 57.08 0.300 1 320 64 67 ASP CB C 39.34 0.300 1 321 64 67 ASP N N 123.21 0.300 1 322 65 68 ASP H H 7.52 0.020 1 323 65 68 ASP C C 177.79 0.300 1 324 65 68 ASP CA C 57.28 0.300 1 325 65 68 ASP CB C 40.97 0.300 1 326 65 68 ASP N N 121.20 0.300 1 327 66 69 TYR H H 8.21 0.020 1 328 66 69 TYR C C 178.67 0.300 1 329 66 69 TYR CA C 62.42 0.300 1 330 66 69 TYR CB C 37.87 0.300 1 331 66 69 TYR N N 122.40 0.300 1 332 67 70 ILE H H 8.84 0.020 1 333 67 70 ILE C C 179.70 0.300 1 334 67 70 ILE CA C 60.69 0.300 1 335 67 70 ILE CB C 35.45 0.300 1 336 67 70 ILE N N 122.42 0.300 1 337 68 71 ALA H H 8.20 0.020 1 338 68 71 ALA C C 179.30 0.300 1 339 68 71 ALA CA C 55.17 0.300 1 340 68 71 ALA CB C 17.94 0.300 1 341 68 71 ALA N N 123.41 0.300 1 342 69 72 THR H H 7.48 0.020 1 343 69 72 THR C C 175.14 0.300 1 344 69 72 THR CA C 64.64 0.300 1 345 69 72 THR CB C 69.64 0.300 1 346 69 72 THR N N 110.11 0.300 1 347 70 73 ASN H H 8.36 0.020 1 348 70 73 ASN C C 175.74 0.300 1 349 70 73 ASN CA C 54.88 0.300 1 350 70 73 ASN CB C 41.03 0.300 1 351 70 73 ASN N N 117.07 0.300 1 352 71 74 GLY H H 8.35 0.020 1 353 71 74 GLY C C 169.32 0.300 1 354 71 74 GLY CA C 44.45 0.300 1 355 71 74 GLY N N 110.34 0.300 1 356 72 75 PRO C C 177.79 0.300 1 357 72 75 PRO CA C 62.22 0.300 1 358 72 75 PRO CB C 31.81 0.300 1 359 73 76 LEU H H 8.38 0.020 1 360 73 76 LEU C C 174.78 0.300 1 361 73 76 LEU CA C 54.99 0.300 1 362 73 76 LEU CB C 44.10 0.300 1 363 73 76 LEU N N 120.80 0.300 1 364 74 77 LYS H H 7.71 0.020 1 365 74 77 LYS C C 177.21 0.300 1 366 74 77 LYS CA C 54.05 0.300 1 367 74 77 LYS CB C 33.91 0.300 1 368 74 77 LYS N N 115.30 0.300 1 369 75 78 VAL H H 8.46 0.020 1 370 75 78 VAL C C 177.17 0.300 1 371 75 78 VAL CA C 65.56 0.300 1 372 75 78 VAL CB C 29.79 0.300 1 373 75 78 VAL N N 122.05 0.300 1 374 76 79 GLY H H 8.88 0.020 1 375 76 79 GLY C C 173.02 0.300 1 376 76 79 GLY CA C 44.88 0.300 1 377 76 79 GLY N N 117.81 0.300 1 378 77 80 GLY H H 8.55 0.020 1 379 77 80 GLY C C 171.52 0.300 1 380 77 80 GLY CA C 43.53 0.300 1 381 77 80 GLY N N 108.52 0.300 1 382 78 81 SER H H 8.03 0.020 1 383 78 81 SER C C 173.52 0.300 1 384 78 81 SER CA C 57.10 0.300 1 385 78 81 SER CB C 68.74 0.300 1 386 78 81 SER N N 106.98 0.300 1 387 79 82 CYS H H 8.58 0.020 1 388 79 82 CYS C C 171.49 0.300 1 389 79 82 CYS CA C 55.78 0.300 1 390 79 82 CYS CB C 30.64 0.300 1 391 79 82 CYS N N 111.96 0.300 1 392 80 83 VAL H H 8.50 0.020 1 393 80 83 VAL C C 175.24 0.300 1 394 80 83 VAL CA C 61.38 0.300 1 395 80 83 VAL CB C 32.28 0.300 1 396 80 83 VAL N N 121.82 0.300 1 397 81 84 LEU H H 8.98 0.020 1 398 81 84 LEU C C 176.57 0.300 1 399 81 84 LEU CA C 52.82 0.300 1 400 81 84 LEU CB C 44.79 0.300 1 401 81 84 LEU N N 130.06 0.300 1 402 82 85 SER H H 10.11 0.020 1 403 82 85 SER C C 175.15 0.300 1 404 82 85 SER CA C 59.67 0.300 1 405 82 85 SER CB C 62.97 0.300 1 406 82 85 SER N N 118.69 0.300 1 407 83 86 GLY H H 7.30 0.020 1 408 83 86 GLY C C 173.58 0.300 1 409 83 86 GLY CA C 45.27 0.300 1 410 83 86 GLY N N 110.89 0.300 1 411 84 87 HIS H H 8.57 0.020 1 412 84 87 HIS C C 174.00 0.300 1 413 84 87 HIS CA C 57.66 0.300 1 414 84 87 HIS CB C 28.55 0.300 1 415 84 87 HIS N N 117.55 0.300 1 416 85 88 ASN H H 9.38 0.020 1 417 85 88 ASN C C 174.47 0.300 1 418 85 88 ASN CA C 53.60 0.300 1 419 85 88 ASN CB C 35.99 0.300 1 420 85 88 ASN N N 116.21 0.300 1 421 86 89 LEU H H 8.38 0.020 1 422 86 89 LEU C C 174.16 0.300 1 423 86 89 LEU CA C 55.69 0.300 1 424 86 89 LEU CB C 43.94 0.300 1 425 86 89 LEU N N 119.90 0.300 1 426 87 90 ALA H H 6.96 0.020 1 427 87 90 ALA C C 176.18 0.300 1 428 87 90 ALA CA C 50.45 0.300 1 429 87 90 ALA CB C 23.39 0.300 1 430 87 90 ALA N N 115.34 0.300 1 431 88 91 LYS H H 7.45 0.020 1 432 88 91 LYS C C 178.09 0.300 1 433 88 91 LYS CA C 60.21 0.300 1 434 88 91 LYS CB C 31.44 0.300 1 435 88 91 LYS N N 119.80 0.300 1 436 89 92 HIS H H 8.43 0.020 1 437 89 92 HIS C C 173.25 0.300 1 438 89 92 HIS CA C 54.06 0.300 1 439 89 92 HIS CB C 33.70 0.300 1 440 89 92 HIS N N 115.92 0.300 1 441 90 93 CYS H H 8.54 0.020 1 442 90 93 CYS C C 172.90 0.300 1 443 90 93 CYS CA C 55.40 0.300 1 444 90 93 CYS CB C 29.35 0.300 1 445 90 93 CYS N N 120.69 0.300 1 446 91 94 LEU H H 8.54 0.020 1 447 91 94 LEU C C 174.13 0.300 1 448 91 94 LEU CA C 52.58 0.300 1 449 91 94 LEU CB C 43.27 0.300 1 450 91 94 LEU N N 130.86 0.300 1 451 92 95 HIS H H 9.04 0.020 1 452 92 95 HIS C C 174.65 0.300 1 453 92 95 HIS CA C 56.40 0.300 1 454 92 95 HIS CB C 31.74 0.300 1 455 92 95 HIS N N 130.30 0.300 1 456 93 96 VAL H H 8.37 0.020 1 457 93 96 VAL C C 174.52 0.300 1 458 93 96 VAL CA C 60.44 0.300 1 459 93 96 VAL CB C 33.91 0.300 1 460 93 96 VAL N N 121.25 0.300 1 461 94 97 VAL H H 8.37 0.020 1 462 94 97 VAL C C 176.61 0.300 1 463 94 97 VAL CA C 60.45 0.300 1 464 94 97 VAL CB C 30.84 0.300 1 465 94 97 VAL N N 128.18 0.300 1 466 95 98 GLY H H 9.07 0.020 1 467 95 98 GLY CA C 42.38 0.300 1 468 95 98 GLY N N 114.76 0.300 1 469 96 99 PRO C C 175.90 0.300 1 470 96 99 PRO CA C 62.05 0.300 1 471 96 99 PRO CB C 32.17 0.300 1 472 97 100 ASN H H 10.23 0.020 1 473 97 100 ASN C C 176.65 0.300 1 474 97 100 ASN CA C 51.21 0.300 1 475 97 100 ASN CB C 36.86 0.300 1 476 97 100 ASN N N 121.58 0.300 1 477 98 101 VAL H H 8.36 0.020 1 478 98 101 VAL C C 179.65 0.300 1 479 98 101 VAL CA C 64.22 0.300 1 480 98 101 VAL CB C 31.45 0.300 1 481 98 101 VAL N N 124.05 0.300 1 482 99 102 ASN H H 8.06 0.020 1 483 99 102 ASN C C 176.68 0.300 1 484 99 102 ASN CA C 55.45 0.300 1 485 99 102 ASN CB C 37.90 0.300 1 486 99 102 ASN N N 120.36 0.300 1 487 100 103 LYS H H 7.22 0.020 1 488 100 103 LYS C C 176.59 0.300 1 489 100 103 LYS CA C 54.85 0.300 1 490 100 103 LYS CB C 32.47 0.300 1 491 100 103 LYS N N 117.85 0.300 1 492 101 104 GLY H H 7.72 0.020 1 493 101 104 GLY C C 174.70 0.300 1 494 101 104 GLY CA C 45.68 0.300 1 495 101 104 GLY N N 106.76 0.300 1 496 102 105 GLU H H 7.43 0.020 1 497 102 105 GLU C C 175.97 0.300 1 498 102 105 GLU CA C 55.78 0.300 1 499 102 105 GLU CB C 29.46 0.300 1 500 102 105 GLU N N 119.30 0.300 1 501 103 106 ASP H H 8.26 0.020 1 502 103 106 ASP C C 177.58 0.300 1 503 103 106 ASP CA C 54.51 0.300 1 504 103 106 ASP CB C 41.69 0.300 1 505 103 106 ASP N N 120.45 0.300 1 506 104 107 ILE H H 8.66 0.020 1 507 104 107 ILE C C 177.98 0.300 1 508 104 107 ILE CA C 61.18 0.300 1 509 104 107 ILE CB C 38.44 0.300 1 510 104 107 ILE N N 128.24 0.300 1 511 105 108 GLN H H 9.18 0.020 1 512 105 108 GLN C C 178.81 0.300 1 513 105 108 GLN CA C 58.48 0.300 1 514 105 108 GLN CB C 28.00 0.300 1 515 105 108 GLN N N 124.36 0.300 1 516 106 109 LEU H H 8.08 0.020 1 517 106 109 LEU C C 177.48 0.300 1 518 106 109 LEU CA C 55.98 0.300 1 519 106 109 LEU CB C 41.37 0.300 1 520 106 109 LEU N N 117.61 0.300 1 521 107 110 LEU H H 8.27 0.020 1 522 107 110 LEU C C 177.57 0.300 1 523 107 110 LEU CA C 57.24 0.300 1 524 107 110 LEU CB C 42.61 0.300 1 525 107 110 LEU N N 122.40 0.300 1 526 108 111 LYS H H 7.51 0.020 1 527 108 111 LYS C C 177.53 0.300 1 528 108 111 LYS CA C 60.40 0.300 1 529 108 111 LYS CB C 31.83 0.300 1 530 108 111 LYS N N 118.75 0.300 1 531 109 112 SER H H 7.10 0.020 1 532 109 112 SER C C 175.85 0.300 1 533 109 112 SER CA C 61.85 0.300 1 534 109 112 SER CB C 62.38 0.300 1 535 109 112 SER N N 112.84 0.300 1 536 110 113 ALA H H 8.04 0.020 1 537 110 113 ALA C C 179.98 0.300 1 538 110 113 ALA CA C 54.67 0.300 1 539 110 113 ALA CB C 18.04 0.300 1 540 110 113 ALA N N 121.77 0.300 1 541 111 114 TYR H H 7.94 0.020 1 542 111 114 TYR C C 178.28 0.300 1 543 111 114 TYR CA C 62.09 0.300 1 544 111 114 TYR CB C 37.63 0.300 1 545 111 114 TYR N N 115.72 0.300 1 546 112 115 GLU H H 8.29 0.020 1 547 112 115 GLU C C 179.59 0.300 1 548 112 115 GLU CA C 59.30 0.300 1 549 112 115 GLU CB C 28.76 0.300 1 550 112 115 GLU N N 121.07 0.300 1 551 113 116 ASN H H 7.29 0.020 1 552 113 116 ASN C C 176.58 0.300 1 553 113 116 ASN CA C 56.61 0.300 1 554 113 116 ASN CB C 39.65 0.300 1 555 113 116 ASN N N 113.49 0.300 1 556 114 117 PHE H H 8.76 0.020 1 557 114 117 PHE C C 177.19 0.300 1 558 114 117 PHE CA C 58.25 0.300 1 559 114 117 PHE CB C 37.57 0.300 1 560 114 117 PHE N N 117.89 0.300 1 561 115 118 ASN H H 7.53 0.020 1 562 115 118 ASN C C 175.29 0.300 1 563 115 118 ASN CA C 54.60 0.300 1 564 115 118 ASN CB C 37.54 0.300 1 565 115 118 ASN N N 112.28 0.300 1 566 116 119 GLN H H 6.96 0.020 1 567 116 119 GLN C C 173.47 0.300 1 568 116 119 GLN CA C 55.67 0.300 1 569 116 119 GLN CB C 28.93 0.300 1 570 116 119 GLN N N 116.99 0.300 1 571 117 120 HIS H H 7.71 0.020 1 572 117 120 HIS C C 173.33 0.300 1 573 117 120 HIS CA C 54.70 0.300 1 574 117 120 HIS CB C 33.69 0.300 1 575 117 120 HIS N N 119.23 0.300 1 576 118 121 GLU H H 8.69 0.020 1 577 118 121 GLU C C 176.89 0.300 1 578 118 121 GLU CA C 60.00 0.300 1 579 118 121 GLU CB C 30.58 0.300 1 580 118 121 GLU N N 120.38 0.300 1 581 119 122 VAL H H 7.84 0.020 1 582 119 122 VAL C C 175.62 0.300 1 583 119 122 VAL CA C 60.39 0.300 1 584 119 122 VAL CB C 34.79 0.300 1 585 119 122 VAL N N 115.09 0.300 1 586 120 123 LEU H H 8.76 0.020 1 587 120 123 LEU C C 173.49 0.300 1 588 120 123 LEU CA C 55.09 0.300 1 589 120 123 LEU CB C 45.64 0.300 1 590 120 123 LEU N N 126.50 0.300 1 591 121 124 LEU H H 7.84 0.020 1 592 121 124 LEU C C 174.48 0.300 1 593 121 124 LEU CA C 53.64 0.300 1 594 121 124 LEU CB C 43.96 0.300 1 595 121 124 LEU N N 123.59 0.300 1 596 122 125 ALA H H 9.63 0.020 1 597 122 125 ALA C C 172.81 0.300 1 598 122 125 ALA CA C 49.75 0.300 1 599 122 125 ALA CB C 22.80 0.300 1 600 122 125 ALA N N 129.35 0.300 1 601 123 126 PRO C C 174.47 0.300 1 602 123 126 PRO CA C 60.65 0.300 1 603 123 126 PRO CB C 31.87 0.300 1 604 124 127 LEU H H 8.27 0.020 1 605 124 127 LEU C C 178.09 0.300 1 606 124 127 LEU CA C 54.34 0.300 1 607 124 127 LEU CB C 42.68 0.300 1 608 124 127 LEU N N 113.97 0.300 1 609 125 128 LEU H H 7.43 0.020 1 610 125 128 LEU C C 177.42 0.300 1 611 125 128 LEU CA C 54.61 0.300 1 612 125 128 LEU CB C 42.66 0.300 1 613 125 128 LEU N N 122.35 0.300 1 614 126 129 SER H H 9.53 0.020 1 615 126 129 SER C C 170.67 0.300 1 616 126 129 SER CA C 60.58 0.300 1 617 126 129 SER CB C 62.88 0.300 1 618 126 129 SER N N 112.51 0.300 1 619 127 130 ALA H H 7.06 0.020 1 620 127 130 ALA C C 178.11 0.300 1 621 127 130 ALA CA C 50.77 0.300 1 622 127 130 ALA CB C 19.19 0.300 1 623 127 130 ALA N N 120.43 0.300 1 624 128 131 GLY H H 9.05 0.020 1 625 128 131 GLY C C 177.81 0.300 1 626 128 131 GLY CA C 46.50 0.300 1 627 128 131 GLY N N 110.60 0.300 1 628 129 132 ILE H H 8.97 0.020 1 629 129 132 ILE C C 176.55 0.300 1 630 129 132 ILE CA C 63.42 0.300 1 631 129 132 ILE CB C 38.10 0.300 1 632 129 132 ILE N N 125.50 0.300 1 633 130 133 PHE H H 7.91 0.020 1 634 130 133 PHE C C 178.20 0.300 1 635 130 133 PHE CA C 58.47 0.300 1 636 130 133 PHE CB C 38.68 0.300 1 637 130 133 PHE N N 121.21 0.300 1 638 131 134 GLY H H 7.62 0.020 1 639 131 134 GLY C C 174.19 0.300 1 640 131 134 GLY CA C 47.58 0.300 1 641 131 134 GLY N N 102.92 0.300 1 642 132 135 ALA H H 8.96 0.020 1 643 132 135 ALA C C 176.75 0.300 1 644 132 135 ALA CA C 51.30 0.300 1 645 132 135 ALA CB C 19.17 0.300 1 646 132 135 ALA N N 122.55 0.300 1 647 133 136 ASP H H 8.75 0.020 1 648 133 136 ASP C C 176.15 0.300 1 649 133 136 ASP CA C 51.59 0.300 1 650 133 136 ASP CB C 42.08 0.300 1 651 133 136 ASP N N 122.97 0.300 1 652 134 137 PRO C C 177.45 0.300 1 653 134 137 PRO CA C 64.83 0.300 1 654 134 137 PRO CB C 32.72 0.300 1 655 135 138 ILE H H 7.94 0.020 1 656 135 138 ILE C C 178.15 0.300 1 657 135 138 ILE CA C 64.47 0.300 1 658 135 138 ILE CB C 36.44 0.300 1 659 135 138 ILE N N 117.93 0.300 1 660 136 139 HIS H H 7.48 0.020 1 661 136 139 HIS C C 176.65 0.300 1 662 136 139 HIS CA C 59.37 0.300 1 663 136 139 HIS CB C 30.64 0.300 1 664 136 139 HIS N N 120.07 0.300 1 665 137 140 SER H H 8.13 0.020 1 666 137 140 SER C C 176.65 0.300 1 667 137 140 SER CA C 60.92 0.300 1 668 137 140 SER CB C 63.28 0.300 1 669 137 140 SER N N 109.72 0.300 1 670 138 141 LEU H H 8.30 0.020 1 671 138 141 LEU C C 177.22 0.300 1 672 138 141 LEU CA C 57.33 0.300 1 673 138 141 LEU CB C 40.94 0.300 1 674 138 141 LEU N N 118.59 0.300 1 675 139 142 ARG H H 8.04 0.020 1 676 139 142 ARG C C 178.07 0.300 1 677 139 142 ARG CA C 59.10 0.300 1 678 139 142 ARG CB C 29.27 0.300 1 679 139 142 ARG N N 119.92 0.300 1 680 140 143 VAL H H 8.30 0.020 1 681 140 143 VAL C C 178.63 0.300 1 682 140 143 VAL CA C 66.07 0.300 1 683 140 143 VAL CB C 30.79 0.300 1 684 140 143 VAL N N 118.41 0.300 1 685 141 144 CYS H H 7.97 0.020 1 686 141 144 CYS C C 175.92 0.300 1 687 141 144 CYS CA C 62.51 0.300 1 688 141 144 CYS CB C 25.71 0.300 1 689 141 144 CYS N N 123.32 0.300 1 690 142 145 VAL H H 8.33 0.020 1 691 142 145 VAL C C 177.76 0.300 1 692 142 145 VAL CA C 65.59 0.300 1 693 142 145 VAL CB C 31.47 0.300 1 694 142 145 VAL N N 115.52 0.300 1 695 143 146 ASP H H 7.89 0.020 1 696 143 146 ASP C C 176.83 0.300 1 697 143 146 ASP CA C 55.69 0.300 1 698 143 146 ASP CB C 41.51 0.300 1 699 143 146 ASP N N 117.06 0.300 1 700 144 147 THR H H 7.70 0.020 1 701 144 147 THR C C 174.53 0.300 1 702 144 147 THR CA C 64.84 0.300 1 703 144 147 THR CB C 70.64 0.300 1 704 144 147 THR N N 114.37 0.300 1 705 145 148 VAL H H 8.59 0.020 1 706 145 148 VAL C C 176.63 0.300 1 707 145 148 VAL CA C 63.86 0.300 1 708 145 148 VAL CB C 31.07 0.300 1 709 145 148 VAL N N 122.71 0.300 1 710 146 149 ARG H H 10.23 0.020 1 711 146 149 ARG C C 177.03 0.300 1 712 146 149 ARG CA C 55.22 0.300 1 713 146 149 ARG CB C 31.83 0.300 1 714 146 149 ARG N N 126.90 0.300 1 715 147 150 THR H H 7.34 0.020 1 716 147 150 THR C C 172.93 0.300 1 717 147 150 THR CA C 60.29 0.300 1 718 147 150 THR CB C 68.10 0.300 1 719 147 150 THR N N 113.05 0.300 1 720 148 151 ASN H H 7.83 0.020 1 721 148 151 ASN C C 172.55 0.300 1 722 148 151 ASN CA C 54.05 0.300 1 723 148 151 ASN CB C 39.89 0.300 1 724 148 151 ASN N N 115.67 0.300 1 725 149 152 VAL H H 8.84 0.020 1 726 149 152 VAL C C 170.96 0.300 1 727 149 152 VAL CA C 59.33 0.300 1 728 149 152 VAL CB C 34.77 0.300 1 729 149 152 VAL N N 123.60 0.300 1 730 150 153 TYR H H 8.68 0.020 1 731 150 153 TYR C C 174.00 0.300 1 732 150 153 TYR CA C 56.56 0.300 1 733 150 153 TYR CB C 37.53 0.300 1 734 150 153 TYR N N 129.06 0.300 1 735 151 154 LEU H H 9.05 0.020 1 736 151 154 LEU C C 175.92 0.300 1 737 151 154 LEU CA C 53.24 0.300 1 738 151 154 LEU CB C 45.06 0.300 1 739 151 154 LEU N N 123.22 0.300 1 740 152 155 ALA H H 8.25 0.020 1 741 152 155 ALA C C 176.77 0.300 1 742 152 155 ALA CA C 50.11 0.300 1 743 152 155 ALA CB C 18.98 0.300 1 744 152 155 ALA N N 124.44 0.300 1 745 153 156 VAL H H 8.79 0.020 1 746 153 156 VAL C C 175.44 0.300 1 747 153 156 VAL CA C 61.18 0.300 1 748 153 156 VAL CB C 34.70 0.300 1 749 153 156 VAL N N 124.23 0.300 1 750 154 157 PHE H H 8.89 0.020 1 751 154 157 PHE C C 175.69 0.300 1 752 154 157 PHE CA C 60.61 0.300 1 753 154 157 PHE CB C 39.92 0.300 1 754 154 157 PHE N N 130.89 0.300 1 755 155 158 ASP H H 8.19 0.020 1 756 155 158 ASP C C 176.00 0.300 1 757 155 158 ASP CA C 54.20 0.300 1 758 155 158 ASP CB C 42.40 0.300 1 759 155 158 ASP N N 120.08 0.300 1 760 156 159 LYS H H 8.83 0.020 1 761 156 159 LYS C C 176.94 0.300 1 762 156 159 LYS CA C 59.61 0.300 1 763 156 159 LYS CB C 32.75 0.300 1 764 156 159 LYS N N 129.95 0.300 1 765 157 160 ASN H H 8.19 0.020 1 766 157 160 ASN C C 178.37 0.300 1 767 157 160 ASN CA C 56.17 0.300 1 768 157 160 ASN CB C 37.58 0.300 1 769 157 160 ASN N N 115.96 0.300 1 770 158 161 LEU H H 8.07 0.020 1 771 158 161 LEU C C 177.62 0.300 1 772 158 161 LEU CA C 57.28 0.300 1 773 158 161 LEU CB C 40.72 0.300 1 774 158 161 LEU N N 122.26 0.300 1 775 159 162 TYR H H 8.66 0.020 1 776 159 162 TYR C C 175.71 0.300 1 777 159 162 TYR CA C 62.97 0.300 1 778 159 162 TYR CB C 38.09 0.300 1 779 159 162 TYR N N 120.31 0.300 1 780 160 163 ASP H H 8.70 0.020 1 781 160 163 ASP C C 179.48 0.300 1 782 160 163 ASP CA C 57.13 0.300 1 783 160 163 ASP CB C 39.72 0.300 1 784 160 163 ASP N N 117.78 0.300 1 785 161 164 LYS H H 7.77 0.020 1 786 161 164 LYS C C 179.24 0.300 1 787 161 164 LYS CA C 58.83 0.300 1 788 161 164 LYS CB C 32.48 0.300 1 789 161 164 LYS N N 121.63 0.300 1 790 162 165 LEU H H 8.78 0.020 1 791 162 165 LEU C C 178.88 0.300 1 792 162 165 LEU CA C 58.01 0.300 1 793 162 165 LEU CB C 41.50 0.300 1 794 162 165 LEU N N 121.77 0.300 1 795 163 166 VAL H H 8.20 0.020 1 796 163 166 VAL C C 178.24 0.300 1 797 163 166 VAL CA C 67.15 0.300 1 798 163 166 VAL CB C 31.55 0.300 1 799 163 166 VAL N N 117.10 0.300 1 800 164 167 SER H H 7.94 0.020 1 801 164 167 SER C C 176.86 0.300 1 802 164 167 SER CA C 61.56 0.300 1 803 164 167 SER CB C 62.72 0.300 1 804 164 167 SER N N 113.07 0.300 1 805 165 168 SER H H 7.92 0.020 1 806 165 168 SER C C 175.56 0.300 1 807 165 168 SER CA C 61.11 0.300 1 808 165 168 SER CB C 62.98 0.300 1 809 165 168 SER N N 115.27 0.300 1 810 166 169 PHE H H 8.03 0.020 1 811 166 169 PHE C C 176.86 0.300 1 812 166 169 PHE CA C 60.74 0.300 1 813 166 169 PHE CB C 40.17 0.300 1 814 166 169 PHE N N 121.38 0.300 1 815 167 170 LEU H H 8.05 0.020 1 816 167 170 LEU C C 177.59 0.300 1 817 167 170 LEU CA C 55.75 0.300 1 818 167 170 LEU CB C 42.11 0.300 1 819 167 170 LEU N N 118.15 0.300 1 820 168 171 GLU H H 7.75 0.020 1 821 168 171 GLU C C 176.29 0.300 1 822 168 171 GLU CA C 56.50 0.300 1 823 168 171 GLU CB C 29.82 0.300 1 824 168 171 GLU N N 118.66 0.300 1 825 169 172 MET H H 7.91 0.020 1 826 169 172 MET C C 175.09 0.300 1 827 169 172 MET CA C 55.47 0.300 1 828 169 172 MET CB C 32.21 0.300 1 829 169 172 MET N N 120.50 0.300 1 830 170 173 LYS H H 7.79 0.020 1 831 170 173 LYS C C 181.25 0.300 1 832 170 173 LYS CA C 57.36 0.300 1 833 170 173 LYS CB C 33.46 0.300 1 834 170 173 LYS N N 127.49 0.300 1 stop_ save_