data_50388 ####################### # 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 bound to ADPr ; _BMRB_accession_number 50388 _BMRB_flat_file_name bmr50388.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 Fancesca . . 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" 145 "13C chemical shifts" 437 "15N chemical shifts" 145 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 50387 'macrodomain of SARS-CoV-2 non-structural protein 3b, apo form' 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_ADPr _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Nsp3b $entity_1 APRr $entity_APR 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_ ############# # Ligands # ############# save_APR _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common ADENOSINE-5-DIPHOSPHORIBOSE _BMRB_code APR _PDB_code APR _Molecular_mass 559.316 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N1 N1 N . 0 . ? C2 C2 C . 0 . ? N3 N3 N . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? N6 N6 N . 0 . ? N7 N7 N . 0 . ? C8 C8 C . 0 . ? N9 N9 N . 0 . ? C1' C1' C . 0 . ? C2' C2' C . 0 . ? O2' O2' O . 0 . ? C3' C3' C . 0 . ? O3' O3' O . 0 . ? O4' O4' O . 0 . ? C4' C4' C . 0 . ? C5' C5' C . 0 . ? O5' O5' O . 0 . ? PA PA P . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? O3A O3A O . 0 . ? PB PB P . 0 . ? O1B O1B O . 0 . ? O2B O2B O . 0 . ? O5D O5D O . 0 . ? C5D C5D C . 0 . ? O4D O4D O . 0 . ? O1D O1D O . 0 . ? C1D C1D C . 0 . ? O2D O2D O . 0 . ? C2D C2D C . 0 . ? O3D O3D O . 0 . ? C3D C3D C . 0 . ? C4D C4D C . 0 . ? H2 H2 H . 0 . ? H61 H61 H . 0 . ? H62 H62 H . 0 . ? H8 H8 H . 0 . ? H'1 H'1 H . 0 . ? H'2 H'2 H . 0 . ? HO'2 HO'2 H . 0 . ? H'3 H'3 H . 0 . ? HO'3 HO'3 H . 0 . ? H'4 H'4 H . 0 . ? H5'1 H5'1 H . 0 . ? H5'2 H5'2 H . 0 . ? HOA2 HOA2 H . 0 . ? HOB2 HOB2 H . 0 . ? H5R1 H5R1 H . 0 . ? H5R2 H5R2 H . 0 . ? HOR1 HOR1 H . 0 . ? HR'1 HR'1 H . 0 . ? HOR2 HOR2 H . 0 . ? HR'2 HR'2 H . 0 . ? HOR3 HOR3 H . 0 . ? HR'3 HR'3 H . 0 . ? HR'4 HR'4 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N1 C2 ? ? DOUB N1 C6 ? ? DOUB C2 N3 ? ? SING C2 H2 ? ? SING N3 C4 ? ? DOUB C4 C5 ? ? SING C4 N9 ? ? SING C5 C6 ? ? SING C5 N7 ? ? SING C6 N6 ? ? SING N6 H61 ? ? SING N6 H62 ? ? DOUB N7 C8 ? ? SING C8 N9 ? ? SING C8 H8 ? ? SING N9 C1' ? ? SING C1' C2' ? ? SING C1' O4' ? ? SING C1' H'1 ? ? SING C2' O2' ? ? SING C2' C3' ? ? SING C2' H'2 ? ? SING O2' HO'2 ? ? SING C3' O3' ? ? SING C3' C4' ? ? SING C3' H'3 ? ? SING O3' HO'3 ? ? SING O4' C4' ? ? SING C4' C5' ? ? SING C4' H'4 ? ? SING C5' O5' ? ? SING C5' H5'1 ? ? SING C5' H5'2 ? ? SING O5' PA ? ? DOUB PA O1A ? ? SING PA O2A ? ? SING PA O3A ? ? SING O2A HOA2 ? ? SING O3A PB ? ? DOUB PB O1B ? ? SING PB O2B ? ? SING PB O5D ? ? SING O2B HOB2 ? ? SING O5D C5D ? ? SING C5D C4D ? ? SING C5D H5R1 ? ? SING C5D H5R2 ? ? SING O4D C1D ? ? SING O4D C4D ? ? SING O1D C1D ? ? SING O1D HOR1 ? ? SING C1D C2D ? ? SING C1D HR'1 ? ? SING O2D C2D ? ? SING O2D HOR2 ? ? SING C2D C3D ? ? SING C2D HR'2 ? ? SING O3D C3D ? ? SING O3D HOR3 ? ? SING C3D C4D ? ? SING C3D HR'3 ? ? SING C4D HR'4 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . 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' ADPr 6.5 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 TOPSPIN _Version 4.0.6 loop_ _Task 'acquisition and processing' stop_ _Details . save_ save_software_3 _Saveframe_category software _Name CARA _Version . loop_ _Task 'chemical shift assignment' 'peak picking' 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_best-TROSY_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D best-TROSY HSQC' _Sample_label $sample_1 save_ save_2D_HSQC_HN_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D HSQC HN' _Sample_label $sample_1 save_ save_3D_best-TROSYHNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D best-TROSYHNCACB' _Sample_label $sample_1 save_ save_3D_best-TROSY_HN(CO)CACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D best-TROSY HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_best-TROSY_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D best-TROSY HNCO' _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' 184 . 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 best-TROSY HSQC' '2D HSQC HN' '3D best-TROSYHNCACB' '3D best-TROSY HN(CO)CACB' '3D best-TROSY HNCO' 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 174.76 0.300 1 2 -1 2 HIS CA C 55.94 0.300 1 3 -1 2 HIS CB C 30.55 0.300 1 4 0 3 MET H H 8.44 0.020 1 5 0 3 MET C C 175.55 0.300 1 6 0 3 MET CA C 55.31 0.300 1 7 0 3 MET CB C 32.65 0.300 1 8 0 3 MET N N 122.27 0.300 1 9 1 4 VAL H H 7.96 0.020 1 10 1 4 VAL C C 175.49 0.300 1 11 1 4 VAL CA C 61.12 0.300 1 12 1 4 VAL CB C 33.16 0.300 1 13 1 4 VAL N N 119.35 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 53.77 0.300 1 17 2 5 ASN CB C 37.59 0.300 1 18 2 5 ASN N N 119.62 0.300 1 19 3 6 SER H H 8.29 0.020 1 20 3 6 SER C C 173.87 0.300 1 21 3 6 SER CA C 56.55 0.300 1 22 3 6 SER CB C 62.26 0.300 1 23 3 6 SER N N 115.43 0.300 1 24 4 7 PHE H H 7.50 0.020 1 25 4 7 PHE C C 176.41 0.300 1 26 4 7 PHE CA C 58.46 0.300 1 27 4 7 PHE CB C 39.38 0.300 1 28 4 7 PHE N N 122.27 0.300 1 29 5 8 SER H H 9.47 0.020 1 30 5 8 SER C C 174.02 0.300 1 31 5 8 SER CA C 57.62 0.300 1 32 5 8 SER CB C 65.30 0.300 1 33 5 8 SER N N 119.22 0.300 1 34 6 9 GLY H H 9.03 0.020 1 35 6 9 GLY C C 174.95 0.300 1 36 6 9 GLY CA C 46.16 0.300 1 37 6 9 GLY N N 111.73 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 58.58 0.300 1 41 7 10 TYR CB C 39.65 0.300 1 42 7 10 TYR N N 118.50 0.300 1 43 8 11 LEU H H 9.65 0.020 1 44 8 11 LEU C C 175.72 0.300 1 45 8 11 LEU CA C 53.89 0.300 1 46 8 11 LEU CB C 43.58 0.300 1 47 8 11 LEU N N 125.66 0.300 1 48 9 12 LYS H H 8.74 0.020 1 49 9 12 LYS C C 175.38 0.300 1 50 9 12 LYS CA C 57.33 0.300 1 51 9 12 LYS CB C 32.97 0.300 1 52 9 12 LYS N N 128.63 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 56.33 0.300 1 56 10 13 LEU CB C 42.02 0.300 1 57 10 13 LEU N N 128.19 0.300 1 58 11 14 THR H H 7.75 0.020 1 59 11 14 THR C C 172.94 0.300 1 60 11 14 THR CA C 58.61 0.300 1 61 11 14 THR CB C 71.36 0.300 1 62 11 14 THR N N 109.39 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 57.42 0.300 1 66 12 15 ASP CB C 40.73 0.300 1 67 12 15 ASP N N 113.25 0.300 1 68 13 16 ASN H H 7.84 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 111.34 0.300 1 73 14 17 VAL H H 6.73 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 119.20 0.300 1 78 15 18 TYR H H 8.67 0.020 1 79 15 18 TYR C C 174.89 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 127.59 0.300 1 83 16 19 ILE H H 9.80 0.020 1 84 16 19 ILE C C 172.41 0.300 1 85 16 19 ILE CA C 60.15 0.300 1 86 16 19 ILE CB C 44.07 0.300 1 87 16 19 ILE N N 120.54 0.300 1 88 17 20 LYS H H 9.02 0.020 1 89 17 20 LYS C C 173.19 0.300 1 90 17 20 LYS CA C 55.86 0.300 1 91 17 20 LYS CB C 38.73 0.300 1 92 17 20 LYS N N 127.78 0.300 1 93 18 21 ASN H H 8.30 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 124.64 0.300 1 98 19 22 ALA H H 7.72 0.020 1 99 19 22 ALA C C 173.86 0.300 1 100 19 22 ALA CA C 51.15 0.300 1 101 19 22 ALA CB C 22.30 0.300 1 102 19 22 ALA N N 128.81 0.300 1 103 20 23 ASP H H 8.45 0.020 1 104 20 23 ASP C C 178.07 0.300 1 105 20 23 ASP CA C 52.58 0.300 1 106 20 23 ASP CB C 42.24 0.300 1 107 20 23 ASP N N 117.92 0.300 1 108 21 24 ILE H H 10.97 0.020 1 109 21 24 ILE C C 175.17 0.300 1 110 21 24 ILE CA C 65.85 0.300 1 111 21 24 ILE CB C 38.95 0.300 1 112 21 24 ILE N N 131.54 0.300 1 113 22 25 VAL H H 8.36 0.020 1 114 22 25 VAL C C 177.51 0.300 1 115 22 25 VAL CA C 66.79 0.300 1 116 22 25 VAL CB C 30.94 0.300 1 117 22 25 VAL N N 122.05 0.300 1 118 23 26 GLU H H 6.86 0.020 1 119 23 26 GLU C C 180.00 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 117.75 0.300 1 123 24 27 GLU H H 8.34 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 117.99 0.300 1 128 25 28 ALA H H 8.48 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 122.52 0.300 1 133 26 29 LYS H H 7.94 0.020 1 134 26 29 LYS C C 178.22 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 114.65 0.300 1 138 27 30 LYS H H 7.49 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 116.65 0.300 1 143 28 31 VAL H H 8.52 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 117.65 0.300 1 148 29 32 LYS H H 8.28 0.020 1 149 29 32 LYS CA C 55.66 0.300 1 150 29 32 LYS CB C 29.36 0.300 1 151 29 32 LYS N N 114.16 0.300 1 152 30 33 PRO C C 176.69 0.300 1 153 30 33 PRO CA C 61.79 0.300 1 154 30 33 PRO CB C 31.96 0.300 1 155 31 34 THR H H 8.54 0.020 1 156 31 34 THR C C 174.93 0.300 1 157 31 34 THR CA C 66.12 0.300 1 158 31 34 THR CB C 68.74 0.300 1 159 31 34 THR N N 115.89 0.300 1 160 32 35 VAL H H 8.54 0.020 1 161 32 35 VAL C C 174.01 0.300 1 162 32 35 VAL CA C 61.18 0.300 1 163 32 35 VAL CB C 35.68 0.300 1 164 32 35 VAL N N 118.23 0.300 1 165 33 36 VAL H H 7.93 0.020 1 166 33 36 VAL C C 172.01 0.300 1 167 33 36 VAL CA C 57.40 0.300 1 168 33 36 VAL CB C 35.22 0.300 1 169 33 36 VAL N N 125.37 0.300 1 170 34 37 VAL H H 8.69 0.020 1 171 34 37 VAL C C 172.85 0.300 1 172 34 37 VAL CA C 60.56 0.300 1 173 34 37 VAL CB C 32.99 0.300 1 174 34 37 VAL N N 129.68 0.300 1 175 54 57 ALA H H 7.69 0.020 1 176 54 57 ALA C C 178.63 0.300 1 177 54 57 ALA CA C 54.52 0.300 1 178 54 57 ALA CB C 19.29 0.300 1 179 54 57 ALA N N 122.34 0.300 1 180 55 58 THR H H 7.64 0.020 1 181 55 58 THR C C 175.99 0.300 1 182 55 58 THR CA C 61.06 0.300 1 183 55 58 THR CB C 70.81 0.300 1 184 55 58 THR N N 107.40 0.300 1 185 56 59 ASN H H 8.55 0.020 1 186 56 59 ASN C C 175.45 0.300 1 187 56 59 ASN CA C 54.48 0.300 1 188 56 59 ASN CB C 36.59 0.300 1 189 56 59 ASN N N 122.07 0.300 1 190 57 60 ASN H H 7.57 0.020 1 191 57 60 ASN C C 174.37 0.300 1 192 57 60 ASN CA C 54.66 0.300 1 193 57 60 ASN CB C 39.90 0.300 1 194 57 60 ASN N N 110.18 0.300 1 195 58 61 ALA H H 7.61 0.020 1 196 58 61 ALA C C 180.72 0.300 1 197 58 61 ALA CA C 54.89 0.300 1 198 58 61 ALA CB C 18.28 0.300 1 199 58 61 ALA N N 123.95 0.300 1 200 59 62 MET H H 8.19 0.020 1 201 59 62 MET C C 179.18 0.300 1 202 59 62 MET CA C 59.28 0.300 1 203 59 62 MET CB C 33.36 0.300 1 204 59 62 MET N N 116.44 0.300 1 205 60 63 GLN H H 8.28 0.020 1 206 60 63 GLN C C 176.98 0.300 1 207 60 63 GLN CA C 58.05 0.300 1 208 60 63 GLN CB C 29.59 0.300 1 209 60 63 GLN N N 125.27 0.300 1 210 61 64 VAL H H 7.81 0.020 1 211 61 64 VAL C C 178.82 0.300 1 212 61 64 VAL CA C 66.60 0.300 1 213 61 64 VAL CB C 32.33 0.300 1 214 61 64 VAL N N 121.03 0.300 1 215 62 65 GLU H H 7.99 0.020 1 216 62 65 GLU C C 180.04 0.300 1 217 62 65 GLU CA C 58.62 0.300 1 218 62 65 GLU CB C 30.55 0.300 1 219 62 65 GLU N N 120.51 0.300 1 220 63 66 SER H H 8.52 0.020 1 221 63 66 SER C C 174.17 0.300 1 222 63 66 SER CA C 62.52 0.300 1 223 63 66 SER CB C 63.39 0.300 1 224 63 66 SER N N 117.34 0.300 1 225 64 67 ASP H H 8.76 0.020 1 226 64 67 ASP C C 179.65 0.300 1 227 64 67 ASP CA C 57.25 0.300 1 228 64 67 ASP CB C 39.62 0.300 1 229 64 67 ASP N N 122.83 0.300 1 230 65 68 ASP H H 7.68 0.020 1 231 65 68 ASP C C 177.86 0.300 1 232 65 68 ASP CA C 57.42 0.300 1 233 65 68 ASP CB C 40.97 0.300 1 234 65 68 ASP N N 121.31 0.300 1 235 66 69 TYR H H 8.30 0.020 1 236 66 69 TYR C C 178.67 0.300 1 237 66 69 TYR CA C 62.42 0.300 1 238 66 69 TYR CB C 37.87 0.300 1 239 66 69 TYR N N 122.41 0.300 1 240 67 70 ILE H H 8.68 0.020 1 241 67 70 ILE C C 179.70 0.300 1 242 67 70 ILE CA C 60.69 0.300 1 243 67 70 ILE CB C 35.45 0.300 1 244 67 70 ILE N N 122.39 0.300 1 245 68 71 ALA H H 8.28 0.020 1 246 68 71 ALA C C 179.39 0.300 1 247 68 71 ALA CA C 55.17 0.300 1 248 68 71 ALA CB C 17.94 0.300 1 249 68 71 ALA N N 123.70 0.300 1 250 69 72 THR H H 7.49 0.020 1 251 69 72 THR C C 175.14 0.300 1 252 69 72 THR CA C 64.64 0.300 1 253 69 72 THR CB C 69.64 0.300 1 254 69 72 THR N N 110.28 0.300 1 255 70 73 ASN H H 8.33 0.020 1 256 70 73 ASN C C 175.74 0.300 1 257 70 73 ASN CA C 54.88 0.300 1 258 70 73 ASN CB C 41.03 0.300 1 259 70 73 ASN N N 117.05 0.300 1 260 71 74 GLY H H 8.32 0.020 1 261 71 74 GLY CA C 44.45 0.300 1 262 71 74 GLY N N 110.52 0.300 1 263 72 75 PRO C C 177.79 0.300 1 264 72 75 PRO CA C 62.22 0.300 1 265 72 75 PRO CB C 31.81 0.300 1 266 73 76 LEU H H 8.43 0.020 1 267 73 76 LEU C C 174.97 0.300 1 268 73 76 LEU CA C 54.99 0.300 1 269 73 76 LEU CB C 44.10 0.300 1 270 73 76 LEU N N 121.12 0.300 1 271 74 77 LYS H H 7.69 0.020 1 272 74 77 LYS C C 177.04 0.300 1 273 74 77 LYS CA C 54.05 0.300 1 274 74 77 LYS CB C 33.91 0.300 1 275 74 77 LYS N N 115.38 0.300 1 276 75 78 VAL H H 8.32 0.020 1 277 75 78 VAL C C 177.57 0.300 1 278 75 78 VAL CA C 65.56 0.300 1 279 75 78 VAL CB C 29.79 0.300 1 280 75 78 VAL N N 122.13 0.300 1 281 76 79 GLY H H 9.09 0.020 1 282 76 79 GLY C C 173.02 0.300 1 283 76 79 GLY CA C 44.88 0.300 1 284 76 79 GLY N N 118.42 0.300 1 285 77 80 GLY H H 8.55 0.020 1 286 77 80 GLY C C 171.24 0.300 1 287 77 80 GLY CA C 43.53 0.300 1 288 77 80 GLY N N 108.73 0.300 1 289 78 81 SER H H 7.92 0.020 1 290 78 81 SER C C 173.72 0.300 1 291 78 81 SER CA C 57.10 0.300 1 292 78 81 SER CB C 68.74 0.300 1 293 78 81 SER N N 106.24 0.300 1 294 79 82 CYS H H 8.75 0.020 1 295 79 82 CYS C C 171.49 0.300 1 296 79 82 CYS CA C 55.78 0.300 1 297 79 82 CYS CB C 30.64 0.300 1 298 79 82 CYS N N 112.39 0.300 1 299 80 83 VAL H H 8.45 0.020 1 300 80 83 VAL C C 175.24 0.300 1 301 80 83 VAL CA C 61.38 0.300 1 302 80 83 VAL CB C 32.28 0.300 1 303 80 83 VAL N N 121.79 0.300 1 304 81 84 LEU H H 9.01 0.020 1 305 81 84 LEU C C 176.72 0.300 1 306 81 84 LEU CA C 52.82 0.300 1 307 81 84 LEU CB C 44.79 0.300 1 308 81 84 LEU N N 130.15 0.300 1 309 82 85 SER H H 10.11 0.020 1 310 82 85 SER C C 175.27 0.300 1 311 82 85 SER CA C 59.67 0.300 1 312 82 85 SER CB C 62.97 0.300 1 313 82 85 SER N N 118.65 0.300 1 314 83 86 GLY H H 7.28 0.020 1 315 83 86 GLY C C 173.58 0.300 1 316 83 86 GLY CA C 45.27 0.300 1 317 83 86 GLY N N 110.93 0.300 1 318 84 87 HIS H H 8.64 0.020 1 319 84 87 HIS C C 174.00 0.300 1 320 84 87 HIS CA C 57.66 0.300 1 321 84 87 HIS CB C 28.55 0.300 1 322 84 87 HIS N N 117.65 0.300 1 323 85 88 ASN H H 9.37 0.020 1 324 85 88 ASN C C 174.47 0.300 1 325 85 88 ASN CA C 53.60 0.300 1 326 85 88 ASN CB C 35.99 0.300 1 327 85 88 ASN N N 116.08 0.300 1 328 86 89 LEU H H 8.36 0.020 1 329 86 89 LEU C C 174.16 0.300 1 330 86 89 LEU CA C 55.69 0.300 1 331 86 89 LEU CB C 43.94 0.300 1 332 86 89 LEU N N 120.06 0.300 1 333 87 90 ALA H H 6.99 0.020 1 334 87 90 ALA C C 176.22 0.300 1 335 87 90 ALA CA C 50.45 0.300 1 336 87 90 ALA CB C 23.39 0.300 1 337 87 90 ALA N N 115.68 0.300 1 338 88 91 LYS H H 7.47 0.020 1 339 88 91 LYS C C 178.09 0.300 1 340 88 91 LYS CA C 60.21 0.300 1 341 88 91 LYS CB C 31.44 0.300 1 342 88 91 LYS N N 119.84 0.300 1 343 89 92 HIS H H 8.37 0.020 1 344 89 92 HIS C C 173.05 0.300 1 345 89 92 HIS CA C 54.06 0.300 1 346 89 92 HIS CB C 33.70 0.300 1 347 89 92 HIS N N 115.66 0.300 1 348 90 93 CYS H H 8.45 0.020 1 349 90 93 CYS C C 172.90 0.300 1 350 90 93 CYS CA C 55.67 0.300 1 351 90 93 CYS CB C 29.35 0.300 1 352 90 93 CYS N N 120.89 0.300 1 353 91 94 LEU H H 8.55 0.020 1 354 91 94 LEU C C 173.91 0.300 1 355 91 94 LEU CA C 52.58 0.300 1 356 91 94 LEU CB C 43.41 0.300 1 357 91 94 LEU N N 131.34 0.300 1 358 92 95 HIS H H 8.95 0.020 1 359 92 95 HIS C C 174.52 0.300 1 360 92 95 HIS CA C 56.40 0.300 1 361 92 95 HIS CB C 32.26 0.300 1 362 92 95 HIS N N 129.84 0.300 1 363 93 96 VAL H H 8.64 0.020 1 364 93 96 VAL C C 172.88 0.300 1 365 93 96 VAL CA C 60.47 0.300 1 366 93 96 VAL CB C 33.99 0.300 1 367 93 96 VAL N N 122.34 0.300 1 368 94 97 VAL H H 7.87 0.020 1 369 94 97 VAL C C 177.18 0.300 1 370 94 97 VAL CA C 60.09 0.300 1 371 94 97 VAL CB C 31.47 0.300 1 372 94 97 VAL N N 125.27 0.300 1 373 95 98 GLY H H 9.15 0.020 1 374 95 98 GLY CA C 42.96 0.300 1 375 95 98 GLY N N 115.47 0.300 1 376 96 99 PRO C C 176.28 0.300 1 377 96 99 PRO CA C 61.63 0.300 1 378 96 99 PRO CB C 31.62 0.300 1 379 97 100 ASN H H 9.57 0.020 1 380 97 100 ASN C C 176.61 0.300 1 381 97 100 ASN CA C 50.61 0.300 1 382 97 100 ASN CB C 35.35 0.300 1 383 97 100 ASN N N 120.64 0.300 1 384 98 101 VAL H H 7.99 0.020 1 385 98 101 VAL C C 179.84 0.300 1 386 98 101 VAL CA C 65.00 0.300 1 387 98 101 VAL CB C 31.45 0.300 1 388 98 101 VAL N N 126.27 0.300 1 389 99 102 ASN H H 8.08 0.020 1 390 99 102 ASN C C 176.53 0.300 1 391 99 102 ASN CA C 55.45 0.300 1 392 99 102 ASN CB C 38.25 0.300 1 393 99 102 ASN N N 119.75 0.300 1 394 100 103 LYS H H 6.96 0.020 1 395 100 103 LYS C C 176.59 0.300 1 396 100 103 LYS CA C 54.85 0.300 1 397 100 103 LYS CB C 32.47 0.300 1 398 100 103 LYS N N 117.28 0.300 1 399 101 104 GLY H H 7.75 0.020 1 400 101 104 GLY C C 174.93 0.300 1 401 101 104 GLY CA C 45.68 0.300 1 402 101 104 GLY N N 106.79 0.300 1 403 102 105 GLU H H 7.39 0.020 1 404 102 105 GLU C C 175.97 0.300 1 405 102 105 GLU CA C 56.23 0.300 1 406 102 105 GLU CB C 29.46 0.300 1 407 102 105 GLU N N 119.50 0.300 1 408 103 106 ASP H H 8.20 0.020 1 409 103 106 ASP C C 177.58 0.300 1 410 103 106 ASP CA C 54.55 0.300 1 411 103 106 ASP CB C 41.59 0.300 1 412 103 106 ASP N N 120.45 0.300 1 413 104 107 ILE H H 8.61 0.020 1 414 104 107 ILE C C 178.08 0.300 1 415 104 107 ILE CA C 62.15 0.300 1 416 104 107 ILE CB C 38.65 0.300 1 417 104 107 ILE N N 128.27 0.300 1 418 105 108 GLN H H 9.14 0.020 1 419 105 108 GLN C C 178.95 0.300 1 420 105 108 GLN CA C 58.48 0.300 1 421 105 108 GLN CB C 28.00 0.300 1 422 105 108 GLN N N 124.13 0.300 1 423 106 109 LEU H H 8.14 0.020 1 424 106 109 LEU C C 177.93 0.300 1 425 106 109 LEU CA C 56.44 0.300 1 426 106 109 LEU CB C 41.37 0.300 1 427 106 109 LEU N N 118.31 0.300 1 428 107 110 LEU H H 8.31 0.020 1 429 107 110 LEU C C 177.75 0.300 1 430 107 110 LEU CA C 57.24 0.300 1 431 107 110 LEU CB C 42.61 0.300 1 432 107 110 LEU N N 121.71 0.300 1 433 108 111 LYS H H 7.54 0.020 1 434 108 111 LYS C C 177.53 0.300 1 435 108 111 LYS CA C 60.40 0.300 1 436 108 111 LYS CB C 31.83 0.300 1 437 108 111 LYS N N 119.08 0.300 1 438 109 112 SER H H 6.91 0.020 1 439 109 112 SER C C 175.85 0.300 1 440 109 112 SER CA C 61.85 0.300 1 441 109 112 SER CB C 62.38 0.300 1 442 109 112 SER N N 112.73 0.300 1 443 110 113 ALA H H 8.07 0.020 1 444 110 113 ALA C C 180.10 0.300 1 445 110 113 ALA CA C 54.67 0.300 1 446 110 113 ALA CB C 18.04 0.300 1 447 110 113 ALA N N 121.83 0.300 1 448 111 114 TYR H H 8.04 0.020 1 449 111 114 TYR C C 178.28 0.300 1 450 111 114 TYR CA C 62.09 0.300 1 451 111 114 TYR CB C 37.63 0.300 1 452 111 114 TYR N N 115.59 0.300 1 453 112 115 GLU H H 8.28 0.020 1 454 112 115 GLU C C 179.70 0.300 1 455 112 115 GLU CA C 59.30 0.300 1 456 112 115 GLU CB C 28.76 0.300 1 457 112 115 GLU N N 121.33 0.300 1 458 113 116 ASN H H 7.32 0.020 1 459 113 116 ASN C C 176.58 0.300 1 460 113 116 ASN CA C 56.61 0.300 1 461 113 116 ASN CB C 39.65 0.300 1 462 113 116 ASN N N 113.56 0.300 1 463 114 117 PHE H H 8.78 0.020 1 464 114 117 PHE C C 177.27 0.300 1 465 114 117 PHE CA C 58.25 0.300 1 466 114 117 PHE CB C 37.57 0.300 1 467 114 117 PHE N N 118.12 0.300 1 468 115 118 ASN H H 7.54 0.020 1 469 115 118 ASN C C 175.35 0.300 1 470 115 118 ASN CA C 54.81 0.300 1 471 115 118 ASN CB C 37.69 0.300 1 472 115 118 ASN N N 112.26 0.300 1 473 116 119 GLN H H 6.96 0.020 1 474 116 119 GLN C C 173.47 0.300 1 475 116 119 GLN CA C 55.67 0.300 1 476 116 119 GLN CB C 28.93 0.300 1 477 116 119 GLN N N 117.07 0.300 1 478 117 120 HIS H H 7.74 0.020 1 479 117 120 HIS C C 173.33 0.300 1 480 117 120 HIS CA C 54.70 0.300 1 481 117 120 HIS CB C 33.69 0.300 1 482 117 120 HIS N N 119.28 0.300 1 483 118 121 GLU H H 8.70 0.020 1 484 118 121 GLU C C 176.89 0.300 1 485 118 121 GLU CA C 60.00 0.300 1 486 118 121 GLU CB C 30.58 0.300 1 487 118 121 GLU N N 120.51 0.300 1 488 119 122 VAL H H 7.82 0.020 1 489 119 122 VAL C C 175.62 0.300 1 490 119 122 VAL CA C 60.39 0.300 1 491 119 122 VAL CB C 34.79 0.300 1 492 119 122 VAL N N 115.03 0.300 1 493 120 123 LEU H H 8.77 0.020 1 494 120 123 LEU C C 173.49 0.300 1 495 120 123 LEU CA C 55.09 0.300 1 496 120 123 LEU CB C 45.64 0.300 1 497 120 123 LEU N N 126.87 0.300 1 498 121 124 LEU H H 7.79 0.020 1 499 121 124 LEU C C 174.48 0.300 1 500 121 124 LEU CA C 53.64 0.300 1 501 121 124 LEU CB C 43.96 0.300 1 502 121 124 LEU N N 123.70 0.300 1 503 122 125 ALA H H 9.66 0.020 1 504 122 125 ALA CA C 49.75 0.300 1 505 122 125 ALA CB C 22.80 0.300 1 506 122 125 ALA N N 129.41 0.300 1 507 123 126 PRO C C 173.93 0.300 1 508 123 126 PRO CA C 60.65 0.300 1 509 123 126 PRO CB C 33.79 0.300 1 510 124 127 LEU H H 8.08 0.020 1 511 124 127 LEU C C 175.97 0.300 1 512 124 127 LEU CA C 53.70 0.300 1 513 124 127 LEU CB C 42.91 0.300 1 514 124 127 LEU N N 114.03 0.300 1 515 125 128 LEU H H 7.17 0.020 1 516 125 128 LEU C C 177.95 0.300 1 517 125 128 LEU CA C 55.65 0.300 1 518 125 128 LEU CB C 42.66 0.300 1 519 125 128 LEU N N 121.45 0.300 1 520 126 129 SER H H 8.67 0.020 1 521 126 129 SER C C 172.53 0.300 1 522 126 129 SER CA C 61.11 0.300 1 523 126 129 SER CB C 64.18 0.300 1 524 126 129 SER N N 112.89 0.300 1 525 127 130 ALA H H 6.69 0.020 1 526 127 130 ALA C C 176.57 0.300 1 527 127 130 ALA CA C 52.32 0.300 1 528 127 130 ALA CB C 20.46 0.300 1 529 127 130 ALA N N 118.72 0.300 1 530 128 131 GLY H H 9.92 0.020 1 531 128 131 GLY CA C 44.88 0.300 1 532 128 131 GLY N N 114.96 0.300 1 533 131 134 GLY H H 7.66 0.020 1 534 131 134 GLY C C 174.86 0.300 1 535 131 134 GLY CA C 47.87 0.300 1 536 131 134 GLY N N 104.61 0.300 1 537 132 135 ALA H H 9.51 0.020 1 538 132 135 ALA C C 176.57 0.300 1 539 132 135 ALA CA C 51.30 0.300 1 540 132 135 ALA CB C 19.17 0.300 1 541 132 135 ALA N N 123.30 0.300 1 542 133 136 ASP H H 8.63 0.020 1 543 133 136 ASP CA C 52.07 0.300 1 544 133 136 ASP CB C 42.08 0.300 1 545 133 136 ASP N N 122.30 0.300 1 546 134 137 PRO C C 177.71 0.300 1 547 134 137 PRO CA C 65.57 0.300 1 548 134 137 PRO CB C 33.61 0.300 1 549 135 138 ILE H H 7.90 0.020 1 550 135 138 ILE C C 178.03 0.300 1 551 135 138 ILE CA C 64.33 0.300 1 552 135 138 ILE CB C 36.67 0.300 1 553 135 138 ILE N N 116.28 0.300 1 554 136 139 HIS H H 7.62 0.020 1 555 136 139 HIS C C 176.65 0.300 1 556 136 139 HIS CA C 59.66 0.300 1 557 136 139 HIS CB C 30.53 0.300 1 558 136 139 HIS N N 120.11 0.300 1 559 137 140 SER H H 8.16 0.020 1 560 137 140 SER C C 176.41 0.300 1 561 137 140 SER CA C 61.43 0.300 1 562 137 140 SER CB C 63.41 0.300 1 563 137 140 SER N N 109.93 0.300 1 564 138 141 LEU H H 8.26 0.020 1 565 138 141 LEU C C 177.22 0.300 1 566 138 141 LEU CA C 57.59 0.300 1 567 138 141 LEU CB C 41.00 0.300 1 568 138 141 LEU N N 118.18 0.300 1 569 139 142 ARG H H 8.21 0.020 1 570 139 142 ARG C C 178.07 0.300 1 571 139 142 ARG CA C 59.38 0.300 1 572 139 142 ARG CB C 29.20 0.300 1 573 139 142 ARG N N 119.85 0.300 1 574 140 143 VAL H H 8.37 0.020 1 575 140 143 VAL C C 178.63 0.300 1 576 140 143 VAL CA C 66.26 0.300 1 577 140 143 VAL CB C 30.79 0.300 1 578 140 143 VAL N N 118.21 0.300 1 579 141 144 CYS H H 7.83 0.020 1 580 141 144 CYS C C 175.92 0.300 1 581 141 144 CYS CA C 62.82 0.300 1 582 141 144 CYS CB C 25.55 0.300 1 583 141 144 CYS N N 123.48 0.300 1 584 142 145 VAL H H 8.31 0.020 1 585 142 145 VAL C C 177.76 0.300 1 586 142 145 VAL CA C 65.59 0.300 1 587 142 145 VAL CB C 31.47 0.300 1 588 142 145 VAL N N 115.42 0.300 1 589 143 146 ASP H H 7.95 0.020 1 590 143 146 ASP C C 176.91 0.300 1 591 143 146 ASP CA C 55.69 0.300 1 592 143 146 ASP CB C 41.51 0.300 1 593 143 146 ASP N N 117.00 0.300 1 594 144 147 THR H H 7.73 0.020 1 595 144 147 THR C C 174.53 0.300 1 596 144 147 THR CA C 64.84 0.300 1 597 144 147 THR CB C 70.64 0.300 1 598 144 147 THR N N 114.51 0.300 1 599 145 148 VAL H H 8.56 0.020 1 600 145 148 VAL C C 176.63 0.300 1 601 145 148 VAL CA C 63.86 0.300 1 602 145 148 VAL CB C 31.07 0.300 1 603 145 148 VAL N N 122.62 0.300 1 604 146 149 ARG H H 10.24 0.020 1 605 146 149 ARG C C 177.03 0.300 1 606 146 149 ARG CA C 55.22 0.300 1 607 146 149 ARG CB C 31.83 0.300 1 608 146 149 ARG N N 126.84 0.300 1 609 147 150 THR H H 7.35 0.020 1 610 147 150 THR C C 172.93 0.300 1 611 147 150 THR CA C 60.29 0.300 1 612 147 150 THR CB C 68.10 0.300 1 613 147 150 THR N N 113.08 0.300 1 614 148 151 ASN H H 7.80 0.020 1 615 148 151 ASN C C 172.55 0.300 1 616 148 151 ASN CA C 54.05 0.300 1 617 148 151 ASN CB C 39.89 0.300 1 618 148 151 ASN N N 115.73 0.300 1 619 149 152 VAL H H 8.85 0.020 1 620 149 152 VAL C C 170.96 0.300 1 621 149 152 VAL CA C 59.65 0.300 1 622 149 152 VAL CB C 34.59 0.300 1 623 149 152 VAL N N 123.75 0.300 1 624 150 153 TYR H H 8.70 0.020 1 625 150 153 TYR C C 174.00 0.300 1 626 150 153 TYR CA C 56.53 0.300 1 627 150 153 TYR CB C 37.45 0.300 1 628 150 153 TYR N N 129.22 0.300 1 629 151 154 LEU H H 9.12 0.020 1 630 151 154 LEU C C 175.92 0.300 1 631 151 154 LEU CA C 53.24 0.300 1 632 151 154 LEU CB C 44.84 0.300 1 633 151 154 LEU N N 123.55 0.300 1 634 152 155 ALA H H 8.36 0.020 1 635 152 155 ALA C C 175.94 0.300 1 636 152 155 ALA CA C 50.11 0.300 1 637 152 155 ALA CB C 18.98 0.300 1 638 152 155 ALA N N 125.31 0.300 1 639 153 156 VAL H H 8.80 0.020 1 640 153 156 VAL C C 175.44 0.300 1 641 153 156 VAL CA C 61.18 0.300 1 642 153 156 VAL CB C 35.25 0.300 1 643 153 156 VAL N N 122.06 0.300 1 644 154 157 PHE H H 6.94 0.020 1 645 154 157 PHE C C 175.33 0.300 1 646 154 157 PHE CA C 59.58 0.300 1 647 154 157 PHE CB C 38.20 0.300 1 648 154 157 PHE N N 131.34 0.300 1 649 155 158 ASP H H 8.62 0.020 1 650 155 158 ASP C C 176.00 0.300 1 651 155 158 ASP CA C 54.20 0.300 1 652 155 158 ASP CB C 41.99 0.300 1 653 155 158 ASP N N 121.15 0.300 1 654 156 159 LYS H H 8.72 0.020 1 655 156 159 LYS C C 176.94 0.300 1 656 156 159 LYS CA C 59.61 0.300 1 657 156 159 LYS CB C 32.75 0.300 1 658 156 159 LYS N N 129.81 0.300 1 659 157 160 ASN H H 8.11 0.020 1 660 157 160 ASN C C 178.37 0.300 1 661 157 160 ASN CA C 56.17 0.300 1 662 157 160 ASN CB C 37.58 0.300 1 663 157 160 ASN N N 116.07 0.300 1 664 158 161 LEU H H 8.10 0.020 1 665 158 161 LEU C C 177.62 0.300 1 666 158 161 LEU CA C 57.43 0.300 1 667 158 161 LEU CB C 41.03 0.300 1 668 158 161 LEU N N 122.53 0.300 1 669 159 162 TYR H H 8.65 0.020 1 670 159 162 TYR C C 175.71 0.300 1 671 159 162 TYR CA C 62.97 0.300 1 672 159 162 TYR CB C 38.09 0.300 1 673 159 162 TYR N N 120.15 0.300 1 674 160 163 ASP H H 8.61 0.020 1 675 160 163 ASP C C 179.48 0.300 1 676 160 163 ASP CA C 57.13 0.300 1 677 160 163 ASP CB C 39.72 0.300 1 678 160 163 ASP N N 117.67 0.300 1 679 161 164 LYS H H 7.76 0.020 1 680 161 164 LYS C C 179.24 0.300 1 681 161 164 LYS CA C 58.83 0.300 1 682 161 164 LYS CB C 32.48 0.300 1 683 161 164 LYS N N 121.73 0.300 1 684 162 165 LEU H H 8.82 0.020 1 685 162 165 LEU C C 178.88 0.300 1 686 162 165 LEU CA C 58.01 0.300 1 687 162 165 LEU CB C 41.50 0.300 1 688 162 165 LEU N N 121.73 0.300 1 689 163 166 VAL H H 8.21 0.020 1 690 163 166 VAL C C 178.24 0.300 1 691 163 166 VAL CA C 67.15 0.300 1 692 163 166 VAL CB C 31.55 0.300 1 693 163 166 VAL N N 116.98 0.300 1 694 164 167 SER H H 7.88 0.020 1 695 164 167 SER C C 176.86 0.300 1 696 164 167 SER CA C 61.56 0.300 1 697 164 167 SER CB C 62.72 0.300 1 698 164 167 SER N N 113.08 0.300 1 699 165 168 SER H H 7.92 0.020 1 700 165 168 SER C C 175.69 0.300 1 701 165 168 SER CA C 61.11 0.300 1 702 165 168 SER CB C 63.26 0.300 1 703 165 168 SER N N 115.17 0.300 1 704 166 169 PHE H H 8.11 0.020 1 705 166 169 PHE C C 176.86 0.300 1 706 166 169 PHE CA C 61.09 0.300 1 707 166 169 PHE CB C 40.17 0.300 1 708 166 169 PHE N N 121.47 0.300 1 709 167 170 LEU H H 8.06 0.020 1 710 167 170 LEU C C 177.59 0.300 1 711 167 170 LEU CA C 55.75 0.300 1 712 167 170 LEU CB C 42.11 0.300 1 713 167 170 LEU N N 117.86 0.300 1 714 168 171 GLU H H 7.72 0.020 1 715 168 171 GLU C C 176.29 0.300 1 716 168 171 GLU CA C 56.71 0.300 1 717 168 171 GLU CB C 29.82 0.300 1 718 168 171 GLU N N 118.58 0.300 1 719 169 172 MET H H 7.91 0.020 1 720 169 172 MET C C 175.09 0.300 1 721 169 172 MET CA C 55.66 0.300 1 722 169 172 MET CB C 32.59 0.300 1 723 169 172 MET N N 120.44 0.300 1 724 170 173 LYS H H 7.79 0.020 1 725 170 173 LYS CA C 57.60 0.300 1 726 170 173 LYS CB C 33.46 0.300 1 727 170 173 LYS N N 127.53 0.300 1 stop_ save_