data_26858 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone chemical shift assignments for the U1 protein from the Bas-Congo virus. Seattle Structural Genomic Center for Infectious Disease target RhbaA.18619.a.D16. ; _BMRB_accession_number 26858 _BMRB_flat_file_name bmr26858.str _Entry_type original _Submission_date 2016-07-24 _Accession_date 2016-07-24 _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 Buchko Garry W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 273 "13C chemical shifts" 395 "15N chemical shifts" 124 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-03-14 update BMRB 'update entry citation' 2016-08-23 original author 'original release' stop_ _Original_release_date 2016-08-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone chemical shift assignments and secondary structure analysis of the U1 protein from the Bas-Congo virus ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 27981424 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Buchko Garry W. . 2 Clifton Matthew C. . 3 Wallace Ellen G. . 4 Atkins Kateri A. . 5 Myler Peter J. . stop_ _Journal_abbreviation 'Biomol NMR Assign' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 11 _Journal_issue 1 _Journal_ISSN 1874-270X _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 51 _Page_last 56 _Year 2017 _Details . loop_ _Keyword Tibrovirus rhabdovirus 'viral hemorrhagic fever' viroporins stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name BASV-U1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label BASV-U1 $BASV_U1 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_BASV_U1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common BASV_U1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 177 _Mol_residue_sequence ; ATMAFHPMLCRLELSVSAAP PASPIDATLLRSLITSVLNS SWVDLGGNTANEKVLCAIGL IEAFCRERVIPPTSNSFNTS VTYHIMVEDLDPDDLGNIQL INKPLLSLEGDLKVLGSYQL TFQTIPGHSEPRSMTDNGIY HSDSPFFQIALGHALLGTGK IYDHITRALRVAPITIA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 27 ALA 2 28 THR 3 29 MET 4 30 ALA 5 31 PHE 6 32 HIS 7 33 PRO 8 34 MET 9 35 LEU 10 36 CYS 11 37 ARG 12 38 LEU 13 39 GLU 14 40 LEU 15 41 SER 16 42 VAL 17 43 SER 18 44 ALA 19 45 ALA 20 46 PRO 21 47 PRO 22 48 ALA 23 49 SER 24 50 PRO 25 51 ILE 26 52 ASP 27 53 ALA 28 54 THR 29 55 LEU 30 56 LEU 31 57 ARG 32 58 SER 33 59 LEU 34 60 ILE 35 61 THR 36 62 SER 37 63 VAL 38 64 LEU 39 65 ASN 40 66 SER 41 67 SER 42 68 TRP 43 69 VAL 44 70 ASP 45 71 LEU 46 72 GLY 47 73 GLY 48 74 ASN 49 75 THR 50 76 ALA 51 77 ASN 52 78 GLU 53 79 LYS 54 80 VAL 55 81 LEU 56 82 CYS 57 83 ALA 58 84 ILE 59 85 GLY 60 86 LEU 61 87 ILE 62 88 GLU 63 89 ALA 64 90 PHE 65 91 CYS 66 92 ARG 67 93 GLU 68 94 ARG 69 95 VAL 70 96 ILE 71 97 PRO 72 98 PRO 73 99 THR 74 100 SER 75 101 ASN 76 102 SER 77 103 PHE 78 104 ASN 79 105 THR 80 106 SER 81 107 VAL 82 108 THR 83 109 TYR 84 110 HIS 85 111 ILE 86 112 MET 87 113 VAL 88 114 GLU 89 115 ASP 90 116 LEU 91 117 ASP 92 118 PRO 93 119 ASP 94 120 ASP 95 121 LEU 96 122 GLY 97 123 ASN 98 124 ILE 99 125 GLN 100 126 LEU 101 127 ILE 102 128 ASN 103 129 LYS 104 130 PRO 105 131 LEU 106 132 LEU 107 133 SER 108 134 LEU 109 135 GLU 110 136 GLY 111 137 ASP 112 138 LEU 113 139 LYS 114 140 VAL 115 141 LEU 116 142 GLY 117 143 SER 118 144 TYR 119 145 GLN 120 146 LEU 121 147 THR 122 148 PHE 123 149 GLN 124 150 THR 125 151 ILE 126 152 PRO 127 153 GLY 128 154 HIS 129 155 SER 130 156 GLU 131 157 PRO 132 158 ARG 133 159 SER 134 160 MET 135 161 THR 136 162 ASP 137 163 ASN 138 164 GLY 139 165 ILE 140 166 TYR 141 167 HIS 142 168 SER 143 169 ASP 144 170 SER 145 171 PRO 146 172 PHE 147 173 PHE 148 174 GLN 149 175 ILE 150 176 ALA 151 177 LEU 152 177 GLY 153 178 HIS 154 179 ALA 155 180 LEU 156 181 LEU 157 182 GLY 158 183 THR 159 184 GLY 160 185 LYS 161 186 ILE 162 187 TYR 163 188 ASP 164 189 HIS 165 190 ILE 166 191 THR 167 192 ARG 168 193 ALA 169 194 LEU 170 195 ARG 171 196 VAL 172 197 ALA 173 198 PRO 174 199 ILE 175 200 THR 176 201 ILE 177 202 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $BASV_U1 'Bas-Congo viruses' 1231712 Viruses . . . 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 $BASV_U1 'recombinant technology' . Escherichia coli BL21(DE3) pEMB32 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 $BASV_U1 1 mM '[U-99% 13C; U-99% 15N]' 'sodium chloride' 100 mM 'natural abundance' TRIS 20 mM 'natural abundance' DTT 1 mM 'natural abundance' urea 500 mM 'natural abundance' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $BASV_U1 1 mM '[U-100% 13C; U-100% 15N; U-80% 2H]' 'sodium chloride' 100 mM 'natural abundance' TRIS 20 mM 'natural abundance' DTT 1 mM 'natural abundance' urea 500 mM 'natural abundance' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.115 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_Felix _Saveframe_category software _Name Felix _Version 2007 loop_ _Vendor _Address _Electronic_address 'Accelrys Software Inc.' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model VXRS _Field_strength 750 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _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_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_2 save_ save_3D_C(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_2 save_ save_3D_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HNCACB_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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' 0.62 0.005 M pH 7.0 0.1 pH pressure 1 . atm temperature 293 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details 'C13-beta chemical shifts obtained from the 90% deuterated sample were corrected for the deuterium isotope effect.' loop_ _Experiment_label '2D 1H-15N HSQC' '3D HN(CO)CA' '3D HNCA' '3D HNCACB' '3D C(CO)NH' stop_ loop_ _Sample_label $sample_2 $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name BASV-U1 _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 27 1 ALA C C 177.9 0.2 1 2 27 1 ALA CA C 52.8 0.2 1 3 27 1 ALA CB C 19.3 0.2 1 4 28 2 THR H H 8.29 0.02 1 5 28 2 THR C C 174.5 0.2 1 6 28 2 THR CA C 61.9 0.2 1 7 28 2 THR CB C 69.6 0.2 1 8 28 2 THR N N 113.2 0.2 1 9 29 3 MET H H 8.46 0.02 1 10 29 3 MET HA H 4.46 0.02 1 11 29 3 MET C C 175.1 0.2 1 12 29 3 MET CA C 55.6 0.2 1 13 29 3 MET CB C 33.1 0.2 1 14 29 3 MET CG C 32.3 0.2 1 15 29 3 MET N N 122.7 0.2 1 16 30 4 ALA H H 8.41 0.02 1 17 30 4 ALA HA H 4.41 0.02 1 18 30 4 ALA HB H 1.37 0.02 1 19 30 4 ALA C C 176.3 0.2 1 20 30 4 ALA CA C 52.2 0.2 1 21 30 4 ALA CB C 19.8 0.2 1 22 30 4 ALA N N 124.8 0.2 1 23 31 5 PHE H H 8.05 0.02 1 24 31 5 PHE HA H 4.94 0.02 1 25 31 5 PHE HB2 H 2.95 0.02 2 26 31 5 PHE HB3 H 2.75 0.02 2 27 31 5 PHE CA C 56.5 0.2 1 28 31 5 PHE CB C 41.6 0.2 1 29 31 5 PHE N N 118.0 0.2 1 30 35 9 LEU C C 175.3 0.2 1 31 35 9 LEU CA C 55.1 0.2 1 32 35 9 LEU CB C 41.4 0.2 1 33 36 10 CYS H H 9.08 0.02 1 34 36 10 CYS HA H 4.95 0.02 1 35 36 10 CYS C C 172.9 0.2 1 36 36 10 CYS CA C 56.9 0.2 1 37 36 10 CYS CB C 30.3 0.2 1 38 36 10 CYS N N 122.5 0.2 1 39 37 11 ARG H H 8.59 0.02 1 40 37 11 ARG HA H 5.02 0.02 1 41 37 11 ARG C C 173.8 0.2 1 42 37 11 ARG CA C 55.5 0.2 1 43 37 11 ARG CB C 32.7 0.2 1 44 37 11 ARG N N 121.3 0.2 1 45 38 12 LEU H H 9.25 0.02 1 46 38 12 LEU HA H 5.72 0.02 1 47 38 12 LEU C C 174.6 0.2 1 48 38 12 LEU CA C 53.9 0.2 1 49 38 12 LEU CB C 46.6 0.2 1 50 38 12 LEU N N 127.9 0.2 1 51 39 13 GLU H H 9.34 0.02 1 52 39 13 GLU HA H 5.08 0.02 1 53 39 13 GLU C C 174.2 0.2 1 54 39 13 GLU CA C 55.8 0.2 1 55 39 13 GLU CB C 31.3 0.2 1 56 39 13 GLU N N 127.2 0.2 1 57 40 14 LEU H H 8.91 0.02 1 58 40 14 LEU HA H 5.41 0.02 1 59 40 14 LEU HD1 H 1.08 0.02 1 60 40 14 LEU C C 173.7 0.2 1 61 40 14 LEU CA C 53.8 0.2 1 62 40 14 LEU CB C 46.9 0.2 1 63 40 14 LEU N N 125.5 0.2 1 64 41 15 SER H H 9.13 0.02 1 65 41 15 SER HA H 5.38 0.02 1 66 41 15 SER HB2 H 3.80 0.02 2 67 41 15 SER HB3 H 3.80 0.02 2 68 41 15 SER C C 173.1 0.2 1 69 41 15 SER CA C 56.6 0.2 1 70 41 15 SER CB C 65.4 0.2 1 71 41 15 SER N N 121.7 0.2 1 72 42 16 VAL H H 7.89 0.02 1 73 42 16 VAL HA H 4.51 0.02 1 74 42 16 VAL HG1 H 0.84 0.02 2 75 42 16 VAL HG2 H 0.69 0.02 2 76 42 16 VAL C C 174.3 0.2 1 77 42 16 VAL CA C 61.2 0.2 1 78 42 16 VAL CB C 35.5 0.2 1 79 42 16 VAL N N 124.3 0.2 1 80 43 17 SER H H 8.75 0.02 1 81 43 17 SER HA H 5.02 0.02 1 82 43 17 SER HB2 H 3.64 0.02 2 83 43 17 SER HB3 H 3.56 0.02 2 84 43 17 SER C C 172.6 0.2 1 85 43 17 SER CA C 56.6 0.2 1 86 43 17 SER CB C 65.1 0.2 1 87 43 17 SER N N 120.3 0.2 1 88 44 18 ALA H H 8.91 0.02 1 89 44 18 ALA HA H 4.94 0.02 1 90 44 18 ALA HB H 1.08 0.02 1 91 44 18 ALA C C 176.7 0.2 1 92 44 18 ALA CA C 50.5 . 1 93 44 18 ALA CB C 21.4 . 1 94 44 18 ALA N N 125.6 0.2 1 95 45 19 ALA H H 8.52 0.02 1 96 45 19 ALA HA H 4.75 0.02 1 97 45 19 ALA HB H 1.25 0.02 1 98 45 19 ALA C C 174.7 0.2 1 99 45 19 ALA CA C 49.3 0.2 1 100 45 19 ALA CB C 17.4 0.2 1 101 45 19 ALA N N 127.9 0.2 1 102 47 21 PRO C C 175.8 0.2 1 103 47 21 PRO CA C 64.0 0.2 1 104 47 21 PRO CB C 33.4 0.2 1 105 47 21 PRO CG C 24.1 0.2 1 106 48 22 ALA H H 8.37 0.02 1 107 48 22 ALA HA H 4.33 0.02 1 108 48 22 ALA HB H 1.54 0.02 1 109 48 22 ALA C C 175.6 0.2 1 110 48 22 ALA CA C 53.2 0.2 1 111 48 22 ALA CB C 19.5 0.2 1 112 48 22 ALA N N 128.6 0.2 1 113 49 23 SER H H 8.36 0.02 1 114 49 23 SER HA H 5.01 0.02 1 115 49 23 SER HB2 H 4.13 0.02 2 116 49 23 SER HB3 H 3.81 0.02 2 117 49 23 SER C C 174.6 0.2 1 118 49 23 SER CA C 54.0 0.2 1 119 49 23 SER CB C 64.6 0.2 1 120 49 23 SER N N 115.5 0.2 1 121 50 24 PRO C C 172.8 0.2 1 122 50 24 PRO CA C 64.1 0.2 1 123 50 24 PRO CB C 31.2 0.2 1 124 51 25 ILE H H 6.70 0.02 1 125 51 25 ILE HA H 4.67 0.02 1 126 51 25 ILE C C 176.1 0.2 1 127 51 25 ILE CA C 59.3 0.2 1 128 51 25 ILE CB C 36.3 0.2 1 129 51 25 ILE N N 127.1 0.2 1 130 52 26 ASP H H 7.40 0.02 1 131 52 26 ASP HA H 4.56 0.02 1 132 52 26 ASP C C 177.4 0.2 1 133 52 26 ASP CA C 55.4 . 1 134 52 26 ASP CB C 42.6 . 1 135 52 26 ASP N N 121.0 0.2 1 136 53 27 ALA H H 9.24 0.02 1 137 53 27 ALA CA C 55.5 0.2 1 138 53 27 ALA CB C 18.6 0.2 1 139 53 27 ALA N N 125.3 0.2 1 140 54 28 THR C C 176.6 0.2 1 141 54 28 THR CA C 65.4 0.2 1 142 54 28 THR CB C 68.4 0.2 1 143 55 29 LEU H H 7.15 0.02 1 144 55 29 LEU HA H 3.94 0.02 1 145 55 29 LEU C C 178.2 0.2 1 146 55 29 LEU CA C 59.6 0.2 1 147 55 29 LEU CB C 40.8 0.2 1 148 55 29 LEU N N 124.5 0.2 1 149 56 30 LEU H H 7.61 0.02 1 150 56 30 LEU C C 177.5 0.2 1 151 56 30 LEU CA C 57.4 0.2 1 152 56 30 LEU CB C 38.9 0.2 1 153 56 30 LEU N N 119.3 0.2 1 154 57 31 ARG H H 7.91 0.02 1 155 57 31 ARG HA H 3.57 0.02 1 156 57 31 ARG C C 178.4 0.2 1 157 57 31 ARG CA C 60.5 0.2 1 158 57 31 ARG CB C 29.9 0.2 1 159 57 31 ARG N N 117.4 0.2 1 160 58 32 SER H H 7.52 0.02 1 161 58 32 SER HA H 4.04 0.02 1 162 58 32 SER C C 176.2 0.2 1 163 58 32 SER CA C 62.3 0.2 1 164 58 32 SER CB C 63.4 0.2 1 165 58 32 SER N N 114.0 0.2 1 166 59 33 LEU H H 8.49 0.02 1 167 59 33 LEU HA H 3.94 0.02 1 168 59 33 LEU HD1 H 0.83 0.02 1 169 59 33 LEU C C 177.3 0.2 1 170 59 33 LEU CA C 58.4 0.2 1 171 59 33 LEU CB C 41.5 0.2 1 172 59 33 LEU N N 124.9 0.2 1 173 60 34 ILE H H 8.55 0.02 1 174 60 34 ILE C C 177.1 0.2 1 175 60 34 ILE CA C 65.7 0.2 1 176 60 34 ILE CB C 37.5 0.2 1 177 60 34 ILE N N 118.1 0.2 1 178 61 35 THR H H 8.06 0.02 1 179 61 35 THR HA H 4.15 0.02 1 180 61 35 THR C C 175.4 0.2 1 181 61 35 THR CA C 67.7 0.2 1 182 61 35 THR CB C 69.2 0.2 1 183 61 35 THR N N 115.3 0.2 1 184 62 36 SER H H 8.20 0.02 1 185 62 36 SER C C 179.1 0.2 1 186 62 36 SER CA C 61.1 0.2 1 187 62 36 SER CB C 62.8 0.2 1 188 62 36 SER N N 114.6 0.2 1 189 63 37 VAL H H 8.51 0.02 1 190 63 37 VAL C C 178.7 0.2 1 191 63 37 VAL CA C 67.7 0.2 1 192 63 37 VAL CB C 31.6 0.2 1 193 63 37 VAL N N 121.7 0.2 1 194 64 38 LEU H H 8.74 0.02 1 195 64 38 LEU C C 179.4 0.2 1 196 64 38 LEU CA C 58.1 0.2 1 197 64 38 LEU CB C 40.0 0.2 1 198 64 38 LEU N N 118.1 0.2 1 199 65 39 ASN H H 7.77 0.02 1 200 65 39 ASN HB2 H 3.02 0.02 2 201 65 39 ASN HB3 H 2.79 0.02 2 202 65 39 ASN HD21 H 7.68 0.02 2 203 65 39 ASN HD22 H 7.17 0.02 2 204 65 39 ASN C C 175.5 0.2 1 205 65 39 ASN CA C 53.3 0.2 1 206 65 39 ASN N N 115.9 0.2 1 207 65 39 ASN ND2 N 113.6 0.2 1 208 66 40 SER H H 7.67 0.02 1 209 66 40 SER HA H 4.91 0.02 1 210 66 40 SER CA C 60.6 0.2 1 211 66 40 SER CB C 64.6 0.2 1 212 66 40 SER N N 117.7 0.2 1 213 71 45 LEU CB C 43.1 0.2 1 214 73 47 GLY H H 8.46 0.02 1 215 73 47 GLY CA C 44.8 0.2 1 216 73 47 GLY N N 108.9 0.2 1 217 83 57 ALA C C 177.9 0.2 1 218 83 57 ALA CB C 17.3 0.2 1 219 84 58 ILE H H 7.87 0.02 1 220 84 58 ILE C C 176.7 0.2 1 221 84 58 ILE CA C 66.3 0.2 1 222 84 58 ILE N N 115.3 0.2 1 223 85 59 GLY H H 7.15 0.02 1 224 85 59 GLY C C 175.4 0.2 1 225 85 59 GLY CA C 47.1 0.2 1 226 85 59 GLY N N 105.5 0.2 1 227 86 60 LEU H H 8.37 0.02 1 228 86 60 LEU HA H 4.61 0.02 1 229 86 60 LEU C C 177.9 0.2 1 230 86 60 LEU CA C 57.9 0.2 1 231 86 60 LEU CB C 39.3 0.2 1 232 86 60 LEU N N 120.9 0.2 1 233 87 61 ILE H H 7.63 0.02 1 234 87 61 ILE C C 178.4 0.2 1 235 87 61 ILE CA C 65.4 0.2 1 236 87 61 ILE N N 117.8 0.2 1 237 88 62 GLU H H 8.04 0.02 1 238 88 62 GLU HA H 4.35 0.02 1 239 88 62 GLU C C 178.3 0.2 1 240 88 62 GLU CA C 59.6 0.2 1 241 88 62 GLU CB C 28.4 0.2 1 242 88 62 GLU N N 122.0 0.2 1 243 89 63 ALA H H 8.79 0.02 1 244 89 63 ALA HA H 4.46 0.02 1 245 89 63 ALA C C 179.7 0.2 1 246 89 63 ALA CA C 55.7 0.2 1 247 89 63 ALA CB C 18.1 0.2 1 248 89 63 ALA N N 119.8 0.2 1 249 90 64 PHE H H 8.30 0.02 1 250 90 64 PHE HA H 3.70 0.02 1 251 90 64 PHE C C 178.2 0.2 1 252 90 64 PHE CA C 62.4 0.2 1 253 90 64 PHE CB C 40.5 0.2 1 254 90 64 PHE N N 117.7 0.2 1 255 91 65 CYS H H 8.46 0.02 1 256 91 65 CYS HA H 3.65 0.02 1 257 91 65 CYS C C 177.4 0.2 1 258 91 65 CYS CA C 64.7 0.2 1 259 91 65 CYS CB C 27.6 0.2 1 260 91 65 CYS N N 115.7 0.2 1 261 92 66 ARG H H 8.31 0.02 1 262 92 66 ARG HA H 3.70 0.02 1 263 92 66 ARG C C 179.6 0.2 1 264 92 66 ARG CA C 59.4 0.2 1 265 92 66 ARG CB C 30.3 0.2 1 266 92 66 ARG N N 117.9 0.2 1 267 93 67 GLU H H 7.45 0.02 1 268 93 67 GLU C C 176.0 0.2 1 269 93 67 GLU CA C 57.2 0.2 1 270 93 67 GLU CB C 28.8 0.2 1 271 93 67 GLU N N 118.8 0.2 1 272 94 68 ARG H H 7.24 0.02 1 273 94 68 ARG HA H 3.74 0.02 1 274 94 68 ARG C C 176.3 0.2 1 275 94 68 ARG CA C 57.2 0.2 1 276 94 68 ARG CB C 31.3 0.2 1 277 94 68 ARG N N 113.4 0.2 1 278 95 69 VAL H H 6.87 0.02 1 279 95 69 VAL HA H 3.59 0.02 1 280 95 69 VAL HB H 2.05 0.02 1 281 95 69 VAL C C 176.7 0.2 1 282 95 69 VAL CA C 66.2 0.2 1 283 95 69 VAL CB C 31.6 0.2 1 284 95 69 VAL N N 118.8 0.2 1 285 96 70 ILE H H 7.43 0.02 1 286 96 70 ILE HA H 4.40 0.02 1 287 96 70 ILE HB H 1.84 0.02 1 288 96 70 ILE C C 172.3 0.2 1 289 96 70 ILE CA C 58.4 0.2 1 290 96 70 ILE CB C 37.9 0.2 1 291 96 70 ILE N N 118.4 0.2 1 292 98 72 PRO CA C 62.9 0.2 1 293 99 73 THR H H 7.76 0.02 1 294 99 73 THR C C 174.8 0.2 1 295 99 73 THR CA C 61.7 0.2 1 296 99 73 THR CB C 69.2 0.2 1 297 99 73 THR CG2 C 21.8 0.2 1 298 99 73 THR N N 116.6 0.2 1 299 100 74 SER H H 7.75 0.02 1 300 100 74 SER HB2 H 4.18 0.02 2 301 100 74 SER HB3 H 4.02 0.02 2 302 100 74 SER C C 173.5 0.2 1 303 100 74 SER CA C 56.8 0.2 1 304 100 74 SER CB C 64.3 0.2 1 305 100 74 SER N N 116.7 0.2 1 306 101 75 ASN C C 173.5 0.2 1 307 101 75 ASN CA C 54.2 0.2 1 308 101 75 ASN CB C 38.6 0.2 1 309 102 76 SER H H 7.96 0.02 1 310 102 76 SER HA H 5.75 0.02 1 311 102 76 SER HB2 H 3.79 0.02 2 312 102 76 SER HB3 H 3.79 0.02 2 313 102 76 SER C C 172.8 0.2 1 314 102 76 SER CA C 56.6 0.2 1 315 102 76 SER CB C 67.2 0.2 1 316 102 76 SER N N 112.7 0.2 1 317 103 77 PHE H H 8.38 0.02 1 318 103 77 PHE HA H 4.95 0.02 1 319 103 77 PHE C C 172.2 0.2 1 320 103 77 PHE CA C 57.0 0.2 1 321 103 77 PHE CB C 42.2 0.2 1 322 103 77 PHE N N 114.5 0.2 1 323 104 78 ASN H H 8.70 0.02 1 324 104 78 ASN HA H 5.73 0.02 1 325 104 78 ASN HB2 H 2.73 0.02 2 326 104 78 ASN HB3 H 2.73 0.02 2 327 104 78 ASN HD21 H 7.80 0.02 2 328 104 78 ASN HD22 H 7.11 0.02 2 329 104 78 ASN C C 173.7 0.2 1 330 104 78 ASN CA C 52.8 0.2 1 331 104 78 ASN CB C 42.0 0.2 1 332 104 78 ASN N N 118.1 0.2 1 333 104 78 ASN ND2 N 113.4 0.2 1 334 105 79 THR H H 9.48 0.02 1 335 105 79 THR HA H 4.93 0.02 1 336 105 79 THR C C 171.6 0.2 1 337 105 79 THR CA C 60.8 0.2 1 338 105 79 THR CB C 69.6 0.2 1 339 105 79 THR N N 118.5 0.2 1 340 106 80 SER H H 8.19 0.02 1 341 106 80 SER HA H 5.74 0.02 1 342 106 80 SER HB2 H 3.94 0.02 2 343 106 80 SER HB3 H 3.94 0.02 2 344 106 80 SER C C 173.5 0.2 1 345 106 80 SER CA C 56.7 0.2 1 346 106 80 SER CB C 65.6 0.2 1 347 106 80 SER N N 118.7 0.2 1 348 107 81 VAL H H 9.47 0.02 1 349 107 81 VAL HA H 4.70 0.02 1 350 107 81 VAL C C 174.5 0.2 1 351 107 81 VAL CA C 61.8 0.2 1 352 107 81 VAL CB C 35.8 0.2 1 353 107 81 VAL N N 123.0 0.2 1 354 108 82 THR H H 8.57 0.02 1 355 108 82 THR HA H 5.57 0.02 1 356 108 82 THR C C 176.7 0.2 1 357 108 82 THR CA C 61.8 0.2 1 358 108 82 THR CB C 70.4 0.2 1 359 108 82 THR N N 123.3 0.2 1 360 109 83 TYR H H 9.01 0.02 1 361 109 83 TYR HA H 5.34 0.02 1 362 109 83 TYR C C 172.6 0.2 1 363 109 83 TYR CA C 56.1 0.2 1 364 109 83 TYR CB C 38.9 0.2 1 365 109 83 TYR N N 124.5 0.2 1 366 110 84 HIS H H 8.68 0.02 1 367 110 84 HIS HA H 5.73 0.02 1 368 110 84 HIS C C 173.2 0.2 1 369 110 84 HIS CA C 55.5 0.2 1 370 110 84 HIS CB C 34.6 0.2 1 371 110 84 HIS N N 116.7 0.2 1 372 111 85 ILE H H 8.37 0.02 1 373 111 85 ILE HA H 4.62 0.02 1 374 111 85 ILE CA C 59.0 0.2 1 375 111 85 ILE CB C 41.1 0.2 1 376 111 85 ILE N N 120.3 0.2 1 377 120 94 ASP C C 175.0 0.2 1 378 120 94 ASP CA C 53.5 0.2 1 379 120 94 ASP CB C 41.3 0.2 1 380 121 95 LEU H H 8.52 0.02 1 381 121 95 LEU C C 175.6 0.2 1 382 121 95 LEU CA C 52.2 0.2 1 383 121 95 LEU CB C 38.7 0.2 1 384 121 95 LEU N N 122.6 0.2 1 385 122 96 GLY H H 8.08 0.02 1 386 122 96 GLY C C 170.3 0.2 1 387 122 96 GLY CA C 45.4 . 1 388 122 96 GLY N N 106.1 0.2 1 389 123 97 ASN H H 6.50 0.02 1 390 123 97 ASN HA H 4.02 0.02 1 391 123 97 ASN HB2 H 2.26 0.02 2 392 123 97 ASN C C 177.0 0.2 1 393 123 97 ASN CA C 57.1 0.2 1 394 123 97 ASN CB C 35.7 0.2 1 395 123 97 ASN N N 114.8 0.2 1 396 125 99 GLN C C 174.8 0.2 1 397 125 99 GLN CA C 52.4 0.2 1 398 125 99 GLN CB C 29.7 0.2 1 399 126 100 LEU H H 8.14 0.02 1 400 126 100 LEU HA H 5.27 0.02 1 401 126 100 LEU HB2 H 1.60 0.02 1 402 126 100 LEU C C 176.1 0.2 1 403 126 100 LEU CA C 54.9 0.2 1 404 126 100 LEU CB C 42.8 0.2 1 405 126 100 LEU N N 124.6 0.2 1 406 127 101 ILE H H 8.81 0.02 1 407 127 101 ILE HA H 4.35 0.02 1 408 127 101 ILE C C 173.7 0.2 1 409 127 101 ILE CA C 61.2 0.2 1 410 127 101 ILE CB C 41.9 0.2 1 411 127 101 ILE N N 124.1 0.2 1 412 128 102 ASN H H 8.50 0.02 1 413 128 102 ASN HA H 5.23 0.02 1 414 128 102 ASN HB2 H 2.67 0.02 2 415 128 102 ASN HD21 H 8.10 0.02 2 416 128 102 ASN HD22 H 7.12 0.02 2 417 128 102 ASN C C 173.7 0.2 1 418 128 102 ASN CA C 52.5 0.2 1 419 128 102 ASN CB C 40.1 0.2 1 420 128 102 ASN N N 126.4 0.2 1 421 128 102 ASN ND2 N 114.1 0.2 1 422 129 103 LYS H H 7.22 0.02 1 423 129 103 LYS HA H 4.81 0.02 1 424 129 103 LYS C C 172.5 0.2 1 425 129 103 LYS CA C 54.4 0.2 1 426 129 103 LYS CB C 38.1 0.2 1 427 129 103 LYS N N 123.0 0.2 1 428 130 104 PRO C C 175.5 0.2 1 429 130 104 PRO CA C 61.7 0.2 1 430 130 104 PRO CB C 32.4 0.2 1 431 131 105 LEU H H 8.27 0.02 1 432 131 105 LEU HA H 4.65 0.02 1 433 131 105 LEU C C 174.7 0.2 1 434 131 105 LEU CA C 53.4 0.2 1 435 131 105 LEU CB C 43.4 0.2 1 436 131 105 LEU N N 119.9 0.2 1 437 132 106 LEU H H 8.53 0.02 1 438 132 106 LEU HA H 5.24 0.02 1 439 132 106 LEU C C 177.6 0.2 1 440 132 106 LEU CA C 53.1 0.2 1 441 132 106 LEU CB C 43.9 0.2 1 442 132 106 LEU N N 124.2 0.2 1 443 133 107 SER H H 8.83 0.02 1 444 133 107 SER HA H 5.67 0.02 1 445 133 107 SER HB2 H 4.29 0.02 2 446 133 107 SER HB3 H 3.94 0.02 2 447 133 107 SER C C 175.1 0.2 1 448 133 107 SER CA C 58.1 0.2 1 449 133 107 SER CB C 63.9 0.2 1 450 133 107 SER N N 116.0 0.2 1 451 134 108 LEU H H 8.77 0.02 1 452 134 108 LEU HA H 4.46 0.02 1 453 134 108 LEU C C 177.7 0.2 1 454 134 108 LEU CA C 55.2 0.2 1 455 134 108 LEU CB C 42.3 0.2 1 456 134 108 LEU N N 122.2 0.2 1 457 135 109 GLU H H 8.02 0.02 1 458 135 109 GLU HA H 4.42 0.02 1 459 135 109 GLU HB2 H 2.22 0.02 2 460 135 109 GLU HB3 H 1.98 0.02 2 461 135 109 GLU C C 176.1 0.2 1 462 135 109 GLU CA C 56.3 0.2 1 463 135 109 GLU CB C 30.7 0.2 1 464 135 109 GLU N N 117.1 0.2 1 465 136 110 GLY H H 8.35 0.02 1 466 136 110 GLY C C 174.0 0.2 1 467 136 110 GLY CA C 45.4 0.2 1 468 136 110 GLY N N 108.2 0.2 1 469 137 111 ASP H H 8.43 0.02 1 470 137 111 ASP HA H 4.46 0.02 1 471 137 111 ASP C C 176.0 0.2 1 472 137 111 ASP CA C 54.1 0.2 1 473 137 111 ASP CB C 40.4 0.2 1 474 137 111 ASP N N 119.9 0.2 1 475 138 112 LEU H H 8.60 0.02 1 476 138 112 LEU HA H 3.97 0.02 1 477 138 112 LEU C C 175.9 0.2 1 478 138 112 LEU CA C 55.9 0.2 1 479 138 112 LEU CB C 40.3 0.2 1 480 138 112 LEU CD1 C 25.1 0.2 1 481 138 112 LEU CD2 C 24.0 0.2 1 482 138 112 LEU N N 120.0 0.2 1 483 139 113 LYS H H 8.05 0.02 1 484 139 113 LYS HA H 4.35 0.02 1 485 139 113 LYS C C 175.6 0.2 1 486 139 113 LYS CA C 55.9 0.2 1 487 139 113 LYS CB C 34.3 0.2 1 488 139 113 LYS N N 121.6 0.2 1 489 140 114 VAL H H 8.60 0.02 1 490 140 114 VAL HA H 4.27 0.02 1 491 140 114 VAL HB H 2.06 0.02 1 492 140 114 VAL C C 176.7 0.2 1 493 140 114 VAL CA C 63.3 0.2 1 494 140 114 VAL CB C 31.9 0.2 1 495 140 114 VAL N N 123.1 0.2 1 496 141 115 LEU H H 9.26 0.02 1 497 141 115 LEU HA H 4.54 0.02 1 498 141 115 LEU C C 176.8 0.2 1 499 141 115 LEU CA C 54.8 0.2 1 500 141 115 LEU CB C 42.8 0.2 1 501 141 115 LEU N N 126.9 0.2 1 502 142 116 GLY H H 7.61 0.02 1 503 142 116 GLY C C 172.6 0.2 1 504 142 116 GLY CA C 45.5 0.2 1 505 142 116 GLY N N 104.5 0.2 1 506 143 117 SER H H 9.55 0.02 1 507 143 117 SER HA H 5.04 0.02 1 508 143 117 SER C C 170.6 0.2 1 509 143 117 SER CA C 58.4 0.2 1 510 143 117 SER CB C 65.5 0.2 1 511 143 117 SER N N 118.9 0.2 1 512 144 118 TYR H H 8.83 0.02 1 513 144 118 TYR HA H 5.67 0.02 1 514 144 118 TYR C C 173.4 0.2 1 515 144 118 TYR CA C 56.2 0.2 1 516 144 118 TYR CB C 42.6 0.2 1 517 144 118 TYR N N 115.5 0.2 1 518 145 119 GLN H H 8.96 0.02 1 519 145 119 GLN HA H 5.18 0.02 1 520 145 119 GLN HB2 H 1.97 0.02 1 521 145 119 GLN HE21 H 7.23 0.02 2 522 145 119 GLN HE22 H 6.68 0.02 2 523 145 119 GLN C C 174.3 0.2 1 524 145 119 GLN CA C 55.1 0.2 1 525 145 119 GLN CB C 32.4 0.2 1 526 145 119 GLN N N 118.9 0.2 1 527 145 119 GLN NE2 N 111.1 0.2 1 528 146 120 LEU H H 9.63 0.02 1 529 146 120 LEU HA H 5.74 0.02 1 530 146 120 LEU C C 175.7 0.2 1 531 146 120 LEU CA C 53.8 0.2 1 532 146 120 LEU CB C 47.0 0.2 1 533 146 120 LEU N N 125.8 0.2 1 534 147 121 THR H H 9.19 0.02 1 535 147 121 THR HA H 5.39 0.02 1 536 147 121 THR HB H 4.11 0.02 1 537 147 121 THR C C 173.5 0.2 1 538 147 121 THR CA C 61.9 0.2 1 539 147 121 THR CB C 70.6 0.2 1 540 147 121 THR N N 120.5 0.2 1 541 148 122 PHE H H 9.20 0.02 1 542 148 122 PHE HA H 5.84 0.02 1 543 148 122 PHE C C 172.1 0.2 1 544 148 122 PHE CA C 56.0 0.2 1 545 148 122 PHE CB C 43.1 0.2 1 546 148 122 PHE N N 126.6 0.2 1 547 149 123 GLN H H 8.77 0.02 1 548 149 123 GLN HA H 5.30 0.02 1 549 149 123 GLN C C 173.6 0.2 1 550 149 123 GLN CA C 53.5 0.2 1 551 149 123 GLN CB C 32.0 0.2 1 552 149 123 GLN N N 128.2 0.2 1 553 150 124 THR H H 8.50 0.02 1 554 150 124 THR HA H 4.99 0.02 1 555 150 124 THR CA C 58.3 0.2 1 556 150 124 THR CB C 70.4 0.2 1 557 150 124 THR N N 114.4 0.2 1 558 151 125 ILE H H 8.89 0.02 1 559 151 125 ILE HA H 4.57 0.02 1 560 151 125 ILE CA C 58.9 0.2 1 561 151 125 ILE CB C 41.1 0.2 1 562 151 125 ILE N N 121.1 0.2 1 563 152 126 PRO C C 177.5 0.2 1 564 152 126 PRO CA C 63.5 0.2 1 565 152 126 PRO CB C 32.3 0.2 1 566 153 127 GLY H H 8.58 0.02 1 567 153 127 GLY C C 173.7 0.2 1 568 153 127 GLY CA C 45.7 0.2 1 569 153 127 GLY N N 109.3 0.2 1 570 166 140 TYR C C 178.7 0.2 1 571 166 140 TYR CB C 39.0 0.2 1 572 167 141 HIS H H 9.66 0.02 1 573 167 141 HIS HA H 4.70 0.02 1 574 167 141 HIS C C 176.2 0.2 1 575 167 141 HIS CA C 57.1 0.2 1 576 167 141 HIS N N 120.6 0.2 1 577 168 142 SER H H 7.86 0.02 1 578 168 142 SER C C 173.6 0.2 1 579 168 142 SER CA C 60.6 0.2 1 580 168 142 SER CB C 62.3 0.2 1 581 168 142 SER N N 116.3 0.2 1 582 169 143 ASP H H 8.16 0.02 1 583 169 143 ASP HA H 4.62 0.02 1 584 169 143 ASP HB2 H 2.64 0.02 2 585 169 143 ASP HB3 H 2.52 0.02 2 586 169 143 ASP C C 176.6 0.2 1 587 169 143 ASP CA C 53.9 0.2 1 588 169 143 ASP CB C 40.5 0.2 1 589 169 143 ASP N N 117.9 0.2 1 590 170 144 SER H H 8.07 0.02 1 591 170 144 SER C C 174.0 0.2 1 592 170 144 SER CA C 56.4 0.2 1 593 170 144 SER CB C 64.6 0.2 1 594 170 144 SER N N 117.0 0.2 1 595 171 145 PRO C C 178.1 0.2 1 596 171 145 PRO CA C 65.5 0.2 1 597 172 146 PHE H H 8.24 0.02 1 598 172 146 PHE C C 177.9 0.2 1 599 172 146 PHE CA C 61.7 0.2 1 600 172 146 PHE CB C 39.7 0.2 1 601 172 146 PHE N N 116.7 0.2 1 602 173 147 PHE H H 7.45 0.02 1 603 173 147 PHE HA H 3.76 0.02 1 604 173 147 PHE C C 177.9 0.2 1 605 173 147 PHE CA C 58.6 0.2 1 606 173 147 PHE CB C 40.0 0.2 1 607 173 147 PHE N N 119.0 0.2 1 608 174 148 GLN H H 8.45 0.02 1 609 174 148 GLN HE21 H 7.50 0.02 2 610 174 148 GLN HE22 H 6.70 0.02 2 611 174 148 GLN C C 179.6 0.2 1 612 174 148 GLN CA C 59.3 0.2 1 613 174 148 GLN CB C 28.2 0.2 1 614 174 148 GLN N N 116.3 0.2 1 615 174 148 GLN NE2 N 111.7 0.2 1 616 175 149 ILE H H 8.73 0.02 1 617 175 149 ILE HA H 3.79 0.02 1 618 175 149 ILE CA C 64.3 0.2 1 619 175 149 ILE CB C 37.4 0.2 1 620 175 149 ILE N N 121.5 0.2 1 621 176 150 ALA H H 7.04 0.02 1 622 176 150 ALA HA H 3.92 0.02 1 623 176 150 ALA HB H 1.02 0.02 1 624 176 150 ALA C C 178.2 0.2 1 625 176 150 ALA CA C 54.9 0.2 1 626 176 150 ALA CB C 19.0 0.2 1 627 176 150 ALA N N 122.9 0.2 1 628 177 151 LEU H H 8.97 0.02 1 629 177 151 LEU C C 179.0 0.2 1 630 177 151 LEU CA C 57.4 0.2 1 631 177 151 LEU CB C 42.0 0.2 1 632 177 151 LEU N N 120.4 0.2 1 633 178 152 GLY H H 7.88 0.02 1 634 178 152 GLY HA2 H 3.89 0.02 2 635 178 152 GLY HA3 H 3.77 0.02 2 636 178 152 GLY C C 176.3 0.2 1 637 178 152 GLY CA C 46.8 0.2 1 638 178 152 GLY N N 104.4 0.2 1 639 179 153 HIS H H 7.02 0.02 1 640 179 153 HIS HA H 4.40 0.02 1 641 179 153 HIS C C 177.0 0.2 1 642 179 153 HIS CA C 59.1 0.2 1 643 179 153 HIS CB C 30.9 0.2 1 644 179 153 HIS N N 119.1 0.2 1 645 180 154 ALA H H 8.02 0.02 1 646 180 154 ALA HA H 3.71 0.02 1 647 180 154 ALA C C 177.7 0.2 1 648 180 154 ALA CA C 54.6 0.2 1 649 180 154 ALA CB C 18.9 0.2 1 650 180 154 ALA N N 119.5 0.2 1 651 181 155 LEU H H 7.99 0.02 1 652 181 155 LEU HA H 4.28 0.02 1 653 181 155 LEU C C 179.1 0.2 1 654 181 155 LEU CA C 54.4 0.2 1 655 181 155 LEU CB C 41.0 0.2 1 656 181 155 LEU N N 110.1 0.2 1 657 182 156 LEU H H 7.13 0.02 1 658 182 156 LEU C C 178.7 0.2 1 659 182 156 LEU CA C 57.5 0.2 1 660 182 156 LEU CB C 41.7 0.2 1 661 182 156 LEU N N 125.3 0.2 1 662 183 157 GLY C C 175.4 0.2 1 663 183 157 GLY CA C 46.0 0.2 1 664 184 158 THR H H 8.12 0.02 1 665 184 158 THR HA H 4.27 0.02 1 666 184 158 THR C C 177.0 0.2 1 667 184 158 THR CA C 63.3 0.2 1 668 184 158 THR CB C 71.8 0.2 1 669 184 158 THR N N 109.1 0.2 1 670 185 159 GLY C C 174.0 0.2 1 671 185 159 GLY CA C 46.3 0.2 1 672 186 160 LYS H H 7.96 0.02 1 673 186 160 LYS HA H 5.32 0.02 1 674 186 160 LYS C C 174.8 0.2 1 675 186 160 LYS CA C 54.0 0.2 1 676 186 160 LYS CB C 36.2 0.2 1 677 186 160 LYS N N 118.5 0.2 1 678 187 161 ILE H H 8.94 0.02 1 679 187 161 ILE HA H 4.58 0.02 1 680 187 161 ILE C C 174.7 0.2 1 681 187 161 ILE CA C 59.6 0.2 1 682 187 161 ILE CB C 42.3 0.2 1 683 187 161 ILE N N 113.6 0.2 1 684 188 162 TYR H H 8.38 0.02 1 685 188 162 TYR HA H 5.31 0.02 1 686 188 162 TYR C C 173.4 0.2 1 687 188 162 TYR CA C 56.6 0.2 1 688 188 162 TYR CB C 39.6 0.2 1 689 188 162 TYR N N 121.6 0.2 1 690 189 163 ASP H H 8.82 0.02 1 691 189 163 ASP HA H 4.62 0.02 1 692 189 163 ASP C C 175.0 0.2 1 693 189 163 ASP CA C 51.3 0.2 1 694 189 163 ASP CB C 42.1 0.2 1 695 189 163 ASP N N 129.0 0.2 1 696 190 164 HIS H H 8.59 0.02 1 697 190 164 HIS C C 177.1 0.2 1 698 190 164 HIS CA C 59.1 0.2 1 699 190 164 HIS CB C 31.0 0.2 1 700 190 164 HIS N N 124.6 0.2 1 701 191 165 ILE H H 7.78 0.02 1 702 191 165 ILE HA H 3.06 0.02 1 703 191 165 ILE HB H 2.15 0.02 1 704 191 165 ILE C C 177.8 0.2 1 705 191 165 ILE CA C 64.0 0.2 1 706 191 165 ILE CB C 35.8 0.2 1 707 191 165 ILE N N 117.6 0.2 1 708 192 166 THR H H 6.74 0.02 1 709 192 166 THR HA H 4.18 0.02 1 710 192 166 THR C C 173.2 0.2 1 711 192 166 THR CA C 61.1 0.2 1 712 192 166 THR CB C 68.9 0.2 1 713 192 166 THR N N 106.1 0.2 1 714 193 167 ARG H H 7.69 0.02 1 715 193 167 ARG HA H 3.68 0.02 1 716 193 167 ARG C C 174.1 0.2 1 717 193 167 ARG CA C 56.6 0.2 1 718 193 167 ARG CB C 26.4 0.2 1 719 193 167 ARG N N 119.3 0.2 1 720 194 168 ALA H H 7.51 0.02 1 721 194 168 ALA HA H 5.57 0.02 1 722 194 168 ALA HB H 1.01 0.02 1 723 194 168 ALA C C 175.5 0.2 1 724 194 168 ALA CA C 50.9 0.2 1 725 194 168 ALA CB C 23.9 0.2 1 726 194 168 ALA N N 117.6 0.2 1 727 195 169 LEU H H 8.81 0.02 1 728 195 169 LEU HA H 5.29 0.02 1 729 195 169 LEU CA C 53.7 0.2 1 730 195 169 LEU CB C 43.6 0.2 1 731 195 169 LEU N N 123.3 0.2 1 732 196 170 ARG H H 9.07 0.02 1 733 196 170 ARG HA H 5.13 0.02 1 734 196 170 ARG C C 174.9 0.2 1 735 196 170 ARG CA C 54.1 0.2 1 736 196 170 ARG CB C 33.5 0.2 1 737 196 170 ARG N N 124.9 0.2 1 738 197 171 VAL H H 9.79 0.02 1 739 197 171 VAL HA H 4.07 0.02 1 740 197 171 VAL C C 176.1 0.2 1 741 197 171 VAL CA C 63.3 0.2 1 742 197 171 VAL CB C 31.8 0.2 1 743 197 171 VAL N N 120.8 0.2 1 744 198 172 ALA H H 8.45 0.02 1 745 198 172 ALA HA H 4.38 0.02 1 746 198 172 ALA HB H 1.20 0.02 1 747 198 172 ALA C C 174.9 0.2 1 748 198 172 ALA CA C 50.4 0.2 1 749 198 172 ALA CB C 18.1 0.2 1 750 198 172 ALA N N 130.3 0.2 1 751 199 173 PRO C C 176.6 0.2 1 752 199 173 PRO CA C 62.7 0.2 1 753 199 173 PRO CB C 32.0 0.2 1 754 199 173 PRO CG C 27.2 0.2 1 755 199 173 PRO CD C 50.5 0.2 1 756 200 174 ILE H H 8.33 0.02 1 757 200 174 ILE HA H 4.19 0.02 1 758 200 174 ILE HB H 1.85 0.02 1 759 200 174 ILE HD1 H 0.92 0.2 1 760 200 174 ILE C C 176.4 0.2 1 761 200 174 ILE CA C 61.2 0.2 1 762 200 174 ILE CB C 38.8 0.2 1 763 200 174 ILE CG2 C 17.5 0.2 1 764 200 174 ILE CD1 C 12.9 0.02 1 765 200 174 ILE N N 121.4 0.2 1 766 201 175 THR H H 8.33 0.02 1 767 201 175 THR HA H 4.39 0.02 1 768 201 175 THR HB H 4.14 0.02 1 769 201 175 THR HG2 H 1.17 0.02 1 770 201 175 THR C C 173.9 0.2 1 771 201 175 THR CA C 61.6 0.2 1 772 201 175 THR CB C 69.9 0.2 1 773 201 175 THR CG2 C 21.6 0.2 1 774 201 175 THR N N 119.7 0.2 1 775 202 176 ILE H H 8.32 0.02 1 776 202 176 ILE HA H 4.20 0.02 1 777 202 176 ILE HB H 1.89 0.02 1 778 202 176 ILE HD1 H 0.94 0.02 1 779 202 176 ILE C C 174.7 0.2 1 780 202 176 ILE CA C 61.0 0.2 1 781 202 176 ILE CB C 38.8 0.2 1 782 202 176 ILE CG1 C 26.9 0.2 1 783 202 176 ILE CG2 C 17.5 0.2 1 784 202 176 ILE CD1 C 12.7 0.2 1 785 202 176 ILE N N 124.5 0.2 1 786 203 177 ALA H H 8.03 0.02 1 787 203 177 ALA HA H 4.14 0.02 1 788 203 177 ALA HB H 1.34 0.02 1 789 203 177 ALA C C 182.2 0.2 1 790 203 177 ALA CA C 53.9 0.2 1 791 203 177 ALA CB C 20.2 0.2 1 792 203 177 ALA N N 133.9 0.2 1 stop_ save_