data_50099 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Nipah virus phosphoprotein residues 91-190 ; _BMRB_accession_number 50099 _BMRB_flat_file_name bmr50099.str _Entry_type original _Submission_date 2019-11-29 _Accession_date 2019-11-29 _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 Jensen Malene . . 2 Blackledge Martin . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 93 "13C chemical shifts" 283 "15N chemical shifts" 93 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-05-29 update BMRB 'update entry citation' 2020-01-10 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 50098 'Nipah virus phosphoprotein residues 1-100' 50100 'Nipah virus phosphoprotein residues 173-240' 50101 'Nipah virus phosphoprotein residues 223-319' 50102 'Nipah virus phosphoprotein residues 299-401' 50103 'Nipah virus phosphoprotein residues 387-479' 50105 'Nipah virus phosphoprotein residues 588-650' stop_ _Original_release_date 2019-12-02 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural Description of the Nipah Virus Phosphoprotein and Its Interaction With STAT1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32348724 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jensen 'Malene Ringkjybing' R. . 2 Yabukarski Filip . . 3 Communie Guillaume . . 4 Condamine Eric . . 5 Mas Caroline . . 6 Volchkova Valentina . . 7 Tarbouriech Nicolas . . 8 Bourhis Jean-Marie M. . 9 Volchkov Viktor . . 10 Blackledge Martin . . 11 Jamin Marc . . stop_ _Journal_abbreviation 'Biophys. J.' _Journal_name_full 'Biophysical journal' _Journal_volume 118 _Journal_issue 10 _Journal_ISSN 1542-0086 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2470 _Page_last 2488 _Year 2020 _Details . save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name 'Nipah virus phosphoprotein, residues 91-190' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Nipah virus phosphoprotein' $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 'Nipah virus phosphoprotein, residues 91-190' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 109 _Mol_residue_sequence ; MRVSNTRDWAEGSDDIQLDP VVTDVVYHDHGGECTGYGFT SSPERGWSDYTSGANNGNVC LVSDAKMLSYAPEIAVSKED RETDLVHLENKLSTTGLNPT ALEHHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 90 MET 2 91 ARG 3 92 VAL 4 93 SER 5 94 ASN 6 95 THR 7 96 ARG 8 97 ASP 9 98 TRP 10 99 ALA 11 100 GLU 12 101 GLY 13 102 SER 14 103 ASP 15 104 ASP 16 105 ILE 17 106 GLN 18 107 LEU 19 108 ASP 20 109 PRO 21 110 VAL 22 111 VAL 23 112 THR 24 113 ASP 25 114 VAL 26 115 VAL 27 116 TYR 28 117 HIS 29 118 ASP 30 119 HIS 31 120 GLY 32 121 GLY 33 122 GLU 34 123 CYS 35 124 THR 36 125 GLY 37 126 TYR 38 127 GLY 39 128 PHE 40 129 THR 41 130 SER 42 131 SER 43 132 PRO 44 133 GLU 45 134 ARG 46 135 GLY 47 136 TRP 48 137 SER 49 138 ASP 50 139 TYR 51 140 THR 52 141 SER 53 142 GLY 54 143 ALA 55 144 ASN 56 145 ASN 57 146 GLY 58 147 ASN 59 148 VAL 60 149 CYS 61 150 LEU 62 151 VAL 63 152 SER 64 153 ASP 65 154 ALA 66 155 LYS 67 156 MET 68 157 LEU 69 158 SER 70 159 TYR 71 160 ALA 72 161 PRO 73 162 GLU 74 163 ILE 75 164 ALA 76 165 VAL 77 166 SER 78 167 LYS 79 168 GLU 80 169 ASP 81 170 ARG 82 171 GLU 83 172 THR 84 173 ASP 85 174 LEU 86 175 VAL 87 176 HIS 88 177 LEU 89 178 GLU 90 179 ASN 91 180 LYS 92 181 LEU 93 182 SER 94 183 THR 95 184 THR 96 185 GLY 97 186 LEU 98 187 ASN 99 188 PRO 100 189 THR 101 190 ALA 102 191 LEU 103 192 GLU 104 193 HIS 105 194 HIS 106 195 HIS 107 196 HIS 108 197 HIS 109 198 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_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 $entity_1 'Nipah virus' 121791 Virus . henipavirus 'Nipah virus' 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' . . . . plasmid pET28 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 0.5 mM '[U-13C; U-15N]' 'Bis-Tris ph 6.0' 20 mM 'natural abundance' NaCl 150 mM 'natural abundance' Arginine 50 mM 'natural abundance' glutamate 50 mM 'natural abundance' TCEP 0.5 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Agilent _Model Unity _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACO' _Sample_label $sample_1 save_ save_3D_HNCOCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCOCA' _Sample_label $sample_1 save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCOCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCOCACB' _Sample_label $sample_1 save_ save_3D_HNCACB_7 _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' 150 . mM pH 6.0 . 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 water C 13 protons ppm 4.774 internal indirect . . . 0.251449530 water H 1 protons ppm 4.774 internal direct . . . 1 water N 15 protons ppm 4.774 internal 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_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCACO' '3D HNCOCA' '3D HNCA' '3D HNCOCACB' '3D HNCACB' 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 'Nipah virus phosphoprotein' _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 93 4 SER C C 174.190 . 1 2 93 4 SER CA C 58.140 . 1 3 93 4 SER CB C 63.960 . 1 4 94 5 ASN H H 8.550 . 1 5 94 5 ASN C C 175.390 . 1 6 94 5 ASN CA C 53.300 . 1 7 94 5 ASN CB C 38.990 . 1 8 94 5 ASN N N 121.440 . 1 9 95 6 THR H H 8.140 . 1 10 95 6 THR C C 174.530 . 1 11 95 6 THR CA C 62.060 . 1 12 95 6 THR CB C 69.790 . 1 13 95 6 THR N N 114.170 . 1 14 96 7 ARG H H 8.290 . 1 15 96 7 ARG C C 175.890 . 1 16 96 7 ARG CA C 56.170 . 1 17 96 7 ARG CB C 30.600 . 1 18 96 7 ARG N N 122.960 . 1 19 97 8 ASP H H 8.270 . 1 20 97 8 ASP C C 175.910 . 1 21 97 8 ASP CA C 54.410 . 1 22 97 8 ASP CB C 41.040 . 1 23 97 8 ASP N N 121.450 . 1 24 98 9 TRP H H 7.960 . 1 25 98 9 TRP C C 175.840 . 1 26 98 9 TRP CA C 57.430 . 1 27 98 9 TRP CB C 29.490 . 1 28 98 9 TRP N N 121.530 . 1 29 99 10 ALA H H 8.000 . 1 30 99 10 ALA C C 177.300 . 1 31 99 10 ALA CA C 52.350 . 1 32 99 10 ALA CB C 19.470 . 1 33 99 10 ALA N N 125.490 . 1 34 100 11 GLU H H 8.130 . 1 35 100 11 GLU C C 177.060 . 1 36 100 11 GLU CA C 56.910 . 1 37 100 11 GLU CB C 30.080 . 1 38 100 11 GLU N N 120.210 . 1 39 101 12 GLY H H 8.410 . 1 40 101 12 GLY C C 174.310 . 1 41 101 12 GLY CA C 45.390 . 1 42 101 12 GLY N N 110.440 . 1 43 102 13 SER H H 8.130 . 1 44 102 13 SER C C 174.400 . 1 45 102 13 SER CA C 58.430 . 1 46 102 13 SER CB C 64.100 . 1 47 102 13 SER N N 115.410 . 1 48 103 14 ASP H H 8.440 . 1 49 103 14 ASP C C 175.880 . 1 50 103 14 ASP CA C 54.510 . 1 51 103 14 ASP CB C 41.200 . 1 52 103 14 ASP N N 122.080 . 1 53 104 15 ASP H H 8.230 . 1 54 104 15 ASP C C 176.040 . 1 55 104 15 ASP CA C 54.410 . 1 56 104 15 ASP CB C 41.120 . 1 57 104 15 ASP N N 120.270 . 1 58 105 16 ILE H H 7.960 . 1 59 105 16 ILE C C 176.000 . 1 60 105 16 ILE CA C 61.200 . 1 61 105 16 ILE CB C 38.800 . 1 62 105 16 ILE N N 120.850 . 1 63 106 17 GLN H H 8.410 . 1 64 106 17 GLN C C 175.510 . 1 65 106 17 GLN CA C 55.470 . 1 66 106 17 GLN CB C 29.350 . 1 67 106 17 GLN N N 124.700 . 1 68 107 18 LEU H H 8.280 . 1 69 107 18 LEU C C 176.790 . 1 70 107 18 LEU CA C 54.820 . 1 71 107 18 LEU CB C 42.720 . 1 72 107 18 LEU N N 124.480 . 1 73 108 19 ASP H H 8.320 . 1 74 108 19 ASP C C 174.320 . 1 75 108 19 ASP CA C 52.570 . 1 76 108 19 ASP CB C 40.270 . 1 77 108 19 ASP N N 122.770 . 1 78 109 20 PRO C C 176.870 . 1 79 109 20 PRO CA C 63.200 . 1 80 109 20 PRO CB C 32.120 . 1 81 110 21 VAL H H 8.240 . 1 82 110 21 VAL C C 176.450 . 1 83 110 21 VAL CA C 62.710 . 1 84 110 21 VAL CB C 32.490 . 1 85 110 21 VAL N N 120.710 . 1 86 111 22 VAL H H 8.220 . 1 87 111 22 VAL C C 176.260 . 1 88 111 22 VAL CA C 62.350 . 1 89 111 22 VAL CB C 32.670 . 1 90 111 22 VAL N N 124.320 . 1 91 112 23 THR H H 8.170 . 1 92 112 23 THR C C 174.070 . 1 93 112 23 THR CA C 61.680 . 1 94 112 23 THR CB C 69.870 . 1 95 112 23 THR N N 117.690 . 1 96 113 24 ASP H H 8.280 . 1 97 113 24 ASP C C 175.920 . 1 98 113 24 ASP CA C 54.390 . 1 99 113 24 ASP CB C 41.190 . 1 100 113 24 ASP N N 123.010 . 1 101 114 25 VAL H H 8.020 . 1 102 114 25 VAL C C 175.760 . 1 103 114 25 VAL CA C 62.510 . 1 104 114 25 VAL CB C 32.710 . 1 105 114 25 VAL N N 120.510 . 1 106 115 26 VAL H H 8.050 . 1 107 115 26 VAL C C 175.460 . 1 108 115 26 VAL CA C 62.160 . 1 109 115 26 VAL CB C 32.790 . 1 110 115 26 VAL N N 123.950 . 1 111 116 27 TYR H H 8.270 . 1 112 116 27 TYR C C 175.410 . 1 113 116 27 TYR CA C 57.930 . 1 114 116 27 TYR CB C 38.980 . 1 115 116 27 TYR N N 124.530 . 1 116 117 28 HIS H H 8.220 . 1 117 117 28 HIS C C 173.830 . 1 118 117 28 HIS CA C 55.190 . 1 119 117 28 HIS CB C 30.120 . 1 120 117 28 HIS N N 121.300 . 1 121 118 29 ASP H H 8.320 . 1 122 118 29 ASP C C 176.110 . 1 123 118 29 ASP CA C 54.380 . 1 124 118 29 ASP CB C 41.240 . 1 125 118 29 ASP N N 121.610 . 1 126 119 30 HIS H H 8.530 . 1 127 119 30 HIS C C 175.320 . 1 128 119 30 HIS CA C 55.840 . 1 129 119 30 HIS CB C 29.060 . 1 130 119 30 HIS N N 119.400 . 1 131 120 31 GLY H H 8.540 . 1 132 120 31 GLY C C 174.750 . 1 133 120 31 GLY CA C 45.670 . 1 134 120 31 GLY N N 109.850 . 1 135 121 32 GLY H H 8.330 . 1 136 121 32 GLY C C 174.290 . 1 137 121 32 GLY CA C 45.290 . 1 138 121 32 GLY N N 109.060 . 1 139 122 33 GLU H H 8.380 . 1 140 122 33 GLU C C 176.650 . 1 141 122 33 GLU CA C 56.730 . 1 142 122 33 GLU CB C 30.210 . 1 143 122 33 GLU N N 120.600 . 1 144 123 34 CYS H H 8.480 . 1 145 123 34 CYS C C 174.880 . 1 146 123 34 CYS CA C 58.580 . 1 147 123 34 CYS CB C 27.820 . 1 148 123 34 CYS N N 120.170 . 1 149 124 35 THR H H 8.190 . 1 150 124 35 THR C C 174.950 . 1 151 124 35 THR CA C 62.100 . 1 152 124 35 THR CB C 69.840 . 1 153 124 35 THR N N 115.970 . 1 154 125 36 GLY H H 8.310 . 1 155 125 36 GLY C C 173.820 . 1 156 125 36 GLY CA C 45.260 . 1 157 125 36 GLY N N 110.880 . 1 158 126 37 TYR H H 8.090 . 1 159 126 37 TYR C C 176.340 . 1 160 126 37 TYR CA C 58.220 . 1 161 126 37 TYR CB C 38.760 . 1 162 126 37 TYR N N 120.100 . 1 163 127 38 GLY H H 8.290 . 1 164 127 38 GLY C C 173.780 . 1 165 127 38 GLY CA C 45.280 . 1 166 127 38 GLY N N 110.490 . 1 167 128 39 PHE H H 8.000 . 1 168 128 39 PHE C C 176.090 . 1 169 128 39 PHE CA C 57.860 . 1 170 128 39 PHE CB C 39.730 . 1 171 128 39 PHE N N 119.860 . 1 172 129 40 THR H H 8.120 . 1 173 129 40 THR C C 174.060 . 1 174 129 40 THR CA C 61.650 . 1 175 129 40 THR CB C 70.020 . 1 176 129 40 THR N N 115.570 . 1 177 130 41 SER H H 8.250 . 1 178 130 41 SER C C 174.010 . 1 179 130 41 SER CA C 58.200 . 1 180 130 41 SER CB C 63.990 . 1 181 130 41 SER N N 118.120 . 1 182 131 42 SER H H 8.290 . 1 183 131 42 SER CA C 56.410 . 1 184 131 42 SER CB C 63.690 . 1 185 131 42 SER N N 118.470 . 1 186 132 43 PRO C C 177.100 . 1 187 132 43 PRO CA C 63.590 . 1 188 132 43 PRO CB C 31.960 . 1 189 133 44 GLU H H 8.430 . 1 190 133 44 GLU C C 176.670 . 1 191 133 44 GLU CA C 56.960 . 1 192 133 44 GLU CB C 29.860 . 1 193 133 44 GLU N N 120.430 . 1 194 134 45 ARG H H 8.190 . 1 195 134 45 ARG C C 176.690 . 1 196 134 45 ARG CA C 56.290 . 1 197 134 45 ARG CB C 30.680 . 1 198 134 45 ARG N N 121.270 . 1 199 135 46 GLY H H 8.330 . 1 200 135 46 GLY C C 173.950 . 1 201 135 46 GLY CA C 45.330 . 1 202 135 46 GLY N N 109.570 . 1 203 136 47 TRP H H 8.020 . 1 204 136 47 TRP C C 176.430 . 1 205 136 47 TRP CA C 57.600 . 1 206 136 47 TRP CB C 29.750 . 1 207 136 47 TRP N N 120.890 . 1 208 137 48 SER H H 8.060 . 1 209 137 48 SER C C 173.790 . 1 210 137 48 SER CA C 58.390 . 1 211 137 48 SER CB C 64.030 . 1 212 137 48 SER N N 116.990 . 1 213 138 49 ASP H H 8.110 . 1 214 138 49 ASP C C 176.130 . 1 215 138 49 ASP CA C 54.390 . 1 216 138 49 ASP CB C 41.180 . 1 217 138 49 ASP N N 121.770 . 1 218 139 50 TYR H H 8.100 . 1 219 139 50 TYR C C 176.310 . 1 220 139 50 TYR CA C 58.420 . 1 221 139 50 TYR CB C 38.600 . 1 222 139 50 TYR N N 120.540 . 1 223 140 51 THR H H 8.030 . 1 224 140 51 THR C C 174.690 . 1 225 140 51 THR CA C 62.090 . 1 226 140 51 THR CB C 69.960 . 1 227 140 51 THR N N 115.020 . 1 228 141 52 SER H H 8.200 . 1 229 141 52 SER C C 175.130 . 1 230 141 52 SER CA C 58.790 . 1 231 141 52 SER CB C 63.850 . 1 232 141 52 SER N N 117.850 . 1 233 142 53 GLY H H 8.320 . 1 234 142 53 GLY C C 174.030 . 1 235 142 53 GLY CA C 45.410 . 1 236 142 53 GLY N N 110.850 . 1 237 143 54 ALA H H 8.090 . 1 238 143 54 ALA C C 177.640 . 1 239 143 54 ALA CA C 52.710 . 1 240 143 54 ALA CB C 19.260 . 1 241 143 54 ALA N N 123.500 . 1 242 144 55 ASN H H 8.410 . 1 243 144 55 ASN C C 175.100 . 1 244 144 55 ASN CA C 53.290 . 1 245 144 55 ASN CB C 38.800 . 1 246 144 55 ASN N N 117.420 . 1 247 145 56 ASN H H 8.320 . 1 248 145 56 ASN C C 175.700 . 1 249 145 56 ASN CA C 53.460 . 1 250 145 56 ASN CB C 38.870 . 1 251 145 56 ASN N N 118.970 . 1 252 146 57 GLY H H 8.370 . 1 253 146 57 GLY C C 173.990 . 1 254 146 57 GLY CA C 45.590 . 1 255 146 57 GLY N N 108.700 . 1 256 147 58 ASN H H 8.250 . 1 257 147 58 ASN C C 175.220 . 1 258 147 58 ASN CA C 53.290 . 1 259 147 58 ASN CB C 38.930 . 1 260 147 58 ASN N N 118.710 . 1 261 148 59 VAL H H 8.050 . 1 262 148 59 VAL C C 175.830 . 1 263 148 59 VAL CA C 62.440 . 1 264 148 59 VAL CB C 32.760 . 1 265 148 59 VAL N N 120.160 . 1 266 149 60 CYS H H 8.440 . 1 267 149 60 CYS C C 174.340 . 1 268 149 60 CYS CA C 58.550 . 1 269 149 60 CYS CB C 27.880 . 1 270 149 60 CYS N N 123.410 . 1 271 150 61 LEU H H 8.390 . 1 272 150 61 LEU C C 177.230 . 1 273 150 61 LEU CA C 55.260 . 1 274 150 61 LEU CB C 42.450 . 1 275 150 61 LEU N N 125.580 . 1 276 151 62 VAL H H 8.110 . 1 277 151 62 VAL C C 176.090 . 1 278 151 62 VAL CA C 62.320 . 1 279 151 62 VAL CB C 32.810 . 1 280 151 62 VAL N N 121.030 . 1 281 152 63 SER H H 8.330 . 1 282 152 63 SER C C 174.320 . 1 283 152 63 SER CA C 58.370 . 1 284 152 63 SER CB C 63.970 . 1 285 152 63 SER N N 119.250 . 1 286 153 64 ASP H H 8.270 . 1 287 153 64 ASP C C 176.260 . 1 288 153 64 ASP CA C 54.440 . 1 289 153 64 ASP CB C 41.270 . 1 290 153 64 ASP N N 122.790 . 1 291 154 65 ALA H H 8.220 . 1 292 154 65 ALA C C 178.240 . 1 293 154 65 ALA CA C 53.260 . 1 294 154 65 ALA CB C 19.040 . 1 295 154 65 ALA N N 124.350 . 1 296 155 66 LYS H H 8.230 . 1 297 155 66 LYS C C 176.960 . 1 298 155 66 LYS CA C 56.780 . 1 299 155 66 LYS CB C 32.590 . 1 300 155 66 LYS N N 119.380 . 1 301 156 67 MET H H 8.140 . 1 302 156 67 MET C C 176.320 . 1 303 156 67 MET CA C 55.670 . 1 304 156 67 MET CB C 32.650 . 1 305 156 67 MET N N 120.210 . 1 306 157 68 LEU H H 8.110 . 1 307 157 68 LEU C C 177.230 . 1 308 157 68 LEU CA C 55.360 . 1 309 157 68 LEU CB C 42.350 . 1 310 157 68 LEU N N 122.770 . 1 311 158 69 SER H H 8.090 . 1 312 158 69 SER C C 173.810 . 1 313 158 69 SER CA C 58.210 . 1 314 158 69 SER CB C 63.930 . 1 315 158 69 SER N N 115.710 . 1 316 159 70 TYR H H 8.030 . 1 317 159 70 TYR C C 174.790 . 1 318 159 70 TYR CA C 57.560 . 1 319 159 70 TYR CB C 39.050 . 1 320 159 70 TYR N N 121.990 . 1 321 160 71 ALA H H 8.100 . 1 322 160 71 ALA C C 174.850 . 1 323 160 71 ALA CA C 50.240 . 1 324 160 71 ALA CB C 18.550 . 1 325 160 71 ALA N N 127.440 . 1 326 161 72 PRO C C 176.910 . 1 327 161 72 PRO CA C 63.150 . 1 328 161 72 PRO CB C 32.030 . 1 329 162 73 GLU H H 8.530 . 1 330 162 73 GLU C C 176.500 . 1 331 162 73 GLU CA C 56.780 . 1 332 162 73 GLU CB C 30.060 . 1 333 162 73 GLU N N 120.680 . 1 334 163 74 ILE H H 8.070 . 1 335 163 74 ILE C C 175.770 . 1 336 163 74 ILE CA C 60.920 . 1 337 163 74 ILE CB C 38.750 . 1 338 163 74 ILE N N 121.970 . 1 339 164 75 ALA H H 8.320 . 1 340 164 75 ALA C C 177.460 . 1 341 164 75 ALA CA C 52.400 . 1 342 164 75 ALA CB C 19.340 . 1 343 164 75 ALA N N 128.420 . 1 344 165 76 VAL H H 8.090 . 1 345 165 76 VAL C C 176.220 . 1 346 165 76 VAL CA C 62.180 . 1 347 165 76 VAL CB C 32.980 . 1 348 165 76 VAL N N 119.870 . 1 349 166 77 SER H H 8.470 . 1 350 166 77 SER C C 174.650 . 1 351 166 77 SER CA C 58.100 . 1 352 166 77 SER CB C 64.050 . 1 353 166 77 SER N N 120.100 . 1 354 167 78 LYS H H 8.490 . 1 355 167 78 LYS C C 176.730 . 1 356 167 78 LYS CA C 56.840 . 1 357 167 78 LYS CB C 32.990 . 1 358 167 78 LYS N N 123.990 . 1 359 168 79 GLU H H 8.460 . 1 360 168 79 GLU C C 176.350 . 1 361 168 79 GLU CA C 56.960 . 1 362 168 79 GLU CB C 30.130 . 1 363 168 79 GLU N N 121.180 . 1 364 169 80 ASP H H 8.300 . 1 365 169 80 ASP C C 176.290 . 1 366 169 80 ASP CA C 54.590 . 1 367 169 80 ASP CB C 41.140 . 1 368 169 80 ASP N N 121.570 . 1 369 170 81 ARG H H 8.210 . 1 370 170 81 ARG C C 176.620 . 1 371 170 81 ARG CA C 56.300 . 1 372 170 81 ARG CB C 30.890 . 1 373 170 81 ARG N N 120.980 . 1 374 171 82 GLU H H 8.470 . 1 375 171 82 GLU C C 176.940 . 1 376 171 82 GLU CA C 57.090 . 1 377 171 82 GLU N N 121.420 . 1 378 172 83 THR H H 8.060 . 1 379 172 83 THR C C 174.370 . 1 380 172 83 THR CA C 62.320 . 1 381 172 83 THR CB C 69.790 . 1 382 172 83 THR N N 114.320 . 1 383 173 84 ASP H H 8.320 . 1 384 173 84 ASP C C 176.260 . 1 385 173 84 ASP CA C 54.560 . 1 386 173 84 ASP CB C 41.060 . 1 387 173 84 ASP N N 122.620 . 1 388 174 85 LEU H H 8.100 . 1 389 174 85 LEU C C 177.620 . 1 390 174 85 LEU CA C 55.740 . 1 391 174 85 LEU CB C 42.260 . 1 392 174 85 LEU N N 121.960 . 1 393 175 86 VAL H H 7.930 . 1 394 175 86 VAL C C 176.190 . 1 395 175 86 VAL CA C 63.020 . 1 396 175 86 VAL CB C 32.530 . 1 397 175 86 VAL N N 119.790 . 1 398 176 87 HIS H H 8.390 . 1 399 176 87 HIS C C 174.730 . 1 400 176 87 HIS CA C 55.710 . 1 401 176 87 HIS CB C 29.060 . 1 402 176 87 HIS N N 121.610 . 1 403 177 88 LEU H H 8.210 . 1 404 177 88 LEU C C 177.390 . 1 405 177 88 LEU CA C 55.520 . 1 406 177 88 LEU CB C 42.480 . 1 407 177 88 LEU N N 123.720 . 1 408 178 89 GLU H H 8.510 . 1 409 178 89 GLU C C 176.350 . 1 410 178 89 GLU CA C 56.920 . 1 411 178 89 GLU CB C 30.090 . 1 412 178 89 GLU N N 121.280 . 1 413 179 90 ASN H H 8.390 . 1 414 179 90 ASN C C 175.290 . 1 415 179 90 ASN CA C 53.360 . 1 416 179 90 ASN CB C 38.840 . 1 417 179 90 ASN N N 119.710 . 1 418 180 91 LYS H H 8.270 . 1 419 180 91 LYS C C 176.660 . 1 420 180 91 LYS CA C 56.650 . 1 421 180 91 LYS CB C 32.890 . 1 422 180 91 LYS N N 121.800 . 1 423 181 92 LEU H H 8.240 . 1 424 181 92 LEU C C 177.620 . 1 425 181 92 LEU CA C 55.330 . 1 426 181 92 LEU CB C 42.330 . 1 427 181 92 LEU N N 122.500 . 1 428 182 93 SER H H 8.280 . 1 429 182 93 SER C C 175.100 . 1 430 182 93 SER CA C 58.390 . 1 431 182 93 SER CB C 63.850 . 1 432 182 93 SER N N 116.320 . 1 433 183 94 THR H H 8.220 . 1 434 183 94 THR C C 175.090 . 1 435 183 94 THR CA C 61.930 . 1 436 183 94 THR CB C 69.640 . 1 437 183 94 THR N N 115.360 . 1 438 184 95 THR H H 8.090 . 1 439 184 95 THR C C 175.150 . 1 440 184 95 THR CA C 62.280 . 1 441 184 95 THR CB C 69.790 . 1 442 184 95 THR N N 115.430 . 1 443 185 96 GLY H H 8.370 . 1 444 185 96 GLY C C 173.870 . 1 445 185 96 GLY CA C 45.350 . 1 446 185 96 GLY N N 111.130 . 1 447 186 97 LEU H H 8.030 . 1 448 186 97 LEU C C 176.850 . 1 449 186 97 LEU CA C 54.990 . 1 450 186 97 LEU CB C 42.580 . 1 451 186 97 LEU N N 121.210 . 1 452 187 98 ASN H H 8.480 . 1 453 187 98 ASN C C 173.580 . 1 454 187 98 ASN CA C 51.350 . 1 455 187 98 ASN CB C 38.880 . 1 456 187 98 ASN N N 120.510 . 1 457 188 99 PRO C C 177.570 . 1 458 188 99 PRO CA C 63.950 . 1 459 188 99 PRO CB C 32.140 . 1 460 189 100 THR H H 8.140 . 1 461 189 100 THR C C 174.750 . 1 462 189 100 THR CA C 62.520 . 1 463 189 100 THR CB C 69.620 . 1 464 189 100 THR N N 113.240 . 1 465 190 101 ALA H H 8.080 . 1 466 190 101 ALA C C 177.830 . 1 467 190 101 ALA CA C 52.870 . 1 468 190 101 ALA CB C 19.160 . 1 469 190 101 ALA N N 125.720 . 1 stop_ save_