data_12039 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignment for the segmental-labeled basic region and HMG-box in the phosphorylated DNA-binding domain of Drosophila melanogaster SSRP1 ; _BMRB_accession_number 12039 _BMRB_flat_file_name bmr12039.str _Entry_type original _Submission_date 2019-10-28 _Accession_date 2019-11-07 _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 Aoki Daisuke . . 2 Uewaki Jun-ichi . . 3 Tochio Naoya . . 4 Tate Shin-ichi . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 89 "13C chemical shifts" 276 "15N chemical shifts" 89 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-07-09 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 12035 'Backbone assignment for the segmental-labeled acidic region in the DNA-binding domain of Drosophila melanogaster SSRP1' 12036 ; Backbone assignment for the segmental-labeled basic region and HMG-box in the DNA-binding domain of Drosophila melanogaster SSRP1 ; 12037 ; Backbone assignment for the segmental-labeled acidic region (L24G mutant) in the DNA-binding domain of Drosophila melanogaster SSRP1 ; 12038 ; Backbone assignment for the segmental-labeled acidic region in the phosphorylated DNA-binding domain of Drosophila melanogaster SSRP1 ; stop_ _Original_release_date 2019-11-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Ultrasensitive Change in Nucleosome Binding by Multiple Phosphorylations to the Intrinsically Disordered Region of the Histone Chaperone FACT. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32553729 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Aoki Daisuke . . 2 Awazu Akinori . . 3 Fujii Masashi . . 4 Uewaki Jun-ichi . . 5 Hashimoto Manami . . 6 Tochio Naoya . . 7 Umehara Takashi . . 8 Tate Shin-ichi . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume . _Journal_issue . _Journal_ISSN 0022-2836 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2020 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name BID-HMG _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'component 1' $BID-HMG 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_BID-HMG _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common BID-HMG _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 192 _Mol_residue_sequence ; MGYKDVDFGDSDNENEPDAY LARLKAEAREKEEDDDDGDS DEESTDEDFKPNENESDVAE EYDSNVESDSDDDSDASGGG GDSDGACKKKEKKSEKKEKK EKKHKEKERTKKPSKKKKDS GKPKRATTAFMLWLNDTRES IKRENPGIKVTEIAKKGGEM WKELKDKSKWEDAAAKDKQR YHDEMRNYKPEA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 GLY 3 3 TYR 4 4 LYS 5 5 ASP 6 6 VAL 7 7 ASP 8 8 PHE 9 9 GLY 10 10 ASP 11 11 SER 12 12 ASP 13 13 ASN 14 14 GLU 15 15 ASN 16 16 GLU 17 17 PRO 18 18 ASP 19 19 ALA 20 20 TYR 21 21 LEU 22 22 ALA 23 23 ARG 24 24 LEU 25 25 LYS 26 26 ALA 27 27 GLU 28 28 ALA 29 29 ARG 30 30 GLU 31 31 LYS 32 32 GLU 33 33 GLU 34 34 ASP 35 35 ASP 36 36 ASP 37 37 ASP 38 38 GLY 39 39 ASP 40 40 SER 41 41 ASP 42 42 GLU 43 43 GLU 44 44 SER 45 45 THR 46 46 ASP 47 47 GLU 48 48 ASP 49 49 PHE 50 50 LYS 51 51 PRO 52 52 ASN 53 53 GLU 54 54 ASN 55 55 GLU 56 56 SER 57 57 ASP 58 58 VAL 59 59 ALA 60 60 GLU 61 61 GLU 62 62 TYR 63 63 ASP 64 64 SER 65 65 ASN 66 66 VAL 67 67 GLU 68 68 SER 69 69 ASP 70 70 SER 71 71 ASP 72 72 ASP 73 73 ASP 74 74 SER 75 75 ASP 76 76 ALA 77 77 SER 78 78 GLY 79 79 GLY 80 80 GLY 81 81 GLY 82 82 ASP 83 83 SER 84 84 ASP 85 85 GLY 86 86 ALA 87 87 CYS 88 88 LYS 89 89 LYS 90 90 LYS 91 91 GLU 92 92 LYS 93 93 LYS 94 94 SER 95 95 GLU 96 96 LYS 97 97 LYS 98 98 GLU 99 99 LYS 100 100 LYS 101 101 GLU 102 102 LYS 103 103 LYS 104 104 HIS 105 105 LYS 106 106 GLU 107 107 LYS 108 108 GLU 109 109 ARG 110 110 THR 111 111 LYS 112 112 LYS 113 113 PRO 114 114 SER 115 115 LYS 116 116 LYS 117 117 LYS 118 118 LYS 119 119 ASP 120 120 SER 121 121 GLY 122 122 LYS 123 123 PRO 124 124 LYS 125 125 ARG 126 126 ALA 127 127 THR 128 128 THR 129 129 ALA 130 130 PHE 131 131 MET 132 132 LEU 133 133 TRP 134 134 LEU 135 135 ASN 136 136 ASP 137 137 THR 138 138 ARG 139 139 GLU 140 140 SER 141 141 ILE 142 142 LYS 143 143 ARG 144 144 GLU 145 145 ASN 146 146 PRO 147 147 GLY 148 148 ILE 149 149 LYS 150 150 VAL 151 151 THR 152 152 GLU 153 153 ILE 154 154 ALA 155 155 LYS 156 156 LYS 157 157 GLY 158 158 GLY 159 159 GLU 160 160 MET 161 161 TRP 162 162 LYS 163 163 GLU 164 164 LEU 165 165 LYS 166 166 ASP 167 167 LYS 168 168 SER 169 169 LYS 170 170 TRP 171 171 GLU 172 172 ASP 173 173 ALA 174 174 ALA 175 175 ALA 176 176 LYS 177 177 ASP 178 178 LYS 179 179 GLN 180 180 ARG 181 181 TYR 182 182 HIS 183 183 ASP 184 184 GLU 185 185 MET 186 186 ARG 187 187 ASN 188 188 TYR 189 189 LYS 190 190 PRO 191 191 GLU 192 192 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 $BID-HMG 'fruit fly' 7227 Eukaryota Metazoa Drosophila melanogaster 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 $BID-HMG 'recombinant technology' . Escherichia coli . 'pTWIN1-his and 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 $BID-HMG 0.55 mM '[U-13C; U-15N]' TRIS 50 mM 'natural abundance' DTT 1 mM 'natural abundance' 'sodium azide' 0.03 % 'natural abundance' D2O 6 % [U-2H] H2O 94 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_Magro _Saveframe_category software _Name Magro _Version . loop_ _Vendor _Address _Electronic_address 'Kobayashi N' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _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_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_C(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _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' 50 . mM pH 6.6 . pH pressure 1 . atm temperature 300 . 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 water C 13 protons ppm 4.767 internal indirect . . . 0.251449530 water H 1 protons ppm 4.767 internal indirect . . . 1 water N 15 protons ppm 4.767 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $Magro stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HN(CA)CO' '3D HN(CO)CA' '3D HNCA' '3D CBCA(CO)NH' '3D HNCACB' '3D C(CO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'component 1' _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 87 87 CYS C C 174.758 0.300 1 2 87 87 CYS CA C 55.763 0.300 1 3 87 87 CYS CB C 40.637 0.300 1 4 88 88 LYS H H 8.270 0.030 1 5 88 88 LYS C C 176.495 0.300 1 6 88 88 LYS CA C 56.444 0.300 1 7 88 88 LYS CB C 33.078 0.300 1 8 88 88 LYS N N 123.143 0.300 1 9 89 89 LYS H H 8.388 0.030 1 10 89 89 LYS C C 176.692 0.300 1 11 89 89 LYS CA C 56.499 0.300 1 12 89 89 LYS CB C 33.078 0.300 1 13 89 89 LYS N N 123.360 0.300 1 14 90 90 LYS H H 8.403 0.030 1 15 90 90 LYS C C 176.618 0.300 1 16 90 90 LYS CA C 56.720 0.300 1 17 90 90 LYS CB C 33.035 0.300 1 18 90 90 LYS N N 122.057 0.300 1 19 91 91 GLU H H 8.391 0.030 1 20 91 91 GLU C C 176.576 0.300 1 21 91 91 GLU CA C 56.757 0.300 1 22 91 91 GLU CB C 30.356 0.300 1 23 91 91 GLU N N 121.890 0.300 1 24 93 93 LYS C C 176.916 0.300 1 25 93 93 LYS CA C 56.867 0.300 1 26 93 93 LYS CB C 33.034 0.300 1 27 94 94 SER H H 8.374 0.030 1 28 94 94 SER C C 174.754 0.300 1 29 94 94 SER CA C 58.410 0.300 1 30 94 94 SER CB C 63.748 0.300 1 31 94 94 SER N N 116.766 0.300 1 32 95 95 GLU H H 8.477 0.030 1 33 95 95 GLU C C 176.647 0.300 1 34 95 95 GLU CA C 56.407 0.300 1 35 95 95 GLU CB C 33.120 0.300 1 36 95 95 GLU N N 123.837 0.300 1 37 96 96 LYS H H 8.496 0.030 1 38 96 96 LYS C C 176.876 0.300 1 39 96 96 LYS CA C 56.720 0.300 1 40 96 96 LYS CB C 33.034 0.300 1 41 96 96 LYS N N 123.330 0.300 1 42 102 102 LYS C C 176.461 0.300 1 43 102 102 LYS CA C 56.425 0.300 1 44 102 102 LYS CB C 30.269 0.300 1 45 103 103 LYS H H 8.426 0.030 1 46 103 103 LYS C C 176.617 0.300 1 47 103 103 LYS CA C 56.481 0.300 1 48 103 103 LYS CB C 33.078 0.300 1 49 103 103 LYS N N 123.221 0.300 1 50 104 104 HIS H H 8.426 0.030 1 51 104 104 HIS C C 176.553 0.300 1 52 104 104 HIS CA C 56.554 0.300 1 53 104 104 HIS CB C 30.326 0.300 1 54 104 104 HIS N N 122.753 0.300 1 55 105 105 LYS H H 8.321 0.030 1 56 105 105 LYS C C 176.610 0.300 1 57 105 105 LYS CA C 56.646 0.300 1 58 105 105 LYS CB C 33.078 0.300 1 59 105 105 LYS N N 122.649 0.300 1 60 106 106 GLU H H 8.525 0.030 1 61 106 106 GLU C C 176.610 0.300 1 62 106 106 GLU CA C 56.849 0.300 1 63 106 106 GLU CB C 30.183 0.300 1 64 106 106 GLU N N 122.261 0.300 1 65 107 107 LYS H H 8.286 0.030 1 66 107 107 LYS C C 176.654 0.300 1 67 107 107 LYS CA C 56.665 0.300 1 68 107 107 LYS CB C 32.991 0.300 1 69 107 107 LYS N N 122.114 0.300 1 70 108 108 GLU H H 8.470 0.030 1 71 108 108 GLU C C 175.012 0.300 1 72 108 108 GLU CA C 56.020 0.300 1 73 108 108 GLU CB C 29.765 0.300 1 74 108 108 GLU N N 120.189 0.300 1 75 109 109 ARG C C 176.509 0.300 1 76 109 109 ARG CA C 56.315 0.300 1 77 109 109 ARG CB C 30.701 0.300 1 78 110 110 THR H H 8.198 0.030 1 79 110 110 THR C C 174.334 0.300 1 80 110 110 THR CA C 62.058 0.300 1 81 110 110 THR CB C 69.579 0.300 1 82 110 110 THR N N 115.619 0.300 1 83 111 111 LYS H H 8.302 0.030 1 84 111 111 LYS C C 176.166 0.300 1 85 111 111 LYS CA C 56.168 0.300 1 86 111 111 LYS CB C 33.078 0.300 1 87 111 111 LYS N N 124.192 0.300 1 88 112 112 LYS H H 8.419 0.030 1 89 112 112 LYS C C 174.436 0.300 1 90 112 112 LYS CA C 54.327 0.300 1 91 112 112 LYS CB C 32.861 0.300 1 92 112 112 LYS N N 124.508 0.300 1 93 113 113 PRO C C 176.889 0.300 1 94 113 113 PRO CA C 63.163 0.300 1 95 113 113 PRO CB C 32.084 0.300 1 96 114 114 SER H H 8.452 0.030 1 97 114 114 SER C C 174.800 0.300 1 98 114 114 SER CA C 58.393 0.300 1 99 114 114 SER CB C 63.770 0.300 1 100 114 114 SER N N 116.643 0.300 1 101 115 115 LYS H H 8.384 0.030 1 102 115 115 LYS C C 176.599 0.300 1 103 115 115 LYS CA C 56.573 0.300 1 104 115 115 LYS CB C 30.356 0.300 1 105 115 115 LYS N N 123.050 0.300 1 106 116 116 LYS C C 176.599 0.300 1 107 116 116 LYS CA C 56.609 0.300 1 108 116 116 LYS CB C 33.034 0.300 1 109 117 117 LYS H H 8.339 0.030 1 110 117 117 LYS C C 176.597 0.300 1 111 117 117 LYS CA C 56.573 0.300 1 112 117 117 LYS CB C 32.948 0.300 1 113 117 117 LYS N N 122.988 0.300 1 114 118 118 LYS H H 8.368 0.030 1 115 118 118 LYS C C 176.445 0.300 1 116 118 118 LYS CA C 56.555 0.300 1 117 118 118 LYS CB C 33.120 0.300 1 118 118 118 LYS N N 122.304 0.300 1 119 119 119 ASP H H 8.449 0.030 1 120 119 119 ASP C C 176.498 0.300 1 121 119 119 ASP CA C 54.234 0.300 1 122 119 119 ASP CB C 41.371 0.300 1 123 119 119 ASP N N 121.985 0.300 1 124 120 120 SER H H 8.412 0.030 1 125 120 120 SER C C 175.322 0.300 1 126 120 120 SER CA C 59.186 0.300 1 127 120 120 SER CB C 63.671 0.300 1 128 120 120 SER N N 117.611 0.300 1 129 121 121 GLY H H 8.622 0.030 1 130 121 121 GLY C C 173.704 0.300 1 131 121 121 GLY CA C 45.307 0.300 1 132 121 121 GLY N N 111.041 0.300 1 133 122 122 LYS H H 7.738 0.030 1 134 122 122 LYS C C 174.367 0.300 1 135 122 122 LYS CA C 54.621 0.300 1 136 122 122 LYS CB C 32.602 0.300 1 137 122 122 LYS N N 122.029 0.300 1 138 123 123 PRO C C 175.979 0.300 1 139 123 123 PRO CA C 63.016 0.300 1 140 123 123 PRO CB C 31.825 0.300 1 141 124 124 LYS H H 8.774 0.030 1 142 124 124 LYS C C 177.497 0.300 1 143 124 124 LYS CA C 56.241 0.300 1 144 124 124 LYS CB C 32.516 0.300 1 145 124 124 LYS N N 123.686 0.300 1 146 125 125 ARG C C 175.895 0.300 1 147 125 125 ARG CA C 56.573 0.300 1 148 125 125 ARG CB C 30.269 0.300 1 149 126 126 ALA H H 7.701 0.030 1 150 126 126 ALA C C 177.577 0.300 1 151 126 126 ALA CA C 51.860 0.300 1 152 126 126 ALA CB C 18.822 0.300 1 153 126 126 ALA N N 124.235 0.300 1 154 127 127 THR H H 8.724 0.030 1 155 127 127 THR C C 174.381 0.300 1 156 127 127 THR CA C 61.727 0.300 1 157 127 127 THR CB C 69.450 0.300 1 158 127 127 THR N N 118.506 0.300 1 159 128 128 THR H H 8.065 0.030 1 160 128 128 THR C C 174.663 0.300 1 161 128 128 THR CA C 60.898 0.300 1 162 128 128 THR CB C 70.840 0.300 1 163 128 128 THR N N 114.621 0.300 1 164 129 129 ALA H H 8.980 0.030 1 165 129 129 ALA C C 177.971 0.300 1 166 129 129 ALA CA C 55.966 0.300 1 167 129 129 ALA CB C 18.711 0.300 1 168 129 129 ALA N N 123.668 0.300 1 169 130 130 PHE H H 8.300 0.030 1 170 130 130 PHE C C 175.863 0.300 1 171 130 130 PHE CA C 59.665 0.300 1 172 130 130 PHE N N 115.599 0.300 1 173 131 131 MET H H 7.314 0.030 1 174 131 131 MET C C 179.246 0.300 1 175 131 131 MET CA C 57.162 0.300 1 176 131 131 MET N N 116.721 0.300 1 177 132 132 LEU H H 8.075 0.030 1 178 132 132 LEU CA C 57.898 0.300 1 179 132 132 LEU N N 120.844 0.300 1 180 133 133 TRP C C 179.200 0.300 1 181 133 133 TRP CA C 61.764 0.300 1 182 134 134 LEU H H 9.004 0.030 1 183 134 134 LEU C C 178.908 0.300 1 184 134 134 LEU CA C 57.456 0.300 1 185 134 134 LEU N N 124.417 0.300 1 186 135 135 ASN H H 7.885 0.030 1 187 135 135 ASN C C 177.807 0.300 1 188 135 135 ASN CA C 55.966 0.300 1 189 135 135 ASN CB C 37.755 0.300 1 190 135 135 ASN N N 116.743 0.300 1 191 136 136 ASP H H 7.199 0.030 1 192 136 136 ASP C C 177.808 0.300 1 193 136 136 ASP CA C 56.241 0.300 1 194 136 136 ASP N N 118.790 0.300 1 195 137 137 THR H H 7.426 0.030 1 196 137 137 THR C C 175.144 0.300 1 197 137 137 THR CA C 63.475 0.300 1 198 137 137 THR N N 114.308 0.300 1 199 138 138 ARG H H 8.188 0.030 1 200 138 138 ARG C C 177.029 0.300 1 201 138 138 ARG CA C 60.917 0.300 1 202 138 138 ARG CB C 30.053 0.300 1 203 138 138 ARG N N 124.225 0.300 1 204 139 139 GLU H H 8.532 0.030 1 205 139 139 GLU C C 179.121 0.300 1 206 139 139 GLU CA C 59.537 0.300 1 207 139 139 GLU CB C 28.671 0.300 1 208 139 139 GLU N N 117.597 0.300 1 209 140 140 SER H H 7.944 0.030 1 210 140 140 SER C C 176.273 0.300 1 211 140 140 SER CA C 61.690 0.300 1 212 140 140 SER CB C 62.273 0.300 1 213 140 140 SER N N 117.131 0.300 1 214 141 141 ILE H H 7.862 0.030 1 215 141 141 ILE C C 179.044 0.300 1 216 141 141 ILE CA C 65.888 0.300 1 217 141 141 ILE N N 122.483 0.300 1 218 142 142 LYS H H 8.012 0.030 1 219 142 142 LYS C C 178.707 0.300 1 220 142 142 LYS CA C 59.850 0.300 1 221 142 142 LYS CB C 32.343 0.300 1 222 142 142 LYS N N 119.098 0.300 1 223 143 143 ARG H H 7.933 0.030 1 224 143 143 ARG C C 178.511 0.300 1 225 143 143 ARG CA C 59.131 0.300 1 226 143 143 ARG CB C 30.502 0.300 1 227 143 143 ARG N N 118.583 0.300 1 228 144 144 GLU H H 7.819 0.030 1 229 144 144 GLU C C 175.742 0.300 1 230 144 144 GLU CA C 56.941 0.300 1 231 144 144 GLU CB C 30.269 0.300 1 232 144 144 GLU N N 114.839 0.300 1 233 145 145 ASN H H 7.282 0.030 1 234 145 145 ASN C C 170.133 0.300 1 235 145 145 ASN CA C 50.976 0.300 1 236 145 145 ASN CB C 40.550 0.300 1 237 145 145 ASN N N 116.780 0.300 1 238 146 146 PRO C C 178.740 0.300 1 239 146 146 PRO CA C 64.267 0.300 1 240 147 147 GLY H H 8.769 0.030 1 241 147 147 GLY C C 174.960 0.300 1 242 147 147 GLY CA C 45.252 0.300 1 243 147 147 GLY N N 112.023 0.300 1 244 148 148 ILE H H 7.848 0.030 1 245 148 148 ILE C C 174.761 0.300 1 246 148 148 ILE CA C 62.297 0.300 1 247 148 148 ILE CB C 37.858 0.300 1 248 148 148 ILE N N 121.922 0.300 1 249 149 149 LYS H H 8.513 0.030 1 250 149 149 LYS C C 179.339 0.300 1 251 149 149 LYS CA C 55.966 0.300 1 252 149 149 LYS CB C 33.953 0.300 1 253 149 149 LYS N N 126.167 0.300 1 254 150 150 VAL H H 8.825 0.030 1 255 150 150 VAL C C 178.437 0.300 1 256 150 150 VAL CA C 66.606 0.300 1 257 150 150 VAL CB C 34.071 0.300 1 258 150 150 VAL N N 121.459 0.300 1 259 151 151 THR H H 7.647 0.030 1 260 151 151 THR C C 176.127 0.300 1 261 151 151 THR CA C 63.881 0.300 1 262 151 151 THR CB C 68.111 0.300 1 263 151 151 THR N N 109.496 0.300 1 264 152 152 GLU H H 7.539 0.030 1 265 152 152 GLU C C 178.089 0.300 1 266 152 152 GLU CA C 57.051 0.300 1 267 152 152 GLU CB C 30.340 0.300 1 268 152 152 GLU N N 120.437 0.300 1 269 153 153 ILE H H 7.665 0.030 1 270 153 153 ILE C C 177.410 0.300 1 271 153 153 ILE CA C 66.227 0.300 1 272 153 153 ILE N N 122.289 0.300 1 273 154 154 ALA H H 8.317 0.030 1 274 154 154 ALA C C 180.424 0.300 1 275 154 154 ALA CA C 55.597 0.300 1 276 154 154 ALA CB C 17.828 0.300 1 277 154 154 ALA N N 120.669 0.300 1 278 155 155 LYS H H 7.648 0.030 1 279 155 155 LYS C C 179.273 0.300 1 280 155 155 LYS CA C 59.389 0.300 1 281 155 155 LYS CB C 32.472 0.300 1 282 155 155 LYS N N 120.043 0.300 1 283 156 156 LYS H H 8.257 0.030 1 284 156 156 LYS C C 179.614 0.300 1 285 156 156 LYS CA C 58.340 0.300 1 286 156 156 LYS CB C 31.523 0.300 1 287 156 156 LYS N N 121.431 0.300 1 288 157 157 GLY H H 9.282 0.030 1 289 157 157 GLY C C 175.429 0.300 1 290 157 157 GLY CA C 47.332 0.300 1 291 157 157 GLY N N 106.640 0.300 1 292 158 158 GLY H H 8.665 0.030 1 293 158 158 GLY C C 176.093 0.300 1 294 158 158 GLY CA C 47.811 0.300 1 295 158 158 GLY N N 109.983 0.300 1 296 159 159 GLU H H 7.578 0.030 1 297 159 159 GLU C C 179.246 0.300 1 298 159 159 GLU CA C 59.260 0.300 1 299 159 159 GLU N N 121.542 0.300 1 300 160 160 MET H H 8.030 0.030 1 301 160 160 MET C C 179.263 0.300 1 302 160 160 MET CA C 59.002 0.300 1 303 160 160 MET N N 119.471 0.300 1 304 161 161 TRP H H 8.947 0.030 1 305 161 161 TRP C C 177.721 0.300 1 306 161 161 TRP CA C 59.168 0.300 1 307 161 161 TRP N N 122.007 0.300 1 308 162 162 LYS H H 7.394 0.030 1 309 162 162 LYS C C 178.031 0.300 1 310 162 162 LYS CA C 59.205 0.300 1 311 162 162 LYS N N 115.954 0.300 1 312 163 163 GLU H H 6.903 0.030 1 313 163 163 GLU C C 175.921 0.300 1 314 163 163 GLU CA C 55.707 0.300 1 315 163 163 GLU CB C 30.486 0.300 1 316 163 163 GLU N N 114.348 0.300 1 317 164 164 LEU H H 6.949 0.030 1 318 164 164 LEU C C 177.370 0.300 1 319 164 164 LEU CA C 55.561 0.300 1 320 164 164 LEU CB C 42.538 0.300 1 321 164 164 LEU N N 122.865 0.300 1 322 165 165 LYS H H 8.495 0.030 1 323 165 165 LYS C C 176.892 0.300 1 324 165 165 LYS CA C 58.359 0.300 1 325 165 165 LYS CB C 32.380 0.300 1 326 165 165 LYS N N 126.230 0.300 1 327 166 166 ASP H H 7.829 0.030 1 328 166 166 ASP C C 175.886 0.300 1 329 166 166 ASP CA C 52.947 0.300 1 330 166 166 ASP CB C 40.683 0.300 1 331 166 166 ASP N N 116.843 0.300 1 332 167 167 LYS H H 8.676 0.030 1 333 167 167 LYS C C 178.179 0.300 1 334 167 167 LYS CA C 56.370 0.300 1 335 167 167 LYS CB C 33.553 0.300 1 336 167 167 LYS N N 124.969 0.300 1 337 168 168 SER H H 8.356 0.030 1 338 168 168 SER C C 175.947 0.300 1 339 168 168 SER CA C 62.978 0.300 1 340 168 168 SER CB C 64.223 0.300 1 341 168 168 SER N N 117.827 0.300 1 342 169 169 LYS H H 8.620 0.030 1 343 169 169 LYS C C 178.832 0.300 1 344 169 169 LYS CA C 59.628 0.300 1 345 169 169 LYS CB C 31.306 0.300 1 346 169 169 LYS N N 122.534 0.300 1 347 170 170 TRP H H 7.117 0.030 1 348 170 170 TRP C C 178.164 0.300 1 349 170 170 TRP N N 119.210 0.300 1 350 171 171 GLU H H 8.537 0.030 1 351 171 171 GLU C C 180.235 0.300 1 352 171 171 GLU CA C 59.997 0.300 1 353 171 171 GLU N N 120.676 0.300 1 354 172 172 ASP H H 8.904 0.030 1 355 172 172 ASP C C 178.624 0.300 1 356 172 172 ASP CA C 57.519 0.300 1 357 172 172 ASP N N 121.435 0.300 1 358 173 173 ALA H H 7.447 0.030 1 359 173 173 ALA C C 180.765 0.300 1 360 173 173 ALA CA C 55.284 0.300 1 361 173 173 ALA CB C 18.711 0.300 1 362 173 173 ALA N N 121.930 0.300 1 363 174 174 ALA H H 8.562 0.030 1 364 174 174 ALA C C 180.063 0.300 1 365 174 174 ALA CA C 55.136 0.300 1 366 174 174 ALA CB C 18.303 0.300 1 367 174 174 ALA N N 122.816 0.300 1 368 175 175 ALA H H 8.176 0.030 1 369 175 175 ALA C C 181.183 0.300 1 370 175 175 ALA CA C 55.340 0.300 1 371 175 175 ALA CB C 18.001 0.300 1 372 175 175 ALA N N 123.181 0.300 1 373 176 176 LYS H H 7.952 0.030 1 374 176 176 LYS C C 179.191 0.300 1 375 176 176 LYS CA C 59.094 0.300 1 376 176 176 LYS CB C 32.300 0.300 1 377 176 176 LYS N N 119.539 0.300 1 378 177 177 ASP H H 8.096 0.030 1 379 177 177 ASP C C 177.774 0.300 1 380 177 177 ASP CA C 57.088 0.300 1 381 177 177 ASP CB C 41.674 0.300 1 382 177 177 ASP N N 121.356 0.300 1 383 178 178 LYS H H 8.209 0.030 1 384 178 178 LYS C C 178.417 0.300 1 385 178 178 LYS CA C 59.353 0.300 1 386 178 178 LYS CB C 31.770 0.300 1 387 178 178 LYS N N 120.178 0.300 1 388 179 179 GLN H H 7.711 0.030 1 389 179 179 GLN C C 177.184 0.300 1 390 179 179 GLN CA C 58.469 0.300 1 391 179 179 GLN CB C 28.196 0.300 1 392 179 179 GLN N N 119.381 0.300 1 393 180 180 ARG H H 7.986 0.030 1 394 180 180 ARG C C 178.529 0.300 1 395 180 180 ARG CA C 59.058 0.300 1 396 180 180 ARG CB C 27.555 0.300 1 397 180 180 ARG N N 121.081 0.300 1 398 181 181 TYR H H 8.278 0.030 1 399 181 181 TYR C C 176.520 0.300 1 400 181 181 TYR CA C 61.671 0.300 1 401 181 181 TYR N N 120.577 0.300 1 402 182 182 HIS H H 8.266 0.030 1 403 182 182 HIS C C 177.717 0.300 1 404 182 182 HIS CA C 59.223 0.300 1 405 182 182 HIS CB C 29.233 0.300 1 406 182 182 HIS N N 117.926 0.300 1 407 183 183 ASP H H 8.664 0.030 1 408 183 183 ASP C C 178.837 0.300 1 409 183 183 ASP CA C 57.222 0.300 1 410 183 183 ASP CB C 40.246 0.300 1 411 183 183 ASP N N 121.086 0.300 1 412 184 184 GLU H H 8.618 0.030 1 413 184 184 GLU C C 180.036 0.300 1 414 184 184 GLU CA C 59.352 0.300 1 415 184 184 GLU CB C 30.010 0.300 1 416 184 184 GLU N N 120.364 0.300 1 417 185 185 MET H H 8.380 0.030 1 418 185 185 MET C C 178.588 0.300 1 419 185 185 MET CA C 56.334 0.300 1 420 185 185 MET CB C 31.025 0.300 1 421 185 185 MET N N 118.938 0.300 1 422 186 186 ARG H H 7.694 0.030 1 423 186 186 ARG C C 177.026 0.300 1 424 186 186 ARG CA C 58.285 0.300 1 425 186 186 ARG CB C 30.194 0.300 1 426 186 186 ARG N N 119.580 0.300 1 427 187 187 ASN H H 7.518 0.030 1 428 187 187 ASN C C 174.462 0.300 1 429 187 187 ASN CA C 53.222 0.300 1 430 187 187 ASN CB C 39.557 0.300 1 431 187 187 ASN N N 115.251 0.300 1 432 188 188 TYR H H 7.638 0.030 1 433 188 188 TYR C C 174.643 0.300 1 434 188 188 TYR CA C 58.413 0.300 1 435 188 188 TYR CB C 39.038 0.300 1 436 188 188 TYR N N 121.696 0.300 1 437 189 189 LYS H H 8.013 0.030 1 438 189 189 LYS C C 172.987 0.300 1 439 189 189 LYS CA C 53.185 0.300 1 440 189 189 LYS CB C 33.207 0.300 1 441 189 189 LYS N N 126.732 0.300 1 442 190 190 PRO C C 176.933 0.300 1 443 190 190 PRO CA C 62.979 0.300 1 444 190 190 PRO CB C 31.997 0.300 1 445 191 191 GLU H H 8.437 0.030 1 446 191 191 GLU C C 175.300 0.300 1 447 191 191 GLU CA C 56.462 0.300 1 448 191 191 GLU CB C 30.356 0.300 1 449 191 191 GLU N N 121.174 0.300 1 450 192 192 ALA H H 7.893 0.030 1 451 192 192 ALA C C 182.421 0.300 1 452 192 192 ALA CA C 53.811 0.300 1 453 192 192 ALA CB C 20.507 0.300 1 454 192 192 ALA N N 130.469 0.300 1 stop_ save_