data_12036 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignment for the segmental-labeled basic region and HMG-box in the DNA-binding domain of Drosophila melanogaster SSRP1 ; _BMRB_accession_number 12036 _BMRB_flat_file_name bmr12036.str _Entry_type original _Submission_date 2019-10-25 _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" 94 "13C chemical shifts" 302 "15N chemical shifts" 94 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' 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 ; 12039 ; Backbone assignment for the segmental-labeled basic region and HMG-box 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 0.41 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 H H 8.261 0.030 1 2 87 87 CYS C C 174.907 0.300 1 3 87 87 CYS CA C 58.929 0.300 1 4 87 87 CYS CB C 27.780 0.300 1 5 87 87 CYS N N 117.733 0.300 1 6 88 88 LYS H H 8.286 0.030 1 7 88 88 LYS C C 176.611 0.300 1 8 88 88 LYS CA C 56.481 0.300 1 9 88 88 LYS CB C 33.087 0.300 1 10 88 88 LYS N N 123.537 0.300 1 11 89 89 LYS H H 8.402 0.030 1 12 89 89 LYS C C 176.538 0.300 1 13 89 89 LYS CA C 56.462 0.300 1 14 89 89 LYS CB C 33.173 0.300 1 15 89 89 LYS N N 123.473 0.300 1 16 90 90 LYS H H 8.438 0.030 1 17 90 90 LYS C C 175.012 0.300 1 18 90 90 LYS CA C 56.131 0.300 1 19 90 90 LYS CB C 30.110 0.300 1 20 90 90 LYS N N 120.498 0.300 1 21 93 93 LYS C C 176.768 0.300 1 22 93 93 LYS CA C 56.757 0.300 1 23 93 93 LYS CB C 33.130 0.300 1 24 94 94 SER H H 8.371 0.030 1 25 94 94 SER C C 174.672 0.300 1 26 94 94 SER CA C 58.358 0.300 1 27 94 94 SER CB C 63.674 0.300 1 28 94 94 SER N N 116.890 0.300 1 29 95 95 GLU H H 8.454 0.030 1 30 95 95 GLU C C 176.586 0.300 1 31 95 95 GLU CA C 56.407 0.300 1 32 95 95 GLU CB C 33.044 0.300 1 33 95 95 GLU N N 123.740 0.300 1 34 96 96 LYS H H 8.465 0.030 1 35 96 96 LYS C C 176.675 0.300 1 36 96 96 LYS CA C 56.591 0.300 1 37 96 96 LYS CB C 33.044 0.300 1 38 96 96 LYS N N 123.321 0.300 1 39 97 97 LYS H H 8.257 0.030 1 40 97 97 LYS C C 176.645 0.300 1 41 97 97 LYS CA C 56.609 0.300 1 42 97 97 LYS CB C 33.044 0.300 1 43 97 97 LYS N N 122.391 0.300 1 44 98 98 GLU H H 8.543 0.030 1 45 98 98 GLU C C 176.611 0.300 1 46 98 98 GLU CA C 56.665 0.300 1 47 98 98 GLU CB C 33.046 0.300 1 48 98 98 GLU N N 122.436 0.300 1 49 99 99 LYS H H 8.341 0.030 1 50 99 99 LYS C C 176.553 0.300 1 51 99 99 LYS CA C 56.517 0.300 1 52 99 99 LYS CB C 33.087 0.300 1 53 99 99 LYS N N 122.900 0.300 1 54 100 100 LYS H H 8.419 0.030 1 55 100 100 LYS C C 176.461 0.300 1 56 100 100 LYS CA C 56.536 0.300 1 57 100 100 LYS CB C 30.628 0.300 1 58 100 100 LYS N N 122.273 0.300 1 59 102 102 LYS C C 176.415 0.300 1 60 102 102 LYS CA C 56.499 0.300 1 61 102 102 LYS CB C 30.369 0.300 1 62 103 103 LYS H H 8.386 0.030 1 63 103 103 LYS C C 176.564 0.300 1 64 103 103 LYS CA C 56.517 0.300 1 65 103 103 LYS CB C 33.044 0.300 1 66 103 103 LYS N N 123.141 0.300 1 67 104 104 HIS H H 8.420 0.030 1 68 104 104 HIS C C 176.553 0.300 1 69 104 104 HIS CA C 56.554 0.300 1 70 104 104 HIS CB C 33.002 0.300 1 71 104 104 HIS N N 122.091 0.300 1 72 105 105 LYS H H 8.331 0.030 1 73 105 105 LYS C C 176.611 0.300 1 74 105 105 LYS CA C 56.591 0.300 1 75 105 105 LYS CB C 33.044 0.300 1 76 105 105 LYS N N 122.733 0.300 1 77 106 106 GLU H H 8.391 0.030 1 78 106 106 GLU C C 176.570 0.300 1 79 106 106 GLU CA C 56.775 0.300 1 80 106 106 GLU CB C 30.239 0.300 1 81 106 106 GLU N N 121.924 0.300 1 82 107 107 LYS H H 8.338 0.030 1 83 107 107 LYS C C 176.565 0.300 1 84 107 107 LYS CA C 56.665 0.300 1 85 107 107 LYS CB C 30.338 0.300 1 86 107 107 LYS N N 122.048 0.300 1 87 108 108 GLU H H 8.310 0.030 1 88 108 108 GLU C C 176.565 0.300 1 89 108 108 GLU CA C 56.591 0.300 1 90 108 108 GLU CB C 33.001 0.300 1 91 108 108 GLU N N 122.323 0.300 1 92 109 109 ARG H H 8.385 0.030 1 93 109 109 ARG C C 176.495 0.300 1 94 109 109 ARG CA C 56.444 0.300 1 95 109 109 ARG CB C 30.800 0.300 1 96 109 109 ARG N N 122.419 0.300 1 97 110 110 THR H H 8.172 0.030 1 98 110 110 THR C C 174.307 0.300 1 99 110 110 THR CA C 62.040 0.300 1 100 110 110 THR CB C 69.627 0.300 1 101 110 110 THR N N 115.510 0.300 1 102 111 111 LYS H H 8.317 0.030 1 103 111 111 LYS C C 176.179 0.300 1 104 111 111 LYS CA C 56.150 0.300 1 105 111 111 LYS CB C 33.130 0.300 1 106 111 111 LYS N N 124.184 0.300 1 107 112 112 LYS H H 8.413 0.030 1 108 112 112 LYS C C 174.459 0.300 1 109 112 112 LYS CA C 54.253 0.300 1 110 112 112 LYS CB C 32.785 0.300 1 111 112 112 LYS N N 124.468 0.300 1 112 113 113 PRO C C 176.883 0.300 1 113 113 113 PRO CA C 63.126 0.300 1 114 113 113 PRO CB C 32.008 0.300 1 115 114 114 SER H H 8.458 0.030 1 116 114 114 SER C C 174.649 0.300 1 117 114 114 SER CA C 58.340 0.300 1 118 114 114 SER CB C 63.684 0.300 1 119 114 114 SER N N 116.698 0.300 1 120 115 115 LYS H H 8.419 0.030 1 121 115 115 LYS C C 176.523 0.300 1 122 115 115 LYS CA C 56.536 0.300 1 123 115 115 LYS CB C 33.130 0.300 1 124 115 115 LYS N N 123.260 0.300 1 125 116 116 LYS H H 8.543 0.030 1 126 116 116 LYS C C 176.611 0.300 1 127 116 116 LYS CA C 56.665 0.300 1 128 116 116 LYS CB C 33.046 0.300 1 129 116 116 LYS N N 122.436 0.300 1 130 117 117 LYS H H 8.341 0.030 1 131 117 117 LYS C C 176.553 0.300 1 132 117 117 LYS CA C 56.517 0.300 1 133 117 117 LYS CB C 33.087 0.300 1 134 117 117 LYS N N 122.900 0.300 1 135 118 118 LYS H H 8.419 0.030 1 136 118 118 LYS C C 176.461 0.300 1 137 118 118 LYS CA C 56.536 0.300 1 138 118 118 LYS CB C 30.628 0.300 1 139 118 118 LYS N N 122.273 0.300 1 140 119 119 ASP C C 176.482 0.300 1 141 119 119 ASP CA C 54.253 0.300 1 142 119 119 ASP CB C 41.413 0.300 1 143 120 120 SER H H 8.387 0.030 1 144 120 120 SER C C 175.300 0.300 1 145 120 120 SER CA C 59.168 0.300 1 146 120 120 SER CB C 63.716 0.300 1 147 120 120 SER N N 117.345 0.300 1 148 121 121 GLY H H 8.617 0.030 1 149 121 121 GLY C C 173.676 0.300 1 150 121 121 GLY CA C 45.306 0.300 1 151 121 121 GLY N N 111.039 0.300 1 152 122 122 LYS H H 7.768 0.030 1 153 122 122 LYS C C 174.390 0.300 1 154 122 122 LYS CA C 54.621 0.300 1 155 122 122 LYS CB C 32.699 0.300 1 156 122 122 LYS N N 121.947 0.300 1 157 123 123 PRO C C 176.056 0.300 1 158 123 123 PRO CA C 63.052 0.300 1 159 123 123 PRO CB C 31.836 0.300 1 160 124 124 LYS H H 8.798 0.030 1 161 124 124 LYS C C 177.451 0.300 1 162 124 124 LYS CA C 56.352 0.300 1 163 124 124 LYS CB C 32.699 0.300 1 164 124 124 LYS N N 123.793 0.300 1 165 125 125 ARG C C 175.848 0.300 1 166 125 125 ARG CA C 56.573 0.300 1 167 125 125 ARG CB C 30.541 0.300 1 168 126 126 ALA H H 7.704 0.030 1 169 126 126 ALA C C 177.589 0.300 1 170 126 126 ALA CA C 51.879 0.300 1 171 126 126 ALA CB C 19.023 0.300 1 172 126 126 ALA N N 124.339 0.300 1 173 127 127 THR H H 8.744 0.030 1 174 127 127 THR C C 174.361 0.300 1 175 127 127 THR CA C 61.709 0.300 1 176 127 127 THR CB C 69.411 0.300 1 177 127 127 THR N N 118.557 0.300 1 178 128 128 THR H H 8.054 0.030 1 179 128 128 THR C C 174.644 0.300 1 180 128 128 THR CA C 60.752 0.300 1 181 128 128 THR CB C 70.886 0.300 1 182 128 128 THR N N 114.500 0.300 1 183 129 129 ALA H H 8.975 0.030 1 184 129 129 ALA C C 178.014 0.300 1 185 129 129 ALA CA C 55.928 0.300 1 186 129 129 ALA CB C 18.861 0.300 1 187 129 129 ALA N N 123.697 0.300 1 188 130 130 PHE H H 8.305 0.030 1 189 130 130 PHE C C 175.989 0.300 1 190 130 130 PHE CA C 59.702 0.300 1 191 130 130 PHE CB C 38.720 0.300 1 192 130 130 PHE N N 115.610 0.300 1 193 131 131 MET H H 7.319 0.030 1 194 131 131 MET C C 179.223 0.300 1 195 131 131 MET CA C 57.106 0.300 1 196 131 131 MET CB C 31.491 0.300 1 197 131 131 MET N N 116.668 0.300 1 198 132 132 LEU H H 8.061 0.030 1 199 132 132 LEU C C 179.430 0.300 1 200 132 132 LEU CA C 58.008 0.300 1 201 132 132 LEU CB C 42.017 0.300 1 202 132 132 LEU N N 120.806 0.300 1 203 133 133 TRP C C 179.154 0.300 1 204 133 133 TRP CA C 61.580 0.300 1 205 134 134 LEU H H 8.992 0.030 1 206 134 134 LEU C C 178.924 0.300 1 207 134 134 LEU CA C 57.475 0.300 1 208 134 134 LEU N N 124.356 0.300 1 209 135 135 ASN H H 7.868 0.030 1 210 135 135 ASN C C 177.831 0.300 1 211 135 135 ASN CA C 55.966 0.300 1 212 135 135 ASN CB C 37.789 0.300 1 213 135 135 ASN N N 116.706 0.300 1 214 136 136 ASP H H 7.203 0.030 1 215 136 136 ASP C C 177.831 0.300 1 216 136 136 ASP CA C 56.370 0.300 1 217 136 136 ASP CB C 41.967 0.300 1 218 136 136 ASP N N 118.798 0.300 1 219 137 137 THR H H 7.431 0.030 1 220 137 137 THR C C 175.104 0.300 1 221 137 137 THR CA C 63.475 0.300 1 222 137 137 THR CB C 68.832 0.300 1 223 137 137 THR N N 114.285 0.300 1 224 138 138 ARG H H 8.184 0.030 1 225 138 138 ARG C C 177.084 0.300 1 226 138 138 ARG CA C 60.936 0.300 1 227 138 138 ARG CB C 30.163 0.300 1 228 138 138 ARG N N 124.206 0.300 1 229 139 139 GLU H H 8.532 0.030 1 230 139 139 GLU C C 179.125 0.300 1 231 139 139 GLU CA C 59.537 0.300 1 232 139 139 GLU CB C 28.471 0.300 1 233 139 139 GLU N N 117.521 0.300 1 234 140 140 SER H H 7.952 0.030 1 235 140 140 SER C C 176.239 0.300 1 236 140 140 SER CA C 61.709 0.300 1 237 140 140 SER CB C 62.422 0.300 1 238 140 140 SER N N 117.234 0.300 1 239 141 141 ILE H H 7.872 0.030 1 240 141 141 ILE C C 179.108 0.300 1 241 141 141 ILE CA C 65.869 0.300 1 242 141 141 ILE CB C 37.617 0.300 1 243 141 141 ILE N N 122.464 0.300 1 244 142 142 LYS H H 8.000 0.030 1 245 142 142 LYS C C 178.735 0.300 1 246 142 142 LYS CA C 59.831 0.300 1 247 142 142 LYS CB C 32.435 0.300 1 248 142 142 LYS N N 119.036 0.300 1 249 143 143 ARG H H 7.934 0.030 1 250 143 143 ARG C C 178.498 0.300 1 251 143 143 ARG CA C 59.132 0.300 1 252 143 143 ARG CB C 30.514 0.300 1 253 143 143 ARG N N 118.620 0.300 1 254 144 144 GLU H H 7.831 0.030 1 255 144 144 GLU C C 175.712 0.300 1 256 144 144 GLU CA C 56.960 0.300 1 257 144 144 GLU CB C 30.385 0.300 1 258 144 144 GLU N N 114.858 0.300 1 259 145 145 ASN H H 7.282 0.030 1 260 145 145 ASN C C 170.179 0.300 1 261 145 145 ASN CA C 50.866 0.300 1 262 145 145 ASN CB C 40.723 0.300 1 263 145 145 ASN N N 116.747 0.300 1 264 146 146 PRO C C 178.740 0.300 1 265 146 146 PRO CA C 64.304 0.300 1 266 146 146 PRO CB C 31.404 0.300 1 267 147 147 GLY H H 8.768 0.030 1 268 147 147 GLY C C 174.972 0.300 1 269 147 147 GLY CA C 45.252 0.300 1 270 147 147 GLY N N 111.951 0.300 1 271 148 148 ILE H H 7.858 0.030 1 272 148 148 ILE C C 174.803 0.300 1 273 148 148 ILE CA C 62.335 0.300 1 274 148 148 ILE CB C 38.221 0.300 1 275 148 148 ILE N N 121.990 0.300 1 276 149 149 LYS H H 8.518 0.030 1 277 149 149 LYS C C 179.367 0.300 1 278 149 149 LYS CA C 55.928 0.300 1 279 149 149 LYS CB C 33.992 0.300 1 280 149 149 LYS N N 126.161 0.300 1 281 150 150 VAL H H 8.808 0.030 1 282 150 150 VAL C C 178.325 0.300 1 283 150 150 VAL CA C 66.569 0.300 1 284 150 150 VAL CB C 31.634 0.300 1 285 150 150 VAL N N 121.373 0.300 1 286 151 151 THR H H 7.616 0.030 1 287 151 151 THR C C 176.103 0.300 1 288 151 151 THR CA C 63.862 0.300 1 289 151 151 THR CB C 68.005 0.300 1 290 151 151 THR N N 109.328 0.300 1 291 152 152 GLU H H 7.555 0.030 1 292 152 152 GLU C C 178.036 0.300 1 293 152 152 GLU CA C 56.978 0.300 1 294 152 152 GLU CB C 30.369 0.300 1 295 152 152 GLU N N 120.432 0.300 1 296 153 153 ILE H H 7.650 0.030 1 297 153 153 ILE C C 177.377 0.300 1 298 153 153 ILE CA C 56.973 0.300 1 299 153 153 ILE CB C 37.444 0.300 1 300 153 153 ILE N N 122.290 0.300 1 301 154 154 ALA H H 8.332 0.030 1 302 154 154 ALA C C 180.392 0.300 1 303 154 154 ALA CA C 55.652 0.300 1 304 154 154 ALA CB C 17.901 0.300 1 305 154 154 ALA N N 120.678 0.300 1 306 155 155 LYS H H 7.658 0.030 1 307 155 155 LYS C C 179.267 0.300 1 308 155 155 LYS CA C 59.481 0.300 1 309 155 155 LYS CB C 32.569 0.300 1 310 155 155 LYS N N 120.100 0.300 1 311 156 156 LYS H H 8.247 0.030 1 312 156 156 LYS C C 179.602 0.300 1 313 156 156 LYS CA C 58.303 0.300 1 314 156 156 LYS CB C 31.517 0.300 1 315 156 156 LYS N N 121.418 0.300 1 316 157 157 GLY H H 9.287 0.030 1 317 157 157 GLY C C 175.410 0.300 1 318 157 157 GLY CA C 47.368 0.300 1 319 157 157 GLY N N 106.608 0.300 1 320 158 158 GLY H H 8.669 0.030 1 321 158 158 GLY C C 176.116 0.300 1 322 158 158 GLY CA C 47.829 0.300 1 323 158 158 GLY N N 109.938 0.300 1 324 159 159 GLU H H 7.583 0.030 1 325 159 159 GLU C C 179.303 0.300 1 326 159 159 GLU CA C 59.168 0.300 1 327 159 159 GLU CB C 29.558 0.300 1 328 159 159 GLU N N 121.576 0.300 1 329 160 160 MET H H 8.048 0.030 1 330 160 160 MET C C 179.246 0.300 1 331 160 160 MET CA C 58.947 0.300 1 332 160 160 MET CB C 34.856 0.300 1 333 160 160 MET N N 119.498 0.300 1 334 161 161 TRP H H 8.949 0.030 1 335 161 161 TRP C C 177.692 0.300 1 336 161 161 TRP CA C 59.113 0.300 1 337 161 161 TRP CB C 30.469 0.300 1 338 161 161 TRP N N 121.973 0.300 1 339 162 162 LYS H H 7.399 0.030 1 340 162 162 LYS C C 178.049 0.300 1 341 162 162 LYS CA C 59.260 0.300 1 342 162 162 LYS CB C 32.428 0.300 1 343 162 162 LYS N N 115.982 0.300 1 344 163 163 GLU H H 6.909 0.030 1 345 163 163 GLU C C 175.959 0.300 1 346 163 163 GLU CA C 55.745 0.300 1 347 163 163 GLU CB C 30.498 0.300 1 348 163 163 GLU N N 114.308 0.300 1 349 164 164 LEU H H 6.954 0.030 1 350 164 164 LEU C C 177.382 0.300 1 351 164 164 LEU CA C 55.561 0.300 1 352 164 164 LEU CB C 42.516 0.300 1 353 164 164 LEU N N 122.865 0.300 1 354 165 165 LYS H H 8.509 0.030 1 355 165 165 LYS C C 176.912 0.300 1 356 165 165 LYS CA C 58.395 0.300 1 357 165 165 LYS CB C 34.165 0.300 1 358 165 165 LYS N N 126.326 0.300 1 359 166 166 ASP H H 7.844 0.030 1 360 166 166 ASP C C 175.897 0.300 1 361 166 166 ASP CA C 52.983 0.300 1 362 166 166 ASP CB C 40.680 0.300 1 363 166 166 ASP N N 116.860 0.300 1 364 167 167 LYS H H 8.675 0.030 1 365 167 167 LYS C C 178.177 0.300 1 366 167 167 LYS CA C 56.278 0.300 1 367 167 167 LYS CB C 33.873 0.300 1 368 167 167 LYS N N 124.941 0.300 1 369 168 168 SER H H 8.366 0.030 1 370 168 168 SER C C 175.963 0.300 1 371 168 168 SER CA C 62.960 0.300 1 372 168 168 SER N N 117.815 0.300 1 373 169 169 LYS H H 8.631 0.030 1 374 169 169 LYS C C 178.901 0.300 1 375 169 169 LYS CA C 59.702 0.300 1 376 169 169 LYS CB C 31.749 0.300 1 377 169 169 LYS N N 122.543 0.300 1 378 170 170 TRP H H 7.123 0.030 1 379 170 170 TRP C C 178.141 0.300 1 380 170 170 TRP CA C 56.499 0.300 1 381 170 170 TRP CB C 30.541 0.300 1 382 170 170 TRP N N 119.297 0.300 1 383 171 171 GLU H H 8.540 0.030 1 384 171 171 GLU C C 180.212 0.300 1 385 171 171 GLU CA C 60.015 0.300 1 386 171 171 GLU CB C 29.938 0.300 1 387 171 171 GLU N N 120.712 0.300 1 388 172 172 ASP H H 8.918 0.030 1 389 172 172 ASP C C 178.716 0.300 1 390 172 172 ASP CA C 57.511 0.300 1 391 172 172 ASP CB C 40.378 0.300 1 392 172 172 ASP N N 121.488 0.300 1 393 173 173 ALA H H 7.455 0.030 1 394 173 173 ALA C C 180.787 0.300 1 395 173 173 ALA CA C 55.247 0.300 1 396 173 173 ALA CB C 18.598 0.300 1 397 173 173 ALA N N 121.947 0.300 1 398 174 174 ALA H H 8.570 0.030 1 399 174 174 ALA C C 180.118 0.300 1 400 174 174 ALA CA C 55.156 0.300 1 401 174 174 ALA CB C 18.120 0.300 1 402 174 174 ALA N N 122.783 0.300 1 403 175 175 ALA H H 8.189 0.030 1 404 175 175 ALA C C 181.206 0.300 1 405 175 175 ALA CA C 55.339 0.300 1 406 175 175 ALA CB C 17.901 0.300 1 407 175 175 ALA N N 123.240 0.300 1 408 176 176 LYS H H 7.962 0.030 1 409 176 176 LYS C C 179.216 0.300 1 410 176 176 LYS CA C 59.132 0.300 1 411 176 176 LYS CB C 32.353 0.300 1 412 176 176 LYS N N 119.560 0.300 1 413 177 177 ASP H H 8.098 0.030 1 414 177 177 ASP C C 177.769 0.300 1 415 177 177 ASP CA C 57.125 0.300 1 416 177 177 ASP CB C 41.888 0.300 1 417 177 177 ASP N N 121.330 0.300 1 418 178 178 LYS H H 8.202 0.030 1 419 178 178 LYS C C 178.452 0.300 1 420 178 178 LYS CA C 59.463 0.300 1 421 178 178 LYS CB C 32.130 0.300 1 422 178 178 LYS N N 120.091 0.300 1 423 179 179 GLN H H 7.714 0.030 1 424 179 179 GLN C C 177.208 0.300 1 425 179 179 GLN CA C 58.450 0.300 1 426 179 179 GLN CB C 28.341 0.300 1 427 179 179 GLN N N 119.378 0.300 1 428 180 180 ARG H H 7.995 0.030 1 429 180 180 ARG C C 178.501 0.300 1 430 180 180 ARG CA C 59.076 0.300 1 431 180 180 ARG CB C 28.039 0.300 1 432 180 180 ARG N N 121.055 0.300 1 433 181 181 TYR H H 8.272 0.030 1 434 181 181 TYR C C 176.423 0.300 1 435 181 181 TYR CA C 61.671 0.300 1 436 181 181 TYR CB C 38.674 0.300 1 437 181 181 TYR N N 120.539 0.300 1 438 182 182 HIS H H 8.251 0.030 1 439 182 182 HIS C C 177.739 0.300 1 440 182 182 HIS CA C 59.224 0.300 1 441 182 182 HIS CB C 29.380 0.300 1 442 182 182 HIS N N 118.053 0.300 1 443 183 183 ASP H H 8.662 0.030 1 444 183 183 ASP C C 178.749 0.300 1 445 183 183 ASP CA C 57.217 0.300 1 446 183 183 ASP CB C 40.291 0.300 1 447 183 183 ASP N N 121.066 0.300 1 448 184 184 GLU H H 8.620 0.030 1 449 184 184 GLU C C 180.013 0.300 1 450 184 184 GLU CA C 59.334 0.300 1 451 184 184 GLU CB C 29.815 0.300 1 452 184 184 GLU N N 120.371 0.300 1 453 185 185 MET H H 8.366 0.030 1 454 185 185 MET C C 178.589 0.300 1 455 185 185 MET CA C 56.315 0.300 1 456 185 185 MET CB C 31.145 0.300 1 457 185 185 MET N N 118.854 0.300 1 458 186 186 ARG H H 7.698 0.030 1 459 186 186 ARG C C 176.993 0.300 1 460 186 186 ARG CA C 58.340 0.300 1 461 186 186 ARG CB C 30.252 0.300 1 462 186 186 ARG N N 119.632 0.300 1 463 187 187 ASN H H 7.537 0.030 1 464 187 187 ASN C C 174.459 0.300 1 465 187 187 ASN CA C 53.167 0.300 1 466 187 187 ASN CB C 39.557 0.300 1 467 187 187 ASN N N 115.278 0.300 1 468 188 188 TYR H H 7.623 0.030 1 469 188 188 TYR C C 174.632 0.300 1 470 188 188 TYR CA C 58.395 0.300 1 471 188 188 TYR CB C 39.041 0.300 1 472 188 188 TYR N N 121.715 0.300 1 473 189 189 LYS H H 8.020 0.030 1 474 189 189 LYS C C 173.010 0.300 1 475 189 189 LYS CA C 53.185 0.300 1 476 189 189 LYS CB C 33.302 0.300 1 477 189 189 LYS N N 127.225 0.300 1 478 190 190 PRO C C 176.905 0.300 1 479 190 190 PRO CA C 62.979 0.300 1 480 190 190 PRO CB C 32.008 0.300 1 481 191 191 GLU H H 8.442 0.030 1 482 191 191 GLU C C 175.268 0.300 1 483 191 191 GLU CA C 56.573 0.300 1 484 191 191 GLU CB C 30.412 0.300 1 485 191 191 GLU N N 121.184 0.300 1 486 192 192 ALA H H 7.899 0.030 1 487 192 192 ALA C C 182.444 0.300 1 488 192 192 ALA CA C 53.885 0.300 1 489 192 192 ALA CB C 20.447 0.300 1 490 192 192 ALA N N 130.423 0.300 1 stop_ save_