data_27607 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence specific chemical shift assignments of the Caenorhabditis elegans SAS-6 N-terminal domain ; _BMRB_accession_number 27607 _BMRB_flat_file_name bmr27607.str _Entry_type original _Submission_date 2018-09-13 _Accession_date 2018-09-13 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Erat Michele C. . 2 Vakonakis Ioannis . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 153 "13C chemical shifts" 320 "15N chemical shifts" 153 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-03-21 update BMRB 'update entry citation' 2019-02-15 original author 'original release' stop_ _Original_release_date 2018-09-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; A dynamically interacting flexible loop assists oligomerisation of the Caenorhabditis elegans centriolar protein SAS-6 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30837637 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Busch Julia . . 2 Erat Michele C. . 3 Blank Iris D. . 4 Musgaard Maria . . 5 Biggin Philip C. . 6 Vakonakis Ioannis . . stop_ _Journal_abbreviation 'Sci. Rep.' _Journal_name_full 'Scientific reports' _Journal_volume 9 _Journal_issue 1 _Journal_ISSN 2045-2322 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3526 _Page_last 3526 _Year 2019 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name CeSAS-6N _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CeSAS-6N $CeSAS-6N 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_CeSAS-6N _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CeSAS-6N _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'Centriole assembly' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 170 _Mol_residue_sequence ; GSMTSKIALFDQTLIASLLQ PLSLNQPDFKAYKTKVKLKI SEQRNETSGEKELKFEISRS DDFEFLFSETLNNEKYQILA RDHDLTVDFDAFPKVIIQHL LCKNIVKNLEEDGEVDARKK AGYHEIADPGKPTEINIILD AEKNFCSFELFSKTPESKGK IFSIKLHAVR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -1 GLY 2 0 SER 3 1 MET 4 2 THR 5 3 SER 6 4 LYS 7 5 ILE 8 6 ALA 9 7 LEU 10 8 PHE 11 9 ASP 12 10 GLN 13 11 THR 14 12 LEU 15 13 ILE 16 14 ALA 17 15 SER 18 16 LEU 19 17 LEU 20 18 GLN 21 19 PRO 22 20 LEU 23 21 SER 24 22 LEU 25 23 ASN 26 24 GLN 27 25 PRO 28 26 ASP 29 27 PHE 30 28 LYS 31 29 ALA 32 30 TYR 33 31 LYS 34 32 THR 35 33 LYS 36 34 VAL 37 35 LYS 38 36 LEU 39 37 LYS 40 38 ILE 41 39 SER 42 40 GLU 43 41 GLN 44 42 ARG 45 43 ASN 46 44 GLU 47 45 THR 48 46 SER 49 47 GLY 50 48 GLU 51 49 LYS 52 50 GLU 53 51 LEU 54 52 LYS 55 53 PHE 56 54 GLU 57 55 ILE 58 56 SER 59 57 ARG 60 58 SER 61 59 ASP 62 60 ASP 63 61 PHE 64 62 GLU 65 63 PHE 66 64 LEU 67 65 PHE 68 66 SER 69 67 GLU 70 68 THR 71 69 LEU 72 70 ASN 73 71 ASN 74 72 GLU 75 73 LYS 76 74 TYR 77 75 GLN 78 76 ILE 79 77 LEU 80 78 ALA 81 79 ARG 82 80 ASP 83 81 HIS 84 82 ASP 85 83 LEU 86 84 THR 87 85 VAL 88 86 ASP 89 87 PHE 90 88 ASP 91 89 ALA 92 90 PHE 93 91 PRO 94 92 LYS 95 93 VAL 96 94 ILE 97 95 ILE 98 96 GLN 99 97 HIS 100 98 LEU 101 99 LEU 102 100 CYS 103 101 LYS 104 102 ASN 105 103 ILE 106 104 VAL 107 105 LYS 108 106 ASN 109 107 LEU 110 108 GLU 111 109 GLU 112 110 ASP 113 111 GLY 114 112 GLU 115 113 VAL 116 114 ASP 117 115 ALA 118 116 ARG 119 117 LYS 120 118 LYS 121 119 ALA 122 120 GLY 123 121 TYR 124 122 HIS 125 123 GLU 126 124 ILE 127 125 ALA 128 126 ASP 129 127 PRO 130 128 GLY 131 129 LYS 132 130 PRO 133 131 THR 134 132 GLU 135 133 ILE 136 134 ASN 137 135 ILE 138 136 ILE 139 137 LEU 140 138 ASP 141 139 ALA 142 140 GLU 143 141 LYS 144 142 ASN 145 143 PHE 146 144 CYS 147 145 SER 148 146 PHE 149 147 GLU 150 148 LEU 151 149 PHE 152 150 SER 153 151 LYS 154 152 THR 155 153 PRO 156 154 GLU 157 155 SER 158 156 LYS 159 157 GLY 160 158 LYS 161 159 ILE 162 160 PHE 163 161 SER 164 162 ILE 165 163 LYS 166 164 LEU 167 165 HIS 168 166 ALA 169 167 VAL 170 168 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value UNP O62479 'Spindle assembly abnormal protein 6' . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $CeSAS-6N 'C. elegans' 6239 Eukaryota Metazoa Caenorhabditis elegans sas6 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 $CeSAS-6N 'recombinant technology' . Escherichia coli BL21(DE3) pHis 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CeSAS-6N 0.75 mM 0.5 1 '[U-98% 13C; U-98% 15N]' 'sodium chloride' 150 mM . . 'natural abundance' 'sodium phosphate' 20 mM . . 'natural abundance' DTT 2 mM . . 'natural abundance' D2O 5 '% v/v' . . 'natural abundance' 'sodium azide' 0.02 '% w/v' . . 'natural abundance' DSS 50 uM . . '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_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_PIPP _Saveframe_category software _Name PIPP _Version . loop_ _Vendor _Address _Electronic_address Garrett . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details 'TCI cryoprobe' 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_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _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' 0.38 . M pH 7 . pH pressure 1 . atm temperature 273 . 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 . loop_ _Software_label $TOPSPIN $NMRPipe $SPARKY $PIPP stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D HNCA' 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 CeSAS-6N _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 3 MET CA C 55.55 0.1 1 2 1 3 MET CB C 32.51 0.1 1 3 2 4 THR H H 8.259 0.02 1 4 2 4 THR CA C 61.99 0.1 1 5 2 4 THR CB C 69.85 0.1 1 6 2 4 THR N N 115.2 0.1 1 7 3 5 SER H H 8.384 0.02 1 8 3 5 SER CA C 58.52 0.1 1 9 3 5 SER CB C 63.95 0.1 1 10 3 5 SER N N 118.34 0.1 1 11 4 6 LYS H H 8.258 0.02 1 12 4 6 LYS CA C 56.25 0.1 1 13 4 6 LYS CB C 33.7 0.1 1 14 4 6 LYS N N 123.56 0.1 1 15 5 7 ILE H H 8.68 0.02 1 16 5 7 ILE CA C 60.34 0.1 1 17 5 7 ILE CB C 40.31 0.1 1 18 5 7 ILE N N 124.05 0.1 1 19 6 8 ALA H H 8.758 0.02 1 20 6 8 ALA CA C 52.32 0.1 1 21 6 8 ALA CB C 18.45 0.1 1 22 6 8 ALA N N 129.34 0.1 1 23 7 9 LEU H H 8.728 0.02 1 24 7 9 LEU CA C 56.06 0.1 1 25 7 9 LEU CB C 43.04 0.1 1 26 7 9 LEU N N 124.01 0.1 1 27 8 10 PHE H H 7.849 0.02 1 28 8 10 PHE CA C 57.81 0.1 1 29 8 10 PHE CB C 43.51 0.1 1 30 8 10 PHE N N 118.08 0.1 1 31 9 11 ASP H H 8.318 0.02 1 32 9 11 ASP CA C 53.81 0.1 1 33 9 11 ASP CB C 40.68 0.1 1 34 9 11 ASP N N 129.4 0.1 1 35 10 12 GLN H H 8.04 0.02 1 36 10 12 GLN CA C 54.03 0.1 1 37 10 12 GLN CB C 33.37 0.1 1 38 10 12 GLN N N 120.31 0.1 1 39 11 13 THR H H 8.605 0.02 1 40 11 13 THR CA C 62.81 0.1 1 41 11 13 THR CB C 69.35 0.1 1 42 11 13 THR N N 118.43 0.1 1 43 12 14 LEU H H 9.635 0.02 1 44 12 14 LEU CA C 53.38 0.1 1 45 12 14 LEU CB C 45.64 0.1 1 46 12 14 LEU N N 127.11 0.1 1 47 13 15 ILE H H 8.441 0.02 1 48 13 15 ILE CA C 60.5 0.1 1 49 13 15 ILE CB C 37.54 0.1 1 50 13 15 ILE N N 120.64 0.1 1 51 14 16 ALA H H 8.873 0.02 1 52 14 16 ALA CA C 50.19 0.1 1 53 14 16 ALA CB C 23.77 0.1 1 54 14 16 ALA N N 129.15 0.1 1 55 15 17 SER H H 8.388 0.02 1 56 15 17 SER CA C 58.42 0.1 1 57 15 17 SER CB C 63.7 0.1 1 58 15 17 SER N N 115.69 0.1 1 59 16 18 LEU H H 9.054 0.02 1 60 16 18 LEU CA C 53.92 0.1 1 61 16 18 LEU CB C 43.43 0.1 1 62 16 18 LEU N N 128.77 0.1 1 63 17 19 LEU H H 8.989 0.02 1 64 17 19 LEU CA C 54.25 0.1 1 65 17 19 LEU CB C 43.74 0.1 1 66 17 19 LEU N N 126.9 0.1 1 67 18 20 GLN H H 8.72 0.02 1 68 18 20 GLN CA C 52.62 0.1 1 69 18 20 GLN CB C 31.16 0.1 1 70 18 20 GLN N N 121.85 0.1 1 71 19 21 PRO CA C 62.92 0.1 1 72 19 21 PRO CB C 31.93 0.1 1 73 20 22 LEU H H 8.379 0.02 1 74 20 22 LEU CA C 56.33 0.1 1 75 20 22 LEU CB C 42.43 0.1 1 76 20 22 LEU N N 122.24 0.1 1 77 21 23 SER H H 8.13 0.02 1 78 21 23 SER CA C 57.63 0.1 1 79 21 23 SER CB C 64.64 0.1 1 80 21 23 SER N N 113.05 0.1 1 81 22 24 LEU H H 8.396 0.02 1 82 22 24 LEU CA C 56.52 0.1 1 83 22 24 LEU CB C 42.26 0.1 1 84 22 24 LEU N N 121.74 0.1 1 85 23 25 ASN H H 8.378 0.02 1 86 23 25 ASN CA C 53.66 0.1 1 87 23 25 ASN CB C 38.86 0.1 1 88 23 25 ASN N N 115.44 0.1 1 89 24 26 GLN H H 7.737 0.02 1 90 24 26 GLN CA C 53.62 0.1 1 91 24 26 GLN CB C 29.89 0.1 1 92 24 26 GLN N N 119.29 0.1 1 93 25 27 PRO CA C 63.55 0.1 1 94 25 27 PRO CB C 31.35 0.1 1 95 26 28 ASP H H 8.06 0.02 1 96 26 28 ASP CA C 54.01 0.1 1 97 26 28 ASP CB C 41.66 0.1 1 98 26 28 ASP N N 119.17 0.1 1 99 27 29 PHE H H 8.381 0.02 1 100 27 29 PHE CA C 57.69 0.1 1 101 27 29 PHE CB C 41.23 0.1 1 102 27 29 PHE N N 120.02 0.1 1 103 28 30 LYS H H 8.509 0.02 1 104 28 30 LYS CA C 55.42 0.1 1 105 28 30 LYS CB C 34.27 0.1 1 106 28 30 LYS N N 123.32 0.1 1 107 29 31 ALA H H 8.417 0.02 1 108 29 31 ALA CA C 51.38 0.1 1 109 29 31 ALA CB C 21.16 0.1 1 110 29 31 ALA N N 126.46 0.1 1 111 30 32 TYR H H 8.568 0.02 1 112 30 32 TYR CA C 56.58 0.1 1 113 30 32 TYR CB C 40.2 0.1 1 114 30 32 TYR N N 119.89 0.1 1 115 31 33 LYS H H 8.686 0.02 1 116 31 33 LYS CA C 55.82 0.1 1 117 31 33 LYS CB C 33.37 0.1 1 118 31 33 LYS N N 123.32 0.1 1 119 32 34 THR H H 9.095 0.02 1 120 32 34 THR CA C 60.56 0.1 1 121 32 34 THR CB C 70.63 0.1 1 122 32 34 THR N N 119.12 0.1 1 123 33 35 LYS H H 8.184 0.02 1 124 33 35 LYS CA C 56.06 0.1 1 125 33 35 LYS CB C 33.76 0.1 1 126 33 35 LYS N N 123.51 0.1 1 127 34 36 VAL H H 9.318 0.02 1 128 34 36 VAL CA C 59.34 0.1 1 129 34 36 VAL CB C 35.26 0.1 1 130 34 36 VAL N N 119.56 0.1 1 131 35 37 LYS H H 9.072 0.02 1 132 35 37 LYS CA C 55.24 0.1 1 133 35 37 LYS CB C 32.11 0.1 1 134 35 37 LYS N N 124.54 0.1 1 135 36 38 LEU H H 8.599 0.02 1 136 36 38 LEU CA C 53.42 0.1 1 137 36 38 LEU CB C 45.72 0.1 1 138 36 38 LEU N N 127.81 0.1 1 139 37 39 LYS H H 9.062 0.02 1 140 37 39 LYS CA C 54.28 0.1 1 141 37 39 LYS CB C 36.44 0.1 1 142 37 39 LYS N N 125.98 0.1 1 143 38 40 ILE H H 9.123 0.02 1 144 38 40 ILE CA C 59.7 0.1 1 145 38 40 ILE CB C 40.45 0.1 1 146 38 40 ILE N N 125.02 0.1 1 147 39 41 SER H H 9.097 0.02 1 148 39 41 SER CA C 56.89 0.1 1 149 39 41 SER CB C 66.02 0.1 1 150 39 41 SER N N 121.49 0.1 1 151 40 42 GLU H H 9.187 0.02 1 152 40 42 GLU CA C 54.91 0.1 1 153 40 42 GLU CB C 32.57 0.1 1 154 40 42 GLU N N 123.46 0.1 1 155 41 43 GLN H H 8.844 0.02 1 156 41 43 GLN CA C 53.87 0.1 1 157 41 43 GLN CB C 31.45 0.1 1 158 41 43 GLN N N 120.63 0.1 1 159 42 44 ARG H H 8.607 0.02 1 160 42 44 ARG CA C 53.74 0.1 1 161 42 44 ARG CB C 31.81 0.1 1 162 42 44 ARG N N 119.26 0.1 1 163 43 45 ASN H H 9.068 0.02 1 164 43 45 ASN CA C 55.26 0.1 1 165 43 45 ASN CB C 40.28 0.1 1 166 43 45 ASN N N 124.58 0.1 1 167 44 46 GLU H H 9.341 0.02 1 168 44 46 GLU CA C 59.32 0.1 1 169 44 46 GLU CB C 29.98 0.1 1 170 44 46 GLU N N 127.76 0.1 1 171 45 47 THR H H 8.417 0.02 1 172 45 47 THR CA C 64.66 0.1 1 173 45 47 THR CB C 69.05 0.1 1 174 45 47 THR N N 113.91 0.1 1 175 46 48 SER H H 8.707 0.02 1 176 46 48 SER CA C 58.32 0.1 1 177 46 48 SER CB C 65.63 0.1 1 178 46 48 SER N N 115.73 0.1 1 179 47 49 GLY H H 8.177 0.02 1 180 47 49 GLY CA C 46.07 0.1 1 181 47 49 GLY N N 111.8 0.1 1 182 48 50 GLU H H 7.939 0.02 1 183 48 50 GLU CA C 56.65 0.1 1 184 48 50 GLU CB C 31.27 0.1 1 185 48 50 GLU N N 120.07 0.1 1 186 49 51 LYS H H 8.893 0.02 1 187 49 51 LYS CA C 58.17 0.1 1 188 49 51 LYS CB C 32.92 0.1 1 189 49 51 LYS N N 123.31 0.1 1 190 50 52 GLU H H 8.985 0.02 1 191 50 52 GLU CA C 54.17 0.1 1 192 50 52 GLU CB C 35.19 0.1 1 193 50 52 GLU N N 123.32 0.1 1 194 51 53 LEU H H 9.034 0.02 1 195 51 53 LEU CA C 52.92 0.1 1 196 51 53 LEU CB C 46.8 0.1 1 197 51 53 LEU N N 120.98 0.1 1 198 52 54 LYS H H 9.553 0.02 1 199 52 54 LYS CA C 55.36 0.1 1 200 52 54 LYS CB C 35.64 0.1 1 201 52 54 LYS N N 126.79 0.1 1 202 53 55 PHE H H 9.367 0.02 1 203 53 55 PHE CA C 56.76 0.1 1 204 53 55 PHE CB C 42.74 0.1 1 205 53 55 PHE N N 126.99 0.1 1 206 54 56 GLU H H 9.129 0.02 1 207 54 56 GLU CA C 55.46 0.1 1 208 54 56 GLU CB C 35.01 0.1 1 209 54 56 GLU N N 121.45 0.1 1 210 55 57 ILE CA C 58.56 0.1 1 211 55 57 ILE CB C 41.5 0.1 1 212 56 58 SER H H 8.954 0.02 1 213 56 58 SER CA C 57.21 0.1 1 214 56 58 SER CB C 66.78 0.1 1 215 56 58 SER N N 117.98 0.1 1 216 57 59 ARG H H 9.025 0.02 1 217 57 59 ARG CB C 35.24 0.1 1 218 57 59 ARG N N 117.98 0.1 1 219 58 60 SER CA C 60.31 0.1 1 220 58 60 SER CB C 62.97 0.1 1 221 59 61 ASP H H 8.602 0.02 1 222 59 61 ASP CA C 53.46 0.1 1 223 59 61 ASP CB C 40.28 0.1 1 224 59 61 ASP N N 116.98 0.1 1 225 60 62 ASP H H 7.173 0.02 1 226 60 62 ASP CA C 54 0.1 1 227 60 62 ASP CB C 41.45 0.1 1 228 60 62 ASP N N 117.25 0.1 1 229 61 63 PHE H H 8.812 0.02 1 230 61 63 PHE CA C 58.85 0.1 1 231 61 63 PHE CB C 38.56 0.1 1 232 61 63 PHE N N 125.25 0.1 1 233 62 64 GLU H H 8.205 0.02 1 234 62 64 GLU N N 117.1 0.1 1 235 64 66 LEU CA C 55.27 0.1 1 236 64 66 LEU CB C 44.38 0.1 1 237 65 67 PHE H H 8.566 0.02 1 238 65 67 PHE CA C 55.65 0.1 1 239 65 67 PHE CB C 44.18 0.1 1 240 65 67 PHE N N 123.2 0.1 1 241 66 68 SER H H 9.562 0.02 1 242 66 68 SER CA C 57.12 0.1 1 243 66 68 SER CB C 67.64 0.1 1 244 66 68 SER N N 116.28 0.1 1 245 67 69 GLU H H 8.899 0.02 1 246 67 69 GLU CA C 56.35 0.1 1 247 67 69 GLU CB C 34.94 0.1 1 248 67 69 GLU N N 122.89 0.1 1 249 68 70 THR H H 9.521 0.02 1 250 68 70 THR CA C 61.63 0.1 1 251 68 70 THR CB C 70.45 0.1 1 252 68 70 THR N N 122.22 0.1 1 253 69 71 LEU H H 9.927 0.02 1 254 69 71 LEU CA C 54.62 0.1 1 255 69 71 LEU CB C 46.24 0.1 1 256 69 71 LEU N N 125.25 0.1 1 257 70 72 ASN H H 7.043 0.02 1 258 70 72 ASN CA C 50.78 0.1 1 259 70 72 ASN CB C 40.03 0.1 1 260 70 72 ASN N N 119.44 0.1 1 261 71 73 ASN H H 9.091 0.02 1 262 71 73 ASN CA C 57.6 0.1 1 263 71 73 ASN CB C 39.09 0.1 1 264 71 73 ASN N N 118.91 0.1 1 265 72 74 GLU H H 8.309 0.02 1 266 72 74 GLU CA C 60.36 0.1 1 267 72 74 GLU CB C 29.31 0.1 1 268 72 74 GLU N N 118.93 0.1 1 269 73 75 LYS H H 8.469 0.02 1 270 73 75 LYS CA C 59.6 0.1 1 271 73 75 LYS CB C 34.55 0.1 1 272 73 75 LYS N N 118.13 0.1 1 273 74 76 TYR H H 8.937 0.02 1 274 74 76 TYR CA C 62.02 0.1 1 275 74 76 TYR CB C 38.95 0.1 1 276 74 76 TYR N N 121.05 0.1 1 277 75 77 GLN H H 8.385 0.02 1 278 75 77 GLN CA C 58.86 0.1 1 279 75 77 GLN CB C 27.95 0.1 1 280 75 77 GLN N N 116.57 0.1 1 281 76 78 ILE H H 6.959 0.02 1 282 76 78 ILE CA C 64.54 0.1 1 283 76 78 ILE CB C 38.24 0.1 1 284 76 78 ILE N N 118.31 0.1 1 285 77 79 LEU H H 7.12 0.02 1 286 77 79 LEU CA C 58.37 0.1 1 287 77 79 LEU CB C 42.77 0.1 1 288 77 79 LEU N N 121.62 0.1 1 289 78 80 ALA H H 9.062 0.02 1 290 78 80 ALA CA C 55.22 0.1 1 291 78 80 ALA CB C 17.16 0.1 1 292 78 80 ALA N N 121.23 0.1 1 293 79 81 ARG H H 7.485 0.02 1 294 79 81 ARG CA C 58.7 0.1 1 295 79 81 ARG CB C 29.95 0.1 1 296 79 81 ARG N N 117.76 0.1 1 297 80 82 ASP H H 8.058 0.02 1 298 80 82 ASP CA C 56.73 0.1 1 299 80 82 ASP CB C 40.34 0.1 1 300 80 82 ASP N N 119.18 0.1 1 301 81 83 HIS H H 7.667 0.02 1 302 81 83 HIS CA C 56.51 0.1 1 303 81 83 HIS CB C 30.24 0.1 1 304 81 83 HIS N N 114.47 0.1 1 305 82 84 ASP H H 7.816 0.02 1 306 82 84 ASP CA C 55.55 0.1 1 307 82 84 ASP CB C 39.51 0.1 1 308 82 84 ASP N N 119.86 0.1 1 309 83 85 LEU H H 8.435 0.02 1 310 83 85 LEU CA C 54.55 0.1 1 311 83 85 LEU CB C 39.3 0.1 1 312 83 85 LEU N N 117.7 0.1 1 313 86 88 ASP H H 8.19 0.02 1 314 86 88 ASP CA C 53.05 0.1 1 315 86 88 ASP CB C 39.33 0.1 1 316 86 88 ASP N N 118.58 0.1 1 317 87 89 PHE H H 8.05 0.02 1 318 87 89 PHE CA C 58.77 0.1 1 319 87 89 PHE CB C 39.64 0.1 1 320 87 89 PHE N N 118.9 0.1 1 321 88 90 ASP H H 8.017 0.02 1 322 88 90 ASP CA C 56.65 0.1 1 323 88 90 ASP CB C 40.75 0.1 1 324 88 90 ASP N N 115.2 0.1 1 325 89 91 ALA H H 7.717 0.02 1 326 89 91 ALA CA C 52.91 0.1 1 327 89 91 ALA CB C 19.62 0.1 1 328 89 91 ALA N N 121.17 0.1 1 329 90 92 PHE H H 7.781 0.02 1 330 90 92 PHE CA C 61.64 0.1 1 331 90 92 PHE CB C 36.6 0.1 1 332 90 92 PHE N N 118.85 0.1 1 333 91 93 PRO CA C 65.91 0.1 1 334 91 93 PRO CB C 29.83 0.1 1 335 92 94 LYS H H 7.041 0.02 1 336 92 94 LYS CA C 59.61 0.1 1 337 92 94 LYS CB C 32.03 0.1 1 338 92 94 LYS N N 114.09 0.1 1 339 93 95 VAL H H 7.495 0.02 1 340 93 95 VAL CA C 66 0.1 1 341 93 95 VAL CB C 31.94 0.1 1 342 93 95 VAL N N 119.19 0.1 1 343 94 96 ILE H H 7.69 0.02 1 344 94 96 ILE CA C 63.51 0.1 1 345 94 96 ILE CB C 36.97 0.1 1 346 94 96 ILE N N 117.51 0.1 1 347 95 97 ILE H H 8.057 0.02 1 348 95 97 ILE CA C 66.18 0.1 1 349 95 97 ILE CB C 37.37 0.1 1 350 95 97 ILE N N 121.1 0.1 1 351 96 98 GLN H H 7.64 0.02 1 352 96 98 GLN CA C 59.22 0.1 1 353 96 98 GLN CB C 28 0.1 1 354 96 98 GLN N N 117.44 0.1 1 355 97 99 HIS H H 7.441 0.02 1 356 97 99 HIS CA C 59.54 0.1 1 357 97 99 HIS CB C 31.23 0.1 1 358 97 99 HIS N N 115.76 0.1 1 359 98 100 LEU H H 8.042 0.02 1 360 98 100 LEU CA C 56.76 0.1 1 361 98 100 LEU CB C 42.49 0.1 1 362 98 100 LEU N N 118.96 0.1 1 363 99 101 LEU H H 7.948 0.02 1 364 99 101 LEU CA C 55.33 0.1 1 365 99 101 LEU CB C 42.42 0.1 1 366 99 101 LEU N N 117.34 0.1 1 367 100 102 CYS H H 7.868 0.02 1 368 100 102 CYS CA C 59.78 0.1 1 369 100 102 CYS CB C 27.63 0.1 1 370 100 102 CYS N N 118.87 0.1 1 371 101 103 LYS H H 8.515 0.02 1 372 101 103 LYS CA C 56.51 0.1 1 373 101 103 LYS CB C 33.04 0.1 1 374 101 103 LYS N N 122.73 0.1 1 375 102 104 ASN H H 8.42 0.02 1 376 102 104 ASN CA C 53.69 0.1 1 377 102 104 ASN CB C 39.14 0.1 1 378 102 104 ASN N N 118.55 0.1 1 379 103 105 ILE H H 8.078 0.02 1 380 103 105 ILE CA C 61.42 0.1 1 381 103 105 ILE CB C 38.93 0.1 1 382 103 105 ILE N N 120.71 0.1 1 383 104 106 VAL H H 8.299 0.02 1 384 104 106 VAL CA C 62.48 0.1 1 385 104 106 VAL CB C 32.63 0.1 1 386 104 106 VAL N N 124.56 0.1 1 387 105 107 LYS H H 8.453 0.02 1 388 105 107 LYS CA C 56.28 0.1 1 389 105 107 LYS CB C 33.32 0.1 1 390 105 107 LYS N N 125.6 0.1 1 391 106 108 ASN H H 8.541 0.02 1 392 106 108 ASN CA C 53.28 0.1 1 393 106 108 ASN CB C 38.98 0.1 1 394 106 108 ASN N N 120.28 0.1 1 395 107 109 LEU H H 8.427 0.02 1 396 107 109 LEU CA C 55.65 0.1 1 397 107 109 LEU CB C 42.33 0.1 1 398 107 109 LEU N N 122.95 0.1 1 399 108 110 GLU H H 8.461 0.02 1 400 108 110 GLU CA C 56.92 0.1 1 401 108 110 GLU CB C 30.09 0.1 1 402 108 110 GLU N N 120.76 0.1 1 403 109 111 GLU H H 8.358 0.02 1 404 109 111 GLU CA C 56.82 0.1 1 405 109 111 GLU CB C 30.34 0.1 1 406 109 111 GLU N N 121.29 0.1 1 407 110 112 ASP H H 8.401 0.02 1 408 110 112 ASP CA C 54.76 0.1 1 409 110 112 ASP CB C 41.39 0.1 1 410 110 112 ASP N N 121.36 0.1 1 411 111 113 GLY H H 8.396 0.02 1 412 111 113 GLY CA C 45.68 0.1 1 413 111 113 GLY N N 109.18 0.1 1 414 112 114 GLU H H 8.3 0.02 1 415 112 114 GLU CA C 56.83 0.1 1 416 112 114 GLU CB C 30.17 0.1 1 417 112 114 GLU N N 120.95 0.1 1 418 113 115 VAL H H 8.181 0.02 1 419 113 115 VAL CA C 63.58 0.1 1 420 113 115 VAL CB C 32.48 0.1 1 421 113 115 VAL N N 121.11 0.1 1 422 114 116 ASP H H 8.434 0.02 1 423 114 116 ASP CA C 55.18 0.1 1 424 114 116 ASP CB C 41.21 0.1 1 425 114 116 ASP N N 122.95 0.1 1 426 115 117 ALA H H 8.338 0.02 1 427 115 117 ALA CA C 54.08 0.1 1 428 115 117 ALA CB C 18.83 0.1 1 429 115 117 ALA N N 124.8 0.1 1 430 116 118 ARG H H 8.203 0.02 1 431 116 118 ARG CA C 57.49 0.1 1 432 116 118 ARG CB C 30.2 0.1 1 433 116 118 ARG N N 117.66 0.1 1 434 117 119 LYS H H 7.986 0.02 1 435 117 119 LYS CA C 57.22 0.1 1 436 117 119 LYS CB C 32.76 0.1 1 437 117 119 LYS N N 120.19 0.1 1 438 118 120 LYS H H 8.067 0.02 1 439 118 120 LYS CA C 56.93 0.1 1 440 118 120 LYS CB C 32.96 0.1 1 441 118 120 LYS N N 121.23 0.1 1 442 119 121 ALA H H 8.196 0.02 1 443 119 121 ALA CA C 52.96 0.1 1 444 119 121 ALA CB C 19.11 0.1 1 445 119 121 ALA N N 124.02 0.1 1 446 120 122 GLY H H 8.343 0.02 1 447 120 122 GLY CA C 45.36 0.1 1 448 120 122 GLY N N 107.94 0.1 1 449 121 123 TYR H H 7.985 0.02 1 450 121 123 TYR CA C 58.4 0.1 1 451 121 123 TYR CB C 38.79 0.1 1 452 121 123 TYR N N 120.22 0.1 1 453 122 124 HIS H H 8.198 0.02 1 454 122 124 HIS CA C 55.94 0.1 1 455 122 124 HIS CB C 30.78 0.1 1 456 122 124 HIS N N 121.68 0.1 1 457 123 125 GLU H H 8.264 0.02 1 458 123 125 GLU CA C 56.5 0.1 1 459 123 125 GLU CB C 30.49 0.1 1 460 123 125 GLU N N 122.14 0.1 1 461 124 126 ILE H H 8.245 0.02 1 462 124 126 ILE CA C 61.08 0.1 1 463 124 126 ILE CB C 38.81 0.1 1 464 124 126 ILE N N 122.03 0.1 1 465 125 127 ALA H H 8.382 0.02 1 466 125 127 ALA CA C 52.35 0.1 1 467 125 127 ALA CB C 19.38 0.1 1 468 125 127 ALA N N 128.02 0.1 1 469 126 128 ASP H H 8.358 0.02 1 470 126 128 ASP CA C 52.15 0.1 1 471 126 128 ASP CB C 41.62 0.1 1 472 126 128 ASP N N 121.22 0.1 1 473 127 129 PRO CA C 63.51 0.1 1 474 127 129 PRO CB C 31.99 0.1 1 475 128 130 GLY H H 8.542 0.02 1 476 128 130 GLY CA C 45.22 0.1 1 477 128 130 GLY N N 108.29 0.1 1 478 129 131 LYS H H 8.099 0.02 1 479 129 131 LYS CA C 53.92 0.1 1 480 129 131 LYS CB C 33 0.1 1 481 129 131 LYS N N 121.5 0.1 1 482 130 132 PRO CA C 63.52 0.1 1 483 130 132 PRO CB C 31.92 0.1 1 484 131 133 THR H H 7.946 0.02 1 485 131 133 THR CA C 61.24 0.1 1 486 131 133 THR CB C 71.36 0.1 1 487 131 133 THR N N 114.68 0.1 1 488 132 134 GLU H H 8.95 0.02 1 489 132 134 GLU CA C 55.62 0.1 1 490 132 134 GLU CB C 33 0.1 1 491 132 134 GLU N N 123.32 0.1 1 492 133 135 ILE H H 8.562 0.02 1 493 133 135 ILE CA C 59.86 0.1 1 494 133 135 ILE CB C 40.5 0.1 1 495 133 135 ILE N N 121.6 0.1 1 496 134 136 ASN H H 8.972 0.02 1 497 134 136 ASN CA C 51.28 0.1 1 498 134 136 ASN CB C 41.98 0.1 1 499 134 136 ASN N N 125.58 0.1 1 500 135 137 ILE H H 9.161 0.02 1 501 135 137 ILE CA C 59.26 0.1 1 502 135 137 ILE CB C 39.75 0.1 1 503 135 137 ILE N N 121.98 0.1 1 504 136 138 ILE H H 8.932 0.02 1 505 136 138 ILE CA C 60.64 0.1 1 506 136 138 ILE CB C 39.36 0.1 1 507 136 138 ILE N N 126.83 0.1 1 508 137 139 LEU H H 8.874 0.02 1 509 137 139 LEU CA C 54.84 0.1 1 510 137 139 LEU CB C 43.87 0.1 1 511 137 139 LEU N N 130.6 0.1 1 512 138 140 ASP H H 7.71 0.02 1 513 138 140 ASP CA C 53.39 0.1 1 514 138 140 ASP CB C 43.24 0.1 1 515 138 140 ASP N N 120.16 0.1 1 516 139 141 ALA H H 8.848 0.02 1 517 139 141 ALA CA C 55.66 0.1 1 518 139 141 ALA CB C 18.56 0.1 1 519 139 141 ALA N N 128.1 0.1 1 520 140 142 GLU H H 7.701 0.02 1 521 140 142 GLU CA C 56.2 0.1 1 522 140 142 GLU CB C 29.73 0.1 1 523 140 142 GLU N N 113.9 0.1 1 524 141 143 LYS H H 7.53 0.02 1 525 141 143 LYS CA C 57.06 0.1 1 526 141 143 LYS N N 122.88 0.1 1 527 142 144 ASN CA C 55.13 0.1 1 528 142 144 ASN CB C 39.38 0.1 1 529 143 145 PHE H H 7.872 0.02 1 530 143 145 PHE CA C 56.39 0.1 1 531 143 145 PHE CB C 41.42 0.1 1 532 143 145 PHE N N 115.79 0.1 1 533 144 146 CYS H H 9.048 0.02 1 534 144 146 CYS CA C 55.6 0.1 1 535 144 146 CYS CB C 31.41 0.1 1 536 144 146 CYS N N 114.03 0.1 1 537 145 147 SER H H 9.058 0.02 1 538 145 147 SER CA C 57.3 0.1 1 539 145 147 SER CB C 63.8 0.1 1 540 145 147 SER N N 117.71 0.1 1 541 146 148 PHE H H 9.116 0.02 1 542 146 148 PHE CA C 56.99 0.1 1 543 146 148 PHE CB C 40.94 0.1 1 544 146 148 PHE N N 129.29 0.1 1 545 147 149 GLU H H 8.824 0.02 1 546 147 149 GLU CA C 54.7 0.1 1 547 147 149 GLU CB C 33.18 0.1 1 548 147 149 GLU N N 125.78 0.1 1 549 148 150 LEU H H 7.879 0.02 1 550 148 150 LEU CA C 53.23 0.1 1 551 148 150 LEU CB C 45.74 0.1 1 552 148 150 LEU N N 122.21 0.1 1 553 149 151 PHE H H 9.18 0.02 1 554 149 151 PHE CA C 56.47 0.1 1 555 149 151 PHE CB C 42.35 0.1 1 556 149 151 PHE N N 124.65 0.1 1 557 150 152 SER H H 8.926 0.02 1 558 150 152 SER CA C 56.92 0.1 1 559 150 152 SER CB C 64.51 0.1 1 560 150 152 SER N N 116.12 0.1 1 561 151 153 LYS H H 8.877 0.02 1 562 151 153 LYS CA C 55.96 0.1 1 563 151 153 LYS CB C 33.25 0.1 1 564 151 153 LYS N N 126.29 0.1 1 565 152 154 THR H H 8.254 0.02 1 566 152 154 THR CA C 59.94 0.1 1 567 152 154 THR CB C 69.19 0.1 1 568 152 154 THR N N 117.01 0.1 1 569 153 155 PRO CA C 65.19 0.1 1 570 153 155 PRO CB C 31.65 0.1 1 571 154 156 GLU H H 8.398 0.02 1 572 154 156 GLU CA C 57.46 0.1 1 573 154 156 GLU CB C 29.82 0.1 1 574 154 156 GLU N N 114.08 0.1 1 575 155 157 SER H H 7.741 0.02 1 576 155 157 SER CA C 57.65 0.1 1 577 155 157 SER CB C 64.53 0.1 1 578 155 157 SER N N 114.31 0.1 1 579 156 158 LYS H H 8.334 0.02 1 580 156 158 LYS CA C 56.28 0.1 1 581 156 158 LYS CB C 33.4 0.1 1 582 156 158 LYS N N 123.17 0.1 1 583 157 159 GLY H H 8.437 0.02 1 584 157 159 GLY CA C 45.06 0.1 1 585 157 159 GLY N N 110.03 0.1 1 586 158 160 LYS H H 8.601 0.02 1 587 158 160 LYS CA C 57.19 0.1 1 588 158 160 LYS CB C 32.17 0.1 1 589 158 160 LYS N N 123.98 0.1 1 590 159 161 ILE H H 8.9 0.02 1 591 159 161 ILE CA C 62.01 0.1 1 592 159 161 ILE CB C 38.74 0.1 1 593 159 161 ILE N N 126.44 0.1 1 594 160 162 PHE H H 8.383 0.02 1 595 160 162 PHE CA C 58.46 0.1 1 596 160 162 PHE N N 119.46 0.1 1 597 161 163 SER CA C 56.16 0.1 1 598 161 163 SER CB C 65.49 0.1 1 599 162 164 ILE H H 8.507 0.02 1 600 162 164 ILE CA C 59.84 0.1 1 601 162 164 ILE CB C 41.53 0.1 1 602 162 164 ILE N N 119.27 0.1 1 603 163 165 LYS H H 8.41 0.02 1 604 163 165 LYS CA C 55.82 0.1 1 605 163 165 LYS CB C 32.86 0.1 1 606 163 165 LYS N N 128.77 0.1 1 607 164 166 LEU H H 9.061 0.02 1 608 164 166 LEU CA C 53.67 0.1 1 609 164 166 LEU CB C 44.62 0.1 1 610 164 166 LEU N N 124.56 0.1 1 611 165 167 HIS H H 8.667 0.02 1 612 165 167 HIS CA C 56.43 0.1 1 613 165 167 HIS CB C 32.5 0.1 1 614 165 167 HIS N N 120.6 0.1 1 615 166 168 ALA H H 8.383 0.02 1 616 166 168 ALA CA C 53.21 0.1 1 617 166 168 ALA CB C 18.57 0.1 1 618 166 168 ALA N N 125.63 0.1 1 619 167 169 VAL H H 7.836 0.02 1 620 167 169 VAL CA C 62.88 0.1 1 621 167 169 VAL CB C 32 0.1 1 622 167 169 VAL N N 124.25 0.1 1 623 168 170 ARG H H 8.036 0.02 1 624 168 170 ARG CA C 56.87 0.1 1 625 168 170 ARG CB C 32.08 0.1 1 626 168 170 ARG N N 131.33 0.1 1 stop_ save_