data_50308 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific resonance assignments of the human SAS-6 F131D head domain ; _BMRB_accession_number 50308 _BMRB_flat_file_name bmr50308.str _Entry_type original _Submission_date 2020-06-07 _Accession_date 2020-06-07 _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 Busch Julia M.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" 110 "13C chemical shifts" 224 "15N chemical shifts" 110 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-12-30 update BMRB 'update entry citation' 2020-09-01 original author 'original release' stop_ _Original_release_date 2020-06-08 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Identification of compounds that bind the centriolar protein SAS-6 and inhibit its oligomerization ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32873708 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Busch Julia M.C. . 2 Matsoukas Minos-Timotheos . . 3 Musgaard Maria . . 4 Spyroulias Georgios A. . 5 Biggin Philip C. . 6 Vakonakis Ioannis . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 295 _Journal_issue 52 _Journal_ISSN 1083-351X _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 17922 _Page_last 17934 _Year 2020 _Details . save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name hsSAS-6 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label hsSAS-6 $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 entity_1 _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'Structural protein, centriole assembly' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 154 _Mol_residue_sequence ; GPMSQVLFHQLVPLQVKCKD CEERRVSIRMSIELQSVSNP VHRKDLVIRLTDDTDPFFLY NLVISEEDFQSLKFQQGLLV DFLAFPQKFIDLLQQCTQEH AKEIPRFLLQLVSPAAILDN SPAFLNVVETNPDKHLTHLS LKLLPGNDVEIKKF ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 PRO 3 MET 4 SER 5 GLN 6 VAL 7 LEU 8 PHE 9 HIS 10 GLN 11 LEU 12 VAL 13 PRO 14 LEU 15 GLN 16 VAL 17 LYS 18 CYS 19 LYS 20 ASP 21 CYS 22 GLU 23 GLU 24 ARG 25 ARG 26 VAL 27 SER 28 ILE 29 ARG 30 MET 31 SER 32 ILE 33 GLU 34 LEU 35 GLN 36 SER 37 VAL 38 SER 39 ASN 40 PRO 41 VAL 42 HIS 43 ARG 44 LYS 45 ASP 46 LEU 47 VAL 48 ILE 49 ARG 50 LEU 51 THR 52 ASP 53 ASP 54 THR 55 ASP 56 PRO 57 PHE 58 PHE 59 LEU 60 TYR 61 ASN 62 LEU 63 VAL 64 ILE 65 SER 66 GLU 67 GLU 68 ASP 69 PHE 70 GLN 71 SER 72 LEU 73 LYS 74 PHE 75 GLN 76 GLN 77 GLY 78 LEU 79 LEU 80 VAL 81 ASP 82 PHE 83 LEU 84 ALA 85 PHE 86 PRO 87 GLN 88 LYS 89 PHE 90 ILE 91 ASP 92 LEU 93 LEU 94 GLN 95 GLN 96 CYS 97 THR 98 GLN 99 GLU 100 HIS 101 ALA 102 LYS 103 GLU 104 ILE 105 PRO 106 ARG 107 PHE 108 LEU 109 LEU 110 GLN 111 LEU 112 VAL 113 SER 114 PRO 115 ALA 116 ALA 117 ILE 118 LEU 119 ASP 120 ASN 121 SER 122 PRO 123 ALA 124 PHE 125 LEU 126 ASN 127 VAL 128 VAL 129 GLU 130 THR 131 ASN 132 PRO 133 ASP 134 LYS 135 HIS 136 LEU 137 THR 138 HIS 139 LEU 140 SER 141 LEU 142 LYS 143 LEU 144 LEU 145 PRO 146 GLY 147 ASN 148 ASP 149 VAL 150 GLU 151 ILE 152 LYS 153 LYS 154 PHE 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 Q6UVJ0 SAS-6 . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source_1 _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $entity_1 Human 9606 Eukaryota Metazoa Homo sapiens sas-6 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 _Details $entity_1 'recombinant technology' . Escherichia coli BL21(DE3) plasmid pFLOAT 'pET30a derivative' 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-99% 13C; U-99% 15N]' D2O 5 % 'natural abundance' DSS 50 uM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' 'sodium azide' 0.02 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name TOPSPIN _Version . loop_ _Task collection stop_ _Details . save_ save_software_2 _Saveframe_category software _Name NMRPipe _Version . loop_ _Task processing stop_ _Details . save_ save_software_3 _Saveframe_category software _Name SPARKY _Version . loop_ _Task 'data analysis' stop_ _Details . save_ save_software_4 _Saveframe_category software _Name PINE _Version . loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'AVANCE III' _Field_strength 17.6 _Details 'Oxford Instruments superconducting magnet at 17.6T strength, Bruker Avance III console, TCI probe' 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_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _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 7.5 . 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 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $software_1 $software_2 $software_3 $software_4 stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D HNCA' '3D HN(CO)CA' 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 hsSAS-6 _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 5 5 GLN H H 8.602 0.01 1 2 5 5 GLN CA C 54.5 0.2 1 3 5 5 GLN CB C 31.3 0.2 1 4 5 5 GLN N N 124.09 0.2 1 5 6 6 VAL H H 9.04 0.01 1 6 6 6 VAL CA C 63.9 0.2 1 7 6 6 VAL CB C 31.4 0.2 1 8 6 6 VAL N N 127.19 0.2 1 9 7 7 LEU H H 9.078 0.01 1 10 7 7 LEU CA C 55.2 0.2 1 11 7 7 LEU CB C 43.2 0.2 1 12 7 7 LEU N N 128.37 0.2 1 13 8 8 PHE H H 7.721 0.01 1 14 8 8 PHE CA C 57.6 0.2 1 15 8 8 PHE CB C 43.5 0.2 1 16 8 8 PHE N N 119.76 0.2 1 17 9 9 HIS H H 8.616 0.01 1 18 9 9 HIS CA C 55.4 0.2 1 19 9 9 HIS CB C 29.5 0.2 1 20 9 9 HIS N N 128.69 0.2 1 21 10 10 GLN H H 8.039 0.01 1 22 10 10 GLN CA C 54.3 0.2 1 23 10 10 GLN CB C 33 0.2 1 24 10 10 GLN N N 122.43 0.2 1 25 11 11 LEU H H 8.242 0.01 1 26 11 11 LEU CA C 56 0.2 1 27 11 11 LEU CB C 41.8 0.2 1 28 11 11 LEU N N 121.58 0.2 1 29 13 13 PRO CA C 64.7 0.2 1 30 13 13 PRO CB C 33.3 0.2 1 31 14 14 LEU H H 8.3 0.01 1 32 14 14 LEU CA C 56 0.2 1 33 14 14 LEU CB C 41.9 0.2 1 34 14 14 LEU N N 117.43 0.2 1 35 19 19 LYS H H 8.3 0.01 1 36 19 19 LYS CA C 52.8 0.2 1 37 19 19 LYS CB C 33.3 0.2 1 38 19 19 LYS N N 117.43 0.2 1 39 20 20 ASP H H 8.347 0.01 1 40 20 20 ASP CA C 52.8 0.2 1 41 20 20 ASP CB C 39.6 0.2 1 42 20 20 ASP N N 120.91 0.2 1 43 21 21 CYS H H 6.89 0.01 1 44 21 21 CYS CA C 58.3 0.2 1 45 21 21 CYS CB C 27.7 0.2 1 46 21 21 CYS N N 113.25 0.2 1 47 22 22 GLU H H 8.856 0.01 1 48 22 22 GLU CA C 58.9 0.2 1 49 22 22 GLU CB C 27.7 0.2 1 50 22 22 GLU N N 120.64 0.2 1 51 30 30 MET H H 8.834 0.01 1 52 30 30 MET CA C 53.9 0.2 1 53 30 30 MET CB C 35.9 0.2 1 54 30 30 MET N N 124.87 0.2 1 55 31 31 SER H H 9.056 0.01 1 56 31 31 SER CA C 56.3 0.2 1 57 31 31 SER CB C 65.6 0.2 1 58 31 31 SER N N 119.48 0.2 1 59 32 32 ILE H H 9.047 0.01 1 60 32 32 ILE CA C 60.5 0.2 1 61 32 32 ILE CB C 40.6 0.2 1 62 32 32 ILE N N 123.07 0.2 1 63 33 33 GLU H H 9.506 0.01 1 64 33 33 GLU CA C 53.8 0.2 1 65 33 33 GLU CB C 34.5 0.2 1 66 33 33 GLU N N 127.26 0.2 1 67 34 34 LEU H H 8.965 0.01 1 68 34 34 LEU CA C 53.4 0.2 1 69 34 34 LEU CB C 44.7 0.2 1 70 34 34 LEU N N 123.38 0.2 1 71 35 35 GLN H H 9.644 0.01 1 72 35 35 GLN CA C 54.6 0.2 1 73 35 35 GLN CB C 31.2 0.2 1 74 35 35 GLN N N 127.83 0.2 1 75 36 36 SER H H 8.855 0.01 1 76 36 36 SER CA C 58.3 0.2 1 77 36 36 SER CB C 64.8 0.2 1 78 36 36 SER N N 120.09 0.2 1 79 37 37 VAL H H 8.644 0.01 1 80 37 37 VAL CA C 61.1 0.2 1 81 37 37 VAL CB C 35 0.2 1 82 37 37 VAL N N 122.59 0.2 1 83 40 40 PRO CA C 64.5 0.2 1 84 40 40 PRO CB C 34.1 0.2 1 85 41 41 VAL H H 7.339 0.01 1 86 41 41 VAL CA C 60.3 0.2 1 87 41 41 VAL CB C 34.7 0.2 1 88 41 41 VAL N N 117.63 0.2 1 89 42 42 HIS H H 8.286 0.01 1 90 42 42 HIS CA C 56.8 0.2 1 91 42 42 HIS CB C 30 0.2 1 92 42 42 HIS N N 121.5 0.2 1 93 43 43 ARG H H 8.329 0.01 1 94 43 43 ARG CA C 55.6 0.2 1 95 43 43 ARG CB C 32.9 0.2 1 96 43 43 ARG N N 124.47 0.2 1 97 44 44 LYS H H 8.347 0.01 1 98 44 44 LYS CA C 55.1 0.2 1 99 44 44 LYS CB C 35.8 0.2 1 100 44 44 LYS N N 121.42 0.2 1 101 45 45 ASP H H 8.821 0.01 1 102 45 45 ASP CA C 53.1 0.2 1 103 45 45 ASP CB C 44.4 0.2 1 104 45 45 ASP N N 121.1 0.2 1 105 46 46 LEU H H 9.087 0.01 1 106 46 46 LEU CA C 53.8 0.2 1 107 46 46 LEU CB C 44.8 0.2 1 108 46 46 LEU N N 123.94 0.2 1 109 47 47 VAL H H 9.516 0.01 1 110 47 47 VAL CA C 62.1 0.2 1 111 47 47 VAL CB C 34.3 0.2 1 112 47 47 VAL N N 126.69 0.2 1 113 48 48 ILE H H 9.389 0.01 1 114 48 48 ILE CA C 60 0.2 1 115 48 48 ILE CB C 40.8 0.2 1 116 48 48 ILE N N 129.79 0.2 1 117 49 49 ARG H H 8.945 0.01 1 118 49 49 ARG CA C 55.2 0.2 1 119 49 49 ARG CB C 34.5 0.2 1 120 49 49 ARG N N 125.25 0.2 1 121 50 50 LEU H H 9.078 0.01 1 122 50 50 LEU CA C 54.6 0.2 1 123 50 50 LEU CB C 45.6 0.2 1 124 50 50 LEU N N 124.91 0.2 1 125 51 51 THR H H 9.073 0.01 1 126 51 51 THR CA C 60.4 0.2 1 127 51 51 THR CB C 72 0.2 1 128 51 51 THR N N 112.47 0.2 1 129 52 52 ASP H H 9.412 0.01 1 130 52 52 ASP CA C 52.5 0.2 1 131 52 52 ASP N N 119.77 0.2 1 132 53 53 ASP H H 9.123 0.01 1 133 53 53 ASP CA C 52.5 0.2 1 134 53 53 ASP CB C 41 0.2 1 135 53 53 ASP N N 127.34 0.2 1 136 56 56 PRO CA C 63.8 0.2 1 137 56 56 PRO CB C 32.4 0.2 1 138 57 57 PHE H H 8.012 0.01 1 139 57 57 PHE CA C 57.8 0.2 1 140 57 57 PHE CB C 38.3 0.2 1 141 57 57 PHE N N 115.45 0.2 1 142 58 58 PHE H H 7.33 0.01 1 143 58 58 PHE CA C 58.1 0.2 1 144 58 58 PHE CB C 38.9 0.2 1 145 58 58 PHE N N 122.85 0.2 1 146 59 59 LEU H H 7.533 0.01 1 147 59 59 LEU CA C 55.1 0.2 1 148 59 59 LEU CB C 45.2 0.2 1 149 59 59 LEU N N 130.3 0.2 1 150 60 60 TYR H H 8.459 0.01 1 151 60 60 TYR CA C 57.6 0.2 1 152 60 60 TYR CB C 44.4 0.2 1 153 60 60 TYR N N 123.64 0.2 1 154 61 61 ASN H H 9.543 0.01 1 155 61 61 ASN CA C 52.6 0.2 1 156 61 61 ASN N N 118.13 0.2 1 157 62 62 LEU H H 8.935 0.01 1 158 62 62 LEU CA C 55.8 0.2 1 159 62 62 LEU CB C 46.6 0.2 1 160 62 62 LEU N N 121.74 0.2 1 161 63 63 VAL H H 8.418 0.01 1 162 63 63 VAL CA C 61.2 0.2 1 163 63 63 VAL CB C 33.2 0.2 1 164 63 63 VAL N N 126.36 0.2 1 165 64 64 ILE H H 9.874 0.01 1 166 64 64 ILE CA C 60.7 0.2 1 167 64 64 ILE CB C 41 0.2 1 168 64 64 ILE N N 128.5 0.2 1 169 65 65 SER H H 9.023 0.01 1 170 65 65 SER CA C 56.6 0.2 1 171 65 65 SER CB C 66.6 0.2 1 172 65 65 SER N N 123.61 0.2 1 173 66 66 GLU H H 8.891 0.01 1 174 66 66 GLU CA C 60.3 0.2 1 175 66 66 GLU CB C 29.4 0.2 1 176 66 66 GLU N N 122.56 0.2 1 177 67 67 GLU H H 8.365 0.01 1 178 67 67 GLU CA C 59.7 0.2 1 179 67 67 GLU CB C 29.4 0.2 1 180 67 67 GLU N N 118.25 0.2 1 181 68 68 ASP H H 7.928 0.01 1 182 68 68 ASP CA C 56.8 0.2 1 183 68 68 ASP CB C 40.8 0.2 1 184 68 68 ASP N N 121.31 0.2 1 185 69 69 PHE H H 8.708 0.01 1 186 69 69 PHE CA C 61.7 0.2 1 187 69 69 PHE CB C 39.5 0.2 1 188 69 69 PHE N N 121.25 0.2 1 189 70 70 GLN H H 7.788 0.01 1 190 70 70 GLN CA C 58.7 0.2 1 191 70 70 GLN CB C 27.8 0.2 1 192 70 70 GLN N N 116.51 0.2 1 193 71 71 SER H H 7.301 0.01 1 194 71 71 SER CA C 61.2 0.2 1 195 71 71 SER CB C 62.8 0.2 1 196 71 71 SER N N 112.86 0.2 1 197 72 72 LEU H H 7.326 0.01 1 198 72 72 LEU CA C 58.3 0.2 1 199 72 72 LEU CB C 41.2 0.2 1 200 72 72 LEU N N 123.85 0.2 1 201 73 73 LYS H H 8.856 0.01 1 202 73 73 LYS CA C 59.3 0.2 1 203 73 73 LYS N N 120.64 0.2 1 204 74 74 PHE H H 7.537 0.01 1 205 74 74 PHE CA C 59.9 0.2 1 206 74 74 PHE CB C 39.4 0.2 1 207 74 74 PHE N N 117.38 0.2 1 208 75 75 GLN H H 8.418 0.01 1 209 75 75 GLN CA C 58.5 0.2 1 210 75 75 GLN CB C 29 0.2 1 211 75 75 GLN N N 118.56 0.2 1 212 76 76 GLN H H 8.11 0.01 1 213 76 76 GLN CA C 55.7 0.2 1 214 76 76 GLN CB C 28.7 0.2 1 215 76 76 GLN N N 113.37 0.2 1 216 77 77 GLY H H 7.37 0.01 1 217 77 77 GLY CA C 43.4 0.2 1 218 77 77 GLY N N 110.42 0.2 1 219 78 78 LEU H H 8.373 0.01 1 220 78 78 LEU CA C 56 0.2 1 221 78 78 LEU CB C 41.3 0.2 1 222 78 78 LEU N N 111.82 0.2 1 223 79 79 LEU H H 9.123 0.01 1 224 79 79 LEU CA C 56 0.2 1 225 79 79 LEU CB C 41.3 0.2 1 226 79 79 LEU N N 127.34 0.2 1 227 80 80 VAL H H 6.89 0.01 1 228 80 80 VAL CA C 59.6 0.2 1 229 80 80 VAL CB C 34.1 0.2 1 230 80 80 VAL N N 113.25 0.2 1 231 81 81 ASP H H 7.879 0.01 1 232 81 81 ASP CA C 52.5 0.2 1 233 81 81 ASP CB C 42.2 0.2 1 234 81 81 ASP N N 119.57 0.2 1 235 82 82 PHE H H 8.632 0.01 1 236 82 82 PHE CA C 60.6 0.2 1 237 82 82 PHE CB C 39.5 0.2 1 238 82 82 PHE N N 119.6 0.2 1 239 83 83 LEU H H 7.985 0.01 1 240 83 83 LEU CA C 56.9 0.2 1 241 83 83 LEU CB C 41.1 0.2 1 242 83 83 LEU N N 115.4 0.2 1 243 84 84 ALA H H 7.548 0.01 1 244 84 84 ALA CA C 52.2 0.2 1 245 84 84 ALA CB C 19.7 0.2 1 246 84 84 ALA N N 120.18 0.2 1 247 85 85 PHE H H 7.772 0.01 1 248 85 85 PHE CA C 61.9 0.2 1 249 85 85 PHE CB C 36.9 0.2 1 250 85 85 PHE N N 119.94 0.2 1 251 86 86 PRO CA C 67 0.2 1 252 86 86 PRO CB C 30.1 0.2 1 253 87 87 GLN H H 7.667 0.01 1 254 87 87 GLN CA C 58.2 0.2 1 255 87 87 GLN CB C 28.2 0.2 1 256 87 87 GLN N N 113.61 0.2 1 257 88 88 LYS H H 7.34 0.01 1 258 88 88 LYS CA C 57.9 0.2 1 259 88 88 LYS CB C 31.5 0.2 1 260 88 88 LYS N N 119.64 0.2 1 261 89 89 PHE H H 8.236 0.01 1 262 89 89 PHE CA C 57.6 0.2 1 263 89 89 PHE CB C 38 0.2 1 264 89 89 PHE N N 119.12 0.2 1 265 90 90 ILE H H 8.462 0.01 1 266 90 90 ILE CA C 66 0.2 1 267 90 90 ILE CB C 37.8 0.2 1 268 90 90 ILE N N 119.85 0.2 1 269 91 91 ASP H H 8.397 0.01 1 270 91 91 ASP CA C 57.6 0.2 1 271 91 91 ASP CB C 40 0.2 1 272 91 91 ASP N N 120.79 0.2 1 273 92 92 LEU H H 7.671 0.01 1 274 92 92 LEU CA C 56.1 0.2 1 275 92 92 LEU CB C 41.6 0.2 1 276 92 92 LEU N N 120.23 0.2 1 277 99 99 GLU H H 7.55 0.01 1 278 99 99 GLU CA C 59.2 0.2 1 279 99 99 GLU CB C 28.3 0.2 1 280 99 99 GLU N N 117.72 0.2 1 281 100 100 HIS H H 8.054 0.01 1 282 100 100 HIS CA C 63.3 0.2 1 283 100 100 HIS CB C 26.9 0.2 1 284 100 100 HIS N N 116.62 0.2 1 285 101 101 ALA H H 8.199 0.01 1 286 101 101 ALA CA C 52.1 0.2 1 287 101 101 ALA CB C 18.9 0.2 1 288 101 101 ALA N N 123.74 0.2 1 289 102 102 LYS H H 7.729 0.01 1 290 102 102 LYS CA C 55.6 0.2 1 291 102 102 LYS CB C 33.2 0.2 1 292 102 102 LYS N N 118.92 0.2 1 293 103 103 GLU H H 8.375 0.01 1 294 103 103 GLU CA C 59.1 0.2 1 295 103 103 GLU CB C 29.8 0.2 1 296 103 103 GLU N N 120.34 0.2 1 297 104 104 ILE H H 7.972 0.01 1 298 104 104 ILE CB C 38.1 0.2 1 299 104 104 ILE N N 117.35 0.2 1 300 105 105 PRO CA C 63.3 0.2 1 301 105 105 PRO CB C 33.2 0.2 1 302 106 106 ARG H H 9.69 0.01 1 303 106 106 ARG CA C 56.7 0.2 1 304 106 106 ARG CB C 31.4 0.2 1 305 106 106 ARG N N 123.04 0.2 1 306 107 107 PHE H H 7.008 0.01 1 307 107 107 PHE CA C 56 0.2 1 308 107 107 PHE CB C 44 0.2 1 309 107 107 PHE N N 113.46 0.2 1 310 108 108 LEU H H 9.409 0.01 1 311 108 108 LEU CA C 53.9 0.2 1 312 108 108 LEU CB C 46.4 0.2 1 313 108 108 LEU N N 121.31 0.2 1 314 109 109 LEU H H 8.907 0.01 1 315 109 109 LEU CA C 53.3 0.2 1 316 109 109 LEU CB C 43.4 0.2 1 317 109 109 LEU N N 125.19 0.2 1 318 110 110 GLN H H 9.268 0.01 1 319 110 110 GLN CA C 53.4 0.2 1 320 110 110 GLN CB C 33.1 0.2 1 321 110 110 GLN N N 124.49 0.2 1 322 111 111 LEU H H 9.137 0.01 1 323 111 111 LEU CA C 53.2 0.2 1 324 111 111 LEU CB C 45.5 0.2 1 325 111 111 LEU N N 126.33 0.2 1 326 112 112 VAL H H 9.764 0.01 1 327 112 112 VAL CA C 61.4 0.2 1 328 112 112 VAL CB C 34.1 0.2 1 329 112 112 VAL N N 127.31 0.2 1 330 113 113 SER H H 7.337 0.01 1 331 113 113 SER N N 119.12 0.2 1 332 121 121 SER H H 8.091 0.01 1 333 121 121 SER CA C 56.9 0.2 1 334 121 121 SER CB C 64 0.2 1 335 121 121 SER N N 115.78 0.2 1 336 122 122 PRO CA C 63.8 0.2 1 337 122 122 PRO CB C 32.6 0.2 1 338 123 123 ALA H H 8.243 0.01 1 339 123 123 ALA CA C 50.6 0.2 1 340 123 123 ALA CB C 22.3 0.2 1 341 123 123 ALA N N 122.35 0.2 1 342 124 124 PHE H H 8.771 0.01 1 343 124 124 PHE CA C 57.1 0.2 1 344 124 124 PHE CB C 40.7 0.2 1 345 124 124 PHE N N 118.47 0.2 1 346 125 125 LEU H H 9.583 0.01 1 347 125 125 LEU CA C 53.1 0.2 1 348 125 125 LEU CB C 44.3 0.2 1 349 125 125 LEU N N 125.8 0.2 1 350 126 126 ASN H H 9.611 0.01 1 351 126 126 ASN CA C 50.9 0.2 1 352 126 126 ASN CB C 41.4 0.2 1 353 126 126 ASN N N 125.1 0.2 1 354 127 127 VAL H H 8.661 0.01 1 355 127 127 VAL CA C 61.9 0.2 1 356 127 127 VAL CB C 33.3 0.2 1 357 127 127 VAL N N 121.46 0.2 1 358 129 129 GLU H H 9.323 0.01 1 359 129 129 GLU CA C 53.1 0.2 1 360 129 129 GLU CB C 32.6 0.2 1 361 129 129 GLU N N 127.08 0.2 1 362 130 130 THR H H 8.602 0.01 1 363 130 130 THR CA C 60.3 0.2 1 364 130 130 THR CB C 68.8 0.2 1 365 130 130 THR N N 120.51 0.2 1 366 131 131 ASN H H 7.871 0.01 1 367 131 131 ASN CA C 51.9 0.2 1 368 131 131 ASN CB C 39.7 0.2 1 369 131 131 ASN N N 122.86 0.2 1 370 132 132 PRO CA C 65.2 0.2 1 371 132 132 PRO CB C 31.9 0.2 1 372 133 133 ASP H H 8.435 0.01 1 373 133 133 ASP CA C 55.1 0.2 1 374 133 133 ASP CB C 41.4 0.2 1 375 133 133 ASP N N 114.88 0.2 1 376 134 134 LYS H H 7.54 0.01 1 377 134 134 LYS CA C 56 0.2 1 378 134 134 LYS CB C 33.3 0.2 1 379 134 134 LYS N N 118.7 0.2 1 380 135 135 HIS H H 8.3 0.01 1 381 135 135 HIS CA C 56.2 0.2 1 382 135 135 HIS N N 117.43 0.2 1 383 138 138 HIS H H 9.025 0.01 1 384 138 138 HIS CA C 59 0.2 1 385 138 138 HIS CB C 33.8 0.2 1 386 138 138 HIS N N 127.77 0.2 1 387 139 139 LEU H H 7.257 0.01 1 388 139 139 LEU CA C 54.6 0.2 1 389 139 139 LEU CB C 46.3 0.2 1 390 139 139 LEU N N 116.65 0.2 1 391 140 140 SER H H 8.679 0.01 1 392 140 140 SER CA C 56.5 0.2 1 393 140 140 SER CB C 64.6 0.2 1 394 140 140 SER N N 120.08 0.2 1 395 141 141 LEU H H 9.301 0.01 1 396 141 141 LEU CA C 52.8 0.2 1 397 141 141 LEU CB C 45.2 0.2 1 398 141 141 LEU N N 128.21 0.2 1 399 142 142 LYS H H 8.727 0.01 1 400 142 142 LYS CA C 56 0.2 1 401 142 142 LYS CB C 32.4 0.2 1 402 142 142 LYS N N 125.12 0.2 1 403 143 143 LEU H H 8.831 0.01 1 404 143 143 LEU CA C 53.8 0.2 1 405 143 143 LEU CB C 44.2 0.2 1 406 143 143 LEU N N 125.59 0.2 1 407 144 144 LEU H H 8.546 0.01 1 408 144 144 LEU CB C 41.9 0.2 1 409 144 144 LEU N N 119.58 0.2 1 410 145 145 PRO CA C 62.1 0.2 1 411 145 145 PRO CB C 31.7 0.2 1 412 146 146 GLY H H 7.781 0.01 1 413 146 146 GLY CA C 45 0.2 1 414 146 146 GLY N N 108.18 0.2 1 415 147 147 ASN H H 8.373 0.01 1 416 147 147 ASN CA C 56 0.2 1 417 147 147 ASN CB C 41.3 0.2 1 418 147 147 ASN N N 111.82 0.2 1 419 148 148 ASP H H 7.931 0.01 1 420 148 148 ASP CA C 54.3 0.2 1 421 148 148 ASP CB C 40.9 0.2 1 422 148 148 ASP N N 120.49 0.2 1 423 149 149 VAL H H 7.907 0.01 1 424 149 149 VAL CA C 62.2 0.2 1 425 149 149 VAL CB C 32.6 0.2 1 426 149 149 VAL N N 119.25 0.2 1 427 150 150 GLU H H 8.321 0.01 1 428 150 150 GLU CA C 56.4 0.2 1 429 150 150 GLU CB C 30.3 0.2 1 430 150 150 GLU N N 124.08 0.2 1 431 151 151 ILE H H 8.117 0.01 1 432 151 151 ILE CA C 60.9 0.2 1 433 151 151 ILE CB C 38.2 0.2 1 434 151 151 ILE N N 123.2 0.2 1 435 152 152 LYS H H 8.33 0.01 1 436 152 152 LYS CA C 56.1 0.2 1 437 152 152 LYS CB C 32.9 0.2 1 438 152 152 LYS N N 126.31 0.2 1 439 153 153 LYS H H 8.203 0.01 1 440 153 153 LYS CA C 56.1 0.2 1 441 153 153 LYS CB C 33.2 0.2 1 442 153 153 LYS N N 123.34 0.2 1 443 154 154 PHE H H 7.694 0.01 1 444 154 154 PHE N N 125.69 0.2 1 stop_ save_