data_18807 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shifts for the N-terminal head group of ceSAS-6 ; _BMRB_accession_number 18807 _BMRB_flat_file_name bmr18807.str _Entry_type original _Submission_date 2012-10-25 _Accession_date 2012-10-25 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'chemical shift assignments for the monomeric N-terminal head group of C.elegans SAS-6, residues 1-168 S123E I154E' 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" 472 "15N chemical shifts" 153 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-08-30 original BMRB . stop_ _Original_release_date 2012-10-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Caenorhabditis elegans centriolar protein SAS-6 forms a spiral that is consistent with imparting a ninefold symmetry ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23798409 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hilbert Manuel . . 2 Erat Michele C. . 3 Hachet Virginie . . 4 Guichard Paul . . 5 Blank Iris D. . 6 Fluckiger Isabelle . . 7 Slater Leanne . . 8 Lowe Edward D. . 9 Hatzopoulos Georgios N. . 10 Steinmetz Michel O. . 11 Gonczy Pierre . . 12 Vakonakis Ioannis . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Journal_volume 110 _Journal_issue 28 _Journal_ISSN 1091-6490 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 11373 _Page_last 11378 _Year 2013 _Details . loop_ _Keyword 'central tube' centriole spiral 'structural basis' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_reference _Saveframe_category citation _Citation_full . _Citation_title ; Structural basis of the 9-fold symmetry of centrioles. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21277013 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kitagawa Daiju . . 2 Vakonakis Ioannis . . 3 Olieric Natasha . . 4 Hilbert Manuel . . 5 Keller Deborah . . 6 Olieric Vincent . . 7 Bortfeld Miriam . . 8 Erat Michele C. . 9 Flueckiger Isabelle . . 10 Goenczy Pierre . . 11 Steinmetz Michel O. . stop_ _Journal_abbreviation Cell _Journal_name_full . _Journal_volume 144 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 364 _Page_last 375 _Year 2011 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'ceN SAS-6' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ceN SAS-6' $ce_SAS-6 stop_ _System_molecular_weight 19425 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'structural part of centriolar central tube' stop_ _Database_query_date . _Details monomer save_ ######################## # Monomeric polymers # ######################## save_ce_SAS-6 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ce_SAS-6 _Molecular_mass 19425 _Mol_thiol_state 'all free' loop_ _Biological_function 'centriole assembly' 'structural protein' 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 SAS6_CAEEL . . . . . PDB PYI 'ceN SAS-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 $ce_SAS-6 Nematodes 6239 Eukaryota Metazoa Caenorhabditis elegans 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 $ce_SAS-6 'recombinant technology' . Escherichia coli 'BL-21 (DE3)' 'modified p15b' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '15N enriched' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ce_SAS-6 0.5 mM [U-15N] H2O 95 % 'natural abundance' D2O 5 % '[U-100% 2H]' DSS 0.1 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details '15N, 13C enriched' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ce_SAS-6 0.5 mM '[U-100% 13C; U-100% 15N]' H2O 95 % 'natural abundance' D2O 5 % '[U-100% 2H]' DSS 0.1 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' 'potassium phosphate' 20 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 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_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_Omega_Spectrometer_Operating_Software_Beta_6.03b2 _Saveframe_category software _Name Omega_Spectrometer_Operating_Software_Beta_6.03b2 _Version . loop_ _Vendor _Address _Electronic_address GE . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer GE/home-built _Model OMEGA _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _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_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_2 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_2 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_2 save_ save_3D_CBCANH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCANH' _Sample_label $sample_2 save_ save_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_2 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' 0.1 . M pH 7 . pH pressure 1 . atm temperature 298 . 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_ _Experiment_label '3D HNCA' '3D HNCACB' '3D CBCA(CO)NH' '3D CBCANH' stop_ loop_ _Sample_label $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'ceN SAS-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 1 3 MET C C 176.591 0.2 1 2 1 3 MET CA C 55.67 0.2 1 3 1 3 MET CB C 32.6 0.2 1 4 2 4 THR H H 8.259 0.02 1 5 2 4 THR C C 174.502 0.2 1 6 2 4 THR CA C 61.92 0.2 1 7 2 4 THR CB C 69.78 0.2 1 8 2 4 THR N N 115.2 0.2 1 9 3 5 SER H H 8.382 0.02 1 10 3 5 SER C C 173.944 0.2 1 11 3 5 SER CA C 58.43 0.2 1 12 3 5 SER CB C 63.9 0.2 1 13 3 5 SER N N 118.3 0.2 1 14 4 6 LYS H H 8.259 0.02 1 15 4 6 LYS C C 176.128 0.2 1 16 4 6 LYS CA C 56.16 0.2 1 17 4 6 LYS CB C 33.64 0.2 1 18 4 6 LYS N N 123.6 0.2 1 19 5 7 ILE H H 8.679 0.02 1 20 5 7 ILE C C 175.397 0.2 1 21 5 7 ILE CA C 60.27 0.2 1 22 5 7 ILE CB C 40.23 0.2 1 23 5 7 ILE N N 124.1 0.2 1 24 6 8 ALA H H 8.757 0.02 1 25 6 8 ALA C C 176.904 0.2 1 26 6 8 ALA CA C 52.25 0.2 1 27 6 8 ALA CB C 18.37 0.2 1 28 6 8 ALA N N 129.3 0.2 1 29 7 9 LEU H H 8.726 0.02 1 30 7 9 LEU C C 177.04 0.2 1 31 7 9 LEU CA C 55.81 0.2 1 32 7 9 LEU CB C 42.96 0.2 1 33 7 9 LEU N N 124 0.2 1 34 8 10 PHE H H 7.849 0.02 1 35 8 10 PHE C C 173.529 0.2 1 36 8 10 PHE CA C 57.76 0.2 1 37 8 10 PHE CB C 43.42 0.2 1 38 8 10 PHE N N 118.1 0.2 1 39 9 11 ASP H H 8.322 0.02 1 40 9 11 ASP C C 174.4 0.2 1 41 9 11 ASP CA C 53.81 0.2 1 42 9 11 ASP CB C 40.68 0.2 1 43 9 11 ASP N N 129.4 0.2 1 44 10 12 GLN H H 8.04 0.02 1 45 10 12 GLN C C 174.523 0.2 1 46 10 12 GLN CA C 54.39 0.2 1 47 10 12 GLN CB C 33.48 0.2 1 48 10 12 GLN N N 120.31 0.2 1 49 11 13 THR H H 8.605 0.02 1 50 11 13 THR C C 173.996 0.2 1 51 11 13 THR CA C 62.72 0.2 1 52 11 13 THR CB C 69.26 0.2 1 53 11 13 THR N N 118.5 0.2 1 54 12 14 LEU H H 9.632 0.02 1 55 12 14 LEU C C 175.4 0.2 1 56 12 14 LEU CA C 53.38 0.2 1 57 12 14 LEU CB C 45.64 0.2 1 58 12 14 LEU N N 127.1 0.2 1 59 13 15 ILE H H 8.441 0.02 1 60 13 15 ILE C C 175.034 0.2 1 61 13 15 ILE CA C 60.39 0.2 1 62 13 15 ILE CB C 37.33 0.2 1 63 13 15 ILE N N 120.64 0.2 1 64 14 16 ALA H H 8.872 0.02 1 65 14 16 ALA C C 176.121 0.2 1 66 14 16 ALA CA C 50.13 0.2 1 67 14 16 ALA CB C 23.74 0.2 1 68 14 16 ALA N N 129.2 0.2 1 69 15 17 SER H H 8.386 0.02 1 70 15 17 SER C C 172.35 0.2 1 71 15 17 SER CA C 58.37 0.2 1 72 15 17 SER CB C 63.57 0.2 1 73 15 17 SER N N 115.7 0.2 1 74 16 18 LEU H H 9.054 0.02 1 75 16 18 LEU C C 175.348 0.2 1 76 16 18 LEU CA C 53.77 0.2 1 77 16 18 LEU CB C 43.29 0.2 1 78 16 18 LEU N N 128.8 0.2 1 79 17 19 LEU H H 8.995 0.02 1 80 17 19 LEU C C 175.136 0.2 1 81 17 19 LEU CA C 54.25 0.2 1 82 17 19 LEU CB C 43.86 0.2 1 83 17 19 LEU N N 126.9 0.2 1 84 18 20 GLN H H 8.723 0.02 1 85 18 20 GLN CA C 52.62 0.2 1 86 18 20 GLN CB C 31.16 0.2 1 87 18 20 GLN N N 121.9 0.2 1 88 19 21 PRO C C 177.28 0.2 1 89 19 21 PRO CA C 62.92 0.2 1 90 19 21 PRO CB C 31.93 0.2 1 91 20 22 LEU H H 8.38 0.02 1 92 20 22 LEU C C 177.46 0.2 1 93 20 22 LEU CA C 56.19 0.2 1 94 20 22 LEU CB C 42.4 0.2 1 95 20 22 LEU N N 122.2 0.2 1 96 21 23 SER H H 8.131 0.02 1 97 21 23 SER C C 174.216 0.2 1 98 21 23 SER CA C 57.48 0.2 1 99 21 23 SER CB C 64.55 0.2 1 100 21 23 SER N N 113.1 0.2 1 101 22 24 LEU H H 8.397 0.02 1 102 22 24 LEU C C 177.559 0.2 1 103 22 24 LEU CA C 56.48 0.2 1 104 22 24 LEU CB C 42.08 0.2 1 105 22 24 LEU N N 121.8 0.2 1 106 23 25 ASN H H 8.378 0.02 1 107 23 25 ASN C C 174.474 0.2 1 108 23 25 ASN CA C 53.41 0.2 1 109 23 25 ASN CB C 38.78 0.2 1 110 23 25 ASN N N 115.4 0.2 1 111 24 26 GLN H H 7.734 0.02 1 112 24 26 GLN CA C 53.58 0.2 1 113 24 26 GLN CB C 29.89 0.2 1 114 24 26 GLN N N 119.3 0.2 1 115 25 27 PRO C C 176.321 0.2 1 116 25 27 PRO CA C 63.67 0.2 1 117 25 27 PRO CB C 31.45 0.2 1 118 26 28 ASP H H 8.059 0.02 1 119 26 28 ASP C C 175.446 0.2 1 120 26 28 ASP CA C 53.93 0.2 1 121 26 28 ASP CB C 41.51 0.2 1 122 26 28 ASP N N 119.2 0.2 1 123 27 29 PHE H H 8.384 0.02 1 124 27 29 PHE C C 175.591 0.2 1 125 27 29 PHE CA C 57.63 0.2 1 126 27 29 PHE CB C 40.82 0.2 1 127 27 29 PHE N N 120 0.2 1 128 28 30 LYS H H 8.505 0.02 1 129 28 30 LYS C C 174.664 0.2 1 130 28 30 LYS CA C 55.36 0.2 1 131 28 30 LYS CB C 34.18 0.2 1 132 28 30 LYS N N 123.3 0.2 1 133 29 31 ALA H H 8.419 0.02 1 134 29 31 ALA C C 177.083 0.2 1 135 29 31 ALA CA C 51.26 0.2 1 136 29 31 ALA CB C 21.1 0.2 1 137 29 31 ALA N N 126.5 0.2 1 138 30 32 TYR H H 8.575 0.02 1 139 30 32 TYR C C 174.4 0.2 1 140 30 32 TYR CA C 56.52 0.2 1 141 30 32 TYR CB C 40.2 0.2 1 142 30 32 TYR N N 119.9 0.2 1 143 31 33 LYS H H 8.686 0.02 1 144 31 33 LYS C C 176.433 0.2 1 145 31 33 LYS CA C 55.68 0.2 1 146 31 33 LYS CB C 33.31 0.2 1 147 31 33 LYS N N 123.32 0.2 1 148 32 34 THR H H 9.098 0.02 1 149 32 34 THR C C 171.9 0.2 1 150 32 34 THR CA C 60.46 0.2 1 151 32 34 THR CB C 70.55 0.2 1 152 32 34 THR N N 119.2 0.2 1 153 33 35 LYS H H 8.183 0.02 1 154 33 35 LYS C C 176.968 0.2 1 155 33 35 LYS CA C 55.96 0.2 1 156 33 35 LYS CB C 33.73 0.2 1 157 33 35 LYS N N 123.5 0.2 1 158 34 36 VAL H H 9.317 0.02 1 159 34 36 VAL C C 173.147 0.2 1 160 34 36 VAL CA C 59.24 0.2 1 161 34 36 VAL CB C 35.19 0.2 1 162 34 36 VAL N N 119.6 0.2 1 163 35 37 LYS H H 9.072 0.02 1 164 35 37 LYS C C 174.86 0.2 1 165 35 37 LYS CA C 55.63 0.2 1 166 35 37 LYS CB C 32.4 0.2 1 167 35 37 LYS N N 124.54 0.2 1 168 36 38 LEU H H 8.597 0.02 1 169 36 38 LEU C C 173.284 0.2 1 170 36 38 LEU CA C 53.29 0.2 1 171 36 38 LEU CB C 45.58 0.2 1 172 36 38 LEU N N 127.8 0.2 1 173 37 39 LYS H H 9.061 0.02 1 174 37 39 LYS C C 176.346 0.2 1 175 37 39 LYS CA C 54.11 0.2 1 176 37 39 LYS CB C 36.32 0.2 1 177 37 39 LYS N N 126 0.2 1 178 38 40 ILE H H 9.12 0.02 1 179 38 40 ILE C C 175.6 0.2 1 180 38 40 ILE CA C 59.68 0.2 1 181 38 40 ILE CB C 40.29 0.2 1 182 38 40 ILE N N 125 0.2 1 183 39 41 SER H H 9.11 0.02 1 184 39 41 SER C C 172 0.2 1 185 39 41 SER CA C 56.87 0.2 1 186 39 41 SER CB C 65.89 0.2 1 187 39 41 SER N N 121.4 0.2 1 188 40 42 GLU H H 9.185 0.02 1 189 40 42 GLU C C 174.923 0.2 1 190 40 42 GLU CA C 54.82 0.2 1 191 40 42 GLU CB C 32.45 0.2 1 192 40 42 GLU N N 123.5 0.2 1 193 41 43 GLN H H 8.845 0.02 1 194 41 43 GLN C C 173.824 0.2 1 195 41 43 GLN CA C 53.76 0.2 1 196 41 43 GLN CB C 31.37 0.2 1 197 41 43 GLN N N 120.6 0.2 1 198 42 44 ARG H H 8.609 0.02 1 199 42 44 ARG C C 175.958 0.2 1 200 42 44 ARG CA C 53.61 0.2 1 201 42 44 ARG CB C 31.73 0.2 1 202 42 44 ARG N N 119.3 0.2 1 203 43 45 ASN H H 9.064 0.02 1 204 43 45 ASN C C 177.482 0.2 1 205 43 45 ASN CA C 55.08 0.2 1 206 43 45 ASN CB C 40.19 0.2 1 207 43 45 ASN N N 124.6 0.2 1 208 44 46 GLU H H 9.34 0.02 1 209 44 46 GLU C C 176.85 0.2 1 210 44 46 GLU CA C 59.22 0.2 1 211 44 46 GLU CB C 29.87 0.2 1 212 44 46 GLU N N 127.8 0.2 1 213 45 47 THR H H 8.421 0.02 1 214 45 47 THR C C 175.812 0.2 1 215 45 47 THR CA C 64.6 0.2 1 216 45 47 THR CB C 69.01 0.2 1 217 45 47 THR N N 113.9 0.2 1 218 46 48 SER H H 8.708 0.02 1 219 46 48 SER C C 176.58 0.2 1 220 46 48 SER CA C 58.27 0.2 1 221 46 48 SER CB C 65.56 0.2 1 222 46 48 SER N N 115.7 0.2 1 223 47 49 GLY H H 8.178 0.02 1 224 47 49 GLY C C 173.8 0.2 1 225 47 49 GLY CA C 46.07 0.2 1 226 47 49 GLY N N 111.8 0.2 1 227 48 50 GLU H H 7.939 0.02 1 228 48 50 GLU C C 175.839 0.2 1 229 48 50 GLU CA C 56.35 0.2 1 230 48 50 GLU CB C 31.14 0.2 1 231 48 50 GLU N N 120.07 0.2 1 232 49 51 LYS H H 8.89 0.02 1 233 49 51 LYS C C 175.366 0.2 1 234 49 51 LYS CA C 58.12 0.2 1 235 49 51 LYS CB C 32.9 0.2 1 236 49 51 LYS N N 123.3 0.2 1 237 50 52 GLU H H 8.975 0.02 1 238 50 52 GLU C C 175.286 0.2 1 239 50 52 GLU CA C 54.05 0.2 1 240 50 52 GLU CB C 35.08 0.2 1 241 50 52 GLU N N 123.3 0.2 1 242 51 53 LEU H H 9.03 0.02 1 243 51 53 LEU C C 174.845 0.2 1 244 51 53 LEU CA C 52.82 0.2 1 245 51 53 LEU CB C 46.72 0.2 1 246 51 53 LEU N N 120.9 0.2 1 247 52 54 LYS H H 9.55 0.02 1 248 52 54 LYS C C 175.071 0.2 1 249 52 54 LYS CA C 55.33 0.2 1 250 52 54 LYS CB C 35.52 0.2 1 251 52 54 LYS N N 126.8 0.2 1 252 53 55 PHE H H 9.36 0.02 1 253 53 55 PHE C C 175.1 0.2 1 254 53 55 PHE CA C 56.76 0.2 1 255 53 55 PHE CB C 42.74 0.2 1 256 53 55 PHE N N 127 0.2 1 257 54 56 GLU H H 9.129 0.02 1 258 54 56 GLU C C 175.2 0.2 1 259 54 56 GLU CA C 55.36 0.2 1 260 54 56 GLU CB C 34.925 0.2 1 261 54 56 GLU N N 121.45 0.2 1 262 55 57 ILE H H 9.179 0.02 1 263 55 57 ILE C C 174 0.2 1 264 55 57 ILE CA C 58.645 0.2 1 265 55 57 ILE CB C 41.645 0.2 1 266 55 57 ILE N N 122.35 0.2 1 267 56 58 SER H H 8.954 0.02 1 268 56 58 SER C C 173.3 0.2 1 269 56 58 SER CA C 57.21 0.2 1 270 56 58 SER CB C 66.65 0.2 1 271 56 58 SER N N 117.98 0.2 1 272 57 59 ARG H H 9.025 0.02 1 273 57 59 ARG CB C 35.24 0.2 1 274 57 59 ARG N N 117.98 0.2 1 275 58 60 SER C C 174.4 0.2 1 276 58 60 SER CA C 60.31 0.2 1 277 58 60 SER CB C 62.97 0.2 1 278 59 61 ASP H H 8.602 0.02 1 279 59 61 ASP C C 175.1 0.2 1 280 59 61 ASP CA C 53.355 0.2 1 281 59 61 ASP CB C 40.165 0.2 1 282 59 61 ASP N N 116.98 0.2 1 283 60 62 ASP H H 7.173 0.02 1 284 60 62 ASP C C 176.4 0.2 1 285 60 62 ASP CA C 54 0.2 1 286 60 62 ASP CB C 41.45 0.2 1 287 60 62 ASP N N 117.25 0.2 1 288 61 63 PHE H H 8.812 0.02 1 289 61 63 PHE CA C 58.725 0.2 1 290 61 63 PHE CB C 38.415 0.2 1 291 61 63 PHE N N 125.25 0.2 1 292 62 64 GLU H H 8.205 0.02 1 293 62 64 GLU CA C 56.49 0.2 1 294 62 64 GLU N N 117.1 0.2 1 295 64 66 LEU C C 174.62 0.2 1 296 64 66 LEU CA C 55.2 0.2 1 297 64 66 LEU CB C 44.3 0.2 1 298 65 67 PHE H H 8.566 0.02 1 299 65 67 PHE C C 174.716 0.2 1 300 65 67 PHE CA C 55.78 0.2 1 301 65 67 PHE CB C 43.9 0.2 1 302 65 67 PHE N N 123.2 0.2 1 303 66 68 SER H H 9.564 0.02 1 304 66 68 SER C C 173.269 0.2 1 305 66 68 SER CA C 56.94 0.2 1 306 66 68 SER CB C 67.55 0.2 1 307 66 68 SER N N 116.3 0.2 1 308 67 69 GLU H H 8.899 0.02 1 309 67 69 GLU C C 174.482 0.2 1 310 67 69 GLU CA C 56.24 0.2 1 311 67 69 GLU CB C 34.79 0.2 1 312 67 69 GLU N N 122.9 0.2 1 313 68 70 THR H H 9.518 0.02 1 314 68 70 THR C C 173.854 0.2 1 315 68 70 THR CA C 61.54 0.2 1 316 68 70 THR CB C 70.36 0.2 1 317 68 70 THR N N 122.2 0.2 1 318 69 71 LEU H H 9.928 0.02 1 319 69 71 LEU C C 175.158 0.2 1 320 69 71 LEU CA C 54.48 0.2 1 321 69 71 LEU CB C 46.2 0.2 1 322 69 71 LEU N N 125.3 0.2 1 323 70 72 ASN H H 7.042 0.02 1 324 70 72 ASN C C 174.819 0.2 1 325 70 72 ASN CA C 50.73 0.2 1 326 70 72 ASN CB C 39.87 0.2 1 327 70 72 ASN N N 119.4 0.2 1 328 71 73 ASN H H 9.089 0.02 1 329 71 73 ASN C C 176.587 0.2 1 330 71 73 ASN CA C 57.57 0.2 1 331 71 73 ASN CB C 38.95 0.2 1 332 71 73 ASN N N 118.9 0.2 1 333 72 74 GLU H H 8.313 0.02 1 334 72 74 GLU C C 179.534 0.2 1 335 72 74 GLU CA C 60.21 0.2 1 336 72 74 GLU CB C 29.24 0.2 1 337 72 74 GLU N N 118.9 0.2 1 338 73 75 LYS H H 8.471 0.02 1 339 73 75 LYS C C 180.28 0.2 1 340 73 75 LYS CA C 59.5 0.2 1 341 73 75 LYS CB C 34.55 0.2 1 342 73 75 LYS N N 118.1 0.2 1 343 74 76 TYR H H 8.941 0.02 1 344 74 76 TYR C C 175.824 0.2 1 345 74 76 TYR CA C 61.94 0.2 1 346 74 76 TYR CB C 38.85 0.2 1 347 74 76 TYR N N 121.1 0.2 1 348 75 77 GLN H H 8.385 0.02 1 349 75 77 GLN C C 179.107 0.2 1 350 75 77 GLN CA C 58.81 0.2 1 351 75 77 GLN CB C 27.87 0.2 1 352 75 77 GLN N N 116.6 0.2 1 353 76 78 ILE H H 6.958 0.02 1 354 76 78 ILE C C 177.235 0.2 1 355 76 78 ILE CA C 64.42 0.2 1 356 76 78 ILE CB C 38.14 0.2 1 357 76 78 ILE N N 118.3 0.2 1 358 77 79 LEU H H 7.115 0.02 1 359 77 79 LEU C C 179.829 0.2 1 360 77 79 LEU CA C 58.24 0.2 1 361 77 79 LEU CB C 42.68 0.2 1 362 77 79 LEU N N 121.6 0.2 1 363 78 80 ALA H H 9.058 0.02 1 364 78 80 ALA C C 180.233 0.2 1 365 78 80 ALA CA C 55.19 0.2 1 366 78 80 ALA CB C 17.08 0.2 1 367 78 80 ALA N N 121.2 0.2 1 368 79 81 ARG H H 7.485 0.02 1 369 79 81 ARG C C 179.421 0.2 1 370 79 81 ARG CA C 58.55 0.2 1 371 79 81 ARG CB C 29.93 0.2 1 372 79 81 ARG N N 117.8 0.2 1 373 80 82 ASP H H 8.064 0.02 1 374 80 82 ASP C C 177.3 0.2 1 375 80 82 ASP CA C 56.63 0.2 1 376 80 82 ASP CB C 40.34 0.2 1 377 80 82 ASP N N 119.3 0.2 1 378 81 83 HIS H H 7.667 0.02 1 379 81 83 HIS C C 173.5 0.2 1 380 81 83 HIS CA C 56.355 0.2 1 381 81 83 HIS CB C 30.16 0.2 1 382 81 83 HIS N N 114.47 0.2 1 383 82 84 ASP H H 7.816 0.02 1 384 82 84 ASP C C 175.4 0.2 1 385 82 84 ASP CA C 55.45 0.2 1 386 82 84 ASP CB C 39.39 0.2 1 387 82 84 ASP N N 119.86 0.2 1 388 83 85 LEU H H 8.435 0.02 1 389 83 85 LEU CA C 54.55 0.2 1 390 83 85 LEU CB C 39.3 0.2 1 391 83 85 LEU N N 117.7 0.2 1 392 86 88 ASP C C 174.01 0.2 1 393 86 88 ASP CA C 52.93 0.2 1 394 86 88 ASP CB C 39.18 0.2 1 395 87 89 PHE H H 8.05 0.02 1 396 87 89 PHE C C 177.207 0.2 1 397 87 89 PHE CA C 58.77 0.2 1 398 87 89 PHE CB C 39.64 0.2 1 399 87 89 PHE N N 118.9 0.2 1 400 88 90 ASP H H 8.017 0.02 1 401 88 90 ASP C C 177.816 0.2 1 402 88 90 ASP CA C 56.62 0.2 1 403 88 90 ASP CB C 40.66 0.2 1 404 88 90 ASP N N 115.2 0.2 1 405 89 91 ALA H H 7.721 0.02 1 406 89 91 ALA C C 178.442 0.2 1 407 89 91 ALA CA C 52.8 0.2 1 408 89 91 ALA CB C 19.52 0.2 1 409 89 91 ALA N N 121.2 0.2 1 410 90 92 PHE H H 7.78 0.02 1 411 90 92 PHE CA C 61.64 0.2 1 412 90 92 PHE CB C 36.6 0.2 1 413 90 92 PHE N N 118.8 0.2 1 414 91 93 PRO C C 177.14 0.2 1 415 91 93 PRO CA C 65.9 0.2 1 416 91 93 PRO CB C 29.8 0.2 1 417 92 94 LYS H H 7.042 0.02 1 418 92 94 LYS C C 179.169 0.2 1 419 92 94 LYS CA C 59.6 0.2 1 420 92 94 LYS CB C 32.03 0.2 1 421 92 94 LYS N N 114.1 0.2 1 422 93 95 VAL H H 7.49 0.02 1 423 93 95 VAL C C 178.431 0.2 1 424 93 95 VAL CA C 66 0.2 1 425 93 95 VAL CB C 31.9 0.2 1 426 93 95 VAL N N 119.2 0.2 1 427 94 96 ILE H H 7.66 0.02 1 428 94 96 ILE C C 176.875 0.2 1 429 94 96 ILE CA C 63.5 0.2 1 430 94 96 ILE CB C 36.97 0.2 1 431 94 96 ILE N N 117.5 0.2 1 432 95 97 ILE H H 8.057 0.02 1 433 95 97 ILE C C 177.183 0.2 1 434 95 97 ILE CA C 66.18 0.2 1 435 95 97 ILE CB C 37.3 0.2 1 436 95 97 ILE N N 121.1 0.2 1 437 96 98 GLN H H 7.64 0.02 1 438 96 98 GLN C C 179 0.2 1 439 96 98 GLN CA C 59.22 0.2 1 440 96 98 GLN CB C 28 0.2 1 441 96 98 GLN N N 117.4 0.2 1 442 97 99 HIS H H 7.441 0.02 1 443 97 99 HIS C C 177.95 0.2 1 444 97 99 HIS CA C 59.535 0.2 1 445 97 99 HIS CB C 31.23 0.2 1 446 97 99 HIS N N 115.76 0.2 1 447 98 100 LEU H H 8.042 0.02 1 448 98 100 LEU C C 177.9 0.2 1 449 98 100 LEU CA C 56.76 0.2 1 450 98 100 LEU CB C 42.49 0.2 1 451 98 100 LEU N N 118.96 0.2 1 452 99 101 LEU H H 7.948 0.02 1 453 99 101 LEU C C 177.3 0.2 1 454 99 101 LEU CA C 55.245 0.2 1 455 99 101 LEU CB C 42.295 0.2 1 456 99 101 LEU N N 117.34 0.2 1 457 100 102 CYS H H 7.868 0.02 1 458 100 102 CYS C C 175.1 0.2 1 459 100 102 CYS CA C 59.69 0.2 1 460 100 102 CYS CB C 27.525 0.2 1 461 100 102 CYS N N 118.87 0.2 1 462 101 103 LYS H H 8.515 0.02 1 463 101 103 LYS C C 176.17 0.2 1 464 101 103 LYS CA C 56.47 0.2 1 465 101 103 LYS CB C 33 0.2 1 466 101 103 LYS N N 122.73 0.2 1 467 102 104 ASN H H 8.421 0.02 1 468 102 104 ASN C C 174.86 0.2 1 469 102 104 ASN CA C 53.62 0.2 1 470 102 104 ASN CB C 38.98 0.2 1 471 102 104 ASN N N 118.5 0.2 1 472 103 105 ILE H H 8.075 0.02 1 473 103 105 ILE C C 176.07 0.2 1 474 103 105 ILE CA C 61.33 0.2 1 475 103 105 ILE CB C 38.64 0.2 1 476 103 105 ILE N N 120.7 0.2 1 477 104 106 VAL H H 8.308 0.02 1 478 104 106 VAL C C 175.86 0.2 1 479 104 106 VAL CA C 62.4 0.2 1 480 104 106 VAL CB C 32.56 0.2 1 481 104 106 VAL N N 124.7 0.2 1 482 105 107 LYS H H 8.453 0.02 1 483 105 107 LYS C C 176 0.2 1 484 105 107 LYS CA C 56.2 0.2 1 485 105 107 LYS CB C 33.3 0.2 1 486 105 107 LYS N N 125.6 0.2 1 487 106 108 ASN H H 8.541 0.02 1 488 106 108 ASN C C 175.2 0.2 1 489 106 108 ASN CA C 53.28 0.2 1 490 106 108 ASN CB C 38.98 0.2 1 491 106 108 ASN N N 120.3 0.2 1 492 107 109 LEU H H 8.427 0.02 1 493 107 109 LEU C C 177.6 0.2 1 494 107 109 LEU CA C 55.605 0.2 1 495 107 109 LEU CB C 42.21 0.2 1 496 107 109 LEU N N 122.95 0.2 1 497 108 110 GLU H H 8.461 0.02 1 498 108 110 GLU C C 176.9 0.2 1 499 108 110 GLU CA C 56.825 0.2 1 500 108 110 GLU CB C 30.035 0.2 1 501 108 110 GLU N N 120.76 0.2 1 502 109 111 GLU H H 8.358 0.02 1 503 109 111 GLU C C 176.4 0.2 1 504 109 111 GLU CA C 56.725 0.2 1 505 109 111 GLU CB C 30.225 0.2 1 506 109 111 GLU N N 121.29 0.2 1 507 110 112 ASP H H 8.401 0.02 1 508 110 112 ASP C C 176.96 0.2 1 509 110 112 ASP CA C 54.61 0.2 1 510 110 112 ASP CB C 41.26 0.2 1 511 110 112 ASP N N 121.36 0.2 1 512 111 113 GLY H H 8.395 0.02 1 513 111 113 GLY C C 174.55 0.2 1 514 111 113 GLY CA C 45.59 0.2 1 515 111 113 GLY N N 109.2 0.2 1 516 112 114 GLU H H 8.302 0.02 1 517 112 114 GLU C C 177.11 0.2 1 518 112 114 GLU CA C 56.75 0.2 1 519 112 114 GLU CB C 30.09 0.2 1 520 112 114 GLU N N 121 0.2 1 521 113 115 VAL H H 8.182 0.02 1 522 113 115 VAL C C 176.58 0.2 1 523 113 115 VAL CA C 63.5 0.2 1 524 113 115 VAL CB C 32.41 0.2 1 525 113 115 VAL N N 121.1 0.2 1 526 114 116 ASP H H 8.434 0.02 1 527 114 116 ASP C C 176.96 0.2 1 528 114 116 ASP CA C 54.86 0.2 1 529 114 116 ASP CB C 41.14 0.2 1 530 114 116 ASP N N 123 0.2 1 531 115 117 ALA H H 8.344 0.02 1 532 115 117 ALA C C 179.11 0.2 1 533 115 117 ALA CA C 53.99 0.2 1 534 115 117 ALA CB C 18.77 0.2 1 535 115 117 ALA N N 124.8 0.2 1 536 116 118 ARG H H 8.204 0.02 1 537 116 118 ARG C C 177.48 0.2 1 538 116 118 ARG CA C 57.405 0.2 1 539 116 118 ARG CB C 30.15 0.2 1 540 116 118 ARG N N 117.7 0.2 1 541 117 119 LYS H H 7.984 0.02 1 542 117 119 LYS C C 177.5 0.2 1 543 117 119 LYS CA C 57.09 0.2 1 544 117 119 LYS CB C 32.87 0.2 1 545 117 119 LYS N N 120.2 0.2 1 546 118 120 LYS H H 8.067 0.02 1 547 118 120 LYS C C 176.7 0.2 1 548 118 120 LYS CA C 56.785 0.2 1 549 118 120 LYS CB C 32.895 0.2 1 550 118 120 LYS N N 121.23 0.2 1 551 119 121 ALA H H 8.197 0.02 1 552 119 121 ALA C C 178.29 0.2 1 553 119 121 ALA CA C 52.89 0.2 1 554 119 121 ALA CB C 19.02 0.2 1 555 119 121 ALA N N 124 0.2 1 556 120 122 GLY H H 8.344 0.02 1 557 120 122 GLY C C 174.07 0.2 1 558 120 122 GLY CA C 45.28 0.2 1 559 120 122 GLY N N 107.9 0.2 1 560 121 123 TYR H H 7.984 0.02 1 561 121 123 TYR C C 175.6 0.2 1 562 121 123 TYR CA C 58.4 0.2 1 563 121 123 TYR CB C 38.79 0.2 1 564 121 123 TYR N N 120.3 0.2 1 565 122 124 HIS H H 8.197 0.02 1 566 122 124 HIS C C 174.5 0.2 1 567 122 124 HIS CA C 55.94 0.2 1 568 122 124 HIS CB C 30.78 0.2 1 569 122 124 HIS N N 121.7 0.2 1 570 123 125 GLU H H 8.268 0.02 1 571 123 125 GLU C C 176.2 0.2 1 572 123 125 GLU CA C 56.27 0.2 1 573 123 125 GLU CB C 30.6 0.2 1 574 123 125 GLU N N 122.1 0.2 1 575 124 126 ILE H H 8.244 0.02 1 576 124 126 ILE C C 175.75 0.2 1 577 124 126 ILE CA C 60.99 0.2 1 578 124 126 ILE CB C 38.74 0.2 1 579 124 126 ILE N N 122 0.2 1 580 125 127 ALA H H 8.382 0.02 1 581 125 127 ALA C C 176.85 0.2 1 582 125 127 ALA CA C 52.35 0.2 1 583 125 127 ALA CB C 19.38 0.2 1 584 125 127 ALA N N 128 0.2 1 585 126 128 ASP H H 8.359 0.02 1 586 126 128 ASP CA C 52.15 0.2 1 587 126 128 ASP CB C 41.62 0.2 1 588 126 128 ASP N N 121.2 0.2 1 589 127 129 PRO C C 177.47 0.2 1 590 127 129 PRO CA C 63.51 0.2 1 591 127 129 PRO CB C 31.99 0.2 1 592 128 130 GLY H H 8.544 0.02 1 593 128 130 GLY C C 173.75 0.2 1 594 128 130 GLY CA C 45.22 0.2 1 595 128 130 GLY N N 108.3 0.2 1 596 129 131 LYS H H 8.095 0.02 1 597 129 131 LYS CA C 53.92 0.2 1 598 129 131 LYS CB C 33 0.2 1 599 129 131 LYS N N 121.5 0.2 1 600 130 132 PRO C C 176.46 0.2 1 601 130 132 PRO CA C 63.77 0.2 1 602 130 132 PRO CB C 32.08 0.2 1 603 131 133 THR H H 7.947 0.02 1 604 131 133 THR C C 173.81 0.2 1 605 131 133 THR CA C 60.94 0.2 1 606 131 133 THR CB C 71.275 0.2 1 607 131 133 THR N N 114.7 0.2 1 608 132 134 GLU H H 8.92 0.02 1 609 132 134 GLU C C 174.13 0.2 1 610 132 134 GLU CA C 55.56 0.2 1 611 132 134 GLU CB C 32.48 0.2 1 612 132 134 GLU N N 123.4 0.2 1 613 133 135 ILE H H 8.561 0.02 1 614 133 135 ILE C C 175.56 0.2 1 615 133 135 ILE CA C 59.78 0.2 1 616 133 135 ILE CB C 40.35 0.2 1 617 133 135 ILE N N 121.6 0.2 1 618 134 136 ASN H H 8.973 0.02 1 619 134 136 ASN C C 173.57 0.2 1 620 134 136 ASN CA C 51.21 0.2 1 621 134 136 ASN CB C 41.78 0.2 1 622 134 136 ASN N N 125.6 0.2 1 623 135 137 ILE H H 9.16 0.02 1 624 135 137 ILE C C 174.2 0.2 1 625 135 137 ILE CA C 59.2 0.2 1 626 135 137 ILE CB C 39.5 0.2 1 627 135 137 ILE N N 122 0.2 1 628 136 138 ILE H H 8.93 0.02 1 629 136 138 ILE C C 176.71 0.2 1 630 136 138 ILE CA C 60.53 0.2 1 631 136 138 ILE CB C 38.93 0.2 1 632 136 138 ILE N N 126.8 0.2 1 633 137 139 LEU H H 8.876 0.02 1 634 137 139 LEU CA C 54.84 0.2 1 635 137 139 LEU CB C 43.87 0.2 1 636 137 139 LEU N N 130.6 0.2 1 637 138 140 ASP H H 7.705 0.02 1 638 138 140 ASP C C 178.07 0.2 1 639 138 140 ASP CA C 53.36 0.2 1 640 138 140 ASP CB C 43.17 0.2 1 641 138 140 ASP N N 120.2 0.2 1 642 139 141 ALA H H 8.847 0.02 1 643 139 141 ALA C C 179 0.2 1 644 139 141 ALA CA C 55.66 0.2 1 645 139 141 ALA CB C 18.56 0.2 1 646 139 141 ALA N N 128.1 0.2 1 647 140 142 GLU H H 7.701 0.02 1 648 140 142 GLU C C 175.8 0.2 1 649 140 142 GLU CA C 56.2 0.2 1 650 140 142 GLU CB C 29.73 0.2 1 651 140 142 GLU N N 113.9 0.2 1 652 141 143 LYS H H 7.53 0.02 1 653 141 143 LYS CA C 57.06 0.2 1 654 141 143 LYS N N 122.88 0.2 1 655 142 144 ASN C C 176.12 0.2 1 656 142 144 ASN CA C 55.13 0.2 1 657 142 144 ASN CB C 39.38 0.2 1 658 143 145 PHE H H 7.87 0.02 1 659 143 145 PHE C C 172.7 0.2 1 660 143 145 PHE CA C 56.26 0.2 1 661 143 145 PHE CB C 41.25 0.2 1 662 143 145 PHE N N 115.8 0.2 1 663 144 146 CYS H H 9.051 0.02 1 664 144 146 CYS C C 172.4 0.2 1 665 144 146 CYS CA C 55.52 0.2 1 666 144 146 CYS CB C 31.32 0.2 1 667 144 146 CYS N N 114.1 0.2 1 668 145 147 SER H H 9.054 0.02 1 669 145 147 SER C C 173.02 0.2 1 670 145 147 SER CA C 57.25 0.2 1 671 145 147 SER CB C 63.75 0.2 1 672 145 147 SER N N 117.7 0.2 1 673 146 148 PHE H H 9.114 0.02 1 674 146 148 PHE C C 173.24 0.2 1 675 146 148 PHE CA C 56.64 0.2 1 676 146 148 PHE CB C 40.86 0.2 1 677 146 148 PHE N N 129.3 0.2 1 678 147 149 GLU H H 8.822 0.02 1 679 147 149 GLU C C 173.39 0.2 1 680 147 149 GLU CA C 54.63 0.2 1 681 147 149 GLU CB C 33.08 0.2 1 682 147 149 GLU N N 125.8 0.2 1 683 148 150 LEU H H 7.88 0.02 1 684 148 150 LEU C C 174.78 0.2 1 685 148 150 LEU CA C 51.24 0.2 1 686 148 150 LEU CB C 45.4 0.2 1 687 148 150 LEU N N 122.2 0.2 1 688 149 151 PHE H H 9.184 0.02 1 689 149 151 PHE C C 174.74 0.2 1 690 149 151 PHE CA C 56.37 0.2 1 691 149 151 PHE CB C 42.33 0.2 1 692 149 151 PHE N N 124.7 0.2 1 693 150 152 SER H H 8.925 0.02 1 694 150 152 SER C C 174.8 0.2 1 695 150 152 SER CA C 56.9 0.2 1 696 150 152 SER CB C 64.46 0.2 1 697 150 152 SER N N 116.1 0.2 1 698 151 153 LYS H H 8.877 0.02 1 699 151 153 LYS C C 175.9 0.2 1 700 151 153 LYS CA C 55.845 0.2 1 701 151 153 LYS CB C 33.16 0.2 1 702 151 153 LYS N N 126.29 0.2 1 703 152 154 THR H H 8.254 0.02 1 704 152 154 THR CA C 59.94 0.2 1 705 152 154 THR CB C 69.19 0.2 1 706 152 154 THR N N 117.01 0.2 1 707 153 155 PRO C C 177.7 0.2 1 708 153 155 PRO CA C 65.19 0.2 1 709 153 155 PRO CB C 31.65 0.2 1 710 154 156 GLU H H 8.398 0.02 1 711 154 156 GLU C C 176.4 0.2 1 712 154 156 GLU CA C 57.37 0.2 1 713 154 156 GLU CB C 29.7 0.2 1 714 154 156 GLU N N 114.08 0.2 1 715 155 157 SER H H 7.741 0.02 1 716 155 157 SER C C 173.6 0.2 1 717 155 157 SER CA C 57.59 0.2 1 718 155 157 SER CB C 64.38 0.2 1 719 155 157 SER N N 114.31 0.2 1 720 156 158 LYS H H 8.334 0.02 1 721 156 158 LYS C C 176.47 0.2 1 722 156 158 LYS CA C 56.195 0.2 1 723 156 158 LYS CB C 33.31 0.2 1 724 156 158 LYS N N 123.17 0.2 1 725 157 159 GLY H H 8.438 0.02 1 726 157 159 GLY C C 172.81 0.2 1 727 157 159 GLY CA C 44.84 0.2 1 728 157 159 GLY N N 110 0.2 1 729 158 160 LYS H H 8.599 0.02 1 730 158 160 LYS C C 176.27 0.2 1 731 158 160 LYS CA C 57.03 0.2 1 732 158 160 LYS CB C 32.025 0.2 1 733 158 160 LYS N N 124 0.2 1 734 159 161 ILE H H 8.9 0.02 1 735 159 161 ILE C C 174.5 0.2 1 736 159 161 ILE CA C 61.94 0.2 1 737 159 161 ILE CB C 38.74 0.2 1 738 159 161 ILE N N 126.44 0.2 1 739 160 162 PHE H H 8.383 0.02 1 740 160 162 PHE CA C 58.46 0.2 1 741 160 162 PHE N N 119.46 0.2 1 742 161 163 SER C C 171.4 0.2 1 743 161 163 SER CA C 56.14 0.2 1 744 161 163 SER CB C 65.66 0.2 1 745 162 164 ILE H H 8.509 0.02 1 746 162 164 ILE C C 172.1 0.2 1 747 162 164 ILE CA C 59.82 0.2 1 748 162 164 ILE CB C 41.4 0.2 1 749 162 164 ILE N N 119.3 0.2 1 750 163 165 LYS H H 8.411 0.02 1 751 163 165 LYS C C 175.01 0.2 1 752 163 165 LYS CA C 55.54 0.2 1 753 163 165 LYS CB C 32.75 0.2 1 754 163 165 LYS N N 128.7 0.2 1 755 164 166 LEU H H 9.06 0.02 1 756 164 166 LEU C C 175.89 0.2 1 757 164 166 LEU CA C 53.49 0.2 1 758 164 166 LEU CB C 44.41 0.2 1 759 164 166 LEU N N 124.6 0.2 1 760 165 167 HIS H H 8.669 0.02 1 761 165 167 HIS C C 175.83 0.2 1 762 165 167 HIS CA C 56.17 0.2 1 763 165 167 HIS CB C 32.3 0.2 1 764 165 167 HIS N N 120.6 0.2 1 765 166 168 ALA H H 8.382 0.02 1 766 166 168 ALA C C 177.74 0.2 1 767 166 168 ALA CA C 53.15 0.2 1 768 166 168 ALA CB C 18.54 0.2 1 769 166 168 ALA N N 125.6 0.2 1 770 167 169 VAL H H 7.838 0.02 1 771 167 169 VAL C C 174.95 0.2 1 772 167 169 VAL CA C 62.88 0.2 1 773 167 169 VAL CB C 32 0.2 1 774 167 169 VAL N N 124.3 0.2 1 775 168 170 ARG H H 8.035 0.02 1 776 168 170 ARG CA C 56.87 0.2 1 777 168 170 ARG CB C 32.08 0.2 1 778 168 170 ARG N N 131.3 0.2 1 stop_ save_