data_18855 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignments of 8M urea denatured YibK from Haemophilus influenzae (HI0766) ; _BMRB_accession_number 18855 _BMRB_flat_file_name bmr18855.str _Entry_type original _Submission_date 2012-11-24 _Accession_date 2012-11-24 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Characterisation of knotted proteins in chemically denatured states' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hsieh 'Shu-Ju Micky' . . 2 Hsu 'Shang-Te Danny' . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 146 "13C chemical shifts" 444 "15N chemical shifts" 146 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-08-27 update BMRB 'update entry citation' 2014-02-14 original author 'original release' stop_ _Original_release_date 2012-11-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone 1H, 13C and 15N assignments of YibK and avariant containing a unique cysteine residue at C-terminus in 8 M urea-denatured states ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23853076 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hsieh 'Shu-Ju Micky' . . 2 Mallam Anna L. . 3 Jackson Sophie E. . 4 Hsu 'Shang-Te Danny' . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 8 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 439 _Page_last 442 _Year 2014 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_reference_citation _Saveframe_category citation _Citation_full . _Citation_title ; Experimental detection of knotted conformations in denatured proteins. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20393125 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mallam AL . . 2 Rogers JM . . 3 Jackson SE . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_name_full . _Journal_volume 107 _Journal_issue 18 _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 8189 _Page_last 8194 _Year 2010 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name YibK _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label YibK $YibK stop_ _System_molecular_weight . _System_physical_state denatured _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_YibK _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common YibK _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 160 _Mol_residue_sequence ; MLDIVLYEPEIPQNTGNIIR LCANTGFRLHLIEPLGFTWD DKRLRRSGLDYHEFAEIKRH KTFEAFLESEKPKRLFALTT KGCPAHSQVKFKLGDYLMFG PETRGIPMSILNEMPMEQKI RIPMTANSRSMNLSNSVAVT VYEAWRQLGYKGAVNLPEVK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 LEU 3 3 ASP 4 4 ILE 5 5 VAL 6 6 LEU 7 7 TYR 8 8 GLU 9 9 PRO 10 10 GLU 11 11 ILE 12 12 PRO 13 13 GLN 14 14 ASN 15 15 THR 16 16 GLY 17 17 ASN 18 18 ILE 19 19 ILE 20 20 ARG 21 21 LEU 22 22 CYS 23 23 ALA 24 24 ASN 25 25 THR 26 26 GLY 27 27 PHE 28 28 ARG 29 29 LEU 30 30 HIS 31 31 LEU 32 32 ILE 33 33 GLU 34 34 PRO 35 35 LEU 36 36 GLY 37 37 PHE 38 38 THR 39 39 TRP 40 40 ASP 41 41 ASP 42 42 LYS 43 43 ARG 44 44 LEU 45 45 ARG 46 46 ARG 47 47 SER 48 48 GLY 49 49 LEU 50 50 ASP 51 51 TYR 52 52 HIS 53 53 GLU 54 54 PHE 55 55 ALA 56 56 GLU 57 57 ILE 58 58 LYS 59 59 ARG 60 60 HIS 61 61 LYS 62 62 THR 63 63 PHE 64 64 GLU 65 65 ALA 66 66 PHE 67 67 LEU 68 68 GLU 69 69 SER 70 70 GLU 71 71 LYS 72 72 PRO 73 73 LYS 74 74 ARG 75 75 LEU 76 76 PHE 77 77 ALA 78 78 LEU 79 79 THR 80 80 THR 81 81 LYS 82 82 GLY 83 83 CYS 84 84 PRO 85 85 ALA 86 86 HIS 87 87 SER 88 88 GLN 89 89 VAL 90 90 LYS 91 91 PHE 92 92 LYS 93 93 LEU 94 94 GLY 95 95 ASP 96 96 TYR 97 97 LEU 98 98 MET 99 99 PHE 100 100 GLY 101 101 PRO 102 102 GLU 103 103 THR 104 104 ARG 105 105 GLY 106 106 ILE 107 107 PRO 108 108 MET 109 109 SER 110 110 ILE 111 111 LEU 112 112 ASN 113 113 GLU 114 114 MET 115 115 PRO 116 116 MET 117 117 GLU 118 118 GLN 119 119 LYS 120 120 ILE 121 121 ARG 122 122 ILE 123 123 PRO 124 124 MET 125 125 THR 126 126 ALA 127 127 ASN 128 128 SER 129 129 ARG 130 130 SER 131 131 MET 132 132 ASN 133 133 LEU 134 134 SER 135 135 ASN 136 136 SER 137 137 VAL 138 138 ALA 139 139 VAL 140 140 THR 141 141 VAL 142 142 TYR 143 143 GLU 144 144 ALA 145 145 TRP 146 146 ARG 147 147 GLN 148 148 LEU 149 149 GLY 150 150 TYR 151 151 LYS 152 152 GLY 153 153 ALA 154 154 VAL 155 155 ASN 156 156 LEU 157 157 PRO 158 158 GLU 159 159 VAL 160 160 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $YibK 'Haemophilus influenzae' 727 Bacteria . Haemophilus influenzae 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 $YibK 'recombinant technology' . Escherichia coli . 'Pet 17b' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_YibK_in_denatured_state _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $YibK 350 uM '[U-13C; U-15N]' D2O 10 % 'natural abundance' TRIS 50 mM 'natural abundance' 'potassium chloride' 200 mM 'natural abundance' glycerol 10 % 'natural abundance' urea 7.2 M 'natural abundance' H2O 90 % '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' 'data analysis' 'peak picking' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection 'data analysis' 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_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $YibK_in_denatured_state save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $YibK_in_denatured_state save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $YibK_in_denatured_state save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $YibK_in_denatured_state save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $YibK_in_denatured_state save_ save_3D_C(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $YibK_in_denatured_state save_ ####################### # Sample conditions # ####################### save_SEC-urea _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 . pH pressure 1 . atm temperature 278 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio water C 13 protons ppm 175.4 internal indirect . . . 0.251449530 water H 1 protons ppm 4.964 internal direct . . . 1 water N 15 protons ppm 118.773 internal indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_YibK_wt_in_denatured_state _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCO' '3D HNCACB' '3D HNCA' '3D C(CO)NH' stop_ loop_ _Sample_label $YibK_in_denatured_state stop_ _Sample_conditions_label $SEC-urea _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name YibK _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 2 2 LEU C C 177.000 0.200 1 2 2 2 LEU CB C 41.844 0.003 1 3 3 3 ASP H H 8.754 0.001 1 4 3 3 ASP C C 175.972 0.017 1 5 3 3 ASP CA C 53.962 0.036 1 6 3 3 ASP CB C 40.678 0.050 1 7 3 3 ASP N N 122.084 0.026 1 8 4 4 ILE H H 8.268 0.001 1 9 4 4 ILE C C 176.484 0.654 1 10 4 4 ILE CA C 60.765 0.050 1 11 4 4 ILE CB C 38.166 0.025 1 12 4 4 ILE N N 121.037 0.023 1 13 5 5 VAL H H 8.483 0.001 1 14 5 5 VAL C C 175.661 0.017 1 15 5 5 VAL CA C 61.983 0.088 1 16 5 5 VAL CB C 31.948 0.015 1 17 5 5 VAL N N 125.899 0.020 1 18 6 6 LEU H H 8.553 0.001 1 19 6 6 LEU C C 176.782 0.048 1 20 6 6 LEU CA C 54.457 0.078 1 21 6 6 LEU CB C 41.594 0.076 1 22 6 6 LEU N N 126.923 0.039 1 23 7 7 TYR H H 8.484 0.002 1 24 7 7 TYR C C 176.079 0.013 1 25 7 7 TYR CA C 60.632 0.068 1 26 7 7 TYR CB C 37.917 0.039 1 27 7 7 TYR N N 122.472 0.085 1 28 8 8 GLU H H 8.742 0.001 1 29 8 8 GLU C C 175.941 0.200 1 30 8 8 GLU CA C 55.597 0.200 1 31 8 8 GLU CB C 30.097 0.200 1 32 8 8 GLU N N 126.617 0.058 1 33 12 12 PRO C C 176.958 0.200 1 34 12 12 PRO CA C 62.839 0.130 1 35 12 12 PRO CB C 31.459 0.052 1 36 13 13 GLN H H 8.793 0.001 1 37 13 13 GLN C C 176.045 0.005 1 38 13 13 GLN CA C 55.569 0.081 1 39 13 13 GLN CB C 29.084 0.028 1 40 13 13 GLN N N 121.046 0.023 1 41 14 14 ASN H H 8.808 0.004 1 42 14 14 ASN C C 175.669 0.014 1 43 14 14 ASN CA C 53.014 0.113 1 44 14 14 ASN CB C 38.262 0.060 1 45 14 14 ASN N N 120.063 0.036 1 46 15 15 THR H H 8.436 0.001 1 47 15 15 THR C C 175.297 0.014 1 48 15 15 THR CA C 61.846 0.074 1 49 15 15 THR CB C 69.355 0.043 1 50 15 15 THR N N 113.986 0.029 1 51 16 16 GLY H H 8.606 0.003 1 52 16 16 GLY C C 173.821 0.008 1 53 16 16 GLY CA C 45.005 0.043 1 54 16 16 GLY N N 110.447 0.038 1 55 17 17 ASN H H 8.504 0.002 1 56 17 17 ASN C C 175.113 0.009 1 57 17 17 ASN CA C 52.998 0.113 1 58 17 17 ASN CB C 38.402 0.186 1 59 17 17 ASN N N 118.852 0.028 1 60 18 18 ILE H H 8.350 0.001 1 61 18 18 ILE C C 176.070 0.076 1 62 18 18 ILE CA C 60.921 0.090 1 63 18 18 ILE CB C 37.916 0.036 1 64 18 18 ILE N N 121.800 0.082 1 65 19 19 ILE H H 8.583 0.003 1 66 19 19 ILE C C 176.019 0.044 1 67 19 19 ILE CA C 60.746 0.037 1 68 19 19 ILE CB C 37.751 0.277 1 69 19 19 ILE N N 126.587 0.054 1 70 20 20 ARG H H 8.721 0.002 1 71 20 20 ARG C C 174.407 0.200 1 72 20 20 ARG CA C 54.175 0.005 1 73 20 20 ARG CB C 29.300 0.148 1 74 20 20 ARG N N 126.819 0.066 1 75 21 21 LEU H H 8.570 0.007 1 76 21 21 LEU C C 175.439 0.200 1 77 21 21 LEU CA C 57.537 0.016 1 78 21 21 LEU CB C 38.296 0.127 1 79 21 21 LEU N N 122.590 0.012 1 80 22 22 CYS H H 8.603 0.002 1 81 22 22 CYS C C 174.002 0.200 1 82 22 22 CYS CA C 56.303 0.200 1 83 22 22 CYS N N 124.647 0.046 1 84 23 23 ALA H H 8.400 0.001 1 85 23 23 ALA CA C 52.251 0.200 1 86 23 23 ALA CB C 18.681 0.052 1 87 23 23 ALA N N 124.962 0.043 1 88 24 24 ASN H H 8.403 0.002 1 89 24 24 ASN C C 175.686 0.200 1 90 24 24 ASN CA C 57.624 0.200 1 91 24 24 ASN CB C 38.691 0.200 1 92 24 24 ASN N N 119.597 0.021 1 93 25 25 THR H H 8.468 0.006 1 94 25 25 THR C C 174.809 0.515 1 95 25 25 THR CA C 61.691 0.095 1 96 25 25 THR CB C 69.707 0.014 1 97 25 25 THR N N 115.517 0.007 1 98 26 26 GLY H H 8.510 0.016 1 99 26 26 GLY C C 173.672 0.003 1 100 26 26 GLY CA C 45.018 0.016 1 101 26 26 GLY N N 110.503 0.033 1 102 27 27 PHE H H 8.239 0.001 1 103 27 27 PHE C C 175.601 0.200 1 104 27 27 PHE CA C 57.547 0.200 1 105 27 27 PHE CB C 38.892 0.200 1 106 27 27 PHE N N 120.256 0.027 1 107 28 28 ARG H H 8.593 0.001 1 108 28 28 ARG C C 175.746 0.200 1 109 28 28 ARG CA C 55.391 0.200 1 110 28 28 ARG CB C 30.316 0.020 1 111 28 28 ARG N N 123.688 0.024 1 112 29 29 LEU H H 8.511 0.003 1 113 29 29 LEU C C 176.939 0.068 1 114 29 29 LEU CA C 58.721 3.950 1 115 29 29 LEU CB C 36.673 5.068 1 116 29 29 LEU N N 124.309 0.057 1 117 30 30 HIS H H 8.710 0.003 1 118 30 30 HIS C C 175.261 0.001 1 119 30 30 HIS CA C 56.203 0.200 1 120 30 30 HIS CB C 30.605 0.066 1 121 30 30 HIS N N 121.416 0.052 1 122 31 31 LEU H H 8.432 0.002 1 123 31 31 LEU C C 176.916 0.041 1 124 31 31 LEU CA C 54.450 0.203 1 125 31 31 LEU CB C 41.434 0.030 1 126 31 31 LEU N N 124.255 0.069 1 127 32 32 ILE H H 8.582 0.002 1 128 32 32 ILE C C 175.692 0.291 1 129 32 32 ILE CA C 57.384 0.200 1 130 32 32 ILE CB C 38.517 0.200 1 131 32 32 ILE N N 122.217 0.028 1 132 33 33 GLU H H 8.683 0.001 1 133 33 33 GLU C C 177.197 0.200 1 134 33 33 GLU N N 124.790 0.099 1 135 35 35 LEU H H 8.577 0.004 1 136 35 35 LEU C C 178.106 0.200 1 137 35 35 LEU CA C 55.019 0.060 1 138 35 35 LEU CB C 41.530 0.200 1 139 35 35 LEU N N 122.556 0.059 1 140 36 36 GLY H H 8.601 0.003 1 141 36 36 GLY C C 173.562 0.017 1 142 36 36 GLY CA C 44.722 0.026 1 143 36 36 GLY N N 109.721 0.072 1 144 37 37 PHE H H 8.317 0.002 1 145 37 37 PHE C C 176.041 0.009 1 146 37 37 PHE CA C 57.535 0.191 1 147 37 37 PHE CB C 39.260 0.157 1 148 37 37 PHE N N 120.121 0.028 1 149 38 38 THR H H 8.390 0.001 1 150 38 38 THR C C 174.222 0.010 1 151 38 38 THR CA C 61.274 0.035 1 152 38 38 THR CB C 69.783 0.043 1 153 38 38 THR N N 116.143 0.036 1 154 39 39 TRP H H 8.421 0.002 1 155 39 39 TRP C C 175.844 0.005 1 156 39 39 TRP CA C 57.305 0.113 1 157 39 39 TRP CB C 28.978 0.033 1 158 39 39 TRP N N 123.163 0.031 1 159 40 40 ASP H H 8.414 0.002 1 160 40 40 ASP C C 175.763 0.035 1 161 40 40 ASP CA C 53.618 0.143 1 162 40 40 ASP CB C 40.587 0.041 1 163 40 40 ASP N N 121.748 0.053 1 164 41 41 ASP H H 8.303 0.003 1 165 41 41 ASP C C 176.911 0.030 1 166 41 41 ASP CA C 54.276 0.024 1 167 41 41 ASP CB C 40.630 0.059 1 168 41 41 ASP N N 121.648 0.030 1 169 42 42 LYS H H 8.587 0.001 1 170 42 42 LYS C C 177.091 0.001 1 171 42 42 LYS CA C 56.496 0.123 1 172 42 42 LYS CB C 31.520 0.080 1 173 42 42 LYS N N 122.043 0.055 1 174 43 43 ARG H H 8.383 0.003 1 175 43 43 ARG C C 176.655 0.029 1 176 43 43 ARG CA C 56.343 0.153 1 177 43 43 ARG CB C 29.753 0.053 1 178 43 43 ARG N N 120.219 0.032 1 179 44 44 LEU H H 8.282 0.002 1 180 44 44 LEU C C 177.377 0.200 1 181 44 44 LEU CA C 54.669 0.251 1 182 44 44 LEU CB C 41.436 0.014 1 183 44 44 LEU N N 122.161 0.051 1 184 45 45 ARG H H 8.529 0.053 1 185 45 45 ARG C C 176.446 0.200 1 186 45 45 ARG CA C 55.762 0.200 1 187 45 45 ARG CB C 30.027 0.054 1 188 45 45 ARG N N 122.563 0.079 1 189 46 46 ARG H H 8.777 0.001 1 190 46 46 ARG C C 176.441 0.015 1 191 46 46 ARG CA C 55.995 0.050 1 192 46 46 ARG CB C 30.184 0.006 1 193 46 46 ARG N N 123.420 0.037 1 194 47 47 SER H H 8.720 0.002 1 195 47 47 SER C C 175.041 0.009 1 196 47 47 SER CA C 58.032 0.094 1 197 47 47 SER CB C 63.584 0.048 1 198 47 47 SER N N 117.515 0.018 1 199 48 48 GLY H H 8.688 0.001 1 200 48 48 GLY C C 173.964 0.036 1 201 48 48 GLY CA C 45.123 0.018 1 202 48 48 GLY N N 110.911 0.013 1 203 49 49 LEU H H 8.267 0.001 1 204 49 49 LEU C C 175.792 0.200 1 205 49 49 LEU CA C 54.685 0.072 1 206 49 49 LEU CB C 41.732 0.003 1 207 49 49 LEU N N 121.037 0.025 1 208 50 50 ASP H H 8.600 0.002 1 209 50 50 ASP C C 176.008 0.076 1 210 50 50 ASP CA C 54.093 0.034 1 211 50 50 ASP CB C 40.847 0.081 1 212 50 50 ASP N N 120.638 0.025 1 213 51 51 TYR H H 8.304 0.003 1 214 51 51 TYR C C 175.442 0.026 1 215 51 51 TYR CA C 57.789 0.036 1 216 51 51 TYR CB C 38.278 0.067 1 217 51 51 TYR N N 120.595 0.041 1 218 52 52 HIS H H 8.369 0.001 1 219 52 52 HIS C C 175.181 0.027 1 220 52 52 HIS CA C 56.051 0.200 1 221 52 52 HIS CB C 30.779 0.009 1 222 52 52 HIS N N 122.055 0.068 1 223 53 53 GLU H H 8.414 0.001 1 224 53 53 GLU C C 176.147 0.016 1 225 53 53 GLU CA C 56.194 0.102 1 226 53 53 GLU CB C 29.849 0.024 1 227 53 53 GLU N N 122.584 0.041 1 228 54 54 PHE H H 8.534 0.001 1 229 54 54 PHE C C 175.522 0.014 1 230 54 54 PHE CA C 57.402 0.108 1 231 54 54 PHE CB C 38.957 0.027 1 232 54 54 PHE N N 120.769 0.045 1 233 55 55 ALA H H 8.386 0.002 1 234 55 55 ALA C C 177.318 0.015 1 235 55 55 ALA CA C 52.175 0.001 1 236 55 55 ALA CB C 18.798 0.028 1 237 55 55 ALA N N 125.258 0.052 1 238 56 56 GLU H H 8.507 0.001 1 239 56 56 GLU C C 176.421 0.006 1 240 56 56 GLU CA C 55.773 0.232 1 241 56 56 GLU CB C 29.124 0.649 1 242 56 56 GLU N N 120.820 0.067 1 243 57 57 ILE H H 8.492 0.001 1 244 57 57 ILE C C 176.262 0.048 1 245 57 57 ILE CA C 60.909 0.015 1 246 57 57 ILE CB C 37.759 0.093 1 247 57 57 ILE N N 123.559 0.045 1 248 58 58 LYS H H 8.687 0.003 1 249 58 58 LYS C C 176.436 0.028 1 250 58 58 LYS CA C 55.976 0.018 1 251 58 58 LYS CB C 32.169 0.077 1 252 58 58 LYS N N 126.633 0.079 1 253 59 59 ARG H H 8.677 0.002 1 254 59 59 ARG C C 176.248 0.018 1 255 59 59 ARG CA C 55.724 0.054 1 256 59 59 ARG CB C 30.104 0.009 1 257 59 59 ARG N N 123.359 0.067 1 258 60 60 HIS H H 8.633 0.001 1 259 60 60 HIS C C 175.678 0.003 1 260 60 60 HIS CA C 56.110 0.007 1 261 60 60 HIS CB C 30.968 0.050 1 262 60 60 HIS N N 122.019 0.034 1 263 61 61 LYS H H 8.664 0.003 1 264 61 61 LYS C C 176.594 0.030 1 265 61 61 LYS CA C 55.990 0.070 1 266 61 61 LYS CB C 32.547 0.049 1 267 61 61 LYS N N 123.517 0.049 1 268 62 62 THR H H 8.475 0.002 1 269 62 62 THR C C 174.310 0.007 1 270 62 62 THR CA C 61.626 0.200 1 271 62 62 THR CB C 69.751 0.009 1 272 62 62 THR N N 115.978 0.087 1 273 63 63 PHE H H 8.616 0.002 1 274 63 63 PHE C C 175.519 0.037 1 275 63 63 PHE CA C 57.849 0.200 1 276 63 63 PHE CB C 38.859 0.242 1 277 63 63 PHE N N 122.520 0.022 1 278 64 64 GLU H H 8.580 0.001 1 279 64 64 GLU C C 175.746 0.007 1 280 64 64 GLU CA C 55.918 0.069 1 281 64 64 GLU CB C 29.803 0.025 1 282 64 64 GLU N N 123.314 0.035 1 283 65 65 ALA H H 8.414 0.001 1 284 65 65 ALA C C 177.439 0.012 1 285 65 65 ALA CA C 52.302 0.030 1 286 65 65 ALA CB C 18.572 0.011 1 287 65 65 ALA N N 125.218 0.034 1 288 66 66 PHE H H 8.443 0.001 1 289 66 66 PHE C C 175.700 0.005 1 290 66 66 PHE CA C 57.338 0.012 1 291 66 66 PHE CB C 38.781 0.029 1 292 66 66 PHE N N 119.824 0.024 1 293 67 67 LEU H H 8.430 0.002 1 294 67 67 LEU C C 177.248 0.026 1 295 67 67 LEU CA C 54.501 0.092 1 296 67 67 LEU CB C 41.570 0.089 1 297 67 67 LEU N N 124.457 0.102 1 298 68 68 GLU H H 8.647 0.004 1 299 68 68 GLU C C 176.771 0.200 1 300 68 68 GLU CA C 56.254 0.002 1 301 68 68 GLU CB C 29.683 0.017 1 302 68 68 GLU N N 122.559 0.048 1 303 69 69 SER H H 8.532 0.011 1 304 69 69 SER C C 174.750 0.070 1 305 69 69 SER CA C 58.371 0.020 1 306 69 69 SER CB C 63.336 0.200 1 307 69 69 SER N N 116.608 0.117 1 308 70 70 GLU H H 8.623 0.002 1 309 70 70 GLU C C 176.549 0.039 1 310 70 70 GLU CA C 56.243 0.277 1 311 70 70 GLU CB C 29.994 0.035 1 312 70 70 GLU N N 122.785 0.026 1 313 71 71 LYS H H 8.562 0.002 1 314 71 71 LYS C C 176.260 0.200 1 315 71 71 LYS N N 123.073 0.070 1 316 72 72 PRO C C 176.915 0.200 1 317 72 72 PRO CA C 62.284 0.200 1 318 72 72 PRO CB C 32.148 0.200 1 319 73 73 LYS H H 8.726 0.003 1 320 73 73 LYS C C 176.771 0.014 1 321 73 73 LYS CA C 56.212 0.126 1 322 73 73 LYS CB C 29.243 0.064 1 323 73 73 LYS N N 122.622 0.038 1 324 74 74 ARG H H 8.694 0.002 1 325 74 74 ARG C C 175.976 0.003 1 326 74 74 ARG CA C 55.718 0.175 1 327 74 74 ARG CB C 30.125 0.048 1 328 74 74 ARG N N 123.109 0.016 1 329 75 75 LEU H H 8.592 0.007 1 330 75 75 LEU C C 176.983 0.009 1 331 75 75 LEU CA C 54.676 0.041 1 332 75 75 LEU CB C 41.629 0.068 1 333 75 75 LEU N N 124.574 0.065 1 334 76 76 PHE H H 8.609 0.002 1 335 76 76 PHE C C 175.457 0.013 1 336 76 76 PHE CA C 57.217 0.030 1 337 76 76 PHE CB C 39.105 0.100 1 338 76 76 PHE N N 121.414 0.027 1 339 77 77 ALA H H 8.599 0.002 1 340 77 77 ALA C C 177.410 0.007 1 341 77 77 ALA CA C 51.920 0.065 1 342 77 77 ALA CB C 18.708 0.107 1 343 77 77 ALA N N 125.438 0.024 1 344 78 78 LEU H H 8.538 0.003 1 345 78 78 LEU C C 177.775 0.019 1 346 78 78 LEU CA C 54.687 0.063 1 347 78 78 LEU CB C 41.580 0.045 1 348 78 78 LEU N N 122.189 0.027 1 349 79 79 THR H H 8.496 0.007 1 350 79 79 THR C C 174.868 0.006 1 351 79 79 THR CA C 61.197 0.016 1 352 79 79 THR CB C 69.700 0.017 1 353 79 79 THR N N 115.001 0.016 1 354 80 80 THR H H 8.484 0.002 1 355 80 80 THR C C 174.694 0.007 1 356 80 80 THR CA C 61.498 0.065 1 357 80 80 THR CB C 69.516 0.032 1 358 80 80 THR N N 116.404 0.090 1 359 81 81 LYS H H 8.606 0.002 1 360 81 81 LYS C C 177.074 0.200 1 361 81 81 LYS CA C 56.164 0.200 1 362 81 81 LYS CB C 32.423 0.200 1 363 81 81 LYS N N 123.741 0.020 1 364 82 82 GLY H H 8.610 0.000 1 365 82 82 GLY C C 173.583 0.200 1 366 82 82 GLY CA C 44.707 0.200 1 367 82 82 GLY N N 110.010 0.017 1 368 83 83 CYS H H 8.306 0.001 1 369 83 83 CYS C C 174.772 0.200 1 370 83 83 CYS CA C 58.538 0.200 1 371 83 83 CYS CB C 38.116 0.200 1 372 83 83 CYS N N 121.650 0.024 1 373 84 84 PRO C C 176.751 0.200 1 374 84 84 PRO CA C 62.905 0.197 1 375 84 84 PRO CB C 31.822 0.112 1 376 85 85 ALA H H 8.713 0.002 1 377 85 85 ALA C C 177.883 0.001 1 378 85 85 ALA CA C 52.541 0.054 1 379 85 85 ALA CB C 18.503 0.132 1 380 85 85 ALA N N 124.463 0.071 1 381 86 86 HIS H H 8.342 0.002 1 382 86 86 HIS C C 175.901 0.025 1 383 86 86 HIS CA C 56.579 0.037 1 384 86 86 HIS CB C 30.727 0.090 1 385 86 86 HIS N N 118.495 0.021 1 386 87 87 SER H H 8.396 0.033 1 387 87 87 SER C C 174.610 0.006 1 388 87 87 SER CA C 58.135 0.200 1 389 87 87 SER CB C 63.195 0.200 1 390 87 87 SER N N 116.554 0.124 1 391 88 88 GLN H H 8.554 0.004 1 392 88 88 GLN C C 176.400 0.056 1 393 88 88 GLN CA C 56.157 0.082 1 394 88 88 GLN CB C 29.815 0.032 1 395 88 88 GLN N N 122.737 0.084 1 396 89 89 VAL H H 8.547 0.002 1 397 89 89 VAL C C 175.528 0.392 1 398 89 89 VAL CA C 62.075 0.057 1 399 89 89 VAL CB C 31.782 0.047 1 400 89 89 VAL N N 123.976 0.059 1 401 90 90 LYS H H 8.575 0.003 1 402 90 90 LYS C C 176.207 0.012 1 403 90 90 LYS CA C 55.829 0.139 1 404 90 90 LYS CB C 32.444 0.133 1 405 90 90 LYS N N 125.698 0.037 1 406 91 91 PHE H H 8.535 0.006 1 407 91 91 PHE C C 175.534 0.200 1 408 91 91 PHE CA C 57.240 0.014 1 409 91 91 PHE CB C 39.197 0.037 1 410 91 91 PHE N N 122.251 0.059 1 411 92 92 LYS H H 8.696 0.002 1 412 92 92 LYS C C 176.209 0.009 1 413 92 92 LYS CA C 55.606 0.024 1 414 92 92 LYS CB C 32.607 0.032 1 415 92 92 LYS N N 124.248 0.026 1 416 93 93 LEU H H 8.614 0.002 1 417 93 93 LEU C C 177.922 0.002 1 418 93 93 LEU CA C 55.146 0.028 1 419 93 93 LEU CB C 41.542 0.014 1 420 93 93 LEU N N 124.606 0.017 1 421 94 94 GLY H H 8.657 0.021 1 422 94 94 GLY C C 173.791 0.013 1 423 94 94 GLY CA C 44.858 0.046 1 424 94 94 GLY N N 109.825 0.100 1 425 95 95 ASP H H 8.375 0.001 1 426 95 95 ASP C C 176.133 0.008 1 427 95 95 ASP CA C 54.411 0.008 1 428 95 95 ASP CB C 40.757 0.050 1 429 95 95 ASP N N 120.765 0.018 1 430 96 96 TYR H H 8.310 0.003 1 431 96 96 TYR C C 175.661 0.029 1 432 96 96 TYR CA C 57.834 0.004 1 433 96 96 TYR CB C 38.120 0.060 1 434 96 96 TYR N N 120.401 0.076 1 435 97 97 LEU H H 8.393 0.001 1 436 97 97 LEU C C 176.868 0.001 1 437 97 97 LEU CA C 54.548 0.086 1 438 97 97 LEU CB C 41.398 0.029 1 439 97 97 LEU N N 123.908 0.028 1 440 98 98 MET H H 8.425 0.002 1 441 98 98 MET C C 175.851 0.006 1 442 98 98 MET CA C 55.103 0.052 1 443 98 98 MET CB C 32.385 0.044 1 444 98 98 MET N N 121.209 0.031 1 445 99 99 PHE H H 8.510 0.002 1 446 99 99 PHE C C 176.072 0.009 1 447 99 99 PHE CA C 57.167 0.041 1 448 99 99 PHE CB C 39.263 0.012 1 449 99 99 PHE N N 120.508 0.039 1 450 100 100 GLY H H 8.525 0.001 1 451 100 100 GLY C C 171.835 0.200 1 452 100 100 GLY CA C 44.345 0.200 1 453 100 100 GLY N N 109.932 0.022 1 454 101 101 PRO C C 177.231 0.200 1 455 101 101 PRO CA C 63.070 0.144 1 456 101 101 PRO CB C 31.629 0.127 1 457 102 102 GLU H H 8.951 0.001 1 458 102 102 GLU C C 176.995 0.022 1 459 102 102 GLU CA C 56.483 0.177 1 460 102 102 GLU CB C 29.350 0.064 1 461 102 102 GLU N N 120.783 0.021 1 462 103 103 THR H H 8.388 0.001 1 463 103 103 THR C C 174.677 0.016 1 464 103 103 THR CA C 61.718 0.170 1 465 103 103 THR CB C 69.511 0.092 1 466 103 103 THR N N 115.640 0.051 1 467 104 104 ARG H H 8.635 0.003 1 468 104 104 ARG C C 176.749 0.032 1 469 104 104 ARG CA C 55.983 0.047 1 470 104 104 ARG CB C 30.267 0.047 1 471 104 104 ARG N N 123.665 0.043 1 472 105 105 GLY H H 8.607 0.002 1 473 105 105 GLY C C 173.700 0.131 1 474 105 105 GLY CA C 44.861 0.115 1 475 105 105 GLY N N 110.031 0.064 1 476 106 106 ILE H H 8.275 0.005 1 477 106 106 ILE C C 176.043 0.200 1 478 106 106 ILE CA C 57.500 0.200 1 479 106 106 ILE CB C 39.068 0.200 1 480 106 106 ILE N N 120.327 0.044 1 481 107 107 PRO C C 176.874 0.200 1 482 107 107 PRO CA C 62.693 0.056 1 483 107 107 PRO CB C 31.399 0.066 1 484 108 108 MET H H 8.753 0.004 1 485 108 108 MET C C 176.601 0.022 1 486 108 108 MET CA C 55.592 0.098 1 487 108 108 MET CB C 32.427 0.027 1 488 108 108 MET N N 121.599 0.016 1 489 109 109 SER H H 8.648 0.002 1 490 109 109 SER C C 174.611 0.004 1 491 109 109 SER CA C 58.072 0.087 1 492 109 109 SER CB C 63.212 0.030 1 493 109 109 SER N N 117.360 0.031 1 494 110 110 ILE H H 8.438 0.003 1 495 110 110 ILE C C 176.327 0.012 1 496 110 110 ILE CA C 60.894 0.125 1 497 110 110 ILE CB C 37.854 0.052 1 498 110 110 ILE N N 123.201 0.011 1 499 111 111 LEU H H 8.474 0.002 1 500 111 111 LEU C C 177.150 0.010 1 501 111 111 LEU CA C 54.871 0.163 1 502 111 111 LEU CB C 41.369 0.028 1 503 111 111 LEU N N 125.721 0.042 1 504 112 112 ASN H H 8.683 0.001 1 505 112 112 ASN C C 175.103 0.001 1 506 112 112 ASN CA C 52.852 0.071 1 507 112 112 ASN CB C 38.441 0.033 1 508 112 112 ASN N N 119.815 0.018 1 509 113 113 GLU H H 8.500 0.002 1 510 113 113 GLU C C 176.296 0.002 1 511 113 113 GLU CA C 56.115 0.068 1 512 113 113 GLU CB C 29.976 0.041 1 513 113 113 GLU N N 121.141 0.044 1 514 114 114 MET H H 8.682 0.001 1 515 114 114 MET C C 174.265 0.200 1 516 114 114 MET CA C 53.237 0.200 1 517 114 114 MET CB C 31.890 0.200 1 518 114 114 MET N N 122.810 0.016 1 519 115 115 PRO C C 176.956 0.200 1 520 115 115 PRO CA C 62.808 0.200 1 521 115 115 PRO CB C 31.470 0.200 1 522 116 116 MET H H 8.768 0.001 1 523 116 116 MET C C 176.539 0.200 1 524 116 116 MET CA C 55.597 0.200 1 525 116 116 MET CB C 32.378 0.029 1 526 116 116 MET N N 121.622 0.013 1 527 117 117 GLU H H 8.785 0.001 1 528 117 117 GLU C C 176.427 0.044 1 529 117 117 GLU CA C 56.096 0.037 1 530 117 117 GLU CB C 29.763 0.035 1 531 117 117 GLU N N 122.646 0.026 1 532 118 118 GLN H H 8.707 0.002 1 533 118 118 GLN C C 175.993 0.001 1 534 118 118 GLN CA C 55.293 0.125 1 535 118 118 GLN CB C 29.020 0.038 1 536 118 118 GLN N N 122.324 0.034 1 537 119 119 LYS H H 8.638 0.002 1 538 119 119 LYS C C 176.627 0.031 1 539 119 119 LYS CA C 56.145 0.049 1 540 119 119 LYS CB C 32.236 0.051 1 541 119 119 LYS N N 123.645 0.042 1 542 120 120 ILE H H 8.533 0.001 1 543 120 120 ILE C C 176.147 0.200 1 544 120 120 ILE CA C 60.657 0.032 1 545 120 120 ILE CB C 37.991 0.200 1 546 120 120 ILE N N 123.027 0.027 1 547 121 121 ARG H H 8.730 0.009 1 548 121 121 ARG C C 176.044 0.200 1 549 121 121 ARG CA C 55.331 0.200 1 550 121 121 ARG CB C 29.983 0.015 1 551 121 121 ARG N N 126.590 0.076 1 552 122 122 ILE H H 8.620 0.001 1 553 122 122 ILE C C 174.636 0.200 1 554 122 122 ILE CA C 58.309 0.200 1 555 122 122 ILE CB C 37.675 0.200 1 556 122 122 ILE N N 125.026 0.025 1 557 124 124 MET H H 8.768 0.003 1 558 124 124 MET C C 176.620 0.048 1 559 124 124 MET CA C 55.600 0.018 1 560 124 124 MET CB C 32.387 0.107 1 561 124 124 MET N N 121.618 0.016 1 562 125 125 THR H H 8.402 0.001 1 563 125 125 THR C C 174.485 0.002 1 564 125 125 THR CA C 61.350 0.031 1 565 125 125 THR CB C 69.728 0.008 1 566 125 125 THR N N 115.183 0.025 1 567 126 126 ALA H H 8.612 0.002 1 568 126 126 ALA C C 177.570 0.200 1 569 126 126 ALA CA C 52.530 0.042 1 570 126 126 ALA CB C 18.616 0.071 1 571 126 126 ALA N N 126.073 0.016 1 572 127 127 ASN H H 8.643 0.001 1 573 127 127 ASN C C 175.570 0.009 1 574 127 127 ASN CA C 52.966 0.114 1 575 127 127 ASN CB C 38.373 0.057 1 576 127 127 ASN N N 118.079 0.015 1 577 128 128 SER H H 8.493 0.049 1 578 128 128 SER C C 174.729 0.010 1 579 128 128 SER CA C 58.349 0.214 1 580 128 128 SER CB C 63.257 0.023 1 581 128 128 SER N N 116.596 0.047 1 582 129 129 ARG H H 8.601 0.035 1 583 129 129 ARG C C 176.560 0.022 1 584 129 129 ARG CA C 56.174 0.040 1 585 129 129 ARG CB C 29.803 0.135 1 586 129 129 ARG N N 122.723 0.095 1 587 130 130 SER H H 8.548 0.008 1 588 130 130 SER C C 174.779 0.012 1 589 130 130 SER CA C 58.288 0.032 1 590 130 130 SER CB C 63.212 0.018 1 591 130 130 SER N N 116.738 0.126 1 592 131 131 MET H H 8.642 0.002 1 593 131 131 MET C C 175.905 0.004 1 594 131 131 MET CA C 55.150 0.042 1 595 131 131 MET CB C 32.203 0.041 1 596 131 131 MET N N 122.428 0.113 1 597 132 132 ASN H H 8.711 0.001 1 598 132 132 ASN C C 175.358 0.013 1 599 132 132 ASN CA C 53.081 0.060 1 600 132 132 ASN CB C 38.214 0.033 1 601 132 132 ASN N N 120.074 0.027 1 602 133 133 LEU H H 8.564 0.001 1 603 133 133 LEU C C 177.675 0.200 1 604 133 133 LEU CA C 54.824 0.090 1 605 133 133 LEU CB C 41.388 0.061 1 606 133 133 LEU N N 123.298 0.028 1 607 134 134 SER H H 8.578 0.001 1 608 134 134 SER C C 174.599 0.011 1 609 134 134 SER CA C 58.369 0.019 1 610 134 134 SER CB C 63.222 0.044 1 611 134 134 SER N N 116.234 0.027 1 612 135 135 ASN H H 8.664 0.002 1 613 135 135 ASN C C 175.322 0.017 1 614 135 135 ASN CA C 53.025 0.092 1 615 135 135 ASN CB C 38.399 0.090 1 616 135 135 ASN N N 120.828 0.028 1 617 136 136 SER H H 8.443 0.002 1 618 136 136 SER C C 174.486 0.001 1 619 136 136 SER CA C 58.150 0.142 1 620 136 136 SER CB C 63.280 0.044 1 621 136 136 SER N N 116.049 0.016 1 622 137 137 VAL H H 8.336 0.002 1 623 137 137 VAL C C 175.863 0.005 1 624 137 137 VAL CA C 61.713 0.132 1 625 137 137 VAL CB C 32.120 0.016 1 626 137 137 VAL N N 121.699 0.081 1 627 138 138 ALA H H 8.530 0.001 1 628 138 138 ALA C C 177.639 0.005 1 629 138 138 ALA CA C 52.139 0.108 1 630 138 138 ALA CB C 18.569 0.081 1 631 138 138 ALA N N 127.814 0.024 1 632 139 139 VAL H H 8.378 0.001 1 633 139 139 VAL C C 176.440 0.015 1 634 139 139 VAL CA C 61.780 0.039 1 635 139 139 VAL CB C 32.203 0.025 1 636 139 139 VAL N N 120.169 0.029 1 637 140 140 THR H H 8.487 0.001 1 638 140 140 THR C C 174.265 0.005 1 639 140 140 THR CA C 61.764 0.118 1 640 140 140 THR CB C 69.545 0.088 1 641 140 140 THR N N 119.218 0.032 1 642 141 141 VAL H H 8.434 0.002 1 643 141 141 VAL C C 175.769 0.017 1 644 141 141 VAL CA C 61.668 0.033 1 645 141 141 VAL CB C 32.178 0.009 1 646 141 141 VAL N N 123.431 0.024 1 647 142 142 TYR H H 8.549 0.002 1 648 142 142 TYR C C 175.815 0.009 1 649 142 142 TYR CA C 57.708 0.200 1 650 142 142 TYR CB C 38.477 0.230 1 651 142 142 TYR N N 124.976 0.152 1 652 143 143 GLU H H 8.593 0.001 1 653 143 143 GLU C C 176.306 0.006 1 654 143 143 GLU CA C 55.594 0.056 1 655 143 143 GLU CB C 29.554 0.103 1 656 143 143 GLU N N 123.726 0.031 1 657 144 144 ALA H H 8.492 0.001 1 658 144 144 ALA C C 177.934 0.004 1 659 144 144 ALA CA C 53.273 0.053 1 660 144 144 ALA CB C 18.154 0.059 1 661 144 144 ALA N N 125.507 0.026 1 662 145 145 TRP H H 8.006 0.001 1 663 145 145 TRP C C 176.560 0.002 1 664 145 145 TRP CA C 56.878 0.017 1 665 145 145 TRP CB C 28.255 0.044 1 666 145 145 TRP N N 117.915 0.014 1 667 146 146 ARG H H 7.808 0.001 1 668 146 146 ARG C C 176.123 0.200 1 669 146 146 ARG CA C 56.040 0.011 1 670 146 146 ARG CB C 29.924 0.006 1 671 146 146 ARG N N 122.329 0.021 1 672 147 147 GLN H H 8.290 0.002 1 673 147 147 GLN C C 176.286 0.026 1 674 147 147 GLN CA C 55.659 0.253 1 675 147 147 GLN CB C 29.178 0.625 1 676 147 147 GLN N N 120.794 0.013 1 677 148 148 LEU H H 8.493 0.001 1 678 148 148 LEU C C 177.996 0.019 1 679 148 148 LEU CA C 55.192 0.113 1 680 148 148 LEU CB C 41.433 0.200 1 681 148 148 LEU N N 123.629 0.040 1 682 149 149 GLY H H 8.594 0.001 1 683 149 149 GLY C C 173.820 0.035 1 684 149 149 GLY CA C 44.854 0.018 1 685 149 149 GLY N N 109.497 0.034 1 686 150 150 TYR H H 8.269 0.002 1 687 150 150 TYR C C 176.007 0.001 1 688 150 150 TYR CA C 57.750 0.208 1 689 150 150 TYR CB C 38.369 0.110 1 690 150 150 TYR N N 120.794 0.022 1 691 151 151 LYS H H 8.593 0.002 1 692 151 151 LYS C C 176.488 0.002 1 693 151 151 LYS CA C 56.095 0.020 1 694 151 151 LYS CB C 32.339 0.048 1 695 151 151 LYS N N 125.123 0.025 1 696 152 152 GLY H H 7.829 0.001 1 697 152 152 GLY C C 173.348 0.006 1 698 152 152 GLY CA C 44.647 0.001 1 699 152 152 GLY N N 109.277 0.015 1 700 153 153 ALA H H 8.365 0.000 1 701 153 153 ALA C C 177.834 0.005 1 702 153 153 ALA CA C 52.189 0.053 1 703 153 153 ALA CB C 18.885 0.133 1 704 153 153 ALA N N 123.556 0.014 1 705 154 154 VAL H H 8.385 0.001 1 706 154 154 VAL C C 175.772 0.009 1 707 154 154 VAL CA C 61.775 0.001 1 708 154 154 VAL CB C 32.249 0.098 1 709 154 154 VAL N N 119.270 0.013 1 710 155 155 ASN H H 8.719 0.002 1 711 155 155 ASN C C 174.797 0.007 1 712 155 155 ASN CA C 52.723 0.129 1 713 155 155 ASN CB C 38.447 0.051 1 714 155 155 ASN N N 122.625 0.028 1 715 156 156 LEU H H 8.542 0.002 1 716 156 156 LEU C C 174.639 0.200 1 717 156 156 LEU CA C 54.420 0.200 1 718 156 156 LEU N N 123.987 0.064 1 719 157 157 PRO C C 176.651 0.200 1 720 157 157 PRO CA C 62.735 0.200 1 721 157 157 PRO CB C 31.312 0.200 1 722 158 158 GLU H H 8.714 0.001 1 723 158 158 GLU C C 176.483 0.200 1 724 158 158 GLU CA C 56.246 0.030 1 725 158 158 GLU CB C 29.970 0.086 1 726 158 158 GLU N N 121.688 0.050 1 727 159 159 VAL H H 8.527 0.001 1 728 159 159 VAL C C 175.391 0.200 1 729 159 159 VAL CA C 62.130 0.079 1 730 159 159 VAL CB C 31.979 0.064 1 731 159 159 VAL N N 123.257 0.040 1 732 160 160 LYS H H 8.309 0.001 1 733 160 160 LYS C C 181.530 0.200 1 734 160 160 LYS CA C 57.694 0.200 1 735 160 160 LYS CB C 33.077 0.200 1 736 160 160 LYS N N 131.057 0.022 1 stop_ save_