data_19134 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignments of 8M urea-denatured YbeA from Escherichia coli ; _BMRB_accession_number 19134 _BMRB_flat_file_name bmr19134.str _Entry_type original _Submission_date 2013-04-02 _Accession_date 2013-04-02 _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" 135 "13C chemical shifts" 422 "15N chemical shifts" 135 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-09-26 original author . stop_ _Original_release_date 2014-09-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone NMR assignments of a topologically knotted protein in urea-denatured state.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23821130 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hsieh 'Shu-Ju Micky' J. . 2 Mallam Anna L. . 3 Jackson Sophie E. . 4 Hsu 'Shang-Te Danny' T. . stop_ _Journal_abbreviation 'Biomol. NMR Assign.' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 8 _Journal_issue 2 _Journal_ISSN 1874-270X _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 283 _Page_last 285 _Year 2014 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_entry_citation_2 _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 ? 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 YbeA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label YbeA $YbeA 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_YbeA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common YbeA _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 155 _Mol_residue_sequence ; MKLQLVAVGTKMPDWVQTGF TEYLRRFPKDMPFELIEIPA GKRGKNADIKRILDKEGEQM LAAAGKNRIVTLDIPGKPWD TPQLAAELERWKLDGRDVSL LIGGPEGLSPACKAAAEQSW SLSALTLPHPLVRVLVAESL YRAWSITTNHPYHRE ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 LEU 4 GLN 5 LEU 6 VAL 7 ALA 8 VAL 9 GLY 10 THR 11 LYS 12 MET 13 PRO 14 ASP 15 TRP 16 VAL 17 GLN 18 THR 19 GLY 20 PHE 21 THR 22 GLU 23 TYR 24 LEU 25 ARG 26 ARG 27 PHE 28 PRO 29 LYS 30 ASP 31 MET 32 PRO 33 PHE 34 GLU 35 LEU 36 ILE 37 GLU 38 ILE 39 PRO 40 ALA 41 GLY 42 LYS 43 ARG 44 GLY 45 LYS 46 ASN 47 ALA 48 ASP 49 ILE 50 LYS 51 ARG 52 ILE 53 LEU 54 ASP 55 LYS 56 GLU 57 GLY 58 GLU 59 GLN 60 MET 61 LEU 62 ALA 63 ALA 64 ALA 65 GLY 66 LYS 67 ASN 68 ARG 69 ILE 70 VAL 71 THR 72 LEU 73 ASP 74 ILE 75 PRO 76 GLY 77 LYS 78 PRO 79 TRP 80 ASP 81 THR 82 PRO 83 GLN 84 LEU 85 ALA 86 ALA 87 GLU 88 LEU 89 GLU 90 ARG 91 TRP 92 LYS 93 LEU 94 ASP 95 GLY 96 ARG 97 ASP 98 VAL 99 SER 100 LEU 101 LEU 102 ILE 103 GLY 104 GLY 105 PRO 106 GLU 107 GLY 108 LEU 109 SER 110 PRO 111 ALA 112 CYS 113 LYS 114 ALA 115 ALA 116 ALA 117 GLU 118 GLN 119 SER 120 TRP 121 SER 122 LEU 123 SER 124 ALA 125 LEU 126 THR 127 LEU 128 PRO 129 HIS 130 PRO 131 LEU 132 VAL 133 ARG 134 VAL 135 LEU 136 VAL 137 ALA 138 GLU 139 SER 140 LEU 141 TYR 142 ARG 143 ALA 144 TRP 145 SER 146 ILE 147 THR 148 THR 149 ASN 150 HIS 151 PRO 152 TYR 153 HIS 154 ARG 155 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-14 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 PDB 1NS5 "X-Ray Structure Of Ybea From E.Coli. Northeast Structural Genomics Research Consortium (Nesg) Target Er45" 99.35 155 98.05 98.05 3.16e-104 DBJ BAA35283 "conserved hypothetical protein [Escherichia coli str. K12 substr. W3110]" 100.00 155 100.00 100.00 3.80e-108 DBJ BAB34097 "hypothetical protein [Escherichia coli O157:H7 str. Sakai]" 100.00 155 100.00 100.00 3.80e-108 DBJ BAG76228 "conserved hypothetical protein [Escherichia coli SE11]" 100.00 155 100.00 100.00 3.80e-108 DBJ BAI24039 "conserved predicted protein [Escherichia coli O26:H11 str. 11368]" 100.00 155 100.00 100.00 3.80e-108 DBJ BAI29506 "conserved predicted protein [Escherichia coli O103:H2 str. 12009]" 100.00 155 99.35 99.35 1.51e-107 EMBL CAA28200 "unnamed protein product [Escherichia coli K-12]" 100.00 155 100.00 100.00 3.80e-108 EMBL CAD05118 "conserved hypothetical protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 155 98.71 98.71 1.76e-106 EMBL CAP75135 "UPF0247 protein ybeA [Escherichia coli LF82]" 100.00 155 100.00 100.00 3.80e-108 EMBL CAQ31111 "23S rRNA m[3]Psi1915 methyltransferase [Escherichia coli BL21(DE3)]" 100.00 155 100.00 100.00 3.80e-108 EMBL CAQ89966 "conserved hypothetical protein [Escherichia fergusonii ATCC 35469]" 100.00 155 97.42 99.35 9.08e-106 GB AAB40836 "hypothetical protein [Escherichia coli]" 100.00 155 100.00 100.00 3.80e-108 GB AAC73737 "23S rRNA m(3)Psi1915 pseudouridine methyltransferase, SAM-dependent [Escherichia coli str. K-12 substr. MG1655]" 100.00 155 100.00 100.00 3.80e-108 GB AAG54970 "orf, hypothetical protein [Escherichia coli O157:H7 str. EDL933]" 100.00 155 100.00 100.00 3.80e-108 GB AAL19592 "putative cytoplasmic protein [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 155 98.71 98.71 1.76e-106 GB AAN42281 "conserved hypothetical protein [Shigella flexneri 2a str. 301]" 100.00 155 100.00 100.00 3.80e-108 PIR AD0581 "conserved hypothetical protein STY0692 [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 155 98.71 98.71 1.76e-106 REF NP_308701 "rRNA large subunit methyltransferase [Escherichia coli O157:H7 str. Sakai]" 100.00 155 100.00 100.00 3.80e-108 REF NP_415169 "23S rRNA m(3)Psi1915 pseudouridine methyltransferase, SAM-dependent [Escherichia coli str. K-12 substr. MG1655]" 100.00 155 100.00 100.00 3.80e-108 REF NP_455217 "rRNA large subunit m3Psi methyltransferase RlmH [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 155 98.71 98.71 1.76e-106 REF NP_459633 "rRNA large subunit methyltransferase H [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 155 98.71 98.71 1.76e-106 REF NP_706574 "rRNA large subunit methyltransferase [Shigella flexneri 2a str. 301]" 100.00 155 100.00 100.00 3.80e-108 SP A1A8R1 "RecName: Full=Ribosomal RNA large subunit methyltransferase H; AltName: Full=23S rRNA (pseudouridine1915-N3)-methyltransferase;" 100.00 155 100.00 100.00 3.80e-108 SP A4W822 "RecName: Full=Ribosomal RNA large subunit methyltransferase H; AltName: Full=23S rRNA (pseudouridine1915-N3)-methyltransferase;" 100.00 155 97.42 98.06 3.92e-105 SP A7ZJ25 "RecName: Full=Ribosomal RNA large subunit methyltransferase H; AltName: Full=23S rRNA (pseudouridine1915-N3)-methyltransferase;" 100.00 155 100.00 100.00 3.80e-108 SP A7ZXR2 "RecName: Full=Ribosomal RNA large subunit methyltransferase H; AltName: Full=23S rRNA (pseudouridine1915-N3)-methyltransferase;" 100.00 155 100.00 100.00 3.80e-108 SP A8AJG7 "RecName: Full=Ribosomal RNA large subunit methyltransferase H; AltName: Full=23S rRNA (pseudouridine1915-N3)-methyltransferase;" 100.00 155 99.35 99.35 1.51e-107 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $YbeA 'E. coli' 562 Bacteria . Escherichia coli 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 $YbeA 'recombinant technology' . Escherichia coli . 'Pet 17b' 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 $YbeA 350 uM '[U-13C; U-15N]' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' TRIS 50 mM 'natural abundance' 'potassium chloride' 200 mM 'natural abundance' glycerol 10 % 'natural abundance' urea 7.2 M 'natural abundance' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HCACO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCACO' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _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 175.900 internal indirect . . . 0.251449530 water H 1 protons ppm 4.964 internal direct . . . 1.000000000 water N 15 protons ppm 118.472 internal indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCO' '3D HNCACB' '3D HNCA' '3D HCACO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name YbeA _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 1 MET C C 177.514 0.006 1 2 1 1 MET CA C 54.886 0.000 1 3 2 2 LYS H H 8.455 0.002 1 4 2 2 LYS C C 176.014 0.004 1 5 2 2 LYS CA C 61.830 0.178 1 6 2 2 LYS CB C 32.120 0.096 1 7 2 2 LYS N N 122.250 0.037 1 8 3 3 LEU H H 8.686 0.004 1 9 3 3 LEU C C 176.073 0.000 1 10 3 3 LEU CA C 55.657 0.128 1 11 3 3 LEU CB C 30.120 0.054 1 12 3 3 LEU N N 126.050 0.052 1 13 4 4 GLN H H 8.565 0.001 1 14 4 4 GLN C C 175.963 0.010 1 15 4 4 GLN CA C 61.900 0.143 1 16 4 4 GLN CB C 32.057 0.075 1 17 4 4 GLN N N 123.333 0.037 1 18 5 5 LEU H H 8.654 0.005 1 19 5 5 LEU C C 177.134 0.006 1 20 5 5 LEU CA C 54.663 0.151 1 21 5 5 LEU CB C 41.453 0.050 1 22 5 5 LEU N N 127.228 0.022 1 23 6 6 VAL H H 8.524 0.002 1 24 6 6 VAL C C 175.911 0.048 1 25 6 6 VAL CA C 61.909 0.000 1 26 6 6 VAL CB C 32.144 0.000 1 27 6 6 VAL N N 122.404 0.025 1 28 7 7 ALA H H 8.633 0.002 1 29 7 7 ALA C C 177.691 0.007 1 30 7 7 ALA CA C 52.046 0.053 1 31 7 7 ALA CB C 18.600 0.104 1 32 7 7 ALA N N 128.188 0.068 1 33 8 8 VAL H H 8.428 0.001 1 34 8 8 VAL C C 176.828 0.005 1 35 8 8 VAL CA C 62.274 0.051 1 36 8 8 VAL CB C 32.193 0.029 1 37 8 8 VAL N N 120.550 0.094 1 38 9 9 GLY H H 8.680 0.001 1 39 9 9 GLY C C 174.251 0.005 1 40 9 9 GLY CA C 44.927 0.011 1 41 9 9 GLY N N 112.583 0.052 1 42 10 10 THR H H 8.254 0.002 1 43 10 10 THR C C 174.574 0.014 1 44 10 10 THR CA C 61.760 0.032 1 45 10 10 THR CB C 69.651 0.042 1 46 10 10 THR N N 114.315 0.023 1 47 11 11 LYS H H 8.639 0.001 1 48 11 11 LYS C C 176.555 0.008 1 49 11 11 LYS CA C 56.098 0.119 1 50 11 11 LYS CB C 32.468 0.073 1 51 11 11 LYS N N 124.524 0.021 1 52 12 12 MET H H 8.822 0.002 1 53 12 12 MET C C 174.397 0.000 1 54 12 12 MET CA C 53.252 0.000 1 55 12 12 MET CB C 32.084 0.000 1 56 12 12 MET N N 124.289 0.026 1 57 13 13 PRO C C 176.563 0.000 1 58 13 13 PRO CA C 62.683 0.119 1 59 13 13 PRO CB C 31.293 0.120 1 60 14 14 ASP H H 8.633 0.002 1 61 14 14 ASP C C 176.172 0.009 1 62 14 14 ASP CA C 54.657 0.084 1 63 14 14 ASP CB C 40.492 0.043 1 64 14 14 ASP N N 120.627 0.030 1 65 15 15 TRP H H 7.986 0.001 1 66 15 15 TRP C C 176.173 0.004 1 67 15 15 TRP CA C 56.829 0.131 1 68 15 15 TRP CB C 28.682 0.103 1 69 15 15 TRP N N 119.611 0.025 1 70 16 16 VAL H H 7.959 0.001 1 71 16 16 VAL C C 175.751 0.019 1 72 16 16 VAL CA C 62.070 0.120 1 73 16 16 VAL N N 122.799 0.018 1 74 17 17 GLN H H 8.553 0.002 1 75 17 17 GLN C C 176.226 0.003 1 76 17 17 GLN CA C 55.443 0.191 1 77 17 17 GLN CB C 28.796 0.015 1 78 17 17 GLN N N 124.445 0.104 1 79 18 18 THR H H 8.439 0.001 1 80 18 18 THR C C 175.153 0.012 1 81 18 18 THR CA C 61.816 0.051 1 82 18 18 THR CB C 69.617 0.072 1 83 18 18 THR N N 115.675 0.022 1 84 19 19 GLY H H 8.584 0.001 1 85 19 19 GLY C C 173.752 0.006 1 86 19 19 GLY CA C 45.016 0.094 1 87 19 19 GLY N N 110.738 0.023 1 88 20 20 PHE H H 8.391 0.007 1 89 20 20 PHE C C 175.974 0.006 1 90 20 20 PHE CA C 57.778 0.133 1 91 20 20 PHE CB C 39.266 0.005 1 92 20 20 PHE N N 120.517 0.077 1 93 21 21 THR H H 8.395 0.002 1 94 21 21 THR C C 174.069 0.014 1 95 21 21 THR CA C 61.753 0.000 1 96 21 21 THR CB C 69.584 0.065 1 97 21 21 THR N N 117.323 0.030 1 98 22 22 GLU H H 8.555 0.001 1 99 22 22 GLU C C 176.046 0.012 1 100 22 22 GLU CA C 56.202 0.038 1 101 22 22 GLU CB C 29.748 0.016 1 102 22 22 GLU N N 123.957 0.047 1 103 23 23 TYR H H 8.448 0.001 1 104 23 23 TYR C C 175.676 0.009 1 105 23 23 TYR CA C 57.806 0.023 1 106 23 23 TYR CB C 38.064 0.000 1 107 23 23 TYR N N 121.875 0.028 1 108 24 24 LEU H H 8.437 0.002 1 109 24 24 LEU C C 174.805 0.012 1 110 24 24 LEU N N 122.441 0.055 1 111 25 25 ARG H H 8.420 0.005 1 112 25 25 ARG C C 175.104 0.000 1 113 25 25 ARG N N 124.210 0.034 1 114 28 28 PRO C C 176.866 0.002 1 115 28 28 PRO CA C 63.085 0.000 1 116 28 28 PRO CB C 31.572 0.000 1 117 29 29 LYS H H 8.638 0.002 1 118 29 29 LYS C C 176.426 0.016 1 119 29 29 LYS CA C 56.362 0.133 1 120 29 29 LYS CB C 32.465 0.000 1 121 29 29 LYS N N 121.326 0.092 1 122 30 30 ASP H H 8.593 0.001 1 123 30 30 ASP C C 175.886 0.005 1 124 30 30 ASP CA C 54.022 0.313 1 125 30 30 ASP CB C 40.685 0.182 1 126 30 30 ASP N N 120.797 0.090 1 127 31 31 MET H H 8.447 0.003 1 128 31 31 MET C C 174.224 0.000 1 129 31 31 MET CA C 53.262 0.000 1 130 31 31 MET CB C 32.141 0.000 1 131 31 31 MET N N 121.367 0.052 1 132 32 32 PRO C C 176.633 0.005 1 133 32 32 PRO CA C 62.828 0.089 1 134 32 32 PRO CB C 31.285 0.103 1 135 33 33 PHE H H 8.482 0.001 1 136 33 33 PHE C C 175.745 0.012 1 137 33 33 PHE CA C 57.807 0.094 1 138 33 33 PHE CB C 38.931 0.068 1 139 33 33 PHE N N 120.933 0.024 1 140 34 34 GLU H H 8.629 0.002 1 141 34 34 GLU C C 175.721 0.023 1 142 34 34 GLU CA C 55.890 0.120 1 143 34 34 GLU CB C 30.044 0.054 1 144 34 34 GLU N N 122.528 0.043 1 145 35 35 LEU H H 8.472 0.002 1 146 35 35 LEU C C 176.957 0.015 1 147 35 35 LEU CA C 54.529 0.000 1 148 35 35 LEU CB C 41.465 0.050 1 149 35 35 LEU N N 124.080 0.041 1 150 36 36 ILE H H 8.488 0.002 1 151 36 36 ILE C C 176.073 0.003 1 152 36 36 ILE CA C 60.931 0.204 1 153 36 36 ILE CB C 37.975 0.000 1 154 36 36 ILE N N 123.456 0.093 1 155 37 37 GLU H H 8.675 0.003 1 156 37 37 GLU C C 176.211 0.187 1 157 37 37 GLU CA C 55.978 0.000 1 158 37 37 GLU CB C 29.560 0.000 1 159 37 37 GLU N N 125.885 0.056 1 160 38 38 ILE H H 8.602 0.001 1 161 38 38 ILE C C 174.694 0.000 1 162 38 38 ILE CA C 58.453 0.000 1 163 38 38 ILE CB C 37.920 0.000 1 164 38 38 ILE N N 124.700 0.016 1 165 39 39 PRO C C 176.663 0.003 1 166 39 39 PRO CA C 62.862 0.068 1 167 39 39 PRO CB C 31.452 0.036 1 168 40 40 ALA H H 8.667 0.001 1 169 40 40 ALA C C 178.493 0.006 1 170 40 40 ALA CA C 52.596 0.122 1 171 40 40 ALA CB C 18.644 0.120 1 172 40 40 ALA N N 124.756 0.022 1 173 41 41 GLY H H 8.566 0.001 1 174 41 41 GLY C C 174.115 0.016 1 175 41 41 GLY CA C 44.853 0.072 1 176 41 41 GLY N N 108.035 0.028 1 177 42 42 LYS H H 8.429 0.002 1 178 42 42 LYS C C 176.844 0.008 1 179 42 42 LYS CA C 55.948 0.000 1 180 42 42 LYS CB C 32.604 0.000 1 181 42 42 LYS N N 120.955 0.032 1 182 43 43 ARG H H 8.679 0.001 1 183 43 43 ARG C C 176.953 0.014 1 184 43 43 ARG CA C 55.971 0.106 1 185 43 43 ARG CB C 30.289 0.022 1 186 43 43 ARG N N 122.641 0.029 1 187 44 44 GLY H H 8.682 0.002 1 188 44 44 GLY C C 173.923 0.007 1 189 44 44 GLY CA C 44.743 0.033 1 190 44 44 GLY N N 110.474 0.030 1 191 45 45 LYS H H 8.533 0.002 1 192 45 45 LYS C C 176.742 0.005 1 193 45 45 LYS CA C 56.155 0.055 1 194 45 45 LYS CB C 32.533 0.042 1 195 45 45 LYS N N 121.138 0.019 1 196 46 46 ASN H H 8.823 0.002 1 197 46 46 ASN C C 175.195 0.009 1 198 46 46 ASN CA C 53.176 0.082 1 199 46 46 ASN CB C 38.394 0.044 1 200 46 46 ASN N N 120.304 0.068 1 201 47 47 ALA H H 8.522 0.002 1 202 47 47 ALA C C 177.306 0.006 1 203 47 47 ALA CA C 52.438 0.092 1 204 47 47 ALA CB C 18.748 0.140 1 205 47 47 ALA N N 124.348 0.029 1 206 48 48 ASP H H 8.543 0.001 1 207 48 48 ASP C C 176.215 0.013 1 208 48 48 ASP CA C 54.115 0.145 1 209 48 48 ASP CB C 40.572 0.027 1 210 48 48 ASP N N 119.940 0.028 1 211 49 49 ILE H H 8.218 0.002 1 212 49 49 ILE C C 176.244 0.004 1 213 49 49 ILE CA C 60.897 0.111 1 214 49 49 ILE CB C 37.957 0.020 1 215 49 49 ILE N N 121.365 0.021 1 216 50 50 LYS H H 8.649 0.007 1 217 50 50 LYS C C 176.460 0.021 1 218 50 50 LYS CA C 55.912 0.000 1 219 50 50 LYS CB C 32.244 0.033 1 220 50 50 LYS N N 126.163 0.022 1 221 51 51 ARG H H 8.671 0.002 1 222 51 51 ARG C C 176.184 0.008 1 223 51 51 ARG CA C 55.823 0.177 1 224 51 51 ARG CB C 30.233 0.047 1 225 51 51 ARG N N 123.768 0.029 1 226 52 52 ILE H H 8.648 0.002 1 227 52 52 ILE C C 176.241 0.008 1 228 52 52 ILE CA C 60.926 0.052 1 229 52 52 ILE CB C 37.728 0.000 1 230 52 52 ILE N N 123.995 0.031 1 231 53 53 LEU H H 8.679 0.002 1 232 53 53 LEU C C 177.101 0.013 1 233 53 53 LEU CA C 54.637 0.108 1 234 53 53 LEU CB C 41.428 0.000 1 235 53 53 LEU N N 127.206 0.037 1 236 54 54 ASP H H 8.626 0.002 1 237 54 54 ASP C C 176.436 0.049 1 238 54 54 ASP CA C 53.967 0.000 1 239 54 54 ASP CB C 40.882 0.100 1 240 54 54 ASP N N 121.825 0.038 1 241 55 55 LYS H H 8.598 0.010 1 242 55 55 LYS C C 176.952 0.007 1 243 55 55 LYS CA C 56.548 0.000 1 244 55 55 LYS CB C 32.247 0.000 1 245 55 55 LYS N N 121.695 0.065 1 246 56 56 GLU H H 8.691 0.002 1 247 56 56 GLU C C 177.310 0.006 1 248 56 56 GLU CA C 56.615 0.072 1 249 56 56 GLU CB C 29.527 0.010 1 250 56 56 GLU N N 121.649 0.026 1 251 57 57 GLY H H 8.554 0.002 1 252 57 57 GLY C C 174.253 0.003 1 253 57 57 GLY CA C 45.089 0.084 1 254 57 57 GLY N N 109.615 0.035 1 255 58 58 GLU H H 8.445 0.003 1 256 58 58 GLU C C 176.897 0.007 1 257 58 58 GLU CA C 56.428 0.179 1 258 58 58 GLU CB C 29.811 0.028 1 259 58 58 GLU N N 120.699 0.061 1 260 59 59 GLN H H 8.724 0.003 1 261 59 59 GLN C C 176.281 0.007 1 262 59 59 GLN CA C 55.866 0.193 1 263 59 59 GLN CB C 28.849 0.019 1 264 59 59 GLN N N 121.499 0.023 1 265 60 60 MET H H 8.686 0.002 1 266 60 60 MET C C 176.372 0.005 1 267 60 60 MET CA C 55.414 0.000 1 268 60 60 MET CB C 32.247 0.000 1 269 60 60 MET N N 122.282 0.071 1 270 61 61 LEU H H 8.558 0.001 1 271 61 61 LEU C C 177.330 0.021 1 272 61 61 LEU CA C 54.755 0.067 1 273 61 61 LEU CB C 41.545 0.072 1 274 61 61 LEU N N 124.080 0.080 1 275 62 62 ALA H H 8.576 0.001 1 276 62 62 ALA C C 177.720 0.029 1 277 62 62 ALA CA C 52.214 0.049 1 278 62 62 ALA CB C 18.619 0.108 1 279 62 62 ALA N N 125.163 0.028 1 280 63 63 ALA H H 8.472 0.002 5 281 63 63 ALA C C 177.638 0.005 5 282 63 63 ALA CA C 52.334 0.000 5 283 63 63 ALA CB C 18.509 0.000 5 284 63 63 ALA N N 123.505 0.022 5 285 64 64 ALA H H 8.454 0.004 1 286 64 64 ALA C C 178.318 0.004 1 287 64 64 ALA CA C 52.393 0.028 1 288 64 64 ALA CB C 18.770 0.144 1 289 64 64 ALA N N 123.287 0.069 1 290 65 65 GLY H H 8.498 0.001 1 291 65 65 GLY C C 174.197 0.007 1 292 65 65 GLY CA C 44.958 0.054 1 293 65 65 GLY N N 108.065 0.025 1 294 66 66 LYS H H 8.402 0.023 1 295 66 66 LYS C C 176.613 0.018 1 296 66 66 LYS CA C 56.176 0.101 1 297 66 66 LYS CB C 32.447 0.075 1 298 66 66 LYS N N 120.757 0.083 1 299 67 67 ASN H H 8.739 0.002 1 300 67 67 ASN C C 175.185 0.004 1 301 67 67 ASN CA C 53.198 0.140 1 302 67 67 ASN CB C 38.425 0.062 1 303 67 67 ASN N N 119.767 0.022 1 304 68 68 ARG H H 8.578 0.001 1 305 68 68 ARG C C 176.089 0.001 1 306 68 68 ARG CA C 55.805 0.072 1 307 68 68 ARG CB C 30.107 0.047 1 308 68 68 ARG N N 122.061 0.039 1 309 69 69 ILE H H 8.609 0.001 1 310 69 69 ILE C C 176.247 0.030 1 311 69 69 ILE CA C 60.820 0.077 1 312 69 69 ILE CB C 37.851 0.029 1 313 69 69 ILE N N 123.831 0.028 1 314 70 70 VAL H H 8.626 0.001 1 315 70 70 VAL C C 176.183 0.018 1 316 70 70 VAL CA C 61.706 0.063 1 317 70 70 VAL CB C 32.260 0.056 1 318 70 70 VAL N N 126.089 0.039 1 319 71 71 THR H H 8.539 0.001 1 320 71 71 THR C C 174.268 0.013 1 321 71 71 THR CA C 61.296 0.000 1 322 71 71 THR CB C 69.543 0.009 1 323 71 71 THR N N 119.605 0.037 1 324 72 72 LEU H H 8.598 0.001 1 325 72 72 LEU C C 176.877 0.010 1 326 72 72 LEU CA C 54.672 0.000 1 327 72 72 LEU CB C 41.866 0.000 1 328 72 72 LEU N N 125.051 0.021 1 329 73 73 ASP H H 8.664 0.001 1 330 73 73 ASP C C 175.733 0.014 1 331 73 73 ASP CA C 53.939 0.302 1 332 73 73 ASP CB C 40.626 0.083 1 333 73 73 ASP N N 121.988 0.027 1 334 74 74 ILE H H 8.351 0.001 1 335 74 74 ILE C C 174.599 0.000 1 336 74 74 ILE CA C 58.396 0.000 1 337 74 74 ILE CB C 38.223 0.000 1 338 74 74 ILE N N 122.354 0.019 1 339 75 75 PRO C C 177.391 0.001 1 340 75 75 PRO CA C 63.005 0.157 1 341 75 75 PRO CB C 31.544 0.085 1 342 76 76 GLY H H 8.596 0.001 1 343 76 76 GLY C C 173.642 0.004 1 344 76 76 GLY CA C 44.645 0.038 1 345 76 76 GLY N N 109.187 0.026 1 346 77 77 LYS H H 8.420 0.001 1 347 77 77 LYS C C 175.060 0.000 1 348 77 77 LYS CA C 53.675 0.003 1 349 77 77 LYS CB C 31.565 0.000 1 350 77 77 LYS N N 121.723 0.022 1 351 78 78 PRO C C 176.796 0.003 1 352 78 78 PRO CA C 63.065 0.207 1 353 78 78 PRO CB C 31.293 0.080 1 354 79 79 TRP H H 8.138 0.001 1 355 79 79 TRP C C 176.081 0.004 1 356 79 79 TRP CA C 56.875 0.173 1 357 79 79 TRP CB C 28.643 0.153 1 358 79 79 TRP N N 119.747 0.022 1 359 80 80 ASP H H 8.306 0.002 1 360 80 80 ASP C C 175.820 0.015 1 361 80 80 ASP CA C 53.849 0.157 1 362 80 80 ASP CB C 40.709 0.048 1 363 80 80 ASP N N 121.956 0.035 1 364 81 81 THR H H 8.188 0.002 1 365 81 81 THR C C 172.889 0.000 1 366 81 81 THR CA C 59.817 0.000 1 367 81 81 THR CB C 69.331 0.000 1 368 81 81 THR N N 115.981 0.022 1 369 84 84 LEU C C 177.301 0.004 1 370 84 84 LEU CA C 54.655 0.003 1 371 84 84 LEU CB C 41.550 0.001 1 372 85 85 ALA H H 8.620 0.002 1 373 85 85 ALA C C 177.746 0.007 1 374 85 85 ALA CA C 52.265 0.033 1 375 85 85 ALA CB C 18.474 0.000 1 376 85 85 ALA N N 125.392 0.063 1 377 86 86 ALA H H 8.490 0.006 1 378 86 86 ALA C C 178.182 0.007 1 379 86 86 ALA CA C 52.569 0.026 1 380 86 86 ALA CB C 18.632 0.095 1 381 86 86 ALA N N 123.415 0.058 1 382 87 87 GLU H H 8.579 0.001 1 383 87 87 GLU C C 176.792 0.011 1 384 87 87 GLU CA C 56.530 0.000 1 385 87 87 GLU CB C 29.480 0.000 1 386 87 87 GLU N N 119.854 0.034 1 387 88 88 LEU H H 8.381 0.001 1 388 88 88 LEU C C 177.635 0.018 1 389 88 88 LEU N N 122.744 0.063 1 390 89 89 GLU H H 8.628 0.002 1 391 89 89 GLU C C 176.904 0.008 1 392 89 89 GLU CA C 56.407 0.213 1 393 89 89 GLU CB C 29.452 0.007 1 394 89 89 GLU N N 121.719 0.031 1 395 90 90 ARG H H 8.498 0.002 1 396 90 90 ARG C C 176.473 0.009 1 397 90 90 ARG CA C 56.273 0.000 1 398 90 90 ARG CB C 29.777 0.040 1 399 90 90 ARG N N 122.124 0.046 1 400 91 91 TRP H H 8.273 0.002 1 401 91 91 TRP C C 176.381 0.013 1 402 91 91 TRP CA C 56.648 0.213 1 403 91 91 TRP CB C 28.812 0.181 1 404 91 91 TRP N N 120.944 0.027 1 405 92 92 LYS H H 8.269 0.003 1 406 92 92 LYS C C 176.567 0.004 1 407 92 92 LYS CA C 56.117 0.000 1 408 92 92 LYS CB C 32.359 0.028 1 409 92 92 LYS N N 122.811 0.023 1 410 93 93 LEU H H 8.377 0.002 1 411 93 93 LEU C C 177.254 0.015 1 412 93 93 LEU CA C 54.924 0.074 1 413 93 93 LEU CB C 41.547 0.154 1 414 93 93 LEU N N 123.289 0.056 1 415 94 94 ASP H H 8.595 0.001 1 416 94 94 ASP C C 176.841 0.007 1 417 94 94 ASP CA C 54.054 0.188 1 418 94 94 ASP CB C 40.985 0.064 1 419 94 94 ASP N N 121.080 0.056 1 420 95 95 GLY H H 8.544 0.003 1 421 95 95 GLY C C 174.358 0.044 1 422 95 95 GLY CA C 45.092 0.000 1 423 95 95 GLY N N 109.361 0.055 1 424 96 96 ARG H H 8.363 0.001 1 425 96 96 ARG C C 176.166 0.001 1 426 96 96 ARG CA C 56.210 0.013 1 427 96 96 ARG CB C 30.133 0.030 1 428 96 96 ARG N N 120.269 0.026 1 429 97 97 ASP H H 8.682 0.002 1 430 97 97 ASP C C 176.693 0.013 1 431 97 97 ASP CA C 53.889 0.000 1 432 97 97 ASP CB C 40.635 0.040 1 433 97 97 ASP N N 121.306 0.071 1 434 98 98 VAL H H 8.315 0.001 1 435 98 98 VAL C C 176.435 0.001 1 436 98 98 VAL CA C 61.932 0.194 1 437 98 98 VAL CB C 31.812 0.021 1 438 98 98 VAL N N 120.398 0.026 1 439 99 99 SER H H 8.639 0.001 1 440 99 99 SER C C 174.726 0.002 1 441 99 99 SER CA C 58.638 0.134 1 442 99 99 SER CB C 63.076 0.059 1 443 99 99 SER N N 119.076 0.028 1 444 100 100 LEU H H 8.329 0.001 1 445 100 100 LEU C C 177.127 0.008 1 446 100 100 LEU CA C 54.799 0.135 1 447 100 100 LEU CB C 41.608 0.164 1 448 100 100 LEU N N 123.970 0.026 1 449 101 101 LEU H H 8.414 0.003 1 450 101 101 LEU C C 177.297 0.002 1 451 101 101 LEU CA C 54.710 0.125 1 452 101 101 LEU CB C 41.260 0.022 1 453 101 101 LEU N N 123.076 0.037 1 454 102 102 ILE H H 8.493 0.001 1 455 102 102 ILE C C 176.852 0.013 1 456 102 102 ILE CA C 61.053 0.100 1 457 102 102 ILE CB C 38.063 0.066 1 458 102 102 ILE N N 122.684 0.021 1 459 103 103 GLY H H 8.683 0.002 1 460 103 103 GLY C C 174.232 0.004 1 461 103 103 GLY CA C 44.730 0.035 1 462 103 103 GLY N N 113.164 0.025 1 463 104 104 GLY H H 8.327 0.001 1 464 104 104 GLY C C 172.029 0.000 1 465 104 104 GLY CA C 44.364 0.086 1 466 104 104 GLY N N 108.501 0.029 1 467 105 105 PRO C C 177.325 0.006 1 468 105 105 PRO CA C 63.213 0.080 1 469 105 105 PRO CB C 31.523 0.162 1 470 106 106 GLU H H 8.876 0.001 1 471 106 106 GLU C C 177.170 0.028 1 472 106 106 GLU CA C 56.563 0.076 1 473 106 106 GLU CB C 29.578 0.081 1 474 106 106 GLU N N 120.732 0.025 1 475 107 107 GLY H H 8.463 0.001 1 476 107 107 GLY C C 173.918 0.003 1 477 107 107 GLY CA C 44.964 0.031 1 478 107 107 GLY N N 109.404 0.027 1 479 108 108 LEU H H 8.308 0.002 1 480 108 108 LEU C C 177.547 0.002 1 481 108 108 LEU CA C 54.627 0.066 1 482 108 108 LEU CB C 41.863 0.034 1 483 108 108 LEU N N 121.385 0.025 1 484 109 109 SER H H 8.736 0.002 1 485 109 109 SER C C 172.839 0.000 1 486 109 109 SER CA C 56.498 0.084 1 487 109 109 SER CB C 62.609 0.000 1 488 109 109 SER N N 118.916 0.024 1 489 110 110 PRO C C 176.823 0.022 1 490 110 110 PRO CA C 55.390 3.739 1 491 110 110 PRO CB C 31.712 0.000 1 492 111 111 ALA H H 8.555 0.002 1 493 111 111 ALA C C 177.925 0.008 1 494 111 111 ALA CA C 52.582 0.098 1 495 111 111 ALA CB C 18.576 0.075 1 496 111 111 ALA N N 123.857 0.102 1 497 112 112 CYS H H 8.428 0.002 1 498 112 112 CYS C C 175.192 0.025 1 499 112 112 CYS CA C 58.931 0.058 1 500 112 112 CYS CB C 27.948 0.123 1 501 112 112 CYS N N 119.369 0.028 1 502 113 113 LYS H H 8.645 0.002 1 503 113 113 LYS C C 176.531 0.023 1 504 113 113 LYS CA C 56.390 0.190 1 505 113 113 LYS CB C 32.468 0.111 1 506 113 113 LYS N N 124.556 0.045 1 507 114 114 ALA H H 8.619 0.001 1 508 114 114 ALA C C 177.780 0.004 1 509 114 114 ALA CA C 52.478 0.000 1 510 114 114 ALA CB C 18.477 0.000 1 511 114 114 ALA N N 125.459 0.069 1 512 115 115 ALA H H 8.485 0.001 5 513 115 115 ALA C C 177.853 0.007 5 514 115 115 ALA CA C 52.379 0.000 5 515 115 115 ALA CB C 18.666 0.000 5 516 115 115 ALA N N 123.487 0.016 5 517 116 116 ALA H H 8.433 0.004 1 518 116 116 ALA C C 178.021 0.036 1 519 116 116 ALA CA C 52.387 0.036 1 520 116 116 ALA CB C 18.636 0.115 1 521 116 116 ALA N N 123.058 0.020 1 522 117 117 GLU H H 8.503 0.001 1 523 117 117 GLU C C 176.737 0.005 1 524 117 117 GLU CA C 56.211 0.000 1 525 117 117 GLU CB C 29.613 0.001 1 526 117 117 GLU N N 119.983 0.022 1 527 118 118 GLN H H 8.538 0.003 1 528 118 118 GLN C C 176.115 0.017 1 529 118 118 GLN CA C 55.522 0.164 1 530 118 118 GLN CB C 28.854 0.059 1 531 118 118 GLN N N 121.150 0.032 1 532 119 119 SER H H 8.534 0.001 1 533 119 119 SER C C 174.486 0.003 1 534 119 119 SER CA C 58.162 0.105 1 535 119 119 SER CB C 63.179 0.098 1 536 119 119 SER N N 116.985 0.024 1 537 120 120 TRP H H 8.365 0.003 1 538 120 120 TRP C C 176.293 0.014 1 539 120 120 TRP CA C 57.083 0.000 1 540 120 120 TRP CB C 29.218 0.000 1 541 120 120 TRP N N 123.126 0.018 1 542 121 121 SER H H 8.361 0.002 1 543 121 121 SER C C 174.655 0.017 1 544 121 121 SER CA C 57.797 0.000 1 545 121 121 SER CB C 63.380 0.000 1 546 121 121 SER N N 116.987 0.083 1 547 122 122 LEU H H 8.436 0.001 1 548 122 122 LEU C C 177.738 0.002 1 549 122 122 LEU CA C 54.933 0.000 1 550 122 122 LEU CB C 41.389 0.056 1 551 122 122 LEU N N 124.354 0.021 1 552 123 123 SER H H 8.473 0.002 1 553 123 123 SER C C 174.479 0.007 1 554 123 123 SER CA C 58.180 0.109 1 555 123 123 SER CB C 63.255 0.064 1 556 123 123 SER N N 116.260 0.023 1 557 124 124 ALA H H 8.452 0.001 1 558 124 124 ALA C C 177.681 0.003 1 559 124 124 ALA CA C 52.444 0.073 1 560 124 124 ALA CB C 18.599 0.084 1 561 124 124 ALA N N 125.776 0.020 1 562 125 125 LEU H H 8.351 0.001 1 563 125 125 LEU C C 177.638 0.007 1 564 125 125 LEU CA C 54.939 0.166 1 565 125 125 LEU CB C 41.570 0.062 1 566 125 125 LEU N N 120.912 0.029 1 567 126 126 THR H H 8.343 0.002 1 568 126 126 THR C C 174.394 0.013 1 569 126 126 THR CA C 61.407 0.055 1 570 126 126 THR CB C 69.642 0.089 1 571 126 126 THR N N 115.428 0.033 1 572 127 127 LEU H H 8.541 0.001 1 573 127 127 LEU C C 175.250 0.000 1 574 127 127 LEU CA C 52.907 0.000 1 575 127 127 LEU CB C 40.990 0.000 1 576 127 127 LEU N N 125.833 0.019 1 577 132 132 VAL C C 176.488 0.001 1 578 132 132 VAL CA C 55.841 0.048 1 579 132 132 VAL CB C 32.380 0.015 1 580 133 133 ARG H H 8.705 0.001 1 581 133 133 ARG C C 177.300 0.009 1 582 133 133 ARG CA C 54.656 0.057 1 583 133 133 ARG CB C 41.674 0.098 1 584 133 133 ARG N N 125.040 0.018 1 585 134 134 VAL H H 8.858 0.001 1 586 134 134 VAL C C 175.826 0.019 1 587 134 134 VAL CA C 55.180 0.130 1 588 134 134 VAL CB C 28.786 0.047 1 589 134 134 VAL N N 122.631 0.020 1 590 135 135 LEU H H 8.619 0.001 1 591 135 135 LEU C C 177.295 0.004 1 592 135 135 LEU CA C 54.916 0.180 1 593 135 135 LEU CB C 41.463 0.000 1 594 135 135 LEU N N 124.838 0.036 1 595 136 136 VAL H H 8.515 0.001 1 596 136 136 VAL C C 175.812 0.000 1 597 136 136 VAL CA C 61.645 0.080 1 598 136 136 VAL CB C 32.264 0.023 1 599 136 136 VAL N N 121.842 0.033 1 600 137 137 ALA H H 8.634 0.002 1 601 137 137 ALA C C 177.700 0.010 1 602 137 137 ALA CA C 52.310 0.179 1 603 137 137 ALA CB C 18.546 0.083 1 604 137 137 ALA N N 128.339 0.028 1 605 138 138 GLU H H 8.650 0.002 1 606 138 138 GLU C C 176.691 0.025 1 607 138 138 GLU CA C 56.291 0.188 1 608 138 138 GLU CB C 29.772 0.024 1 609 138 138 GLU N N 120.818 0.043 1 610 139 139 SER H H 8.587 0.001 1 611 139 139 SER C C 174.695 0.000 1 612 139 139 SER CA C 58.016 0.115 1 613 139 139 SER CB C 63.201 0.055 1 614 139 139 SER N N 116.760 0.025 1 615 140 140 LEU H H 8.446 0.003 1 616 140 140 LEU C C 177.078 0.007 1 617 140 140 LEU CA C 55.082 0.159 1 618 140 140 LEU CB C 41.542 0.055 1 619 140 140 LEU N N 124.446 0.033 1 620 141 141 TYR H H 8.382 0.002 1 621 141 141 TYR C C 175.678 0.008 1 622 141 141 TYR CA C 57.764 0.141 1 623 141 141 TYR CB C 38.099 0.032 1 624 141 141 TYR N N 121.031 0.029 1 625 142 142 ARG H H 8.379 0.002 1 626 142 142 ARG C C 175.493 0.004 1 627 142 142 ARG CA C 55.169 0.163 1 628 142 142 ARG CB C 30.207 0.039 1 629 142 142 ARG N N 124.225 0.024 1 630 143 143 ALA H H 8.431 0.002 1 631 143 143 ALA C C 177.415 0.008 1 632 143 143 ALA CA C 52.212 0.085 1 633 143 143 ALA CB C 18.554 0.108 1 634 143 143 ALA N N 125.742 0.021 1 635 144 144 TRP H H 8.297 0.004 1 636 144 144 TRP C C 176.237 0.009 1 637 144 144 TRP CA C 56.817 0.133 1 638 144 144 TRP CB C 29.135 0.109 1 639 144 144 TRP N N 120.361 0.014 1 640 145 145 SER H H 8.364 0.002 1 641 145 145 SER C C 174.224 0.015 1 642 145 145 SER CA C 57.712 0.097 1 643 145 145 SER CB C 63.411 0.040 1 644 145 145 SER N N 117.292 0.078 1 645 146 146 ILE H H 8.391 0.001 1 646 146 146 ILE C C 176.502 0.008 1 647 146 146 ILE CA C 61.118 0.142 1 648 146 146 ILE CB C 38.255 0.037 1 649 146 146 ILE N N 122.567 0.019 1 650 147 147 THR H H 8.432 0.001 1 651 147 147 THR C C 174.726 0.023 1 652 147 147 THR CA C 61.384 0.051 1 653 147 147 THR CB C 69.562 0.074 1 654 147 147 THR N N 117.619 0.017 1 655 148 148 THR H H 8.352 0.002 1 656 148 148 THR C C 174.146 0.015 1 657 148 148 THR CA C 61.310 0.000 1 658 148 148 THR CB C 69.556 0.057 1 659 148 148 THR N N 116.013 0.023 1 660 149 149 ASN H H 8.635 0.002 1 661 149 149 ASN C C 174.583 0.004 1 662 149 149 ASN CA C 52.733 0.038 1 663 149 149 ASN CB C 38.459 0.061 1 664 149 149 ASN N N 121.038 0.087 1 665 150 150 HIS H H 8.481 0.002 1 666 150 150 HIS C C 174.062 0.000 1 667 150 150 HIS CA C 54.813 0.000 1 668 150 150 HIS CB C 30.392 0.000 1 669 150 150 HIS N N 121.874 0.022 1 670 151 151 PRO C C 176.526 0.007 1 671 151 151 PRO CA C 63.133 0.058 1 672 151 151 PRO CB C 31.252 0.083 1 673 152 152 TYR H H 8.716 0.003 1 674 152 152 TYR C C 175.620 0.008 1 675 152 152 TYR CA C 57.653 0.042 1 676 152 152 TYR CB C 38.192 0.009 1 677 152 152 TYR N N 120.703 0.086 1 678 153 153 HIS H H 8.436 0.001 1 679 153 153 HIS C C 174.876 0.007 1 680 153 153 HIS CA C 56.334 0.149 1 681 153 153 HIS CB C 30.982 0.015 1 682 153 153 HIS N N 122.511 0.024 1 683 154 154 ARG H H 8.416 0.001 1 684 154 154 ARG C C 175.196 0.007 1 685 154 154 ARG CA C 55.673 0.084 1 686 154 154 ARG CB C 30.533 0.098 1 687 154 154 ARG N N 124.229 0.025 1 688 155 155 GLU H H 8.392 0.001 1 689 155 155 GLU C C 181.353 0.000 1 690 155 155 GLU CA C 58.016 0.000 1 691 155 155 GLU CB C 30.299 0.000 1 692 155 155 GLU N N 127.922 0.022 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 280,512 281,513 282,514 283,515 284,516 stop_ save_