data_27046 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone chemical shift assignments for the oxidized alpha-crystallin domain of HSP27 (HSPB1) ; _BMRB_accession_number 27046 _BMRB_flat_file_name bmr27046.str _Entry_type original _Submission_date 2017-03-09 _Accession_date 2017-03-09 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Alderson T. Reid . 2 Gastall Heidi Y. . 3 Benesch Justin L.P. . 4 Baldwin Andrew J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 80 "13C chemical shifts" 249 "15N chemical shifts" 77 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-06-30 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 25645 'Chemical Shift Assignments and Structure of HSPB1_ACD' stop_ _Original_release_date 2017-03-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Proline isomerization in the C-terminal region of HSP27 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 28547731 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Alderson 'T Reid' R. . 2 Benesch Justin . . 3 Baldwin Andrew J. . stop_ _Journal_abbreviation 'Cell Stress Chaperones' _Journal_name_full 'Cell stress & chaperones' _Journal_volume 22 _Journal_issue 4 _Journal_ISSN 1466-1268 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 639 _Page_last 651 _Year 2017 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'cHSP27 dimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label cHSP27_dimer $cHSP27 cHSP27_dimer2 $cHSP27 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 cHSP27_dimer 1 cHSP27_dimer2 stop_ _Database_query_date . _Details 'Symmetric homo-dimer with an intermolecular disulfide bond between adjacent C137 residues.' save_ ######################## # Monomeric polymers # ######################## save_cHSP27 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common cHSP27 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details ; The residue C137 forms an intermolecular disulfide bond. The protein is a symmetric homo-dimer. ; ############################## # Polymer residue sequence # ############################## _Residue_count 88 _Mol_residue_sequence ; GVSEIRHTADRWRVSLDVNH FAPDELTVKTKDGVVEITGK HEERQDEHGYISRCFTRKYT LPPGVDPTQVSSSLSPEGTL TVEAPMPK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 84 GLY 2 85 VAL 3 86 SER 4 87 GLU 5 88 ILE 6 89 ARG 7 90 HIS 8 91 THR 9 92 ALA 10 93 ASP 11 94 ARG 12 95 TRP 13 96 ARG 14 97 VAL 15 98 SER 16 99 LEU 17 100 ASP 18 101 VAL 19 102 ASN 20 103 HIS 21 104 PHE 22 105 ALA 23 106 PRO 24 107 ASP 25 108 GLU 26 109 LEU 27 110 THR 28 111 VAL 29 112 LYS 30 113 THR 31 114 LYS 32 115 ASP 33 116 GLY 34 117 VAL 35 118 VAL 36 119 GLU 37 120 ILE 38 121 THR 39 122 GLY 40 123 LYS 41 124 HIS 42 125 GLU 43 126 GLU 44 127 ARG 45 128 GLN 46 129 ASP 47 130 GLU 48 131 HIS 49 132 GLY 50 133 TYR 51 134 ILE 52 135 SER 53 136 ARG 54 137 CYS 55 138 PHE 56 139 THR 57 140 ARG 58 141 LYS 59 142 TYR 60 143 THR 61 144 LEU 62 145 PRO 63 146 PRO 64 147 GLY 65 148 VAL 66 149 ASP 67 150 PRO 68 151 THR 69 152 GLN 70 153 VAL 71 154 SER 72 155 SER 73 156 SER 74 157 LEU 75 158 SER 76 159 PRO 77 160 GLU 78 161 GLY 79 162 THR 80 163 LEU 81 164 THR 82 165 VAL 83 166 GLU 84 167 ALA 85 168 PRO 86 169 MET 87 170 PRO 88 171 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 _Gene_mnemonic $cHSP27 Human 9606 Eukaryota Metazoa Homo sapiens hspb1 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 _Details $cHSP27 'recombinant technology' . Escherichia coli BL21(DE3) pET28a 'Hexahistidine tag followed by a TEV protease recognition site followed by cHSP27 amino acids.' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '1 mM [U-13C,15N]-cHSP27 in 30 mM NaH2PO4, 2 mM EDTA, pH 7' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $cHSP27 1 mM '[U-100% 13C; U-100% 15N]' 'sodium phosphate' 30 mM 'natural abundance' EDTA 2 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_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details 'Room temperature probe' save_ ############################# # NMR applied experiments # ############################# save_3D_HNCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_C(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 30 . mM 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 water C 13 protons ppm 4.773 internal indirect . . . 0.251449530 water H 1 protons ppm 4.773 internal direct . . . 1 water N 15 protons ppm 4.773 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HNCO' '3D HNCA' '3D HN(CO)CA' '3D HN(CA)CO' '3D C(CO)NH' '2D 1H-15N HSQC' 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 cHSP27_dimer _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 85 2 VAL C C 175.856 0.1 . 2 85 2 VAL CA C 62.450 0.1 . 3 85 2 VAL CB C 33.230 0.1 . 4 86 3 SER H H 8.379 0.01 . 5 86 3 SER C C 174.026 0.1 . 6 86 3 SER CA C 60.810 0.1 . 7 86 3 SER CB C 63.670 0.1 . 8 86 3 SER N N 119.454 0.05 . 9 87 4 GLU H H 8.487 0.01 . 10 87 4 GLU C C 175.451 0.1 . 11 87 4 GLU CA C 56.280 0.1 . 12 87 4 GLU CB C 31.290 0.1 . 13 87 4 GLU N N 123.690 0.05 . 14 88 5 ILE H H 8.220 0.01 . 15 88 5 ILE C C 176.249 0.1 . 16 88 5 ILE CA C 60.850 0.1 . 17 88 5 ILE CB C 37.720 0.1 . 18 88 5 ILE N N 122.268 0.05 . 19 89 6 ARG H H 8.338 0.01 . 20 89 6 ARG CA C 54.98 0.1 . 21 89 6 ARG N N 126.514 0.05 . 22 90 7 HIS C C 176.464 0.1 . 23 90 7 HIS CA C 56.092 0.1 . 24 90 7 HIS CB C 31.487 0.1 . 25 91 8 THR H H 8.689 0.01 . 26 91 8 THR C C 174.466 0.1 . 27 91 8 THR CA C 60.600 0.1 . 28 91 8 THR CB C 70.770 0.1 . 29 91 8 THR N N 115.185 0.05 . 30 92 9 ALA H H 8.497 0.01 . 31 92 9 ALA HB H 1.135 0.01 . 32 92 9 ALA C C 177.712 0.1 . 33 92 9 ALA CA C 53.650 0.1 . 34 92 9 ALA CB C 19.060 0.1 . 35 92 9 ALA N N 123.340 0.05 . 36 93 10 ASP H H 8.227 0.01 . 37 93 10 ASP C C 176.375 0.1 . 38 93 10 ASP CA C 54.140 0.1 . 39 93 10 ASP CB C 41.740 0.1 . 40 93 10 ASP N N 114.544 0.05 . 41 94 11 ARG H H 7.927 0.01 . 42 94 11 ARG C C 173.972 0.1 . 43 94 11 ARG CA C 55.300 0.1 . 44 94 11 ARG CB C 33.250 0.1 . 45 94 11 ARG N N 121.211 0.05 . 46 95 12 TRP H H 9.148 0.01 . 47 95 12 TRP C C 175.193 0.1 . 48 95 12 TRP CA C 57.374 0.1 . 49 95 12 TRP N N 128.685 0.05 . 50 96 13 ARG C C 173.634 0.1 . 51 96 13 ARG CA C 55.330 0.1 . 52 96 13 ARG CB C 33.820 0.1 . 53 97 14 VAL H H 8.346 0.01 . 54 97 14 VAL C C 173.800 0.1 . 55 97 14 VAL CA C 59.360 0.1 . 56 97 14 VAL CB C 35.290 0.1 . 57 97 14 VAL N N 119.863 0.05 . 58 98 15 SER H H 8.265 0.01 . 59 98 15 SER C C 172.784 0.1 . 60 98 15 SER CA C 56.977 0.1 . 61 98 15 SER CB C 66.363 0.1 . 62 98 15 SER N N 115.758 0.05 . 63 99 16 LEU H H 9.241 0.01 . 64 99 16 LEU C C 174.712 0.1 . 65 99 16 LEU CA C 54.137 0.1 . 66 99 16 LEU CB C 45.157 0.1 . 67 99 16 LEU N N 123.601 0.05 . 68 100 17 ASP H H 8.428 0.01 . 69 100 17 ASP C C 176.632 0.1 . 70 100 17 ASP CA C 54.671 0.1 . 71 100 17 ASP CB C 40.835 0.1 . 72 100 17 ASP N N 123.383 0.05 . 73 101 18 VAL H H 8.799 0.01 . 74 101 18 VAL C C 176.457 0.1 . 75 101 18 VAL CA C 59.435 0.1 . 76 101 18 VAL N N 121.203 0.05 . 77 102 19 ASN H H 8.10 0.01 . 78 102 19 ASN C C 175.657 0.1 . 79 102 19 ASN CA C 56.558 0.1 . 80 102 19 ASN CB C 38.972 0.1 . 81 102 19 ASN N N 119.118 0.05 . 82 103 20 HIS H H 7.956 0.01 . 83 103 20 HIS C C 174.134 0.1 . 84 103 20 HIS CA C 57.931 0.1 . 85 103 20 HIS CB C 30.240 0.1 . 86 103 20 HIS N N 113.744 0.05 . 87 104 21 PHE H H 8.342 0.01 . 88 104 21 PHE C C 174.094 0.1 . 89 104 21 PHE CA C 58.101 0.1 . 90 104 21 PHE CB C 40.987 0.1 . 91 104 21 PHE N N 117.361 0.05 . 92 105 22 ALA H H 9.336 0.01 . 93 105 22 ALA C C 177.115 0.1 . 94 105 22 ALA CA C 49.928 0.1 . 95 105 22 ALA N N 126.918 0.05 . 96 106 23 PRO C C 178.389 0.1 . 97 106 23 PRO CA C 66.238 0.1 . 98 106 23 PRO CB C 31.790 0.1 . 99 107 24 ASP H H 8.205 0.01 . 100 107 24 ASP C C 176.993 0.1 . 101 107 24 ASP CA C 54.468 0.1 . 102 107 24 ASP CB C 39.67 0.1 . 103 107 24 ASP N N 110.354 0.05 . 104 108 25 GLU H H 8.223 0.01 . 105 108 25 GLU C C 174.932 0.1 . 106 108 25 GLU CA C 55.980 0.1 . 107 108 25 GLU CB C 30.134 0.1 . 108 108 25 GLU N N 120.277 0.05 . 109 109 26 LEU H H 7.168 0.01 . 110 109 26 LEU C C 176.579 0.1 . 111 109 26 LEU CA C 53.165 0.1 . 112 109 26 LEU CB C 46.283 0.1 . 113 109 26 LEU N N 120.351 0.05 . 114 110 27 THR H H 8.857 0.01 . 115 110 27 THR C C 172.765 0.1 . 116 110 27 THR CA C 61.038 0.1 . 117 110 27 THR CB C 71.786 0.1 . 118 110 27 THR N N 115.131 0.05 . 119 111 28 VAL H H 8.532 0.01 . 120 111 28 VAL C C 175.200 0.1 . 121 111 28 VAL CA C 61.704 0.1 . 122 111 28 VAL CB C 34.050 0.1 . 123 111 28 VAL N N 124.709 0.05 . 124 112 29 LYS H H 9.133 0.01 . 125 112 29 LYS C C 174.771 0.1 . 126 112 29 LYS CA C 54.970 0.1 . 127 112 29 LYS CB C 36.648 0.1 . 128 112 29 LYS N N 127.749 0.05 . 129 113 30 THR H H 8.601 0.01 . 130 113 30 THR C C 174.206 0.1 . 131 113 30 THR CA C 61.211 0.1 . 132 113 30 THR CB C 69.582 0.1 . 133 113 30 THR N N 118.477 0.05 . 134 114 31 LYS H H 8.734 0.01 . 135 114 31 LYS C C 175.231 0.1 . 136 114 31 LYS CA C 55.752 0.1 . 137 114 31 LYS CB C 34.752 0.1 . 138 114 31 LYS N N 125.406 0.05 . 139 115 32 ASP H H 9.053 0.01 . 140 115 32 ASP C C 175.938 0.1 . 141 115 32 ASP CA C 55.855 0.1 . 142 115 32 ASP CB C 39.835 0.1 . 143 115 32 ASP N N 124.036 0.05 . 144 116 33 GLY H H 8.744 0.01 . 145 116 33 GLY C C 173.585 0.1 . 146 116 33 GLY CA C 46.023 0.1 . 147 116 33 GLY N N 105.293 0.05 . 148 117 34 VAL H H 7.875 0.01 . 149 117 34 VAL C C 174.870 0.1 . 150 117 34 VAL CA C 60.097 0.1 . 151 117 34 VAL CB C 37.815 0.1 . 152 117 34 VAL N N 119.951 0.05 . 153 118 35 VAL H H 8.993 0.01 . 154 118 35 VAL C C 173.817 0.1 . 155 118 35 VAL CA C 61.285 0.1 . 156 118 35 VAL CB C 33.946 0.1 . 157 118 35 VAL N N 124.728 0.05 . 158 119 36 GLU H H 9.473 0.01 . 159 119 36 GLU C C 175.151 0.1 . 160 119 36 GLU CA C 54.748 0.1 . 161 119 36 GLU CB C 33.044 0.1 . 162 119 36 GLU N N 129.114 0.05 . 163 120 37 ILE H H 9.768 0.01 . 164 120 37 ILE C C 174.535 0.1 . 165 120 37 ILE CA C 59.833 0.1 . 166 120 37 ILE CB C 41.614 0.1 . 167 120 37 ILE N N 129.661 0.05 . 168 121 38 THR H H 8.738 0.01 . 169 121 38 THR C C 173.014 0.1 . 170 121 38 THR CA C 60.273 0.1 . 171 121 38 THR CB C 71.491 0.1 . 172 121 38 THR N N 122.177 0.05 . 173 122 39 GLY H H 7.461 0.01 . 174 122 39 GLY C C 172.129 0.1 . 175 122 39 GLY CA C 43.98 0.1 . 176 122 39 GLY N N 111.962 0.05 . 177 123 40 LYS H H 8.107 0.01 . 178 123 40 LYS C C 174.619 0.1 . 179 123 40 LYS CA C 53.915 0.1 . 180 123 40 LYS CB C 35.078 0.1 . 181 123 40 LYS N N 123.061 0.05 . 182 124 41 HIS H H 9.057 0.01 . 183 124 41 HIS C C 175.048 0.1 . 184 124 41 HIS CA C 53.911 0.1 . 185 124 41 HIS CB C 32.815 0.1 . 186 124 41 HIS N N 122.110 0.05 . 187 125 42 GLU H H 9.054 0.01 . 188 125 42 GLU C C 176.472 0.1 . 189 125 42 GLU CA C 54.870 0.1 . 190 125 42 GLU CB C 30.21 0.1 . 191 125 42 GLU N N 122.487 0.05 . 192 126 43 GLU H H 8.846 0.01 . 193 126 43 GLU C C 176.095 0.1 . 194 126 43 GLU CA C 53.437 0.1 . 195 126 43 GLU CB C 32.12 0.1 . 196 126 43 GLU N N 120.911 0.05 . 197 127 44 ARG H H 8.974 0.01 . 198 127 44 ARG C C 174.775 0.1 . 199 127 44 ARG CA C 54.294 0.1 . 200 127 44 ARG CB C 35.459 0.1 . 201 127 44 ARG N N 124.417 0.05 . 202 128 45 GLN H H 8.794 0.01 . 203 128 45 GLN C C 176.236 0.1 . 204 128 45 GLN CA C 55.586 0.1 . 205 128 45 GLN CB C 34.027 0.1 . 206 128 45 GLN N N 122.715 0.05 . 207 129 46 ASP H H 8.970 0.01 . 208 129 46 ASP C C 176.224 0.1 . 209 129 46 ASP CA C 52.199 0.1 . 210 129 46 ASP CB C 41.752 0.1 . 211 129 46 ASP N N 128.214 0.05 . 212 130 47 GLU H H 9.005 0.01 . 213 130 47 GLU C C 176.768 0.1 . 214 130 47 GLU CA C 58.973 0.1 . 215 130 47 GLU CB C 28.901 0.1 . 216 130 47 GLU N N 116.066 0.05 . 217 131 48 HIS H H 7.911 0.01 . 218 131 48 HIS C C 175.663 0.1 . 219 131 48 HIS CA C 55.803 0.1 . 220 131 48 HIS CB C 33.046 0.1 . 221 131 48 HIS N N 115.792 0.05 . 222 132 49 GLY H H 7.527 0.01 . 223 132 49 GLY C C 170.921 0.1 . 224 132 49 GLY CA C 43.319 0.1 . 225 132 49 GLY N N 108.342 0.05 . 226 133 50 TYR H H 8.518 0.01 . 227 133 50 TYR C C 175.400 0.1 . 228 133 50 TYR CA C 56.986 0.1 . 229 133 50 TYR CB C 42.37 0.1 . 230 133 50 TYR N N 121.994 0.05 . 231 134 51 ILE H H 9.402 0.01 . 232 134 51 ILE C C 172.800 0.1 . 233 134 51 ILE CA C 58.052 0.1 . 234 134 51 ILE CB C 42.010 0.1 . 235 134 51 ILE N N 121.108 0.05 . 236 135 52 SER H H 9.092 0.01 . 237 135 52 SER C C 172.652 0.1 . 238 135 52 SER CA C 57.142 0.1 . 239 135 52 SER CB C 65.986 0.1 . 240 135 52 SER N N 122.342 0.05 . 241 136 53 ARG H H 6.035 0.01 . 242 136 53 ARG C C 175.189 0.1 . 243 136 53 ARG CA C 55.716 0.1 . 244 136 53 ARG CB C 37.740 0.1 . 245 136 53 ARG N N 115.235 0.05 . 246 137 54 CYS H H 9.646 0.01 . 247 137 54 CYS C C 173.714 0.1 . 248 137 54 CYS CA C 56.782 0.1 . 249 137 54 CYS CB C 42.12 0.1 . 250 137 54 CYS N N 117.955 0.05 . 251 138 55 PHE H H 9.019 0.01 . 252 138 55 PHE C C 173.541 0.1 . 253 138 55 PHE CA C 58.413 0.1 . 254 138 55 PHE CB C 41.318 0.1 . 255 138 55 PHE N N 118.703 0.05 . 256 139 56 THR H H 8.414 0.01 . 257 139 56 THR C C 172.772 0.1 . 258 139 56 THR CA C 62.749 0.1 . 259 139 56 THR CB C 71.942 0.1 . 260 139 56 THR N N 116.186 0.05 . 261 140 57 ARG H H 9.899 0.01 . 262 140 57 ARG C C 176.212 0.1 . 263 140 57 ARG CA C 54.354 0.1 . 264 140 57 ARG CB C 29.758 0.1 . 265 140 57 ARG N N 129.372 0.05 . 266 141 58 LYS H H 8.989 0.01 . 267 141 58 LYS C C 176.212 0.1 . 268 141 58 LYS CA C 54.440 0.1 . 269 141 58 LYS CB C 36.779 0.1 . 270 141 58 LYS N N 124.730 0.05 . 271 142 59 TYR H H 9.360 0.01 . 272 142 59 TYR HB2 H 3.196 0.01 . 273 142 59 TYR HB3 H 2.614 0.01 . 274 142 59 TYR C C 175.586 0.1 . 275 142 59 TYR CA C 56.776 0.1 . 276 142 59 TYR CB C 41.994 0.1 . 277 142 59 TYR N N 121.393 0.05 . 278 143 60 THR H H 8.917 0.01 . 279 143 60 THR C C 174.471 0.1 . 280 143 60 THR CA C 62.951 0.1 . 281 143 60 THR CB C 69.156 0.1 . 282 143 60 THR N N 119.276 0.05 . 283 144 61 LEU H H 8.210 0.01 . 284 144 61 LEU C C 175.592 0.1 . 285 144 61 LEU CA C 52.619 0.1 . 286 144 61 LEU N N 128.507 0.05 . 287 146 63 PRO C C 177.621 0.1 . 288 146 63 PRO CA C 63.628 0.1 . 289 146 63 PRO CB C 31.647 0.1 . 290 146 63 PRO CG C 27.2663 0.1 . 291 147 64 GLY H H 8.539 0.01 . 292 147 64 GLY C C 174.671 0.1 . 293 147 64 GLY CA C 45.217 0.1 . 294 147 64 GLY N N 109.487 0.05 . 295 148 65 VAL H H 7.075 0.01 . 296 148 65 VAL C C 175.100 0.1 . 297 148 65 VAL CA C 62.699 0.1 . 298 148 65 VAL CB C 32.056 0.1 . 299 148 65 VAL N N 120.349 0.05 . 300 149 66 ASP H H 8.844 0.01 . 301 149 66 ASP C C 175.359 0.1 . 302 149 66 ASP CA C 50.440 0.1 . 303 149 66 ASP N N 130.322 0.05 . 304 150 67 PRO C C 178.501 0.1 . 305 150 67 PRO CA C 64.420 0.1 . 306 150 67 PRO CB C 32.420 0.1 . 307 150 67 PRO CG C 27.782 0.1 . 308 151 68 THR H H 8.379 0.01 . 309 151 68 THR C C 175.980 0.1 . 310 151 68 THR CA C 63.870 0.1 . 311 151 68 THR CB C 69.254 0.1 . 312 151 68 THR N N 108.584 0.05 . 313 152 69 GLN H H 8.069 0.01 . 314 152 69 GLN C C 174.988 0.1 . 315 152 69 GLN CA C 55.015 0.1 . 316 152 69 GLN CB C 29.395 0.1 . 317 152 69 GLN N N 119.118 0.05 . 318 153 70 VAL H H 6.951 0.01 . 319 153 70 VAL C C 176.157 0.1 . 320 153 70 VAL CA C 62.754 0.1 . 321 153 70 VAL CB C 32.200 0.1 . 322 153 70 VAL N N 120.733 0.05 . 323 154 71 SER H H 9.537 0.01 . 324 154 71 SER C C 172.165 0.1 . 325 154 71 SER CA C 56.811 0.1 . 326 154 71 SER CB C 66.154 0.1 . 327 154 71 SER N N 124.946 0.05 . 328 155 72 SER H H 8.442 0.01 . 329 155 72 SER C C 173.605 0.1 . 330 155 72 SER CA C 57.002 0.1 . 331 155 72 SER CB C 67.298 0.1 . 332 155 72 SER N N 114.067 0.05 . 333 156 73 SER H H 8.726 0.01 . 334 156 73 SER C C 171.850 0.1 . 335 156 73 SER CA C 57.510 0.1 . 336 156 73 SER CB C 65.413 0.1 . 337 156 73 SER N N 114.265 0.05 . 338 157 74 LEU H H 8.667 0.01 . 339 157 74 LEU C C 176.243 0.1 . 340 157 74 LEU CA C 53.369 0.1 . 341 157 74 LEU CB C 44.863 0.1 . 342 157 74 LEU N N 127.124 0.05 . 343 158 75 SER H H 8.938 0.01 . 344 158 75 SER C C 174.914 0.1 . 345 158 75 SER CA C 56.151 0.1 . 346 158 75 SER N N 124.246 0.05 . 347 159 76 PRO C C 177.234 0.1 . 348 159 76 PRO CA C 64.691 0.1 . 349 159 76 PRO CB C 31.820 0.1 . 350 159 76 PRO CG C 27.782 0.1 . 351 160 77 GLU H H 7.981 0.01 . 352 160 77 GLU C C 176.641 0.1 . 353 160 77 GLU CA C 56.786 0.1 . 354 160 77 GLU CB C 28.859 0.1 . 355 160 77 GLU N N 113.924 0.05 . 356 161 78 GLY H H 8.166 0.01 . 357 161 78 GLY C C 172.826 0.1 . 358 161 78 GLY CA C 46.570 0.1 . 359 161 78 GLY N N 108.228 0.05 . 360 162 79 THR H H 7.469 0.01 . 361 162 79 THR C C 173.889 0.1 . 362 162 79 THR CA C 61.468 0.1 . 363 162 79 THR CB C 69.567 0.1 . 364 162 79 THR N N 114.140 0.05 . 365 163 80 LEU H H 9.584 0.01 . 366 163 80 LEU C C 174.824 0.1 . 367 163 80 LEU CA C 53.701 0.1 . 368 163 80 LEU CB C 44.960 0.1 . 369 163 80 LEU N N 134.550 0.05 . 370 164 81 THR H H 9.227 0.01 . 371 164 81 THR C C 173.730 0.1 . 372 164 81 THR CA C 61.719 0.1 . 373 164 81 THR CB C 70.305 0.1 . 374 164 81 THR N N 123.920 0.05 . 375 165 82 VAL H H 8.921 0.01 . 376 165 82 VAL C C 173.391 0.1 . 377 165 82 VAL CA C 60.708 0.1 . 378 165 82 VAL CB C 33.392 0.1 . 379 165 82 VAL N N 128.824 0.05 . 380 166 83 GLU H H 8.973 0.01 . 381 166 83 GLU C C 174.361 0.1 . 382 166 83 GLU CA C 54.133 0.1 . 383 166 83 GLU CB C 35.900 0.1 . 384 166 83 GLU N N 122.018 0.05 . 385 167 84 ALA H H 9.392 0.01 . 386 167 84 ALA C C 173.654 0.1 . 387 167 84 ALA CA C 50.401 0.1 . 388 167 84 ALA N N 120.898 0.05 . 389 168 85 PRO C C 176.317 0.1 . 390 168 85 PRO CA C 62.742 0.1 . 391 168 85 PRO CB C 32.078 0.1 . 392 168 85 PRO CG C 27.463 0.1 . 393 168 85 PRO CD C 50.875 0.1 . 394 169 86 MET H H 7.813 0.01 . 395 169 86 MET C C 174.491 0.1 . 396 169 86 MET CA C 52.467 0.1 . 397 169 86 MET N N 120.595 0.05 . 398 170 87 PRO C C 175.860 0.1 . 399 170 87 PRO CA C 63.208 0.1 . 400 170 87 PRO CB C 32.082 0.1 . 401 170 87 PRO CG C 27.541 0.1 . 402 170 87 PRO CD C 50.556 0.1 . 403 171 88 LYS H H 8.001 0.01 . 404 171 88 LYS C C 181.500 0.1 . 405 171 88 LYS CA C 57.563 0.1 . 406 171 88 LYS N N 126.935 0.05 . stop_ save_