data_27636 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Thioredoxin-huntingtin exon 1(Q7) fusion ; _BMRB_accession_number 27636 _BMRB_flat_file_name bmr27636.str _Entry_type original _Submission_date 2018-10-03 _Accession_date 2018-10-03 _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 Ulmer Tobias . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 154 "13C chemical shifts" 288 "15N chemical shifts" 154 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-01-18 update BMRB 'update entry citation' 2018-11-14 original author 'original release' stop_ _Original_release_date 2018-10-03 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The folding equilibrium of huntingtin exon 1 monomer depends on its polyglutamine tract. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30315108 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bravo-Arredondo Jose M. . 2 Kegulian Natalie C. . 3 Schmidt Thomas . . 4 Pandey Nitin K. . 5 Situ Alan J. . 6 Langen Ralf . . 7 Ulmer Tobias S. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 293 _Journal_issue 51 _Journal_ISSN 1083-351X _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 19613 _Page_last 19623 _Year 2018 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'huntingtin exon 1 mutant' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label monomer $Thr-Httex1(Q7) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Thr-Httex1(Q7) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Thr-Httex1(Q7) _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 212 _Mol_residue_sequence ; MSDKIIHLTDDSFDTDVLKA DGAILVDFWAEWSGPSKMIA PILDEIADEYQGKLTVAKLN IDQNPGTAPKYGIRGIPTLL LFKNGEVAATKVGALSKGQL KEFLDANLAGSGSGERQHMD SPDLGTDDDDKAMATLEKLM KAFESLKSFQQQQQQQPPPP PPPPPPPQLPQPPPQAQPLL PQPQPPPPPPPPPPGPAVAE EPLHRPHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 ASP 4 LYS 5 ILE 6 ILE 7 HIS 8 LEU 9 THR 10 ASP 11 ASP 12 SER 13 PHE 14 ASP 15 THR 16 ASP 17 VAL 18 LEU 19 LYS 20 ALA 21 ASP 22 GLY 23 ALA 24 ILE 25 LEU 26 VAL 27 ASP 28 PHE 29 TRP 30 ALA 31 GLU 32 TRP 33 SER 34 GLY 35 PRO 36 SER 37 LYS 38 MET 39 ILE 40 ALA 41 PRO 42 ILE 43 LEU 44 ASP 45 GLU 46 ILE 47 ALA 48 ASP 49 GLU 50 TYR 51 GLN 52 GLY 53 LYS 54 LEU 55 THR 56 VAL 57 ALA 58 LYS 59 LEU 60 ASN 61 ILE 62 ASP 63 GLN 64 ASN 65 PRO 66 GLY 67 THR 68 ALA 69 PRO 70 LYS 71 TYR 72 GLY 73 ILE 74 ARG 75 GLY 76 ILE 77 PRO 78 THR 79 LEU 80 LEU 81 LEU 82 PHE 83 LYS 84 ASN 85 GLY 86 GLU 87 VAL 88 ALA 89 ALA 90 THR 91 LYS 92 VAL 93 GLY 94 ALA 95 LEU 96 SER 97 LYS 98 GLY 99 GLN 100 LEU 101 LYS 102 GLU 103 PHE 104 LEU 105 ASP 106 ALA 107 ASN 108 LEU 109 ALA 110 GLY 111 SER 112 GLY 113 SER 114 GLY 115 GLU 116 ARG 117 GLN 118 HIS 119 MET 120 ASP 121 SER 122 PRO 123 ASP 124 LEU 125 GLY 126 THR 127 ASP 128 ASP 129 ASP 130 ASP 131 LYS 132 ALA 133 MET 134 ALA 135 THR 136 LEU 137 GLU 138 LYS 139 LEU 140 MET 141 LYS 142 ALA 143 PHE 144 GLU 145 SER 146 LEU 147 LYS 148 SER 149 PHE 150 GLN 151 GLN 152 GLN 153 GLN 154 GLN 155 GLN 156 GLN 157 PRO 158 PRO 159 PRO 160 PRO 161 PRO 162 PRO 163 PRO 164 PRO 165 PRO 166 PRO 167 PRO 168 GLN 169 LEU 170 PRO 171 GLN 172 PRO 173 PRO 174 PRO 175 GLN 176 ALA 177 GLN 178 PRO 179 LEU 180 LEU 181 PRO 182 GLN 183 PRO 184 GLN 185 PRO 186 PRO 187 PRO 188 PRO 189 PRO 190 PRO 191 PRO 192 PRO 193 PRO 194 PRO 195 GLY 196 PRO 197 ALA 198 VAL 199 ALA 200 GLU 201 GLU 202 PRO 203 LEU 204 HIS 205 ARG 206 PRO 207 HIS 208 HIS 209 HIS 210 HIS 211 HIS 212 HIS 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 $Thr-Httex1(Q7) Human 9606 Eukaryota Metazoa Homo sapiens 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 $Thr-Httex1(Q7) 'recombinant technology' . Escherichia coli . pET32a 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 $Thr-Httex1(Q7) 0.3 mM '[U-99% 13C; U-99% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . 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_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.05 . M pH 6.0 . pH pressure ambient . 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 4.771 internal indirect . . . 0.25144954 water H 1 protons ppm 4.771 internal direct . . . 1 water N 15 protons ppm 4.771 internal indirect . . . 0.10132900 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 HNCA' '3D HNCACB' '3D CBCA(CO)NH' 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 monomer _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 3 3 ASP H H 8.885 0.020 1 2 3 3 ASP CA C 54.445 0.3 1 3 3 3 ASP CB C 40.855 0.3 1 4 3 3 ASP N N 123.395 0.3 1 5 4 4 LYS H H 8.411 0.020 1 6 4 4 LYS CA C 56.596 0.3 1 7 4 4 LYS CB C 33.206 0.3 1 8 4 4 LYS N N 119.711 0.3 1 9 5 5 ILE H H 7.508 0.020 1 10 5 5 ILE CA C 60.421 0.3 1 11 5 5 ILE CB C 38.146 0.3 1 12 5 5 ILE N N 120.810 0.3 1 13 6 6 ILE H H 8.441 0.020 1 14 6 6 ILE CA C 60.527 0.3 1 15 6 6 ILE CB C 38.996 0.3 1 16 6 6 ILE N N 126.685 0.3 1 17 7 7 HIS H H 8.973 0.020 1 18 7 7 HIS CA C 55.640 0.3 1 19 7 7 HIS CB C 29.700 0.3 1 20 7 7 HIS N N 126.714 0.3 1 21 8 8 LEU H H 8.714 0.020 1 22 8 8 LEU CA C 53.887 0.3 1 23 8 8 LEU CB C 45.742 0.3 1 24 8 8 LEU N N 125.072 0.3 1 25 9 9 THR H H 8.104 0.020 1 26 9 9 THR CA C 58.827 0.3 1 27 9 9 THR CB C 72.790 0.3 1 28 9 9 THR N N 108.138 0.3 1 29 10 10 ASP H H 8.163 0.020 1 30 10 10 ASP CA C 58.057 0.3 1 31 10 10 ASP CB C 40.324 0.3 1 32 10 10 ASP N N 119.648 0.3 1 33 11 11 ASP H H 8.229 0.020 1 34 11 11 ASP CA C 56.304 0.3 1 35 11 11 ASP N N 116.307 0.3 1 36 12 12 SER H H 8.233 0.020 1 37 12 12 SER CA C 59.226 0.3 1 38 12 12 SER N N 117.728 0.3 1 39 13 13 PHE H H 7.646 0.020 1 40 13 13 PHE CA C 63.422 0.3 1 41 13 13 PHE CB C 40.590 0.3 1 42 13 13 PHE N N 125.187 0.3 1 43 14 14 ASP H H 8.788 0.020 1 44 14 14 ASP CA C 58.057 0.3 1 45 14 14 ASP CB C 40.590 0.3 1 46 14 14 ASP N N 117.469 0.3 1 47 15 15 THR H H 7.826 0.020 1 48 15 15 THR CA C 65.812 0.3 1 49 15 15 THR CB C 69.062 0.3 1 50 15 15 THR N N 112.602 0.3 1 51 16 16 ASP H H 8.424 0.020 1 52 16 16 ASP CA C 56.410 0.3 1 53 16 16 ASP CB C 41.546 0.3 1 54 16 16 ASP N N 118.541 0.3 1 55 17 17 VAL H H 7.586 0.020 1 56 17 17 VAL CA C 63.183 0.3 1 57 17 17 VAL CB C 32.250 0.3 1 58 17 17 VAL N N 112.919 0.3 1 59 18 18 LEU H H 6.958 0.020 1 60 18 18 LEU CA C 58.084 0.3 1 61 18 18 LEU CB C 39.368 0.3 1 62 18 18 LEU N N 116.288 0.3 1 63 19 19 LYS H H 7.420 0.020 1 64 19 19 LYS CA C 54.870 0.3 1 65 19 19 LYS CB C 31.931 0.3 1 66 19 19 LYS N N 115.165 0.3 1 67 20 20 ALA H H 6.588 0.020 1 68 20 20 ALA CA C 52.161 0.3 1 69 20 20 ALA CB C 20.192 0.3 1 70 20 20 ALA N N 122.308 0.3 1 71 21 21 ASP H H 8.563 0.020 1 72 21 21 ASP CA C 54.179 0.3 1 73 21 21 ASP CB C 41.865 0.3 1 74 21 21 ASP N N 121.394 0.3 1 75 22 22 GLY H H 8.178 0.020 1 76 22 22 GLY CA C 44.299 0.3 1 77 22 22 GLY N N 108.628 0.3 1 78 23 23 ALA H H 8.515 0.020 1 79 23 23 ALA CA C 51.603 0.3 1 80 23 23 ALA CB C 19.979 0.3 1 81 23 23 ALA N N 123.258 0.3 1 82 24 24 ILE H H 8.982 0.020 1 83 24 24 ILE CA C 58.774 0.3 1 84 24 24 ILE CB C 40.855 0.3 1 85 24 24 ILE N N 123.834 0.3 1 86 25 25 LEU H H 9.269 0.020 1 87 25 25 LEU CA C 52.905 0.3 1 88 25 25 LEU CB C 45.105 0.3 1 89 25 25 LEU N N 130.349 0.3 1 90 26 26 VAL H H 9.749 0.020 1 91 26 26 VAL CA C 61.457 0.3 1 92 26 26 VAL CB C 33.578 0.3 1 93 26 26 VAL N N 126.599 0.3 1 94 27 27 ASP H H 8.834 0.020 1 95 27 27 ASP CA C 51.470 0.3 1 96 27 27 ASP CB C 39.315 0.3 1 97 27 27 ASP N N 124.237 0.3 1 98 28 28 PHE H H 9.305 0.020 1 99 28 28 PHE CA C 58.296 0.3 1 100 28 28 PHE CB C 39.262 0.3 1 101 28 28 PHE N N 128.874 0.3 1 102 29 29 TRP H H 8.474 0.020 1 103 29 29 TRP CA C 54.817 0.3 1 104 29 29 TRP N N 120.269 0.3 1 105 30 30 ALA H H 6.911 0.020 1 106 30 30 ALA CA C 51.258 0.3 1 107 30 30 ALA CB C 21.891 0.3 1 108 30 30 ALA N N 116.519 0.3 1 109 31 31 GLU H H 9.107 0.020 1 110 31 31 GLU CA C 58.907 0.3 1 111 31 31 GLU CB C 29.859 0.3 1 112 31 31 GLU N N 120.868 0.3 1 113 32 32 TRP H H 6.569 0.020 1 114 32 32 TRP CA C 54.153 0.3 1 115 32 32 TRP CB C 28.744 0.3 1 116 32 32 TRP N N 110.471 0.3 1 117 33 33 SER H H 6.666 0.020 1 118 33 33 SER CA C 55.507 0.3 1 119 33 33 SER CB C 61.749 0.3 1 120 33 33 SER N N 115.223 0.3 1 121 34 34 GLY H H 9.592 0.020 1 122 34 34 GLY CA C 48.496 0.3 1 123 34 34 GLY N N 120.378 0.3 1 124 36 36 SER H H 7.762 0.020 1 125 36 36 SER CA C 62.997 0.3 1 126 36 36 SER N N 112.890 0.3 1 127 37 37 LYS H H 7.868 0.020 1 128 37 37 LYS CA C 59.093 0.3 1 129 37 37 LYS CB C 31.347 0.3 1 130 37 37 LYS N N 123.575 0.3 1 131 38 38 MET H H 8.084 0.020 1 132 38 38 MET CA C 58.216 0.3 1 133 38 38 MET CB C 32.462 0.3 1 134 38 38 MET N N 118.578 0.3 1 135 39 39 ILE H H 7.179 0.020 1 136 39 39 ILE CA C 61.749 0.3 1 137 39 39 ILE CB C 39.315 0.3 1 138 39 39 ILE N N 108.455 0.3 1 139 40 40 ALA H H 7.212 0.020 1 140 40 40 ALA CA C 57.393 0.3 1 141 40 40 ALA CB C 15.029 0.3 1 142 40 40 ALA N N 125.562 0.3 1 143 42 42 ILE H H 6.579 0.020 1 144 42 42 ILE CA C 64.378 0.3 1 145 42 42 ILE CB C 37.827 0.3 1 146 42 42 ILE N N 116.692 0.3 1 147 43 43 LEU H H 7.923 0.020 1 148 43 43 LEU CA C 57.712 0.3 1 149 43 43 LEU CB C 40.754 0.3 1 150 43 43 LEU N N 119.629 0.3 1 151 44 44 ASP H H 7.281 0.020 1 152 44 44 ASP CA C 58.004 0.3 1 153 44 44 ASP CB C 40.430 0.3 1 154 44 44 ASP N N 118.333 0.3 1 155 45 45 GLU H H 7.203 0.020 1 156 45 45 GLU CA C 59.358 0.3 1 157 45 45 GLU CB C 29.381 0.3 1 158 45 45 GLU N N 118.045 0.3 1 159 47 47 ALA H H 8.608 0.020 1 160 47 47 ALA CA C 55.082 0.3 1 161 47 47 ALA CB C 18.014 0.3 1 162 47 47 ALA N N 122.221 0.3 1 163 48 48 ASP H H 7.096 0.020 1 164 48 48 ASP CA C 56.942 0.3 1 165 48 48 ASP CB C 41.121 0.3 1 166 48 48 ASP N N 114.964 0.3 1 167 49 49 GLU H H 8.552 0.020 1 168 49 49 GLU CA C 59.173 0.3 1 169 49 49 GLU CB C 30.019 0.3 1 170 49 49 GLU N N 120.568 0.3 1 171 50 50 TYR H H 8.765 0.020 1 172 50 50 TYR CA C 58.243 0.3 1 173 50 50 TYR CB C 37.031 0.3 1 174 50 50 TYR N N 115.367 0.3 1 175 51 51 GLN H H 7.087 0.020 1 176 51 51 GLN CA C 58.482 0.3 1 177 51 51 GLN CB C 28.585 0.3 1 178 51 51 GLN N N 121.386 0.3 1 179 52 52 GLY H H 9.287 0.020 1 180 52 52 GLY CA C 45.548 0.3 1 181 52 52 GLY N N 115.568 0.3 1 182 53 53 LYS H H 8.215 0.020 1 183 53 53 LYS CA C 56.410 0.3 1 184 53 53 LYS CB C 34.971 0.3 1 185 53 53 LYS N N 117.815 0.3 1 186 54 54 LEU H H 7.849 0.020 1 187 54 54 LEU CA C 54.312 0.3 1 188 54 54 LEU CB C 47.070 0.3 1 189 54 54 LEU N N 119.276 0.3 1 190 55 55 THR H H 8.095 0.020 1 191 55 55 THR CA C 61.961 0.3 1 192 55 55 THR CB C 70.390 0.3 1 193 55 55 THR N N 123.120 0.3 1 194 56 56 VAL H H 9.962 0.020 1 195 56 56 VAL CA C 61.908 0.3 1 196 56 56 VAL CB C 32.462 0.3 1 197 56 56 VAL N N 129.730 0.3 1 198 57 57 ALA H H 9.315 0.020 1 199 57 57 ALA CA C 49.399 0.3 1 200 57 57 ALA CB C 23.804 0.3 1 201 57 57 ALA N N 129.392 0.3 1 202 58 58 LYS H H 8.658 0.020 1 203 58 58 LYS CA C 55.003 0.3 1 204 58 58 LYS CB C 37.296 0.3 1 205 58 58 LYS N N 118.160 0.3 1 206 59 59 LEU H H 8.963 0.020 1 207 59 59 LEU CA C 54.073 0.3 1 208 59 59 LEU CB C 44.414 0.3 1 209 59 59 LEU N N 123.604 0.3 1 210 60 60 ASN H H 8.973 0.020 1 211 60 60 ASN CA C 51.948 0.3 1 212 60 60 ASN CB C 38.146 0.3 1 213 60 60 ASN N N 126.282 0.3 1 214 61 61 ILE H H 8.500 0.020 1 215 61 61 ILE CA C 63.509 0.3 1 216 61 61 ILE CB C 37.915 0.3 1 217 61 61 ILE N N 122.522 0.3 1 218 62 62 ASP H H 7.683 0.020 1 219 62 62 ASP CA C 56.525 0.3 1 220 62 62 ASP CB C 40.596 0.3 1 221 62 62 ASP N N 121.501 0.3 1 222 63 63 GLN H H 7.215 0.020 1 223 63 63 GLN CA C 56.145 0.3 1 224 63 63 GLN CB C 30.284 0.3 1 225 63 63 GLN N N 115.981 0.3 1 226 64 64 ASN H H 7.327 0.020 1 227 64 64 ASN CA C 51.709 0.3 1 228 64 64 ASN CB C 40.962 0.3 1 229 64 64 ASN N N 116.173 0.3 1 230 66 66 GLY H H 10.267 0.020 1 231 66 66 GLY CA C 46.291 0.3 1 232 66 66 GLY N N 112.487 0.3 1 233 70 70 LYS H H 7.415 0.020 1 234 70 70 LYS CA C 58.695 0.3 1 235 70 70 LYS CB C 31.825 0.3 1 236 70 70 LYS N N 116.605 0.3 1 237 71 71 TYR H H 7.323 0.020 1 238 71 71 TYR CA C 58.243 0.3 1 239 71 71 TYR CB C 39.474 0.3 1 240 71 71 TYR N N 114.532 0.3 1 241 72 72 GLY H H 7.489 0.020 1 242 72 72 GLY CA C 46.822 0.3 1 243 72 72 GLY N N 108.081 0.3 1 244 73 73 ILE H H 6.985 0.020 1 245 73 73 ILE CA C 61.218 0.3 1 246 73 73 ILE CB C 36.181 0.3 1 247 73 73 ILE N N 118.621 0.3 1 248 74 74 ARG H H 8.732 0.020 1 249 74 74 ARG CA C 55.720 0.3 1 250 74 74 ARG CB C 31.878 0.3 1 251 74 74 ARG N N 127.607 0.3 1 252 75 75 GLY H H 7.766 0.020 1 253 75 75 GLY CA C 44.698 0.3 1 254 75 75 GLY N N 108.340 0.3 1 255 76 76 ILE H H 8.407 0.020 1 256 76 76 ILE CA C 56.065 0.3 1 257 76 76 ILE CB C 40.005 0.3 1 258 76 76 ILE N N 118.278 0.3 1 259 78 78 THR H H 8.094 0.020 1 260 78 78 THR CA C 63.900 0.3 1 261 78 78 THR CB C 72.949 0.3 1 262 78 78 THR N N 116.116 0.3 1 263 79 79 LEU H H 9.324 0.020 1 264 79 79 LEU CA C 52.745 0.3 1 265 79 79 LEU CB C 43.033 0.3 1 266 79 79 LEU N N 126.829 0.3 1 267 80 80 LEU H H 9.134 0.020 1 268 80 80 LEU CA C 53.276 0.3 1 269 80 80 LEU CB C 45.795 0.3 1 270 80 80 LEU N N 121.703 0.3 1 271 81 81 LEU H H 8.829 0.020 1 272 81 81 LEU CA C 53.144 0.3 1 273 81 81 LEU CB C 44.308 0.3 1 274 81 81 LEU N N 125.159 0.3 1 275 82 82 PHE H H 9.978 0.020 1 276 82 82 PHE CA C 57.287 0.3 1 277 82 82 PHE CB C 41.918 0.3 1 278 82 82 PHE N N 128.343 0.3 1 279 83 83 LYS H H 8.769 0.020 1 280 83 83 LYS CA C 56.251 0.3 1 281 83 83 LYS CB C 36.181 0.3 1 282 83 83 LYS N N 116.893 0.3 1 283 84 84 ASN H H 9.449 0.020 1 284 84 84 ASN CA C 54.312 0.3 1 285 84 84 ASN CB C 37.456 0.3 1 286 84 84 ASN N N 124.179 0.3 1 287 85 85 GLY H H 9.647 0.020 1 288 85 85 GLY CA C 46.397 0.3 1 289 85 85 GLY N N 104.365 0.3 1 290 86 86 GLU H H 7.842 0.020 1 291 86 86 GLU CA C 53.967 0.3 1 292 86 86 GLU CB C 33.100 0.3 1 293 86 86 GLU N N 118.620 0.3 1 294 87 87 VAL H H 8.829 0.020 1 295 87 87 VAL CA C 64.378 0.3 1 296 87 87 VAL CB C 31.506 0.3 1 297 87 87 VAL N N 122.826 0.3 1 298 88 88 ALA H H 9.707 0.020 1 299 88 88 ALA CA C 52.506 0.3 1 300 88 88 ALA CB C 20.245 0.3 1 301 88 88 ALA N N 133.108 0.3 1 302 89 89 ALA H H 7.660 0.020 1 303 89 89 ALA CA C 52.426 0.3 1 304 89 89 ALA CB C 22.210 0.3 1 305 89 89 ALA N N 117.412 0.3 1 306 90 90 THR H H 8.524 0.020 1 307 90 90 THR CA C 61.829 0.3 1 308 90 90 THR CB C 72.365 0.3 1 309 90 90 THR N N 115.424 0.3 1 310 91 91 LYS H H 9.070 0.020 1 311 91 91 LYS CA C 54.392 0.3 1 312 91 91 LYS CB C 34.640 0.3 1 313 91 91 LYS N N 126.397 0.3 1 314 92 92 VAL H H 8.649 0.020 1 315 92 92 VAL CA C 61.855 0.3 1 316 92 92 VAL CB C 33.656 0.3 1 317 92 92 VAL N N 126.023 0.3 1 318 93 93 GLY H H 8.390 0.020 1 319 93 93 GLY CA C 43.688 0.3 1 320 93 93 GLY N N 114.359 0.3 1 321 94 94 ALA H H 8.205 0.020 1 322 94 94 ALA CA C 52.639 0.3 1 323 94 94 ALA CB C 19.129 0.3 1 324 94 94 ALA N N 117.613 0.3 1 325 95 95 LEU H H 6.680 0.020 1 326 95 95 LEU CA C 54.233 0.3 1 327 95 95 LEU CB C 43.724 0.3 1 328 95 95 LEU N N 119.485 0.3 1 329 96 96 SER H H 8.464 0.020 1 330 96 96 SER CA C 56.357 0.3 1 331 96 96 SER CB C 65.875 0.3 1 332 96 96 SER N N 114.676 0.3 1 333 97 97 LYS H H 9.347 0.020 1 334 97 97 LYS CA C 60.846 0.3 1 335 97 97 LYS CB C 32.197 0.3 1 336 97 97 LYS N N 121.472 0.3 1 337 98 98 GLY H H 8.811 0.020 1 338 98 98 GLY CA C 47.035 0.3 1 339 98 98 GLY N N 105.431 0.3 1 340 99 99 GLN H H 7.743 0.020 1 341 99 99 GLN CA C 58.402 0.3 1 342 99 99 GLN CB C 29.275 0.3 1 343 99 99 GLN N N 120.896 0.3 1 344 100 100 LEU H H 8.598 0.020 1 345 100 100 LEU CA C 58.084 0.3 1 346 100 100 LEU CB C 40.802 0.3 1 347 100 100 LEU N N 123.604 0.3 1 348 101 101 LYS H H 8.755 0.020 1 349 101 101 LYS CA C 60.766 0.3 1 350 101 101 LYS CB C 31.187 0.3 1 351 101 101 LYS N N 119.658 0.3 1 352 102 102 GLU H H 7.822 0.020 1 353 102 102 GLU CA C 59.730 0.3 1 354 102 102 GLU CB C 29.700 0.3 1 355 102 102 GLU N N 117.728 0.3 1 356 103 103 PHE H H 7.655 0.020 1 357 103 103 PHE CA C 59.916 0.3 1 358 103 103 PHE CB C 38.890 0.3 1 359 103 103 PHE N N 120.176 0.3 1 360 104 104 LEU H H 8.628 0.020 1 361 104 104 LEU CA C 57.712 0.3 1 362 104 104 LEU CB C 40.855 0.3 1 363 104 104 LEU N N 121.000 0.3 1 364 105 105 ASP H H 9.245 0.020 1 365 105 105 ASP CA C 57.473 0.3 1 366 105 105 ASP CB C 39.102 0.3 1 367 105 105 ASP N N 120.176 0.3 1 368 106 106 ALA H H 7.595 0.020 1 369 106 106 ALA CA C 54.100 0.3 1 370 106 106 ALA CB C 18.704 0.3 1 371 106 106 ALA N N 118.736 0.3 1 372 107 107 ASN H H 7.226 0.020 1 373 107 107 ASN CA C 54.843 0.3 1 374 107 107 ASN CB C 41.705 0.3 1 375 107 107 ASN N N 112.948 0.3 1 376 108 108 LEU H H 8.061 0.020 1 377 108 108 LEU CA C 55.454 0.3 1 378 108 108 LEU CB C 41.971 0.3 1 379 108 108 LEU N N 120.437 0.3 1 380 109 109 ALA H H 7.762 0.020 1 381 109 109 ALA CA C 52.851 0.3 1 382 109 109 ALA CB C 19.023 0.3 1 383 109 109 ALA N N 122.711 0.3 1 384 110 110 GLY H H 8.275 0.020 1 385 110 110 GLY CA C 45.229 0.3 1 386 110 110 GLY N N 108.081 0.3 1 387 111 111 SER H H 8.343 0.020 1 388 111 111 SER CA C 58.562 0.3 1 389 111 111 SER CB C 63.900 0.3 1 390 111 111 SER N N 115.623 0.3 1 391 112 112 GLY H H 8.543 0.020 1 392 112 112 GLY CA C 45.388 0.3 1 393 112 112 GLY N N 111.018 0.3 1 394 113 113 SER H H 8.358 0.020 1 395 113 113 SER CA C 58.557 0.3 1 396 113 113 SER CB C 63.836 0.3 1 397 113 113 SER N N 115.742 0.3 1 398 114 114 GLY H H 8.574 0.020 1 399 114 114 GLY CA C 45.378 0.3 1 400 114 114 GLY N N 111.054 0.3 1 401 115 115 GLU H H 8.284 0.020 1 402 115 115 GLU CA C 56.596 0.3 1 403 115 115 GLU CB C 30.190 0.3 1 404 115 115 GLU N N 120.682 0.3 1 405 116 116 ARG H H 8.421 0.020 1 406 116 116 ARG CA C 56.092 0.3 1 407 116 116 ARG CB C 30.444 0.3 1 408 116 116 ARG N N 122.108 0.3 1 409 117 117 GLN H H 8.427 0.020 1 410 117 117 GLN CA C 55.985 0.3 1 411 117 117 GLN CB C 29.381 0.3 1 412 117 117 GLN N N 121.188 0.3 1 413 118 118 HIS H H 8.589 0.020 1 414 118 118 HIS CA C 55.587 0.3 1 415 118 118 HIS CB C 29.063 0.3 1 416 118 118 HIS N N 119.860 0.3 1 417 119 119 MET H H 8.431 0.020 1 418 119 119 MET CA C 55.348 0.3 1 419 119 119 MET CB C 33.047 0.3 1 420 119 119 MET N N 122.322 0.3 1 421 120 120 ASP H H 8.498 0.020 1 422 120 120 ASP CA C 54.312 0.3 1 423 120 120 ASP CB C 41.227 0.3 1 424 120 120 ASP N N 121.807 0.3 1 425 121 121 SER H H 8.246 0.020 1 426 121 121 SER CA C 56.198 0.3 1 427 121 121 SER CB C 63.484 0.3 1 428 121 121 SER N N 116.739 0.3 1 429 123 123 ASP H H 8.373 0.020 1 430 123 123 ASP CA C 54.206 0.3 1 431 123 123 ASP CB C 40.855 0.3 1 432 123 123 ASP N N 120.068 0.3 1 433 124 124 LEU H H 8.248 0.020 1 434 124 124 LEU CA C 55.215 0.3 1 435 124 124 LEU CB C 42.174 0.3 1 436 124 124 LEU N N 123.190 0.3 1 437 125 125 GLY H H 8.501 0.020 1 438 125 125 GLY CA C 45.494 0.3 1 439 125 125 GLY N N 109.348 0.3 1 440 126 126 THR H H 8.099 0.020 1 441 126 126 THR CA C 61.563 0.3 1 442 126 126 THR CB C 69.965 0.3 1 443 126 126 THR N N 112.746 0.3 1 444 127 127 ASP H H 8.509 0.020 1 445 127 127 ASP CA C 54.551 0.3 1 446 127 127 ASP CB C 41.068 0.3 1 447 127 127 ASP N N 122.408 0.3 1 448 128 128 ASP H H 8.288 0.020 1 449 128 128 ASP CA C 54.595 0.3 1 450 128 128 ASP N N 120.422 0.3 1 451 130 130 ASP H H 8.307 0.020 1 452 130 130 ASP CA C 55.052 0.3 1 453 130 130 ASP CB C 40.544 0.3 1 454 130 130 ASP N N 120.353 0.3 1 455 131 131 LYS H H 8.151 0.020 1 456 131 131 LYS CA C 56.835 0.3 1 457 131 131 LYS CB C 32.409 0.3 1 458 131 131 LYS N N 121.174 0.3 1 459 132 132 ALA H H 8.147 0.020 1 460 132 132 ALA CA C 53.144 0.3 1 461 132 132 ALA CB C 18.811 0.3 1 462 132 132 ALA N N 123.541 0.3 1 463 133 133 MET H H 8.162 0.020 1 464 133 133 MET CA C 55.746 0.3 1 465 133 133 MET CB C 32.622 0.3 1 466 133 133 MET N N 118.537 0.3 1 467 134 134 ALA H H 8.168 0.020 1 468 134 134 ALA CA C 52.931 0.3 1 469 134 134 ALA CB C 19.023 0.3 1 470 134 134 ALA N N 124.404 0.3 1 471 135 135 THR H H 8.049 0.020 1 472 135 135 THR CA C 62.068 0.3 1 473 135 135 THR CB C 69.646 0.3 1 474 135 135 THR N N 113.138 0.3 1 475 136 136 LEU H H 8.126 0.020 1 476 136 136 LEU CA C 55.507 0.3 1 477 136 136 LEU CB C 42.396 0.3 1 478 136 136 LEU N N 124.168 0.3 1 479 138 138 LYS H H 8.211 0.020 1 480 138 138 LYS CA C 56.012 0.3 1 481 138 138 LYS CB C 32.940 0.3 1 482 138 138 LYS N N 122.175 0.3 1 483 139 139 LEU H H 8.279 0.020 1 484 139 139 LEU CA C 55.215 0.3 1 485 139 139 LEU CB C 42.130 0.3 1 486 139 139 LEU N N 124.287 0.3 1 487 140 140 MET H H 8.300 0.020 1 488 140 140 MET CA C 55.257 0.3 1 489 140 140 MET CB C 29.554 0.3 1 490 140 140 MET N N 119.359 0.3 1 491 143 143 PHE H H 8.387 0.020 1 492 143 143 PHE CA C 58.004 0.3 1 493 143 143 PHE CB C 39.262 0.3 1 494 143 143 PHE N N 119.900 0.3 1 495 144 144 GLU H H 8.299 0.020 1 496 144 144 GLU CA C 56.331 0.3 1 497 144 144 GLU CB C 30.550 0.3 1 498 144 144 GLU N N 123.135 0.3 1 499 145 145 SER H H 8.312 0.020 1 500 145 145 SER CA C 58.296 0.3 1 501 145 145 SER CB C 63.697 0.3 1 502 145 145 SER N N 117.025 0.3 1 503 146 146 LEU H H 8.312 0.020 1 504 146 146 LEU CA C 55.560 0.3 1 505 146 146 LEU CB C 42.183 0.3 1 506 146 146 LEU N N 124.207 0.3 1 507 148 148 SER H H 8.189 0.020 1 508 148 148 SER CA C 58.535 0.3 1 509 148 148 SER CB C 63.625 0.3 1 510 148 148 SER N N 116.212 0.3 1 511 149 149 PHE H H 8.224 0.020 1 512 149 149 PHE CA C 58.391 0.3 1 513 149 149 PHE CB C 39.209 0.3 1 514 149 149 PHE N N 121.955 0.3 1 515 150 150 GLN H H 8.218 0.020 1 516 150 150 GLN CA C 56.198 0.3 1 517 150 150 GLN CB C 29.187 0.3 1 518 150 150 GLN N N 121.255 0.3 1 519 153 153 GLN H H 8.374 0.020 1 520 153 153 GLN CA C 56.157 0.3 1 521 153 153 GLN CB C 29.240 0.3 1 522 153 153 GLN N N 121.081 0.3 1 523 168 168 GLN H H 8.409 0.020 1 524 168 168 GLN CA C 55.401 0.3 1 525 168 168 GLN CB C 29.488 0.3 1 526 168 168 GLN N N 120.382 0.3 1 527 169 169 LEU H H 8.358 0.020 1 528 169 169 LEU CA C 52.984 0.3 1 529 169 169 LEU CB C 41.546 0.3 1 530 169 169 LEU N N 125.475 0.3 1 531 171 171 GLN H H 8.445 0.020 1 532 171 171 GLN CA C 55.560 0.3 1 533 171 171 GLN N N 120.316 0.3 1 534 175 175 GLN H H 8.514 0.020 1 535 175 175 GLN CA C 55.605 0.3 1 536 175 175 GLN CB C 29.713 0.3 1 537 175 175 GLN N N 119.011 0.3 1 538 176 176 ALA H H 8.302 0.020 1 539 176 176 ALA CA C 52.400 0.3 1 540 176 176 ALA CB C 19.342 0.3 1 541 176 176 ALA N N 126.195 0.3 1 542 177 177 GLN H H 8.010 0.020 1 543 177 177 GLN CA C 53.170 0.3 1 544 177 177 GLN CB C 29.913 0.3 1 545 177 177 GLN N N 118.053 0.3 1 546 179 179 LEU H H 8.281 0.020 1 547 179 179 LEU CA C 55.268 0.3 1 548 179 179 LEU CB C 42.343 0.3 1 549 179 179 LEU N N 122.928 0.3 1 550 180 180 LEU H H 7.873 0.020 1 551 180 180 LEU CA C 52.134 0.3 1 552 180 180 LEU CB C 43.529 0.3 1 553 180 180 LEU N N 122.020 0.3 1 554 182 182 GLN H H 8.197 0.020 1 555 182 182 GLN CA C 52.666 0.3 1 556 182 182 GLN CB C 30.072 0.3 1 557 182 182 GLN N N 119.123 0.3 1 558 184 184 GLN H H 8.714 0.020 1 559 184 184 GLN CA C 53.993 0.3 1 560 184 184 GLN CB C 28.956 0.3 1 561 184 184 GLN N N 121.588 0.3 1 562 195 195 GLY H H 8.349 0.020 1 563 195 195 GLY CA C 44.618 0.3 1 564 195 195 GLY N N 112.400 0.3 1 565 197 197 ALA H H 8.418 0.020 1 566 197 197 ALA CA C 52.347 0.3 1 567 197 197 ALA CB C 18.970 0.3 1 568 197 197 ALA N N 124.381 0.3 1 569 198 198 VAL H H 8.107 0.020 1 570 198 198 VAL CA C 61.961 0.3 1 571 198 198 VAL CB C 32.781 0.3 1 572 198 198 VAL N N 119.761 0.3 1 573 199 199 ALA H H 8.372 0.020 1 574 199 199 ALA CA C 52.320 0.3 1 575 199 199 ALA CB C 19.289 0.3 1 576 199 199 ALA N N 127.895 0.3 1 577 200 200 GLU H H 8.330 0.020 1 578 200 200 GLU CA C 56.118 0.3 1 579 200 200 GLU CB C 30.550 0.3 1 580 200 200 GLU N N 120.575 0.3 1 581 201 201 GLU H H 8.455 0.020 1 582 201 201 GLU CA C 54.525 0.3 1 583 201 201 GLU CB C 29.700 0.3 1 584 201 201 GLU N N 124.093 0.3 1 585 203 203 LEU H H 8.250 0.020 1 586 203 203 LEU CA C 55.534 0.3 1 587 203 203 LEU CB C 42.130 0.3 1 588 203 203 LEU N N 120.674 0.3 1 589 204 204 HIS H H 8.328 0.020 1 590 204 204 HIS CA C 55.136 0.3 1 591 204 204 HIS CB C 29.275 0.3 1 592 204 204 HIS N N 118.522 0.3 1 593 205 205 ARG H H 8.234 0.020 1 594 205 205 ARG CA C 53.967 0.3 1 595 205 205 ARG CB C 30.019 0.3 1 596 205 205 ARG N N 122.993 0.3 1 stop_ save_