data_16965 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone NMR assignment of the globular domain of HET-s(1-227) prion protein. ; _BMRB_accession_number 16965 _BMRB_flat_file_name bmr16965.str _Entry_type original _Submission_date 2010-05-30 _Accession_date 2010-05-30 _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 Schuetz Anne . . 2 Greenwald Jason . . 3 Riek Roland . . 4 Bockmann Anja . . 5 Meier Beat H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 367 "15N chemical shifts" 188 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-08-19 update BMRB 'complete entry citation' 2010-06-30 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16964 'HET-s(1-227) solution state' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Protocols for the sequential solid-state NMR spectroscopic assignment of a uniformly labeled 25 kDa protein: HET-s(1-227).' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20572250 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schuetz Anne . . 2 Wasmer Christian . . 3 Habenstein Birgit . . 4 Verel Rene . . 5 Greenwald Jason . . 6 Riek Roland . . 7 Bockmann Anja . . 8 Meier Beat H. . stop_ _Journal_abbreviation Chembiochem _Journal_name_full 'Chembiochem : a European journal of chemical biology' _Journal_volume 11 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1543 _Page_last 1551 _Year 2010 _Details . loop_ _Keyword 'prion proteins' 'sequence determination' 'solid-state NMR' spectroscopy 'structure determination' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name HET-s(1-227) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label HET-s(1-227) $HET-s stop_ _System_molecular_weight 25470 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 HET-s(1-227) stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HET-s _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HET-s _Molecular_mass 25470 _Mol_thiol_state 'all free' loop_ _Biological_function 'heterokaryon incompatibility' 'prion protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 229 _Mol_residue_sequence ; GSMSEPFGIVAGALNVAGLF NNCVDCFEYVQLGRPFGRDY ERCQLRLDIAKARLSRWGEA VKINDDPRFHSSAPTDKSVQ LAKSIVEEILLLFESAQKTS KRYELVADQQDLVVFEDKDM KPIGRALHRRLNDLVSRRQK QTSLAKKTAWALYDGKSLEK IVDQVARFVDELEKAFPIEA VCHKLAEIEIEEVEDEASLT ILKDAAGGIDAAMSDAAAQK IDAIVGRNS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -1 GLY 2 0 SER 3 1 MET 4 2 SER 5 3 GLU 6 4 PRO 7 5 PHE 8 6 GLY 9 7 ILE 10 8 VAL 11 9 ALA 12 10 GLY 13 11 ALA 14 12 LEU 15 13 ASN 16 14 VAL 17 15 ALA 18 16 GLY 19 17 LEU 20 18 PHE 21 19 ASN 22 20 ASN 23 21 CYS 24 22 VAL 25 23 ASP 26 24 CYS 27 25 PHE 28 26 GLU 29 27 TYR 30 28 VAL 31 29 GLN 32 30 LEU 33 31 GLY 34 32 ARG 35 33 PRO 36 34 PHE 37 35 GLY 38 36 ARG 39 37 ASP 40 38 TYR 41 39 GLU 42 40 ARG 43 41 CYS 44 42 GLN 45 43 LEU 46 44 ARG 47 45 LEU 48 46 ASP 49 47 ILE 50 48 ALA 51 49 LYS 52 50 ALA 53 51 ARG 54 52 LEU 55 53 SER 56 54 ARG 57 55 TRP 58 56 GLY 59 57 GLU 60 58 ALA 61 59 VAL 62 60 LYS 63 61 ILE 64 62 ASN 65 63 ASP 66 64 ASP 67 65 PRO 68 66 ARG 69 67 PHE 70 68 HIS 71 69 SER 72 70 SER 73 71 ALA 74 72 PRO 75 73 THR 76 74 ASP 77 75 LYS 78 76 SER 79 77 VAL 80 78 GLN 81 79 LEU 82 80 ALA 83 81 LYS 84 82 SER 85 83 ILE 86 84 VAL 87 85 GLU 88 86 GLU 89 87 ILE 90 88 LEU 91 89 LEU 92 90 LEU 93 91 PHE 94 92 GLU 95 93 SER 96 94 ALA 97 95 GLN 98 96 LYS 99 97 THR 100 98 SER 101 99 LYS 102 100 ARG 103 101 TYR 104 102 GLU 105 103 LEU 106 104 VAL 107 105 ALA 108 106 ASP 109 107 GLN 110 108 GLN 111 109 ASP 112 110 LEU 113 111 VAL 114 112 VAL 115 113 PHE 116 114 GLU 117 115 ASP 118 116 LYS 119 117 ASP 120 118 MET 121 119 LYS 122 120 PRO 123 121 ILE 124 122 GLY 125 123 ARG 126 124 ALA 127 125 LEU 128 126 HIS 129 127 ARG 130 128 ARG 131 129 LEU 132 130 ASN 133 131 ASP 134 132 LEU 135 133 VAL 136 134 SER 137 135 ARG 138 136 ARG 139 137 GLN 140 138 LYS 141 139 GLN 142 140 THR 143 141 SER 144 142 LEU 145 143 ALA 146 144 LYS 147 145 LYS 148 146 THR 149 147 ALA 150 148 TRP 151 149 ALA 152 150 LEU 153 151 TYR 154 152 ASP 155 153 GLY 156 154 LYS 157 155 SER 158 156 LEU 159 157 GLU 160 158 LYS 161 159 ILE 162 160 VAL 163 161 ASP 164 162 GLN 165 163 VAL 166 164 ALA 167 165 ARG 168 166 PHE 169 167 VAL 170 168 ASP 171 169 GLU 172 170 LEU 173 171 GLU 174 172 LYS 175 173 ALA 176 174 PHE 177 175 PRO 178 176 ILE 179 177 GLU 180 178 ALA 181 179 VAL 182 180 CYS 183 181 HIS 184 182 LYS 185 183 LEU 186 184 ALA 187 185 GLU 188 186 ILE 189 187 GLU 190 188 ILE 191 189 GLU 192 190 GLU 193 191 VAL 194 192 GLU 195 193 ASP 196 194 GLU 197 195 ALA 198 196 SER 199 197 LEU 200 198 THR 201 199 ILE 202 200 LEU 203 201 LYS 204 202 ASP 205 203 ALA 206 204 ALA 207 205 GLY 208 206 GLY 209 207 ILE 210 208 ASP 211 209 ALA 212 210 ALA 213 211 MET 214 212 SER 215 213 ASP 216 214 ALA 217 215 ALA 218 216 ALA 219 217 GLN 220 218 LYS 221 219 ILE 222 220 ASP 223 221 ALA 224 222 ILE 225 223 VAL 226 224 GLY 227 225 ARG 228 226 ASN 229 227 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 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 BMRB 16964 HET-s 100.00 229 100.00 100.00 1.71e-164 PDB 2WVN "Structure Of The Het-S N-Terminal Domain" 100.00 229 99.56 99.56 1.51e-163 GB AAB19707 "s gene 30 kDa polypeptide [Podospora anserina=fungus, Peptide, 289 aa]" 99.13 289 99.56 99.56 1.50e-161 GB AAB94631 "small s protein [Podospora anserina]" 99.13 289 99.56 99.56 1.25e-161 PRF 1718317A "vegetative incompatibility gene s" 99.13 289 99.12 99.12 3.81e-160 SP Q03689 "RecName: Full=Heterokaryon incompatibility protein s; AltName: Full=Small s protein; AltName: Full=Vegetative incompatibility p" 99.13 289 99.56 99.56 1.25e-161 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HET-s ascomycetes 5145 Eukaryota Fungi Podospora anserina 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 $HET-s 'recombinant technology' . Escherichia coli BL21 pET 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 $HET-s 1 mM '[U-100% 13C; U-100% 15N; U-99% 2H]' DTT 2 mM 'natural abundance' 'potassium phosphate' 50 mM 'natural abundance' 'sodium chloride' 20 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.115 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 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_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _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' 70 5 mM pH 7 0.1 pH pressure 1 . atm temperature 297 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.00 . 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 HNCA' '3D HNCACB' '3D HNCO' 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 HET-s(1-227) _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 4 6 PRO CA C 63.3 0.2 1 2 4 6 PRO CB C 31.4 0.2 1 3 5 7 PHE CA C 58.3 0.2 1 4 5 7 PHE CB C 38.3 0.2 1 5 5 7 PHE N N 119.2 0.2 1 6 6 8 GLY CA C 45.5 0.2 1 7 6 8 GLY N N 109.1 0.2 1 8 7 9 ILE CA C 61.3 0.2 1 9 7 9 ILE CB C 38.0 0.2 1 10 7 9 ILE N N 121.0 0.2 1 11 8 10 VAL CA C 61.9 0.2 1 12 8 10 VAL CB C 32.0 0.2 1 13 8 10 VAL N N 125.0 0.2 1 14 9 11 ALA CA C 53.4 0.2 1 15 9 11 ALA CB C 18.5 0.2 1 16 9 11 ALA N N 128.7 0.2 1 17 10 12 GLY CA C 45.5 0.2 1 18 10 12 GLY N N 108.4 0.2 1 19 11 13 ALA CA C 52.4 0.2 1 20 11 13 ALA CB C 19.3 0.2 1 21 11 13 ALA N N 123.0 0.2 1 22 12 14 LEU CA C 54.5 0.2 1 23 12 14 LEU CB C 43.2 0.2 1 24 12 14 LEU N N 120.4 0.2 1 25 13 15 ASN CA C 51.0 0.2 1 26 13 15 ASN CB C 38.6 0.2 1 27 13 15 ASN N N 116.5 0.2 1 28 14 16 VAL CA C 67.9 0.2 1 29 14 16 VAL CB C 30.8 0.2 1 30 14 16 VAL N N 117.0 0.2 1 31 15 17 ALA CA C 55.8 0.2 1 32 15 17 ALA CB C 17.5 0.2 1 33 15 17 ALA N N 121.4 0.2 1 34 16 18 GLY CA C 47.4 0.2 1 35 16 18 GLY N N 107.3 0.2 1 36 17 19 LEU CA C 58.7 0.2 1 37 17 19 LEU CB C 42.4 0.2 1 38 17 19 LEU N N 126.3 0.2 1 39 18 20 PHE CA C 62.4 0.2 1 40 18 20 PHE CB C 39.1 0.2 1 41 18 20 PHE N N 120.6 0.2 1 42 19 21 ASN CA C 56.8 0.2 1 43 19 21 ASN CB C 38.3 0.2 1 44 19 21 ASN N N 118.9 0.2 1 45 20 22 ASN CA C 57.9 0.2 1 46 20 22 ASN CB C 39.9 0.2 1 47 20 22 ASN N N 117.9 0.2 1 48 21 23 CYS CA C 63.6 0.2 1 49 21 23 CYS CB C 26.7 0.2 1 50 21 23 CYS N N 121.9 0.2 1 51 22 24 VAL CA C 66.9 0.2 1 52 22 24 VAL N N 118.0 0.2 1 53 23 25 ASP CA C 56.7 0.2 1 54 23 25 ASP CB C 43.7 0.2 1 55 23 25 ASP N N 117.4 0.2 1 56 24 26 CYS CA C 65.2 0.2 1 57 24 26 CYS CB C 26.2 0.2 1 58 24 26 CYS N N 115.0 0.2 1 59 25 27 PHE CA C 62.2 0.2 1 60 25 27 PHE CB C 39.7 0.2 1 61 25 27 PHE N N 114.2 0.2 1 62 26 28 GLU CA C 56.9 0.2 1 63 26 28 GLU CB C 28.4 0.2 1 64 26 28 GLU N N 116.2 0.2 1 65 27 29 TYR CA C 59.0 0.2 1 66 27 29 TYR CB C 39.4 0.2 1 67 27 29 TYR N N 116.3 0.2 1 68 28 30 VAL CA C 61.5 0.2 1 69 28 30 VAL CB C 31.8 0.2 1 70 28 30 VAL N N 117.8 0.2 1 71 29 31 GLN CA C 53.4 0.2 1 72 29 31 GLN CB C 31.0 0.2 1 73 29 31 GLN N N 127.6 0.2 1 74 30 32 LEU CA C 54.7 0.2 1 75 30 32 LEU CB C 40.4 0.2 1 76 30 32 LEU N N 121.8 0.2 1 77 31 33 GLY CA C 43.8 0.2 1 78 31 33 GLY N N 107.2 0.2 1 79 32 34 ARG CA C 59.5 0.2 1 80 32 34 ARG CB C 28.9 0.2 1 81 32 34 ARG N N 120.1 0.2 1 82 33 35 PRO CB C 30.9 0.2 1 83 34 36 PHE CA C 62.8 0.2 1 84 34 36 PHE CB C 38.9 0.2 1 85 34 36 PHE N N 114.1 0.2 1 86 35 37 GLY CA C 47.3 0.2 1 87 35 37 GLY N N 107.1 0.2 1 88 36 38 ARG CA C 57.7 0.2 1 89 36 38 ARG N N 125.1 0.2 1 90 37 39 ASP CA C 54.9 0.2 1 91 37 39 ASP CB C 41.3 0.2 1 92 37 39 ASP N N 119.9 0.2 1 93 38 40 TYR CA C 61.1 0.2 1 94 38 40 TYR CB C 36.8 0.2 1 95 38 40 TYR N N 120.5 0.2 1 96 39 41 GLU CA C 60.4 0.2 1 97 39 41 GLU CB C 30.0 0.2 1 98 39 41 GLU N N 118.7 0.2 1 99 40 42 ARG CA C 59.3 0.2 1 100 40 42 ARG CB C 29.7 0.2 1 101 40 42 ARG N N 117.3 0.2 1 102 41 43 CYS CA C 65.4 0.2 1 103 41 43 CYS CB C 27.1 0.2 1 104 41 43 CYS N N 115.6 0.2 1 105 42 44 GLN CA C 57.7 0.2 1 106 42 44 GLN CB C 28.0 0.2 1 107 42 44 GLN N N 119.6 0.2 1 108 43 45 LEU CA C 57.6 0.2 1 109 43 45 LEU CB C 40.9 0.2 1 110 43 45 LEU N N 119.0 0.2 1 111 44 46 ARG CA C 60.6 0.2 1 112 44 46 ARG CB C 29.3 0.2 1 113 44 46 ARG N N 118.7 0.2 1 114 45 47 LEU CA C 58.6 0.2 1 115 45 47 LEU CB C 41.5 0.2 1 116 45 47 LEU N N 119.9 0.2 1 117 46 48 ASP CA C 56.6 0.2 1 118 46 48 ASP CB C 40.0 0.2 1 119 46 48 ASP N N 118.1 0.2 1 120 47 49 ILE CA C 65.0 0.2 1 121 47 49 ILE N N 122.6 0.2 1 122 48 50 ALA CA C 55.9 0.2 1 123 48 50 ALA CB C 18.3 0.2 1 124 48 50 ALA N N 124.0 0.2 1 125 55 57 TRP CA C 63.0 0.2 1 126 55 57 TRP CB C 27.0 0.2 1 127 56 58 GLY CA C 46.5 0.2 1 128 56 58 GLY N N 102.7 0.2 1 129 57 59 GLU CA C 58.3 0.2 1 130 57 59 GLU CB C 28.7 0.2 1 131 57 59 GLU N N 121.4 0.2 1 132 58 60 ALA CA C 55.0 0.2 1 133 58 60 ALA CB C 20.0 0.2 1 134 58 60 ALA N N 123.6 0.2 1 135 59 61 VAL CA C 60.6 0.2 1 136 59 61 VAL N N 108.5 0.2 1 137 60 62 LYS CA C 56.1 0.2 1 138 60 62 LYS CB C 28.5 0.2 1 139 60 62 LYS N N 118.2 0.2 1 140 61 63 ILE CA C 62.7 0.2 1 141 61 63 ILE CB C 37.9 0.2 1 142 61 63 ILE N N 119.5 0.2 1 143 62 64 ASN CA C 55.2 0.2 1 144 62 64 ASN CB C 39.1 0.2 1 145 62 64 ASN N N 114.2 0.2 1 146 63 65 ASP CA C 58.4 0.2 1 147 63 65 ASP CB C 40.4 0.2 1 148 63 65 ASP N N 116.9 0.2 1 149 64 66 ASP CA C 51.8 0.2 1 150 64 66 ASP CB C 41.4 0.2 1 151 64 66 ASP N N 123.1 0.2 1 152 65 67 PRO CA C 64.0 0.2 1 153 65 67 PRO CB C 31.9 0.2 1 154 66 68 ARG CA C 58.7 0.2 1 155 66 68 ARG CB C 29.6 0.2 1 156 66 68 ARG N N 120.5 0.2 1 157 67 69 PHE CA C 58.8 0.2 1 158 67 69 PHE CB C 39.2 0.2 1 159 67 69 PHE N N 113.6 0.2 1 160 68 70 HIS CA C 55.5 0.2 1 161 68 70 HIS CB C 30.5 0.2 1 162 68 70 HIS N N 119.4 0.2 1 163 69 71 SER CA C 56.5 0.2 1 164 69 71 SER CB C 64.8 0.2 1 165 69 71 SER N N 113.2 0.2 1 166 74 76 ASP CA C 54.1 0.2 1 167 74 76 ASP CB C 42.5 0.2 1 168 74 76 ASP N N 124.3 0.2 1 169 75 77 LYS CA C 60.3 0.2 1 170 75 77 LYS N N 127.9 0.2 1 171 76 78 SER CA C 62.4 0.2 1 172 76 78 SER CB C 61.4 0.2 1 173 76 78 SER N N 116.4 0.2 1 174 77 79 VAL CA C 66.5 0.2 1 175 77 79 VAL CB C 30.9 0.2 1 176 77 79 VAL N N 123.4 0.2 1 177 78 80 GLN CA C 59.9 0.2 1 178 78 80 GLN CB C 28.1 0.2 1 179 78 80 GLN N N 120.2 0.2 1 180 79 81 LEU CA C 58.7 0.2 1 181 79 81 LEU CB C 40.7 0.2 1 182 79 81 LEU N N 120.6 0.2 1 183 80 82 ALA CA C 55.2 0.2 1 184 80 82 ALA CB C 17.8 0.2 1 185 80 82 ALA N N 120.6 0.2 1 186 81 83 LYS CA C 60.1 0.2 1 187 81 83 LYS CB C 32.7 0.2 1 188 81 83 LYS N N 117.2 0.2 1 189 90 92 LEU CA C 58.1 0.2 1 190 90 92 LEU CB C 41.1 0.2 1 191 90 92 LEU N N 124.1 0.2 1 192 91 93 PHE CA C 62.7 0.2 1 193 91 93 PHE CB C 38.7 0.2 1 194 91 93 PHE N N 118.6 0.2 1 195 92 94 GLU CA C 59.7 0.2 1 196 92 94 GLU CB C 29.1 0.2 1 197 92 94 GLU N N 120.7 0.2 1 198 93 95 SER CA C 62.3 0.2 1 199 93 95 SER N N 114.8 0.2 1 200 94 96 ALA CA C 54.9 0.2 1 201 94 96 ALA CB C 18.7 0.2 1 202 94 96 ALA N N 124.4 0.2 1 203 95 97 GLN CA C 59.1 0.2 1 204 96 98 LYS CA C 59.3 0.2 1 205 96 98 LYS CB C 30.9 0.2 1 206 96 98 LYS N N 120.1 0.2 1 207 97 99 THR CA C 67.1 0.2 1 208 97 99 THR CB C 69.3 0.2 1 209 97 99 THR N N 117.4 0.2 1 210 98 100 SER CA C 62.9 0.2 1 211 98 100 SER N N 119.5 0.2 1 212 99 101 LYS CA C 58.2 0.2 1 213 99 101 LYS CB C 30.9 0.2 1 214 99 101 LYS N N 121.2 0.2 1 215 100 102 ARG CA C 60.2 0.2 1 216 100 102 ARG CB C 30.7 0.2 1 217 100 102 ARG N N 117.5 0.2 1 218 101 103 TYR CA C 61.2 0.2 1 219 101 103 TYR CB C 37.8 0.2 1 220 101 103 TYR N N 121.1 0.2 1 221 102 104 GLU CA C 58.8 0.2 1 222 102 104 GLU CB C 29.3 0.2 1 223 102 104 GLU N N 117.3 0.2 1 224 103 105 LEU CA C 57.2 0.2 1 225 103 105 LEU N N 116.5 0.2 1 226 104 106 VAL CA C 60.5 0.2 1 227 104 106 VAL N N 108.8 0.2 1 228 105 107 ALA CA C 52.0 0.2 1 229 105 107 ALA CB C 20.1 0.2 1 230 105 107 ALA N N 125.2 0.2 1 231 106 108 ASP CA C 54.3 0.2 1 232 106 108 ASP CB C 42.0 0.2 1 233 106 108 ASP N N 121.1 0.2 1 234 107 109 GLN CA C 58.8 0.2 1 235 107 109 GLN CB C 28.2 0.2 1 236 107 109 GLN N N 123.9 0.2 1 237 108 110 GLN CA C 57.9 0.2 1 238 108 110 GLN CB C 28.1 0.2 1 239 108 110 GLN N N 117.9 0.2 1 240 109 111 ASP CA C 55.8 0.2 1 241 109 111 ASP CB C 41.1 0.2 1 242 109 111 ASP N N 118.1 0.2 1 243 110 112 LEU CA C 54.7 0.2 1 244 110 112 LEU CB C 40.3 0.2 1 245 110 112 LEU N N 116.0 0.2 1 246 111 113 VAL CA C 62.3 0.2 1 247 111 113 VAL CB C 32.5 0.2 1 248 111 113 VAL N N 119.7 0.2 1 249 112 114 VAL CA C 59.5 0.2 1 250 112 114 VAL CB C 33.3 0.2 1 251 112 114 VAL N N 119.2 0.2 1 252 113 115 PHE CA C 58.9 0.2 1 253 113 115 PHE CB C 39.2 0.2 1 254 113 115 PHE N N 120.3 0.2 1 255 114 116 GLU CA C 54.4 0.2 1 256 114 116 GLU CB C 34.0 0.2 1 257 114 116 GLU N N 119.3 0.2 1 258 115 117 ASP CA C 57.7 0.2 1 259 115 117 ASP CB C 39.5 0.2 1 260 115 117 ASP N N 119.9 0.2 1 261 116 118 LYS CA C 57.9 0.2 1 262 116 118 LYS CB C 30.8 0.2 1 263 116 118 LYS N N 119.0 0.2 1 264 117 119 ASP CA C 55.9 0.2 1 265 117 119 ASP CB C 41.6 0.2 1 266 117 119 ASP N N 119.5 0.2 1 267 118 120 MET CA C 56.4 0.2 1 268 118 120 MET CB C 34.4 0.2 1 269 118 120 MET N N 118.5 0.2 1 270 119 121 LYS CA C 55.9 0.2 1 271 119 121 LYS CB C 29.8 0.2 1 272 119 121 LYS N N 123.5 0.2 1 273 120 122 PRO CA C 67.0 0.2 1 274 120 122 PRO CB C 32.0 0.2 1 275 121 123 ILE CA C 64.4 0.2 1 276 121 123 ILE CB C 36.5 0.2 1 277 121 123 ILE N N 117.6 0.2 1 278 122 124 GLY CA C 47.0 0.2 1 279 122 124 GLY N N 111.2 0.2 1 280 123 125 ARG CA C 59.6 0.2 1 281 123 125 ARG CB C 29.8 0.2 1 282 123 125 ARG N N 123.0 0.2 1 283 124 126 ALA CA C 54.8 0.2 1 284 124 126 ALA CB C 17.7 0.2 1 285 124 126 ALA N N 119.7 0.2 1 286 125 127 LEU CA C 57.8 0.2 1 287 125 127 LEU CB C 42.4 0.2 1 288 125 127 LEU N N 120.6 0.2 1 289 126 128 HIS CA C 58.3 0.2 1 290 126 128 HIS CB C 29.6 0.2 1 291 126 128 HIS N N 119.9 0.2 1 292 127 129 ARG CA C 59.2 0.2 1 293 127 129 ARG CB C 29.3 0.2 1 294 127 129 ARG N N 117.8 0.2 1 295 128 130 ARG CA C 59.3 0.2 1 296 128 130 ARG CB C 29.5 0.2 1 297 128 130 ARG N N 120.6 0.2 1 298 129 131 LEU CA C 57.8 0.2 1 299 129 131 LEU CB C 40.9 0.2 1 300 129 131 LEU N N 119.8 0.2 1 301 130 132 ASN CA C 56.2 0.2 1 302 130 132 ASN CB C 37.6 0.2 1 303 130 132 ASN N N 117.5 0.2 1 304 131 133 ASP CA C 57.5 0.2 1 305 131 133 ASP CB C 40.5 0.2 1 306 131 133 ASP N N 123.0 0.2 1 307 132 134 LEU CA C 58.1 0.2 1 308 132 134 LEU CB C 40.7 0.2 1 309 132 134 LEU N N 120.8 0.2 1 310 133 135 VAL CA C 66.5 0.2 1 311 133 135 VAL CB C 31.9 0.2 1 312 133 135 VAL N N 118.8 0.2 1 313 134 136 SER CA C 61.9 0.2 1 314 134 136 SER N N 116.8 0.2 1 315 135 137 ARG CA C 58.6 0.2 1 316 135 137 ARG CB C 29.8 0.2 1 317 135 137 ARG N N 118.9 0.2 1 318 136 138 ARG CA C 57.6 0.2 1 319 136 138 ARG CB C 31.5 0.2 1 320 136 138 ARG N N 117.6 0.2 1 321 137 139 GLN CA C 55.6 0.2 1 322 137 139 GLN CB C 31.0 0.2 1 323 137 139 GLN N N 119.3 0.2 1 324 138 140 LYS CA C 55.3 0.2 1 325 138 140 LYS CB C 32.3 0.2 1 326 138 140 LYS N N 122.6 0.2 1 327 139 141 GLN CA C 56.4 0.2 1 328 139 141 GLN CB C 28.3 0.2 1 329 139 141 GLN N N 121.1 0.2 1 330 140 142 THR CA C 62.3 0.2 1 331 140 142 THR CB C 70.0 0.2 1 332 140 142 THR N N 113.5 0.2 1 333 141 143 SER CA C 58.0 0.2 1 334 141 143 SER CB C 62.6 0.2 1 335 141 143 SER N N 116.3 0.2 1 336 142 144 LEU CA C 54.3 0.2 1 337 142 144 LEU CB C 42.2 0.2 1 338 142 144 LEU N N 123.9 0.2 1 339 143 145 ALA CA C 51.3 0.2 1 340 143 145 ALA CB C 19.0 0.2 1 341 143 145 ALA N N 126.2 0.2 1 342 144 146 LYS CA C 57.3 0.2 1 343 144 146 LYS CB C 31.7 0.2 1 344 144 146 LYS N N 125.4 0.2 1 345 145 147 LYS CA C 55.0 0.2 1 346 145 147 LYS CB C 33.5 0.2 1 347 145 147 LYS N N 124.9 0.2 1 348 146 148 THR CA C 60.6 0.2 1 349 146 148 THR CB C 70.9 0.2 1 350 146 148 THR N N 112.7 0.2 1 351 147 149 ALA CA C 52.6 0.2 1 352 147 149 ALA CB C 19.1 0.2 1 353 147 149 ALA N N 127.6 0.2 1 354 148 150 TRP CA C 55.5 0.2 1 355 148 150 TRP CB C 30.3 0.2 1 356 148 150 TRP N N 121.7 0.2 1 357 149 151 ALA CA C 49.9 0.2 1 358 149 151 ALA CB C 21.3 0.2 1 359 149 151 ALA N N 120.4 0.2 1 360 150 152 LEU CA C 53.6 0.2 1 361 150 152 LEU CB C 45.3 0.2 1 362 150 152 LEU N N 119.5 0.2 1 363 151 153 TYR CA C 58.7 0.2 1 364 151 153 TYR CB C 40.1 0.2 1 365 151 153 TYR N N 117.0 0.2 1 366 152 154 ASP CA C 52.5 0.2 1 367 152 154 ASP CB C 44.4 0.2 1 368 152 154 ASP N N 115.3 0.2 1 369 153 155 GLY CA C 47.3 0.2 1 370 153 155 GLY N N 111.7 0.2 1 371 154 156 LYS CA C 59.4 0.2 1 372 154 156 LYS CB C 30.9 0.2 1 373 154 156 LYS N N 123.0 0.2 1 374 155 157 SER CA C 62.2 0.2 1 375 155 157 SER CB C 65.1 0.2 1 376 155 157 SER N N 117.9 0.2 1 377 156 158 LEU CA C 58.5 0.2 1 378 156 158 LEU CB C 40.9 0.2 1 379 156 158 LEU N N 122.2 0.2 1 380 157 159 GLU CA C 58.6 0.2 1 381 157 159 GLU CB C 28.7 0.2 1 382 157 159 GLU N N 119.3 0.2 1 383 158 160 LYS CA C 59.4 0.2 1 384 158 160 LYS CB C 31.9 0.2 1 385 158 160 LYS N N 118.3 0.2 1 386 159 161 ILE CA C 65.4 0.2 1 387 159 161 ILE CB C 37.9 0.2 1 388 159 161 ILE N N 117.6 0.2 1 389 160 162 VAL CA C 66.9 0.2 1 390 160 162 VAL CB C 31.3 0.2 1 391 160 162 VAL N N 115.6 0.2 1 392 161 163 ASP CA C 57.6 0.2 1 393 161 163 ASP CB C 41.7 0.2 1 394 161 163 ASP N N 119.5 0.2 1 395 162 164 GLN CA C 58.6 0.2 1 396 162 164 GLN CB C 28.5 0.2 1 397 162 164 GLN N N 116.6 0.2 1 398 163 165 VAL CA C 68.5 0.2 1 399 163 165 VAL CB C 30.6 0.2 1 400 163 165 VAL N N 119.5 0.2 1 401 164 166 ALA CA C 56.0 0.2 1 402 164 166 ALA CB C 18.3 0.2 1 403 164 166 ALA N N 122.0 0.2 1 404 165 167 ARG CA C 58.9 0.2 1 405 165 167 ARG CB C 30.1 0.2 1 406 165 167 ARG N N 117.4 0.2 1 407 166 168 PHE CA C 59.2 0.2 1 408 166 168 PHE CB C 37.7 0.2 1 409 166 168 PHE N N 120.8 0.2 1 410 167 169 VAL CA C 66.6 0.2 1 411 167 169 VAL CB C 30.4 0.2 1 412 167 169 VAL N N 121.3 0.2 1 413 168 170 ASP CA C 58.0 0.2 1 414 168 170 ASP CB C 39.8 0.2 1 415 168 170 ASP N N 121.7 0.2 1 416 169 171 GLU CA C 59.6 0.2 1 417 169 171 GLU CB C 29.7 0.2 1 418 169 171 GLU N N 118.5 0.2 1 419 170 172 LEU CA C 58.0 0.2 1 420 170 172 LEU CB C 38.7 0.2 1 421 170 172 LEU N N 122.3 0.2 1 422 171 173 GLU CA C 59.1 0.2 1 423 171 173 GLU CB C 29.7 0.2 1 424 171 173 GLU N N 118.0 0.2 1 425 172 174 LYS CA C 57.5 0.2 1 426 172 174 LYS CB C 32.7 0.2 1 427 172 174 LYS N N 115.1 0.2 1 428 173 175 ALA CA C 53.2 0.2 1 429 173 175 ALA CB C 19.1 0.2 1 430 173 175 ALA N N 120.0 0.2 1 431 174 176 PHE CA C 55.1 0.2 1 432 174 176 PHE CB C 41.9 0.2 1 433 174 176 PHE N N 116.2 0.2 1 434 175 177 PRO CA C 63.2 0.2 1 435 176 178 ILE CA C 60.4 0.2 1 436 176 178 ILE CB C 39.5 0.2 1 437 176 178 ILE N N 115.7 0.2 1 438 177 179 GLU CA C 61.2 0.2 1 439 177 179 GLU CB C 29.2 0.2 1 440 177 179 GLU N N 126.1 0.2 1 441 188 190 ILE CA C 59.7 0.2 1 442 188 190 ILE CB C 36.5 0.2 1 443 188 190 ILE N N 106.5 0.2 1 444 189 191 GLU CA C 59.6 0.2 1 445 189 191 GLU CB C 29.3 0.2 1 446 189 191 GLU N N 124.7 0.2 1 447 190 192 GLU CA C 56.5 0.2 1 448 190 192 GLU CB C 29.4 0.2 1 449 190 192 GLU N N 113.5 0.2 1 450 191 193 VAL CA C 62.7 0.2 1 451 191 193 VAL CB C 30.2 0.2 1 452 191 193 VAL N N 122.4 0.2 1 453 192 194 GLU CA C 56.2 0.2 1 454 192 194 GLU CB C 32.0 0.2 1 455 192 194 GLU N N 124.2 0.2 1 456 193 195 ASP CA C 52.2 0.2 1 457 193 195 ASP CB C 42.2 0.2 1 458 193 195 ASP N N 115.8 0.2 1 459 194 196 GLU CA C 60.1 0.2 1 460 194 196 GLU CB C 29.5 0.2 1 461 194 196 GLU N N 123.6 0.2 1 462 195 197 ALA CA C 56.0 0.2 1 463 195 197 ALA CB C 17.7 0.2 1 464 195 197 ALA N N 123.3 0.2 1 465 196 198 SER CA C 62.6 0.2 1 466 196 198 SER CB C 63.7 0.2 1 467 196 198 SER N N 116.5 0.2 1 468 197 199 LEU CA C 58.0 0.2 1 469 197 199 LEU CB C 42.2 0.2 1 470 197 199 LEU N N 121.1 0.2 1 471 198 200 THR CA C 67.1 0.2 1 472 198 200 THR CB C 68.3 0.2 1 473 198 200 THR N N 116.9 0.2 1 474 199 201 ILE CA C 64.7 0.2 1 475 199 201 ILE CB C 37.1 0.2 1 476 199 201 ILE N N 122.4 0.2 1 477 200 202 LEU CA C 58.1 0.2 1 478 200 202 LEU CB C 41.6 0.2 1 479 200 202 LEU N N 120.3 0.2 1 480 201 203 LYS CA C 60.2 0.2 1 481 201 203 LYS CB C 32.2 0.2 1 482 201 203 LYS N N 118.0 0.2 1 483 202 204 ASP CA C 56.8 0.2 1 484 202 204 ASP CB C 41.4 0.2 1 485 202 204 ASP N N 117.7 0.2 1 486 203 205 ALA CA C 54.8 0.2 1 487 203 205 ALA CB C 17.8 0.2 1 488 203 205 ALA N N 122.8 0.2 1 489 204 206 ALA CA C 52.7 0.2 1 490 204 206 ALA CB C 18.4 0.2 1 491 204 206 ALA N N 116.0 0.2 1 492 205 207 GLY CA C 47.8 0.2 1 493 205 207 GLY N N 108.1 0.2 1 494 206 208 GLY CA C 46.0 0.2 1 495 206 208 GLY N N 116.8 0.2 1 496 207 209 ILE CA C 61.5 0.2 1 497 207 209 ILE CB C 40.9 0.2 1 498 207 209 ILE N N 115.2 0.2 1 499 208 210 ASP CA C 53.1 0.2 1 500 208 210 ASP CB C 41.7 0.2 1 501 208 210 ASP N N 120.6 0.2 1 502 209 211 ALA CA C 54.0 0.2 1 503 209 211 ALA CB C 18.3 0.2 1 504 209 211 ALA N N 129.3 0.2 1 505 210 212 ALA CA C 55.0 0.2 1 506 210 212 ALA CB C 17.7 0.2 1 507 210 212 ALA N N 120.0 0.2 1 508 211 213 MET CA C 58.4 0.2 1 509 211 213 MET CB C 33.4 0.2 1 510 211 213 MET N N 121.2 0.2 1 511 212 214 SER CA C 62.7 0.2 1 512 212 214 SER N N 113.5 0.2 1 513 213 215 ASP CA C 57.1 0.2 1 514 213 215 ASP CB C 40.4 0.2 1 515 213 215 ASP N N 119.6 0.2 1 516 214 216 ALA CA C 55.0 0.2 1 517 214 216 ALA CB C 17.3 0.2 1 518 214 216 ALA N N 123.0 0.2 1 519 215 217 ALA CA C 55.2 0.2 1 520 215 217 ALA CB C 17.2 0.2 1 521 215 217 ALA N N 121.9 0.2 1 522 216 218 ALA CA C 55.3 0.2 1 523 216 218 ALA CB C 18.3 0.2 1 524 216 218 ALA N N 119.9 0.2 1 525 217 219 GLN CA C 58.6 0.2 1 526 217 219 GLN CB C 28.3 0.2 1 527 217 219 GLN N N 116.9 0.2 1 528 218 220 LYS CA C 59.9 0.2 1 529 218 220 LYS CB C 32.4 0.2 1 530 218 220 LYS N N 121.2 0.2 1 531 219 221 ILE CA C 66.2 0.2 1 532 219 221 ILE CB C 37.8 0.2 1 533 219 221 ILE N N 120.9 0.2 1 534 220 222 ASP CA C 57.2 0.2 1 535 220 222 ASP CB C 40.3 0.2 1 536 220 222 ASP N N 118.6 0.2 1 537 221 223 ALA CA C 54.1 0.2 1 538 221 223 ALA CB C 18.3 0.2 1 539 221 223 ALA N N 121.2 0.2 1 540 222 224 ILE CA C 64.4 0.2 1 541 222 224 ILE CB C 38.4 0.2 1 542 222 224 ILE N N 119.6 0.2 1 543 223 225 VAL CA C 64.1 0.2 1 544 223 225 VAL CB C 31.7 0.2 1 545 224 226 GLY CA C 45.8 0.2 1 546 224 226 GLY N N 109.5 0.2 1 547 225 227 ARG CA C 56.6 0.2 1 548 225 227 ARG CB C 30.3 0.2 1 549 225 227 ARG N N 120.3 0.2 1 550 226 228 ASN CA C 53.4 0.2 1 551 226 228 ASN CB C 39.1 0.2 1 552 226 228 ASN N N 119.8 0.2 1 553 227 229 SER CA C 60.1 0.2 1 554 227 229 SER CB C 64.5 0.2 1 555 227 229 SER N N 121.7 0.2 1 stop_ save_