data_19194 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance assignment of the alpha-subunit within the megadalton proteasome-activator complex ; _BMRB_accession_number 19194 _BMRB_flat_file_name bmr19194.str _Entry_type original _Submission_date 2013-04-25 _Accession_date 2013-04-25 _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 Mainz Andi . . 2 Religa Tomasz L. . 3 Sprangers Remco . . 4 Linser Rasmus . . 5 Kay Lewis E. . 6 Reif Bernd . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 109 "13C chemical shifts" 247 "15N chemical shifts" 109 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-08-13 original author . stop_ _Original_release_date 2013-08-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR spectroscopy of soluble protein complexes at one mega-dalton and beyond' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23873792 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mainz Andi . . 2 Religa Tomasz L. . 3 Sprangers Remco . . 4 Linser Rasmus . . 5 Kay Lewis E. . 6 Reif Bernd . . stop_ _Journal_abbreviation 'Angew. Chem. Int. Ed.' _Journal_volume 52 _Journal_issue 33 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 8746 _Page_last 8751 _Year 2013 _Details . loop_ _Keyword FROSTY 'large protein complexes' 'magic angle spinning' proteasome sedimentation stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name '20S-11S proteasome-activator complex' _Enzyme_commission_number 'EC 3.4.25.1' loop_ _Mol_system_component_name _Mol_label 'alpha subunit' $proteasome_alpha_subunit 'beta subunit' $proteasome_beta_subunit '11S activator' $proteasome_activator_PA26 stop_ _System_molecular_weight 1030652 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 14 'alpha subunit' 14 'beta subunit' 14 '11S activator' stop_ loop_ _Biological_function 'controlled protein degradation; protein homeostasis' stop_ _Database_query_date . _Details '20S-11S proteasome-activator complex' save_ ######################## # Monomeric polymers # ######################## save_proteasome_alpha_subunit _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common proteasome_alpha_subunit _Molecular_mass 26115.8 _Mol_thiol_state 'all free' loop_ _Biological_function 'Component of the 20S proteasome' 'large protease complex with broad specificity involved in protein degradation' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 237 _Mol_residue_sequence ; GAMGMQQGQMAYDRAITVFS PDGRLFQVEYAREAVKKGST ALGMKFANGVLLISDKKVRS RLIEQNSIEKIQLIDDYVAA VTSGLVADARVLVDFARISA QQEKVTYGSLVNIENLVKRV ADQMQQYTQYGGVRPYGVSL IFAGIDQIGPRLFDCDPAGT INEYKATAIGSGKDAVVSFL EREYKENLPEKEAVTLGIKA LKSSLEEGEELKAPEIASIT VGNKYRIYDQEEVKKFL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -3 GLY 2 -2 ALA 3 -1 MET 4 0 GLY 5 1 MET 6 2 GLN 7 3 GLN 8 4 GLY 9 5 GLN 10 6 MET 11 7 ALA 12 8 TYR 13 9 ASP 14 10 ARG 15 11 ALA 16 12 ILE 17 13 THR 18 14 VAL 19 15 PHE 20 16 SER 21 17 PRO 22 18 ASP 23 19 GLY 24 20 ARG 25 21 LEU 26 22 PHE 27 23 GLN 28 24 VAL 29 25 GLU 30 26 TYR 31 27 ALA 32 28 ARG 33 29 GLU 34 30 ALA 35 31 VAL 36 32 LYS 37 33 LYS 38 34 GLY 39 35 SER 40 36 THR 41 37 ALA 42 38 LEU 43 39 GLY 44 40 MET 45 41 LYS 46 42 PHE 47 43 ALA 48 44 ASN 49 45 GLY 50 46 VAL 51 47 LEU 52 48 LEU 53 49 ILE 54 50 SER 55 51 ASP 56 52 LYS 57 53 LYS 58 54 VAL 59 55 ARG 60 56 SER 61 57 ARG 62 58 LEU 63 59 ILE 64 60 GLU 65 61 GLN 66 62 ASN 67 63 SER 68 64 ILE 69 65 GLU 70 66 LYS 71 67 ILE 72 68 GLN 73 69 LEU 74 70 ILE 75 71 ASP 76 72 ASP 77 73 TYR 78 74 VAL 79 75 ALA 80 76 ALA 81 77 VAL 82 78 THR 83 79 SER 84 80 GLY 85 81 LEU 86 82 VAL 87 83 ALA 88 84 ASP 89 85 ALA 90 86 ARG 91 87 VAL 92 88 LEU 93 89 VAL 94 90 ASP 95 91 PHE 96 92 ALA 97 93 ARG 98 94 ILE 99 95 SER 100 96 ALA 101 97 GLN 102 98 GLN 103 99 GLU 104 100 LYS 105 101 VAL 106 102 THR 107 103 TYR 108 104 GLY 109 105 SER 110 106 LEU 111 107 VAL 112 108 ASN 113 109 ILE 114 110 GLU 115 111 ASN 116 112 LEU 117 113 VAL 118 114 LYS 119 115 ARG 120 116 VAL 121 117 ALA 122 118 ASP 123 119 GLN 124 120 MET 125 121 GLN 126 122 GLN 127 123 TYR 128 124 THR 129 125 GLN 130 126 TYR 131 127 GLY 132 128 GLY 133 129 VAL 134 130 ARG 135 131 PRO 136 132 TYR 137 133 GLY 138 134 VAL 139 135 SER 140 136 LEU 141 137 ILE 142 138 PHE 143 139 ALA 144 140 GLY 145 141 ILE 146 142 ASP 147 143 GLN 148 144 ILE 149 145 GLY 150 146 PRO 151 147 ARG 152 148 LEU 153 149 PHE 154 150 ASP 155 151 CYS 156 152 ASP 157 153 PRO 158 154 ALA 159 155 GLY 160 156 THR 161 157 ILE 162 158 ASN 163 159 GLU 164 160 TYR 165 161 LYS 166 162 ALA 167 163 THR 168 164 ALA 169 165 ILE 170 166 GLY 171 167 SER 172 168 GLY 173 169 LYS 174 170 ASP 175 171 ALA 176 172 VAL 177 173 VAL 178 174 SER 179 175 PHE 180 176 LEU 181 177 GLU 182 178 ARG 183 179 GLU 184 180 TYR 185 181 LYS 186 182 GLU 187 183 ASN 188 184 LEU 189 185 PRO 190 186 GLU 191 187 LYS 192 188 GLU 193 189 ALA 194 190 VAL 195 191 THR 196 192 LEU 197 193 GLY 198 194 ILE 199 195 LYS 200 196 ALA 201 197 LEU 202 198 LYS 203 199 SER 204 200 SER 205 201 LEU 206 202 GLU 207 203 GLU 208 204 GLY 209 205 GLU 210 206 GLU 211 207 LEU 212 208 LYS 213 209 ALA 214 210 PRO 215 211 GLU 216 212 ILE 217 213 ALA 218 214 SER 219 215 ILE 220 216 THR 221 217 VAL 222 218 GLY 223 219 ASN 224 220 LYS 225 221 TYR 226 222 ARG 227 223 ILE 228 224 TYR 229 225 ASP 230 226 GLN 231 227 GLU 232 228 GLU 233 229 VAL 234 230 LYS 235 231 LYS 236 232 PHE 237 233 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 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 1PMA "Proteasome From Thermoplasma Acidophilum" 98.31 233 100.00 100.00 2.37e-165 PDB 1YA7 "Implications For Interactions Of Proteasome With Pan And Pa700 From The 1.9 A Structure Of A Proteasome-11s Activator Complex" 98.31 233 100.00 100.00 2.37e-165 PDB 1YAR "Structure Of Archeabacterial 20s Proteasome Mutant D9s- Pa26 Complex" 98.31 233 99.57 99.57 1.65e-164 PDB 1YAU "Structure Of Archeabacterial 20s Proteasome- Pa26 Complex" 98.31 233 99.14 99.14 1.58e-162 PDB 2KU1 "Dynamic Regulation Of Archaeal Proteasome Gate Opening As Studied By Trosy-Nmr" 100.00 237 100.00 100.00 2.31e-168 PDB 2KU2 "Dynamic Regulation Of Archaeal Proteasome Gate Opening As Studied By Trosy-Nmr" 100.00 237 99.16 99.16 1.00e-165 PDB 3C91 "Thermoplasma Acidophilum 20s Proteasome With An Open Gate" 98.31 233 100.00 100.00 2.37e-165 PDB 3C92 "Thermoplasma Acidophilum 20s Proteasome With A Closed Gate" 98.31 233 100.00 100.00 2.37e-165 PDB 3IPM "Crystal Structure Of Archaeal 20s Proteasome In Complex With The C- Terminus Of Pan" 98.31 233 100.00 100.00 2.37e-165 PDB 3J9I "Thermoplasma Acidophilum 20s Proteasome" 94.51 224 100.00 100.00 1.25e-157 PDB 3JRM "Crystal Structure Of Archaeal 20s Proteasome In Complex With Mutated P26 Activator" 95.78 227 100.00 100.00 7.07e-160 PDB 3JSE "Crystal Structure Of Archaeal 20s Proteasome In Complex With Mutated P26 Activator" 95.78 227 100.00 100.00 7.07e-160 PDB 3JTL "Crystal Structure Of Archaeal 20s Proteasome In Complex With Mutated P26 Activator" 95.78 227 100.00 100.00 7.07e-160 EMBL CAA42094 "alpha-subunit of the proteasome [Thermoplasma acidophilum]" 98.31 233 100.00 100.00 2.37e-165 EMBL CAC12411 "proteasome alpha subunit [Thermoplasma acidophilum]" 98.31 233 100.00 100.00 2.37e-165 REF WP_010901695 "proteasome endopeptidase complex,subunit alpha [Thermoplasma acidophilum]" 98.31 233 100.00 100.00 2.37e-165 SP P25156 "RecName: Full=Proteasome subunit alpha; AltName: Full=20S proteasome alpha subunit; AltName: Full=Proteasome core protein PsmA" 98.31 233 100.00 100.00 2.37e-165 stop_ save_ save_proteasome_beta_subunit _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common proteasome_beta_subunit _Molecular_mass 22271.8 _Mol_thiol_state 'not present' loop_ _Biological_function 'Component of the 20S proteasome' 'large protease complex with broad specificity involved in protein degradation' stop_ _Details . _Residue_count 203 _Mol_residue_sequence ; TTTVGITLKDAVIMATERRV TMENFIMHKNGKKLFQIDTY TGMTIAGLVGDAQVLVRYMK AELELYRLQRRVNMPIEAVA TLLSNMLNQVKYMPYMVQLL VGGIDTAPHVFSIDAAGGSV EDIYASTGSGSPFVYGVLES QYSEKMTVDEGVDLVIRAIS AAKQRDSASGGMIDVAVITR KDGYVQLPTDQIESRIRKLG LIL ; loop_ _Residue_seq_code _Residue_label 1 THR 2 THR 3 THR 4 VAL 5 GLY 6 ILE 7 THR 8 LEU 9 LYS 10 ASP 11 ALA 12 VAL 13 ILE 14 MET 15 ALA 16 THR 17 GLU 18 ARG 19 ARG 20 VAL 21 THR 22 MET 23 GLU 24 ASN 25 PHE 26 ILE 27 MET 28 HIS 29 LYS 30 ASN 31 GLY 32 LYS 33 LYS 34 LEU 35 PHE 36 GLN 37 ILE 38 ASP 39 THR 40 TYR 41 THR 42 GLY 43 MET 44 THR 45 ILE 46 ALA 47 GLY 48 LEU 49 VAL 50 GLY 51 ASP 52 ALA 53 GLN 54 VAL 55 LEU 56 VAL 57 ARG 58 TYR 59 MET 60 LYS 61 ALA 62 GLU 63 LEU 64 GLU 65 LEU 66 TYR 67 ARG 68 LEU 69 GLN 70 ARG 71 ARG 72 VAL 73 ASN 74 MET 75 PRO 76 ILE 77 GLU 78 ALA 79 VAL 80 ALA 81 THR 82 LEU 83 LEU 84 SER 85 ASN 86 MET 87 LEU 88 ASN 89 GLN 90 VAL 91 LYS 92 TYR 93 MET 94 PRO 95 TYR 96 MET 97 VAL 98 GLN 99 LEU 100 LEU 101 VAL 102 GLY 103 GLY 104 ILE 105 ASP 106 THR 107 ALA 108 PRO 109 HIS 110 VAL 111 PHE 112 SER 113 ILE 114 ASP 115 ALA 116 ALA 117 GLY 118 GLY 119 SER 120 VAL 121 GLU 122 ASP 123 ILE 124 TYR 125 ALA 126 SER 127 THR 128 GLY 129 SER 130 GLY 131 SER 132 PRO 133 PHE 134 VAL 135 TYR 136 GLY 137 VAL 138 LEU 139 GLU 140 SER 141 GLN 142 TYR 143 SER 144 GLU 145 LYS 146 MET 147 THR 148 VAL 149 ASP 150 GLU 151 GLY 152 VAL 153 ASP 154 LEU 155 VAL 156 ILE 157 ARG 158 ALA 159 ILE 160 SER 161 ALA 162 ALA 163 LYS 164 GLN 165 ARG 166 ASP 167 SER 168 ALA 169 SER 170 GLY 171 GLY 172 MET 173 ILE 174 ASP 175 VAL 176 ALA 177 VAL 178 ILE 179 THR 180 ARG 181 LYS 182 ASP 183 GLY 184 TYR 185 VAL 186 GLN 187 LEU 188 PRO 189 THR 190 ASP 191 GLN 192 ILE 193 GLU 194 SER 195 ARG 196 ILE 197 ARG 198 LYS 199 LEU 200 GLY 201 LEU 202 ILE 203 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 1PMA "Proteasome From Thermoplasma Acidophilum" 100.00 211 100.00 100.00 4.11e-143 PDB 1YA7 "Implications For Interactions Of Proteasome With Pan And Pa700 From The 1.9 A Structure Of A Proteasome-11s Activator Complex" 100.00 217 100.00 100.00 1.88e-143 PDB 1YAR "Structure Of Archeabacterial 20s Proteasome Mutant D9s- Pa26 Complex" 100.00 217 100.00 100.00 1.88e-143 PDB 1YAU "Structure Of Archeabacterial 20s Proteasome- Pa26 Complex" 100.00 217 100.00 100.00 1.88e-143 PDB 3C91 "Thermoplasma Acidophilum 20s Proteasome With An Open Gate" 100.00 203 100.00 100.00 2.33e-143 PDB 3C92 "Thermoplasma Acidophilum 20s Proteasome With A Closed Gate" 100.00 203 100.00 100.00 2.33e-143 PDB 3IPM "Crystal Structure Of Archaeal 20s Proteasome In Complex With The C- Terminus Of Pan" 100.00 217 100.00 100.00 1.88e-143 PDB 3JRM "Crystal Structure Of Archaeal 20s Proteasome In Complex With Mutated P26 Activator" 100.00 203 100.00 100.00 2.33e-143 PDB 3JSE "Crystal Structure Of Archaeal 20s Proteasome In Complex With Mutated P26 Activator" 100.00 203 100.00 100.00 2.33e-143 PDB 3JTL "Crystal Structure Of Archaeal 20s Proteasome In Complex With Mutated P26 Activator" 100.00 203 100.00 100.00 2.33e-143 EMBL CAC11751 "proteasome, beta chain [Thermoplasma acidophilum]" 100.00 211 100.00 100.00 4.11e-143 GB AAA72102 "proteasome beta-subunit [Thermoplasma acidophilum]" 100.00 211 100.00 100.00 4.11e-143 REF NP_394085 "proteasome, beta chain [Thermoplasma acidophilum DSM 1728]" 100.00 211 100.00 100.00 4.11e-143 REF WP_010901036 "proteasome subunit beta [Thermoplasma acidophilum]" 100.00 211 100.00 100.00 4.11e-143 SP P28061 "RecName: Full=Proteasome subunit beta; AltName: Full=20S proteasome beta subunit; AltName: Full=Proteasome core protein PsmB; F" 100.00 211 100.00 100.00 4.11e-143 stop_ save_ save_proteasome_activator_PA26 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common proteasome_activator_PA26 _Molecular_mass 25229.7 _Mol_thiol_state 'all free' loop_ _Biological_function 'proteasome-activating protein' stop_ _Details . _Residue_count 235 _Mol_residue_sequence ; GAMGMPPKRAALIQNLRDSY TETSSFAVIEEWAAGTLQEI EGIAKAAAEAHGTIRNSTYG RAQAEKSPEQLLGVLQRYQD LCHNVYCQAETIRTVIAIRI PEHKEEDNLGVAVQHAVLKI IDELEIKTLGSGEKSGSGGA PTPIGMYALREYLSARSTVE DKLLGSVDAESGKTKGGSQS PSLLLELRQIDADFMLKVEL ATTHLSTMVRAVINAYLLNW KKLIQPRTGSDHMVS ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ALA 3 MET 4 GLY 5 MET 6 PRO 7 PRO 8 LYS 9 ARG 10 ALA 11 ALA 12 LEU 13 ILE 14 GLN 15 ASN 16 LEU 17 ARG 18 ASP 19 SER 20 TYR 21 THR 22 GLU 23 THR 24 SER 25 SER 26 PHE 27 ALA 28 VAL 29 ILE 30 GLU 31 GLU 32 TRP 33 ALA 34 ALA 35 GLY 36 THR 37 LEU 38 GLN 39 GLU 40 ILE 41 GLU 42 GLY 43 ILE 44 ALA 45 LYS 46 ALA 47 ALA 48 ALA 49 GLU 50 ALA 51 HIS 52 GLY 53 THR 54 ILE 55 ARG 56 ASN 57 SER 58 THR 59 TYR 60 GLY 61 ARG 62 ALA 63 GLN 64 ALA 65 GLU 66 LYS 67 SER 68 PRO 69 GLU 70 GLN 71 LEU 72 LEU 73 GLY 74 VAL 75 LEU 76 GLN 77 ARG 78 TYR 79 GLN 80 ASP 81 LEU 82 CYS 83 HIS 84 ASN 85 VAL 86 TYR 87 CYS 88 GLN 89 ALA 90 GLU 91 THR 92 ILE 93 ARG 94 THR 95 VAL 96 ILE 97 ALA 98 ILE 99 ARG 100 ILE 101 PRO 102 GLU 103 HIS 104 LYS 105 GLU 106 GLU 107 ASP 108 ASN 109 LEU 110 GLY 111 VAL 112 ALA 113 VAL 114 GLN 115 HIS 116 ALA 117 VAL 118 LEU 119 LYS 120 ILE 121 ILE 122 ASP 123 GLU 124 LEU 125 GLU 126 ILE 127 LYS 128 THR 129 LEU 130 GLY 131 SER 132 GLY 133 GLU 134 LYS 135 SER 136 GLY 137 SER 138 GLY 139 GLY 140 ALA 141 PRO 142 THR 143 PRO 144 ILE 145 GLY 146 MET 147 TYR 148 ALA 149 LEU 150 ARG 151 GLU 152 TYR 153 LEU 154 SER 155 ALA 156 ARG 157 SER 158 THR 159 VAL 160 GLU 161 ASP 162 LYS 163 LEU 164 LEU 165 GLY 166 SER 167 VAL 168 ASP 169 ALA 170 GLU 171 SER 172 GLY 173 LYS 174 THR 175 LYS 176 GLY 177 GLY 178 SER 179 GLN 180 SER 181 PRO 182 SER 183 LEU 184 LEU 185 LEU 186 GLU 187 LEU 188 ARG 189 GLN 190 ILE 191 ASP 192 ALA 193 ASP 194 PHE 195 MET 196 LEU 197 LYS 198 VAL 199 GLU 200 LEU 201 ALA 202 THR 203 THR 204 HIS 205 LEU 206 SER 207 THR 208 MET 209 VAL 210 ARG 211 ALA 212 VAL 213 ILE 214 ASN 215 ALA 216 TYR 217 LEU 218 LEU 219 ASN 220 TRP 221 LYS 222 LYS 223 LEU 224 ILE 225 GLN 226 PRO 227 ARG 228 THR 229 GLY 230 SER 231 ASP 232 HIS 233 MET 234 VAL 235 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 1FNT "Crystal Structure Of The 20s Proteasome From Yeast In Complex With The Proteasome Activator Pa26 From Trypanosome Brucei At 3.2" 98.30 231 99.13 99.57 2.79e-166 PDB 1YA7 "Implications For Interactions Of Proteasome With Pan And Pa700 From The 1.9 A Structure Of A Proteasome-11s Activator Complex" 97.87 237 99.57 99.57 2.32e-165 PDB 1YAR "Structure Of Archeabacterial 20s Proteasome Mutant D9s- Pa26 Complex" 97.87 237 99.57 99.57 2.32e-165 PDB 1YAU "Structure Of Archeabacterial 20s Proteasome- Pa26 Complex" 97.87 237 99.57 99.57 2.32e-165 PDB 1Z7Q "Crystal Structure Of The 20s Proteasome From Yeast In Complex With The Proteasome Activator Pa26 From Trypanosome Brucei At 3.2" 98.72 231 98.71 98.71 2.50e-162 PDB 3IPM "Crystal Structure Of Archaeal 20s Proteasome In Complex With The C- Terminus Of Pan" 95.32 239 97.77 98.21 2.87e-157 PDB 3JRM "Crystal Structure Of Archaeal 20s Proteasome In Complex With Mutated P26 Activator" 97.02 228 98.25 98.68 2.41e-161 PDB 3JSE "Crystal Structure Of Archaeal 20s Proteasome In Complex With Mutated P26 Activator" 97.02 228 98.68 99.12 1.73e-162 PDB 3JTL "Crystal Structure Of Archaeal 20s Proteasome In Complex With Mutated P26 Activator" 95.32 228 98.66 98.66 9.32e-158 EMBL CBH15376 "proteasome activator protein pa26, putative [Trypanosoma brucei gambiense DAL972]" 98.30 231 99.57 99.57 1.19e-166 GB AAD50581 "proteasome activator protein PA26 [Trypanosoma brucei]" 98.30 231 100.00 100.00 1.77e-167 GB EAN77792 "proteasome activator protein PA26 [Trypanosoma brucei brucei TREU927]" 98.30 231 98.70 99.13 5.68e-166 REF XP_822620 "proteasome activator protein PA26 [Trypanosoma brucei brucei TREU927]" 98.30 231 98.70 99.13 5.68e-166 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $proteasome_alpha_subunit 'Thermoplasma acidophilum' 2303 Archaea . Thermoplasma acidophilum 'The alpha and beta subunits originate from the 20S proteasome of Thermoplasma acidophilum. The PA26 activator originates from Trypanosoma brucei.' 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 $proteasome_alpha_subunit 'recombinant technology' . Escherichia coli . pETM-11 'the other components were similarly produced' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_20S-11S_complex _Saveframe_category sample _Sample_type 'gel solid' _Details ; All subunits were deuterated at non-exchangeable sites, whereas exchangeable sites were back-exchanged to an H2O/D2O ratio of 2:8. The concentrated solution of the proteasome-activator complex was filled into a 3.2mm MAS rotor and sedimented by 22 kHz MAS. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $proteasome_alpha_subunit 3.0 mM '[U-13C; U-15N; U-2H]' $proteasome_beta_subunit 3.0 mM [U-2H] $proteasome_activator_PA26 4.5 mM [U-2H] 'potassium phosphate' 50 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' DTT 1 mM 'natural abundance' 'sodium azide' 0.03 '% w/v' 'natural abundance' glycerol 30 '% v/v' [U-2H] Cu(II)-EDTA 60 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection 'data analysis' processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_via_CP_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC via CP' _Sample_label $20S-11S_complex save_ save_2D_1H-15N_HSQC_via_INEPT_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC via INEPT' _Sample_label $20S-11S_complex save_ save_3D_hCOhNH_via_long-range_CP_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D hCOhNH via long-range CP' _Sample_label $20S-11S_complex save_ save_3D_hCAhNH_via_long-range_CP_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D hCAhNH via long-range CP' _Sample_label $20S-11S_complex 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 'All experiments were performed at 22 kHz magic-angle spinning.' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 . pH temperature 303 . 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 adamantane C 13 'methylene carbon' ppm 38.48 external direct . . . 1 adamantane H 1 'methylene carbon' ppm 38.48 external indirect . . . 3.9767799 adamantane N 15 'methylene carbon' ppm 38.48 external indirect . . . 0.40298 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 via CP' '3D hCOhNH via long-range CP' '3D hCAhNH via long-range CP' stop_ loop_ _Sample_label $20S-11S_complex stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'alpha subunit' _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 35 39 SER C C 174.758 0.000 1 2 36 40 THR H H 8.529 0.000 1 3 36 40 THR C C 172.630 0.000 1 4 36 40 THR CA C 63.249 0.040 1 5 36 40 THR N N 122.195 0.000 1 6 37 41 ALA H H 8.180 0.000 1 7 37 41 ALA C C 174.427 0.175 1 8 37 41 ALA CA C 50.081 0.075 1 9 37 41 ALA N N 126.913 0.000 1 10 38 42 LEU H H 9.272 0.000 1 11 38 42 LEU C C 173.704 0.000 1 12 38 42 LEU CA C 54.079 0.038 1 13 38 42 LEU N N 116.807 0.000 1 14 39 43 GLY H H 8.213 0.000 1 15 39 43 GLY C C 172.324 0.000 1 16 39 43 GLY CA C 45.175 0.000 1 17 39 43 GLY N N 104.906 0.000 1 18 40 44 MET H H 8.466 0.000 1 19 40 44 MET C C 174.339 0.000 1 20 40 44 MET CA C 55.475 0.000 1 21 40 44 MET N N 116.916 0.000 1 22 41 45 LYS H H 9.159 0.000 1 23 41 45 LYS C C 176.520 0.000 1 24 41 45 LYS CA C 57.221 0.103 1 25 41 45 LYS CB C 34.800 0.000 1 26 41 45 LYS N N 123.403 0.000 1 27 42 46 PHE H H 8.522 0.000 1 28 42 46 PHE C C 173.901 0.000 1 29 42 46 PHE CA C 56.236 0.000 1 30 42 46 PHE N N 125.838 0.000 1 31 43 47 ALA H H 9.174 0.000 1 32 43 47 ALA CA C 54.419 0.000 1 33 43 47 ALA N N 124.407 0.000 1 34 44 48 ASN C C 173.967 0.000 1 35 44 48 ASN CA C 53.174 0.000 1 36 45 49 GLY H H 6.938 0.000 1 37 45 49 GLY C C 170.045 0.000 1 38 45 49 GLY CA C 46.760 0.000 1 39 45 49 GLY N N 105.320 0.000 1 40 46 50 VAL H H 8.095 0.000 1 41 46 50 VAL C C 171.053 0.000 1 42 46 50 VAL CA C 59.738 0.000 1 43 46 50 VAL N N 118.083 0.000 1 44 47 51 LEU H H 8.619 0.000 1 45 47 51 LEU C C 174.646 0.000 1 46 47 51 LEU CA C 53.150 0.000 1 47 47 51 LEU N N 125.653 0.000 1 48 48 52 LEU H H 8.922 0.000 1 49 48 52 LEU C C 174.909 0.000 1 50 48 52 LEU CA C 53.211 0.000 1 51 48 52 LEU N N 120.573 0.000 1 52 49 53 ILE H H 8.589 0.000 1 53 49 53 ILE C C 175.430 0.000 1 54 49 53 ILE CA C 59.192 0.018 1 55 49 53 ILE CB C 41.478 0.000 1 56 49 53 ILE N N 118.374 0.000 1 57 50 54 SER H H 8.797 0.000 1 58 50 54 SER C C 173.726 0.000 1 59 50 54 SER CA C 56.391 0.103 1 60 50 54 SER N N 118.965 0.000 1 61 51 55 ASP H H 8.427 0.000 1 62 51 55 ASP CA C 53.852 0.000 1 63 51 55 ASP N N 125.899 0.000 1 64 67 71 ILE C C 174.953 0.000 1 65 67 71 ILE CA C 61.491 0.000 1 66 68 72 GLN H H 8.615 0.000 1 67 68 72 GLN CA C 53.026 0.000 1 68 68 72 GLN N N 125.804 0.000 1 69 74 78 VAL C C 171.859 0.000 1 70 75 79 ALA H H 8.859 0.000 1 71 75 79 ALA C C 173.552 0.000 1 72 75 79 ALA N N 128.938 0.000 1 73 76 80 ALA H H 8.702 0.000 1 74 76 80 ALA C C 175.435 0.000 1 75 76 80 ALA CA C 49.401 0.000 1 76 76 80 ALA N N 120.706 0.000 1 77 77 81 VAL H H 8.135 0.000 1 78 77 81 VAL C C 173.222 0.000 1 79 77 81 VAL CA C 59.248 0.000 1 80 77 81 VAL N N 115.015 0.000 1 81 78 82 THR H H 7.151 0.000 1 82 78 82 THR C C 173.200 0.000 1 83 78 82 THR CA C 59.522 0.066 1 84 78 82 THR N N 112.618 0.000 1 85 79 83 SER H H 8.132 0.000 1 86 79 83 SER C C 173.134 0.000 1 87 79 83 SER CA C 58.437 0.132 1 88 79 83 SER CB C 64.153 0.000 1 89 79 83 SER N N 113.551 0.000 1 90 80 84 GLY H H 7.777 0.000 1 91 80 84 GLY C C 173.495 0.000 1 92 80 84 GLY CA C 43.629 0.000 1 93 80 84 GLY N N 111.538 0.000 1 94 81 85 LEU H H 8.517 0.000 1 95 81 85 LEU C C 178.239 0.000 1 96 81 85 LEU CA C 55.264 0.127 1 97 81 85 LEU N N 123.908 0.000 1 98 82 86 VAL H H 8.027 0.000 1 99 82 86 VAL C C 178.213 0.000 1 100 82 86 VAL CA C 65.605 0.019 1 101 82 86 VAL N N 126.214 0.000 1 102 83 87 ALA H H 8.712 0.000 1 103 83 87 ALA C C 179.094 0.000 1 104 83 87 ALA CA C 55.046 0.000 1 105 83 87 ALA N N 124.817 0.000 1 106 84 88 ASP H H 6.417 0.000 1 107 84 88 ASP CA C 56.720 0.000 1 108 84 88 ASP N N 117.533 0.000 1 109 85 89 ALA C C 178.422 0.000 1 110 86 90 ARG H H 7.458 0.000 1 111 86 90 ARG C C 178.607 0.000 1 112 86 90 ARG CA C 59.010 0.000 1 113 86 90 ARG N N 118.610 0.000 1 114 87 91 VAL H H 7.245 0.000 1 115 87 91 VAL CA C 65.041 0.000 1 116 87 91 VAL N N 116.109 0.000 1 117 95 99 SER CA C 58.493 0.000 1 118 96 100 ALA H H 7.449 0.000 1 119 96 100 ALA CA C 53.966 0.000 1 120 96 100 ALA N N 124.359 0.000 1 121 104 108 GLY H H 8.744 0.000 1 122 104 108 GLY C C 173.343 0.000 1 123 104 108 GLY CA C 45.614 0.061 1 124 104 108 GLY N N 104.050 0.000 1 125 105 109 SER H H 7.006 0.000 1 126 105 109 SER CA C 57.238 0.000 1 127 105 109 SER N N 109.584 0.000 1 128 108 112 ASN C C 177.297 0.000 1 129 109 113 ILE H H 11.664 0.000 1 130 109 113 ILE CA C 64.775 0.000 1 131 109 113 ILE N N 131.359 0.000 1 132 134 138 VAL H H 7.364 0.000 1 133 134 138 VAL C C 173.025 0.000 1 134 134 138 VAL CA C 59.998 0.117 1 135 134 138 VAL N N 120.206 0.000 1 136 135 139 SER H H 7.867 0.000 1 137 135 139 SER C C 172.828 0.000 1 138 135 139 SER CA C 57.201 0.010 1 139 135 139 SER CB C 65.775 0.000 1 140 135 139 SER N N 117.444 0.000 1 141 136 140 LEU H H 8.677 0.000 1 142 136 140 LEU C C 175.175 0.000 1 143 136 140 LEU CA C 54.623 0.041 1 144 136 140 LEU N N 120.124 0.000 1 145 137 141 ILE H H 8.113 0.000 1 146 137 141 ILE C C 175.522 0.000 1 147 137 141 ILE CA C 59.639 0.051 1 148 137 141 ILE N N 118.780 0.000 1 149 138 142 PHE H H 8.924 0.000 1 150 138 142 PHE C C 174.996 0.000 1 151 138 142 PHE CA C 55.815 0.151 1 152 138 142 PHE N N 122.043 0.000 1 153 139 143 ALA H H 9.176 0.000 1 154 139 143 ALA C C 178.370 0.000 1 155 139 143 ALA CA C 50.231 0.000 1 156 139 143 ALA N N 122.859 0.000 1 157 140 144 GLY H H 8.632 0.000 1 158 140 144 GLY C C 169.585 0.000 1 159 140 144 GLY CA C 46.687 0.002 1 160 140 144 GLY N N 114.344 0.000 1 161 141 145 ILE H H 7.839 0.000 1 162 141 145 ILE C C 173.900 0.000 1 163 141 145 ILE CA C 59.195 0.004 1 164 141 145 ILE N N 119.495 0.000 1 165 142 146 ASP H H 7.748 0.000 1 166 142 146 ASP C C 176.474 0.000 1 167 142 146 ASP CA C 52.249 0.000 1 168 142 146 ASP N N 129.870 0.000 1 169 143 147 GLN H H 7.563 0.000 1 170 143 147 GLN CA C 57.645 0.000 1 171 143 147 GLN N N 114.102 0.000 1 172 146 150 PRO C C 176.311 0.000 1 173 146 150 PRO CA C 62.229 0.000 1 174 147 151 ARG H H 9.349 0.000 1 175 147 151 ARG C C 175.384 0.000 1 176 147 151 ARG CA C 52.042 0.000 1 177 147 151 ARG N N 123.295 0.000 1 178 148 152 LEU H H 6.900 0.000 1 179 148 152 LEU C C 173.244 0.000 1 180 148 152 LEU CA C 54.343 0.075 1 181 148 152 LEU N N 122.793 0.000 1 182 149 153 PHE H H 9.429 0.000 1 183 149 153 PHE C C 176.126 0.000 1 184 149 153 PHE CA C 55.928 0.000 1 185 149 153 PHE CB C 35.366 0.000 1 186 149 153 PHE N N 125.401 0.000 1 187 150 154 ASP H H 8.892 0.000 1 188 150 154 ASP C C 174.387 0.000 1 189 150 154 ASP CA C 52.603 0.034 1 190 150 154 ASP N N 119.355 0.000 1 191 151 155 CYS H H 8.066 0.000 1 192 151 155 CYS C C 173.262 0.012 1 193 151 155 CYS CA C 57.655 0.161 1 194 151 155 CYS N N 117.335 0.000 1 195 152 156 ASP H H 7.889 0.000 1 196 152 156 ASP CA C 52.514 0.000 1 197 152 156 ASP N N 131.843 0.000 1 198 157 161 ILE C C 174.897 0.000 1 199 157 161 ILE CA C 59.138 0.000 1 200 158 162 ASN H H 7.958 0.000 1 201 158 162 ASN C C 171.871 0.035 1 202 158 162 ASN CA C 52.775 0.064 1 203 158 162 ASN N N 120.798 0.000 1 204 159 163 GLU H H 8.281 0.000 1 205 159 163 GLU C C 174.967 0.000 1 206 159 163 GLU CA C 54.312 0.188 1 207 159 163 GLU N N 122.239 0.000 1 208 160 164 TYR H H 8.029 0.000 1 209 160 164 TYR C C 174.909 0.000 1 210 160 164 TYR CA C 57.531 0.018 1 211 160 164 TYR N N 121.560 0.000 1 212 161 165 LYS H H 8.851 0.000 1 213 161 165 LYS C C 175.801 0.000 1 214 161 165 LYS CA C 58.135 0.094 1 215 161 165 LYS N N 116.248 0.000 1 216 162 166 ALA H H 6.819 0.000 1 217 162 166 ALA C C 174.455 0.094 1 218 162 166 ALA CA C 51.589 0.000 1 219 162 166 ALA N N 116.881 0.000 1 220 163 167 THR H H 8.089 0.000 1 221 163 167 THR C C 169.881 0.011 1 222 163 167 THR CA C 59.361 0.038 1 223 163 167 THR N N 112.197 0.000 1 224 164 168 ALA H H 7.484 0.000 1 225 164 168 ALA C C 173.989 0.000 1 226 164 168 ALA CA C 50.721 0.000 1 227 164 168 ALA N N 121.698 0.000 1 228 165 169 ILE H H 8.590 0.000 1 229 165 169 ILE C C 174.624 0.000 1 230 165 169 ILE CA C 59.739 0.075 1 231 165 169 ILE N N 112.033 0.000 1 232 166 170 GLY H H 7.781 0.000 1 233 166 170 GLY C C 176.860 0.130 1 234 166 170 GLY CA C 44.044 0.000 1 235 166 170 GLY N N 105.100 0.000 1 236 167 171 SER H H 8.049 0.000 1 237 167 171 SER CA C 61.625 0.000 1 238 167 171 SER N N 115.894 0.000 1 239 169 173 LYS C C 176.590 0.000 1 240 169 173 LYS CA C 60.112 0.000 1 241 170 174 ASP H H 8.415 0.000 1 242 170 174 ASP C C 178.501 0.000 1 243 170 174 ASP CA C 57.599 0.125 1 244 170 174 ASP N N 117.671 0.000 1 245 171 175 ALA H H 7.598 0.000 1 246 171 175 ALA CA C 54.381 0.000 1 247 171 175 ALA N N 123.506 0.000 1 248 172 176 VAL C C 178.120 0.000 1 249 173 177 VAL H H 8.827 0.000 1 250 173 177 VAL C C 177.912 0.000 1 251 173 177 VAL CA C 66.756 0.000 1 252 173 177 VAL N N 119.235 0.000 1 253 174 178 SER H H 7.818 0.000 1 254 174 178 SER C C 176.617 0.000 1 255 174 178 SER CA C 61.893 0.000 1 256 174 178 SER N N 115.688 0.000 1 257 175 179 PHE H H 7.665 0.000 1 258 175 179 PHE CA C 61.549 0.000 1 259 175 179 PHE N N 122.218 0.000 1 260 176 180 LEU C C 178.458 0.000 1 261 176 180 LEU CA C 57.022 0.000 1 262 177 181 GLU H H 9.159 0.000 1 263 177 181 GLU C C 178.631 0.000 1 264 177 181 GLU CA C 59.927 0.038 1 265 177 181 GLU CB C 28.047 0.000 1 266 177 181 GLU N N 121.880 0.000 1 267 178 182 ARG H H 6.871 0.000 1 268 178 182 ARG C C 178.020 0.000 1 269 178 182 ARG CA C 58.114 0.073 1 270 178 182 ARG N N 116.087 0.000 1 271 179 183 GLU H H 7.825 0.000 1 272 179 183 GLU C C 177.012 0.000 1 273 179 183 GLU CA C 56.701 0.000 1 274 179 183 GLU N N 115.080 0.000 1 275 180 184 TYR H H 9.222 0.000 1 276 180 184 TYR C C 174.602 0.000 1 277 180 184 TYR CA C 61.493 0.038 1 278 180 184 TYR N N 119.659 0.000 1 279 181 185 LYS H H 5.396 0.000 1 280 181 185 LYS C C 173.213 0.031 1 281 181 185 LYS CA C 53.822 0.026 1 282 181 185 LYS CB C 34.800 0.000 1 283 181 185 LYS N N 126.148 0.000 1 284 182 186 GLU H H 8.126 0.000 1 285 182 186 GLU CA C 56.118 0.000 1 286 182 186 GLU CB C 30.009 0.000 1 287 182 186 GLU N N 119.887 0.000 1 288 185 189 PRO C C 177.109 0.000 1 289 186 190 GLU H H 8.461 0.000 1 290 186 190 GLU C C 176.868 0.000 1 291 186 190 GLU CA C 60.130 0.000 1 292 186 190 GLU N N 123.707 0.000 1 293 187 191 LYS H H 8.481 0.000 1 294 187 191 LYS C C 179.094 0.000 1 295 187 191 LYS CA C 59.983 0.020 1 296 187 191 LYS N N 115.260 0.000 1 297 188 192 GLU H H 7.037 0.000 1 298 188 192 GLU C C 177.888 0.000 1 299 188 192 GLU CA C 58.600 0.082 1 300 188 192 GLU N N 118.572 0.000 1 301 189 193 ALA H H 7.965 0.000 1 302 189 193 ALA C C 178.329 0.000 1 303 189 193 ALA CA C 54.968 0.054 1 304 189 193 ALA CB C 16.917 0.000 1 305 189 193 ALA N N 125.031 0.000 1 306 190 194 VAL H H 8.194 0.000 1 307 190 194 VAL C C 177.332 0.000 1 308 190 194 VAL CA C 66.785 0.000 1 309 190 194 VAL N N 118.761 0.000 1 310 191 195 THR H H 7.350 0.000 1 311 191 195 THR C C 175.916 0.000 1 312 191 195 THR CA C 67.155 0.091 1 313 191 195 THR N N 115.146 0.000 1 314 192 196 LEU H H 7.935 0.000 1 315 192 196 LEU CA C 57.890 0.000 1 316 192 196 LEU N N 123.090 0.000 1 317 193 197 GLY C C 174.712 0.000 1 318 194 198 ILE H H 8.336 0.000 1 319 194 198 ILE C C 178.213 0.000 1 320 194 198 ILE CA C 62.368 0.030 1 321 194 198 ILE N N 122.592 0.000 1 322 195 199 LYS H H 8.052 0.000 1 323 195 199 LYS CA C 60.155 0.000 1 324 195 199 LYS CB C 31.385 0.000 1 325 195 199 LYS N N 121.572 0.000 1 326 196 200 ALA C C 179.673 0.000 1 327 196 200 ALA CA C 54.106 0.000 1 328 197 201 LEU H H 7.873 0.000 1 329 197 201 LEU C C 180.528 0.011 1 330 197 201 LEU CA C 57.369 0.000 1 331 197 201 LEU N N 119.938 0.000 1 332 198 202 LYS H H 8.688 0.000 1 333 198 202 LYS C C 178.631 0.000 1 334 198 202 LYS CA C 59.752 0.119 1 335 198 202 LYS N N 121.205 0.000 1 336 199 203 SER H H 7.408 0.000 1 337 199 203 SER CA C 60.665 0.000 1 338 199 203 SER N N 115.675 0.000 1 339 200 204 SER H H 7.398 0.000 1 340 200 204 SER C C 173.331 0.000 1 341 200 204 SER CA C 58.014 0.050 1 342 200 204 SER N N 115.682 0.000 1 343 201 205 LEU H H 6.949 0.000 1 344 201 205 LEU C C 177.143 0.000 1 345 201 205 LEU CA C 54.258 0.010 1 346 201 205 LEU N N 123.599 0.000 1 347 202 206 GLU H H 8.507 0.000 1 348 202 206 GLU C C 176.822 0.000 1 349 202 206 GLU CA C 55.413 0.070 1 350 202 206 GLU CB C 29.613 0.000 1 351 202 206 GLU N N 121.854 0.000 1 352 203 207 GLU H H 8.344 0.000 1 353 203 207 GLU C C 177.494 0.000 1 354 203 207 GLU CA C 58.172 0.171 1 355 203 207 GLU CB C 29.073 0.000 1 356 203 207 GLU N N 122.376 0.000 1 357 204 208 GLY H H 8.430 0.000 1 358 204 208 GLY C C 173.989 0.000 1 359 204 208 GLY CA C 44.874 0.000 1 360 204 208 GLY N N 113.584 0.000 1 361 205 209 GLU H H 7.728 0.000 1 362 205 209 GLU CA C 55.551 0.000 1 363 205 209 GLU N N 121.496 0.000 1 364 206 210 GLU C C 175.522 0.000 1 365 206 210 GLU CA C 54.513 0.000 1 366 207 211 LEU H H 8.360 0.000 1 367 207 211 LEU CA C 54.430 0.000 1 368 207 211 LEU CB C 41.465 0.000 1 369 207 211 LEU N N 124.714 0.000 1 370 210 214 PRO C C 175.268 0.000 1 371 210 214 PRO CA C 62.591 0.000 1 372 211 215 GLU H H 8.255 0.000 1 373 211 215 GLU C C 175.616 0.000 1 374 211 215 GLU CA C 54.143 0.000 1 375 211 215 GLU N N 118.553 0.000 1 376 212 216 ILE H H 8.307 0.000 1 377 212 216 ILE C C 173.251 0.000 1 378 212 216 ILE CA C 60.286 0.000 1 379 212 216 ILE N N 121.146 0.000 1 380 213 217 ALA H H 8.678 0.000 1 381 213 217 ALA C C 174.953 0.000 1 382 213 217 ALA CA C 50.042 0.000 1 383 213 217 ALA N N 128.658 0.000 1 384 214 218 SER H H 9.265 0.000 1 385 214 218 SER C C 170.646 0.031 1 386 214 218 SER CA C 56.154 0.000 1 387 214 218 SER CB C 66.982 0.000 1 388 214 218 SER N N 115.941 0.000 1 389 215 219 ILE H H 8.517 0.000 1 390 215 219 ILE C C 172.230 0.000 1 391 215 219 ILE CA C 59.898 0.122 1 392 215 219 ILE N N 120.544 0.000 1 393 216 220 THR H H 6.861 0.000 1 394 216 220 THR C C 174.493 0.000 1 395 216 220 THR CA C 58.064 0.062 1 396 216 220 THR CB C 72.143 0.000 1 397 216 220 THR N N 114.638 0.000 1 398 217 221 VAL H H 7.924 0.000 1 399 217 221 VAL C C 176.398 0.000 1 400 217 221 VAL CA C 64.764 0.008 1 401 217 221 VAL CB C 30.916 0.000 1 402 217 221 VAL N N 119.251 0.000 1 403 218 222 GLY H H 8.558 0.000 1 404 218 222 GLY C C 173.353 0.000 1 405 218 222 GLY CA C 44.789 0.085 1 406 218 222 GLY N N 116.406 0.000 1 407 219 223 ASN H H 8.316 0.000 1 408 219 223 ASN C C 173.200 0.000 1 409 219 223 ASN CA C 51.919 0.029 1 410 219 223 ASN N N 121.112 0.000 1 411 220 224 LYS H H 7.621 0.000 1 412 220 224 LYS C C 177.198 0.164 1 413 220 224 LYS CA C 54.806 0.028 1 414 220 224 LYS CB C 34.498 0.000 1 415 220 224 LYS N N 115.177 0.000 1 416 221 225 TYR H H 8.262 0.000 1 417 221 225 TYR C C 176.880 0.000 1 418 221 225 TYR CA C 61.880 0.085 1 419 221 225 TYR CB C 39.912 0.000 1 420 221 225 TYR N N 120.496 0.000 1 421 222 226 ARG H H 9.363 0.000 1 422 222 226 ARG C C 174.405 0.000 1 423 222 226 ARG CA C 54.626 0.019 1 424 222 226 ARG CB C 32.197 0.000 1 425 222 226 ARG N N 122.451 0.000 1 426 223 227 ILE H H 8.395 0.000 1 427 223 227 ILE C C 176.990 0.044 1 428 223 227 ILE CA C 59.880 0.009 1 429 223 227 ILE CB C 36.687 0.000 1 430 223 227 ILE N N 127.053 0.000 1 431 224 228 TYR H H 9.043 0.000 1 432 224 228 TYR C C 176.267 0.000 1 433 224 228 TYR CA C 58.088 0.009 1 434 224 228 TYR CB C 37.649 0.000 1 435 224 228 TYR N N 131.235 0.000 1 436 225 229 ASP H H 8.814 0.000 1 437 225 229 ASP CA C 53.249 0.000 1 438 225 229 ASP CB C 42.308 0.000 1 439 225 229 ASP N N 123.086 0.000 1 440 227 231 GLU C C 178.631 0.000 1 441 228 232 GLU H H 7.621 0.000 1 442 228 232 GLU C C 178.687 0.000 1 443 228 232 GLU CA C 58.676 0.000 1 444 228 232 GLU N N 120.016 0.000 1 445 229 233 VAL H H 7.969 0.000 1 446 229 233 VAL C C 178.190 0.000 1 447 229 233 VAL CA C 66.521 0.000 1 448 229 233 VAL N N 117.973 0.000 1 449 230 234 LYS H H 7.553 0.000 1 450 230 234 LYS C C 178.515 0.000 1 451 230 234 LYS CA C 59.025 0.072 1 452 230 234 LYS N N 115.608 0.000 1 453 231 235 LYS H H 7.128 0.000 1 454 231 235 LYS C C 177.495 0.045 1 455 231 235 LYS CA C 57.890 0.000 1 456 231 235 LYS N N 116.883 0.000 1 457 232 236 PHE H H 7.810 0.000 1 458 232 236 PHE C C 174.514 0.000 1 459 232 236 PHE CA C 58.305 0.076 1 460 232 236 PHE N N 116.391 0.000 1 461 233 237 LEU H H 6.883 0.000 1 462 233 237 LEU C C 178.120 0.000 1 463 233 237 LEU CA C 56.494 0.000 1 464 233 237 LEU CB C 41.478 0.000 1 465 233 237 LEU N N 124.684 0.000 1 stop_ save_