data_19560 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; N-terminal and Middle domains of human Hsp90alpha ; _BMRB_accession_number 19560 _BMRB_flat_file_name bmr19560.str _Entry_type original _Submission_date 2013-10-15 _Accession_date 2013-10-15 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details "1HN, 15N, 13Calpha, 13Cbeta, 13C' for isolated N-terminal and middle domains of human Hsp90alpha" loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Dyson Jane . . 2 Park 'Sung Jean' . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 404 "13C chemical shifts" 1181 "15N chemical shifts" 404 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-11-27 update author 'update chemical shifts' 2013-11-11 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The client protein p53 forms a molten globule-like state in the presence of Hsp90' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21460846 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Dyson 'H. Jane' . . 2 Park 'Sung Jean' . . 3 Martinez-Yamout Maria A. . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_volume 18 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 537 _Page_last 542 _Year 2011 _Details . loop_ _Keyword chaperone 'client protein' 'protein-protein interaction' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Middle domain of Hsp90alpha' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'N-terminal domain' $Hsp90_N_domain 'Middle domain' $Hsp90_M_domain stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'molecular chaperone' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Hsp90_N_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Hsp90_N_domain _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'molecular chaperone' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 221 _Mol_residue_sequence ; GHVETFAFQAEIAQLMSLII NTFYSNKEIFLRELISNSSD ALDKIRYETLTDPSKLDSGK ELHINLIPNKQDRTLTIVDT GIGMTKADLINNLGTIAKSG TKAFMEALQAGADISMIGQF GVGFYSAYLVAEKVTVITKH NDDEQYAWESSAGGSFTVRT DTGEPMGRGTKVILHLKEDQ TEYLEERRIKEIVKKHSQFI GYPITLFVEKERDKEVSDDE A ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 15 GLY 2 16 HIS 3 17 VAL 4 18 GLU 5 19 THR 6 20 PHE 7 21 ALA 8 22 PHE 9 23 GLN 10 24 ALA 11 25 GLU 12 26 ILE 13 27 ALA 14 28 GLN 15 29 LEU 16 30 MET 17 31 SER 18 32 LEU 19 33 ILE 20 34 ILE 21 35 ASN 22 36 THR 23 37 PHE 24 38 TYR 25 39 SER 26 40 ASN 27 41 LYS 28 42 GLU 29 43 ILE 30 44 PHE 31 45 LEU 32 46 ARG 33 47 GLU 34 48 LEU 35 49 ILE 36 50 SER 37 51 ASN 38 52 SER 39 53 SER 40 54 ASP 41 55 ALA 42 56 LEU 43 57 ASP 44 58 LYS 45 59 ILE 46 60 ARG 47 61 TYR 48 62 GLU 49 63 THR 50 64 LEU 51 65 THR 52 66 ASP 53 67 PRO 54 68 SER 55 69 LYS 56 70 LEU 57 71 ASP 58 72 SER 59 73 GLY 60 74 LYS 61 75 GLU 62 76 LEU 63 77 HIS 64 78 ILE 65 79 ASN 66 80 LEU 67 81 ILE 68 82 PRO 69 83 ASN 70 84 LYS 71 85 GLN 72 86 ASP 73 87 ARG 74 88 THR 75 89 LEU 76 90 THR 77 91 ILE 78 92 VAL 79 93 ASP 80 94 THR 81 95 GLY 82 96 ILE 83 97 GLY 84 98 MET 85 99 THR 86 100 LYS 87 101 ALA 88 102 ASP 89 103 LEU 90 104 ILE 91 105 ASN 92 106 ASN 93 107 LEU 94 108 GLY 95 109 THR 96 110 ILE 97 111 ALA 98 112 LYS 99 113 SER 100 114 GLY 101 115 THR 102 116 LYS 103 117 ALA 104 118 PHE 105 119 MET 106 120 GLU 107 121 ALA 108 122 LEU 109 123 GLN 110 124 ALA 111 125 GLY 112 126 ALA 113 127 ASP 114 128 ILE 115 129 SER 116 130 MET 117 131 ILE 118 132 GLY 119 133 GLN 120 134 PHE 121 135 GLY 122 136 VAL 123 137 GLY 124 138 PHE 125 139 TYR 126 140 SER 127 141 ALA 128 142 TYR 129 143 LEU 130 144 VAL 131 145 ALA 132 146 GLU 133 147 LYS 134 148 VAL 135 149 THR 136 150 VAL 137 151 ILE 138 152 THR 139 153 LYS 140 154 HIS 141 155 ASN 142 156 ASP 143 157 ASP 144 158 GLU 145 159 GLN 146 160 TYR 147 161 ALA 148 162 TRP 149 163 GLU 150 164 SER 151 165 SER 152 166 ALA 153 167 GLY 154 168 GLY 155 169 SER 156 170 PHE 157 171 THR 158 172 VAL 159 173 ARG 160 174 THR 161 175 ASP 162 176 THR 163 177 GLY 164 178 GLU 165 179 PRO 166 180 MET 167 181 GLY 168 182 ARG 169 183 GLY 170 184 THR 171 185 LYS 172 186 VAL 173 187 ILE 174 188 LEU 175 189 HIS 176 190 LEU 177 191 LYS 178 192 GLU 179 193 ASP 180 194 GLN 181 195 THR 182 196 GLU 183 197 TYR 184 198 LEU 185 199 GLU 186 200 GLU 187 201 ARG 188 202 ARG 189 203 ILE 190 204 LYS 191 205 GLU 192 206 ILE 193 207 VAL 194 208 LYS 195 209 LYS 196 210 HIS 197 211 SER 198 212 GLN 199 213 PHE 200 214 ILE 201 215 GLY 202 216 TYR 203 217 PRO 204 218 ILE 205 219 THR 206 220 LEU 207 221 PHE 208 222 VAL 209 223 GLU 210 224 LYS 211 225 GLU 212 226 ARG 213 227 ASP 214 228 LYS 215 229 GLU 216 230 VAL 217 231 SER 218 232 ASP 219 233 ASP 220 234 GLU 221 235 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 1BYQ "Hsp90 N-Terminal Domain Bound To Adp-Mg" 99.10 228 100.00 100.00 6.44e-157 PDB 1OSF "Human Hsp90 In Complex With 17-desmethoxy-17-n,n- Dimethylaminoethylamino-geldanamycin" 93.67 215 99.52 100.00 1.28e-147 PDB 1UY6 "Human Hsp90-Alpha With 9-Butyl-8-(3,4,5-Trimethoxy-Benzyl)-9h-Purin-6-Ylamine" 99.10 236 99.54 100.00 9.56e-157 PDB 1UY7 "Human Hsp90-alpha With 9-butyl-8-(4-methoxy-benzyl)-9h-purin-6-ylamine" 99.10 236 99.54 100.00 9.56e-157 PDB 1UY8 "Human Hsp90-Alpha With 9-Butyl-8-(3-Trimethoxy-Benzyl)-9h-Purin-6ylamine" 99.10 236 99.54 100.00 9.56e-157 PDB 1UY9 "Human Hsp90-Alpha With 8-Benzo[1,3]dioxol-,5-Ylmethyl-9-Butyl-9h-Purin-6-Ylamine" 99.10 236 99.54 100.00 9.56e-157 PDB 1UYC "Human Hsp90-Alpha With 9-Butyl-8-(2,5-Dimethoxy-Benzyl)-9h-Purin-6-Ylamine" 99.10 236 99.54 100.00 9.56e-157 PDB 1UYD "Human Hsp90-Alpha With 9-Butyl-8- (2-Chloro-3,4,5-Trimethoxy-Benzyl)-9h-Purin-6-Ylamine" 99.10 236 99.54 100.00 9.56e-157 PDB 1UYE "Human Hsp90-Alpha With 8-(2-Chloro-3,4,5-Trimethoxy-Benzyl) -9-Pent-4-Ylnyl-9h-Purin-6-Ylamine" 99.10 236 99.54 100.00 9.56e-157 PDB 1UYF "Human Hsp90-Alpha With 8-(2-Chloro-3,4,5-Trimethoxy-Benzyl) -2-Fluoro-9-Pent-4-Ylnyl-9h-Purin-6-Ylamine" 99.10 236 99.54 100.00 9.56e-157 PDB 1UYG "Human Hsp90-Alpha With 8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9h-Purin-6-Ylamine" 99.10 236 99.54 100.00 9.56e-157 PDB 1UYH "Human Hsp90-Alpha With 9-Butyl-8- (2,5-Dimethoxy-Benzyl)-2-Fluoro-9h-Purin-6-Ylamine" 99.10 236 99.54 100.00 9.56e-157 PDB 1UYI "Human Hsp90-Alpha With 8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9- Pent-9h-Purin-6-Ylamine" 99.55 236 99.55 100.00 8.62e-158 PDB 1UYK "Human Hsp90-Alpha With 8-Benzo[1,3]dioxol-,5-Ylmethyl-9-But Yl-2-Fluoro-9h-Purin-6-Ylamine" 99.10 236 99.54 100.00 9.56e-157 PDB 1UYL "Structure-Activity Relationships In Purine-Based Inhibitor Binding To Hsp90 Isoforms" 99.10 236 99.54 100.00 9.56e-157 PDB 1YC1 "Crystal Structures Of Human Hsp90alpha Complexed With Dihydroxyphenylpyrazoles" 99.10 264 100.00 100.00 9.86e-156 PDB 1YC3 "Crystal Structure Of Human Hsp90alpha Complexed With Dihydroxyphenylpyrazoles" 99.10 264 100.00 100.00 9.86e-156 PDB 1YC4 "Crystal Structure Of Human Hsp90alpha Complexed With Dihydroxyphenylpyrazoles" 99.10 264 100.00 100.00 9.86e-156 PDB 1YER 'Human Hsp90 Geldanamycin-Binding Domain, "closed" Conformation' 99.10 228 100.00 100.00 6.44e-157 PDB 1YES 'Human Hsp90 Geldanamycin-Binding Domain, "open" Conformation' 99.10 228 100.00 100.00 6.44e-157 PDB 1YET "Geldanamycin Bound To The Hsp90 Geldanamycin-Binding Domain" 99.10 228 100.00 100.00 6.44e-157 PDB 2BSM "Novel, Potent Small Molecule Inhibitors Of The Molecular Chaperone Hsp90 Discovered Through Structure-Based Design" 99.10 235 99.54 100.00 1.35e-156 PDB 2BT0 "Novel, Potent Small Molecule Inhibitors Of The Molecular Chaperone Hsp90 Discovered Through Structure-Based Design" 99.10 235 99.54 100.00 1.35e-156 PDB 2BYH "3-(5-Chloro-2,4-Dihydroxyphenyl)-Pyrazole-4-Carboxamides As Inhibitors Of The Hsp90 Molecular Chaperone" 99.10 235 99.54 100.00 1.35e-156 PDB 2BYI "3-(5-Chloro-2,4-Dihydroxyphenyl)-Pyrazole-4-Carboxamides As Inhibitors Of The Hsp90 Molecular Chaperone" 99.10 235 99.54 100.00 1.35e-156 PDB 2BZ5 "Structure-Based Discovery Of A New Class Of Hsp90 Inhibitors" 99.10 235 99.54 100.00 1.35e-156 PDB 2CCS "Human Hsp90 With 4-Chloro-6-(4-Piperazin-1-Yl-1h-Pyrazol-3- Yl)-Benzene-1,2-Diol" 99.10 236 100.00 100.00 3.07e-157 PDB 2CCT "Human Hsp90 With 5-(5-Chloro-2,4-Dihydroxy-Phenyl)-4- Piperazin-1-Yl-2h-Pyrazole-3-Carboxylic Acid Ethylamide" 99.10 236 100.00 100.00 3.07e-157 PDB 2CCU "Human Hsp90 With 4-Chloro-6-(4-(4-(4-Methanesulphonyl- Benzyl)-Pierazin-1-Yl)-1h-Pyrazol-3-Yl)-Benzene-1,3-Diol" 99.10 236 100.00 100.00 3.07e-157 PDB 2FWY "Structure Of Human Hsp90-Alpha Bound To The Potent Water Soluble Inhibitor Pu-H64" 99.10 256 99.54 100.00 2.90e-156 PDB 2FWZ "Structure Of Human Hsp90-alpha Bound To The Potent Water Soluble Inhibitor Pu-h71" 99.10 256 99.54 100.00 2.90e-156 PDB 2H55 "Structure Of Human Hsp90-Alpha Bound To The Potent Water Soluble Inhibitor Pu-Dz8" 99.10 256 99.54 100.00 2.90e-156 PDB 2JJC "Hsp90 Alpha Atpase Domain With Bound Small Molecule Fragment" 93.67 218 99.52 100.00 1.89e-147 PDB 2K5B "Human Cdc37-Hsp90 Docking Model Based On Nmr" 93.67 210 100.00 100.00 2.89e-148 PDB 2QF6 "Hsp90 Complexed With A56322" 93.67 207 100.00 100.00 3.16e-148 PDB 2QFO "Hsp90 Complexed With A143571 And A516383" 93.67 207 99.52 100.00 1.16e-147 PDB 2QG0 "Hsp90 Complexed With A943037" 93.67 207 99.52 100.00 1.16e-147 PDB 2QG2 "Hsp90 Complexed With A917985" 93.67 207 100.00 100.00 3.16e-148 PDB 2UWD "Inhibition Of The Hsp90 Molecular Chaperone In Vitro And In Vivo By Novel, Synthetic, Potent Resorcinylic Pyrazole, Isoxazole A" 99.10 236 99.54 100.00 9.56e-157 PDB 2VCI "4,5 Diaryl Isoxazole Hsp90 Chaperone Inhibitors: Potential Therapeutic Agents For The Treatment Of Cancer" 99.10 236 99.54 100.00 9.56e-157 PDB 2VCJ "4,5 Diaryl Isoxazole Hsp90 Chaperone Inhibitors: Potential Therapeutic Agents For The Treatment Of Cancer" 99.10 236 99.54 100.00 9.56e-157 PDB 2WI1 "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" 99.10 236 99.54 100.00 9.56e-157 PDB 2WI2 "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" 99.10 236 99.54 100.00 9.56e-157 PDB 2WI3 "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" 99.10 236 99.54 100.00 9.56e-157 PDB 2WI4 "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" 99.10 236 99.54 100.00 9.56e-157 PDB 2WI5 "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" 99.10 236 99.54 100.00 9.56e-157 PDB 2WI6 "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" 99.10 236 99.54 100.00 9.56e-157 PDB 2WI7 "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" 99.10 236 99.54 100.00 9.56e-157 PDB 2XAB "Structure Of Hsp90 With An Inhibitor Bound" 99.10 249 99.54 100.00 3.61e-156 PDB 2XDK "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.10 249 99.54 100.00 3.61e-156 PDB 2XDL "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.10 249 99.54 100.00 3.61e-156 PDB 2XDS "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.10 249 99.54 100.00 3.61e-156 PDB 2XDU "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 94.12 236 99.52 100.00 5.97e-148 PDB 2XDX "Structre Of Hsp90 With Small Molecule Inhibitor Bound" 99.10 249 99.54 100.00 3.61e-156 PDB 2XHR "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.10 249 99.54 100.00 3.61e-156 PDB 2XHT "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.10 249 99.54 100.00 3.61e-156 PDB 2XHX "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.10 249 100.00 100.00 1.00e-156 PDB 2XJG "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.10 249 100.00 100.00 1.00e-156 PDB 2XJJ "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.10 249 99.09 99.54 6.13e-155 PDB 2XJX "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.10 249 99.54 100.00 3.61e-156 PDB 2XK2 "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.10 249 99.54 100.00 3.61e-156 PDB 2YE2 "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.10 252 99.54 100.00 2.96e-156 PDB 2YE3 "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.10 252 99.54 100.00 2.96e-156 PDB 2YE4 "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.10 252 99.54 100.00 2.96e-156 PDB 2YE5 "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.10 252 99.54 100.00 2.96e-156 PDB 2YE6 "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.10 252 99.54 100.00 2.96e-156 PDB 2YE7 "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.55 252 99.55 100.00 1.70e-157 PDB 2YE8 "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.55 252 99.55 100.00 1.70e-157 PDB 2YE9 "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.10 252 99.54 100.00 2.96e-156 PDB 2YEA "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.10 252 99.54 100.00 2.96e-156 PDB 2YEB "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.10 252 99.54 100.00 2.96e-156 PDB 2YEC "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.10 252 99.54 100.00 2.96e-156 PDB 2YED "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.10 252 99.54 100.00 2.96e-156 PDB 2YEE "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.55 252 99.09 99.55 1.85e-156 PDB 2YEF "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.10 252 99.54 100.00 2.96e-156 PDB 2YEG "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.10 252 99.54 100.00 2.96e-156 PDB 2YEH "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.10 252 99.54 100.00 2.96e-156 PDB 2YEI "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.55 252 99.55 100.00 1.70e-157 PDB 2YEJ "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.55 252 99.55 100.00 1.70e-157 PDB 2YI0 "Structural Characterization Of 5-Aryl-4-(5-Substituted-2-4- Dihydroxyphenyl)-1,2,3-Thiadiazole Hsp90 Inhibitors." 96.38 229 99.53 100.00 2.37e-152 PDB 2YI5 "Structural Characterization Of 5-Aryl-4-(5-Substituted-2-4- Dihydroxyphenyl)-1,2,3-Thiadiazole Hsp90 Inhibitors." 96.38 229 99.53 100.00 2.37e-152 PDB 2YI6 "Structural Characterization Of 5-Aryl-4-(5-Substituted-2- 4-Dihydroxyphenyl)-1,2,3-Thiadiazole Hsp90 Inhibitors." 96.38 229 99.53 100.00 2.37e-152 PDB 2YI7 "Structural Characterization Of 5-Aryl-4-(5-Substituted-2-4- Dihydroxyphenyl)-1,2,3-Thiadiazole Hsp90 Inhibitors" 96.38 229 99.53 100.00 2.37e-152 PDB 2YJW "Tricyclic Series Of Hsp90 Inhibitors" 94.57 209 99.04 100.00 3.13e-149 PDB 2YJX "Tricyclic Series Of Hsp90 Inhibitors" 94.57 209 99.04 100.00 3.13e-149 PDB 2YK2 "Tricyclic Series Of Hsp90 Inhibitors" 94.57 209 99.04 100.00 3.13e-149 PDB 2YK9 "Tricyclic Series Of Hsp90 Inhibitors" 94.57 209 99.04 100.00 3.13e-149 PDB 2YKB "Tricyclic Series Of Hsp90 Inhibitors" 94.57 209 99.04 100.00 3.13e-149 PDB 2YKC "Tricyclic Series Of Hsp90 Inhibitors" 94.57 209 99.04 100.00 3.13e-149 PDB 2YKE "Tricyclic Series Of Hsp90 Inhibitors" 94.57 209 99.04 100.00 3.13e-149 PDB 2YKI "Tricyclic Series Of Hsp90 Inhibitors" 94.57 209 99.04 100.00 3.13e-149 PDB 2YKJ "Tricyclic Series Of Hsp90 Inhibitors" 94.57 209 99.04 100.00 3.13e-149 PDB 3B24 "Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazine Fragment Molecule" 99.10 229 99.54 100.00 9.90e-157 PDB 3B25 "Hsp90 Alpha N-terminal Domain In Complex With An Inhibitor Ch4675194" 99.10 229 99.54 100.00 9.90e-157 PDB 3B26 "Hsp90 Alpha N-terminal Domain In Complex With An Inhibitor Ro1127850" 99.10 229 99.54 100.00 9.90e-157 PDB 3B27 "Hsp90 Alpha N-terminal Domain In Complex With An Inhibitor Ro4919127" 99.10 229 99.54 100.00 9.90e-157 PDB 3B28 "Hsp90 Alpha N-terminal Domain In Complex With An Inhibitor Ch5015765" 99.10 229 99.54 100.00 9.90e-157 PDB 3BM9 "Discovery Of Benzisoxazoles As Potent Inhibitors Of Chaperone Hsp90" 99.10 226 99.54 100.00 9.19e-157 PDB 3BMY "Discovery Of Benzisoxazoles As Potent Inhibitors Of Chaperone Hsp90" 99.10 226 99.54 100.00 9.19e-157 PDB 3D0B "Crystal Structure Of Benzamide Tetrahydro-4h-Carbazol-4-One Bound To Hsp90" 97.74 232 99.54 100.00 1.90e-154 PDB 3EKO "Dihydroxylphenyl Amides As Inhibitors Of The Hsp90 Molecular Chaperone" 94.57 226 99.52 100.00 9.06e-149 PDB 3EKR "Dihydroxylphenyl Amides As Inhibitors Of The Hsp90 Molecular Chaperone" 94.57 226 99.52 100.00 9.06e-149 PDB 3FT5 "Structure Of Hsp90 Bound With A Novel Fragment" 99.10 249 99.54 100.00 3.61e-156 PDB 3FT8 "Structure Of Hsp90 Bound With A Noval Fragment." 99.10 249 99.54 100.00 3.61e-156 PDB 3HEK "Hsp90 N-Terminal Domain In Complex With 1-{4-[(2r)-1-(5- Chloro-2,4-Dihydroxybenzoyl)pyrrolidin-2-Yl]benzyl}-3,3- Difluoropyrro" 94.57 226 99.52 100.00 9.06e-149 PDB 3HHU "Human Heat-Shock Protein 90 (Hsp90) In Complex With {4-[3- (2,4-Dihydroxy-5-Isopropyl-Phenyl)-5-Thioxo- 1,5-Dihydro- [1,2,4]tri" 94.12 224 99.52 100.00 2.46e-148 PDB 3HYY "Crystal Structure Of Hsp90 With Fragment 37-D04" 99.10 249 99.54 100.00 3.61e-156 PDB 3HYZ "Crystal Structure Of Hsp90 With Fragment 42-C03" 99.10 249 99.54 100.00 3.61e-156 PDB 3HZ1 "Crystal Structure Of Hsp90 With Fragments 37-D04 And 42-C03" 99.10 249 99.54 100.00 3.61e-156 PDB 3HZ5 "Crystal Structure Of Hsp90 With Fragment Z064" 99.10 249 99.54 100.00 3.61e-156 PDB 3INW "Hsp90 N-Terminal Domain With Pochoxime A" 99.10 228 99.54 100.00 9.65e-157 PDB 3INX "Hsp90 N-Terminal Domain With Pochoxime B" 99.10 228 99.54 100.00 9.65e-157 PDB 3K97 "Hsp90 N-Terminal Domain In Complex With 4-Chloro-6-{[(2r)-2- (2-Methylphenyl)pyrrolidin-1-Yl]carbonyl}benzene-1,3-Diol" 99.10 251 99.54 100.00 6.55e-156 PDB 3K98 "Hsp90 N-Terminal Domain In Complex With (1r)-2-(5-Chloro-2, 4-Dihydroxybenzoyl)-N-Ethylisoindoline-1-Carboxamide" 94.57 232 99.52 100.00 4.52e-149 PDB 3K99 "Hsp90 N-Terminal Domain In Complex With 4-(1,3-Dihydro-2h- Isoindol-2-Ylcarbonyl)benzene-1,3-Diol" 94.57 232 99.52 100.00 4.52e-149 PDB 3MNR "Crystal Structure Of Benzamide Snx-1321 Bound To Hsp90" 97.74 232 99.54 100.00 1.90e-154 PDB 3O0I "Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Pu-h54" 99.10 256 99.54 100.00 2.90e-156 PDB 3OW6 "Crystal Structure Of Hsp90 With N-Aryl-Benzimidazolone I" 93.67 207 100.00 100.00 3.16e-148 PDB 3OWB "Crystal Structure Of Hsp90 With Ver-49009" 93.67 207 100.00 100.00 3.16e-148 PDB 3OWD "Crystal Structure Of Hsp90 With N-Aryl-Benzimidazolone Ii" 93.67 207 100.00 100.00 3.16e-148 PDB 3QDD "Hsp90a N-Terminal Domain In Complex With Biib021" 99.10 237 99.54 100.00 1.18e-156 PDB 3QTF "Design And Sar Of Macrocyclic Hsp90 Inhibitors With Increased Metabolic Stability And Potent Cell-Proliferation Activity" 99.10 226 99.54 100.00 9.19e-157 PDB 3R4M "Optimization Of Potent, Selective, And Orally Bioavailable Pyrrolodinopyrimidine-Containing Inhibitors Of Heat Shock Protein 90" 99.10 228 99.54 100.00 1.61e-156 PDB 3R4N "Optimization Of Potent, Selective, And Orally Bioavailable Pyrrolodinopyrimidine-Containing Inhibitors Of Heat Shock Protein 90" 94.57 226 99.52 100.00 9.06e-149 PDB 3R4O "Optimization Of Potent, Selective, And Orally Bioavailable Pyrrolodinopyrimidine-Containing Inhibitors Of Heat Shock Protein 90" 94.57 226 99.52 100.00 9.06e-149 PDB 3R4P "Optimization Of Potent, Selective, And Orally Bioavailable Pyrrolodinopyrimidine-Containing Inhibitors Of Heat Shock Protein 90" 94.57 226 99.52 100.00 9.06e-149 PDB 3R91 "Macrocyclic Lactams As Potent Hsp90 Inhibitors With Excellent Tumor Exposure And Extended Biomarker Activity." 99.10 226 99.54 100.00 9.19e-157 PDB 3R92 "Discovery Of A Macrocyclic O-Aminobenzamide Hsp90 Inhibitor With Heterocyclic Tether That Shows Extended Biomarker Activity And" 99.10 226 99.54 100.00 9.19e-157 PDB 3RKZ "Discovery Of A Stable Macrocyclic O-Aminobenzamide Hsp90 Inhibitor Capable Of Significantly Decreasing Tumor Volume In A Mouse " 99.10 226 99.54 100.00 9.19e-157 PDB 3RLP "Co-crystal Structure Of The Hsp90 Atp Binding Domain In Complex With 4-(2,4-dichloro-5-methoxyphenyl)-6-methylpyrimidin-2-amine" 94.57 226 99.52 100.00 9.06e-149 PDB 3RLQ "Co-Crystal Structure Of The Hsp90 Atp Binding Domain In Complex With 4-(2,4-Dichloro-5-Methoxyphenyl)-2-Methyl-7h-Pyrrolo[2,3- " 94.57 226 99.52 100.00 9.06e-149 PDB 3RLR "Co-crystal Structure Of The Hsp90 Atp Binding Domain In Complex With 4-(2,4-dichloro-5-methoxyphenyl)-2,6-dimethyl-7h-pyrrolo[2" 94.57 226 99.52 100.00 9.06e-149 PDB 3T0H "Structure Insights Into Mechanisms Of Atp Hydrolysis And The Activation Of Human Hsp90" 99.10 228 99.54 100.00 1.61e-156 PDB 3T0Z "Hsp90 N-Terminal Domain Bound To Atp" 99.10 228 99.54 100.00 1.61e-156 PDB 3T10 "Hsp90 N-Terminal Domain Bound To Acp" 99.10 228 99.54 100.00 1.61e-156 PDB 3T1K "Hsp90 N-Terminal Domain Bound To Anp" 99.10 228 99.54 100.00 1.61e-156 PDB 3T2S "Hsp90 N-Terminal Domain Bound To Ags" 99.10 228 99.54 100.00 1.61e-156 PDB 3TUH "Crystal Structure Of The N-Terminal Domain Of An Hsp90 In The Presence Of An The Inhibitor Ganetespib" 94.12 209 99.52 100.00 2.70e-148 PDB 3VHA "Hsp90 Alpha N-Terminal Domain In Complex With A Macrocyclic Inhibitor" 99.10 229 99.54 100.00 9.90e-157 PDB 3VHC "Hsp90 Alpha N-Terminal Domain In Complex With A Macrocyclic Inhibitor" 99.10 229 99.54 100.00 9.90e-157 PDB 3VHD "Hsp90 Alpha N-Terminal Domain In Complex With A Macrocyclic Inhibitor, Ch5164840" 99.10 229 99.54 100.00 9.90e-157 PDB 3WHA "Hsp90 Alpha N-terminal Domain In Complex With A Tricyclic Inhibitor" 99.10 229 99.54 100.00 9.90e-157 PDB 3WQ9 "Crystal Structure Of Hsp90-alpha N-terminal Domain In Complex With 2- (4-hydroxy-cyclohexylamino)-4-[5-(4-phenyl-imidazol-1-yl)" 99.10 237 99.54 100.00 1.18e-156 PDB 4AWO "Complex Of Hsp90 Atpase Domain With Tropane Derived Inhibitors" 99.10 230 99.54 100.00 1.47e-156 PDB 4AWP "Complex Of Hsp90 Atpase Domain With Tropane Derived Inhibitors" 99.10 230 99.54 100.00 1.47e-156 PDB 4AWQ "Complex Of Hsp90 Atpase Domain With Tropane Derived Inhibitors" 99.10 230 99.54 100.00 1.47e-156 PDB 4B7P "Structure Of Hsp90 With Nms-e973 Inhibitor Bound" 99.10 230 99.54 100.00 2.66e-156 PDB 4BQG "Structure Of Hsp90 With An Inhibitor Bound" 99.10 230 99.54 100.00 2.66e-156 PDB 4BQJ "Structure Of Hsp90 With An Inhibitor Bound" 99.10 230 99.54 100.00 2.66e-156 PDB 4CWF "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" 99.10 230 99.54 100.00 2.66e-156 PDB 4CWN "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" 99.10 230 99.54 100.00 2.66e-156 PDB 4CWO "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" 99.10 230 99.54 100.00 2.66e-156 PDB 4CWP "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" 99.10 230 99.54 100.00 2.66e-156 PDB 4CWQ "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" 99.10 230 99.54 100.00 2.66e-156 PDB 4CWR "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" 99.10 230 99.54 100.00 2.66e-156 PDB 4CWS "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" 99.10 230 99.54 100.00 2.66e-156 PDB 4CWT "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" 99.10 230 99.54 100.00 2.66e-156 PDB 4EEH "Hsp90 Alpha N-Terminal Domain In Complex With An Inhibitor 3-(4- Hydroxy-Phenyl)-1h-Indazol-6-Ol" 99.10 229 99.54 100.00 2.06e-156 PDB 4EFT "Hsp90 Alpha N-Terminal Domain In Complex With An Inhibitor 3- Cyclohexyl-2-(6-Hydroxy-1h-Indazol-3-Yl)-Propionitrile" 99.10 229 99.54 100.00 2.06e-156 PDB 4EFU "Hsp90 Alpha N-Terminal Domain In Complex With An Inhibitor 6-Hydroxy- 3-(3-Methyl-Benzyl)-1h-Indazole-5-Carboxylic Acid Benzyl-" 99.10 229 99.54 100.00 2.06e-156 PDB 4EGH "Hsp90-Alpha Atpase Domain In Complex With (4-Hydroxyphenyl)morpholin- 4-Yl Methanone" 99.10 232 99.54 100.00 2.10e-156 PDB 4EGI "Hsp90-Alpha Atpase Domain In Complex With 2-Amino-4-Ethylthio-6- Methyl-1,3,5-Triazine" 99.10 232 99.54 100.00 2.10e-156 PDB 4EGK "Human Hsp90-Alpha Atpase Domain Bound To Radicicol" 99.10 232 99.54 100.00 2.10e-156 PDB 4FCP "Targetting Conserved Water Molecules: Design Of 4-Aryl-5-Cyanopyrrolo [2,3-D] Pyrimidine Hsp90 Inhibitors Using Fragment-Based " 99.10 236 99.54 100.00 9.56e-157 PDB 4FCQ "Targeting Conserved Water Molecules: Design Of 4-Aryl-5- Cyanopyrrolo[2,3-D]pyrimidine Hsp90 Inhibitors Using Fragment-Based Sc" 99.10 236 99.54 100.00 9.56e-157 PDB 4FCR "Targeting Conserved Water Molecules: Design Of 4-Aryl-5- Cyanopyrrolo[2,3-D]pyrimidine Hsp90 Inhibitors Using Fragment-Based Sc" 99.10 236 99.54 100.00 9.56e-157 PDB 4HY6 "Crystal Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Fj1" 99.10 228 99.54 100.00 1.61e-156 PDB 4JQL "Synthesis Of Benzoquinone-ansamycin-inspired Macrocyclic Lactams From Shikimic Acid" 99.10 249 99.54 100.00 3.61e-156 PDB 4L8Z "Crystal Structure Of Human Hsp90 With Rl1" 99.10 228 99.54 100.00 1.61e-156 PDB 4L90 "Crystal Structure Of Human Hsp90 With Rl3" 99.10 228 99.54 100.00 1.61e-156 PDB 4L91 "Crystal Structure Of Human Hsp90 With X29" 99.10 228 99.54 100.00 1.61e-156 PDB 4L93 "Crystal Structure Of Human Hsp90 With S36" 99.10 228 99.54 100.00 1.61e-156 PDB 4L94 "Crystal Structure Of Human Hsp90 With S46" 99.10 228 99.54 100.00 1.61e-156 PDB 4LWE "Crystal Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Fj2" 94.12 208 99.52 100.00 2.84e-148 PDB 4LWF "Crystal Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Fj3" 94.12 208 99.52 100.00 2.84e-148 PDB 4LWG "Crystal Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Fj4" 94.12 208 99.52 100.00 2.84e-148 PDB 4LWH "Crystal Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Fj5" 94.12 209 99.52 100.00 2.70e-148 PDB 4LWI "Crystal Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Fj6" 94.12 208 99.52 100.00 2.84e-148 PDB 4NH7 "Correlation Between Chemotype-dependent Binding Conformations Of Hsp90 Alpha/beta And Isoform Selectivity" 99.10 233 99.54 100.00 1.99e-156 PDB 4NH8 "Correlation Between Chemotype-dependent Binding Conformations Of Hsp90 Alpha/beta And Isoform Selectivity" 99.10 233 99.54 100.00 1.99e-156 PDB 4O05 "Identification Of Novel Hsp90/isoform Selective Inhibitors Using Structure-based Drug Design. Demonstration Of Potential Utilit" 99.10 233 99.54 100.00 1.99e-156 PDB 4O07 "Identification Of Novel Hsp90/isoform Selective Inhibitors Using Structure-based Drug Design. Demonstration Of Potential Utilit" 99.10 233 99.54 100.00 1.99e-156 PDB 4O09 "Identification Of Novel Hsp90 / Isoform Selective Inhibitors Using Structure-based Drug Design. Demonstration Of Potential Util" 99.10 233 99.54 100.00 1.99e-156 PDB 4O0B "Identification Of Novel Hsp90/isoform Selective Inhibitors Using Structure-based Drug Design. Demonstration Of Potential Utilit" 99.10 233 99.54 100.00 1.99e-156 PDB 4R3M "Crystal Structure Of Human Hsp90 With Jr9" 94.12 209 99.52 100.00 2.70e-148 PDB 4U93 "Crystal Structure Of Hsp90-alpha N-domain Bound To The Inhibitor Nvp- Hsp990" 99.10 236 99.54 100.00 9.56e-157 PDB 4W7T "Crystal Structure Of Hsp90-alpha N-domain Bound To The Inhibitor Nvp- Hsp990" 99.10 236 99.54 100.00 9.56e-157 PDB 4XIP "Discovery Of Novel Oxazepine And Diazepine Carboxamides As Two New Classes Of Heat Shock Protein 90 Inhibitors" 99.10 233 99.54 100.00 1.99e-156 PDB 4XIQ "Discovery Of Novel Oxazepine And Diazepine Carboxamides As Two New Classes Of Heat Shock Protein 90 Inhibitors" 99.10 233 99.54 100.00 1.99e-156 PDB 4XIR "Discovery Of Novel Oxazepine And Diazepine Carboxamides As Two New Classes Of Heat Shock Protein 90 Inhibitors" 99.10 233 99.54 100.00 1.99e-156 PDB 4XIT "Discovery Of Novel Oxazepine And Diazepine Carboxamides As Two New Classes Of Heat Shock Protein 90 Inhibitors" 99.10 233 99.54 100.00 1.99e-156 DBJ BAB20777 "heat shock protein 90 alpha [Equus caballus]" 99.10 719 99.54 100.00 7.85e-151 DBJ BAB23449 "unnamed protein product [Mus musculus]" 99.10 733 99.09 100.00 7.75e-150 DBJ BAC36610 "unnamed protein product [Mus musculus]" 99.10 557 99.09 100.00 1.24e-151 DBJ BAC40681 "unnamed protein product [Mus musculus]" 99.55 274 98.64 99.55 4.09e-156 DBJ BAC82487 "90-kDa heat shock protein alpha [Bos taurus]" 99.10 733 99.54 100.00 1.05e-150 EMBL CAA30255 "unnamed protein product [Homo sapiens]" 99.55 312 99.09 99.55 2.47e-156 EMBL CAA33259 "unnamed protein product [Homo sapiens]" 99.10 732 100.00 100.00 3.94e-151 EMBL CAC39453 "heat shock protein 86 [Rattus norvegicus]" 99.10 733 99.54 100.00 1.08e-150 EMBL CAD21648 "heat shock protein 86 [Rattus norvegicus]" 99.10 733 99.54 100.00 1.08e-150 EMBL CAD66568 "unnamed protein product [Homo sapiens]" 56.11 262 99.19 100.00 8.48e-80 GB AAA36023 "heat shock protein 86, partial [Homo sapiens]" 99.55 312 99.09 99.55 2.47e-156 GB AAA36992 "heat shock protein 90A [Cricetulus griseus]" 99.10 733 98.17 100.00 4.05e-149 GB AAA37868 "heat-shock protein hsp86, partial [Mus musculus]" 99.10 347 99.09 100.00 4.69e-154 GB AAA53068 "heat shock protein 86 [Mus musculus]" 99.10 733 99.09 100.00 7.75e-150 GB AAA63194 "heat shock protein [Homo sapiens]" 99.10 732 99.54 100.00 1.41e-150 REF NP_001012688 "heat shock protein HSP 90-alpha [Bos taurus]" 99.10 733 99.54 100.00 1.05e-150 REF NP_001017963 "heat shock protein HSP 90-alpha isoform 1 [Homo sapiens]" 99.10 854 99.54 100.00 6.83e-149 REF NP_001092042 "heat shock protein HSP 90-alpha [Pan troglodytes]" 99.10 733 99.09 99.54 1.00e-149 REF NP_001157427 "heat shock protein HSP 90-alpha [Equus caballus]" 99.10 733 99.54 100.00 2.17e-150 REF NP_001182596 "heat shock protein 90kDa alpha (cytosolic), class A member 1 [Macaca mulatta]" 99.10 733 99.54 100.00 9.22e-151 SP A5A6K9 "RecName: Full=Heat shock protein HSP 90-alpha" 99.10 733 99.09 99.54 1.00e-149 SP O02705 "RecName: Full=Heat shock protein HSP 90-alpha" 99.10 733 99.54 100.00 9.12e-151 SP P07900 "RecName: Full=Heat shock protein HSP 90-alpha; AltName: Full=Heat shock 86 kDa; Short=HSP 86; Short=HSP86; AltName: Full=Lipopo" 99.10 732 99.54 100.00 1.41e-150 SP P07901 "RecName: Full=Heat shock protein HSP 90-alpha; AltName: Full=Heat shock 86 kDa; Short=HSP 86; Short=HSP86; AltName: Full=Tumor-" 99.10 733 99.09 100.00 7.75e-150 SP P30946 "RecName: Full=Heat shock protein HSP 90-alpha" 99.10 694 98.63 99.54 9.59e-150 TPG DAA17282 "TPA: heat shock protein HSP 90-alpha [Bos taurus]" 99.10 733 99.54 100.00 1.05e-150 stop_ save_ save_Hsp90_M_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Hsp90_M_domain _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'molecular chaperone' stop_ _Details . _Residue_count 261 _Mol_residue_sequence ; KPIWTRNPDDITNEEYGEFY KSLTNDWEDHLAVKHFSVEG QLEFRALLFVPRRAPFDLFE NRKKKNNIKLYVRRVFIMDN CEELIPEYLNFIRGVVDSED LPLNISREMLQQSKILKVIR KNLVKKCLELFTELAEDKEN YKKFYEQFSKNIKLGIHEDS QNRKKLSELLRYYTSASGDE MVSLKDYCTRMKENQKHIYY ITGETKDQVANSAFVERLRK HGLEVIYMIEPIDEYCVQQL KEFEGKTLVSVTKEGLELPE D ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 294 LYS 2 295 PRO 3 296 ILE 4 297 TRP 5 298 THR 6 299 ARG 7 300 ASN 8 301 PRO 9 302 ASP 10 303 ASP 11 304 ILE 12 305 THR 13 306 ASN 14 307 GLU 15 308 GLU 16 309 TYR 17 310 GLY 18 311 GLU 19 312 PHE 20 313 TYR 21 314 LYS 22 315 SER 23 316 LEU 24 317 THR 25 318 ASN 26 319 ASP 27 320 TRP 28 321 GLU 29 322 ASP 30 323 HIS 31 324 LEU 32 325 ALA 33 326 VAL 34 327 LYS 35 328 HIS 36 329 PHE 37 330 SER 38 331 VAL 39 332 GLU 40 333 GLY 41 334 GLN 42 335 LEU 43 336 GLU 44 337 PHE 45 338 ARG 46 339 ALA 47 340 LEU 48 341 LEU 49 342 PHE 50 343 VAL 51 344 PRO 52 345 ARG 53 346 ARG 54 347 ALA 55 348 PRO 56 349 PHE 57 350 ASP 58 351 LEU 59 352 PHE 60 353 GLU 61 354 ASN 62 355 ARG 63 356 LYS 64 357 LYS 65 358 LYS 66 359 ASN 67 360 ASN 68 361 ILE 69 362 LYS 70 363 LEU 71 364 TYR 72 365 VAL 73 366 ARG 74 367 ARG 75 368 VAL 76 369 PHE 77 370 ILE 78 371 MET 79 372 ASP 80 373 ASN 81 374 CYS 82 375 GLU 83 376 GLU 84 377 LEU 85 378 ILE 86 379 PRO 87 380 GLU 88 381 TYR 89 382 LEU 90 383 ASN 91 384 PHE 92 385 ILE 93 386 ARG 94 387 GLY 95 388 VAL 96 389 VAL 97 390 ASP 98 391 SER 99 392 GLU 100 393 ASP 101 394 LEU 102 395 PRO 103 396 LEU 104 397 ASN 105 398 ILE 106 399 SER 107 400 ARG 108 401 GLU 109 402 MET 110 403 LEU 111 404 GLN 112 405 GLN 113 406 SER 114 407 LYS 115 408 ILE 116 409 LEU 117 410 LYS 118 411 VAL 119 412 ILE 120 413 ARG 121 414 LYS 122 415 ASN 123 416 LEU 124 417 VAL 125 418 LYS 126 419 LYS 127 420 CYS 128 421 LEU 129 422 GLU 130 423 LEU 131 424 PHE 132 425 THR 133 426 GLU 134 427 LEU 135 428 ALA 136 429 GLU 137 430 ASP 138 431 LYS 139 432 GLU 140 433 ASN 141 434 TYR 142 435 LYS 143 436 LYS 144 437 PHE 145 438 TYR 146 439 GLU 147 440 GLN 148 441 PHE 149 442 SER 150 443 LYS 151 444 ASN 152 445 ILE 153 446 LYS 154 447 LEU 155 448 GLY 156 449 ILE 157 450 HIS 158 451 GLU 159 452 ASP 160 453 SER 161 454 GLN 162 455 ASN 163 456 ARG 164 457 LYS 165 458 LYS 166 459 LEU 167 460 SER 168 461 GLU 169 462 LEU 170 463 LEU 171 464 ARG 172 465 TYR 173 466 TYR 174 467 THR 175 468 SER 176 469 ALA 177 470 SER 178 471 GLY 179 472 ASP 180 473 GLU 181 474 MET 182 475 VAL 183 476 SER 184 477 LEU 185 478 LYS 186 479 ASP 187 480 TYR 188 481 CYS 189 482 THR 190 483 ARG 191 484 MET 192 485 LYS 193 486 GLU 194 487 ASN 195 488 GLN 196 489 LYS 197 490 HIS 198 491 ILE 199 492 TYR 200 493 TYR 201 494 ILE 202 495 THR 203 496 GLY 204 497 GLU 205 498 THR 206 499 LYS 207 500 ASP 208 501 GLN 209 502 VAL 210 503 ALA 211 504 ASN 212 505 SER 213 506 ALA 214 507 PHE 215 508 VAL 216 509 GLU 217 510 ARG 218 511 LEU 219 512 ARG 220 513 LYS 221 514 HIS 222 515 GLY 223 516 LEU 224 517 GLU 225 518 VAL 226 519 ILE 227 520 TYR 228 521 MET 229 522 ILE 230 523 GLU 231 524 PRO 232 525 ILE 233 526 ASP 234 527 GLU 235 528 TYR 236 529 CYS 237 530 VAL 238 531 GLN 239 532 GLN 240 533 LEU 241 534 LYS 242 535 GLU 243 536 PHE 244 537 GLU 245 538 GLY 246 539 LYS 247 540 THR 248 541 LEU 249 542 VAL 250 543 SER 251 544 VAL 252 545 THR 253 546 LYS 254 547 GLU 255 548 GLY 256 549 LEU 257 550 GLU 258 551 LEU 259 552 PRO 260 553 GLU 261 554 ASP 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 3Q6M "Crystal Structure Of Human Mc-hsp90 In C2221 Space Group" 100.00 448 100.00 100.00 0.00e+00 PDB 3Q6N "Crystal Structure Of Human Mc-hsp90 In P21 Space Group" 100.00 448 100.00 100.00 0.00e+00 DBJ BAB20777 "heat shock protein 90 alpha [Equus caballus]" 100.00 719 99.62 99.62 0.00e+00 DBJ BAB23449 "unnamed protein product [Mus musculus]" 100.00 733 99.23 100.00 0.00e+00 DBJ BAC36610 "unnamed protein product [Mus musculus]" 100.00 557 99.23 100.00 0.00e+00 DBJ BAC82487 "90-kDa heat shock protein alpha [Bos taurus]" 100.00 733 100.00 100.00 0.00e+00 DBJ BAE01934 "unnamed protein product [Macaca fascicularis]" 100.00 733 100.00 100.00 0.00e+00 EMBL CAA30251 "unnamed protein product [Gallus gallus]" 100.00 728 99.23 100.00 0.00e+00 EMBL CAA33259 "unnamed protein product [Homo sapiens]" 100.00 732 100.00 100.00 0.00e+00 EMBL CAC39453 "heat shock protein 86 [Rattus norvegicus]" 100.00 733 99.23 100.00 0.00e+00 EMBL CAD21648 "heat shock protein 86 [Rattus norvegicus]" 100.00 733 99.23 100.00 0.00e+00 EMBL CAD62296 "unnamed protein product [Homo sapiens]" 100.00 413 100.00 100.00 0.00e+00 GB AAA36992 "heat shock protein 90A [Cricetulus griseus]" 100.00 733 97.70 99.23 0.00e+00 GB AAA53068 "heat shock protein 86 [Mus musculus]" 100.00 733 99.23 100.00 0.00e+00 GB AAA63194 "heat shock protein [Homo sapiens]" 100.00 732 100.00 100.00 0.00e+00 GB AAC25497 "Hsp89-alpha-delta-N [Homo sapiens]" 100.00 539 100.00 100.00 0.00e+00 GB AAC48718 "90-kDa heat shock protein [Sus scrofa]" 100.00 733 100.00 100.00 0.00e+00 REF NP_001012688 "heat shock protein HSP 90-alpha [Bos taurus]" 100.00 733 100.00 100.00 0.00e+00 REF NP_001016282 "heat shock protein 90kDa alpha (cytosolic), class A member 1, gene 1 [Xenopus (Silurana) tropicalis]" 100.00 729 98.08 99.62 0.00e+00 REF NP_001017963 "heat shock protein HSP 90-alpha isoform 1 [Homo sapiens]" 100.00 854 100.00 100.00 0.00e+00 REF NP_001092042 "heat shock protein HSP 90-alpha [Pan troglodytes]" 100.00 733 100.00 100.00 0.00e+00 REF NP_001103255 "heat shock protein HSP 90-alpha [Gallus gallus]" 100.00 728 99.23 100.00 0.00e+00 SP A5A6K9 "RecName: Full=Heat shock protein HSP 90-alpha [Pan troglodytes]" 100.00 733 100.00 100.00 0.00e+00 SP O02705 "RecName: Full=Heat shock protein HSP 90-alpha [Sus scrofa]" 100.00 733 100.00 100.00 0.00e+00 SP P07900 "RecName: Full=Heat shock protein HSP 90-alpha; AltName: Full=Heat shock 86 kDa; Short=HSP 86; Short=HSP86; AltName: Full=Lipopo" 100.00 732 100.00 100.00 0.00e+00 SP P07901 "RecName: Full=Heat shock protein HSP 90-alpha; AltName: Full=Heat shock 86 kDa; Short=HSP 86; Short=HSP86; AltName: Full=Tumor-" 100.00 733 99.23 100.00 0.00e+00 SP P11501 "RecName: Full=Heat shock protein HSP 90-alpha [Gallus gallus]" 100.00 728 99.23 100.00 0.00e+00 TPG DAA17282 "TPA: heat shock protein HSP 90-alpha [Bos taurus]" 100.00 733 100.00 100.00 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Hsp90_N_domain Human 9606 Eukaryota Metazoa Homo sapiens $Hsp90_M_domain 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 $Hsp90_N_domain 'recombinant technology' . Escherichia coli BL21(DE3)DNAY pET21 $Hsp90_M_domain 'recombinant technology' . Escherichia coli BL21(DE3)DNAY pET21 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'sample details can be found in the published papers (NSMB 18, 537 and JMB 411, 158)' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Hsp90_N_domain . mM 0.1 0.3 '[U-100% 13C; U-100% 15N; U-80% 2H]' 'sodium phosphate' 25 mM . . 'natural abundance' 'sodium chloride' 100 mM . . 'natural abundance' EDTA 1 mM . . 'natural abundance' DTT 4 mM . . 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details 'sample details can be found in the published papers (NSMB 18, 537 and JMB 411, 158)' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Hsp90_M_domain . mM 0.1 0.3 '[U-100% 13C; U-100% 15N; U-80% 2H]' 'sodium phosphate' 25 mM . . 'natural abundance' 'sodium chloride' 100 mM . . 'natural abundance' EDTA 1 mM . . 'natural abundance' DTT 4 mM . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version 5 loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'data analysis' 'peak picking' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_UXNMR _Saveframe_category software _Name UXNMR _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details cryoprobe save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _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_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(COCA)CB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _Sample_label $sample_1 save_ save_3D_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _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' 0.1 . M pH 7.2 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HNCA' '3D HN(CO)CA' '3D HNCACB' '3D HN(COCA)CB' '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 'N-terminal domain' _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 16 2 HIS C C 173.025 0.05 1 2 16 2 HIS CA C 54.098 0.05 1 3 16 2 HIS CB C 27.20 0.05 1 4 17 3 VAL H H 7.91 0.05 1 5 17 3 VAL C C 172.59 0.05 1 6 17 3 VAL CA C 58.733 0.05 1 7 17 3 VAL CB C 30.67 0.05 1 8 17 3 VAL N N 120.91 0.05 1 9 18 4 GLU H H 8.34 0.05 1 10 18 4 GLU C C 171.72 0.05 1 11 18 4 GLU CA C 53.066 0.05 1 12 18 4 GLU CB C 30.16 0.05 1 13 18 4 GLU N N 126.44 0.05 1 14 19 5 THR H H 7.83 0.05 1 15 19 5 THR C C 170.23 0.05 1 16 19 5 THR CA C 59.252 0.05 1 17 19 5 THR CB C 67.034 0.05 1 18 19 5 THR N N 118.61 0.05 1 19 20 6 PHE H H 8.57 0.05 1 20 20 6 PHE C C 170.83 0.05 1 21 20 6 PHE CA C 53.292 0.05 1 22 20 6 PHE CB C 39.353 0.05 1 23 20 6 PHE N N 125.35 0.05 1 24 21 7 ALA H H 8.15 0.05 1 25 21 7 ALA C C 176.28 0.05 1 26 21 7 ALA CA C 48.072 0.05 1 27 21 7 ALA CB C 16.473 0.05 1 28 21 7 ALA N N 122.50 0.05 1 29 22 8 PHE H H 7.58 0.05 1 30 22 8 PHE C C 176.16 0.05 1 31 22 8 PHE CA C 57.319 0.05 1 32 22 8 PHE CB C 37.821 0.05 1 33 22 8 PHE N N 118.56 0.05 1 34 25 11 GLU C C 175.87 0.05 1 35 25 11 GLU CA C 57.64 0.05 1 36 26 12 ILE H H 7.16 0.05 1 37 26 12 ILE CA C 61.38 0.05 1 38 26 12 ILE N N 120.04 0.05 1 39 27 13 ALA H H 8.08 0.05 1 40 27 13 ALA C C 178.16 0.05 1 41 27 13 ALA CA C 52.68 0.05 1 42 27 13 ALA CB C 14.413 0.05 1 43 27 13 ALA N N 121.62 0.05 1 44 28 14 GLN H H 7.80 0.05 1 45 28 14 GLN CA C 56.159 0.05 1 46 28 14 GLN N N 118.71 0.05 1 47 29 15 LEU H H 7.98 0.05 1 48 29 15 LEU C C 175.45 0.05 1 49 29 15 LEU CA C 55.708 0.05 1 50 29 15 LEU CB C 37.635 0.05 1 51 29 15 LEU N N 123.21 0.05 1 52 30 16 MET H H 8.23 0.05 1 53 30 16 MET C C 174.26 0.05 1 54 30 16 MET CA C 57.899 0.05 1 55 30 16 MET CB C 30.328 0.05 1 56 30 16 MET N N 116.90 0.05 1 57 31 17 SER H H 7.51 0.05 1 58 31 17 SER C C 173.83 0.05 1 59 31 17 SER CA C 58.995 0.05 1 60 31 17 SER CB C 59.956 0.05 1 61 31 17 SER N N 111.87 0.05 1 62 32 18 LEU H H 7.70 0.05 1 63 32 18 LEU C C 177.15 0.05 1 64 32 18 LEU CA C 55.612 0.05 1 65 32 18 LEU CB C 38.836 0.05 1 66 32 18 LEU N N 122.02 0.05 1 67 33 19 ILE H H 8.04 0.05 1 68 33 19 ILE C C 175.68 0.05 1 69 33 19 ILE CA C 62.345 0.05 1 70 33 19 ILE CB C 34.532 0.05 1 71 33 19 ILE N N 119.89 0.05 1 72 34 20 ILE H H 7.99 0.05 1 73 34 20 ILE CA C 61.862 0.05 1 74 34 20 ILE N N 116.66 0.05 1 75 35 21 ASN H H 7.58 0.05 1 76 35 21 ASN C C 172.36 0.05 1 77 35 21 ASN CA C 51.745 0.05 1 78 35 21 ASN CB C 37.335 0.05 1 79 35 21 ASN N N 114.64 0.05 1 80 36 22 THR H H 7.19 0.05 1 81 36 22 THR CA C 60.155 0.05 1 82 36 22 THR N N 116.80 0.05 1 83 37 23 PHE H H 7.18 0.05 1 84 37 23 PHE CA C 48.685 0.05 1 85 37 23 PHE N N 117.34 0.05 1 86 40 26 ASN C C 171.90 0.05 1 87 40 26 ASN CA C 49.555 0.05 1 88 40 26 ASN CB C 34.732 0.05 1 89 41 27 LYS H H 7.78 0.05 1 90 41 27 LYS C C 174.19 0.05 1 91 41 27 LYS CA C 56.546 0.05 1 92 41 27 LYS CB C 29.728 0.05 1 93 41 27 LYS N N 117.24 0.05 1 94 42 28 GLU H H 8.28 0.05 1 95 42 28 GLU C C 172.70 0.05 1 96 42 28 GLU CA C 55.579 0.05 1 97 42 28 GLU CB C 26.224 0.05 1 98 42 28 GLU N N 114.54 0.05 1 99 43 29 ILE H H 6.75 0.05 1 100 43 29 ILE CA C 59.607 0.05 1 101 43 29 ILE N N 112.31 0.05 1 102 44 30 PHE H H 7.84 0.05 1 103 44 30 PHE C C 173.09 0.05 1 104 44 30 PHE CA C 56.9 0.05 1 105 44 30 PHE N N 120.57 0.05 1 106 45 31 LEU H H 5.47 0.05 1 107 45 31 LEU C C 175.34 0.05 1 108 45 31 LEU CA C 53.807 0.05 1 109 45 31 LEU N N 122.58 0.05 1 110 46 32 ARG H H 6.34 0.05 1 111 46 32 ARG C C 176.26 0.05 1 112 46 32 ARG CA C 55.934 0.05 1 113 46 32 ARG CB C 26.124 0.05 1 114 46 32 ARG N N 117.44 0.05 1 115 47 33 GLU H H 7.59 0.05 1 116 47 33 GLU C C 176.60 0.05 1 117 47 33 GLU CA C 55.483 0.05 1 118 47 33 GLU CB C 25.53 0.05 1 119 47 33 GLU N N 116.89 0.05 1 120 48 34 LEU H H 7.74 0.05 1 121 48 34 LEU C C 177.15 0.05 1 122 48 34 LEU CA C 55.354 0.05 1 123 48 34 LEU CB C 37.435 0.05 1 124 48 34 LEU N N 119.53 0.05 1 125 49 35 ILE H H 8.10 0.05 1 126 49 35 ILE C C 175.16 0.05 1 127 49 35 ILE CA C 63.505 0.05 1 128 49 35 ILE CB C 34.332 0.05 1 129 49 35 ILE N N 120.04 0.05 1 130 50 36 SER H H 8.14 0.05 1 131 50 36 SER C C 172.48 0.05 1 132 50 36 SER CA C 59.639 0.05 1 133 50 36 SER N N 116.98 0.05 1 134 51 37 ASN H H 7.76 0.05 1 135 51 37 ASN C C 171.72 0.05 1 136 51 37 ASN CA C 53.389 0.05 1 137 51 37 ASN CB C 34.732 0.05 1 138 51 37 ASN N N 120.22 0.05 1 139 52 38 SER H H 8.25 0.05 1 140 52 38 SER C C 172.50 0.05 1 141 52 38 SER CA C 61.089 0.05 1 142 52 38 SER CB C 60.456 0.05 1 143 52 38 SER N N 120.84 0.05 1 144 53 39 SER H H 8.45 0.05 1 145 53 39 SER C C 173.74 0.05 1 146 53 39 SER CA C 59.188 0.05 1 147 53 39 SER CB C 60.356 0.05 1 148 53 39 SER N N 116.09 0.05 1 149 54 40 ASP H H 8.06 0.05 1 150 54 40 ASP C C 175.71 0.05 1 151 54 40 ASP CA C 54.935 0.05 1 152 54 40 ASP CB C 37.535 0.05 1 153 54 40 ASP N N 119.60 0.05 1 154 55 41 ALA H H 7.73 0.05 1 155 55 41 ALA C C 179.05 0.05 1 156 55 41 ALA CA C 52.551 0.05 1 157 55 41 ALA CB C 16.015 0.05 1 158 55 41 ALA N N 123.30 0.05 1 159 56 42 LEU H H 8.34 0.05 1 160 56 42 LEU C C 175.11 0.05 1 161 56 42 LEU CA C 55.096 0.05 1 162 56 42 LEU CB C 37.535 0.05 1 163 56 42 LEU N N 124.59 0.05 1 164 57 43 ASP H H 8.69 0.05 1 165 57 43 ASP C C 176.23 0.05 1 166 57 43 ASP CA C 54.548 0.05 1 167 57 43 ASP CB C 37.135 0.05 1 168 57 43 ASP N N 119.91 0.05 1 169 58 44 LYS H H 7.64 0.05 1 170 58 44 LYS C C 176.92 0.05 1 171 58 44 LYS CA C 57.674 0.05 1 172 58 44 LYS CB C 29.828 0.05 1 173 58 44 LYS N N 117.36 0.05 1 174 59 45 ILE H H 7.24 0.05 1 175 59 45 ILE CA C 57.513 0.05 1 176 59 45 ILE N N 116.98 0.05 1 177 60 46 ARG H H 8.46 0.05 1 178 60 46 ARG C C 176.99 0.05 1 179 60 46 ARG CA C 57.448 0.05 1 180 60 46 ARG CB C 27.125 0.05 1 181 60 46 ARG N N 127.09 0.05 1 182 61 47 TYR H H 8.57 0.05 1 183 61 47 TYR C C 177.13 0.05 1 184 61 47 TYR CA C 58.415 0.05 1 185 61 47 TYR CB C 34.632 0.05 1 186 61 47 TYR N N 118.48 0.05 1 187 62 48 GLU H H 7.97 0.05 1 188 62 48 GLU C C 172.20 0.05 1 189 62 48 GLU CA C 57.416 0.05 1 190 62 48 GLU CB C 26.925 0.05 1 191 62 48 GLU N N 119.36 0.05 1 192 63 49 THR H H 8.19 0.05 1 193 63 49 THR C C 177.17 0.05 1 194 63 49 THR CA C 57.609 0.05 1 195 63 49 THR CB C 60.657 0.05 1 196 63 49 THR N N 114.19 0.05 1 197 64 50 LEU H H 7.25 0.05 1 198 64 50 LEU C C 176.44 0.05 1 199 64 50 LEU CA C 54.613 0.05 1 200 64 50 LEU CB C 38.135 0.05 1 201 64 50 LEU N N 121.82 0.05 1 202 65 51 THR H H 6.88 0.05 1 203 65 51 THR C C 171.95 0.05 1 204 65 51 THR CA C 59.381 0.05 1 205 65 51 THR CB C 66.762 0.05 1 206 65 51 THR N N 106.48 0.05 1 207 66 52 ASP H H 7.19 0.05 1 208 66 52 ASP C C 170.67 0.05 1 209 66 52 ASP CA C 48.685 0.05 1 210 66 52 ASP CB C 38.236 0.05 1 211 66 52 ASP N N 117.94 0.05 1 212 67 53 PRO C C 176.21 0.05 1 213 67 53 PRO CA C 61.927 0.05 1 214 67 53 PRO CB C 28.927 0.05 1 215 68 54 SER H H 7.93 0.05 1 216 68 54 SER C C 174.24 0.05 1 217 68 54 SER CA C 58.318 0.05 1 218 68 54 SER CB C 60.156 0.05 1 219 68 54 SER N N 115.26 0.05 1 220 69 55 LYS H H 7.72 0.05 1 221 69 55 LYS C C 174.13 0.05 1 222 69 55 LYS CA C 55.064 0.05 1 223 69 55 LYS CB C 29.327 0.05 1 224 69 55 LYS N N 123.13 0.05 1 225 70 56 LEU H H 7.11 0.05 1 226 70 56 LEU C C 175.80 0.05 1 227 70 56 LEU CA C 51.101 0.05 1 228 70 56 LEU CB C 37.235 0.05 1 229 70 56 LEU N N 111.72 0.05 1 230 71 57 ASP H H 7.88 0.05 1 231 71 57 ASP C C 174.45 0.05 1 232 71 57 ASP CA C 54.838 0.05 1 233 71 57 ASP CB C 36.434 0.05 1 234 71 57 ASP N N 123.68 0.05 1 235 72 58 SER H H 7.34 0.05 1 236 72 58 SER C C 171.88 0.05 1 237 72 58 SER CA C 54.194 0.05 1 238 72 58 SER CB C 59.456 0.05 1 239 72 58 SER N N 109.05 0.05 1 240 73 59 GLY H H 7.55 0.05 1 241 73 59 GLY C C 171.92 0.05 1 242 73 59 GLY CA C 44.013 0.05 1 243 73 59 GLY N N 111.49 0.05 1 244 74 60 LYS H H 8.76 0.05 1 245 74 60 LYS C C 174.77 0.05 1 246 74 60 LYS CA C 54.967 0.05 1 247 74 60 LYS CB C 30.228 0.05 1 248 74 60 LYS N N 127.16 0.05 1 249 75 61 GLU H H 7.52 0.05 1 250 75 61 GLU C C 174.24 0.05 1 251 75 61 GLU CA C 53.807 0.05 1 252 75 61 GLU CB C 26.825 0.05 1 253 75 61 GLU N N 116.77 0.05 1 254 76 62 LEU H H 8.53 0.05 1 255 76 62 LEU C C 170.76 0.05 1 256 76 62 LEU CA C 51.327 0.05 1 257 76 62 LEU CB C 37.735 0.05 1 258 76 62 LEU N N 127.39 0.05 1 259 77 63 HIS H H 7.53 0.05 1 260 77 63 HIS C C 169.64 0.05 1 261 77 63 HIS CA C 51.842 0.05 1 262 77 63 HIS CB C 30.128 0.05 1 263 77 63 HIS N N 118.88 0.05 1 264 78 64 ILE H H 8.05 0.05 1 265 78 64 ILE CA C 57.674 0.05 1 266 78 64 ILE CB C 37.935 0.05 1 267 78 64 ILE N N 117.70 0.05 1 268 79 65 ASN H H 9.60 0.05 1 269 79 65 ASN C C 170.62 0.05 1 270 79 65 ASN CA C 48.362 0.05 1 271 79 65 ASN CB C 39.337 0.05 1 272 79 65 ASN N N 125.30 0.05 1 273 80 66 LEU H H 8.88 0.05 1 274 80 66 LEU C C 173.35 0.05 1 275 80 66 LEU CA C 50.714 0.05 1 276 80 66 LEU CB C 41.439 0.05 1 277 80 66 LEU N N 122.19 0.05 1 278 81 67 ILE H H 9.20 0.05 1 279 81 67 ILE CA C 56.288 0.05 1 280 81 67 ILE CB C 38.636 0.05 1 281 81 67 ILE N N 120.05 0.05 1 282 82 68 PRO C C 172.91 0.05 1 283 82 68 PRO CA C 59.478 0.05 1 284 82 68 PRO CB C 30.228 0.05 1 285 83 69 ASN H H 9.00 0.05 1 286 83 69 ASN C C 172.59 0.05 1 287 83 69 ASN CA C 49.973 0.05 1 288 83 69 ASN CB C 37.034 0.05 1 289 83 69 ASN N N 121.45 0.05 1 290 84 70 LYS H H 9.31 0.05 1 291 84 70 LYS C C 175.61 0.05 1 292 84 70 LYS CA C 56.9 0.05 1 293 84 70 LYS CB C 29.728 0.05 1 294 84 70 LYS N N 125.03 0.05 1 295 85 71 GLN H H 8.33 0.05 1 296 85 71 GLN C C 174.77 0.05 1 297 85 71 GLN CA C 56.321 0.05 1 298 85 71 GLN CB C 25.223 0.05 1 299 85 71 GLN N N 119.67 0.05 1 300 86 72 ASP H H 7.51 0.05 1 301 86 72 ASP C C 172.52 0.05 1 302 86 72 ASP CA C 50.875 0.05 1 303 86 72 ASP CB C 38.035 0.05 1 304 86 72 ASP N N 116.46 0.05 1 305 87 73 ARG H H 7.76 0.05 1 306 87 73 ARG C C 171.72 0.05 1 307 87 73 ARG CA C 54.512 0.05 1 308 87 73 ARG CB C 26.525 0.05 1 309 87 73 ARG N N 120.22 0.05 1 310 88 74 THR H H 7.92 0.05 1 311 88 74 THR C C 170.35 0.05 1 312 88 74 THR CA C 55.193 0.05 1 313 88 74 THR CB C 70.266 0.05 1 314 88 74 THR N N 106.09 0.05 1 315 89 75 LEU H H 8.30 0.05 1 316 89 75 LEU C C 171.51 0.05 1 317 89 75 LEU CA C 51.037 0.05 1 318 89 75 LEU CB C 42.139 0.05 1 319 89 75 LEU N N 122.53 0.05 1 320 90 76 THR H H 7.90 0.05 1 321 90 76 THR C C 170.48 0.05 1 322 90 76 THR CA C 59.091 0.05 1 323 90 76 THR CB C 66.963 0.05 1 324 90 76 THR N N 124.17 0.05 1 325 91 77 ILE H H 9.32 0.05 1 326 91 77 ILE C C 172.41 0.05 1 327 91 77 ILE CA C 57.803 0.05 1 328 91 77 ILE N N 127.88 0.05 1 329 92 78 VAL H H 9.51 0.05 1 330 92 78 VAL C C 171.26 0.05 1 331 92 78 VAL CA C 57.803 0.05 1 332 92 78 VAL CB C 31.83 0.05 1 333 92 78 VAL N N 129.75 0.05 1 334 93 79 ASP H H 9.35 0.05 1 335 93 79 ASP C C 173.23 0.05 1 336 93 79 ASP CA C 49.941 0.05 1 337 93 79 ASP CB C 43.841 0.05 1 338 93 79 ASP N N 123.49 0.05 1 339 94 80 THR H H 7.11 0.05 1 340 94 80 THR C C 171.95 0.05 1 341 94 80 THR CA C 56.224 0.05 1 342 94 80 THR CB C 63.559 0.05 1 343 94 80 THR N N 108.93 0.05 1 344 95 81 GLY H H 9.43 0.05 1 345 95 81 GLY C C 169.41 0.05 1 346 95 81 GLY CA C 41.79 0.05 1 347 95 81 GLY N N 108.87 0.05 1 348 96 82 ILE H H 6.73 0.05 1 349 96 82 ILE CA C 59.929 0.05 1 350 96 82 ILE N N 115.71 0.05 1 351 97 83 GLY H H 7.55 0.05 1 352 97 83 GLY CA C 41.113 0.05 1 353 97 83 GLY N N 103.64 0.05 1 354 98 84 MET H H 7.56 0.05 1 355 98 84 MET C C 172.25 0.05 1 356 98 84 MET CA C 52.68 0.05 1 357 98 84 MET CB C 34.632 0.05 1 358 98 84 MET N N 116.85 0.05 1 359 99 85 THR H H 7.92 0.05 1 360 99 85 THR C C 171.17 0.05 1 361 99 85 THR CA C 58.318 0.05 1 362 99 85 THR CB C 67.964 0.05 1 363 99 85 THR N N 112.20 0.05 1 364 100 86 LYS H H 7.77 0.05 1 365 100 86 LYS C C 175.32 0.05 1 366 100 86 LYS CA C 58.177 0.05 1 367 100 86 LYS N N 120.95 0.05 1 368 101 87 ALA H H 7.76 0.05 1 369 101 87 ALA C C 177.10 0.05 1 370 101 87 ALA CA C 51.918 0.05 1 371 101 87 ALA CB C 14.914 0.05 1 372 101 87 ALA N N 116.60 0.05 1 373 102 88 ASP H H 7.29 0.05 1 374 102 88 ASP C C 175.18 0.05 1 375 102 88 ASP CA C 54.4 0.05 1 376 102 88 ASP CB C 37.735 0.05 1 377 102 88 ASP N N 117.53 0.05 1 378 103 89 LEU H H 8.08 0.05 1 379 103 89 LEU C C 174.79 0.05 1 380 103 89 LEU CA C 55.169 0.05 1 381 103 89 LEU N N 121.62 0.05 1 382 104 90 ILE H H 7.45 0.05 1 383 104 90 ILE CA C 62.03 0.05 1 384 104 90 ILE N N 116.04 0.05 1 385 105 91 ASN H H 8.17 0.05 1 386 105 91 ASN CA C 52.687 0.05 1 387 105 91 ASN N N 117.62 0.05 1 388 106 92 ASN H H 8.66 0.05 1 389 106 92 ASN CA C 52.302 0.05 1 390 106 92 ASN N N 116.22 0.05 1 391 107 93 LEU CA C 55.254 0.05 1 392 108 94 GLY H H 7.52 0.05 1 393 108 94 GLY C C 173.34 0.05 1 394 108 94 GLY CA C 43.775 0.05 1 395 108 94 GLY N N 105.54 0.05 1 396 116 102 LYS C C 175.66 0.05 1 397 116 102 LYS CA C 56.976 0.05 1 398 116 102 LYS CB C 29.027 0.05 1 399 117 103 ALA H H 7.77 0.05 1 400 117 103 ALA C C 177.84 0.05 1 401 117 103 ALA CA C 51.97 0.05 1 402 117 103 ALA CB C 15.114 0.05 1 403 117 103 ALA N N 120.61 0.05 1 404 118 104 PHE H H 8.21 0.05 1 405 118 104 PHE C C 173.69 0.05 1 406 118 104 PHE CA C 56.497 0.05 1 407 118 104 PHE CB C 35.033 0.05 1 408 118 104 PHE N N 120.00 0.05 1 409 119 105 MET H H 7.74 0.05 1 410 119 105 MET C C 176.26 0.05 1 411 119 105 MET CA C 57.167 0.05 1 412 119 105 MET CB C 29.828 0.05 1 413 119 105 MET N N 117.40 0.05 1 414 120 106 GLU H H 7.96 0.05 1 415 120 106 GLU C C 176.55 0.05 1 416 120 106 GLU CA C 56.529 0.05 1 417 120 106 GLU CB C 26.224 0.05 1 418 120 106 GLU N N 118.62 0.05 1 419 121 107 ALA H H 7.67 0.05 1 420 121 107 ALA C C 177.79 0.05 1 421 121 107 ALA CA C 52.257 0.05 1 422 121 107 ALA CB C 13.713 0.05 1 423 121 107 ALA N N 124.14 0.05 1 424 122 108 LEU H H 8.20 0.05 1 425 122 108 LEU C C 173.67 0.05 1 426 122 108 LEU CA C 54.967 0.05 1 427 122 108 LEU CB C 38.035 0.05 1 428 122 108 LEU N N 120.12 0.05 1 429 123 109 GLN H H 7.69 0.05 1 430 123 109 GLN C C 173.96 0.05 1 431 123 109 GLN CA C 55.586 0.05 1 432 123 109 GLN CB C 25.223 0.05 1 433 123 109 GLN N N 119.40 0.05 1 434 124 110 ALA H H 7.28 0.05 1 435 124 110 ALA C C 174.77 0.05 1 436 124 110 ALA CA C 49.194 0.05 1 437 124 110 ALA CB C 15.815 0.05 1 438 124 110 ALA N N 120.29 0.05 1 439 125 111 GLY H H 7.54 0.05 1 440 125 111 GLY C C 175.73 0.05 1 441 125 111 GLY CA C 42.632 0.05 1 442 125 111 GLY N N 106.03 0.05 1 443 126 112 ALA H H 7.98 0.05 1 444 126 112 ALA C C 172.68 0.05 1 445 126 112 ALA CA C 49.67 0.05 1 446 126 112 ALA CB C 16.415 0.05 1 447 126 112 ALA N N 123.21 0.05 1 448 127 113 ASP H H 8.03 0.05 1 449 127 113 ASP C C 174.31 0.05 1 450 127 113 ASP CA C 51.234 0.05 1 451 127 113 ASP CB C 41.539 0.05 1 452 127 113 ASP N N 118.50 0.05 1 453 128 114 ILE H H 7.57 0.05 1 454 128 114 ILE CA C 59.02 0.05 1 455 128 114 ILE N N 123.12 0.05 1 456 129 115 SER H H 8.41 0.05 1 457 129 115 SER C C 172.89 0.05 1 458 129 115 SER CA C 57.964 0.05 1 459 129 115 SER CB C 60.256 0.05 1 460 129 115 SER N N 114.41 0.05 1 461 130 116 MET H H 7.85 0.05 1 462 130 116 MET C C 173.64 0.05 1 463 130 116 MET CA C 53.723 0.05 1 464 130 116 MET CB C 29.828 0.05 1 465 130 116 MET N N 119.96 0.05 1 466 131 117 ILE H H 7.69 0.05 1 467 131 117 ILE CA C 62.389 0.05 1 468 131 117 ILE N N 119.40 0.05 1 469 132 118 GLY CA C 44.03 0.05 1 470 133 119 GLN H H 7.88 0.05 1 471 133 119 GLN C C 173.96 0.05 1 472 133 119 GLN CA C 54.393 0.05 1 473 133 119 GLN CB C 24.823 0.05 1 474 133 119 GLN N N 120.01 0.05 1 475 134 120 PHE H H 7.21 0.05 1 476 134 120 PHE C C 173.30 0.05 1 477 134 120 PHE CA C 55.254 0.05 1 478 134 120 PHE CB C 36.934 0.05 1 479 134 120 PHE N N 115.53 0.05 1 480 135 121 GLY H H 7.59 0.05 1 481 135 121 GLY CA C 44.062 0.05 1 482 135 121 GLY N N 108.92 0.05 1 483 136 122 VAL H H 6.48 0.05 1 484 136 122 VAL C C 172.21 0.05 1 485 136 122 VAL CA C 57.008 0.05 1 486 136 122 VAL N N 107.91 0.05 1 487 137 123 GLY H H 8.62 0.05 1 488 137 123 GLY C C 172.84 0.05 1 489 137 123 GLY CA C 44.977 0.05 1 490 137 123 GLY N N 107.65 0.05 1 491 138 124 PHE H H 8.99 0.05 1 492 138 124 PHE C C 172.16 0.05 1 493 138 124 PHE CA C 58.511 0.05 1 494 138 124 PHE CB C 37.034 0.05 1 495 138 124 PHE N N 123.55 0.05 1 496 139 125 TYR H H 7.01 0.05 1 497 139 125 TYR C C 174.24 0.05 1 498 139 125 TYR CA C 58.857 0.05 1 499 139 125 TYR CB C 34.132 0.05 1 500 139 125 TYR N N 110.19 0.05 1 501 140 126 SER H H 7.87 0.05 1 502 140 126 SER C C 172.48 0.05 1 503 140 126 SER CA C 59.304 0.05 1 504 140 126 SER N N 114.29 0.05 1 505 141 127 ALA H H 7.88 0.05 1 506 141 127 ALA C C 175.84 0.05 1 507 141 127 ALA CA C 52.384 0.05 1 508 141 127 ALA CB C 15.614 0.05 1 509 141 127 ALA N N 125.37 0.05 1 510 142 128 TYR H H 7.28 0.05 1 511 142 128 TYR C C 172.66 0.05 1 512 142 128 TYR CA C 58.219 0.05 1 513 142 128 TYR CB C 33.431 0.05 1 514 142 128 TYR N N 111.89 0.05 1 515 143 129 LEU H H 7.94 0.05 1 516 143 129 LEU C C 175.89 0.05 1 517 143 129 LEU CA C 54.903 0.05 1 518 143 129 LEU CB C 40.237 0.05 1 519 143 129 LEU N N 118.48 0.05 1 520 144 130 VAL H H 6.48 0.05 1 521 144 130 VAL C C 170.57 0.05 1 522 144 130 VAL CA C 57.422 0.05 1 523 144 130 VAL N N 102.40 0.05 1 524 145 131 ALA H H 7.55 0.05 1 525 145 131 ALA C C 172.73 0.05 1 526 145 131 ALA CA C 48.016 0.05 1 527 145 131 ALA CB C 18.717 0.05 1 528 145 131 ALA N N 124.25 0.05 1 529 146 132 GLU H H 8.40 0.05 1 530 146 132 GLU C C 172.45 0.05 1 531 146 132 GLU CA C 53.181 0.05 1 532 146 132 GLU CB C 27.626 0.05 1 533 146 132 GLU N N 117.98 0.05 1 534 147 133 LYS H H 7.30 0.05 1 535 147 133 LYS C C 170.30 0.05 1 536 147 133 LYS CA C 52.99 0.05 1 537 147 133 LYS CB C 32.33 0.05 1 538 147 133 LYS N N 116.88 0.05 1 539 148 134 VAL H H 7.93 0.05 1 540 148 134 VAL C C 171.28 0.05 1 541 148 134 VAL CA C 58.793 0.05 1 542 148 134 VAL CB C 32.33 0.05 1 543 148 134 VAL N N 125.85 0.05 1 544 149 135 THR H H 8.94 0.05 1 545 149 135 THR C C 173.90 0.05 1 546 149 135 THR CA C 58.985 0.05 1 547 149 135 THR CB C 67.763 0.05 1 548 149 135 THR N N 124.88 0.05 1 549 150 136 VAL H H 10.35 0.05 1 550 150 136 VAL C C 171.67 0.05 1 551 150 136 VAL CA C 58.219 0.05 1 552 150 136 VAL CB C 31.329 0.05 1 553 150 136 VAL N N 128.37 0.05 1 554 151 137 ILE H H 9.49 0.05 1 555 151 137 ILE C C 172.75 0.05 1 556 151 137 ILE CA C 56.223 0.05 1 557 151 137 ILE N N 128.65 0.05 1 558 152 138 THR H H 9.04 0.05 1 559 152 138 THR C C 166.70 0.05 1 560 152 138 THR CA C 57.076 0.05 1 561 152 138 THR CB C 68.564 0.05 1 562 152 138 THR N N 122.07 0.05 1 563 153 139 LYS H H 8.77 0.05 1 564 153 139 LYS C C 169.38 0.05 1 565 153 139 LYS CA C 52.151 0.05 1 566 153 139 LYS CB C 33.831 0.05 1 567 153 139 LYS N N 127.29 0.05 1 568 154 140 HIS H H 9.57 0.05 1 569 154 140 HIS C C 173.80 0.05 1 570 154 140 HIS CA C 51.492 0.05 1 571 154 140 HIS N N 131.91 0.05 1 572 155 141 ASN H H 9.51 0.05 1 573 155 141 ASN CA C 53.245 0.05 1 574 155 141 ASN N N 126.06 0.05 1 575 157 143 ASP H H 8.22 0.05 1 576 157 143 ASP C C 171.26 0.05 1 577 157 143 ASP CA C 50.83 0.05 1 578 157 143 ASP CB C 43.14 0.05 1 579 157 143 ASP N N 123.50 0.05 1 580 158 144 GLU H H 9.22 0.05 1 581 158 144 GLU C C 170.12 0.05 1 582 158 144 GLU CA C 51.686 0.05 1 583 158 144 GLU CB C 27.626 0.05 1 584 158 144 GLU N N 117.77 0.05 1 585 159 145 GLN H H 8.01 0.05 1 586 159 145 GLN C C 173.28 0.05 1 587 159 145 GLN CA C 53.309 0.05 1 588 159 145 GLN CB C 27.726 0.05 1 589 159 145 GLN N N 119.50 0.05 1 590 160 146 TYR H H 8.54 0.05 1 591 160 146 TYR C C 170.83 0.05 1 592 160 146 TYR CA C 55.828 0.05 1 593 160 146 TYR CB C 41.839 0.05 1 594 160 146 TYR N N 124.43 0.05 1 595 161 147 ALA H H 9.19 0.05 1 596 161 147 ALA C C 173.07 0.05 1 597 161 147 ALA CA C 47.792 0.05 1 598 161 147 ALA CB C 19.018 0.05 1 599 161 147 ALA N N 119.92 0.05 1 600 162 148 TRP H H 10.23 0.05 1 601 162 148 TRP C C 173.21 0.05 1 602 162 148 TRP CA C 52.48 0.05 1 603 162 148 TRP CB C 32.73 0.05 1 604 162 148 TRP N N 130.20 0.05 1 605 163 149 GLU H H 8.52 0.05 1 606 163 149 GLU C C 172.36 0.05 1 607 163 149 GLU CA C 53.628 0.05 1 608 163 149 GLU CB C 31.429 0.05 1 609 163 149 GLU N N 126.56 0.05 1 610 164 150 SER H H 8.11 0.05 1 611 164 150 SER C C 174.19 0.05 1 612 164 150 SER CA C 56.848 0.05 1 613 164 150 SER CB C 63.459 0.05 1 614 164 150 SER N N 113.37 0.05 1 615 165 151 SER C C 170.53 0.05 1 616 165 151 SER CA C 55.381 0.05 1 617 166 152 ALA H H 8.98 0.05 1 618 166 152 ALA C C 173.92 0.05 1 619 166 152 ALA CA C 50.988 0.05 1 620 166 152 ALA CB C 13.913 0.05 1 621 166 152 ALA N N 119.63 0.05 1 622 167 153 GLY H H 8.35 0.05 1 623 167 153 GLY C C 172.98 0.05 1 624 167 153 GLY CA C 43.038 0.05 1 625 167 153 GLY N N 106.78 0.05 1 626 168 154 GLY H H 8.37 0.05 1 627 168 154 GLY C C 171.81 0.05 1 628 168 154 GLY CA C 43.193 0.05 1 629 168 154 GLY N N 106.30 0.05 1 630 169 155 SER H H 7.66 0.05 1 631 169 155 SER C C 168.95 0.05 1 632 169 155 SER CA C 54.323 0.05 1 633 169 155 SER CB C 64.56 0.05 1 634 169 155 SER N N 115.45 0.05 1 635 170 156 PHE H H 8.68 0.05 1 636 170 156 PHE C C 169.64 0.05 1 637 170 156 PHE CA C 52.345 0.05 1 638 170 156 PHE CB C 39.036 0.05 1 639 170 156 PHE N N 119.55 0.05 1 640 171 157 THR H H 8.64 0.05 1 641 171 157 THR C C 172.02 0.05 1 642 171 157 THR CA C 56.068 0.05 1 643 171 157 THR CB C 70.065 0.05 1 644 171 157 THR N N 109.26 0.05 1 645 172 158 VAL H H 8.74 0.05 1 646 172 158 VAL C C 171.93 0.05 1 647 172 158 VAL CA C 58.899 0.05 1 648 172 158 VAL CB C 33.231 0.05 1 649 172 158 VAL N N 117.99 0.05 1 650 173 159 ARG H H 8.98 0.05 1 651 173 159 ARG C C 172.68 0.05 1 652 173 159 ARG CA C 51.259 0.05 1 653 173 159 ARG CB C 31.329 0.05 1 654 173 159 ARG N N 124.20 0.05 1 655 174 160 THR H H 8.98 0.05 1 656 174 160 THR C C 171.66 0.05 1 657 174 160 THR CA C 61.187 0.05 1 658 174 160 THR CB C 66.162 0.05 1 659 174 160 THR N N 118.52 0.05 1 660 175 161 ASP H H 8.52 0.05 1 661 175 161 ASP C C 172.41 0.05 1 662 175 161 ASP CA C 51.906 0.05 1 663 175 161 ASP CB C 41.138 0.05 1 664 175 161 ASP N N 126.28 0.05 1 665 176 162 THR H H 7.89 0.05 1 666 176 162 THR C C 172.41 0.05 1 667 176 162 THR CA C 58.092 0.05 1 668 176 162 THR CB C 66.062 0.05 1 669 176 162 THR N N 115.73 0.05 1 670 177 163 GLY H H 7.68 0.05 1 671 177 163 GLY C C 170.18 0.05 1 672 177 163 GLY CA C 41.32 0.05 1 673 177 163 GLY N N 110.07 0.05 1 674 178 164 GLU H H 8.14 0.05 1 675 178 164 GLU CA C 52.097 0.05 1 676 178 164 GLU CB C 26.625 0.05 1 677 178 164 GLU N N 120.86 0.05 1 678 179 165 PRO C C 175.20 0.05 1 679 179 165 PRO CA C 60.547 0.05 1 680 179 165 PRO CB C 29.227 0.05 1 681 180 166 MET H H 9.33 0.05 1 682 180 166 MET C C 174.01 0.05 1 683 180 166 MET CA C 52.288 0.05 1 684 180 166 MET CB C 31.93 0.05 1 685 180 166 MET N N 123.96 0.05 1 686 181 167 GLY H H 8.49 0.05 1 687 181 167 GLY C C 171.15 0.05 1 688 181 167 GLY CA C 44.189 0.05 1 689 181 167 GLY N N 111.40 0.05 1 690 182 168 ARG H H 7.32 0.05 1 691 182 168 ARG C C 171.86 0.05 1 692 182 168 ARG CA C 54.329 0.05 1 693 182 168 ARG CB C 27.325 0.05 1 694 182 168 ARG N N 120.01 0.05 1 695 183 169 GLY H H 9.05 0.05 1 696 183 169 GLY C C 169.59 0.05 1 697 183 169 GLY CA C 41.16 0.05 1 698 183 169 GLY N N 115.50 0.05 1 699 184 170 THR H H 7.61 0.05 1 700 184 170 THR C C 168.26 0.05 1 701 184 170 THR CA C 59.527 0.05 1 702 184 170 THR CB C 69.565 0.05 1 703 184 170 THR N N 115.85 0.05 1 704 185 171 LYS H H 9.90 0.05 1 705 185 171 LYS C C 170.71 0.05 1 706 185 171 LYS CA C 51.587 0.05 1 707 185 171 LYS CB C 32.33 0.05 1 708 185 171 LYS N N 128.32 0.05 1 709 186 172 VAL H H 9.05 0.05 1 710 186 172 VAL C C 171.65 0.05 1 711 186 172 VAL CA C 59.176 0.05 1 712 186 172 VAL CB C 29.928 0.05 1 713 186 172 VAL N N 126.46 0.05 1 714 187 173 ILE H H 9.84 0.05 1 715 187 173 ILE CA C 58.744 0.05 1 716 187 173 ILE N N 127.79 0.05 1 717 188 174 LEU H H 8.76 0.05 1 718 188 174 LEU C C 172.54 0.05 1 719 188 174 LEU CA C 51.337 0.05 1 720 188 174 LEU CB C 38.836 0.05 1 721 188 174 LEU N N 125.84 0.05 1 722 189 175 HIS H H 8.20 0.05 1 723 189 175 HIS C C 172.68 0.05 1 724 189 175 HIS CA C 52.694 0.05 1 725 189 175 HIS CB C 25.323 0.05 1 726 189 175 HIS N N 124.79 0.05 1 727 190 176 LEU H H 7.89 0.05 1 728 190 176 LEU C C 175.18 0.05 1 729 190 176 LEU CA C 53.353 0.05 1 730 190 176 LEU CB C 38.736 0.05 1 731 190 176 LEU N N 123.56 0.05 1 732 191 177 LYS H H 8.31 0.05 1 733 191 177 LYS C C 175.55 0.05 1 734 191 177 LYS CA C 54.297 0.05 1 735 191 177 LYS CB C 30.929 0.05 1 736 191 177 LYS N N 120.51 0.05 1 737 192 178 GLU H H 8.89 0.05 1 738 192 178 GLU C C 173.53 0.05 1 739 192 178 GLU CA C 56.976 0.05 1 740 192 178 GLU CB C 26.725 0.05 1 741 192 178 GLU N N 120.60 0.05 1 742 193 179 ASP H H 8.25 0.05 1 743 193 179 ASP C C 174.63 0.05 1 744 193 179 ASP CA C 50.694 0.05 1 745 193 179 ASP CB C 36.634 0.05 1 746 193 179 ASP N N 113.20 0.05 1 747 194 180 GLN H H 7.73 0.05 1 748 194 180 GLN C C 173.23 0.05 1 749 194 180 GLN CA C 51.268 0.05 1 750 194 180 GLN CB C 24.723 0.05 1 751 194 180 GLN N N 118.42 0.05 1 752 195 181 THR H H 7.29 0.05 1 753 195 181 THR C C 174.63 0.05 1 754 195 181 THR CA C 61.759 0.05 1 755 195 181 THR CB C 65.561 0.05 1 756 195 181 THR N N 106.35 0.05 1 757 196 182 GLU H H 8.74 0.05 1 758 196 182 GLU C C 173.80 0.05 1 759 196 182 GLU CA C 55.955 0.05 1 760 196 182 GLU CB C 25.624 0.05 1 761 196 182 GLU N N 123.95 0.05 1 762 197 183 TYR H H 6.52 0.05 1 763 197 183 TYR C C 168.83 0.05 1 764 197 183 TYR CA C 57.103 0.05 1 765 197 183 TYR CB C 34.232 0.05 1 766 197 183 TYR N N 114.59 0.05 1 767 198 184 LEU H H 7.16 0.05 1 768 198 184 LEU C C 173.76 0.05 1 769 198 184 LEU CA C 50.694 0.05 1 770 198 184 LEU CB C 39.036 0.05 1 771 198 184 LEU N N 110.98 0.05 1 772 199 185 GLU H H 7.18 0.05 1 773 199 185 GLU C C 174.33 0.05 1 774 199 185 GLU CA C 52.288 0.05 1 775 199 185 GLU CB C 27.025 0.05 1 776 199 185 GLU N N 116.51 0.05 1 777 200 186 GLU H H 9.02 0.05 1 778 200 186 GLU C C 174.77 0.05 1 779 200 186 GLU CA C 57.709 0.05 1 780 200 186 GLU CB C 26.725 0.05 1 781 200 186 GLU N N 126.66 0.05 1 782 201 187 ARG H H 8.78 0.05 1 783 201 187 ARG C C 175.64 0.05 1 784 201 187 ARG CA C 56.816 0.05 1 785 201 187 ARG CB C 26.525 0.05 1 786 201 187 ARG N N 116.16 0.05 1 787 202 188 ARG H H 6.64 0.05 1 788 202 188 ARG C C 175.39 0.05 1 789 202 188 ARG CA C 54.393 0.05 1 790 202 188 ARG CB C 27.425 0.05 1 791 202 188 ARG N N 119.33 0.05 1 792 203 189 ILE H H 7.98 0.05 1 793 203 189 ILE CA C 63.048 0.05 1 794 203 189 ILE N N 117.66 0.05 1 795 204 190 LYS H H 8.31 0.05 1 796 204 190 LYS C C 176.69 0.05 1 797 204 190 LYS CA C 57.852 0.05 1 798 204 190 LYS CB C 29.327 0.05 1 799 204 190 LYS N N 116.75 0.05 1 800 205 191 GLU H H 7.58 0.05 1 801 205 191 GLU C C 176.14 0.05 1 802 205 191 GLU CA C 56.378 0.05 1 803 205 191 GLU CB C 26.381 0.05 1 804 205 191 GLU N N 118.57 0.05 1 805 206 192 ILE H H 7.74 0.05 1 806 206 192 ILE C C 171.72 0.05 1 807 206 192 ILE CA C 62.816 0.05 1 808 206 192 ILE CB C 34.732 0.05 1 809 206 192 ILE N N 120.88 0.05 1 810 207 193 VAL H H 8.26 0.05 1 811 207 193 VAL C C 175.68 0.05 1 812 207 193 VAL CA C 64.173 0.05 1 813 207 193 VAL CB C 28.927 0.05 1 814 207 193 VAL N N 120.55 0.05 1 815 208 194 LYS H H 7.80 0.05 1 816 208 194 LYS C C 175.16 0.05 1 817 208 194 LYS CA C 56.145 0.05 1 818 208 194 LYS CB C 29.027 0.05 1 819 208 194 LYS N N 118.71 0.05 1 820 209 195 LYS H H 7.38 0.05 1 821 209 195 LYS C C 175.68 0.05 1 822 209 195 LYS CA C 55.99 0.05 1 823 209 195 LYS CB C 30.528 0.05 1 824 209 195 LYS N N 116.32 0.05 1 825 210 196 HIS H H 7.69 0.05 1 826 210 196 HIS C C 174.70 0.05 1 827 210 196 HIS CA C 54.633 0.05 1 828 210 196 HIS CB C 30.929 0.05 1 829 210 196 HIS N N 113.31 0.05 1 830 211 197 SER H H 7.97 0.05 1 831 211 197 SER C C 174.76 0.05 1 832 211 197 SER CA C 56.306 0.05 1 833 211 197 SER CB C 60.657 0.05 1 834 211 197 SER N N 115.42 0.05 1 835 212 198 GLN C C 173.62 0.05 1 836 212 198 GLN CA C 55.06 0.05 1 837 212 198 GLN CB C 25.323 0.05 1 838 213 199 PHE H H 7.97 0.05 1 839 213 199 PHE C C 172.77 0.05 1 840 213 199 PHE CA C 54.245 0.05 1 841 213 199 PHE CB C 35.133 0.05 1 842 213 199 PHE N N 115.42 0.05 1 843 214 200 ILE H H 7.00 0.05 1 844 214 200 ILE C C 171.86 0.05 1 845 214 200 ILE CA C 56.688 0.05 1 846 214 200 ILE N N 121.50 0.05 1 847 215 201 GLY H H 9.05 0.05 1 848 215 201 GLY C C 170.21 0.05 1 849 215 201 GLY CA C 43.046 0.05 1 850 215 201 GLY N N 115.50 0.05 1 851 216 202 TYR H H 6.62 0.05 1 852 216 202 TYR C C 169.29 0.05 1 853 216 202 TYR CA C 53.222 0.05 1 854 216 202 TYR CB C 37.935 0.05 1 855 216 202 TYR N N 117.60 0.05 1 856 217 203 PRO C C 172.73 0.05 1 857 218 204 ILE H H 7.92 0.05 1 858 218 204 ILE CA C 57.425 0.05 1 859 218 204 ILE N N 123.32 0.05 1 860 219 205 THR H H 8.60 0.05 1 861 219 205 THR C C 169.73 0.05 1 862 219 205 THR CA C 58.55 0.05 1 863 219 205 THR CB C 67.863 0.05 1 864 219 205 THR N N 122.72 0.05 1 865 220 206 LEU H H 8.56 0.05 1 866 220 206 LEU C C 172.82 0.05 1 867 220 206 LEU CA C 51.298 0.05 1 868 220 206 LEU CB C 40.438 0.05 1 869 220 206 LEU N N 127.67 0.05 1 870 221 207 PHE H H 8.68 0.05 1 871 221 207 PHE C C 171.28 0.05 1 872 221 207 PHE CA C 54.749 0.05 1 873 221 207 PHE CB C 36.734 0.05 1 874 221 207 PHE N N 127.21 0.05 1 875 222 208 VAL H H 7.78 0.05 1 876 222 208 VAL C C 172.89 0.05 1 877 222 208 VAL CA C 58.278 0.05 1 878 222 208 VAL CB C 30.628 0.05 1 879 222 208 VAL N N 121.52 0.05 1 880 223 209 GLU H H 8.40 0.05 1 881 223 209 GLU C C 173.62 0.05 1 882 223 209 GLU CA C 54.051 0.05 1 883 223 209 GLU CB C 27.425 0.05 1 884 223 209 GLU N N 125.69 0.05 1 885 229 215 GLU C C 173.35 0.05 1 886 229 215 GLU CA C 53.974 0.05 1 887 229 215 GLU CB C 27.125 0.05 1 888 230 216 VAL H H 8.00 0.05 1 889 230 216 VAL C C 173.28 0.05 1 890 230 216 VAL CA C 59.364 0.05 1 891 230 216 VAL CB C 29.828 0.05 1 892 230 216 VAL N N 120.88 0.05 1 893 231 217 SER H H 8.29 0.05 1 894 231 217 SER C C 171.65 0.05 1 895 231 217 SER CA C 55.37 0.05 1 896 231 217 SER CB C 61.157 0.05 1 897 231 217 SER N N 119.79 0.05 1 898 232 218 ASP H H 8.28 0.05 1 899 232 218 ASP C C 173.30 0.05 1 900 232 218 ASP CA C 51.957 0.05 1 901 232 218 ASP CB C 38.336 0.05 1 902 232 218 ASP N N 122.97 0.05 1 903 233 219 ASP H H 8.13 0.05 1 904 233 219 ASP C C 173.44 0.05 1 905 233 219 ASP CA C 51.996 0.05 1 906 233 219 ASP CB C 38.436 0.05 1 907 233 219 ASP N N 120.15 0.05 1 908 234 220 GLU H H 8.04 0.05 1 909 234 220 GLU C C 172.57 0.05 1 910 234 220 GLU CA C 53.741 0.05 1 911 234 220 GLU CB C 27.325 0.05 1 912 234 220 GLU N N 120.96 0.05 1 913 235 221 ALA H H 7.72 0.05 1 914 235 221 ALA C C 179.94 0.05 1 915 235 221 ALA CA C 51.259 0.05 1 916 235 221 ALA CB C 17.016 0.05 1 917 235 221 ALA N N 130.63 0.05 1 stop_ save_ save_assigned_chem_shift_list_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HNCA' '3D HN(CO)CA' '3D HNCACB' '3D HN(COCA)CB' '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 'Middle domain' _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 1 296 3 ILE C C 174.74 0.05 1 2 297 4 TRP H H 6.07 0.05 1 3 297 4 TRP C C 177.18 0.05 1 4 297 4 TRP CA C 56.16 0.05 1 5 297 4 TRP CB C 24.38 0.05 1 6 297 4 TRP N N 113.93 0.05 1 7 298 5 THR H H 7.29 0.05 1 8 298 5 THR C C 174.20 0.05 1 9 298 5 THR CA C 59.30 0.05 1 10 298 5 THR CB C 66.15 0.05 1 11 298 5 THR N N 114.05 0.05 1 12 299 6 ARG H H 6.89 0.05 1 13 299 6 ARG C C 176.53 0.05 1 14 299 6 ARG CA C 52.59 0.05 1 15 299 6 ARG CB C 27.83 0.05 1 16 299 6 ARG N N 123.55 0.05 1 17 300 7 ASN H H 8.45 0.05 1 18 300 7 ASN CA C 47.93 0.05 1 19 300 7 ASN CB C 35.26 0.05 1 20 300 7 ASN N N 121.46 0.05 1 21 301 8 PRO C C 177.76 0.05 1 22 301 8 PRO CA C 61.94 0.05 1 23 301 8 PRO CB C 28.98 0.05 1 24 302 9 ASP H H 7.90 0.05 1 25 302 9 ASP C C 176.84 0.05 1 26 302 9 ASP CA C 52.89 0.05 1 27 302 9 ASP CB C 36.94 0.05 1 28 302 9 ASP N N 114.38 0.05 1 29 303 10 ASP H H 8.07 0.05 1 30 303 10 ASP C C 175.28 0.05 1 31 303 10 ASP CA C 51.01 0.05 1 32 303 10 ASP CB C 39.45 0.05 1 33 303 10 ASP N N 118.87 0.05 1 34 304 11 ILE H H 7.05 0.05 1 35 304 11 ILE C C 176.33 0.05 1 36 304 11 ILE CA C 58.14 0.05 1 37 304 11 ILE CB C 36.27 0.05 1 38 304 11 ILE N N 123.32 0.05 1 39 305 12 THR H H 8.43 0.05 1 40 305 12 THR CA C 57.74 0.05 1 41 305 12 THR CB C 68.30 0.05 1 42 305 12 THR N N 118.99 0.05 1 43 306 13 ASN C C 178.45 0.05 1 44 306 13 ASN CA C 54.60 0.05 1 45 307 14 GLU H H 8.83 0.05 1 46 307 14 GLU C C 179.25 0.05 1 47 307 14 GLU CA C 57.14 0.05 1 48 307 14 GLU CB C 25.53 0.05 1 49 307 14 GLU N N 120.47 0.05 1 50 308 15 GLU H H 7.72 0.05 1 51 308 15 GLU C C 181.16 0.05 1 52 308 15 GLU CA C 56.44 0.05 1 53 308 15 GLU CB C 26.80 0.05 1 54 308 15 GLU N N 122.48 0.05 1 55 309 16 TYR H H 8.21 0.05 1 56 309 16 TYR C C 178.26 0.05 1 57 309 16 TYR CA C 59.09 0.05 1 58 309 16 TYR CB C 34.71 0.05 1 59 309 16 TYR N N 120.57 0.05 1 60 310 17 GLY H H 8.84 0.05 1 61 310 17 GLY C C 176.02 0.05 1 62 310 17 GLY CA C 44.37 0.05 1 63 310 17 GLY N N 109.03 0.05 1 64 311 18 GLU H H 8.25 0.05 1 65 311 18 GLU C C 179.72 0.05 1 66 311 18 GLU CA C 56.04 0.05 1 67 311 18 GLU CB C 26.02 0.05 1 68 311 18 GLU N N 122.76 0.05 1 69 312 19 PHE H H 7.85 0.05 1 70 312 19 PHE C C 177.33 0.05 1 71 312 19 PHE CA C 58.27 0.05 1 72 312 19 PHE CB C 35.88 0.05 1 73 312 19 PHE N N 121.74 0.05 1 74 313 20 TYR H H 8.95 0.05 1 75 313 20 TYR C C 178.83 0.05 1 76 313 20 TYR CA C 59.03 0.05 1 77 313 20 TYR CB C 33.95 0.05 1 78 313 20 TYR N N 123.07 0.05 1 79 314 21 LYS H H 8.35 0.05 1 80 314 21 LYS C C 179.05 0.05 1 81 314 21 LYS CA C 57.71 0.05 1 82 314 21 LYS CB C 28.53 0.05 1 83 314 21 LYS N N 122.14 0.05 1 84 315 22 SER H H 7.60 0.05 1 85 315 22 SER C C 175.68 0.05 1 86 315 22 SER CA C 57.80 0.05 1 87 315 22 SER CB C 60.13 0.05 1 88 315 22 SER N N 117.40 0.05 1 89 316 23 LEU H H 7.73 0.05 1 90 316 23 LEU C C 178.56 0.05 1 91 316 23 LEU CA C 53.60 0.05 1 92 316 23 LEU CB C 39.27 0.05 1 93 316 23 LEU N N 122.60 0.05 1 94 317 24 THR H H 7.14 0.05 1 95 317 24 THR C C 175.70 0.05 1 96 317 24 THR CA C 58.91 0.05 1 97 317 24 THR CB C 68.35 0.05 1 98 317 24 THR N N 105.79 0.05 1 99 318 25 ASN H H 8.19 0.05 1 100 318 25 ASN C C 173.79 0.05 1 101 318 25 ASN CA C 51.85 0.05 1 102 318 25 ASN CB C 34.55 0.05 1 103 318 25 ASN N N 120.08 0.05 1 104 319 26 ASP H H 7.46 0.05 1 105 319 26 ASP C C 175.77 0.05 1 106 319 26 ASP CA C 51.14 0.05 1 107 319 26 ASP CB C 38.06 0.05 1 108 319 26 ASP N N 121.17 0.05 1 109 320 27 TRP H H 8.07 0.05 1 110 320 27 TRP C C 176.44 0.05 1 111 320 27 TRP CA C 53.72 0.05 1 112 320 27 TRP CB C 25.58 0.05 1 113 320 27 TRP N N 123.19 0.05 1 114 321 28 GLU H H 7.43 0.05 1 115 321 28 GLU C C 174.27 0.05 1 116 321 28 GLU CA C 51.62 0.05 1 117 321 28 GLU CB C 28.82 0.05 1 118 321 28 GLU N N 123.40 0.05 1 119 322 29 ASP H H 7.63 0.05 1 120 322 29 ASP C C 175.03 0.05 1 121 322 29 ASP CA C 50.01 0.05 1 122 322 29 ASP CB C 36.75 0.05 1 123 322 29 ASP N N 116.55 0.05 1 124 323 30 HIS H H 8.31 0.05 1 125 323 30 HIS C C 173.53 0.05 1 126 323 30 HIS CA C 53.20 0.05 1 127 323 30 HIS CB C 27.04 0.05 1 128 323 30 HIS N N 119.24 0.05 1 129 324 31 LEU H H 8.60 0.05 1 130 324 31 LEU C C 177.25 0.05 1 131 324 31 LEU CA C 53.12 0.05 1 132 324 31 LEU CB C 39.89 0.05 1 133 324 31 LEU N N 120.90 0.05 1 134 325 32 ALA H H 7.55 0.05 1 135 325 32 ALA C C 174.13 0.05 1 136 325 32 ALA CA C 47.96 0.05 1 137 325 32 ALA CB C 19.89 0.05 1 138 325 32 ALA N N 116.19 0.05 1 139 326 33 VAL H H 8.73 0.05 1 140 326 33 VAL C C 171.09 0.05 1 141 326 33 VAL CA C 55.39 0.05 1 142 326 33 VAL CB C 30.96 0.05 1 143 326 33 VAL N N 122.54 0.05 1 144 327 34 LYS H H 8.71 0.05 1 145 327 34 LYS C C 172.27 0.05 1 146 327 34 LYS CA C 50.65 0.05 1 147 327 34 LYS CB C 31.00 0.05 1 148 327 34 LYS N N 127.01 0.05 1 149 328 35 HIS H H 9.13 0.05 1 150 328 35 HIS C C 173.53 0.05 1 151 328 35 HIS CA C 48.98 0.05 1 152 328 35 HIS CB C 31.72 0.05 1 153 328 35 HIS N N 132.69 0.05 1 154 329 36 PHE H H 9.04 0.05 1 155 329 36 PHE C C 171.07 0.05 1 156 329 36 PHE CA C 52.63 0.05 1 157 329 36 PHE CB C 38.05 0.05 1 158 329 36 PHE N N 123.28 0.05 1 159 330 37 SER H H 8.44 0.05 1 160 330 37 SER C C 172.76 0.05 1 161 330 37 SER CA C 53.06 0.05 1 162 330 37 SER CB C 62.92 0.05 1 163 330 37 SER N N 114.53 0.05 1 164 331 38 VAL H H 8.40 0.05 1 165 331 38 VAL C C 174.03 0.05 1 166 331 38 VAL CA C 58.78 0.05 1 167 331 38 VAL CB C 30.58 0.05 1 168 331 38 VAL N N 125.60 0.05 1 169 332 39 GLU H H 8.19 0.05 1 170 332 39 GLU C C 175.41 0.05 1 171 332 39 GLU CA C 51.85 0.05 1 172 332 39 GLU CB C 29.26 0.05 1 173 332 39 GLU N N 125.93 0.05 1 174 333 40 GLY H H 8.41 0.05 1 175 333 40 GLY CA C 42.08 0.05 1 176 333 40 GLY N N 111.18 0.05 1 177 334 41 GLN C C 175.38 0.05 1 178 334 41 GLN CA C 55.35 0.05 1 179 334 41 GLN CB C 25.28 0.05 1 180 335 42 LEU H H 7.52 0.05 1 181 335 42 LEU C C 174.57 0.05 1 182 335 42 LEU CA C 50.81 0.05 1 183 335 42 LEU CB C 40.46 0.05 1 184 335 42 LEU N N 119.10 0.05 1 185 336 43 GLU H H 9.27 0.05 1 186 336 43 GLU C C 176.62 0.05 1 187 336 43 GLU CA C 51.36 0.05 1 188 336 43 GLU CB C 28.55 0.05 1 189 336 43 GLU N N 122.73 0.05 1 190 337 44 PHE H H 8.38 0.05 1 191 337 44 PHE C C 171.39 0.05 1 192 337 44 PHE CA C 53.52 0.05 1 193 337 44 PHE CB C 37.34 0.05 1 194 337 44 PHE N N 121.79 0.05 1 195 338 45 ARG H H 8.42 0.05 1 196 338 45 ARG C C 174.17 0.05 1 197 338 45 ARG CA C 51.25 0.05 1 198 338 45 ARG CB C 30.88 0.05 1 199 338 45 ARG N N 118.38 0.05 1 200 339 46 ALA H H 8.48 0.05 1 201 339 46 ALA CA C 47.38 0.05 1 202 339 46 ALA CB C 20.00 0.05 1 203 339 46 ALA N N 122.72 0.05 1 204 344 51 PRO C C 174.32 0.05 1 205 344 51 PRO CA C 59.26 0.05 1 206 345 52 ARG H H 9.27 0.05 1 207 345 52 ARG C C 176.65 0.05 1 208 345 52 ARG CA C 55.04 0.05 1 209 345 52 ARG N N 115.59 0.05 1 210 346 53 ARG H H 7.51 0.05 1 211 346 53 ARG C C 175.15 0.05 1 212 346 53 ARG CA C 49.85 0.05 1 213 346 53 ARG CB C 28.88 0.05 1 214 346 53 ARG N N 114.45 0.05 1 215 347 54 ALA H H 8.30 0.05 1 216 347 54 ALA CA C 47.15 0.05 1 217 347 54 ALA CB C 13.81 0.05 1 218 347 54 ALA N N 126.90 0.05 1 219 356 63 LYS C C 176.60 0.05 1 220 357 64 LYS H H 8.05 0.05 1 221 357 64 LYS C C 176.37 0.05 1 222 357 64 LYS CA C 52.96 0.05 1 223 357 64 LYS CB C 28.92 0.05 1 224 357 64 LYS N N 122.57 0.05 1 225 358 65 LYS H H 8.35 0.05 1 226 358 65 LYS CA C 53.22 0.05 1 227 358 65 LYS CB C 29.64 0.05 1 228 358 65 LYS N N 123.70 0.05 1 229 359 66 ASN C C 175.11 0.05 1 230 360 67 ASN H H 8.98 0.05 1 231 360 67 ASN C C 175.50 0.05 1 232 360 67 ASN CA C 50.26 0.05 1 233 360 67 ASN N N 118.60 0.05 1 234 361 68 ILE H H 8.15 0.05 1 235 361 68 ILE C C 175.51 0.05 1 236 361 68 ILE CA C 57.68 0.05 1 237 361 68 ILE CB C 34.26 0.05 1 238 361 68 ILE N N 123.72 0.05 1 239 362 69 LYS H H 8.65 0.05 1 240 362 69 LYS C C 173.55 0.05 1 241 362 69 LYS CA C 53.46 0.05 1 242 362 69 LYS CB C 31.09 0.05 1 243 362 69 LYS N N 127.45 0.05 1 244 363 70 LEU H H 8.68 0.05 1 245 363 70 LEU C C 173.82 0.05 1 246 363 70 LEU CA C 51.15 0.05 1 247 363 70 LEU CB C 40.21 0.05 1 248 363 70 LEU N N 126.28 0.05 1 249 364 71 TYR H H 9.61 0.05 1 250 364 71 TYR C C 174.66 0.05 1 251 364 71 TYR CA C 53.08 0.05 1 252 364 71 TYR CB C 38.22 0.05 1 253 364 71 TYR N N 129.37 0.05 1 254 365 72 VAL H H 8.94 0.05 1 255 365 72 VAL C C 176.00 0.05 1 256 365 72 VAL CA C 57.71 0.05 1 257 365 72 VAL CB C 31.22 0.05 1 258 365 72 VAL N N 120.89 0.05 1 259 366 73 ARG H H 8.69 0.05 1 260 366 73 ARG C C 176.00 0.05 1 261 366 73 ARG CA C 54.72 0.05 1 262 366 73 ARG CB C 24.36 0.05 1 263 366 73 ARG N N 128.04 0.05 1 264 367 74 ARG H H 9.57 0.05 1 265 367 74 ARG C C 176.17 0.05 1 266 367 74 ARG CA C 55.90 0.05 1 267 367 74 ARG CB C 24.77 0.05 1 268 367 74 ARG N N 111.33 0.05 1 269 368 75 VAL H H 8.44 0.05 1 270 368 75 VAL C C 175.50 0.05 1 271 368 75 VAL CA C 59.07 0.05 1 272 368 75 VAL CB C 29.38 0.05 1 273 368 75 VAL N N 125.71 0.05 1 274 369 76 PHE H H 8.72 0.05 1 275 369 76 PHE C C 174.37 0.05 1 276 369 76 PHE CA C 56.08 0.05 1 277 369 76 PHE CB C 35.05 0.05 1 278 369 76 PHE N N 129.85 0.05 1 279 370 77 ILE H H 8.26 0.05 1 280 370 77 ILE C C 178.04 0.05 1 281 370 77 ILE CA C 56.83 0.05 1 282 370 77 ILE CB C 34.92 0.05 1 283 370 77 ILE N N 127.36 0.05 1 284 371 78 MET H H 6.77 0.05 1 285 371 78 MET C C 173.15 0.05 1 286 371 78 MET CA C 52.86 0.05 1 287 371 78 MET CB C 31.35 0.05 1 288 371 78 MET N N 113.65 0.05 1 289 372 79 ASP H H 8.41 0.05 1 290 372 79 ASP C C 175.15 0.05 1 291 372 79 ASP CA C 49.60 0.05 1 292 372 79 ASP CB C 39.69 0.05 1 293 372 79 ASP N N 121.25 0.05 1 294 373 80 ASN H H 7.60 0.05 1 295 373 80 ASN C C 174.82 0.05 1 296 373 80 ASN CB C 34.61 0.05 1 297 373 80 ASN N N 115.94 0.05 1 298 374 81 CYS H H 9.32 0.05 1 299 374 81 CYS C C 175.84 0.05 1 300 374 81 CYS N N 122.06 0.05 1 301 375 82 GLU H H 8.83 0.05 1 302 375 82 GLU C C 176.56 0.05 1 303 375 82 GLU CA C 56.10 0.05 1 304 375 82 GLU N N 132.80 0.05 1 305 376 83 GLU H H 8.47 0.05 1 306 376 83 GLU C C 177.13 0.05 1 307 376 83 GLU CA C 54.55 0.05 1 308 376 83 GLU CB C 25.35 0.05 1 309 376 83 GLU N N 115.75 0.05 1 310 377 84 LEU H H 7.29 0.05 1 311 377 84 LEU C C 172.89 0.05 1 312 377 84 LEU CA C 54.22 0.05 1 313 377 84 LEU CB C 39.72 0.05 1 314 377 84 LEU N N 120.75 0.05 1 315 378 85 ILE H H 6.66 0.05 1 316 378 85 ILE CA C 54.19 0.05 1 317 378 85 ILE CB C 40.01 0.05 1 318 378 85 ILE N N 109.09 0.05 1 319 379 86 PRO C C 176.55 0.05 1 320 379 86 PRO CA C 59.11 0.05 1 321 379 86 PRO CB C 29.07 0.05 1 322 380 87 GLU H H 8.98 0.05 1 323 380 87 GLU CB C 25.96 0.05 1 324 380 87 GLU N N 123.54 0.05 1 325 381 88 TYR C C 175.38 0.05 1 326 381 88 TYR CB C 32.11 0.05 1 327 382 89 LEU H H 6.94 0.05 1 328 382 89 LEU C C 176.35 0.05 1 329 382 89 LEU CA C 50.02 0.05 1 330 382 89 LEU CB C 36.88 0.05 1 331 382 89 LEU N N 119.96 0.05 1 332 383 90 ASN H H 7.85 0.05 1 333 383 90 ASN C C 175.10 0.05 1 334 383 90 ASN CA C 52.20 0.05 1 335 383 90 ASN CB C 34.19 0.05 1 336 383 90 ASN N N 118.56 0.05 1 337 384 91 PHE H H 6.77 0.05 1 338 384 91 PHE C C 174.30 0.05 1 339 384 91 PHE CA C 52.80 0.05 1 340 384 91 PHE CB C 35.59 0.05 1 341 384 91 PHE N N 115.50 0.05 1 342 385 92 ILE H H 6.83 0.05 1 343 385 92 ILE C C 175.63 0.05 1 344 385 92 ILE CA C 55.78 0.05 1 345 385 92 ILE CB C 32.26 0.05 1 346 385 92 ILE N N 123.56 0.05 1 347 386 93 ARG H H 8.31 0.05 1 348 386 93 ARG C C 175.68 0.05 1 349 386 93 ARG CA C 49.09 0.05 1 350 386 93 ARG CB C 29.23 0.05 1 351 386 93 ARG N N 125.06 0.05 1 352 387 94 GLY H H 8.53 0.05 1 353 387 94 GLY CA C 42.32 0.05 1 354 387 94 GLY N N 107.56 0.05 1 355 389 96 VAL H H 8.46 0.05 1 356 389 96 VAL C C 174.36 0.05 1 357 389 96 VAL CA C 57.62 0.05 1 358 389 96 VAL CB C 31.78 0.05 1 359 389 96 VAL N N 124.94 0.05 1 360 390 97 ASP H H 8.79 0.05 1 361 390 97 ASP C C 177.25 0.05 1 362 390 97 ASP CA C 48.56 0.05 1 363 390 97 ASP CB C 40.00 0.05 1 364 390 97 ASP N N 127.13 0.05 1 365 391 98 SER H H 8.91 0.05 1 366 391 98 SER C C 174.96 0.05 1 367 391 98 SER CA C 53.90 0.05 1 368 391 98 SER CB C 62.23 0.05 1 369 391 98 SER N N 121.87 0.05 1 370 392 99 GLU H H 8.37 0.05 1 371 392 99 GLU C C 177.90 0.05 1 372 392 99 GLU CA C 53.74 0.05 1 373 392 99 GLU N N 125.86 0.05 1 374 393 100 ASP H H 7.70 0.05 1 375 393 100 ASP C C 176.42 0.05 1 376 393 100 ASP CA C 52.36 0.05 1 377 393 100 ASP CB C 41.24 0.05 1 378 393 100 ASP N N 115.16 0.05 1 379 394 101 LEU H H 6.82 0.05 1 380 394 101 LEU CA C 50.54 0.05 1 381 394 101 LEU CB C 38.61 0.05 1 382 394 101 LEU N N 121.44 0.05 1 383 395 102 PRO C C 176.26 0.05 1 384 395 102 PRO CA C 59.14 0.05 1 385 395 102 PRO CB C 28.30 0.05 1 386 396 103 LEU H H 8.03 0.05 1 387 396 103 LEU C C 177.60 0.05 1 388 396 103 LEU CA C 53.02 0.05 1 389 396 103 LEU CB C 38.91 0.05 1 390 396 103 LEU N N 120.37 0.05 1 391 397 104 ASN H H 7.93 0.05 1 392 397 104 ASN C C 174.81 0.05 1 393 397 104 ASN CA C 49.33 0.05 1 394 397 104 ASN CB C 34.07 0.05 1 395 397 104 ASN N N 115.67 0.05 1 396 398 105 ILE H H 7.22 0.05 1 397 398 105 ILE C C 173.79 0.05 1 398 398 105 ILE CA C 57.71 0.05 1 399 398 105 ILE CB C 35.77 0.05 1 400 398 105 ILE N N 119.85 0.05 1 401 399 106 SER H H 7.69 0.05 1 402 399 106 SER CA C 53.50 0.05 1 403 399 106 SER CB C 62.55 0.05 1 404 399 106 SER N N 121.24 0.05 1 405 400 107 ARG C C 178.49 0.05 1 406 401 108 GLU H H 8.69 0.05 1 407 401 108 GLU C C 178.77 0.05 1 408 401 108 GLU CA C 56.50 0.05 1 409 401 108 GLU CB C 25.46 0.05 1 410 401 108 GLU N N 119.35 0.05 1 411 402 109 MET H H 7.56 0.05 1 412 402 109 MET C C 179.55 0.05 1 413 402 109 MET CA C 54.47 0.05 1 414 402 109 MET CB C 29.13 0.05 1 415 402 109 MET N N 119.45 0.05 1 416 403 110 LEU H H 8.10 0.05 1 417 403 110 LEU C C 178.75 0.05 1 418 403 110 LEU CA C 54.89 0.05 1 419 403 110 LEU CB C 37.77 0.05 1 420 403 110 LEU N N 122.83 0.05 1 421 404 111 GLN H H 7.70 0.05 1 422 404 111 GLN C C 176.86 0.05 1 423 404 111 GLN CA C 55.21 0.05 1 424 404 111 GLN CB C 25.12 0.05 1 425 404 111 GLN N N 116.91 0.05 1 426 405 112 GLN H H 7.22 0.05 1 427 405 112 GLN C C 176.16 0.05 1 428 405 112 GLN CA C 51.95 0.05 1 429 405 112 GLN CB C 28.79 0.05 1 430 405 112 GLN N N 115.34 0.05 1 431 406 113 SER H H 7.33 0.05 1 432 406 113 SER CA C 55.72 0.05 1 433 406 113 SER CB C 60.66 0.05 1 434 406 113 SER N N 115.74 0.05 1 435 407 114 LYS C C 178.89 0.05 1 436 407 114 LYS CA C 55.98 0.05 1 437 408 115 ILE H H 7.69 0.05 1 438 408 115 ILE C C 177.72 0.05 1 439 408 115 ILE CA C 61.02 0.05 1 440 408 115 ILE CB C 34.44 0.05 1 441 408 115 ILE N N 120.11 0.05 1 442 409 116 LEU H H 7.32 0.05 1 443 409 116 LEU C C 178.08 0.05 1 444 409 116 LEU CA C 54.45 0.05 1 445 409 116 LEU CB C 37.56 0.05 1 446 409 116 LEU N N 120.25 0.05 1 447 410 117 LYS H H 7.10 0.05 1 448 410 117 LYS C C 179.33 0.05 1 449 410 117 LYS CA C 56.46 0.05 1 450 410 117 LYS CB C 28.59 0.05 1 451 410 117 LYS N N 117.26 0.05 1 452 411 118 VAL H H 7.40 0.05 1 453 411 118 VAL C C 179.70 0.05 1 454 411 118 VAL CA C 63.05 0.05 1 455 411 118 VAL CB C 28.14 0.05 1 456 411 118 VAL N N 121.74 0.05 1 457 412 119 ILE H H 8.03 0.05 1 458 412 119 ILE C C 177.44 0.05 1 459 412 119 ILE CA C 63.50 0.05 1 460 412 119 ILE CB C 33.75 0.05 1 461 412 119 ILE N N 124.46 0.05 1 462 413 120 ARG H H 8.48 0.05 1 463 413 120 ARG C C 177.74 0.05 1 464 413 120 ARG CA C 56.46 0.05 1 465 413 120 ARG CB C 26.73 0.05 1 466 413 120 ARG N N 121.85 0.05 1 467 414 121 LYS H H 7.65 0.05 1 468 414 121 LYS C C 180.07 0.05 1 469 414 121 LYS CA C 56.58 0.05 1 470 414 121 LYS CB C 28.75 0.05 1 471 414 121 LYS N N 117.61 0.05 1 472 415 122 ASN H H 7.69 0.05 1 473 415 122 ASN C C 176.77 0.05 1 474 415 122 ASN CA C 54.40 0.05 1 475 415 122 ASN CB C 38.22 0.05 1 476 415 122 ASN N N 118.34 0.05 1 477 416 123 LEU H H 9.05 0.05 1 478 416 123 LEU C C 179.20 0.05 1 479 416 123 LEU CA C 55.89 0.05 1 480 416 123 LEU CB C 37.24 0.05 1 481 416 123 LEU N N 121.63 0.05 1 482 417 124 VAL H H 8.39 0.05 1 483 417 124 VAL C C 177.39 0.05 1 484 417 124 VAL CA C 64.45 0.05 1 485 417 124 VAL CB C 28.11 0.05 1 486 417 124 VAL N N 120.06 0.05 1 487 418 125 LYS H H 7.44 0.05 1 488 418 125 LYS C C 179.86 0.05 1 489 418 125 LYS CA C 56.63 0.05 1 490 418 125 LYS CB C 29.02 0.05 1 491 418 125 LYS N N 118.73 0.05 1 492 419 126 LYS H H 7.77 0.05 1 493 419 126 LYS CA C 54.16 0.05 1 494 419 126 LYS CB C 28.48 0.05 1 495 419 126 LYS N N 118.70 0.05 1 496 421 128 LEU C C 180.15 0.05 1 497 421 128 LEU CA C 55.15 0.05 1 498 421 128 LEU CB C 36.06 0.05 1 499 422 129 GLU H H 7.79 0.05 1 500 422 129 GLU C C 178.17 0.05 1 501 422 129 GLU CA C 56.35 0.05 1 502 422 129 GLU CB C 26.79 0.05 1 503 422 129 GLU N N 122.47 0.05 1 504 423 130 LEU H H 7.64 0.05 1 505 423 130 LEU CA C 54.24 0.05 1 506 423 130 LEU CB C 36.98 0.05 1 507 423 130 LEU N N 122.20 0.05 1 508 424 131 PHE H H 8.18 0.05 1 509 424 131 PHE C C 177.11 0.05 1 510 424 131 PHE CA C 54.14 0.05 1 511 424 131 PHE CB C 33.80 0.05 1 512 424 131 PHE N N 118.59 0.05 1 513 425 132 THR H H 7.89 0.05 1 514 425 132 THR C C 176.79 0.05 1 515 425 132 THR CA C 63.60 0.05 1 516 425 132 THR CB C 65.60 0.05 1 517 425 132 THR N N 114.89 0.05 1 518 426 133 GLU H H 8.00 0.05 1 519 426 133 GLU C C 181.09 0.05 1 520 426 133 GLU CA C 56.03 0.05 1 521 426 133 GLU CB C 25.33 0.05 1 522 426 133 GLU N N 124.96 0.05 1 523 427 134 LEU H H 8.63 0.05 1 524 427 134 LEU C C 178.72 0.05 1 525 427 134 LEU CA C 54.39 0.05 1 526 427 134 LEU CB C 38.35 0.05 1 527 427 134 LEU N N 123.79 0.05 1 528 428 135 ALA H H 7.49 0.05 1 529 428 135 ALA C C 178.42 0.05 1 530 428 135 ALA CA C 50.33 0.05 1 531 428 135 ALA CB C 13.33 0.05 1 532 428 135 ALA N N 119.13 0.05 1 533 429 136 GLU H H 7.20 0.05 1 534 429 136 GLU C C 176.17 0.05 1 535 429 136 GLU CA C 54.56 0.05 1 536 429 136 GLU CB C 26.38 0.05 1 537 429 136 GLU N N 117.20 0.05 1 538 430 137 ASP H H 7.67 0.05 1 539 430 137 ASP C C 175.08 0.05 1 540 430 137 ASP CA C 49.04 0.05 1 541 430 137 ASP CB C 38.36 0.05 1 542 430 137 ASP N N 121.39 0.05 1 543 431 138 LYS H H 8.41 0.05 1 544 431 138 LYS C C 179.42 0.05 1 545 431 138 LYS CA C 57.51 0.05 1 546 431 138 LYS CB C 28.92 0.05 1 547 431 138 LYS N N 124.47 0.05 1 548 432 139 GLU H H 8.34 0.05 1 549 432 139 GLU C C 179.36 0.05 1 550 432 139 GLU CA C 55.90 0.05 1 551 432 139 GLU CB C 25.79 0.05 1 552 432 139 GLU N N 118.66 0.05 1 553 433 140 ASN H H 8.00 0.05 1 554 433 140 ASN C C 178.50 0.05 1 555 433 140 ASN CA C 52.47 0.05 1 556 433 140 ASN CB C 35.07 0.05 1 557 433 140 ASN N N 119.91 0.05 1 558 434 141 TYR H H 9.31 0.05 1 559 434 141 TYR C C 177.83 0.05 1 560 434 141 TYR CA C 59.96 0.05 1 561 434 141 TYR CB C 34.07 0.05 1 562 434 141 TYR N N 123.70 0.05 1 563 435 142 LYS H H 7.71 0.05 1 564 435 142 LYS C C 179.14 0.05 1 565 435 142 LYS CA C 56.94 0.05 1 566 435 142 LYS CB C 28.84 0.05 1 567 435 142 LYS N N 118.34 0.05 1 568 436 143 LYS H H 7.05 0.05 1 569 436 143 LYS C C 178.97 0.05 1 570 436 143 LYS CA C 55.90 0.05 1 571 436 143 LYS CB C 28.59 0.05 1 572 436 143 LYS N N 118.42 0.05 1 573 437 144 PHE H H 7.49 0.05 1 574 437 144 PHE C C 176.03 0.05 1 575 437 144 PHE CA C 57.14 0.05 1 576 437 144 PHE CB C 36.00 0.05 1 577 437 144 PHE N N 120.18 0.05 1 578 438 145 TYR H H 9.18 0.05 1 579 438 145 TYR C C 176.88 0.05 1 580 438 145 TYR CA C 59.57 0.05 1 581 438 145 TYR CB C 35.29 0.05 1 582 438 145 TYR N N 123.80 0.05 1 583 439 146 GLU H H 7.77 0.05 1 584 439 146 GLU C C 178.47 0.05 1 585 439 146 GLU CA C 55.53 0.05 1 586 439 146 GLU CB C 26.24 0.05 1 587 439 146 GLU N N 117.17 0.05 1 588 440 147 GLN H H 6.45 0.05 1 589 440 147 GLN C C 178.01 0.05 1 590 440 147 GLN CA C 53.09 0.05 1 591 440 147 GLN CB C 25.18 0.05 1 592 440 147 GLN N N 113.76 0.05 1 593 441 148 PHE H H 7.45 0.05 1 594 441 148 PHE C C 176.08 0.05 1 595 441 148 PHE CA C 55.01 0.05 1 596 441 148 PHE CB C 34.92 0.05 1 597 441 148 PHE N N 114.85 0.05 1 598 442 149 SER H H 7.64 0.05 1 599 442 149 SER C C 176.65 0.05 1 600 442 149 SER CA C 59.22 0.05 1 601 442 149 SER CB C 57.14 0.05 1 602 442 149 SER N N 118.97 0.05 1 603 443 150 LYS H H 7.94 0.05 1 604 443 150 LYS C C 177.37 0.05 1 605 443 150 LYS CA C 56.69 0.05 1 606 443 150 LYS CB C 28.09 0.05 1 607 443 150 LYS N N 121.79 0.05 1 608 444 151 ASN H H 7.31 0.05 1 609 444 151 ASN CA C 55.33 0.05 1 610 444 151 ASN CB C 35.00 0.05 1 611 444 151 ASN N N 117.71 0.05 1 612 446 153 LYS C C 174.74 0.05 1 613 446 153 LYS CA C 57.73 0.05 1 614 447 154 LEU H H 8.47 0.05 1 615 447 154 LEU C C 179.85 0.05 1 616 447 154 LEU CA C 54.86 0.05 1 617 447 154 LEU CB C 37.95 0.05 1 618 447 154 LEU N N 121.62 0.05 1 619 448 155 GLY H H 8.05 0.05 1 620 448 155 GLY C C 174.77 0.05 1 621 448 155 GLY CA C 42.89 0.05 1 622 448 155 GLY N N 110.22 0.05 1 623 449 156 ILE H H 7.66 0.05 1 624 449 156 ILE C C 177.39 0.05 1 625 449 156 ILE CA C 61.26 0.05 1 626 449 156 ILE CB C 32.99 0.05 1 627 449 156 ILE N N 122.35 0.05 1 628 450 157 HIS H H 7.46 0.05 1 629 450 157 HIS C C 176.58 0.05 1 630 450 157 HIS CA C 56.76 0.05 1 631 450 157 HIS CB C 27.48 0.05 1 632 450 157 HIS N N 119.22 0.05 1 633 451 158 GLU H H 8.00 0.05 1 634 451 158 GLU C C 176.85 0.05 1 635 451 158 GLU CA C 54.78 0.05 1 636 451 158 GLU CB C 28.68 0.05 1 637 451 158 GLU N N 115.97 0.05 1 638 452 159 ASP H H 8.86 0.05 1 639 452 159 ASP C C 175.10 0.05 1 640 452 159 ASP CA C 49.17 0.05 1 641 452 159 ASP CB C 37.87 0.05 1 642 452 159 ASP N N 123.74 0.05 1 643 453 160 SER H H 8.08 0.05 1 644 453 160 SER C C 177.21 0.05 1 645 453 160 SER CA C 58.05 0.05 1 646 453 160 SER CB C 59.20 0.05 1 647 453 160 SER N N 118.28 0.05 1 648 454 161 GLN H H 8.27 0.05 1 649 454 161 GLN C C 177.81 0.05 1 650 454 161 GLN CA C 55.42 0.05 1 651 454 161 GLN CB C 25.11 0.05 1 652 454 161 GLN N N 122.17 0.05 1 653 455 162 ASN H H 7.47 0.05 1 654 455 162 ASN C C 174.48 0.05 1 655 455 162 ASN CA C 49.70 0.05 1 656 455 162 ASN CB C 35.93 0.05 1 657 455 162 ASN N N 115.11 0.05 1 658 456 163 ARG H H 7.24 0.05 1 659 456 163 ARG CA C 57.83 0.05 1 660 456 163 ARG CB C 26.89 0.05 1 661 456 163 ARG N N 122.38 0.05 1 662 457 164 LYS C C 180.01 0.05 1 663 457 164 LYS CA C 57.25 0.05 1 664 458 165 LYS H H 7.91 0.05 1 665 458 165 LYS C C 179.58 0.05 1 666 458 165 LYS CA C 55.57 0.05 1 667 458 165 LYS CB C 27.85 0.05 1 668 458 165 LYS N N 123.06 0.05 1 669 459 166 LEU H H 8.32 0.05 1 670 459 166 LEU C C 180.07 0.05 1 671 459 166 LEU CA C 55.13 0.05 1 672 459 166 LEU CB C 39.25 0.05 1 673 459 166 LEU N N 118.52 0.05 1 674 460 167 SER H H 8.46 0.05 1 675 460 167 SER C C 176.56 0.05 1 676 460 167 SER CA C 58.75 0.05 1 677 460 167 SER CB C 60.21 0.05 1 678 460 167 SER N N 115.27 0.05 1 679 461 168 GLU H H 7.53 0.05 1 680 461 168 GLU C C 177.44 0.05 1 681 461 168 GLU CA C 55.41 0.05 1 682 461 168 GLU CB C 26.31 0.05 1 683 461 168 GLU N N 123.14 0.05 1 684 462 169 LEU H H 7.74 0.05 1 685 462 169 LEU CA C 51.56 0.05 1 686 462 169 LEU CB C 37.40 0.05 1 687 462 169 LEU N N 118.91 0.05 1 688 465 172 TYR C C 177.25 0.05 1 689 465 172 TYR CA C 54.36 0.05 1 690 465 172 TYR CB C 41.93 0.05 1 691 466 173 TYR H H 9.75 0.05 1 692 466 173 TYR C C 175.87 0.05 1 693 466 173 TYR CA C 56.52 0.05 1 694 466 173 TYR CB C 36.03 0.05 1 695 466 173 TYR N N 123.44 0.05 1 696 467 174 THR H H 9.15 0.05 1 697 467 174 THR C C 176.24 0.05 1 698 467 174 THR CA C 55.35 0.05 1 699 467 174 THR CB C 69.13 0.05 1 700 467 174 THR N N 110.77 0.05 1 701 468 175 SER H H 8.89 0.05 1 702 468 175 SER C C 174.94 0.05 1 703 468 175 SER CA C 57.23 0.05 1 704 468 175 SER CB C 59.50 0.05 1 705 468 175 SER N N 115.97 0.05 1 706 469 176 ALA H H 8.30 0.05 1 707 469 176 ALA C C 177.81 0.05 1 708 469 176 ALA CA C 48.20 0.05 1 709 469 176 ALA CB C 17.05 0.05 1 710 469 176 ALA N N 125.62 0.05 1 711 470 177 SER H H 7.67 0.05 1 712 470 177 SER C C 176.26 0.05 1 713 470 177 SER CA C 57.09 0.05 1 714 470 177 SER CB C 62.30 0.05 1 715 470 177 SER N N 118.30 0.05 1 716 471 178 GLY H H 8.60 0.05 1 717 471 178 GLY C C 175.33 0.05 1 718 471 178 GLY CA C 44.42 0.05 1 719 471 178 GLY N N 116.14 0.05 1 720 472 179 ASP H H 8.94 0.05 1 721 472 179 ASP C C 175.36 0.05 1 722 472 179 ASP CB C 37.75 0.05 1 723 472 179 ASP N N 127.60 0.05 1 724 473 180 GLU H H 7.98 0.05 1 725 473 180 GLU C C 174.98 0.05 1 726 473 180 GLU CA C 51.92 0.05 1 727 473 180 GLU CB C 28.75 0.05 1 728 473 180 GLU N N 120.96 0.05 1 729 474 181 MET H H 8.41 0.05 1 730 474 181 MET C C 173.82 0.05 1 731 474 181 MET CA C 51.78 0.05 1 732 474 181 MET CB C 30.60 0.05 1 733 474 181 MET N N 121.89 0.05 1 734 475 182 VAL H H 8.96 0.05 1 735 475 182 VAL C C 174.92 0.05 1 736 475 182 VAL CA C 56.07 0.05 1 737 475 182 VAL CB C 30.97 0.05 1 738 475 182 VAL N N 118.87 0.05 1 739 476 183 SER H H 8.69 0.05 1 740 476 183 SER C C 174.49 0.05 1 741 476 183 SER CA C 53.06 0.05 1 742 476 183 SER CB C 62.52 0.05 1 743 476 183 SER N N 117.94 0.05 1 744 477 184 LEU H H 8.68 0.05 1 745 477 184 LEU C C 179.45 0.05 1 746 477 184 LEU CA C 54.75 0.05 1 747 477 184 LEU CB C 34.63 0.05 1 748 477 184 LEU N N 120.55 0.05 1 749 478 185 LYS H H 8.52 0.05 1 750 478 185 LYS C C 179.13 0.05 1 751 478 185 LYS CA C 57.15 0.05 1 752 478 185 LYS CB C 28.64 0.05 1 753 478 185 LYS N N 122.43 0.05 1 754 479 186 ASP H H 8.08 0.05 1 755 479 186 ASP C C 179.25 0.05 1 756 479 186 ASP CA C 54.73 0.05 1 757 479 186 ASP CB C 37.64 0.05 1 758 479 186 ASP N N 122.62 0.05 1 759 480 187 TYR H H 7.81 0.05 1 760 480 187 TYR C C 179.33 0.05 1 761 480 187 TYR CA C 58.66 0.05 1 762 480 187 TYR CB C 34.79 0.05 1 763 480 187 TYR N N 121.20 0.05 1 764 481 188 CYS H H 8.43 0.05 1 765 481 188 CYS C C 177.59 0.05 1 766 481 188 CYS CA C 60.83 0.05 1 767 481 188 CYS CB C 24.61 0.05 1 768 481 188 CYS N N 118.86 0.05 1 769 482 189 THR H H 7.98 0.05 1 770 482 189 THR C C 175.29 0.05 1 771 482 189 THR CA C 62.10 0.05 1 772 482 189 THR CB C 66.48 0.05 1 773 482 189 THR N N 114.44 0.05 1 774 483 190 ARG H H 6.93 0.05 1 775 483 190 ARG C C 175.77 0.05 1 776 483 190 ARG CA C 52.53 0.05 1 777 483 190 ARG CB C 28.40 0.05 1 778 483 190 ARG N N 119.81 0.05 1 779 484 191 MET H H 6.93 0.05 1 780 484 191 MET C C 176.74 0.05 1 781 484 191 MET CA C 54.34 0.05 1 782 484 191 MET CB C 30.86 0.05 1 783 484 191 MET N N 120.56 0.05 1 784 485 192 LYS H H 7.93 0.05 1 785 485 192 LYS C C 178.39 0.05 1 786 485 192 LYS CA C 52.90 0.05 1 787 485 192 LYS CB C 29.65 0.05 1 788 485 192 LYS N N 121.19 0.05 1 789 486 193 GLU H H 8.87 0.05 1 790 486 193 GLU C C 175.77 0.05 1 791 486 193 GLU CA C 56.20 0.05 1 792 486 193 GLU CB C 25.87 0.05 1 793 486 193 GLU N N 123.86 0.05 1 794 487 194 ASN H H 8.32 0.05 1 795 487 194 ASN C C 174.34 0.05 1 796 487 194 ASN CA C 49.58 0.05 1 797 487 194 ASN CB C 34.32 0.05 1 798 487 194 ASN N N 115.18 0.05 1 799 488 195 GLN H H 7.62 0.05 1 800 488 195 GLN CA C 52.82 0.05 1 801 488 195 GLN CB C 25.74 0.05 1 802 488 195 GLN N N 123.07 0.05 1 803 494 201 ILE C C 172.50 0.05 1 804 494 201 ILE CB C 39.06 0.05 1 805 495 202 THR H H 7.96 0.05 1 806 495 202 THR C C 174.85 0.05 1 807 495 202 THR CA C 66.97 0.05 1 808 495 202 THR CB C 66.99 0.05 1 809 495 202 THR N N 117.81 0.05 1 810 496 203 GLY H H 7.72 0.05 1 811 496 203 GLY C C 171.81 0.05 1 812 496 203 GLY CA C 42.24 0.05 1 813 496 203 GLY N N 107.99 0.05 1 814 497 204 GLU H H 8.66 0.05 1 815 497 204 GLU C C 177.04 0.05 1 816 497 204 GLU CA C 55.02 0.05 1 817 497 204 GLU CB C 28.43 0.05 1 818 497 204 GLU N N 117.86 0.05 1 819 498 205 THR H H 7.01 0.05 1 820 498 205 THR C C 173.84 0.05 1 821 498 205 THR CA C 55.46 0.05 1 822 498 205 THR CB C 70.02 0.05 1 823 498 205 THR N N 104.66 0.05 1 824 499 206 LYS H H 8.98 0.05 1 825 499 206 LYS C C 176.77 0.05 1 826 499 206 LYS CA C 56.66 0.05 1 827 499 206 LYS CB C 28.45 0.05 1 828 499 206 LYS N N 123.84 0.05 1 829 500 207 ASP H H 8.13 0.05 1 830 500 207 ASP C C 177.89 0.05 1 831 500 207 ASP CA C 53.95 0.05 1 832 500 207 ASP CB C 37.40 0.05 1 833 500 207 ASP N N 116.86 0.05 1 834 501 208 GLN H H 7.49 0.05 1 835 501 208 GLN C C 179.37 0.05 1 836 501 208 GLN CA C 55.51 0.05 1 837 501 208 GLN CB C 25.68 0.05 1 838 501 208 GLN N N 118.34 0.05 1 839 502 209 VAL H H 7.18 0.05 1 840 502 209 VAL C C 177.68 0.05 1 841 502 209 VAL CA C 60.77 0.05 1 842 502 209 VAL CB C 27.24 0.05 1 843 502 209 VAL N N 111.93 0.05 1 844 503 210 ALA H H 7.99 0.05 1 845 503 210 ALA C C 178.94 0.05 1 846 503 210 ALA CA C 51.16 0.05 1 847 503 210 ALA CB C 15.17 0.05 1 848 503 210 ALA N N 123.43 0.05 1 849 504 211 ASN H H 6.95 0.05 1 850 504 211 ASN C C 174.60 0.05 1 851 504 211 ASN CA C 49.40 0.05 1 852 504 211 ASN CB C 36.17 0.05 1 853 504 211 ASN N N 112.82 0.05 1 854 505 212 SER H H 7.19 0.05 1 855 505 212 SER CA C 55.29 0.05 1 856 505 212 SER CB C 61.11 0.05 1 857 505 212 SER N N 115.98 0.05 1 858 506 213 ALA C C 180.32 0.05 1 859 507 214 PHE H H 7.63 0.05 1 860 507 214 PHE C C 178.19 0.05 1 861 507 214 PHE CA C 57.37 0.05 1 862 507 214 PHE CB C 35.82 0.05 1 863 507 214 PHE N N 115.63 0.05 1 864 508 215 VAL H H 6.94 0.05 1 865 508 215 VAL C C 177.53 0.05 1 866 508 215 VAL CA C 63.04 0.05 1 867 508 215 VAL CB C 28.63 0.05 1 868 508 215 VAL N N 118.87 0.05 1 869 509 216 GLU H H 7.84 0.05 1 870 509 216 GLU C C 177.64 0.05 1 871 509 216 GLU CA C 55.94 0.05 1 872 509 216 GLU CB C 25.55 0.05 1 873 509 216 GLU N N 122.37 0.05 1 874 510 217 ARG H H 7.40 0.05 1 875 510 217 ARG C C 177.40 0.05 1 876 510 217 ARG CA C 56.03 0.05 1 877 510 217 ARG CB C 26.45 0.05 1 878 510 217 ARG N N 117.23 0.05 1 879 511 218 LEU H H 6.94 0.05 1 880 511 218 LEU C C 179.47 0.05 1 881 511 218 LEU CA C 56.00 0.05 1 882 511 218 LEU CB C 36.24 0.05 1 883 511 218 LEU N N 120.64 0.05 1 884 512 219 ARG H H 8.67 0.05 1 885 512 219 ARG C C 181.11 0.05 1 886 512 219 ARG CA C 56.92 0.05 1 887 512 219 ARG CB C 26.86 0.05 1 888 512 219 ARG N N 123.86 0.05 1 889 513 220 LYS H H 8.00 0.05 1 890 513 220 LYS C C 177.51 0.05 1 891 513 220 LYS CA C 55.71 0.05 1 892 513 220 LYS CB C 28.42 0.05 1 893 513 220 LYS N N 121.00 0.05 1 894 514 221 HIS H H 7.25 0.05 1 895 514 221 HIS C C 174.92 0.05 1 896 514 221 HIS CA C 53.14 0.05 1 897 514 221 HIS CB C 27.91 0.05 1 898 514 221 HIS N N 117.72 0.05 1 899 515 222 GLY H H 7.96 0.05 1 900 515 222 GLY C C 173.90 0.05 1 901 515 222 GLY CA C 42.97 0.05 1 902 515 222 GLY N N 109.46 0.05 1 903 516 223 LEU H H 7.49 0.05 1 904 516 223 LEU C C 174.36 0.05 1 905 516 223 LEU CA C 50.32 0.05 1 906 516 223 LEU CB C 40.02 0.05 1 907 516 223 LEU N N 121.25 0.05 1 908 517 224 GLU H H 8.79 0.05 1 909 517 224 GLU C C 175.70 0.05 1 910 517 224 GLU CA C 52.46 0.05 1 911 517 224 GLU CB C 27.01 0.05 1 912 517 224 GLU N N 127.16 0.05 1 913 518 225 VAL H H 8.84 0.05 1 914 518 225 VAL CA C 57.64 0.05 1 915 518 225 VAL CB C 31.90 0.05 1 916 518 225 VAL N N 128.76 0.05 1 917 520 227 TYR C C 173.62 0.05 1 918 520 227 TYR CA C 49.77 0.05 1 919 520 227 TYR CB C 33.47 0.05 1 920 521 228 MET H H 8.88 0.05 1 921 521 228 MET C C 176.61 0.05 1 922 521 228 MET CA C 53.34 0.05 1 923 521 228 MET CB C 28.12 0.05 1 924 521 228 MET N N 126.65 0.05 1 925 522 229 ILE H H 7.92 0.05 1 926 522 229 ILE C C 177.85 0.05 1 927 522 229 ILE CA C 57.06 0.05 1 928 522 229 ILE CB C 34.36 0.05 1 929 522 229 ILE N N 116.76 0.05 1 930 523 230 GLU H H 8.46 0.05 1 931 523 230 GLU CA C 50.41 0.05 1 932 523 230 GLU N N 121.48 0.05 1 933 524 231 PRO C C 179.26 0.05 1 934 524 231 PRO CA C 63.06 0.05 1 935 525 232 ILE H H 7.82 0.05 1 936 525 232 ILE C C 176.38 0.05 1 937 525 232 ILE CA C 58.33 0.05 1 938 525 232 ILE CB C 34.88 0.05 1 939 525 232 ILE N N 115.08 0.05 1 940 526 233 ASP H H 8.10 0.05 1 941 526 233 ASP C C 177.99 0.05 1 942 526 233 ASP CA C 55.87 0.05 1 943 526 233 ASP N N 123.50 0.05 1 944 527 234 GLU H H 7.75 0.05 1 945 527 234 GLU C C 178.01 0.05 1 946 527 234 GLU CA C 56.42 0.05 1 947 527 234 GLU CB C 25.90 0.05 1 948 527 234 GLU N N 118.96 0.05 1 949 528 235 TYR H H 7.29 0.05 1 950 528 235 TYR C C 178.34 0.05 1 951 528 235 TYR CA C 56.68 0.05 1 952 528 235 TYR CB C 34.41 0.05 1 953 528 235 TYR N N 118.98 0.05 1 954 529 236 CYS H H 7.94 0.05 1 955 529 236 CYS C C 176.72 0.05 1 956 529 236 CYS CA C 59.76 0.05 1 957 529 236 CYS CB C 23.97 0.05 1 958 529 236 CYS N N 119.61 0.05 1 959 530 237 VAL H H 8.14 0.05 1 960 530 237 VAL C C 177.29 0.05 1 961 530 237 VAL CA C 62.76 0.05 1 962 530 237 VAL CB C 27.70 0.05 1 963 530 237 VAL N N 117.62 0.05 1 964 531 238 GLN H H 7.31 0.05 1 965 531 238 GLN C C 177.39 0.05 1 966 531 238 GLN CA C 55.07 0.05 1 967 531 238 GLN CB C 25.16 0.05 1 968 531 238 GLN N N 118.95 0.05 1 969 532 239 GLN H H 7.16 0.05 1 970 532 239 GLN C C 176.22 0.05 1 971 532 239 GLN CA C 52.23 0.05 1 972 532 239 GLN CB C 26.30 0.05 1 973 532 239 GLN N N 114.06 0.05 1 974 533 240 LEU H H 7.94 0.05 1 975 533 240 LEU C C 176.31 0.05 1 976 533 240 LEU CA C 52.42 0.05 1 977 533 240 LEU CB C 38.71 0.05 1 978 533 240 LEU N N 122.58 0.05 1 979 534 241 LYS H H 7.99 0.05 1 980 534 241 LYS C C 177.53 0.05 1 981 534 241 LYS CA C 56.67 0.05 1 982 534 241 LYS CB C 29.18 0.05 1 983 534 241 LYS N N 117.73 0.05 1 984 535 242 GLU H H 8.55 0.05 1 985 535 242 GLU C C 173.39 0.05 1 986 535 242 GLU CA C 51.29 0.05 1 987 535 242 GLU CB C 29.46 0.05 1 988 535 242 GLU N N 119.21 0.05 1 989 536 243 PHE H H 8.56 0.05 1 990 536 243 PHE C C 174.02 0.05 1 991 536 243 PHE CA C 55.00 0.05 1 992 536 243 PHE CB C 38.75 0.05 1 993 536 243 PHE N N 121.21 0.05 1 994 537 244 GLU H H 8.67 0.05 1 995 537 244 GLU C C 176.40 0.05 1 996 537 244 GLU CA C 53.95 0.05 1 997 537 244 GLU CB C 23.49 0.05 1 998 537 244 GLU N N 126.90 0.05 1 999 538 245 GLY H H 8.41 0.05 1 1000 538 245 GLY C C 174.18 0.05 1 1001 538 245 GLY CA C 42.27 0.05 1 1002 538 245 GLY N N 104.91 0.05 1 1003 539 246 LYS H H 7.96 0.05 1 1004 539 246 LYS CA C 51.30 0.05 1 1005 539 246 LYS CB C 28.30 0.05 1 1006 539 246 LYS N N 122.95 0.05 1 1007 540 247 THR C C 174.53 0.05 1 1008 540 247 THR CA C 59.21 0.05 1 1009 541 248 LEU H H 7.65 0.05 1 1010 541 248 LEU C C 176.74 0.05 1 1011 541 248 LEU CA C 52.76 0.05 1 1012 541 248 LEU CB C 38.28 0.05 1 1013 541 248 LEU N N 127.23 0.05 1 1014 542 249 VAL H H 8.93 0.05 1 1015 542 249 VAL C C 172.81 0.05 1 1016 542 249 VAL CA C 57.95 0.05 1 1017 542 249 VAL CB C 32.53 0.05 1 1018 542 249 VAL N N 125.56 0.05 1 1019 543 250 SER H H 8.06 0.05 1 1020 543 250 SER C C 177.51 0.05 1 1021 543 250 SER CA C 52.37 0.05 1 1022 543 250 SER CB C 59.67 0.05 1 1023 543 250 SER N N 122.12 0.05 1 1024 544 251 VAL H H 8.38 0.05 1 1025 544 251 VAL C C 175.54 0.05 1 1026 544 251 VAL CA C 59.73 0.05 1 1027 544 251 VAL CB C 27.03 0.05 1 1028 544 251 VAL N N 119.22 0.05 1 1029 545 252 THR H H 7.53 0.05 1 1030 545 252 THR C C 174.28 0.05 1 1031 545 252 THR CA C 57.70 0.05 1 1032 545 252 THR CB C 64.75 0.05 1 1033 545 252 THR N N 110.62 0.05 1 1034 546 253 LYS H H 7.00 0.05 1 1035 546 253 LYS C C 176.65 0.05 1 1036 546 253 LYS CA C 53.49 0.05 1 1037 546 253 LYS CB C 29.68 0.05 1 1038 546 253 LYS N N 124.46 0.05 1 1039 547 254 GLU H H 8.64 0.05 1 1040 547 254 GLU CA C 54.46 0.05 1 1041 547 254 GLU CB C 26.04 0.05 1 1042 547 254 GLU N N 128.85 0.05 1 1043 548 255 GLY H H 8.77 0.05 1 1044 548 255 GLY C C 174.50 0.05 1 1045 548 255 GLY CA C 42.57 0.05 1 1046 548 255 GLY N N 113.37 0.05 1 1047 549 256 LEU H H 7.13 0.05 1 1048 549 256 LEU C C 176.28 0.05 1 1049 549 256 LEU CA C 52.79 0.05 1 1050 549 256 LEU CB C 38.89 0.05 1 1051 549 256 LEU N N 122.17 0.05 1 1052 550 257 GLU H H 8.62 0.05 1 1053 550 257 GLU C C 175.32 0.05 1 1054 550 257 GLU CA C 52.55 0.05 1 1055 550 257 GLU CB C 27.01 0.05 1 1056 550 257 GLU N N 129.11 0.05 1 1057 551 258 LEU H H 8.37 0.05 1 1058 551 258 LEU CA C 49.09 0.05 1 1059 551 258 LEU CB C 37.78 0.05 1 1060 551 258 LEU N N 126.91 0.05 1 1061 552 259 PRO C C 176.41 0.05 1 1062 552 259 PRO CA C 59.81 0.05 1 1063 552 259 PRO CB C 28.22 0.05 1 1064 553 260 GLU H H 8.39 0.05 1 1065 553 260 GLU C C 175.58 0.05 1 1066 553 260 GLU CA C 53.21 0.05 1 1067 553 260 GLU CB C 26.93 0.05 1 1068 553 260 GLU N N 123.10 0.05 1 1069 554 261 ASP H H 7.98 0.05 1 1070 554 261 ASP CA C 53.15 0.05 1 1071 554 261 ASP CB C 38.91 0.05 1 1072 554 261 ASP N N 127.99 0.05 1 stop_ save_