data_7003 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR backbone assignment of the human HSP90 N-terminal domain ; _BMRB_accession_number 7003 _BMRB_flat_file_name bmr7003.str _Entry_type original _Submission_date 2006-02-23 _Accession_date 2006-02-23 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schwalbe Harald . . 2 Jacobs Doris M. . 3 Elshorst Bettina . . 4 Saxena Krishna . . 5 Fiebig Klaus M. . 6 Vogtherr Martin . . 7 Langer Thomas . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 168 "13C chemical shifts" 558 "15N chemical shifts" 168 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-02-08 update BMRB 'complete entry citation' 2006-08-07 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR Backbone Assignment of the N-terminal Domain of Human HSP90' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16821127 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jacobs Doris M. . 2 Langer Thomas . . 3 Elshorst Bettina . . 4 Saxena Krishna . . 5 Fiebig Klaus M. . 6 Vogtherr Martin . . 7 Schwalbe Harald . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 36 _Journal_issue 'Suppl. 5' _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 52 _Page_last 52 _Year 2006 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name hsp90 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'human heat shock protein 90 N-terminal domain' $hsp90 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details 'human heat shock protein 90 N-terminal domain' save_ ######################## # Monomeric polymers # ######################## save_hsp90 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common hsp90 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 209 _Mol_residue_sequence ; GHVETFAFQAEIAQLMSLII NTFYSNKEIFLRELISNSSD ALDKIRYETLTDPSKLDSGK ELHINLIPNKQDRTLTIVDT GIGMTKADLINNLGTIAKSG TKAFMEALQAGADISMIGQF GVGFYSAYLVAEKVTVITKH NDDEQYAWESSAGGSFTVRT DTGEPMGRGTKVILHLKEDQ TEYLEERRIKEIVKKHSQFI GYPITLFVE ; 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 stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 19560 Hsp90_N_domain 100.00 221 100.00 100.00 2.49e-150 PDB 1BYQ "Hsp90 N-Terminal Domain Bound To Adp-Mg" 99.52 228 99.52 99.52 2.04e-148 PDB 1OSF "Human Hsp90 In Complex With 17-desmethoxy-17-n,n- Dimethylaminoethylamino-geldanamycin" 99.04 215 99.52 100.00 9.30e-148 PDB 1UY6 "Human Hsp90-Alpha With 9-Butyl-8-(3,4,5-Trimethoxy-Benzyl)-9h-Purin-6-Ylamine" 99.52 236 99.04 99.52 5.64e-148 PDB 1UY7 "Human Hsp90-alpha With 9-butyl-8-(4-methoxy-benzyl)-9h-purin-6-ylamine" 99.52 236 99.04 99.52 5.64e-148 PDB 1UY8 "Human Hsp90-Alpha With 9-Butyl-8-(3-Trimethoxy-Benzyl)-9h-Purin-6ylamine" 99.52 236 99.04 99.52 5.64e-148 PDB 1UY9 "Human Hsp90-Alpha With 8-Benzo[1,3]dioxol-,5-Ylmethyl-9-Butyl-9h-Purin-6-Ylamine" 99.52 236 99.04 99.52 5.64e-148 PDB 1UYC "Human Hsp90-Alpha With 9-Butyl-8-(2,5-Dimethoxy-Benzyl)-9h-Purin-6-Ylamine" 99.52 236 99.04 99.52 5.64e-148 PDB 1UYD "Human Hsp90-Alpha With 9-Butyl-8- (2-Chloro-3,4,5-Trimethoxy-Benzyl)-9h-Purin-6-Ylamine" 99.52 236 99.04 99.52 5.64e-148 PDB 1UYE "Human Hsp90-Alpha With 8-(2-Chloro-3,4,5-Trimethoxy-Benzyl) -9-Pent-4-Ylnyl-9h-Purin-6-Ylamine" 99.52 236 99.04 99.52 5.64e-148 PDB 1UYF "Human Hsp90-Alpha With 8-(2-Chloro-3,4,5-Trimethoxy-Benzyl) -2-Fluoro-9-Pent-4-Ylnyl-9h-Purin-6-Ylamine" 99.52 236 99.04 99.52 5.64e-148 PDB 1UYG "Human Hsp90-Alpha With 8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9h-Purin-6-Ylamine" 99.52 236 99.04 99.52 5.64e-148 PDB 1UYH "Human Hsp90-Alpha With 9-Butyl-8- (2,5-Dimethoxy-Benzyl)-2-Fluoro-9h-Purin-6-Ylamine" 99.52 236 99.04 99.52 5.64e-148 PDB 1UYI "Human Hsp90-Alpha With 8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9- Pent-9h-Purin-6-Ylamine" 99.52 236 99.52 100.00 3.87e-149 PDB 1UYK "Human Hsp90-Alpha With 8-Benzo[1,3]dioxol-,5-Ylmethyl-9-But Yl-2-Fluoro-9h-Purin-6-Ylamine" 99.52 236 99.04 99.52 5.64e-148 PDB 1UYL "Structure-Activity Relationships In Purine-Based Inhibitor Binding To Hsp90 Isoforms" 99.52 236 99.04 99.52 5.64e-148 PDB 1YC1 "Crystal Structures Of Human Hsp90alpha Complexed With Dihydroxyphenylpyrazoles" 99.04 264 100.00 100.00 3.68e-147 PDB 1YC3 "Crystal Structure Of Human Hsp90alpha Complexed With Dihydroxyphenylpyrazoles" 99.04 264 100.00 100.00 3.68e-147 PDB 1YC4 "Crystal Structure Of Human Hsp90alpha Complexed With Dihydroxyphenylpyrazoles" 99.04 264 100.00 100.00 3.68e-147 PDB 1YER 'Human Hsp90 Geldanamycin-Binding Domain, "closed" Conformation' 99.52 228 99.52 99.52 2.04e-148 PDB 1YES 'Human Hsp90 Geldanamycin-Binding Domain, "open" Conformation' 99.52 228 99.52 99.52 2.04e-148 PDB 1YET "Geldanamycin Bound To The Hsp90 Geldanamycin-Binding Domain" 99.52 228 99.52 99.52 2.04e-148 PDB 2BSM "Novel, Potent Small Molecule Inhibitors Of The Molecular Chaperone Hsp90 Discovered Through Structure-Based Design" 99.52 235 99.04 99.52 7.63e-148 PDB 2BT0 "Novel, Potent Small Molecule Inhibitors Of The Molecular Chaperone Hsp90 Discovered Through Structure-Based Design" 99.52 235 99.04 99.52 7.63e-148 PDB 2BYH "3-(5-Chloro-2,4-Dihydroxyphenyl)-Pyrazole-4-Carboxamides As Inhibitors Of The Hsp90 Molecular Chaperone" 99.52 235 99.04 99.52 7.63e-148 PDB 2BYI "3-(5-Chloro-2,4-Dihydroxyphenyl)-Pyrazole-4-Carboxamides As Inhibitors Of The Hsp90 Molecular Chaperone" 99.52 235 99.04 99.52 7.63e-148 PDB 2BZ5 "Structure-Based Discovery Of A New Class Of Hsp90 Inhibitors" 99.52 235 99.04 99.52 7.63e-148 PDB 2CCS "Human Hsp90 With 4-Chloro-6-(4-Piperazin-1-Yl-1h-Pyrazol-3- Yl)-Benzene-1,2-Diol" 99.52 236 99.52 99.52 1.55e-148 PDB 2CCT "Human Hsp90 With 5-(5-Chloro-2,4-Dihydroxy-Phenyl)-4- Piperazin-1-Yl-2h-Pyrazole-3-Carboxylic Acid Ethylamide" 99.52 236 99.52 99.52 1.55e-148 PDB 2CCU "Human Hsp90 With 4-Chloro-6-(4-(4-(4-Methanesulphonyl- Benzyl)-Pierazin-1-Yl)-1h-Pyrazol-3-Yl)-Benzene-1,3-Diol" 99.52 236 99.52 99.52 1.55e-148 PDB 2FWY "Structure Of Human Hsp90-Alpha Bound To The Potent Water Soluble Inhibitor Pu-H64" 99.04 256 99.52 100.00 2.04e-147 PDB 2FWZ "Structure Of Human Hsp90-alpha Bound To The Potent Water Soluble Inhibitor Pu-h71" 99.04 256 99.52 100.00 2.04e-147 PDB 2H55 "Structure Of Human Hsp90-Alpha Bound To The Potent Water Soluble Inhibitor Pu-Dz8" 99.04 256 99.52 100.00 2.04e-147 PDB 2JJC "Hsp90 Alpha Atpase Domain With Bound Small Molecule Fragment" 99.04 218 99.52 100.00 1.23e-147 PDB 2K5B "Human Cdc37-Hsp90 Docking Model Based On Nmr" 99.04 210 100.00 100.00 2.10e-148 PDB 2QF6 "Hsp90 Complexed With A56322" 99.04 207 100.00 100.00 2.79e-148 PDB 2QFO "Hsp90 Complexed With A143571 And A516383" 99.04 207 99.52 100.00 7.81e-148 PDB 2QG0 "Hsp90 Complexed With A943037" 99.04 207 99.52 100.00 7.81e-148 PDB 2QG2 "Hsp90 Complexed With A917985" 99.04 207 100.00 100.00 2.79e-148 PDB 2UWD "Inhibition Of The Hsp90 Molecular Chaperone In Vitro And In Vivo By Novel, Synthetic, Potent Resorcinylic Pyrazole, Isoxazole A" 99.52 236 99.04 99.52 5.64e-148 PDB 2VCI "4,5 Diaryl Isoxazole Hsp90 Chaperone Inhibitors: Potential Therapeutic Agents For The Treatment Of Cancer" 99.52 236 99.04 99.52 5.64e-148 PDB 2VCJ "4,5 Diaryl Isoxazole Hsp90 Chaperone Inhibitors: Potential Therapeutic Agents For The Treatment Of Cancer" 99.52 236 99.04 99.52 5.64e-148 PDB 2WI1 "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" 99.52 236 99.04 99.52 5.64e-148 PDB 2WI2 "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" 99.52 236 99.04 99.52 5.64e-148 PDB 2WI3 "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" 99.52 236 99.04 99.52 5.64e-148 PDB 2WI4 "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" 99.52 236 99.04 99.52 5.64e-148 PDB 2WI5 "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" 99.52 236 99.04 99.52 5.64e-148 PDB 2WI6 "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" 99.52 236 99.04 99.52 5.64e-148 PDB 2WI7 "Orally Active 2-Amino Thienopyrimidine Inhibitors Of The Hsp90 Chaperone" 99.52 236 99.04 99.52 5.64e-148 PDB 2XAB "Structure Of Hsp90 With An Inhibitor Bound" 99.04 249 99.52 100.00 2.47e-147 PDB 2XDK "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.04 249 99.52 100.00 2.47e-147 PDB 2XDL "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.04 249 99.52 100.00 2.47e-147 PDB 2XDS "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.04 249 99.52 100.00 2.47e-147 PDB 2XDU "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.04 236 99.52 100.00 1.70e-147 PDB 2XDX "Structre Of Hsp90 With Small Molecule Inhibitor Bound" 99.04 249 99.52 100.00 2.47e-147 PDB 2XHR "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.04 249 99.52 100.00 2.47e-147 PDB 2XHT "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.04 249 99.52 100.00 2.47e-147 PDB 2XHX "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.04 249 100.00 100.00 8.46e-148 PDB 2XJG "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.04 249 100.00 100.00 8.46e-148 PDB 2XJJ "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.04 249 99.03 99.52 3.72e-146 PDB 2XJX "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.04 249 99.52 100.00 2.47e-147 PDB 2XK2 "Structure Of Hsp90 With Small Molecule Inhibitor Bound" 99.04 249 99.52 100.00 2.47e-147 PDB 2YE2 "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.04 252 99.52 100.00 1.31e-147 PDB 2YE3 "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.04 252 99.52 100.00 1.31e-147 PDB 2YE4 "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.04 252 99.52 100.00 1.31e-147 PDB 2YE5 "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.04 252 99.52 100.00 1.31e-147 PDB 2YE6 "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.04 252 99.52 100.00 1.31e-147 PDB 2YE7 "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.52 252 99.52 100.00 1.01e-148 PDB 2YE8 "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.52 252 99.52 100.00 1.01e-148 PDB 2YE9 "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.04 252 99.52 100.00 1.31e-147 PDB 2YEA "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.04 252 99.52 100.00 1.31e-147 PDB 2YEB "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.04 252 99.52 100.00 1.31e-147 PDB 2YEC "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.04 252 99.52 100.00 1.31e-147 PDB 2YED "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.04 252 99.52 100.00 1.31e-147 PDB 2YEE "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.52 252 99.04 99.52 1.54e-147 PDB 2YEF "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.04 252 99.52 100.00 1.31e-147 PDB 2YEG "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.04 252 99.52 100.00 1.31e-147 PDB 2YEH "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.04 252 99.52 100.00 1.31e-147 PDB 2YEI "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.52 252 99.52 100.00 1.01e-148 PDB 2YEJ "Hsp90 Inhibitors And Drugs From Fragment And Virtual Screening" 99.52 252 99.52 100.00 1.01e-148 PDB 2YI0 "Structural Characterization Of 5-Aryl-4-(5-Substituted-2-4- Dihydroxyphenyl)-1,2,3-Thiadiazole Hsp90 Inhibitors." 99.04 229 99.52 100.00 8.29e-148 PDB 2YI5 "Structural Characterization Of 5-Aryl-4-(5-Substituted-2-4- Dihydroxyphenyl)-1,2,3-Thiadiazole Hsp90 Inhibitors." 99.04 229 99.52 100.00 8.29e-148 PDB 2YI6 "Structural Characterization Of 5-Aryl-4-(5-Substituted-2- 4-Dihydroxyphenyl)-1,2,3-Thiadiazole Hsp90 Inhibitors." 99.04 229 99.52 100.00 8.29e-148 PDB 2YI7 "Structural Characterization Of 5-Aryl-4-(5-Substituted-2-4- Dihydroxyphenyl)-1,2,3-Thiadiazole Hsp90 Inhibitors" 99.04 229 99.52 100.00 8.29e-148 PDB 2YJW "Tricyclic Series Of Hsp90 Inhibitors" 100.00 209 99.04 100.00 3.97e-149 PDB 2YJX "Tricyclic Series Of Hsp90 Inhibitors" 100.00 209 99.04 100.00 3.97e-149 PDB 2YK2 "Tricyclic Series Of Hsp90 Inhibitors" 100.00 209 99.04 100.00 3.97e-149 PDB 2YK9 "Tricyclic Series Of Hsp90 Inhibitors" 100.00 209 99.04 100.00 3.97e-149 PDB 2YKB "Tricyclic Series Of Hsp90 Inhibitors" 100.00 209 99.04 100.00 3.97e-149 PDB 2YKC "Tricyclic Series Of Hsp90 Inhibitors" 100.00 209 99.04 100.00 3.97e-149 PDB 2YKE "Tricyclic Series Of Hsp90 Inhibitors" 100.00 209 99.04 100.00 3.97e-149 PDB 2YKI "Tricyclic Series Of Hsp90 Inhibitors" 100.00 209 99.04 100.00 3.97e-149 PDB 2YKJ "Tricyclic Series Of Hsp90 Inhibitors" 100.00 209 99.04 100.00 3.97e-149 PDB 3B24 "Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazine Fragment Molecule" 99.52 229 99.04 99.52 6.45e-148 PDB 3B25 "Hsp90 Alpha N-terminal Domain In Complex With An Inhibitor Ch4675194" 99.52 229 99.04 99.52 6.45e-148 PDB 3B26 "Hsp90 Alpha N-terminal Domain In Complex With An Inhibitor Ro1127850" 99.52 229 99.04 99.52 6.45e-148 PDB 3B27 "Hsp90 Alpha N-terminal Domain In Complex With An Inhibitor Ro4919127" 99.52 229 99.04 99.52 6.45e-148 PDB 3B28 "Hsp90 Alpha N-terminal Domain In Complex With An Inhibitor Ch5015765" 99.52 229 99.04 99.52 6.45e-148 PDB 3BM9 "Discovery Of Benzisoxazoles As Potent Inhibitors Of Chaperone Hsp90" 99.04 226 99.52 100.00 8.05e-148 PDB 3BMY "Discovery Of Benzisoxazoles As Potent Inhibitors Of Chaperone Hsp90" 99.04 226 99.52 100.00 8.05e-148 PDB 3D0B "Crystal Structure Of Benzamide Tetrahydro-4h-Carbazol-4-One Bound To Hsp90" 99.52 232 99.04 99.52 8.36e-148 PDB 3EKO "Dihydroxylphenyl Amides As Inhibitors Of The Hsp90 Molecular Chaperone" 99.04 226 99.52 100.00 1.53e-147 PDB 3EKR "Dihydroxylphenyl Amides As Inhibitors Of The Hsp90 Molecular Chaperone" 99.04 226 99.52 100.00 1.53e-147 PDB 3FT5 "Structure Of Hsp90 Bound With A Novel Fragment" 99.04 249 99.52 100.00 2.47e-147 PDB 3FT8 "Structure Of Hsp90 Bound With A Noval Fragment." 99.04 249 99.52 100.00 2.47e-147 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" 99.04 226 99.52 100.00 1.53e-147 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" 99.04 224 99.52 100.00 9.64e-148 PDB 3HYY "Crystal Structure Of Hsp90 With Fragment 37-D04" 99.04 249 99.52 100.00 2.47e-147 PDB 3HYZ "Crystal Structure Of Hsp90 With Fragment 42-C03" 99.04 249 99.52 100.00 2.47e-147 PDB 3HZ1 "Crystal Structure Of Hsp90 With Fragments 37-D04 And 42-C03" 99.04 249 99.52 100.00 2.47e-147 PDB 3HZ5 "Crystal Structure Of Hsp90 With Fragment Z064" 99.04 249 99.52 100.00 2.47e-147 PDB 3INW "Hsp90 N-Terminal Domain With Pochoxime A" 99.52 228 99.04 99.52 6.29e-148 PDB 3INX "Hsp90 N-Terminal Domain With Pochoxime B" 99.52 228 99.04 99.52 6.29e-148 PDB 3K97 "Hsp90 N-Terminal Domain In Complex With 4-Chloro-6-{[(2r)-2- (2-Methylphenyl)pyrrolidin-1-Yl]carbonyl}benzene-1,3-Diol" 99.04 251 99.52 100.00 5.95e-147 PDB 3K98 "Hsp90 N-Terminal Domain In Complex With (1r)-2-(5-Chloro-2, 4-Dihydroxybenzoyl)-N-Ethylisoindoline-1-Carboxamide" 99.04 232 99.52 100.00 1.10e-147 PDB 3K99 "Hsp90 N-Terminal Domain In Complex With 4-(1,3-Dihydro-2h- Isoindol-2-Ylcarbonyl)benzene-1,3-Diol" 99.04 232 99.52 100.00 1.10e-147 PDB 3MNR "Crystal Structure Of Benzamide Snx-1321 Bound To Hsp90" 99.52 232 99.04 99.52 8.36e-148 PDB 3O0I "Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Pu-h54" 99.04 256 99.52 100.00 2.04e-147 PDB 3OW6 "Crystal Structure Of Hsp90 With N-Aryl-Benzimidazolone I" 99.04 207 100.00 100.00 2.79e-148 PDB 3OWB "Crystal Structure Of Hsp90 With Ver-49009" 99.04 207 100.00 100.00 2.79e-148 PDB 3OWD "Crystal Structure Of Hsp90 With N-Aryl-Benzimidazolone Ii" 99.04 207 100.00 100.00 2.79e-148 PDB 3QDD "Hsp90a N-Terminal Domain In Complex With Biib021" 99.04 237 99.52 100.00 7.76e-148 PDB 3QTF "Design And Sar Of Macrocyclic Hsp90 Inhibitors With Increased Metabolic Stability And Potent Cell-Proliferation Activity" 99.04 226 99.52 100.00 8.05e-148 PDB 3R4M "Optimization Of Potent, Selective, And Orally Bioavailable Pyrrolodinopyrimidine-Containing Inhibitors Of Heat Shock Protein 90" 99.52 228 99.04 99.52 6.15e-148 PDB 3R4N "Optimization Of Potent, Selective, And Orally Bioavailable Pyrrolodinopyrimidine-Containing Inhibitors Of Heat Shock Protein 90" 99.04 226 99.52 100.00 1.53e-147 PDB 3R4O "Optimization Of Potent, Selective, And Orally Bioavailable Pyrrolodinopyrimidine-Containing Inhibitors Of Heat Shock Protein 90" 99.04 226 99.52 100.00 1.53e-147 PDB 3R4P "Optimization Of Potent, Selective, And Orally Bioavailable Pyrrolodinopyrimidine-Containing Inhibitors Of Heat Shock Protein 90" 99.04 226 99.52 100.00 1.53e-147 PDB 3R91 "Macrocyclic Lactams As Potent Hsp90 Inhibitors With Excellent Tumor Exposure And Extended Biomarker Activity." 99.04 226 99.52 100.00 8.05e-148 PDB 3R92 "Discovery Of A Macrocyclic O-Aminobenzamide Hsp90 Inhibitor With Heterocyclic Tether That Shows Extended Biomarker Activity And" 99.04 226 99.52 100.00 8.05e-148 PDB 3RKZ "Discovery Of A Stable Macrocyclic O-Aminobenzamide Hsp90 Inhibitor Capable Of Significantly Decreasing Tumor Volume In A Mouse " 99.04 226 99.52 100.00 8.05e-148 PDB 3RLP "Co-Crystal Structure Of The Hsp90 Atp Binding Domain In Complex With 4-(2,4-Dichloro-5-Methoxyphenyl)-6-Methylpyrimidin-2-Amine" 99.04 226 99.52 100.00 1.53e-147 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- " 99.04 226 99.52 100.00 1.53e-147 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" 99.04 226 99.52 100.00 1.53e-147 PDB 3T0H "Structure Insights Into Mechanisms Of Atp Hydrolysis And The Activation Of Human Hsp90" 99.52 228 99.04 99.52 6.15e-148 PDB 3T0Z "Hsp90 N-Terminal Domain Bound To Atp" 99.52 228 99.04 99.52 6.15e-148 PDB 3T10 "Hsp90 N-Terminal Domain Bound To Acp" 99.52 228 99.04 99.52 6.15e-148 PDB 3T1K "Hsp90 N-Terminal Domain Bound To Anp" 99.52 228 99.04 99.52 6.15e-148 PDB 3T2S "Hsp90 N-Terminal Domain Bound To Ags" 99.52 228 99.04 99.52 6.15e-148 PDB 3TUH "Crystal Structure Of The N-Terminal Domain Of An Hsp90 In The Presence Of An The Inhibitor Ganetespib" 99.04 209 99.52 100.00 6.52e-148 PDB 3VHA "Hsp90 Alpha N-Terminal Domain In Complex With A Macrocyclic Inhibitor" 99.52 229 99.04 99.52 6.45e-148 PDB 3VHC "Hsp90 Alpha N-Terminal Domain In Complex With A Macrocyclic Inhibitor" 99.52 229 99.04 99.52 6.45e-148 PDB 3VHD "Hsp90 Alpha N-Terminal Domain In Complex With A Macrocyclic Inhibitor, Ch5164840" 99.52 229 99.04 99.52 6.45e-148 PDB 3WHA "Hsp90 Alpha N-terminal Domain In Complex With A Tricyclic Inhibitor" 99.52 229 99.04 99.52 6.45e-148 PDB 4AWO "Complex Of Hsp90 Atpase Domain With Tropane Derived Inhibitors" 99.52 230 99.04 99.52 7.70e-148 PDB 4AWP "Complex Of Hsp90 Atpase Domain With Tropane Derived Inhibitors" 99.52 230 99.04 99.52 7.70e-148 PDB 4AWQ "Complex Of Hsp90 Atpase Domain With Tropane Derived Inhibitors" 99.52 230 99.04 99.52 7.70e-148 PDB 4B7P "Structure Of Hsp90 With Nms-e973 Inhibitor Bound" 99.52 230 99.04 99.52 1.13e-147 PDB 4BQG "Structure Of Hsp90 With An Inhibitor Bound" 99.52 230 99.04 99.52 1.13e-147 PDB 4BQJ "Structure Of Hsp90 With An Inhibitor Bound" 99.52 230 99.04 99.52 1.13e-147 PDB 4CWF "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" 99.52 230 99.04 99.52 1.13e-147 PDB 4CWN "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" 99.52 230 99.04 99.52 1.13e-147 PDB 4CWO "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" 99.52 230 99.04 99.52 1.13e-147 PDB 4CWP "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" 99.52 230 99.04 99.52 1.13e-147 PDB 4CWQ "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" 99.52 230 99.04 99.52 1.13e-147 PDB 4CWR "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" 99.52 230 99.04 99.52 1.13e-147 PDB 4CWS "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" 99.52 230 99.04 99.52 1.13e-147 PDB 4CWT "Human Hsp90 Alpha N-terminal Domain In Complex With An Aminotriazoloquinazoline Inhibitor" 99.52 230 99.04 99.52 1.13e-147 PDB 4EEH "Hsp90 Alpha N-Terminal Domain In Complex With An Inhibitor 3-(4- Hydroxy-Phenyl)-1h-Indazol-6-Ol" 99.52 229 99.04 99.52 8.76e-148 PDB 4EFT "Hsp90 Alpha N-Terminal Domain In Complex With An Inhibitor 3- Cyclohexyl-2-(6-Hydroxy-1h-Indazol-3-Yl)-Propionitrile" 99.52 229 99.04 99.52 8.76e-148 PDB 4EFU "Hsp90 Alpha N-Terminal Domain In Complex With An Inhibitor 6-Hydroxy- 3-(3-Methyl-Benzyl)-1h-Indazole-5-Carboxylic Acid Benzyl-" 99.52 229 99.04 99.52 8.76e-148 PDB 4EGH "Hsp90-Alpha Atpase Domain In Complex With (4-Hydroxyphenyl)morpholin- 4-Yl Methanone" 99.04 232 99.52 100.00 1.11e-147 PDB 4EGI "Hsp90-Alpha Atpase Domain In Complex With 2-Amino-4-Ethylthio-6- Methyl-1,3,5-Triazine" 99.04 232 99.52 100.00 1.11e-147 PDB 4EGK "Human Hsp90-Alpha Atpase Domain Bound To Radicicol" 99.04 232 99.52 100.00 1.11e-147 PDB 4FCP "Targetting Conserved Water Molecules: Design Of 4-Aryl-5-Cyanopyrrolo [2,3-D] Pyrimidine Hsp90 Inhibitors Using Fragment-Based " 99.52 236 99.04 99.52 5.64e-148 PDB 4FCQ "Targeting Conserved Water Molecules: Design Of 4-Aryl-5- Cyanopyrrolo[2,3-D]pyrimidine Hsp90 Inhibitors Using Fragment-Based Sc" 99.52 236 99.04 99.52 5.64e-148 PDB 4FCR "Targeting Conserved Water Molecules: Design Of 4-Aryl-5- Cyanopyrrolo[2,3-D]pyrimidine Hsp90 Inhibitors Using Fragment-Based Sc" 99.52 236 99.04 99.52 5.64e-148 PDB 4HY6 "Crystal Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Fj1" 99.52 228 99.04 99.52 6.15e-148 PDB 4JQL "Synthesis Of Benzoquinone-ansamycin-inspired Macrocyclic Lactams From Shikimic Acid" 99.04 249 99.52 100.00 2.47e-147 PDB 4L8Z "Crystal Structure Of Human Hsp90 With Rl1" 99.52 228 99.04 99.52 6.15e-148 PDB 4L90 "Crystal Structure Of Human Hsp90 With Rl3" 99.52 228 99.04 99.52 6.15e-148 PDB 4L91 "Crystal Structure Of Human Hsp90 With X29" 99.52 228 99.04 99.52 6.15e-148 PDB 4L93 "Crystal Structure Of Human Hsp90 With S36" 99.52 228 99.04 99.52 6.15e-148 PDB 4L94 "Crystal Structure Of Human Hsp90 With S46" 99.52 228 99.04 99.52 6.15e-148 PDB 4LWE "Crystal Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Fj2" 99.04 208 99.52 100.00 7.75e-148 PDB 4LWF "Crystal Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Fj3" 99.04 208 99.52 100.00 7.75e-148 PDB 4LWG "Crystal Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Fj4" 99.04 208 99.52 100.00 7.75e-148 PDB 4LWH "Crystal Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Fj5" 99.04 209 99.52 100.00 6.52e-148 PDB 4LWI "Crystal Structure Of The Human Hsp90-alpha N-domain Bound To The Hsp90 Inhibitor Fj6" 99.04 208 99.52 100.00 7.75e-148 PDB 4NH7 "Correlation Between Chemotype-dependent Binding Conformations Of Hsp90 Alpha/beta And Isoform Selectivity" 99.04 233 99.52 100.00 1.36e-147 PDB 4NH8 "Correlation Between Chemotype-dependent Binding Conformations Of Hsp90 Alpha/beta And Isoform Selectivity" 99.04 233 99.52 100.00 1.36e-147 PDB 4O05 "Identification Of Novel Hsp90/isoform Selective Inhibitors Using Structure-based Drug Design. Demonstration Of Potential Utilit" 99.04 233 99.52 100.00 1.36e-147 PDB 4O07 "Identification Of Novel Hsp90/isoform Selective Inhibitors Using Structure-based Drug Design. Demonstration Of Potential Utilit" 99.04 233 99.52 100.00 1.36e-147 PDB 4O09 "Identification Of Novel Hsp90 / Isoform Selective Inhibitors Using Structure-based Drug Design. Demonstration Of Potential Util" 99.04 233 99.52 100.00 1.36e-147 PDB 4O0B "Identification Of Novel Hsp90/isoform Selective Inhibitors Using Structure-based Drug Design. Demonstration Of Potential Utilit" 99.04 233 99.52 100.00 1.36e-147 PDB 4R3M "Crystal Structure Of Human Hsp90 With Jr9" 99.04 209 99.52 100.00 6.52e-148 PDB 4U93 "Crystal Structure Of Hsp90-alpha N-domain Bound To The Inhibitor Nvp- Hsp990" 99.52 236 99.04 99.52 5.64e-148 PDB 4W7T "Crystal Structure Of Hsp90-alpha N-domain Bound To The Inhibitor Nvp- Hsp990" 99.52 236 99.04 99.52 5.64e-148 DBJ BAB20777 "heat shock protein 90 alpha [Equus caballus]" 99.52 719 99.04 99.52 2.08e-142 DBJ BAB23449 "unnamed protein product [Mus musculus]" 99.52 733 98.56 99.52 2.16e-141 DBJ BAC36610 "unnamed protein product [Mus musculus]" 99.52 557 98.56 99.52 3.79e-143 DBJ BAC40681 "unnamed protein product [Mus musculus]" 99.52 274 98.56 99.52 1.76e-147 DBJ BAC82487 "90-kDa heat shock protein alpha [Bos taurus]" 99.52 733 99.04 99.52 2.53e-142 EMBL CAA30255 "unnamed protein product [Homo sapiens]" 99.52 312 99.04 99.52 8.53e-148 EMBL CAA33259 "unnamed protein product [Homo sapiens]" 99.52 732 99.52 99.52 8.92e-143 EMBL CAC39453 "heat shock protein 86 [Rattus norvegicus]" 99.52 733 99.04 99.52 2.91e-142 EMBL CAD21648 "heat shock protein 86 [Rattus norvegicus]" 99.52 733 99.04 99.52 2.91e-142 EMBL CAD66568 "unnamed protein product [Homo sapiens]" 59.33 262 99.19 100.00 4.91e-80 GB AAA36023 "heat shock protein 86, partial [Homo sapiens]" 99.52 312 99.04 99.52 8.53e-148 GB AAA36992 "heat shock protein 90A [Cricetulus griseus]" 99.52 733 97.60 99.52 7.88e-141 GB AAA37868 "heat-shock protein hsp86, partial [Mus musculus]" 99.52 347 98.56 99.52 1.40e-145 GB AAA53068 "heat shock protein 86 [Mus musculus]" 99.52 733 98.56 99.52 2.16e-141 GB AAA63194 "heat shock protein [Homo sapiens]" 99.52 732 99.04 99.52 3.02e-142 REF NP_001012688 "heat shock protein HSP 90-alpha [Bos taurus]" 99.52 733 99.04 99.52 2.53e-142 REF NP_001017963 "heat shock protein HSP 90-alpha isoform 1 [Homo sapiens]" 99.52 854 99.04 99.52 2.22e-140 REF NP_001092042 "heat shock protein HSP 90-alpha [Pan troglodytes]" 99.52 733 98.56 99.04 2.99e-141 REF NP_001157427 "heat shock protein HSP 90-alpha [Equus caballus]" 99.52 733 99.04 99.52 3.31e-142 REF NP_001182596 "heat shock protein 90kDa alpha (cytosolic), class A member 1 [Macaca mulatta]" 99.52 733 99.04 99.52 2.88e-142 SP A5A6K9 "RecName: Full=Heat shock protein HSP 90-alpha [Pan troglodytes]" 99.52 733 98.56 99.04 2.99e-141 SP O02705 "RecName: Full=Heat shock protein HSP 90-alpha [Sus scrofa]" 99.52 733 99.04 99.52 2.88e-142 SP P07900 "RecName: Full=Heat shock protein HSP 90-alpha; AltName: Full=Heat shock 86 kDa; Short=HSP 86; Short=HSP86; AltName: Full=Lipopo" 99.52 732 99.04 99.52 3.02e-142 SP P07901 "RecName: Full=Heat shock protein HSP 90-alpha; AltName: Full=Heat shock 86 kDa; Short=HSP 86; Short=HSP86; AltName: Full=Tumor-" 99.52 733 98.56 99.52 2.16e-141 SP P30946 "RecName: Full=Heat shock protein HSP 90-alpha [Oryctolagus cuniculus]" 99.52 694 98.08 99.04 3.93e-141 TPG DAA17282 "TPA: heat shock protein HSP 90-alpha [Bos taurus]" 99.52 733 99.04 99.52 2.53e-142 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 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 'recombinant technology' 'E. coli' . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $hsp90 1.5 mM '[U-2H; U-13C; U-15N]' 'sodium phosphate' 20 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_800MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX800 _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H15N_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 1H15N_TROSY _Sample_label $sample_1 save_ save_TROSY_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY_HNCO _Sample_label $sample_1 save_ save_TROSY_HNCACO_3 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY_HNCACO _Sample_label $sample_1 save_ save_TROSY_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY_HNCACB _Sample_label $sample_1 save_ save_TROSY_HNCOCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY_HNCOCACB _Sample_label $sample_1 save_ save_TROSY_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY_HNCA _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 0.1 pH temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label 1H15N_TROSY TROSY_HNCO TROSY_HNCACO TROSY_HNCACB TROSY_HNCOCACB stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'human heat shock protein 90 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 17 3 VAL C C 177.757 0.500 1 2 17 3 VAL CA C 52.822 0.500 1 3 17 3 VAL CB C 31.788 0.500 1 4 18 4 GLU H H 8.501 0.002 1 5 18 4 GLU C C 178.081 0.209 1 6 18 4 GLU CA C 52.931 0.087 1 7 18 4 GLU CB C 31.073 0.153 1 8 18 4 GLU N N 124.977 0.500 1 9 19 5 THR H H 7.855 0.004 1 10 19 5 THR C C 179.533 0.122 1 11 19 5 THR CA C 59.294 0.500 1 12 19 5 THR CB C 67.108 0.500 1 13 19 5 THR N N 118.211 0.500 1 14 20 6 PHE H H 8.617 0.001 1 15 20 6 PHE C C 178.785 0.121 1 16 20 6 PHE CA C 53.360 0.500 1 17 20 6 PHE CB C 39.612 0.087 1 18 20 6 PHE N N 125.406 0.500 1 19 21 7 ALA H H 8.151 0.001 1 20 21 7 ALA C C 173.266 0.135 1 21 21 7 ALA CA C 48.052 0.500 1 22 21 7 ALA CB C 16.600 0.500 1 23 21 7 ALA N N 122.437 0.500 1 24 22 8 PHE H H 7.583 0.001 1 25 22 8 PHE C C 174.908 0.500 1 26 22 8 PHE CA C 56.338 0.500 1 27 22 8 PHE CB C 38.007 0.500 1 28 22 8 PHE N N 118.638 0.500 1 29 25 11 GLU C C 173.797 0.500 1 30 25 11 GLU CA C 57.504 0.500 1 31 25 11 GLU CB C 25.986 0.500 1 32 26 12 ILE H H 7.159 0.006 1 33 26 12 ILE C C 174.550 0.065 1 34 26 12 ILE CA C 61.272 0.153 1 35 26 12 ILE CB C 34.238 0.500 1 36 26 12 ILE N N 120.211 0.500 1 37 27 13 ALA H H 8.082 0.002 1 38 27 13 ALA C C 171.456 0.058 1 39 27 13 ALA CA C 52.667 0.500 1 40 27 13 ALA CB C 14.621 0.087 1 41 27 13 ALA N N 121.571 0.500 1 42 28 14 GLN H H 7.807 0.005 1 43 28 14 GLN C C 173.931 0.091 1 44 28 14 GLN CA C 55.964 0.500 1 45 28 14 GLN CB C 25.270 0.021 1 46 28 14 GLN N N 118.860 0.500 1 47 29 15 LEU H H 7.994 0.100 1 48 29 15 LEU C C 174.154 0.171 1 49 29 15 LEU CA C 55.700 0.087 1 50 29 15 LEU CB C 37.700 0.500 1 51 29 15 LEU N N 123.376 0.500 1 52 30 16 MET H H 8.230 0.003 1 53 30 16 MET C C 175.334 0.027 1 54 30 16 MET CA C 57.843 0.021 1 55 30 16 MET CB C 30.479 0.153 1 56 30 16 MET N N 116.907 0.500 1 57 31 17 SER H H 7.517 0.005 1 58 31 17 SER C C 175.819 0.022 1 59 31 17 SER CA C 58.832 0.500 1 60 31 17 SER CB C 60.283 0.500 1 61 31 17 SER N N 111.961 0.500 1 62 32 18 LEU H H 7.704 0.004 1 63 32 18 LEU C C 172.391 0.066 1 64 32 18 LEU CA C 55.634 0.500 1 65 32 18 LEU CB C 38.985 0.021 1 66 32 18 LEU N N 122.111 0.500 1 67 33 19 ILE H H 8.045 0.003 1 68 33 19 ILE C C 175.663 0.076 1 69 33 19 ILE CA C 62.162 0.219 1 70 33 19 ILE CB C 35.029 0.500 1 71 33 19 ILE N N 120.088 0.500 1 72 34 20 ILE H H 8.009 0.005 1 73 34 20 ILE C C 174.629 0.053 1 74 34 20 ILE CA C 61.668 0.153 1 75 34 20 ILE CB C 35.985 0.087 1 76 34 20 ILE N N 116.795 0.500 1 77 35 21 ASN H H 7.598 0.001 1 78 35 21 ASN C C 177.203 0.072 1 79 35 21 ASN CA C 51.678 0.500 1 80 35 21 ASN CB C 37.469 0.500 1 81 35 21 ASN N N 114.603 0.500 1 82 36 22 THR H H 7.199 0.007 1 83 36 22 THR C C 179.487 0.500 1 84 36 22 THR CA C 59.898 0.500 1 85 36 22 THR CB C 66.888 0.500 1 86 36 22 THR N N 117.019 0.500 1 87 37 23 PHE C C 177.424 0.500 1 88 37 23 PHE CA C 58.427 0.500 1 89 37 23 PHE CB C 37.129 0.500 1 90 38 24 TYR H H 7.026 0.002 1 91 38 24 TYR C C 175.349 0.150 1 92 38 24 TYR CA C 58.800 0.500 1 93 38 24 TYR CB C 34.436 0.500 1 94 38 24 TYR N N 110.256 0.500 1 95 39 25 SER H H 7.879 0.100 1 96 39 25 SER C C 175.289 0.500 1 97 39 25 SER CA C 59.173 0.500 1 98 39 25 SER CB C 60.492 0.500 1 99 39 25 SER N N 114.412 0.500 1 100 40 26 ASN C C 177.732 0.500 1 101 40 26 ASN CA C 49.459 0.500 1 102 40 26 ASN CB C 34.623 0.500 1 103 41 27 LYS H H 7.777 0.008 1 104 41 27 LYS C C 175.357 0.073 1 105 41 27 LYS CA C 56.525 0.500 1 106 41 27 LYS CB C 29.787 0.500 1 107 41 27 LYS N N 117.300 0.500 1 108 42 28 GLU H H 8.275 0.003 1 109 42 28 GLU C C 176.866 0.070 1 110 42 28 GLU CA C 55.536 0.152 1 111 42 28 GLU CB C 26.194 0.500 1 112 42 28 GLU N N 114.535 0.500 1 113 43 29 ILE H H 6.742 0.003 1 114 43 29 ILE C C 175.844 0.131 1 115 43 29 ILE CA C 59.492 0.021 1 116 43 29 ILE CB C 35.128 0.500 1 117 43 29 ILE N N 112.419 0.500 1 118 44 30 PHE H H 7.843 0.003 1 119 44 30 PHE C C 176.342 0.500 1 120 44 30 PHE CA C 56.799 0.500 1 121 44 30 PHE CB C 35.040 0.500 1 122 44 30 PHE N N 120.582 0.500 1 123 45 31 LEU C C 174.316 0.500 1 124 45 31 LEU CA C 53.679 0.500 1 125 45 31 LEU CB C 37.591 0.500 1 126 46 32 ARG H H 6.331 0.100 1 127 46 32 ARG C C 173.326 0.073 1 128 46 32 ARG CA C 55.733 0.153 1 129 46 32 ARG CB C 26.292 0.500 1 130 46 32 ARG N N 117.514 0.500 1 131 47 33 GLU H H 7.587 0.005 1 132 47 33 GLU C C 173.095 0.500 1 133 47 33 GLU CA C 55.634 0.087 1 134 47 33 GLU CB C 25.534 0.021 1 135 47 33 GLU N N 116.974 0.500 1 136 48 34 LEU H H 7.749 0.004 1 137 48 34 LEU C C 172.423 0.038 1 138 48 34 LEU CA C 55.437 0.500 1 139 48 34 LEU CB C 37.634 0.087 1 140 48 34 LEU N N 119.604 0.500 1 141 49 35 ILE H H 8.112 0.100 1 142 49 35 ILE C C 174.414 0.174 1 143 49 35 ILE CA C 63.382 0.153 1 144 49 35 ILE CB C 34.205 0.087 1 145 49 35 ILE N N 120.166 0.500 1 146 50 36 SER H H 8.127 0.003 1 147 50 36 SER C C 175.569 0.131 1 148 50 36 SER CA C 59.393 0.500 1 149 50 36 SER CB C 60.448 0.087 1 150 50 36 SER N N 117.008 0.500 1 151 51 37 ASN H H 7.772 0.001 1 152 51 37 ASN C C 173.198 0.500 1 153 51 37 ASN CA C 53.360 0.021 1 154 51 37 ASN CB C 34.930 0.500 1 155 51 37 ASN N N 120.719 0.500 1 156 52 38 SER H H 8.266 0.100 1 157 52 38 SER C C 176.995 0.120 1 158 52 38 SER CA C 60.909 0.500 1 159 52 38 SER CB C 60.184 0.500 1 160 52 38 SER N N 121.009 0.500 1 161 53 39 SER H H 8.451 0.002 1 162 53 39 SER C C 175.814 0.104 1 163 53 39 SER CA C 59.030 0.500 1 164 53 39 SER CB C 60.514 0.500 1 165 53 39 SER N N 116.143 0.500 1 166 54 40 ASP H H 8.068 0.001 1 167 54 40 ASP C C 173.816 0.106 1 168 54 40 ASP CA C 54.810 0.500 1 169 54 40 ASP CB C 37.601 0.021 1 170 54 40 ASP N N 119.661 0.500 1 171 55 41 ALA H H 7.732 0.001 1 172 55 41 ALA C C 170.427 0.106 1 173 55 41 ALA CA C 52.568 0.021 1 174 55 41 ALA CB C 16.072 0.087 1 175 55 41 ALA N N 123.376 0.500 1 176 56 42 LEU H H 8.351 0.001 1 177 56 42 LEU C C 174.473 0.077 1 178 56 42 LEU CA C 55.107 0.500 1 179 56 42 LEU CB C 37.700 0.086 1 180 56 42 LEU N N 124.670 0.500 1 181 57 43 ASP H H 8.701 0.002 1 182 57 43 ASP C C 173.418 0.074 1 183 57 43 ASP CA C 54.514 0.500 1 184 57 43 ASP CB C 37.073 0.153 1 185 57 43 ASP N N 119.930 0.500 1 186 58 44 LYS H H 7.648 0.001 1 187 58 44 LYS C C 172.675 0.144 1 188 58 44 LYS CA C 57.481 0.219 1 189 58 44 LYS CB C 29.820 0.500 1 190 58 44 LYS N N 117.469 0.500 1 191 59 45 ILE H H 7.241 0.002 1 192 59 45 ILE C C 176.134 0.071 1 193 59 45 ILE CA C 57.448 0.021 1 194 59 45 ILE CB C 35.326 0.500 1 195 59 45 ILE N N 117.143 0.500 1 196 60 46 ARG H H 8.462 0.100 1 197 60 46 ARG C C 172.634 0.103 1 198 60 46 ARG CA C 57.382 0.021 1 199 60 46 ARG CB C 27.084 0.500 1 200 60 46 ARG N N 127.098 0.500 1 201 61 47 TYR H H 8.569 0.100 1 202 61 47 TYR C C 172.514 0.035 1 203 61 47 TYR CA C 58.404 0.500 1 204 61 47 TYR CB C 34.864 0.087 1 205 61 47 TYR N N 118.627 0.500 1 206 62 48 GLU H H 7.986 0.100 1 207 62 48 GLU C C 172.445 0.051 1 208 62 48 GLU CA C 57.382 0.500 1 209 62 48 GLU CB C 26.919 0.500 1 210 62 48 GLU N N 119.380 0.500 1 211 63 49 THR H H 8.193 0.005 1 212 63 49 THR C C 177.336 0.093 1 213 63 49 THR CA C 57.481 0.087 1 214 63 49 THR CB C 60.975 0.087 1 215 63 49 THR N N 114.367 0.500 1 216 64 50 LEU H H 7.252 0.003 1 217 64 50 LEU C C 173.060 0.500 1 218 64 50 LEU CA C 54.557 0.500 1 219 64 50 LEU CB C 38.337 0.500 1 220 64 50 LEU N N 121.886 0.500 1 221 65 51 THR C C 177.685 0.500 1 222 65 51 THR CA C 59.482 0.500 1 223 65 51 THR CB C 66.735 0.500 1 224 66 52 ASP H H 7.197 0.004 1 225 66 52 ASP C C 178.831 0.500 1 226 66 52 ASP CA C 48.557 0.500 1 227 66 52 ASP CB C 38.403 0.500 1 228 66 52 ASP N N 118.098 0.500 1 229 67 53 PRO C C 173.393 0.500 1 230 67 53 PRO CA C 61.790 0.500 1 231 67 53 PRO CB C 28.887 0.500 1 232 68 54 SER H H 7.939 0.100 1 233 68 54 SER C C 175.364 0.077 1 234 68 54 SER CA C 58.239 0.153 1 235 68 54 SER CB C 60.316 0.219 1 236 68 54 SER N N 115.378 0.500 1 237 69 55 LYS H H 7.729 0.002 1 238 69 55 LYS C C 175.487 0.090 1 239 69 55 LYS CA C 54.942 0.153 1 240 69 55 LYS CB C 29.358 0.021 1 241 69 55 LYS N N 123.309 0.500 1 242 70 56 LEU H H 7.106 0.004 1 243 70 56 LEU C C 173.784 0.134 1 244 70 56 LEU CA C 51.151 0.500 1 245 70 56 LEU CB C 37.370 0.219 1 246 70 56 LEU N N 111.739 0.500 1 247 71 57 ASP H H 7.895 0.001 1 248 71 57 ASP C C 175.150 0.087 1 249 71 57 ASP CA C 54.843 0.500 1 250 71 57 ASP CB C 36.513 0.500 1 251 71 57 ASP N N 123.641 0.500 1 252 72 58 SER H H 7.336 0.100 1 253 72 58 SER C C 177.648 0.107 1 254 72 58 SER CA C 54.250 0.219 1 255 72 58 SER CB C 59.854 0.087 1 256 72 58 SER N N 109.174 0.500 1 257 73 59 GLY H H 7.538 0.001 1 258 73 59 GLY C C 177.743 0.500 1 259 73 59 GLY CA C 43.876 0.500 1 260 73 59 GLY N N 111.545 0.500 1 261 74 60 LYS C C 176.516 0.500 1 262 74 60 LYS CA C 54.932 0.500 1 263 74 60 LYS CB C 30.403 0.500 1 264 75 61 GLU H H 7.505 0.100 1 265 75 61 GLU C C 175.274 0.500 1 266 75 61 GLU CA C 53.832 0.500 1 267 75 61 GLU CB C 26.732 0.500 1 268 75 61 GLU N N 116.828 0.500 1 269 76 62 LEU C C 178.862 0.500 1 270 76 62 LEU CA C 51.174 0.500 1 271 76 62 LEU CB C 37.722 0.500 1 272 77 63 HIS H H 7.537 0.004 1 273 77 63 HIS C C 179.847 0.170 1 274 77 63 HIS CA C 52.041 0.500 1 275 77 63 HIS CB C 30.249 0.218 1 276 77 63 HIS N N 119.245 0.500 1 277 78 64 ILE H H 8.027 0.001 1 278 78 64 ILE C C 177.351 0.063 1 279 78 64 ILE CA C 57.613 0.500 1 280 78 64 ILE CB C 37.930 0.021 1 281 78 64 ILE N N 117.548 0.500 1 282 79 65 ASN H H 9.622 0.003 1 283 79 65 ASN C C 178.987 0.072 1 284 79 65 ASN CA C 48.381 0.087 1 285 79 65 ASN CB C 39.315 0.021 1 286 79 65 ASN N N 125.259 0.500 1 287 80 66 LEU H H 8.908 0.004 1 288 80 66 LEU C C 176.264 0.025 1 289 80 66 LEU CA C 50.656 0.500 1 290 80 66 LEU CB C 41.524 0.087 1 291 80 66 LEU N N 122.313 0.500 1 292 81 67 ILE H H 9.206 0.004 1 293 81 67 ILE C C 177.090 0.500 1 294 81 67 ILE CA C 56.206 0.500 1 295 81 67 ILE CB C 38.667 0.500 1 296 81 67 ILE N N 120.166 0.500 1 297 82 68 PRO C C 176.847 0.500 1 298 82 68 PRO CA C 59.482 0.500 1 299 82 68 PRO CB C 30.272 0.500 1 300 83 69 ASN H H 9.032 0.006 1 301 83 69 ASN C C 176.816 0.500 1 302 83 69 ASN CA C 49.876 0.500 1 303 83 69 ASN CB C 37.018 0.500 1 304 83 69 ASN N N 121.717 0.500 1 305 84 70 LYS C C 173.993 0.500 1 306 84 70 LYS CA C 56.844 0.500 1 307 84 70 LYS CB C 29.678 0.500 1 308 85 71 GLN H H 8.351 0.002 1 309 85 71 GLN C C 174.721 0.083 1 310 85 71 GLN CA C 56.294 0.219 1 311 85 71 GLN CB C 25.204 0.021 1 312 85 71 GLN N N 119.885 0.500 1 313 86 72 ASP H H 7.638 0.001 1 314 86 72 ASP C C 177.007 0.046 1 315 86 72 ASP CA C 51.085 0.500 1 316 86 72 ASP CB C 37.996 0.153 1 317 86 72 ASP N N 116.795 0.500 1 318 87 73 ARG H H 7.800 0.001 1 319 87 73 ARG C C 177.855 0.185 1 320 87 73 ARG CA C 54.415 0.500 1 321 87 73 ARG CB C 26.655 0.021 1 322 87 73 ARG N N 120.605 0.500 1 323 88 74 THR H H 7.898 0.001 1 324 88 74 THR C C 179.315 0.022 1 325 88 74 THR CA C 55.140 0.500 1 326 88 74 THR CB C 69.877 0.500 1 327 88 74 THR N N 106.258 0.500 1 328 89 75 LEU H H 8.317 0.002 1 329 89 75 LEU C C 178.035 0.087 1 330 89 75 LEU CA C 51.052 0.500 1 331 89 75 LEU CB C 42.282 0.021 1 332 89 75 LEU N N 122.336 0.500 1 333 90 76 THR H H 7.917 0.001 1 334 90 76 THR C C 179.108 0.187 1 335 90 76 THR CA C 58.997 0.500 1 336 90 76 THR CB C 67.108 0.086 1 337 90 76 THR N N 124.217 0.500 1 338 91 77 ILE H H 9.336 0.002 1 339 91 77 ILE C C 177.095 0.074 1 340 91 77 ILE CA C 57.711 0.021 1 341 91 77 ILE CB C 37.106 0.500 1 342 91 77 ILE N N 127.895 0.500 1 343 92 78 VAL H H 9.532 0.005 1 344 92 78 VAL C C 178.332 0.026 1 345 92 78 VAL CA C 57.810 0.500 1 346 92 78 VAL CB C 32.095 0.500 1 347 92 78 VAL N N 129.906 0.500 1 348 93 79 ASP H H 9.353 0.001 1 349 93 79 ASP C C 176.319 0.149 1 350 93 79 ASP CA C 50.059 0.161 1 351 93 79 ASP CB C 43.667 0.021 1 352 93 79 ASP N N 123.371 0.500 1 353 94 80 THR H H 7.134 0.008 1 354 94 80 THR C C 177.594 0.091 1 355 94 80 THR CA C 56.162 0.500 1 356 94 80 THR CB C 63.415 0.500 1 357 94 80 THR N N 109.299 0.500 1 358 95 81 GLY H H 9.432 0.002 1 359 95 81 GLY C C 180.181 0.117 1 360 95 81 GLY CA C 41.821 0.021 1 361 95 81 GLY N N 108.907 0.500 1 362 96 82 ILE H H 6.732 0.001 1 363 96 82 ILE C C 179.203 0.134 1 364 96 82 ILE CA C 59.887 0.021 1 365 96 82 ILE CB C 37.667 0.021 1 366 96 82 ILE N N 115.862 0.500 1 367 97 83 GLY H H 7.559 0.002 1 368 97 83 GLY C C 179.237 0.312 1 369 97 83 GLY CA C 41.095 0.021 1 370 97 83 GLY N N 103.655 0.500 1 371 98 84 MET H H 7.576 0.001 1 372 98 84 MET C C 177.310 0.104 1 373 98 84 MET CA C 52.634 0.021 1 374 98 84 MET CB C 34.699 0.021 1 375 98 84 MET N N 117.000 0.500 1 376 99 85 THR H H 7.951 0.005 1 377 99 85 THR C C 178.340 0.118 1 378 99 85 THR CA C 58.272 0.087 1 379 99 85 THR CB C 67.866 0.500 1 380 99 85 THR N N 112.315 0.500 1 381 100 86 LYS H H 8.515 0.007 1 382 100 86 LYS C C 174.345 0.035 1 383 100 86 LYS CA C 58.206 0.087 1 384 100 86 LYS CB C 28.468 0.500 1 385 100 86 LYS N N 121.133 0.500 1 386 101 87 ALA H H 7.753 0.001 1 387 101 87 ALA C C 172.521 0.082 1 388 101 87 ALA CA C 51.975 0.500 1 389 101 87 ALA CB C 15.050 0.021 1 390 101 87 ALA N N 116.705 0.500 1 391 102 88 ASP H H 7.292 0.001 1 392 102 88 ASP C C 174.360 0.125 1 393 102 88 ASP CA C 54.448 0.218 1 394 102 88 ASP CB C 37.667 0.152 1 395 102 88 ASP N N 117.593 0.500 1 396 103 89 LEU H H 8.045 0.005 1 397 103 89 LEU C C 174.721 0.268 1 398 103 89 LEU CA C 55.173 0.500 1 399 103 89 LEU CB C 40.106 0.153 1 400 103 89 LEU N N 121.459 0.500 1 401 104 90 ILE H H 7.472 0.004 1 402 104 90 ILE C C 173.380 0.242 1 403 104 90 ILE CA C 62.030 0.500 1 404 104 90 ILE CB C 35.853 0.500 1 405 104 90 ILE N N 116.042 0.500 1 406 105 91 ASN H H 8.208 0.009 1 407 105 91 ASN C C 174.920 0.184 1 408 105 91 ASN CA C 52.634 0.021 1 409 105 91 ASN CB C 35.886 0.500 1 410 105 91 ASN N N 117.683 0.500 1 411 106 92 ASN H H 8.641 0.006 1 412 106 92 ASN C C 176.259 0.500 1 413 106 92 ASN CA C 52.184 0.500 1 414 106 92 ASN CB C 35.436 0.500 1 415 106 92 ASN N N 116.278 0.500 1 416 116 102 LYS C C 173.947 0.500 1 417 116 102 LYS CA C 56.976 0.500 1 418 116 102 LYS CB C 28.953 0.500 1 419 117 103 ALA H H 7.773 0.001 1 420 117 103 ALA C C 171.740 0.085 1 421 117 103 ALA CA C 52.074 0.500 1 422 117 103 ALA CB C 15.248 0.021 1 423 117 103 ALA N N 120.719 0.500 1 424 118 104 PHE H H 8.215 0.100 1 425 118 104 PHE C C 175.893 0.139 1 426 118 104 PHE CA C 56.590 0.021 1 427 118 104 PHE CB C 35.161 0.153 1 428 118 104 PHE N N 120.121 0.500 1 429 119 105 MET H H 7.738 0.007 1 430 119 105 MET C C 173.364 0.088 1 431 119 105 MET CA C 57.019 0.500 1 432 119 105 MET CB C 29.556 0.021 1 433 119 105 MET N N 117.447 0.500 1 434 120 106 GLU H H 7.970 0.006 1 435 120 106 GLU C C 172.997 0.500 1 436 120 106 GLU CA C 56.656 0.021 1 437 120 106 GLU CB C 26.128 0.152 1 438 120 106 GLU N N 118.672 0.500 1 439 121 107 ALA H H 7.674 0.002 1 440 121 107 ALA C C 171.247 0.036 1 441 121 107 ALA CA C 52.338 0.500 1 442 121 107 ALA CB C 13.830 0.500 1 443 121 107 ALA N N 124.180 0.500 1 444 122 108 LEU H H 8.197 0.001 1 445 122 108 LEU C C 170.750 0.067 1 446 122 108 LEU CA C 54.909 0.087 1 447 122 108 LEU CB C 38.293 0.087 1 448 122 108 LEU N N 120.188 0.500 1 449 123 109 GLN H H 7.701 0.002 1 450 123 109 GLN C C 175.632 0.076 1 451 123 109 GLN CA C 55.569 0.500 1 452 123 109 GLN CB C 25.303 0.500 1 453 123 109 GLN N N 119.515 0.500 1 454 124 110 ALA H H 7.281 0.001 1 455 124 110 ALA C C 174.805 0.069 1 456 124 110 ALA CA C 49.107 0.500 1 457 124 110 ALA CB C 15.940 0.087 1 458 124 110 ALA N N 120.391 0.500 1 459 125 111 GLY H H 7.539 0.100 1 460 125 111 GLY C C 177.474 0.245 1 461 125 111 GLY CA C 42.612 0.500 1 462 125 111 GLY N N 106.137 0.500 1 463 126 112 ALA H H 7.988 0.001 1 464 126 112 ALA C C 176.882 0.131 1 465 126 112 ALA CA C 49.667 0.021 1 466 126 112 ALA CB C 16.468 0.500 1 467 126 112 ALA N N 123.395 0.500 1 468 127 113 ASP H H 8.040 0.003 1 469 127 113 ASP C C 175.247 0.097 1 470 127 113 ASP CA C 51.217 0.087 1 471 127 113 ASP CB C 41.392 0.219 1 472 127 113 ASP N N 118.649 0.500 1 473 128 114 ILE H H 7.585 0.006 1 474 128 114 ILE C C 177.076 0.500 1 475 128 114 ILE CA C 58.997 0.500 1 476 128 114 ILE CB C 35.095 0.021 1 477 128 114 ILE N N 123.236 0.500 1 478 129 115 SER H H 8.430 0.003 1 479 129 115 SER C C 176.514 0.202 1 480 129 115 SER CA C 58.008 0.500 1 481 129 115 SER CB C 60.481 0.500 1 482 129 115 SER N N 114.535 0.500 1 483 130 116 MET H H 7.859 0.002 1 484 130 116 MET C C 175.943 0.169 1 485 130 116 MET CA C 53.887 0.153 1 486 130 116 MET CB C 30.183 0.500 1 487 130 116 MET N N 120.188 0.500 1 488 131 117 ILE H H 7.721 0.006 1 489 131 117 ILE C C 176.968 0.500 1 490 131 117 ILE CA C 62.338 0.500 1 491 131 117 ILE CB C 34.381 0.500 1 492 131 117 ILE N N 119.391 0.500 1 493 132 118 GLY C C 174.760 0.500 1 494 132 118 GLY CA C 44.052 0.500 1 495 133 119 GLN H H 7.873 0.100 1 496 133 119 GLN C C 175.731 0.090 1 497 133 119 GLN CA C 54.349 0.500 1 498 133 119 GLN CB C 24.875 0.021 1 499 133 119 GLN N N 120.133 0.500 1 500 134 120 PHE H H 7.220 0.100 1 501 134 120 PHE C C 176.228 0.500 1 502 134 120 PHE CA C 55.305 0.500 1 503 134 120 PHE CB C 37.348 0.500 1 504 134 120 PHE N N 115.671 0.500 1 505 135 121 GLY H H 7.601 0.003 1 506 135 121 GLY C C 177.747 0.500 1 507 135 121 GLY CA C 44.128 0.021 1 508 135 121 GLY N N 109.271 0.500 1 509 136 122 VAL H H 6.471 0.004 1 510 136 122 VAL C C 176.833 0.104 1 511 136 122 VAL CA C 57.118 0.021 1 512 136 122 VAL CB C 28.172 0.500 1 513 136 122 VAL N N 108.203 0.500 1 514 137 123 GLY H H 8.618 0.002 1 515 137 123 GLY C C 176.696 0.500 1 516 137 123 GLY CA C 44.997 0.500 1 517 137 123 GLY N N 107.730 0.500 1 518 138 124 PHE C C 176.847 0.500 1 519 138 124 PHE CA C 54.075 0.500 1 520 138 124 PHE CB C 35.283 0.500 1 521 139 125 TYR H H 7.002 0.003 1 522 139 125 TYR C C 175.152 0.500 1 523 139 125 TYR CA C 56.667 0.500 1 524 139 125 TYR CB C 33.458 0.500 1 525 139 125 TYR N N 121.661 0.500 1 526 140 126 SER C C 177.079 0.500 1 527 140 126 SER CA C 59.416 0.500 1 528 140 126 SER CB C 60.405 0.500 1 529 141 127 ALA H H 7.884 0.002 1 530 141 127 ALA C C 173.632 0.106 1 531 141 127 ALA CA C 52.436 0.021 1 532 141 127 ALA CB C 15.611 0.086 1 533 141 127 ALA N N 125.382 0.500 1 534 142 128 TYR H H 7.280 0.005 1 535 142 128 TYR C C 176.912 0.101 1 536 142 128 TYR CA C 58.305 0.153 1 537 142 128 TYR CB C 33.644 0.500 1 538 142 128 TYR N N 112.003 0.500 1 539 143 129 LEU H H 7.940 0.001 1 540 143 129 LEU C C 173.686 0.030 1 541 143 129 LEU CA C 54.942 0.153 1 542 143 129 LEU CB C 40.469 0.087 1 543 143 129 LEU N N 118.593 0.500 1 544 144 130 VAL H H 6.482 0.003 1 545 144 130 VAL C C 178.958 0.131 1 546 144 130 VAL CA C 57.415 0.500 1 547 144 130 VAL CB C 30.512 0.087 1 548 144 130 VAL N N 102.671 0.500 1 549 145 131 ALA H H 7.558 0.001 1 550 145 131 ALA C C 176.736 0.176 1 551 145 131 ALA CA C 48.019 0.021 1 552 145 131 ALA CB C 18.808 0.021 1 553 145 131 ALA N N 124.388 0.500 1 554 146 132 GLU H H 8.425 0.001 1 555 146 132 GLU C C 176.974 0.316 1 556 146 132 GLU CA C 53.129 0.087 1 557 146 132 GLU CB C 27.908 0.021 1 558 146 132 GLU N N 118.053 0.500 1 559 147 133 LYS H H 7.319 0.004 1 560 147 133 LYS C C 179.333 0.058 1 561 147 133 LYS CA C 53.030 0.153 1 562 147 133 LYS CB C 32.392 0.500 1 563 147 133 LYS N N 117.042 0.500 1 564 148 134 VAL H H 7.922 0.002 1 565 148 134 VAL C C 178.176 0.125 1 566 148 134 VAL CA C 58.766 0.021 1 567 148 134 VAL CB C 32.425 0.500 1 568 148 134 VAL N N 125.664 0.500 1 569 149 135 THR H H 8.976 0.002 1 570 149 135 THR C C 179.029 0.061 1 571 149 135 THR CA C 58.865 0.500 1 572 149 135 THR CB C 67.965 0.087 1 573 149 135 THR N N 124.916 0.500 1 574 150 136 VAL H H 10.349 0.004 1 575 150 136 VAL C C 177.783 0.127 1 576 150 136 VAL CA C 58.371 0.021 1 577 150 136 VAL CB C 31.435 0.500 1 578 150 136 VAL N N 128.373 0.500 1 579 151 137 ILE H H 9.516 0.100 1 580 151 137 ILE C C 176.914 0.081 1 581 151 137 ILE CA C 56.294 0.500 1 582 151 137 ILE CB C 36.183 0.500 1 583 151 137 ILE N N 128.643 0.500 1 584 152 138 THR H H 9.072 0.002 1 585 152 138 THR C C 175.901 0.500 1 586 152 138 THR CA C 57.052 0.500 1 587 152 138 THR CB C 68.525 0.153 1 588 152 138 THR N N 122.133 0.500 1 589 153 139 LYS H H 8.778 0.003 1 590 153 139 LYS C C 180.224 0.059 1 591 153 139 LYS CA C 52.107 0.021 1 592 153 139 LYS CB C 33.809 0.500 1 593 153 139 LYS N N 127.368 0.500 1 594 154 140 HIS H H 9.553 0.004 1 595 154 140 HIS C C 175.632 0.041 1 596 154 140 HIS CA C 51.711 0.285 1 597 154 140 HIS CB C 31.996 0.153 1 598 154 140 HIS N N 132.015 0.500 1 599 155 141 ASN H H 9.521 0.004 1 600 155 141 ASN C C 174.890 0.500 1 601 155 141 ASN CA C 53.371 0.500 1 602 155 141 ASN CB C 35.633 0.500 1 603 155 141 ASN N N 126.203 0.500 1 604 156 142 ASP C C 176.758 0.500 1 605 156 142 ASP CA C 52.031 0.500 1 606 156 142 ASP CB C 37.920 0.500 1 607 157 143 ASP H H 8.251 0.003 1 608 157 143 ASP C C 178.337 0.112 1 609 157 143 ASP CA C 49.960 0.079 1 610 157 143 ASP CB C 43.238 0.087 1 611 157 143 ASP N N 123.800 0.500 1 612 158 144 GLU H H 9.245 0.001 1 613 158 144 GLU C C 179.399 0.068 1 614 158 144 GLU CA C 51.645 0.153 1 615 158 144 GLU CB C 27.842 0.021 1 616 158 144 GLU N N 117.705 0.500 1 617 159 145 GLN H H 8.014 0.100 1 618 159 145 GLN C C 176.163 0.500 1 619 159 145 GLN CA C 53.459 0.500 1 620 159 145 GLN CB C 27.743 0.087 1 621 159 145 GLN N N 119.526 0.500 1 622 160 146 TYR H H 8.584 0.100 1 623 160 146 TYR C C 178.685 0.106 1 624 160 146 TYR CA C 55.799 0.500 1 625 160 146 TYR CB C 42.051 0.500 1 626 160 146 TYR N N 124.695 0.500 1 627 161 147 ALA H H 9.178 0.004 1 628 161 147 ALA C C 176.571 0.089 1 629 161 147 ALA CA C 47.788 0.219 1 630 161 147 ALA CB C 18.940 0.500 1 631 161 147 ALA N N 119.672 0.500 1 632 162 148 TRP H H 10.232 0.001 1 633 162 148 TRP C C 176.297 0.139 1 634 162 148 TRP CA C 52.667 0.087 1 635 162 148 TRP CB C 33.216 0.087 1 636 162 148 TRP N N 130.041 0.500 1 637 163 149 GLU H H 8.619 0.002 1 638 163 149 GLU C C 177.065 0.134 1 639 163 149 GLU CA C 53.590 0.087 1 640 163 149 GLU CB C 31.600 0.021 1 641 163 149 GLU N N 126.460 0.500 1 642 164 150 SER H H 8.164 0.002 1 643 164 150 SER C C 175.320 0.500 1 644 164 150 SER CA C 56.997 0.500 1 645 164 150 SER CB C 63.723 0.500 1 646 164 150 SER N N 113.704 0.500 1 647 168 154 GLY C C 177.839 0.500 1 648 168 154 GLY CA C 43.195 0.500 1 649 169 155 SER H H 7.659 0.001 1 650 169 155 SER C C 180.711 0.157 1 651 169 155 SER CA C 54.481 0.500 1 652 169 155 SER CB C 64.668 0.087 1 653 169 155 SER N N 115.738 0.500 1 654 170 156 PHE H H 8.689 0.005 1 655 170 156 PHE C C 180.046 0.172 1 656 170 156 PHE CA C 52.404 0.500 1 657 170 156 PHE CB C 39.117 0.021 1 658 170 156 PHE N N 119.560 0.500 1 659 171 157 THR H H 8.685 0.001 1 660 171 157 THR C C 177.701 0.092 1 661 171 157 THR CA C 56.195 0.500 1 662 171 157 THR CB C 69.877 0.087 1 663 171 157 THR N N 110.366 0.500 1 664 172 158 VAL H H 8.734 0.001 1 665 172 158 VAL C C 177.467 0.081 1 666 172 158 VAL CA C 58.700 0.021 1 667 172 158 VAL CB C 33.249 0.021 1 668 172 158 VAL N N 118.481 0.500 1 669 173 159 ARG H H 9.107 0.100 1 670 173 159 ARG C C 176.842 0.149 1 671 173 159 ARG CA C 51.217 0.219 1 672 173 159 ARG CB C 31.106 0.500 1 673 173 159 ARG N N 124.683 0.500 1 674 174 160 THR H H 8.730 0.001 1 675 174 160 THR C C 177.745 0.058 1 676 174 160 THR CA C 60.975 0.087 1 677 174 160 THR CB C 66.184 0.500 1 678 174 160 THR N N 117.705 0.500 1 679 175 161 ASP H H 8.481 0.002 1 680 175 161 ASP C C 176.167 0.500 1 681 175 161 ASP CA C 51.854 0.500 1 682 175 161 ASP CB C 41.040 0.500 1 683 175 161 ASP N N 126.362 0.500 1 684 176 162 THR C C 177.362 0.500 1 685 176 162 THR CA C 58.295 0.500 1 686 176 162 THR CB C 65.878 0.500 1 687 177 163 GLY H H 7.689 0.001 1 688 177 163 GLY C C 179.360 0.111 1 689 177 163 GLY CA C 41.491 0.153 1 690 177 163 GLY N N 110.255 0.500 1 691 178 164 GLU H H 8.168 0.001 1 692 178 164 GLU C C 176.648 0.500 1 693 178 164 GLU CA C 52.052 0.500 1 694 178 164 GLU CB C 26.402 0.500 1 695 178 164 GLU N N 121.019 0.069 1 696 179 165 PRO C C 174.529 0.500 1 697 179 165 PRO CA C 60.537 0.500 1 698 179 165 PRO CB C 29.217 0.500 1 699 180 166 MET H H 9.295 0.001 1 700 180 166 MET C C 175.778 0.113 1 701 180 166 MET CA C 52.206 0.500 1 702 180 166 MET CB C 32.139 0.500 1 703 180 166 MET N N 124.094 0.500 1 704 181 167 GLY H H 8.455 0.017 1 705 181 167 GLY C C 178.482 0.500 1 706 181 167 GLY CA C 44.392 0.500 1 707 181 167 GLY N N 111.432 0.500 1 708 182 168 ARG H H 7.308 0.002 1 709 182 168 ARG C C 177.724 0.108 1 710 182 168 ARG CA C 54.316 0.087 1 711 182 168 ARG CB C 27.347 0.500 1 712 182 168 ARG N N 120.020 0.500 1 713 183 169 GLY H H 9.051 0.002 1 714 183 169 GLY C C 179.955 0.138 1 715 183 169 GLY CA C 41.326 0.500 1 716 183 169 GLY N N 115.525 0.500 1 717 184 170 THR H H 7.635 0.001 1 718 184 170 THR C C 181.341 0.500 1 719 184 170 THR CA C 59.525 0.087 1 720 184 170 THR CB C 69.745 0.087 1 721 184 170 THR N N 116.120 0.500 1 722 185 171 LYS H H 9.912 0.002 1 723 185 171 LYS C C 178.832 0.133 1 724 185 171 LYS CA C 51.678 0.500 1 725 185 171 LYS CB C 32.556 0.087 1 726 185 171 LYS N N 128.263 0.500 1 727 186 172 VAL H H 9.066 0.001 1 728 186 172 VAL C C 177.947 0.083 1 729 186 172 VAL CA C 59.195 0.500 1 730 186 172 VAL CB C 30.117 0.500 1 731 186 172 VAL N N 126.546 0.500 1 732 187 173 ILE H H 9.858 0.100 1 733 187 173 ILE C C 177.388 0.500 1 734 187 173 ILE CA C 58.832 0.153 1 735 187 173 ILE CB C 36.447 0.500 1 736 187 173 ILE N N 127.871 0.500 1 737 188 174 LEU H H 8.760 0.100 1 738 188 174 LEU C C 177.059 0.500 1 739 188 174 LEU CA C 51.217 0.087 1 740 188 174 LEU CB C 39.051 0.021 1 741 188 174 LEU N N 125.811 0.500 1 742 189 175 HIS H H 8.204 0.001 1 743 189 175 HIS C C 176.860 0.011 1 744 189 175 HIS CA C 52.898 0.021 1 745 189 175 HIS CB C 25.468 0.021 1 746 189 175 HIS N N 125.210 0.500 1 747 190 176 LEU H H 7.884 0.100 1 748 190 176 LEU C C 174.456 0.074 1 749 190 176 LEU CA C 53.360 0.500 1 750 190 176 LEU CB C 38.722 0.021 1 751 190 176 LEU N N 123.616 0.500 1 752 191 177 LYS H H 8.324 0.100 1 753 191 177 LYS C C 174.054 0.094 1 754 191 177 LYS CA C 54.250 0.087 1 755 191 177 LYS CB C 31.007 0.021 1 756 191 177 LYS N N 120.504 0.500 1 757 192 178 GLU H H 8.892 0.004 1 758 192 178 GLU C C 176.031 0.170 1 759 192 178 GLU CA C 56.854 0.021 1 760 192 178 GLU CB C 26.820 0.500 1 761 192 178 GLU N N 120.616 0.500 1 762 193 179 ASP H H 8.254 0.004 1 763 193 179 ASP C C 174.931 0.138 1 764 193 179 ASP CA C 50.755 0.500 1 765 193 179 ASP CB C 36.743 0.500 1 766 193 179 ASP N N 113.265 0.500 1 767 194 180 GLN H H 7.746 0.003 1 768 194 180 GLN C C 176.368 0.082 1 769 194 180 GLN CA C 51.283 0.500 1 770 194 180 GLN CB C 24.743 0.021 1 771 194 180 GLN N N 118.638 0.500 1 772 195 181 THR H H 7.299 0.004 1 773 195 181 THR C C 174.946 0.108 1 774 195 181 THR CA C 61.569 0.500 1 775 195 181 THR CB C 65.657 0.087 1 776 195 181 THR N N 106.525 0.500 1 777 196 182 GLU H H 8.743 0.003 1 778 196 182 GLU C C 175.740 0.107 1 779 196 182 GLU CA C 55.931 0.021 1 780 196 182 GLU CB C 25.633 0.087 1 781 196 182 GLU N N 124.008 0.500 1 782 197 183 TYR H H 6.531 0.003 1 783 197 183 TYR C C 180.812 0.116 1 784 197 183 TYR CA C 57.118 0.021 1 785 197 183 TYR CB C 34.370 0.021 1 786 197 183 TYR N N 114.749 0.500 1 787 198 184 LEU H H 7.168 0.006 1 788 198 184 LEU C C 175.816 0.108 1 789 198 184 LEU CA C 50.689 0.500 1 790 198 184 LEU CB C 39.150 0.500 1 791 198 184 LEU N N 111.046 0.500 1 792 199 185 GLU H H 7.176 0.001 1 793 199 185 GLU C C 175.289 0.500 1 794 199 185 GLU CA C 52.250 0.500 1 795 199 185 GLU CB C 27.128 0.500 1 796 199 185 GLU N N 116.547 0.500 1 797 200 186 GLU C C 174.916 0.500 1 798 200 186 GLU CA C 57.767 0.500 1 799 200 186 GLU CB C 26.777 0.500 1 800 201 187 ARG H H 8.759 0.001 1 801 201 187 ARG C C 173.962 0.062 1 802 201 187 ARG CA C 56.821 0.500 1 803 201 187 ARG CB C 26.589 0.021 1 804 201 187 ARG N N 116.176 0.500 1 805 202 188 ARG H H 6.644 0.001 1 806 202 188 ARG C C 174.223 0.095 1 807 202 188 ARG CA C 54.250 0.500 1 808 202 188 ARG CB C 27.380 0.021 1 809 202 188 ARG N N 119.436 0.500 1 810 203 189 ILE H H 7.987 0.003 1 811 203 189 ILE C C 174.284 0.035 1 812 203 189 ILE CA C 62.953 0.500 1 813 203 189 ILE CB C 35.029 0.021 1 814 203 189 ILE N N 117.727 0.500 1 815 204 190 LYS H H 8.313 0.100 1 816 204 190 LYS C C 172.909 0.094 1 817 204 190 LYS CA C 57.810 0.087 1 818 204 190 LYS CB C 29.260 0.500 1 819 204 190 LYS N N 116.761 0.500 1 820 205 191 GLU H H 7.580 0.100 1 821 205 191 GLU C C 173.340 0.131 1 822 205 191 GLU CA C 56.459 0.021 1 823 205 191 GLU CB C 26.292 0.500 1 824 205 191 GLU N N 118.594 0.500 1 825 206 192 ILE H H 7.753 0.002 1 826 206 192 ILE C C 173.751 0.129 1 827 206 192 ILE CA C 62.690 0.087 1 828 206 192 ILE CB C 35.326 0.219 1 829 206 192 ILE N N 121.133 0.500 1 830 207 193 VAL H H 8.262 0.002 1 831 207 193 VAL C C 173.858 0.129 1 832 207 193 VAL CA C 64.009 0.218 1 833 207 193 VAL CB C 28.798 0.500 1 834 207 193 VAL N N 120.695 0.500 1 835 208 194 LYS H H 7.786 0.002 1 836 208 194 LYS C C 174.445 0.112 1 837 208 194 LYS CA C 56.096 0.500 1 838 208 194 LYS CB C 29.260 0.086 1 839 208 194 LYS N N 118.773 0.500 1 840 209 195 LYS H H 7.382 0.002 1 841 209 195 LYS C C 173.916 0.032 1 842 209 195 LYS CA C 55.997 0.021 1 843 209 195 LYS CB C 30.545 0.500 1 844 209 195 LYS N N 116.446 0.500 1 845 210 196 HIS H H 7.709 0.004 1 846 210 196 HIS C C 174.867 0.131 1 847 210 196 HIS CA C 54.579 0.500 1 848 210 196 HIS CB C 30.941 0.500 1 849 210 196 HIS N N 113.389 0.500 1 850 211 197 SER H H 8.051 0.004 1 851 211 197 SER C C 176.724 0.500 1 852 211 197 SER CA C 56.206 0.500 1 853 211 197 SER CB C 61.085 0.500 1 854 211 197 SER N N 115.558 0.500 1 855 215 201 GLY C C 179.470 0.500 1 856 215 201 GLY CA C 43.195 0.500 1 857 216 202 TYR H H 6.619 0.100 1 858 216 202 TYR C C 180.296 0.500 1 859 216 202 TYR CA C 53.173 0.500 1 860 216 202 TYR CB C 38.007 0.500 1 861 216 202 TYR N N 117.795 0.500 1 862 217 203 PRO C C 176.901 0.500 1 863 217 203 PRO CA C 60.669 0.500 1 864 217 203 PRO CB C 29.019 0.500 1 865 218 204 ILE H H 7.921 0.001 1 866 218 204 ILE C C 175.880 0.114 1 867 218 204 ILE CA C 57.448 0.500 1 868 218 204 ILE CB C 37.040 0.087 1 869 218 204 ILE N N 123.444 0.500 1 870 219 205 THR H H 8.584 0.004 1 871 219 205 THR C C 179.946 0.153 1 872 219 205 THR CA C 58.569 0.500 1 873 219 205 THR CB C 67.668 0.500 1 874 219 205 THR N N 122.978 0.500 1 875 220 206 LEU H H 8.528 0.001 1 876 220 206 LEU C C 176.725 0.103 1 877 220 206 LEU CA C 51.414 0.087 1 878 220 206 LEU CB C 40.601 0.087 1 879 220 206 LEU N N 127.723 0.500 1 880 221 207 PHE H H 8.672 0.001 1 881 221 207 PHE C C 178.378 0.113 1 882 221 207 PHE CA C 54.612 0.500 1 883 221 207 PHE CB C 37.271 0.021 1 884 221 207 PHE N N 127.037 0.500 1 885 222 208 VAL H H 7.890 0.002 1 886 222 208 VAL C C 177.163 0.083 1 887 222 208 VAL CA C 58.734 0.500 1 888 222 208 VAL CB C 30.677 0.500 1 889 222 208 VAL N N 121.380 0.500 1 890 223 209 GLU H H 7.929 0.001 1 891 223 209 GLU C C 171.134 0.500 1 892 223 209 GLU CA C 55.547 0.500 1 893 223 209 GLU CB C 28.512 0.500 1 894 223 209 GLU N N 129.918 0.500 1 stop_ save_