data_7003 #Corrected using PDB structure: 2UWDA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 17 V CA 55.26 60.59 #138 F CA 56.52 61.82 # #After reference correction, the following residues still #have a CO chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 17 V C 177.75 171.18 # 19 T C 179.53 173.57 # 25 E C 173.79 179.51 # 27 A C 171.45 179.76 # 32 L C 172.38 179.01 # 36 T C 179.48 174.13 # 47 E C 173.09 179.45 # 48 L C 172.42 179.39 # 54 D C 173.81 178.82 # 55 A C 170.42 179.80 # 57 D C 173.41 179.37 # 58 K C 172.67 179.33 # 61 Y C 172.51 178.07 # 62 E C 172.44 179.49 # 66 D C 178.82 173.53 # 67 P C 173.39 179.11 # 72 S C 177.64 171.89 # 77 H C 179.84 172.43 # 79 N C 178.98 173.64 # 84 K C 173.99 180.10 # 88 T C 179.31 173.52 # 90 T C 179.10 173.22 # 95 G C 180.17 174.51 # 97 G C 179.23 172.00 #101 A C 172.51 178.87 #103 L C 174.71 179.89 #117 A C 171.73 179.21 #119 M C 173.36 178.50 #120 E C 172.99 179.34 #121 A C 171.24 179.70 #122 L C 170.74 180.13 #123 Q C 175.63 181.22 #141 A C 173.63 178.75 #149 T C 179.02 173.26 #153 K C 180.22 174.21 #169 S C 180.70 173.33 #170 F C 180.04 173.55 #177 G C 179.35 172.50 #181 G C 178.48 173.08 #183 G C 179.95 171.90 #184 T C 181.33 173.09 #201 R C 173.96 178.97 #204 K C 172.90 178.86 #205 E C 173.33 179.06 #215 G C 179.46 172.48 #216 Y C 180.29 172.90 #219 T C 179.94 173.89 #223 E C 171.13 177.10 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 38 Y N 110.47 128.77 # 39 S N 114.63 124.84 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #N/A 2.44 2.72 -0.01 0.22 0.17 # #bmr7003.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr7003.str file): #HA CA CB CO N HN #N/A +2.58 +2.58 -0.01 +0.22 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN # N/A +/-0.15 +/-0.15 +/-0.26 +/-0.27 +/-0.05 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #N/A 0.961 0.996 -0.777 0.824 0.735 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #N/A 0.987 1.009 1.519 1.735 0.329 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR backbone assignment of the human HSP90 N-terminal domain ; 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_ _BMRB_accession_number 7003 _BMRB_flat_file_name bmr7003.str _Entry_type new _Submission_date 2006-02-23 _Accession_date 2006-02-23 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 558 "1H chemical shifts" 168 "15N chemical shifts" 168 stop_ _Release_immediately no _Release_on_publication yes save_ save_contact_persons _Saveframe_category contact_persons loop_ _Family_name _Given_name _Middle_initials _Family_title _Department_and_Institution _Mailing_address _Phone_number _Email_address _FAX_number Vogtherr Martin ? ? ; AstraZeneca R&D ; ; 50F23 Mereside Alderley Park, Macclesfield, Cheshire, England SK10 4TG ; "+44 1625 514832" martin.vogtherr@astrazeneca.com ? Schwalbe Harald ? ? ; Institut fuer Organische Chemie und Chemische Biologie, Zentrum fuer Biomolekulare Magnetische Resonanz, Goethe-Universitaet Frankfurt am Main ; ; Marie-Curie-Str. 11, D-60439 Frankfurt, Germany ; "+49 69 79829130" schwalbe@nmr.uni-frankfurt.de ? stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; NMR Backbone Assignment of the N-terminal Domain of Human HSP90 ; _Citation_status published _Citation_type journal _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 ? _Journal_issue ? _Page_first ? _Page_last ? _Year 2006 save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name hsp90 _Abbreviation_common hsp90 loop_ _Mol_system_component_name _Mol_label "human heat shock protein 90 N-terminal domain" $hsp90 stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state "not present" _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 _Name_variant "hsp90 n-terminal domain" _Abbreviation_common "hsp90 n-terminal domain" _Mol_thiol_state "not present" ############################## # 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 2006-10-26 _Sequence_homology_query_revised_last_date 2006-10-05 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 1OSF "A Chain A, Human Hsp90 In Complex With17-Desmethoxy-17-N,N-Dimethylaminoethylamino-Geldanamycin" 97.21 215 100 100 10e-113 PDB 1BYQ "A Chain A, Hsp90 N-Terminal Domain Bound ToAdp-Mg" 91.67 228 100 100 10e-113 PDB 1YER 'Chain , Human Hsp90 Geldanamycin-BindingDomain, "closed" Conformation' 91.67 228 100 100 10e-113 PDB 1YES 'Chain , Human Hsp90 Geldanamycin-BindingDomain, "open" Conformation' 91.67 228 100 100 10e-113 PDB 1YET "Chain , Geldanamycin Bound To The Hsp90Geldanamycin-Binding Domain" 91.67 228 100 100 10e-113 PDB 2BSM "A Chain A, Novel, Potent Small MoleculeInhibitors Of The Molecular Chaperone Hsp90 DiscoveredThrough Structure-Based Design" 88.94 235 100 100 10e-113 PDB 2BT0 "A Chain A, Novel, Potent Small MoleculeInhibitors Of The Molecular Chaperone Hsp90 DiscoveredThrough Structure-Based Design" 88.94 235 100 100 10e-113 PDB 2BYH "A Chain A,3-(5-Chloro-2,4-Dihydroxyphenyl)-Pyrazole-4-CarboxamidesAs Inhibitors Of The Hsp90 Molecular Chaperone" 88.94 235 100 100 10e-113 PDB 2BYI "A Chain A,3-(5-Chloro-2,4-Dihydroxyphenyl)-Pyrazole-4-CarboxamidesAs Inhibitors Of The Hsp90 Molecular Chaperone" 88.94 235 100 100 10e-113 PDB 2BZ5 "A Chain A, Structure-Based Discovery Of A NewClass Of Hsp90 Inhibitors" 88.94 235 100 100 10e-113 PDB 2CCS "A Chain A, Human Hsp90 With4-Chloro-6-(4-Piperazin-1-Yl-1h-Pyrazol-3-Yl)-Benzene-1,2-Diol" 88.56 236 100 100 10e-113 PDB 2CCT "A Chain A, Human Hsp90 With5-(5-Chloro-2,4-Dihydroxy-Phenyl)-4-Piperazin-1-Yl-2h-Pyrazole-3-Carboxylic Acid Ethylamide" 88.56 236 100 100 10e-113 PDB 2CCU "A Chain A, Human Hsp90 With4-Chloro-6-(4-(4-(4-Methanesulphonyl-Benzyl)-Pierazin-1-Yl)-1h-Pyrazol-3-Yl)-Benzene-1,3-Diol" 88.56 236 100 100 10e-113 PDB 1UY6 "A Chain A, Human Hsp90-Alpha With9-Butyl-8-(3,4,5-Trimethoxy-Benzyl)-9h-Purin-6-Ylamine" 88.56 236 100 100 10e-113 PDB 1UY7 "A Chain A, Human Hsp90-Alpha With9-Butyl-8-(4-Methoxy-Benzyl)-9h-Purin-6-Ylamine" 88.56 236 100 100 10e-113 PDB 1UY8 "A Chain A, Human Hsp90-Alpha With9-Butyl-8-(3-Trimethoxy-Benzyl)-9h-Purin-6ylamine" 88.56 236 100 100 10e-113 PDB 1UY9 "A Chain A, Human Hsp90-Alpha With8-Benzo[1,3]dioxol-,5-Ylmethyl-9-Butyl-9h-Purin-6-Ylamine" 88.56 236 100 100 10e-113 PDB 1UYC "A Chain A, Human Hsp90-Alpha With9-Butyl-8-(2,5-Dimethoxy-Benzyl)-9h-Purin-6-Ylamine" 88.56 236 100 100 10e-113 PDB 1UYD "A Chain A, Human Hsp90-Alpha With 9-Butyl-8-(2-Chloro-3,4,5-Trimethoxy-Benzyl)-9h-Purin-6-Ylamine" 88.56 236 100 100 10e-113 PDB 1UYE "A Chain A, Human Hsp90-Alpha With8-(2-Chloro-3,4,5-Trimethoxy-Benzyl)-9-Pent-4-Ylnyl-9h-Purin-6-Ylamine" 88.56 236 100 100 10e-113 PDB 1UYF "A Chain A, Human Hsp90-Alpha With8-(2-Chloro-3,4,5-Trimethoxy-Benzyl)-2-Fluoro-9-Pent-4-Ylnyl-9h-Purin-6-Ylamine" 88.56 236 100 100 10e-113 PDB 1UYG "A Chain A, Human Hsp90-Alpha With8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9h-Purin-6-Ylamine" 88.56 236 100 100 10e-113 PDB 1UYH "A Chain A, Human Hsp90-Alpha With 9-Butyl-8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9h-Purin-6-Ylamine" 88.56 236 100 100 10e-113 PDB 1UYI "A Chain A, Human Hsp90-Alpha With8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9-Pent-9h-Purin-6-Ylamine" 88.56 236 100 100 1e-113 PDB 1UYK "A Chain A, Human Hsp90-Alpha With8-Benzo[1,3]dioxol-,5-Ylmethyl-9-ButYl-2-Fluoro-9h-Purin-6-Ylamine" 88.56 236 100 100 10e-113 PDB 1UYL "A Chain A, Structure-Activity Relationships InPurine-Based Inhibitor Binding To Hsp90 Isoforms" 88.56 236 100 100 10e-113 PDB 2CDD "A Chain A, Human Hsp90 With4-(4-(2,3-Dihydro-Benzol(1,4)dioxin-6-Yl)-5-Methyl-1h-Pyrazol-3-Yl)-6-Ethyl-Benzene-1,3-Diol" 88.56 236 100 100 10e-113 PDB 1YC1 "A Chain A, Crystal Structures Of HumanHsp90alpha Complexed With Dihydroxyphenylpyrazoles" 79.17 264 100 100 10e-113 PDB 1YC3 "A Chain A, Crystal Structure Of HumanHsp90alpha Complexed With Dihydroxyphenylpyrazoles" 79.17 264 100 100 10e-113 PDB 1YC4 "A Chain A, Crystal Structure Of HumanHsp90alpha Complexed With Dihydroxyphenylpyrazoles" 79.17 264 100 100 10e-113 DBJ BAC40681.1 "unnamed protein product [Mus musculus]" 76.28 274 99 100 1e-111 DBJ BAC36610.1 "unnamed protein product [Mus musculus]" 37.52 557 99 100 1e-111 DBJ BAB20777.1 "heat shock protein 90 alpha [Equuscaballus]" 29.07 719 100 100 10e-113 DBJ BAC82487.1 "90-kDa heat shock protein alpha [Bostaurus]" 28.51 733 100 100 10e-113 DBJ BAE01934.1 "unnamed protein product [Macacafascicularis]" 28.51 733 100 100 10e-113 EMBL CAA33259.1 "unnamed protein product [Homo sapiens]" 28.55 732 100 100 10e-113 EMBL CAH92137.1 "hypothetical protein [Pongo pygmaeus]" 28.55 732 100 100 10e-113 EMBL CAI64496.1 "Heat shock protein HSP 90-alpha 4 [Homosapiens]" 28.55 732 100 100 10e-113 EMBL CAC39453.1 "heat shock protein 86 [Rattusnorvegicus]" 28.51 733 100 100 10e-113 EMBL CAD21648.1 "heat shock protein 86 [Rattusnorvegicus]" 28.51 733 100 100 10e-113 GenBank AAI02619.1 "HSPCA protein [Bos taurus]" 83.60 250 100 100 10e-113 GenBank AAI08696.1 "HSP90AA1 protein [Homo sapiens]" 35.73 585 100 100 10e-113 GenBank AAH72489.1 "Heat shock protein 1, alpha [Rattusnorvegicus]" 28.51 733 100 100 10e-113 GenBank AAH85120.1 "Heat shock protein 1, alpha [Rattusnorvegicus]" 28.51 733 100 100 10e-113 GenBank ABC40730.1 "heat shock 90kDa protein 1, alpha [Homosapiens]" 24.47 854 100 100 10e-113 REF NP_005339.2 "heat shock protein 90kDa alpha(cytosolic), class A member 1 isoform 2 [Homo sapiens]" 28.55 732 100 100 10e-113 REF XP_001161435.1 "PREDICTED: hypothetical proteinisoform 5 [Pan troglodytes]" 28.51 733 100 100 10e-113 REF XP_001161624.1 "PREDICTED: hypothetical proteinisoform 9 [Pan troglodytes]" 28.51 733 100 100 10e-113 REF XP_001161572.1 "PREDICTED: heat shock protein90kDa alpha (cytosolic), class A member 1 isoform 8 [Pantroglodytes]" 24.47 854 100 100 10e-113 REF XP_001160832.1 "PREDICTED: heat shock protein90kDa alpha (cytosolic), class A member 1 isoform 1 [Pantroglodytes]" 24.44 855 100 100 10e-113 SWISS-PROT Q9GKX7 "HS90A_HORSE Heat shock protein HSP 90-alpha(HSP 86)" 29.07 719 100 100 10e-113 SWISS-PROT P07900 "HS90A_HUMAN Heat shock protein HSP 90-alpha(HSP 86) (NY-REN-38 antigen)" 28.55 732 100 100 10e-113 SWISS-PROT O02705 "HS90A_PIG Heat shock protein HSP 90-alpha (HSP86)" 28.51 733 100 100 10e-113 SWISS-PROT P07901 "HS90A_MOUSE Heat shock protein HSP 90-alpha(HSP 86) (Tumor-specific transplantation 86 kDa antigen)(TSTA)" 28.51 733 99 100 1e-111 SWISS-PROT Q76LV2 "HS90A_BOVIN Heat shock protein HSP 90-alpha" 28.51 733 100 100 10e-113 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 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 save_ ############################# # NMR applied experiments # ############################# save_NMR_experiment_list _Saveframe_category NMR_applied_experiment _Experiment_name ; 1H15N TROSY TROSY HNCO TROSY HNCACO TROSY HNCACB TROSY HNCOCACB TROSY HNCA ; save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions 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 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 H 1 "methyl protons" ppm 0.0 internal direct ? ? ? 1.0 DSS C 13 "methyl protons" ppm 0.0 . indirect ? ? ? 0.251449530 DSS N 15 "methyl protons" ppm 0.0 . indirect ? ? ? 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 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) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts 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" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 17 VAL C C 177.75 0.500 1 2 17 VAL CA C 55.40 0.500 1 3 17 VAL CB C 34.37 0.500 1 4 18 GLU H H 8.50 0.002 1 5 18 GLU C C 178.07 0.209 1 6 18 GLU CA C 55.51 0.087 1 7 18 GLU CB C 33.65 0.153 1 8 18 GLU N N 125.19 0.500 1 9 19 THR H H 7.86 0.004 1 10 19 THR C C 179.53 0.122 1 11 19 THR CA C 61.88 0.500 1 12 19 THR CB C 69.69 0.500 1 13 19 THR N N 118.43 0.500 1 14 20 PHE H H 8.62 0.001 1 15 20 PHE C C 178.78 0.121 1 16 20 PHE CA C 55.94 0.500 1 17 20 PHE CB C 42.19 0.087 1 18 20 PHE N N 125.62 0.500 1 19 21 ALA H H 8.15 0.001 1 20 21 ALA C C 173.26 0.135 1 21 21 ALA CA C 50.63 0.500 1 22 21 ALA CB C 19.18 0.500 1 24 22 PHE H H 7.58 0.001 1 25 22 PHE C C 174.90 0.500 1 26 22 PHE CA C 58.92 0.500 1 27 22 PHE CB C 40.59 0.500 1 28 22 PHE N N 118.85 0.500 1 29 25 GLU C C 173.79 0.500 1 30 25 GLU CA C 60.09 0.500 1 31 25 GLU CB C 28.57 0.500 1 32 26 ILE H H 7.16 0.006 1 33 26 ILE C C 174.54 0.065 1 34 26 ILE CA C 63.85 0.153 1 35 26 ILE CB C 36.82 0.500 1 36 26 ILE N N 120.43 0.500 1 37 27 ALA H H 8.08 0.002 1 38 27 ALA C C 171.45 0.058 1 39 27 ALA CA C 55.25 0.500 1 40 27 ALA CB C 17.20 0.087 1 41 27 ALA N N 121.79 0.500 1 42 28 GLN H H 7.81 0.005 1 43 28 GLN C C 173.92 0.091 1 44 28 GLN CA C 58.55 0.500 1 45 28 GLN CB C 27.85 0.021 1 46 28 GLN N N 119.08 0.500 1 47 29 LEU H H 7.99 0.100 1 48 29 LEU C C 174.15 0.171 1 49 29 LEU CA C 58.28 0.087 1 50 29 LEU CB C 40.28 0.500 1 52 30 MET H H 8.23 0.003 1 53 30 MET C C 175.33 0.027 1 54 30 MET CA C 60.42 0.021 1 55 30 MET CB C 33.06 0.153 1 56 30 MET N N 117.12 0.500 1 57 31 SER H H 7.52 0.005 1 58 31 SER C C 175.81 0.022 1 59 31 SER CA C 61.41 0.500 1 60 31 SER CB C 62.86 0.500 1 61 31 SER N N 112.18 0.500 1 62 32 LEU H H 7.70 0.004 1 63 32 LEU C C 172.38 0.066 1 64 32 LEU CA C 58.22 0.500 1 65 32 LEU CB C 41.57 0.021 1 66 32 LEU N N 122.33 0.500 1 67 33 ILE H H 8.04 0.003 1 68 33 ILE C C 175.66 0.076 1 69 33 ILE CA C 64.74 0.219 1 70 33 ILE CB C 37.61 0.500 1 71 33 ILE N N 120.30 0.500 1 72 34 ILE H H 8.01 0.005 1 73 34 ILE C C 174.62 0.053 1 74 34 ILE CA C 64.25 0.153 1 75 34 ILE CB C 38.57 0.087 1 76 34 ILE N N 117.01 0.500 1 77 35 ASN H H 7.60 0.001 1 78 35 ASN C C 177.20 0.072 1 79 35 ASN CA C 54.26 0.500 1 80 35 ASN CB C 40.05 0.500 1 81 35 ASN N N 114.82 0.500 1 82 36 THR H H 7.20 0.007 1 83 36 THR C C 179.48 0.500 1 84 36 THR CA C 62.48 0.500 1 85 36 THR CB C 69.47 0.500 1 86 36 THR N N 117.23 0.500 1 87 37 PHE C C 177.42 0.500 1 88 37 PHE CA C 61.01 0.500 1 89 37 PHE CB C 39.71 0.500 1 90 38 TYR H H 7.03 0.002 1 91 38 TYR C C 175.34 0.150 1 92 38 TYR CA C 61.38 0.500 1 93 38 TYR CB C 37.02 0.500 1 94 38 TYR N N 110.47 0.500 1 95 39 SER H H 7.88 0.100 1 96 39 SER C C 175.28 0.500 1 97 39 SER CA C 61.75 0.500 1 98 39 SER CB C 63.07 0.500 1 99 39 SER N N 114.63 0.500 1 100 40 ASN C C 177.73 0.500 1 101 40 ASN CA C 52.04 0.500 1 102 40 ASN CB C 37.20 0.500 1 103 41 LYS H H 7.78 0.008 1 104 41 LYS C C 175.35 0.073 1 105 41 LYS CA C 59.11 0.500 1 106 41 LYS CB C 32.37 0.500 1 107 41 LYS N N 117.52 0.500 1 108 42 GLU H H 8.28 0.003 1 109 42 GLU C C 176.86 0.070 1 110 42 GLU CA C 58.12 0.152 1 111 42 GLU CB C 28.78 0.500 1 112 42 GLU N N 114.75 0.500 1 113 43 ILE H H 6.74 0.003 1 114 43 ILE C C 175.84 0.131 1 115 43 ILE CA C 62.07 0.021 1 116 43 ILE CB C 37.71 0.500 1 117 43 ILE N N 112.63 0.500 1 118 44 PHE H H 7.84 0.003 1 119 44 PHE C C 176.34 0.500 1 120 44 PHE CA C 59.38 0.500 1 121 44 PHE CB C 37.62 0.500 1 122 44 PHE N N 120.80 0.500 1 123 45 LEU C C 174.31 0.500 1 124 45 LEU CA C 56.26 0.500 1 125 45 LEU CB C 40.17 0.500 1 126 46 ARG H H 6.33 0.100 1 127 46 ARG C C 173.32 0.073 1 128 46 ARG CA C 58.31 0.153 1 129 46 ARG CB C 28.87 0.500 1 130 46 ARG N N 117.73 0.500 1 131 47 GLU H H 7.59 0.005 1 132 47 GLU C C 173.09 0.500 1 133 47 GLU CA C 58.22 0.087 1 134 47 GLU CB C 28.12 0.021 1 135 47 GLU N N 117.19 0.500 1 136 48 LEU H H 7.75 0.004 1 137 48 LEU C C 172.42 0.038 1 138 48 LEU CA C 58.02 0.500 1 139 48 LEU CB C 40.22 0.087 1 140 48 LEU N N 119.82 0.500 1 141 49 ILE H H 8.11 0.100 1 142 49 ILE C C 174.41 0.174 1 143 49 ILE CA C 65.96 0.153 1 144 49 ILE CB C 36.79 0.087 1 146 50 SER H H 8.13 0.003 1 147 50 SER C C 175.56 0.131 1 148 50 SER CA C 61.97 0.500 1 149 50 SER CB C 63.03 0.087 1 150 50 SER N N 117.22 0.500 1 151 51 ASN H H 7.77 0.001 1 152 51 ASN C C 173.19 0.500 1 153 51 ASN CA C 55.94 0.021 1 154 51 ASN CB C 37.51 0.500 1 156 52 SER H H 8.27 0.100 1 157 52 SER C C 176.99 0.120 1 158 52 SER CA C 63.49 0.500 1 159 52 SER CB C 62.77 0.500 1 160 52 SER N N 121.22 0.500 1 161 53 SER H H 8.45 0.002 1 162 53 SER C C 175.81 0.104 1 163 53 SER CA C 61.61 0.500 1 164 53 SER CB C 63.10 0.500 1 165 53 SER N N 116.36 0.500 1 166 54 ASP H H 8.07 0.001 1 167 54 ASP C C 173.81 0.106 1 168 54 ASP CA C 57.39 0.500 1 169 54 ASP CB C 40.18 0.021 1 170 54 ASP N N 119.88 0.500 1 171 55 ALA H H 7.73 0.001 1 172 55 ALA C C 170.42 0.106 1 173 55 ALA CA C 55.15 0.021 1 174 55 ALA CB C 18.65 0.087 1 175 55 ALA N N 123.59 0.500 1 176 56 LEU H H 8.35 0.001 1 177 56 LEU C C 174.47 0.077 1 178 56 LEU CA C 57.69 0.500 1 179 56 LEU CB C 40.28 0.086 1 180 56 LEU N N 124.89 0.500 1 181 57 ASP H H 8.70 0.002 1 182 57 ASP C C 173.41 0.074 1 183 57 ASP CA C 57.10 0.500 1 185 57 ASP N N 120.15 0.500 1 186 58 LYS H H 7.65 0.001 1 187 58 LYS C C 172.67 0.144 1 188 58 LYS CA C 60.06 0.219 1 189 58 LYS CB C 32.40 0.500 1 191 59 ILE H H 7.24 0.002 1 192 59 ILE C C 176.13 0.071 1 193 59 ILE CA C 60.03 0.021 1 194 59 ILE CB C 37.91 0.500 1 195 59 ILE N N 117.36 0.500 1 196 60 ARG H H 8.46 0.100 1 197 60 ARG C C 172.63 0.103 1 198 60 ARG CA C 59.96 0.021 1 199 60 ARG CB C 29.67 0.500 1 201 61 TYR H H 8.57 0.100 1 202 61 TYR C C 172.51 0.035 1 203 61 TYR CA C 60.99 0.500 1 204 61 TYR CB C 37.45 0.087 1 205 61 TYR N N 118.84 0.500 1 206 62 GLU H H 7.99 0.100 1 207 62 GLU C C 172.44 0.051 1 208 62 GLU CA C 59.96 0.500 1 209 62 GLU CB C 29.50 0.500 1 210 62 GLU N N 119.60 0.500 1 211 63 THR H H 8.19 0.005 1 212 63 THR C C 177.33 0.093 1 213 63 THR CA C 60.06 0.087 1 214 63 THR CB C 63.56 0.087 1 215 63 THR N N 114.58 0.500 1 216 64 LEU H H 7.25 0.003 1 217 64 LEU C C 173.05 0.500 1 218 64 LEU CA C 57.14 0.500 1 219 64 LEU CB C 40.92 0.500 1 220 64 LEU N N 122.10 0.500 1 221 65 THR C C 177.68 0.500 1 222 65 THR CA C 62.06 0.500 1 223 65 THR CB C 69.32 0.500 1 224 66 ASP H H 7.20 0.004 1 225 66 ASP C C 178.82 0.500 1 226 66 ASP CA C 51.14 0.500 1 227 66 ASP CB C 40.98 0.500 1 229 67 PRO C C 173.39 0.500 1 230 67 PRO CA C 64.37 0.500 1 231 67 PRO CB C 31.47 0.500 1 232 68 SER H H 7.94 0.100 1 233 68 SER C C 175.36 0.077 1 234 68 SER CA C 60.82 0.153 1 235 68 SER CB C 62.90 0.219 1 237 69 LYS H H 7.73 0.002 1 238 69 LYS C C 175.48 0.090 1 239 69 LYS CA C 57.52 0.153 1 240 69 LYS CB C 31.94 0.021 1 241 69 LYS N N 123.52 0.500 1 242 70 LEU H H 7.11 0.004 1 243 70 LEU C C 173.78 0.134 1 244 70 LEU CA C 53.73 0.500 1 245 70 LEU CB C 39.95 0.219 1 246 70 LEU N N 111.95 0.500 1 247 71 ASP H H 7.89 0.001 1 248 71 ASP C C 175.14 0.087 1 249 71 ASP CA C 57.42 0.500 1 250 71 ASP CB C 39.09 0.500 1 251 71 ASP N N 123.86 0.500 1 252 72 SER H H 7.34 0.100 1 253 72 SER C C 177.64 0.107 1 254 72 SER CA C 56.83 0.219 1 255 72 SER CB C 62.44 0.087 1 256 72 SER N N 109.39 0.500 1 257 73 GLY H H 7.54 0.001 1 258 73 GLY C C 177.74 0.500 1 259 73 GLY CA C 46.46 0.500 1 260 73 GLY N N 111.76 0.500 1 261 74 LYS C C 176.51 0.500 1 262 74 LYS CA C 57.51 0.500 1 263 74 LYS CB C 32.98 0.500 1 264 75 GLU H H 7.50 0.100 1 265 75 GLU C C 175.27 0.500 1 266 75 GLU CA C 56.41 0.500 1 267 75 GLU CB C 29.31 0.500 1 268 75 GLU N N 117.04 0.500 1 269 76 LEU C C 178.86 0.500 1 270 76 LEU CA C 53.76 0.500 1 271 76 LEU CB C 40.30 0.500 1 272 77 HIS H H 7.54 0.004 1 273 77 HIS C C 179.84 0.170 1 274 77 HIS CA C 54.62 0.500 1 275 77 HIS CB C 32.83 0.218 1 276 77 HIS N N 119.46 0.500 1 277 78 ILE H H 8.03 0.001 1 278 78 ILE C C 177.34 0.063 1 279 78 ILE CA C 60.19 0.500 1 280 78 ILE CB C 40.51 0.021 1 281 78 ILE N N 117.76 0.500 1 282 79 ASN H H 9.62 0.003 1 283 79 ASN C C 178.98 0.072 1 284 79 ASN CA C 50.96 0.087 1 286 79 ASN N N 125.47 0.500 1 287 80 LEU H H 8.91 0.004 1 288 80 LEU C C 176.26 0.025 1 289 80 LEU CA C 53.24 0.500 1 290 80 LEU CB C 44.11 0.087 1 291 80 LEU N N 122.53 0.500 1 292 81 ILE H H 9.21 0.004 1 293 81 ILE C C 177.08 0.500 1 294 81 ILE CA C 58.79 0.500 1 296 81 ILE N N 120.38 0.500 1 297 82 PRO C C 176.84 0.500 1 298 82 PRO CA C 62.06 0.500 1 299 82 PRO CB C 32.85 0.500 1 300 83 ASN H H 9.03 0.006 1 301 83 ASN C C 176.81 0.500 1 302 83 ASN CA C 52.46 0.500 1 303 83 ASN CB C 39.60 0.500 1 304 83 ASN N N 121.93 0.500 1 305 84 LYS C C 173.99 0.500 1 306 84 LYS CA C 59.43 0.500 1 307 84 LYS CB C 32.26 0.500 1 308 85 GLN H H 8.35 0.002 1 309 85 GLN C C 174.71 0.083 1 310 85 GLN CA C 58.88 0.219 1 311 85 GLN CB C 27.79 0.021 1 312 85 GLN N N 120.10 0.500 1 313 86 ASP H H 7.64 0.001 1 314 86 ASP C C 177.00 0.046 1 315 86 ASP CA C 53.67 0.500 1 316 86 ASP CB C 40.58 0.153 1 317 86 ASP N N 117.01 0.500 1 318 87 ARG H H 7.80 0.001 1 319 87 ARG C C 177.85 0.185 1 320 87 ARG CA C 57.00 0.500 1 321 87 ARG CB C 29.24 0.021 1 322 87 ARG N N 120.82 0.500 1 323 88 THR H H 7.90 0.001 1 324 88 THR C C 179.31 0.022 1 325 88 THR CA C 57.72 0.500 1 326 88 THR CB C 72.46 0.500 1 327 88 THR N N 106.47 0.500 1 328 89 LEU H H 8.32 0.002 1 329 89 LEU C C 178.03 0.087 1 330 89 LEU CA C 53.63 0.500 1 331 89 LEU CB C 44.86 0.021 1 332 89 LEU N N 122.55 0.500 1 333 90 THR H H 7.92 0.001 1 334 90 THR C C 179.10 0.187 1 335 90 THR CA C 61.58 0.500 1 336 90 THR CB C 69.69 0.086 1 337 90 THR N N 124.43 0.500 1 338 91 ILE H H 9.34 0.002 1 343 92 VAL H H 9.53 0.005 1 348 93 ASP H H 9.35 0.001 1 353 94 THR H H 7.13 0.008 1 358 95 GLY H H 9.43 0.002 1 362 96 ILE H H 6.73 0.001 1 367 97 GLY H H 7.56 0.002 1 371 98 MET H H 7.58 0.001 1 376 99 THR H H 7.95 0.005 1 381 100 LYS H H 8.52 0.007 1 382 100 LYS C C 174.34 0.035 1 383 100 LYS CA C 60.79 0.087 1 384 100 LYS CB C 31.05 0.500 1 386 101 ALA H H 7.75 0.001 1 387 101 ALA C C 172.51 0.082 1 388 101 ALA CA C 54.56 0.500 1 389 101 ALA CB C 17.63 0.021 1 390 101 ALA N N 116.92 0.500 1 391 102 ASP H H 7.29 0.001 1 392 102 ASP C C 174.35 0.125 1 393 102 ASP CA C 57.03 0.218 1 394 102 ASP CB C 40.25 0.152 1 395 102 ASP N N 117.81 0.500 1 396 103 LEU H H 8.04 0.005 1 397 103 LEU C C 174.71 0.268 1 398 103 LEU CA C 57.75 0.500 1 399 103 LEU CB C 42.69 0.153 1 400 103 LEU N N 121.67 0.500 1 401 104 ILE H H 7.47 0.004 1 402 104 ILE C C 173.37 0.242 1 403 104 ILE CA C 64.61 0.500 1 404 104 ILE CB C 38.43 0.500 1 405 104 ILE N N 116.26 0.500 1 406 105 ASN H H 8.21 0.009 1 407 105 ASN C C 174.91 0.184 1 408 105 ASN CA C 55.22 0.021 1 409 105 ASN CB C 38.47 0.500 1 410 105 ASN N N 117.90 0.500 1 411 106 ASN H H 8.64 0.006 1 412 106 ASN C C 176.25 0.500 1 413 106 ASN CA C 54.77 0.500 1 414 106 ASN CB C 38.02 0.500 1 415 106 ASN N N 116.49 0.500 1 416 116 LYS C C 173.94 0.500 1 417 116 LYS CA C 59.56 0.500 1 419 117 ALA H H 7.77 0.001 1 420 117 ALA C C 171.73 0.085 1 421 117 ALA CA C 54.66 0.500 1 422 117 ALA CB C 17.83 0.021 1 423 117 ALA N N 120.93 0.500 1 424 118 PHE H H 8.21 0.100 1 425 118 PHE C C 175.89 0.139 1 426 118 PHE CA C 59.17 0.021 1 427 118 PHE CB C 37.74 0.153 1 428 118 PHE N N 120.34 0.500 1 429 119 MET H H 7.74 0.007 1 430 119 MET C C 173.36 0.088 1 431 119 MET CA C 59.60 0.500 1 433 119 MET N N 117.66 0.500 1 434 120 GLU H H 7.97 0.006 1 435 120 GLU C C 172.99 0.500 1 436 120 GLU CA C 59.24 0.021 1 437 120 GLU CB C 28.71 0.152 1 438 120 GLU N N 118.89 0.500 1 439 121 ALA H H 7.67 0.002 1 440 121 ALA C C 171.24 0.036 1 441 121 ALA CA C 54.92 0.500 1 443 121 ALA N N 124.40 0.500 1 444 122 LEU H H 8.20 0.001 1 445 122 LEU C C 170.74 0.067 1 446 122 LEU CA C 57.49 0.087 1 447 122 LEU CB C 40.87 0.087 1 449 123 GLN H H 7.70 0.002 1 450 123 GLN C C 175.63 0.076 1 451 123 GLN CA C 58.15 0.500 1 452 123 GLN CB C 27.88 0.500 1 453 123 GLN N N 119.73 0.500 1 454 124 ALA H H 7.28 0.001 1 455 124 ALA C C 174.80 0.069 1 456 124 ALA CA C 51.69 0.500 1 457 124 ALA CB C 18.52 0.087 1 459 125 GLY H H 7.54 0.100 1 460 125 GLY C C 177.47 0.245 1 461 125 GLY CA C 45.19 0.500 1 462 125 GLY N N 106.35 0.500 1 463 126 ALA H H 7.99 0.001 1 464 126 ALA C C 176.88 0.131 1 465 126 ALA CA C 52.25 0.021 1 466 126 ALA CB C 19.05 0.500 1 467 126 ALA N N 123.61 0.500 1 468 127 ASP H H 8.04 0.003 1 469 127 ASP C C 175.24 0.097 1 470 127 ASP CA C 53.80 0.087 1 471 127 ASP CB C 43.97 0.219 1 472 127 ASP N N 118.86 0.500 1 473 128 ILE H H 7.58 0.006 1 474 128 ILE C C 177.07 0.500 1 475 128 ILE CA C 61.58 0.500 1 476 128 ILE CB C 37.68 0.021 1 477 128 ILE N N 123.45 0.500 1 478 129 SER H H 8.43 0.003 1 479 129 SER C C 176.51 0.202 1 480 129 SER CA C 60.59 0.500 1 481 129 SER CB C 63.06 0.500 1 482 129 SER N N 114.75 0.500 1 483 130 MET H H 7.86 0.002 1 484 130 MET C C 175.94 0.169 1 485 130 MET CA C 56.47 0.153 1 486 130 MET CB C 32.76 0.500 1 487 130 MET N N 120.40 0.500 1 488 131 ILE H H 7.72 0.006 1 489 131 ILE C C 176.96 0.500 1 490 131 ILE CA C 64.92 0.500 1 491 131 ILE CB C 36.96 0.500 1 492 131 ILE N N 119.61 0.500 1 493 132 GLY C C 174.75 0.500 1 494 132 GLY CA C 46.63 0.500 1 495 133 GLN H H 7.87 0.100 1 496 133 GLN C C 175.72 0.090 1 497 133 GLN CA C 56.93 0.500 1 498 133 GLN CB C 27.46 0.021 1 499 133 GLN N N 120.35 0.500 1 500 134 PHE H H 7.22 0.100 1 501 134 PHE C C 176.22 0.500 1 502 134 PHE CA C 57.89 0.500 1 503 134 PHE CB C 39.93 0.500 1 504 134 PHE N N 115.89 0.500 1 505 135 GLY H H 7.60 0.003 1 506 135 GLY C C 177.74 0.500 1 507 135 GLY CA C 46.71 0.021 1 508 135 GLY N N 109.49 0.500 1 509 136 VAL H H 6.47 0.004 1 510 136 VAL C C 176.83 0.104 1 511 136 VAL CA C 59.70 0.021 1 512 136 VAL CB C 30.75 0.500 1 513 136 VAL N N 108.42 0.500 1 514 137 GLY H H 8.62 0.002 1 515 137 GLY C C 176.69 0.500 1 516 137 GLY CA C 47.58 0.500 1 517 137 GLY N N 107.95 0.500 1 518 138 PHE C C 176.84 0.500 1 519 138 PHE CA C 56.66 0.500 1 520 138 PHE CB C 37.86 0.500 1 521 139 TYR H H 7.00 0.003 1 522 139 TYR C C 175.15 0.500 1 523 139 TYR CA C 59.25 0.500 1 524 139 TYR CB C 36.04 0.500 1 525 139 TYR N N 121.88 0.500 1 526 140 SER C C 177.07 0.500 1 527 140 SER CA C 62.00 0.500 1 528 140 SER CB C 62.99 0.500 1 529 141 ALA H H 7.88 0.002 1 530 141 ALA C C 173.63 0.106 1 531 141 ALA CA C 55.02 0.021 1 532 141 ALA CB C 18.19 0.086 1 533 141 ALA N N 125.60 0.500 1 534 142 TYR H H 7.28 0.005 1 535 142 TYR C C 176.91 0.101 1 536 142 TYR CA C 60.89 0.153 1 537 142 TYR CB C 36.23 0.500 1 538 142 TYR N N 112.22 0.500 1 539 143 LEU H H 7.94 0.001 1 540 143 LEU C C 173.68 0.030 1 541 143 LEU CA C 57.52 0.153 1 542 143 LEU CB C 43.05 0.087 1 543 143 LEU N N 118.81 0.500 1 544 144 VAL H H 6.48 0.003 1 545 144 VAL C C 178.95 0.131 1 546 144 VAL CA C 60.00 0.500 1 547 144 VAL CB C 33.09 0.087 1 548 144 VAL N N 102.89 0.500 1 549 145 ALA H H 7.56 0.001 1 550 145 ALA C C 176.73 0.176 1 551 145 ALA CA C 50.60 0.021 1 552 145 ALA CB C 21.39 0.021 1 553 145 ALA N N 124.60 0.500 1 554 146 GLU H H 8.43 0.001 1 555 146 GLU C C 176.97 0.316 1 556 146 GLU CA C 55.71 0.087 1 557 146 GLU CB C 30.49 0.021 1 558 146 GLU N N 118.27 0.500 1 559 147 LYS H H 7.32 0.004 1 560 147 LYS C C 179.33 0.058 1 561 147 LYS CA C 55.61 0.153 1 562 147 LYS CB C 34.97 0.500 1 563 147 LYS N N 117.26 0.500 1 564 148 VAL H H 7.92 0.002 1 565 148 VAL C C 178.17 0.125 1 566 148 VAL CA C 61.35 0.021 1 567 148 VAL CB C 35.01 0.500 1 568 148 VAL N N 125.88 0.500 1 569 149 THR H H 8.98 0.002 1 574 150 VAL H H 10.35 0.004 1 579 151 ILE H H 9.52 0.100 1 584 152 THR H H 9.07 0.002 1 585 152 THR C C 175.89 0.500 1 586 152 THR CA C 59.63 0.500 1 589 153 LYS H H 8.78 0.003 1 590 153 LYS C C 180.22 0.059 1 591 153 LYS CA C 54.69 0.021 1 592 153 LYS CB C 36.39 0.500 1 593 153 LYS N N 127.58 0.500 1 594 154 HIS H H 9.55 0.004 1 595 154 HIS C C 175.63 0.041 1 596 154 HIS CA C 54.29 0.285 1 597 154 HIS CB C 34.58 0.153 1 598 154 HIS N N 132.23 0.500 1 599 155 ASN H H 9.52 0.004 1 600 155 ASN C C 174.88 0.500 1 601 155 ASN CA C 55.95 0.500 1 602 155 ASN CB C 38.21 0.500 1 603 155 ASN N N 126.42 0.500 1 604 156 ASP C C 176.75 0.500 1 605 156 ASP CA C 54.61 0.500 1 606 156 ASP CB C 40.50 0.500 1 607 157 ASP H H 8.25 0.003 1 608 157 ASP C C 178.33 0.112 1 609 157 ASP CA C 52.54 0.079 1 610 157 ASP CB C 45.82 0.087 1 611 157 ASP N N 124.02 0.500 1 612 158 GLU H H 9.24 0.001 1 613 158 GLU C C 179.39 0.068 1 614 158 GLU CA C 54.23 0.153 1 615 158 GLU CB C 30.42 0.021 1 616 158 GLU N N 117.92 0.500 1 617 159 GLN H H 8.01 0.100 1 618 159 GLN C C 176.16 0.500 1 619 159 GLN CA C 56.04 0.500 1 620 159 GLN CB C 30.32 0.087 1 621 159 GLN N N 119.74 0.500 1 622 160 TYR H H 8.58 0.100 1 623 160 TYR C C 178.68 0.106 1 624 160 TYR CA C 58.38 0.500 1 625 160 TYR CB C 44.63 0.500 1 627 161 ALA H H 9.18 0.004 1 628 161 ALA C C 176.56 0.089 1 629 161 ALA CA C 50.37 0.219 1 631 161 ALA N N 119.89 0.500 1 632 162 TRP H H 10.23 0.001 1 633 162 TRP C C 176.29 0.139 1 634 162 TRP CA C 55.25 0.087 1 635 162 TRP CB C 35.80 0.087 1 636 162 TRP N N 130.26 0.500 1 637 163 GLU H H 8.62 0.002 1 638 163 GLU C C 177.06 0.134 1 639 163 GLU CA C 56.17 0.087 1 640 163 GLU CB C 34.18 0.021 1 642 164 SER H H 8.16 0.002 1 643 164 SER C C 175.31 0.500 1 644 164 SER CA C 59.58 0.500 1 645 164 SER CB C 66.30 0.500 1 646 164 SER N N 113.92 0.500 1 647 168 GLY C C 177.83 0.500 1 648 168 GLY CA C 45.78 0.500 1 649 169 SER H H 7.66 0.001 1 650 169 SER C C 180.70 0.157 1 651 169 SER CA C 57.06 0.500 1 652 169 SER CB C 67.25 0.087 1 653 169 SER N N 115.95 0.500 1 654 170 PHE H H 8.69 0.005 1 655 170 PHE C C 180.04 0.172 1 656 170 PHE CA C 54.99 0.500 1 657 170 PHE CB C 41.70 0.021 1 658 170 PHE N N 119.78 0.500 1 659 171 THR H H 8.69 0.001 1 660 171 THR C C 177.69 0.092 1 661 171 THR CA C 58.78 0.500 1 662 171 THR CB C 72.46 0.087 1 663 171 THR N N 110.58 0.500 1 664 172 VAL H H 8.73 0.001 1 665 172 VAL C C 177.46 0.081 1 666 172 VAL CA C 61.28 0.021 1 667 172 VAL CB C 35.83 0.021 1 668 172 VAL N N 118.70 0.500 1 669 173 ARG H H 9.11 0.100 1 670 173 ARG C C 176.84 0.149 1 671 173 ARG CA C 53.80 0.219 1 672 173 ARG CB C 33.69 0.500 1 673 173 ARG N N 124.90 0.500 1 674 174 THR H H 8.73 0.001 1 675 174 THR C C 177.74 0.058 1 676 174 THR CA C 63.56 0.087 1 677 174 THR CB C 68.77 0.500 1 678 174 THR N N 117.92 0.500 1 679 175 ASP H H 8.48 0.002 1 680 175 ASP C C 176.16 0.500 1 681 175 ASP CA C 54.44 0.500 1 682 175 ASP CB C 43.62 0.500 1 683 175 ASP N N 126.58 0.500 1 684 176 THR C C 177.36 0.500 1 685 176 THR CA C 60.88 0.500 1 686 176 THR CB C 68.46 0.500 1 687 177 GLY H H 7.69 0.001 1 688 177 GLY C C 179.35 0.111 1 689 177 GLY CA C 44.07 0.153 1 690 177 GLY N N 110.47 0.500 1 691 178 GLU H H 8.17 0.001 1 692 178 GLU C C 176.64 0.500 1 693 178 GLU CA C 54.63 0.500 1 694 178 GLU CB C 28.98 0.500 1 695 178 GLU N N 121.23 0.069 1 696 179 PRO C C 174.52 0.500 1 697 179 PRO CA C 63.12 0.500 1 698 179 PRO CB C 31.80 0.500 1 699 180 MET H H 9.29 0.001 1 700 180 MET C C 175.77 0.113 1 701 180 MET CA C 54.79 0.500 1 702 180 MET CB C 34.72 0.500 1 703 180 MET N N 124.31 0.500 1 704 181 GLY H H 8.46 0.017 1 705 181 GLY C C 178.48 0.500 1 706 181 GLY CA C 46.97 0.500 1 707 181 GLY N N 111.65 0.500 1 708 182 ARG H H 7.31 0.002 1 709 182 ARG C C 177.72 0.108 1 710 182 ARG CA C 56.90 0.087 1 711 182 ARG CB C 29.93 0.500 1 712 182 ARG N N 120.24 0.500 1 713 183 GLY H H 9.05 0.002 1 714 183 GLY C C 179.95 0.138 1 715 183 GLY CA C 43.91 0.500 1 716 183 GLY N N 115.74 0.500 1 717 184 THR H H 7.63 0.001 1 718 184 THR C C 181.33 0.500 1 719 184 THR CA C 62.11 0.087 1 720 184 THR CB C 72.33 0.087 1 722 185 LYS H H 9.91 0.002 1 723 185 LYS C C 178.83 0.133 1 724 185 LYS CA C 54.26 0.500 1 725 185 LYS CB C 35.14 0.087 1 726 185 LYS N N 128.48 0.500 1 727 186 VAL H H 9.07 0.001 1 728 186 VAL C C 177.94 0.083 1 729 186 VAL CA C 61.78 0.500 1 730 186 VAL CB C 32.70 0.500 1 731 186 VAL N N 126.76 0.500 1 732 187 ILE H H 9.86 0.100 1 733 187 ILE C C 177.38 0.500 1 734 187 ILE CA C 61.41 0.153 1 735 187 ILE CB C 39.03 0.500 1 736 187 ILE N N 128.09 0.500 1 737 188 LEU H H 8.76 0.100 1 738 188 LEU C C 177.05 0.500 1 739 188 LEU CA C 53.80 0.087 1 740 188 LEU CB C 41.63 0.021 1 741 188 LEU N N 126.03 0.500 1 742 189 HIS H H 8.20 0.001 1 743 189 HIS C C 176.85 0.011 1 744 189 HIS CA C 55.48 0.021 1 745 189 HIS CB C 28.05 0.021 1 746 189 HIS N N 125.43 0.500 1 747 190 LEU H H 7.88 0.100 1 748 190 LEU C C 174.45 0.074 1 749 190 LEU CA C 55.94 0.500 1 750 190 LEU CB C 41.30 0.021 1 751 190 LEU N N 123.83 0.500 1 752 191 LYS H H 8.32 0.100 1 753 191 LYS C C 174.05 0.094 1 754 191 LYS CA C 56.83 0.087 1 755 191 LYS CB C 33.59 0.021 1 756 191 LYS N N 120.72 0.500 1 757 192 GLU H H 8.89 0.004 1 758 192 GLU C C 176.02 0.170 1 759 192 GLU CA C 59.44 0.021 1 760 192 GLU CB C 29.40 0.500 1 761 192 GLU N N 120.83 0.500 1 762 193 ASP H H 8.25 0.004 1 763 193 ASP C C 174.92 0.138 1 764 193 ASP CA C 53.34 0.500 1 765 193 ASP CB C 39.32 0.500 1 766 193 ASP N N 113.48 0.500 1 767 194 GLN H H 7.75 0.003 1 768 194 GLN C C 176.36 0.082 1 769 194 GLN CA C 53.86 0.500 1 770 194 GLN CB C 27.32 0.021 1 771 194 GLN N N 118.85 0.500 1 772 195 THR H H 7.30 0.004 1 773 195 THR C C 174.94 0.108 1 774 195 THR CA C 64.15 0.500 1 775 195 THR CB C 68.24 0.087 1 776 195 THR N N 106.74 0.500 1 777 196 GLU H H 8.74 0.003 1 782 197 TYR H H 6.53 0.003 1 787 198 LEU H H 7.17 0.006 1 792 199 GLU H H 7.18 0.001 1 793 199 GLU C C 175.28 0.500 1 794 199 GLU CA C 54.83 0.500 1 797 200 GLU C C 174.91 0.500 1 798 200 GLU CA C 60.35 0.500 1 799 200 GLU CB C 29.36 0.500 1 800 201 ARG H H 8.76 0.001 1 801 201 ARG C C 173.96 0.062 1 802 201 ARG CA C 59.40 0.500 1 803 201 ARG CB C 29.17 0.021 1 805 202 ARG H H 6.64 0.001 1 806 202 ARG C C 174.22 0.095 1 807 202 ARG CA C 56.83 0.500 1 808 202 ARG CB C 29.96 0.021 1 809 202 ARG N N 119.65 0.500 1 810 203 ILE H H 7.99 0.003 1 811 203 ILE C C 174.28 0.035 1 812 203 ILE CA C 65.53 0.500 1 813 203 ILE CB C 37.61 0.021 1 814 203 ILE N N 117.94 0.500 1 815 204 LYS H H 8.31 0.100 1 816 204 LYS C C 172.90 0.094 1 817 204 LYS CA C 60.39 0.087 1 818 204 LYS CB C 31.84 0.500 1 819 204 LYS N N 116.98 0.500 1 820 205 GLU H H 7.58 0.100 1 821 205 GLU C C 173.33 0.131 1 822 205 GLU CA C 59.04 0.021 1 823 205 GLU CB C 28.87 0.500 1 824 205 GLU N N 118.81 0.500 1 825 206 ILE H H 7.75 0.002 1 826 206 ILE C C 173.74 0.129 1 827 206 ILE CA C 65.27 0.087 1 828 206 ILE CB C 37.91 0.219 1 829 206 ILE N N 121.35 0.500 1 830 207 VAL H H 8.26 0.002 1 831 207 VAL C C 173.85 0.129 1 832 207 VAL CA C 66.59 0.218 1 833 207 VAL CB C 31.38 0.500 1 834 207 VAL N N 120.91 0.500 1 835 208 LYS H H 7.79 0.002 1 840 209 LYS H H 7.38 0.002 1 845 210 HIS H H 7.71 0.004 1 850 211 SER H H 8.05 0.004 1 857 216 TYR H H 6.62 0.100 1 865 218 ILE H H 7.92 0.001 1 870 219 THR H H 8.58 0.004 1 875 220 LEU H H 8.53 0.001 1 880 221 PHE H H 8.67 0.001 1 885 222 VAL H H 7.89 0.002 1 890 223 GLU H H 7.93 0.001 1 stop_ save_