data_5355 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance assignments of the 25kD N-terminal ATPase domain from the Hsp90 chaperone ; _BMRB_accession_number 5355 _BMRB_flat_file_name bmr5355.str _Entry_type original _Submission_date 2002-04-27 _Accession_date 2002-04-29 _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 Williams Mark A. . 2 Salek Reza M. . 3 Ladbury John E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 370 "13C chemical shifts" 572 "15N chemical shifts" 192 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-09-25 original author . stop_ _Original_release_date 2002-09-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone resonance assignments of the 25kD N-terminal ATPase domain from the Hsp90 chaperone ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Salek Reza M. . 2 Williams Mark A. . 3 Prodromou Christosmos . . 4 Pearl Laurence H. . 5 Ladbury John E. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 23 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 327 _Page_last 328 _Year 2002 _Details . loop_ _Keyword Hsp90 'heat shock protein' 'Saccharomyces Cerevisiae' 'heteronuclear NMR' 'resonance assignments' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Pearl LH, Prodromou C. Structure, function, and mechanism of the Hsp90 molecular chaperone. Adv Protein Chem. 2001;59:157-86. ; _Citation_title 'Structure, function, and mechanism of the Hsp90 molecular chaperone.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11868271 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pearl 'L H' H. . 2 Prodromou C . . stop_ _Journal_abbreviation 'Adv. Protein Chem.' _Journal_name_full 'Advances in protein chemistry' _Journal_volume 59 _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 157 _Page_last 186 _Year 2001 _Details . save_ save_ref_2 _Saveframe_category citation _Citation_full ; Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell. 1997 Jul 11;90(1):65-75. ; _Citation_title 'Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9230303 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Prodromou C . . 2 Roe 'S M' M. . 3 O'Brien R . . 4 Ladbury 'J E' E. . 5 Piper 'P W' W. . 6 Pearl 'L H' H. . stop_ _Journal_abbreviation Cell _Journal_name_full Cell _Journal_volume 90 _Journal_issue 1 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 65 _Page_last 75 _Year 1997 _Details ; Hsp90 molecular chaperones in eukaryotic cells play essential roles in the folding and activation of a range of client proteins involved in cell cycle regulation, steroid hormone responsiveness, and signal transduction. The biochemical mechanism of Hsp90 is poorly understood, and the involvement of ATP in particular is controversial. Crystal structures of complexes between the N-terminal domain of the yeast Hsp90 chaperone and ADP/ATP unambiguously identify a specific adenine nucleotide binding site homologous to the ATP-binding site of DNA gyrase B. This site is the same as that identified for the antitumor agent geldanamycin, suggesting that geldanamycin acts by blocking the binding of nucleotides to Hsp90 and not the binding of incompletely folded client polypeptides as previously suggested. These results finally resolve the question of the direct involvement of ATP in Hsp90 function. ; save_ ################################## # Molecular system description # ################################## save_system_Hsp90 _Saveframe_category molecular_system _Mol_system_name 'Hsp90 N-terminal ATPase domain' _Abbreviation_common Hsp90 _Enzyme_commission_number 3.4.6.10 loop_ _Mol_system_component_name _Mol_label 'Hsp90 N-terminal ATPase domain' $Hsp90 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'molecular chaperone' 'heat shock protein' ATPase stop_ _Database_query_date . _Details ; The system reported consists of residues 1 to 207 of the sequence entry, plus an N-terminal hexahistidine-tag (MRGSHHHHHHG). ; save_ ######################## # Monomeric polymers # ######################## save_Hsp90 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Heat shock protein 90 N-terminal domain' _Abbreviation_common 'Hsp90 ATPase' _Molecular_mass 24709 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 218 _Mol_residue_sequence ; MRGSHHHHHHGMASETFEFQ AEITQLMSLIINTVYSNKEI FLRELISNASDALDKIRYKS LSDPKQLETEPDLFIRITPK PEQKVLEIRDSGIGMTKAEL INNLGTIAKSGTKAFMEALS AGADVSMIGQFGVGFYSLFL VADRVQVISKSNDDEQYIWE SNAGGSFTVTLDEVNERIGR GTILRLFLKDDQLEYLEEKR IKEVIKRHSEFVAYPIQL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -10 MET 2 -9 ARG 3 -8 GLY 4 -7 SER 5 -6 HIS 6 -5 HIS 7 -4 HIS 8 -3 HIS 9 -2 HIS 10 -1 HIS 11 0 GLY 12 1 MET 13 2 ALA 14 3 SER 15 4 GLU 16 5 THR 17 6 PHE 18 7 GLU 19 8 PHE 20 9 GLN 21 10 ALA 22 11 GLU 23 12 ILE 24 13 THR 25 14 GLN 26 15 LEU 27 16 MET 28 17 SER 29 18 LEU 30 19 ILE 31 20 ILE 32 21 ASN 33 22 THR 34 23 VAL 35 24 TYR 36 25 SER 37 26 ASN 38 27 LYS 39 28 GLU 40 29 ILE 41 30 PHE 42 31 LEU 43 32 ARG 44 33 GLU 45 34 LEU 46 35 ILE 47 36 SER 48 37 ASN 49 38 ALA 50 39 SER 51 40 ASP 52 41 ALA 53 42 LEU 54 43 ASP 55 44 LYS 56 45 ILE 57 46 ARG 58 47 TYR 59 48 LYS 60 49 SER 61 50 LEU 62 51 SER 63 52 ASP 64 53 PRO 65 54 LYS 66 55 GLN 67 56 LEU 68 57 GLU 69 58 THR 70 59 GLU 71 60 PRO 72 61 ASP 73 62 LEU 74 63 PHE 75 64 ILE 76 65 ARG 77 66 ILE 78 67 THR 79 68 PRO 80 69 LYS 81 70 PRO 82 71 GLU 83 72 GLN 84 73 LYS 85 74 VAL 86 75 LEU 87 76 GLU 88 77 ILE 89 78 ARG 90 79 ASP 91 80 SER 92 81 GLY 93 82 ILE 94 83 GLY 95 84 MET 96 85 THR 97 86 LYS 98 87 ALA 99 88 GLU 100 89 LEU 101 90 ILE 102 91 ASN 103 92 ASN 104 93 LEU 105 94 GLY 106 95 THR 107 96 ILE 108 97 ALA 109 98 LYS 110 99 SER 111 100 GLY 112 101 THR 113 102 LYS 114 103 ALA 115 104 PHE 116 105 MET 117 106 GLU 118 107 ALA 119 108 LEU 120 109 SER 121 110 ALA 122 111 GLY 123 112 ALA 124 113 ASP 125 114 VAL 126 115 SER 127 116 MET 128 117 ILE 129 118 GLY 130 119 GLN 131 120 PHE 132 121 GLY 133 122 VAL 134 123 GLY 135 124 PHE 136 125 TYR 137 126 SER 138 127 LEU 139 128 PHE 140 129 LEU 141 130 VAL 142 131 ALA 143 132 ASP 144 133 ARG 145 134 VAL 146 135 GLN 147 136 VAL 148 137 ILE 149 138 SER 150 139 LYS 151 140 SER 152 141 ASN 153 142 ASP 154 143 ASP 155 144 GLU 156 145 GLN 157 146 TYR 158 147 ILE 159 148 TRP 160 149 GLU 161 150 SER 162 151 ASN 163 152 ALA 164 153 GLY 165 154 GLY 166 155 SER 167 156 PHE 168 157 THR 169 158 VAL 170 159 THR 171 160 LEU 172 161 ASP 173 162 GLU 174 163 VAL 175 164 ASN 176 165 GLU 177 166 ARG 178 167 ILE 179 168 GLY 180 169 ARG 181 170 GLY 182 171 THR 183 172 ILE 184 173 LEU 185 174 ARG 186 175 LEU 187 176 PHE 188 177 LEU 189 178 LYS 190 179 ASP 191 180 ASP 192 181 GLN 193 182 LEU 194 183 GLU 195 184 TYR 196 185 LEU 197 186 GLU 198 187 GLU 199 188 LYS 200 189 ARG 201 190 ILE 202 191 LYS 203 192 GLU 204 193 VAL 205 194 ILE 206 195 LYS 207 196 ARG 208 197 HIS 209 198 SER 210 199 GLU 211 200 PHE 212 201 VAL 213 202 ALA 214 203 TYR 215 204 PRO 216 205 ILE 217 206 GLN 218 207 LEU 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 PDB 1A4H "Structure Of The N-Terminal Domain Of The Yeast Hsp90 Chaperone In Complex With Geldanamycin" 100.00 230 99.54 99.54 8.49e-155 PDB 1AH6 "Structure Of The Tetragonal Form Of The N-Terminal Domain Of The Yeast Hsp90 Chaperone" 94.95 220 100.00 100.00 7.96e-147 PDB 1AH8 "Structure Of The Orthorhombic Form Of The N-Terminal Domain Of The Yeast Hsp90 Chaperone" 94.95 220 100.00 100.00 7.96e-147 PDB 1AM1 "Atp Binding Site In The Hsp90 Molecular Chaperone" 94.50 213 100.00 100.00 4.16e-146 PDB 1AMW "Adp Binding Site In The Hsp90 Molecular Chaperone" 94.95 214 100.00 100.00 3.64e-147 PDB 1BGQ "Radicicol Bound To The Atp Binding Site Of The N-Terminal Domain Of The Yeast Hsp90 Chaperone" 100.00 225 100.00 100.00 1.00e-157 PDB 1US7 "Complex Of Hsp90 And P50" 94.95 214 100.00 100.00 3.64e-147 PDB 2AKP "Hsp90 Delta24-n210 Mutant" 83.94 186 100.00 100.00 1.83e-128 PDB 2BRC "Structure Of A Hsp90 Inhibitor Bound To The N-Terminus Of Yeast Hsp90." 94.95 214 100.00 100.00 3.64e-147 PDB 2BRE "Structure Of A Hsp90 Inhibitor Bound To The N-Terminus Of Yeast Hsp90." 94.95 219 100.00 100.00 4.85e-147 PDB 2CG9 "Crystal Structure Of An Hsp90-Sba1 Closed Chaperone Complex" 94.95 677 100.00 100.00 1.95e-141 PDB 2CGF "A Radicicol Analogue Bound To The Atp Binding Site Of The N- Terminal Domain Of The Yeast Hsp90 Chaperone" 100.00 225 99.54 100.00 3.45e-157 PDB 2IWS "Radicicol Analogues Bound To The Atp Site Of Hsp90" 94.95 214 100.00 100.00 3.64e-147 PDB 2IWU "Analogues Of Radicicol Bound To The Atp-Binding Site Of Hsp90" 94.95 214 100.00 100.00 3.64e-147 PDB 2IWX "Analogues Of Radicicol Bound To The Atp-Binding Site Of Hsp90." 94.95 214 100.00 100.00 3.64e-147 PDB 2VW5 "Structure Of The Hsp90 Inhibitor 7-O-Carbamoylpremacbecin Bound To The N- Terminus Of Yeast Hsp90" 94.95 214 100.00 100.00 3.64e-147 PDB 2VWC "Structure Of The Hsp90 Inhibitor Macbecin Bound To The N- Terminus Of Yeast Hsp90" 94.95 219 100.00 100.00 4.85e-147 PDB 2WEP "Yeast Hsp90 N-Terminal Domain Li-Iv Mutant With Adp" 94.95 220 99.03 100.00 2.43e-146 PDB 2WEQ "Yeast Hsp90 N-Terminal Domain Li-Iv Mutant With Geldanamycin" 94.95 220 99.03 100.00 2.43e-146 PDB 2WER "Yeast Hsp90 N-Terminal Domain Li-Iv Mutant With Radicicol" 94.95 220 99.03 100.00 2.43e-146 PDB 2XD6 "Hsp90 Complexed With A Resorcylic Acid Macrolactone." 94.95 214 100.00 100.00 3.64e-147 PDB 2XX2 "Macrolactone Inhibitor Bound To Hsp90 N-Term" 94.50 214 100.00 100.00 4.31e-146 PDB 2XX4 "Macrolactone Inhibitor Bound To Hsp90 N-Term" 94.95 214 100.00 100.00 3.64e-147 PDB 2XX5 "Macrolactone Inhibitor Bound To Hsp90 N-Term" 94.95 214 100.00 100.00 3.64e-147 PDB 2YGA "E88g-n92l Mutant Of N-term Hsp90 Complexed With Geldanamycin" 94.50 220 99.03 99.03 3.16e-143 PDB 2YGE "E88g-n92l Mutant Of N-term Hsp90 Complexed With Geldanamycin" 94.50 220 99.03 99.51 9.78e-145 PDB 2YGF "L89v, L93i And V136m Mutant Of N-term Hsp90 Complexed With Geldanamycin" 94.95 220 98.55 100.00 2.12e-145 PDB 4AS9 "The Structure Of Modified Benzoquinone Ansamycins Bound To Yeast N-terminal Hsp90" 94.95 220 100.00 100.00 7.96e-147 PDB 4ASA "The Structure Of Modified Benzoquinone Ansamycins Bound To Yeast N-terminal Hsp90" 94.95 220 100.00 100.00 7.96e-147 PDB 4ASB "The Structure Of Modified Benzoquinone Ansamycins Bound To Yeast N-terminal Hsp90" 94.95 220 100.00 100.00 7.96e-147 PDB 4ASF "The Structure Of Modified Benzoquinone Ansamycins Bound To Yeast N-terminal Hsp90" 94.95 220 100.00 100.00 7.96e-147 PDB 4ASG "The Structure Of Modified Benzoquinone Ansamycins Bound To Yeast N-terminal Hsp90" 94.95 220 100.00 100.00 7.96e-147 PDB 4CE1 "Hsp90 N-terminal Domain Bound To Macrolactam Analogues Of Radicicol." 94.95 214 100.00 100.00 3.64e-147 PDB 4CE2 "Hsp90 N-terminal Domain Bound To Macrolactam Analogues Of Radicicol." 94.95 214 100.00 100.00 3.64e-147 PDB 4CE3 "Hsp90 N-terminal Domain Bound To Macrolactam Analogues Of Radicicol" 94.95 214 100.00 100.00 3.64e-147 DBJ GAA26739 "K7_Hsp82p [Saccharomyces cerevisiae Kyokai no. 7]" 94.95 709 100.00 100.00 3.44e-141 EMBL CAA91604 "HSP90/HSP82? [Saccharomyces cerevisiae]" 94.95 709 100.00 100.00 3.83e-141 EMBL CAA97961 "HSP82 [Saccharomyces cerevisiae]" 94.95 709 100.00 100.00 3.83e-141 EMBL CAY86720 "Hsp82p [Saccharomyces cerevisiae EC1118]" 94.95 709 99.52 100.00 1.21e-140 GB AAA02743 "hsp82 protein [Saccharomyces cerevisiae]" 94.95 709 100.00 100.00 3.83e-141 GB AHY77944 "Hsp82p [Saccharomyces cerevisiae YJM993]" 94.95 705 98.55 100.00 8.44e-140 GB EDN60908 "heat shock protein 90 [Saccharomyces cerevisiae YJM789]" 94.95 709 100.00 100.00 3.83e-141 GB EDV10990 "heat shock protein 90 [Saccharomyces cerevisiae RM11-1a]" 94.95 709 100.00 100.00 3.83e-141 GB EDZ70041 "YMR186Wp-like protein [Saccharomyces cerevisiae AWRI1631]" 56.88 622 97.58 100.00 1.61e-76 REF NP_015084 "Hsp90 family chaperone HSP82 [Saccharomyces cerevisiae S288c]" 94.95 709 100.00 100.00 3.83e-141 SP P02829 "RecName: Full=ATP-dependent molecular chaperone HSP82; AltName: Full=82 kDa heat shock protein; AltName: Full=Heat shock protei" 94.95 709 100.00 100.00 3.83e-141 TPG DAA11197 "TPA: Hsp90 family chaperone HSP82 [Saccharomyces cerevisiae S288c]" 94.95 709 100.00 100.00 3.83e-141 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $Hsp90 'Baker's yeast' 4932 Eukaryota Fungi Saccharomyces cerevisiae S288c stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $Hsp90 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3)pLysS plasmid PET stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Hsp90 0.5 mM '[U-98% 13C; U-98% 15N; U-70% 2H]' Tris 20 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Hsp90 0.5 mM '[U-98% 15N]' Tris 20.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_NmrPipe _Saveframe_category software _Name NmrPipe _Version 2.1 loop_ _Task 'spectral processing' stop_ _Details ; Delaglio, F., Grzesiek, S., Vuister, G.W., Pfeifer, J. and Bax, A. J. Biomol. NMR 6, 277-293 (1995)." ; save_ save_type_prob-seq_prob _Saveframe_category software _Name type_prob-seq_prob _Version 1.0 loop_ _Task 'amino acid type determination' 'sequential assignment' stop_ _Details ; Grzesiek, S. and Bax, A. J Biomol. NMR 3, 185-204 (1993). ; save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version 3.3 loop_ _Task 'spectral visualization' analysis stop_ _Details ; Kraulis, P.J., Domaille, P.J., Campbell-Burke, S.L., van Aken, T. and Laue, E.D. Biochemistry 33, 3515-3531 (1994)." ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _Sample_label . save_ save_1H-15N_NOESY-HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _Sample_label . save_ save_1H-15N_TOCSY-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY-HSQC' _Sample_label . save_ save_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CA)CB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CB _Sample_label . save_ save_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HN(COCA)CB_8 _Saveframe_category NMR_applied_experiment _Experiment_name HN(COCA)CB _Sample_label . save_ save_HNCO_9 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HN(CA)CO_10 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HN(COCA)CB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 8.0 0.1 na temperature 298 0.2 K 'ionic strength' 0.0435 0.001 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details ; Conformational and solvent exchange has resulted in a number of missing peaks in the 3D spectra and consequently there are no assignements for residues 9-11, 23-25 and 97-100. ; loop_ _Experiment_label '1H-15N HSQC' '1H-13C HSQC' '1H-15N NOESY-HSQC' '1H-15N TOCSY-HSQC' HNCA HN(CA)CB HN(CO)CA HN(COCA)CB HNCO HN(CA)CO stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Hsp90 N-terminal ATPase 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 . 10 HIS CA C 56.296 0.400 1 2 . 10 HIS C C 176.606 0.400 1 3 . 10 HIS CB C 30.160 0.400 1 4 . 11 GLY N N 109.984 0.100 1 5 . 11 GLY H H 8.384 0.020 1 6 . 11 GLY CA C 45.012 0.400 1 7 . 11 GLY C C 174.790 0.400 1 8 . 11 GLY HA2 H 3.928 0.020 2 9 . 12 MET N N 119.986 0.100 1 10 . 12 MET H H 8.313 0.020 1 11 . 12 MET CA C 55.093 0.400 1 12 . 12 MET HA H 4.505 0.020 1 13 . 12 MET C C 176.776 0.400 1 14 . 12 MET CB C 32.271 0.400 1 15 . 12 MET HB2 H 2.004 0.020 2 16 . 12 MET HB3 H 2.092 0.020 2 17 . 13 ALA N N 125.437 0.100 1 18 . 13 ALA H H 8.500 0.020 1 19 . 13 ALA CA C 52.323 0.400 1 20 . 13 ALA HA H 4.409 0.020 1 21 . 13 ALA C C 178.014 0.400 1 22 . 13 ALA CB C 18.425 0.400 1 23 . 13 ALA HB H 1.442 0.020 1 24 . 14 SER N N 114.844 0.100 1 25 . 14 SER H H 8.062 0.020 1 26 . 14 SER CA C 57.780 0.400 1 27 . 14 SER HA H 4.914 0.020 1 28 . 14 SER C C 174.360 0.400 1 29 . 14 SER CB C 64.462 0.400 1 30 . 14 SER HB2 H 3.674 0.020 1 31 . 15 GLU N N 123.898 0.100 1 32 . 15 GLU H H 8.432 0.020 1 33 . 15 GLU CA C 55.416 0.400 1 34 . 15 GLU HA H 4.452 0.020 1 35 . 15 GLU C C 174.974 0.400 1 36 . 15 GLU CB C 33.551 0.400 1 37 . 16 THR N N 118.315 0.100 1 38 . 16 THR H H 8.044 0.020 1 39 . 16 THR CA C 61.399 0.400 1 40 . 16 THR C C 173.220 0.400 1 41 . 16 THR CB C 69.574 0.400 1 42 . 17 PHE N N 124.748 0.100 1 43 . 17 PHE H H 8.575 0.020 1 44 . 17 PHE HA H 4.315 0.020 1 45 . 17 PHE C C 174.391 0.400 1 46 . 17 PHE CB C 42.435 0.400 1 47 . 17 PHE HD1 H 6.815 0.020 1 48 . 18 GLU N N 118.626 0.100 1 49 . 18 GLU H H 8.344 0.020 1 50 . 18 GLU CA C 55.180 0.400 1 51 . 18 GLU HA H 4.611 0.020 1 52 . 18 GLU C C 178.688 0.400 1 53 . 18 GLU CB C 30.459 0.400 1 54 . 19 PHE N N 120.471 0.100 1 55 . 19 PHE H H 8.097 0.020 1 56 . 19 PHE CA C 59.354 0.400 1 57 . 19 PHE C C 177.237 0.400 1 58 . 19 PHE CB C 40.429 0.400 1 59 . 22 GLU CA C 60.050 0.400 1 60 . 22 GLU C C 179.191 0.400 1 61 . 22 GLU CB C 28.971 0.400 1 62 . 23 ILE N N 118.642 0.100 1 63 . 23 ILE H H 7.502 0.020 1 64 . 23 ILE CA C 63.761 0.400 1 65 . 23 ILE C C 178.471 0.400 1 66 . 23 ILE CB C 37.535 0.400 1 67 . 24 THR N N 117.320 0.100 1 68 . 24 THR H H 7.635 0.020 1 69 . 24 THR CA C 66.380 0.400 1 70 . 24 THR C C 177.885 0.400 1 71 . 24 THR CB C 67.481 0.400 1 72 . 25 GLN N N 120.733 0.100 1 73 . 25 GLN H H 7.899 0.020 1 74 . 25 GLN CA C 58.526 0.400 1 75 . 25 GLN HA H 3.952 0.020 1 76 . 25 GLN C C 179.086 0.400 1 77 . 25 GLN CB C 27.391 0.400 1 78 . 26 LEU N N 122.424 0.100 1 79 . 26 LEU H H 7.948 0.020 1 80 . 26 LEU CA C 58.019 0.400 1 81 . 26 LEU C C 178.917 0.400 1 82 . 26 LEU CB C 39.966 0.400 1 83 . 27 MET N N 117.255 0.100 1 84 . 27 MET H H 8.487 0.020 1 85 . 27 MET CA C 60.469 0.400 1 86 . 27 MET CB C 32.275 0.400 1 87 . 28 SER N N 111.934 0.100 1 88 . 28 SER H H 7.785 0.020 1 89 . 28 SER CA C 61.267 0.400 1 90 . 28 SER HA H 4.059 0.020 1 91 . 28 SER C C 177.144 0.400 1 92 . 28 SER CB C 62.443 0.400 1 93 . 28 SER HB2 H 3.899 0.020 1 94 . 29 LEU N N 121.563 0.100 1 95 . 29 LEU H H 7.756 0.020 1 96 . 29 LEU CA C 57.730 0.400 1 97 . 29 LEU HA H 4.088 0.020 1 98 . 29 LEU C C 181.015 0.400 1 99 . 29 LEU CB C 41.162 0.400 1 100 . 30 ILE N N 119.684 0.100 1 101 . 30 ILE H H 8.338 0.020 1 102 . 30 ILE CA C 64.006 0.400 1 103 . 30 ILE HA H 3.588 0.020 1 104 . 30 ILE C C 178.327 0.400 1 105 . 30 ILE CB C 36.626 0.400 1 106 . 31 ILE N N 118.359 0.100 1 107 . 31 ILE H H 8.460 0.020 1 108 . 31 ILE CA C 64.244 0.400 1 109 . 31 ILE HA H 3.928 0.020 1 110 . 31 ILE C C 177.746 0.400 1 111 . 31 ILE CB C 37.446 0.400 1 112 . 32 ASN N N 114.259 0.100 1 113 . 32 ASN H H 7.363 0.020 1 114 . 32 ASN CA C 53.740 0.400 1 115 . 32 ASN C C 176.193 0.400 1 116 . 32 ASN CB C 40.170 0.400 1 117 . 33 THR N N 116.461 0.100 1 118 . 33 THR H H 7.465 0.020 1 119 . 33 THR HA H 4.309 0.020 1 120 . 33 THR HG2 H 1.182 0.020 1 121 . 37 ASN CA C 51.751 0.400 1 122 . 37 ASN C C 175.601 0.400 1 123 . 37 ASN CB C 37.377 0.400 1 124 . 38 LYS N N 117.590 0.100 1 125 . 38 LYS H H 8.194 0.020 1 126 . 38 LYS CA C 59.302 0.400 1 127 . 38 LYS C C 177.290 0.400 1 128 . 38 LYS CB C 31.629 0.400 1 129 . 39 GLU N N 115.241 0.100 1 130 . 39 GLU H H 8.517 0.020 1 131 . 39 GLU CA C 57.999 0.400 1 132 . 39 GLU HA H 4.070 0.020 1 133 . 39 GLU C C 176.478 0.400 1 134 . 39 GLU CB C 28.087 0.400 1 135 . 40 ILE N N 113.243 0.100 1 136 . 40 ILE H H 7.066 0.020 1 137 . 40 ILE CA C 62.405 0.400 1 138 . 40 ILE HA H 3.541 0.020 1 139 . 40 ILE C C 177.389 0.400 1 140 . 40 ILE CB C 37.429 0.400 1 141 . 41 PHE N N 120.920 0.100 1 142 . 41 PHE H H 8.137 0.020 1 143 . 41 PHE CA C 59.234 0.400 1 144 . 41 PHE C C 176.598 0.400 1 145 . 41 PHE CB C 37.031 0.400 1 146 . 42 LEU N N 123.030 0.100 1 147 . 42 LEU H H 5.969 0.020 1 148 . 42 LEU CA C 56.574 0.400 1 149 . 42 LEU HA H 3.059 0.020 1 150 . 42 LEU C C 178.804 0.400 1 151 . 42 LEU CB C 39.891 0.400 1 152 . 43 ARG N N 117.799 0.100 1 153 . 43 ARG H H 6.495 0.020 1 154 . 43 ARG CA C 58.375 0.400 1 155 . 43 ARG HA H 3.595 0.020 1 156 . 43 ARG C C 179.785 0.400 1 157 . 43 ARG CB C 28.578 0.400 1 158 . 44 GLU N N 116.558 0.100 1 159 . 44 GLU H H 7.612 0.020 1 160 . 44 GLU CA C 57.604 0.400 1 161 . 44 GLU HA H 3.980 0.020 1 162 . 44 GLU C C 180.047 0.400 1 163 . 44 GLU CB C 27.806 0.400 1 164 . 45 LEU N N 118.559 0.100 1 165 . 45 LEU H H 8.034 0.020 1 166 . 45 LEU CA C 57.319 0.400 1 167 . 45 LEU HA H 4.085 0.020 1 168 . 45 LEU C C 181.613 0.400 1 169 . 45 LEU CB C 39.259 0.400 1 170 . 46 ILE N N 122.686 0.100 1 171 . 46 ILE H H 8.442 0.020 1 172 . 46 ILE CA C 65.163 0.400 1 173 . 46 ILE HA H 3.631 0.020 1 174 . 46 ILE C C 178.290 0.400 1 175 . 46 ILE CB C 35.749 0.400 1 176 . 47 SER N N 117.519 0.100 1 177 . 47 SER H H 8.208 0.020 1 178 . 47 SER CA C 61.790 0.400 1 179 . 47 SER HA H 4.219 0.020 1 180 . 47 SER C C 177.581 0.400 1 181 . 47 SER CB C 62.226 0.400 1 182 . 48 ASN N N 119.344 0.100 1 183 . 48 ASN H H 7.940 0.020 1 184 . 48 ASN CA C 55.667 0.400 1 185 . 48 ASN HA H 4.342 0.020 1 186 . 48 ASN C C 178.562 0.400 1 187 . 48 ASN CB C 37.612 0.400 1 188 . 49 ALA N N 124.515 0.100 1 189 . 49 ALA H H 7.802 0.020 1 190 . 49 ALA CA C 54.561 0.400 1 191 . 49 ALA HA H 4.096 0.020 1 192 . 49 ALA C C 179.151 0.400 1 193 . 49 ALA CB C 17.676 0.400 1 194 . 49 ALA HB H 1.468 0.020 1 195 . 50 SER N N 112.366 0.100 1 196 . 50 SER H H 8.556 0.020 1 197 . 50 SER CA C 61.478 0.400 1 198 . 50 SER C C 177.251 0.400 1 199 . 50 SER CB C 62.795 0.400 1 200 . 51 ASP N N 119.564 0.100 1 201 . 51 ASP H H 8.169 0.020 1 202 . 51 ASP CA C 57.280 0.400 1 203 . 51 ASP HA H 4.364 0.020 1 204 . 51 ASP C C 178.894 0.400 1 205 . 51 ASP CB C 40.152 0.400 1 206 . 52 ALA N N 122.528 0.100 1 207 . 52 ALA H H 7.758 0.020 1 208 . 52 ALA CA C 54.976 0.400 1 209 . 52 ALA HA H 4.114 0.020 1 210 . 52 ALA C C 182.523 0.400 1 211 . 52 ALA CB C 18.067 0.400 1 212 . 52 ALA HB H 1.607 0.020 1 213 . 53 LEU N N 124.246 0.100 1 214 . 53 LEU H H 8.277 0.020 1 215 . 53 LEU CA C 57.529 0.400 1 216 . 53 LEU HA H 3.832 0.020 1 217 . 53 LEU C C 178.740 0.400 1 218 . 53 LEU CB C 40.040 0.400 1 219 . 54 ASP N N 120.539 0.100 1 220 . 54 ASP H H 8.867 0.020 1 221 . 54 ASP CA C 57.118 0.400 1 222 . 54 ASP C C 179.884 0.400 1 223 . 54 ASP CB C 39.195 0.400 1 224 . 55 LYS N N 116.961 0.100 1 225 . 55 LYS H H 7.950 0.020 1 226 . 55 LYS CA C 59.977 0.400 1 227 . 55 LYS HA H 4.121 0.020 1 228 . 55 LYS C C 181.113 0.400 1 229 . 55 LYS CB C 32.404 0.400 1 230 . 56 ILE N N 118.265 0.100 1 231 . 56 ILE H H 7.512 0.020 1 232 . 56 ILE CA C 59.651 0.400 1 233 . 56 ILE HA H 4.492 0.020 1 234 . 56 ILE C C 176.906 0.400 1 235 . 56 ILE CB C 37.615 0.400 1 236 . 57 ARG N N 127.786 0.100 1 237 . 57 ARG H H 8.645 0.020 1 238 . 57 ARG CA C 59.825 0.400 1 239 . 57 ARG HA H 3.871 0.020 1 240 . 57 ARG C C 180.317 0.400 1 241 . 57 ARG CB C 29.216 0.400 1 242 . 58 TYR N N 118.168 0.100 1 243 . 58 TYR H H 8.621 0.020 1 244 . 58 TYR CA C 60.891 0.400 1 245 . 58 TYR HA H 4.311 0.020 1 246 . 58 TYR C C 180.131 0.400 1 247 . 58 TYR CB C 37.132 0.400 1 248 . 59 LYS N N 120.258 0.100 1 249 . 59 LYS H H 7.896 0.020 1 250 . 59 LYS CA C 59.035 0.400 1 251 . 59 LYS HA H 4.026 0.020 1 252 . 59 LYS C C 179.587 0.400 1 253 . 59 LYS CB C 32.326 0.400 1 254 . 60 SER N N 113.184 0.100 1 255 . 60 SER H H 8.223 0.020 1 256 . 60 SER CA C 60.018 0.400 1 257 . 60 SER HA H 4.310 0.020 1 258 . 60 SER C C 175.571 0.400 1 259 . 60 SER CB C 63.067 0.400 1 260 . 61 LEU N N 121.838 0.100 1 261 . 61 LEU H H 7.359 0.020 1 262 . 61 LEU CA C 57.130 0.400 1 263 . 61 LEU HA H 4.117 0.020 1 264 . 61 LEU C C 179.540 0.400 1 265 . 61 LEU CB C 40.260 0.400 1 266 . 62 SER N N 109.618 0.100 1 267 . 62 SER H H 7.169 0.020 1 268 . 62 SER CA C 58.237 0.400 1 269 . 62 SER HA H 4.595 0.020 1 270 . 62 SER C C 175.008 0.400 1 271 . 62 SER CB C 63.598 0.400 1 272 . 63 ASP N N 118.301 0.100 1 273 . 63 ASP H H 7.433 0.020 1 274 . 63 ASP CA C 51.416 0.400 1 275 . 63 ASP HA H 5.058 0.020 1 276 . 63 ASP C C 174.050 0.400 1 277 . 64 PRO CA C 64.725 0.400 1 278 . 64 PRO C C 179.962 0.400 1 279 . 64 PRO CB C 31.225 0.400 1 280 . 65 LYS N N 118.148 0.100 1 281 . 65 LYS H H 8.046 0.020 1 282 . 65 LYS CA C 58.285 0.400 1 283 . 65 LYS HA H 4.069 0.020 1 284 . 65 LYS C C 180.131 0.400 1 285 . 65 LYS CB C 30.568 0.400 1 286 . 66 GLN N N 116.267 0.100 1 287 . 66 GLN H H 7.963 0.020 1 288 . 66 GLN CA C 56.860 0.400 1 289 . 66 GLN HA H 3.754 0.020 1 290 . 66 GLN C C 177.675 0.400 1 291 . 66 GLN CB C 26.865 0.400 1 292 . 67 LEU N N 113.322 0.100 1 293 . 67 LEU H H 7.221 0.020 1 294 . 67 LEU CA C 54.727 0.400 1 295 . 67 LEU HA H 4.219 0.020 1 296 . 67 LEU C C 179.756 0.400 1 297 . 67 LEU CB C 41.846 0.400 1 298 . 68 GLU N N 116.570 0.100 1 299 . 68 GLU H H 7.449 0.020 1 300 . 68 GLU CA C 59.015 0.400 1 301 . 68 GLU HA H 3.845 0.020 1 302 . 68 GLU C C 177.623 0.400 1 303 . 68 GLU CB C 28.973 0.400 1 304 . 69 THR N N 105.443 0.100 1 305 . 69 THR H H 7.036 0.020 1 306 . 69 THR CA C 62.097 0.400 1 307 . 69 THR HA H 3.910 0.020 1 308 . 69 THR C C 176.356 0.400 1 309 . 69 THR CB C 68.449 0.400 1 310 . 70 GLU N N 114.736 0.100 1 311 . 70 GLU H H 7.204 0.020 1 312 . 70 GLU CA C 55.022 0.400 1 313 . 70 GLU HA H 4.570 0.020 1 314 . 70 GLU C C 173.041 0.400 1 315 . 70 GLU CB C 28.921 0.400 1 316 . 71 PRO CA C 64.482 0.400 1 317 . 71 PRO C C 176.808 0.400 1 318 . 71 PRO CB C 31.796 0.400 1 319 . 72 ASP N N 117.416 0.100 1 320 . 72 ASP H H 8.603 0.020 1 321 . 72 ASP CA C 53.502 0.400 1 322 . 72 ASP HA H 4.895 0.020 1 323 . 72 ASP C C 176.104 0.400 1 324 . 72 ASP CB C 41.838 0.400 1 325 . 72 ASP HB2 H 2.752 0.020 1 326 . 73 LEU N N 122.899 0.100 1 327 . 73 LEU H H 8.321 0.020 1 328 . 73 LEU CA C 53.491 0.400 1 329 . 73 LEU HA H 4.216 0.020 1 330 . 73 LEU C C 175.217 0.400 1 331 . 73 LEU CB C 39.838 0.400 1 332 . 74 PHE N N 119.987 0.100 1 333 . 74 PHE H H 7.613 0.020 1 334 . 74 PHE CA C 56.126 0.400 1 335 . 74 PHE HA H 4.953 0.020 1 336 . 74 PHE C C 172.255 0.400 1 337 . 74 PHE CB C 41.373 0.400 1 338 . 75 ILE N N 118.577 0.100 1 339 . 75 ILE H H 8.186 0.020 1 340 . 75 ILE CA C 59.973 0.400 1 341 . 75 ILE HA H 4.922 0.020 1 342 . 75 ILE C C 175.040 0.400 1 343 . 75 ILE CB C 39.408 0.400 1 344 . 76 ARG N N 128.655 0.100 1 345 . 76 ARG H H 10.055 0.020 1 346 . 76 ARG CA C 54.324 0.400 1 347 . 76 ARG HA H 5.560 0.020 1 348 . 76 ARG C C 175.719 0.400 1 349 . 76 ARG CB C 33.817 0.400 1 350 . 77 ILE N N 130.252 0.100 1 351 . 77 ILE H H 9.075 0.020 1 352 . 77 ILE CA C 60.129 0.400 1 353 . 77 ILE HA H 5.047 0.020 1 354 . 77 ILE C C 175.176 0.400 1 355 . 77 ILE CB C 38.528 0.400 1 356 . 78 THR N N 122.003 0.100 1 357 . 78 THR H H 9.264 0.020 1 358 . 78 THR CA C 59.104 0.400 1 359 . 78 THR HA H 4.858 0.020 1 360 . 78 THR C C 173.321 0.400 1 361 . 78 THR CB C 70.771 0.400 1 362 . 79 PRO CA C 62.011 0.400 1 363 . 79 PRO C C 176.878 0.400 1 364 . 79 PRO CB C 32.815 0.400 1 365 . 80 LYS N N 122.160 0.100 1 366 . 80 LYS H H 9.124 0.020 1 367 . 80 LYS CA C 53.019 0.400 1 368 . 80 LYS HA H 4.983 0.020 1 369 . 80 LYS C C 176.265 0.400 1 370 . 80 LYS CB C 31.171 0.400 1 371 . 81 PRO CA C 65.627 0.400 1 372 . 81 PRO C C 179.891 0.400 1 373 . 81 PRO CB C 31.309 0.400 1 374 . 82 GLU N N 118.468 0.100 1 375 . 82 GLU H H 9.503 0.020 1 376 . 82 GLU CA C 58.843 0.400 1 377 . 82 GLU HA H 4.174 0.020 1 378 . 82 GLU C C 178.112 0.400 1 379 . 82 GLU CB C 27.715 0.400 1 380 . 83 GLN N N 115.603 0.100 1 381 . 83 GLN H H 7.283 0.020 1 382 . 83 GLN CA C 55.106 0.400 1 383 . 83 GLN HA H 4.464 0.020 1 384 . 83 GLN C C 175.034 0.400 1 385 . 83 GLN CB C 29.779 0.400 1 386 . 84 LYS N N 115.137 0.100 1 387 . 84 LYS H H 7.884 0.020 1 388 . 84 LYS CA C 58.065 0.400 1 389 . 84 LYS HA H 3.507 0.020 1 390 . 84 LYS C C 174.317 0.400 1 391 . 84 LYS CB C 28.829 0.400 1 392 . 85 VAL N N 116.417 0.100 1 393 . 85 VAL H H 7.151 0.020 1 394 . 85 VAL CA C 58.526 0.400 1 395 . 85 VAL HA H 5.076 0.020 1 396 . 85 VAL C C 173.904 0.400 1 397 . 85 VAL CB C 36.202 0.400 1 398 . 86 LEU N N 126.272 0.100 1 399 . 86 LEU H H 8.484 0.020 1 400 . 86 LEU CA C 52.886 0.400 1 401 . 86 LEU HA H 4.664 0.020 1 402 . 86 LEU C C 175.254 0.400 1 403 . 86 LEU CB C 45.760 0.400 1 404 . 87 GLU N N 124.823 0.100 1 405 . 87 GLU H H 8.122 0.020 1 406 . 87 GLU CA C 54.000 0.400 1 407 . 87 GLU HA H 5.722 0.020 1 408 . 87 GLU C C 176.789 0.400 1 409 . 87 GLU CB C 31.192 0.400 1 410 . 88 ILE N N 122.550 0.100 1 411 . 88 ILE H H 9.053 0.020 1 412 . 88 ILE CA C 60.632 0.400 1 413 . 88 ILE HA H 4.691 0.020 1 414 . 88 ILE C C 175.014 0.400 1 415 . 88 ILE CB C 39.496 0.400 1 416 . 89 ARG N N 130.802 0.100 1 417 . 89 ARG H H 9.772 0.020 1 418 . 89 ARG CA C 52.561 0.400 1 419 . 89 ARG HA H 5.806 0.020 1 420 . 89 ARG C C 174.352 0.400 1 421 . 89 ARG CB C 32.558 0.400 1 422 . 90 ASP N N 122.053 0.100 1 423 . 90 ASP H H 9.591 0.020 1 424 . 90 ASP CA C 52.364 0.400 1 425 . 90 ASP HA H 5.590 0.020 1 426 . 90 ASP C C 177.358 0.400 1 427 . 90 ASP CB C 46.408 0.400 1 428 . 91 SER N N 115.473 0.100 1 429 . 91 SER H H 7.473 0.020 1 430 . 91 SER CA C 54.501 0.400 1 431 . 91 SER C C 174.614 0.400 1 432 . 91 SER CB C 61.739 0.400 1 433 . 92 GLY N N 109.835 0.100 1 434 . 92 GLY H H 9.911 0.020 1 435 . 92 GLY CA C 44.222 0.400 1 436 . 92 GLY C C 172.958 0.400 1 437 . 93 ILE N N 115.893 0.100 1 438 . 93 ILE H H 6.878 0.020 1 439 . 93 ILE CA C 62.558 0.400 1 440 . 93 ILE C C 174.787 0.400 1 441 . 93 ILE CB C 39.458 0.400 1 442 . 94 GLY N N 106.093 0.100 1 443 . 94 GLY H H 7.669 0.020 1 444 . 94 GLY CA C 43.465 0.400 1 445 . 94 GLY HA2 H 3.139 0.020 2 446 . 94 GLY HA3 H 3.889 0.020 2 447 . 94 GLY C C 172.818 0.400 1 448 . 95 MET N N 117.842 0.100 1 449 . 95 MET H H 8.149 0.020 1 450 . 95 MET CA C 54.248 0.400 1 451 . 95 MET HA H 4.893 0.020 1 452 . 95 MET C C 176.171 0.400 1 453 . 95 MET CB C 36.269 0.400 1 454 . 96 THR N N 113.515 0.100 1 455 . 96 THR H H 8.998 0.020 1 456 . 96 THR CA C 60.260 0.400 1 457 . 96 THR C C 174.469 0.400 1 458 . 96 THR CB C 69.862 0.400 1 459 . 97 LYS N N 120.567 0.100 1 460 . 97 LYS H H 8.803 0.020 1 461 . 97 LYS CA C 60.872 0.400 1 462 . 97 LYS C C 178.436 0.400 1 463 . 97 LYS CB C 30.597 0.400 1 464 . 98 ALA N N 116.273 0.100 1 465 . 98 ALA H H 8.016 0.020 1 466 . 98 ALA CA C 54.476 0.400 1 467 . 98 ALA C C 181.223 0.400 1 468 . 98 ALA CB C 17.571 0.400 1 469 . 98 ALA HB H 1.256 0.020 1 470 . 99 GLU N N 117.641 0.100 1 471 . 99 GLU H H 7.636 0.020 1 472 . 99 GLU CA C 58.736 0.400 1 473 . 99 GLU HA H 3.794 0.020 1 474 . 99 GLU C C 179.299 0.400 1 475 . 99 GLU CB C 29.226 0.400 1 476 . 100 LEU N N 121.593 0.100 1 477 . 100 LEU H H 8.580 0.020 1 478 . 100 LEU CA C 57.930 0.400 1 479 . 100 LEU C C 178.715 0.400 1 480 . 100 LEU CB C 41.481 0.400 1 481 . 101 ILE N N 115.166 0.100 1 482 . 101 ILE H H 7.443 0.020 1 483 . 101 ILE CA C 65.107 0.400 1 484 . 101 ILE C C 179.409 0.400 1 485 . 101 ILE CB C 38.515 0.400 1 486 . 102 ASN N N 116.087 0.100 1 487 . 102 ASN H H 8.357 0.020 1 488 . 102 ASN CA C 55.553 0.400 1 489 . 102 ASN HA H 4.542 0.020 1 490 . 102 ASN CB C 39.148 0.400 1 491 . 103 ASN N N 117.271 0.100 1 492 . 103 ASN H H 9.173 0.020 1 493 . 103 ASN CA C 55.053 0.400 1 494 . 103 ASN C C 177.404 0.400 1 495 . 103 ASN CB C 30.589 0.400 1 496 . 104 LEU N N 114.862 0.100 1 497 . 104 LEU H H 6.844 0.020 1 498 . 104 LEU CA C 54.405 0.400 1 499 . 104 LEU HA H 4.164 0.020 1 500 . 104 LEU C C 178.759 0.400 1 501 . 104 LEU CB C 38.504 0.400 1 502 . 105 GLY N N 103.619 0.100 1 503 . 105 GLY H H 7.129 0.020 1 504 . 105 GLY CA C 46.723 0.400 1 505 . 105 GLY C C 174.956 0.400 1 506 . 106 THR N N 111.648 0.100 1 507 . 106 THR H H 7.680 0.020 1 508 . 106 THR CA C 63.452 0.400 1 509 . 106 THR C C 175.411 0.400 1 510 . 107 ILE N N 120.852 0.100 1 511 . 107 ILE H H 8.295 0.020 1 512 . 107 ILE CA C 61.388 0.400 1 513 . 107 ILE HA H 4.449 0.020 1 514 . 112 THR C C 176.722 0.400 1 515 . 113 LYS N N 121.322 0.100 1 516 . 113 LYS H H 8.091 0.020 1 517 . 113 LYS CA C 59.402 0.400 1 518 . 113 LYS C C 179.177 0.400 1 519 . 113 LYS CB C 31.594 0.400 1 520 . 114 ALA N N 120.532 0.100 1 521 . 114 ALA H H 7.895 0.020 1 522 . 114 ALA CA C 54.494 0.400 1 523 . 114 ALA HA H 4.153 0.020 1 524 . 114 ALA C C 181.056 0.400 1 525 . 114 ALA CB C 17.585 0.400 1 526 . 114 ALA HB H 1.657 0.020 1 527 . 115 PHE N N 120.073 0.100 1 528 . 115 PHE H H 8.325 0.020 1 529 . 115 PHE CA C 58.903 0.400 1 530 . 115 PHE CB C 37.647 0.400 1 531 . 116 MET N N 117.275 0.100 1 532 . 116 MET H H 7.998 0.020 1 533 . 116 MET CA C 59.388 0.400 1 534 . 116 MET C C 180.047 0.400 1 535 . 116 MET CB C 31.648 0.400 1 536 . 117 GLU N N 119.499 0.100 1 537 . 117 GLU H H 8.100 0.020 1 538 . 117 GLU CA C 58.891 0.400 1 539 . 117 GLU HA H 3.903 0.020 1 540 . 117 GLU C C 179.957 0.400 1 541 . 117 GLU CB C 28.377 0.400 1 542 . 118 ALA N N 123.979 0.100 1 543 . 118 ALA H H 7.749 0.020 1 544 . 118 ALA CA C 54.716 0.400 1 545 . 118 ALA HA H 4.117 0.020 1 546 . 118 ALA C C 181.691 0.400 1 547 . 118 ALA CB C 16.725 0.400 1 548 . 118 ALA HB H 1.326 0.020 1 549 . 119 LEU N N 120.321 0.100 1 550 . 119 LEU H H 8.323 0.020 1 551 . 119 LEU CA C 57.330 0.400 1 552 . 119 LEU C C 181.808 0.400 1 553 . 119 LEU CB C 40.485 0.400 1 554 . 120 SER N N 115.736 0.100 1 555 . 120 SER H H 7.819 0.020 1 556 . 120 SER CA C 60.982 0.400 1 557 . 120 SER HA H 4.207 0.020 1 558 . 120 SER C C 175.198 0.400 1 559 . 120 SER CB C 62.579 0.400 1 560 . 121 ALA N N 122.265 0.100 1 561 . 121 ALA H H 7.390 0.020 1 562 . 121 ALA CA C 51.405 0.400 1 563 . 121 ALA HA H 4.513 0.020 1 564 . 121 ALA C C 178.126 0.400 1 565 . 121 ALA CB C 18.271 0.400 1 566 . 121 ALA HB H 1.467 0.020 1 567 . 122 GLY N N 106.043 0.100 1 568 . 122 GLY H H 7.679 0.020 1 569 . 122 GLY CA C 45.055 0.400 1 570 . 122 GLY HA2 H 3.720 0.020 2 571 . 122 GLY HA3 H 4.408 0.020 2 572 . 122 GLY C C 175.471 0.400 1 573 . 123 ALA N N 122.989 0.100 1 574 . 123 ALA H H 8.032 0.020 1 575 . 123 ALA CA C 51.953 0.400 1 576 . 123 ALA HA H 4.351 0.020 1 577 . 123 ALA C C 175.843 0.400 1 578 . 123 ALA CB C 18.663 0.400 1 579 . 123 ALA HB H 1.246 0.020 1 580 . 124 ASP N N 118.031 0.100 1 581 . 124 ASP H H 7.999 0.020 1 582 . 124 ASP CA C 53.135 0.400 1 583 . 124 ASP HA H 4.782 0.020 1 584 . 124 ASP C C 177.910 0.400 1 585 . 124 ASP CB C 43.663 0.400 1 586 . 125 VAL N N 121.278 0.100 1 587 . 125 VAL H H 8.022 0.020 1 588 . 125 VAL CA C 64.554 0.400 1 589 . 125 VAL C C 176.181 0.400 1 590 . 125 VAL CB C 31.776 0.400 1 591 . 126 SER N N 113.923 0.100 1 592 . 126 SER H H 8.655 0.020 1 593 . 126 SER CA C 60.672 0.400 1 594 . 126 SER C C 176.507 0.400 1 595 . 126 SER CB C 62.458 0.400 1 596 . 127 MET N N 120.209 0.100 1 597 . 127 MET H H 8.052 0.020 1 598 . 127 MET CA C 56.118 0.400 1 599 . 127 MET HA H 4.543 0.020 1 600 . 127 MET C C 177.140 0.400 1 601 . 127 MET CB C 32.093 0.400 1 602 . 128 ILE N N 119.417 0.100 1 603 . 128 ILE H H 7.807 0.020 1 604 . 128 ILE CA C 64.940 0.400 1 605 . 128 ILE C C 176.094 0.400 1 606 . 128 ILE CB C 36.543 0.400 1 607 . 129 GLY N N 109.350 0.100 1 608 . 129 GLY H H 7.932 0.020 1 609 . 129 GLY CA C 46.375 0.400 1 610 . 129 GLY HA2 H 3.790 0.020 2 611 . 129 GLY HA3 H 4.184 0.020 2 612 . 129 GLY C C 178.387 0.400 1 613 . 130 GLN N N 120.400 0.100 1 614 . 130 GLN H H 8.059 0.020 1 615 . 130 GLN CA C 56.952 0.400 1 616 . 130 GLN HA H 4.063 0.020 1 617 . 130 GLN C C 177.340 0.400 1 618 . 130 GLN CB C 27.174 0.400 1 619 . 131 PHE N N 115.408 0.100 1 620 . 131 PHE H H 7.357 0.020 1 621 . 131 PHE CA C 57.712 0.400 1 622 . 131 PHE HA H 4.521 0.020 1 623 . 131 PHE C C 176.647 0.400 1 624 . 131 PHE CB C 39.609 0.400 1 625 . 132 GLY N N 105.793 0.100 1 626 . 132 GLY H H 7.712 0.020 1 627 . 132 GLY CA C 46.055 0.400 1 628 . 132 GLY HA2 H 4.026 0.020 2 629 . 132 GLY HA3 H 4.144 0.020 2 630 . 132 GLY C C 175.561 0.400 1 631 . 133 VAL N N 108.209 0.100 1 632 . 133 VAL H H 6.693 0.020 1 633 . 133 VAL CA C 59.386 0.400 1 634 . 133 VAL HA H 4.949 0.020 1 635 . 133 VAL C C 176.274 0.400 1 636 . 133 VAL CB C 30.232 0.400 1 637 . 134 GLY N N 108.291 0.100 1 638 . 134 GLY H H 8.863 0.020 1 639 . 134 GLY CA C 47.264 0.400 1 640 . 134 GLY C C 176.082 0.400 1 641 . 135 PHE N N 123.907 0.100 1 642 . 135 PHE H H 9.029 0.020 1 643 . 135 PHE CA C 60.984 0.400 1 644 . 135 PHE C C 175.391 0.400 1 645 . 135 PHE CB C 39.820 0.400 1 646 . 136 TYR N N 109.614 0.100 1 647 . 136 TYR H H 7.240 0.020 1 648 . 136 TYR CA C 60.785 0.400 1 649 . 136 TYR C C 177.231 0.400 1 650 . 136 TYR CB C 36.976 0.400 1 651 . 137 SER N N 113.863 0.100 1 652 . 137 SER H H 8.106 0.020 1 653 . 137 SER CA C 61.624 0.400 1 654 . 137 SER HA H 4.535 0.020 1 655 . 137 SER C C 176.423 0.400 1 656 . 137 SER CB C 62.481 0.400 1 657 . 138 LEU N N 122.994 0.100 1 658 . 138 LEU H H 7.609 0.020 1 659 . 138 LEU CA C 57.812 0.400 1 660 . 138 LEU C C 178.004 0.400 1 661 . 138 LEU CB C 39.634 0.400 1 662 . 139 PHE N N 118.155 0.100 1 663 . 139 PHE H H 7.466 0.020 1 664 . 139 PHE CA C 60.422 0.400 1 665 . 139 PHE HA H 4.964 0.020 1 666 . 139 PHE C C 176.134 0.400 1 667 . 139 PHE CB C 36.853 0.400 1 668 . 140 LEU N N 117.850 0.100 1 669 . 140 LEU H H 8.083 0.020 1 670 . 140 LEU CA C 57.178 0.400 1 671 . 140 LEU HA H 4.275 0.020 1 672 . 140 LEU C C 179.494 0.400 1 673 . 140 LEU CB C 42.467 0.400 1 674 . 141 VAL N N 103.767 0.100 1 675 . 141 VAL H H 6.892 0.020 1 676 . 141 VAL CA C 60.012 0.400 1 677 . 141 VAL HA H 4.537 0.020 1 678 . 141 VAL C C 173.421 0.400 1 679 . 141 VAL CB C 32.584 0.400 1 680 . 142 ALA N N 124.640 0.100 1 681 . 142 ALA H H 7.743 0.020 1 682 . 142 ALA CA C 50.623 0.400 1 683 . 142 ALA HA H 5.038 0.020 1 684 . 142 ALA C C 175.816 0.400 1 685 . 142 ALA CB C 21.534 0.400 1 686 . 142 ALA HB H 1.031 0.020 1 687 . 143 ASP N N 117.281 0.100 1 688 . 143 ASP H H 8.256 0.020 1 689 . 143 ASP CA C 53.887 0.400 1 690 . 143 ASP HA H 4.911 0.020 1 691 . 143 ASP C C 176.165 0.400 1 692 . 143 ASP CB C 41.817 0.400 1 693 . 144 ARG N N 114.982 0.100 1 694 . 144 ARG H H 7.564 0.020 1 695 . 144 ARG CA C 54.699 0.400 1 696 . 144 ARG HA H 5.061 0.020 1 697 . 144 ARG C C 173.495 0.400 1 698 . 144 ARG CB C 32.608 0.400 1 699 . 145 VAL N N 121.575 0.100 1 700 . 145 VAL H H 8.742 0.020 1 701 . 145 VAL CA C 58.288 0.400 1 702 . 145 VAL HA H 5.720 0.020 1 703 . 145 VAL C C 174.105 0.400 1 704 . 145 VAL CB C 34.444 0.400 1 705 . 146 GLN N N 123.119 0.100 1 706 . 146 GLN H H 8.925 0.020 1 707 . 146 GLN CA C 53.680 0.400 1 708 . 146 GLN HA H 5.649 0.020 1 709 . 146 GLN C C 175.139 0.400 1 710 . 146 GLN CB C 30.587 0.400 1 711 . 146 GLN HE22 H 9.090 0.020 1 712 . 147 VAL N N 125.441 0.100 1 713 . 147 VAL H H 10.459 0.020 1 714 . 147 VAL CA C 61.260 0.400 1 715 . 147 VAL HA H 4.893 0.020 1 716 . 147 VAL C C 174.917 0.400 1 717 . 147 VAL CB C 32.032 0.400 1 718 . 148 ILE N N 130.248 0.100 1 719 . 148 ILE H H 9.612 0.020 1 720 . 148 ILE CA C 59.649 0.400 1 721 . 148 ILE HA H 5.183 0.020 1 722 . 148 ILE C C 176.328 0.400 1 723 . 148 ILE CB C 39.027 0.400 1 724 . 149 SER N N 119.401 0.100 1 725 . 149 SER H H 9.259 0.020 1 726 . 149 SER CA C 56.854 0.400 1 727 . 149 SER HA H 5.542 0.020 1 728 . 149 SER C C 172.292 0.400 1 729 . 149 SER CB C 66.672 0.400 1 730 . 149 SER HB2 H 3.415 0.020 2 731 . 149 SER HB3 H 3.882 0.020 2 732 . 150 LYS N N 127.340 0.100 1 733 . 150 LYS H H 9.366 0.020 1 734 . 150 LYS CA C 53.529 0.400 1 735 . 150 LYS HA H 4.822 0.020 1 736 . 150 LYS C C 174.416 0.400 1 737 . 150 LYS CB C 36.146 0.400 1 738 . 151 SER N N 123.324 0.100 1 739 . 151 SER H H 9.322 0.020 1 740 . 151 SER CA C 54.809 0.400 1 741 . 151 SER HA H 4.948 0.020 1 742 . 151 SER C C 177.337 0.400 1 743 . 151 SER CB C 63.153 0.400 1 744 . 152 ASN N N 126.508 0.100 1 745 . 152 ASN H H 10.395 0.020 1 746 . 152 ASN CA C 55.028 0.400 1 747 . 152 ASN HA H 4.384 0.020 1 748 . 152 ASN C C 177.494 0.400 1 749 . 152 ASN CB C 36.710 0.400 1 750 . 153 ASP N N 116.164 0.100 1 751 . 153 ASP H H 8.262 0.020 1 752 . 153 ASP CA C 54.290 0.400 1 753 . 153 ASP C C 175.306 0.400 1 754 . 153 ASP CB C 41.560 0.400 1 755 . 154 ASP N N 121.062 0.100 1 756 . 154 ASP H H 8.026 0.020 1 757 . 154 ASP HA H 5.032 0.020 1 758 . 154 ASP C C 174.648 0.400 1 759 . 154 ASP CB C 44.706 0.400 1 760 . 155 GLU N N 116.283 0.100 1 761 . 155 GLU H H 9.152 0.020 1 762 . 155 GLU CA C 54.123 0.400 1 763 . 155 GLU HA H 4.447 0.020 1 764 . 155 GLU C C 174.679 0.400 1 765 . 155 GLU CB C 30.580 0.400 1 766 . 156 GLN N N 119.631 0.100 1 767 . 156 GLN H H 8.411 0.020 1 768 . 156 GLN CA C 56.186 0.400 1 769 . 156 GLN HA H 5.129 0.020 1 770 . 156 GLN C C 176.281 0.400 1 771 . 156 GLN CB C 29.476 0.400 1 772 . 156 GLN NE2 N 122.152 0.100 1 773 . 156 GLN HE21 H 7.800 0.020 1 774 . 157 TYR N N 125.255 0.100 1 775 . 157 TYR H H 8.685 0.020 1 776 . 157 TYR CA C 58.471 0.400 1 777 . 157 TYR HA H 5.029 0.020 1 778 . 157 TYR C C 174.434 0.400 1 779 . 157 TYR CB C 45.357 0.400 1 780 . 158 ILE N N 116.080 0.100 1 781 . 158 ILE H H 9.212 0.020 1 782 . 158 ILE CA C 59.963 0.400 1 783 . 158 ILE HA H 5.154 0.020 1 784 . 158 ILE C C 176.560 0.400 1 785 . 158 ILE CB C 41.400 0.400 1 786 . 159 TRP N N 134.639 0.100 1 787 . 159 TRP H H 10.371 0.020 1 788 . 159 TRP CA C 55.651 0.400 1 789 . 159 TRP HA H 5.925 0.020 1 790 . 159 TRP C C 176.126 0.400 1 791 . 159 TRP CB C 34.315 0.400 1 792 . 160 GLU N N 128.746 0.100 1 793 . 160 GLU H H 9.062 0.020 1 794 . 160 GLU CA C 54.999 0.400 1 795 . 160 GLU HA H 5.659 0.020 1 796 . 160 GLU C C 174.841 0.400 1 797 . 160 GLU CB C 32.738 0.400 1 798 . 161 SER N N 115.908 0.100 1 799 . 161 SER H H 8.207 0.020 1 800 . 161 SER CA C 57.574 0.400 1 801 . 161 SER HA H 4.799 0.020 1 802 . 161 SER C C 173.995 0.400 1 803 . 161 SER CB C 67.323 0.400 1 804 . 162 ASN N N 125.074 0.100 1 805 . 162 ASN H H 8.570 0.020 1 806 . 162 ASN CA C 52.175 0.400 1 807 . 162 ASN HA H 5.327 0.020 1 808 . 162 ASN C C 175.595 0.400 1 809 . 162 ASN CB C 38.256 0.400 1 810 . 163 ALA N N 117.582 0.100 1 811 . 163 ALA H H 8.593 0.020 1 812 . 163 ALA CA C 53.285 0.400 1 813 . 163 ALA HA H 3.923 0.020 1 814 . 163 ALA C C 177.207 0.400 1 815 . 163 ALA CB C 16.296 0.400 1 816 . 163 ALA HB H 1.135 0.020 1 817 . 164 GLY N N 106.244 0.100 1 818 . 164 GLY H H 8.109 0.020 1 819 . 164 GLY CA C 44.900 0.400 1 820 . 164 GLY HA2 H 3.870 0.020 2 821 . 164 GLY HA3 H 4.285 0.020 2 822 . 164 GLY C C 175.860 0.400 1 823 . 165 GLY N N 105.755 0.100 1 824 . 165 GLY H H 8.398 0.020 1 825 . 165 GLY CA C 46.155 0.400 1 826 . 165 GLY HA2 H 4.222 0.020 2 827 . 165 GLY C C 175.074 0.400 1 828 . 166 SER N N 114.783 0.100 1 829 . 166 SER H H 7.980 0.020 1 830 . 166 SER CA C 56.649 0.400 1 831 . 166 SER HA H 5.393 0.020 1 832 . 166 SER C C 172.845 0.400 1 833 . 166 SER CB C 66.522 0.400 1 834 . 167 PHE N N 119.049 0.100 1 835 . 167 PHE H H 8.774 0.020 1 836 . 167 PHE CA C 54.926 0.400 1 837 . 167 PHE HA H 5.201 0.020 1 838 . 167 PHE C C 173.448 0.400 1 839 . 167 PHE CB C 40.709 0.400 1 840 . 168 THR N N 109.941 0.100 1 841 . 168 THR H H 8.541 0.020 1 842 . 168 THR CA C 58.993 0.400 1 843 . 168 THR HA H 5.613 0.020 1 844 . 168 THR C C 175.389 0.400 1 845 . 168 THR CB C 71.916 0.400 1 846 . 169 VAL N N 120.600 0.100 1 847 . 169 VAL H H 9.060 0.020 1 848 . 169 VAL CA C 61.410 0.400 1 849 . 169 VAL HA H 5.540 0.020 1 850 . 169 VAL C C 176.793 0.400 1 851 . 169 VAL CB C 34.561 0.400 1 852 . 170 THR N N 124.685 0.100 1 853 . 170 THR H H 9.325 0.020 1 854 . 170 THR CA C 61.290 0.400 1 855 . 170 THR HA H 5.044 0.020 1 856 . 170 THR C C 174.063 0.400 1 857 . 170 THR CB C 71.712 0.400 1 858 . 171 LEU N N 130.986 0.100 1 859 . 171 LEU H H 8.998 0.020 1 860 . 171 LEU CA C 56.605 0.400 1 861 . 171 LEU C C 177.178 0.400 1 862 . 171 LEU CB C 41.029 0.400 1 863 . 172 ASP N N 126.853 0.100 1 864 . 172 ASP H H 8.468 0.020 1 865 . 172 ASP CA C 54.197 0.400 1 866 . 172 ASP HA H 4.423 0.020 1 867 . 172 ASP C C 177.747 0.400 1 868 . 172 ASP CB C 42.109 0.400 1 869 . 173 GLU N N 128.068 0.100 1 870 . 173 GLU H H 8.805 0.020 1 871 . 173 GLU CA C 54.988 0.400 1 872 . 173 GLU HA H 4.699 0.020 1 873 . 173 GLU C C 176.854 0.400 1 874 . 173 GLU CB C 30.205 0.400 1 875 . 174 VAL N N 114.845 0.100 1 876 . 174 VAL H H 8.636 0.020 1 877 . 174 VAL CA C 62.322 0.400 1 878 . 174 VAL HA H 4.471 0.020 1 879 . 174 VAL C C 176.772 0.400 1 880 . 174 VAL CB C 34.329 0.400 1 881 . 175 ASN N N 121.270 0.100 1 882 . 175 ASN H H 9.888 0.020 1 883 . 175 ASN CA C 53.916 0.400 1 884 . 175 ASN HA H 4.811 0.020 1 885 . 175 ASN C C 176.655 0.400 1 886 . 175 ASN CB C 38.882 0.400 1 887 . 176 GLU N N 120.356 0.100 1 888 . 176 GLU H H 8.823 0.020 1 889 . 176 GLU CA C 56.390 0.400 1 890 . 176 GLU HA H 4.120 0.020 1 891 . 176 GLU C C 176.240 0.400 1 892 . 176 GLU CB C 28.865 0.400 1 893 . 177 ARG N N 121.078 0.100 1 894 . 177 ARG H H 8.628 0.020 1 895 . 177 ARG CA C 54.621 0.400 1 896 . 177 ARG HA H 4.411 0.020 1 897 . 177 ARG C C 178.303 0.400 1 898 . 177 ARG CB C 29.984 0.400 1 899 . 178 ILE N N 123.081 0.100 1 900 . 178 ILE H H 8.531 0.020 1 901 . 178 ILE CA C 60.174 0.400 1 902 . 178 ILE HA H 4.165 0.020 1 903 . 178 ILE C C 176.881 0.400 1 904 . 178 ILE CB C 38.999 0.400 1 905 . 179 GLY N N 114.112 0.100 1 906 . 179 GLY H H 8.384 0.020 1 907 . 179 GLY CA C 47.496 0.400 1 908 . 179 GLY HA2 H 3.637 0.020 2 909 . 179 GLY C C 174.999 0.400 1 910 . 180 ARG N N 118.628 0.100 1 911 . 180 ARG H H 7.327 0.020 1 912 . 180 ARG CA C 56.667 0.400 1 913 . 180 ARG C C 174.750 0.400 1 914 . 180 ARG CB C 30.442 0.400 1 915 . 181 GLY N N 116.142 0.100 1 916 . 181 GLY H H 9.319 0.020 1 917 . 181 GLY CA C 43.286 0.400 1 918 . 181 GLY C C 172.486 0.400 1 919 . 182 THR N N 116.196 0.100 1 920 . 182 THR H H 7.848 0.020 1 921 . 182 THR CA C 61.462 0.400 1 922 . 182 THR HA H 5.344 0.020 1 923 . 182 THR C C 173.757 0.400 1 924 . 182 THR CB C 72.102 0.400 1 925 . 183 ILE N N 125.082 0.100 1 926 . 183 ILE H H 9.992 0.020 1 927 . 183 ILE CA C 61.080 0.400 1 928 . 183 ILE HA H 4.504 0.020 1 929 . 183 ILE C C 175.248 0.400 1 930 . 183 ILE CB C 41.076 0.400 1 931 . 184 LEU N N 128.326 0.100 1 932 . 184 LEU H H 9.133 0.020 1 933 . 184 LEU CA C 53.524 0.400 1 934 . 184 LEU HA H 4.900 0.020 1 935 . 184 LEU C C 175.646 0.400 1 936 . 184 LEU CB C 42.007 0.400 1 937 . 185 ARG N N 125.094 0.100 1 938 . 185 ARG H H 9.668 0.020 1 939 . 185 ARG CA C 55.009 0.400 1 940 . 185 ARG HA H 4.483 0.020 1 941 . 185 ARG C C 173.658 0.400 1 942 . 185 ARG CB C 30.656 0.400 1 943 . 186 LEU N N 125.493 0.100 1 944 . 186 LEU H H 8.829 0.020 1 945 . 186 LEU CA C 54.344 0.400 1 946 . 186 LEU HA H 4.441 0.020 1 947 . 186 LEU C C 175.505 0.400 1 948 . 186 LEU CB C 41.812 0.400 1 949 . 187 PHE N N 123.661 0.100 1 950 . 187 PHE H H 8.146 0.020 1 951 . 187 PHE CA C 57.007 0.400 1 952 . 187 PHE HA H 4.576 0.020 1 953 . 187 PHE C C 175.705 0.400 1 954 . 187 PHE CB C 36.105 0.400 1 955 . 188 LEU N N 121.766 0.100 1 956 . 188 LEU H H 7.745 0.020 1 957 . 188 LEU CA C 55.293 0.400 1 958 . 188 LEU HA H 4.345 0.020 1 959 . 188 LEU C C 178.288 0.400 1 960 . 188 LEU CB C 41.921 0.400 1 961 . 189 LYS N N 119.970 0.100 1 962 . 189 LYS H H 8.480 0.020 1 963 . 189 LYS CA C 56.080 0.400 1 964 . 189 LYS HA H 4.269 0.020 1 965 . 189 LYS C C 178.899 0.400 1 966 . 189 LYS CB C 34.005 0.400 1 967 . 190 ASP N N 118.882 0.100 1 968 . 190 ASP H H 8.660 0.020 1 969 . 190 ASP CA C 57.038 0.400 1 970 . 190 ASP HA H 4.312 0.020 1 971 . 190 ASP C C 177.649 0.400 1 972 . 190 ASP CB C 40.279 0.400 1 973 . 191 ASP N N 113.860 0.100 1 974 . 191 ASP H H 8.440 0.020 1 975 . 191 ASP CA C 53.050 0.400 1 976 . 191 ASP HA H 4.842 0.020 1 977 . 191 ASP C C 177.856 0.400 1 978 . 191 ASP CB C 39.141 0.400 1 979 . 192 GLN N N 119.753 0.100 1 980 . 192 GLN H H 8.020 0.020 1 981 . 192 GLN CA C 53.705 0.400 1 982 . 192 GLN HA H 4.961 0.020 1 983 . 192 GLN C C 176.239 0.400 1 984 . 192 GLN CB C 27.233 0.400 1 985 . 193 LEU N N 115.001 0.100 1 986 . 193 LEU H H 7.733 0.020 1 987 . 193 LEU CA C 56.091 0.400 1 988 . 193 LEU HA H 4.035 0.020 1 989 . 193 LEU C C 180.426 0.400 1 990 . 193 LEU CB C 38.179 0.400 1 991 . 194 GLU N N 120.864 0.100 1 992 . 194 GLU H H 8.704 0.020 1 993 . 194 GLU CA C 57.907 0.400 1 994 . 194 GLU C C 177.252 0.400 1 995 . 194 GLU CB C 27.848 0.400 1 996 . 195 TYR N N 114.477 0.100 1 997 . 195 TYR H H 6.724 0.020 1 998 . 195 TYR CA C 59.971 0.400 1 999 . 195 TYR HA H 4.191 0.020 1 1000 . 195 TYR CB C 36.456 0.400 1 1001 . 196 LEU N N 110.977 0.100 1 1002 . 196 LEU H H 7.356 0.020 1 1003 . 196 LEU CA C 53.684 0.400 1 1004 . 196 LEU HA H 4.365 0.020 1 1005 . 196 LEU C C 177.516 0.400 1 1006 . 196 LEU CB C 41.371 0.400 1 1007 . 197 GLU N N 117.556 0.100 1 1008 . 197 GLU H H 7.461 0.020 1 1009 . 197 GLU CA C 55.020 0.400 1 1010 . 197 GLU HA H 4.315 0.020 1 1011 . 197 GLU C C 177.595 0.400 1 1012 . 197 GLU CB C 29.203 0.400 1 1013 . 198 GLU N N 127.304 0.100 1 1014 . 198 GLU H H 9.064 0.020 1 1015 . 198 GLU CA C 60.431 0.400 1 1016 . 198 GLU C C 178.345 0.400 1 1017 . 198 GLU CB C 28.857 0.400 1 1018 . 199 LYS N N 116.684 0.100 1 1019 . 199 LYS H H 8.890 0.020 1 1020 . 199 LYS CA C 59.539 0.400 1 1021 . 199 LYS HA H 3.926 0.020 1 1022 . 199 LYS C C 179.372 0.400 1 1023 . 199 LYS CB C 31.395 0.400 1 1024 . 200 ARG N N 119.938 0.100 1 1025 . 200 ARG H H 6.905 0.020 1 1026 . 200 ARG CA C 56.861 0.400 1 1027 . 200 ARG HA H 4.219 0.020 1 1028 . 200 ARG C C 178.618 0.400 1 1029 . 200 ARG CB C 29.057 0.400 1 1030 . 201 ILE N N 118.554 0.100 1 1031 . 201 ILE H H 8.126 0.020 1 1032 . 201 ILE CA C 65.322 0.400 1 1033 . 201 ILE HA H 3.462 0.020 1 1034 . 201 ILE C C 178.866 0.400 1 1035 . 201 ILE CB C 37.267 0.400 1 1036 . 202 LYS N N 116.446 0.100 1 1037 . 202 LYS H H 8.473 0.020 1 1038 . 202 LYS CA C 60.208 0.400 1 1039 . 202 LYS HA H 3.787 0.020 1 1040 . 202 LYS C C 179.799 0.400 1 1041 . 202 LYS CB C 31.733 0.400 1 1042 . 203 GLU N N 119.536 0.100 1 1043 . 203 GLU H H 7.667 0.020 1 1044 . 203 GLU CA C 58.832 0.400 1 1045 . 203 GLU HA H 4.019 0.020 1 1046 . 203 GLU C C 179.561 0.400 1 1047 . 203 GLU CB C 28.917 0.400 1 1048 . 204 VAL N N 120.845 0.100 1 1049 . 204 VAL H H 8.032 0.020 1 1050 . 204 VAL CA C 66.389 0.400 1 1051 . 204 VAL C C 179.465 0.400 1 1052 . 204 VAL CB C 30.887 0.400 1 1053 . 205 ILE N N 119.725 0.100 1 1054 . 205 ILE H H 8.369 0.020 1 1055 . 205 ILE CA C 64.705 0.400 1 1056 . 205 ILE HA H 3.603 0.020 1 1057 . 205 ILE C C 178.830 0.400 1 1058 . 205 ILE CB C 37.023 0.400 1 1059 . 206 LYS N N 119.231 0.100 1 1060 . 206 LYS H H 7.894 0.020 1 1061 . 206 LYS CA C 58.281 0.400 1 1062 . 206 LYS C C 178.471 0.400 1 1063 . 206 LYS CB C 31.181 0.400 1 1064 . 207 ARG N N 115.680 0.100 1 1065 . 207 ARG H H 7.503 0.020 1 1066 . 207 ARG CA C 58.050 0.400 1 1067 . 207 ARG HA H 3.978 0.020 1 1068 . 207 ARG C C 178.870 0.400 1 1069 . 207 ARG CB C 30.079 0.400 1 1070 . 208 HIS N N 113.267 0.100 1 1071 . 208 HIS H H 7.713 0.020 1 1072 . 208 HIS CA C 57.105 0.400 1 1073 . 208 HIS HA H 4.890 0.020 1 1074 . 208 HIS C C 177.782 0.400 1 1075 . 208 HIS CB C 33.206 0.400 1 1076 . 209 SER N N 115.767 0.100 1 1077 . 209 SER H H 8.420 0.020 1 1078 . 209 SER CA C 57.908 0.400 1 1079 . 209 SER C C 175.789 0.400 1 1080 . 209 SER CB C 63.437 0.400 1 1081 . 210 GLU N N 121.117 0.100 1 1082 . 210 GLU H H 8.006 0.020 1 1083 . 210 GLU CA C 58.276 0.400 1 1084 . 210 GLU HA H 3.830 0.020 1 1085 . 210 GLU C C 177.431 0.400 1 1086 . 210 GLU CB C 28.898 0.400 1 1087 . 211 PHE N N 114.689 0.100 1 1088 . 211 PHE H H 8.034 0.020 1 1089 . 211 PHE CA C 56.623 0.400 1 1090 . 211 PHE HA H 4.657 0.020 1 1091 . 211 PHE C C 176.265 0.400 1 1092 . 211 PHE CB C 37.548 0.400 1 1093 . 211 PHE HB2 H 2.900 0.020 2 1094 . 211 PHE HB3 H 3.269 0.020 2 1095 . 212 VAL N N 122.452 0.100 1 1096 . 212 VAL H H 7.219 0.020 1 1097 . 212 VAL CA C 62.621 0.400 1 1098 . 212 VAL HA H 3.974 0.020 1 1099 . 212 VAL C C 176.800 0.400 1 1100 . 212 VAL CB C 31.681 0.400 1 1101 . 213 ALA N N 129.306 0.100 1 1102 . 213 ALA H H 8.925 0.020 1 1103 . 213 ALA CA C 52.662 0.400 1 1104 . 213 ALA HA H 4.094 0.020 1 1105 . 213 ALA C C 176.710 0.400 1 1106 . 213 ALA CB C 18.235 0.400 1 1107 . 213 ALA HB H 1.085 0.020 1 1108 . 214 TYR N N 116.484 0.100 1 1109 . 214 TYR H H 6.698 0.020 1 1110 . 214 TYR CA C 55.428 0.400 1 1111 . 214 TYR C C 172.509 0.400 1 1112 . 214 TYR CB C 39.707 0.400 1 1113 . 215 PRO CA C 62.844 0.400 1 1114 . 215 PRO C C 175.703 0.400 1 1115 . 216 ILE N N 121.212 0.100 1 1116 . 216 ILE H H 7.994 0.020 1 1117 . 216 ILE CA C 59.988 0.400 1 1118 . 216 ILE HA H 4.669 0.020 1 1119 . 216 ILE C C 177.093 0.400 1 1120 . 216 ILE CB C 37.446 0.400 1 1121 . 217 GLN N N 128.630 0.100 1 1122 . 217 GLN H H 9.555 0.020 1 1123 . 217 GLN CA C 55.045 0.400 1 1124 . 217 GLN HA H 4.421 0.020 1 1125 . 217 GLN C C 174.213 0.400 1 1126 . 217 GLN CB C 28.660 0.400 1 1127 . 218 LEU N N 128.958 0.100 1 1128 . 218 LEU H H 7.716 0.020 1 1129 . 218 LEU CA C 56.589 0.400 1 1130 . 218 LEU HA H 4.699 0.020 1 1131 . 218 LEU C C 182.369 0.400 1 1132 . 218 LEU CB C 43.745 0.400 1 1133 . 218 LEU HB2 H 1.506 0.020 2 1134 . 218 LEU HB3 H 1.707 0.020 2 stop_ save_