data_6445 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N and 13CB Chemical Shift Assignments for Six C2H2 Zinc Fingers (F1-6) of MTF-1 in the DNA Bound State (22 bp) ; _BMRB_accession_number 6445 _BMRB_flat_file_name bmr6445.str _Entry_type original _Submission_date 2004-12-23 _Accession_date 2004-12-23 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Potter Belinda M. . 2 Laity John H. . 3 Wilson Jed A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 165 "13C chemical shifts" 490 "15N chemical shifts" 165 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-07-15 update BMRB 'update DNA residue label to two-letter code' 2005-07-25 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 6275 'MTF-1 in the free state' 6276 'MTF-1 in the DNA bound state (17 bp)' 6408 'Two Zinc MTF-1' 6409 'Four Zinc MTF-1' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR Assignment of the Six Zinc Fingers of MTF-1 in the Free and DNA Bound States' _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 Potter Belinda M. . 2 Knudsen Nathan A. . 3 Feng Linda S. . 4 Matskevich Viktor A. . 5 Wilson Jed A. . 6 Andrews Glen K. . 7 Laity John H. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 31 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 94 _Page_last 94 _Year 2005 _Details . loop_ _Keyword 'Zinc fingers' Metal-sensing 'Transcription factor' 'Zinc affinities' 'Zinc homeostasis' 'DNA binding' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_Original_cloning_of_MTF-1 _Saveframe_category citation _Citation_full ; Radtke, F., Heuchel, R., Georgiev, O., Hergersberg, M., Gariglio, M., Dembic, Z., and Schaffner, W. (1993). Cloned transcription factor MTF-1 activates the mouse metallothionein I promoter. EMBO J., 12, 1355-1362. ; _Citation_title 'Cloned transcription factor MTF-1 activates the mouse metallothionein I promoter.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8467794 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Radtke F. . . 2 Heuchel R. . . 3 Georgiev O. . . 4 Hergersberg M. . . 5 Gariglio M. . . 6 Dembic Z. . . 7 Schaffner W. . . stop_ _Journal_abbreviation 'EMBO J.' _Journal_name_full 'The EMBO journal' _Journal_volume 12 _Journal_issue 4 _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 1355 _Page_last 1362 _Year 1993 _Details ; Metallothioneins (MTs) are small cysteine-rich proteins whose structure is conserved from fungi to man. MTs strongly bind heavy metals, notably zinc, copper and cadmium. Upon exposure of cells to heavy metal and other adverse treatments, MT gene transcription is strongly enhanced. Metal induction is mediated by several copies of a 15 bp consensus sequence (metal-responsive element, MRE) present in the promoter region of MT genes. We and others have demonstrated the presence of an MRE-binding factor in HeLa cell nuclear extracts. We found that this factor, termed MTF-1 (MRE-binding transcription factor) is inactivated/reactivated in vitro by zinc withdrawal/addition. Here we report that the amounts of MTF-1-DNA complexes are elevated several-fold in zinc-treated cells, as measured by bandshift assay. We have also cloned the cDNA of mouse MTF-1, a 72.5 kDa protein. MTF-1 contains six zinc fingers and separate transcriptional activation domains with high contents of acidic and proline residues. Ectopic expression of MTF-1 in primate or rodent cells strongly enhances transcription of a reporter gene that is driven by four consensus MREd sites, or by the complete mouse MT-I promoter, even at normal zinc levels. ; save_ ################################## # Molecular system description # ################################## save_system_MTF-1_MRE _Saveframe_category molecular_system _Mol_system_name 'Metal-response element-binding transcription factor-1 complex with MRE DNA (22bp)' _Abbreviation_common MTF-1/MRE _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'MTF-1 monomer' $MTF-1 'DNA strand one' $MRE_sense 'DNA strand two' $MRE_antisense 'ZINC (II) ION 1' $ZN 'ZINC (II) ION 2' $ZN 'ZINC (II) ION 3' $ZN 'ZINC (II) ION 4' $ZN 'ZINC (II) ION 5' $ZN 'ZINC (II) ION 6' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state 'protein-DNA complex' _System_paramagnetic no _System_thiol_state 'all other bound' loop_ _Biological_function 'transcription factor' 'metalloregulatory protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MRE_sense _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class DNA _Name_common 'Metal response element' _Name_variant 'MREd (murine)' _Abbreviation_common MRE _Molecular_mass 13633 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 22 _Mol_residue_sequence ; GCTCTGCACTCCGCCCGAAA AG ; loop_ _Residue_seq_code _Residue_label 1 DG 2 DC 3 DT 4 DC 5 DT 6 DG 7 DC 8 DA 9 DC 10 DT 11 DC 12 DC 13 DG 14 DC 15 DC 16 DC 17 DG 18 DA 19 DA 20 DA 21 DA 22 DG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_MRE_antisense _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class DNA _Name_common 'Metal response element' _Name_variant 'MREd (murine)' _Abbreviation_common MRE _Molecular_mass 13633 _Mol_thiol_state 'not present' _Details . _Residue_count 22 _Mol_residue_sequence ; CTTTTCGGGCGGAGTGCAGA GC ; loop_ _Residue_seq_code _Residue_label 1 DC 2 DT 3 DT 4 DT 5 DT 6 DC 7 DG 8 DG 9 DG 10 DC 11 DG 12 DG 13 DA 14 DG 15 DT 16 DG 17 DC 18 DA 19 DG 20 DA 21 DG 22 DC stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_MTF-1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'metal-response element-binding transcription factor-1' _Abbreviation_common MTF-1 _Molecular_mass 20367 _Mol_thiol_state 'all other bound' _Details . _Residue_count 177 _Mol_residue_sequence ; VKRYQCTFEGCPRTYSTAGN LRTHQKTHRGEYTFVCNQEG CGKAFLTSYSLRIHVRVHTK EKPFECDVQGCEKAFNTLYR LKAHQRLHTGKTFNCESQGC SKYFTTLSDLRKHIRTHTGE KPFRCDHDGCGKAFAASHHL KTHVRTHTGERPFFCPSNGC EKTFSTQYSLKSHMKGH ; loop_ _Residue_seq_code _Residue_label 1 VAL 2 LYS 3 ARG 4 TYR 5 GLN 6 CYS 7 THR 8 PHE 9 GLU 10 GLY 11 CYS 12 PRO 13 ARG 14 THR 15 TYR 16 SER 17 THR 18 ALA 19 GLY 20 ASN 21 LEU 22 ARG 23 THR 24 HIS 25 GLN 26 LYS 27 THR 28 HIS 29 ARG 30 GLY 31 GLU 32 TYR 33 THR 34 PHE 35 VAL 36 CYS 37 ASN 38 GLN 39 GLU 40 GLY 41 CYS 42 GLY 43 LYS 44 ALA 45 PHE 46 LEU 47 THR 48 SER 49 TYR 50 SER 51 LEU 52 ARG 53 ILE 54 HIS 55 VAL 56 ARG 57 VAL 58 HIS 59 THR 60 LYS 61 GLU 62 LYS 63 PRO 64 PHE 65 GLU 66 CYS 67 ASP 68 VAL 69 GLN 70 GLY 71 CYS 72 GLU 73 LYS 74 ALA 75 PHE 76 ASN 77 THR 78 LEU 79 TYR 80 ARG 81 LEU 82 LYS 83 ALA 84 HIS 85 GLN 86 ARG 87 LEU 88 HIS 89 THR 90 GLY 91 LYS 92 THR 93 PHE 94 ASN 95 CYS 96 GLU 97 SER 98 GLN 99 GLY 100 CYS 101 SER 102 LYS 103 TYR 104 PHE 105 THR 106 THR 107 LEU 108 SER 109 ASP 110 LEU 111 ARG 112 LYS 113 HIS 114 ILE 115 ARG 116 THR 117 HIS 118 THR 119 GLY 120 GLU 121 LYS 122 PRO 123 PHE 124 ARG 125 CYS 126 ASP 127 HIS 128 ASP 129 GLY 130 CYS 131 GLY 132 LYS 133 ALA 134 PHE 135 ALA 136 ALA 137 SER 138 HIS 139 HIS 140 LEU 141 LYS 142 THR 143 HIS 144 VAL 145 ARG 146 THR 147 HIS 148 THR 149 GLY 150 GLU 151 ARG 152 PRO 153 PHE 154 PHE 155 CYS 156 PRO 157 SER 158 ASN 159 GLY 160 CYS 161 GLU 162 LYS 163 THR 164 PHE 165 SER 166 THR 167 GLN 168 TYR 169 SER 170 LEU 171 LYS 172 SER 173 HIS 174 MET 175 LYS 176 GLY 177 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-21 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 6275 MTF-1 100.00 177 100.00 100.00 2.09e-125 BMRB 6276 "metal-response element-binding transcription factor-1" 100.00 177 100.00 100.00 2.09e-125 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Aug 2 11:24:12 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ _Tissue _Fraction _Plasmid _Gene_mnemonic $MRE_antisense mouse 10090 Eukaryota Metazoa Mus musculus ubiquitous ubiquitous nucleus 'commercially synthesized' 'MREd promotor' $MRE_sense mouse 10090 Eukaryota Metazoa Mus musculus ubiquitous ubiquitous nucleus 'commercially synthesized' 'MREd promotor' $MTF-1 mouse 10090 Eukaryota Metazoa Mus musculus ubiquitous ubiquitous 'cytoplasm and nucleus' 'I.M.A.G.E. Consortium Clone ID 1260636' MTF-1 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 $MRE_antisense 'chemical synthesis' . . . . . $MRE_sense 'chemical synthesis' . . . . . $MTF-1 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_all_samples _Saveframe_category sample _Sample_type solution _Details 'All spectra were recorded with 95% H2O/5% D2O.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $MTF-1 . mM 0.3 0.6 '[U-98% 13C; U-98% 15N]' $MRE_sense . mM 0.3 0.6 . $MRE_antisense . mM 0.3 0.6 . H2O 95 % . . . D2O 5 % . . . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 97.027.12.56 loop_ _Task 'Raw spectral data processing' stop_ _Details ; Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., & Bax, A. (1995). NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293. ; save_ save_NMRView _Saveframe_category software _Name NMRView _Version 5.0.4 loop_ _Task 'Data analysis' stop_ _Details ; Johnson, B.A. and Blevins, R.A.(1994) NMRView: A computer program for the visualization and analysis of NMR Data. J. Biomol. NMR 4, 603-614. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $all_samples save_ save_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $all_samples save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $all_samples save_ save_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $all_samples save_ save_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $all_samples save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details 'A cryogenically cooled HCN Triax probe (cryoprobe) was used for all experiments.' save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details 'A cryogenically cooled HCN Triax probe (cryoprobe) was used for all experiments.' save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details 'A cryogenically cooled HCN Triax probe (cryoprobe) was used for all experiments.' save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details 'A cryogenically cooled HCN Triax probe (cryoprobe) was used for all experiments.' save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details 'A cryogenically cooled HCN Triax probe (cryoprobe) was used for all experiments.' save_ ####################### # Sample conditions # ####################### save_Cond_1 _Saveframe_category sample_conditions _Details ; Protein was produced in a reduced lyopholized form (free thiols). Protein was subsequently resuspended in degassed buffer under anaerobic conditions. Protein was titrated into DNA solution in small aliquots to make complex. ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.9 0.03 pH temperature 303 0.1 K 'ionic strength' 0.01 0.01 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 . . . 1.0 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_MTF-1_MRE_bound_(22bp) _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $all_samples stop_ _Sample_conditions_label $Cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'MTF-1 monomer' _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 . 3 ARG C C 175.9 0.08 1 2 . 3 ARG CA C 55.07 0.2 1 3 . 3 ARG CB C 31.84 0.31 1 4 . 4 TYR H H 9.03 0.015 1 5 . 4 TYR C C 176.0 0.08 1 6 . 4 TYR CA C 58.25 0.2 1 7 . 4 TYR CB C 39.11 0.31 1 8 . 4 TYR N N 121.0 0.14 1 9 . 5 GLN H H 8.67 0.015 1 10 . 5 GLN C C 174.9 0.08 1 11 . 5 GLN CA C 55.38 0.2 1 12 . 5 GLN CB C 30.29 0.31 1 13 . 5 GLN N N 125.2 0.14 1 14 . 6 CYS H H 8.58 0.015 1 15 . 6 CYS C C 176.5 0.08 1 16 . 6 CYS CA C 62.53 0.2 1 17 . 6 CYS CB C 30.27 0.31 1 18 . 6 CYS N N 126.8 0.14 1 19 . 7 THR H H 7.56 0.015 1 20 . 7 THR C C 175.8 0.08 1 21 . 7 THR CA C 61.94 0.2 1 22 . 7 THR CB C 69.14 0.31 1 23 . 7 THR N N 116.4 0.14 1 24 . 8 PHE H H 9.09 0.015 1 25 . 8 PHE C C 176.5 0.08 1 26 . 8 PHE CA C 59.86 0.2 1 27 . 8 PHE CB C 39.08 0.31 1 28 . 8 PHE N N 129.1 0.14 1 29 . 9 GLU H H 8.25 0.015 1 30 . 9 GLU C C 177.8 0.08 1 31 . 9 GLU CA C 58.48 0.2 1 32 . 9 GLU CB C 28.84 0.31 1 33 . 9 GLU N N 127.9 0.14 1 34 . 10 GLY H H 8.75 0.015 5 35 . 10 GLY C C 174.1 0.08 5 36 . 10 GLY CA C 45.65 0.2 5 37 . 10 GLY N N 113.8 0.14 5 38 . 11 CYS H H 8.20 0.015 1 39 . 11 CYS CA C 57.04 0.2 1 40 . 11 CYS CB C 31.10 0.31 1 41 . 11 CYS N N 125.6 0.14 1 42 . 12 PRO C C 177.7 0.08 1 43 . 12 PRO CA C 63.41 0.2 1 44 . 12 PRO CB C 32.09 0.31 1 45 . 13 ARG H H 7.97 0.015 1 46 . 13 ARG C C 175.8 0.08 1 47 . 13 ARG CA C 58.89 0.2 1 48 . 13 ARG CB C 30.75 0.31 1 49 . 13 ARG N N 123.2 0.14 1 50 . 14 THR H H 7.17 0.015 1 51 . 14 THR C C 173.5 0.08 1 52 . 14 THR CA C 60.20 0.2 1 53 . 14 THR CB C 73.18 0.31 1 54 . 14 THR N N 109.2 0.14 1 55 . 15 TYR H H 8.49 0.015 1 56 . 15 TYR C C 177.1 0.08 1 57 . 15 TYR CA C 59.34 0.2 1 58 . 15 TYR CB C 45.12 0.31 1 59 . 15 TYR N N 116.0 0.14 1 60 . 16 SER H H 10.62 0.015 1 61 . 16 SER C C 175.7 0.08 1 62 . 16 SER CA C 60.69 0.2 1 63 . 16 SER CB C 64.43 0.31 1 64 . 16 SER N N 118.0 0.14 1 65 . 17 THR H H 7.26 0.015 1 66 . 17 THR C C 174.0 0.08 1 67 . 17 THR CA C 59.11 0.2 1 68 . 17 THR CB C 73.00 0.31 1 69 . 17 THR N N 109.1 0.14 1 70 . 18 ALA H H 8.21 0.015 1 71 . 18 ALA C C 181.1 0.08 1 72 . 18 ALA CA C 54.48 0.2 1 73 . 18 ALA CB C 17.91 0.31 1 74 . 18 ALA N N 124.4 0.14 1 75 . 19 GLY H H 8.63 0.015 1 76 . 19 GLY C C 176.1 0.08 1 77 . 19 GLY CA C 47.61 0.2 1 78 . 19 GLY N N 107.5 0.14 1 79 . 20 ASN H H 8.28 0.015 1 80 . 20 ASN C C 179.2 0.08 1 81 . 20 ASN CA C 55.59 0.2 1 82 . 20 ASN CB C 36.73 0.31 1 83 . 20 ASN N N 122.9 0.14 1 84 . 21 LEU H H 7.26 0.015 1 85 . 21 LEU C C 178.1 0.08 1 86 . 21 LEU CA C 58.19 0.2 1 87 . 21 LEU CB C 39.49 0.31 1 88 . 21 LEU N N 123.8 0.14 1 89 . 22 ARG H H 8.27 0.015 1 90 . 22 ARG C C 180.8 0.08 1 91 . 22 ARG CA C 60.44 0.2 1 92 . 22 ARG CB C 29.59 0.31 1 93 . 22 ARG N N 121.1 0.14 1 94 . 23 THR H H 8.27 0.015 1 95 . 23 THR C C 175.7 0.08 1 96 . 23 THR CA C 67.27 0.2 1 97 . 23 THR CB C 68.29 0.31 1 98 . 23 THR N N 118.0 0.14 1 99 . 24 HIS H H 7.16 0.015 1 100 . 24 HIS C C 179.6 0.08 1 101 . 24 HIS CA C 58.81 0.2 1 102 . 24 HIS CB C 31.82 0.31 1 103 . 24 HIS N N 118.1 0.14 1 104 . 25 GLN H H 8.94 0.015 1 105 . 25 GLN C C 177.9 0.08 1 106 . 25 GLN CA C 60.33 0.2 1 107 . 25 GLN CB C 27.81 0.31 1 108 . 25 GLN N N 120.8 0.14 1 109 . 26 LYS H H 7.37 0.015 1 110 . 26 LYS C C 180.2 0.08 1 111 . 26 LYS CA C 60.65 0.2 1 112 . 26 LYS CB C 32.60 0.31 1 113 . 26 LYS N N 118.1 0.14 1 114 . 27 THR H H 7.69 0.015 1 115 . 27 THR C C 178.1 0.08 1 116 . 27 THR CA C 64.99 0.2 1 117 . 27 THR CB C 69.09 0.31 1 118 . 27 THR N N 109.8 0.14 1 119 . 28 HIS H H 6.47 0.015 1 120 . 28 HIS C C 176.8 0.08 1 121 . 28 HIS CA C 57.55 0.2 1 122 . 28 HIS CB C 28.23 0.31 1 123 . 28 HIS N N 120.0 0.14 1 124 . 29 ARG H H 7.03 0.015 1 125 . 29 ARG C C 176.5 0.08 1 126 . 29 ARG CA C 56.17 0.2 1 127 . 29 ARG CB C 31.17 0.31 1 128 . 29 ARG N N 114.6 0.14 1 129 . 30 GLY H H 7.55 0.015 1 130 . 30 GLY C C 175.4 0.08 1 131 . 30 GLY CA C 46.35 0.2 1 132 . 30 GLY N N 109.1 0.14 1 133 . 31 GLU H H 7.78 0.015 1 134 . 31 GLU C C 173.9 0.08 1 135 . 31 GLU CA C 55.19 0.2 1 136 . 31 GLU CB C 28.68 0.31 1 137 . 31 GLU N N 123.5 0.14 1 138 . 32 TYR H H 7.50 0.015 1 139 . 32 TYR C C 176.7 0.08 1 140 . 32 TYR CA C 56.68 0.2 1 141 . 32 TYR CB C 38.49 0.31 1 142 . 32 TYR N N 124.8 0.14 1 143 . 33 THR H H 8.23 0.015 1 144 . 33 THR C C 174.7 0.08 1 145 . 33 THR CA C 63.29 0.2 1 146 . 33 THR CB C 69.43 0.31 1 147 . 33 THR N N 112.2 0.14 1 148 . 34 PHE H H 8.08 0.015 1 149 . 34 PHE C C 175.1 0.08 1 150 . 34 PHE CA C 58.23 0.2 1 151 . 34 PHE CB C 38.51 0.31 1 152 . 34 PHE N N 122.9 0.14 1 153 . 35 VAL H H 8.24 0.015 1 154 . 35 VAL C C 175.4 0.08 1 155 . 35 VAL CA C 62.02 0.2 1 156 . 35 VAL CB C 33.97 0.31 1 157 . 35 VAL N N 125.7 0.14 1 158 . 36 CYS H H 9.06 0.015 1 159 . 36 CYS C C 176.4 0.08 1 160 . 36 CYS CA C 61.48 0.2 1 161 . 36 CYS CB C 30.11 0.31 1 162 . 36 CYS N N 129.8 0.14 1 163 . 37 ASN H H 8.52 0.015 1 164 . 37 ASN C C 176.1 0.08 1 165 . 37 ASN CA C 53.41 0.2 1 166 . 37 ASN CB C 39.20 0.31 1 167 . 37 ASN N N 127.5 0.14 1 168 . 38 GLN H H 8.82 0.015 1 169 . 38 GLN C C 177.3 0.08 1 170 . 38 GLN CA C 56.67 0.2 1 171 . 38 GLN CB C 27.65 0.31 1 172 . 38 GLN N N 124.5 0.14 1 173 . 39 GLU H H 8.86 0.015 1 174 . 39 GLU C C 178.1 0.08 1 175 . 39 GLU CA C 58.58 0.2 1 176 . 39 GLU CB C 29.05 0.31 1 177 . 39 GLU N N 129.8 0.14 1 178 . 40 GLY H H 8.88 0.015 5 179 . 40 GLY C C 173.9 0.08 5 180 . 40 GLY CA C 45.73 0.2 5 181 . 40 GLY N N 114.0 0.14 5 182 . 41 CYS H H 7.81 0.015 1 183 . 41 CYS C C 176.2 0.08 1 184 . 41 CYS CA C 60.55 0.2 1 185 . 41 CYS CB C 29.40 0.31 1 186 . 41 CYS N N 122.9 0.14 1 187 . 42 GLY H H 7.99 0.015 1 188 . 42 GLY C C 174.8 0.08 1 189 . 42 GLY CA C 45.97 0.2 1 190 . 42 GLY N N 106.3 0.14 1 191 . 43 LYS H H 8.18 0.015 1 192 . 43 LYS C C 173.9 0.08 1 193 . 43 LYS CA C 58.36 0.2 1 194 . 43 LYS CB C 33.11 0.31 1 195 . 43 LYS N N 123.4 0.14 1 196 . 44 ALA H H 7.64 0.015 1 197 . 44 ALA C C 176.6 0.08 1 198 . 44 ALA CA C 50.70 0.2 1 199 . 44 ALA CB C 22.55 0.31 1 200 . 44 ALA N N 124.0 0.14 1 201 . 45 PHE H H 9.04 0.015 1 202 . 45 PHE C C 176.5 0.08 1 203 . 45 PHE CA C 57.88 0.2 1 204 . 45 PHE CB C 43.71 0.31 1 205 . 45 PHE N N 118.0 0.14 1 206 . 46 LEU H H 9.31 0.015 1 207 . 46 LEU C C 178.6 0.08 1 208 . 46 LEU CA C 57.00 0.2 1 209 . 46 LEU CB C 44.40 0.31 1 210 . 46 LEU N N 120.7 0.14 1 211 . 47 THR H H 7.31 0.015 1 212 . 47 THR C C 173.4 0.08 1 213 . 47 THR CA C 58.95 0.2 1 214 . 47 THR CB C 72.47 0.31 1 215 . 47 THR N N 104.6 0.14 1 216 . 48 SER H H 8.19 0.015 1 217 . 48 SER C C 178.3 0.08 1 218 . 48 SER CA C 60.66 0.2 1 219 . 48 SER CB C 62.24 0.31 1 220 . 48 SER N N 117.6 0.14 1 221 . 49 TYR H H 8.80 0.015 1 222 . 49 TYR C C 176.8 0.08 1 223 . 49 TYR CA C 62.42 0.2 1 224 . 49 TYR CB C 37.84 0.31 1 225 . 49 TYR N N 125.8 0.14 1 226 . 50 SER H H 7.80 0.015 1 227 . 50 SER C C 177.3 0.08 1 228 . 50 SER CA C 62.52 0.2 1 229 . 50 SER N N 114.5 0.14 1 230 . 51 LEU H H 7.01 0.015 1 231 . 51 LEU C C 177.1 0.08 1 232 . 51 LEU CA C 57.95 0.2 1 233 . 51 LEU CB C 40.30 0.31 1 234 . 51 LEU N N 121.5 0.14 1 235 . 52 ARG H H 8.04 0.015 1 236 . 52 ARG C C 180.0 0.08 1 237 . 52 ARG CA C 60.34 0.2 1 238 . 52 ARG CB C 29.63 0.31 1 239 . 52 ARG N N 120.0 0.14 1 240 . 53 ILE H H 7.58 0.015 1 241 . 53 ILE C C 178.8 0.08 1 242 . 53 ILE CA C 63.81 0.2 1 243 . 53 ILE CB C 35.90 0.31 1 244 . 53 ILE N N 115.9 0.14 1 245 . 54 HIS H H 7.22 0.015 1 246 . 54 HIS C C 178.4 0.08 1 247 . 54 HIS CA C 59.78 0.2 1 248 . 54 HIS CB C 28.44 0.31 1 249 . 54 HIS N N 121.7 0.14 1 250 . 55 VAL H H 8.80 0.015 1 251 . 55 VAL C C 179.1 0.08 1 252 . 55 VAL CA C 67.45 0.2 1 253 . 55 VAL CB C 31.50 0.31 1 254 . 55 VAL N N 120.1 0.14 1 255 . 56 ARG H H 7.12 0.015 1 256 . 56 ARG C C 180.7 0.08 1 257 . 56 ARG CA C 59.29 0.2 1 258 . 56 ARG CB C 29.10 0.31 1 259 . 56 ARG N N 116.2 0.14 1 260 . 57 VAL H H 8.28 0.015 1 261 . 57 VAL C C 179.3 0.08 1 262 . 57 VAL CA C 66.07 0.2 1 263 . 57 VAL CB C 30.68 0.31 1 264 . 57 VAL N N 124.1 0.14 1 265 . 58 HIS H H 7.13 0.015 1 266 . 58 HIS C C 178.3 0.08 1 267 . 58 HIS CA C 57.64 0.2 1 268 . 58 HIS CB C 28.65 0.31 1 269 . 58 HIS N N 115.7 0.14 1 270 . 59 THR H H 8.14 0.015 1 271 . 59 THR C C 176.4 0.08 1 272 . 59 THR CA C 63.13 0.2 1 273 . 59 THR CB C 69.88 0.31 1 274 . 59 THR N N 108.4 0.14 1 275 . 60 LYS H H 7.98 0.015 1 276 . 60 LYS C C 175.8 0.08 1 277 . 60 LYS CA C 57.47 0.2 1 278 . 60 LYS CB C 28.95 0.31 1 279 . 60 LYS N N 116.1 0.14 1 280 . 61 GLU H H 7.46 0.015 1 281 . 61 GLU C C 176.7 0.08 1 282 . 61 GLU CA C 57.49 0.2 1 283 . 61 GLU CB C 30.99 0.31 1 284 . 61 GLU N N 120.0 0.14 1 285 . 62 LYS H H 8.42 0.015 1 286 . 62 LYS CA C 53.87 0.2 1 287 . 62 LYS CB C 33.93 0.31 1 288 . 62 LYS N N 124.3 0.14 1 289 . 63 PRO C C 177.0 0.08 1 290 . 63 PRO CA C 63.63 0.2 1 291 . 63 PRO CB C 31.91 0.31 1 292 . 64 PHE H H 7.72 0.015 1 293 . 64 PHE C C 175.1 0.08 1 294 . 64 PHE CA C 57.67 0.2 1 295 . 64 PHE CB C 38.41 0.31 1 296 . 64 PHE N N 117.3 0.14 1 297 . 65 GLU H H 8.44 0.015 1 298 . 65 GLU C C 175.7 0.08 1 299 . 65 GLU CA C 55.66 0.2 1 300 . 65 GLU CB C 31.36 0.31 1 301 . 65 GLU N N 125.1 0.14 1 302 . 66 CYS H H 8.65 0.015 1 303 . 66 CYS C C 175.6 0.08 1 304 . 66 CYS CA C 62.21 0.2 1 305 . 66 CYS CB C 29.71 0.31 1 306 . 66 CYS N N 126.3 0.14 1 307 . 67 ASP H H 8.30 0.015 1 308 . 67 ASP C C 177.0 0.08 1 309 . 67 ASP CA C 54.04 0.2 1 310 . 67 ASP CB C 40.68 0.31 1 311 . 67 ASP N N 127.8 0.14 1 312 . 68 VAL H H 8.36 0.015 1 313 . 68 VAL C C 177.4 0.08 1 314 . 68 VAL CA C 64.21 0.2 1 315 . 68 VAL CB C 31.15 0.31 1 316 . 68 VAL N N 126.1 0.14 1 317 . 69 GLN H H 8.67 0.015 1 318 . 69 GLN C C 177.5 0.08 1 319 . 69 GLN CA C 58.19 0.2 1 320 . 69 GLN CB C 27.96 0.31 1 321 . 69 GLN N N 130.3 0.14 1 322 . 70 GLY H H 9.02 0.015 1 323 . 70 GLY C C 173.6 0.08 1 324 . 70 GLY CA C 45.55 0.2 1 325 . 70 GLY N N 115.0 0.14 1 326 . 71 CYS H H 8.11 0.015 1 327 . 71 CYS C C 175.7 0.08 1 328 . 71 CYS CA C 60.80 0.2 1 329 . 71 CYS CB C 29.73 0.31 1 330 . 71 CYS N N 124.6 0.14 1 331 . 72 GLU H H 8.61 0.015 1 332 . 72 GLU C C 176.9 0.08 1 333 . 72 GLU CA C 56.18 0.2 1 334 . 72 GLU CB C 28.71 0.31 1 335 . 72 GLU N N 120.8 0.14 1 336 . 73 LYS H H 7.88 0.015 1 337 . 73 LYS C C 175.0 0.08 1 338 . 73 LYS CA C 57.06 0.2 1 339 . 73 LYS CB C 32.75 0.31 1 340 . 73 LYS N N 121.4 0.14 1 341 . 74 ALA H H 7.35 0.015 1 342 . 74 ALA C C 175.8 0.08 1 343 . 74 ALA CA C 51.04 0.2 1 344 . 74 ALA CB C 22.89 0.31 1 345 . 74 ALA N N 122.2 0.14 1 346 . 75 PHE H H 8.64 0.015 1 347 . 75 PHE C C 175.6 0.08 1 348 . 75 PHE CA C 57.75 0.2 1 349 . 75 PHE CB C 44.74 0.31 1 350 . 75 PHE N N 115.9 0.14 1 351 . 76 ASN H H 8.85 0.015 1 352 . 76 ASN C C 175.1 0.08 1 353 . 76 ASN CA C 54.26 0.2 1 354 . 76 ASN CB C 39.45 0.31 1 355 . 76 ASN N N 118.0 0.14 1 356 . 77 THR H H 7.33 0.015 1 357 . 77 THR C C 174.2 0.08 1 358 . 77 THR CA C 59.61 0.2 1 359 . 77 THR CB C 74.00 0.31 1 360 . 77 THR N N 104.4 0.14 1 361 . 78 LEU H H 7.55 0.015 1 362 . 78 LEU C C 179.3 0.08 1 363 . 78 LEU CA C 57.36 0.2 1 364 . 78 LEU CB C 40.90 0.31 1 365 . 78 LEU N N 124.6 0.14 1 366 . 79 TYR H H 8.31 0.015 1 367 . 79 TYR C C 177.8 0.08 1 368 . 79 TYR CA C 61.98 0.2 1 369 . 79 TYR CB C 38.15 0.31 1 370 . 79 TYR N N 117.9 0.14 1 371 . 80 ARG H H 7.19 0.015 1 372 . 80 ARG C C 179.4 0.08 1 373 . 80 ARG CA C 58.39 0.2 1 374 . 80 ARG CB C 28.95 0.31 1 375 . 80 ARG N N 115.8 0.14 1 376 . 81 LEU H H 7.09 0.015 1 377 . 81 LEU C C 178.0 0.08 1 378 . 81 LEU CA C 58.49 0.2 1 379 . 81 LEU CB C 39.55 0.31 1 380 . 81 LEU N N 121.8 0.14 1 381 . 82 LYS H H 8.47 0.015 1 382 . 82 LYS C C 180.3 0.08 1 383 . 82 LYS CA C 59.91 0.2 1 384 . 82 LYS CB C 31.94 0.31 1 385 . 82 LYS N N 120.4 0.14 1 386 . 83 ALA H H 8.37 0.015 1 387 . 83 ALA C C 179.4 0.08 1 388 . 83 ALA CA C 55.64 0.2 1 389 . 83 ALA CB C 17.12 0.31 1 390 . 83 ALA N N 122.7 0.14 1 391 . 84 HIS H H 7.11 0.015 1 392 . 84 HIS C C 177.7 0.08 1 393 . 84 HIS CA C 59.55 0.2 1 394 . 84 HIS CB C 28.97 0.31 1 395 . 84 HIS N N 117.0 0.14 1 396 . 85 GLN H H 8.49 0.015 1 397 . 85 GLN C C 178.3 0.08 1 398 . 85 GLN CA C 59.66 0.2 1 399 . 85 GLN CB C 27.63 0.31 1 400 . 85 GLN N N 115.6 0.14 1 401 . 86 ARG H H 7.50 0.015 1 402 . 86 ARG C C 178.9 0.08 1 403 . 86 ARG CA C 59.60 0.2 1 404 . 86 ARG CB C 28.79 0.31 1 405 . 86 ARG N N 120.3 0.14 1 406 . 87 LEU H H 7.77 0.015 1 407 . 87 LEU C C 180.2 0.08 1 408 . 87 LEU CA C 57.11 0.2 1 409 . 87 LEU CB C 40.94 0.31 1 410 . 87 LEU N N 115.2 0.14 1 411 . 88 HIS H H 7.19 0.015 1 412 . 88 HIS C C 177.6 0.08 1 413 . 88 HIS CA C 56.61 0.2 1 414 . 88 HIS CB C 28.78 0.31 1 415 . 88 HIS N N 114.6 0.14 1 416 . 89 THR H H 8.19 0.015 1 417 . 89 THR C C 177.0 0.08 1 418 . 89 THR CA C 62.37 0.2 1 419 . 89 THR CB C 70.67 0.31 1 420 . 89 THR N N 108.8 0.14 1 421 . 90 GLY H H 7.79 0.015 1 422 . 90 GLY C C 175.4 0.08 1 423 . 90 GLY CA C 45.70 0.2 1 424 . 90 GLY N N 110.1 0.14 1 425 . 91 LYS H H 7.54 0.015 1 426 . 91 LYS C C 176.3 0.08 1 427 . 91 LYS CA C 54.47 0.2 1 428 . 91 LYS CB C 29.48 0.31 1 429 . 91 LYS N N 124.6 0.14 1 430 . 92 THR H H 7.25 0.015 1 431 . 92 THR C C 174.0 0.08 1 432 . 92 THR CA C 60.53 0.2 1 433 . 92 THR CB C 70.05 0.31 1 434 . 92 THR N N 108.3 0.14 1 435 . 93 PHE H H 8.80 0.015 1 436 . 93 PHE C C 175.6 0.08 1 437 . 93 PHE CA C 57.63 0.2 1 438 . 93 PHE CB C 39.13 0.31 1 439 . 93 PHE N N 119.0 0.14 1 440 . 94 ASN H H 8.71 0.015 1 441 . 94 ASN C C 174.7 0.08 1 442 . 94 ASN CA C 53.19 0.2 1 443 . 94 ASN CB C 38.76 0.31 1 444 . 94 ASN N N 125.3 0.14 1 445 . 95 CYS H H 8.37 0.015 1 446 . 95 CYS C C 176.8 0.08 1 447 . 95 CYS CA C 61.96 0.2 1 448 . 95 CYS CB C 30.27 0.31 1 449 . 95 CYS N N 125.0 0.14 1 450 . 96 GLU H H 8.76 0.015 1 451 . 96 GLU C C 177.4 0.08 1 452 . 96 GLU CA C 56.31 0.2 1 453 . 96 GLU CB C 30.35 0.31 1 454 . 96 GLU N N 127.4 0.14 1 455 . 97 SER H H 8.92 0.015 1 456 . 97 SER C C 176.1 0.08 1 457 . 97 SER CA C 60.50 0.2 1 458 . 97 SER CB C 63.10 0.31 1 459 . 97 SER N N 121.7 0.14 1 460 . 98 GLN H H 8.59 0.015 1 461 . 98 GLN C C 178.2 0.08 1 462 . 98 GLN CA C 58.19 0.2 1 463 . 98 GLN CB C 28.05 0.31 1 464 . 98 GLN N N 127.8 0.14 1 465 . 99 GLY H H 9.01 0.015 1 466 . 99 GLY C C 173.5 0.08 1 467 . 99 GLY CA C 45.70 0.2 1 468 . 99 GLY N N 115.2 0.14 1 469 . 100 CYS H H 8.01 0.015 1 470 . 100 CYS C C 175.7 0.08 1 471 . 100 CYS CA C 60.13 0.2 1 472 . 100 CYS CB C 31.06 0.31 1 473 . 100 CYS N N 124.6 0.14 1 474 . 101 SER H H 8.73 0.015 1 475 . 101 SER C C 175.6 0.08 1 476 . 101 SER CA C 58.08 0.2 1 477 . 101 SER CB C 64.14 0.31 1 478 . 101 SER N N 121.0 0.14 1 479 . 102 LYS H H 8.41 0.015 1 480 . 102 LYS C C 175.5 0.08 1 481 . 102 LYS CA C 56.71 0.2 1 482 . 102 LYS CB C 32.24 0.31 1 483 . 102 LYS N N 123.1 0.14 1 484 . 103 TYR H H 6.95 0.015 1 485 . 103 TYR C C 173.9 0.08 1 486 . 103 TYR CA C 55.48 0.2 1 487 . 103 TYR CB C 41.46 0.31 1 488 . 103 TYR N N 116.5 0.14 1 489 . 104 PHE H H 8.75 0.015 1 490 . 104 PHE C C 176.5 0.08 1 491 . 104 PHE CA C 57.93 0.2 1 492 . 104 PHE CB C 44.54 0.31 1 493 . 104 PHE N N 115.5 0.14 1 494 . 105 THR H H 9.95 0.015 1 495 . 105 THR C C 174.1 0.08 1 496 . 105 THR CA C 63.00 0.2 1 497 . 105 THR CB C 69.79 0.31 1 498 . 105 THR N N 110.8 0.14 1 499 . 106 THR H H 7.36 0.015 1 500 . 106 THR C C 174.1 0.08 1 501 . 106 THR CA C 60.54 0.2 1 502 . 106 THR CB C 73.49 0.31 1 503 . 106 THR N N 108.3 0.14 1 504 . 107 LEU H H 8.45 0.015 1 505 . 107 LEU C C 179.9 0.08 1 506 . 107 LEU CA C 57.24 0.2 1 507 . 107 LEU CB C 39.88 0.31 1 508 . 107 LEU N N 125.6 0.14 1 509 . 108 SER H H 8.19 0.015 1 510 . 108 SER C C 178.3 0.08 1 511 . 108 SER CA C 61.82 0.2 1 512 . 108 SER CB C 63.05 0.31 1 513 . 108 SER N N 113.5 0.14 1 514 . 109 ASP H H 7.89 0.015 1 515 . 109 ASP C C 178.8 0.08 1 516 . 109 ASP CA C 57.56 0.2 1 517 . 109 ASP CB C 40.35 0.31 1 518 . 109 ASP N N 120.4 0.14 1 519 . 110 LEU H H 7.30 0.015 1 520 . 110 LEU C C 178.3 0.08 1 521 . 110 LEU CA C 58.57 0.2 1 522 . 110 LEU CB C 39.92 0.31 1 523 . 110 LEU N N 123.2 0.14 1 524 . 111 ARG H H 8.76 0.015 1 525 . 111 ARG C C 179.5 0.08 1 526 . 111 ARG CA C 60.59 0.2 1 527 . 111 ARG CB C 29.44 0.31 1 528 . 111 ARG N N 119.3 0.14 1 529 . 112 LYS H H 7.64 0.015 1 530 . 112 LYS C C 179.1 0.08 1 531 . 112 LYS CA C 59.87 0.2 1 532 . 112 LYS CB C 32.49 0.31 1 533 . 112 LYS N N 120.4 0.14 1 534 . 113 HIS H H 7.48 0.015 1 535 . 113 HIS C C 179.0 0.08 1 536 . 113 HIS CA C 59.34 0.2 1 537 . 113 HIS CB C 29.15 0.31 1 538 . 113 HIS N N 120.0 0.14 1 539 . 114 ILE H H 8.88 0.015 1 540 . 114 ILE C C 178.1 0.08 1 541 . 114 ILE CA C 66.13 0.2 1 542 . 114 ILE CB C 37.85 0.31 1 543 . 114 ILE N N 122.8 0.14 1 544 . 115 ARG H H 7.19 0.015 1 545 . 115 ARG C C 180.0 0.08 1 546 . 115 ARG CA C 59.51 0.2 1 547 . 115 ARG CB C 29.42 0.31 1 548 . 115 ARG N N 118.1 0.14 1 549 . 116 THR H H 8.07 0.015 1 550 . 116 THR C C 176.9 0.08 1 551 . 116 THR CA C 64.81 0.2 1 552 . 116 THR CB C 69.05 0.31 1 553 . 116 THR N N 112.9 0.14 1 554 . 117 HIS H H 7.51 0.015 1 555 . 117 HIS C C 177.9 0.08 1 556 . 117 HIS CA C 56.82 0.2 1 557 . 117 HIS CB C 29.12 0.31 1 558 . 117 HIS N N 119.1 0.14 1 559 . 118 THR H H 8.10 0.015 1 560 . 118 THR C C 177.6 0.08 1 561 . 118 THR CA C 63.15 0.2 1 562 . 118 THR CB C 69.89 0.31 1 563 . 118 THR N N 109.7 0.14 1 564 . 119 GLY H H 7.92 0.015 1 565 . 119 GLY C C 174.7 0.08 1 566 . 119 GLY CA C 46.17 0.2 1 567 . 119 GLY N N 109.6 0.14 1 568 . 120 GLU H H 7.73 0.015 1 569 . 120 GLU C C 176.7 0.08 1 570 . 120 GLU CA C 57.88 0.2 1 571 . 120 GLU CB C 30.01 0.31 1 572 . 120 GLU N N 121.2 0.14 1 573 . 121 LYS H H 8.37 0.015 1 574 . 121 LYS CA C 53.87 0.2 1 575 . 121 LYS CB C 34.32 0.31 1 576 . 121 LYS N N 125.6 0.14 1 577 . 122 PRO C C 176.6 0.08 1 578 . 122 PRO CA C 63.63 0.2 1 579 . 123 PHE H H 7.69 0.015 1 580 . 123 PHE C C 175.1 0.08 1 581 . 123 PHE CA C 57.68 0.2 1 582 . 123 PHE CB C 39.04 0.31 1 583 . 123 PHE N N 117.5 0.14 1 584 . 124 ARG H H 8.62 0.015 1 585 . 124 ARG C C 175.3 0.08 1 586 . 124 ARG CA C 55.77 0.2 1 587 . 124 ARG CB C 32.21 0.31 1 588 . 124 ARG N N 125.8 0.14 1 589 . 125 CYS H H 8.87 0.015 1 590 . 125 CYS C C 176.8 0.08 1 591 . 125 CYS CA C 61.28 0.2 1 592 . 125 CYS CB C 30.49 0.31 1 593 . 125 CYS N N 126.9 0.14 1 594 . 126 ASP H H 8.79 0.015 1 595 . 126 ASP C C 176.9 0.08 1 596 . 126 ASP CA C 54.23 0.2 1 597 . 126 ASP CB C 41.29 0.31 1 598 . 126 ASP N N 129.6 0.14 1 599 . 127 HIS H H 9.08 0.015 1 600 . 127 HIS C C 176.9 0.08 1 601 . 127 HIS CA C 58.48 0.2 1 602 . 127 HIS CB C 30.36 0.31 1 603 . 127 HIS N N 125.2 0.14 1 604 . 128 ASP H H 8.41 0.015 1 605 . 128 ASP C C 177.5 0.08 1 606 . 128 ASP CA C 56.64 0.2 1 607 . 128 ASP CB C 40.74 0.31 1 608 . 128 ASP N N 129.0 0.14 1 609 . 129 GLY H H 8.74 0.015 1 610 . 129 GLY C C 174.3 0.08 1 611 . 129 GLY CA C 45.83 0.2 1 612 . 129 GLY N N 113.0 0.14 1 613 . 130 CYS H H 7.88 0.015 1 614 . 130 CYS C C 176.7 0.08 1 615 . 130 CYS CA C 61.31 0.2 1 616 . 130 CYS CB C 29.66 0.31 1 617 . 130 CYS N N 122.9 0.14 1 618 . 131 GLY H H 8.57 0.015 1 619 . 131 GLY C C 178.3 0.08 1 620 . 131 GLY CA C 45.97 0.2 1 621 . 131 GLY N N 106.4 0.14 1 622 . 132 LYS H H 8.16 0.015 1 623 . 132 LYS C C 174.6 0.08 1 624 . 132 LYS CA C 57.96 0.2 1 625 . 132 LYS CB C 33.48 0.31 1 626 . 132 LYS N N 122.6 0.14 1 627 . 133 ALA H H 7.65 0.015 1 628 . 133 ALA C C 175.7 0.08 1 629 . 133 ALA CA C 50.79 0.2 1 630 . 133 ALA CB C 22.53 0.31 1 631 . 133 ALA N N 122.9 0.14 1 632 . 134 PHE H H 8.82 0.015 1 633 . 134 PHE C C 175.6 0.08 1 634 . 134 PHE CA C 57.65 0.2 1 635 . 134 PHE CB C 44.39 0.31 1 636 . 134 PHE N N 116.2 0.14 1 637 . 135 ALA H H 9.61 0.015 1 638 . 135 ALA C C 177.0 0.08 1 639 . 135 ALA CA C 54.34 0.2 1 640 . 135 ALA CB C 20.55 0.31 1 641 . 135 ALA N N 123.1 0.14 1 642 . 136 ALA H H 7.34 0.015 1 643 . 136 ALA C C 177.9 0.08 1 644 . 136 ALA CA C 50.59 0.2 1 645 . 136 ALA CB C 21.60 0.31 1 646 . 136 ALA N N 117.0 0.14 1 647 . 137 SER H H 8.35 0.015 1 648 . 137 SER CA C 61.15 0.2 1 649 . 137 SER CB C 62.70 0.31 1 650 . 137 SER N N 120.0 0.14 1 651 . 138 HIS H H 8.40 0.015 1 652 . 138 HIS C C 177.8 0.08 1 653 . 138 HIS N N 126.0 0.14 1 654 . 139 HIS H H 6.31 0.015 1 655 . 139 HIS C C 179.1 0.08 1 656 . 139 HIS CA C 56.77 0.2 1 657 . 139 HIS N N 119.8 0.14 1 658 . 140 LEU H H 6.82 0.015 1 659 . 140 LEU C C 177.6 0.08 1 660 . 140 LEU CA C 57.95 0.2 1 661 . 140 LEU CB C 40.01 0.31 1 662 . 140 LEU N N 120.8 0.14 1 663 . 141 LYS H H 7.96 0.015 1 664 . 141 LYS C C 179.7 0.08 1 665 . 141 LYS CA C 60.25 0.2 1 666 . 141 LYS CB C 32.23 0.31 1 667 . 141 LYS N N 119.0 0.14 1 668 . 142 THR H H 7.71 0.015 1 669 . 142 THR C C 177.3 0.08 1 670 . 142 THR CA C 66.50 0.2 1 671 . 142 THR CB C 68.70 0.31 1 672 . 142 THR N N 112.9 0.14 1 673 . 143 HIS H H 7.67 0.015 1 674 . 143 HIS C C 179.2 0.08 1 675 . 143 HIS CA C 59.84 0.2 1 676 . 143 HIS CB C 28.61 0.31 1 677 . 143 HIS N N 123.5 0.14 1 678 . 144 VAL H H 8.80 0.015 1 679 . 144 VAL CA C 67.09 0.2 1 680 . 144 VAL CB C 31.77 0.31 1 681 . 144 VAL N N 120.1 0.14 1 682 . 145 ARG H H 7.19 0.015 1 683 . 145 ARG C C 180.0 0.08 1 684 . 145 ARG CA C 59.37 0.2 1 685 . 145 ARG CB C 29.43 0.31 1 686 . 145 ARG N N 118.1 0.14 1 687 . 146 THR H H 8.08 0.015 1 688 . 146 THR C C 176.8 0.08 1 689 . 146 THR CA C 65.06 0.2 1 690 . 146 THR CB C 67.03 0.31 1 691 . 146 THR N N 112.9 0.14 1 692 . 147 HIS H H 7.30 0.015 1 693 . 147 HIS C C 177.6 0.08 1 694 . 147 HIS CA C 56.38 0.2 1 695 . 147 HIS CB C 29.06 0.31 1 696 . 147 HIS N N 118.1 0.14 1 697 . 148 THR H H 7.94 0.015 1 698 . 148 THR C C 177.3 0.08 1 699 . 148 THR CA C 62.74 0.2 1 700 . 148 THR CB C 70.39 0.31 1 701 . 148 THR N N 108.8 0.14 1 702 . 149 GLY H H 8.07 0.015 1 703 . 149 GLY C C 175.4 0.08 1 704 . 149 GLY CA C 45.77 0.2 1 705 . 149 GLY N N 110.2 0.14 1 706 . 150 GLU H H 7.54 0.015 1 707 . 150 GLU CA C 54.44 0.2 1 708 . 150 GLU CB C 29.60 0.31 1 709 . 150 GLU N N 124.8 0.14 1 710 . 152 PRO C C 177.1 0.08 1 711 . 152 PRO CA C 63.66 0.2 1 712 . 153 PHE H H 7.82 0.015 1 713 . 153 PHE C C 175.0 0.08 1 714 . 153 PHE CA C 57.67 0.2 1 715 . 153 PHE CB C 39.03 0.31 1 716 . 153 PHE N N 117.6 0.14 1 717 . 154 PHE H H 8.42 0.015 1 718 . 154 PHE C C 174.4 0.08 1 719 . 154 PHE CA C 55.96 0.2 1 720 . 154 PHE CB C 40.92 0.31 1 721 . 154 PHE N N 123.5 0.14 1 722 . 155 CYS H H 8.40 0.015 1 723 . 155 CYS CA C 57.94 0.2 1 724 . 155 CYS CB C 30.97 0.31 1 725 . 155 CYS N N 125.9 0.14 1 726 . 156 PRO C C 177.8 0.08 1 727 . 156 PRO CA C 63.57 0.2 1 728 . 157 SER H H 8.80 0.015 1 729 . 157 SER C C 176.3 0.08 1 730 . 157 SER CA C 60.36 0.2 1 731 . 157 SER CB C 63.18 0.31 1 732 . 157 SER N N 121.8 0.14 1 733 . 158 ASN H H 8.66 0.015 1 734 . 158 ASN C C 177.3 0.08 1 735 . 158 ASN CA C 55.95 0.2 1 736 . 158 ASN CB C 38.54 0.31 1 737 . 158 ASN N N 127.2 0.14 1 738 . 159 GLY H H 9.06 0.015 1 739 . 159 GLY C C 173.6 0.08 1 740 . 159 GLY CA C 45.73 0.2 1 741 . 159 GLY N N 115.2 0.14 1 742 . 160 CYS H H 7.90 0.015 1 743 . 160 CYS C C 176.8 0.08 1 744 . 160 CYS CA C 61.00 0.2 1 745 . 160 CYS CB C 30.42 0.31 1 746 . 160 CYS N N 124.2 0.14 1 747 . 161 GLU C C 176.8 0.08 1 748 . 161 GLU CA C 56.37 0.2 1 749 . 162 LYS H H 8.03 0.015 1 750 . 162 LYS C C 175.7 0.08 1 751 . 162 LYS CA C 57.63 0.2 1 752 . 162 LYS CB C 33.14 0.31 1 753 . 162 LYS N N 121.7 0.14 1 754 . 163 THR H H 7.36 0.015 1 755 . 163 THR C C 174.3 0.08 1 756 . 163 THR CA C 59.43 0.2 1 757 . 163 THR CB C 71.84 0.31 1 758 . 163 THR N N 110.1 0.14 1 759 . 164 PHE H H 8.80 0.015 1 760 . 164 PHE C C 176.0 0.08 1 761 . 164 PHE CA C 58.12 0.2 1 762 . 164 PHE CB C 44.41 0.31 1 763 . 164 PHE N N 116.9 0.14 1 764 . 165 SER H H 9.63 0.015 1 765 . 165 SER C C 174.6 0.08 1 766 . 165 SER CA C 60.57 0.2 1 767 . 165 SER CB C 64.72 0.31 1 768 . 165 SER N N 115.9 0.14 1 769 . 166 THR H H 7.27 0.015 1 770 . 166 THR C C 174.1 0.08 1 771 . 166 THR CA C 59.65 0.2 1 772 . 166 THR CB C 73.38 0.31 1 773 . 166 THR N N 107.1 0.14 1 774 . 167 GLN H H 8.43 0.015 1 775 . 167 GLN C C 178.4 0.08 1 776 . 167 GLN CA C 58.36 0.2 1 777 . 167 GLN CB C 27.78 0.31 1 778 . 167 GLN N N 122.8 0.14 1 779 . 168 TYR H H 8.36 0.015 1 780 . 168 TYR CA C 62.00 0.2 1 781 . 168 TYR CB C 38.42 0.31 1 782 . 168 TYR N N 120.0 0.14 1 783 . 169 SER C C 177.3 0.08 1 784 . 169 SER CA C 62.42 0.2 4 785 . 169 SER CB C 62.42 0.31 4 786 . 170 LEU H H 7.11 0.015 1 787 . 170 LEU CA C 58.29 0.2 1 788 . 170 LEU CB C 40.08 0.31 1 789 . 170 LEU N N 124.5 0.14 1 790 . 171 LYS C C 180.1 0.08 1 791 . 171 LYS CA C 60.17 0.2 1 792 . 171 LYS CB C 31.53 0.31 1 793 . 172 SER H H 7.76 0.015 1 794 . 172 SER C C 177.7 0.08 1 795 . 172 SER CA C 61.47 0.2 1 796 . 172 SER CB C 62.54 0.31 1 797 . 172 SER N N 113.8 0.14 1 798 . 173 HIS H H 7.80 0.015 1 799 . 173 HIS C C 178.5 0.08 1 800 . 173 HIS CA C 59.12 0.2 1 801 . 173 HIS CB C 28.47 0.31 1 802 . 173 HIS N N 121.1 0.14 1 803 . 174 MET H H 8.40 0.015 1 804 . 174 MET C C 178.4 0.08 1 805 . 174 MET CA C 58.86 0.2 1 806 . 174 MET CB C 31.59 0.31 1 807 . 174 MET N N 118.1 0.14 1 808 . 175 LYS H H 7.16 0.015 1 809 . 175 LYS C C 177.7 0.08 1 810 . 175 LYS CA C 58.63 0.2 1 811 . 175 LYS CB C 31.96 0.31 1 812 . 175 LYS N N 118.1 0.14 1 813 . 176 GLY H H 7.58 0.015 1 814 . 176 GLY C C 174.9 0.08 1 815 . 176 GLY CA C 45.36 0.2 1 816 . 176 GLY N N 105.1 0.14 1 817 . 177 HIS H H 7.11 0.015 1 818 . 177 HIS CA C 57.87 0.2 1 819 . 177 HIS CB C 30.17 0.31 1 820 . 177 HIS N N 124.5 0.14 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 178,34 179,35 180,36 181,37 785,784 stop_ save_