data_7093 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignment of monomeric chorimate mutase from methanococcus jannaschii in a complex with a transition state analog ; _BMRB_accession_number 7093 _BMRB_flat_file_name bmr7093.str _Entry_type original _Submission_date 2006-05-02 _Accession_date 2006-05-02 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'chemical shift assignments of the protein, the free and bound transition state analog' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vogeli Beat R. . 2 Pervushin Konstantin . . 3 Vamvaca Katherina . . 4 Hilvert Donald . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 519 "13C chemical shifts" 279 "15N chemical shifts" 101 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-15 update BMRB 'complete entry citation' 2007-11-21 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_paper_mMjCM _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structure and dynamics of a molten globular enzyme' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17994104 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pervushin Konstantin . . 2 Vamvaca Katherina . . 3 Vogeli Beat . . 4 Hilvert Donald . . stop_ _Journal_abbreviation 'Nat. Struct. Mol. Biol.' _Journal_volume 14 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1202 _Page_last 1206 _Year 2007 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'mMjCM in complex with a TSA' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label mMjCM $mMjCM TSA $TSA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_mMjCM _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'monomeric chorismate mutase from methanococcus jannaschii' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 104 _Mol_residue_sequence ; MIEKLAEIRKKIDEIDNKIL KARWPWAEKLIAERNSLAKD VAEIKNQLGIPINDPEREKY IYDRIRKLCKEHNVDENIGI KIFQRLIEHNKALQKQYLEE TLEH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ILE 3 GLU 4 LYS 5 LEU 6 ALA 7 GLU 8 ILE 9 ARG 10 LYS 11 LYS 12 ILE 13 ASP 14 GLU 15 ILE 16 ASP 17 ASN 18 LYS 19 ILE 20 LEU 21 LYS 22 ALA 23 ARG 24 TRP 25 PRO 26 TRP 27 ALA 28 GLU 29 LYS 30 LEU 31 ILE 32 ALA 33 GLU 34 ARG 35 ASN 36 SER 37 LEU 38 ALA 39 LYS 40 ASP 41 VAL 42 ALA 43 GLU 44 ILE 45 LYS 46 ASN 47 GLN 48 LEU 49 GLY 50 ILE 51 PRO 52 ILE 53 ASN 54 ASP 55 PRO 56 GLU 57 ARG 58 GLU 59 LYS 60 TYR 61 ILE 62 TYR 63 ASP 64 ARG 65 ILE 66 ARG 67 LYS 68 LEU 69 CYS 70 LYS 71 GLU 72 HIS 73 ASN 74 VAL 75 ASP 76 GLU 77 ASN 78 ILE 79 GLY 80 ILE 81 LYS 82 ILE 83 PHE 84 GLN 85 ARG 86 LEU 87 ILE 88 GLU 89 HIS 90 ASN 91 LYS 92 ALA 93 LEU 94 GLN 95 LYS 96 GLN 97 TYR 98 LEU 99 GLU 100 GLU 101 THR 102 LEU 103 GLU 104 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-05-12 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 17093 mMjCM 100.00 104 100.00 100.00 9.76e-66 PDB 2GTV "Nmr Structure Of Monomeric Chorismate Mutase From Methanococcus Jannaschii" 100.00 104 100.00 100.00 9.76e-66 stop_ save_ ############# # Ligands # ############# save_TSA _Saveframe_category ligand _Mol_type non-polymer _Name_common "TSA (8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC ACID)" _BMRB_code . _PDB_code TSA _Molecular_mass 228.199 _Mol_charge 0 _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 Oct 4 15:31:47 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? O5 O5 O . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? O7 O7 O . 0 . ? C8 C8 C . 0 . ? C9 C9 C . 0 . ? C10 C10 C . 0 . ? O1 O1 O . 0 . ? O2 O2 O . 0 . ? C11 C11 C . 0 . ? O3 O3 O . 0 . ? O4 O4 O . 0 . ? H2 H2 H . 0 . ? H3 H3 H . 0 . ? H4 H4 H . 0 . ? HO5 HO5 H . 0 . ? H5 H5 H . 0 . ? H61 H61 H . 0 . ? H62 H62 H . 0 . ? H8 H8 H . 0 . ? H91 H91 H . 0 . ? H92 H92 H . 0 . ? HO2 HO2 H . 0 . ? HO4 HO4 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING C1 C2 ? ? SING C1 C6 ? ? SING C1 C9 ? ? SING C1 C10 ? ? DOUB C2 C3 ? ? SING C2 H2 ? ? SING C3 C4 ? ? SING C3 H3 ? ? SING C4 O5 ? ? SING C4 C5 ? ? SING C4 H4 ? ? SING O5 HO5 ? ? SING C5 C6 ? ? SING C5 O7 ? ? SING C5 H5 ? ? SING C6 H61 ? ? SING C6 H62 ? ? SING O7 C8 ? ? SING C8 C9 ? ? SING C8 C11 ? ? SING C8 H8 ? ? SING C9 H91 ? ? SING C9 H92 ? ? DOUB C10 O1 ? ? SING C10 O2 ? ? SING O2 HO2 ? ? DOUB C11 O3 ? ? SING C11 O4 ? ? SING O4 HO4 ? ? 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 $mMjCM 'Methanococcus jannaschii' 2190 Archaea . Methanococcus jannaschii 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 $mMjCM 'recombinant technology' 'escherichia coli' . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'mMjCM in complex with TSA low concentration' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $assembly 0.07 mM [U-15N] stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details 'mMjCM in complex with TSA high concentration' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $assembly 0.6 mM '[U-13C; U-15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_900MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ save_600MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_standard_suite_for_NMR_assignment_procedure_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'standard suite for NMR assignment procedure' _Sample_label . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0 pH temperature 293 0 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl carbons' ppm 0 internal indirect . . . 1.0 $paper_mMjCM $paper_mMjCM DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.0 $paper_mMjCM $paper_mMjCM DSS N 15 nitrogen ppm 0 internal indirect . . . 1.0 $paper_mMjCM $paper_mMjCM stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_list_1_1 _Saveframe_category assigned_chemical_shifts _Details ; TSA free 3000 6.06 H2 3001 5.73 H3 3002 4.30 H4 3003 4.13 H5 3004 1.91 1H6 3005 1.91 2H6 3006 4.18 H8 3007 2.09 1H9 3008 2.20 2H9 ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name mMjCM _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 3 GLU H H 9.360 0.020 1 2 3 3 GLU HA H 4.157 0.020 1 3 3 3 GLU HB2 H 2.364 0.020 2 4 3 3 GLU HB3 H 2.286 0.020 2 5 3 3 GLU CA C 58.937 0.400 1 6 3 3 GLU CB C 35.691 0.400 1 7 3 3 GLU N N 126.963 0.400 1 8 4 4 LYS H H 8.250 0.020 1 9 4 4 LYS N N 120.801 0.400 1 10 5 5 LEU H H 7.688 0.020 1 11 5 5 LEU HA H 4.152 0.020 1 12 5 5 LEU HB2 H 1.999 0.020 2 13 5 5 LEU HB3 H 1.285 0.020 2 14 5 5 LEU HG H 1.998 0.020 1 15 5 5 LEU HD1 H 0.827 0.020 2 16 5 5 LEU HD2 H 0.825 0.020 2 17 5 5 LEU CA C 56.540 0.400 1 18 5 5 LEU CB C 41.250 0.400 1 19 5 5 LEU CG C 31.173 0.400 1 20 5 5 LEU CD1 C 25.266 0.400 1 21 5 5 LEU CD2 C 25.266 0.400 1 22 5 5 LEU N N 120.596 0.400 1 23 6 6 ALA H H 7.770 0.020 1 24 6 6 ALA HA H 3.940 0.020 1 25 6 6 ALA HB H 1.459 0.020 1 26 6 6 ALA CA C 54.769 0.400 1 27 6 6 ALA CB C 17.236 0.400 1 28 6 6 ALA N N 122.146 0.400 1 29 7 7 GLU H H 7.959 0.020 1 30 7 7 GLU HA H 4.000 0.020 1 31 7 7 GLU HB2 H 2.146 0.020 1 32 7 7 GLU HB3 H 2.146 0.020 1 33 7 7 GLU HG2 H 2.385 0.020 1 34 7 7 GLU HG3 H 2.385 0.020 1 35 7 7 GLU CA C 58.946 0.400 1 36 7 7 GLU CB C 29.088 0.400 1 37 7 7 GLU CG C 35.691 0.400 1 38 7 7 GLU N N 119.454 0.400 1 39 8 8 ILE H H 7.932 0.020 1 40 8 8 ILE HA H 3.784 0.020 1 41 8 8 ILE HB H 1.806 0.020 1 42 8 8 ILE HG12 H 1.184 0.020 2 43 8 8 ILE HG2 H 0.931 0.020 1 44 8 8 ILE HD1 H 0.793 0.020 1 45 8 8 ILE CA C 64.146 0.400 1 46 8 8 ILE CB C 37.403 0.400 1 47 8 8 ILE CG1 C 29.088 0.400 1 48 8 8 ILE CG2 C 18.316 0.400 1 49 8 8 ILE CD1 C 13.763 0.400 1 50 8 8 ILE N N 122.206 0.400 1 51 9 9 ARG H H 8.290 0.020 1 52 9 9 ARG HA H 3.828 0.020 1 53 9 9 ARG HB2 H 1.887 0.020 2 54 9 9 ARG HB3 H 1.822 0.020 2 55 9 9 ARG HG2 H 1.642 0.020 2 56 9 9 ARG HG3 H 1.293 0.020 2 57 9 9 ARG HD2 H 2.883 0.020 2 58 9 9 ARG HD3 H 2.610 0.020 2 59 9 9 ARG HE H 9.423 0.020 1 60 9 9 ARG HH21 H 7.736 0.020 2 61 9 9 ARG HH22 H 10.175 0.020 2 62 9 9 ARG CA C 59.979 0.400 1 63 9 9 ARG CB C 32.216 0.400 1 64 9 9 ARG CG C 28.036 0.400 1 65 9 9 ARG CD C 44.030 0.400 1 66 9 9 ARG N N 120.859 0.400 1 67 9 9 ARG NE N 84.925 0.400 1 68 9 9 ARG NH2 N 76.511 0.400 1 69 10 10 LYS H H 7.777 0.020 1 70 10 10 LYS HA H 3.999 0.020 1 71 10 10 LYS HB2 H 1.933 0.020 1 72 10 10 LYS HB3 H 1.933 0.020 1 73 10 10 LYS HE2 H 2.938 0.020 1 74 10 10 LYS HE3 H 2.938 0.020 1 75 10 10 LYS CA C 58.937 0.400 1 76 10 10 LYS CB C 31.521 0.400 1 77 10 10 LYS CE C 41.571 0.400 1 78 10 10 LYS N N 120.929 0.400 1 79 11 11 LYS H H 7.401 0.020 1 80 11 11 LYS HA H 4.110 0.020 1 81 11 11 LYS HB2 H 2.122 0.020 1 82 11 11 LYS HB3 H 2.122 0.020 1 83 11 11 LYS HG2 H 1.626 0.020 2 84 11 11 LYS HG3 H 1.444 0.020 2 85 11 11 LYS HD2 H 1.634 0.020 1 86 11 11 LYS HD3 H 1.634 0.020 1 87 11 11 LYS HE2 H 2.920 0.020 1 88 11 11 LYS HE3 H 2.920 0.020 1 89 11 11 LYS CA C 58.972 0.400 1 90 11 11 LYS CB C 31.173 0.400 1 91 11 11 LYS CG C 24.918 0.400 1 92 11 11 LYS CD C 28.741 0.400 1 93 11 11 LYS CE C 41.945 0.400 1 94 11 11 LYS N N 121.273 0.400 1 95 12 12 ILE H H 8.403 0.020 1 96 12 12 ILE HA H 3.471 0.020 1 97 12 12 ILE HB H 1.819 0.020 1 98 12 12 ILE HG12 H 1.954 0.020 2 99 12 12 ILE HG13 H 1.040 0.020 2 100 12 12 ILE HG2 H 1.037 0.020 1 101 12 12 ILE HD1 H 0.754 0.020 1 102 12 12 ILE CA C 65.906 0.400 1 103 12 12 ILE CB C 37.776 0.400 1 104 12 12 ILE CG2 C 16.542 0.400 1 105 12 12 ILE CD1 C 12.326 0.400 1 106 12 12 ILE N N 122.726 0.400 1 107 13 13 ASP H H 8.531 0.020 1 108 13 13 ASP HA H 4.539 0.020 1 109 13 13 ASP HB2 H 2.969 0.020 2 110 13 13 ASP HB3 H 2.523 0.020 2 111 13 13 ASP CA C 56.540 0.400 1 112 13 13 ASP CB C 39.165 0.400 1 113 13 13 ASP N N 120.031 0.400 1 114 14 14 GLU H H 7.602 0.020 1 115 14 14 GLU HA H 4.148 0.020 1 116 14 14 GLU HB2 H 2.169 0.020 1 117 14 14 GLU HB3 H 2.169 0.020 1 118 14 14 GLU HG2 H 2.455 0.020 2 119 14 14 GLU HG3 H 2.263 0.020 2 120 14 14 GLU CA C 58.625 0.400 1 121 14 14 GLU CG C 35.691 0.400 1 122 14 14 GLU N N 120.328 0.400 1 123 15 15 ILE H H 8.079 0.020 1 124 15 15 ILE HA H 3.574 0.020 1 125 15 15 ILE HB H 2.013 0.020 1 126 15 15 ILE HG12 H 1.777 0.020 2 127 15 15 ILE HG13 H 0.987 0.020 2 128 15 15 ILE HG2 H 0.986 0.020 1 129 15 15 ILE HD1 H 0.734 0.020 1 130 15 15 ILE CA C 65.228 0.400 1 131 15 15 ILE CB C 38.123 0.400 1 132 15 15 ILE CG1 C 29.436 0.400 1 133 15 15 ILE CG2 C 17.621 0.400 1 134 15 15 ILE CD1 C 14.146 0.400 1 135 15 15 ILE N N 124.300 0.400 1 136 16 16 ASP H H 9.367 0.020 1 137 16 16 ASP HA H 4.574 0.020 1 138 16 16 ASP HB2 H 2.564 0.020 2 139 16 16 ASP HB3 H 2.118 0.020 2 140 16 16 ASP CA C 58.277 0.400 1 141 16 16 ASP CB C 39.165 0.400 1 142 16 16 ASP N N 125.542 0.400 1 143 17 17 ASN H H 7.650 0.020 1 144 17 17 ASN HA H 4.253 0.020 1 145 17 17 ASN HB2 H 2.845 0.020 1 146 17 17 ASN HB3 H 2.845 0.020 1 147 17 17 ASN HD21 H 7.484 0.020 2 148 17 17 ASN HD22 H 7.018 0.020 2 149 17 17 ASN CA C 55.498 0.400 1 150 17 17 ASN CB C 38.470 0.400 1 151 17 17 ASN N N 116.538 0.400 1 152 17 17 ASN ND2 N 112.604 0.400 1 153 18 18 LYS H H 7.615 0.020 1 154 18 18 LYS HA H 3.912 0.020 1 155 18 18 LYS HB2 H 1.852 0.020 1 156 18 18 LYS HB3 H 1.852 0.020 1 157 18 18 LYS HG2 H 1.841 0.020 2 158 18 18 LYS HG3 H 1.385 0.020 2 159 18 18 LYS HD2 H 2.164 0.020 1 160 18 18 LYS HD3 H 2.164 0.020 1 161 18 18 LYS HE2 H 2.932 0.020 1 162 18 18 LYS HE3 H 2.932 0.020 1 163 18 18 LYS CA C 59.667 0.400 1 164 18 18 LYS CB C 33.258 0.400 1 165 18 18 LYS CG C 25.961 0.400 1 166 18 18 LYS CD C 28.741 0.400 1 167 18 18 LYS CE C 41.945 0.400 1 168 18 18 LYS N N 118.747 0.400 1 169 19 19 ILE H H 9.084 0.020 1 170 19 19 ILE HA H 3.442 0.020 1 171 19 19 ILE HB H 2.198 0.020 1 172 19 19 ILE HG12 H 2.084 0.020 2 173 19 19 ILE HG13 H 2.001 0.020 2 174 19 19 ILE HG2 H 0.792 0.020 1 175 19 19 ILE HD1 H 0.634 0.020 1 176 19 19 ILE CA C 65.909 0.400 1 177 19 19 ILE CB C 37.776 0.400 1 178 19 19 ILE CG1 C 31.521 0.400 1 179 19 19 ILE CG2 C 13.763 0.400 1 180 19 19 ILE CD1 C 16.578 0.400 1 181 19 19 ILE N N 122.977 0.400 1 182 20 20 LEU H H 7.809 0.020 1 183 20 20 LEU HA H 4.165 0.020 1 184 20 20 LEU HB2 H 1.856 0.020 2 185 20 20 LEU HB3 H 1.640 0.020 2 186 20 20 LEU HG H 1.885 0.020 1 187 20 20 LEU HD1 H 1.031 0.020 2 188 20 20 LEU HD2 H 1.032 0.020 2 189 20 20 LEU CA C 57.235 0.400 1 190 20 20 LEU CB C 41.945 0.400 1 191 20 20 LEU CG C 27.351 0.400 1 192 20 20 LEU CD1 C 24.918 0.400 1 193 20 20 LEU CD2 C 24.918 0.400 1 194 20 20 LEU N N 118.995 0.400 1 195 22 22 ALA H H 7.938 0.020 1 196 22 22 ALA HA H 4.160 0.020 1 197 22 22 ALA HB H 1.512 0.020 1 198 22 22 ALA CA C 54.769 0.400 1 199 22 22 ALA CB C 17.236 0.400 1 200 22 22 ALA N N 121.003 0.400 1 201 23 23 ARG H H 7.736 0.020 1 202 23 23 ARG HA H 4.001 0.020 1 203 23 23 ARG HB2 H 2.064 0.020 1 204 23 23 ARG HB3 H 2.064 0.020 1 205 23 23 ARG HE H 7.261 0.020 1 206 23 23 ARG CA C 58.955 0.400 1 207 23 23 ARG CB C 29.436 0.400 1 208 23 23 ARG N N 121.678 0.400 1 209 23 23 ARG NE N 85.745 0.400 1 210 24 24 TRP H H 8.307 0.020 1 211 24 24 TRP HA H 3.612 0.020 1 212 24 24 TRP HB2 H 3.423 0.020 2 213 24 24 TRP HB3 H 3.236 0.020 2 214 24 24 TRP HD1 H 7.309 0.020 1 215 24 24 TRP HE1 H 10.335 0.020 1 216 24 24 TRP HE3 H 7.663 0.020 1 217 24 24 TRP HZ2 H 7.471 0.020 1 218 24 24 TRP HZ3 H 7.103 0.020 1 219 24 24 TRP HH2 H 7.201 0.020 1 220 24 24 TRP CA C 59.667 0.400 1 221 24 24 TRP CB C 25.613 0.400 1 222 24 24 TRP CD1 C 126.730 0.400 1 223 24 24 TRP CE3 C 120.626 0.400 1 224 24 24 TRP CZ2 C 113.828 0.400 1 225 24 24 TRP CZ3 C 120.626 0.400 1 226 24 24 TRP CH2 C 123.517 0.400 1 227 24 24 TRP N N 124.172 0.400 1 228 24 24 TRP NE1 N 130.367 0.400 1 229 26 26 TRP HD1 H 7.248 0.020 1 230 26 26 TRP HE1 H 10.287 0.020 1 231 26 26 TRP HE3 H 7.339 0.020 1 232 26 26 TRP HZ2 H 7.423 0.020 1 233 26 26 TRP HZ3 H 6.995 0.020 1 234 26 26 TRP HH2 H 7.139 0.020 1 235 26 26 TRP CD1 C 126.017 0.400 1 236 26 26 TRP CE3 C 119.688 0.400 1 237 26 26 TRP CZ2 C 113.828 0.400 1 238 26 26 TRP CZ3 C 121.095 0.400 1 239 26 26 TRP CH2 C 123.673 0.400 1 240 26 26 TRP NE1 N 131.409 0.400 1 241 27 27 ALA HA H 4.324 0.020 1 242 27 27 ALA HB H 1.451 0.020 1 243 27 27 ALA CA C 52.370 0.400 1 244 27 27 ALA CB C 19.358 0.400 1 245 30 30 LEU HD1 H 0.909 0.020 2 246 30 30 LEU HD2 H 0.759 0.020 2 247 31 31 ILE HG2 H 0.216 0.020 1 248 31 31 ILE CG2 C 15.883 0.400 1 249 33 33 GLU H H 8.298 0.020 1 250 33 33 GLU HB2 H 1.972 0.020 1 251 33 33 GLU HB3 H 1.972 0.020 1 252 33 33 GLU CB C 31.521 0.400 1 253 34 34 ARG HE H 7.136 0.020 1 254 34 34 ARG NE N 84.925 0.400 1 255 35 35 ASN H H 8.549 0.020 1 256 35 35 ASN HD21 H 7.221 0.020 2 257 35 35 ASN HD22 H 6.647 0.020 2 258 35 35 ASN N N 115.768 0.400 1 259 35 35 ASN ND2 N 111.598 0.400 1 260 36 36 SER H H 8.309 0.020 1 261 36 36 SER HA H 4.277 0.020 1 262 36 36 SER HB2 H 4.085 0.020 2 263 36 36 SER HB3 H 4.051 0.020 2 264 36 36 SER CA C 61.057 0.400 1 265 36 36 SER CB C 62.447 0.400 1 266 36 36 SER N N 118.770 0.400 1 267 37 37 LEU H H 7.215 0.020 1 268 37 37 LEU HA H 4.466 0.020 1 269 37 37 LEU HB2 H 1.984 0.020 2 270 37 37 LEU HB3 H 1.425 0.020 2 271 37 37 LEU HG H 1.893 0.020 1 272 37 37 LEU HD1 H 0.890 0.020 2 273 37 37 LEU HD2 H 0.816 0.020 2 274 37 37 LEU CA C 55.498 0.400 1 275 37 37 LEU CB C 40.903 0.400 1 276 37 37 LEU CG C 26.308 0.400 1 277 37 37 LEU CD1 C 22.486 0.400 1 278 37 37 LEU CD2 C 26.308 0.400 1 279 37 37 LEU N N 120.901 0.400 1 280 38 38 ALA H H 7.695 0.020 1 281 38 38 ALA HA H 4.042 0.020 1 282 38 38 ALA HB H 1.542 0.020 1 283 38 38 ALA CA C 55.131 0.400 1 284 38 38 ALA CB C 20.054 0.400 1 285 38 38 ALA N N 122.111 0.400 1 286 39 39 LYS H H 7.498 0.020 1 287 39 39 LYS HA H 3.301 0.020 1 288 39 39 LYS HB2 H 1.468 0.020 2 289 39 39 LYS HB3 H 1.376 0.020 2 290 39 39 LYS HG2 H 1.026 0.020 2 291 39 39 LYS HG3 H 0.994 0.020 2 292 39 39 LYS HD2 H 2.178 0.020 2 293 39 39 LYS HD3 H 1.496 0.020 2 294 39 39 LYS HE2 H 2.911 0.020 1 295 39 39 LYS HE3 H 2.911 0.020 1 296 39 39 LYS CA C 58.972 0.400 1 297 39 39 LYS CB C 31.173 0.400 1 298 39 39 LYS CG C 23.528 0.400 1 299 39 39 LYS CD C 29.088 0.400 1 300 39 39 LYS CE C 41.571 0.400 1 301 39 39 LYS N N 116.872 0.400 1 302 40 40 ASP H H 7.301 0.020 1 303 40 40 ASP HA H 4.220 0.020 1 304 40 40 ASP HB2 H 2.661 0.020 2 305 40 40 ASP HB3 H 2.499 0.020 2 306 40 40 ASP CA C 56.192 0.400 1 307 40 40 ASP CB C 40.208 0.400 1 308 40 40 ASP N N 119.593 0.400 1 309 41 41 VAL H H 8.297 0.020 1 310 41 41 VAL HA H 3.455 0.020 1 311 41 41 VAL HB H 1.997 0.020 1 312 41 41 VAL HG1 H 0.931 0.020 2 313 41 41 VAL HG2 H 0.825 0.020 2 314 41 41 VAL CA C 65.918 0.400 1 315 41 41 VAL CB C 31.173 0.400 1 316 41 41 VAL CG1 C 18.316 0.400 1 317 41 41 VAL CG2 C 21.443 0.400 1 318 41 41 VAL N N 119.171 0.400 1 319 42 42 ALA H H 8.412 0.020 1 320 42 42 ALA HA H 4.034 0.020 1 321 42 42 ALA HB H 1.567 0.020 1 322 42 42 ALA CA C 55.125 0.400 1 323 42 42 ALA CB C 18.278 0.400 1 324 42 42 ALA N N 123.572 0.400 1 325 43 43 GLU H H 7.827 0.020 1 326 43 43 GLU HA H 4.070 0.020 1 327 43 43 GLU HB2 H 2.166 0.020 2 328 43 43 GLU HB3 H 1.766 0.020 2 329 43 43 GLU HG2 H 1.866 0.020 1 330 43 43 GLU HG3 H 1.866 0.020 1 331 43 43 GLU CA C 59.320 0.400 1 332 43 43 GLU CB C 30.826 0.400 1 333 43 43 GLU CG C 37.751 0.400 1 334 43 43 GLU N N 117.496 0.400 1 335 44 44 ILE H H 7.344 0.020 1 336 44 44 ILE HA H 3.863 0.020 1 337 44 44 ILE HB H 1.871 0.020 1 338 44 44 ILE HG12 H 1.138 0.020 2 339 44 44 ILE HG2 H 0.867 0.020 1 340 44 44 ILE HD1 H 0.792 0.020 1 341 44 44 ILE CA C 63.452 0.400 1 342 44 44 ILE CB C 37.751 0.400 1 343 44 44 ILE CG1 C 28.741 0.400 1 344 44 44 ILE CG2 C 18.316 0.400 1 345 44 44 ILE CD1 C 13.763 0.400 1 346 44 44 ILE N N 120.066 0.400 1 347 45 45 LYS H H 8.644 0.020 1 348 45 45 LYS HA H 3.745 0.020 1 349 45 45 LYS HB2 H 2.169 0.020 2 350 45 45 LYS HB3 H 1.757 0.020 2 351 45 45 LYS HG2 H 1.664 0.020 2 352 45 45 LYS HG3 H 0.913 0.020 2 353 45 45 LYS CA C 60.710 0.400 1 354 45 45 LYS CB C 30.826 0.400 1 355 45 45 LYS CG C 27.351 0.400 1 356 45 45 LYS N N 120.687 0.400 1 357 46 46 ASN H H 8.662 0.020 1 358 46 46 ASN HA H 4.512 0.020 1 359 46 46 ASN HB2 H 2.910 0.020 1 360 46 46 ASN HB3 H 2.910 0.020 1 361 46 46 ASN HD21 H 8.022 0.020 2 362 46 46 ASN HD22 H 7.052 0.020 2 363 46 46 ASN CB C 39.165 0.400 1 364 46 46 ASN N N 117.451 0.400 1 365 46 46 ASN ND2 N 115.666 0.400 1 366 47 47 GLN H H 7.716 0.020 1 367 47 47 GLN HA H 4.041 0.020 1 368 47 47 GLN HB2 H 2.294 0.020 2 369 47 47 GLN HB3 H 2.198 0.020 2 370 47 47 GLN HG2 H 2.613 0.020 2 371 47 47 GLN HG3 H 2.445 0.020 2 372 47 47 GLN HE21 H 7.591 0.020 2 373 47 47 GLN HE22 H 6.785 0.020 2 374 47 47 GLN CA C 58.277 0.400 1 375 47 47 GLN CB C 28.046 0.400 1 376 47 47 GLN CG C 33.606 0.400 1 377 47 47 GLN N N 119.142 0.400 1 378 47 47 GLN NE2 N 112.714 0.400 1 379 48 48 LEU H H 7.943 0.020 1 380 48 48 LEU HA H 4.352 0.020 1 381 48 48 LEU HB2 H 1.714 0.020 2 382 48 48 LEU HB3 H 1.638 0.020 2 383 48 48 LEU HG H 1.825 0.020 1 384 48 48 LEU HD1 H 0.829 0.020 2 385 48 48 LEU HD2 H 0.709 0.020 2 386 48 48 LEU CA C 54.786 0.400 1 387 48 48 LEU CB C 43.335 0.400 1 388 48 48 LEU CG C 26.308 0.400 1 389 48 48 LEU CD1 C 25.961 0.400 1 390 48 48 LEU CD2 C 25.613 0.400 1 391 48 48 LEU N N 117.191 0.400 1 392 49 49 GLY H H 7.982 0.020 1 393 49 49 GLY HA2 H 3.946 0.020 1 394 49 49 GLY HA3 H 3.946 0.020 1 395 49 49 GLY CA C 46.115 0.400 1 396 49 49 GLY N N 111.444 0.400 1 397 50 50 ILE H H 7.803 0.020 1 398 50 50 ILE HA H 3.746 0.020 1 399 50 50 ILE HB H 1.733 0.020 1 400 50 50 ILE HG12 H 1.439 0.020 2 401 50 50 ILE HG13 H 1.033 0.020 2 402 50 50 ILE HG2 H 0.968 0.020 1 403 50 50 ILE HD1 H 0.831 0.020 1 404 50 50 ILE CA C 60.710 0.400 1 405 50 50 ILE CB C 39.165 0.400 1 406 50 50 ILE CG1 C 25.961 0.400 1 407 50 50 ILE CG2 C 16.231 0.400 1 408 50 50 ILE CD1 C 13.451 0.400 1 409 50 50 ILE N N 119.446 0.400 1 410 51 51 PRO HA H 4.428 0.020 1 411 51 51 PRO HB2 H 2.389 0.020 2 412 51 51 PRO HB3 H 2.014 0.020 2 413 51 51 PRO HG2 H 2.086 0.020 2 414 51 51 PRO HG3 H 1.990 0.020 2 415 51 51 PRO HD2 H 3.889 0.020 2 416 51 51 PRO HD3 H 3.666 0.020 2 417 51 51 PRO CA C 61.715 0.400 1 418 51 51 PRO CB C 32.194 0.400 1 419 51 51 PRO CG C 26.984 0.400 1 420 51 51 PRO CD C 50.601 0.400 1 421 52 52 ILE H H 8.192 0.020 1 422 52 52 ILE HA H 3.460 0.020 1 423 52 52 ILE HB H 1.673 0.020 1 424 52 52 ILE HG12 H 1.692 0.020 2 425 52 52 ILE HG13 H 1.215 0.020 2 426 52 52 ILE HG2 H 0.868 0.020 1 427 52 52 ILE HD1 H 0.890 0.020 1 428 52 52 ILE CA C 64.185 0.400 1 429 52 52 ILE CB C 37.751 0.400 1 430 52 52 ILE CG1 C 28.046 0.400 1 431 52 52 ILE CG2 C 16.578 0.400 1 432 52 52 ILE CD1 C 12.408 0.400 1 433 52 52 ILE N N 119.942 0.400 1 434 53 53 ASN HB2 H 2.663 0.020 1 435 53 53 ASN HB3 H 2.663 0.020 1 436 53 53 ASN HD21 H 7.451 0.020 2 437 53 53 ASN HD22 H 6.834 0.020 2 438 53 53 ASN CB C 38.818 0.400 1 439 53 53 ASN ND2 N 112.842 0.400 1 440 54 54 ASP H H 9.584 0.020 1 441 54 54 ASP HA H 5.107 0.020 1 442 54 54 ASP HB2 H 2.920 0.020 2 443 54 54 ASP HB3 H 2.483 0.020 2 444 54 54 ASP CA C 49.938 0.400 1 445 54 54 ASP CB C 41.250 0.400 1 446 54 54 ASP N N 126.040 0.400 1 447 55 55 PRO HA H 4.174 0.020 1 448 55 55 PRO HB2 H 2.435 0.020 2 449 55 55 PRO HB3 H 2.016 0.020 2 450 55 55 PRO HG2 H 2.133 0.020 2 451 55 55 PRO HG3 H 1.997 0.020 2 452 55 55 PRO HD2 H 3.943 0.020 2 453 55 55 PRO HD3 H 3.411 0.020 2 454 55 55 PRO CA C 64.146 0.400 1 455 55 55 PRO CB C 31.846 0.400 1 456 55 55 PRO CG C 26.637 0.400 1 457 55 55 PRO CD C 49.938 0.400 1 458 56 56 GLU H H 7.821 0.020 1 459 56 56 GLU HA H 4.112 0.020 1 460 56 56 GLU HB2 H 2.118 0.020 1 461 56 56 GLU HB3 H 2.118 0.020 1 462 56 56 GLU HG2 H 2.339 0.020 2 463 56 56 GLU HG3 H 2.262 0.020 2 464 56 56 GLU CA C 58.972 0.400 1 465 56 56 GLU CB C 28.741 0.400 1 466 56 56 GLU CG C 36.386 0.400 1 467 56 56 GLU N N 120.297 0.400 1 468 57 57 ARG H H 7.606 0.020 1 469 57 57 ARG HA H 4.314 0.020 1 470 57 57 ARG HB2 H 1.828 0.020 1 471 57 57 ARG HB3 H 1.828 0.020 1 472 57 57 ARG HD2 H 2.707 0.020 1 473 57 57 ARG HD3 H 2.707 0.020 1 474 57 57 ARG HE H 8.021 0.020 1 475 57 57 ARG CA C 56.540 0.400 1 476 57 57 ARG CB C 28.741 0.400 1 477 57 57 ARG CD C 42.640 0.400 1 478 57 57 ARG N N 124.051 0.400 1 479 57 57 ARG NE N 85.054 0.400 1 480 58 58 GLU H H 8.080 0.020 1 481 58 58 GLU HA H 3.646 0.020 1 482 58 58 GLU HB2 H 2.068 0.020 2 483 58 58 GLU HB3 H 1.880 0.020 2 484 58 58 GLU CA C 60.362 0.400 1 485 58 58 GLU N N 118.768 0.400 1 486 59 59 LYS H H 7.956 0.020 1 487 59 59 LYS HA H 4.116 0.020 1 488 59 59 LYS HG2 H 1.600 0.020 2 489 59 59 LYS HG3 H 1.475 0.020 2 490 59 59 LYS HD2 H 1.651 0.020 1 491 59 59 LYS HD3 H 1.651 0.020 1 492 59 59 LYS HE2 H 3.029 0.020 2 493 59 59 LYS HE3 H 2.879 0.020 2 494 59 59 LYS CA C 59.667 0.400 1 495 59 59 LYS CG C 24.571 0.400 1 496 59 59 LYS CD C 29.088 0.400 1 497 59 59 LYS N N 119.154 0.400 1 498 60 60 TYR H H 7.470 0.020 1 499 60 60 TYR HA H 4.218 0.020 1 500 60 60 TYR HB2 H 3.488 0.020 2 501 60 60 TYR HB3 H 3.155 0.020 2 502 60 60 TYR HD1 H 7.090 0.020 1 503 60 60 TYR HE1 H 6.891 0.020 1 504 60 60 TYR CA C 60.710 0.400 1 505 60 60 TYR CB C 36.733 0.400 1 506 60 60 TYR CD1 C 132.815 0.400 1 507 60 60 TYR CE1 C 117.426 0.400 1 508 60 60 TYR N N 119.732 0.400 1 509 61 61 ILE H H 8.079 0.020 1 510 61 61 ILE HA H 3.268 0.020 1 511 61 61 ILE HB H 1.624 0.020 1 512 61 61 ILE HG12 H 1.833 0.020 2 513 61 61 ILE HG13 H 1.210 0.020 2 514 61 61 ILE HG2 H 0.875 0.020 1 515 61 61 ILE HD1 H 0.507 0.020 1 516 61 61 ILE CA C 65.575 0.400 1 517 61 61 ILE CB C 37.428 0.400 1 518 61 61 ILE CG1 C 27.351 0.400 1 519 61 61 ILE CG2 C 14.493 0.400 1 520 61 61 ILE CD1 C 15.536 0.400 1 521 61 61 ILE N N 122.464 0.400 1 522 62 62 TYR H H 8.734 0.020 1 523 62 62 TYR HA H 4.048 0.020 1 524 62 62 TYR HB2 H 2.906 0.020 1 525 62 62 TYR HB3 H 2.906 0.020 1 526 62 62 TYR HD1 H 7.004 0.020 1 527 62 62 TYR HE1 H 6.674 0.020 1 528 62 62 TYR CA C 61.405 0.400 1 529 62 62 TYR CB C 39.165 0.400 1 530 62 62 TYR CD1 C 131.907 0.400 1 531 62 62 TYR CE1 C 116.707 0.400 1 532 62 62 TYR N N 118.762 0.400 1 533 63 63 ASP H H 8.378 0.020 1 534 63 63 ASP HA H 4.327 0.020 1 535 63 63 ASP HB2 H 2.772 0.020 2 536 63 63 ASP HB3 H 2.497 0.020 2 537 63 63 ASP CA C 57.235 0.400 1 538 63 63 ASP CB C 39.860 0.400 1 539 63 63 ASP N N 118.839 0.400 1 540 64 64 ARG H H 7.939 0.020 1 541 64 64 ARG HA H 3.925 0.020 1 542 64 64 ARG HB2 H 1.576 0.020 2 543 64 64 ARG HB3 H 1.484 0.020 2 544 64 64 ARG HE H 7.392 0.020 1 545 64 64 ARG CA C 58.625 0.400 1 546 64 64 ARG CB C 29.088 0.400 1 547 64 64 ARG N N 123.158 0.400 1 548 64 64 ARG NE N 85.551 0.400 1 549 65 65 ILE H H 8.969 0.020 1 550 65 65 ILE HA H 3.630 0.020 1 551 65 65 ILE HB H 2.095 0.020 1 552 65 65 ILE HG12 H 1.367 0.020 2 553 65 65 ILE HG13 H 0.514 0.020 2 554 65 65 ILE HG2 H 0.637 0.020 1 555 65 65 ILE HD1 H -0.068 0.020 1 556 65 65 ILE CA C 61.752 0.400 1 557 65 65 ILE CB C 35.343 0.400 1 558 65 65 ILE CG1 C 26.656 0.400 1 559 65 65 ILE CG2 C 17.968 0.400 1 560 65 65 ILE CD1 C 8.934 0.400 1 561 65 65 ILE N N 121.816 0.400 1 562 66 66 ARG H H 8.287 0.020 1 563 66 66 ARG HA H 3.823 0.020 1 564 66 66 ARG HB2 H 2.063 0.020 2 565 66 66 ARG HB3 H 1.989 0.020 2 566 66 66 ARG HG2 H 1.988 0.020 2 567 66 66 ARG HG3 H 1.450 0.020 2 568 66 66 ARG HD2 H 3.274 0.020 2 569 66 66 ARG HD3 H 3.167 0.020 2 570 66 66 ARG CA C 61.405 0.400 1 571 66 66 ARG CB C 29.436 0.400 1 572 66 66 ARG CG C 29.088 0.400 1 573 66 66 ARG CD C 42.969 0.400 1 574 66 66 ARG N N 121.926 0.400 1 575 67 67 LYS H H 7.338 0.020 1 576 67 67 LYS HA H 4.005 0.020 1 577 67 67 LYS HB2 H 1.922 0.020 1 578 67 67 LYS HB3 H 1.922 0.020 1 579 67 67 LYS CA C 59.667 0.400 1 580 67 67 LYS CB C 32.563 0.400 1 581 67 67 LYS N N 119.688 0.400 1 582 68 68 LEU H H 8.602 0.020 1 583 68 68 LEU HA H 4.079 0.020 1 584 68 68 LEU HB2 H 1.367 0.020 2 585 68 68 LEU HB3 H 1.920 0.020 2 586 68 68 LEU HG H 1.768 0.020 1 587 68 68 LEU HD1 H 0.781 0.020 2 588 68 68 LEU CA C 57.235 0.400 1 589 68 68 LEU CB C 42.640 0.400 1 590 68 68 LEU CG C 26.656 0.400 1 591 68 68 LEU CD1 C 24.571 0.400 1 592 68 68 LEU N N 122.290 0.400 1 593 69 69 CYS H H 8.897 0.020 1 594 69 69 CYS HA H 4.076 0.020 1 595 69 69 CYS CA C 65.575 0.400 1 596 69 69 CYS N N 119.253 0.400 1 597 70 70 LYS H H 7.355 0.020 1 598 70 70 LYS HA H 4.238 0.020 1 599 70 70 LYS HB2 H 1.980 0.020 1 600 70 70 LYS HB3 H 1.980 0.020 1 601 70 70 LYS HG2 H 1.613 0.020 2 602 70 70 LYS HG3 H 1.491 0.020 2 603 70 70 LYS HD2 H 1.722 0.020 2 604 70 70 LYS HD3 H 1.681 0.020 2 605 70 70 LYS HE2 H 3.025 0.020 1 606 70 70 LYS HE3 H 3.025 0.020 1 607 70 70 LYS CA C 58.625 0.400 1 608 70 70 LYS CB C 31.173 0.400 1 609 70 70 LYS CG C 24.571 0.400 1 610 70 70 LYS CD C 28.741 0.400 1 611 70 70 LYS CE C 41.598 0.400 1 612 70 70 LYS N N 119.243 0.400 1 613 71 71 GLU H H 7.684 0.020 1 614 71 71 GLU HA H 3.920 0.020 1 615 71 71 GLU HB2 H 1.910 0.020 2 616 71 71 GLU HB3 H 1.734 0.020 2 617 71 71 GLU HG2 H 2.144 0.020 2 618 71 71 GLU HG3 H 1.882 0.020 2 619 71 71 GLU CA C 58.277 0.400 1 620 71 71 GLU CB C 29.088 0.400 1 621 71 71 GLU CG C 34.996 0.400 1 622 71 71 GLU N N 120.396 0.400 1 623 72 72 HIS H H 7.984 0.020 1 624 72 72 HIS HB2 H 3.395 0.020 2 625 72 72 HIS HB3 H 2.734 0.020 2 626 72 72 HIS HD2 H 6.886 0.020 1 627 72 72 HIS HE1 H 7.802 0.020 1 628 72 72 HIS CB C 30.131 0.400 1 629 72 72 HIS CD2 C 119.220 0.400 1 630 72 72 HIS CE1 C 137.504 0.400 1 631 72 72 HIS N N 114.903 0.400 1 632 73 73 ASN H H 7.795 0.020 1 633 73 73 ASN HA H 4.433 0.020 1 634 73 73 ASN HB2 H 3.203 0.020 2 635 73 73 ASN HB3 H 2.797 0.020 2 636 73 73 ASN HD21 H 7.596 0.020 2 637 73 73 ASN HD22 H 6.833 0.020 2 638 73 73 ASN CA C 54.108 0.400 1 639 73 73 ASN CB C 36.386 0.400 1 640 73 73 ASN N N 118.082 0.400 1 641 73 73 ASN ND2 N 113.484 0.400 1 642 74 74 VAL H H 8.677 0.020 1 643 74 74 VAL HA H 4.247 0.020 1 644 74 74 VAL HB H 1.891 0.020 1 645 74 74 VAL HG2 H 1.032 0.020 2 646 74 74 VAL CA C 60.326 0.400 1 647 74 74 VAL CB C 34.625 0.400 1 648 74 74 VAL CG2 C 21.080 0.400 1 649 74 74 VAL N N 120.888 0.400 1 650 75 75 ASP H H 8.577 0.020 1 651 75 75 ASP HA H 4.352 0.020 1 652 75 75 ASP HB2 H 2.735 0.020 1 653 75 75 ASP HB3 H 2.735 0.020 1 654 75 75 ASP CA C 54.803 0.400 1 655 75 75 ASP CB C 41.598 0.400 1 656 75 75 ASP N N 128.341 0.400 1 657 76 76 GLU HA H 4.342 0.020 1 658 76 76 GLU HB2 H 2.134 0.020 2 659 76 76 GLU HB3 H 2.050 0.020 2 660 76 76 GLU HG2 H 2.313 0.020 2 661 76 76 GLU CA C 58.972 0.400 1 662 76 76 GLU CB C 30.131 0.400 1 663 76 76 GLU CG C 36.386 0.400 1 664 77 77 ASN H H 8.442 0.020 1 665 77 77 ASN HA H 4.426 0.020 1 666 77 77 ASN HB2 H 2.921 0.020 2 667 77 77 ASN HB3 H 2.695 0.020 2 668 77 77 ASN HD21 H 7.999 0.020 2 669 77 77 ASN HD22 H 7.080 0.020 2 670 77 77 ASN CA C 55.845 0.400 1 671 77 77 ASN CB C 37.776 0.400 1 672 77 77 ASN N N 116.822 0.400 1 673 77 77 ASN ND2 N 116.392 0.400 1 674 78 78 ILE H H 7.745 0.020 1 675 78 78 ILE HA H 3.856 0.020 1 676 78 78 ILE HB H 2.096 0.020 1 677 78 78 ILE HG12 H 1.635 0.020 2 678 78 78 ILE HG13 H 1.289 0.020 2 679 78 78 ILE HG2 H 0.947 0.020 1 680 78 78 ILE HD1 H 0.862 0.020 1 681 78 78 ILE CA C 63.452 0.400 1 682 78 78 ILE CB C 37.056 0.400 1 683 78 78 ILE CG1 C 28.026 0.400 1 684 78 78 ILE CG2 C 16.542 0.400 1 685 78 78 ILE CD1 C 11.713 0.400 1 686 78 78 ILE N N 121.274 0.400 1 687 79 79 GLY HA2 H 3.755 0.020 2 688 79 79 GLY HA3 H 3.708 0.020 2 689 79 79 GLY CA C 47.128 0.400 1 690 80 80 ILE H H 8.494 0.020 1 691 80 80 ILE HA H 3.987 0.020 1 692 80 80 ILE HB H 2.127 0.020 1 693 80 80 ILE HG12 H 1.570 0.020 2 694 80 80 ILE HG2 H 0.762 0.020 1 695 80 80 ILE HD1 H 0.857 0.020 1 696 80 80 ILE CA C 63.142 0.400 1 697 80 80 ILE CB C 35.691 0.400 1 698 80 80 ILE CG1 C 27.351 0.400 1 699 80 80 ILE CG2 C 16.578 0.400 1 700 80 80 ILE CD1 C 11.019 0.400 1 701 80 80 ILE N N 120.464 0.400 1 702 81 81 LYS H H 7.439 0.020 1 703 81 81 LYS HA H 4.110 0.020 1 704 81 81 LYS HB2 H 2.626 0.020 2 705 81 81 LYS HB3 H 2.393 0.020 2 706 81 81 LYS HG2 H 1.615 0.020 2 707 81 81 LYS CA C 59.320 0.400 1 708 81 81 LYS CB C 33.258 0.400 1 709 81 81 LYS N N 119.751 0.400 1 710 83 83 PHE HA H 3.929 0.020 1 711 83 83 PHE HB2 H 2.920 0.020 1 712 83 83 PHE HB3 H 2.920 0.020 1 713 83 83 PHE HD1 H 7.361 0.020 1 714 83 83 PHE HE1 H 7.262 0.020 1 715 83 83 PHE HZ H 7.296 0.020 1 716 83 83 PHE CA C 64.185 0.400 1 717 83 83 PHE CB C 38.123 0.400 1 718 83 83 PHE CD1 C 130.567 0.400 1 719 83 83 PHE CE1 C 130.519 0.400 1 720 83 83 PHE CZ C 128.830 0.400 1 721 84 84 GLN H H 9.153 0.020 1 722 84 84 GLN HE21 H 7.531 0.020 2 723 84 84 GLN HE22 H 6.474 0.020 2 724 84 84 GLN N N 121.434 0.400 1 725 84 84 GLN NE2 N 110.147 0.400 1 726 85 85 ARG H H 7.354 0.020 1 727 85 85 ARG N N 118.180 0.400 1 728 87 87 ILE H H 9.022 0.020 1 729 87 87 ILE HB H 1.924 0.020 1 730 87 87 ILE HG12 H 1.748 0.020 2 731 87 87 ILE HG13 H 1.299 0.020 2 732 87 87 ILE HG2 H 0.725 0.020 1 733 87 87 ILE HD1 H 0.498 0.020 1 734 87 87 ILE CB C 38.470 0.400 1 735 87 87 ILE CG1 C 28.393 0.400 1 736 87 87 ILE CG2 C 17.621 0.400 1 737 87 87 ILE CD1 C 13.451 0.400 1 738 87 87 ILE N N 127.030 0.400 1 739 88 88 GLU H H 7.965 0.020 1 740 88 88 GLU N N 119.368 0.400 1 741 89 89 HIS HA H 4.525 0.020 1 742 89 89 HIS HD2 H 7.048 0.020 1 743 89 89 HIS HE1 H 7.977 0.020 1 744 89 89 HIS CD2 C 118.516 0.400 1 745 89 89 HIS CE1 C 137.504 0.400 1 746 90 90 ASN H H 8.558 0.020 1 747 90 90 ASN HA H 3.923 0.020 1 748 90 90 ASN HB2 H 3.313 0.020 2 749 90 90 ASN HB3 H 3.176 0.020 2 750 90 90 ASN HD21 H 7.579 0.020 2 751 90 90 ASN HD22 H 6.702 0.020 2 752 90 90 ASN CA C 58.277 0.400 1 753 90 90 ASN CB C 39.860 0.400 1 754 90 90 ASN N N 121.816 0.400 1 755 90 90 ASN ND2 N 112.223 0.400 1 756 91 91 LYS H H 8.020 0.020 1 757 91 91 LYS HA H 3.839 0.020 1 758 91 91 LYS CA C 60.710 0.400 1 759 91 91 LYS N N 116.154 0.400 1 760 92 92 ALA H H 7.864 0.020 1 761 92 92 ALA HA H 4.099 0.020 1 762 92 92 ALA HB H 1.538 0.020 1 763 92 92 ALA CA C 55.116 0.400 1 764 92 92 ALA CB C 17.236 0.400 1 765 92 92 ALA N N 125.314 0.400 1 766 93 93 LEU H H 8.302 0.020 1 767 93 93 LEU HA H 3.904 0.020 1 768 93 93 LEU HB2 H 1.976 0.020 2 769 93 93 LEU HB3 H 1.113 0.020 2 770 93 93 LEU HG H 1.201 0.020 1 771 93 93 LEU HD1 H 0.709 0.020 2 772 93 93 LEU CA C 56.887 0.400 1 773 93 93 LEU CB C 41.250 0.400 1 774 93 93 LEU CG C 25.613 0.400 1 775 93 93 LEU CD1 C 25.613 0.400 1 776 93 93 LEU N N 120.938 0.400 1 777 94 94 GLN H H 8.453 0.020 1 778 94 94 GLN HA H 3.783 0.020 1 779 94 94 GLN HB2 H 2.168 0.020 1 780 94 94 GLN HB3 H 2.168 0.020 1 781 94 94 GLN HG2 H 2.669 0.020 2 782 94 94 GLN HG3 H 2.468 0.020 2 783 94 94 GLN HE21 H 7.680 0.020 2 784 94 94 GLN HE22 H 6.912 0.020 2 785 94 94 GLN CA C 60.015 0.400 1 786 94 94 GLN CB C 29.436 0.400 1 787 94 94 GLN CG C 34.996 0.400 1 788 94 94 GLN N N 121.226 0.400 1 789 94 94 GLN NE2 N 113.741 0.400 1 790 95 95 LYS H H 8.066 0.020 1 791 95 95 LYS HA H 3.848 0.020 1 792 95 95 LYS HB2 H 1.960 0.020 2 793 95 95 LYS HB3 H 1.859 0.020 2 794 95 95 LYS HG2 H 1.499 0.020 2 795 95 95 LYS HG3 H 1.376 0.020 2 796 95 95 LYS HE2 H 2.957 0.020 1 797 95 95 LYS HE3 H 2.957 0.020 1 798 95 95 LYS CA C 59.320 0.400 1 799 95 95 LYS CB C 32.563 0.400 1 800 95 95 LYS CG C 24.571 0.400 1 801 95 95 LYS CE C 41.945 0.400 1 802 95 95 LYS N N 119.987 0.400 1 803 96 96 GLN H H 7.862 0.020 1 804 96 96 GLN HA H 4.050 0.020 1 805 96 96 GLN HB2 H 2.019 0.020 1 806 96 96 GLN HB3 H 2.019 0.020 1 807 96 96 GLN HG2 H 2.421 0.020 2 808 96 96 GLN HG3 H 2.266 0.020 2 809 96 96 GLN HE21 H 7.611 0.020 2 810 96 96 GLN HE22 H 6.800 0.020 2 811 96 96 GLN CA C 57.930 0.400 1 812 96 96 GLN CB C 29.088 0.400 1 813 96 96 GLN CG C 32.911 0.400 1 814 96 96 GLN N N 119.463 0.400 1 815 96 96 GLN NE2 N 112.457 0.400 1 816 97 97 TYR H H 8.111 0.020 1 817 97 97 TYR HA H 4.333 0.020 1 818 97 97 TYR HB2 H 3.064 0.020 1 819 97 97 TYR HB3 H 3.064 0.020 1 820 97 97 TYR HD1 H 6.991 0.020 1 821 97 97 TYR HE1 H 6.711 0.020 1 822 97 97 TYR CA C 60.710 0.400 1 823 97 97 TYR CB C 37.081 0.400 1 824 97 97 TYR CD1 C 132.112 0.400 1 825 97 97 TYR CE1 C 117.110 0.400 1 826 97 97 TYR N N 120.258 0.400 1 827 98 98 LEU H H 8.221 0.020 1 828 98 98 LEU HA H 3.974 0.020 1 829 98 98 LEU HB2 H 1.925 0.020 2 830 98 98 LEU HB3 H 1.578 0.020 2 831 98 98 LEU HD1 H 0.945 0.020 2 832 98 98 LEU HD2 H 0.874 0.020 2 833 98 98 LEU CA C 56.887 0.400 1 834 98 98 LEU CB C 40.876 0.400 1 835 98 98 LEU CD1 C 24.571 0.400 1 836 98 98 LEU CD2 C 24.571 0.400 1 837 98 98 LEU N N 120.844 0.400 1 838 99 99 GLU H H 8.150 0.020 1 839 99 99 GLU HA H 4.035 0.020 1 840 99 99 GLU HB2 H 2.621 0.020 2 841 99 99 GLU HB3 H 2.438 0.020 2 842 99 99 GLU CB C 33.258 0.400 1 843 99 99 GLU N N 119.717 0.400 1 844 100 100 GLU H H 8.054 0.020 1 845 100 100 GLU HA H 4.166 0.020 1 846 100 100 GLU HB2 H 2.109 0.020 2 847 100 100 GLU HB3 H 2.048 0.020 2 848 100 100 GLU HG2 H 2.444 0.020 2 849 100 100 GLU HG3 H 2.242 0.020 2 850 100 100 GLU CA C 57.235 0.400 1 851 100 100 GLU CB C 29.783 0.400 1 852 100 100 GLU CG C 36.386 0.400 1 853 100 100 GLU N N 119.154 0.400 1 854 101 101 THR H H 7.785 0.020 1 855 101 101 THR HA H 4.120 0.020 1 856 101 101 THR HB H 4.025 0.020 1 857 101 101 THR HG2 H 1.071 0.020 1 858 101 101 THR CA C 63.490 0.400 1 859 101 101 THR CB C 69.05 0.400 1 860 101 101 THR CG2 C 21.096 0.400 1 861 101 101 THR N N 113.840 0.400 1 862 102 102 LEU H H 7.804 0.020 1 863 102 102 LEU HA H 4.180 0.020 1 864 102 102 LEU HB2 H 1.713 0.020 2 865 102 102 LEU HB3 H 1.490 0.020 2 866 102 102 LEU HG H 1.615 0.020 1 867 102 102 LEU HD1 H 0.830 0.020 2 868 102 102 LEU CA C 55.845 0.400 1 869 102 102 LEU CB C 41.598 0.400 1 870 102 102 LEU CG C 26.308 0.400 1 871 102 102 LEU CD1 C 22.833 0.400 1 872 102 102 LEU N N 123.273 0.400 1 873 103 103 GLU H H 8.005 0.020 1 874 103 103 GLU HA H 4.102 0.020 1 875 103 103 GLU HG3 H 1.911 0.020 2 876 103 103 GLU CA C 56.540 0.400 1 877 103 103 GLU CG C 29.088 0.400 1 878 103 103 GLU N N 120.055 0.400 1 879 104 104 HIS H H 8.166 0.020 1 880 104 104 HIS HA H 4.408 0.020 1 881 104 104 HIS HB2 H 3.185 0.020 2 882 104 104 HIS HB3 H 3.064 0.020 2 883 104 104 HIS HD2 H 7.019 0.020 1 884 104 104 HIS HE1 H 8.065 0.020 1 885 104 104 HIS CA C 56.887 0.400 1 886 104 104 HIS CB C 30.131 0.400 1 887 104 104 HIS CD2 C 118.751 0.400 1 888 104 104 HIS CE1 C 136.801 0.400 1 889 104 104 HIS N N 126.357 0.400 1 stop_ save_ save_chem_shift_list_1_2 _Saveframe_category assigned_chemical_shifts _Details ; TSA free 3000 6.06 H2 3001 5.73 H3 3002 4.30 H4 3003 4.13 H5 3004 1.91 1H6 3005 1.91 2H6 3006 4.18 H8 3007 2.09 1H9 3008 2.20 2H9 ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name TSA _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 . 1 TSA H2 H 6.49 0.005 1 2 . 1 TSA H3 H 5.69 0.005 1 3 . 1 TSA H4 H 4.37 0.005 1 4 . 1 TSA H5 H 4.30 0.005 1 5 . 1 TSA H8 H 4.00 0.005 1 6 . 1 TSA HO5 H 6.33 0.005 1 7 . 1 TSA H61 H 1.74 0.005 1 8 . 1 TSA H91 H 1.82 0.005 1 9 . 1 TSA H62 H 1.93 0.005 1 10 . 1 TSA H92 H 2.41 0.005 1 stop_ save_