data_5308 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure and Dynamics of the Human-Escherichia coli Thioredoxin Chimera: Insights into Thermodynamic Stability ; _BMRB_accession_number 5308 _BMRB_flat_file_name bmr5308.str _Entry_type original _Submission_date 2002-03-02 _Accession_date 2002-03-04 _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 Dangi Bindi . . 2 Dubrodumov Anatoliy V. . 3 Louis John M . 4 Gronenborn Angela M . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 542 "13C chemical shifts" 455 "15N chemical shifts" 108 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-09-11 original BMRB . stop_ _Original_release_date 2002-03-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure and Dynamics of the Human-Escherichia coli Thioredoxin Chimera: Insights into Thermodynamic Stability ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22130999 _PubMed_ID 12135359 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Dangi Bindi . . 2 Dubrodumov Anatoliy V. . 3 Louis John M . 4 Gronenborn Angela M . stop_ _Journal_abbreviation Biochemistry _Journal_volume 41 _Journal_issue 30 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 9376 _Page_last 9388 _Year 2002 _Details . loop_ _Keyword E.coli Human assignments chimera 'structure dynamics' thioredoxin stop_ save_ ################################## # Molecular system description # ################################## save_system_TRX _Saveframe_category molecular_system _Mol_system_name 'Human-E.coli chimeric thioredoxin' _Abbreviation_common TRX _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label trx-he $trx-he stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function oxidoreductase stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_trx-he _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common thioredoxin _Abbreviation_common trx _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 107 _Mol_residue_sequence ; MVKQIESKTAFQEALDAAGD KLVVVDFSATWCGPCKMIKP FFHSLSEKYSNVIFLEVDVD DAQDVAPKYGIRGIPTLLLF KNGEVAATKVGALSKGQLKE FLDANLV ; loop_ _Residue_seq_code _Residue_label 1 MET 2 VAL 3 LYS 4 GLN 5 ILE 6 GLU 7 SER 8 LYS 9 THR 10 ALA 11 PHE 12 GLN 13 GLU 14 ALA 15 LEU 16 ASP 17 ALA 18 ALA 19 GLY 20 ASP 21 LYS 22 LEU 23 VAL 24 VAL 25 VAL 26 ASP 27 PHE 28 SER 29 ALA 30 THR 31 TRP 32 CYS 33 GLY 34 PRO 35 CYS 36 LYS 37 MET 38 ILE 39 LYS 40 PRO 41 PHE 42 PHE 43 HIS 44 SER 45 LEU 46 SER 47 GLU 48 LYS 49 TYR 50 SER 51 ASN 52 VAL 53 ILE 54 PHE 55 LEU 56 GLU 57 VAL 58 ASP 59 VAL 60 ASP 61 ASP 62 ALA 63 GLN 64 ASP 65 VAL 66 ALA 67 PRO 68 LYS 69 TYR 70 GLY 71 ILE 72 ARG 73 GLY 74 ILE 75 PRO 76 THR 77 LEU 78 LEU 79 LEU 80 PHE 81 LYS 82 ASN 83 GLY 84 GLU 85 VAL 86 ALA 87 ALA 88 THR 89 LYS 90 VAL 91 GLY 92 ALA 93 LEU 94 SER 95 LYS 96 GLY 97 GLN 98 LEU 99 LYS 100 GLU 101 PHE 102 LEU 103 ASP 104 ALA 105 ASN 106 LEU 107 VAL stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 1M7T 'Solution Structure And Dynamics Of The Human-Escherichia Coli Thioredoxin Chimera: Insights Into Thermodynamic Stability' 100.00 107 100.00 100.00 1.46e-55 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $trx-he 'Escherichia coli' 562 Bacteria . Escherichia coli 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 $trx-he 'recombinant technology' . . . . . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $trx-he . mM 1 2 '[U-95% 13C; U-95% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_nmrPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task processing stop_ _Details 'Delaglio et al.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DMX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DMX _Field_strength 500 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DRX _Field_strength 800 _Details . save_ save_NMR_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DMX _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC' _Sample_label . save_ save_15N_TOCSY-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '15N TOCSY-HSQC' _Sample_label . save_ save_15N_NOESY-HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '15N NOESY-HSQC' _Sample_label . save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_C(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _Sample_label . save_ save_H(CCO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH _Sample_label . save_ save_4D_13C_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 13C NOESY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.2 n/a temperature 308 1 K 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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 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 . loop_ _Experiment_label '15N HSQC' '15N TOCSY-HSQC' '15N NOESY-HSQC' HNCACB C(CO)NH H(CCO)NH '4D 13C NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name trx-he _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 MET CE C 17.43 0.1 1 2 . 1 MET HE H 2.16 0.02 1 3 . 2 VAL CA C 60.7619 0.1 1 4 . 2 VAL CB C 34.5308 0.1 1 5 . 2 VAL CG1 C 22.0752 0.1 1 6 . 2 VAL CG2 C 21.4274 0.1 1 7 . 2 VAL HA H 4.2885 0.02 1 8 . 2 VAL HB H 1.5956 0.02 1 9 . 2 VAL HG1 H 0.784 0.02 1 10 . 2 VAL HG2 H 0.458 0.02 1 11 . 2 VAL C C 175.1987 0.1 1 12 . 3 LYS CA C 55.099 0.1 1 13 . 3 LYS CB C 34.464 0.1 1 14 . 3 LYS CG C 25.078 0.1 1 15 . 3 LYS CD C 29.026 0.1 1 16 . 3 LYS CE C 41.984 0.1 1 17 . 3 LYS H H 8.3163 0.02 1 18 . 3 LYS N N 128.9421 0.1 1 19 . 3 LYS HA H 4.5187 0.02 1 20 . 3 LYS HB2 H 1.7898 0.02 2 21 . 3 LYS HB3 H 1.5965 0.02 2 22 . 3 LYS HG2 H 1.3678 0.02 2 23 . 3 LYS HG3 H 1.2592 0.02 2 24 . 3 LYS HE2 H 2.9453 0.02 2 25 . 4 GLN C C 175.99 0.1 1 26 . 4 GLN CA C 55.31 0.1 1 27 . 4 GLN CB C 29.21 0.1 1 28 . 4 GLN CG C 34.11 0.1 1 29 . 4 GLN HA H 4.698 0.02 1 30 . 4 GLN HB3 H 2.044 0.02 2 31 . 4 GLN HG2 H 2.322 0.02 2 32 . 4 GLN H H 8.686 0.02 1 33 . 4 GLN N N 126.84 0.1 1 34 . 4 GLN NE2 N 112.9561 0.1 1 35 . 4 GLN HE21 H 6.9737 0.02 2 36 . 4 GLN HE22 H 7.7041 0.02 2 37 . 5 ILE C C 176.71 0.1 1 38 . 5 ILE CA C 57.65 0.1 1 39 . 5 ILE CB C 36.8 0.1 1 40 . 5 ILE CD1 C 9.73 0.1 1 41 . 5 ILE CG2 C 19.11 0.1 1 42 . 5 ILE CG1 C 26.97 0.1 1 43 . 5 ILE HA H 4.399 0.02 1 44 . 5 ILE HB H 2.151 0.02 1 45 . 5 ILE HD1 H 0.673 0.02 1 46 . 5 ILE HG12 H 1.164 0.02 2 47 . 5 ILE HG13 H 1.71 0.02 2 48 . 5 ILE HG2 H 1.037 0.02 1 49 . 5 ILE H H 8.615 0.02 1 50 . 5 ILE N N 126.75 0.1 1 51 . 6 GLU C C 175.28 0.1 1 52 . 6 GLU CA C 56.84 0.1 1 53 . 6 GLU CB C 31.16 0.1 1 54 . 6 GLU CG C 36.45 0.1 1 55 . 6 GLU HA H 4.527 0.02 1 56 . 6 GLU HB2 H 2.086 0.02 1 57 . 6 GLU HB3 H 2.279 0.02 1 58 . 6 GLU HG3 H 2.236 0.02 2 59 . 6 GLU H H 9.261 0.02 1 60 . 6 GLU N N 124.87 0.1 1 61 . 7 SER C C 174.23 0.1 1 62 . 7 SER CA C 56.92 0.1 1 63 . 7 SER CB C 66.84 0.1 1 64 . 7 SER HA H 4.892 0.02 1 65 . 7 SER HB2 H 4.325 0.02 2 66 . 7 SER HB3 H 4.095 0.02 2 67 . 7 SER H H 7.34 0.02 1 68 . 7 SER N N 109.91 0.1 1 69 . 8 LYS C C 170.99 0.1 1 70 . 8 LYS CA C 59.96 0.1 1 71 . 8 LYS CB C 31.6524 0.1 1 72 . 8 LYS CG C 25.0934 0.1 1 73 . 8 LYS CD C 29.812 0.1 1 74 . 8 LYS CE C 42.0412 0.1 1 75 . 8 LYS HA H 4.0194 0.02 1 76 . 8 LYS HB2 H 1.895 0.02 2 77 . 8 LYS HG2 H 1.5152 0.02 2 78 . 8 LYS HD2 H 1.7248 0.02 2 79 . 8 LYS HE2 H 2.9963 0.02 2 80 . 8 LYS H H 9.631 0.02 1 81 . 8 LYS N N 122.36 0.1 1 82 . 9 THR C C 176.33 0.1 1 83 . 9 THR CA C 66 0.1 1 84 . 9 THR CB C 68.3 0.1 1 85 . 9 THR CG2 C 22.39 0.1 1 86 . 9 THR HA H 4.048 0.02 1 87 . 9 THR HB H 4.079 0.02 1 88 . 9 THR HG2 H 1.254 0.02 1 89 . 9 THR H H 8.163 0.02 1 90 . 9 THR N N 116.8 0.1 1 91 . 10 ALA C C 180.45 0.1 1 92 . 10 ALA CA C 54.63 0.1 1 93 . 10 ALA CB C 18.89 0.1 1 94 . 10 ALA HA H 4.249 0.02 1 95 . 10 ALA HB H 1.594 0.02 1 96 . 10 ALA H H 7.917 0.02 1 97 . 10 ALA N N 124.42 0.1 1 98 . 11 PHE C C 175.91 0.1 1 99 . 11 PHE CA C 61.81 0.1 1 100 . 11 PHE CB C 39.27 0.1 1 101 . 11 PHE HA H 3.911 0.02 1 102 . 11 PHE HB2 H 3.387 0.02 1 103 . 11 PHE HB3 H 3.085 0.02 1 104 . 11 PHE H H 8.213 0.02 1 105 . 11 PHE N N 120.65 0.1 1 106 . 11 PHE CD1 C 130.602 0.1 1 107 . 11 PHE HD1 H 7 0.02 1 108 . 11 PHE CE1 C 131.43 0.1 1 109 . 11 PHE HE1 H 6.88 0.02 1 110 . 12 GLN C C 178.17 0.1 1 111 . 12 GLN CA C 58.4 0.1 1 112 . 12 GLN CB C 28.6 0.1 1 113 . 12 GLN CG C 34.11 0.1 1 114 . 12 GLN HA H 3.692 0.02 1 115 . 12 GLN HB2 H 2.215 0.02 2 116 . 12 GLN HB3 H 2.301 0.02 2 117 . 12 GLN HG2 H 2.472 0.02 2 118 . 12 GLN H H 8.097 0.02 1 119 . 12 GLN N N 118 0.1 1 120 . 12 GLN NE2 N 116.126 0.1 1 121 . 12 GLN HE21 H 7.8589 0.02 1 122 . 12 GLN HE22 H 6.9971 0.02 1 123 . 13 GLU C C 179.31 0.1 1 124 . 13 GLU CA C 59.54 0.1 1 125 . 13 GLU CB C 29.57 0.1 1 126 . 13 GLU CG C 36.92 0.1 1 127 . 13 GLU HA H 3.992 0.02 1 128 . 13 GLU HB2 H 1.958 0.02 2 129 . 13 GLU HB3 H 2.065 0.02 2 130 . 13 GLU HG2 H 2.215 0.02 2 131 . 13 GLU HG3 H 2.472 0.02 2 132 . 13 GLU H H 8.116 0.02 1 133 . 13 GLU N N 117.52 0.1 1 134 . 14 ALA C C 180.52 0.1 1 135 . 14 ALA CA C 54.64 0.1 1 136 . 14 ALA CB C 18.52 0.1 1 137 . 14 ALA HA H 4.056 0.02 1 138 . 14 ALA HB H 1.251 0.02 1 139 . 14 ALA H H 7.917 0.02 1 140 . 14 ALA N N 124.42 0.1 1 141 . 15 LEU C C 180.64 0.1 1 142 . 15 LEU CA C 57.84 0.1 1 143 . 15 LEU CB C 41.51 0.1 1 144 . 15 LEU CD2 C 25.2 0.1 1 145 . 15 LEU CD1 C 21.92 0.1 1 146 . 15 LEU CG C 26.14 0.1 1 147 . 15 LEU HA H 3.649 0.02 1 148 . 15 LEU HB2 H 1.573 0.02 2 149 . 15 LEU HB3 H 1.08 0.02 2 150 . 15 LEU HD1 H 0.095 0.02 1 151 . 15 LEU HD2 H -0.204 0.02 1 152 . 15 LEU HG H 0.93 0.02 1 153 . 15 LEU H H 7.685 0.02 1 154 . 15 LEU N N 117.82 0.1 1 155 . 16 ASP C C 178.77 0.1 1 156 . 16 ASP CA C 57.02 0.1 1 157 . 16 ASP CB C 40.36 0.1 1 158 . 16 ASP HA H 4.292 0.02 1 159 . 16 ASP HB2 H 2.643 0.02 2 160 . 16 ASP H H 8.39 0.02 1 161 . 16 ASP N N 120.1 0.1 1 162 . 17 ALA C C 178.64 0.1 1 163 . 17 ALA CA C 52.98 0.1 1 164 . 17 ALA CB C 18.8 0.1 1 165 . 17 ALA HA H 4.21 0.02 1 166 . 17 ALA HB H 1.42 0.02 1 167 . 17 ALA H H 7.854 0.02 1 168 . 17 ALA N N 121.09 0.1 1 169 . 18 ALA C C 179.35 0.1 1 170 . 18 ALA CA C 54.17 0.1 1 171 . 18 ALA CB C 19.78 0.1 1 172 . 18 ALA HA H 3.885 0.02 1 173 . 18 ALA HB H 1.337 0.02 1 174 . 18 ALA H H 7.321 0.02 1 175 . 18 ALA N N 120.19 0.1 1 176 . 19 GLY C C 175.31 0.1 1 177 . 19 GLY CA C 47.32 0.1 1 178 . 19 GLY HA2 H 3.72 0.02 1 179 . 19 GLY HA3 H 3.88 0.02 1 180 . 19 GLY H H 7.632 0.02 1 181 . 19 GLY N N 105.62 0.1 1 182 . 20 ASP C C 176.44 0.1 1 183 . 20 ASP CA C 54.2 0.1 1 184 . 20 ASP CB C 40.81 0.1 1 185 . 20 ASP HA H 4.6868 0.02 1 186 . 20 ASP HB2 H 2.783 0.02 2 187 . 20 ASP H H 8.745 0.02 1 188 . 20 ASP N N 127.07 0.1 1 189 . 21 LYS C C 176.47 0.1 1 190 . 21 LYS CA C 57.18 0.1 1 191 . 21 LYS CB C 33.56 0.1 1 192 . 21 LYS CG C 26.0521 0.1 1 193 . 21 LYS CD C 29.7784 0.1 1 194 . 21 LYS CE C 42.9152 0.1 1 195 . 21 LYS HA H 4.25 0.02 1 196 . 21 LYS HB2 H 1.8091 0.02 2 197 . 21 LYS HD2 H 1.6159 0.02 2 198 . 21 LYS HE2 H 3.0475 0.02 2 199 . 21 LYS H H 7.778 0.02 1 200 . 21 LYS N N 120.4 0.1 1 201 . 22 LEU C C 175.34 0.1 1 202 . 22 LEU CA C 55.58 0.1 1 203 . 22 LEU CB C 43.21 0.1 1 204 . 22 LEU CD1 C 24.73 0.1 2 205 . 22 LEU CD2 C 25.2 0.1 2 206 . 22 LEU CG C 28.01 0.1 1 207 . 22 LEU HA H 4.484 0.02 1 208 . 22 LEU HB2 H 1.68 0.02 2 209 . 22 LEU HB3 H 1.508 0.02 2 210 . 22 LEU HD1 H 0.823 0.02 2 211 . 22 LEU HD2 H 0.93 0.02 2 212 . 22 LEU HG H 1.72 0.02 1 213 . 22 LEU H H 8.316 0.02 1 214 . 22 LEU N N 122.49 0.1 1 215 . 23 VAL C C 175.12 0.1 1 216 . 23 VAL CA C 60.13 0.1 1 217 . 23 VAL CB C 34.94 0.1 1 218 . 23 VAL CG1 C 21.45 0.1 1 219 . 23 VAL CG2 C 21.45 0.1 1 220 . 23 VAL HA H 4.891 0.02 1 221 . 23 VAL HB H 1.851 0.02 1 222 . 23 VAL HG1 H 0.716 0.02 1 223 . 23 VAL HG2 H 0.523 0.02 1 224 . 23 VAL H H 8.169 0.02 1 225 . 23 VAL N N 121.64 0.1 1 226 . 24 VAL C C 173.78 0.1 1 227 . 24 VAL CA C 59.68 0.1 1 228 . 24 VAL CB C 34.07 0.1 1 229 . 24 VAL CG1 C 22.39 0.1 1 230 . 24 VAL CG2 C 20.98 0.1 1 231 . 24 VAL HA H 5.084 0.02 1 232 . 24 VAL HB H 1.401 0.02 1 233 . 24 VAL HG1 H 0.652 0.02 1 234 . 24 VAL HG2 H 0.502 0.02 1 235 . 24 VAL H H 9.315 0.02 1 236 . 24 VAL N N 127.61 0.1 1 237 . 25 VAL C C 174.13 0.1 1 238 . 25 VAL CA C 60.23 0.1 1 239 . 25 VAL CB C 34.53 0.1 1 240 . 25 VAL CG1 C 22.39 0.1 1 241 . 25 VAL CG2 C 23.33 0.1 1 242 . 25 VAL HA H 4.913 0.02 1 243 . 25 VAL HB H 2.151 0.02 1 244 . 25 VAL HG1 H 0.952 0.02 1 245 . 25 VAL HG2 H 0.309 0.02 1 246 . 25 VAL H H 9.388 0.02 1 247 . 25 VAL N N 126.62 0.1 1 248 . 26 ASP C C 174.23 0.1 1 249 . 26 ASP CA C 52.03 0.1 1 250 . 26 ASP CB C 40.5 0.1 1 251 . 26 ASP HA H 4.9276 0.02 1 252 . 26 ASP HB2 H 2.2858 0.02 2 253 . 26 ASP H H 8.416 0.02 1 254 . 26 ASP N N 125.16 0.1 1 255 . 27 PHE C C 174.31 0.1 1 256 . 27 PHE CA C 58.15 0.1 1 257 . 27 PHE CB C 39.55 0.1 1 258 . 27 PHE HA H 4.9796 0.02 1 259 . 27 PHE HB2 H 3.1817 0.02 2 260 . 27 PHE HB3 H 2.5737 0.02 2 261 . 27 PHE CD1 C 131.97 0.1 1 262 . 27 PHE HD1 H 7.15 0.02 1 263 . 27 PHE CE1 C 130.631 0.1 1 264 . 27 PHE HE1 H 6.982 0.02 1 265 . 27 PHE CZ C 128.089 0.1 1 266 . 27 PHE HZ H 6.73 0.02 1 267 . 27 PHE H H 8.701 0.02 1 268 . 27 PHE N N 125.26 0.1 1 269 . 28 SER C C 171.46 0.1 1 270 . 28 SER CA C 56.07 0.1 1 271 . 28 SER CB C 66.01 0.1 1 272 . 28 SER HA H 4.613 0.02 1 273 . 28 SER HB2 H 3.414 0.02 2 274 . 28 SER H H 8.757 0.02 1 275 . 28 SER N N 117.63 0.1 1 276 . 29 ALA C C 179.67 0.1 1 277 . 29 ALA CA C 51.77 0.1 1 278 . 29 ALA CB C 22.1 0.1 1 279 . 29 ALA HA H 4.549 0.02 1 280 . 29 ALA HB H 0.186 0.02 1 281 . 29 ALA H H 6.754 0.02 1 282 . 29 ALA N N 116.73 0.1 1 283 . 30 THR C C 175.1 0.1 1 284 . 30 THR CA C 65.25 0.1 1 285 . 30 THR CB C 69.2 0.1 1 286 . 30 THR CG2 C 21.92 0.1 1 287 . 30 THR HA H 3.885 0.02 1 288 . 30 THR HB H 4.249 0.02 1 289 . 30 THR HG2 H 1.358 0.02 1 290 . 30 THR H H 9.671 0.02 1 291 . 30 THR N N 116.25 0.1 1 292 . 31 TRP C C 175.98 0.1 1 293 . 31 TRP CA C 53.52 0.1 1 294 . 31 TRP CB C 29.3 0.1 1 295 . 31 TRP CD1 C 129.2 0.1 1 296 . 31 TRP NE1 N 135.674 0.1 1 297 . 31 TRP CE3 C 121 0.1 1 298 . 31 TRP CZ3 C 121.789 0.1 1 299 . 31 TRP CH2 C 125.31 0.1 1 300 . 31 TRP CZ2 C 115.43 0.1 1 301 . 31 TRP HA H 4.638 0.02 1 302 . 31 TRP HB2 H 3.165 0.02 2 303 . 31 TRP HB3 H 3.699 0.02 2 304 . 31 TRP HD1 H 7.342 0.02 1 305 . 31 TRP HE1 H 11.32 0.02 1 306 . 31 TRP H H 6.51 0.02 1 307 . 31 TRP HE3 H 7.35 0.02 1 308 . 31 TRP HZ3 H 7.125 0.02 1 309 . 31 TRP HH2 H 7.18 0.02 1 310 . 31 TRP HZ2 H 7.41 0.02 1 311 . 31 TRP N N 114.79 0.1 1 312 . 32 CYS CA C 53.48 0.1 1 313 . 32 CYS CB C 43.33 0.1 1 314 . 32 CYS HA H 4.64 0.02 1 315 . 32 CYS HB2 H 2.809 0.02 2 316 . 32 CYS H H 6.701 0.02 1 317 . 32 CYS N N 120.47 0.1 1 318 . 34 PRO C C 178.48 0.1 1 319 . 34 PRO CA C 65.21 0.1 1 320 . 34 PRO CB C 32.38 0.1 1 321 . 34 PRO CG C 28.01 0.1 1 322 . 34 PRO HA H 4.3854 0.02 1 323 . 34 PRO HB2 H 2.488 0.02 2 324 . 34 PRO HB3 H 1.6294 0.02 2 325 . 34 PRO HG2 H 2.1908 0.02 2 326 . 34 PRO HG3 H 2.0584 0.02 2 327 . 35 CYS C C 176.61 0.1 1 328 . 35 CYS CA C 62.68 0.1 1 329 . 35 CYS CB C 34.6 0.1 1 330 . 35 CYS HA H 4.394 0.02 1 331 . 35 CYS HB2 H 3.32 0.02 2 332 . 35 CYS HB3 H 3.684 0.02 2 333 . 35 CYS H H 8.105 0.02 1 334 . 35 CYS N N 111.27 0.1 1 335 . 36 LYS C C 178.84 0.1 1 336 . 36 LYS CA C 59.48 0.1 1 337 . 36 LYS CB C 32.39 0.1 1 338 . 36 LYS CD C 29.42 0.1 1 339 . 36 LYS CE C 43.01 0.1 1 340 . 36 LYS CG C 25.67 0.1 1 341 . 36 LYS HA H 3.928 0.02 1 342 . 36 LYS HB2 H 1.981 0.02 2 343 . 36 LYS HD2 H 1.722 0.02 2 344 . 36 LYS HE2 H 2.943 0.02 2 345 . 36 LYS HE3 H 3.028 0.02 2 346 . 36 LYS HG2 H 1.508 0.02 2 347 . 36 LYS H H 7.877 0.02 1 348 . 36 LYS N N 120.67 0.1 1 349 . 37 MET C C 177.43 0.1 1 350 . 37 MET CA C 57.76 0.1 1 351 . 37 MET CB C 32.49 0.1 1 352 . 37 MET CE C 17.23 0.1 1 353 . 37 MET CG C 32.7 0.1 1 354 . 37 MET HA H 4.185 0.02 1 355 . 37 MET HB2 H 2.729 0.02 1 356 . 37 MET HB3 H 2.579 0.02 1 357 . 37 MET HE H 2.13 0.02 1 358 . 37 MET HG2 H 2.193 0.02 2 359 . 37 MET H H 7.397 0.02 1 360 . 37 MET N N 116.18 0.1 1 361 . 38 ILE C C 176.73 0.1 1 362 . 38 ILE CA C 61.69 0.1 1 363 . 38 ILE CB C 39.83 0.1 1 364 . 38 ILE CD1 C 14.5 0.1 1 365 . 38 ILE CG1 C 28.95 0.1 1 366 . 38 ILE CG2 C 17.7 0.1 1 367 . 38 ILE HA H 4.016 0.02 1 368 . 38 ILE HB H 1.897 0.02 1 369 . 38 ILE HD1 H 0.859 0.02 1 370 . 38 ILE HG12 H 1.348 0.02 2 371 . 38 ILE HG13 H 1.618 0.02 2 372 . 38 ILE HG2 H 0.936 0.02 1 373 . 38 ILE H H 7.131 0.02 1 374 . 38 ILE N N 113.37 0.1 1 375 . 39 LYS CA C 61.63 0.1 1 376 . 39 LYS CB C 30.29 0.1 1 377 . 39 LYS CG C 25.16 0.1 1 378 . 39 LYS CD C 29.29 0.1 1 379 . 39 LYS CE C 39.97 0.1 1 380 . 39 LYS HA H 4.1541 0.02 1 381 . 39 LYS HB2 H 2.01 0.02 1 382 . 39 LYS HB3 H 1.976 0.02 1 383 . 39 LYS HG3 H 1.318 0.02 2 384 . 39 LYS HG2 H 1.592 0.02 2 385 . 39 LYS HD2 H 1.63 0.02 2 386 . 39 LYS HE2 H 3.05 0.02 2 387 . 39 LYS HE3 H 3.347 0.02 2 388 . 39 LYS H H 7.236 0.02 1 389 . 39 LYS N N 121.85 0.1 1 390 . 39 LYS C C 176.73 0.1 1 391 . 40 PRO C C 180.0851 0.1 1 392 . 40 PRO CA C 65.73 0.1 1 393 . 40 PRO CB C 31.08 0.1 1 394 . 40 PRO CG C 28.8565 0.1 1 395 . 40 PRO CD C 50.4449 0.1 1 396 . 40 PRO HA H 4.3713 0.02 1 397 . 40 PRO HB2 H 2.2822 0.02 2 398 . 40 PRO HB3 H 1.8795 0.02 2 399 . 40 PRO HG2 H 1.9 0.02 2 400 . 40 PRO HD2 H 3.5723 0.02 2 401 . 41 PHE C C 177.5694 0.1 1 402 . 41 PHE CA C 58.18 0.1 1 403 . 41 PHE CB C 38.49 0.1 1 404 . 41 PHE HA H 4.848 0.02 1 405 . 41 PHE HB2 H 3.248 0.02 2 406 . 41 PHE HB3 H 3.353 0.02 2 407 . 41 PHE CD1 C 131.2774 0.1 1 408 . 41 PHE HD1 H 7.3 0.02 1 409 . 41 PHE CD2 C 131.2774 0.1 1 410 . 41 PHE HD2 H 7.3 0.02 1 411 . 41 PHE HE1 H 7.5 0.02 1 412 . 41 PHE CE1 C 132.36 0.1 1 413 . 41 PHE H H 7.087 0.02 1 414 . 41 PHE N N 117.01 0.1 1 415 . 42 PHE C C 176.86 0.1 1 416 . 42 PHE CA C 62.44 0.1 1 417 . 42 PHE CB C 40 0.1 1 418 . 42 PHE HA H 4.1164 0.02 1 419 . 42 PHE HB2 H 3.0032 0.02 1 420 . 42 PHE HB3 H 3.3121 0.02 1 421 . 42 PHE CD1 C 131.87 0.1 1 422 . 42 PHE HD1 H 7.212 0.02 1 423 . 42 PHE H H 8.578 0.02 1 424 . 42 PHE N N 123.42 0.1 1 425 . 43 HIS C C 179.81 0.1 1 426 . 43 HIS CA C 60.19 0.1 1 427 . 43 HIS CB C 30.6 0.1 1 428 . 43 HIS CD2 C 119.11 0.1 1 429 . 43 HIS HA H 3.8576 0.02 1 430 . 43 HIS HB2 H 3.1182 0.02 1 431 . 43 HIS HD2 H 7.31 0.02 1 432 . 43 HIS H H 8.397 0.02 1 433 . 43 HIS N N 115.3 0.1 1 434 . 44 SER C C 177.46 0.1 1 435 . 44 SER CA C 61.96 0.1 1 436 . 44 SER CB C 63.03 0.1 1 437 . 44 SER HA H 4.163 0.02 1 438 . 44 SER HB2 H 4.035 0.02 2 439 . 44 SER H H 8.391 0.02 1 440 . 44 SER N N 117.41 0.1 1 441 . 45 LEU C C 178.73 0.1 1 442 . 45 LEU CA C 57.34 0.1 1 443 . 45 LEU CB C 41.45 0.1 1 444 . 45 LEU CG C 26.059 0.1 1 445 . 45 LEU CD1 C 23.247 0.1 1 446 . 45 LEU HA H 4.056 0.02 1 447 . 45 LEU HB2 H 1.6711 0.02 1 448 . 45 LEU HB3 H 1.3628 0.02 1 449 . 45 LEU HD1 H 0.8255 0.02 1 450 . 45 LEU HG H 0.87 0.02 1 451 . 45 LEU H H 8.119 0.02 1 452 . 45 LEU N N 121.57 0.1 1 453 . 46 SER C C 175.56 0.1 1 454 . 46 SER CA C 60.88 0.1 1 455 . 46 SER CB C 62.04 0.1 1 456 . 46 SER HA H 3.0079 0.02 1 457 . 46 SER HB2 H 3 0.02 2 458 . 46 SER H H 7.238 0.02 1 459 . 46 SER N N 114.94 0.1 1 460 . 47 GLU C C 177.35 0.1 1 461 . 47 GLU CA C 57.64 0.1 1 462 . 47 GLU CB C 29.98 0.1 1 463 . 47 GLU CG C 36.355 0.1 1 464 . 47 GLU HA H 4.1193 0.02 1 465 . 47 GLU HB2 H 2.0341 0.02 2 466 . 47 GLU HG2 H 2.2524 0.02 2 467 . 47 GLU H H 6.986 0.02 1 468 . 47 GLU N N 118.57 0.1 1 469 . 48 LYS C C 176.55 0.1 1 470 . 48 LYS CA C 56.45 0.1 1 471 . 48 LYS CB C 33.27 0.1 1 472 . 48 LYS CD C 25.41 0.1 1 473 . 48 LYS CE C 42.54 0.1 1 474 . 48 LYS CG C 28.95 0.1 1 475 . 48 LYS HA H 4.249 0.02 1 476 . 48 LYS HB2 H 1.7395 0.02 2 477 . 48 LYS HD2 H 1.3241 0.02 2 478 . 48 LYS HD3 H 1.2001 0.02 2 479 . 48 LYS HE2 H 2.8727 0.02 2 480 . 48 LYS HG2 H 1.5145 0.02 2 481 . 48 LYS H H 7.443 0.02 1 482 . 48 LYS N N 117.5 0.1 1 483 . 49 TYR C C 176.03 0.1 1 484 . 49 TYR CA C 56.79 0.1 1 485 . 49 TYR CB C 38.62 0.1 1 486 . 49 TYR HA H 4.784 0.02 1 487 . 49 TYR HB2 H 2.964 0.02 2 488 . 49 TYR H H 7.441 0.02 1 489 . 49 TYR HE1 H 6.773 0.02 1 490 . 49 TYR CE1 C 118.19 0.1 1 491 . 49 TYR HD1 H 7.27 0.02 1 492 . 49 TYR CD1 C 133.55 0.1 1 493 . 49 TYR N N 119.28 0.1 1 494 . 50 SER C C 175 0.1 1 495 . 50 SER CA C 59.9 0.1 1 496 . 50 SER CB C 63.47 0.1 1 497 . 50 SER HA H 4.441 0.02 1 498 . 50 SER HB2 H 3.992 0.02 2 499 . 50 SER HB3 H 3.885 0.02 2 500 . 50 SER H H 8.087 0.02 1 501 . 50 SER N N 115.7 0.1 1 502 . 51 ASN C C 172.91 0.1 1 503 . 51 ASN CA C 53.03 0.1 1 504 . 51 ASN CB C 38.08 0.1 1 505 . 51 ASN HA H 4.771 0.02 1 506 . 51 ASN HB2 H 2.967 0.02 2 507 . 51 ASN H H 8.947 0.02 1 508 . 51 ASN N N 118.38 0.1 1 509 . 51 ASN ND2 N 112.5902 0.1 1 510 . 51 ASN HD21 H 7.5986 0.02 2 511 . 51 ASN HD22 H 6.7958 0.02 2 512 . 52 VAL C C 174.605 0.1 1 513 . 52 VAL CA C 60.72 0.1 1 514 . 52 VAL CB C 34.99 0.1 1 515 . 52 VAL CG1 C 22.86 0.1 1 516 . 52 VAL CG2 C 22.39 0.1 1 517 . 52 VAL HA H 4.567 0.02 1 518 . 52 VAL HB H 2.044 0.02 1 519 . 52 VAL HG1 H 0.887 0.02 1 520 . 52 VAL HG2 H 0.331 0.02 1 521 . 52 VAL H H 7.502 0.02 1 522 . 52 VAL N N 119.66 0.1 1 523 . 53 ILE C C 174.06 0.1 1 524 . 53 ILE CA C 60.26 0.1 1 525 . 53 ILE CB C 38.97 0.1 1 526 . 53 ILE CD1 C 12.93 0.1 1 527 . 53 ILE CG1 C 17.70 0.1 1 528 . 53 ILE CG2 C 28.01 0.1 1 529 . 53 ILE HA H 4.334 0.02 1 530 . 53 ILE HB H 1.872 0.02 1 531 . 53 ILE HD1 H 0.845 0.02 1 532 . 53 ILE HG12 H 1.444 0.02 1 533 . 53 ILE HG13 H 1.615 0.02 1 534 . 53 ILE HG2 H 1.251 0.02 1 535 . 53 ILE H H 8.66 0.02 1 536 . 53 ILE N N 128.03 0.1 1 537 . 54 PHE C C 174.98 0.1 1 538 . 54 PHE CA C 56.4 0.1 1 539 . 54 PHE CB C 40.55 0.1 1 540 . 54 PHE HA H 5.255 0.02 1 541 . 54 PHE HB2 H 3.243 0.02 1 542 . 54 PHE HB3 H 2.386 0.02 1 543 . 54 PHE CD1 C 132.311 0.1 1 544 . 54 PHE HD1 H 6.524 0.02 1 545 . 54 PHE CE1 C 130.829 0.1 1 546 . 54 PHE HE1 H 6.957 0.02 1 547 . 54 PHE CZ C 128.468 0.1 1 548 . 54 PHE HZ H 6.622 0.02 1 549 . 54 PHE H H 9.118 0.02 1 550 . 54 PHE N N 127.73 0.1 1 551 . 55 LEU C C 175.02 0.1 1 552 . 55 LEU CA C 52.72 0.1 1 553 . 55 LEU CB C 45.59 0.1 1 554 . 55 LEU CG C 24.2035 0.1 1 555 . 55 LEU CD1 C 26.084 0.1 1 556 . 55 LEU HA H 5.4906 0.02 1 557 . 55 LEU HB2 H 1.7054 0.02 1 558 . 55 LEU HB3 H 1.2445 0.02 1 559 . 55 LEU HG H 1.4423 0.02 1 560 . 55 LEU HD1 H 0.7651 0.02 1 561 . 55 LEU HD2 H 0.4161 0.02 1 562 . 55 LEU H H 9.387 0.02 1 563 . 55 LEU N N 122.11 0.1 1 564 . 56 GLU C C 173.77 0.1 1 565 . 56 GLU CA C 54.66 0.1 1 566 . 56 GLU CB C 33.68 0.1 1 567 . 56 GLU CG C 33.17 0.1 1 568 . 56 GLU HA H 4.934 0.02 1 569 . 56 GLU HB2 H 1.829 0.02 2 570 . 56 GLU HG2 H 1.979 0.02 2 571 . 56 GLU HG3 H 2.086 0.02 2 572 . 56 GLU H H 8.473 0.02 1 573 . 56 GLU N N 121.35 0.1 1 574 . 57 VAL C C 173.63 0.1 1 575 . 57 VAL CA C 60.58 0.1 1 576 . 57 VAL CB C 34.64 0.1 1 577 . 57 VAL CG1 C 21.45 0.1 1 578 . 57 VAL CG2 C 20.98 0.1 1 579 . 57 VAL HA H 4.12 0.02 1 580 . 57 VAL HB H 1.273 0.02 1 581 . 57 VAL HG1 H 0.673 0.02 1 582 . 57 VAL HG2 H 0.309 0.02 1 583 . 57 VAL H H 8.487 0.02 1 584 . 57 VAL N N 125.48 0.1 1 585 . 58 ASP C C 177.99 0.1 1 586 . 58 ASP CA C 52.52 0.1 1 587 . 58 ASP CB C 42.06 0.1 1 588 . 58 ASP HA H 4.955 0.02 1 589 . 58 ASP HB2 H 2.921 0.02 2 590 . 58 ASP HB3 H 2.301 0.02 2 591 . 58 ASP H H 8.858 0.02 1 592 . 58 ASP N N 128.79 0.1 1 593 . 59 VAL C C 176.84 0.1 1 594 . 59 VAL CA C 63.98 0.1 1 595 . 59 VAL CB C 31.25 0.1 1 596 . 59 VAL CG1 C 18.17 0.1 1 597 . 59 VAL CG2 C 22.86 0.1 1 598 . 59 VAL HA H 4.08 0.02 1 599 . 59 VAL HB H 2.491 0.02 1 600 . 59 VAL HG1 H 1.011 0.02 1 601 . 59 VAL HG2 H 1.235 0.02 1 602 . 59 VAL H H 8.789 0.02 1 603 . 59 VAL N N 119.32 0.1 1 604 . 60 ASP C C 177.29 0.1 1 605 . 60 ASP CA C 56.07 0.1 1 606 . 60 ASP CB C 40.98 0.1 1 607 . 60 ASP HA H 4.87 0.02 1 608 . 60 ASP HB2 H 2.793 0.02 2 609 . 60 ASP HB3 H 2.9 0.02 2 610 . 60 ASP H H 8.625 0.02 1 611 . 60 ASP N N 119.88 0.1 1 612 . 61 ASP C C 176.39 0.1 1 613 . 61 ASP CA C 55.99 0.1 1 614 . 61 ASP CB C 41.91 0.1 1 615 . 61 ASP HA H 4.741 0.02 1 616 . 61 ASP HB2 H 2.879 0.02 1 617 . 61 ASP HB3 H 2.686 0.02 1 618 . 61 ASP H H 8.064 0.02 1 619 . 61 ASP N N 121.14 0.1 1 620 . 62 ALA C C 177.03 0.1 1 621 . 62 ALA CA C 50.35 0.1 1 622 . 62 ALA CB C 18 0.1 1 623 . 62 ALA HA H 4.724 0.02 1 624 . 62 ALA HB H 1.123 0.02 1 625 . 62 ALA H H 8.072 0.02 1 626 . 62 ALA N N 123.89 0.1 1 627 . 63 GLN C C 176.69 0.1 1 628 . 63 GLN CA C 58.24 0.1 1 629 . 63 GLN CB C 29.23 0.1 1 630 . 63 GLN CG C 34.57 0.1 1 631 . 63 GLN HB2 H 2.09 0.02 2 632 . 63 GLN HB3 H 2.211 0.02 2 633 . 63 GLN HG2 H 2.51 0.02 2 634 . 63 GLN HA H 4.228 0.02 1 635 . 63 GLN H H 8.087 0.02 1 636 . 63 GLN N N 120.33 0.1 1 637 . 63 GLN NE2 N 111.5219 0.1 1 638 . 63 GLN HE21 H 7.5639 0.02 2 639 . 63 GLN HE22 H 6.8111 0.02 2 640 . 64 ASP C C 176.38 0.1 1 641 . 64 ASP CA C 54.45 0.1 1 642 . 64 ASP CB C 40.09 0.1 1 643 . 64 ASP HA H 4.484 0.02 1 644 . 64 ASP HB2 H 2.772 0.02 1 645 . 64 ASP HB3 H 2.9 0.02 1 646 . 64 ASP H H 9.039 0.02 1 647 . 64 ASP N N 115.52 0.1 1 648 . 65 VAL C C 177.05 0.1 1 649 . 65 VAL CA C 65.82 0.1 1 650 . 65 VAL CB C 32.62 0.1 1 651 . 65 VAL CG1 C 22.39 0.1 1 652 . 65 VAL CG2 C 21.92 0.1 1 653 . 65 VAL HA H 3.799 0.02 1 654 . 65 VAL HB H 1.915 0.02 1 655 . 65 VAL HG1 H 0.716 0.02 1 656 . 65 VAL HG2 H 0.545 0.02 1 657 . 65 VAL H H 7.542 0.02 1 658 . 65 VAL N N 119.58 0.1 1 659 . 66 ALA CA C 56.46 0.1 1 660 . 66 ALA CB C 16.46 0.1 1 661 . 66 ALA HA H 3.93 0.02 1 662 . 66 ALA HB H 1.36 0.02 1 663 . 66 ALA H H 9.119 0.02 1 664 . 66 ALA N N 121.08 0.1 1 665 . 67 PRO C C 179.59 0.1 1 666 . 67 PRO CA C 65.67 0.1 1 667 . 67 PRO CB C 30.771 0.1 1 668 . 67 PRO CG C 28.0266 0.1 1 669 . 67 PRO CD C 50.445 0.1 1 670 . 67 PRO HA H 4.3051 0.02 1 671 . 67 PRO HB2 H 2.2896 0.02 2 672 . 67 PRO HB3 H 2.0365 0.02 2 673 . 67 PRO HG2 H 2.0365 0.02 2 674 . 67 PRO HG3 H 1.7454 0.02 2 675 . 67 PRO HD2 H 3.381 0.02 2 676 . 67 PRO HD3 H 3.6955 0.02 2 677 . 68 LYS C C 177.17 0.1 1 678 . 68 LYS CA C 58.26 0.1 1 679 . 68 LYS CB C 31.86 0.1 1 680 . 68 LYS CD C 29.2 0.1 1 681 . 68 LYS CE C 42.54 0.1 1 682 . 68 LYS CG C 25.2 0.1 1 683 . 68 LYS HA H 3.885 0.02 1 684 . 68 LYS HB2 H 1.68 0.02 2 685 . 68 LYS HB3 H 1.573 0.02 2 686 . 68 LYS HD2 H 1.466 0.02 2 687 . 68 LYS HE2 H 2.964 0.02 2 688 . 68 LYS HE3 H 2.857 0.02 2 689 . 68 LYS HG2 H 1.037 0.02 2 690 . 68 LYS HG3 H 0.673 0.02 2 691 . 68 LYS H H 7.122 0.02 1 692 . 68 LYS N N 117.76 0.1 1 693 . 69 TYR C C 175.3 0.1 1 694 . 69 TYR CA C 58.13 0.1 1 695 . 69 TYR CB C 39.13 0.1 1 696 . 69 TYR HA H 4.527 0.02 1 697 . 69 TYR HB2 H 3.392 0.02 1 698 . 69 TYR HB3 H 2.215 0.02 1 699 . 69 TYR CD1 C 133.187 0.1 1 700 . 69 TYR HD1 H 7.17 0.02 1 701 . 69 TYR CD2 C 133.187 0.1 1 702 . 69 TYR HD2 H 7.17 0.02 1 703 . 69 TYR CE1 C 117.964 0.1 1 704 . 69 TYR HE1 H 6.798 0.02 1 705 . 69 TYR CE2 C 117.964 0.1 1 706 . 69 TYR HE2 H 6.798 0.02 1 707 . 69 TYR H H 7.134 0.02 1 708 . 69 TYR N N 114.32 0.1 1 709 . 70 GLY C C 174.63 0.1 1 710 . 70 GLY CA C 46.77 0.1 1 711 . 70 GLY HA2 H 3.721 0.02 1 712 . 70 GLY HA3 H 3.88 0.02 1 713 . 70 GLY H H 7.542 0.02 1 714 . 70 GLY N N 107.69 0.1 1 715 . 71 ILE C C 176.47 0.1 1 716 . 71 ILE CA C 60.25 0.1 1 717 . 71 ILE CB C 35.96 0.1 1 718 . 71 ILE CD1 C 11.14 0.1 1 719 . 71 ILE CG1 C 27.08 0.1 1 720 . 71 ILE CG2 C 17.23 0.1 1 721 . 71 ILE HA H 3.799 0.02 1 722 . 71 ILE HB H 1.573 0.02 1 723 . 71 ILE HD1 H 0.095 0.02 1 724 . 71 ILE HG12 H 0.973 0.02 2 725 . 71 ILE HG13 H 0.459 0.02 2 726 . 71 ILE HG2 H 0.566 0.02 1 727 . 71 ILE H H 7.192 0.02 1 728 . 71 ILE N N 118.92 0.1 1 729 . 72 ARG C C 175.55 0.1 1 730 . 72 ARG CA C 55.94 0.1 1 731 . 72 ARG CB C 31.56 0.1 1 732 . 72 ARG CD C 43 0.1 1 733 . 72 ARG CG C 27.08 0.1 1 734 . 72 ARG HA H 4.42 0.02 1 735 . 72 ARG HB2 H 1.665 0.02 2 736 . 72 ARG HB3 H 1.876 0.02 2 737 . 72 ARG HD2 H 3.135 0.02 2 738 . 72 ARG HG2 H 1.551 0.02 2 739 . 72 ARG H H 8.615 0.02 1 740 . 72 ARG N N 128.1 0.1 1 741 . 73 GLY C C 171 0.1 1 742 . 73 GLY CA C 44.81 0.1 1 743 . 73 GLY HA2 H 3.669 0.02 1 744 . 73 GLY HA3 H 4.196 0.02 1 745 . 73 GLY H H 7.649 0.02 1 746 . 73 GLY N N 108.41 0.1 1 747 . 74 ILE CA C 57.41 0.1 1 748 . 74 ILE CB C 39.97 0.1 1 749 . 74 ILE CD1 C 14.88 0.1 1 750 . 74 ILE CG1 C 25.2 0.1 1 751 . 74 ILE CG2 C 18.64 0.1 1 752 . 74 ILE HA H 4.62 0.02 1 753 . 74 ILE HB H 1.872 0.02 1 754 . 74 ILE HD1 H 0.459 0.02 1 755 . 74 ILE HG12 H 1.209 0.02 2 756 . 74 ILE HG13 H 1.358 0.02 2 757 . 74 ILE HG2 H 0.695 0.02 1 758 . 74 ILE H H 8.131 0.02 1 759 . 74 ILE N N 115.87 0.1 1 760 . 75 PRO C C 177.04 0.1 1 761 . 75 PRO CA C 63.546 0.1 1 762 . 75 PRO CB C 34.96 0.1 1 763 . 75 PRO CG C 25.117 0.1 1 764 . 75 PRO CD C 51 0.1 1 765 . 75 PRO HA H 4.8597 0.02 1 766 . 75 PRO HB2 H 1.9996 0.02 2 767 . 75 PRO HB3 H 2.6449 0.02 2 768 . 75 PRO HG2 H 1.6896 0.02 2 769 . 75 PRO HD2 H 3.6 0.02 2 770 . 76 THR C C 171.65 0.1 1 771 . 76 THR CA C 63.77 0.1 1 772 . 76 THR CB C 73.851 0.1 1 773 . 76 THR CG2 C 22.39 0.1 1 774 . 76 THR HA H 4.89 0.02 1 775 . 76 THR HB H 3.7981 0.02 1 776 . 76 THR HG2 H 1.05 0.02 1 777 . 76 THR H H 7.753 0.02 1 778 . 76 THR N N 117.85 0.1 1 779 . 77 LEU C C 171.62 0.1 1 780 . 77 LEU CA C 53.41 0.1 1 781 . 77 LEU CB C 44.93 0.1 1 782 . 77 LEU CD1 C 26.14 0.1 1 783 . 77 LEU CD2 C 26.14 0.1 1 784 . 77 LEU CG C 28.01 0.1 1 785 . 77 LEU HA H 5.769 0.02 1 786 . 77 LEU HB2 H 1.551 0.02 1 787 . 77 LEU HB3 H 1.337 0.02 1 788 . 77 LEU HD1 H 0.738 0.02 1 789 . 77 LEU HD2 H 0.738 0.02 1 790 . 77 LEU HG H 1.615 0.02 1 791 . 77 LEU H H 9.061 0.02 1 792 . 77 LEU N N 127.35 0.1 1 793 . 78 LEU C C 175.02 0.1 1 794 . 78 LEU CA C 53.5 0.1 1 795 . 78 LEU CB C 47.24 0.1 1 796 . 78 LEU CD1 C 26.61 0.1 1 797 . 78 LEU CD2 C 25.2 0.1 1 798 . 78 LEU CG C 27.54 0.1 1 799 . 78 LEU HA H 5.169 0.02 1 800 . 78 LEU HG H 1.6209 0.02 1 801 . 78 LEU HB2 H 1.7313 0.02 1 802 . 78 LEU HB3 H 1.3318 0.02 1 803 . 78 LEU HD1 H 0.82 0.02 1 804 . 78 LEU HD2 H 0.87 0.02 1 805 . 78 LEU H H 8.988 0.02 1 806 . 78 LEU N N 121.73 0.1 1 807 . 79 LEU C C 175.92 0.1 1 808 . 79 LEU CA C 53.3 0.1 1 809 . 79 LEU CB C 45.13 0.1 1 810 . 79 LEU CD1 C 25.2 0.1 1 811 . 79 LEU CD2 C 25.67 0.1 1 812 . 79 LEU CG C 28.01 0.1 1 813 . 79 LEU HA H 5.578 0.02 1 814 . 79 LEU HB2 H 1.35 0.02 1 815 . 79 LEU HB3 H 1.61 0.02 1 816 . 79 LEU HG H 1.45 0.02 1 817 . 79 LEU HD1 H 0.5 0.02 2 818 . 79 LEU HD2 H 0.607 0.02 2 819 . 79 LEU H H 8.447 0.02 1 820 . 79 LEU N N 122.51 0.1 1 821 . 80 PHE C C 175.12 0.1 1 822 . 80 PHE CA C 56.79 0.1 1 823 . 80 PHE CB C 43.22 0.1 1 824 . 80 PHE HA H 5.232 0.02 1 825 . 80 PHE HB2 H 2.565 0.02 1 826 . 80 PHE HB3 H 2.844 0.02 1 827 . 80 PHE CD1 C 131.323 0.1 1 828 . 80 PHE HD1 H 6.752 0.02 1 829 . 80 PHE CE1 C 131.638 0.1 1 830 . 80 PHE HE1 H 7.102 0.02 1 831 . 80 PHE H H 10.079 0.02 1 832 . 80 PHE N N 124.68 0.1 1 833 . 81 LYS C C 176.56 0.1 1 834 . 81 LYS CA C 56.03 0.1 1 835 . 81 LYS CB C 36.09 0.1 1 836 . 81 LYS CD C 29.42 0.1 1 837 . 81 LYS CE C 42.54 0.1 1 838 . 81 LYS CG C 25.67 0.1 1 839 . 81 LYS HA H 4.506 0.02 1 840 . 81 LYS HB2 H 1.765 0.02 1 841 . 81 LYS HB3 H 1.506 0.02 1 842 . 81 LYS HD2 H 1.62 0.02 2 843 . 81 LYS HE2 H 2.9123 0.02 2 844 . 81 LYS HG2 H 1.316 0.02 2 845 . 81 LYS HG3 H 1.2606 0.02 2 846 . 81 LYS H H 8.742 0.02 1 847 . 81 LYS N N 118.82 0.1 1 848 . 82 ASN C C 175.87 0.1 1 849 . 82 ASN CA C 54.63 0.1 1 850 . 82 ASN CB C 37.75 0.1 1 851 . 82 ASN HA H 4.42 0.02 1 852 . 82 ASN HB2 H 2.814 0.02 1 853 . 82 ASN HB3 H 3.088 0.02 1 854 . 82 ASN H H 9.869 0.02 1 855 . 82 ASN N N 126.6 0.1 1 856 . 82 ASN ND2 N 112.0175 0.1 1 857 . 82 ASN HD21 H 7.546 0.02 1 858 . 82 ASN HD22 H 6.9704 0.02 1 859 . 83 GLY C C 173.3 0.1 1 860 . 83 GLY CA C 46.03 0.1 1 861 . 83 GLY HA2 H 3.405 0.02 1 862 . 83 GLY HA3 H 4.249 0.02 1 863 . 83 GLY H H 9.146 0.02 1 864 . 83 GLY N N 103.17 0.1 1 865 . 84 GLU C C 175.53 0.1 1 866 . 84 GLU CA C 54.19 0.1 1 867 . 84 GLU CB C 33.14 0.1 1 868 . 84 GLU CG C 35.98 0.1 1 869 . 84 GLU HA H 4.955 0.02 1 870 . 84 GLU HB2 H 1.915 0.02 2 871 . 84 GLU HB3 H 2.108 0.02 2 872 . 84 GLU HG2 H 2.279 0.02 2 873 . 84 GLU HG3 H 2.343 0.02 2 874 . 84 GLU H H 7.758 0.02 1 875 . 84 GLU N N 119.39 0.1 1 876 . 85 VAL C C 176.36 0.1 1 877 . 85 VAL CA C 64.51 0.1 1 878 . 85 VAL CB C 31.66 0.1 1 879 . 85 VAL CG2 C 23.33 0.1 2 880 . 85 VAL HA H 3.23 0.02 1 881 . 85 VAL HB H 1.836 0.02 1 882 . 85 VAL HG2 H 0.627 0.02 2 883 . 85 VAL H H 8.79 0.02 1 884 . 85 VAL N N 123.27 0.1 1 885 . 86 ALA C C 177.24 0.1 1 886 . 86 ALA CA C 52.15 0.1 1 887 . 86 ALA CB C 21.01 0.1 1 888 . 86 ALA HA H 4.566 0.02 1 889 . 86 ALA HB H 1.273 0.02 1 890 . 86 ALA H H 9.587 0.02 1 891 . 86 ALA N N 132.73 0.1 1 892 . 87 ALA C C 175.02 0.1 1 893 . 87 ALA CA C 52.51 0.1 1 894 . 87 ALA CB C 22.28 0.1 1 895 . 87 ALA HA H 4.618 0.02 1 896 . 87 ALA HB H 1.444 0.02 1 897 . 87 ALA H H 7.677 0.02 1 898 . 87 ALA N N 118.05 0.1 1 899 . 88 THR C C 173.29 0.1 1 900 . 88 THR CA C 61.54 0.1 1 901 . 88 THR CB C 72.18 0.1 1 902 . 88 THR CG2 C 20.985 0.1 1 903 . 88 THR HA H 5.115 0.02 1 904 . 88 THR HB H 3.818 0.02 1 905 . 88 THR HG2 H 1.051 0.02 1 906 . 88 THR H H 8.358 0.02 1 907 . 88 THR N N 114.01 0.1 1 908 . 89 LYS C C 174.39 0.1 1 909 . 89 LYS CA C 54.77 0.1 1 910 . 89 LYS CB C 34.59 0.1 1 911 . 89 LYS CE C 42.54 0.1 1 912 . 89 LYS CG C 28.48 0.1 1 913 . 89 LYS HA H 4.506 0.02 1 914 . 89 LYS HB2 H 1.251 0.02 1 915 . 89 LYS HB3 H 0.78 0.02 1 916 . 89 LYS HE2 H 2.664 0.02 2 917 . 89 LYS HG2 H 1.423 0.02 2 918 . 89 LYS H H 8.963 0.02 1 919 . 89 LYS N N 126.05 0.1 1 920 . 90 VAL C C 176.4 0.1 1 921 . 90 VAL CA C 61.82 0.1 1 922 . 90 VAL CB C 34.05 0.1 1 923 . 90 VAL CG1 C 20.98 0.1 2 924 . 90 VAL HA H 4.506 0.02 1 925 . 90 VAL HB H 1.958 0.02 1 926 . 90 VAL HG1 H 0.887 0.02 2 927 . 90 VAL H H 8.733 0.02 1 928 . 90 VAL N N 127.36 0.1 1 929 . 91 GLY C C 172.31 0.1 1 930 . 91 GLY CA C 43.95 0.1 1 931 . 91 GLY HA2 H 3.616 0.02 1 932 . 91 GLY HA3 H 4.355 0.02 1 933 . 91 GLY H H 8.133 0.02 1 934 . 91 GLY N N 113.55 0.1 1 935 . 92 ALA C C 176.58 0.1 1 936 . 92 ALA CA C 52.85 0.1 1 937 . 92 ALA CB C 19.12 0.1 1 938 . 92 ALA HA H 4.035 0.02 1 939 . 92 ALA HB H 1.316 0.02 1 940 . 92 ALA H H 8.159 0.02 1 941 . 92 ALA N N 119.82 0.1 1 942 . 93 LEU C C 175.56 0.1 1 943 . 93 LEU CA C 54.23 0.1 1 944 . 93 LEU CB C 44.79 0.1 1 945 . 93 LEU CD1 C 26.71 0.1 1 946 . 93 LEU CD2 C 24.73 0.1 1 947 . 93 LEU CG C 27.08 0.1 1 948 . 93 LEU HA H 4.673 0.02 1 949 . 93 LEU HB2 H 1.56 0.02 1 950 . 93 LEU HG H 1.7112 0.02 1 951 . 93 LEU HD1 H 0.651 0.02 1 952 . 93 LEU HD2 H 0.697 0.02 1 953 . 93 LEU H H 7.388 0.02 1 954 . 93 LEU N N 121.37 0.1 1 955 . 94 SER C C 174.77 0.1 1 956 . 94 SER CA C 56.34 0.1 1 957 . 94 SER CB C 65.77 0.1 1 958 . 94 SER HA H 4.62 0.02 1 959 . 94 SER HB2 H 3.885 0.02 1 960 . 94 SER HB3 H 4.249 0.02 1 961 . 94 SER H H 8.318 0.02 1 962 . 94 SER N N 115.21 0.1 1 963 . 95 LYS C C 178.72 0.1 1 964 . 95 LYS CA C 60.68 0.1 1 965 . 95 LYS CB C 31.8 0.1 1 966 . 95 LYS CD C 29.799 0.1 1 967 . 95 LYS CG C 25.139 0.1 1 968 . 95 LYS CE C 42.001 0.1 1 969 . 95 LYS HA H 3.3335 0.02 1 970 . 95 LYS HB2 H 1.4418 0.02 2 971 . 95 LYS HD2 H 1.1853 0.02 2 972 . 95 LYS HG2 H 1.043 0.02 2 973 . 95 LYS HG3 H 0.9203 0.02 2 974 . 95 LYS HE2 H 2.7818 0.02 2 975 . 95 LYS H H 8.389 0.02 1 976 . 95 LYS N N 121.92 0.1 1 977 . 96 GLY C C 177.05 0.1 1 978 . 96 GLY CA C 46.87 0.1 1 979 . 96 GLY HA2 H 3.79 0.02 1 980 . 96 GLY H H 8.501 0.02 1 981 . 96 GLY N N 105.56 0.1 1 982 . 97 GLN C C 179.62 0.1 1 983 . 97 GLN CA C 58.33 0.1 1 984 . 97 GLN CB C 29.8 0.1 1 985 . 97 GLN CG C 35 0.1 1 986 . 97 GLN HA H 4.142 0.02 1 987 . 97 GLN HB2 H 1.928 0.02 1 988 . 97 GLN HB3 H 2.087 0.02 1 989 . 97 GLN HG2 H 2.423 0.02 2 990 . 97 GLN H H 7.685 0.02 1 991 . 97 GLN N N 120.98 0.1 1 992 . 97 GLN NE2 N 112.2188 0.1 1 993 . 97 GLN HE21 H 7.6762 0.02 2 994 . 97 GLN HE22 H 6.8613 0.02 2 995 . 98 LEU C C 177.6 0.1 1 996 . 98 LEU CA C 58.49 0.1 1 997 . 98 LEU CB C 41.45 0.1 1 998 . 98 LEU CD1 C 26.61 0.1 1 999 . 98 LEU CD2 C 24.73 0.1 1 1000 . 98 LEU HA H 4.12 0.02 1 1001 . 98 LEU HB2 H 1.658 0.02 1 1002 . 98 LEU HD1 H 1.123 0.02 1 1003 . 98 LEU HD2 H 1.08 0.02 1 1004 . 98 LEU H H 8.351 0.02 1 1005 . 98 LEU N N 122.85 0.1 1 1006 . 99 LYS C C 177.64 0.1 1 1007 . 99 LYS CA C 60.32 0.1 1 1008 . 99 LYS CB C 32.9 0.1 1 1009 . 99 LYS CD C 29.89 0.1 1 1010 . 99 LYS CE C 42.08 0.1 1 1011 . 99 LYS CG C 25.4143 0.1 1 1012 . 99 LYS HA H 3.9199 0.02 1 1013 . 99 LYS HB2 H 1.903 0.02 2 1014 . 99 LYS HB3 H 2.0419 0.02 2 1015 . 99 LYS HD2 H 1.7254 0.02 2 1016 . 99 LYS HE2 H 3.0579 0.02 2 1017 . 99 LYS HG2 H 1.51 0.02 2 1018 . 99 LYS HG3 H 1.66 0.02 2 1019 . 99 LYS H H 8.169 0.02 1 1020 . 99 LYS N N 119.2 0.1 1 1021 . 100 GLU C C 178.91 0.1 1 1022 . 100 GLU CA C 59.84 0.1 1 1023 . 100 GLU CB C 30.06 0.1 1 1024 . 100 GLU CG C 36.3562 0.1 1 1025 . 100 GLU HB2 H 2.13 0.02 2 1026 . 100 GLU HG2 H 2.472 0.02 2 1027 . 100 GLU HG3 H 2.305 0.02 2 1028 . 100 GLU HA H 4.0813 0.02 1 1029 . 100 GLU H H 8.042 0.02 1 1030 . 100 GLU N N 117.06 0.1 1 1031 . 101 PHE C C 177.28 0.1 1 1032 . 101 PHE CA C 59.94 0.1 1 1033 . 101 PHE CB C 39.39 0.1 1 1034 . 101 PHE HA H 4.441 0.02 1 1035 . 101 PHE HB2 H 3.243 0.02 2 1036 . 101 PHE CD1 C 131.57 0.1 1 1037 . 101 PHE HD1 H 7.14 0.02 1 1038 . 101 PHE CE1 C 130.76 0.1 1 1039 . 101 PHE HE1 H 6.97 0.02 1 1040 . 101 PHE H H 7.82 0.02 1 1041 . 101 PHE N N 119.93 0.1 1 1042 . 102 LEU C C 178.72 0.1 1 1043 . 102 LEU CA C 58.13 0.1 1 1044 . 102 LEU CB C 40.63 0.1 1 1045 . 102 LEU CD1 C 23.33 0.1 1 1046 . 102 LEU CD2 C 26.14 0.1 1 1047 . 102 LEU CG C 27.08 0.1 1 1048 . 102 LEU HA H 3.585 0.02 1 1049 . 102 LEU HB2 H 0.994 0.02 1 1050 . 102 LEU HB3 H 1.82 0.02 1 1051 . 102 LEU HD1 H 0.481 0.02 1 1052 . 102 LEU HD2 H 0.588 0.02 1 1053 . 102 LEU HG H 1.808 0.02 1 1054 . 102 LEU H H 8.014 0.02 1 1055 . 102 LEU N N 119.42 0.1 1 1056 . 103 ASP C C 179.17 0.1 1 1057 . 103 ASP CA C 57.76 0.1 1 1058 . 103 ASP CB C 40.17 0.1 1 1059 . 103 ASP HA H 4.399 0.02 1 1060 . 103 ASP HB2 H 2.729 0.02 2 1061 . 103 ASP HB3 H 2.643 0.02 2 1062 . 103 ASP H H 8.886 0.02 1 1063 . 103 ASP N N 118.65 0.1 1 1064 . 104 ALA C C 178.56 0.1 1 1065 . 104 ALA CA C 53.9 0.1 1 1066 . 104 ALA CB C 19.24 0.1 1 1067 . 104 ALA HA H 4.1652 0.02 1 1068 . 104 ALA HB H 1.423 0.02 1 1069 . 104 ALA H H 7.771 0.02 1 1070 . 104 ALA N N 118.44 0.1 1 1071 . 105 ASN C C 174.1 0.1 1 1072 . 105 ASN CA C 54.19 0.1 1 1073 . 105 ASN CB C 42.11 0.1 1 1074 . 105 ASN HA H 4.6887 0.02 1 1075 . 105 ASN HB2 H 1.9675 0.02 2 1076 . 105 ASN HB3 H 2.3569 0.02 2 1077 . 105 ASN H H 7.334 0.02 1 1078 . 105 ASN N N 113.63 0.1 1 1079 . 105 ASN ND2 N 116.3319 0.1 1 1080 . 105 ASN HD21 H 7.2278 0.02 2 1081 . 105 ASN HD22 H 6.6522 0.02 2 1082 . 106 LEU C C 176.18 0.1 1 1083 . 106 LEU CA C 55.59 0.1 1 1084 . 106 LEU CB C 42.29 0.1 1 1085 . 106 LEU CD1 C 23.79 0.1 2 1086 . 106 LEU CD2 C 26.14 0.1 2 1087 . 106 LEU CG C 26.577 0.1 1 1088 . 106 LEU HA H 4.313 0.02 1 1089 . 106 LEU HB2 H 1.722 0.02 2 1090 . 106 LEU HB3 H 1.573 0.02 2 1091 . 106 LEU HG H 1.723 0.02 1 1092 . 106 LEU HD1 H 0.738 0.02 1 1093 . 106 LEU HD2 H 0.738 0.02 1 1094 . 106 LEU H H 7.506 0.02 1 1095 . 106 LEU N N 120.92 0.1 1 1096 . 107 VAL CA C 63.56 0.1 1 1097 . 107 VAL CB C 33.36 0.1 1 1098 . 107 VAL CG1 C 20.04 0.1 2 1099 . 107 VAL CG2 C 21.92 0.1 2 1100 . 107 VAL HA H 4.034 0.02 1 1101 . 107 VAL HB H 2.093 0.02 1 1102 . 107 VAL HG1 H 0.889 0.02 1 1103 . 107 VAL HG2 H 0.889 0.02 1 1104 . 107 VAL H H 7.089 0.02 1 1105 . 107 VAL N N 122.21 0.1 1 stop_ save_