data_27798 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N backbone chemical shift assignments of a mutated variant of UBE2S ; _BMRB_accession_number 27798 _BMRB_flat_file_name bmr27798.str _Entry_type original _Submission_date 2019-02-22 _Accession_date 2019-02-22 _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 Schweimer Kristian . . 2 Liess Anna K.L. . 3 Lorenz Sonja . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 137 "13C chemical shifts" 423 "15N chemical shifts" 137 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-09-20 update BMRB 'update entry citation' 2019-06-27 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 17437 '1H, 13C and 15N backbone chemical shift assignments of the UBC domain of Ube2S WT' 27799 '1H, 13C and 15N backbone chemical shift assignments of an Ube2S-ubiquitin -conjugate' stop_ _Original_release_date 2019-02-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Autoinhibition Mechanism of the Ubiquitin-Conjugating Enzyme UBE2S by Autoubiquitination ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 31230944 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liess Anna . . 2 Kucerova Alena . . 3 Schweimer Kristian . . 4 Yu Lu . . 5 Roumeliotis Theodoros I. . 6 Diebold Mathias . . 7 Dybkov Olexandr . . 8 Sotriffer Christoph . . 9 Urlaub Henning . . 10 Choudhary Jyoti S. . 11 Mansfeld Jorg . . 12 Lorenz Sonja . . stop_ _Journal_abbreviation Structure _Journal_volume 27 _Journal_issue 8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1195 _Page_last 1210 _Year 2019 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'UBE2S monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'UBE2S UBC' $UBE2S stop_ _System_molecular_weight 17355.96 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_UBE2S _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common UBE2S _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'ubiquitin-conjugating enzyme, catalytic domain' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 156 _Mol_residue_sequence ; MNSNVENLPPHIIRLVYKEV TTLTADPPDGIKVFPNEEDL TDLQVTIEGPEGTPYAGGLF RMKLLLGKDFPASPPKGYFL TKIFHPNVGANGEISVNVLC RDWTAELGIRHVLLTIKMLL IHPNPESALNEEAGRLLLEN YEEYAARARLLTEIHG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 ASN 3 3 SER 4 4 ASN 5 5 VAL 6 6 GLU 7 7 ASN 8 8 LEU 9 9 PRO 10 10 PRO 11 11 HIS 12 12 ILE 13 13 ILE 14 14 ARG 15 15 LEU 16 16 VAL 17 17 TYR 18 18 LYS 19 19 GLU 20 20 VAL 21 21 THR 22 22 THR 23 23 LEU 24 24 THR 25 25 ALA 26 26 ASP 27 27 PRO 28 28 PRO 29 29 ASP 30 30 GLY 31 31 ILE 32 32 LYS 33 33 VAL 34 34 PHE 35 35 PRO 36 36 ASN 37 37 GLU 38 38 GLU 39 39 ASP 40 40 LEU 41 41 THR 42 42 ASP 43 43 LEU 44 44 GLN 45 45 VAL 46 46 THR 47 47 ILE 48 48 GLU 49 49 GLY 50 50 PRO 51 51 GLU 52 52 GLY 53 53 THR 54 54 PRO 55 55 TYR 56 56 ALA 57 57 GLY 58 58 GLY 59 59 LEU 60 60 PHE 61 61 ARG 62 62 MET 63 63 LYS 64 64 LEU 65 65 LEU 66 66 LEU 67 67 GLY 68 68 LYS 69 69 ASP 70 70 PHE 71 71 PRO 72 72 ALA 73 73 SER 74 74 PRO 75 75 PRO 76 76 LYS 77 77 GLY 78 78 TYR 79 79 PHE 80 80 LEU 81 81 THR 82 82 LYS 83 83 ILE 84 84 PHE 85 85 HIS 86 86 PRO 87 87 ASN 88 88 VAL 89 89 GLY 90 90 ALA 91 91 ASN 92 92 GLY 93 93 GLU 94 94 ILE 95 95 SER 96 96 VAL 97 97 ASN 98 98 VAL 99 99 LEU 100 100 CYS 101 101 ARG 102 102 ASP 103 103 TRP 104 104 THR 105 105 ALA 106 106 GLU 107 107 LEU 108 108 GLY 109 109 ILE 110 110 ARG 111 111 HIS 112 112 VAL 113 113 LEU 114 114 LEU 115 115 THR 116 116 ILE 117 117 LYS 118 118 MET 119 119 LEU 120 120 LEU 121 121 ILE 122 122 HIS 123 123 PRO 124 124 ASN 125 125 PRO 126 126 GLU 127 127 SER 128 128 ALA 129 129 LEU 130 130 ASN 131 131 GLU 132 132 GLU 133 133 ALA 134 134 GLY 135 135 ARG 136 136 LEU 137 137 LEU 138 138 LEU 139 139 GLU 140 140 ASN 141 141 TYR 142 142 GLU 143 143 GLU 144 144 TYR 145 145 ALA 146 146 ALA 147 147 ARG 148 148 ALA 149 149 ARG 150 150 LEU 151 151 LEU 152 152 THR 153 153 GLU 154 154 ILE 155 155 HIS 156 156 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 1zdn Ube2S . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $UBE2S Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name _Details $UBE2S 'recombinant technology' . Escherichia coli . 'modified pSKB2 vector' 'For vector details, see Wickliffe et al., Cell 2011' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $UBE2S 0.6 mM '[U-100% 13C; U-100% 15N]' D2O 5 % 'natural abundance' 'sodium phosphate' 75 mM 'natural abundance' DTT 5 mM 'natural abundance' EDTA 1 mM 'natural abundance' TCEP 2 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details CryoProbe save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(COCA)CB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _Sample_label $sample_1 save_ save_3D_C(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 0.00 na indirect . 'separate tube (no insert) similar to the experimental sample tube' . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . 'separate tube (no insert) similar to the experimental sample tube' . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . 'separate tube (no insert) similar to the experimental sample tube' . 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCA' '3D HNCACB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'UBE2S UBC' _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 1 MET C C 176.04 0.20 1 2 1 1 MET CA C 56.62 0.20 1 3 1 1 MET CB C 30.25 0.20 1 4 2 2 ASN H H 8.28 0.03 1 5 2 2 ASN CA C 53.26 0.20 1 6 2 2 ASN CB C 39.55 0.20 1 7 2 2 ASN N N 118.80 0.20 1 8 4 4 ASN C C 175.55 0.20 1 9 4 4 ASN CA C 53.73 0.20 1 10 4 4 ASN CB C 38.82 0.20 1 11 5 5 VAL H H 8.04 0.03 1 12 5 5 VAL C C 176.14 0.20 1 13 5 5 VAL CA C 62.89 0.20 1 14 5 5 VAL CB C 32.63 0.20 1 15 5 5 VAL N N 119.59 0.20 1 16 6 6 GLU H H 8.34 0.03 1 17 6 6 GLU CA C 56.62 0.20 1 18 6 6 GLU CB C 30.27 0.20 1 19 6 6 GLU N N 122.82 0.20 1 20 7 7 ASN C C 174.94 0.20 1 21 7 7 ASN CA C 53.27 0.20 1 22 7 7 ASN CB C 39.53 0.20 1 23 8 8 LEU H H 8.16 0.03 1 24 8 8 LEU CA C 52.95 0.20 1 25 8 8 LEU CB C 42.69 0.20 1 26 8 8 LEU N N 121.98 0.20 1 27 11 11 HIS C C 177.36 0.20 1 28 11 11 HIS CA C 59.12 0.20 1 29 11 11 HIS CB C 29.46 0.20 1 30 12 12 ILE H H 7.06 0.03 1 31 12 12 ILE C C 177.63 0.20 1 32 12 12 ILE CA C 61.62 0.20 1 33 12 12 ILE CB C 36.22 0.20 1 34 12 12 ILE N N 122.37 0.20 1 35 13 13 ILE H H 7.76 0.03 1 36 13 13 ILE C C 177.78 0.20 1 37 13 13 ILE CA C 64.80 0.20 1 38 13 13 ILE CB C 37.05 0.20 1 39 13 13 ILE N N 121.49 0.20 1 40 14 14 ARG H H 7.76 0.03 1 41 14 14 ARG C C 178.82 0.20 1 42 14 14 ARG CA C 59.68 0.20 1 43 14 14 ARG CB C 30.22 0.20 1 44 14 14 ARG N N 116.80 0.20 1 45 15 15 LEU H H 7.41 0.03 1 46 15 15 LEU C C 179.93 0.20 1 47 15 15 LEU CA C 58.33 0.20 1 48 15 15 LEU CB C 42.42 0.20 1 49 15 15 LEU N N 120.66 0.20 1 50 16 16 VAL H H 8.62 0.03 1 51 16 16 VAL C C 177.55 0.20 1 52 16 16 VAL CA C 67.01 0.20 1 53 16 16 VAL CB C 31.72 0.20 1 54 16 16 VAL N N 121.34 0.20 1 55 17 17 TYR H H 8.91 0.03 1 56 17 17 TYR C C 178.94 0.20 1 57 17 17 TYR CA C 62.14 0.20 1 58 17 17 TYR CB C 38.06 0.20 1 59 17 17 TYR N N 119.87 0.20 1 60 18 18 LYS H H 8.14 0.03 1 61 18 18 LYS C C 174.00 0.20 1 62 18 18 LYS CA C 59.74 0.20 1 63 18 18 LYS CB C 32.40 0.20 1 64 18 18 LYS N N 120.36 0.20 1 65 19 19 GLU H H 8.11 0.03 1 66 19 19 GLU C C 179.88 0.20 1 67 19 19 GLU CA C 59.86 0.20 1 68 19 19 GLU CB C 29.73 0.20 1 69 19 19 GLU N N 120.49 0.20 1 70 20 20 VAL H H 9.18 0.03 1 71 20 20 VAL C C 178.31 0.20 1 72 20 20 VAL CA C 67.47 0.20 1 73 20 20 VAL CB C 31.32 0.20 1 74 20 20 VAL N N 118.94 0.20 1 75 21 21 THR H H 8.22 0.03 1 76 21 21 THR C C 177.42 0.20 1 77 21 21 THR CA C 66.89 0.20 1 78 21 21 THR CB C 68.50 0.20 1 79 21 21 THR N N 116.18 0.20 1 80 22 22 THR H H 7.75 0.03 1 81 22 22 THR C C 176.50 0.20 1 82 22 22 THR CA C 66.21 0.20 1 83 22 22 THR CB C 68.60 0.20 1 84 22 22 THR N N 117.47 0.20 1 85 23 23 LEU H H 8.08 0.03 1 86 23 23 LEU C C 177.57 0.20 1 87 23 23 LEU CA C 57.42 0.20 1 88 23 23 LEU CB C 42.96 0.20 1 89 23 23 LEU N N 122.71 0.20 1 90 24 24 THR H H 7.93 0.03 1 91 24 24 THR C C 176.22 0.20 1 92 24 24 THR CA C 65.08 0.20 1 93 24 24 THR CB C 68.84 0.20 1 94 24 24 THR N N 110.64 0.20 1 95 25 25 ALA H H 7.31 0.03 1 96 25 25 ALA C C 177.76 0.20 1 97 25 25 ALA CA C 53.86 0.20 1 98 25 25 ALA CB C 19.40 0.20 1 99 25 25 ALA N N 122.82 0.20 1 100 26 26 ASP H H 7.76 0.03 1 101 26 26 ASP CA C 51.79 0.20 1 102 26 26 ASP CB C 41.17 0.20 1 103 26 26 ASP N N 115.66 0.20 1 104 28 28 PRO C C 175.31 0.20 1 105 28 28 PRO CA C 61.65 0.20 1 106 28 28 PRO CB C 31.45 0.20 1 107 29 29 ASP H H 8.29 0.03 1 108 29 29 ASP C C 177.63 0.20 1 109 29 29 ASP CA C 56.07 0.20 1 110 29 29 ASP CB C 40.76 0.20 1 111 29 29 ASP N N 120.36 0.20 1 112 30 30 GLY H H 8.68 0.03 1 113 30 30 GLY C C 173.50 0.20 1 114 30 30 GLY CA C 45.74 0.20 1 115 30 30 GLY N N 112.34 0.20 1 116 31 31 ILE H H 7.89 0.03 1 117 31 31 ILE C C 174.12 0.20 1 118 31 31 ILE CA C 59.88 0.20 1 119 31 31 ILE CB C 40.34 0.20 1 120 31 31 ILE N N 121.45 0.20 1 121 32 32 LYS H H 8.46 0.03 1 122 32 32 LYS C C 174.64 0.20 1 123 32 32 LYS CA C 54.74 0.20 1 124 32 32 LYS CB C 36.50 0.20 1 125 32 32 LYS N N 125.13 0.20 1 126 33 33 VAL H H 8.34 0.03 1 127 33 33 VAL C C 173.83 0.20 1 128 33 33 VAL CA C 60.58 0.20 1 129 33 33 VAL CB C 33.91 0.20 1 130 33 33 VAL N N 119.03 0.20 1 131 34 34 PHE H H 8.71 0.03 1 132 34 34 PHE CA C 54.93 0.20 1 133 34 34 PHE CB C 39.41 0.20 1 134 34 34 PHE N N 123.12 0.20 1 135 35 35 PRO C C 175.83 0.20 1 136 35 35 PRO CA C 62.87 0.20 1 137 35 35 PRO CB C 32.44 0.20 1 138 36 36 ASN H H 8.92 0.03 1 139 36 36 ASN C C 176.18 0.20 1 140 36 36 ASN CA C 52.24 0.20 1 141 36 36 ASN CB C 39.05 0.20 1 142 36 36 ASN N N 121.71 0.20 1 143 37 37 GLU H H 9.03 0.03 1 144 37 37 GLU C C 177.05 0.20 1 145 37 37 GLU CA C 58.94 0.20 1 146 37 37 GLU CB C 29.56 0.20 1 147 37 37 GLU N N 124.02 0.20 1 148 38 38 GLU H H 8.15 0.03 1 149 38 38 GLU C C 176.58 0.20 1 150 38 38 GLU CA C 57.12 0.20 1 151 38 38 GLU CB C 30.23 0.20 1 152 38 38 GLU N N 116.18 0.20 1 153 39 39 ASP H H 7.54 0.03 1 154 39 39 ASP C C 175.50 0.20 1 155 39 39 ASP CA C 53.78 0.20 1 156 39 39 ASP CB C 40.60 0.20 1 157 39 39 ASP N N 117.55 0.20 1 158 40 40 LEU H H 8.66 0.03 1 159 40 40 LEU C C 175.51 0.20 1 160 40 40 LEU CA C 56.23 0.20 1 161 40 40 LEU CB C 42.16 0.20 1 162 40 40 LEU N N 125.87 0.20 1 163 41 41 THR H H 7.99 0.03 1 164 41 41 THR C C 173.17 0.20 1 165 41 41 THR CA C 62.65 0.20 1 166 41 41 THR CB C 69.18 0.20 1 167 41 41 THR N N 103.41 0.20 1 168 42 42 ASP H H 7.20 0.03 1 169 42 42 ASP C C 174.95 0.20 1 170 42 42 ASP CA C 52.72 0.20 1 171 42 42 ASP CB C 42.22 0.20 1 172 42 42 ASP N N 122.23 0.20 1 173 43 43 LEU H H 8.64 0.03 1 174 43 43 LEU C C 175.35 0.20 1 175 43 43 LEU CA C 53.87 0.20 1 176 43 43 LEU CB C 44.47 0.20 1 177 43 43 LEU N N 124.97 0.20 1 178 44 44 GLN H H 8.10 0.03 1 179 44 44 GLN C C 174.87 0.20 1 180 44 44 GLN CA C 55.36 0.20 1 181 44 44 GLN CB C 29.82 0.20 1 182 44 44 GLN N N 124.17 0.20 1 183 45 45 VAL H H 8.69 0.03 1 184 45 45 VAL C C 175.84 0.20 1 185 45 45 VAL CA C 59.72 0.20 1 186 45 45 VAL CB C 37.22 0.20 1 187 45 45 VAL N N 121.45 0.20 1 188 46 46 THR H H 9.39 0.03 1 189 46 46 THR C C 173.55 0.20 1 190 46 46 THR CA C 60.36 0.20 1 191 46 46 THR CB C 71.29 0.20 1 192 46 46 THR N N 117.01 0.20 1 193 47 47 ILE H H 9.19 0.03 1 194 47 47 ILE C C 175.09 0.20 1 195 47 47 ILE CA C 59.58 0.20 1 196 47 47 ILE CB C 42.40 0.20 1 197 47 47 ILE N N 122.03 0.20 1 198 48 48 GLU H H 8.75 0.03 1 199 48 48 GLU C C 177.73 0.20 1 200 48 48 GLU CA C 55.63 0.20 1 201 48 48 GLU CB C 30.44 0.20 1 202 48 48 GLU N N 127.86 0.20 1 203 49 49 GLY H H 9.57 0.03 1 204 49 49 GLY CA C 44.30 0.20 1 205 49 49 GLY N N 112.63 0.20 1 206 50 50 PRO C C 176.79 0.20 1 207 50 50 PRO CA C 63.12 0.20 1 208 50 50 PRO CB C 32.32 0.20 1 209 51 51 GLU H H 8.93 0.03 1 210 51 51 GLU C C 177.17 0.20 1 211 51 51 GLU CA C 57.74 0.20 1 212 51 51 GLU CB C 29.77 0.20 1 213 51 51 GLU N N 124.57 0.20 1 214 52 52 GLY H H 9.16 0.03 1 215 52 52 GLY C C 173.99 0.20 1 216 52 52 GLY CA C 45.59 0.20 1 217 52 52 GLY N N 110.77 0.20 1 218 53 53 THR H H 7.51 0.03 1 219 53 53 THR CA C 59.53 0.20 1 220 53 53 THR CB C 70.70 0.20 1 221 53 53 THR N N 108.50 0.20 1 222 54 54 PRO C C 174.41 0.20 1 223 54 54 PRO CA C 63.83 0.20 1 224 54 54 PRO CB C 32.58 0.20 1 225 55 55 TYR H H 6.93 0.03 1 226 55 55 TYR C C 175.15 0.20 1 227 55 55 TYR CA C 55.94 0.20 1 228 55 55 TYR CB C 38.40 0.20 1 229 55 55 TYR N N 113.95 0.20 1 230 56 56 ALA H H 7.28 0.03 1 231 56 56 ALA C C 178.55 0.20 1 232 56 56 ALA CA C 53.75 0.20 1 233 56 56 ALA CB C 19.65 0.20 1 234 56 56 ALA N N 123.29 0.20 1 235 57 57 GLY H H 8.69 0.03 1 236 57 57 GLY C C 174.74 0.20 1 237 57 57 GLY CA C 45.32 0.20 1 238 57 57 GLY N N 111.77 0.20 1 239 58 58 GLY H H 8.28 0.03 1 240 58 58 GLY C C 171.89 0.20 1 241 58 58 GLY CA C 44.57 0.20 1 242 58 58 GLY N N 107.17 0.20 1 243 59 59 LEU H H 9.31 0.03 1 244 59 59 LEU C C 175.01 0.20 1 245 59 59 LEU CA C 54.07 0.20 1 246 59 59 LEU CB C 43.24 0.20 1 247 59 59 LEU N N 126.95 0.20 1 248 60 60 PHE H H 8.83 0.03 1 249 60 60 PHE C C 174.77 0.20 1 250 60 60 PHE CA C 57.39 0.20 1 251 60 60 PHE CB C 40.52 0.20 1 252 60 60 PHE N N 123.66 0.20 1 253 61 61 ARG H H 9.40 0.03 1 254 61 61 ARG C C 176.07 0.20 1 255 61 61 ARG CA C 55.39 0.20 1 256 61 61 ARG CB C 31.62 0.20 1 257 61 61 ARG N N 123.68 0.20 1 258 62 62 MET H H 9.47 0.03 1 259 62 62 MET C C 173.07 0.20 1 260 62 62 MET CA C 54.43 0.20 1 261 62 62 MET CB C 37.26 0.20 1 262 62 62 MET N N 123.97 0.20 1 263 63 63 LYS H H 9.07 0.03 1 264 63 63 LYS C C 174.38 0.20 1 265 63 63 LYS CA C 54.44 0.20 1 266 63 63 LYS CB C 36.15 0.20 1 267 63 63 LYS N N 120.24 0.20 1 268 64 64 LEU H H 8.96 0.03 1 269 64 64 LEU C C 174.63 0.20 1 270 64 64 LEU CA C 52.83 0.20 1 271 64 64 LEU CB C 44.99 0.20 1 272 64 64 LEU N N 123.57 0.20 1 273 65 65 LEU H H 8.99 0.03 1 274 65 65 LEU C C 177.00 0.20 1 275 65 65 LEU CA C 52.97 0.20 1 276 65 65 LEU CB C 43.72 0.20 1 277 65 65 LEU N N 122.87 0.20 1 278 66 66 LEU H H 9.02 0.03 1 279 66 66 LEU C C 175.93 0.20 1 280 66 66 LEU CA C 55.36 0.20 1 281 66 66 LEU CB C 40.97 0.20 1 282 66 66 LEU N N 126.77 0.20 1 283 67 67 GLY H H 7.97 0.03 1 284 67 67 GLY C C 173.99 0.20 1 285 67 67 GLY CA C 44.28 0.20 1 286 67 67 GLY N N 108.49 0.20 1 287 68 68 LYS H H 8.37 0.03 1 288 68 68 LYS C C 176.23 0.20 1 289 68 68 LYS CA C 58.25 0.20 1 290 68 68 LYS CB C 32.26 0.20 1 291 68 68 LYS N N 116.68 0.20 1 292 69 69 ASP H H 8.50 0.03 1 293 69 69 ASP C C 175.74 0.20 1 294 69 69 ASP CA C 52.89 0.20 1 295 69 69 ASP CB C 40.67 0.20 1 296 69 69 ASP N N 116.18 0.20 1 297 70 70 PHE H H 7.69 0.03 1 298 70 70 PHE CA C 56.76 0.20 1 299 70 70 PHE CB C 40.16 0.20 1 300 70 70 PHE N N 124.97 0.20 1 301 71 71 PRO C C 175.13 0.20 1 302 71 71 PRO CA C 63.96 0.20 1 303 71 71 PRO CB C 32.25 0.20 1 304 72 72 ALA H H 8.58 0.03 1 305 72 72 ALA C C 178.77 0.20 1 306 72 72 ALA CA C 55.76 0.20 1 307 72 72 ALA CB C 18.28 0.20 1 308 72 72 ALA N N 128.40 0.20 1 309 73 73 SER H H 7.72 0.03 1 310 73 73 SER CA C 55.02 0.20 1 311 73 73 SER CB C 63.96 0.20 1 312 73 73 SER N N 111.57 0.20 1 313 75 75 PRO C C 174.42 0.20 1 314 75 75 PRO CA C 62.00 0.20 1 315 75 75 PRO CB C 32.78 0.20 1 316 76 76 LYS H H 7.89 0.03 1 317 76 76 LYS C C 175.90 0.20 1 318 76 76 LYS CA C 55.38 0.20 1 319 76 76 LYS CB C 34.76 0.20 1 320 76 76 LYS N N 117.77 0.20 1 321 77 77 GLY H H 8.33 0.03 1 322 77 77 GLY C C 171.45 0.20 1 323 77 77 GLY CA C 44.64 0.20 1 324 77 77 GLY N N 107.37 0.20 1 325 78 78 TYR H H 8.63 0.03 1 326 78 78 TYR C C 176.34 0.20 1 327 78 78 TYR CA C 56.12 0.20 1 328 78 78 TYR CB C 41.66 0.20 1 329 78 78 TYR N N 118.84 0.20 1 330 79 79 PHE H H 10.04 0.03 1 331 79 79 PHE C C 176.46 0.20 1 332 79 79 PHE CA C 60.58 0.20 1 333 79 79 PHE CB C 39.64 0.20 1 334 79 79 PHE N N 122.62 0.20 1 335 80 80 LEU H H 9.40 0.03 1 336 80 80 LEU C C 177.81 0.20 1 337 80 80 LEU CA C 55.37 0.20 1 338 80 80 LEU CB C 41.80 0.20 1 339 80 80 LEU N N 125.22 0.20 1 340 81 81 THR H H 7.49 0.03 1 341 81 81 THR C C 173.69 0.20 1 342 81 81 THR CA C 63.19 0.20 1 343 81 81 THR CB C 71.38 0.20 1 344 81 81 THR N N 118.59 0.20 1 345 82 82 LYS H H 8.49 0.03 1 346 82 82 LYS C C 174.68 0.20 1 347 82 82 LYS CA C 57.47 0.20 1 348 82 82 LYS CB C 31.95 0.20 1 349 82 82 LYS N N 127.74 0.20 1 350 83 83 ILE H H 8.15 0.03 1 351 83 83 ILE C C 171.65 0.20 1 352 83 83 ILE CA C 60.04 0.20 1 353 83 83 ILE CB C 41.59 0.20 1 354 83 83 ILE N N 120.92 0.20 1 355 84 84 PHE H H 8.42 0.03 1 356 84 84 PHE C C 173.60 0.20 1 357 84 84 PHE CA C 56.82 0.20 1 358 84 84 PHE CB C 39.97 0.20 1 359 84 84 PHE N N 128.06 0.20 1 360 85 85 HIS H H 9.47 0.03 1 361 85 85 HIS CA C 55.26 0.20 1 362 85 85 HIS CB C 35.18 0.20 1 363 85 85 HIS N N 129.88 0.20 1 364 86 86 PRO C C 176.77 0.20 1 365 87 87 ASN H H 11.50 0.03 1 366 87 87 ASN C C 171.33 0.20 1 367 87 87 ASN CA C 54.23 0.20 1 368 87 87 ASN CB C 41.03 0.20 1 369 87 87 ASN N N 116.37 0.20 1 370 88 88 VAL H H 7.42 0.03 1 371 88 88 VAL C C 176.24 0.20 1 372 88 88 VAL CA C 60.83 0.20 1 373 88 88 VAL CB C 34.01 0.20 1 374 88 88 VAL N N 119.00 0.20 1 375 89 89 GLY H H 9.44 0.03 1 376 89 89 GLY CA C 44.66 0.20 1 377 89 89 GLY N N 112.99 0.20 1 378 90 90 ALA C C 178.87 0.20 1 379 90 90 ALA CA C 55.17 0.20 1 380 91 91 ASN H H 8.67 0.03 1 381 91 91 ASN C C 175.66 0.20 1 382 91 91 ASN CA C 52.42 0.20 1 383 91 91 ASN CB C 38.22 0.20 1 384 91 91 ASN N N 115.00 0.20 1 385 92 92 GLY H H 8.20 0.03 1 386 92 92 GLY C C 174.11 0.20 1 387 92 92 GLY CA C 45.53 0.20 1 388 92 92 GLY N N 107.45 0.20 1 389 93 93 GLU H H 8.77 0.03 1 390 93 93 GLU C C 174.90 0.20 1 391 93 93 GLU CA C 57.34 0.20 1 392 93 93 GLU CB C 30.09 0.20 1 393 93 93 GLU N N 122.85 0.20 1 394 94 94 ILE H H 7.68 0.03 1 395 94 94 ILE C C 176.04 0.20 1 396 94 94 ILE CA C 60.57 0.20 1 397 94 94 ILE CB C 39.47 0.20 1 398 94 94 ILE N N 123.00 0.20 1 399 95 95 SER H H 8.20 0.03 1 400 95 95 SER C C 175.63 0.20 1 401 95 95 SER CA C 58.43 0.20 1 402 95 95 SER CB C 64.18 0.20 1 403 95 95 SER N N 119.90 0.20 1 404 96 96 VAL H H 8.65 0.03 1 405 96 96 VAL C C 177.33 0.20 1 406 96 96 VAL CA C 64.69 0.20 1 407 96 96 VAL CB C 32.25 0.20 1 408 96 96 VAL N N 128.04 0.20 1 409 97 97 ASN H H 8.26 0.03 1 410 97 97 ASN C C 177.45 0.20 1 411 97 97 ASN CA C 56.10 0.20 1 412 97 97 ASN CB C 37.73 0.20 1 413 97 97 ASN N N 118.30 0.20 1 414 98 98 VAL H H 7.35 0.03 1 415 98 98 VAL C C 176.92 0.20 1 416 98 98 VAL CA C 64.39 0.20 1 417 98 98 VAL CB C 31.76 0.20 1 418 98 98 VAL N N 115.58 0.20 1 419 99 99 LEU H H 7.44 0.03 1 420 99 99 LEU C C 177.75 0.20 1 421 99 99 LEU CA C 56.72 0.20 1 422 99 99 LEU CB C 41.75 0.20 1 423 99 99 LEU N N 118.13 0.20 1 424 100 100 CYS H H 8.01 0.03 1 425 100 100 CYS C C 175.75 0.20 1 426 100 100 CYS CA C 59.52 0.20 1 427 100 100 CYS CB C 27.80 0.20 1 428 100 100 CYS N N 113.06 0.20 1 429 101 101 ARG H H 7.48 0.03 1 430 101 101 ARG C C 176.68 0.20 1 431 101 101 ARG CA C 58.77 0.20 1 432 101 101 ARG CB C 30.09 0.20 1 433 101 101 ARG N N 123.07 0.20 1 434 102 102 ASP H H 8.69 0.03 1 435 102 102 ASP C C 174.77 0.20 1 436 102 102 ASP CA C 54.41 0.20 1 437 102 102 ASP CB C 40.25 0.20 1 438 102 102 ASP N N 119.79 0.20 1 439 103 103 TRP H H 7.49 0.03 1 440 103 103 TRP CA C 59.35 0.20 1 441 103 103 TRP CB C 30.15 0.20 1 442 103 103 TRP N N 119.14 0.20 1 443 104 104 THR H H 5.89 0.03 1 444 104 104 THR C C 172.20 0.20 1 445 104 104 THR CA C 59.42 0.20 1 446 104 104 THR CB C 71.50 0.20 1 447 104 104 THR N N 117.36 0.20 1 448 105 105 ALA H H 8.09 0.03 1 449 105 105 ALA C C 178.00 0.20 1 450 105 105 ALA CA C 53.81 0.20 1 451 105 105 ALA CB C 18.71 0.20 1 452 105 105 ALA N N 120.73 0.20 1 453 106 106 GLU H H 7.82 0.03 1 454 106 106 GLU C C 177.26 0.20 1 455 106 106 GLU CA C 57.20 0.20 1 456 106 106 GLU CB C 29.52 0.20 1 457 106 106 GLU N N 114.78 0.20 1 458 107 107 LEU H H 7.07 0.03 1 459 107 107 LEU C C 177.51 0.20 1 460 107 107 LEU CA C 55.80 0.20 1 461 107 107 LEU CB C 40.97 0.20 1 462 107 107 LEU N N 120.82 0.20 1 463 108 108 GLY H H 7.36 0.03 1 464 108 108 GLY C C 174.43 0.20 1 465 108 108 GLY CA C 45.19 0.20 1 466 108 108 GLY N N 103.89 0.20 1 467 109 109 ILE H H 10.15 0.03 1 468 109 109 ILE C C 178.66 0.20 1 469 109 109 ILE CA C 64.91 0.20 1 470 109 109 ILE CB C 37.74 0.20 1 471 109 109 ILE N N 121.18 0.20 1 472 110 110 ARG H H 9.59 0.03 1 473 110 110 ARG C C 177.18 0.20 1 474 110 110 ARG CA C 61.11 0.20 1 475 110 110 ARG CB C 30.65 0.20 1 476 110 110 ARG N N 121.75 0.20 1 477 111 111 HIS H H 7.73 0.03 1 478 111 111 HIS C C 179.17 0.20 1 479 111 111 HIS CA C 60.53 0.20 1 480 111 111 HIS CB C 32.19 0.20 1 481 111 111 HIS N N 115.79 0.20 1 482 112 112 VAL H H 7.77 0.03 1 483 112 112 VAL C C 177.36 0.20 1 484 112 112 VAL CA C 66.48 0.20 1 485 112 112 VAL CB C 31.58 0.20 1 486 112 112 VAL N N 120.86 0.20 1 487 113 113 LEU H H 8.06 0.03 1 488 113 113 LEU C C 179.05 0.20 1 489 113 113 LEU CA C 58.13 0.20 1 490 113 113 LEU CB C 41.01 0.20 1 491 113 113 LEU N N 118.11 0.20 1 492 114 114 LEU H H 8.20 0.03 1 493 114 114 LEU C C 179.77 0.20 1 494 114 114 LEU CA C 57.94 0.20 1 495 114 114 LEU CB C 41.20 0.20 1 496 114 114 LEU N N 118.48 0.20 1 497 115 115 THR H H 8.13 0.03 1 498 115 115 THR C C 176.50 0.20 1 499 115 115 THR CA C 67.30 0.20 1 500 115 115 THR CB C 68.79 0.20 1 501 115 115 THR N N 118.14 0.20 1 502 116 116 ILE H H 8.06 0.03 1 503 116 116 ILE C C 176.63 0.20 1 504 116 116 ILE CA C 65.90 0.20 1 505 116 116 ILE CB C 37.44 0.20 1 506 116 116 ILE N N 122.96 0.20 1 507 117 117 LYS H H 7.91 0.03 1 508 117 117 LYS C C 178.31 0.20 1 509 117 117 LYS CA C 61.13 0.20 1 510 117 117 LYS CB C 32.43 0.20 1 511 117 117 LYS N N 119.34 0.20 1 512 118 118 MET H H 8.06 0.03 1 513 118 118 MET C C 178.66 0.20 1 514 118 118 MET CA C 57.68 0.20 1 515 118 118 MET CB C 31.26 0.20 1 516 118 118 MET N N 115.23 0.20 1 517 119 119 LEU H H 8.08 0.03 1 518 119 119 LEU C C 180.47 0.20 1 519 119 119 LEU CA C 56.56 0.20 1 520 119 119 LEU CB C 42.69 0.20 1 521 119 119 LEU N N 121.64 0.20 1 522 120 120 LEU H H 7.71 0.03 1 523 120 120 LEU C C 176.55 0.20 1 524 120 120 LEU CA C 58.25 0.20 1 525 120 120 LEU CB C 41.10 0.20 1 526 120 120 LEU N N 118.82 0.20 1 527 121 121 ILE H H 7.15 0.03 1 528 121 121 ILE C C 175.89 0.20 1 529 121 121 ILE CA C 63.87 0.20 1 530 121 121 ILE CB C 39.52 0.20 1 531 121 121 ILE N N 117.32 0.20 1 532 122 122 HIS H H 8.66 0.03 1 533 122 122 HIS CA C 52.38 0.20 1 534 122 122 HIS CB C 30.59 0.20 1 535 122 122 HIS N N 117.11 0.20 1 536 123 123 PRO C C 174.99 0.20 1 537 123 123 PRO CA C 62.67 0.20 1 538 123 123 PRO CB C 32.30 0.20 1 539 124 124 ASN H H 9.02 0.03 1 540 124 124 ASN CA C 50.04 0.20 1 541 124 124 ASN CB C 40.46 0.20 1 542 124 124 ASN N N 120.13 0.20 1 543 125 125 PRO C C 176.33 0.20 1 544 125 125 PRO CA C 64.30 0.20 1 545 125 125 PRO CB C 32.31 0.20 1 546 126 126 GLU H H 8.23 0.03 1 547 126 126 GLU C C 176.23 0.20 1 548 126 126 GLU CA C 57.63 0.20 1 549 126 126 GLU CB C 29.58 0.20 1 550 126 126 GLU N N 118.86 0.20 1 551 127 127 SER H H 7.59 0.03 1 552 127 127 SER C C 174.57 0.20 1 553 127 127 SER CA C 56.53 0.20 1 554 127 127 SER CB C 62.65 0.20 1 555 127 127 SER N N 115.23 0.20 1 556 128 128 ALA H H 7.80 0.03 1 557 128 128 ALA C C 177.33 0.20 1 558 128 128 ALA CA C 52.57 0.20 1 559 128 128 ALA CB C 18.85 0.20 1 560 128 128 ALA N N 124.36 0.20 1 561 129 129 LEU H H 8.02 0.03 1 562 129 129 LEU C C 177.42 0.20 1 563 129 129 LEU CA C 55.70 0.20 1 564 129 129 LEU CB C 43.83 0.20 1 565 129 129 LEU N N 122.58 0.20 1 566 130 130 ASN H H 7.79 0.03 1 567 130 130 ASN C C 175.66 0.20 1 568 130 130 ASN CA C 51.62 0.20 1 569 130 130 ASN CB C 37.80 0.20 1 570 130 130 ASN N N 117.40 0.20 1 571 131 131 GLU H H 8.84 0.03 1 572 131 131 GLU C C 178.65 0.20 1 573 131 131 GLU CA C 59.62 0.20 1 574 131 131 GLU CB C 29.55 0.20 1 575 131 131 GLU N N 124.26 0.20 1 576 132 132 GLU H H 8.33 0.03 1 577 132 132 GLU C C 178.32 0.20 1 578 132 132 GLU CA C 59.36 0.20 1 579 132 132 GLU CB C 29.72 0.20 1 580 132 132 GLU N N 121.04 0.20 1 581 133 133 ALA H H 7.23 0.03 1 582 133 133 ALA C C 179.05 0.20 1 583 133 133 ALA CA C 54.91 0.20 1 584 133 133 ALA CB C 16.42 0.20 1 585 133 133 ALA N N 119.25 0.20 1 586 134 134 GLY H H 8.26 0.03 1 587 134 134 GLY C C 174.00 0.20 1 588 134 134 GLY CA C 47.45 0.20 1 589 134 134 GLY N N 102.85 0.20 1 590 135 135 ARG H H 8.13 0.03 1 591 135 135 ARG C C 178.47 0.20 1 592 135 135 ARG CA C 59.42 0.20 1 593 135 135 ARG CB C 30.03 0.20 1 594 135 135 ARG N N 120.38 0.20 1 595 136 136 LEU H H 8.19 0.03 1 596 136 136 LEU C C 177.82 0.20 1 597 136 136 LEU CA C 57.78 0.20 1 598 136 136 LEU CB C 43.21 0.20 1 599 136 136 LEU N N 118.60 0.20 1 600 137 137 LEU H H 7.84 0.03 1 601 137 137 LEU C C 177.23 0.20 1 602 137 137 LEU CA C 59.06 0.20 1 603 137 137 LEU CB C 41.85 0.20 1 604 137 137 LEU N N 118.25 0.20 1 605 138 138 LEU H H 6.83 0.03 1 606 138 138 LEU C C 179.39 0.20 1 607 138 138 LEU CA C 56.37 0.20 1 608 138 138 LEU CB C 43.32 0.20 1 609 138 138 LEU N N 112.98 0.20 1 610 139 139 GLU H H 8.53 0.03 1 611 139 139 GLU C C 177.54 0.20 1 612 139 139 GLU CA C 58.05 0.20 1 613 139 139 GLU CB C 31.68 0.20 1 614 139 139 GLU N N 117.73 0.20 1 615 140 140 ASN H H 9.16 0.03 1 616 140 140 ASN C C 173.69 0.20 1 617 140 140 ASN CA C 52.55 0.20 1 618 140 140 ASN CB C 37.69 0.20 1 619 140 140 ASN N N 118.52 0.20 1 620 141 141 TYR H H 9.13 0.03 1 621 141 141 TYR C C 176.98 0.20 1 622 141 141 TYR CA C 63.47 0.20 1 623 141 141 TYR CB C 38.55 0.20 1 624 141 141 TYR N N 126.82 0.20 1 625 142 142 GLU H H 8.74 0.03 1 626 142 142 GLU C C 179.50 0.20 1 627 142 142 GLU CA C 59.81 0.20 1 628 142 142 GLU CB C 29.14 0.20 1 629 142 142 GLU N N 115.64 0.20 1 630 143 143 GLU H H 7.59 0.03 1 631 143 143 GLU C C 178.98 0.20 1 632 143 143 GLU CA C 58.49 0.20 1 633 143 143 GLU CB C 29.67 0.20 1 634 143 143 GLU N N 121.11 0.20 1 635 144 144 TYR H H 7.81 0.03 1 636 144 144 TYR C C 175.64 0.20 1 637 144 144 TYR CA C 61.33 0.20 1 638 144 144 TYR CB C 36.69 0.20 1 639 144 144 TYR N N 121.23 0.20 1 640 145 145 ALA H H 8.67 0.03 1 641 145 145 ALA C C 179.24 0.20 1 642 145 145 ALA CA C 54.94 0.20 1 643 145 145 ALA CB C 17.56 0.20 1 644 145 145 ALA N N 121.51 0.20 1 645 146 146 ALA H H 7.83 0.03 1 646 146 146 ALA C C 180.76 0.20 1 647 146 146 ALA CA C 55.00 0.20 1 648 146 146 ALA CB C 18.09 0.20 1 649 146 146 ALA N N 119.66 0.20 1 650 147 147 ARG H H 7.84 0.03 1 651 147 147 ARG C C 178.50 0.20 1 652 147 147 ARG CA C 58.47 0.20 1 653 147 147 ARG CB C 29.16 0.20 1 654 147 147 ARG N N 119.63 0.20 1 655 148 148 ALA H H 8.46 0.03 1 656 148 148 ALA C C 180.76 0.20 1 657 148 148 ALA CA C 55.02 0.20 1 658 148 148 ALA CB C 17.75 0.20 1 659 148 148 ALA N N 120.49 0.20 1 660 149 149 ARG H H 8.52 0.03 1 661 149 149 ARG C C 178.50 0.20 1 662 149 149 ARG CA C 59.01 0.20 1 663 149 149 ARG CB C 30.59 0.20 1 664 149 149 ARG N N 121.05 0.20 1 665 150 150 LEU H H 7.87 0.03 1 666 150 150 LEU C C 179.03 0.20 1 667 150 150 LEU CA C 57.93 0.20 1 668 150 150 LEU CB C 41.73 0.20 1 669 150 150 LEU N N 121.42 0.20 1 670 151 151 LEU H H 7.71 0.03 1 671 151 151 LEU C C 180.23 0.20 1 672 151 151 LEU CA C 57.60 0.20 1 673 151 151 LEU CB C 41.32 0.20 1 674 151 151 LEU N N 116.14 0.20 1 675 152 152 THR H H 7.95 0.03 1 676 152 152 THR C C 175.79 0.20 1 677 152 152 THR CA C 67.31 0.20 1 678 152 152 THR CB C 68.61 0.20 1 679 152 152 THR N N 121.31 0.20 1 680 153 153 GLU H H 8.29 0.03 1 681 153 153 GLU C C 177.84 0.20 1 682 153 153 GLU CA C 58.56 0.20 1 683 153 153 GLU CB C 29.56 0.20 1 684 153 153 GLU N N 124.22 0.20 1 685 154 154 ILE H H 7.87 0.03 1 686 154 154 ILE C C 177.35 0.20 1 687 154 154 ILE CA C 63.42 0.20 1 688 154 154 ILE CB C 39.47 0.20 1 689 154 154 ILE N N 118.62 0.20 1 690 155 155 HIS H H 8.20 0.03 1 691 155 155 HIS C C 175.43 0.20 1 692 155 155 HIS CA C 56.92 0.20 1 693 155 155 HIS CB C 32.22 0.20 1 694 155 155 HIS N N 118.02 0.20 1 695 156 156 GLY H H 8.23 0.03 1 696 156 156 GLY CA C 45.98 0.20 1 697 156 156 GLY N N 115.67 0.20 1 stop_ save_