data_26607 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Neisseria meningititis Fic ; _BMRB_accession_number 26607 _BMRB_flat_file_name bmr26607.str _Entry_type original _Submission_date 2015-07-13 _Accession_date 2015-07-13 _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 Burmann Bjoern M. . 2 Hiller Sebastian . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 172 "13C chemical shifts" 524 "15N chemical shifts" 172 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-01-06 original BMRB . stop_ _Original_release_date 2016-01-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification ; _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Stanger Frederic V. . 2 Burmann Bjoern M. . 3 Harms Alexander . . 4 Correia Hugo . . 5 Mazur Adam . . 6 Sharpe Timothy . . 7 Dehio Christoph . . 8 Hiller Sebastian . . 9 Schirmer Tilman . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U. S. A.' _Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name NmFic _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label NmFic $NmFic stop_ _System_molecular_weight 22100 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_NmFic _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common NmFic _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 188 _Mol_residue_sequence ; MHHHHHHMKSIDEQSLHNAR RLFESGDIDRIEVGTTAGLQ QIHRYLFGGLYDFAGQIRED NISKGGFRFANAMYLKEALV KIEQMPERTFEEIIAKYVRM NIAAPFLEGNGRSTRIWLDL VLKKNLKKVVNWQNVSKTLY LQAMERSPVNDLRLRFLLKD NLTDDVDNREIIFKGIEQSY YYEGYEKG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 4 MET 2 5 HIS 3 6 HIS 4 7 HIS 5 8 HIS 6 9 HIS 7 10 HIS 8 11 MET 9 12 LYS 10 13 SER 11 14 ILE 12 15 ASP 13 16 GLU 14 17 GLN 15 18 SER 16 19 LEU 17 20 HIS 18 21 ASN 19 22 ALA 20 23 ARG 21 24 ARG 22 25 LEU 23 26 PHE 24 27 GLU 25 28 SER 26 29 GLY 27 30 ASP 28 31 ILE 29 32 ASP 30 33 ARG 31 34 ILE 32 35 GLU 33 36 VAL 34 37 GLY 35 38 THR 36 39 THR 37 40 ALA 38 41 GLY 39 42 LEU 40 43 GLN 41 44 GLN 42 45 ILE 43 46 HIS 44 47 ARG 45 48 TYR 46 49 LEU 47 50 PHE 48 51 GLY 49 52 GLY 50 53 LEU 51 54 TYR 52 55 ASP 53 56 PHE 54 57 ALA 55 58 GLY 56 59 GLN 57 60 ILE 58 61 ARG 59 62 GLU 60 63 ASP 61 64 ASN 62 65 ILE 63 66 SER 64 67 LYS 65 68 GLY 66 69 GLY 67 70 PHE 68 71 ARG 69 72 PHE 70 73 ALA 71 74 ASN 72 75 ALA 73 76 MET 74 77 TYR 75 78 LEU 76 79 LYS 77 80 GLU 78 81 ALA 79 82 LEU 80 83 VAL 81 84 LYS 82 85 ILE 83 86 GLU 84 87 GLN 85 88 MET 86 89 PRO 87 90 GLU 88 91 ARG 89 92 THR 90 93 PHE 91 94 GLU 92 95 GLU 93 96 ILE 94 97 ILE 95 98 ALA 96 99 LYS 97 100 TYR 98 101 VAL 99 102 ARG 100 103 MET 101 104 ASN 102 105 ILE 103 106 ALA 104 107 ALA 105 108 PRO 106 109 PHE 107 110 LEU 108 111 GLU 109 112 GLY 110 113 ASN 111 114 GLY 112 115 ARG 113 116 SER 114 117 THR 115 118 ARG 116 119 ILE 117 120 TRP 118 121 LEU 119 122 ASP 120 123 LEU 121 124 VAL 122 125 LEU 123 126 LYS 124 127 LYS 125 128 ASN 126 129 LEU 127 130 LYS 128 131 LYS 129 132 VAL 130 133 VAL 131 134 ASN 132 135 TRP 133 136 GLN 134 137 ASN 135 138 VAL 136 139 SER 137 140 LYS 138 141 THR 139 142 LEU 140 143 TYR 141 144 LEU 142 145 GLN 143 146 ALA 144 147 MET 145 148 GLU 146 149 ARG 147 150 SER 148 151 PRO 149 152 VAL 150 153 ASN 151 154 ASP 152 155 LEU 153 156 ARG 154 157 LEU 155 158 ARG 156 159 PHE 157 160 LEU 158 161 LEU 159 162 LYS 160 163 ASP 161 164 ASN 162 165 LEU 163 166 THR 164 167 ASP 165 168 ASP 166 169 VAL 167 170 ASP 168 171 ASN 169 172 ARG 170 173 GLU 171 174 ILE 172 175 ILE 173 176 PHE 174 177 LYS 175 178 GLY 176 179 ILE 177 180 GLU 178 181 GLN 179 182 SER 180 183 TYR 181 184 TYR 182 185 TYR 183 186 GLU 184 187 GLY 185 188 TYR 186 189 GLU 187 190 LYS 188 191 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $NmFic b-proteobacteria 487 Bacteria . Neisseria meningitidis 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 $NmFic 'recombinant technology' . Escherichia coli . pRSF-DUET1 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 $NmFic 500 uM '[U-100% 13C; U-100% 15N]' D2O 10 % 'natural abundance' MES 25 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' H2O 90 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.0 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . Guntert . . 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' collection processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . 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_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _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 'ionic strength' 150 . mM pH 6.5 . pH pressure 1 . atm temperature 298.15 . 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 . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $TOPSPIN stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HNCACB' '3D HNCO' '3D HN(CA)CO' 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 NmFic _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 10 7 HIS C C 175.9 0.3 1 2 10 7 HIS CA C 56.0 0.3 1 3 10 7 HIS CB C 29.7 0.3 1 4 11 8 MET H H 8.28 0.02 1 5 11 8 MET C C 176.8 0.3 1 6 11 8 MET CA C 55.9 0.3 1 7 11 8 MET CB C 33.4 0.3 1 8 11 8 MET N N 122.6 0.3 1 9 12 9 LYS H H 8.48 0.02 1 10 12 9 LYS C C 176.2 0.3 1 11 12 9 LYS CA C 57.6 0.3 1 12 12 9 LYS CB C 33.3 0.3 1 13 12 9 LYS N N 123.1 0.3 1 14 13 10 SER H H 8.41 0.02 1 15 13 10 SER C C 176.5 0.3 1 16 13 10 SER CA C 59.5 0.3 1 17 13 10 SER CB C 63.9 0.3 1 18 13 10 SER N N 117.3 0.3 1 19 14 11 ILE H H 8.08 0.02 1 20 14 11 ILE CA C 64.6 0.3 1 21 14 11 ILE CB C 38.1 0.3 1 22 14 11 ILE N N 122.7 0.3 1 23 15 12 ASP H H 7.72 0.02 1 24 15 12 ASP CA C 57.5 0.3 1 25 15 12 ASP CB C 38.4 0.3 1 26 15 12 ASP N N 119.2 0.3 1 27 16 13 GLU C C 179.5 0.3 1 28 16 13 GLU CA C 60.9 0.3 1 29 16 13 GLU CB C 29.5 0.3 1 30 17 14 GLN H H 7.69 0.02 1 31 17 14 GLN C C 178.8 0.3 1 32 17 14 GLN CA C 59.3 0.3 1 33 17 14 GLN CB C 29.5 0.3 1 34 17 14 GLN N N 118.5 0.3 1 35 18 15 SER H H 8.48 0.02 1 36 18 15 SER C C 175.6 0.3 1 37 18 15 SER CA C 61.2 0.3 1 38 18 15 SER CB C 63.1 0.3 1 39 18 15 SER N N 115.4 0.3 1 40 19 16 LEU H H 7.99 0.02 1 41 19 16 LEU C C 179.2 0.3 1 42 19 16 LEU CA C 58.5 0.3 1 43 19 16 LEU CB C 41.0 0.3 1 44 19 16 LEU N N 125.4 0.3 1 45 20 17 HIS H H 7.37 0.02 1 46 20 17 HIS C C 178.6 0.3 1 47 20 17 HIS CA C 59.7 0.3 1 48 20 17 HIS CB C 28.6 0.3 1 49 20 17 HIS N N 118.0 0.3 1 50 21 18 ASN H H 7.94 0.02 1 51 21 18 ASN C C 177.3 0.3 1 52 21 18 ASN CA C 56.2 0.3 1 53 21 18 ASN CB C 38.3 0.3 1 54 21 18 ASN N N 121.2 0.3 1 55 22 19 ALA H H 8.50 0.02 1 56 22 19 ALA C C 178.8 0.3 1 57 22 19 ALA CA C 55.6 0.3 1 58 22 19 ALA CB C 18.1 0.3 1 59 22 19 ALA N N 124.4 0.3 1 60 23 20 ARG H H 7.86 0.02 1 61 23 20 ARG C C 179.3 0.3 1 62 23 20 ARG CA C 60.4 0.3 1 63 23 20 ARG CB C 30.3 0.3 1 64 23 20 ARG N N 115.5 0.3 1 65 24 21 ARG H H 8.01 0.02 1 66 24 21 ARG C C 178.7 0.3 1 67 24 21 ARG CA C 59.4 0.3 1 68 24 21 ARG CB C 30.0 0.3 1 69 24 21 ARG N N 120.8 0.3 1 70 25 22 LEU H H 8.14 0.02 1 71 25 22 LEU C C 177.0 0.3 1 72 25 22 LEU CA C 58.4 0.3 1 73 25 22 LEU CB C 40.9 0.3 1 74 25 22 LEU N N 124.5 0.3 1 75 26 23 PHE H H 6.92 0.02 1 76 26 23 PHE C C 179.5 0.3 1 77 26 23 PHE CA C 61.4 0.3 1 78 26 23 PHE CB C 40.7 0.3 1 79 26 23 PHE N N 113.9 0.3 1 80 27 24 GLU H H 9.13 0.02 1 81 27 24 GLU C C 178.7 0.3 1 82 27 24 GLU CA C 60.2 0.3 1 83 27 24 GLU CB C 30.8 0.3 1 84 27 24 GLU N N 122.1 0.3 1 85 28 25 SER H H 8.62 0.02 1 86 28 25 SER C C 176.4 0.3 1 87 28 25 SER CA C 60.1 0.3 1 88 28 25 SER CB C 65.5 0.3 1 89 28 25 SER N N 110.9 0.3 1 90 29 26 GLY H H 7.25 0.02 1 91 29 26 GLY C C 175.1 0.3 1 92 29 26 GLY CA C 45.5 0.3 1 93 29 26 GLY N N 109.6 0.3 1 94 30 27 ASP H H 8.73 0.02 1 95 30 27 ASP C C 178.9 0.3 1 96 30 27 ASP CA C 57.7 0.3 1 97 30 27 ASP CB C 39.4 0.3 1 98 30 27 ASP N N 125.9 0.3 1 99 31 28 ILE H H 7.46 0.02 1 100 31 28 ILE C C 174.9 0.3 1 101 31 28 ILE CA C 59.9 0.3 1 102 31 28 ILE CB C 38.3 0.3 1 103 31 28 ILE N N 119.8 0.3 1 104 32 29 ASP H H 7.18 0.02 1 105 32 29 ASP C C 176.8 0.3 1 106 32 29 ASP CA C 56.4 0.3 1 107 32 29 ASP CB C 40.7 0.3 1 108 32 29 ASP N N 121.7 0.3 1 109 33 30 ARG H H 7.54 0.02 1 110 33 30 ARG C C 176.2 0.3 1 111 33 30 ARG CA C 55.6 0.3 1 112 33 30 ARG CB C 30.6 0.3 1 113 33 30 ARG N N 117.6 0.3 1 114 34 31 ILE H H 6.74 0.02 1 115 34 31 ILE C C 176.3 0.3 1 116 34 31 ILE CA C 59.6 0.3 1 117 34 31 ILE CB C 37.5 0.3 1 118 34 31 ILE N N 121.5 0.3 1 119 35 32 GLU H H 8.64 0.02 1 120 35 32 GLU C C 175.5 0.3 1 121 35 32 GLU CA C 57.7 0.3 1 122 35 32 GLU CB C 31.1 0.3 1 123 35 32 GLU N N 130.8 0.3 1 124 36 33 VAL H H 8.34 0.02 1 125 36 33 VAL C C 179.6 0.3 1 126 36 33 VAL CA C 63.6 0.3 1 127 36 33 VAL CB C 32.7 0.3 1 128 36 33 VAL N N 127.0 0.3 1 129 37 34 GLY H H 9.10 0.02 1 130 37 34 GLY C C 173.3 0.3 1 131 37 34 GLY CA C 46.7 0.3 1 132 37 34 GLY N N 115.3 0.3 1 133 38 35 THR H H 6.97 0.02 1 134 38 35 THR C C 177.1 0.3 1 135 38 35 THR CA C 58.7 0.3 1 136 38 35 THR CB C 72.3 0.3 1 137 38 35 THR N N 104.2 0.3 1 138 39 36 THR H H 9.75 0.02 1 139 39 36 THR C C 176.8 0.3 1 140 39 36 THR CA C 68.0 0.3 1 141 39 36 THR CB C 72.3 0.3 1 142 39 36 THR N N 124.7 0.3 1 143 40 37 ALA H H 9.32 0.02 1 144 40 37 ALA C C 181.8 0.3 1 145 40 37 ALA CA C 55.3 0.3 1 146 40 37 ALA CB C 17.7 0.3 1 147 40 37 ALA N N 125.2 0.3 1 148 41 38 GLY H H 8.52 0.02 1 149 41 38 GLY C C 177.6 0.3 1 150 41 38 GLY CA C 47.2 0.3 1 151 41 38 GLY N N 108.0 0.3 1 152 42 39 LEU H H 7.85 0.02 1 153 42 39 LEU C C 179.7 0.3 1 154 42 39 LEU CA C 58.4 0.3 1 155 42 39 LEU CB C 40.6 0.3 1 156 42 39 LEU N N 124.3 0.3 1 157 43 40 GLN H H 8.89 0.02 1 158 43 40 GLN C C 178.7 0.3 1 159 43 40 GLN CA C 61.5 0.3 1 160 43 40 GLN CB C 30.9 0.3 1 161 43 40 GLN N N 118.9 0.3 1 162 44 41 GLN H H 8.53 0.02 1 163 44 41 GLN C C 180.5 0.3 1 164 44 41 GLN CA C 59.7 0.3 1 165 44 41 GLN CB C 29.4 0.3 1 166 44 41 GLN N N 119.2 0.3 1 167 45 42 ILE H H 8.06 0.02 1 168 45 42 ILE C C 176.8 0.3 1 169 45 42 ILE CA C 66.5 0.3 1 170 45 42 ILE CB C 39.0 0.3 1 171 45 42 ILE N N 121.1 0.3 1 172 46 43 HIS H H 8.52 0.02 1 173 46 43 HIS C C 177.7 0.3 1 174 46 43 HIS CA C 63.2 0.3 1 175 46 43 HIS CB C 33.4 0.3 1 176 46 43 HIS N N 121.7 0.3 1 177 47 44 ARG H H 8.76 0.02 1 178 47 44 ARG C C 178.1 0.3 1 179 47 44 ARG CA C 59.8 0.3 1 180 47 44 ARG CB C 30.4 0.3 1 181 47 44 ARG N N 117.5 0.3 1 182 48 45 TYR H H 7.79 0.02 1 183 48 45 TYR C C 179.4 0.3 1 184 48 45 TYR CA C 61.1 0.3 1 185 48 45 TYR CB C 39.3 0.3 1 186 48 45 TYR N N 122.5 0.3 1 187 49 46 LEU H H 8.27 0.02 1 188 49 46 LEU C C 180.7 0.3 1 189 49 46 LEU CA C 58.6 0.3 1 190 49 46 LEU CB C 42.1 0.3 1 191 49 46 LEU N N 115.7 0.3 1 192 50 47 PHE H H 7.80 0.02 1 193 50 47 PHE C C 175.8 0.3 1 194 50 47 PHE CA C 57.3 0.3 1 195 50 47 PHE CB C 40.0 0.3 1 196 50 47 PHE N N 112.1 0.3 1 197 51 48 GLY H H 7.89 0.02 1 198 51 48 GLY C C 174.6 0.3 1 199 51 48 GLY CA C 47.5 0.3 1 200 51 48 GLY N N 115.4 0.3 1 201 52 49 GLY H H 9.09 0.02 1 202 52 49 GLY C C 173.4 0.3 1 203 52 49 GLY CA C 45.5 0.3 1 204 52 49 GLY N N 116.6 0.3 1 205 53 50 LEU H H 7.91 0.02 1 206 53 50 LEU C C 175.3 0.3 1 207 53 50 LEU CA C 55.5 0.3 1 208 53 50 LEU CB C 42.9 0.3 1 209 53 50 LEU N N 119.8 0.3 1 210 56 53 PHE C C 174.6 0.3 1 211 56 53 PHE CA C 54.9 0.3 1 212 57 54 ALA H H 6.86 0.02 1 213 57 54 ALA C C 179.1 0.3 1 214 57 54 ALA CA C 53.9 0.3 1 215 57 54 ALA CB C 18.2 0.3 1 216 57 54 ALA N N 124.2 0.3 1 217 58 55 GLY H H 12.04 0.02 1 218 58 55 GLY C C 177.8 0.3 1 219 58 55 GLY CA C 46.3 0.3 1 220 58 55 GLY N N 117.0 0.3 1 221 59 56 GLN H H 8.67 0.02 1 222 59 56 GLN C C 176.2 0.3 1 223 59 56 GLN CA C 55.1 0.3 1 224 59 56 GLN CB C 30.0 0.3 1 225 59 56 GLN N N 121.8 0.3 1 226 60 57 ILE H H 8.17 0.02 1 227 60 57 ILE C C 175.9 0.3 1 228 60 57 ILE CA C 60.1 0.3 1 229 60 57 ILE CB C 36.6 0.3 1 230 60 57 ILE N N 123.8 0.3 1 231 61 58 ARG H H 8.60 0.02 1 232 61 58 ARG C C 180.9 0.3 1 233 61 58 ARG CA C 56.7 0.3 1 234 61 58 ARG CB C 31.2 0.3 1 235 61 58 ARG N N 128.3 0.3 1 236 62 59 GLU H H 8.30 0.02 1 237 62 59 GLU C C 178.7 0.3 1 238 62 59 GLU CA C 55.6 0.3 1 239 62 59 GLU CB C 31.1 0.3 1 240 62 59 GLU N N 118.3 0.3 1 241 63 60 ASP H H 7.56 0.02 1 242 63 60 ASP C C 175.8 0.3 1 243 63 60 ASP CA C 53.3 0.3 1 244 63 60 ASP CB C 43.1 0.3 1 245 63 60 ASP N N 120.4 0.3 1 246 64 61 ASN H H 8.54 0.02 1 247 64 61 ASN C C 175.2 0.3 1 248 64 61 ASN CA C 53.5 0.3 1 249 64 61 ASN CB C 39.1 0.3 1 250 64 61 ASN N N 119.9 0.3 1 251 65 62 ILE H H 7.92 0.02 1 252 65 62 ILE C C 176.2 0.3 1 253 65 62 ILE CA C 61.2 0.3 1 254 65 62 ILE CB C 39.9 0.3 1 255 65 62 ILE N N 118.9 0.3 1 256 66 63 SER H H 8.27 0.02 1 257 66 63 SER C C 175.9 0.3 1 258 66 63 SER CA C 58.5 0.3 1 259 66 63 SER CB C 64.4 0.3 1 260 66 63 SER N N 119.2 0.3 1 261 67 64 LYS H H 8.23 0.02 1 262 67 64 LYS C C 176.6 0.3 1 263 67 64 LYS CA C 56.8 0.3 1 264 67 64 LYS CB C 33.5 0.3 1 265 67 64 LYS N N 123.8 0.3 1 266 68 65 GLY H H 8.41 0.02 1 267 68 65 GLY C C 175.0 0.3 1 268 68 65 GLY CA C 45.8 0.3 1 269 68 65 GLY N N 111.7 0.3 1 270 69 66 GLY H H 8.17 0.02 1 271 69 66 GLY C C 175.0 0.3 1 272 69 66 GLY CA C 45.3 0.3 1 273 69 66 GLY N N 109.5 0.3 1 274 70 67 PHE H H 7.76 0.02 1 275 70 67 PHE C C 175.3 0.3 1 276 70 67 PHE CA C 58.1 0.3 1 277 70 67 PHE CB C 40.0 0.3 1 278 70 67 PHE N N 121.1 0.3 1 279 71 68 ARG H H 7.85 0.02 1 280 71 68 ARG C C 174.1 0.3 1 281 71 68 ARG CA C 56.2 0.3 1 282 71 68 ARG CB C 30.3 0.3 1 283 71 68 ARG N N 124.2 0.3 1 284 72 69 PHE H H 7.75 0.02 1 285 72 69 PHE C C 178.0 0.3 1 286 72 69 PHE CA C 56.9 0.3 1 287 72 69 PHE CB C 40.0 0.3 1 288 72 69 PHE N N 121.6 0.3 1 289 73 70 ALA H H 7.97 0.02 1 290 73 70 ALA C C 176.6 0.3 1 291 73 70 ALA CA C 53.1 0.3 1 292 73 70 ALA CB C 19.1 0.3 1 293 73 70 ALA N N 123.3 0.3 1 294 74 71 ASN H H 7.46 0.02 1 295 74 71 ASN C C 178.2 0.3 1 296 74 71 ASN CA C 53.1 0.3 1 297 74 71 ASN CB C 39.8 0.3 1 298 74 71 ASN N N 115.0 0.3 1 299 75 72 ALA H H 8.45 0.02 1 300 75 72 ALA C C 176.5 0.3 1 301 75 72 ALA CA C 53.7 0.3 1 302 75 72 ALA CB C 18.7 0.3 1 303 75 72 ALA N N 125.3 0.3 1 304 76 73 MET H H 8.18 0.02 1 305 76 73 MET C C 181.3 0.3 1 306 76 73 MET CA C 57.0 0.3 1 307 76 73 MET CB C 33.0 0.3 1 308 76 73 MET N N 118.1 0.3 1 309 77 74 TYR H H 8.04 0.02 1 310 77 74 TYR C C 176.3 0.3 1 311 77 74 TYR CA C 61.5 0.3 1 312 77 74 TYR CB C 38.8 0.3 1 313 77 74 TYR N N 123.3 0.3 1 314 78 75 LEU H H 7.96 0.02 1 315 78 75 LEU C C 180.5 0.3 1 316 78 75 LEU CA C 59.4 0.3 1 317 78 75 LEU CB C 37.8 0.3 1 318 78 75 LEU N N 123.8 0.3 1 319 79 76 LYS H H 8.14 0.02 1 320 79 76 LYS C C 179.3 0.3 1 321 79 76 LYS CA C 59.8 0.3 1 322 79 76 LYS CB C 29.9 0.3 1 323 79 76 LYS N N 120.5 0.3 1 324 80 77 GLU H H 8.09 0.02 1 325 80 77 GLU C C 179.1 0.3 1 326 80 77 GLU CA C 59.0 0.3 1 327 80 77 GLU CB C 29.0 0.3 1 328 80 77 GLU N N 119.0 0.3 1 329 81 78 ALA H H 7.92 0.02 1 330 81 78 ALA C C 180.9 0.3 1 331 81 78 ALA CA C 55.3 0.3 1 332 81 78 ALA CB C 17.7 0.3 1 333 81 78 ALA N N 122.5 0.3 1 334 82 79 LEU H H 8.23 0.02 1 335 82 79 LEU C C 178.8 0.3 1 336 82 79 LEU CA C 58.4 0.3 1 337 82 79 LEU CB C 40.4 0.3 1 338 82 79 LEU N N 118.1 0.3 1 339 83 80 VAL H H 7.10 0.02 1 340 83 80 VAL C C 178.1 0.3 1 341 83 80 VAL CA C 66.3 0.3 1 342 83 80 VAL CB C 31.9 0.3 1 343 83 80 VAL N N 119.9 0.3 1 344 84 81 LYS H H 6.98 0.02 1 345 84 81 LYS C C 180.5 0.3 1 346 84 81 LYS CA C 59.0 0.3 1 347 84 81 LYS CB C 32.0 0.3 1 348 84 81 LYS N N 117.4 0.3 1 349 85 82 ILE H H 8.16 0.02 1 350 85 82 ILE C C 179.3 0.3 1 351 85 82 ILE CA C 65.7 0.3 1 352 85 82 ILE CB C 38.8 0.3 1 353 85 82 ILE N N 120.5 0.3 1 354 86 83 GLU H H 8.31 0.02 1 355 86 83 GLU C C 177.9 0.3 1 356 86 83 GLU CA C 59.8 0.3 1 357 86 83 GLU CB C 29.0 0.3 1 358 86 83 GLU N N 118.7 0.3 1 359 87 84 GLN H H 7.13 0.02 1 360 87 84 GLN C C 176.6 0.3 1 361 87 84 GLN CA C 56.4 0.3 1 362 87 84 GLN CB C 29.0 0.3 1 363 87 84 GLN N N 116.7 0.3 1 364 88 85 MET H H 7.83 0.02 1 365 88 85 MET C C 174.7 0.3 1 366 88 85 MET CA C 56.2 0.3 1 367 88 85 MET CB C 32.3 0.3 1 368 88 85 MET N N 122.5 0.3 1 369 89 86 PRO C C 176.1 0.3 1 370 89 86 PRO CA C 62.9 0.3 1 371 89 86 PRO CB C 33.0 0.3 1 372 90 87 GLU H H 8.33 0.02 1 373 90 87 GLU C C 174.3 0.3 1 374 90 87 GLU CA C 54.1 0.3 1 375 90 87 GLU CB C 30.5 0.3 1 376 90 87 GLU N N 116.7 0.3 1 377 91 88 ARG H H 7.88 0.02 1 378 91 88 ARG C C 178.5 0.3 1 379 91 88 ARG CA C 58.9 0.3 1 380 91 88 ARG CB C 31.3 0.3 1 381 91 88 ARG N N 115.5 0.3 1 382 92 89 THR H H 7.26 0.02 1 383 92 89 THR C C 174.7 0.3 1 384 92 89 THR CA C 57.9 0.3 1 385 92 89 THR CB C 73.0 0.3 1 386 92 89 THR N N 105.1 0.3 1 387 93 90 PHE H H 9.46 0.02 1 388 93 90 PHE C C 175.7 0.3 1 389 93 90 PHE CA C 62.7 0.3 1 390 93 90 PHE CB C 39.3 0.3 1 391 93 90 PHE N N 122.4 0.3 1 392 94 91 GLU H H 9.06 0.02 1 393 94 91 GLU C C 179.9 0.3 1 394 94 91 GLU CA C 62.5 0.3 1 395 94 91 GLU CB C 28.4 0.3 1 396 94 91 GLU N N 117.7 0.3 1 397 95 92 GLU H H 7.71 0.02 1 398 95 92 GLU C C 180.2 0.3 1 399 95 92 GLU CA C 59.6 0.3 1 400 95 92 GLU CB C 29.0 0.3 1 401 95 92 GLU N N 121.4 0.3 1 402 96 93 ILE H H 8.23 0.02 1 403 96 93 ILE C C 177.8 0.3 1 404 96 93 ILE CA C 66.8 0.3 1 405 96 93 ILE CB C 37.9 0.3 1 406 96 93 ILE N N 123.1 0.3 1 407 97 94 ILE H H 8.20 0.02 1 408 97 94 ILE C C 177.8 0.3 1 409 97 94 ILE CA C 61.8 0.3 1 410 97 94 ILE CB C 33.9 0.3 1 411 97 94 ILE N N 119.1 0.3 1 412 98 95 ALA H H 7.76 0.02 1 413 98 95 ALA C C 180.4 0.3 1 414 98 95 ALA CA C 55.8 0.3 1 415 98 95 ALA CB C 17.7 0.3 1 416 98 95 ALA N N 122.6 0.3 1 417 99 96 LYS C C 179.3 0.3 1 418 99 96 LYS CA C 59.8 0.3 1 419 99 96 LYS CB C 31.2 0.3 1 420 100 97 TYR H H 8.48 0.02 1 421 100 97 TYR C C 177.3 0.3 1 422 100 97 TYR CA C 61.2 0.3 1 423 100 97 TYR CB C 39.7 0.3 1 424 100 97 TYR N N 120.2 0.3 1 425 101 98 VAL H H 9.20 0.02 1 426 101 98 VAL C C 179.0 0.3 1 427 101 98 VAL CA C 67.4 0.3 1 428 101 98 VAL CB C 31.7 0.3 1 429 101 98 VAL N N 122.1 0.3 1 430 102 99 ARG H H 7.62 0.02 1 431 102 99 ARG C C 177.9 0.3 1 432 102 99 ARG CA C 59.0 0.3 1 433 102 99 ARG CB C 29.4 0.3 1 434 102 99 ARG N N 117.4 0.3 1 435 103 100 MET H H 8.13 0.02 1 436 103 100 MET C C 177.8 0.3 1 437 103 100 MET CA C 57.6 0.3 1 438 103 100 MET CB C 32.6 0.3 1 439 103 100 MET N N 120.8 0.3 1 440 104 101 ASN H H 8.15 0.02 1 441 104 101 ASN C C 177.4 0.3 1 442 104 101 ASN CA C 57.3 0.3 1 443 104 101 ASN CB C 39.3 0.3 1 444 104 101 ASN N N 117.8 0.3 1 445 105 102 ILE H H 7.58 0.02 1 446 105 102 ILE C C 177.1 0.3 1 447 105 102 ILE CA C 64.6 0.3 1 448 105 102 ILE CB C 38.9 0.3 1 449 105 102 ILE N N 119.7 0.3 1 450 106 103 ALA H H 7.52 0.02 1 451 106 103 ALA C C 176.9 0.3 1 452 106 103 ALA CA C 55.2 0.3 1 453 106 103 ALA CB C 17.5 0.3 1 454 106 103 ALA N N 121.9 0.3 1 455 107 104 ALA H H 7.02 0.02 1 456 107 104 ALA C C 174.2 0.3 1 457 107 104 ALA CA C 52.1 0.3 1 458 107 104 ALA CB C 18.1 0.3 1 459 107 104 ALA N N 112.2 0.3 1 460 108 105 PRO C C 173.7 0.3 1 461 108 105 PRO CA C 64.9 0.3 1 462 108 105 PRO CB C 32.4 0.3 1 463 109 106 PHE H H 8.47 0.02 1 464 109 106 PHE C C 177.8 0.3 1 465 109 106 PHE CA C 54.8 0.3 1 466 109 106 PHE CB C 42.8 0.3 1 467 109 106 PHE N N 116.1 0.3 1 468 110 107 LEU H H 8.47 0.02 1 469 110 107 LEU C C 177.3 0.3 1 470 110 107 LEU CA C 57.9 0.3 1 471 110 107 LEU CB C 39.8 0.3 1 472 110 107 LEU N N 120.4 0.3 1 473 111 108 GLU H H 6.71 0.02 1 474 111 108 GLU C C 176.4 0.3 1 475 111 108 GLU CA C 54.4 0.3 1 476 111 108 GLU CB C 34.3 0.3 1 477 111 108 GLU N N 110.8 0.3 1 478 112 109 GLY H H 9.58 0.02 1 479 112 109 GLY C C 176.7 0.3 1 480 112 109 GLY CA C 47.4 0.3 1 481 112 109 GLY N N 111.1 0.3 1 482 113 110 ASN H H 8.43 0.02 1 483 113 110 ASN C C 179.6 0.3 1 484 113 110 ASN CA C 58.2 0.3 1 485 113 110 ASN CB C 39.9 0.3 1 486 113 110 ASN N N 121.2 0.3 1 487 114 111 GLY H H 9.12 0.02 1 488 114 111 GLY C C 176.2 0.3 1 489 114 111 GLY CA C 48.0 0.3 1 490 114 111 GLY N N 115.7 0.3 1 491 115 112 ARG H H 8.43 0.02 1 492 115 112 ARG C C 179.6 0.3 1 493 115 112 ARG CA C 59.3 0.3 1 494 115 112 ARG CB C 30.6 0.3 1 495 115 112 ARG N N 121.0 0.3 1 496 116 113 SER H H 7.32 0.02 1 497 116 113 SER C C 179.5 0.3 1 498 116 113 SER CA C 62.1 0.3 1 499 116 113 SER CB C 63.2 0.3 1 500 116 113 SER N N 111.0 0.3 1 501 117 114 THR H H 8.29 0.02 1 502 117 114 THR C C 176.3 0.3 1 503 117 114 THR CA C 66.2 0.3 1 504 117 114 THR CB C 69.0 0.3 1 505 117 114 THR N N 115.7 0.3 1 506 118 115 ARG H H 7.96 0.02 1 507 118 115 ARG C C 177.9 0.3 1 508 118 115 ARG CA C 62.8 0.3 1 509 118 115 ARG CB C 30.5 0.3 1 510 118 115 ARG N N 123.2 0.3 1 511 119 116 ILE H H 6.58 0.02 1 512 119 116 ILE C C 177.8 0.3 1 513 119 116 ILE CA C 65.7 0.3 1 514 119 116 ILE CB C 38.9 0.3 1 515 119 116 ILE N N 118.7 0.3 1 516 120 117 TRP H H 7.90 0.02 1 517 120 117 TRP C C 178.4 0.3 1 518 120 117 TRP CA C 62.4 0.3 1 519 120 117 TRP CB C 30.6 0.3 1 520 120 117 TRP N N 121.1 0.3 1 521 121 118 LEU H H 8.83 0.02 1 522 121 118 LEU C C 177.6 0.3 1 523 121 118 LEU CA C 58.5 0.3 1 524 121 118 LEU CB C 41.2 0.3 1 525 121 118 LEU N N 120.9 0.3 1 526 122 119 ASP H H 7.86 0.02 1 527 122 119 ASP C C 179.4 0.3 1 528 122 119 ASP CA C 58.4 0.3 1 529 122 119 ASP CB C 40.8 0.3 1 530 122 119 ASP N N 121.4 0.3 1 531 123 120 LEU H H 7.91 0.02 1 532 123 120 LEU C C 180.4 0.3 1 533 123 120 LEU CA C 58.2 0.3 1 534 123 120 LEU CB C 41.7 0.3 1 535 123 120 LEU N N 117.7 0.3 1 536 124 121 VAL H H 7.43 0.02 1 537 124 121 VAL C C 180.3 0.3 1 538 124 121 VAL CA C 66.9 0.3 1 539 124 121 VAL CB C 31.3 0.3 1 540 124 121 VAL N N 122.0 0.3 1 541 125 122 LEU H H 8.91 0.02 1 542 125 122 LEU C C 179.9 0.3 1 543 125 122 LEU CA C 59.3 0.3 1 544 125 122 LEU CB C 42.6 0.3 1 545 125 122 LEU N N 124.9 0.3 1 546 126 123 LYS H H 9.18 0.02 1 547 126 123 LYS C C 180.1 0.3 1 548 126 123 LYS CA C 61.6 0.3 1 549 126 123 LYS CB C 32.9 0.3 1 550 126 123 LYS N N 125.4 0.3 1 551 127 124 LYS H H 7.91 0.02 1 552 127 124 LYS C C 177.6 0.3 1 553 127 124 LYS CA C 59.5 0.3 1 554 127 124 LYS CB C 34.1 0.3 1 555 127 124 LYS N N 119.5 0.3 1 556 128 125 ASN H H 7.52 0.02 1 557 128 125 ASN C C 176.1 0.3 1 558 128 125 ASN CA C 56.5 0.3 1 559 128 125 ASN CB C 42.3 0.3 1 560 128 125 ASN N N 112.5 0.3 1 561 129 126 LEU H H 8.62 0.02 1 562 129 126 LEU C C 176.2 0.3 1 563 129 126 LEU CA C 53.9 0.3 1 564 129 126 LEU CB C 43.3 0.3 1 565 129 126 LEU N N 117.2 0.3 1 566 130 127 LYS H H 7.60 0.02 1 567 130 127 LYS C C 174.8 0.3 1 568 130 127 LYS CA C 57.6 0.3 1 569 130 127 LYS CB C 29.2 0.3 1 570 130 127 LYS N N 117.2 0.3 1 571 131 128 LYS H H 6.92 0.02 1 572 131 128 LYS C C 174.0 0.3 1 573 131 128 LYS CA C 54.8 0.3 1 574 131 128 LYS CB C 40.2 0.3 1 575 131 128 LYS N N 116.8 0.3 1 576 132 129 VAL H H 7.78 0.02 1 577 132 129 VAL C C 175.2 0.3 1 578 132 129 VAL CA C 59.8 0.3 1 579 132 129 VAL CB C 36.5 0.3 1 580 132 129 VAL N N 106.2 0.3 1 581 133 130 VAL H H 8.92 0.02 1 582 133 130 VAL C C 176.1 0.3 1 583 133 130 VAL CA C 63.8 0.3 1 584 133 130 VAL CB C 31.2 0.3 1 585 133 130 VAL N N 121.4 0.3 1 586 134 131 ASN H H 8.69 0.02 1 587 134 131 ASN C C 176.0 0.3 1 588 134 131 ASN CA C 49.7 0.3 1 589 134 131 ASN CB C 35.8 0.3 1 590 134 131 ASN N N 126.9 0.3 1 591 135 132 TRP H H 7.19 0.02 1 592 135 132 TRP C C 178.4 0.3 1 593 135 132 TRP CA C 60.4 0.3 1 594 135 132 TRP CB C 30.5 0.3 1 595 135 132 TRP N N 121.7 0.3 1 596 136 133 GLN H H 8.61 0.02 1 597 136 133 GLN C C 175.3 0.3 1 598 136 133 GLN CA C 58.5 0.3 1 599 136 133 GLN CB C 27.5 0.3 1 600 136 133 GLN N N 114.5 0.3 1 601 137 134 ASN H H 7.42 0.02 1 602 137 134 ASN C C 174.5 0.3 1 603 137 134 ASN CA C 52.5 0.3 1 604 137 134 ASN CB C 39.6 0.3 1 605 137 134 ASN N N 117.2 0.3 1 606 138 135 VAL H H 8.12 0.02 1 607 138 135 VAL C C 176.1 0.3 1 608 138 135 VAL CA C 62.5 0.3 1 609 138 135 VAL CB C 30.4 0.3 1 610 138 135 VAL N N 124.4 0.3 1 611 139 136 SER H H 8.67 0.02 1 612 139 136 SER C C 174.4 0.3 1 613 139 136 SER CA C 58.4 0.3 1 614 139 136 SER CB C 64.3 0.3 1 615 139 136 SER N N 127.2 0.3 1 616 140 137 LYS H H 9.03 0.02 1 617 140 137 LYS C C 177.6 0.3 1 618 140 137 LYS CA C 60.7 0.3 1 619 140 137 LYS CB C 33.4 0.3 1 620 140 137 LYS N N 126.6 0.3 1 621 141 138 THR H H 8.19 0.02 1 622 141 138 THR C C 177.1 0.3 1 623 141 138 THR CA C 66.6 0.3 1 624 141 138 THR CB C 69.0 0.3 1 625 141 138 THR N N 113.1 0.3 1 626 142 139 LEU H H 7.16 0.02 1 627 142 139 LEU C C 180.2 0.3 1 628 142 139 LEU CA C 57.6 0.3 1 629 142 139 LEU CB C 41.6 0.3 1 630 142 139 LEU N N 119.4 0.3 1 631 143 140 TYR H H 8.69 0.02 1 632 143 140 TYR C C 176.9 0.3 1 633 143 140 TYR CA C 62.4 0.3 1 634 143 140 TYR CB C 38.6 0.3 1 635 143 140 TYR N N 122.3 0.3 1 636 144 141 LEU H H 8.53 0.02 1 637 144 141 LEU C C 181.2 0.3 1 638 144 141 LEU CA C 58.4 0.3 1 639 144 141 LEU CB C 40.6 0.3 1 640 144 141 LEU N N 119.3 0.3 1 641 145 142 GLN H H 7.53 0.02 1 642 145 142 GLN C C 179.1 0.3 1 643 145 142 GLN CA C 59.1 0.3 1 644 145 142 GLN CB C 29.0 0.3 1 645 145 142 GLN N N 118.4 0.3 1 646 146 143 ALA H H 7.89 0.02 1 647 146 143 ALA C C 181.6 0.3 1 648 146 143 ALA CA C 55.3 0.3 1 649 146 143 ALA CB C 17.7 0.3 1 650 146 143 ALA N N 123.5 0.3 1 651 147 144 MET H H 8.58 0.02 1 652 147 144 MET C C 181.4 0.3 1 653 147 144 MET CA C 56.5 0.3 1 654 147 144 MET CB C 29.7 0.3 1 655 147 144 MET N N 118.6 0.3 1 656 148 145 GLU H H 8.06 0.02 1 657 148 145 GLU C C 175.4 0.3 1 658 148 145 GLU CA C 57.4 0.3 1 659 148 145 GLU CB C 30.1 0.3 1 660 148 145 GLU N N 125.9 0.3 1 661 149 146 ARG H H 8.02 0.02 1 662 149 146 ARG C C 176.6 0.3 1 663 149 146 ARG CA C 59.7 0.3 1 664 149 146 ARG CB C 31.1 0.3 1 665 149 146 ARG N N 123.3 0.3 1 666 150 147 SER H H 8.24 0.02 1 667 150 147 SER C C 176.5 0.3 1 668 150 147 SER CA C 58.6 0.3 1 669 150 147 SER CB C 63.9 0.3 1 670 150 147 SER N N 120.2 0.3 1 671 151 148 PRO C C 177.2 0.3 1 672 151 148 PRO CA C 65.7 0.3 1 673 151 148 PRO CB C 31.7 0.3 1 674 152 149 VAL H H 7.48 0.02 1 675 152 149 VAL C C 176.4 0.3 1 676 152 149 VAL CA C 63.3 0.3 1 677 152 149 VAL CB C 33.4 0.3 1 678 152 149 VAL N N 113.7 0.3 1 679 153 150 ASN H H 7.88 0.02 1 680 153 150 ASN C C 175.6 0.3 1 681 153 150 ASN CA C 53.6 0.3 1 682 153 150 ASN CB C 39.9 0.3 1 683 153 150 ASN N N 117.4 0.3 1 684 154 151 ASP H H 8.67 0.02 1 685 154 151 ASP C C 176.5 0.3 1 686 154 151 ASP CA C 53.9 0.3 1 687 154 151 ASP CB C 40.8 0.3 1 688 154 151 ASP N N 128.7 0.3 1 689 155 152 LEU H H 7.87 0.02 1 690 155 152 LEU C C 178.7 0.3 1 691 155 152 LEU CA C 59.8 0.3 1 692 155 152 LEU CB C 42.2 0.3 1 693 155 152 LEU N N 122.4 0.3 1 694 156 153 ARG H H 8.46 0.02 1 695 156 153 ARG C C 179.9 0.3 1 696 156 153 ARG CA C 59.8 0.3 1 697 156 153 ARG CB C 29.4 0.3 1 698 156 153 ARG N N 117.0 0.3 1 699 157 154 LEU H H 7.90 0.02 1 700 157 154 LEU C C 177.7 0.3 1 701 157 154 LEU CA C 58.0 0.3 1 702 157 154 LEU CB C 42.4 0.3 1 703 157 154 LEU N N 120.7 0.3 1 704 158 155 ARG H H 8.73 0.02 1 705 158 155 ARG C C 178.7 0.3 1 706 158 155 ARG CA C 61.4 0.3 1 707 158 155 ARG CB C 31.2 0.3 1 708 158 155 ARG N N 118.5 0.3 1 709 159 156 PHE H H 8.48 0.02 1 710 159 156 PHE C C 177.9 0.3 1 711 159 156 PHE CA C 60.8 0.3 1 712 159 156 PHE CB C 38.3 0.3 1 713 159 156 PHE N N 117.4 0.3 1 714 160 157 LEU H H 7.82 0.02 1 715 160 157 LEU C C 178.7 0.3 1 716 160 157 LEU CA C 57.8 0.3 1 717 160 157 LEU CB C 43.2 0.3 1 718 160 157 LEU N N 120.2 0.3 1 719 161 158 LEU H H 8.30 0.02 1 720 161 158 LEU C C 179.3 0.3 1 721 161 158 LEU CA C 57.9 0.3 1 722 161 158 LEU CB C 40.3 0.3 1 723 161 158 LEU N N 115.3 0.3 1 724 162 159 LYS H H 8.48 0.02 1 725 162 159 LYS C C 179.3 0.3 1 726 162 159 LYS CA C 59.8 0.3 1 727 162 159 LYS CB C 31.8 0.3 1 728 162 159 LYS N N 120.2 0.3 1 729 163 160 ASP H H 7.29 0.02 1 730 163 160 ASP C C 176.4 0.3 1 731 163 160 ASP CA C 55.7 0.3 1 732 163 160 ASP CB C 41.2 0.3 1 733 163 160 ASP N N 116.3 0.3 1 734 164 161 ASN H H 7.38 0.02 1 735 164 161 ASN C C 173.1 0.3 1 736 164 161 ASN CA C 53.3 0.3 1 737 164 161 ASN CB C 41.6 0.3 1 738 164 161 ASN N N 116.6 0.3 1 739 165 162 LEU H H 6.94 0.02 1 740 165 162 LEU C C 177.7 0.3 1 741 165 162 LEU CA C 54.9 0.3 1 742 165 162 LEU CB C 43.5 0.3 1 743 165 162 LEU N N 119.6 0.3 1 744 166 163 THR H H 9.03 0.02 1 745 166 163 THR C C 171.8 0.3 1 746 166 163 THR CA C 59.3 0.3 1 747 166 163 THR CB C 69.5 0.3 1 748 166 163 THR N N 116.6 0.3 1 749 167 164 ASP H H 8.10 0.02 1 750 167 164 ASP C C 177.7 0.3 1 751 167 164 ASP CA C 54.1 0.3 1 752 167 164 ASP CB C 41.3 0.3 1 753 167 164 ASP N N 124.6 0.3 1 754 168 165 ASP H H 8.72 0.02 1 755 168 165 ASP C C 177.5 0.3 1 756 168 165 ASP CA C 52.8 0.3 1 757 168 165 ASP CB C 38.3 0.3 1 758 168 165 ASP N N 128.9 0.3 1 759 169 166 VAL H H 7.17 0.02 1 760 169 166 VAL C C 174.9 0.3 1 761 169 166 VAL CA C 64.0 0.3 1 762 169 166 VAL CB C 31.3 0.3 1 763 169 166 VAL N N 108.7 0.3 1 764 170 167 ASP H H 8.34 0.02 1 765 170 167 ASP C C 176.1 0.3 1 766 170 167 ASP CA C 53.4 0.3 1 767 170 167 ASP CB C 41.6 0.3 1 768 170 167 ASP N N 118.0 0.3 1 769 171 168 ASN H H 6.94 0.02 1 770 171 168 ASN C C 175.8 0.3 1 771 171 168 ASN CA C 53.6 0.3 1 772 171 168 ASN CB C 38.5 0.3 1 773 171 168 ASN N N 120.6 0.3 1 774 172 169 ARG H H 8.68 0.02 1 775 172 169 ARG C C 177.1 0.3 1 776 172 169 ARG CA C 59.4 0.3 1 777 172 169 ARG CB C 29.7 0.3 1 778 172 169 ARG N N 128.4 0.3 1 779 173 170 GLU H H 7.82 0.02 1 780 173 170 GLU C C 179.0 0.3 1 781 173 170 GLU CA C 59.8 0.3 1 782 173 170 GLU CB C 29.2 0.3 1 783 173 170 GLU N N 119.0 0.3 1 784 174 171 ILE H H 6.94 0.02 1 785 174 171 ILE C C 180.2 0.3 1 786 174 171 ILE CA C 65.4 0.3 1 787 174 171 ILE CB C 38.1 0.3 1 788 174 171 ILE N N 119.6 0.3 1 789 175 172 ILE H H 7.89 0.02 1 790 175 172 ILE C C 179.4 0.3 1 791 175 172 ILE CA C 65.3 0.3 1 792 175 172 ILE CB C 38.3 0.3 1 793 175 172 ILE N N 121.4 0.3 1 794 176 173 PHE H H 8.76 0.02 1 795 176 173 PHE C C 180.1 0.3 1 796 176 173 PHE CA C 59.7 0.3 1 797 176 173 PHE CB C 36.7 0.3 1 798 176 173 PHE N N 119.7 0.3 1 799 177 174 LYS H H 8.52 0.02 1 800 177 174 LYS C C 180.6 0.3 1 801 177 174 LYS CA C 59.0 0.3 1 802 177 174 LYS CB C 31.3 0.3 1 803 177 174 LYS N N 120.1 0.3 1 804 178 175 GLY H H 7.93 0.02 1 805 178 175 GLY C C 175.6 0.3 1 806 178 175 GLY CA C 48.3 0.3 1 807 178 175 GLY N N 111.0 0.3 1 808 179 176 ILE H H 7.99 0.02 1 809 179 176 ILE C C 178.3 0.3 1 810 179 176 ILE CA C 64.9 0.3 1 811 179 176 ILE CB C 38.5 0.3 1 812 179 176 ILE N N 123.6 0.3 1 813 180 177 GLU H H 7.45 0.02 1 814 180 177 GLU C C 178.9 0.3 1 815 180 177 GLU CA C 60.5 0.3 1 816 180 177 GLU CB C 29.4 0.3 1 817 180 177 GLU N N 119.3 0.3 1 818 181 178 GLN H H 7.59 0.02 1 819 181 178 GLN C C 177.1 0.3 1 820 181 178 GLN CA C 58.7 0.3 1 821 181 178 GLN CB C 27.6 0.3 1 822 181 178 GLN N N 120.6 0.3 1 823 182 179 SER H H 7.89 0.02 1 824 182 179 SER C C 178.7 0.3 1 825 182 179 SER CA C 58.5 0.3 1 826 182 179 SER CB C 62.9 0.3 1 827 182 179 SER N N 112.1 0.3 1 828 183 180 TYR H H 8.48 0.02 1 829 183 180 TYR C C 179.4 0.3 1 830 183 180 TYR CA C 61.0 0.3 1 831 183 180 TYR CB C 31.7 0.3 1 832 183 180 TYR N N 117.7 0.3 1 833 184 181 TYR C C 173.9 0.3 1 834 184 181 TYR CA C 59.6 0.3 1 835 184 181 TYR CB C 36.7 0.3 1 836 185 182 TYR H H 7.89 0.02 1 837 185 182 TYR C C 177.0 0.3 1 838 185 182 TYR CA C 58.5 0.3 1 839 185 182 TYR CB C 36.9 0.3 1 840 185 182 TYR N N 120.3 0.3 1 841 186 183 GLU H H 7.29 0.02 1 842 186 183 GLU C C 176.7 0.3 1 843 186 183 GLU CA C 55.6 0.3 1 844 186 183 GLU CB C 29.4 0.3 1 845 186 183 GLU N N 113.5 0.3 1 846 187 184 GLY H H 7.45 0.02 1 847 187 184 GLY C C 174.1 0.3 1 848 187 184 GLY CA C 45.5 0.3 1 849 187 184 GLY N N 107.2 0.3 1 850 188 185 TYR H H 7.84 0.02 1 851 188 185 TYR C C 175.1 0.3 1 852 188 185 TYR CA C 58.4 0.3 1 853 188 185 TYR CB C 39.5 0.3 1 854 188 185 TYR N N 122.3 0.3 1 855 189 186 GLU H H 8.08 0.02 1 856 189 186 GLU C C 175.4 0.3 1 857 189 186 GLU CA C 55.8 0.3 1 858 189 186 GLU CB C 31.1 0.3 1 859 189 186 GLU N N 126.5 0.3 1 860 190 187 LYS H H 8.01 0.02 1 861 190 187 LYS C C 176.3 0.3 1 862 190 187 LYS CA C 56.9 0.3 1 863 190 187 LYS CB C 33.2 0.3 1 864 190 187 LYS N N 123.4 0.3 1 865 191 188 GLY H H 7.93 0.02 1 866 191 188 GLY C C 179.2 0.3 1 867 191 188 GLY CA C 46.2 0.3 1 868 191 188 GLY N N 116.9 0.3 1 stop_ save_