data_16831 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of C-domain of Lsr2 ; _BMRB_accession_number 16831 _BMRB_flat_file_name bmr16831.str _Entry_type original _Submission_date 2010-04-02 _Accession_date 2010-04-02 _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 Li Yifei . . 2 Xia Bin . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 244 "13C chemical shifts" 196 "15N chemical shifts" 54 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-05-11 original author . stop_ _Original_release_date 2010-05-11 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Lsr2 is a nucleoid-associated protein that targets AT-rich sequences and virulence genes in Mycobacterium tuberculosis.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20133735 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gordon Blair R.G. . 2 Li Yifei . . 3 Wang Linru . . 4 Sintsova Anna . . 5 'van Bakel' Harm . . 6 Tian Songhai . . 7 Navarre 'William Wiley' . . 8 Xia Bin . . 9 Liu Jun . . 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 107 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5154 _Page_last 5159 _Year 2010 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'C-domain of Lsr2' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Lsr2C $Lsr2C stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Lsr2C _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Lsr2C _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 55 _Mol_residue_sequence ; SGSGRGRGAIDREQSAAIRE WARRNGHNVSTRGRIPADVI DAYHAATLEHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 SER 2 GLY 3 SER 4 GLY 5 ARG 6 GLY 7 ARG 8 GLY 9 ALA 10 ILE 11 ASP 12 ARG 13 GLU 14 GLN 15 SER 16 ALA 17 ALA 18 ILE 19 ARG 20 GLU 21 TRP 22 ALA 23 ARG 24 ARG 25 ASN 26 GLY 27 HIS 28 ASN 29 VAL 30 SER 31 THR 32 ARG 33 GLY 34 ARG 35 ILE 36 PRO 37 ALA 38 ASP 39 VAL 40 ILE 41 ASP 42 ALA 43 TYR 44 HIS 45 ALA 46 ALA 47 THR 48 LEU 49 GLU 50 HIS 51 HIS 52 HIS 53 HIS 54 HIS 55 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-28 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 2KNG "Solution Structure Of C-Domain Of Lsr2" 100.00 55 100.00 100.00 5.37e-29 DBJ BAH27935 "putative lsr2 protein precursor [Mycobacterium bovis BCG str. Tokyo 172]" 70.91 112 100.00 100.00 9.46e-18 DBJ BAL67717 "iron-regulated LSR2 protein precursor [Mycobacterium tuberculosis str. Erdman = ATCC 35801]" 70.91 112 100.00 100.00 9.46e-18 DBJ BAN29552 "LSR2 protein [Mycobacterium avium subsp. hominissuis TH135]" 70.91 112 97.44 100.00 2.32e-17 DBJ BAQ07815 "iron-regulated LSR2 protein precursor [Mycobacterium tuberculosis str. Kurono]" 70.91 112 100.00 100.00 9.46e-18 DBJ GAA43492 "iron-regulated LSR2 protein precursor [Mycobacterium tuberculosis NCGM2209]" 70.91 112 100.00 100.00 9.46e-18 EMBL CAA37572 "LSR2 [Mycobacterium leprae]" 70.91 89 97.44 100.00 4.14e-17 EMBL CAC29742 "lsr2 protein (15 kDa antigen) [Mycobacterium leprae]" 70.91 112 97.44 100.00 3.02e-17 EMBL CAL73651 "Probable lsr2 protein precursor [Mycobacterium bovis BCG str. Pasteur 1173P2]" 70.91 112 100.00 100.00 9.46e-18 EMBL CAR70327 "lsr2 protein (15 kDa antigen) [Mycobacterium leprae Br4923]" 70.91 112 97.44 100.00 3.02e-17 EMBL CCC28679 "putative iron-regulated LSR2 protein precursor [Mycobacterium africanum GM041182]" 70.91 112 100.00 100.00 9.46e-18 GB AAA25351 "antigen 15 kDa [Mycobacterium leprae]" 70.91 112 97.44 100.00 3.02e-17 GB AAK48061 "lsr2 protein [Mycobacterium tuberculosis CDC1551]" 70.91 112 100.00 100.00 9.46e-18 GB AAS02777 "Lsr2 [Mycobacterium avium subsp. paratuberculosis K-10]" 70.91 112 97.44 100.00 2.32e-17 GB ABK67018 "Lsr2 protein [Mycobacterium avium 104]" 70.91 108 97.44 100.00 2.54e-17 GB ABL06215 "iron-regulated Lsr2 protein precursor [Mycobacterium ulcerans Agy99]" 69.09 113 97.37 100.00 1.45e-16 REF NP_218114 "iron-regulated H-NS-like protein [Mycobacterium tuberculosis H37Rv]" 70.91 112 100.00 100.00 9.46e-18 REF NP_301294 "nucleoid-associated protein Lsr2 [Mycobacterium leprae TN]" 70.91 112 97.44 100.00 3.02e-17 REF NP_857267 "LSR2 protein precursor [Mycobacterium bovis AF2122/97]" 70.91 112 100.00 100.00 9.46e-18 REF WP_003419513 "MULTISPECIES: nucleoid-associated protein [Mycobacterium]" 70.91 112 100.00 100.00 9.46e-18 REF WP_003875617 "MULTISPECIES: hypothetical protein [Mycobacterium]" 70.91 112 97.44 100.00 2.32e-17 SP P24094 "RecName: Full=Nucleoid-associated protein Lsr2; AltName: Full=15 kDa antigen; AltName: Full=A15" 70.91 112 97.44 100.00 3.02e-17 SP P65649 "RecName: Full=Nucleoid-associated protein Lsr2" 70.91 112 100.00 100.00 9.46e-18 SP P9WIP6 "RecName: Full=Nucleoid-associated protein Lsr2" 70.91 112 100.00 100.00 9.46e-18 SP P9WIP7 "RecName: Full=Nucleoid-associated protein Lsr2" 70.91 112 100.00 100.00 9.46e-18 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Lsr2C 'Mycobacterium tuberculosis' 1773 Bacteria . Mycobacterium tuberculosis 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 $Lsr2C 'recombinant technology' . Escherichia coli . pET21d 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 $Lsr2C 0.8 mM '[U-13C; U-15N]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' 'PBS Na+' 50 mM 'natural abundance' NaCl 50 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_AMBER _Saveframe_category software _Name AMBER _Version 9 loop_ _Vendor _Address _Electronic_address 'Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm' . . 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 'Duggan, Legge, Dyson & Wright' . . 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _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_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_HCCH-COSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-COSY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _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' 100 . mM pH 6.0 . 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 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0 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_ _Experiment_label '2D 1H-15N HSQC' '3D 1H-15N NOESY' '3D 1H-13C NOESY' 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 Lsr2C _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 66 1 SER H H 8.627 . 1 2 66 1 SER HA H 4.487 . 1 3 66 1 SER HB2 H 3.896 . 2 4 66 1 SER CA C 58.297 . 1 5 66 1 SER CB C 63.901 . 1 6 66 1 SER N N 119.660 . 1 7 67 2 GLY H H 8.580 . 1 8 67 2 GLY HA2 H 4.086 . 2 9 67 2 GLY C C 175.272 . 1 10 67 2 GLY CA C 45.295 . 1 11 67 2 GLY N N 111.865 . 1 12 68 3 SER HA H 4.487 . 1 13 68 3 SER HB2 H 3.897 . 2 14 68 3 SER CA C 58.694 . 1 15 68 3 SER CB C 63.936 . 1 16 69 4 GLY HA2 H 3.959 . 2 17 69 4 GLY CA C 45.299 . 1 18 70 5 ARG H H 8.307 . 1 19 70 5 ARG HA H 4.319 . 1 20 70 5 ARG HB2 H 1.761 . 2 21 70 5 ARG HB3 H 1.884 . 2 22 70 5 ARG HD2 H 3.191 . 2 23 70 5 ARG HG2 H 1.643 . 2 24 70 5 ARG CA C 56.477 . 1 25 70 5 ARG CB C 30.819 . 1 26 70 5 ARG CD C 43.287 . 1 27 70 5 ARG CG C 26.950 . 1 28 71 6 GLY H H 8.533 . 1 29 71 6 GLY HA2 H 3.961 . 2 30 71 6 GLY C C 177.070 . 1 31 71 6 GLY CA C 45.361 . 1 32 71 6 GLY N N 110.645 . 1 33 72 7 ARG H H 8.356 . 1 34 72 7 ARG HA H 4.371 . 1 35 72 7 ARG HB2 H 1.769 . 2 36 72 7 ARG HB3 H 1.870 . 2 37 72 7 ARG HD2 H 3.190 . 2 38 72 7 ARG HG2 H 1.644 . 2 39 72 7 ARG C C 174.366 . 1 40 72 7 ARG CA C 56.773 . 1 41 72 7 ARG CB C 30.845 . 1 42 72 7 ARG CD C 43.321 . 1 43 72 7 ARG CG C 26.821 . 1 44 72 7 ARG N N 121.500 . 1 45 73 8 GLY H H 8.643 . 1 46 73 8 GLY HA2 H 3.959 . 2 47 73 8 GLY C C 176.939 . 1 48 73 8 GLY CA C 45.155 . 1 49 73 8 GLY N N 111.405 . 1 50 74 9 ALA H H 8.142 . 1 51 74 9 ALA HA H 4.315 . 1 52 74 9 ALA HB H 1.372 . 1 53 74 9 ALA C C 173.989 . 1 54 74 9 ALA CA C 52.792 . 1 55 74 9 ALA CB C 19.301 . 1 56 74 9 ALA N N 124.752 . 1 57 75 10 ILE H H 8.108 . 1 58 75 10 ILE HA H 4.167 . 1 59 75 10 ILE HB H 1.852 . 1 60 75 10 ILE HD1 H 0.808 . 1 61 75 10 ILE HG12 H 1.183 . 1 62 75 10 ILE HG13 H 1.483 . 1 63 75 10 ILE HG2 H 0.888 . 1 64 75 10 ILE C C 178.094 . 1 65 75 10 ILE CA C 61.304 . 1 66 75 10 ILE CB C 38.786 . 1 67 75 10 ILE CD1 C 13.275 . 1 68 75 10 ILE CG1 C 27.278 . 1 69 75 10 ILE CG2 C 17.683 . 1 70 75 10 ILE N N 120.225 . 1 71 76 11 ASP H H 8.302 . 1 72 76 11 ASP HA H 4.611 . 1 73 76 11 ASP HB2 H 2.744 . 2 74 76 11 ASP HB3 H 2.819 . 2 75 76 11 ASP C C 176.166 . 1 76 76 11 ASP CA C 54.356 . 1 77 76 11 ASP CB C 41.396 . 1 78 76 11 ASP N N 125.008 . 1 79 77 12 ARG H H 8.412 . 1 80 77 12 ARG HA H 4.145 . 1 81 77 12 ARG HB2 H 1.890 . 2 82 77 12 ARG HD2 H 3.232 . 2 83 77 12 ARG HE H 7.442 . 1 84 77 12 ARG HG2 H 1.644 . 2 85 77 12 ARG HG3 H 1.726 . 2 86 77 12 ARG C C 177.056 . 1 87 77 12 ARG CA C 58.829 . 1 88 77 12 ARG CB C 30.295 . 1 89 77 12 ARG CD C 43.304 . 1 90 77 12 ARG CG C 27.249 . 1 91 77 12 ARG N N 121.965 . 1 92 77 12 ARG NE N 124.752 . 1 93 78 13 GLU H H 8.425 . 1 94 78 13 GLU HA H 4.195 . 1 95 78 13 GLU HB2 H 2.112 . 2 96 78 13 GLU HG2 H 2.329 . 2 97 78 13 GLU C C 178.097 . 1 98 78 13 GLU CA C 58.302 . 1 99 78 13 GLU CB C 29.306 . 1 100 78 13 GLU CG C 36.800 . 1 101 78 13 GLU N N 121.678 . 1 102 79 14 GLN H H 8.505 . 1 103 79 14 GLN HA H 4.257 . 1 104 79 14 GLN HB2 H 2.115 . 2 105 79 14 GLN HE21 H 7.582 . 2 106 79 14 GLN HE22 H 6.959 . 2 107 79 14 GLN HG2 H 2.359 . 2 108 79 14 GLN HG3 H 2.481 . 2 109 79 14 GLN C C 178.455 . 1 110 79 14 GLN CA C 57.320 . 1 111 79 14 GLN CB C 28.806 . 1 112 79 14 GLN CG C 34.282 . 1 113 79 14 GLN N N 121.605 . 1 114 79 14 GLN NE2 N 112.877 . 1 115 80 15 SER H H 8.310 . 1 116 80 15 SER HA H 3.989 . 1 117 80 15 SER HB2 H 3.878 . 2 118 80 15 SER HB3 H 3.978 . 2 119 80 15 SER C C 177.520 . 1 120 80 15 SER CA C 61.513 . 1 121 80 15 SER CB C 63.027 . 1 122 80 15 SER N N 115.925 . 1 123 81 16 ALA H H 8.063 . 1 124 81 16 ALA HA H 4.119 . 1 125 81 16 ALA HB H 1.516 . 1 126 81 16 ALA C C 175.776 . 1 127 81 16 ALA CA C 55.270 . 1 128 81 16 ALA CB C 18.003 . 1 129 81 16 ALA N N 124.407 . 1 130 82 17 ALA H H 7.867 . 1 131 82 17 ALA HA H 4.216 . 1 132 82 17 ALA HB H 1.516 . 1 133 82 17 ALA C C 180.238 . 1 134 82 17 ALA CA C 55.183 . 1 135 82 17 ALA CB C 18.030 . 1 136 82 17 ALA N N 122.204 . 1 137 83 18 ILE H H 8.041 . 1 138 83 18 ILE HA H 3.196 . 1 139 83 18 ILE HB H 1.538 . 1 140 83 18 ILE HD1 H 0.507 . 1 141 83 18 ILE HG12 H -0.678 . 1 142 83 18 ILE HG13 H 1.153 . 1 143 83 18 ILE HG2 H 0.582 . 1 144 83 18 ILE C C 181.176 . 1 145 83 18 ILE CA C 65.574 . 1 146 83 18 ILE CB C 37.212 . 1 147 83 18 ILE CD1 C 13.806 . 1 148 83 18 ILE CG1 C 27.289 . 1 149 83 18 ILE CG2 C 17.788 . 1 150 83 18 ILE N N 120.823 . 1 151 84 19 ARG H H 8.183 . 1 152 84 19 ARG HA H 3.816 . 1 153 84 19 ARG HB2 H 1.834 . 2 154 84 19 ARG HB3 H 1.901 . 2 155 84 19 ARG HD2 H 3.141 . 2 156 84 19 ARG HD3 H 3.291 . 2 157 84 19 ARG HE H 7.264 . 1 158 84 19 ARG HG2 H 1.413 . 2 159 84 19 ARG C C 177.942 . 1 160 84 19 ARG CA C 60.937 . 1 161 84 19 ARG CB C 29.953 . 1 162 84 19 ARG CD C 43.282 . 1 163 84 19 ARG CG C 29.792 . 1 164 84 19 ARG N N 120.433 . 1 165 84 19 ARG NE N 125.377 . 1 166 85 20 GLU H H 8.059 . 1 167 85 20 GLU HA H 4.184 . 1 168 85 20 GLU HB2 H 2.127 . 2 169 85 20 GLU HG2 H 2.386 . 2 170 85 20 GLU C C 178.787 . 1 171 85 20 GLU CA C 59.285 . 1 172 85 20 GLU CB C 29.295 . 1 173 85 20 GLU CG C 35.771 . 1 174 85 20 GLU N N 120.115 . 1 175 86 21 TRP H H 8.139 . 1 176 86 21 TRP HA H 4.053 . 1 177 86 21 TRP HB2 H 3.547 . 2 178 86 21 TRP HB3 H 3.658 . 2 179 86 21 TRP HD1 H 7.411 . 1 180 86 21 TRP HE1 H 10.244 . 1 181 86 21 TRP HE3 H 7.479 . 1 182 86 21 TRP HH2 H 7.024 . 1 183 86 21 TRP HZ2 H 7.351 . 1 184 86 21 TRP HZ3 H 6.822 . 1 185 86 21 TRP C C 178.354 . 1 186 86 21 TRP CA C 62.187 . 1 187 86 21 TRP CB C 29.068 . 1 188 86 21 TRP CD1 C 127.325 . 1 189 86 21 TRP CE3 C 120.072 . 1 190 86 21 TRP CH2 C 124.324 . 1 191 86 21 TRP CZ2 C 114.820 . 1 192 86 21 TRP N N 121.545 . 1 193 86 21 TRP NE1 N 131.856 . 1 194 87 22 ALA H H 9.302 . 1 195 87 22 ALA HA H 3.538 . 1 196 87 22 ALA HB H 1.597 . 1 197 87 22 ALA C C 179.333 . 1 198 87 22 ALA CA C 55.952 . 1 199 87 22 ALA CB C 18.306 . 1 200 87 22 ALA N N 123.676 . 1 201 88 23 ARG H H 7.935 . 1 202 88 23 ARG HA H 4.120 . 1 203 88 23 ARG HB2 H 1.972 . 2 204 88 23 ARG HD2 H 3.231 . 2 205 88 23 ARG HG2 H 1.786 . 2 206 88 23 ARG HG3 H 1.712 . 2 207 88 23 ARG C C 179.494 . 1 208 88 23 ARG CA C 59.302 . 1 209 88 23 ARG CB C 30.261 . 1 210 88 23 ARG CD C 43.308 . 1 211 88 23 ARG CG C 27.543 . 1 212 88 23 ARG N N 118.266 . 1 213 89 24 ARG H H 7.695 . 1 214 89 24 ARG HA H 4.164 . 1 215 89 24 ARG HB2 H 1.777 . 2 216 89 24 ARG HD2 H 3.191 . 2 217 89 24 ARG HG2 H 1.629 . 2 218 89 24 ARG HG3 H 1.735 . 2 219 89 24 ARG C C 179.663 . 1 220 89 24 ARG CA C 57.796 . 1 221 89 24 ARG CB C 30.514 . 1 222 89 24 ARG CD C 43.392 . 1 223 89 24 ARG CG C 27.699 . 1 224 89 24 ARG N N 118.954 . 1 225 90 25 ASN H H 7.333 . 1 226 90 25 ASN HA H 4.560 . 1 227 90 25 ASN HB2 H 1.287 . 2 228 90 25 ASN HB3 H 2.392 . 2 229 90 25 ASN HD21 H 6.580 . 2 230 90 25 ASN HD22 H 6.552 . 2 231 90 25 ASN C C 176.824 . 1 232 90 25 ASN CA C 53.572 . 1 233 90 25 ASN CB C 39.289 . 1 234 90 25 ASN N N 116.762 . 1 235 90 25 ASN ND2 N 116.314 . 1 236 91 26 GLY H H 7.556 . 1 237 91 26 GLY HA2 H 3.680 . 2 238 91 26 GLY HA3 H 3.801 . 2 239 91 26 GLY C C 174.110 . 1 240 91 26 GLY CA C 46.551 . 1 241 91 26 GLY N N 106.774 . 1 242 92 27 HIS H H 8.062 . 1 243 92 27 HIS HA H 4.674 . 1 244 92 27 HIS HB2 H 2.762 . 2 245 92 27 HIS HB3 H 2.935 . 2 246 92 27 HIS HD2 H 6.519 . 1 247 92 27 HIS HE1 H 8.117 . 1 248 92 27 HIS C C 174.173 . 1 249 92 27 HIS CA C 54.813 . 1 250 92 27 HIS CB C 31.188 . 1 251 92 27 HIS N N 119.221 . 1 252 93 28 ASN H H 8.870 . 1 253 93 28 ASN HA H 4.649 . 1 254 93 28 ASN HB2 H 2.718 . 2 255 93 28 ASN HB3 H 2.803 . 2 256 93 28 ASN HD21 H 7.609 . 2 257 93 28 ASN HD22 H 6.884 . 2 258 93 28 ASN C C 174.276 . 1 259 93 28 ASN CA C 53.541 . 1 260 93 28 ASN CB C 38.311 . 1 261 93 28 ASN N N 123.292 . 1 262 93 28 ASN ND2 N 113.346 . 1 263 94 29 VAL H H 8.101 . 1 264 94 29 VAL HA H 4.348 . 1 265 94 29 VAL HB H 2.140 . 1 266 94 29 VAL HG1 H 0.951 . 2 267 94 29 VAL HG2 H 1.020 . 2 268 94 29 VAL C C 174.698 . 1 269 94 29 VAL CA C 60.800 . 1 270 94 29 VAL CB C 34.087 . 1 271 94 29 VAL CG1 C 21.290 . 1 272 94 29 VAL CG2 C 22.286 . 1 273 94 29 VAL N N 122.537 . 1 274 95 30 SER H H 8.720 . 1 275 95 30 SER HA H 4.531 . 1 276 95 30 SER HB2 H 3.921 . 2 277 95 30 SER HB3 H 4.105 . 2 278 95 30 SER C C 175.319 . 1 279 95 30 SER CA C 58.218 . 1 280 95 30 SER CB C 63.917 . 1 281 95 30 SER N N 121.766 . 1 282 96 31 THR H H 8.543 . 1 283 96 31 THR HA H 4.075 . 1 284 96 31 THR HB H 4.264 . 1 285 96 31 THR HG2 H 1.278 . 1 286 96 31 THR C C 175.676 . 1 287 96 31 THR CA C 64.303 . 1 288 96 31 THR CB C 69.146 . 1 289 96 31 THR CG2 C 22.314 . 1 290 96 31 THR N N 117.221 . 1 291 97 32 ARG H H 8.107 . 1 292 97 32 ARG HA H 4.452 . 1 293 97 32 ARG HB2 H 1.696 . 2 294 97 32 ARG HB3 H 1.887 . 2 295 97 32 ARG HD2 H 3.183 . 2 296 97 32 ARG HG2 H 1.570 . 2 297 97 32 ARG C C 174.797 . 1 298 97 32 ARG CA C 55.329 . 1 299 97 32 ARG CB C 31.777 . 1 300 97 32 ARG CD C 43.228 . 1 301 97 32 ARG CG C 27.191 . 1 302 97 32 ARG N N 119.697 . 1 303 98 33 GLY H H 8.183 . 1 304 98 33 GLY HA2 H 3.990 . 2 305 98 33 GLY C C 176.330 . 1 306 98 33 GLY CA C 44.544 . 1 307 98 33 GLY N N 109.701 . 1 308 99 34 ARG H H 8.342 . 1 309 99 34 ARG HA H 4.225 . 1 310 99 34 ARG HB2 H 1.730 . 2 311 99 34 ARG HD2 H 3.185 . 2 312 99 34 ARG HG2 H 1.590 . 2 313 99 34 ARG C C 173.761 . 1 314 99 34 ARG CA C 56.306 . 1 315 99 34 ARG CB C 30.783 . 1 316 99 34 ARG CD C 43.298 . 1 317 99 34 ARG CG C 27.244 . 1 318 99 34 ARG N N 121.140 . 1 319 100 35 ILE H H 8.802 . 1 320 100 35 ILE HA H 4.193 . 1 321 100 35 ILE HB H 1.714 . 1 322 100 35 ILE HD1 H 0.834 . 1 323 100 35 ILE HG12 H 0.844 . 1 324 100 35 ILE HG13 H 1.764 . 1 325 100 35 ILE HG2 H 0.934 . 1 326 100 35 ILE C C 176.827 . 1 327 100 35 ILE CA C 59.284 . 1 328 100 35 ILE CB C 39.074 . 1 329 100 35 ILE CD1 C 14.062 . 1 330 100 35 ILE CG1 C 28.275 . 1 331 100 35 ILE CG2 C 17.799 . 1 332 100 35 ILE N N 128.392 . 1 333 101 36 PRO HA H 4.416 . 1 334 101 36 PRO HB2 H 2.099 . 2 335 101 36 PRO HB3 H 2.529 . 2 336 101 36 PRO HD2 H 3.422 . 2 337 101 36 PRO HD3 H 4.200 . 2 338 101 36 PRO HG2 H 2.105 . 2 339 101 36 PRO HG3 H 2.226 . 2 340 101 36 PRO CA C 63.306 . 1 341 101 36 PRO CB C 33.104 . 1 342 101 36 PRO CD C 51.795 . 1 343 101 36 PRO CG C 28.144 . 1 344 102 37 ALA H H 8.796 . 1 345 102 37 ALA HA H 3.949 . 1 346 102 37 ALA HB H 1.486 . 1 347 102 37 ALA C C 177.720 . 1 348 102 37 ALA CA C 55.629 . 1 349 102 37 ALA CB C 18.765 . 1 350 102 37 ALA N N 126.714 . 1 351 103 38 ASP H H 8.792 . 1 352 103 38 ASP HA H 4.399 . 1 353 103 38 ASP HB2 H 2.642 . 2 354 103 38 ASP HB3 H 2.751 . 2 355 103 38 ASP C C 178.910 . 1 356 103 38 ASP CA C 56.306 . 1 357 103 38 ASP CB C 39.294 . 1 358 103 38 ASP N N 114.538 . 1 359 104 39 VAL H H 7.377 . 1 360 104 39 VAL HA H 3.549 . 1 361 104 39 VAL HB H 2.112 . 1 362 104 39 VAL HG1 H 0.774 . 2 363 104 39 VAL HG2 H 0.891 . 2 364 104 39 VAL C C 179.066 . 1 365 104 39 VAL CA C 65.947 . 1 366 104 39 VAL CB C 31.299 . 1 367 104 39 VAL CG1 C 21.787 . 1 368 104 39 VAL CG2 C 22.794 . 1 369 104 39 VAL N N 123.563 . 1 370 105 40 ILE H H 7.402 . 1 371 105 40 ILE HA H 3.365 . 1 372 105 40 ILE HB H 1.937 . 1 373 105 40 ILE HD1 H 0.794 . 1 374 105 40 ILE HG12 H 0.861 . 1 375 105 40 ILE HG13 H 1.564 . 1 376 105 40 ILE HG2 H 0.823 . 1 377 105 40 ILE C C 176.851 . 1 378 105 40 ILE CA C 65.554 . 1 379 105 40 ILE CB C 37.595 . 1 380 105 40 ILE CD1 C 13.283 . 1 381 105 40 ILE CG1 C 28.820 . 1 382 105 40 ILE CG2 C 17.778 . 1 383 105 40 ILE N N 121.781 . 1 384 106 41 ASP H H 8.334 . 1 385 106 41 ASP HA H 4.429 . 1 386 106 41 ASP HB2 H 2.679 . 2 387 106 41 ASP C C 178.084 . 1 388 106 41 ASP CA C 57.299 . 1 389 106 41 ASP CB C 40.289 . 1 390 106 41 ASP N N 119.666 . 1 391 107 42 ALA H H 7.747 . 1 392 107 42 ALA HA H 4.179 . 1 393 107 42 ALA HB H 1.656 . 1 394 107 42 ALA C C 179.008 . 1 395 107 42 ALA CA C 55.150 . 1 396 107 42 ALA CB C 17.964 . 1 397 107 42 ALA N N 124.685 . 1 398 108 43 TYR H H 8.309 . 1 399 108 43 TYR HA H 2.274 . 1 400 108 43 TYR HB2 H 2.398 . 2 401 108 43 TYR HB3 H 2.723 . 2 402 108 43 TYR HD1 H 6.165 . 3 403 108 43 TYR HD2 H 6.165 . 3 404 108 43 TYR HE1 H 6.455 . 3 405 108 43 TYR HE2 H 6.455 . 3 406 108 43 TYR C C 179.619 . 1 407 108 43 TYR CA C 60.491 . 1 408 108 43 TYR CB C 37.802 . 1 409 108 43 TYR CD1 C 132.576 . 3 410 108 43 TYR CD2 C 132.576 . 3 411 108 43 TYR CE1 C 117.571 . 3 412 108 43 TYR CE2 C 117.571 . 3 413 108 43 TYR N N 122.873 . 1 414 109 44 HIS H H 8.264 . 1 415 109 44 HIS HA H 3.993 . 1 416 109 44 HIS HB2 H 3.208 . 2 417 109 44 HIS HD2 H 7.189 . 1 418 109 44 HIS HE1 H 8.268 . 1 419 109 44 HIS C C 178.157 . 1 420 109 44 HIS CA C 58.552 . 1 421 109 44 HIS CB C 28.792 . 1 422 109 44 HIS N N 119.813 . 1 423 110 45 ALA H H 7.991 . 1 424 110 45 ALA HA H 4.067 . 1 425 110 45 ALA HB H 1.469 . 1 426 110 45 ALA C C 177.055 . 1 427 110 45 ALA CA C 54.627 . 1 428 110 45 ALA CB C 18.025 . 1 429 110 45 ALA N N 121.975 . 1 430 111 46 ALA H H 7.597 . 1 431 111 46 ALA HA H 4.255 . 1 432 111 46 ALA HB H 1.468 . 1 433 111 46 ALA C C 179.303 . 1 434 111 46 ALA CA C 53.892 . 1 435 111 46 ALA CB C 19.347 . 1 436 111 46 ALA N N 120.225 . 1 437 112 47 THR H H 7.466 . 1 438 112 47 THR HA H 4.078 . 1 439 112 47 THR HB H 3.982 . 1 440 112 47 THR HG2 H 0.749 . 1 441 112 47 THR C C 179.380 . 1 442 112 47 THR CA C 62.742 . 1 443 112 47 THR CB C 69.694 . 1 444 112 47 THR CG2 C 20.800 . 1 445 112 47 THR N N 110.333 . 1 446 113 48 LEU H H 7.517 . 1 447 113 48 LEU HA H 4.159 . 1 448 113 48 LEU HB2 H 1.474 . 2 449 113 48 LEU HB3 H 1.617 . 2 450 113 48 LEU HD1 H 0.793 . 2 451 113 48 LEU HD2 H 0.766 . 2 452 113 48 LEU HG H 1.542 . 1 453 113 48 LEU C C 175.155 . 1 454 113 48 LEU CA C 56.051 . 1 455 113 48 LEU CB C 42.291 . 1 456 113 48 LEU CD1 C 24.783 . 1 457 113 48 LEU CD2 C 23.767 . 1 458 113 48 LEU CG C 26.838 . 1 459 113 48 LEU N N 123.658 . 1 460 114 49 GLU H H 7.994 . 1 461 114 49 GLU HA H 4.138 . 1 462 114 49 GLU HB2 H 1.899 . 2 463 114 49 GLU HG2 H 2.140 . 2 464 114 49 GLU HG3 H 2.212 . 2 465 114 49 GLU C C 177.460 . 1 466 114 49 GLU CA C 56.783 . 1 467 114 49 GLU CB C 30.293 . 1 468 114 49 GLU CG C 36.279 . 1 469 114 49 GLU N N 120.846 . 1 470 115 50 HIS H H 8.233 . 1 471 115 50 HIS HA H 4.582 . 1 472 115 50 HIS HB2 H 3.049 . 2 473 115 50 HIS HB3 H 3.139 . 2 474 115 50 HIS HD2 H 7.094 . 1 475 115 50 HIS C C 176.503 . 1 476 115 50 HIS CA C 55.783 . 1 477 115 50 HIS CB C 29.790 . 1 478 115 50 HIS N N 119.726 . 1 479 116 51 HIS H H 8.395 . 1 480 116 51 HIS HA H 4.631 . 1 481 116 51 HIS HB2 H 3.172 . 2 482 116 51 HIS HD2 H 7.114 . 1 483 116 51 HIS C C 174.794 . 1 484 116 51 HIS CA C 55.801 . 1 485 116 51 HIS CB C 29.802 . 1 486 116 51 HIS N N 120.283 . 1 487 117 52 HIS H H 8.277 . 1 488 117 52 HIS HA H 4.793 . 1 489 117 52 HIS HB2 H 3.145 . 2 490 117 52 HIS HB3 H 3.286 . 2 491 117 52 HIS C C 173.834 . 1 492 117 52 HIS CA C 57.341 . 1 493 117 52 HIS CB C 29.793 . 1 494 117 52 HIS N N 126.158 . 1 stop_ save_