data_17777 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the N-terminal domain of the Shigella type III secretion protein MxiG ; _BMRB_accession_number 17777 _BMRB_flat_file_name bmr17777.str _Entry_type original _Submission_date 2011-07-11 _Accession_date 2011-07-11 _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 McDowell Melanie A. . 2 Johnson S. . . 3 Deane J. E. . 4 Mcdonnell J. M. . 5 Lea S. M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 482 "13C chemical shifts" 148 "15N chemical shifts" 98 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-02-15 update BMRB 'update entry citation' 2011-08-03 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural and functional studies on the N-terminal domain of the Shigella type III secretion protein MxiG.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21733840 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 McDowell Melanie A. . 2 Johnson Steven . . 3 Deane Janet E. . 4 Cheung Martin . . 5 Roehrich 'A. Dorothea' . . 6 Blocker Ariel J. . 7 McDonnell James M. . 8 Lea Susan M. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 286 _Journal_issue 35 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 30606 _Page_last 30614 _Year 2011 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Solution structure of the N-terminal domain of the Shigella type III secretion protein MxiG' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'PROTEIN MXIG' $PROTEIN_MXIG stop_ _System_molecular_weight 12147.3457 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PROTEIN_MXIG _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PROTEIN_MXIG _Molecular_mass 12147.3457 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 107 _Mol_residue_sequence ; NSNLAPFRLLVKLTNGVGDE FPLYYGNNLIVLGRTIETLE FGNDNFPENIIPVTDSKSDG IIYLTISKDNICQFSDEKGE QIDINSQFNSFEYDGISFHL KNMREDK ; loop_ _Residue_seq_code _Residue_label 1 ASN 2 SER 3 ASN 4 LEU 5 ALA 6 PRO 7 PHE 8 ARG 9 LEU 10 LEU 11 VAL 12 LYS 13 LEU 14 THR 15 ASN 16 GLY 17 VAL 18 GLY 19 ASP 20 GLU 21 PHE 22 PRO 23 LEU 24 TYR 25 TYR 26 GLY 27 ASN 28 ASN 29 LEU 30 ILE 31 VAL 32 LEU 33 GLY 34 ARG 35 THR 36 ILE 37 GLU 38 THR 39 LEU 40 GLU 41 PHE 42 GLY 43 ASN 44 ASP 45 ASN 46 PHE 47 PRO 48 GLU 49 ASN 50 ILE 51 ILE 52 PRO 53 VAL 54 THR 55 ASP 56 SER 57 LYS 58 SER 59 ASP 60 GLY 61 ILE 62 ILE 63 TYR 64 LEU 65 THR 66 ILE 67 SER 68 LYS 69 ASP 70 ASN 71 ILE 72 CYS 73 GLN 74 PHE 75 SER 76 ASP 77 GLU 78 LYS 79 GLY 80 GLU 81 GLN 82 ILE 83 ASP 84 ILE 85 ASN 86 SER 87 GLN 88 PHE 89 ASN 90 SER 91 PHE 92 GLU 93 TYR 94 ASP 95 GLY 96 ILE 97 SER 98 PHE 99 HIS 100 LEU 101 LYS 102 ASN 103 MET 104 ARG 105 GLU 106 ASP 107 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-16 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 2XXS "Solution Structure Of The N-Terminal Domain Of The Shigella Type Iii Secretion Protein Mxig" 100.00 107 100.00 100.00 1.37e-69 PDB 4A4Y "Structure Of The Cytosolic Domain Of The Shigella T3ss Component Mxig" 100.00 146 100.00 100.00 2.45e-70 DBJ BAA09145 "ORF5 [Shigella sonnei]" 100.00 371 100.00 100.00 9.56e-68 EMBL CAA88822 "MxiG [Shigella flexneri 5a str. M90T]" 100.00 371 100.00 100.00 9.56e-68 EMBL CAC05811 "MxiG, component of the Mxi-Spa secretion machinery, contains one transmembrane segment [Shigella flexneri 5a str. M90T]" 100.00 371 100.00 100.00 9.56e-68 EMBL CEP57538 "MxiG [Shigella flexneri 2a]" 100.00 371 100.00 100.00 9.56e-68 EMBL CSE38521 "MxiG [Shigella sonnei]" 100.00 371 100.00 100.00 9.56e-68 EMBL CSE65222 "MxiG [Shigella sonnei]" 100.00 371 100.00 100.00 9.56e-68 GB AAK18455 "Type III secretion protein [Shigella flexneri 5a str. M90T]" 100.00 371 100.00 100.00 9.56e-68 GB AAL72329 "MxiG, component of the Mxi-Spa secretion machinery, contains one transmembrane segment [Shigella flexneri 2a str. 301]" 100.00 371 100.00 100.00 9.56e-68 GB AAZ91118 "MxiG [Shigella sonnei Ss046]" 100.00 371 100.00 100.00 9.56e-68 GB ABB64687 "MxiG [Shigella dysenteriae Sd197]" 100.00 371 100.00 100.00 1.21e-67 GB ADA76874 "MxiG, component of the Mxi-Spa secretion machinery, contains one transmembrane segment [Shigella flexneri 2002017]" 100.00 371 100.00 100.00 9.56e-68 REF NP_085299 "Type III secretion protein [Shigella flexneri 5a str. M90T]" 100.00 371 100.00 100.00 9.56e-68 REF NP_858269 "MxiG protein [Shigella flexneri 2a str. 301]" 100.00 371 100.00 100.00 9.56e-68 REF WP_001287353 "MULTISPECIES: protein MxiG [Shigella]" 100.00 371 100.00 100.00 9.56e-68 REF WP_001287354 "hypothetical protein [Shigella sonnei]" 100.00 136 100.00 100.00 1.14e-69 REF WP_001287355 "protein mxiG [Shigella dysenteriae]" 100.00 371 100.00 100.00 1.21e-67 SP P0A221 "RecName: Full=Protein MxiG" 100.00 371 100.00 100.00 9.56e-68 SP P0A222 "RecName: Full=Protein MxiG [Shigella sonnei]" 100.00 371 100.00 100.00 9.56e-68 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Variant _ATCC_number $PROTEIN_MXIG 'Shigella flexneri' 623 Bacteria . Shigella flexneri 301 'serotype 2a' 700930 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name $PROTEIN_MXIG 'recombinant technology' 'Escherichia coli' Escherichia coli BL21(DE3) DE3 n/a pET14b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '5.4mM MxiG N-terminal domain' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PROTEIN_MXIG 5.4 mM '[U-13C; U-15N]' NaPi 25 mM 'natural abundance' DTT 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_AutoDep _Saveframe_category software _Name AutoDep _Version 4.3 loop_ _Vendor _Address _Electronic_address PDBE . . stop_ loop_ _Task collection stop_ _Details . save_ save_DYANA-1.5 _Saveframe_category software _Name DYANA-1.5 _Version any loop_ _Vendor _Address _Electronic_address 'P. Guntert, C. Mumenthaler, K. Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details 'REFINEMENT DETAILS CAN BE FOUND' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_Bruker_Avance-500 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_HN(CO)CA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_1 save_ save_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_CBCANH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label $sample_1 save_ save_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_CC(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CC(CO)NH _Sample_label $sample_1 save_ save_H(CCCO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCCO)NH _Sample_label $sample_1 save_ save_15N-NOESY-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-NOESY-HSQC _Sample_label $sample_1 save_ save_13C-NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name 13C-NOESY _Sample_label $sample_1 save_ save_CLEANEX-PM_9 _Saveframe_category NMR_applied_experiment _Experiment_name CLEANEX-PM _Sample_label $sample_1 save_ save_long-range_HNCO_10 _Saveframe_category NMR_applied_experiment _Experiment_name 'long-range HNCO' _Sample_label $sample_1 save_ save_HNHA_11 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details 'pH [6.8], temp [298], pressure [0.0], ionStrength [0.0]' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 25 . mM pH 6.800 . pH pressure 1 . atm temperature 298.000 . 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_ _Experiment_label HN(CO)CA CBCA(CO)NH CBCANH HNCO CC(CO)NH H(CCCO)NH 15N-NOESY-HSQC 13C-NOESY CLEANEX-PM 'long-range HNCO' HNHA 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 'PROTEIN MXIG' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 3 3 ASN HA H 5.053 0.007 1 2 3 3 ASN HB2 H 3.126 0.000 2 3 3 3 ASN HD21 H 7.677 0.000 2 4 3 3 ASN HD22 H 6.981 0.000 2 5 3 3 ASN CA C 50.262 0.000 1 6 3 3 ASN CB C 36.748 0.000 1 7 3 3 ASN ND2 N 113.393 0.044 1 8 4 4 LEU H H 8.085 0.004 1 9 4 4 LEU HA H 3.701 0.006 1 10 4 4 LEU HB2 H 1.389 0.000 2 11 4 4 LEU HB3 H 1.389 0.000 2 12 4 4 LEU HG H 1.408 0.009 1 13 4 4 LEU HD1 H 0.667 0.003 . 14 4 4 LEU HD2 H 0.497 0.013 . 15 4 4 LEU CA C 53.322 0.033 1 16 4 4 LEU CD2 C 22.008 0.016 2 17 4 4 LEU N N 123.725 0.000 1 18 5 5 ALA H H 8.586 0.001 1 19 5 5 ALA HA H 4.143 0.003 1 20 5 5 ALA HB H 0.448 0.007 . 21 5 5 ALA CA C 46.141 0.056 1 22 5 5 ALA CB C 15.938 0.135 1 23 5 5 ALA N N 127.445 0.029 1 24 6 6 PRO HA H 4.528 0.007 1 25 6 6 PRO HD2 H 3.082 0.002 2 26 6 6 PRO HD3 H 3.575 0.003 2 27 6 6 PRO CA C 60.348 0.000 1 28 6 6 PRO CD C 47.726 0.041 1 29 7 7 PHE H H 7.843 0.009 1 30 7 7 PHE HA H 5.463 0.012 1 31 7 7 PHE HB2 H 2.863 0.009 2 32 7 7 PHE HB3 H 1.986 0.010 2 33 7 7 PHE HD1 H 6.689 0.020 . 34 7 7 PHE HD2 H 6.689 0.020 . 35 7 7 PHE HE1 H 6.689 0.020 . 36 7 7 PHE HE2 H 6.689 0.020 . 37 7 7 PHE CA C 53.413 0.041 1 38 7 7 PHE CB C 43.192 0.041 1 39 7 7 PHE N N 117.027 0.009 1 40 8 8 ARG H H 8.935 0.001 1 41 8 8 ARG HA H 4.659 0.017 1 42 8 8 ARG CA C 52.104 0.000 1 43 8 8 ARG N N 119.699 0.042 1 44 9 9 LEU H H 8.858 0.006 1 45 9 9 LEU HA H 5.188 0.019 1 46 9 9 LEU HB2 H 2.064 0.001 2 47 9 9 LEU HB3 H 1.269 0.002 2 48 9 9 LEU HD1 H 0.887 0.000 . 49 9 9 LEU HD2 H 1.066 0.012 . 50 9 9 LEU CA C 50.452 0.078 1 51 9 9 LEU CB C 43.512 0.068 1 52 9 9 LEU CD1 C 24.798 0.127 2 53 9 9 LEU CD2 C 20.799 0.049 2 54 9 9 LEU N N 122.094 0.035 1 55 10 10 LEU H H 9.508 0.014 1 56 10 10 LEU HA H 5.146 0.010 1 57 10 10 LEU HB2 H 1.881 0.004 2 58 10 10 LEU HB3 H 1.491 0.009 2 59 10 10 LEU HD1 H 0.762 0.018 . 60 10 10 LEU HD2 H 0.726 0.036 . 61 10 10 LEU CA C 51.775 0.000 1 62 10 10 LEU CB C 41.123 0.049 1 63 10 10 LEU CD1 C 22.606 0.000 2 64 10 10 LEU N N 130.118 0.005 1 65 11 11 VAL H H 8.953 0.015 1 66 11 11 VAL HA H 4.456 0.002 1 67 11 11 VAL HB H 2.089 0.000 1 68 11 11 VAL HG1 H 0.573 0.012 . 69 11 11 VAL HG2 H 0.903 0.129 . 70 11 11 VAL CA C 58.528 0.118 1 71 11 11 VAL CB C 31.364 0.000 1 72 11 11 VAL CG1 C 18.713 0.027 2 73 11 11 VAL CG2 C 18.564 0.108 2 74 11 11 VAL N N 126.440 0.022 1 75 12 12 LYS H H 8.813 0.005 1 76 12 12 LYS HA H 4.786 0.002 1 77 12 12 LYS HB2 H 1.725 0.019 2 78 12 12 LYS HB3 H 1.488 0.012 2 79 12 12 LYS HG2 H 1.220 0.005 2 80 12 12 LYS HG3 H 1.155 0.008 2 81 12 12 LYS CA C 52.444 0.033 1 82 12 12 LYS CB C 31.606 0.127 1 83 12 12 LYS CG C 21.725 0.098 1 84 12 12 LYS N N 127.565 0.036 1 85 13 13 LEU H H 8.520 0.003 1 86 13 13 LEU HA H 4.475 0.011 1 87 13 13 LEU HB2 H 1.878 0.000 2 88 13 13 LEU HB3 H 1.656 0.000 2 89 13 13 LEU HG H 1.661 0.010 1 90 13 13 LEU HD1 H 0.862 0.005 . 91 13 13 LEU HD2 H 0.713 0.156 . 92 13 13 LEU CA C 52.032 0.058 1 93 13 13 LEU CD1 C 22.702 0.069 2 94 13 13 LEU CD2 C 20.912 0.019 2 95 13 13 LEU N N 125.999 0.017 1 96 14 14 THR H H 8.303 0.001 1 97 14 14 THR HA H 4.026 0.000 1 98 14 14 THR HG2 H 1.173 0.004 . 99 14 14 THR N N 113.139 0.009 1 100 15 15 ASN H H 7.933 0.010 1 101 15 15 ASN HB2 H 2.966 0.000 2 102 15 15 ASN HB3 H 2.760 0.004 2 103 15 15 ASN N N 117.465 0.023 1 104 16 16 GLY H H 7.976 0.003 1 105 16 16 GLY HA2 H 4.029 0.000 . 106 16 16 GLY HA3 H 3.709 0.000 2 107 16 16 GLY N N 107.606 0.013 1 108 17 17 VAL H H 7.710 0.007 1 109 17 17 VAL HA H 3.886 0.000 1 110 17 17 VAL HB H 2.048 0.000 1 111 17 17 VAL HG1 H 0.848 0.000 . 112 17 17 VAL HG2 H 0.848 0.000 . 113 17 17 VAL N N 120.962 0.012 1 114 18 18 GLY H H 8.208 0.000 1 115 18 18 GLY HA2 H 4.748 0.002 . 116 18 18 GLY HA3 H 3.742 0.015 2 117 18 18 GLY CA C 41.987 0.033 1 118 18 18 GLY N N 112.514 0.003 1 119 19 19 ASP H H 8.463 0.002 1 120 19 19 ASP HA H 4.754 0.000 1 121 19 19 ASP HB2 H 2.415 0.001 2 122 19 19 ASP HB3 H 2.302 0.000 2 123 19 19 ASP CB C 42.181 0.161 1 124 19 19 ASP N N 121.529 0.000 1 125 20 20 GLU H H 8.366 0.000 1 126 20 20 GLU HA H 5.460 0.012 1 127 20 20 GLU HB2 H 1.747 0.000 2 128 20 20 GLU HB3 H 1.747 0.000 2 129 20 20 GLU HG2 H 2.008 0.002 2 130 20 20 GLU CA C 51.865 0.006 1 131 20 20 GLU CB C 30.773 0.000 1 132 20 20 GLU CG C 34.858 0.048 1 133 20 20 GLU N N 121.159 0.000 1 134 21 21 PHE H H 9.133 0.008 1 135 21 21 PHE HA H 5.021 0.005 1 136 21 21 PHE HB2 H 2.593 0.011 2 137 21 21 PHE HB3 H 3.300 0.014 2 138 21 21 PHE HD1 H 7.269 0.025 . 139 21 21 PHE HD2 H 7.269 0.025 . 140 21 21 PHE HE1 H 7.269 0.025 . 141 21 21 PHE HE2 H 7.269 0.025 . 142 21 21 PHE CA C 53.016 0.000 1 143 21 21 PHE CB C 39.781 0.166 1 144 21 21 PHE CG C 129.64 0.000 1 145 21 21 PHE N N 122.105 0.032 1 146 22 22 PRO HG2 H 2.245 0.002 2 147 22 22 PRO HG3 H 2.142 0.005 2 148 22 22 PRO HD2 H 3.874 0.005 2 149 22 22 PRO HD3 H 4.087 0.006 2 150 22 22 PRO CG C 24.206 0.058 1 151 22 22 PRO CD C 48.339 0.056 1 152 23 23 LEU H H 8.098 0.000 1 153 23 23 LEU HA H 4.487 0.000 1 154 23 23 LEU HB2 H 0.932 0.022 2 155 23 23 LEU HB3 H 1.421 0.021 2 156 23 23 LEU HG H 0.438 0.011 1 157 23 23 LEU HD1 H 0.699 0.024 . 158 23 23 LEU HD2 H 0.699 0.024 . 159 23 23 LEU CA C 50.527 0.000 1 160 23 23 LEU CD1 C 21.419 0.006 2 161 23 23 LEU N N 116.156 0.000 1 162 24 24 TYR H H 8.486 0.021 1 163 24 24 TYR HA H 4.710 0.021 1 164 24 24 TYR HB2 H 2.276 0.028 2 165 24 24 TYR HB3 H 3.015 0.008 2 166 24 24 TYR HD1 H 6.854 0.002 3 167 24 24 TYR HD2 H 6.854 0.002 3 168 24 24 TYR HE1 H 6.603 0.002 3 169 24 24 TYR HE2 H 6.603 0.002 3 170 24 24 TYR CA C 54.213 0.047 1 171 24 24 TYR CE1 C 115.13 0.067 3 172 24 24 TYR N N 119.090 0.032 1 173 25 25 TYR H H 8.321 0.003 1 174 25 25 TYR HA H 4.122 0.007 1 175 25 25 TYR HB2 H 2.938 0.001 2 176 25 25 TYR HB3 H 2.790 0.009 2 177 25 25 TYR HD1 H 6.858 0.014 3 178 25 25 TYR HD2 H 6.858 0.014 3 179 25 25 TYR HE1 H 7.035 0.008 3 180 25 25 TYR HE2 H 7.035 0.008 3 181 25 25 TYR CA C 59.525 0.000 1 182 25 25 TYR CB C 35.479 0.000 1 183 25 25 TYR N N 118.605 0.048 1 184 26 26 GLY H H 8.913 0.001 1 185 26 26 GLY HA2 H 3.500 0.000 . 186 26 26 GLY HA3 H 4.359 0.000 2 187 26 26 GLY N N 110.480 0.005 1 188 27 27 ASN H H 9.018 0.006 1 189 27 27 ASN HA H 4.867 0.006 1 190 27 27 ASN HB2 H 2.745 0.006 2 191 27 27 ASN HB3 H 2.519 0.001 2 192 27 27 ASN CA C 50.765 0.108 1 193 27 27 ASN CB C 37.015 0.027 1 194 27 27 ASN N N 121.767 0.048 1 195 28 28 ASN H H 8.715 0.001 1 196 28 28 ASN HA H 5.103 0.000 1 197 28 28 ASN HB2 H 3.191 0.010 2 198 28 28 ASN HB3 H 1.898 0.010 2 199 28 28 ASN HD21 H 8.541 0.003 2 200 28 28 ASN HD22 H 6.720 0.011 2 201 28 28 ASN CB C 38.383 0.008 1 202 28 28 ASN N N 122.163 0.066 1 203 28 28 ASN ND2 N 114.922 0.079 1 204 29 29 LEU H H 8.626 0.006 1 205 29 29 LEU HA H 4.399 0.005 1 206 29 29 LEU HB2 H 1.331 0.000 2 207 29 29 LEU HB3 H 1.224 0.000 2 208 29 29 LEU HG H 1.212 0.001 1 209 29 29 LEU HD1 H 0.676 0.003 . 210 29 29 LEU HD2 H 0.600 0.001 . 211 29 29 LEU CA C 52.175 0.000 1 212 29 29 LEU CG C 25.729 0.027 1 213 29 29 LEU CD1 C 23.047 0.137 2 214 29 29 LEU CD2 C 21.731 0.099 2 215 29 29 LEU N N 125.596 0.041 1 216 30 30 ILE H H 9.055 0.010 1 217 30 30 ILE HA H 4.452 0.008 1 218 30 30 ILE HB H 1.813 0.012 1 219 30 30 ILE HG12 H 0.594 0.000 . 220 30 30 ILE HG13 H 0.594 0.000 . 221 30 30 ILE HG2 H 0.653 0.000 . 222 30 30 ILE CA C 58.159 0.021 1 223 30 30 ILE CB C 35.071 0.000 1 224 30 30 ILE CG1 C 25.143 0.000 1 225 30 30 ILE CG2 C 15.568 0.000 1 226 30 30 ILE N N 127.880 0.015 1 227 31 31 VAL H H 8.490 0.009 1 228 31 31 VAL HA H 4.302 0.011 1 229 31 31 VAL HB H 1.663 0.003 1 230 31 31 VAL HG1 H 0.648 0.019 . 231 31 31 VAL HG2 H 0.648 0.019 . 232 31 31 VAL CA C 58.519 0.128 1 233 31 31 VAL CB C 30.198 0.000 1 234 31 31 VAL CG1 C 19.324 0.248 2 235 31 31 VAL N N 125.535 0.027 1 236 32 32 LEU H H 9.086 0.005 1 237 32 32 LEU HA H 4.614 0.013 1 238 32 32 LEU HB2 H 1.661 0.035 2 239 32 32 LEU HB3 H 1.661 0.035 2 240 32 32 LEU HD1 H 0.650 0.010 . 241 32 32 LEU HD2 H 0.813 0.000 . 242 32 32 LEU N N 130.427 0.009 1 243 33 33 GLY H H 8.379 0.005 1 244 33 33 GLY HA2 H 4.248 0.022 . 245 33 33 GLY HA3 H 3.791 0.004 2 246 33 33 GLY CA C 44.213 0.079 1 247 33 33 GLY N N 109.440 0.026 1 248 34 34 ARG H H 8.959 0.002 1 249 34 34 ARG HA H 4.242 0.004 1 250 34 34 ARG HB3 H 1.760 0.000 2 251 34 34 ARG HG2 H 1.712 0.002 2 252 34 34 ARG HG3 H 1.712 0.002 2 253 34 34 ARG CA C 54.239 0.000 1 254 34 34 ARG N N 124.025 0.019 1 255 35 35 THR H H 8.052 0.009 1 256 35 35 THR HA H 3.846 0.010 1 257 35 35 THR HB H 3.939 0.000 1 258 35 35 THR HG2 H 1.093 0.018 . 259 35 35 THR CA C 63.190 0.000 1 260 35 35 THR CB C 65.589 0.000 1 261 35 35 THR N N 118.450 0.039 1 262 36 36 ILE H H 7.406 0.001 1 263 36 36 ILE HA H 3.817 0.007 1 264 36 36 ILE HB H 2.538 0.903 1 265 36 36 ILE HG12 H 1.215 0.013 2 266 36 36 ILE HG13 H 1.373 0.007 2 267 36 36 ILE HG2 H 0.858 0.003 . 268 36 36 ILE HD1 H 0.815 0.023 . 269 36 36 ILE CA C 59.070 0.000 1 270 36 36 ILE CB C 35.462 0.000 1 271 36 36 ILE CG2 C 15.526 0.024 1 272 36 36 ILE N N 119.843 0.029 1 273 37 37 GLU H H 7.723 0.005 1 274 37 37 GLU HA H 4.128 0.000 1 275 37 37 GLU HB2 H 2.039 0.000 2 276 37 37 GLU HB3 H 2.039 0.000 2 277 37 37 GLU HG2 H 2.292 0.001 2 278 37 37 GLU HG3 H 2.292 0.001 2 279 37 37 GLU CG C 33.884 0.000 1 280 37 37 GLU N N 118.980 0.013 1 281 38 38 THR H H 7.451 0.001 1 282 38 38 THR HA H 4.361 0.000 1 283 38 38 THR N N 106.868 0.038 1 284 39 39 LEU H H 7.012 0.006 1 285 39 39 LEU HA H 4.001 0.000 1 286 39 39 LEU HB2 H 1.429 0.020 2 287 39 39 LEU HB3 H 1.210 0.011 2 288 39 39 LEU HD1 H 0.758 0.018 . 289 39 39 LEU HD2 H 0.659 0.000 . 290 39 39 LEU CB C 39.708 0.080 1 291 39 39 LEU CD1 C 22.377 0.000 2 292 39 39 LEU N N 123.044 0.001 1 293 40 40 GLU H H 7.981 0.001 1 294 40 40 GLU HA H 4.243 0.000 1 295 40 40 GLU HB2 H 1.785 0.013 2 296 40 40 GLU HG2 H 1.965 0.000 2 297 40 40 GLU HG3 H 1.965 0.000 2 298 40 40 GLU N N 123.324 0.034 1 299 41 41 PHE H H 8.224 0.001 1 300 41 41 PHE HA H 4.573 0.000 1 301 41 41 PHE HB2 H 3.062 0.000 2 302 41 41 PHE HB3 H 2.621 0.000 2 303 41 41 PHE HD1 H 7.081 0.003 3 304 41 41 PHE HD2 H 7.081 0.003 3 305 41 41 PHE N N 121.305 0.064 1 306 42 42 GLY H H 8.566 0.002 1 307 42 42 GLY HA2 H 4.058 0.000 . 308 42 42 GLY HA3 H 3.843 0.000 2 309 42 42 GLY N N 109.568 0.017 1 310 43 43 ASN H H 8.386 0.000 1 311 43 43 ASN N N 118.013 0.005 1 312 44 44 ASP H H 8.374 0.000 1 313 44 44 ASP HA H 4.497 0.000 1 314 44 44 ASP N N 117.618 0.000 1 315 45 45 ASN H H 7.968 0.004 1 316 45 45 ASN HA H 4.615 0.000 1 317 45 45 ASN N N 117.191 0.000 1 318 46 46 PHE H H 8.098 0.000 1 319 46 46 PHE HD1 H 7.111 0.002 3 320 46 46 PHE HD2 H 7.111 0.002 3 321 46 46 PHE N N 121.484 0.000 1 322 47 47 PRO HA H 4.335 0.009 1 323 47 47 PRO HB3 H 2.449 0.000 2 324 47 47 PRO HD2 H 2.923 0.009 2 325 47 47 PRO HD3 H 2.446 0.002 2 326 47 47 PRO CA C 60.170 0.000 1 327 47 47 PRO CD C 47.031 0.009 1 328 48 48 GLU H H 8.209 0.002 1 329 48 48 GLU HB2 H 1.914 0.016 2 330 48 48 GLU HB3 H 1.659 0.017 2 331 48 48 GLU N N 119.616 0.049 1 332 49 49 ASN H H 7.506 0.001 1 333 49 49 ASN HB2 H 2.583 0.010 2 334 49 49 ASN HB3 H 2.583 0.010 2 335 49 49 ASN N N 114.178 0.062 1 336 50 50 ILE H H 7.916 0.010 1 337 50 50 ILE HA H 4.536 0.010 1 338 50 50 ILE HD1 H 0.648 0.003 . 339 50 50 ILE CD1 C 10.972 0.085 1 340 50 50 ILE N N 125.732 0.000 1 341 51 51 ILE H H 9.298 0.003 1 342 51 51 ILE HA H 4.111 0.003 1 343 51 51 ILE HB H 1.466 0.000 1 344 51 51 ILE HG12 H 1.244 0.014 2 345 51 51 ILE HG13 H 0.752 0.018 2 346 51 51 ILE HG2 H 0.591 0.005 . 347 51 51 ILE HD1 H -0.363 0.006 . 348 51 51 ILE CA C 55.451 0.070 1 349 51 51 ILE CB C 37.124 0.000 1 350 51 51 ILE CG2 C 12.315 0.186 1 351 51 51 ILE CD1 C 12.621 0.042 1 352 51 51 ILE N N 130.406 0.004 1 353 52 52 PRO HA H 4.817 0.004 1 354 52 52 PRO HB2 H 1.876 0.000 2 355 52 52 PRO HB3 H 2.035 0.000 2 356 52 52 PRO HG2 H 2.351 0.006 2 357 52 52 PRO HG3 H 1.856 0.007 2 358 52 52 PRO HD2 H 3.671 0.005 2 359 52 52 PRO HD3 H 3.889 0.003 2 360 52 52 PRO CA C 58.397 0.000 1 361 52 52 PRO CG C 24.409 0.059 1 362 52 52 PRO CD C 48.010 0.107 1 363 53 53 VAL H H 8.819 0.009 1 364 53 53 VAL HA H 4.322 0.000 1 365 53 53 VAL HB H 2.174 0.018 1 366 53 53 VAL HG1 H 0.804 0.095 . 367 53 53 VAL HG2 H 0.828 0.084 . 368 53 53 VAL CB C 28.669 0.000 1 369 53 53 VAL CG1 C 19.233 0.621 2 370 53 53 VAL CG2 C 18.743 0.240 2 371 54 54 THR H H 7.979 0.008 1 372 54 54 THR HA H 4.135 0.000 1 373 54 54 THR HG2 H 1.240 0.003 . 374 54 54 THR CG2 C 19.521 0.044 1 375 54 54 THR N N 118.876 0.015 1 376 55 55 ASP H H 8.414 0.005 1 377 55 55 ASP HA H 4.643 0.000 1 378 55 55 ASP HB2 H 2.762 0.007 2 379 55 55 ASP HB3 H 2.433 0.007 2 380 55 55 ASP CB C 37.882 0.000 1 381 55 55 ASP N N 119.704 0.019 1 382 56 56 SER H H 7.237 0.001 1 383 56 56 SER HA H 4.345 0.014 1 384 56 56 SER HB2 H 3.817 0.024 2 385 56 56 SER HB3 H 3.817 0.024 2 386 56 56 SER CA C 55.312 0.000 1 387 56 56 SER CB C 61.717 0.000 1 388 56 56 SER N N 112.508 0.004 1 389 57 57 LYS H H 8.881 0.001 1 390 57 57 LYS HA H 4.291 0.000 1 391 57 57 LYS HB2 H 1.865 0.000 2 392 57 57 LYS HB3 H 1.865 0.000 2 393 57 57 LYS HG2 H 0.845 0.000 2 394 57 57 LYS HG3 H 0.845 0.000 2 395 57 57 LYS N N 125.938 0.013 1 396 58 58 SER H H 8.029 0.001 1 397 58 58 SER HA H 4.554 0.000 1 398 58 58 SER HB2 H 3.738 0.000 2 399 58 58 SER HB3 H 3.738 0.000 2 400 58 58 SER N N 115.000 0.004 1 401 59 59 ASP H H 8.232 0.000 1 402 59 59 ASP HA H 5.130 0.014 1 403 59 59 ASP HB2 H 2.769 0.002 2 404 59 59 ASP HB3 H 2.438 0.002 2 405 59 59 ASP CA C 50.162 0.108 1 406 59 59 ASP N N 121.989 0.028 1 407 60 60 GLY H H 8.285 0.000 1 408 60 60 GLY HA2 H 4.362 0.000 . 409 60 60 GLY HA3 H 3.923 0.011 2 410 60 60 GLY N N 110.391 0.008 1 411 61 61 ILE H H 7.631 0.003 1 412 61 61 ILE HA H 4.852 0.004 1 413 61 61 ILE HB H 1.352 0.002 1 414 61 61 ILE HG12 H 1.404 0.000 2 415 61 61 ILE HG13 H 0.681 0.000 2 416 61 61 ILE HG2 H 0.227 0.017 . 417 61 61 ILE HD1 H 0.663 0.004 . 418 61 61 ILE CA C 57.434 0.075 1 419 61 61 ILE CB C 39.784 0.137 1 420 61 61 ILE CG1 C 25.486 0.033 1 421 61 61 ILE CG2 C 14.490 0.016 1 422 61 61 ILE CD1 C 10.994 0.000 1 423 61 61 ILE N N 117.055 0.037 1 424 62 62 ILE H H 8.699 0.004 1 425 62 62 ILE HA H 4.201 0.010 1 426 62 62 ILE HB H 1.342 0.036 1 427 62 62 ILE HG12 H 0.986 0.000 2 428 62 62 ILE HG13 H 0.435 0.000 2 429 62 62 ILE HG2 H 0.630 0.008 . 430 62 62 ILE HD1 H 0.116 0.006 . 431 62 62 ILE CA C 57.178 0.019 1 432 62 62 ILE CG2 C 14.935 0.032 1 433 62 62 ILE CD1 C 11.011 0.018 1 434 62 62 ILE N N 124.294 0.071 1 435 63 63 TYR H H 8.998 0.013 1 436 63 63 TYR HA H 4.522 0.007 1 437 63 63 TYR HB2 H 2.849 0.021 2 438 63 63 TYR HB3 H 2.658 0.011 2 439 63 63 TYR HD1 H 6.824 0.019 3 440 63 63 TYR HD2 H 6.824 0.019 3 441 63 63 TYR HE1 H 6.539 0.004 3 442 63 63 TYR HE2 H 6.539 0.004 3 443 63 63 TYR CA C 55.233 0.000 1 444 63 63 TYR CE1 C 114.79 0.061 3 445 63 63 TYR N N 124.978 0.024 1 446 64 64 LEU H H 8.714 0.010 1 447 64 64 LEU HA H 4.911 0.032 1 448 64 64 LEU HB2 H 1.577 0.004 2 449 64 64 LEU HB3 H 0.955 0.006 2 450 64 64 LEU HG H 0.550 0.033 1 451 64 64 LEU HD1 H -0.351 0.015 . 452 64 64 LEU HD2 H -0.351 0.015 . 453 64 64 LEU CA C 50.557 0.000 1 454 64 64 LEU CB C 40.231 0.037 1 455 64 64 LEU CG C 24.795 0.021 1 456 64 64 LEU CD1 C 18.945 0.000 2 457 64 64 LEU CD2 C 18.947 0.000 2 458 64 64 LEU N N 125.519 0.012 1 459 65 65 THR H H 8.890 0.001 1 460 65 65 THR HA H 5.207 0.017 1 461 65 65 THR HB H 3.864 0.004 1 462 65 65 THR HG2 H 1.055 0.001 . 463 65 65 THR CA C 57.572 0.099 1 464 65 65 THR CB C 67.604 0.033 1 465 65 65 THR CG2 C 18.790 0.000 1 466 65 65 THR N N 123.575 0.017 1 467 66 66 ILE H H 8.582 0.008 1 468 66 66 ILE HA H 4.763 0.000 1 469 66 66 ILE HB H 1.811 0.012 1 470 66 66 ILE HG12 H 0.961 0.142 . 471 66 66 ILE HG13 H 0.961 0.142 . 472 66 66 ILE HG2 H 0.766 0.012 . 473 66 66 ILE HD1 H 0.393 0.012 . 474 66 66 ILE CB C 36.687 0.000 1 475 66 66 ILE CG2 C 13.608 0.038 1 476 66 66 ILE CD1 C 11.790 0.120 1 477 66 66 ILE N N 124.481 0.023 1 478 67 67 SER H H 8.787 0.003 1 479 67 67 SER HA H 4.699 0.014 1 480 67 67 SER HB2 H 4.328 0.000 2 481 67 67 SER HB3 H 3.960 0.000 2 482 67 67 SER N N 124.879 0.015 1 483 68 68 LYS H H 8.820 0.007 1 484 68 68 LYS HA H 3.785 0.013 1 485 68 68 LYS HB2 H 1.620 0.000 2 486 68 68 LYS HB3 H 1.620 0.000 2 487 68 68 LYS HG2 H 1.291 0.000 2 488 68 68 LYS HG3 H 1.055 0.000 2 489 68 68 LYS CA C 55.797 0.047 1 490 68 68 LYS N N 119.038 0.004 1 491 69 69 ASP H H 7.771 0.001 1 492 69 69 ASP HA H 4.640 0.000 1 493 69 69 ASP HB2 H 2.656 0.000 2 494 69 69 ASP HB3 H 2.556 0.000 2 495 69 69 ASP N N 115.524 0.013 1 496 70 70 ASN H H 8.525 0.002 1 497 70 70 ASN HA H 4.317 0.000 1 498 70 70 ASN N N 112.965 0.020 1 499 71 71 ILE H H 7.443 0.003 1 500 71 71 ILE HA H 4.140 0.000 1 501 71 71 ILE HB H 1.813 0.000 1 502 71 71 ILE HG12 H 1.280 0.024 2 503 71 71 ILE HG2 H 0.743 0.005 . 504 71 71 ILE HD1 H 0.743 0.005 . 505 71 71 ILE N N 117.908 0.011 1 506 72 72 CYS H H 8.500 0.002 1 507 72 72 CYS HA H 4.920 0.006 1 508 72 72 CYS HB2 H 2.436 0.001 2 509 72 72 CYS HB3 H 1.728 0.000 2 510 72 72 CYS CB C 26.063 0.023 1 511 72 72 CYS N N 127.450 0.012 1 512 73 73 GLN H H 8.494 0.008 1 513 73 73 GLN HA H 4.522 0.000 1 514 73 73 GLN HB2 H 1.905 0.000 2 515 73 73 GLN HB3 H 1.746 0.000 2 516 73 73 GLN HG2 H 2.085 0.000 2 517 73 73 GLN HG3 H 2.085 0.000 2 518 73 73 GLN HE21 H 7.373 0.000 2 519 73 73 GLN CB C 30.213 0.000 1 520 73 73 GLN N N 122.179 0.115 1 521 74 74 PHE H H 9.307 0.001 1 522 74 74 PHE HA H 5.566 0.008 1 523 74 74 PHE HB2 H 2.673 0.010 2 524 74 74 PHE HB3 H 2.248 0.007 2 525 74 74 PHE HD1 H 6.891 0.021 3 526 74 74 PHE HD2 H 6.891 0.021 3 527 74 74 PHE CA C 53.704 0.006 1 528 74 74 PHE CB C 39.254 0.136 1 529 74 74 PHE CD1 C 130.01 0.000 3 530 74 74 PHE N N 125.985 0.015 1 531 75 75 SER H H 9.315 0.001 1 532 75 75 SER HA H 5.149 0.012 1 533 75 75 SER HB2 H 3.605 0.012 2 534 75 75 SER HB3 H 3.482 0.008 2 535 75 75 SER CA C 54.382 0.004 1 536 75 75 SER CB C 63.414 0.106 1 537 75 75 SER N N 116.714 0.025 1 538 76 76 ASP H H 8.534 0.005 1 539 76 76 ASP HA H 4.900 0.023 1 540 76 76 ASP HB2 H 3.463 0.003 2 541 76 76 ASP HB3 H 2.537 0.009 2 542 76 76 ASP CA C 49.590 0.104 1 543 76 76 ASP CB C 39.216 0.000 1 544 76 76 ASP N N 120.484 0.057 1 545 77 77 GLU H H 8.596 0.002 1 546 77 77 GLU HA H 4.124 0.005 1 547 77 77 GLU HB2 H 2.198 0.008 2 548 77 77 GLU HB3 H 2.198 0.008 2 549 77 77 GLU HG2 H 2.350 0.004 2 550 77 77 GLU HG3 H 2.350 0.004 2 551 77 77 GLU CA C 56.242 0.057 1 552 77 77 GLU N N 116.621 0.014 1 553 78 78 LYS H H 8.051 0.016 1 554 78 78 LYS HA H 4.364 0.000 1 555 78 78 LYS HB2 H 1.961 0.000 2 556 78 78 LYS HB3 H 1.961 0.000 2 557 78 78 LYS HG2 H 1.407 0.000 2 558 78 78 LYS HG3 H 1.407 0.000 2 559 78 78 LYS N N 118.118 0.023 1 560 79 79 GLY H H 8.120 0.012 1 561 79 79 GLY HA2 H 3.607 0.000 . 562 79 79 GLY HA3 H 4.073 0.000 2 563 79 79 GLY N N 108.907 0.003 1 564 80 80 GLU H H 8.423 0.000 1 565 80 80 GLU N N 122.795 0.009 1 566 81 81 GLN H H 8.533 0.003 1 567 81 81 GLN HA H 4.298 0.016 1 568 81 81 GLN HB2 H 1.913 0.000 2 569 81 81 GLN HB3 H 1.913 0.000 2 570 81 81 GLN HG2 H 2.257 0.000 2 571 81 81 GLN HG3 H 2.257 0.000 2 572 81 81 GLN CA C 53.703 0.000 1 573 81 81 GLN N N 123.093 0.009 1 574 82 82 ILE H H 8.008 0.005 1 575 82 82 ILE HA H 3.931 0.000 1 576 82 82 ILE HB H 1.044 0.029 1 577 82 82 ILE HG12 H 1.233 0.013 2 578 82 82 ILE HG13 H 0.888 0.000 2 579 82 82 ILE HG2 H 0.075 0.004 . 580 82 82 ILE HD1 H 0.374 0.015 . 581 82 82 ILE CB C 36.745 0.038 1 582 82 82 ILE CG1 C 24.675 0.000 1 583 82 82 ILE CG2 C 13.373 0.052 1 584 82 82 ILE CD1 C 11.349 0.043 1 585 82 82 ILE N N 126.444 0.016 1 586 83 83 ASP H H 8.387 0.001 1 587 83 83 ASP HA H 4.565 0.000 1 588 83 83 ASP HB2 H 2.577 0.000 2 589 83 83 ASP HB3 H 2.472 0.000 2 590 83 83 ASP N N 126.846 0.025 1 591 84 84 ILE H H 8.094 0.002 1 592 84 84 ILE HA H 4.279 0.000 1 593 84 84 ILE HB H 1.672 0.024 1 594 84 84 ILE HG12 H 1.217 0.000 2 595 84 84 ILE HG13 H 1.026 0.000 2 596 84 84 ILE HG2 H 0.630 0.002 . 597 84 84 ILE HD1 H 0.606 0.009 . 598 84 84 ILE CG2 C 14.852 0.000 1 599 84 84 ILE CD1 C 11.068 0.050 1 600 84 84 ILE N N 120.975 0.018 1 601 85 85 ASN H H 8.763 0.002 1 602 85 85 ASN HA H 4.718 0.000 1 603 85 85 ASN HB2 H 3.041 0.000 2 604 85 85 ASN HB3 H 2.924 0.000 2 605 85 85 ASN N N 123.363 0.032 1 606 86 86 SER H H 8.727 0.003 1 607 86 86 SER N N 120.558 0.007 1 608 87 87 GLN H H 8.143 0.001 1 609 87 87 GLN HA H 4.050 0.000 1 610 87 87 GLN HG2 H 2.028 0.000 2 611 87 87 GLN N N 120.972 0.000 1 612 88 88 PHE H H 7.676 0.003 1 613 88 88 PHE HA H 4.687 0.000 1 614 88 88 PHE HB3 H 2.785 0.000 2 615 88 88 PHE HD1 H 7.163 0.000 3 616 88 88 PHE HD2 H 7.163 0.000 3 617 88 88 PHE N N 115.532 0.009 1 618 89 89 ASN H H 8.468 0.003 1 619 89 89 ASN HA H 4.493 0.000 1 620 89 89 ASN HB2 H 3.274 0.008 2 621 89 89 ASN HB3 H 3.146 0.130 2 622 89 89 ASN CB C 35.098 0.044 1 623 89 89 ASN N N 118.545 0.073 1 624 90 90 SER H H 7.537 0.008 1 625 90 90 SER HA H 5.573 0.023 1 626 90 90 SER HB2 H 3.544 0.004 2 627 90 90 SER HB3 H 3.469 0.006 2 628 90 90 SER CA C 53.742 0.000 1 629 90 90 SER CB C 64.543 0.077 1 630 90 90 SER N N 110.305 0.069 1 631 91 91 PHE H H 8.489 0.001 1 632 91 91 PHE HA H 4.854 0.000 1 633 91 91 PHE HB2 H 2.931 0.008 2 634 91 91 PHE HB3 H 3.081 0.000 2 635 91 91 PHE HD1 H 6.587 0.007 3 636 91 91 PHE HD2 H 6.587 0.007 3 637 91 91 PHE HE1 H 5.973 0.006 3 638 91 91 PHE HE2 H 5.973 0.006 3 639 91 91 PHE CD1 C 129.36 0.000 3 640 91 91 PHE N N 116.509 0.020 1 641 92 92 GLU H H 8.540 0.002 1 642 92 92 GLU HA H 5.346 0.009 1 643 92 92 GLU HB2 H 1.829 0.007 2 644 92 92 GLU HB3 H 1.829 0.007 2 645 92 92 GLU HG2 H 2.013 0.013 2 646 92 92 GLU HG3 H 2.013 0.013 2 647 92 92 GLU CA C 51.709 0.014 1 648 92 92 GLU CB C 30.203 0.011 1 649 92 92 GLU CG C 33.704 0.003 1 650 92 92 GLU N N 120.099 0.010 1 651 93 93 TYR H H 9.114 0.010 1 652 93 93 TYR HA H 4.543 0.006 1 653 93 93 TYR HB2 H 3.093 0.006 2 654 93 93 TYR HB3 H 2.845 0.002 2 655 93 93 TYR HD1 H 7.015 0.021 3 656 93 93 TYR HD2 H 7.015 0.021 3 657 93 93 TYR HE1 H 6.760 0.000 3 658 93 93 TYR HE2 H 6.760 0.000 3 659 93 93 TYR N N 125.415 0.031 1 660 94 94 ASP H H 8.765 0.008 1 661 94 94 ASP HB2 H 2.910 0.004 2 662 94 94 ASP HB3 H 2.324 0.342 2 663 94 94 ASP CB C 36.848 0.147 1 664 94 94 ASP N N 127.466 0.092 1 665 95 95 GLY H H 8.477 0.001 1 666 95 95 GLY HA2 H 3.518 0.000 2 667 95 95 GLY N N 103.962 0.006 1 668 96 96 ILE H H 8.039 0.002 1 669 96 96 ILE HA H 3.988 0.008 1 670 96 96 ILE HB H 1.948 0.019 1 671 96 96 ILE HG12 H 1.608 0.034 2 672 96 96 ILE HG13 H 0.888 0.002 2 673 96 96 ILE HG2 H 0.092 0.011 . 674 96 96 ILE HD1 H 0.880 0.015 . 675 96 96 ILE CA C 57.908 0.000 1 676 96 96 ILE CB C 36.197 0.000 1 677 96 96 ILE CG1 C 24.917 0.015 1 678 96 96 ILE CG2 C 16.001 0.030 1 679 96 96 ILE CD1 C 11.451 0.012 1 680 96 96 ILE N N 123.977 0.027 1 681 97 97 SER H H 8.042 0.006 1 682 97 97 SER HA H 4.815 0.006 1 683 97 97 SER HB2 H 3.636 0.006 2 684 97 97 SER HB3 H 3.636 0.006 2 685 97 97 SER CA C 54.420 0.033 1 686 97 97 SER CB C 61.793 0.012 1 687 97 97 SER N N 119.722 0.061 1 688 98 98 PHE H H 8.582 0.002 1 689 98 98 PHE HA H 5.037 0.015 1 690 98 98 PHE HB2 H 1.502 0.005 2 691 98 98 PHE HB3 H 2.107 0.009 2 692 98 98 PHE HD1 H 6.635 0.014 3 693 98 98 PHE HD2 H 6.635 0.014 3 694 98 98 PHE HE1 H 6.974 0.108 3 695 98 98 PHE HE2 H 6.974 0.108 3 696 98 98 PHE CA C 53.790 0.057 1 697 98 98 PHE CD1 C 129.71 0.035 3 698 98 98 PHE CE1 C 127.59 0.042 3 699 98 98 PHE N N 123.561 0.068 1 700 99 99 HIS H H 9.095 0.002 1 701 99 99 HIS HA H 5.121 0.025 1 702 99 99 HIS HB2 H 3.084 0.013 2 703 99 99 HIS HB3 H 3.084 0.013 2 704 99 99 HIS HD2 H 6.777 0.044 1 705 99 99 HIS CB C 29.723 0.027 1 706 99 99 HIS CD2 C 118.876 0.036 1 707 99 99 HIS N N 119.438 0.009 1 708 100 100 LEU H H 8.640 0.001 1 709 100 100 LEU HA H 4.856 0.006 1 710 100 100 LEU HB2 H 1.793 0.004 2 711 100 100 LEU HB3 H 1.377 0.000 2 712 100 100 LEU HD1 H 0.685 0.010 . 713 100 100 LEU HD2 H 0.685 0.010 . 714 100 100 LEU CB C 41.223 0.000 1 715 100 100 LEU CD1 C 22.783 0.000 2 716 100 100 LEU N N 127.001 0.009 1 717 101 101 LYS H H 9.141 0.001 1 718 101 101 LYS N N 127.328 0.044 1 719 102 102 ASN HA H 4.590 0.004 1 720 102 102 ASN CA C 50.310 0.000 1 721 103 103 MET H H 7.942 0.000 1 722 103 103 MET N N 122.351 0.000 1 723 105 105 GLU HA H 4.213 0.000 1 724 106 106 ASP H H 8.291 0.011 1 725 106 106 ASP HA H 4.547 0.000 1 726 106 106 ASP N N 122.018 0.000 1 727 107 107 LYS H H 7.712 0.002 1 728 107 107 LYS N N 126.005 0.000 1 stop_ save_