data_5873 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone and side chains 1H, 13C, and 15N Chemical Shift Assignments for BlaI-NTD ; _BMRB_accession_number 5873 _BMRB_flat_file_name bmr5873.str _Entry_type original _Submission_date 2003-07-18 _Accession_date 2003-07-18 _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 'Van Melckebeke' Helene . . 2 Vreuls Christelle . . 3 Gans Pierre . . 4 Filee Patrice . . 5 Llabres Gabriel . . 6 Joris Bernard . . 7 Simorre Jean-Pierre . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 421 "13C chemical shifts" 351 "15N chemical shifts" 76 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-07-07 original author . stop_ _Original_release_date 2004-07-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structural Study of BlaI : Implications for the Repression of Genes Involved in Beta-lactam Antibiotic Resistance ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22930671 _PubMed_ID 14568532 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 'Van Melckebeke' Helene . . 2 Vreuls Christelle . . 3 Gans Pierre . . 4 Filee Patrice . . 5 Llabres Gabriel . . 6 Joris Bernard . . 7 Simorre Jean-Pierre . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 333 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 711 _Page_last 720 _Year 2003 _Details . loop_ _Keyword 'b-lactamase repressor BlaI' 'NMR spectroscopy' 'Winged Helix Protein' 'protein-DNA interaction' 'bacterial resistance to antibiotics' stop_ save_ ################################## # Molecular system description # ################################## save_BlaI-NTD _Saveframe_category molecular_system _Mol_system_name 'BlaI N-terminal domain' _Abbreviation_common BlaI-NTD _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label BlaI-NTD $BlaI stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'repressor of the b-lactamase gene' 'regulatory protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_BlaI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'b-lactamase gene repressor' _Name_variant 'penicillase repressor' _Abbreviation_common BlaI _Molecular_mass . _Mol_thiol_state 'not present' _Details '82 N-terminal amino-acids of the 128 amino -acids full-length repressor BlaI' ############################## # Polymer residue sequence # ############################## _Residue_count 82 _Mol_residue_sequence ; MKKIPQISDAELEVMKVIWK HSSINTNEVIKELSKTSTWS PKTIQTMLLRLIKKGALNHH KEGRVFVYTPNIDESDYIEV KS ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 LYS 4 ILE 5 PRO 6 GLN 7 ILE 8 SER 9 ASP 10 ALA 11 GLU 12 LEU 13 GLU 14 VAL 15 MET 16 LYS 17 VAL 18 ILE 19 TRP 20 LYS 21 HIS 22 SER 23 SER 24 ILE 25 ASN 26 THR 27 ASN 28 GLU 29 VAL 30 ILE 31 LYS 32 GLU 33 LEU 34 SER 35 LYS 36 THR 37 SER 38 THR 39 TRP 40 SER 41 PRO 42 LYS 43 THR 44 ILE 45 GLN 46 THR 47 MET 48 LEU 49 LEU 50 ARG 51 LEU 52 ILE 53 LYS 54 LYS 55 GLY 56 ALA 57 LEU 58 ASN 59 HIS 60 HIS 61 LYS 62 GLU 63 GLY 64 ARG 65 VAL 66 PHE 67 VAL 68 TYR 69 THR 70 PRO 71 ASN 72 ILE 73 ASP 74 GLU 75 SER 76 ASP 77 TYR 78 ILE 79 GLU 80 VAL 81 LYS 82 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 1P6R "Solution Structure Of The Dna Binding Domain Of The Repressor Blai." 100.00 82 100.00 100.00 5.48e-51 PDB 2P7C "Solution Structure Of The Bacillus Licheniformis Blai Monomeric Form In Complex With The Blap Half-Operator" 100.00 82 100.00 100.00 5.48e-51 GB AAA22648 "penicillinase repressor [Bacillus licheniformis 9945A]" 100.00 128 100.00 100.00 8.03e-51 GB AAA22650 "repressor protein [Bacillus licheniformis]" 100.00 128 98.78 98.78 6.84e-50 GB AAU21886 "putative beta-lactamase repressor protein [Bacillus licheniformis DSM 13 = ATCC 14580]" 100.00 128 98.78 100.00 2.38e-50 GB AAU39238 "penicillinase repressor BlaI [Bacillus licheniformis DSM 13 = ATCC 14580]" 100.00 128 98.78 100.00 2.38e-50 GB AGN34711 "putative beta-lactamase repressor protein BlaI [Bacillus licheniformis 9945A]" 100.00 128 100.00 100.00 8.03e-51 REF WP_003178582 "MULTISPECIES: beta-lactamase [Bacillus]" 100.00 128 98.78 100.00 2.38e-50 REF WP_020449991 "MULTISPECIES: putative beta-lactamase repressor protein BlaI [Bacillus]" 100.00 128 100.00 100.00 8.03e-51 REF WP_026585720 "beta-lactamase repressor [Bacillus sp. NSP9.1]" 100.00 128 97.56 97.56 3.27e-49 REF YP_006711714 "penicillinase repressor BlaI [Bacillus licheniformis DSM 13 = ATCC 14580]" 100.00 128 98.78 100.00 2.38e-50 REF YP_008076448 "putative beta-lactamase repressor protein BlaI [Bacillus licheniformis 9945A]" 100.00 128 100.00 100.00 8.03e-51 SP P06555 "RecName: Full=Penicillinase repressor; AltName: Full=Beta-lactamase repressor protein; AltName: Full=Regulatory protein BlaI [B" 100.00 128 100.00 100.00 8.03e-51 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic _Details $BlaI 'Bacillus licheniformis' 1402 Eubacteria . Bacillus licheniformis 749/I 'Bacteria, Firmicutes, Bacillales, Bacillaceae, Bacillus' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $BlaI 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3)pLys plasmid pET22 'The full-length protein was cleaved with papain to obtain the BlaI-NTD species.' 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 $BlaI 0.5 mM '[U-13C; U-15N]' 'phosphate buffer' 75 mM . KCl 300 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $BlaI 0.75 mM [U-15N] stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 2000 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_CBCANH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label . save_ save_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_(H)C(CO)NH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name (H)C(CO)NH-TOCSY _Sample_label . save_ save_H(CCO)NH-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH-TOCSY _Sample_label . save_ save_1H-15N_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_H(C)CH-TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name H(C)CH-TOCSY _Sample_label . save_ save_2D-NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-NOESY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name (H)C(CO)NH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name H(C)CH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_set_condition_1 _Saveframe_category sample_conditions _Details 'phosphate buffer 75 mM pH 7.6, 300 mM KCl' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.6 0.2 na temperature 298 1 K 'ionic strength' 375 . mM stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set1 _Saveframe_category assigned_chemical_shifts _Details 'The first four residues and the last one (residue 82) have not been assigned' loop_ _Experiment_label HNCA HNCO HN(CA)CO CBCANH CBCA(CO)NH (H)C(CO)NH-TOCSY H(CCO)NH-TOCSY '1H-15N HSQC' H(C)CH-TOCSY 2D-NOESY stop_ _Sample_conditions_label $set_condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name BlaI-NTD _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 . 5 PRO HA H 4.51 0.02 1 2 . 5 PRO HB2 H 2.32 0.02 2 3 . 5 PRO HB3 H 1.76 0.02 2 4 . 5 PRO HG2 H 1.93 0.02 1 5 . 5 PRO HG3 H 1.93 0.02 1 6 . 5 PRO HD2 H 3.97 0.02 2 7 . 5 PRO HD3 H 3.91 0.02 2 8 . 5 PRO CA C 62.4 0.1 1 9 . 5 PRO CB C 31.7 0.2 1 10 . 5 PRO CG C 26.8 0.2 1 11 . 5 PRO CD C 50.1 0.2 1 12 . 6 GLN H H 8.57 0.02 1 13 . 6 GLN HA H 4.47 0.02 1 14 . 6 GLN HB2 H 2.05 0.02 2 15 . 6 GLN HG2 H 2.43 0.02 2 16 . 6 GLN C C 174.8 0.1 1 17 . 6 GLN CA C 55.7 0.1 1 18 . 6 GLN CB C 28.3 0.2 1 19 . 6 GLN CG C 33.6 0.2 1 20 . 6 GLN N N 125.1 0.1 1 21 . 7 ILE H H 8.40 0.02 1 22 . 7 ILE HA H 4.48 0.02 1 23 . 7 ILE HB H 1.93 0.02 1 24 . 7 ILE HG12 H 1.14 0.02 1 25 . 7 ILE HG13 H 1.14 0.02 1 26 . 7 ILE HG2 H 0.67 0.02 1 27 . 7 ILE HD1 H 0.36 0.02 1 28 . 7 ILE C C 174.9 0.1 1 29 . 7 ILE CA C 58.6 0.1 1 30 . 7 ILE CB C 38.7 0.2 1 31 . 7 ILE CG1 C 25.3 0.2 1 32 . 7 ILE CG2 C 16.7 0.2 1 33 . 7 ILE CD1 C 11.5 0.2 1 34 . 7 ILE N N 126.5 0.1 1 35 . 8 SER H H 9.00 0.02 1 36 . 8 SER HA H 4.55 0.02 1 37 . 8 SER HB2 H 4.36 0.02 2 38 . 8 SER HB3 H 3.92 0.02 2 39 . 8 SER C C 173.6 0.1 1 40 . 8 SER CA C 56.8 0.1 1 41 . 8 SER CB C 65.3 0.2 1 42 . 8 SER N N 126.2 0.1 1 43 . 9 ASP H H 8.75 0.02 1 44 . 9 ASP HA H 4.40 0.02 1 45 . 9 ASP HB2 H 2.79 0.02 2 46 . 9 ASP HB3 H 2.71 0.02 2 47 . 9 ASP C C 178.3 0.1 1 48 . 9 ASP CA C 57.5 0.1 1 49 . 9 ASP CB C 39.2 0.2 1 50 . 9 ASP N N 123.0 0.1 1 51 . 10 ALA H H 8.14 0.02 1 52 . 10 ALA HA H 4.34 0.02 1 53 . 10 ALA HB H 1.25 0.02 1 54 . 10 ALA C C 178.8 0.1 1 55 . 10 ALA CA C 54.7 0.1 1 56 . 10 ALA CB C 19.0 0.2 1 57 . 10 ALA N N 125.3 0.1 1 58 . 11 GLU H H 7.41 0.02 1 59 . 11 GLU HA H 3.56 0.02 1 60 . 11 GLU HB2 H 2.36 0.02 2 61 . 11 GLU HB3 H 1.70 0.02 2 62 . 11 GLU HG2 H 2.20 0.02 2 63 . 11 GLU HG3 H 1.92 0.02 2 64 . 11 GLU C C 178.8 0.1 1 65 . 11 GLU CA C 58.5 0.1 1 66 . 11 GLU CB C 30.1 0.2 1 67 . 11 GLU CG C 37.0 0.2 1 68 . 11 GLU N N 119.5 0.1 1 69 . 12 LEU H H 8.60 0.02 1 70 . 12 LEU HA H 3.71 0.02 1 71 . 12 LEU HB2 H 2.02 0.02 2 72 . 12 LEU HB3 H 1.70 0.02 2 73 . 12 LEU HG H 1.70 0.02 4 74 . 12 LEU HD1 H 1.06 0.02 2 75 . 12 LEU HD2 H 1.04 0.02 2 76 . 12 LEU C C 177.8 0.1 1 77 . 12 LEU CA C 57.3 0.1 1 78 . 12 LEU CB C 40.8 0.2 1 79 . 12 LEU CG C 26.8 0.2 1 80 . 12 LEU CD1 C 24.7 0.2 2 81 . 12 LEU CD2 C 23.8 0.2 2 82 . 12 LEU N N 123.8 0.1 1 83 . 13 GLU H H 7.43 0.02 1 84 . 13 GLU HA H 4.00 0.02 1 85 . 13 GLU HB2 H 2.54 0.02 2 86 . 13 GLU HB3 H 2.24 0.02 2 87 . 13 GLU HG2 H 2.54 0.02 2 88 . 13 GLU C C 179.0 0.1 1 89 . 13 GLU CA C 58.8 0.1 1 90 . 13 GLU CB C 28.6 0.2 1 91 . 13 GLU CG C 35.6 0.2 1 92 . 13 GLU N N 119.5 0.1 1 93 . 14 VAL H H 7.01 0.02 1 94 . 14 VAL HA H 3.49 0.02 1 95 . 14 VAL HB H 2.08 0.02 1 96 . 14 VAL HG1 H 0.83 0.02 2 97 . 14 VAL HG2 H 0.48 0.02 2 98 . 14 VAL C C 177.4 0.1 1 99 . 14 VAL CA C 65.7 0.1 1 100 . 14 VAL CB C 30.6 0.2 1 101 . 14 VAL CG1 C 22.2 0.2 2 102 . 14 VAL CG2 C 21.5 0.2 2 103 . 14 VAL N N 120.5 0.1 1 104 . 15 MET H H 7.94 0.02 1 105 . 15 MET HA H 3.69 0.02 1 106 . 15 MET HB2 H 2.01 0.02 2 107 . 15 MET HB3 H 1.75 0.02 2 108 . 15 MET HG2 H 1.39 0.02 2 109 . 15 MET HG3 H -0.11 0.02 2 110 . 15 MET C C 177.0 0.1 1 111 . 15 MET CA C 54.6 0.1 1 112 . 15 MET CB C 29.6 0.2 1 113 . 15 MET CG C 26.8 0.2 1 114 . 15 MET N N 119.7 0.1 1 115 . 16 LYS H H 8.42 0.02 1 116 . 16 LYS HA H 4.34 0.02 1 117 . 16 LYS HB2 H 1.98 0.02 2 118 . 16 LYS HG2 H 1.78 0.02 2 119 . 16 LYS HD2 H 1.46 0.02 2 120 . 16 LYS HE2 H 2.98 0.02 2 121 . 16 LYS C C 179.3 0.1 1 122 . 16 LYS CA C 60.5 0.1 1 123 . 16 LYS CB C 32.4 0.2 1 124 . 16 LYS CG C 29.6 0.2 1 125 . 16 LYS CD C 26.0 0.2 1 126 . 16 LYS CE C 35.8 0.2 1 127 . 16 LYS N N 119.6 0.1 1 128 . 17 VAL H H 7.07 0.02 1 129 . 17 VAL HA H 3.84 0.02 1 130 . 17 VAL HB H 2.37 0.02 1 131 . 17 VAL HG1 H 1.17 0.02 2 132 . 17 VAL HG2 H 0.99 0.02 2 133 . 17 VAL C C 177.0 0.1 1 134 . 17 VAL CA C 65.8 0.1 1 135 . 17 VAL CB C 31.4 0.2 1 136 . 17 VAL CG1 C 22.2 0.2 1 137 . 17 VAL CG2 C 22.2 0.2 1 138 . 17 VAL N N 120.8 0.1 1 139 . 18 ILE H H 7.32 0.02 1 140 . 18 ILE HA H 3.58 0.02 1 141 . 18 ILE HB H 1.59 0.02 1 142 . 18 ILE HG12 H 1.41 0.02 1 143 . 18 ILE HG13 H 1.15 0.02 2 144 . 18 ILE HG2 H 0.63 0.02 1 145 . 18 ILE HD1 H 0.45 0.02 1 146 . 18 ILE C C 178.1 0.1 1 147 . 18 ILE CA C 64.4 0.1 1 148 . 18 ILE CB C 36.0 0.2 1 149 . 18 ILE CG1 C 27.8 0.2 1 150 . 18 ILE CG2 C 16.3 0.2 1 151 . 18 ILE CD1 C 12.6 0.2 1 152 . 18 ILE N N 123.7 0.1 1 153 . 19 TRP H H 9.37 0.02 1 154 . 19 TRP HA H 4.59 0.02 1 155 . 19 TRP HB2 H 3.22 0.02 2 156 . 19 TRP HD1 H 7.37 0.02 1 157 . 19 TRP HE1 H 10.17 0.02 1 158 . 19 TRP HE3 H 7.42 0.02 1 159 . 19 TRP HZ2 H 6.78 0.02 1 160 . 19 TRP HZ3 H 6.82 0.02 1 161 . 19 TRP HH2 H 6.54 0.02 1 162 . 19 TRP C C 178.2 0.1 1 163 . 19 TRP CA C 60.1 0.1 1 164 . 19 TRP CB C 27.7 0.2 1 165 . 19 TRP CD1 C 124.5 0.2 1 166 . 19 TRP CE3 C 121.6 0.2 1 167 . 19 TRP CZ2 C 113.0 0.2 1 168 . 19 TRP CZ3 C 119.8 0.2 1 169 . 19 TRP CH2 C 123.2 0.2 1 170 . 19 TRP N N 121.4 0.1 1 171 . 19 TRP NE1 N 130.6 0.1 1 172 . 20 LYS H H 7.48 0.02 1 173 . 20 LYS HA H 4.16 0.02 1 174 . 20 LYS HB2 H 2.95 0.02 2 175 . 20 LYS HB3 H 2.00 0.02 2 176 . 20 LYS HG2 H 1.85 0.02 2 177 . 20 LYS HG3 H 1.65 0.02 2 178 . 20 LYS HD2 H 1.38 0.02 2 179 . 20 LYS HD3 H 1.12 0.02 2 180 . 20 LYS HE2 H 2.95 0.02 2 181 . 20 LYS C C 176.8 0.1 1 182 . 20 LYS CA C 57.9 0.1 1 183 . 20 LYS CB C 32.2 0.2 1 184 . 20 LYS CG C 28.8 0.2 1 185 . 20 LYS CD C 24.3 0.2 1 186 . 20 LYS CE C 41.8 0.2 1 187 . 20 LYS N N 119.8 0.1 1 188 . 21 HIS H H 7.61 0.02 1 189 . 21 HIS HA H 4.62 0.02 1 190 . 21 HIS HB2 H 3.33 0.02 2 191 . 21 HIS HB3 H 2.76 0.02 2 192 . 21 HIS C C 175.4 0.1 1 193 . 21 HIS CA C 56.8 0.1 1 194 . 21 HIS CB C 31.9 0.2 1 195 . 21 HIS N N 118.8 0.1 1 196 . 22 SER H H 8.65 0.02 1 197 . 22 SER HA H 4.07 0.02 1 198 . 22 SER HB2 H 4.07 0.02 2 199 . 22 SER HB3 H 4.33 0.02 2 200 . 22 SER C C 174.2 0.1 1 201 . 22 SER CA C 63.6 0.1 1 202 . 22 SER CB C 62.2 0.2 1 203 . 22 SER N N 119.4 0.1 1 204 . 23 SER H H 8.17 0.02 1 205 . 23 SER HA H 5.05 0.02 1 206 . 23 SER HB2 H 3.80 0.02 2 207 . 23 SER HB3 H 3.72 0.02 2 208 . 23 SER C C 173.1 0.1 1 209 . 23 SER CA C 57.5 0.1 1 210 . 23 SER CB C 63.3 0.2 1 211 . 23 SER N N 118.3 0.1 1 212 . 24 ILE H H 8.26 0.02 1 213 . 24 ILE HA H 4.73 0.02 1 214 . 24 ILE HB H 1.80 0.02 1 215 . 24 ILE HG12 H 1.61 0.02 2 216 . 24 ILE HG13 H 1.45 0.02 2 217 . 24 ILE HG2 H 0.84 0.02 1 218 . 24 ILE HD1 H 0.30 0.02 1 219 . 24 ILE C C 171.8 0.1 1 220 . 24 ILE CA C 59.9 0.1 1 221 . 24 ILE CB C 40.0 0.2 1 222 . 24 ILE CG1 C 28.1 0.2 1 223 . 24 ILE CG2 C 15.5 0.2 1 224 . 24 ILE CD1 C 13.0 0.2 1 225 . 24 ILE N N 125.3 0.1 1 226 . 25 ASN H H 8.76 0.02 1 227 . 25 ASN HA H 5.91 0.02 1 228 . 25 ASN HB2 H 3.28 0.02 2 229 . 25 ASN HB3 H 2.75 0.02 2 230 . 25 ASN C C 176.3 0.1 1 231 . 25 ASN CA C 51.2 0.1 1 232 . 25 ASN CB C 39.9 0.2 1 233 . 25 ASN N N 127.9 0.1 1 234 . 26 THR H H 8.38 0.02 1 235 . 26 THR HA H 3.76 0.02 1 236 . 26 THR HB H 4.07 0.02 1 237 . 26 THR HG2 H 1.31 0.02 1 238 . 26 THR C C 174.8 0.1 1 239 . 26 THR CA C 67.4 0.1 1 240 . 26 THR CB C 70.0 0.2 1 241 . 26 THR CG2 C 21.7 0.2 1 242 . 26 THR N N 114.6 0.1 1 243 . 27 ASN H H 7.92 0.02 1 244 . 27 ASN HA H 4.39 0.02 1 245 . 27 ASN HB2 H 2.93 0.02 2 246 . 27 ASN HB3 H 2.83 0.02 2 247 . 27 ASN C C 177.8 0.1 1 248 . 27 ASN CA C 56.0 0.1 1 249 . 27 ASN CB C 37.4 0.2 1 250 . 27 ASN N N 119.8 0.1 1 251 . 28 GLU H H 8.26 0.02 1 252 . 28 GLU HA H 4.08 0.02 1 253 . 28 GLU HB2 H 2.28 0.02 2 254 . 28 GLU HB3 H 1.96 0.02 2 255 . 28 GLU HG2 H 2.47 0.02 2 256 . 28 GLU HG3 H 2.28 0.02 2 257 . 28 GLU C C 178.6 0.1 1 258 . 28 GLU CA C 58.5 0.1 1 259 . 28 GLU CB C 28.8 0.2 1 260 . 28 GLU CG C 36.0 0.2 1 261 . 28 GLU N N 124.2 0.1 1 262 . 29 VAL H H 8.27 0.02 1 263 . 29 VAL HA H 3.42 0.02 1 264 . 29 VAL HB H 2.20 0.02 1 265 . 29 VAL HG1 H 0.88 0.02 2 266 . 29 VAL HG2 H 0.80 0.02 2 267 . 29 VAL C C 177.1 0.1 1 268 . 29 VAL CA C 66.8 0.1 1 269 . 29 VAL CB C 30.9 0.2 1 270 . 29 VAL CG1 C 23.1 0.2 2 271 . 29 VAL CG2 C 21.6 0.2 2 272 . 29 VAL N N 123.4 0.1 1 273 . 30 ILE H H 7.84 0.02 1 274 . 30 ILE HA H 3.60 0.02 1 275 . 30 ILE HB H 1.96 0.02 1 276 . 30 ILE HG12 H 1.96 0.02 2 277 . 30 ILE HG13 H 0.94 0.02 2 278 . 30 ILE HG2 H 0.95 0.02 1 279 . 30 ILE HD1 H 0.97 0.02 1 280 . 30 ILE C C 178.3 0.1 1 281 . 30 ILE CA C 65.5 0.1 1 282 . 30 ILE CB C 37.6 0.2 1 283 . 30 ILE CG1 C 29.9 0.2 1 284 . 30 ILE CG2 C 16.7 0.2 1 285 . 30 ILE CD1 C 14.0 0.2 1 286 . 30 ILE N N 121.3 0.1 1 287 . 31 LYS H H 8.11 0.02 1 288 . 31 LYS HA H 3.99 0.02 1 289 . 31 LYS HB2 H 1.42 0.02 2 290 . 31 LYS HG2 H 1.73 0.02 2 291 . 31 LYS HD2 H 1.96 0.02 2 292 . 31 LYS HD3 H 1.57 0.02 2 293 . 31 LYS HE2 H 3.00 0.02 2 294 . 31 LYS C C 179.2 0.1 1 295 . 31 LYS CA C 59.5 0.1 1 296 . 31 LYS CB C 31.9 0.2 1 297 . 31 LYS CG C 28.8 0.2 1 298 . 31 LYS CD C 24.3 0.2 1 299 . 31 LYS N N 124.1 0.1 1 300 . 32 GLU H H 8.18 0.02 1 301 . 32 GLU HA H 4.19 0.02 1 302 . 32 GLU HB2 H 2.12 0.02 2 303 . 32 GLU HG2 H 2.44 0.02 2 304 . 32 GLU HG3 H 2.12 0.02 2 305 . 32 GLU C C 179.5 0.1 1 306 . 32 GLU CA C 58.8 0.1 1 307 . 32 GLU CB C 29.4 0.2 1 308 . 32 GLU CG C 35.5 0.2 1 309 . 32 GLU N N 121.3 0.1 1 310 . 33 LEU H H 8.31 0.02 1 311 . 33 LEU HA H 4.35 0.02 1 312 . 33 LEU HB2 H 1.84 0.02 2 313 . 33 LEU HB3 H 1.47 0.02 2 314 . 33 LEU HG H 0.87 0.02 1 315 . 33 LEU HD1 H 0.87 0.02 2 316 . 33 LEU C C 179.1 0.1 1 317 . 33 LEU CA C 56.3 0.1 1 318 . 33 LEU CB C 41.5 0.2 1 319 . 33 LEU CG C 27.1 0.2 1 320 . 33 LEU CD1 C 23.2 0.2 2 321 . 33 LEU N N 121.4 0.1 1 322 . 34 SER H H 8.15 0.02 1 323 . 34 SER HA H 4.50 0.02 1 324 . 34 SER HB2 H 4.07 0.02 2 325 . 34 SER C C 174.2 0.1 1 326 . 34 SER CA C 60.8 0.1 1 327 . 34 SER CB C 62.5 0.2 1 328 . 34 SER N N 119.2 0.1 1 329 . 35 LYS H H 7.23 0.02 1 330 . 35 LYS HA H 4.27 0.02 1 331 . 35 LYS HB2 H 2.00 0.02 2 332 . 35 LYS HG2 H 1.49 0.02 2 333 . 35 LYS HG3 H 1.78 0.02 2 334 . 35 LYS HD2 H 1.73 0.02 2 335 . 35 LYS C C 177.8 0.1 1 336 . 35 LYS CA C 57.9 0.1 1 337 . 35 LYS CB C 32.9 0.2 1 338 . 35 LYS CG C 29.0 0.2 1 339 . 35 LYS CD C 25.0 0.2 1 340 . 35 LYS CE C 41.5 0.2 1 341 . 35 LYS N N 120.9 0.1 1 342 . 36 THR H H 7.24 0.02 1 343 . 36 THR HA H 4.49 0.02 1 344 . 36 THR HB H 4.38 0.02 1 345 . 36 THR HG2 H 1.14 0.02 1 346 . 36 THR C C 173.3 0.1 1 347 . 36 THR CA C 60.9 0.1 1 348 . 36 THR CB C 69.5 0.2 1 349 . 36 THR CG2 C 21.2 0.2 1 350 . 36 THR N N 108.2 0.1 1 351 . 37 SER H H 7.87 0.02 1 352 . 37 SER HA H 4.58 0.02 1 353 . 37 SER HB2 H 3.29 0.02 2 354 . 37 SER HB3 H 3.09 0.02 2 355 . 37 SER C C 173.7 0.1 1 356 . 37 SER CA C 57.3 0.1 1 357 . 37 SER CB C 65.6 0.2 1 358 . 37 SER N N 120.5 0.1 1 359 . 38 THR H H 7.89 0.02 1 360 . 38 THR HA H 4.40 0.02 1 361 . 38 THR HB H 4.40 0.02 4 362 . 38 THR HG2 H 1.04 0.02 1 363 . 38 THR C C 174.5 0.1 1 364 . 38 THR CA C 60.5 0.1 1 365 . 38 THR CB C 67.9 0.2 1 366 . 38 THR CG2 C 20.8 0.2 1 367 . 38 THR N N 113.5 0.1 1 368 . 39 TRP H H 7.42 0.02 1 369 . 39 TRP HA H 4.87 0.02 1 370 . 39 TRP HB2 H 2.99 0.02 2 371 . 39 TRP HB3 H 1.93 0.02 2 372 . 39 TRP HD1 H 7.27 0.02 1 373 . 39 TRP HE1 H 10.23 0.02 1 374 . 39 TRP HE3 H 7.32 0.02 1 375 . 39 TRP HZ2 H 7.45 0.02 1 376 . 39 TRP HZ3 H 6.89 0.02 1 377 . 39 TRP HH2 H 7.32 0.02 1 378 . 39 TRP C C 175.7 0.1 1 379 . 39 TRP CA C 55.8 0.1 1 380 . 39 TRP CB C 29.6 0.2 1 381 . 39 TRP CD1 C 125.5 0.2 1 382 . 39 TRP CE3 C 120.6 0.2 1 383 . 39 TRP CZ2 C 114.0 0.2 1 384 . 39 TRP CZ3 C 119.8 0.2 1 385 . 39 TRP CH2 C 124.1 0.2 1 386 . 39 TRP N N 125.1 0.1 1 387 . 39 TRP NE1 N 131.7 0.1 1 388 . 40 SER H H 8.77 0.02 1 389 . 40 SER C C 172.9 0.1 1 390 . 40 SER CA C 55.7 0.1 1 391 . 40 SER CB C 62.4 0.2 1 392 . 40 SER N N 121.4 0.1 1 393 . 41 PRO HA H 4.08 0.02 1 394 . 41 PRO HB2 H 2.39 0.02 2 395 . 41 PRO HG2 H 2.01 0.02 2 396 . 41 PRO HD2 H 4.02 0.02 2 397 . 41 PRO CA C 65.9 0.1 1 398 . 41 PRO CB C 31.7 0.2 1 399 . 41 PRO CG C 27.7 0.2 1 400 . 41 PRO CD C 49.6 0.2 1 401 . 42 LYS H H 7.99 0.02 1 402 . 42 LYS HA H 4.06 0.02 1 403 . 42 LYS HB2 H 2.01 0.02 2 404 . 42 LYS HB3 H 1.78 0.02 4 405 . 42 LYS HD2 H 1.54 0.02 4 406 . 42 LYS HD3 H 1.87 0.02 4 407 . 42 LYS HG2 H 1.62 0.02 4 408 . 42 LYS HG3 H 1.42 0.02 4 409 . 42 LYS HE2 H 3.00 0.02 2 410 . 42 LYS C C 178.8 0.1 1 411 . 42 LYS CA C 58.9 0.1 1 412 . 42 LYS CB C 31.7 0.2 1 413 . 42 LYS CG C 28.6 0.2 1 414 . 42 LYS CD C 24.5 0.2 1 415 . 42 LYS CE C 40.7 0.2 1 416 . 42 LYS N N 119.3 0.1 1 417 . 43 THR H H 7.87 0.02 1 418 . 43 THR HA H 3.74 0.02 1 419 . 43 THR HB H 4.38 0.02 1 420 . 43 THR HG2 H 0.91 0.02 1 421 . 43 THR C C 175.9 0.1 1 422 . 43 THR CA C 66.2 0.1 1 423 . 43 THR CB C 67.9 0.2 1 424 . 43 THR CG2 C 21.6 0.2 1 425 . 43 THR N N 122.6 0.1 1 426 . 44 ILE H H 8.13 0.02 1 427 . 44 ILE HA H 3.25 0.02 1 428 . 44 ILE HB H 1.82 0.02 1 429 . 44 ILE HG12 H 1.88 0.02 2 430 . 44 ILE HG13 H 0.80 0.02 2 431 . 44 ILE HG2 H 0.68 0.02 1 432 . 44 ILE HD1 H 0.80 0.02 1 433 . 44 ILE C C 176.7 0.1 1 434 . 44 ILE CA C 65.8 0.1 1 435 . 44 ILE CB C 37.3 0.2 1 436 . 44 ILE CG1 C 29.6 0.2 1 437 . 44 ILE CG2 C 17.5 0.2 1 438 . 44 ILE CD1 C 12.8 0.2 1 439 . 44 ILE N N 124.9 0.1 1 440 . 45 GLN H H 8.42 0.02 1 441 . 45 GLN HA H 3.89 0.02 1 442 . 45 GLN HB2 H 2.22 0.02 2 443 . 45 GLN HB3 H 2.18 0.02 2 444 . 45 GLN HG2 H 2.43 0.02 2 445 . 45 GLN HG3 H 2.20 0.02 2 446 . 45 GLN C C 178.1 0.1 1 447 . 45 GLN CA C 59.4 0.1 1 448 . 45 GLN CB C 28.0 0.2 1 449 . 45 GLN CG C 34.2 0.2 1 450 . 45 GLN N N 120.9 0.1 1 451 . 46 THR H H 8.07 0.02 1 452 . 46 THR HA H 3.84 0.02 1 453 . 46 THR HB H 4.31 0.02 1 454 . 46 THR HG2 H 1.18 0.02 1 455 . 46 THR C C 175.9 0.1 1 456 . 46 THR CA C 66.5 0.1 1 457 . 46 THR CB C 67.9 0.2 1 458 . 46 THR CG2 C 21.0 0.2 1 459 . 46 THR N N 119.5 0.1 1 460 . 47 MET H H 7.90 0.02 1 461 . 47 MET HA H 3.88 0.02 1 462 . 47 MET HB2 H 2.21 0.02 2 463 . 47 MET HB3 H 1.57 0.02 2 464 . 47 MET HG2 H 2.48 0.02 2 465 . 47 MET HG3 H 2.20 0.02 2 466 . 47 MET C C 177.7 0.1 1 467 . 47 MET CA C 59.5 0.1 1 468 . 47 MET CB C 33.2 0.2 1 469 . 47 MET CG C 31.6 0.2 1 470 . 47 MET N N 124.1 0.1 1 471 . 48 LEU H H 8.08 0.02 1 472 . 48 LEU HA H 3.53 0.02 1 473 . 48 LEU HB2 H 1.81 0.02 2 474 . 48 LEU HB3 H 0.88 0.02 2 475 . 48 LEU HG H 1.39 0.02 1 476 . 48 LEU HD1 H 0.58 0.02 2 477 . 48 LEU HD2 H -0.09 0.02 2 478 . 48 LEU C C 177.6 0.1 1 479 . 48 LEU CA C 58.1 0.1 1 480 . 48 LEU CB C 40.4 0.2 1 481 . 48 LEU CG C 26.2 0.2 1 482 . 48 LEU CD1 C 24.9 0.2 2 483 . 48 LEU CD2 C 22.0 0.2 2 484 . 48 LEU N N 122.0 0.1 1 485 . 49 LEU H H 7.49 0.02 1 486 . 49 LEU HA H 3.93 0.02 1 487 . 49 LEU HB2 H 1.78 0.02 2 488 . 49 LEU HB3 H 1.57 0.02 2 489 . 49 LEU HG H 1.67 0.02 1 490 . 49 LEU HD1 H 0.87 0.02 2 491 . 49 LEU HD2 H 0.83 0.02 2 492 . 49 LEU C C 179.5 0.1 1 493 . 49 LEU CA C 57.5 0.1 1 494 . 49 LEU CB C 40.7 0.2 1 495 . 49 LEU CG C 26.5 0.2 1 496 . 49 LEU CD1 C 24.2 0.2 2 497 . 49 LEU CD2 C 22.9 0.2 2 498 . 49 LEU N N 119.8 0.1 1 499 . 50 ARG H H 7.95 0.02 1 500 . 50 ARG HA H 3.96 0.02 1 501 . 50 ARG HB2 H 1.96 0.02 2 502 . 50 ARG HB3 H 1.84 0.02 2 503 . 50 ARG HG2 H 1.81 0.02 2 504 . 50 ARG HG3 H 1.61 0.02 2 505 . 50 ARG HD2 H 3.16 0.02 2 506 . 50 ARG C C 178.6 0.1 1 507 . 50 ARG CA C 59.0 0.1 1 508 . 50 ARG CB C 29.4 0.2 1 509 . 50 ARG CG C 27.3 0.2 1 510 . 50 ARG CD C 43.2 0.2 1 511 . 50 ARG N N 123.2 0.1 1 512 . 51 LEU H H 8.14 0.02 1 513 . 51 LEU HA H 3.88 0.02 1 514 . 51 LEU HB2 H 2.05 0.02 2 515 . 51 LEU HB3 H 1.07 0.02 2 516 . 51 LEU HG H 1.65 0.02 1 517 . 51 LEU HD1 H 0.56 0.02 2 518 . 51 LEU HD2 H 0.64 0.02 2 519 . 51 LEU C C 179.3 0.1 1 520 . 51 LEU CA C 57.5 0.1 1 521 . 51 LEU CB C 41.0 0.2 1 522 . 51 LEU CG C 27.3 0.2 1 523 . 51 LEU CD1 C 24.0 0.2 2 524 . 51 LEU CD2 C 22.5 0.2 2 525 . 51 LEU N N 122.8 0.1 1 526 . 52 ILE H H 8.03 0.02 1 527 . 52 ILE HA H 4.08 0.02 1 528 . 52 ILE HB H 2.00 0.02 1 529 . 52 ILE HG12 H 1.66 0.02 2 530 . 52 ILE HG13 H 0.79 0.02 2 531 . 52 ILE HG2 H 0.87 0.02 1 532 . 52 ILE HD1 H 0.40 0.02 1 533 . 52 ILE C C 179.7 0.1 1 534 . 52 ILE CA C 64.2 0.1 1 535 . 52 ILE CB C 37.6 0.2 1 536 . 52 ILE CG1 C 28.0 0.2 1 537 . 52 ILE CG2 C 16.3 0.2 1 538 . 52 ILE CD1 C 12.8 0.2 1 539 . 52 ILE N N 124.8 0.1 1 540 . 53 LYS H H 7.96 0.02 1 541 . 53 LYS HA H 4.04 0.02 1 542 . 53 LYS HB2 H 1.99 0.02 2 543 . 53 LYS HG2 H 1.58 0.02 2 544 . 53 LYS HG3 H 1.46 0.02 2 545 . 53 LYS HD2 H 1.75 0.02 4 546 . 53 LYS HE2 H 2.99 0.02 2 547 . 53 LYS C C 178.3 0.1 1 548 . 53 LYS CA C 59.0 0.1 1 549 . 53 LYS CB C 31.4 0.2 1 550 . 53 LYS CG C 28.6 0.2 1 551 . 53 LYS CD C 24.6 0.2 1 552 . 53 LYS CE C 41.6 0.2 1 553 . 53 LYS N N 125.3 0.1 1 554 . 54 LYS H H 7.95 0.02 1 555 . 54 LYS HA H 4.34 0.02 1 556 . 54 LYS HB2 H 1.88 0.02 2 557 . 54 LYS HG2 H 1.66 0.02 2 558 . 54 LYS HG3 H 1.70 0.02 2 559 . 54 LYS HD2 H 1.70 0.02 2 560 . 54 LYS HD3 H 1.61 0.02 2 561 . 54 LYS HE2 H 2.95 0.02 2 562 . 54 LYS C C 176.0 0.1 1 563 . 54 LYS CA C 56.8 0.1 1 564 . 54 LYS CB C 33.2 0.2 1 565 . 54 LYS CD C 30.1 0.2 1 566 . 54 LYS CG C 25.3 0.2 1 567 . 54 LYS N N 117.3 0.1 1 568 . 55 GLY H H 7.83 0.02 1 569 . 55 GLY HA2 H 4.23 0.02 2 570 . 55 GLY HA3 H 3.92 0.02 2 571 . 55 GLY C C 174.2 0.1 1 572 . 55 GLY CA C 45.0 0.1 1 573 . 55 GLY N N 109.0 0.1 1 574 . 56 ALA H H 8.07 0.02 1 575 . 56 ALA HA H 4.27 0.02 1 576 . 56 ALA HB H 1.31 0.02 1 577 . 56 ALA C C 176.1 0.1 1 578 . 56 ALA CA C 53.1 0.1 1 579 . 56 ALA CB C 20.0 0.2 1 580 . 56 ALA N N 123.1 0.1 1 581 . 57 LEU H H 6.80 0.02 1 582 . 57 LEU HA H 4.93 0.02 1 583 . 57 LEU HB2 H 1.52 0.02 2 584 . 57 LEU HB3 H 1.27 0.02 2 585 . 57 LEU HG H 0.79 0.02 1 586 . 57 LEU HD1 H 0.60 0.02 2 587 . 57 LEU HD2 H 0.79 0.02 2 588 . 57 LEU C C 174.8 0.1 1 589 . 57 LEU CA C 52.1 0.1 1 590 . 57 LEU CB C 46.7 0.2 1 591 . 57 LEU CG C 26.4 0.2 1 592 . 57 LEU CD1 C 26.4 0.2 2 593 . 57 LEU CD2 C 25.5 0.2 2 594 . 57 LEU N N 117.0 0.1 1 595 . 58 ASN H H 8.92 0.02 1 596 . 58 ASN HA H 5.12 0.02 1 597 . 58 ASN HB2 H 2.75 0.02 2 598 . 58 ASN C C 173.7 0.1 1 599 . 58 ASN CA C 51.5 0.1 1 600 . 58 ASN CB C 40.2 0.2 1 601 . 58 ASN N N 121.9 0.1 1 602 . 59 HIS H H 8.46 0.02 1 603 . 59 HIS HA H 5.80 0.02 1 604 . 59 HIS HB2 H 2.79 0.02 2 605 . 59 HIS HB3 H 2.51 0.02 2 606 . 59 HIS HD2 H 6.16 0.02 1 607 . 59 HIS HE1 H 7.45 0.02 1 608 . 59 HIS C C 173.3 0.1 1 609 . 59 HIS CA C 53.8 0.1 1 610 . 59 HIS CB C 33.5 0.2 1 611 . 59 HIS CD2 C 121.3 0.2 1 612 . 59 HIS CE1 C 138.1 0.2 1 613 . 59 HIS N N 120.3 0.1 1 614 . 60 HIS H H 8.34 0.02 1 615 . 60 HIS HA H 4.71 0.02 1 616 . 60 HIS HB2 H 3.09 0.02 2 617 . 60 HIS C C 172.1 0.1 1 618 . 60 HIS CA C 54.7 0.1 1 619 . 60 HIS CB C 31.4 0.2 1 620 . 60 HIS N N 119.8 0.1 1 621 . 61 LYS H H 8.60 0.02 1 622 . 61 LYS HA H 4.23 0.02 1 623 . 61 LYS HB2 H 1.57 0.02 2 624 . 61 LYS HB3 H 1.31 0.02 2 625 . 61 LYS HD2 H 1.35 0.02 2 626 . 61 LYS HG2 H 0.88 0.02 2 627 . 61 LYS HG3 H 0.80 0.02 2 628 . 61 LYS HE2 H 2.70 0.02 2 629 . 61 LYS HE3 H 2.60 0.02 2 630 . 61 LYS C C 175.5 0.1 1 631 . 61 LYS CA C 55.8 0.1 1 632 . 61 LYS CB C 32.7 0.2 1 633 . 61 LYS CD C 28.6 0.2 1 634 . 61 LYS CG C 24.3 0.2 1 635 . 61 LYS N N 126.0 0.1 1 636 . 62 GLU H H 8.51 0.02 1 637 . 62 GLU HA H 4.44 0.02 1 638 . 62 GLU HB2 H 1.88 0.02 2 639 . 62 GLU HB3 H 1.69 0.02 2 640 . 62 GLU HG2 H 2.18 0.02 2 641 . 62 GLU HG3 H 2.12 0.02 2 642 . 62 GLU C C 175.4 0.1 1 643 . 62 GLU CA C 54.9 0.1 1 644 . 62 GLU CB C 30.4 0.2 1 645 . 62 GLU CG C 35.8 0.2 1 646 . 62 GLU N N 130.2 0.1 1 647 . 63 GLY H H 8.72 0.02 1 648 . 63 GLY HA2 H 4.00 0.02 2 649 . 63 GLY HA3 H 3.58 0.02 2 650 . 63 GLY CA C 46.5 0.1 1 651 . 63 GLY N N 118.5 0.1 1 652 . 64 ARG H H 8.79 0.02 1 653 . 64 ARG HA H 4.26 0.02 1 654 . 64 ARG HB2 H 2.04 0.02 2 655 . 64 ARG HB3 H 1.65 0.02 2 656 . 64 ARG HG2 H 1.74 0.02 2 657 . 64 ARG HG3 H 1.65 0.02 2 658 . 64 ARG HD2 H 3.19 0.02 2 659 . 64 ARG C C 175.5 0.1 1 660 . 64 ARG CA C 55.7 0.1 1 661 . 64 ARG CB C 30.4 0.2 1 662 . 64 ARG CG C 27.0 0.2 1 663 . 64 ARG CD C 42.9 0.2 1 664 . 64 ARG N N 127.4 0.1 1 665 . 65 VAL H H 7.49 0.02 1 666 . 65 VAL HA H 4.54 0.02 1 667 . 65 VAL HB H 2.23 0.02 1 668 . 65 VAL HG1 H 0.99 0.02 2 669 . 65 VAL HG2 H 0.95 0.02 2 670 . 65 VAL C C 173.3 0.1 1 671 . 65 VAL CA C 59.5 0.1 1 672 . 65 VAL CB C 34.5 0.2 1 673 . 65 VAL CG1 C 21.1 0.2 2 674 . 65 VAL CG2 C 19.2 0.2 2 675 . 65 VAL N N 118.0 0.1 1 676 . 66 PHE H H 8.07 0.02 1 677 . 66 PHE HA H 4.76 0.02 1 678 . 66 PHE HB2 H 2.78 0.02 2 679 . 66 PHE HB3 H 2.27 0.02 2 680 . 66 PHE HD1 H 6.91 0.02 1 681 . 66 PHE HD2 H 6.91 0.02 1 682 . 66 PHE HE1 H 7.20 0.02 1 683 . 66 PHE HE2 H 7.20 0.02 1 684 . 66 PHE C C 174.0 0.1 1 685 . 66 PHE CA C 56.8 0.1 1 686 . 66 PHE CB C 40.0 0.2 1 687 . 66 PHE CD1 C 130.7 0.2 1 688 . 66 PHE CD2 C 130.7 0.2 1 689 . 66 PHE CE1 C 130.8 0.2 1 690 . 66 PHE CE2 C 130.8 0.2 1 691 . 66 PHE CZ C 129.2 0.2 1 692 . 66 PHE N N 123.4 0.1 1 693 . 67 VAL H H 8.46 0.02 1 694 . 67 VAL HA H 4.08 0.02 1 695 . 67 VAL HB H 1.11 0.02 2 696 . 67 VAL HG1 H 0.72 0.02 2 697 . 67 VAL HG2 H 0.67 0.02 2 698 . 67 VAL C C 174.2 0.1 1 699 . 67 VAL CA C 60.4 0.1 1 700 . 67 VAL CB C 33.2 0.2 1 701 . 67 VAL CG1 C 21.6 0.2 1 702 . 67 VAL CG2 C 20.3 0.2 1 703 . 67 VAL N N 121.1 0.1 1 704 . 68 TYR H H 8.74 0.02 1 705 . 68 TYR HA H 5.44 0.02 1 706 . 68 TYR HB2 H 2.90 0.02 2 707 . 68 TYR HB3 H 2.74 0.02 2 708 . 68 TYR HD1 H 6.99 0.02 3 709 . 68 TYR HE1 H 6.57 0.02 3 710 . 68 TYR C C 175.0 0.1 1 711 . 68 TYR CA C 56.4 0.1 1 712 . 68 TYR CB C 41.0 0.2 1 713 . 68 TYR CD1 C 132.5 0.2 1 714 . 68 TYR CD2 C 132.5 0.2 1 715 . 68 TYR CE1 C 117.5 0.2 1 716 . 68 TYR CE2 C 117.5 0.2 1 717 . 68 TYR N N 126.3 0.1 1 718 . 69 THR H H 8.35 0.02 1 719 . 69 THR HA H 5.04 0.02 1 720 . 69 THR HB H 4.39 0.02 1 721 . 69 THR HG2 H 1.18 0.02 1 722 . 69 THR C C 171.7 0.1 1 723 . 69 THR CA C 57.3 0.1 1 724 . 69 THR CB C 70.0 0.2 1 725 . 69 THR CG2 C 21.0 0.2 1 726 . 69 THR N N 112.8 0.1 1 727 . 70 PRO HA H 4.65 0.02 1 728 . 70 PRO HB2 H 2.56 0.02 2 729 . 70 PRO HB3 H 2.12 0.02 2 730 . 70 PRO HG2 H 2.71 0.02 2 731 . 70 PRO HG3 H 2.10 0.02 2 732 . 70 PRO HD2 H 4.05 0.02 2 733 . 70 PRO HD3 H 3.93 0.02 2 734 . 70 PRO CA C 62.9 0.1 1 735 . 70 PRO CB C 32.1 0.2 1 736 . 70 PRO CG C 27.3 0.2 1 737 . 70 PRO CD C 50.1 0.2 1 738 . 71 ASN H H 8.57 0.02 1 739 . 71 ASN HA H 5.13 0.02 1 740 . 71 ASN HB2 H 2.79 0.02 2 741 . 71 ASN HB3 H 2.15 0.02 2 742 . 71 ASN C C 173.2 0.1 1 743 . 71 ASN CA C 51.7 0.1 1 744 . 71 ASN CB C 39.9 0.2 1 745 . 71 ASN N N 122.3 0.1 1 746 . 72 ILE H H 7.17 0.02 1 747 . 72 ILE HA H 4.74 0.02 1 748 . 72 ILE HB H 2.40 0.02 1 749 . 72 ILE HG12 H 1.68 0.02 2 750 . 72 ILE HG13 H 1.58 0.02 2 751 . 72 ILE HG2 H 1.20 0.02 1 752 . 72 ILE HD1 H 0.81 0.02 1 753 . 72 ILE C C 174.5 0.1 1 754 . 72 ILE CA C 58.7 0.1 1 755 . 72 ILE CB C 41.3 0.2 1 756 . 72 ILE CG1 C 24.8 0.2 1 757 . 72 ILE CG2 C 18.8 0.2 1 758 . 72 ILE CD1 C 12.8 0.2 1 759 . 72 ILE N N 113.6 0.1 1 760 . 73 ASP H H 9.53 0.02 1 761 . 73 ASP HA H 4.79 0.02 1 762 . 73 ASP HB2 H 2.71 0.02 2 763 . 73 ASP HB3 H 2.56 0.02 2 764 . 73 ASP C C 175.4 0.1 1 765 . 73 ASP CA C 53.5 0.1 1 766 . 73 ASP CB C 42.5 0.2 1 767 . 73 ASP N N 128.8 0.1 1 768 . 74 GLU H H 8.08 0.02 1 769 . 74 GLU HA H 1.97 0.02 1 770 . 74 GLU HG2 H 1.58 0.02 2 771 . 74 GLU HG3 H 1.34 0.02 2 772 . 74 GLU HB2 H 1.07 0.02 2 773 . 74 GLU HB3 H 0.52 0.02 2 774 . 74 GLU C C 177.6 0.1 1 775 . 74 GLU CA C 58.5 0.1 1 776 . 74 GLU CB C 29.1 0.2 1 777 . 74 GLU CG C 35.2 0.2 1 778 . 74 GLU N N 129.1 0.1 1 779 . 75 SER H H 8.12 0.02 1 780 . 75 SER HA H 4.08 0.02 1 781 . 75 SER HB2 H 3.87 0.02 2 782 . 75 SER HB3 H 3.76 0.02 2 783 . 75 SER C C 174.9 0.1 1 784 . 75 SER CA C 60.0 0.1 1 785 . 75 SER CB C 62.2 0.2 1 786 . 75 SER N N 114.2 0.1 1 787 . 76 ASP H H 7.51 0.02 1 788 . 76 ASP HA H 4.55 0.02 1 789 . 76 ASP HB2 H 2.82 0.02 2 790 . 76 ASP HB3 H 2.39 0.02 2 791 . 76 ASP C C 175.2 0.1 1 792 . 76 ASP CA C 55.4 0.1 1 793 . 76 ASP CB C 40.9 0.2 1 794 . 76 ASP N N 122.3 0.1 1 795 . 77 TYR H H 7.61 0.02 1 796 . 77 TYR HA H 4.40 0.02 1 797 . 77 TYR HB2 H 3.23 0.02 2 798 . 77 TYR HB3 H 2.71 0.02 2 799 . 77 TYR HD1 H 7.33 0.02 3 800 . 77 TYR HE1 H 6.99 0.02 3 801 . 77 TYR C C 174.6 0.1 1 802 . 77 TYR CA C 59.3 0.1 1 803 . 77 TYR CB C 41.0 0.2 1 804 . 77 TYR CD1 C 132.9 0.2 1 805 . 77 TYR CD2 C 132.9 0.2 1 806 . 77 TYR CE1 C 118.2 0.2 1 807 . 77 TYR CE2 C 118.2 0.2 1 808 . 77 TYR N N 119.6 0.1 1 809 . 78 ILE H H 7.67 0.02 1 810 . 78 ILE HA H 4.26 0.02 1 811 . 78 ILE HB H 1.78 0.02 1 812 . 78 ILE HG12 H 1.42 0.02 2 813 . 78 ILE HG13 H 1.18 0.02 2 814 . 78 ILE HG2 H 0.87 0.02 1 815 . 78 ILE HD1 H 0.87 0.02 1 816 . 78 ILE C C 174.7 0.1 1 817 . 78 ILE CA C 59.9 0.1 1 818 . 78 ILE CB C 38.6 0.2 1 819 . 78 ILE CG1 C 26.4 0.2 1 820 . 78 ILE CG2 C 17.2 0.2 1 821 . 78 ILE CD1 C 12.6 0.2 1 822 . 78 ILE N N 122.2 0.1 1 823 . 79 GLU H H 8.25 0.02 1 824 . 79 GLU HA H 4.27 0.02 1 825 . 79 GLU HB2 H 1.98 0.02 2 826 . 79 GLU HB3 H 1.93 0.02 2 827 . 79 GLU HG2 H 2.23 0.02 2 828 . 79 GLU HG3 H 2.12 0.02 2 829 . 79 GLU C C 175.5 0.1 1 830 . 79 GLU CA C 55.9 0.1 1 831 . 79 GLU CB C 29.9 0.2 1 832 . 79 GLU CG C 35.9 0.2 1 833 . 79 GLU N N 127.6 0.1 1 834 . 80 VAL H H 8.12 0.02 1 835 . 80 VAL HA H 4.07 0.02 1 836 . 80 VAL HB H 2.01 0.02 1 837 . 80 VAL HG1 H 0.88 0.02 2 838 . 80 VAL C C 174.7 0.1 1 839 . 80 VAL CA C 62.0 0.1 1 840 . 80 VAL CB C 32.0 0.2 1 841 . 80 VAL CG1 C 20.7 0.2 1 842 . 80 VAL CG2 C 20.7 0.2 1 843 . 80 VAL N N 126.3 0.1 1 844 . 81 LYS H H 7.87 0.02 1 845 . 81 LYS C C 174.0 0.1 1 846 . 81 LYS CA C 57.1 0.1 1 847 . 81 LYS CB C 33.2 0.2 1 848 . 81 LYS N N 133.6 0.1 1 stop_ save_