data_17615 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of RfaH carboxyterminal domain ; _BMRB_accession_number 17615 _BMRB_flat_file_name bmr17615.str _Entry_type original _Submission_date 2011-05-02 _Accession_date 2011-05-02 _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 Burmann Bjoern M. . 2 Schweimer Kristian . . 3 Roesch Paul . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 397 "13C chemical shifts" 211 "15N chemical shifts" 62 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-07-16 update author 'update entry citation' 2012-07-30 original author 'original release' stop_ _Original_release_date 2015-07-16 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; An alpha-helix to beta-barrel domain switch transforms the transcription factor RfaH into a translation factor ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22817892 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Burmann Bjoern M. . 2 Schweimer Kristian . . 3 Roesch Paul . . 4 Knauer Stefan H. . 5 Mooney Rachel A. . 6 Sevostyanova Anastasia . . 7 Landick Robert . . 8 Artsimovitch Irina . . stop_ _Journal_abbreviation Cell _Journal_name_full 'Cell Press' _Journal_volume 150 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 291 _Page_last 303 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'RfaH carboxyterminal domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label RfaH $RfaH 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_RfaH _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass 7269.401 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 66 _Mol_residue_sequence ; GAMGPKDIVDPATPYPGDKV IITEGAFEGFQAIFTEPDGE ARSMLLLNLINKEIKHSVKN TEFRKL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 97 GLY 2 98 ALA 3 99 MET 4 100 GLY 5 101 PRO 6 102 LYS 7 103 ASP 8 104 ILE 9 105 VAL 10 106 ASP 11 107 PRO 12 108 ALA 13 109 THR 14 110 PRO 15 111 TYR 16 112 PRO 17 113 GLY 18 114 ASP 19 115 LYS 20 116 VAL 21 117 ILE 22 118 ILE 23 119 THR 24 120 GLU 25 121 GLY 26 122 ALA 27 123 PHE 28 124 GLU 29 125 GLY 30 126 PHE 31 127 GLN 32 128 ALA 33 129 ILE 34 130 PHE 35 131 THR 36 132 GLU 37 133 PRO 38 134 ASP 39 135 GLY 40 136 GLU 41 137 ALA 42 138 ARG 43 139 SER 44 140 MET 45 141 LEU 46 142 LEU 47 143 LEU 48 144 ASN 49 145 LEU 50 146 ILE 51 147 ASN 52 148 LYS 53 149 GLU 54 150 ILE 55 151 LYS 56 152 HIS 57 153 SER 58 154 VAL 59 155 LYS 60 156 ASN 61 157 THR 62 158 GLU 63 159 PHE 64 160 ARG 65 161 LYS 66 162 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-22 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 2LCL "Solution Structure Of Rfah Carboxyterminal Domain" 100.00 66 100.00 100.00 2.17e-39 PDB 2OUG "Crystal Structure Of The Rfah Transcription Factor At 2.1a Resolution" 93.94 162 100.00 100.00 8.97e-36 DBJ BAB38193 "transcriptional activator RfaH [Escherichia coli O157:H7 str. Sakai]" 93.94 162 100.00 100.00 8.97e-36 DBJ BAE77461 "DNA-binding transcriptional antiterminator [Escherichia coli str. K12 substr. W3110]" 93.94 162 100.00 100.00 8.97e-36 DBJ BAG79652 "transcriptional activator [Escherichia coli SE11]" 93.94 162 100.00 100.00 8.97e-36 DBJ BAI27905 "DNA-binding transcriptional antiterminator RfaH [Escherichia coli O26:H11 str. 11368]" 93.94 162 100.00 100.00 8.97e-36 DBJ BAI33028 "DNA-binding transcriptional antiterminator RfaH [Escherichia coli O103:H2 str. 12009]" 93.94 162 100.00 100.00 8.97e-36 EMBL CAA46147 "transcriptional activator of haemolysin synthesis and secretion [Escherichia coli]" 93.94 162 100.00 100.00 8.97e-36 EMBL CAP78305 "Transcriptional activator rfaH [Escherichia coli LF82]" 93.94 162 98.39 100.00 2.24e-35 EMBL CAQ34199 "RfaH transcriptional antiterminator [Escherichia coli BL21(DE3)]" 93.94 162 100.00 100.00 8.97e-36 EMBL CAR00816 "DNA-binding transcriptional antiterminator [Escherichia coli IAI1]" 93.94 162 100.00 100.00 8.97e-36 EMBL CAR05481 "DNA-binding transcriptional antiterminator [Escherichia coli S88]" 93.94 162 98.39 100.00 2.24e-35 GB AAA67638 "also called sfrB, hlyT [Escherichia coli str. K-12 substr. MG1655]" 93.94 162 100.00 100.00 8.97e-36 GB AAA91060 "RfaH [Escherichia coli]" 93.94 162 100.00 100.00 8.97e-36 GB AAC76845 "transcription antitermination protein [Escherichia coli str. K-12 substr. MG1655]" 93.94 162 100.00 100.00 8.97e-36 GB AAG10071 "transcriptional activator RfaH [Escherichia coli]" 93.94 162 98.39 100.00 2.24e-35 GB AAG59036 "transcriptional activator affecting biosynthesis of lipopolysaccharide core, F pilin, and haemolysin [Escherichia coli O157:H7 " 93.94 162 100.00 100.00 8.97e-36 REF NP_312797 "transcriptional activator RfaH [Escherichia coli O157:H7 str. Sakai]" 93.94 162 100.00 100.00 8.97e-36 REF NP_418284 "transcription antitermination protein [Escherichia coli str. K-12 substr. MG1655]" 93.94 162 100.00 100.00 8.97e-36 REF NP_709646 "transcriptional activator RfaH [Shigella flexneri 2a str. 301]" 93.94 162 98.39 98.39 8.92e-35 REF WP_001161073 "transcriptional regulator [Escherichia coli]" 93.94 162 100.00 100.00 1.08e-35 REF WP_001192387 "transcription antitermination protein RfaH [Escherichia coli]" 93.94 162 100.00 100.00 8.22e-36 SP P0AFW0 "RecName: Full=Transcription antitermination protein RfaH" 93.94 162 100.00 100.00 8.97e-36 SP P0AFW1 "RecName: Full=Transcription antitermination protein RfaH" 93.94 162 100.00 100.00 8.97e-36 SP Q0TAL4 "RecName: Full=Transcription antitermination protein RfaH" 93.94 162 98.39 100.00 2.24e-35 SP Q8FBI4 "RecName: Full=Transcription antitermination protein RfaH" 93.94 162 98.39 100.00 2.24e-35 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $RfaH 'E. coli' 562 Bacteria . Escherichia coli 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 $RfaH 'recombinant technology' . Escherichia coli . BL21-DE3 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '0.5 mM RfaH-CTD solved in NMR-buffer' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RfaH 0.5 mM '[U-99% 13C; U-99% 15N]' HEPES 0.025 mM 'natural abundance' NaCl 0.05 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details 'equipped with CryoProbe' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_C(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_aliphatic_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY aliphatic' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_aromatic_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY aromatic' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '25 mM HEPES, 50 mM NaCl, pH 7.5' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 75 . mM pH 7.5 . 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 carbon' ppm 0 na direct . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.0 'liquid anhydrous ammonia' N 15 nitrogen ppm 0 na direct . . . 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 HNCACB' '2D 1H-13C HSQC' '3D C(CO)NH' 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 RfaH _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 97 1 GLY HA2 H 3.76 0.03 2 2 97 1 GLY HA3 H 3.76 0.03 2 3 97 1 GLY CA C 43.94 0.20 1 4 98 2 ALA HA H 4.36 0.03 1 5 98 2 ALA HB H 1.40 0.03 1 6 98 2 ALA CA C 52.64 0.20 1 7 98 2 ALA CB C 19.42 0.20 1 8 99 3 MET HA H 4.56 0.03 1 9 99 3 MET HB2 H 2.02 0.03 2 10 99 3 MET HB3 H 2.13 0.03 2 11 99 3 MET HG2 H 2.57 0.03 2 12 99 3 MET HG3 H 2.64 0.03 2 13 99 3 MET CA C 55.23 0.20 1 14 99 3 MET CB C 33.16 0.20 1 15 99 3 MET CG C 32.08 0.20 1 16 100 4 GLY H H 8.39 0.03 1 17 100 4 GLY HA2 H 4.21 0.03 2 18 100 4 GLY HA3 H 4.03 0.03 2 19 100 4 GLY CA C 44.61 0.20 1 20 100 4 GLY N N 110.83 0.20 1 21 101 5 PRO HA H 4.41 0.03 1 22 101 5 PRO HB2 H 1.95 0.03 2 23 101 5 PRO HB3 H 2.32 0.03 2 24 101 5 PRO HG2 H 2.03 0.03 2 25 101 5 PRO HG3 H 2.03 0.03 2 26 101 5 PRO HD2 H 3.64 0.03 2 27 101 5 PRO HD3 H 3.64 0.03 2 28 101 5 PRO CA C 63.43 0.20 1 29 101 5 PRO CB C 32.21 0.20 1 30 101 5 PRO CG C 27.27 0.20 1 31 101 5 PRO CD C 49.83 0.20 1 32 102 6 LYS H H 8.42 0.03 1 33 102 6 LYS HA H 4.32 0.03 1 34 102 6 LYS HB2 H 1.74 0.03 2 35 102 6 LYS HB3 H 1.85 0.03 2 36 102 6 LYS HG2 H 1.42 0.03 2 37 102 6 LYS HG3 H 1.46 0.03 2 38 102 6 LYS HD2 H 1.69 0.03 2 39 102 6 LYS HD3 H 1.77 0.03 2 40 102 6 LYS HE2 H 3.02 0.03 2 41 102 6 LYS HE3 H 3.02 0.03 2 42 102 6 LYS CA C 56.26 0.20 1 43 102 6 LYS CB C 33.00 0.20 1 44 102 6 LYS CG C 24.75 0.20 1 45 102 6 LYS CD C 29.00 0.20 1 46 102 6 LYS CE C 42.01 0.20 1 47 102 6 LYS N N 120.35 0.20 1 48 103 7 ASP H H 8.19 0.03 1 49 103 7 ASP HA H 4.59 0.03 1 50 103 7 ASP HB2 H 2.60 0.03 2 51 103 7 ASP HB3 H 2.68 0.03 2 52 103 7 ASP CA C 54.55 0.20 1 53 103 7 ASP CB C 41.31 0.20 1 54 103 7 ASP N N 120.73 0.20 1 55 104 8 ILE H H 7.97 0.03 1 56 104 8 ILE HA H 4.17 0.03 1 57 104 8 ILE HB H 1.85 0.03 1 58 104 8 ILE HG12 H 1.16 0.03 2 59 104 8 ILE HG13 H 1.45 0.03 2 60 104 8 ILE HG2 H 0.87 0.03 1 61 104 8 ILE HD1 H 0.85 0.03 1 62 104 8 ILE CA C 60.95 0.20 1 63 104 8 ILE CB C 38.84 0.20 1 64 104 8 ILE CG1 C 27.20 0.20 1 65 104 8 ILE CG2 C 17.56 0.20 1 66 104 8 ILE CD1 C 12.88 0.20 1 67 104 8 ILE N N 120.47 0.20 1 68 105 9 VAL H H 8.17 0.03 1 69 105 9 VAL HA H 4.09 0.03 1 70 105 9 VAL HB H 2.01 0.03 1 71 105 9 VAL HG1 H 0.87 0.03 2 72 105 9 VAL HG2 H 0.89 0.03 2 73 105 9 VAL CA C 61.97 0.20 1 74 105 9 VAL CB C 32.92 0.20 1 75 105 9 VAL CG1 C 21.16 0.20 2 76 105 9 VAL CG2 C 20.65 0.20 2 77 105 9 VAL N N 124.66 0.20 1 78 106 10 ASP H H 8.48 0.03 1 79 106 10 ASP HA H 4.87 0.03 1 80 106 10 ASP HB2 H 2.56 0.03 2 81 106 10 ASP HB3 H 2.85 0.03 2 82 106 10 ASP CA C 52.03 0.20 1 83 106 10 ASP CB C 41.59 0.20 1 84 106 10 ASP N N 126.47 0.20 1 85 107 11 PRO HA H 4.41 0.03 1 86 107 11 PRO HB2 H 2.01 0.03 2 87 107 11 PRO HB3 H 2.30 0.03 2 88 107 11 PRO HG2 H 2.02 0.03 2 89 107 11 PRO HG3 H 2.02 0.03 2 90 107 11 PRO HD2 H 3.87 0.03 2 91 107 11 PRO HD3 H 3.89 0.03 2 92 107 11 PRO CA C 63.78 0.20 1 93 107 11 PRO CB C 32.18 0.20 1 94 107 11 PRO CG C 27.18 0.20 1 95 107 11 PRO CD C 51.05 0.20 1 96 108 12 ALA H H 8.41 0.03 1 97 108 12 ALA HA H 4.32 0.03 1 98 108 12 ALA HB H 1.38 0.03 1 99 108 12 ALA CA C 52.37 0.20 1 100 108 12 ALA CB C 19.33 0.20 1 101 108 12 ALA N N 122.17 0.20 1 102 109 13 THR H H 7.75 0.03 1 103 109 13 THR HA H 4.27 0.03 1 104 109 13 THR HB H 3.98 0.03 1 105 109 13 THR HG2 H 1.02 0.03 1 106 109 13 THR CA C 60.62 0.20 1 107 109 13 THR CB C 70.15 0.20 1 108 109 13 THR CG2 C 21.54 0.02 1 109 109 13 THR N N 117.03 0.20 1 110 110 14 PRO HA H 4.45 0.03 1 111 110 14 PRO HB2 H 0.91 0.03 2 112 110 14 PRO HB3 H 1.61 0.03 2 113 110 14 PRO HG2 H 1.45 0.03 2 114 110 14 PRO HG3 H 1.60 0.03 2 115 110 14 PRO HD2 H 3.37 0.03 2 116 110 14 PRO HD3 H 3.85 0.03 2 117 110 14 PRO CA C 62.10 0.20 1 118 110 14 PRO CB C 31.43 0.20 1 119 110 14 PRO CG C 27.19 0.20 1 120 110 14 PRO CD C 50.58 0.20 1 121 111 15 TYR H H 9.11 0.03 1 122 111 15 TYR HA H 4.77 0.03 1 123 111 15 TYR HB2 H 2.77 0.03 2 124 111 15 TYR HB3 H 3.03 0.03 2 125 111 15 TYR HD1 H 7.27 0.03 1 126 111 15 TYR HD2 H 7.27 0.03 1 127 111 15 TYR HE1 H 6.85 0.03 1 128 111 15 TYR HE2 H 6.85 0.03 1 129 111 15 TYR CA C 55.62 0.20 1 130 111 15 TYR CB C 39.24 0.20 1 131 111 15 TYR N N 123.25 0.20 1 132 112 16 PRO HA H 4.13 0.03 1 133 112 16 PRO HB2 H 1.89 0.03 2 134 112 16 PRO HB3 H 2.35 0.03 2 135 112 16 PRO HG2 H 1.92 0.03 2 136 112 16 PRO HG3 H 2.21 0.03 2 137 112 16 PRO HD2 H 3.92 0.03 2 138 112 16 PRO HD3 H 3.44 0.03 2 139 112 16 PRO CA C 64.71 0.20 1 140 112 16 PRO CB C 31.53 0.20 1 141 112 16 PRO CG C 28.24 0.20 1 142 112 16 PRO CD C 50.64 0.20 1 143 113 17 GLY H H 9.26 0.03 1 144 113 17 GLY HA2 H 3.53 0.03 2 145 113 17 GLY HA3 H 4.57 0.03 2 146 113 17 GLY CA C 44.93 0.20 1 147 113 17 GLY N N 114.38 0.20 1 148 114 18 ASP H H 8.76 0.03 1 149 114 18 ASP HA H 4.71 0.03 1 150 114 18 ASP HB2 H 2.62 0.03 2 151 114 18 ASP HB3 H 2.92 0.03 2 152 114 18 ASP CA C 55.41 0.20 1 153 114 18 ASP CB C 41.60 0.20 1 154 114 18 ASP N N 122.36 0.20 1 155 115 19 LYS H H 8.49 0.03 1 156 115 19 LYS HA H 4.99 0.03 1 157 115 19 LYS HB2 H 1.89 0.03 2 158 115 19 LYS HB3 H 1.89 0.03 2 159 115 19 LYS HG2 H 1.54 0.03 2 160 115 19 LYS HG3 H 1.74 0.03 2 161 115 19 LYS HD2 H 1.75 0.03 2 162 115 19 LYS HD3 H 1.75 0.03 2 163 115 19 LYS HE2 H 3.01 0.03 2 164 115 19 LYS HE3 H 3.01 0.03 2 165 115 19 LYS CA C 56.37 0.20 1 166 115 19 LYS CB C 33.54 0.20 1 167 115 19 LYS CG C 25.57 0.20 1 168 115 19 LYS CD C 29.27 0.20 1 169 115 19 LYS CE C 42.01 0.20 1 170 115 19 LYS N N 120.64 0.20 1 171 116 20 VAL H H 9.17 0.03 1 172 116 20 VAL HA H 5.24 0.03 1 173 116 20 VAL HB H 2.29 0.03 1 174 116 20 VAL HG1 H 0.86 0.03 2 175 116 20 VAL HG2 H 0.46 0.03 2 176 116 20 VAL CA C 58.30 0.20 1 177 116 20 VAL CB C 36.04 0.20 1 178 116 20 VAL CG1 C 20.67 0.20 2 179 116 20 VAL CG2 C 19.41 0.20 2 180 116 20 VAL N N 116.49 0.20 1 181 117 21 ILE H H 9.20 0.03 1 182 117 21 ILE HA H 5.13 0.03 1 183 117 21 ILE HB H 1.67 0.03 1 184 117 21 ILE HG12 H 1.35 0.03 2 185 117 21 ILE HG13 H 1.17 0.03 2 186 117 21 ILE HG2 H 0.92 0.03 1 187 117 21 ILE HD1 H 0.89 0.03 1 188 117 21 ILE CA C 57.80 0.20 1 189 117 21 ILE CB C 42.47 0.20 1 190 117 21 ILE CG1 C 28.73 0.20 1 191 117 21 ILE CG2 C 16.71 0.20 1 192 117 21 ILE CD1 C 14.03 0.20 1 193 117 21 ILE N N 118.71 0.20 1 194 118 22 ILE H H 8.45 0.03 1 195 118 22 ILE HA H 4.62 0.03 1 196 118 22 ILE HB H 2.30 0.03 1 197 118 22 ILE HG12 H 0.92 0.03 2 198 118 22 ILE HG13 H 1.67 0.03 2 199 118 22 ILE HG2 H 1.25 0.03 1 200 118 22 ILE HD1 H 0.85 0.03 1 201 118 22 ILE CA C 62.15 0.20 1 202 118 22 ILE CB C 37.21 0.20 1 203 118 22 ILE CG1 C 29.08 0.20 1 204 118 22 ILE CG2 C 18.86 0.20 1 205 118 22 ILE CD1 C 14.83 0.20 1 206 118 22 ILE N N 128.23 0.20 1 207 119 23 THR H H 9.30 0.03 1 208 119 23 THR HA H 4.53 0.03 1 209 119 23 THR HB H 4.48 0.03 1 210 119 23 THR HG2 H 1.14 0.03 1 211 119 23 THR CA C 62.52 0.20 1 212 119 23 THR CB C 69.07 0.20 1 213 119 23 THR CG2 C 22.45 0.20 1 214 119 23 THR N N 120.31 0.20 1 215 120 24 GLU H H 7.55 0.03 1 216 120 24 GLU HA H 4.75 0.03 1 217 120 24 GLU HB2 H 1.93 0.03 2 218 120 24 GLU HB3 H 2.11 0.03 2 219 120 24 GLU HG2 H 2.20 0.03 2 220 120 24 GLU HG3 H 2.29 0.03 2 221 120 24 GLU CA C 55.44 0.20 1 222 120 24 GLU CB C 34.54 0.20 1 223 120 24 GLU CG C 36.13 0.20 1 224 120 24 GLU N N 119.29 0.20 1 225 121 25 GLY H H 8.72 0.03 1 226 121 25 GLY HA2 H 4.40 0.03 2 227 121 25 GLY HA3 H 3.85 0.03 2 228 121 25 GLY CA C 44.72 0.20 1 229 121 25 GLY N N 107.37 0.20 1 230 122 26 ALA H H 8.71 0.03 1 231 122 26 ALA HA H 3.87 0.03 1 232 122 26 ALA HB H 0.93 0.03 1 233 122 26 ALA CA C 54.75 0.20 1 234 122 26 ALA CB C 18.39 0.20 1 235 122 26 ALA N N 124.04 0.20 1 236 123 27 PHE H H 9.01 0.03 1 237 123 27 PHE HA H 4.47 0.03 1 238 123 27 PHE HB2 H 2.79 0.03 2 239 123 27 PHE HB3 H 3.12 0.03 2 240 123 27 PHE HD1 H 6.42 0.03 1 241 123 27 PHE HD2 H 6.42 0.03 1 242 123 27 PHE HE1 H 6.66 0.03 1 243 123 27 PHE HE2 H 6.66 0.03 1 244 123 27 PHE HZ H 6.68 0.03 1 245 123 27 PHE CA C 56.27 0.20 1 246 123 27 PHE CB C 37.99 0.20 1 247 123 27 PHE N N 114.38 0.20 1 248 124 28 GLU H H 7.23 0.03 1 249 124 28 GLU HA H 3.44 0.03 1 250 124 28 GLU HB2 H 1.88 0.03 2 251 124 28 GLU HB3 H 1.96 0.03 2 252 124 28 GLU HG2 H 2.04 0.03 2 253 124 28 GLU HG3 H 2.07 0.03 2 254 124 28 GLU CA C 58.91 0.20 1 255 124 28 GLU CB C 29.12 0.20 1 256 124 28 GLU CG C 35.44 0.20 1 257 124 28 GLU N N 119.73 0.20 1 258 125 29 GLY H H 8.97 0.03 1 259 125 29 GLY HA2 H 3.66 0.03 2 260 125 29 GLY HA3 H 4.34 0.03 2 261 125 29 GLY CA C 45.12 0.20 1 262 125 29 GLY N N 114.21 0.20 1 263 126 30 PHE H H 8.52 0.03 1 264 126 30 PHE HA H 4.62 0.03 1 265 126 30 PHE HB2 H 3.02 0.03 2 266 126 30 PHE HB3 H 3.54 0.03 2 267 126 30 PHE HD1 H 7.41 0.03 1 268 126 30 PHE HD2 H 7.41 0.03 1 269 126 30 PHE HE1 H 7.47 0.03 1 270 126 30 PHE HE2 H 7.47 0.03 1 271 126 30 PHE HZ H 7.40 0.03 1 272 126 30 PHE CA C 58.62 0.20 1 273 126 30 PHE CB C 38.96 0.20 1 274 126 30 PHE N N 120.87 0.20 1 275 127 31 GLN H H 8.68 0.03 1 276 127 31 GLN HA H 5.19 0.03 1 277 127 31 GLN HB2 H 2.08 0.03 2 278 127 31 GLN HB3 H 2.20 0.03 2 279 127 31 GLN HG2 H 2.35 0.03 2 280 127 31 GLN HG3 H 2.61 0.03 2 281 127 31 GLN HE21 H 7.46 0.03 1 282 127 31 GLN HE22 H 6.88 0.03 1 283 127 31 GLN CA C 55.02 0.20 1 284 127 31 GLN CB C 30.39 0.20 1 285 127 31 GLN CG C 34.97 0.20 1 286 127 31 GLN N N 119.76 0.20 1 287 127 31 GLN NE2 N 110.94 0.20 1 288 128 32 ALA H H 8.97 0.03 1 289 128 32 ALA HA H 5.01 0.03 1 290 128 32 ALA HB H 1.14 0.03 1 291 128 32 ALA CA C 50.57 0.20 1 292 128 32 ALA CB C 25.07 0.20 1 293 128 32 ALA N N 123.16 0.20 1 294 129 33 ILE H H 8.35 0.03 1 295 129 33 ILE HA H 4.89 0.03 1 296 129 33 ILE HB H 1.76 0.03 1 297 129 33 ILE HG12 H 1.54 0.03 2 298 129 33 ILE HG13 H 1.23 0.03 2 299 129 33 ILE HG2 H 0.79 0.03 1 300 129 33 ILE HD1 H 0.84 0.03 1 301 129 33 ILE CA C 58.85 0.20 1 302 129 33 ILE CB C 40.78 0.20 1 303 129 33 ILE CG1 C 27.49 0.20 1 304 129 33 ILE CG2 C 17.20 0.20 1 305 129 33 ILE CD1 C 12.27 0.20 1 306 129 33 ILE N N 118.58 0.20 1 307 130 34 PHE H H 9.10 0.03 1 308 130 34 PHE HA H 4.31 0.03 1 309 130 34 PHE HB2 H 2.62 0.03 2 310 130 34 PHE HB3 H 3.08 0.03 2 311 130 34 PHE HD1 H 6.77 0.03 1 312 130 34 PHE HD2 H 6.77 0.03 1 313 130 34 PHE HE1 H 7.14 0.03 1 314 130 34 PHE HE2 H 7.14 0.03 1 315 130 34 PHE HZ H 7.07 0.03 1 316 130 34 PHE CA C 58.53 0.20 1 317 130 34 PHE CB C 39.28 0.20 1 318 130 34 PHE N N 127.46 0.20 1 319 131 35 THR H H 7.86 0.03 1 320 131 35 THR HA H 4.51 0.03 1 321 131 35 THR HB H 3.85 0.03 1 322 131 35 THR HG2 H 1.02 0.03 1 323 131 35 THR CA C 63.18 0.20 1 324 131 35 THR CB C 69.17 0.20 1 325 131 35 THR CG2 C 22.31 0.20 1 326 131 35 THR N N 120.74 0.20 1 327 132 36 GLU H H 6.76 0.03 1 328 132 36 GLU HA H 4.57 0.03 1 329 132 36 GLU HB2 H 2.01 0.03 2 330 132 36 GLU HB3 H 2.26 0.03 2 331 132 36 GLU HG2 H 2.01 0.03 2 332 132 36 GLU HG3 H 2.08 0.03 2 333 132 36 GLU CA C 54.72 0.20 1 334 132 36 GLU CB C 29.42 0.20 1 335 132 36 GLU CG C 34.36 0.20 1 336 132 36 GLU N N 116.17 0.20 1 337 133 37 PRO HA H 4.78 0.03 1 338 133 37 PRO HB2 H 2.17 0.03 2 339 133 37 PRO HB3 H 2.74 0.03 2 340 133 37 PRO HG2 H 2.21 0.03 2 341 133 37 PRO HG3 H 2.21 0.03 2 342 133 37 PRO HD2 H 3.85 0.03 2 343 133 37 PRO HD3 H 3.88 0.03 2 344 133 37 PRO CA C 63.56 0.20 1 345 133 37 PRO CB C 32.69 0.20 1 346 133 37 PRO CG C 27.73 0.20 1 347 133 37 PRO CD C 51.02 0.20 1 348 134 38 ASP H H 8.65 0.03 1 349 134 38 ASP HA H 4.90 0.03 1 350 134 38 ASP HB2 H 2.10 0.03 2 351 134 38 ASP HB3 H 2.26 0.03 2 352 134 38 ASP CA C 52.27 0.20 1 353 134 38 ASP CB C 41.48 0.20 1 354 134 38 ASP N N 123.84 0.20 1 355 135 39 GLY H H 8.10 0.03 1 356 135 39 GLY HA2 H 4.24 0.03 2 357 135 39 GLY HA3 H 3.74 0.03 2 358 135 39 GLY CA C 44.79 0.20 1 359 135 39 GLY N N 108.76 0.20 1 360 136 40 GLU H H 8.47 0.03 1 361 136 40 GLU HA H 4.21 0.03 1 362 136 40 GLU HB2 H 2.03 0.03 2 363 136 40 GLU HB3 H 2.08 0.03 2 364 136 40 GLU HG2 H 2.31 0.03 2 365 136 40 GLU HG3 H 2.31 0.03 2 366 136 40 GLU CA C 58.10 0.20 1 367 136 40 GLU CB C 30.39 0.20 1 368 136 40 GLU CG C 36.37 0.20 1 369 136 40 GLU N N 117.70 0.20 1 370 137 41 ALA H H 8.73 0.03 1 371 137 41 ALA HA H 4.68 0.03 1 372 137 41 ALA HB H 1.50 0.03 1 373 137 41 ALA CA C 52.07 0.20 1 374 137 41 ALA CB C 21.17 0.20 1 375 137 41 ALA N N 119.36 0.20 1 376 138 42 ARG H H 7.05 0.03 1 377 138 42 ARG HA H 5.11 0.03 1 378 138 42 ARG HB2 H 1.85 0.03 2 379 138 42 ARG HB3 H 2.05 0.03 2 380 138 42 ARG HG2 H 1.23 0.03 2 381 138 42 ARG HG3 H 1.67 0.03 2 382 138 42 ARG HD2 H 2.87 0.03 2 383 138 42 ARG HD3 H 3.30 0.03 2 384 138 42 ARG CA C 55.07 0.20 1 385 138 42 ARG CB C 34.99 0.20 1 386 138 42 ARG CG C 28.26 0.20 1 387 138 42 ARG CD C 43.25 0.20 1 388 138 42 ARG N N 117.66 0.20 1 389 139 43 SER H H 9.38 0.03 1 390 139 43 SER HA H 4.87 0.03 1 391 139 43 SER HB2 H 3.63 0.03 2 392 139 43 SER HB3 H 3.67 0.03 2 393 139 43 SER CA C 59.15 0.20 1 394 139 43 SER CB C 67.99 0.20 1 395 139 43 SER N N 115.71 0.20 1 396 140 44 MET H H 9.14 0.03 1 397 140 44 MET HA H 4.87 0.03 1 398 140 44 MET HB2 H 1.63 0.03 2 399 140 44 MET HB3 H 1.98 0.03 2 400 140 44 MET HG2 H 2.00 0.03 2 401 140 44 MET HG3 H 2.39 0.03 2 402 140 44 MET HE H 1.85 0.03 1 403 140 44 MET CA C 53.45 0.20 1 404 140 44 MET CB C 30.70 0.20 1 405 140 44 MET CG C 31.43 0.20 1 406 140 44 MET CE C 15.92 0.20 1 407 140 44 MET N N 120.59 0.20 1 408 141 45 LEU H H 8.93 0.03 1 409 141 45 LEU HA H 4.99 0.03 1 410 141 45 LEU HB2 H 0.97 0.03 2 411 141 45 LEU HB3 H 1.53 0.03 2 412 141 45 LEU HG H 1.38 0.03 1 413 141 45 LEU HD1 H 0.25 0.03 2 414 141 45 LEU HD2 H 0.13 0.03 2 415 141 45 LEU CA C 52.27 0.20 1 416 141 45 LEU CB C 44.21 0.20 1 417 141 45 LEU CG C 26.94 0.20 1 418 141 45 LEU CD1 C 25.87 0.20 2 419 141 45 LEU CD2 C 23.13 0.20 2 420 141 45 LEU N N 127.06 0.20 1 421 142 46 LEU H H 9.15 0.03 1 422 142 46 LEU HA H 4.90 0.03 1 423 142 46 LEU HB2 H 1.25 0.03 2 424 142 46 LEU HB3 H 1.66 0.03 2 425 142 46 LEU HG H 1.27 0.03 1 426 142 46 LEU HD1 H 0.73 0.03 2 427 142 46 LEU HD2 H 0.71 0.03 2 428 142 46 LEU CA C 53.65 0.20 1 429 142 46 LEU CB C 43.88 0.20 1 430 142 46 LEU CG C 27.16 0.20 1 431 142 46 LEU CD1 C 25.02 0.20 2 432 142 46 LEU CD2 C 24.38 0.20 2 433 142 46 LEU N N 122.56 0.20 1 434 143 47 LEU H H 9.25 0.03 1 435 143 47 LEU HA H 4.55 0.03 1 436 143 47 LEU HB2 H 1.29 0.03 2 437 143 47 LEU HB3 H 1.38 0.03 2 438 143 47 LEU HG H 1.29 0.03 1 439 143 47 LEU HD1 H 0.21 0.03 2 440 143 47 LEU HD2 H 0.19 0.03 2 441 143 47 LEU CA C 55.15 0.20 1 442 143 47 LEU CB C 44.33 0.20 1 443 143 47 LEU CG C 28.03 0.20 1 444 143 47 LEU CD1 C 25.72 0.20 2 445 143 47 LEU CD2 C 25.33 0.20 2 446 143 47 LEU N N 129.21 0.20 1 447 144 48 ASN H H 8.75 0.03 1 448 144 48 ASN HA H 4.99 0.03 1 449 144 48 ASN HB2 H 2.70 0.03 2 450 144 48 ASN HB3 H 2.89 0.03 2 451 144 48 ASN HD21 H 7.50 0.03 1 452 144 48 ASN HD22 H 6.80 0.03 1 453 144 48 ASN CA C 52.91 0.20 1 454 144 48 ASN CB C 39.02 0.20 1 455 144 48 ASN N N 120.92 0.20 1 456 144 48 ASN ND2 N 111.01 0.20 1 457 145 49 LEU H H 8.36 0.03 1 458 145 49 LEU HA H 4.66 0.03 1 459 145 49 LEU HB2 H 1.58 0.03 2 460 145 49 LEU HB3 H 1.68 0.03 2 461 145 49 LEU HG H 1.45 0.03 1 462 145 49 LEU HD1 H 0.76 0.03 2 463 145 49 LEU HD2 H 0.65 0.03 2 464 145 49 LEU CA C 53.70 0.20 1 465 145 49 LEU CB C 42.10 0.20 1 466 145 49 LEU CG C 26.89 0.20 1 467 145 49 LEU CD1 C 25.67 0.20 2 468 145 49 LEU CD2 C 23.74 0.20 2 469 145 49 LEU N N 125.56 0.20 1 470 146 50 ILE H H 8.62 0.03 1 471 146 50 ILE HA H 3.63 0.03 1 472 146 50 ILE HB H 2.33 0.03 1 473 146 50 ILE HG12 H 1.53 0.03 2 474 146 50 ILE HG13 H 1.19 0.03 2 475 146 50 ILE HG2 H 0.93 0.03 1 476 146 50 ILE HD1 H 0.89 0.03 1 477 146 50 ILE CA C 64.56 0.20 1 478 146 50 ILE CB C 35.57 0.20 1 479 146 50 ILE CG1 C 27.87 0.20 1 480 146 50 ILE CG2 C 17.99 0.20 1 481 146 50 ILE CD1 C 12.29 0.20 1 482 146 50 ILE N N 119.42 0.20 1 483 147 51 ASN H H 8.59 0.03 1 484 147 51 ASN HA H 4.62 0.03 1 485 147 51 ASN HB2 H 2.91 0.03 2 486 147 51 ASN HB3 H 2.97 0.03 2 487 147 51 ASN HD21 H 7.61 0.03 1 488 147 51 ASN HD22 H 6.89 0.03 1 489 147 51 ASN CA C 53.70 0.20 1 490 147 51 ASN CB C 38.31 0.20 1 491 147 51 ASN N N 116.70 0.20 1 492 147 51 ASN ND2 N 112.40 0.20 1 493 148 52 LYS H H 7.49 0.03 1 494 148 52 LYS HA H 4.51 0.03 1 495 148 52 LYS HB2 H 1.73 0.03 2 496 148 52 LYS HB3 H 1.85 0.03 2 497 148 52 LYS HG2 H 1.24 0.03 2 498 148 52 LYS HG3 H 1.35 0.03 2 499 148 52 LYS HD2 H 1.65 0.03 2 500 148 52 LYS HD3 H 1.65 0.03 2 501 148 52 LYS HE2 H 2.97 0.03 2 502 148 52 LYS HE3 H 2.97 0.03 2 503 148 52 LYS CA C 55.48 0.20 1 504 148 52 LYS CB C 34.73 0.20 1 505 148 52 LYS CG C 23.92 0.20 1 506 148 52 LYS CD C 29.26 0.20 1 507 148 52 LYS CE C 42.19 0.20 1 508 148 52 LYS N N 117.61 0.20 1 509 149 53 GLU H H 8.37 0.03 1 510 149 53 GLU HA H 5.07 0.03 1 511 149 53 GLU HB2 H 1.83 0.03 2 512 149 53 GLU HB3 H 1.86 0.03 2 513 149 53 GLU HG2 H 2.01 0.03 2 514 149 53 GLU HG3 H 2.13 0.03 2 515 149 53 GLU CA C 55.35 0.20 1 516 149 53 GLU CB C 31.64 0.20 1 517 149 53 GLU CG C 36.97 0.20 1 518 149 53 GLU N N 121.92 0.20 1 519 150 54 ILE H H 8.62 0.03 1 520 150 54 ILE HA H 4.51 0.03 1 521 150 54 ILE HB H 1.68 0.03 1 522 150 54 ILE HG12 H 1.26 0.03 2 523 150 54 ILE HG13 H 0.90 0.03 2 524 150 54 ILE HG2 H 0.72 0.03 1 525 150 54 ILE HD1 H 0.67 0.03 1 526 150 54 ILE CA C 59.35 0.20 1 527 150 54 ILE CB C 41.70 0.20 1 528 150 54 ILE CG1 C 26.80 0.20 1 529 150 54 ILE CG2 C 17.58 0.20 1 530 150 54 ILE CD1 C 13.66 0.20 1 531 150 54 ILE N N 121.39 0.20 1 532 151 55 LYS H H 8.34 0.03 1 533 151 55 LYS HA H 5.16 0.03 1 534 151 55 LYS HB2 H 1.57 0.03 2 535 151 55 LYS HB3 H 1.62 0.03 2 536 151 55 LYS HG2 H 1.14 0.03 2 537 151 55 LYS HG3 H 1.31 0.03 2 538 151 55 LYS HD2 H 1.57 0.03 2 539 151 55 LYS HD3 H 1.57 0.03 2 540 151 55 LYS HE2 H 2.85 0.03 2 541 151 55 LYS HE3 H 2.85 0.03 2 542 151 55 LYS CA C 55.18 0.20 1 543 151 55 LYS CB C 33.67 0.20 1 544 151 55 LYS CG C 25.74 0.20 1 545 151 55 LYS CD C 29.54 0.20 1 546 151 55 LYS CE C 41.65 0.20 1 547 151 55 LYS N N 125.05 0.20 1 548 152 56 HIS H H 9.10 0.03 1 549 152 56 HIS HA H 4.73 0.03 1 550 152 56 HIS HB2 H 2.40 0.03 2 551 152 56 HIS HB3 H 2.63 0.03 2 552 152 56 HIS HE1 H 7.76 0.03 1 553 152 56 HIS CA C 55.49 0.20 1 554 152 56 HIS CB C 35.67 0.20 1 555 152 56 HIS N N 125.55 0.20 1 556 153 57 SER H H 8.10 0.03 1 557 153 57 SER HA H 5.06 0.03 1 558 153 57 SER HB2 H 3.64 0.03 2 559 153 57 SER HB3 H 3.68 0.03 2 560 153 57 SER CA C 57.05 0.20 1 561 153 57 SER CB C 62.51 0.20 1 562 153 57 SER N N 119.92 0.20 1 563 154 58 VAL H H 9.29 0.03 1 564 154 58 VAL HA H 4.56 0.03 1 565 154 58 VAL HB H 2.09 0.03 1 566 154 58 VAL HG1 H 1.33 0.03 2 567 154 58 VAL HG2 H 0.94 0.03 2 568 154 58 VAL CA C 60.64 0.20 1 569 154 58 VAL CB C 35.61 0.20 1 570 154 58 VAL CG1 C 22.47 0.20 2 571 154 58 VAL CG2 C 21.80 0.20 2 572 154 58 VAL N N 129.40 0.20 1 573 155 59 LYS H H 8.78 0.03 1 574 155 59 LYS HA H 4.38 0.03 1 575 155 59 LYS HB2 H 1.70 0.03 2 576 155 59 LYS HB3 H 1.93 0.03 2 577 155 59 LYS HG2 H 1.54 0.03 2 578 155 59 LYS HG3 H 1.62 0.03 2 579 155 59 LYS HD2 H 1.58 0.03 2 580 155 59 LYS HD3 H 1.71 0.03 2 581 155 59 LYS HE2 H 2.97 0.03 2 582 155 59 LYS HE3 H 2.97 0.03 2 583 155 59 LYS CA C 58.28 0.20 1 584 155 59 LYS CB C 33.62 0.20 1 585 155 59 LYS CG C 25.86 0.20 1 586 155 59 LYS CD C 29.59 0.20 1 587 155 59 LYS CE C 41.81 0.20 1 588 155 59 LYS N N 124.78 0.20 1 589 156 60 ASN H H 8.48 0.03 1 590 156 60 ASN HA H 4.55 0.03 1 591 156 60 ASN HB2 H 2.64 0.03 2 592 156 60 ASN HB3 H 2.69 0.03 2 593 156 60 ASN HD21 H 7.27 0.03 1 594 156 60 ASN HD22 H 7.11 0.03 1 595 156 60 ASN CA C 55.30 0.20 1 596 156 60 ASN CB C 36.92 0.20 1 597 156 60 ASN N N 122.16 0.20 1 598 156 60 ASN ND2 N 109.20 0.20 1 599 157 61 THR H H 7.06 0.03 1 600 157 61 THR HA H 4.19 0.03 1 601 157 61 THR HB H 4.48 0.03 1 602 157 61 THR HG2 H 1.23 0.03 1 603 157 61 THR CA C 62.07 0.20 1 604 157 61 THR CB C 68.36 0.20 1 605 157 61 THR CG2 C 22.45 0.20 1 606 157 61 THR N N 104.53 0.20 1 607 158 62 GLU H H 7.99 0.03 1 608 158 62 GLU HA H 4.32 0.03 1 609 158 62 GLU HB2 H 2.31 0.03 2 610 158 62 GLU HB3 H 2.55 0.03 2 611 158 62 GLU HG2 H 2.04 0.03 2 612 158 62 GLU HG3 H 2.21 0.03 2 613 158 62 GLU CA C 56.26 0.20 1 614 158 62 GLU CB C 29.10 0.20 1 615 158 62 GLU CG C 37.55 0.20 1 616 158 62 GLU N N 119.56 0.20 1 617 159 63 PHE H H 7.07 0.03 1 618 159 63 PHE HA H 5.66 0.03 1 619 159 63 PHE HB2 H 2.90 0.03 2 620 159 63 PHE HB3 H 2.95 0.03 2 621 159 63 PHE HD1 H 6.95 0.03 1 622 159 63 PHE HD2 H 6.95 0.03 1 623 159 63 PHE HE1 H 7.17 0.03 1 624 159 63 PHE HE2 H 7.17 0.03 1 625 159 63 PHE HZ H 7.25 0.03 1 626 159 63 PHE CA C 56.06 0.20 1 627 159 63 PHE CB C 42.29 0.20 1 628 159 63 PHE N N 111.58 0.20 1 629 160 64 ARG H H 8.95 0.03 1 630 160 64 ARG HA H 4.74 0.03 1 631 160 64 ARG HB2 H 1.70 0.03 2 632 160 64 ARG HB3 H 1.81 0.03 2 633 160 64 ARG HG2 H 1.54 0.03 2 634 160 64 ARG HG3 H 1.54 0.03 2 635 160 64 ARG HD2 H 3.17 0.03 2 636 160 64 ARG HD3 H 3.17 0.03 2 637 160 64 ARG CA C 53.86 0.20 1 638 160 64 ARG CB C 33.74 0.20 1 639 160 64 ARG CG C 26.53 0.20 1 640 160 64 ARG CD C 43.44 0.20 1 641 160 64 ARG N N 116.43 0.20 1 642 161 65 LYS H H 8.99 0.03 1 643 161 65 LYS HA H 4.38 0.03 1 644 161 65 LYS HB2 H 1.66 0.03 2 645 161 65 LYS HB3 H 1.93 0.03 2 646 161 65 LYS HG2 H 1.55 0.03 2 647 161 65 LYS HG3 H 1.66 0.03 2 648 161 65 LYS HD2 H 1.55 0.03 2 649 161 65 LYS HD3 H 1.70 0.03 2 650 161 65 LYS HE2 H 3.01 0.03 2 651 161 65 LYS HE3 H 3.01 0.03 2 652 161 65 LYS CA C 58.22 0.20 1 653 161 65 LYS CB C 33.83 0.20 1 654 161 65 LYS CG C 26.44 0.20 1 655 161 65 LYS CD C 29.70 0.20 1 656 161 65 LYS CE C 42.10 0.20 1 657 161 65 LYS N N 123.14 0.20 1 658 162 66 LEU H H 7.93 0.03 1 659 162 66 LEU HA H 4.16 0.03 1 660 162 66 LEU HB2 H 1.36 0.03 2 661 162 66 LEU HB3 H 1.55 0.03 2 662 162 66 LEU HG H 1.55 0.03 1 663 162 66 LEU HD1 H 0.87 0.03 2 664 162 66 LEU HD2 H 0.89 0.03 2 665 162 66 LEU CA C 57.32 0.20 1 666 162 66 LEU CB C 43.63 0.20 1 667 162 66 LEU CG C 27.67 0.20 1 668 162 66 LEU CD1 C 25.54 0.20 2 669 162 66 LEU CD2 C 24.31 0.20 2 670 162 66 LEU N N 131.26 0.20 1 stop_ save_