data_4136 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical Shift Assignments, 3JHNHA Coupling Constants and Secondary Structure of E.coli Multidrug Resistance Protein (EmrE) ; _BMRB_accession_number 4136 _BMRB_flat_file_name bmr4136.str _Entry_type original _Submission_date 1998-04-23 _Accession_date 1998-04-23 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; The data presented are for the integral membrane protein E. Coli multidrug resistance protein E (EmrE), a proton-coupled mulitdrug antiporter. A mixed solvent system (chloroform:methanol:water 6:6:1 by volume) has been used to overcome the problems of low aqueous solubility. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schwaiger Manfred . . 2 Lebendiker Mario . . 3 Yerushalmi Hagit . . 4 Coles Murray . . 5 Groeger Adriane . . 6 Schwarz Christian . . 7 Schuldiner Shimon . . 8 Kessler Horst . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 599 "13C chemical shifts" 283 "15N chemical shifts" 113 "coupling constants" 73 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1998-07-02 update author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Schwaiger, M., Lebendiker, M., Yerushalmi, H., Coles, M., Groeger, A., Schwarz, C., Schuldiner, S., Horst, K. , "NMR-Investigations of the Multidrug Transporter EmrE, an Integral Membrane Protein," Eur. J. Biochem. 254, 610-619 (1998). ; _Citation_title ; NMR-Investigations of the Multidrug Transporter EmrE, an Integral Membrane Protein ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98351559 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schwaiger Manfred . . 2 Lebendiker Mario . . 3 Yerushalmi Hagit . . 4 Coles Murray . . 5 Groeger Adriane . . 6 Schwarz Christian . . 7 Schuldiner Shimon . . 8 Kessler Horst . . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_volume . _Journal_issue 254 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 610 _Page_last 619 _Year 1998 _Details . loop_ _Keyword 'coupling constants' EmrE 'integral membrane protein' 'mulitdrug antiporter' 'multidrug resitance' NMR protein 'resonance assignment' 'secondary structure' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_1 _Saveframe_category citation _Citation_full ; Schwaiger, M., Riemer,C., Kessler,H. (1998) Random coil 1H and 13C chemical shifts in chloroform/methanol mixtures. Submitted for publication ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_EmrE _Saveframe_category molecular_system _Mol_system_name 'E. coli multidrug resistance protein E' _Abbreviation_common EmrE _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label EmrE $EmrE stop_ _System_molecular_weight 12000 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'multidrug antiporter' 'multidrug resistance' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_EmrE _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'E. coli Multidrug resistance protein E' _Abbreviation_common EmrE _Molecular_mass 12000 _Mol_thiol_state . _Details 'Disulphide bridging pattern (if any) is unknown' ############################## # Polymer residue sequence # ############################## _Residue_count 110 _Mol_residue_sequence ; MNPYIYLGGAILAEVIGTTL MKFSEGFTRLWPSVGTIICY CASFWLLAQTLAYIPTGIAY AIWSGVGIVLISLLSWGFFG QRLDLPAIIGMMLICAGVLI INLLSRSTPH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASN 3 PRO 4 TYR 5 ILE 6 TYR 7 LEU 8 GLY 9 GLY 10 ALA 11 ILE 12 LEU 13 ALA 14 GLU 15 VAL 16 ILE 17 GLY 18 THR 19 THR 20 LEU 21 MET 22 LYS 23 PHE 24 SER 25 GLU 26 GLY 27 PHE 28 THR 29 ARG 30 LEU 31 TRP 32 PRO 33 SER 34 VAL 35 GLY 36 THR 37 ILE 38 ILE 39 CYS 40 TYR 41 CYS 42 ALA 43 SER 44 PHE 45 TRP 46 LEU 47 LEU 48 ALA 49 GLN 50 THR 51 LEU 52 ALA 53 TYR 54 ILE 55 PRO 56 THR 57 GLY 58 ILE 59 ALA 60 TYR 61 ALA 62 ILE 63 TRP 64 SER 65 GLY 66 VAL 67 GLY 68 ILE 69 VAL 70 LEU 71 ILE 72 SER 73 LEU 74 LEU 75 SER 76 TRP 77 GLY 78 PHE 79 PHE 80 GLY 81 GLN 82 ARG 83 LEU 84 ASP 85 LEU 86 PRO 87 ALA 88 ILE 89 ILE 90 GLY 91 MET 92 MET 93 LEU 94 ILE 95 CYS 96 ALA 97 GLY 98 VAL 99 LEU 100 ILE 101 ILE 102 ASN 103 LEU 104 LEU 105 SER 106 ARG 107 SER 108 THR 109 PRO 110 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-25 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 2I68 "Cryo-Em Based Theoretical Model Structure Of Transmembrane Domain Of The Multidrug-Resistance Antiporter From E. Coli Emre" 100.00 137 100.00 100.00 4.72e-71 PDB 3B5D "Emre Multidrug Transporter In Complex With Tpp, C2 Crystal Form" 100.00 110 100.00 100.00 3.58e-70 PDB 3B61 "Emre Multidrug Transporter, Apo Crystal Form" 100.00 110 100.00 100.00 3.58e-70 PDB 3B62 "Emre Multidrug Transporter In Complex With P4p, P21 Crystal Form" 100.00 110 100.00 100.00 3.58e-70 DBJ BAB35037 "integral membrane drug resistance protein EmrE [Escherichia coli O157:H7 str. Sakai]" 100.00 110 98.18 100.00 6.73e-70 DBJ BAE76318 "multidrug resistance protein [Escherichia coli str. K12 substr. W3110]" 100.00 110 100.00 100.00 3.58e-70 DBJ BAG76102 "hypothetical phage protein [Escherichia coli SE11]" 100.00 110 99.09 100.00 4.85e-70 DBJ BAG77691 "conserved hypothetical protein [Escherichia coli SE11]" 100.00 165 98.18 99.09 4.40e-69 DBJ BAI36380 "integral membrane drug resistance protein EmrE [Escherichia coli O111:H- str. 11128]" 100.00 110 98.18 99.09 2.28e-69 EMBL CAA77936 "ethidium resistance [Escherichia coli]" 100.00 110 100.00 100.00 3.58e-70 EMBL CAP75647 "Multidrug transporter emrE [Escherichia coli LF82]" 100.00 110 99.09 100.00 4.85e-70 EMBL CAP76416 "Multidrug transporter emrE [Escherichia coli LF82]" 100.00 117 98.18 99.09 1.27e-69 EMBL CAQ31015 "EmrE SMR transporter [Escherichia coli BL21(DE3)]" 100.00 110 97.27 98.18 2.78e-68 EMBL CAR03289 "putative multidrug resistance protein; DLP12 prophage [Escherichia coli S88]" 100.00 170 98.18 99.09 6.42e-69 GB AAA24190 "MvrC [Escherichia coli]" 100.00 110 100.00 100.00 3.58e-70 GB AAB40740 "methyl viologen resistance protein C [Escherichia coli]" 100.00 110 100.00 100.00 3.58e-70 GB AAC73644 "DLP12 prophage; multidrug resistance protein [Escherichia coli str. K-12 substr. MG1655]" 100.00 110 100.00 100.00 3.58e-70 GB AAG55967 "methylviologen resistance protein encoded within prophage CP-933X [Escherichia coli O157:H7 str. EDL933]" 100.00 110 98.18 100.00 6.73e-70 GB AAN43529 "resistance protein [Shigella flexneri 2a str. 301]" 100.00 110 98.18 99.09 2.28e-69 PRF 1803250A "ethidium efflux gene" 100.00 110 100.00 100.00 3.58e-70 REF NP_309641 "multidrug efflux protein [Escherichia coli O157:H7 str. Sakai]" 100.00 110 98.18 100.00 6.73e-70 REF NP_415075 "DLP12 prophage; multidrug resistance protein [Escherichia coli str. K-12 substr. MG1655]" 100.00 110 100.00 100.00 3.58e-70 REF NP_707822 "multidrug efflux protein [Shigella flexneri 2a str. 301]" 100.00 110 98.18 99.09 2.28e-69 REF WP_001070433 "multidrug SMR transporter [Escherichia coli]" 100.00 110 97.27 99.09 7.75e-69 REF WP_001070437 "hypothetical protein, partial [Escherichia coli]" 65.45 72 100.00 100.00 2.42e-41 SP P23895 "RecName: Full=Multidrug transporter EmrE; AltName: Full=Efflux-multidrug resistance protein EmrE; AltName: Full=Ethidium resist" 100.00 110 100.00 100.00 3.58e-70 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $EmrE 'E. coli' 562 Eubacteria . 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_type _Vector_name _Details $EmrE 'recombinant technology' 'E. coli' Escherichia coli . plasmid pKK56 'Expression controlled with the lac promoter' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details ; Mixed solvent Chloroform:methanol:water 6:6:1 (v:v:v) 15N labelled several samples of this type used. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling EmrE 2.0 mM [U-15N] 'ammonium acetate' 200 mM . D-chloroform 46.2 % . D3-methanol 46.2 % . H2O 7.6 % . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details 'Mixed solvent Chloroform:methanol:water 6:6:1 (v:v:v) 15N,13C' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling EmrE 1.5 mM '[U-15N; U-13C]' 'ammonium acetate' 200 mM . D-chloroform 46.2 % . D3-methanol 46.2 % . H2O 7.6 % . stop_ save_ save_sample_three _Saveframe_category sample _Sample_type solution _Details 'Mixed solvent Chloroform:methanol:water 6:6:1 (v:v:v) 15N,13C,75%-2H' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling EmrE 1.0 mM '[U-15N; U-13C; U-75% 2H]' 'ammonium acetate' 200 mM . D-chloroform 46.2 % . D3-methanol 46.2 % . H2O 7.6 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX750 _Field_strength 750 _Details 'four channel, three gradient, triple resonance' save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX600 _Field_strength 600 _Details 'four channel, three gradient, triple resonance' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.2 . n/a temperature 300 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference _Details 'Internal TMS referencing for proton, 15N and 13C by frequency ratio' 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 TMS C 13 . ppm 0.0 . indirect . . . 0.25144953 TMS H 1 methyl ppm 0.0 internal direct . . . . TMS N 15 . ppm 0.0 . indirect . . . 0.10132912 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_chemical_shift_one _Saveframe_category assigned_chemical_shifts _Details ; No stereospecific assignments of methylene or valine/luecine methyl groups. Hence ambiguity code 2 even where HB2,HB3 etc. are stated as having different shifts. ; loop_ _Sample_label $sample_one $sample_two $sample_three stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name EmrE _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 . 1 MET H H 8.46 . 1 2 . 1 MET HA H 4.65 . 1 3 . 1 MET HB2 H 2.03 . 2 4 . 1 MET HB3 H 2.16 . 2 5 . 1 MET HG2 H 2.58 . 2 6 . 1 MET HG3 H 2.58 . 2 7 . 1 MET C C 174.2 . 1 8 . 1 MET CA C 53.60 . 1 9 . 1 MET CB C 32.1 . 1 10 . 1 MET CG C 32.1 . 1 11 . 1 MET N N 126.7 . 1 12 . 2 ASN H H 8.25 . 1 13 . 2 ASN HA H 5.02 . 1 14 . 2 ASN HB2 H 2.82 . 2 15 . 2 ASN HB3 H 3.00 . 2 16 . 2 ASN HD21 H 6.85 . 2 17 . 2 ASN HD22 H 7.94 . 2 18 . 2 ASN CA C 50.86 . 1 19 . 2 ASN N N 119.5 . 1 20 . 2 ASN ND2 N 110.1 . 1 21 . 3 PRO HA H 4.39 . 1 22 . 3 PRO HB2 H 2.33 . 2 23 . 3 PRO HB3 H 2.40 . 2 24 . 3 PRO HG2 H 2.01 . 2 25 . 3 PRO HG3 H 1.83 . 2 26 . 3 PRO HD2 H 3.98 . 2 27 . 3 PRO HD3 H 4.20 . 2 28 . 3 PRO CA C 64.3 . 1 29 . 3 PRO CB C 32.2 . 1 30 . 3 PRO CG C 26.6 . 1 31 . 3 PRO CD C 50.7 . 1 32 . 3 PRO C C 177.1 . 1 33 . 4 TYR H H 8.05 . 1 34 . 4 TYR HA H 4.25 . 1 35 . 4 TYR HB2 H 3.15 . 2 36 . 4 TYR HB3 H 3.12 . 2 37 . 4 TYR HD1 H 7.24 . 3 38 . 4 TYR HD2 H 7.24 . 3 39 . 4 TYR HE1 H 6.86 . 3 40 . 4 TYR HE2 H 6.86 . 3 41 . 4 TYR C C 178.2 . 1 42 . 4 TYR CA C 61.50 . 1 43 . 4 TYR CB C 37.3 . 1 44 . 4 TYR N N 116.2 . 1 45 . 5 ILE H H 7.49 . 1 46 . 5 ILE HA H 3.90 . 1 47 . 5 ILE HB H 1.94 . 1 48 . 5 ILE HG12 H 1.61 . 2 49 . 5 ILE HG13 H 1.31 . 2 50 . 5 ILE HG2 H 0.89 . 1 51 . 5 ILE HD1 H 0.95 . 1 52 . 5 ILE C C 177.4 . 1 53 . 5 ILE CA C 63.60 . 1 54 . 5 ILE CB C 26.8 . 1 55 . 5 ILE CG1 C 28.3 . 1 56 . 5 ILE CG2 C 17.1 . 1 57 . 5 ILE CD1 C 12.2 . 1 58 . 5 ILE N N 118.7 . 1 59 . 6 TYR H H 7.40 . 1 60 . 6 TYR HA H 4.27 . 1 61 . 6 TYR HB2 H 3.03 . 2 62 . 6 TYR HB3 H 3.15 . 2 63 . 6 TYR HD1 H 7.11 . 3 64 . 6 TYR HD2 H 7.11 . 3 65 . 6 TYR HE1 H 6.78 . 3 66 . 6 TYR HE2 H 6.78 . 3 67 . 6 TYR C C 177.4 . 1 68 . 6 TYR CA C 61.16 . 1 69 . 6 TYR CB C 38.3 . 1 70 . 6 TYR N N 119.0 . 1 71 . 7 LEU H H 8.12 . 1 72 . 7 LEU HA H 4.15 . 1 73 . 7 LEU HB2 H 1.93 . 2 74 . 7 LEU HB3 H 1.84 . 2 75 . 7 LEU HG H 1.58 . 1 76 . 7 LEU HD1 H 1.04 . 2 77 . 7 LEU HD2 H 1.02 . 2 78 . 7 LEU C C 178.3 . 1 79 . 7 LEU CA C 57.30 . 1 80 . 7 LEU CB C 41.6 . 1 81 . 7 LEU CG C 24.2 . 1 82 . 7 LEU N N 118.9 . 1 83 . 8 GLY H H 8.27 . 1 84 . 8 GLY HA2 H 3.89 . 2 85 . 8 GLY HA3 H 3.89 . 2 86 . 8 GLY C C 175.6 . 1 87 . 8 GLY CA C 47.90 . 1 88 . 8 GLY N N 104.9 . 1 89 . 9 GLY H H 8.26 . 1 90 . 9 GLY HA2 H 3.91 . 2 91 . 9 GLY HA3 H 3.91 . 2 92 . 9 GLY C C 174.8 . 1 93 . 9 GLY CA C 47.30 . 1 94 . 9 GLY N N 107.9 . 1 95 . 10 ALA H H 8.08 . 1 96 . 10 ALA HA H 4.15 . 1 97 . 10 ALA HB H 1.56 . 1 98 . 10 ALA C C 179.5 . 1 99 . 10 ALA CA C 55.30 . 1 100 . 10 ALA CB C 18.00 . 1 101 . 10 ALA N N 124.6 . 1 102 . 11 ILE H H 8.18 . 1 103 . 11 ILE HA H 3.77 . 1 104 . 11 ILE HB H 2.08 . 1 105 . 11 ILE HG12 H 1.01 . 2 106 . 11 ILE HG13 H 2.01 . 2 107 . 11 ILE HD1 H 0.90 . 1 108 . 11 ILE C C 177.9 . 1 109 . 11 ILE CA C 65.25 . 1 110 . 11 ILE N N 118.2 . 1 111 . 12 LEU H H 8.16 . 1 112 . 12 LEU HA H 4.07 . 1 113 . 12 LEU HB2 H 1.95 . 2 114 . 12 LEU HB3 H 1.84 . 2 115 . 12 LEU HG H 1.71 . 1 116 . 12 LEU HD1 H 0.99 . 2 117 . 12 LEU HD2 H 0.94 . 2 118 . 12 LEU C C 180.0 . 1 119 . 12 LEU CA C 58.31 . 1 120 . 12 LEU N N 119.5 . 1 121 . 13 ALA H H 8.39 . 1 122 . 13 ALA HA H 4.23 . 1 123 . 13 ALA HB H 1.63 . 1 124 . 13 ALA C C 180.0 . 1 125 . 13 ALA CA C 55.60 . 1 126 . 13 ALA CB C 18.2 . 1 127 . 13 ALA N N 119.8 . 1 128 . 14 GLU H H 8.12 . 1 129 . 14 GLU HA H 4.20 . 1 130 . 14 GLU HB2 H 2.81 . 2 131 . 14 GLU HB3 H 2.35 . 2 132 . 14 GLU HG2 H 2.53 . 2 133 . 14 GLU HG3 H 2.64 . 2 134 . 14 GLU C C 179.8 . 1 135 . 14 GLU CA C 59.50 . 1 136 . 14 GLU CB C 34.9 . 1 137 . 14 GLU CG C 42.2 . 1 138 . 14 GLU N N 118.6 . 1 139 . 15 VAL H H 8.77 . 1 140 . 15 VAL HA H 3.70 . 1 141 . 15 VAL HB H 2.38 . 1 142 . 15 VAL HG1 H 1.03 . 2 143 . 15 VAL HG2 H 1.03 . 2 144 . 15 VAL C C 179.3 . 1 145 . 15 VAL CA C 67.27 . 1 146 . 15 VAL CB C 37.8 . 1 147 . 15 VAL CG2 C 21.40 . 2 148 . 15 VAL N N 122.9 . 1 149 . 16 ILE H H 8.98 . 1 150 . 16 ILE HA H 3.70 . 1 151 . 16 ILE HB H 1.99 . 1 152 . 16 ILE HG12 H 2.08 . 2 153 . 16 ILE HG2 H 0.98 . 1 154 . 16 ILE HD1 H 0.92 . 1 155 . 16 ILE C C 178.0 . 1 156 . 16 ILE CA C 65.89 . 1 157 . 16 ILE N N 123.2 . 1 158 . 17 GLY H H 8.88 . 1 159 . 17 GLY HA2 H 3.98 . 2 160 . 17 GLY HA3 H 3.81 . 2 161 . 17 GLY C C 175.6 . 1 162 . 17 GLY CA C 47.90 . 1 163 . 17 GLY N N 106.9 . 1 164 . 18 THR H H 8.47 . 1 165 . 18 THR HA H 3.99 . 1 166 . 18 THR HB H 4.29 . 1 167 . 18 THR C C 176.2 . 1 168 . 18 THR CA C 67.44 . 1 169 . 18 THR N N 116.6 . 1 170 . 19 THR H H 8.03 . 1 171 . 19 THR HA H 3.86 . 1 172 . 19 THR HB H 4.44 . 1 173 . 19 THR C C 176.5 . 1 174 . 19 THR CA C 68.17 . 1 175 . 19 THR N N 119.3 . 1 176 . 20 LEU H H 8.49 . 1 177 . 20 LEU HA H 4.11 . 1 178 . 20 LEU HB2 H 1.95 . 2 179 . 20 LEU HB3 H 1.64 . 2 180 . 20 LEU HG H 1.71 . 1 181 . 20 LEU HD1 H 0.98 . 2 182 . 20 LEU HD2 H 0.94 . 2 183 . 20 LEU C C 180.0 . 1 184 . 20 LEU CA C 65.10 . 1 185 . 20 LEU CB C 47.60 . 1 186 . 20 LEU CD1 C 17.30 . 2 187 . 20 LEU CD2 C 17.30 . 2 188 . 20 LEU N N 121.3 . 1 189 . 21 MET H H 8.35 . 1 190 . 21 MET HA H 4.28 . 1 191 . 21 MET HB2 H 2.36 . 2 192 . 21 MET HB3 H 2.25 . 2 193 . 21 MET HG2 H 2.81 . 2 194 . 21 MET HG3 H 2.66 . 2 195 . 21 MET C C 177.8 . 1 196 . 21 MET CA C 58.60 . 1 197 . 21 MET CB C 32.60 . 1 198 . 21 MET N N 119.9 . 1 199 . 22 LYS H H 8.45 . 1 200 . 22 LYS HA H 4.26 . 1 201 . 22 LYS HB2 H 1.85 . 2 202 . 22 LYS HB3 H 1.97 . 2 203 . 22 LYS HG2 H 1.76 . 2 204 . 22 LYS HG3 H 1.65 . 2 205 . 22 LYS HD2 H 0.98 . 2 206 . 22 LYS HD3 H 1.05 . 2 207 . 22 LYS HE2 H 2.91 . 2 208 . 22 LYS HE3 H 2.88 . 2 209 . 22 LYS C C 179.3 . 1 210 . 22 LYS CA C 58.20 . 1 211 . 22 LYS CB C 24.50 . 1 212 . 22 LYS CG C 23.50 . 1 213 . 22 LYS CD C 26.50 . 1 214 . 22 LYS CE C 41.30 . 1 215 . 22 LYS N N 119.8 . 1 216 . 23 PHE H H 8.74 . 1 217 . 23 PHE HA H 4.39 . 1 218 . 23 PHE HB2 H 3.29 . 2 219 . 23 PHE HB3 H 3.36 . 2 220 . 23 PHE HD1 H 7.32 . 3 221 . 23 PHE HD2 H 7.32 . 3 222 . 23 PHE HE1 H 7.30 . 3 223 . 23 PHE HE2 H 7.30 . 3 224 . 23 PHE C C 177.8 . 1 225 . 23 PHE CA C 60.90 . 1 226 . 23 PHE CB C 38.70 . 1 227 . 23 PHE N N 119.8 . 1 228 . 24 SER H H 8.39 . 1 229 . 24 SER HA H 4.29 . 1 230 . 24 SER HB2 H 4.14 . 2 231 . 24 SER HB3 H 4.14 . 2 232 . 24 SER C C 176.5 . 1 233 . 24 SER CA C 62.60 . 1 234 . 24 SER N N 115.0 . 1 235 . 25 GLU H H 8.47 . 1 236 . 25 GLU HA H 4.10 . 1 237 . 25 GLU HB2 H 2.57 . 2 238 . 25 GLU HB3 H 2.92 . 2 239 . 25 GLU HG2 H 2.25 . 2 240 . 25 GLU HG3 H 2.47 . 2 241 . 25 GLU C C 178.7 . 1 242 . 25 GLU CA C 59.30 . 1 243 . 25 GLU CB C 36.00 . 1 244 . 25 GLU CG C 36.00 . 1 245 . 25 GLU N N 123.7 . 1 246 . 26 GLY H H 8.31 . 1 247 . 26 GLY HA2 H 3.83 . 2 248 . 26 GLY HA3 H 3.83 . 2 249 . 26 GLY C C 175.0 . 1 250 . 26 GLY CA C 47.30 . 1 251 . 26 GLY N N 106.2 . 1 252 . 27 PHE H H 8.44 . 1 253 . 27 PHE HA H 4.29 . 1 254 . 27 PHE HB2 H 3.21 . 2 255 . 27 PHE HB3 H 3.08 . 2 256 . 27 PHE HD1 H 7.25 . 3 257 . 27 PHE HD2 H 7.25 . 3 258 . 27 PHE HE1 H 7.16 . 3 259 . 27 PHE HE2 H 7.16 . 3 260 . 27 PHE C C 177.3 . 1 261 . 27 PHE CA C 61.60 . 1 262 . 27 PHE CB C 39.20 . 1 263 . 27 PHE N N 120.4 . 1 264 . 28 THR H H 8.09 . 1 265 . 28 THR HA H 4.00 . 1 266 . 28 THR HB H 4.36 . 1 267 . 28 THR HG2 H 1.40 . 1 268 . 28 THR C C 175.5 . 1 269 . 28 THR CA C 66.02 . 1 270 . 28 THR N N 111.1 . 1 271 . 29 ARG H H 7.71 . 1 272 . 29 ARG HA H 4.27 . 1 273 . 29 ARG HB2 H 1.96 . 2 274 . 29 ARG HB3 H 1.96 . 2 275 . 29 ARG C C 177.2 . 1 276 . 29 ARG CA C 57.88 . 1 277 . 29 ARG CD C 43.00 . 1 278 . 29 ARG N N 117.1 . 1 279 . 30 LEU H H 7.84 . 1 280 . 30 LEU HA H 4.31 . 1 281 . 30 LEU HB2 H 1.79 . 2 282 . 30 LEU HB3 H 1.57 . 2 283 . 30 LEU HG H 1.70 . 1 284 . 30 LEU HD1 H 0.87 . 2 285 . 30 LEU HD2 H 0.92 . 2 286 . 30 LEU C C 177.7 . 1 287 . 30 LEU CA C 56.33 . 1 288 . 30 LEU CB C 47.90 . 1 289 . 30 LEU N N 118.2 . 1 290 . 31 TRP H H 8.07 . 1 291 . 31 TRP HA H 4.62 . 1 292 . 31 TRP HB2 H 3.27 . 2 293 . 31 TRP HB3 H 3.30 . 2 294 . 31 TRP HD1 H 7.18 . 1 295 . 31 TRP HE1 H 9.83 . 1 296 . 31 TRP HE3 H 7.52 . 1 297 . 31 TRP HZ2 H 7.42 . 1 298 . 31 TRP HZ3 H 7.08 . 1 299 . 31 TRP HH2 H 7.17 . 1 300 . 31 TRP CA C 60.60 . 1 301 . 31 TRP N N 119.8 . 1 302 . 31 TRP NE1 N 127.1 . 1 303 . 32 PRO HA H 4.33 . 1 304 . 32 PRO HB2 H 2.71 . 2 305 . 32 PRO HB3 H 2.71 . 2 306 . 32 PRO HG2 H 1.84 . 2 307 . 32 PRO HG3 H 1.84 . 2 308 . 32 PRO HD2 H 3.57 . 2 309 . 32 PRO HD3 H 3.57 . 2 310 . 32 PRO C C 175.9 . 1 311 . 33 SER H H 7.69 . 1 312 . 33 SER HA H 4.32 . 1 313 . 33 SER HB2 H 4.13 . 2 314 . 33 SER HB3 H 3.94 . 2 315 . 33 SER C C 178.5 . 1 316 . 33 SER CA C 61.59 . 1 317 . 33 SER N N 113.8 . 1 318 . 34 VAL H H 8.10 . 1 319 . 34 VAL HA H 3.68 . 1 320 . 34 VAL HB H 2.13 . 1 321 . 34 VAL HG1 H 1.03 . 2 322 . 34 VAL HG2 H 1.10 . 2 323 . 34 VAL C C 178.3 . 1 324 . 34 VAL CA C 58.30 . 1 325 . 34 VAL CB C 40.40 . 1 326 . 34 VAL CG1 C 17.70 . 2 327 . 34 VAL CG2 C 17.70 . 2 328 . 34 VAL N N 122.3 . 1 329 . 35 GLY H H 8.65 . 1 330 . 35 GLY HA2 H 3.67 . 2 331 . 35 GLY HA3 H 3.67 . 2 332 . 35 GLY C C 173.4 . 1 333 . 35 GLY CA C 47.42 . 1 334 . 35 GLY N N 105.7 . 1 335 . 36 THR H H 7.75 . 1 336 . 36 THR HA H 4.22 . 1 337 . 36 THR HB H 4.37 . 1 338 . 36 THR HG2 H 1.28 . 1 339 . 36 THR N N 117.7 . 1 340 . 37 ILE H H 7.79 . 1 341 . 37 ILE HA H 4.36 . 1 342 . 37 ILE HB H 2.15 . 1 343 . 37 ILE HG12 H 1.25 . 2 344 . 37 ILE HG13 H 1.83 . 2 345 . 37 ILE HG2 H 1.06 . 1 346 . 37 ILE HD1 H 0.91 . 1 347 . 37 ILE N N 121.7 . 1 348 . 38 ILE H H 8.42 . 1 349 . 38 ILE HA H 4.29 . 1 350 . 38 ILE HB H 2.11 . 1 351 . 38 ILE HG12 H 1.90 . 2 352 . 38 ILE HG13 H 1.66 . 2 353 . 38 ILE HG2 H 1.03 . 1 354 . 38 ILE HD1 H 1.26 . 1 355 . 38 ILE CA C 61.46 . 1 356 . 38 ILE CB C 39.40 . 1 357 . 38 ILE N N 120.6 . 1 358 . 39 CYS H H 8.26 . 1 359 . 39 CYS HA H 4.17 . 1 360 . 39 CYS HB2 H 2.93 . 2 361 . 39 CYS HB3 H 3.24 . 2 362 . 39 CYS N N 117.4 . 1 363 . 40 TYR H H 8.73 . 1 364 . 40 TYR HA H 4.27 . 1 365 . 40 TYR HB2 H 3.30 . 2 366 . 40 TYR HB3 H 3.30 . 2 367 . 40 TYR HD1 H 7.19 . 3 368 . 40 TYR HD2 H 7.19 . 3 369 . 40 TYR HE1 H 6.79 . 3 370 . 40 TYR HE2 H 6.79 . 3 371 . 40 TYR N N 122.3 . 1 372 . 41 CYS H H 8.74 . 1 373 . 41 CYS HA H 4.20 . 1 374 . 41 CYS HB2 H 2.94 . 2 375 . 41 CYS HB3 H 3.29 . 2 376 . 41 CYS CA C 52.10 . 1 377 . 41 CYS CB C 30.50 . 1 378 . 41 CYS N N 117.9 . 1 379 . 42 ALA H H 8.95 . 1 380 . 42 ALA HA H 4.29 . 1 381 . 42 ALA HB H 1.65 . 1 382 . 42 ALA CA C 55.52 . 1 383 . 42 ALA CB C 18.60 . 1 384 . 42 ALA N N 121.3 . 1 385 . 43 SER H H 8.19 . 1 386 . 43 SER HA H 4.33 . 1 387 . 43 SER HB2 H 3.98 . 2 388 . 43 SER HB3 H 3.98 . 2 389 . 43 SER CA C 55.70 . 1 390 . 43 SER CB C 63.30 . 1 391 . 43 SER N N 113.7 . 1 392 . 44 PHE H H 8.19 . 1 393 . 44 PHE HA H 4.17 . 1 394 . 44 PHE HB2 H 3.11 . 2 395 . 44 PHE HB3 H 3.22 . 2 396 . 44 PHE HD1 H 7.12 . 3 397 . 44 PHE HD2 H 7.12 . 3 398 . 44 PHE HE1 H 7.03 . 3 399 . 44 PHE HE2 H 7.03 . 3 400 . 44 PHE N N 122.3 . 1 401 . 45 TRP H H 8.35 . 1 402 . 45 TRP HA H 4.27 . 1 403 . 45 TRP HB2 H 3.26 . 2 404 . 45 TRP HB3 H 3.43 . 2 405 . 45 TRP HD1 H 7.28 . 1 406 . 45 TRP HE1 H 10.17 . 1 407 . 45 TRP HE3 H 7.65 . 1 408 . 45 TRP HZ2 H 7.44 . 1 409 . 45 TRP HZ3 H 7.12 . 1 410 . 45 TRP HH2 H 7.20 . 1 411 . 45 TRP CA C 59.22 . 1 412 . 45 TRP N N 119.8 . 1 413 . 45 TRP NE1 N 127.8 . 1 414 . 46 LEU H H 8.42 . 1 415 . 46 LEU HA H 3.76 . 1 416 . 46 LEU HB2 H 1.71 . 2 417 . 46 LEU HB3 H 1.71 . 2 418 . 46 LEU HG H 1.34 . 1 419 . 46 LEU HD1 H 1.01 . 2 420 . 46 LEU HD2 H 0.94 . 2 421 . 46 LEU N N 119.1 . 1 422 . 47 LEU H H 8.26 . 1 423 . 47 LEU HA H 4.04 . 1 424 . 47 LEU HB2 H 1.85 . 2 425 . 47 LEU HB3 H 1.85 . 2 426 . 47 LEU N N 122.2 . 1 427 . 48 ALA H H 8.49 . 1 428 . 48 ALA HA H 4.16 . 1 429 . 48 ALA HB H 1.68 . 1 430 . 48 ALA CA C 58.44 . 1 431 . 48 ALA CB C 18.80 . 1 432 . 48 ALA N N 121.4 . 1 433 . 49 GLN H H 8.13 . 1 434 . 49 GLN HA H 3.90 . 1 435 . 49 GLN HB2 H 2.04 . 2 436 . 49 GLN HB3 H 2.04 . 2 437 . 49 GLN HE21 H 5.99 . 2 438 . 49 GLN HE22 H 6.20 . 2 439 . 49 GLN N N 114.8 . 1 440 . 49 GLN NE2 N 106.8 . 1 441 . 50 THR H H 7.89 . 1 442 . 50 THR HA H 3.98 . 1 443 . 50 THR HB H 4.41 . 1 444 . 50 THR HG2 H 1.33 . 1 445 . 50 THR C C 174.9 . 1 446 . 50 THR N N 114.3 . 1 447 . 51 LEU H H 8.14 . 1 448 . 51 LEU HA H 4.06 . 1 449 . 51 LEU HB2 H 1.84 . 2 450 . 51 LEU HB3 H 1.84 . 2 451 . 51 LEU N N 119.8 . 1 452 . 52 ALA H H 7.72 . 1 453 . 52 ALA HA H 4.36 . 1 454 . 52 ALA HB H 1.46 . 1 455 . 52 ALA C C 178.6 . 1 456 . 52 ALA CB C 18.60 . 1 457 . 52 ALA N N 117.7 . 1 458 . 53 TYR H H 7.88 . 1 459 . 53 TYR HA H 4.42 . 1 460 . 53 TYR HB2 H 3.21 . 2 461 . 53 TYR HB3 H 3.21 . 2 462 . 53 TYR HD1 H 7.18 . 3 463 . 53 TYR HD2 H 7.18 . 3 464 . 53 TYR HE1 H 6.77 . 3 465 . 53 TYR HE2 H 6.77 . 3 466 . 53 TYR CA C 60.38 . 1 467 . 53 TYR N N 117.0 . 1 468 . 54 ILE H H 8.09 . 1 469 . 54 ILE HA H 4.08 . 1 470 . 54 ILE HB H 1.97 . 1 471 . 54 ILE N N 119.1 . 1 472 . 55 PRO HA H 4.20 . 1 473 . 55 PRO HB2 H 2.24 . 2 474 . 55 PRO HB3 H 2.30 . 2 475 . 55 PRO HG2 H 2.03 . 2 476 . 55 PRO HG3 H 2.03 . 2 477 . 55 PRO HD2 H 3.94 . 2 478 . 55 PRO HD3 H 3.77 . 2 479 . 56 THR H H 7.34 . 1 480 . 56 THR HA H 3.96 . 1 481 . 56 THR HB H 3.92 . 1 482 . 56 THR HG2 H 1.29 . 1 483 . 56 THR C C 175.7 . 1 484 . 56 THR N N 112.5 . 1 485 . 57 GLY H H 8.29 . 1 486 . 57 GLY HA2 H 3.84 . 2 487 . 57 GLY HA3 H 3.92 . 2 488 . 57 GLY CA C 47.64 . 1 489 . 57 GLY N N 109.6 . 1 490 . 58 ILE H H 8.24 . 1 491 . 58 ILE HA H 4.29 . 1 492 . 58 ILE HB H 1.98 . 1 493 . 58 ILE HG12 H 2.28 . 2 494 . 58 ILE HD1 H 1.09 . 1 495 . 58 ILE CA C 66.90 . 1 496 . 58 ILE N N 121.6 . 1 497 . 59 ALA H H 8.09 . 1 498 . 59 ALA HA H 4.03 . 1 499 . 59 ALA HB H 1.58 . 1 500 . 59 ALA CA C 59.00 . 1 501 . 59 ALA CB C 17.60 . 1 502 . 59 ALA N N 121.4 . 1 503 . 60 TYR H H 8.52 . 1 504 . 60 TYR HA H 4.35 . 1 505 . 60 TYR HB2 H 3.17 . 2 506 . 60 TYR HB3 H 3.24 . 2 507 . 60 TYR HD1 H 7.15 . 3 508 . 60 TYR HD2 H 7.15 . 3 509 . 60 TYR HE1 H 6.81 . 3 510 . 60 TYR HE2 H 6.81 . 3 511 . 60 TYR CA C 55.00 . 1 512 . 60 TYR N N 116.7 . 1 513 . 61 ALA H H 8.48 . 1 514 . 61 ALA HA H 4.11 . 1 515 . 61 ALA HB H 1.71 . 1 516 . 61 ALA C C 177.8 . 1 517 . 61 ALA CA C 58.60 . 1 518 . 61 ALA CB C 24.40 . 1 519 . 61 ALA N N 124.4 . 1 520 . 62 ILE H H 8.45 . 1 521 . 62 ILE HA H 4.02 . 1 522 . 62 ILE HB H 2.00 . 1 523 . 62 ILE HG12 H 1.32 . 2 524 . 62 ILE HG13 H 1.80 . 2 525 . 62 ILE HG2 H 0.85 . 1 526 . 62 ILE HD1 H 0.99 . 1 527 . 62 ILE C C 179.3 . 1 528 . 62 ILE CA C 65.63 . 1 529 . 62 ILE N N 119.1 . 1 530 . 63 TRP H H 8.70 . 1 531 . 63 TRP HA H 4.34 . 1 532 . 63 TRP HB2 H 3.40 . 2 533 . 63 TRP HB3 H 3.36 . 2 534 . 63 TRP HD1 H 7.19 . 1 535 . 63 TRP HE1 H 10.00 . 1 536 . 63 TRP HE3 H 7.56 . 1 537 . 63 TRP HZ2 H 7.42 . 1 538 . 63 TRP HZ3 H 7.09 . 1 539 . 63 TRP HH2 H 7.16 . 1 540 . 63 TRP N N 119.9 . 1 541 . 63 TRP NE1 N 126.3 . 1 542 . 64 SER H H 8.54 . 1 543 . 64 SER HA H 4.11 . 1 544 . 64 SER HB2 H 3.78 . 2 545 . 64 SER HB3 H 3.78 . 2 546 . 64 SER C C 176.0 . 1 547 . 64 SER CA C 62.28 . 1 548 . 64 SER N N 113.9 . 1 549 . 65 GLY H H 8.13 . 1 550 . 65 GLY HA2 H 3.81 . 2 551 . 65 GLY HA3 H 3.93 . 2 552 . 65 GLY C C 175.9 . 1 553 . 65 GLY CA C 47.50 . 1 554 . 65 GLY N N 109.9 . 1 555 . 66 VAL H H 8.36 . 1 556 . 66 VAL HA H 3.62 . 1 557 . 66 VAL HB H 2.26 . 1 558 . 66 VAL HG1 H 1.09 . 2 559 . 66 VAL HG2 H 0.99 . 2 560 . 66 VAL CA C 66.97 . 1 561 . 66 VAL N N 121.3 . 1 562 . 67 GLY H H 8.12 . 1 563 . 67 GLY HA2 H 3.83 . 2 564 . 67 GLY HA3 H 3.83 . 2 565 . 67 GLY C C 178.9 . 1 566 . 67 GLY N N 106.0 . 1 567 . 68 ILE H H 8.60 . 1 568 . 68 ILE HA H 3.85 . 1 569 . 68 ILE HB H 2.01 . 1 570 . 68 ILE HG12 H 1.22 . 2 571 . 68 ILE HG2 H 0.93 . 1 572 . 68 ILE HD1 H 0.92 . 1 573 . 68 ILE C C 179.3 . 1 574 . 68 ILE N N 117.2 . 1 575 . 69 VAL H H 8.29 . 1 576 . 69 VAL HA H 3.90 . 1 577 . 69 VAL HB H 1.97 . 1 578 . 69 VAL C C 175.5 . 1 579 . 69 VAL CA C 63.27 . 1 580 . 69 VAL CB C 36.90 . 1 581 . 69 VAL CG1 C 21.20 . 2 582 . 69 VAL CG2 C 21.20 . 2 583 . 69 VAL N N 119.6 . 1 584 . 70 LEU H H 8.47 . 1 585 . 70 LEU HA H 4.24 . 1 586 . 70 LEU HB2 H 1.67 . 2 587 . 70 LEU HB3 H 1.67 . 2 588 . 70 LEU HG H 1.36 . 1 589 . 70 LEU C C 179.5 . 1 590 . 70 LEU CA C 58.44 . 1 591 . 70 LEU N N 122.8 . 1 592 . 71 ILE H H 8.51 . 1 593 . 71 ILE HA H 4.19 . 1 594 . 71 ILE HB H 1.97 . 1 595 . 71 ILE HG12 H 1.66 . 2 596 . 71 ILE HD1 H 0.97 . 1 597 . 71 ILE C C 179.1 . 1 598 . 71 ILE CA C 58.19 . 1 599 . 71 ILE N N 118.9 . 1 600 . 72 SER H H 8.32 . 1 601 . 72 SER HA H 4.32 . 1 602 . 72 SER HB2 H 3.98 . 2 603 . 72 SER HB3 H 3.98 . 2 604 . 72 SER C C 174.9 . 1 605 . 72 SER CA C 62.62 . 1 606 . 72 SER N N 114.2 . 1 607 . 73 LEU H H 8.05 . 1 608 . 73 LEU HA H 3.83 . 1 609 . 73 LEU HB2 H 1.84 . 2 610 . 73 LEU HB3 H 1.84 . 2 611 . 73 LEU CA C 64.69 . 1 612 . 73 LEU N N 120.3 . 1 613 . 74 LEU H H 8.54 . 1 614 . 74 LEU HA H 4.10 . 1 615 . 74 LEU HB2 H 1.71 . 2 616 . 74 LEU HB3 H 1.93 . 2 617 . 74 LEU HD1 H 1.12 . 2 618 . 74 LEU HD2 H 0.98 . 2 619 . 74 LEU C C 179.0 . 1 620 . 74 LEU CA C 58.87 . 1 621 . 74 LEU N N 119.6 . 1 622 . 75 SER H H 8.05 . 1 623 . 75 SER HA H 3.60 . 1 624 . 75 SER HB2 H 3.84 . 2 625 . 75 SER HB3 H 3.84 . 2 626 . 75 SER C C 175.7 . 1 627 . 75 SER CA C 62.60 . 1 628 . 75 SER N N 123.4 . 1 629 . 76 TRP H H 8.33 . 1 630 . 76 TRP HA H 4.52 . 1 631 . 76 TRP HB2 H 3.53 . 2 632 . 76 TRP HB3 H 3.47 . 2 633 . 76 TRP HD1 H 7.30 . 1 634 . 76 TRP HE1 H 10.08 . 1 635 . 76 TRP HE3 H 7.65 . 1 636 . 76 TRP HZ2 H 7.42 . 1 637 . 76 TRP HZ3 H 7.04 . 1 638 . 76 TRP HH2 H 7.16 . 1 639 . 76 TRP C C 178.4 . 1 640 . 76 TRP CA C 60.30 . 1 641 . 76 TRP CB C 29.60 . 1 642 . 76 TRP N N 122.5 . 1 643 . 76 TRP NE1 N 127.4 . 1 644 . 77 GLY H H 8.44 . 1 645 . 77 GLY HA2 H 3.87 . 2 646 . 77 GLY HA3 H 3.87 . 2 647 . 77 GLY C C 178.0 . 1 648 . 77 GLY CA C 46.70 . 1 649 . 77 GLY N N 105.6 . 1 650 . 78 PHE H H 8.21 . 1 651 . 78 PHE HA H 4.39 . 1 652 . 78 PHE HB2 H 2.96 . 2 653 . 78 PHE HB3 H 2.88 . 2 654 . 78 PHE HD1 H 6.98 . 3 655 . 78 PHE HD2 H 6.98 . 3 656 . 78 PHE HE1 H 7.20 . 3 657 . 78 PHE HE2 H 7.20 . 3 658 . 78 PHE C C 176.8 . 1 659 . 78 PHE CA C 60.42 . 1 660 . 78 PHE CB C 39.50 . 1 661 . 78 PHE N N 119.3 . 1 662 . 79 PHE H H 8.26 . 1 663 . 79 PHE HA H 4.49 . 1 664 . 79 PHE HB2 H 3.12 . 2 665 . 79 PHE HB3 H 3.32 . 2 666 . 79 PHE HD1 H 7.37 . 3 667 . 79 PHE HD2 H 7.37 . 3 668 . 79 PHE HE1 H 7.28 . 3 669 . 79 PHE HE2 H 7.28 . 3 670 . 79 PHE C C 176.8 . 1 671 . 79 PHE CA C 59.78 . 1 672 . 79 PHE CB C 39.40 . 1 673 . 79 PHE N N 116.4 . 1 674 . 80 GLY H H 8.21 . 1 675 . 80 GLY HA2 H 3.75 . 2 676 . 80 GLY HA3 H 3.90 . 2 677 . 80 GLY C C 173.8 . 1 678 . 80 GLY CA C 46.00 . 1 679 . 80 GLY N N 106.3 . 1 680 . 81 GLN H H 7.68 . 1 681 . 81 GLN HA H 4.26 . 1 682 . 81 GLN HB2 H 2.05 . 2 683 . 81 GLN HB3 H 2.16 . 2 684 . 81 GLN HG2 H 2.33 . 2 685 . 81 GLN HG3 H 2.33 . 2 686 . 81 GLN HE21 H 6.33 . 2 687 . 81 GLN HE22 H 7.40 . 2 688 . 81 GLN C C 173.8 . 1 689 . 81 GLN CA C 55.80 . 1 690 . 81 GLN CB C 33.80 . 1 691 . 81 GLN N N 116.8 . 1 692 . 81 GLN NE2 N 108.8 . 1 693 . 82 ARG H H 7.89 . 1 694 . 82 ARG HA H 4.42 . 1 695 . 82 ARG HB2 H 1.88 . 2 696 . 82 ARG HB3 H 2.14 . 2 697 . 82 ARG HD2 H 3.16 . 2 698 . 82 ARG HD3 H 3.16 . 2 699 . 82 ARG C C 176.3 . 1 700 . 82 ARG CA C 55.10 . 1 701 . 82 ARG CB C 30.00 . 1 702 . 82 ARG CG C 26.20 . 1 703 . 82 ARG CD C 42.50 . 1 704 . 82 ARG N N 118.1 . 1 705 . 83 LEU H H 8.24 . 1 706 . 83 LEU HA H 4.28 . 1 707 . 83 LEU HB2 H 1.69 . 2 708 . 83 LEU HB3 H 1.69 . 2 709 . 83 LEU HG H 1.75 . 1 710 . 83 LEU HD1 H 0.98 . 2 711 . 83 LEU HD2 H 0.92 . 2 712 . 83 LEU C C 176.0 . 1 713 . 83 LEU CA C 55.40 . 1 714 . 83 LEU CB C 41.80 . 1 715 . 83 LEU CG C 27.10 . 1 716 . 83 LEU CD1 C 24.90 . 2 717 . 83 LEU CD2 C 23.30 . 2 718 . 83 LEU N N 120.7 . 1 719 . 84 ASP H H 8.60 . 1 720 . 84 ASP HA H 4.54 . 1 721 . 84 ASP HB2 H 2.73 . 2 722 . 84 ASP HB3 H 2.78 . 2 723 . 84 ASP C C 176.7 . 1 724 . 84 ASP CA C 54.00 . 1 725 . 84 ASP CB C 39.80 . 1 726 . 84 ASP N N 116.2 . 1 727 . 85 LEU H H 7.91 . 1 728 . 85 LEU HA H 4.32 . 1 729 . 85 LEU HB2 H 1.80 . 2 730 . 85 LEU HB3 H 1.80 . 2 731 . 85 LEU HG H 1.75 . 1 732 . 85 LEU HD1 H 1.05 . 2 733 . 85 LEU HD2 H 1.00 . 2 734 . 85 LEU CA C 59.35 . 1 735 . 85 LEU N N 119.9 . 1 736 . 86 PRO HA H 4.21 . 1 737 . 86 PRO HB2 H 2.27 . 2 738 . 86 PRO HB3 H 2.27 . 2 739 . 86 PRO HG2 H 1.93 . 2 740 . 86 PRO HG3 H 1.93 . 2 741 . 86 PRO HD2 H 3.94 . 2 742 . 86 PRO HD3 H 3.68 . 2 743 . 86 PRO C C 178.0 . 1 744 . 86 PRO CA C 66.10 . 1 745 . 86 PRO CB C 30.40 . 1 746 . 86 PRO CG C 28.20 . 1 747 . 86 PRO CD C 49.50 . 1 748 . 87 ALA H H 7.46 . 1 749 . 87 ALA HA H 4.22 . 1 750 . 87 ALA HB H 1.60 . 1 751 . 87 ALA C C 179.1 . 1 752 . 87 ALA CA C 55.09 . 1 753 . 87 ALA CB C 18.40 . 1 754 . 87 ALA N N 118.2 . 1 755 . 88 ILE H H 7.99 . 1 756 . 88 ILE HA H 3.78 . 1 757 . 88 ILE HB H 2.09 . 1 758 . 88 ILE HG12 H 1.21 . 2 759 . 88 ILE HG13 H 1.82 . 2 760 . 88 ILE HG2 H 1.01 . 1 761 . 88 ILE HD1 H 0.90 . 1 762 . 88 ILE C C 177.8 . 1 763 . 88 ILE CA C 64.90 . 1 764 . 88 ILE CB C 37.80 . 1 765 . 88 ILE CG1 C 28.70 . 1 766 . 88 ILE CG2 C 17.50 . 1 767 . 88 ILE CD1 C 13.30 . 1 768 . 88 ILE N N 119.0 . 1 769 . 89 ILE H H 8.33 . 1 770 . 89 ILE HA H 3.77 . 1 771 . 89 ILE HB H 2.03 . 1 772 . 89 ILE HG12 H 1.28 . 2 773 . 89 ILE HG13 H 1.98 . 2 774 . 89 ILE HD1 H 1.00 . 1 775 . 89 ILE C C 178.2 . 1 776 . 89 ILE CA C 64.90 . 1 777 . 89 ILE CB C 36.90 . 1 778 . 89 ILE CG1 C 28.70 . 1 779 . 89 ILE CD1 C 17.40 . 1 780 . 89 ILE N N 119.5 . 1 781 . 90 GLY H H 8.38 . 1 782 . 90 GLY HA2 H 3.86 . 2 783 . 90 GLY HA3 H 3.86 . 2 784 . 90 GLY C C 175.0 . 1 785 . 90 GLY CA C 47.80 . 1 786 . 90 GLY N N 105.9 . 1 787 . 91 MET H H 8.24 . 1 788 . 91 MET HA H 4.30 . 1 789 . 91 MET HB2 H 2.38 . 2 790 . 91 MET HB3 H 2.28 . 2 791 . 91 MET HG2 H 2.68 . 2 792 . 91 MET HG3 H 2.80 . 2 793 . 91 MET C C 178.5 . 1 794 . 91 MET CA C 58.60 . 1 795 . 91 MET CB C 32.60 . 1 796 . 91 MET CG C 32.60 . 1 797 . 91 MET N N 119.7 . 1 798 . 92 MET H H 8.46 . 1 799 . 92 MET HA H 4.11 . 1 800 . 92 MET HB2 H 2.22 . 2 801 . 92 MET HB3 H 2.90 . 2 802 . 92 MET HG2 H 2.47 . 2 803 . 92 MET HG3 H 2.51 . 2 804 . 92 MET C C 178.3 . 1 805 . 92 MET CA C 59.70 . 1 806 . 92 MET CB C 32.60 . 1 807 . 92 MET CG C 32.60 . 1 808 . 92 MET N N 119.8 . 1 809 . 93 LEU H H 8.40 . 1 810 . 93 LEU HA H 4.13 . 1 811 . 93 LEU HB2 H 1.95 . 2 812 . 93 LEU HB3 H 2.14 . 2 813 . 93 LEU HD1 H 0.99 . 2 814 . 93 LEU HD2 H 0.94 . 2 815 . 93 LEU C C 179.7 . 1 816 . 93 LEU CA C 58.10 . 1 817 . 93 LEU CB C 41.60 . 1 818 . 93 LEU CD1 C 29.60 . 2 819 . 93 LEU CD2 C 26.30 . 2 820 . 93 LEU N N 119.6 . 1 821 . 94 ILE H H 8.22 . 1 822 . 94 ILE HA H 3.84 . 1 823 . 94 ILE HB H 2.16 . 1 824 . 94 ILE HG12 H 2.06 . 2 825 . 94 ILE HG2 H 1.04 . 1 826 . 94 ILE HD1 H 0.92 . 1 827 . 94 ILE C C 178.2 . 1 828 . 94 ILE CA C 65.00 . 1 829 . 94 ILE CB C 37.40 . 1 830 . 94 ILE CG1 C 29.00 . 1 831 . 94 ILE CD1 C 17.20 . 1 832 . 94 ILE N N 120.3 . 1 833 . 95 CYS H H 8.38 . 1 834 . 95 CYS HA H 4.07 . 1 835 . 95 CYS HB2 H 3.26 . 2 836 . 95 CYS HB3 H 2.88 . 2 837 . 95 CYS C C 175.9 . 1 838 . 95 CYS CA C 64.51 . 1 839 . 95 CYS CB C 27.10 . 1 840 . 95 CYS N N 117.5 . 1 841 . 96 ALA H H 8.52 . 1 842 . 96 ALA HA H 4.12 . 1 843 . 96 ALA HB H 1.63 . 1 844 . 96 ALA C C 179.0 . 1 845 . 96 ALA CA C 55.40 . 1 846 . 96 ALA CB C 18.00 . 1 847 . 96 ALA N N 121.1 . 1 848 . 97 GLY H H 8.31 . 1 849 . 97 GLY HA2 H 3.90 . 2 850 . 97 GLY HA3 H 3.90 . 2 851 . 97 GLY C C 175.0 . 1 852 . 97 GLY CA C 47.70 . 1 853 . 97 GLY N N 105.0 . 1 854 . 98 VAL H H 8.34 . 1 855 . 98 VAL HA H 3.62 . 1 856 . 98 VAL HB H 2.33 . 1 857 . 98 VAL HG1 H 1.00 . 2 858 . 98 VAL HG2 H 1.16 . 2 859 . 98 VAL C C 178.5 . 1 860 . 98 VAL CA C 66.80 . 1 861 . 98 VAL CB C 31.30 . 1 862 . 98 VAL CG1 C 21.90 . 2 863 . 98 VAL CG2 C 21.90 . 2 864 . 98 VAL N N 121.0 . 1 865 . 99 LEU H H 8.13 . 1 866 . 99 LEU HA H 4.10 . 1 867 . 99 LEU HB2 H 1.95 . 2 868 . 99 LEU HB3 H 1.95 . 2 869 . 99 LEU HG H 1.85 . 1 870 . 99 LEU HD1 H 0.98 . 2 871 . 99 LEU HD2 H 0.93 . 2 872 . 99 LEU C C 178.8 . 1 873 . 99 LEU CA C 58.60 . 1 874 . 99 LEU CB C 41.10 . 1 875 . 99 LEU CG C 32.60 . 1 876 . 99 LEU CD1 C 26.80 . 2 877 . 99 LEU CD2 C 24.40 . 2 878 . 99 LEU N N 121.2 . 1 879 . 100 ILE H H 8.47 . 1 880 . 100 ILE HA H 3.73 . 1 881 . 100 ILE HB H 2.12 . 1 882 . 100 ILE HG12 H 1.07 . 2 883 . 100 ILE HG2 H 0.99 . 1 884 . 100 ILE HD1 H 0.92 . 1 885 . 100 ILE C C 177.8 . 1 886 . 100 ILE CA C 65.30 . 1 887 . 100 ILE CB C 37.30 . 1 888 . 100 ILE CG1 C 29.20 . 1 889 . 100 ILE CD1 C 17.70 . 1 890 . 100 ILE N N 119.4 . 1 891 . 101 ILE H H 8.44 . 1 892 . 101 ILE HA H 3.77 . 1 893 . 101 ILE HB H 2.06 . 1 894 . 101 ILE HG12 H 1.06 . 2 895 . 101 ILE HG2 H 0.91 . 1 896 . 101 ILE HD1 H 1.01 . 1 897 . 101 ILE C C 178.8 . 1 898 . 101 ILE CA C 64.80 . 1 899 . 101 ILE CB C 36.80 . 1 900 . 101 ILE CG1 C 29.20 . 1 901 . 101 ILE CG2 C 17.40 . 1 902 . 101 ILE N N 119.4 . 1 903 . 102 ASN H H 8.30 . 1 904 . 102 ASN HA H 4.36 . 1 905 . 102 ASN HB2 H 3.04 . 2 906 . 102 ASN HB3 H 2.74 . 2 907 . 102 ASN HD21 H 6.87 . 2 908 . 102 ASN HD22 H 7.68 . 2 909 . 102 ASN C C 177.3 . 1 910 . 102 ASN CA C 57.76 . 1 911 . 102 ASN CB C 39.50 . 1 912 . 102 ASN N N 120.2 . 1 913 . 102 ASN ND2 N 110.4 . 1 914 . 103 LEU H H 8.50 . 1 915 . 103 LEU HA H 4.09 . 1 916 . 103 LEU HB2 H 1.83 . 2 917 . 103 LEU HB3 H 1.97 . 2 918 . 103 LEU HG H 1.75 . 1 919 . 103 LEU HD1 H 0.98 . 2 920 . 103 LEU HD2 H 0.93 . 2 921 . 103 LEU C C 179.8 . 1 922 . 103 LEU CA C 58.10 . 1 923 . 103 LEU CB C 41.40 . 1 924 . 103 LEU CG C 26.60 . 1 925 . 103 LEU CD1 C 24.20 . 2 926 . 103 LEU N N 120.6 . 1 927 . 104 LEU H H 8.79 . 1 928 . 104 LEU HA H 4.11 . 1 929 . 104 LEU HB2 H 1.81 . 2 930 . 104 LEU HB3 H 1.97 . 2 931 . 104 LEU HG H 1.60 . 1 932 . 104 LEU HD1 H 1.01 . 2 933 . 104 LEU HD2 H 0.93 . 2 934 . 104 LEU C C 179.7 . 1 935 . 104 LEU CA C 57.70 . 1 936 . 104 LEU CB C 41.70 . 1 937 . 104 LEU CG C 26.60 . 1 938 . 104 LEU CD1 C 25.30 . 2 939 . 104 LEU CD2 C 22.90 . 2 940 . 104 LEU N N 119.5 . 1 941 . 105 SER H H 8.36 . 1 942 . 105 SER HA H 4.27 . 1 943 . 105 SER HB2 H 4.05 . 2 944 . 105 SER HB3 H 4.05 . 2 945 . 105 SER C C 175.4 . 1 946 . 105 SER CA C 61.40 . 1 947 . 105 SER CB C 63.40 . 1 948 . 105 SER N N 114.1 . 1 949 . 106 ARG H H 7.70 . 1 950 . 106 ARG HA H 4.37 . 1 951 . 106 ARG HB2 H 1.91 . 2 952 . 106 ARG HB3 H 2.13 . 2 953 . 106 ARG HG2 H 2.54 . 2 954 . 106 ARG HG3 H 2.54 . 2 955 . 106 ARG HD2 H 3.23 . 2 956 . 106 ARG HD3 H 3.23 . 2 957 . 106 ARG C C 176.2 . 1 958 . 106 ARG CA C 56.70 . 1 959 . 106 ARG CB C 30.10 . 1 960 . 106 ARG CG C 27.80 . 1 961 . 106 ARG CD C 43.20 . 1 962 . 106 ARG N N 118.1 . 1 963 . 107 SER H H 7.73 . 1 964 . 107 SER HA H 4.56 . 1 965 . 107 SER HB2 H 4.06 . 2 966 . 107 SER HB3 H 4.06 . 2 967 . 107 SER C C 173.3 . 1 968 . 107 SER CA C 58.90 . 1 969 . 107 SER CB C 64.30 . 1 970 . 107 SER N N 112.3 . 1 971 . 108 THR H H 7.50 . 1 972 . 108 THR HA H 4.71 . 1 973 . 108 THR HB H 4.24 . 1 974 . 108 THR HG2 H 1.31 . 1 975 . 108 THR CA C 59.61 . 1 976 . 108 THR N N 114.6 . 1 977 . 109 PRO HA H 4.42 . 1 978 . 109 PRO HB2 H 2.01 . 2 979 . 109 PRO HB3 H 2.08 . 2 980 . 109 PRO HG2 H 2.25 . 2 981 . 109 PRO HG3 H 2.25 . 2 982 . 109 PRO HD2 H 3.71 . 2 983 . 109 PRO HD3 H 3.86 . 2 984 . 109 PRO C C 174.5 . 1 985 . 109 PRO CA C 63.70 . 1 986 . 109 PRO CB C 31.50 . 1 987 . 109 PRO CG C 27.10 . 1 988 . 109 PRO CD C 50.50 . 1 989 . 110 HIS H H 7.62 . 1 990 . 110 HIS HA H 4.43 . 1 991 . 110 HIS HB2 H 3.28 . 2 992 . 110 HIS HB3 H 3.13 . 2 993 . 110 HIS HD2 H 7.03 . 2 994 . 110 HIS CA C 57.37 . 1 995 . 110 HIS N N 122.3 . 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants _Saveframe_category coupling_constants _Details ; 3JHNHA couplings measured from ratio of cross to diagonal peaks in an HNHA experiment. ; loop_ _Sample_label $sample_one $sample_two $sample_three stop_ _Sample_conditions_label $sample_conditions_one _Spectrometer_frequency_1H . _Mol_system_component_name EmrE _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 1 MET H 1 MET HA 4.6 . . . 2 3JHNHA 2 ASN H 2 ASN HA 5 . . . 3 3JHNHA 4 TYR H 4 TYR HA 5.8 . . . 4 3JHNHA 5 ILE H 5 ILE HA 5.7 . . . 5 3JHNHA 6 TYR H 6 TYR HA 4.5 . . . 6 3JHNHA 7 LEU H 7 LEU HA 3.7 . . . 7 3JHNHA 10 ALA H 10 ALA HA 4.2 . . . 8 3JHNHA 11 ILE H 11 ILE HA 4.1 . . . 9 3JHNHA 12 LEU H 12 LEU HA 3.2 . . . 10 3JHNHA 13 ALA H 13 ALA HA 2.9 . . . 11 3JHNHA 14 GLU H 14 GLU HA 3.7 . . . 12 3JHNHA 15 VAL H 15 VAL HA 3.9 . . . 13 3JHNHA 16 ILE H 16 ILE HA 4 . . . 14 3JHNHA 18 THR H 18 THR HA 4.4 . . . 15 3JHNHA 21 MET H 21 MET HA 2.8 . . . 16 3JHNHA 23 PHE H 23 PHE HA 4 . . . 17 3JHNHA 24 SER H 24 SER HA 3.5 . . . 18 3JHNHA 25 GLU H 25 GLU HA 3.2 . . . 19 3JHNHA 28 THR H 28 THR HA 4.7 . . . 20 3JHNHA 29 ARG H 29 ARG HA 5.3 . . . 21 3JHNHA 34 VAL H 34 VAL HA 2.3 . . . 22 3JHNHA 39 CYS H 39 CYS HA 1.2 . . . 23 3JHNHA 40 TYR H 40 TYR HA 1.2 . . . 24 3JHNHA 41 CYS H 41 CYS HA 1.5 . . . 25 3JHNHA 42 ALA H 42 ALA HA 3.5 . . . 26 3JHNHA 43 SER H 43 SER HA 3.5 . . . 27 3JHNHA 44 PHE H 44 PHE HA 3.7 . . . 28 3JHNHA 47 LEU H 47 LEU HA 3.9 . . . 29 3JHNHA 49 GLN H 49 GLN HA 3.1 . . . 30 3JHNHA 50 THR H 50 THR HA 1.3 . . . 31 3JHNHA 53 TYR H 53 TYR HA 1.7 . . . 32 3JHNHA 56 THR H 56 THR HA 5.2 . . . 33 3JHNHA 59 ALA H 59 ALA HA 3.5 . . . 34 3JHNHA 60 TYR H 60 TYR HA 4.8 . . . 35 3JHNHA 61 ALA H 61 ALA HA 3.5 . . . 36 3JHNHA 62 ILE H 62 ILE HA 2.8 . . . 37 3JHNHA 63 TRP H 63 TRP HA 3.8 . . . 38 3JHNHA 64 SER H 64 SER HA 3.3 . . . 39 3JHNHA 68 ILE H 68 ILE HA 4.4 . . . 40 3JHNHA 70 LEU H 70 LEU HA 4.1 . . . 41 3JHNHA 72 SER H 72 SER HA 2.3 . . . 42 3JHNHA 73 LEU H 73 LEU HA 3.9 . . . 43 3JHNHA 74 LEU H 74 LEU HA 3.5 . . . 44 3JHNHA 75 SER H 75 SER HA 3.3 . . . 45 3JHNHA 76 TRP H 76 TRP HA 3.2 . . . 46 3JHNHA 78 PHE H 78 PHE HA 6 . . . 47 3JHNHA 79 PHE H 79 PHE HA 5.9 . . . 48 3JHNHA 81 GLN H 81 GLN HA 6.1 . . . 49 3JHNHA 82 ARG H 82 ARG HA 5.6 . . . 50 3JHNHA 83 LEU H 83 LEU HA 5.2 . . . 51 3JHNHA 84 ASP H 84 ASP HA 5.7 . . . 52 3JHNHA 85 LEU H 85 LEU HA 3 . . . 53 3JHNHA 87 ALA H 87 ALA HA 4.4 . . . 54 3JHNHA 88 ILE H 88 ILE HA 4.4 . . . 55 3JHNHA 89 ILE H 89 ILE HA 3.7 . . . 56 3JHNHA 91 MET H 91 MET HA 3.6 . . . 57 3JHNHA 92 MET H 92 MET HA 2.8 . . . 58 3JHNHA 93 LEU H 93 LEU HA 3.4 . . . 59 3JHNHA 94 ILE H 94 ILE HA 3 . . . 60 3JHNHA 95 CYS H 95 CYS HA 4 . . . 61 3JHNHA 96 ALA H 96 ALA HA 3.5 . . . 62 3JHNHA 98 VAL H 98 VAL HA 3.8 . . . 63 3JHNHA 99 LEU H 99 LEU HA 3.9 . . . 64 3JHNHA 100 ILE H 100 ILE HA 3.2 . . . 65 3JHNHA 101 ILE H 101 ILE HA 3.2 . . . 66 3JHNHA 102 ASN H 102 ASN HA 4 . . . 67 3JHNHA 103 LEU H 103 LEU HA 4 . . . 68 3JHNHA 104 LEU H 104 LEU HA 4 . . . 69 3JHNHA 105 SER H 105 SER HA 3.9 . . . 70 3JHNHA 106 ARG H 106 ARG HA 5.6 . . . 71 3JHNHA 107 SER H 107 SER HA 6.9 . . . 72 3JHNHA 108 THR H 108 THR HA 7.2 . . . 73 3JHNHA 110 HIS H 110 HIS HA 6.3 . . . stop_ save_