data_5804 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Three-disulfide variant of hen lysozyme: C76A/C94A ; _BMRB_accession_number 5804 _BMRB_flat_file_name bmr5804.str _Entry_type original _Submission_date 2003-05-19 _Accession_date 2003-05-20 _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 Yokota Atsushi . . 2 Hirai Kenichi . . 3 Miyauchi Hiroyo . . 4 Noda Yasuo . . 5 Inoue Kyouko . . 6 Akasaka Kazuyuki . . 7 Tachibana Hideki . . 8 Segawa Shin-ichi . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 658 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-09-14 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5068 'Recombinant hen lysozyme with extra N-terminal Met' 5069 'Two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]' 5803 'Three-disulfide variant of hen lysozyme: C64A/C80A' stop_ _Original_release_date 2004-09-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR characterization of three-disulfide variants of lysozyme, C64A/C80A, C76A/C94A, and C30A/C115A--a marginally stable state in folded proteins. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15157100 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yokota Atsushi . . 2 Hirai Kenichi . . 3 Miyauchi Hiroyo . . 4 Iimura Satoshi . . 5 Noda Yasuo . . 6 Inoue Kyouko . . 7 Akasaka Kazuyuki . . 8 Tachibana Hideki . . 9 Segawa Shin-ichi . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 43 _Journal_issue 21 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6663 _Page_last 6669 _Year 2004 _Details . loop_ _Keyword 'Lysozyme Variants' NMR 'Protein Folding' 'Three-Disulfide Intermediate' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; van den Berg B, Chung EW, Robinson CV, Dobson CM. Characterisation of the dominant oxidative folding intermediate of hen lysozyme. J Mol Biol. 1999 Jul 16;290(3):781-96. ; _Citation_title 'Characterisation of the dominant oxidative folding intermediate of hen lysozyme.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10395829 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 'van den Berg' B . . 2 Chung 'E W' W. . 3 Robinson 'C V' V. . 4 Dobson 'C M' M. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 290 _Journal_issue 3 _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 781 _Page_last 796 _Year 1999 _Details ; Reduced denatured lysozyme has been oxidised and refolded at pH values close to neutral in an efficient way by dilution from buffers containing 8.0 M urea, and refolding intermediates were separated by reverse-phase HPLC at pH 2. By using peptic digestion in combination with high-resolution Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry (MS) and tandem MS/MS the dominant intermediate was identified to be des-[76-94]. This species has three of the four native disulphide bonds, but lacks the Cys76-Cys94 disulphide bond which connects the two folding domains in the native protein. Characterisation of des-[76-94] by 2D1H NMR shows that it has a highly native-like structure. This provides an explanation for the accumulation of this species during refolding as direct oxidation to the fully native protein will be restricted by the burial of Cys94 in the protein interior. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Noda Y, Yokota A, Horii D, Tominaga T, Tanisaka Y, Tachibana H, Segawa S. NMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]--a disulfide intermediate with a partly unfolded structure. Biochemistry. 2002 Feb 19;41(7):2130-9. ; _Citation_title 'NMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]--a disulfide intermediate with a partly unfolded structure.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11841203 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Noda Yasuo . . 2 Yokota Atsushi . . 3 Horii Daisuke . . 4 Tominaga Takeshi . . 5 Tanisaka Yoshiaki . . 6 Tachibana Hideki . . 7 Segawa Shin-ichi . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 41 _Journal_issue 7 _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 2130 _Page_last 2139 _Year 2002 _Details ; The 15N-labeled recombinant hen lysozyme and two species of two-disulfide variants, denoted as 2SS[6-127, 30-115] and 2SS[64-80, 76-94], were studied by means of NMR spectroscopy. The former variant contains two disulfide bridges in the alpha-domain, while the latter has one disulfide bridge in the beta-domain and the other one at the interface between two domains. Resonance assignments were performed using 3D TOCSY-HSQC and NOESY-HSQC spectra. The 15N-1H-HSQC spectrum of 2SS[6-127, 30-115] was similar to that of recombinant lysozyme as a whole, although a number of cross-peaks disappeared. On the other hand, the HSQC spectrum of 2SS[64-80, 76-94] was characteristic of unfolded proteins. The structure of 2SS[6-127, 30-115] was thoroughly examined on the basis of NOE contacts determined by NMR spectroscopy. The structure of the alpha-domain was quite similar to that of authentic lysozyme, while the beta-domain was largely unstructured. However, NMR data clearly demonstrated that some residual structures exist in the beta-domain. The beta1 and beta2 strands were maintained stably as an antiparallel beta-sheet. In addition, the residues 55 and 56 were located in the vicinity of the end of the B-helix. Further, the C-helix was properly set with side-chains of I88, V92, K96, and V99 facing toward the hydrophobic core in the alpha-domain. These residual structures inherent in the amino acid sequence were evaluated concerning the folding process of lysozyme. Our experiments imply that the establishment of the backbone conformation ranging from residues 76-99 plays a key role in attaining the cooperativity between two domains required for the folding transition. ; save_ ################################## # Molecular system description # ################################## save_system_HEWL _Saveframe_category molecular_system _Mol_system_name 'hen egg white lysozyme' _Abbreviation_common HEWL _Enzyme_commission_number 3.2.1.17 loop_ _Mol_system_component_name _Mol_label 'hen lysozyme CYS mutants, C76A/C94A' $HEWL stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function Hydrolase(O-Glycosyl) stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HEWL _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'three-disulfide variant of hen lysozyme' _Name_variant C76A/C94A _Abbreviation_common C76A/C94A _Molecular_mass 14374 _Mol_thiol_state 'all disulfide bound' _Details ; Hen lysozyme with Cys76 and Cys94 replaced by Ala and three disulfide bridges between Cys6 and Cys127, between Cys30 and Cys115, and between Cys64 and Cys80. ; ############################## # Polymer residue sequence # ############################## _Residue_count 130 _Mol_residue_sequence ; MKVFGRCELAAAMKRHGLDN YRGYSLGNWVCAAKFESNFN TQATNRNTDGSTDYGILQIN SRWWCNDGRTPGSRNLANIP CSALLSSDITASVNAAKKIV SDGNGMNAWVAWRNRCKGTD VQAWIRGCRL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 MET 2 1 LYS 3 2 VAL 4 3 PHE 5 4 GLY 6 5 ARG 7 6 CYS 8 7 GLU 9 8 LEU 10 9 ALA 11 10 ALA 12 11 ALA 13 12 MET 14 13 LYS 15 14 ARG 16 15 HIS 17 16 GLY 18 17 LEU 19 18 ASP 20 19 ASN 21 20 TYR 22 21 ARG 23 22 GLY 24 23 TYR 25 24 SER 26 25 LEU 27 26 GLY 28 27 ASN 29 28 TRP 30 29 VAL 31 30 CYS 32 31 ALA 33 32 ALA 34 33 LYS 35 34 PHE 36 35 GLU 37 36 SER 38 37 ASN 39 38 PHE 40 39 ASN 41 40 THR 42 41 GLN 43 42 ALA 44 43 THR 45 44 ASN 46 45 ARG 47 46 ASN 48 47 THR 49 48 ASP 50 49 GLY 51 50 SER 52 51 THR 53 52 ASP 54 53 TYR 55 54 GLY 56 55 ILE 57 56 LEU 58 57 GLN 59 58 ILE 60 59 ASN 61 60 SER 62 61 ARG 63 62 TRP 64 63 TRP 65 64 CYS 66 65 ASN 67 66 ASP 68 67 GLY 69 68 ARG 70 69 THR 71 70 PRO 72 71 GLY 73 72 SER 74 73 ARG 75 74 ASN 76 75 LEU 77 76 ALA 78 77 ASN 79 78 ILE 80 79 PRO 81 80 CYS 82 81 SER 83 82 ALA 84 83 LEU 85 84 LEU 86 85 SER 87 86 SER 88 87 ASP 89 88 ILE 90 89 THR 91 90 ALA 92 91 SER 93 92 VAL 94 93 ASN 95 94 ALA 96 95 ALA 97 96 LYS 98 97 LYS 99 98 ILE 100 99 VAL 101 100 SER 102 101 ASP 103 102 GLY 104 103 ASN 105 104 GLY 106 105 MET 107 106 ASN 108 107 ALA 109 108 TRP 110 109 VAL 111 110 ALA 112 111 TRP 113 112 ARG 114 113 ASN 115 114 ARG 116 115 CYS 117 116 LYS 118 117 GLY 119 118 THR 120 119 ASP 121 120 VAL 122 121 GLN 123 122 ALA 124 123 TRP 125 124 ILE 126 125 ARG 127 126 GLY 128 127 CYS 129 128 ARG 130 129 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Tissue $HEWL Chicken 9031 Eukaryota Metazoa Gallus gallus 'egg white' 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 $HEWL 'recombinant technology' 'E. coli' Escherichia coli AD18 plasmid . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $HEWL . mM 0.3 1.0 [U-15N] stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 2.6 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label . save_ save_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ save_HOHAHA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HOHAHA _Sample_label . save_ save_15N_3D-NOESY-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '15N 3D-NOESY-HSQC' _Sample_label . save_ save_15N_3D-TOCSY-HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N 3D-TOCSY-HSQC' _Sample_label . save_ save_1H-15N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_15N_3D-HSQC-NOESY-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '15N 3D-HSQC-NOESY-HSQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HOHAHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '15N 3D-NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N 3D-TOCSY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '15N 3D-HSQC-NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_EX-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.8 0.1 na temperature 298 0.1 K 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 external direct . . . 1.0 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_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label DQF-COSY NOESY HOHAHA '15N 3D-NOESY-HSQC' '15N 3D-TOCSY-HSQC' '1H-15N HSQC' '15N 3D-HSQC-NOESY-HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $EX-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'hen lysozyme CYS mutants, C76A/C94A' _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 2 LYS H H 8.81 0.02 1 2 1 2 LYS HA H 4.36 0.02 1 3 2 3 VAL H H 8.82 0.02 1 4 2 3 VAL HA H 4.82 0.02 1 5 2 3 VAL HB H 2.00 0.02 1 6 2 3 VAL HG1 H 1.05 0.02 2 7 2 3 VAL HG2 H 0.94 0.02 2 8 3 4 PHE H H 8.66 0.02 1 9 3 4 PHE HA H 4.27 0.02 1 10 3 4 PHE HB2 H 3.18 0.02 2 11 3 4 PHE HB3 H 2.65 0.02 2 12 3 4 PHE HD1 H 6.98 0.02 1 13 3 4 PHE HD2 H 6.98 0.02 1 14 3 4 PHE HE1 H 7.21 0.02 1 15 3 4 PHE HE2 H 7.21 0.02 1 16 3 4 PHE HZ H 7.48 0.02 1 17 4 5 GLY H H 8.45 0.02 1 18 4 5 GLY HA2 H 4.30 0.02 2 19 4 5 GLY HA3 H 3.96 0.02 2 20 5 6 ARG H H 8.58 0.02 1 21 5 6 ARG HA H 3.37 0.02 1 22 5 6 ARG HB2 H 2.11 0.02 2 23 5 6 ARG HD2 H 3.86 0.02 2 24 5 6 ARG HE H 7.58 0.02 1 25 6 7 CYS H H 8.72 0.02 1 26 6 7 CYS HA H 4.73 0.02 1 27 6 7 CYS HB2 H 3.20 0.02 2 28 6 7 CYS HB3 H 2.78 0.02 2 29 7 8 GLU H H 8.29 0.02 1 30 7 8 GLU HA H 4.10 0.02 1 31 7 8 GLU HB2 H 2.28 0.02 2 32 7 8 GLU HB3 H 2.19 0.02 2 33 7 8 GLU HG2 H 2.35 0.02 2 34 7 8 GLU HG3 H 2.52 0.02 2 35 8 9 LEU H H 8.61 0.02 1 36 8 9 LEU HA H 3.75 0.02 1 37 8 9 LEU HB2 H 1.59 0.02 2 38 8 9 LEU HG H 1.52 0.02 1 39 8 9 LEU HD1 H 0.59 0.02 2 40 8 9 LEU HD2 H 0.00 0.02 2 41 9 10 ALA H H 8.44 0.02 1 42 9 10 ALA HA H 3.60 0.02 1 43 9 10 ALA HB H 1.57 0.02 1 44 10 11 ALA H H 8.18 0.02 1 45 10 11 ALA HA H 3.98 0.02 1 46 10 11 ALA HB H 1.56 0.02 1 47 11 12 ALA H H 7.78 0.02 1 48 11 12 ALA HA H 4.28 0.02 1 49 11 12 ALA HB H 1.50 0.02 1 50 12 13 MET H H 9.18 0.02 1 51 12 13 MET HA H 3.43 0.02 1 52 12 13 MET HB2 H 1.91 0.02 2 53 12 13 MET HB3 H 1.55 0.02 2 54 12 13 MET HG2 H 2.74 0.02 2 55 12 13 MET HG3 H 1.33 0.02 2 56 12 13 MET HE H 1.68 0.02 1 57 13 14 LYS H H 8.55 0.02 1 58 13 14 LYS HA H 3.98 0.02 1 59 13 14 LYS HB2 H 2.20 0.02 2 60 13 14 LYS HB3 H 1.86 0.02 2 61 13 14 LYS HG2 H 1.46 0.02 2 62 13 14 LYS HD2 H 1.74 0.02 2 63 13 14 LYS HD3 H 3.02 0.02 2 64 14 15 ARG H H 8.28 0.02 1 65 14 15 ARG HA H 4.12 0.02 1 66 14 15 ARG HB2 H 1.97 0.02 2 67 14 15 ARG HD2 H 3.14 0.02 2 68 14 15 ARG HE H 7.15 0.02 1 69 15 16 HIS H H 7.35 0.02 1 70 15 16 HIS HA H 4.58 0.02 1 71 15 16 HIS HB2 H 3.73 0.02 2 72 15 16 HIS HB3 H 2.57 0.02 2 73 15 16 HIS HD2 H 7.54 0.02 1 74 15 16 HIS HE1 H 8.86 0.02 1 75 16 17 GLY H H 7.62 0.02 1 76 16 17 GLY HA2 H 3.98 0.02 2 77 16 17 GLY HA3 H 4.13 0.02 2 78 17 18 LEU H H 7.19 0.02 1 79 17 18 LEU HA H 3.93 0.02 1 80 17 18 LEU HB2 H 0.73 0.02 2 81 17 18 LEU HB3 H 0.29 0.02 2 82 17 18 LEU HG H 0.69 0.02 1 83 17 18 LEU HD1 H -0.68 0.02 2 84 17 18 LEU HD2 H -0.10 0.02 2 85 18 19 ASP H H 8.80 0.02 1 86 18 19 ASP HA H 4.25 0.02 1 87 18 19 ASP HB2 H 3.01 0.02 2 88 18 19 ASP HB3 H 2.39 0.02 2 89 19 20 ASN H H 8.41 0.02 1 90 19 20 ASN HA H 3.95 0.02 1 91 19 20 ASN HB2 H 2.85 0.02 2 92 19 20 ASN HB3 H 3.05 0.02 2 93 19 20 ASN HD21 H 7.47 0.02 2 94 19 20 ASN HD22 H 6.63 0.02 2 95 20 21 TYR H H 8.13 0.02 1 96 20 21 TYR HA H 4.21 0.02 1 97 20 21 TYR HB2 H 3.04 0.02 2 98 20 21 TYR HB3 H 3.21 0.02 2 99 20 21 TYR HD1 H 7.17 0.02 1 100 20 21 TYR HD2 H 7.17 0.02 1 101 20 21 TYR HE1 H 6.94 0.02 1 102 20 21 TYR HE2 H 6.94 0.02 1 103 21 22 ARG H H 9.01 0.02 1 104 21 22 ARG HA H 3.63 0.02 1 105 21 22 ARG HB2 H 1.90 0.02 2 106 21 22 ARG HB3 H 2.23 0.02 2 107 21 22 ARG HG2 H 1.20 0.02 2 108 21 22 ARG HG3 H 1.39 0.02 2 109 21 22 ARG HD2 H 3.06 0.02 2 110 21 22 ARG HE H 7.13 0.02 1 111 22 23 GLY H H 7.63 0.02 1 112 22 23 GLY HA2 H 3.87 0.02 2 113 22 23 GLY HA3 H 3.49 0.02 2 114 23 24 TYR H H 7.67 0.02 1 115 23 24 TYR HA H 4.54 0.02 1 116 23 24 TYR HB2 H 3.30 0.02 2 117 23 24 TYR HB3 H 2.46 0.02 2 118 23 24 TYR HD1 H 7.02 0.02 1 119 23 24 TYR HD2 H 7.02 0.02 1 120 23 24 TYR HE1 H 6.71 0.02 1 121 23 24 TYR HE2 H 6.71 0.02 1 122 24 25 SER H H 9.09 0.02 1 123 24 25 SER HA H 4.51 0.02 1 124 24 25 SER HB2 H 4.20 0.02 2 125 24 25 SER HB3 H 4.37 0.02 2 126 25 26 LEU H H 9.10 0.02 1 127 25 26 LEU HA H 4.38 0.02 1 128 25 26 LEU HB2 H 1.91 0.02 2 129 25 26 LEU HG H 1.61 0.02 1 130 25 26 LEU HD1 H 0.87 0.02 2 131 25 26 LEU HD2 H 1.00 0.02 2 132 26 27 GLY H H 9.65 0.02 1 133 26 27 GLY HA2 H 4.17 0.02 2 134 26 27 GLY HA3 H 3.66 0.02 2 135 27 28 ASN H H 8.18 0.02 1 136 27 28 ASN HA H 4.18 0.02 1 137 27 28 ASN HB2 H 2.85 0.02 2 138 27 28 ASN HB3 H 2.28 0.02 2 139 27 28 ASN HD21 H 7.81 0.02 2 140 27 28 ASN HD22 H 7.75 0.02 2 141 28 29 TRP H H 7.16 0.02 1 142 28 29 TRP HA H 3.76 0.02 1 143 28 29 TRP HB2 H 3.26 0.02 2 144 28 29 TRP HB3 H 3.19 0.02 2 145 28 29 TRP HD1 H 7.24 0.02 1 146 28 29 TRP HE1 H 9.32 0.02 1 147 28 29 TRP HE3 H 6.68 0.02 1 148 28 29 TRP HZ2 H 7.43 0.02 1 149 28 29 TRP HZ3 H 6.16 0.02 1 150 28 29 TRP HH2 H 6.74 0.02 1 151 29 30 VAL H H 7.58 0.02 1 152 29 30 VAL HA H 3.44 0.02 1 153 29 30 VAL HB H 1.94 0.02 1 154 29 30 VAL HG1 H 1.26 0.02 2 155 29 30 VAL HG2 H 0.94 0.02 2 156 30 31 CYS H H 8.03 0.02 1 157 30 31 CYS HA H 2.49 0.02 1 158 30 31 CYS HB2 H 2.94 0.02 2 159 30 31 CYS HB3 H 2.60 0.02 2 160 31 32 ALA H H 8.16 0.02 1 161 31 32 ALA HA H 3.70 0.02 1 162 31 32 ALA HB H 1.00 0.02 1 163 32 33 ALA H H 7.60 0.02 1 164 32 33 ALA HA H 4.02 0.02 1 165 32 33 ALA HB H 1.32 0.02 1 166 33 34 LYS H H 7.97 0.02 1 167 33 34 LYS HA H 2.53 0.02 1 168 33 34 LYS HB2 H 1.07 0.02 2 169 33 34 LYS HG2 H 0.44 0.02 2 170 33 34 LYS HG3 H -0.50 0.02 2 171 33 34 LYS HD2 H 0.71 0.02 2 172 33 34 LYS HD3 H 0.63 0.02 2 173 33 34 LYS HE2 H 2.66 0.02 2 174 33 34 LYS HE3 H 2.31 0.02 2 175 33 34 LYS HZ H 7.33 0.02 1 176 34 35 PHE H H 7.39 0.02 1 177 34 35 PHE HA H 4.31 0.02 1 178 34 35 PHE HB2 H 2.27 0.02 2 179 34 35 PHE HB3 H 3.18 0.02 2 180 34 35 PHE HD1 H 7.22 0.02 1 181 34 35 PHE HD2 H 7.22 0.02 1 182 34 35 PHE HE1 H 7.36 0.02 1 183 34 35 PHE HE2 H 7.36 0.02 1 184 34 35 PHE HZ H 7.49 0.02 1 185 35 36 GLU H H 8.65 0.02 1 186 35 36 GLU HA H 4.42 0.02 1 187 35 36 GLU HB2 H 2.08 0.02 2 188 36 37 SER H H 8.03 0.02 1 189 36 37 SER HA H 4.57 0.02 1 190 36 37 SER HB2 H 4.42 0.02 2 191 36 37 SER HB3 H 3.58 0.02 2 192 37 38 ASN H H 8.17 0.02 1 193 37 38 ASN HA H 4.53 0.02 1 194 37 38 ASN HB2 H 3.30 0.02 2 195 37 38 ASN HB3 H 2.46 0.02 2 196 37 38 ASN HD21 H 7.38 0.02 2 197 37 38 ASN HD22 H 6.74 0.02 2 198 38 39 PHE H H 7.37 0.02 1 199 38 39 PHE HA H 3.87 0.02 1 200 38 39 PHE HB2 H 3.62 0.02 2 201 38 39 PHE HD1 H 6.95 0.02 1 202 38 39 PHE HD2 H 6.95 0.02 1 203 38 39 PHE HE1 H 7.41 0.02 1 204 38 39 PHE HE2 H 7.41 0.02 1 205 38 39 PHE HZ H 6.95 0.02 1 206 39 40 ASN H H 7.60 0.02 1 207 39 40 ASN HA H 4.95 0.02 1 208 39 40 ASN HB2 H 3.44 0.02 2 209 39 40 ASN HB3 H 2.97 0.02 2 210 39 40 ASN HD21 H 7.62 0.02 2 211 39 40 ASN HD22 H 7.03 0.02 2 212 41 42 GLN H H 8.08 0.02 1 213 41 42 GLN HA H 4.51 0.02 1 214 41 42 GLN HB2 H 2.46 0.02 2 215 41 42 GLN HB3 H 1.89 0.02 2 216 41 42 GLN HE21 H 7.66 0.02 2 217 41 42 GLN HE22 H 6.84 0.02 2 218 42 43 ALA H H 6.86 0.02 1 219 42 43 ALA HA H 4.11 0.02 1 220 42 43 ALA HB H 1.34 0.02 1 221 43 44 THR H H 8.37 0.02 1 222 43 44 THR HA H 5.11 0.02 1 223 43 44 THR HB H 3.71 0.02 1 224 43 44 THR HG2 H 1.03 0.02 1 225 44 45 ASN H H 8.18 0.02 1 226 44 45 ASN HA H 5.00 0.02 1 227 44 45 ASN HB2 H 2.69 0.02 2 228 44 45 ASN HD21 H 7.42 0.02 2 229 44 45 ASN HD22 H 6.91 0.02 2 230 45 46 ARG H H 8.91 0.02 1 231 45 46 ARG HA H 4.50 0.02 1 232 45 46 ARG HB2 H 1.69 0.02 2 233 45 46 ARG HB3 H 1.82 0.02 2 234 45 46 ARG HG2 H 1.62 0.02 2 235 45 46 ARG HD2 H 3.13 0.02 2 236 45 46 ARG HE H 7.08 0.02 1 237 46 47 ASN H H 8.97 0.02 1 238 46 47 ASN HA H 5.11 0.02 1 239 46 47 ASN HB2 H 2.82 0.02 2 240 46 47 ASN HB3 H 2.89 0.02 2 241 46 47 ASN HD21 H 6.96 0.02 2 242 46 47 ASN HD22 H 6.83 0.02 2 243 47 48 THR H H 8.89 0.02 1 244 47 48 THR HA H 4.08 0.02 1 245 47 48 THR HB H 4.34 0.02 1 246 47 48 THR HG2 H 1.35 0.02 1 247 48 49 ASP H H 7.83 0.02 1 248 48 49 ASP HA H 4.55 0.02 1 249 48 49 ASP HB2 H 2.66 0.02 2 250 48 49 ASP HB3 H 3.08 0.02 2 251 49 50 GLY H H 7.94 0.02 1 252 49 50 GLY HA2 H 4.32 0.02 2 253 49 50 GLY HA3 H 3.75 0.02 2 254 50 51 SER H H 8.30 0.02 1 255 50 51 SER HA H 4.55 0.02 1 256 50 51 SER HB2 H 3.83 0.02 2 257 50 51 SER HB3 H 4.12 0.02 2 258 51 52 THR H H 9.24 0.02 1 259 51 52 THR HA H 4.88 0.02 1 260 51 52 THR HB H 3.74 0.02 1 261 51 52 THR HG2 H 0.26 0.02 1 262 52 53 ASP H H 8.74 0.02 1 263 52 53 ASP HA H 5.29 0.02 1 264 52 53 ASP HB2 H 2.64 0.02 2 265 52 53 ASP HB3 H 1.99 0.02 2 266 53 54 TYR H H 9.11 0.02 1 267 53 54 TYR HA H 4.78 0.02 1 268 53 54 TYR HB2 H 2.94 0.02 2 269 53 54 TYR HB3 H 2.62 0.02 2 270 53 54 TYR HD1 H 7.08 0.02 1 271 53 54 TYR HD2 H 7.08 0.02 1 272 53 54 TYR HE1 H 6.83 0.02 1 273 53 54 TYR HE2 H 6.83 0.02 1 274 54 55 GLY H H 9.21 0.02 1 275 54 55 GLY HA2 H 4.48 0.02 2 276 54 55 GLY HA3 H 4.07 0.02 2 277 55 56 ILE H H 9.46 0.02 1 278 55 56 ILE HA H 4.28 0.02 1 279 55 56 ILE HB H 1.64 0.02 1 280 55 56 ILE HG12 H 1.09 0.02 2 281 55 56 ILE HG13 H 1.50 0.02 2 282 55 56 ILE HG2 H 0.92 0.02 1 283 55 56 ILE HD1 H 0.75 0.02 1 284 56 57 LEU H H 9.16 0.02 1 285 56 57 LEU HA H 4.44 0.02 1 286 56 57 LEU HB2 H 1.79 0.02 2 287 56 57 LEU HB3 H 1.52 0.02 2 288 56 57 LEU HG H 1.20 0.02 1 289 56 57 LEU HD1 H 0.53 0.02 2 290 56 57 LEU HD2 H 0.34 0.02 2 291 57 58 GLN H H 7.98 0.02 1 292 57 58 GLN HA H 3.38 0.02 1 293 57 58 GLN HB2 H 2.20 0.02 2 294 57 58 GLN HG2 H 0.82 0.02 2 295 57 58 GLN HE21 H 5.24 0.02 2 296 57 58 GLN HE22 H 8.33 0.02 2 297 58 59 ILE H H 7.73 0.02 1 298 58 59 ILE HA H 4.05 0.02 1 299 58 59 ILE HB H 2.04 0.02 1 300 58 59 ILE HG2 H 0.91 0.02 1 301 59 60 ASN H H 8.68 0.02 1 302 59 60 ASN HA H 5.53 0.02 1 303 59 60 ASN HB2 H 3.00 0.02 2 304 59 60 ASN HB3 H 3.35 0.02 2 305 60 61 SER H H 9.09 0.02 1 306 60 61 SER HA H 5.16 0.02 1 307 61 62 ARG H H 8.79 0.02 1 308 61 62 ARG HA H 3.98 0.02 1 309 61 62 ARG HB2 H 1.51 0.02 2 310 61 62 ARG HB3 H 1.35 0.02 2 311 61 62 ARG HG2 H 0.87 0.02 2 312 61 62 ARG HG3 H 0.42 0.02 2 313 61 62 ARG HD2 H 2.81 0.02 2 314 61 62 ARG HE H 6.73 0.02 1 315 62 63 TRP H H 7.17 0.02 1 316 62 63 TRP HA H 4.57 0.02 1 317 62 63 TRP HB2 H 1.95 0.02 2 318 62 63 TRP HB3 H 2.04 0.02 2 319 62 63 TRP HD1 H 6.98 0.02 1 320 62 63 TRP HE1 H 10.16 0.02 1 321 62 63 TRP HE3 H 7.26 0.02 1 322 62 63 TRP HZ2 H 7.43 0.02 1 323 62 63 TRP HZ3 H 7.05 0.02 1 324 62 63 TRP HH2 H 7.18 0.02 1 325 63 64 TRP H H 7.51 0.02 1 326 63 64 TRP HA H 5.00 0.02 1 327 63 64 TRP HB2 H 3.31 0.02 2 328 63 64 TRP HD1 H 7.53 0.02 1 329 63 64 TRP HE1 H 10.28 0.02 1 330 63 64 TRP HE3 H 7.52 0.02 1 331 63 64 TRP HZ2 H 7.29 0.02 1 332 63 64 TRP HZ3 H 6.96 0.02 1 333 63 64 TRP HH2 H 7.10 0.02 1 334 64 65 CYS H H 7.65 0.02 1 335 64 65 CYS HA H 5.32 0.02 1 336 64 65 CYS HB2 H 2.69 0.02 2 337 65 66 ASN H H 8.65 0.02 1 338 65 66 ASN HA H 5.57 0.02 1 339 65 66 ASN HB2 H 2.81 0.02 2 340 65 66 ASN HB3 H 2.57 0.02 2 341 65 66 ASN HD21 H 6.91 0.02 2 342 65 66 ASN HD22 H 7.53 0.02 2 343 66 67 ASP H H 9.91 0.02 1 344 66 67 ASP HA H 4.91 0.02 1 345 66 67 ASP HB2 H 3.23 0.02 2 346 66 67 ASP HB3 H 2.24 0.02 2 347 67 68 GLY H H 8.28 0.02 1 348 67 68 GLY HA2 H 4.13 0.02 2 349 67 68 GLY HA3 H 3.89 0.02 2 350 68 69 ARG H H 8.12 0.02 1 351 68 69 ARG HA H 4.77 0.02 1 352 68 69 ARG HB2 H 1.81 0.02 2 353 68 69 ARG HG2 H 1.47 0.02 2 354 68 69 ARG HD2 H 3.10 0.02 2 355 68 69 ARG HD3 H 3.18 0.02 2 356 68 69 ARG HE H 7.02 0.02 1 357 69 70 THR H H 8.38 0.02 1 358 69 70 THR HA H 4.58 0.02 1 359 69 70 THR HB H 4.15 0.02 1 360 69 70 THR HG2 H 0.87 0.02 1 361 70 71 PRO HA H 4.35 0.02 1 362 70 71 PRO HB2 H 2.30 0.02 2 363 70 71 PRO HB3 H 1.90 0.02 2 364 70 71 PRO HG2 H 1.98 0.02 2 365 70 71 PRO HD2 H 3.60 0.02 2 366 70 71 PRO HD3 H 4.15 0.02 2 367 71 72 GLY H H 8.77 0.02 1 368 71 72 GLY HA2 H 3.89 0.02 2 369 71 72 GLY HA3 H 3.68 0.02 2 370 72 73 SER H H 7.46 0.02 1 371 72 73 SER HA H 4.45 0.02 1 372 73 74 ARG H H 8.45 0.02 1 373 73 74 ARG HA H 4.33 0.02 1 374 73 74 ARG HB2 H 1.70 0.02 2 375 73 74 ARG HG2 H 1.62 0.02 2 376 73 74 ARG HG3 H 1.52 0.02 2 377 73 74 ARG HD2 H 3.00 0.02 2 378 73 74 ARG HE H 7.07 0.02 1 379 74 75 ASN H H 8.61 0.02 1 380 74 75 ASN HA H 4.17 0.02 1 381 74 75 ASN HB2 H 2.92 0.02 2 382 74 75 ASN HB3 H 2.38 0.02 2 383 74 75 ASN HD21 H 7.32 0.02 2 384 74 75 ASN HD22 H 6.53 0.02 2 385 75 76 LEU H H 8.57 0.02 1 386 75 76 LEU HA H 4.16 0.02 1 387 75 76 LEU HB2 H 1.58 0.02 2 388 75 76 LEU HG H 1.56 0.02 1 389 75 76 LEU HD1 H 0.64 0.02 2 390 75 76 LEU HD2 H 0.81 0.02 2 391 76 77 ALA H H 8.58 0.02 1 392 76 77 ALA HA H 4.53 0.02 1 393 76 77 ALA HB H 1.47 0.02 1 394 77 78 ASN H H 8.08 0.02 1 395 77 78 ASN HA H 4.45 0.02 1 396 77 78 ASN HB2 H 2.65 0.02 2 397 77 78 ASN HB3 H 2.99 0.02 2 398 77 78 ASN HD21 H 6.75 0.02 2 399 77 78 ASN HD22 H 7.48 0.02 2 400 78 79 ILE HB H 1.75 0.02 1 401 78 79 ILE HG12 H 1.20 0.02 2 402 78 79 ILE HG13 H 1.53 0.02 2 403 78 79 ILE HG2 H 0.88 0.02 1 404 78 79 ILE HD1 H 0.92 0.02 1 405 79 80 PRO HA H 5.06 0.02 1 406 79 80 PRO HB2 H 2.36 0.02 2 407 79 80 PRO HB3 H 2.02 0.02 2 408 80 81 CYS H H 8.43 0.02 1 409 80 81 CYS HA H 3.88 0.02 1 410 80 81 CYS HB2 H 1.79 0.02 2 411 80 81 CYS HB3 H 1.17 0.02 2 412 81 82 SER H H 8.56 0.02 1 413 81 82 SER HA H 3.79 0.02 1 414 82 83 ALA H H 7.52 0.02 1 415 82 83 ALA HA H 4.23 0.02 1 416 82 83 ALA HB H 1.49 0.02 1 417 83 84 LEU H H 7.78 0.02 1 418 83 84 LEU HA H 4.26 0.02 1 419 83 84 LEU HB2 H 2.01 0.02 2 420 83 84 LEU HG H 1.64 0.02 1 421 83 84 LEU HD1 H 0.72 0.02 2 422 83 84 LEU HD2 H 0.97 0.02 2 423 84 85 LEU H H 7.06 0.02 1 424 84 85 LEU HA H 4.98 0.02 1 425 84 85 LEU HB2 H 1.88 0.02 2 426 84 85 LEU HG H 1.67 0.02 1 427 84 85 LEU HD1 H 0.96 0.02 2 428 84 85 LEU HD2 H 1.03 0.02 2 429 85 86 SER H H 6.96 0.02 1 430 85 86 SER HA H 4.54 0.02 1 431 85 86 SER HB2 H 4.11 0.02 2 432 85 86 SER HB3 H 3.83 0.02 2 433 86 87 SER H H 8.46 0.02 1 434 86 87 SER HA H 4.23 0.02 1 435 86 87 SER HB2 H 3.82 0.02 2 436 86 87 SER HB3 H 3.92 0.02 2 437 87 88 ASP H H 8.21 0.02 1 438 87 88 ASP HA H 4.91 0.02 1 439 87 88 ASP HB2 H 2.94 0.02 2 440 87 88 ASP HB3 H 2.61 0.02 2 441 88 89 ILE H H 8.13 0.02 1 442 88 89 ILE HA H 4.69 0.02 1 443 88 89 ILE HB H 1.81 0.02 1 444 88 89 ILE HG12 H 0.31 0.02 2 445 88 89 ILE HG13 H 1.11 0.02 2 446 88 89 ILE HG2 H 0.77 0.02 1 447 88 89 ILE HD1 H 0.18 0.02 1 448 89 90 THR H H 8.34 0.02 1 449 89 90 THR HA H 3.08 0.02 1 450 89 90 THR HB H 4.06 0.02 1 451 89 90 THR HG2 H 1.16 0.02 1 452 90 91 ALA H H 9.18 0.02 1 453 90 91 ALA HA H 4.10 0.02 1 454 90 91 ALA HB H 1.36 0.02 1 455 91 92 SER H H 7.70 0.02 1 456 91 92 SER HA H 4.17 0.02 1 457 91 92 SER HB2 H 3.97 0.02 2 458 91 92 SER HB3 H 3.49 0.02 2 459 92 93 VAL H H 8.38 0.02 1 460 92 93 VAL HA H 3.10 0.02 1 461 92 93 VAL HB H 1.97 0.02 1 462 92 93 VAL HG1 H 0.46 0.02 2 463 92 93 VAL HG2 H 0.62 0.02 2 464 93 94 ASN H H 8.51 0.02 1 465 93 94 ASN HA H 4.26 0.02 1 466 93 94 ASN HB2 H 2.90 0.02 2 467 93 94 ASN HB3 H 2.76 0.02 2 468 93 94 ASN HD21 H 6.99 0.02 2 469 93 94 ASN HD22 H 7.68 0.02 2 470 94 95 ALA H H 7.93 0.02 1 471 94 95 ALA HA H 4.13 0.02 1 472 94 95 ALA HB H 1.43 0.02 1 473 95 96 ALA H H 8.43 0.02 1 474 95 96 ALA HA H 4.12 0.02 1 475 95 96 ALA HB H 1.51 0.02 1 476 96 97 LYS H H 8.27 0.02 1 477 96 97 LYS HA H 3.70 0.02 1 478 96 97 LYS HB2 H 1.65 0.02 2 479 96 97 LYS HB3 H 1.10 0.02 2 480 96 97 LYS HG2 H -0.50 0.02 2 481 96 97 LYS HD2 H 1.25 0.02 2 482 96 97 LYS HE2 H 2.04 0.02 2 483 97 98 LYS H H 7.19 0.02 1 484 97 98 LYS HA H 4.09 0.02 1 485 97 98 LYS HB2 H 2.19 0.02 2 486 98 99 ILE H H 7.88 0.02 1 487 98 99 ILE HA H 2.79 0.02 1 488 98 99 ILE HB H 1.43 0.02 1 489 98 99 ILE HG12 H -1.39 0.02 2 490 98 99 ILE HG13 H 0.51 0.02 2 491 98 99 ILE HG2 H -0.23 0.02 1 492 98 99 ILE HD1 H 0.11 0.02 1 493 99 100 VAL H H 8.41 0.02 1 494 99 100 VAL HA H 3.94 0.02 1 495 99 100 VAL HB H 2.45 0.02 1 496 99 100 VAL HG1 H 1.16 0.02 2 497 99 100 VAL HG2 H 1.37 0.02 2 498 100 101 SER H H 7.63 0.02 1 499 100 101 SER HA H 4.47 0.02 1 500 100 101 SER HB2 H 4.13 0.02 2 501 101 102 ASP H H 7.91 0.02 1 502 101 102 ASP HA H 4.77 0.02 1 503 101 102 ASP HB2 H 3.09 0.02 2 504 101 102 ASP HB3 H 3.03 0.02 2 505 102 103 GLY H H 8.20 0.02 1 506 102 103 GLY HA2 H 3.93 0.02 2 507 102 103 GLY HA3 H 4.25 0.02 2 508 103 104 ASN H H 8.18 0.02 1 509 103 104 ASN HA H 5.00 0.02 1 510 103 104 ASN HB2 H 2.69 0.02 2 511 103 104 ASN HB3 H 2.82 0.02 2 512 103 104 ASN HD21 H 7.58 0.02 2 513 103 104 ASN HD22 H 6.95 0.02 2 514 104 105 GLY H H 8.35 0.02 1 515 104 105 GLY HA2 H 4.09 0.02 2 516 104 105 GLY HA3 H 4.24 0.02 2 517 105 106 MET H H 7.17 0.02 1 518 105 106 MET HA H 3.87 0.02 1 519 105 106 MET HB2 H -1.04 0.02 2 520 105 106 MET HB3 H 0.46 0.02 2 521 105 106 MET HG2 H 0.54 0.02 2 522 105 106 MET HG3 H -0.10 0.02 2 523 105 106 MET HE H -0.05 0.02 1 524 106 107 ASN H H 7.70 0.02 1 525 106 107 ASN HA H 4.47 0.02 1 526 106 107 ASN HB2 H 3.04 0.02 2 527 106 107 ASN HB3 H 2.81 0.02 2 528 107 108 ALA H H 6.75 0.02 1 529 107 108 ALA HA H 3.86 0.02 1 530 107 108 ALA HB H 0.64 0.02 1 531 108 109 TRP H H 7.91 0.02 1 532 108 109 TRP HA H 4.64 0.02 1 533 108 109 TRP HB2 H 3.38 0.02 2 534 108 109 TRP HB3 H 3.25 0.02 2 535 108 109 TRP HD1 H 7.03 0.02 1 536 108 109 TRP HE1 H 10.17 0.02 1 537 108 109 TRP HE3 H 7.40 0.02 1 538 108 109 TRP HZ2 H 6.95 0.02 1 539 108 109 TRP HZ3 H 6.52 0.02 1 540 108 109 TRP HH2 H 7.33 0.02 1 541 109 110 VAL H H 8.96 0.02 1 542 109 110 VAL HA H 3.62 0.02 1 543 109 110 VAL HB H 2.16 0.02 1 544 109 110 VAL HG1 H 1.03 0.02 2 545 109 110 VAL HG2 H 1.12 0.02 2 546 110 111 ALA H H 8.03 0.02 1 547 110 111 ALA HA H 4.27 0.02 1 548 110 111 ALA HB H 1.32 0.02 1 549 111 112 TRP H H 7.25 0.02 1 550 111 112 TRP HA H 3.71 0.02 1 551 111 112 TRP HB2 H 4.08 0.02 2 552 111 112 TRP HB3 H 2.78 0.02 2 553 111 112 TRP HD1 H 7.02 0.02 1 554 111 112 TRP HE1 H 10.40 0.02 1 555 111 112 TRP HE3 H 7.28 0.02 1 556 111 112 TRP HZ2 H 7.49 0.02 1 557 111 112 TRP HZ3 H 7.03 0.02 1 558 111 112 TRP HH2 H 7.36 0.02 1 559 112 113 ARG H H 8.30 0.02 1 560 112 113 ARG HA H 3.37 0.02 1 561 112 113 ARG HB2 H 2.00 0.02 2 562 112 113 ARG HB3 H 2.11 0.02 2 563 112 113 ARG HG2 H 1.81 0.02 2 564 112 113 ARG HD2 H 3.36 0.02 2 565 112 113 ARG HD3 H 3.44 0.02 2 566 112 113 ARG HE H 7.31 0.02 1 567 113 114 ASN H H 8.00 0.02 1 568 113 114 ASN HA H 4.50 0.02 1 569 113 114 ASN HB2 H 2.67 0.02 2 570 113 114 ASN HD21 H 7.64 0.02 2 571 113 114 ASN HD22 H 6.91 0.02 2 572 114 115 ARG H H 7.67 0.02 1 573 114 115 ARG HA H 4.30 0.02 1 574 114 115 ARG HB2 H 1.16 0.02 2 575 114 115 ARG HB3 H 0.57 0.02 2 576 114 115 ARG HG2 H 1.08 0.02 2 577 114 115 ARG HG3 H 1.01 0.02 2 578 114 115 ARG HD2 H 2.63 0.02 2 579 114 115 ARG HD3 H 2.76 0.02 2 580 114 115 ARG HE H 7.03 0.02 1 581 115 116 CYS H H 7.38 0.02 1 582 115 116 CYS HA H 4.52 0.02 1 583 115 116 CYS HB2 H 2.48 0.02 2 584 115 116 CYS HB3 H 2.59 0.02 2 585 116 117 LYS H H 7.07 0.02 1 586 116 117 LYS HA H 3.44 0.02 1 587 116 117 LYS HB2 H 1.23 0.02 2 588 116 117 LYS HB3 H -0.24 0.02 2 589 116 117 LYS HG2 H 1.05 0.02 2 590 116 117 LYS HG3 H 1.68 0.02 2 591 116 117 LYS HD2 H 1.57 0.02 2 592 116 117 LYS HE2 H 3.06 0.02 2 593 117 118 GLY H H 8.75 0.02 1 594 117 118 GLY HA2 H 4.13 0.02 2 595 117 118 GLY HA3 H 3.80 0.02 2 596 118 119 THR H H 7.67 0.02 1 597 118 119 THR HA H 4.74 0.02 1 598 118 119 THR HB H 4.30 0.02 1 599 118 119 THR HG2 H 0.94 0.02 1 600 119 120 ASP H H 8.73 0.02 1 601 119 120 ASP HA H 5.00 0.02 1 602 119 120 ASP HB2 H 2.94 0.02 2 603 120 121 VAL H H 8.17 0.02 1 604 120 121 VAL HA H 4.35 0.02 1 605 120 121 VAL HB H 2.14 0.02 1 606 120 121 VAL HG1 H 1.07 0.02 2 607 120 121 VAL HG2 H 1.12 0.02 2 608 121 122 GLN H H 8.50 0.02 1 609 121 122 GLN HA H 4.33 0.02 1 610 121 122 GLN HB2 H 2.27 0.02 2 611 121 122 GLN HE21 H 7.73 0.02 2 612 121 122 GLN HE22 H 6.95 0.02 2 613 122 123 ALA H H 7.71 0.02 1 614 122 123 ALA HA H 3.82 0.02 1 615 122 123 ALA HB H 1.16 0.02 1 616 123 124 TRP H H 7.62 0.02 1 617 123 124 TRP HA H 4.10 0.02 1 618 123 124 TRP HB2 H 3.41 0.02 2 619 123 124 TRP HB3 H 3.49 0.02 2 620 123 124 TRP HD1 H 7.54 0.02 1 621 123 124 TRP HE1 H 10.80 0.02 1 622 123 124 TRP HE3 H 7.50 0.02 1 623 123 124 TRP HZ2 H 7.77 0.02 1 624 123 124 TRP HZ3 H 7.13 0.02 1 625 123 124 TRP HH2 H 7.11 0.02 1 626 124 125 ILE H H 7.56 0.02 1 627 124 125 ILE HA H 4.73 0.02 1 628 124 125 ILE HB H 2.21 0.02 1 629 124 125 ILE HG12 H 1.24 0.02 2 630 124 125 ILE HG13 H 1.44 0.02 2 631 124 125 ILE HG2 H 0.82 0.02 1 632 124 125 ILE HD1 H 0.95 0.02 1 633 125 126 ARG H H 7.34 0.02 1 634 125 126 ARG HA H 4.16 0.02 1 635 125 126 ARG HB2 H 1.80 0.02 2 636 125 126 ARG HB3 H 2.00 0.02 2 637 125 126 ARG HD2 H 3.14 0.02 2 638 125 126 ARG HD3 H 3.19 0.02 2 639 125 126 ARG HE H 7.35 0.02 1 640 126 127 GLY H H 9.19 0.02 1 641 126 127 GLY HA2 H 4.29 0.02 2 642 126 127 GLY HA3 H 3.74 0.02 2 643 127 128 CYS H H 7.47 0.02 1 644 127 128 CYS HA H 4.90 0.02 1 645 127 128 CYS HB2 H 3.08 0.02 2 646 127 128 CYS HB3 H 2.64 0.02 2 647 128 129 ARG H H 8.97 0.02 1 648 128 129 ARG HA H 4.35 0.02 1 649 128 129 ARG HB2 H 1.77 0.02 2 650 128 129 ARG HD2 H 3.20 0.02 2 651 128 129 ARG HE H 7.17 0.02 1 652 129 130 LEU H H 8.03 0.02 1 653 129 130 LEU HA H 4.28 0.02 1 654 129 130 LEU HB2 H 1.46 0.02 2 655 129 130 LEU HB3 H 1.65 0.02 2 656 129 130 LEU HG H 1.40 0.02 1 657 129 130 LEU HD1 H 0.73 0.02 2 658 129 130 LEU HD2 H 0.85 0.02 2 stop_ save_