data_4159 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of LSIII, a Long Neurotoxin from the Venom of Laticauda semifasciata ; _BMRB_accession_number 4159 _BMRB_flat_file_name bmr4159.str _Entry_type original _Submission_date 1998-07-09 _Accession_date 1998-07-09 _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 Connolly Peter J. . 2 Stern Alan S. . 3 Hoch Jeffrey C. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 343 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-03-02 original author . stop_ _Original_release_date 2000-03-02 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure of LSIII, a Long Neurotoxin from the Venom of Laticauda semifasciata ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 96140214 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Connolly Peter J. . 2 Stern Alan S. . 3 Hoch Jeffrey C. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 35 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 418 _Page_last 426 _Year 1996 _Details . loop_ _Keyword 'Long Neurotoxin 1' LSIII NMR 'nuclear magnetic resonance' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Hoch, J. C., and Stern, A.S., The Rowland NMR Toolkit v3, The Rowland Institute for Science, Cambridge MA. ; _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_ save_citation_two _Saveframe_category citation _Citation_full ; Eccles, C., Guntert, P., Billeter, M., and Wutrich, K. J. Biol. NMR, 1, 111-130, (1991). ; _Citation_title 'Efficient analysis of protein 2D NMR spectra using the software package EASY.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 1726780 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Eccles C . . 2 Guntert P . . 3 Billeter M . . 4 Wutrich K . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 1 _Journal_issue 2 _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 111 _Page_last 130 _Year 1991 _Details ; The program EASY supports the spectral analysis of biomacromolecular two-dimensional (2D) nuclear magnetic resonance (NMR) data. It provides a user-friendly, window-based environment in which to view spectra for interactive interpretation. In addition, it includes a number of automated routines for peak-picking, spin-system identification, sequential resonance assignment in polypeptide chains, and cross peak integration. In this uniform environment, all resulting parameter lists can be recorded on disk, so that the paper plots and handwritten notes which normally accompany manual assignment of spectra can be largely eliminated. For example, in a protein structure determination by 2D 1H NMR, EASY accepts the frequency domain datasets as input, and after combined use of the automated and interactive routines it can yield a listing of conformational constraints in the format required as input for the calculation of the 3D structure. The program was extensively tested with current protein structure determinations in our laboratory. In this paper, its main features are illustrated with data on the protein basic pancreatic trypsin inhibitor. ; save_ save_citation_three _Saveframe_category citation _Citation_full ; Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995). ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _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 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_LSIII _Saveframe_category molecular_system _Mol_system_name 'Long Neurotoxin 1 (Component LSIII)' _Abbreviation_common LSIII _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label LSIII $LSIII stop_ _System_molecular_weight 7260 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function neurotoxin stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_LSIII _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Long Neurotoxin 1 (Component LSIII)' _Abbreviation_common LSIII _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 66 _Mol_residue_sequence ; RECYLNPHDTQTCPSGQEIC YVKSWCNAWCSSRGKVLEFG CAATCPSVNTGTEIKCCSAD KCNTYP ; loop_ _Residue_seq_code _Residue_label 1 ARG 2 GLU 3 CYS 4 TYR 5 LEU 6 ASN 7 PRO 8 HIS 9 ASP 10 THR 11 GLN 12 THR 13 CYS 14 PRO 15 SER 16 GLY 17 GLN 18 GLU 19 ILE 20 CYS 21 TYR 22 VAL 23 LYS 24 SER 25 TRP 26 CYS 27 ASN 28 ALA 29 TRP 30 CYS 31 SER 32 SER 33 ARG 34 GLY 35 LYS 36 VAL 37 LEU 38 GLU 39 PHE 40 GLY 41 CYS 42 ALA 43 ALA 44 THR 45 CYS 46 PRO 47 SER 48 VAL 49 ASN 50 THR 51 GLY 52 THR 53 GLU 54 ILE 55 LYS 56 CYS 57 CYS 58 SER 59 ALA 60 ASP 61 LYS 62 CYS 63 ASN 64 THR 65 TYR 66 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 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 1LSI "Lsiii (Nmr, 23 Structures)" 100.00 66 100.00 100.00 6.13e-40 DBJ BAA32991 "long chain alpha-neurotoxins (LsIII) [Laticauda semifasciata]" 100.00 69 100.00 100.00 6.78e-40 DBJ BAA32992 "long chain alpha-neurotoxins (LsIII-isoform) [Laticauda semifasciata]" 100.00 87 98.48 98.48 1.56e-39 PIR N2LT1E "long neurotoxin 1 - broad-banded blue sea krait" 100.00 66 100.00 100.00 6.13e-40 SP P01379 "RecName: Full=Alpha-elapitoxin-Ls2a; Short=Alpha-EPTX-Ls2a; AltName: Full=Long neurotoxin Ls3; AltName: Full=LsIII; AltName: Fu" 100.00 87 100.00 100.00 1.11e-40 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $LSIII 'Broad-banded blue sea krait' 8631 Eucaryota Metazoa Laticauda semifasciata 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 _Vendor_name $LSIII 'chemical synthesis' . . . . . Sigma stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $LSIII 4 mM . stop_ save_ ############################ # Computer software used # ############################ save_software_one _Saveframe_category software _Name RNMRTK _Version 3 loop_ _Task 'data processing' stop_ _Details . _Citation_label $citation_one save_ save_software_two _Saveframe_category software _Name EASY _Version . loop_ _Task 'peak assignment' stop_ _Details . _Citation_label $citation_two save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer JEQL _Model GX _Field_strength 400 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-1H_P.COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H P.COSY' _Sample_label $sample_one save_ save_1H-1H_P.E._COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H P.E. COSY' _Sample_label $sample_one save_ save_1H-1H_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _Sample_label $sample_one save_ save_1H-1H_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label $sample_one save_ save_1H-1H_RELAY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H RELAY' _Sample_label $sample_one save_ save_1H-1H_DOUBLE-RELAY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H DOUBLE-RELAY' _Sample_label $sample_one save_ save_1H-1H-1H_NOESY-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H-1H NOESY-TOCSY' _Sample_label $sample_one save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H P.COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H P.E. COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H RELAY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H DOUBLE-RELAY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H-1H NOESY-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.6 0.1 n/a temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 _Indirect_shift_ratio_citation_label DSS H 1 'methyl protons' ppm 0.00 external direct cylindrical external_to_the_sample parallel_to_Bo 1.0 $citation_three 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_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name LSIII _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 ARG H H 8.386 . 1 2 . 1 ARG HA H 5.234 . 1 3 . 1 ARG HB2 H 1.661 . 1 4 . 1 ARG HB3 H 1.661 . 1 5 . 1 ARG HG2 H 1.812 . 1 6 . 1 ARG HG3 H 1.812 . 1 7 . 1 ARG HD2 H 1.994 . 1 8 . 1 ARG HD3 H 1.994 . 1 9 . 2 GLU H H 8.317 . 1 10 . 2 GLU HA H 5.055 . 1 11 . 2 GLU HB2 H 2.463 . 1 12 . 2 GLU HB3 H 2.463 . 1 13 . 2 GLU HG2 H 3.058 . 1 14 . 2 GLU HG3 H 3.058 . 1 15 . 3 CYS H H 9.522 . 1 16 . 3 CYS HA H 4.420 . 1 17 . 3 CYS HB2 H 2.514 . 1 18 . 3 CYS HB3 H 3.043 . 1 19 . 4 TYR H H 8.486 . 1 20 . 4 TYR HA H 3.924 . 1 21 . 4 TYR HB2 H 3.257 . 2 22 . 4 TYR HB3 H 3.060 . 2 23 . 4 TYR HD1 H 6.867 . 1 24 . 4 TYR HD2 H 6.867 . 1 25 . 4 TYR HE1 H 6.631 . 1 26 . 4 TYR HE2 H 6.631 . 1 27 . 5 LEU H H 9.467 . 1 28 . 5 LEU HA H 3.250 . 1 29 . 5 LEU HB2 H 1.951 . 1 30 . 5 LEU HB3 H 1.498 . 1 31 . 5 LEU HG H 0.528 . 1 32 . 5 LEU HD1 H 0.978 . 1 33 . 5 LEU HD2 H 0.978 . 1 34 . 6 ASN H H 8.903 . 1 35 . 6 ASN HA H 4.967 . 1 36 . 6 ASN HB2 H 2.584 . 1 37 . 6 ASN HB3 H 2.584 . 1 38 . 6 ASN HD21 H 6.453 . 1 39 . 6 ASN HD22 H 6.453 . 1 40 . 7 PRO HA H 4.321 . 1 41 . 7 PRO HB2 H 2.067 . 2 42 . 7 PRO HB3 H 1.758 . 2 43 . 7 PRO HG2 H 2.252 . 2 44 . 7 PRO HG3 H 1.243 . 2 45 . 7 PRO HD2 H 3.557 . 2 46 . 7 PRO HD3 H 3.437 . 2 47 . 8 HIS H H 7.437 . 1 48 . 8 HIS HA H 4.530 . 1 49 . 8 HIS HE1 H 8.524 . 1 50 . 9 ASP H H 7.344 . 1 51 . 9 ASP HA H 3.628 . 1 52 . 9 ASP HB2 H 1.421 . 1 53 . 9 ASP HB3 H 1.421 . 1 54 . 10 THR H H 8.325 . 1 55 . 10 THR HA H 4.952 . 1 56 . 10 THR HB H 3.601 . 1 57 . 10 THR HG2 H 0.140 . 1 58 . 11 GLN H H 8.596 . 1 59 . 11 GLN HA H 4.662 . 1 60 . 11 GLN HB2 H 1.882 . 1 61 . 11 GLN HB3 H 1.882 . 1 62 . 11 GLN HG2 H 2.141 . 2 63 . 11 GLN HG3 H 2.253 . 2 64 . 11 GLN HE21 H 6.450 . 1 65 . 11 GLN HE22 H 6.450 . 1 66 . 12 THR H H 8.604 . 1 67 . 12 THR HA H 4.396 . 1 68 . 12 THR HB H 3.918 . 1 69 . 12 THR HG2 H 1.236 . 1 70 . 13 CYS H H 9.139 . 1 71 . 13 CYS HA H 4.857 . 1 72 . 13 CYS HB2 H 3.287 . 1 73 . 13 CYS HB3 H 2.808 . 1 74 . 14 PRO HA H 4.419 . 1 75 . 14 PRO HB2 H 1.641 . 2 76 . 14 PRO HB3 H 2.093 . 2 77 . 14 PRO HG2 H 1.935 . 2 78 . 14 PRO HG3 H 2.008 . 2 79 . 14 PRO HD2 H 3.414 . 2 80 . 14 PRO HD3 H 3.881 . 2 81 . 15 SER H H 7.876 . 1 82 . 15 SER HA H 4.654 . 1 83 . 15 SER HB2 H 3.883 . 2 84 . 15 SER HB3 H 3.962 . 2 85 . 16 GLY H H 8.908 . 1 86 . 16 GLY HA2 H 4.260 . 2 87 . 16 GLY HA3 H 3.744 . 2 88 . 17 GLN H H 9.049 . 1 89 . 17 GLN HA H 5.011 . 1 90 . 17 GLN HB2 H 2.374 . 1 91 . 17 GLN HB3 H 2.374 . 1 92 . 17 GLN HG2 H 2.867 . 1 93 . 17 GLN HG3 H 2.867 . 1 94 . 18 GLU H H 8.402 . 1 95 . 18 GLU HA H 4.532 . 1 96 . 18 GLU HB2 H 1.818 . 1 97 . 18 GLU HB3 H 1.818 . 1 98 . 18 GLU HG2 H 2.959 . 2 99 . 18 GLU HG3 H 3.076 . 2 100 . 19 ILE H H 8.499 . 1 101 . 19 ILE HA H 4.618 . 1 102 . 19 ILE HB H 1.883 . 1 103 . 19 ILE HG12 H 0.903 . 2 104 . 19 ILE HG13 H 1.208 . 2 105 . 19 ILE HD1 H 0.689 . 1 106 . 20 CYS H H 9.059 . 1 107 . 20 CYS HA H 5.948 . 1 108 . 20 CYS HB2 H 3.136 . 1 109 . 20 CYS HB3 H 3.136 . 1 110 . 21 TYR H H 9.075 . 1 111 . 21 TYR HA H 6.414 . 1 112 . 21 TYR HB2 H 3.019 . 1 113 . 21 TYR HB3 H 2.740 . 1 114 . 21 TYR HD1 H 6.864 . 1 115 . 21 TYR HD2 H 6.864 . 1 116 . 21 TYR HE1 H 6.735 . 1 117 . 21 TYR HE2 H 6.735 . 1 118 . 22 VAL H H 8.884 . 1 119 . 22 VAL HA H 5.113 . 1 120 . 22 VAL HB H 1.831 . 1 121 . 22 VAL HG1 H 0.769 . 2 122 . 22 VAL HG2 H -0.035 . 2 123 . 23 LYS H H 9.808 . 1 124 . 23 LYS HA H 5.485 . 1 125 . 23 LYS HB2 H 1.919 . 2 126 . 23 LYS HB3 H 1.342 . 2 127 . 23 LYS HG2 H 1.320 . 2 128 . 23 LYS HG3 H 1.564 . 2 129 . 23 LYS HD2 H 2.458 . 1 130 . 23 LYS HD3 H 2.458 . 1 131 . 24 SER H H 9.215 . 1 132 . 24 SER HA H 5.669 . 1 133 . 24 SER HB2 H 3.023 . 2 134 . 24 SER HB3 H 3.308 . 2 135 . 25 TRP H H 8.671 . 1 136 . 25 TRP HA H 5.142 . 1 137 . 25 TRP HB2 H 3.220 . 1 138 . 25 TRP HB3 H 3.743 . 1 139 . 25 TRP HD1 H 6.880 . 1 140 . 25 TRP HE1 H 10.194 . 1 141 . 25 TRP HE3 H 6.719 . 1 142 . 25 TRP HZ2 H 7.399 . 1 143 . 25 TRP HZ3 H 7.121 . 1 144 . 25 TRP HH2 H 7.120 . 1 145 . 26 CYS H H 9.039 . 1 146 . 26 CYS HA H 5.067 . 1 147 . 26 CYS HB2 H 2.980 . 2 148 . 26 CYS HB3 H 3.315 . 2 149 . 27 ASN H H 8.355 . 1 150 . 27 ASN HA H 4.910 . 1 151 . 27 ASN HB2 H 3.292 . 2 152 . 27 ASN HB3 H 2.842 . 2 153 . 27 ASN HD21 H 7.809 . 1 154 . 27 ASN HD22 H 7.809 . 1 155 . 28 ALA H H 8.183 . 1 156 . 28 ALA HA H 3.990 . 1 157 . 28 ALA HB H 0.911 . 1 158 . 29 TRP H H 7.915 . 1 159 . 29 TRP HA H 4.863 . 1 160 . 29 TRP HB2 H 3.463 . 1 161 . 29 TRP HB3 H 3.173 . 1 162 . 29 TRP HD1 H 7.160 . 1 163 . 29 TRP HE1 H 10.083 . 1 164 . 29 TRP HE3 H 7.547 . 1 165 . 29 TRP HZ2 H 7.474 . 1 166 . 29 TRP HZ3 H 7.126 . 1 167 . 29 TRP HH2 H 7.216 . 1 168 . 30 CYS H H 7.834 . 1 169 . 30 CYS HA H 4.149 . 1 170 . 30 CYS HB2 H 3.493 . 2 171 . 30 CYS HB3 H 3.167 . 2 172 . 31 SER H H 8.366 . 1 173 . 31 SER HA H 4.089 . 1 174 . 31 SER HB2 H 3.786 . 1 175 . 31 SER HB3 H 3.786 . 1 176 . 32 SER H H 7.958 . 1 177 . 32 SER HA H 4.338 . 1 178 . 32 SER HB2 H 3.698 . 1 179 . 32 SER HB3 H 3.698 . 1 180 . 33 ARG H H 7.133 . 1 181 . 33 ARG HA H 4.415 . 1 182 . 33 ARG HB2 H 1.825 . 1 183 . 33 ARG HB3 H 1.825 . 1 184 . 33 ARG HG2 H 2.361 . 1 185 . 33 ARG HG3 H 2.361 . 1 186 . 34 GLY H H 7.702 . 1 187 . 34 GLY HA2 H 3.911 . 2 188 . 34 GLY HA3 H 4.261 . 2 189 . 35 LYS H H 8.059 . 1 190 . 35 LYS HA H 4.134 . 1 191 . 35 LYS HB2 H 1.324 . 2 192 . 35 LYS HB3 H 1.334 . 2 193 . 35 LYS HG2 H 1.460 . 1 194 . 35 LYS HG3 H 1.460 . 1 195 . 36 VAL H H 8.524 . 1 196 . 36 VAL HA H 3.508 . 1 197 . 36 VAL HB H 0.256 . 1 198 . 36 VAL HG1 H 0.393 . 1 199 . 36 VAL HG2 H 0.485 . 1 200 . 37 LEU H H 7.424 . 1 201 . 37 LEU HA H 5.064 . 1 202 . 37 LEU HB2 H 1.485 . 1 203 . 37 LEU HB3 H 1.151 . 1 204 . 37 LEU HG H 0.665 . 1 205 . 37 LEU HD1 H -0.297 . 2 206 . 37 LEU HD2 H 0.500 . 2 207 . 38 GLU H H 9.025 . 1 208 . 38 GLU HA H 5.405 . 1 209 . 38 GLU HB2 H 2.838 . 1 210 . 38 GLU HB3 H 2.695 . 1 211 . 38 GLU HG2 H 3.684 . 1 212 . 38 GLU HG3 H 3.684 . 1 213 . 39 PHE H H 9.467 . 1 214 . 39 PHE HA H 5.030 . 1 215 . 39 PHE HB2 H 3.448 . 1 216 . 39 PHE HB3 H 3.448 . 1 217 . 39 PHE HD1 H 7.002 . 1 218 . 39 PHE HD2 H 7.002 . 1 219 . 39 PHE HE1 H 7.157 . 1 220 . 39 PHE HE2 H 7.157 . 1 221 . 39 PHE HZ H 7.266 . 1 222 . 40 GLY H H 7.004 . 1 223 . 40 GLY HA2 H 3.809 . 2 224 . 40 GLY HA3 H 4.029 . 2 225 . 41 CYS H H 8.266 . 1 226 . 41 CYS HA H 5.678 . 1 227 . 41 CYS HB2 H 3.435 . 1 228 . 41 CYS HB3 H 3.020 . 1 229 . 42 ALA H H 9.573 . 1 230 . 42 ALA HA H 4.524 . 1 231 . 42 ALA HB H 1.502 . 1 232 . 43 ALA H H 8.935 . 1 233 . 43 ALA HA H 4.746 . 1 234 . 43 ALA HB H 1.515 . 1 235 . 44 THR H H 7.350 . 1 236 . 44 THR HA H 4.326 . 1 237 . 44 THR HB H 3.971 . 1 238 . 44 THR HG2 H 1.079 . 1 239 . 45 CYS H H 8.915 . 1 240 . 45 CYS HA H 4.564 . 1 241 . 45 CYS HB2 H 3.076 . 1 242 . 45 CYS HB3 H 2.855 . 1 243 . 46 PRO HA H 4.087 . 1 244 . 46 PRO HB2 H 1.265 . 2 245 . 46 PRO HB3 H 2.012 . 2 246 . 46 PRO HG2 H 0.547 . 1 247 . 46 PRO HG3 H 0.547 . 1 248 . 46 PRO HD2 H 3.051 . 2 249 . 46 PRO HD3 H 3.728 . 2 250 . 47 SER H H 7.837 . 1 251 . 47 SER HA H 4.328 . 1 252 . 47 SER HB2 H 2.082 . 2 253 . 47 SER HB3 H 2.253 . 2 254 . 48 VAL H H 8.243 . 1 255 . 48 VAL HA H 4.512 . 1 256 . 48 VAL HB H 2.046 . 1 257 . 48 VAL HG1 H 0.663 . 1 258 . 48 VAL HG2 H 0.663 . 1 259 . 49 ASN H H 8.227 . 1 260 . 49 ASN HA H 4.794 . 1 261 . 49 ASN HB2 H 2.794 . 1 262 . 49 ASN HB3 H 2.635 . 1 263 . 49 ASN HD21 H 7.472 . 2 264 . 49 ASN HD22 H 5.472 . 2 265 . 50 THR H H 8.853 . 1 266 . 50 THR HA H 4.283 . 1 267 . 50 THR HB H 4.017 . 1 268 . 50 THR HG2 H 1.248 . 1 269 . 51 GLY H H 8.955 . 1 270 . 51 GLY HA2 H 3.765 . 2 271 . 51 GLY HA3 H 4.376 . 2 272 . 52 THR H H 8.130 . 1 273 . 52 THR HA H 5.001 . 1 274 . 52 THR HB H 4.152 . 1 275 . 52 THR HG2 H 1.182 . 1 276 . 53 GLU H H 8.965 . 1 277 . 53 GLU HA H 4.716 . 1 278 . 53 GLU HB2 H 2.068 . 1 279 . 53 GLU HB3 H 2.068 . 1 280 . 53 GLU HG2 H 2.312 . 1 281 . 53 GLU HG3 H 2.312 . 1 282 . 54 ILE H H 8.856 . 1 283 . 54 ILE HA H 5.295 . 1 284 . 54 ILE HB H 1.530 . 1 285 . 54 ILE HG2 H 0.859 . 1 286 . 55 LYS H H 8.356 . 1 287 . 55 LYS HA H 4.719 . 1 288 . 55 LYS HB2 H 1.730 . 2 289 . 55 LYS HB3 H 1.823 . 2 290 . 55 LYS HG2 H 1.535 . 1 291 . 55 LYS HG3 H 1.535 . 1 292 . 55 LYS HD2 H 1.770 . 1 293 . 55 LYS HD3 H 1.770 . 1 294 . 55 LYS HE2 H 2.959 . 1 295 . 55 LYS HE3 H 2.959 . 1 296 . 56 CYS H H 8.320 . 1 297 . 56 CYS HA H 4.849 . 1 298 . 56 CYS HB2 H 3.169 . 1 299 . 56 CYS HB3 H 3.083 . 1 300 . 57 CYS H H 8.549 . 1 301 . 57 CYS HA H 4.700 . 1 302 . 57 CYS HB2 H 2.173 . 1 303 . 57 CYS HB3 H 2.304 . 1 304 . 58 SER H H 9.031 . 1 305 . 58 SER HA H 5.161 . 1 306 . 58 SER HB2 H 3.880 . 1 307 . 58 SER HB3 H 3.880 . 1 308 . 59 ALA H H 7.269 . 1 309 . 59 ALA HA H 4.547 . 1 310 . 59 ALA HB H 1.377 . 1 311 . 60 ASP H H 8.386 . 1 312 . 60 ASP HA H 4.966 . 1 313 . 60 ASP HB2 H 2.750 . 1 314 . 60 ASP HB3 H 2.456 . 1 315 . 61 LYS H H 8.679 . 1 316 . 61 LYS HA H 4.453 . 1 317 . 61 LYS HB2 H 1.497 . 2 318 . 61 LYS HB3 H 1.628 . 2 319 . 61 LYS HG2 H 0.865 . 2 320 . 61 LYS HG3 H 0.767 . 2 321 . 62 CYS H H 7.621 . 1 322 . 62 CYS HA H 4.733 . 1 323 . 62 CYS HB2 H 3.588 . 1 324 . 62 CYS HB3 H 3.240 . 1 325 . 63 ASN H H 9.363 . 1 326 . 63 ASN HA H 4.528 . 1 327 . 63 ASN HB2 H 2.631 . 1 328 . 63 ASN HB3 H 2.276 . 1 329 . 64 THR H H 7.340 . 1 330 . 64 THR HA H 3.996 . 1 331 . 64 THR HB H 3.971 . 1 332 . 64 THR HG2 H 1.068 . 1 333 . 65 TYR H H 8.624 . 1 334 . 65 TYR HA H 4.644 . 1 335 . 65 TYR HB2 H 2.856 . 1 336 . 65 TYR HB3 H 2.650 . 1 337 . 66 PRO HA H 4.866 . 1 338 . 66 PRO HB2 H 3.188 . 2 339 . 66 PRO HB3 H 3.340 . 2 340 . 66 PRO HG2 H 1.493 . 2 341 . 66 PRO HG3 H 1.596 . 2 342 . 66 PRO HD2 H 3.106 . 2 343 . 66 PRO HD3 H 3.070 . 2 stop_ save_