data_4853 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H Chemical Shift Assignment for the Major Conformer in Solution of the Alpha-like Scorpion Toxin LqhIII ; _BMRB_accession_number 4853 _BMRB_flat_file_name bmr4853.str _Entry_type original _Submission_date 2000-10-11 _Accession_date 2000-10-11 _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 Krimm I. . . 2 Trivelli X. . . 3 Lancelin J. M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 352 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-17 update BMRB 'Updating non-standard residue' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; A Cis-trans Isomerism of a Non-prolyl Peptide Bond in Lqh III Alpha-like Scorpion Toxin Revealed by Solution NMR ; _Citation_status submitted _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Krimm I. . . 2 Trivelli X. . . 3 Lancelin J. M. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword 'alpha-like toxin' 'scorpion toxin' 'sodium channel inhibitor' 'non-proline cis peptide bond' 'cis-trans isomerism' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Pons, J.L., Malliavin, T.E. and Delsuc, M.A., 1996. Gifa V4 : a complete package for NMR data-set processing. J. Biomol. NMR, 8, 445-452. ; _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_ref_2 _Saveframe_category citation _Citation_full ; Krimm, I. et al (1999) NMR Structures and Activity of a Novel Alpha-Like Toxin from the Scorpion Leiurus quinquestriatus hebraeus. J. Mol. Biol., 285: 1749-1763. ; _Citation_title 'NMR structures and activity of a novel alpha-like toxin from the scorpion Leiurus quinquestriatus hebraeus.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9917409 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Krimm I. . . 2 Gilles N. . . 3 Sautire P. . . 4 Stankiewicz M. . . 5 Pelhate M. . . 6 Gordon D. . . 7 Lancelin 'J. M.' M. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 285 _Journal_issue 4 _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 1749 _Page_last 1763 _Year 1999 _Details ; NMR structures of a new toxin from the scorpion Leiurus quinquestriatus hebraeus (Lqh III) have been investigated in conjunction with its pharmacological properties. This toxin is proposed to belong to a new group of scorpion toxins, the alpha-like toxins that target voltage-gated sodium channels with specific properties compared with the classical alpha-scorpion toxins. Electrophysiological analysis showed that Lqh III inhibits a sodium current inactivation in the cockroach axon, but induces in addition a resting depolarization due to a slowly decaying tail current atypical to other alpha-toxin action. Binding studies indicated that radiolabeled Lqh III binds with a high degree of affinity (Ki=2.2 nM) on cockroach sodium channels and that the alpha-toxin from L quinquestriatus hebraeus highly active on insects (LqhalphaIT) and alpha-like toxins compete at low concentration for its receptor binding site, suggesting that the alpha-like toxin receptor site is partially overlapping with the receptor site 3. Conversely, in rat brain, Lqh III competes for binding of the most potent anti-mammal alpha-toxin from Androctonus australis Hector venom (AaH II) only at very high concentration.The NMR structures were used for the scrutiny of the similarities and differences with representative scorpion alpha-toxins targeting the voltage-gated sodium channels of either mammals or insects. Three turn regions involved in the functional binding site of the anti-insect LqhalphaIT toxin reveal significant differences in the Lqh III structure. The electrostatic charge distribution in the Lqh III toxin is also surprisingly different when compared with the anti-mammal alpha-toxin AaH II. Similarities in the electrostatic charge distribution are, however, recognized between alpha-toxins highly active on insects and the alpha-like toxin Lqh III. This affords additional important elements to the definition of the new alpha-like group of scorpion toxins and the mammal versus insect scorpion toxin selectivities. ; save_ ################################## # Molecular system description # ################################## save_system_LqhIII _Saveframe_category molecular_system _Mol_system_name 'LQH III ALPHA-LIKE TOXIN' _Abbreviation_common LqhIII _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label LqhIII $LqhIII stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state momomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'Neurotoxin with binding properties to voltage-gated sodium channels' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_LqhIII _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'LQH III ALPHA-LIKE TOXIN' _Abbreviation_common LqhIII _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details ; The molecule is characterized by a mixture of cis (major form) and trans (minor form) Pro9-Glu10 peptide bond in slow exchange on the NMR chemical shift time scale. ; ############################## # Polymer residue sequence # ############################## _Residue_count 68 _Mol_residue_sequence ; VRDGYIAQPENCVYHCFPGS SGCDTLCKEKGGTSGHCGFK VGHGLACWCNALPDNVGIIV EGEKCHSX ; loop_ _Residue_seq_code _Residue_label 1 VAL 2 ARG 3 ASP 4 GLY 5 TYR 6 ILE 7 ALA 8 GLN 9 PRO 10 GLU 11 ASN 12 CYS 13 VAL 14 TYR 15 HIS 16 CYS 17 PHE 18 PRO 19 GLY 20 SER 21 SER 22 GLY 23 CYS 24 ASP 25 THR 26 LEU 27 CYS 28 LYS 29 GLU 30 LYS 31 GLY 32 GLY 33 THR 34 SER 35 GLY 36 HIS 37 CYS 38 GLY 39 PHE 40 LYS 41 VAL 42 GLY 43 HIS 44 GLY 45 LEU 46 ALA 47 CYS 48 TRP 49 CYS 50 ASN 51 ALA 52 LEU 53 PRO 54 ASP 55 ASN 56 VAL 57 GLY 58 ILE 59 ILE 60 VAL 61 GLU 62 GLY 63 GLU 64 LYS 65 CYS 66 HIS 67 SER 68 NH2 stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1BMR "Alpha-Like Toxin Lqh Iii From Scorpion Leiurus Quinquestriatus Hebraeus, Nmr, 25 Structures" 98.51 68 100.00 100.00 1.01e-39 PDB 1FH3 "Nmr Structures Of Lqh Iii Alpha-Like Scorpion Toxin From Leiurus Quinquestriatus Corresponding To The Major Conformer In Soluti" 98.51 68 100.00 100.00 1.01e-39 SP P56678 "RecName: Full=Alpha-like toxin Lqh3; AltName: Full=Lqh III; Short=LqhIII [Leiurus quinquestriatus hebraeus]" 98.51 67 100.00 100.00 9.81e-40 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_NH2 _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'AMINO GROUP' _BMRB_code . _PDB_code NH2 _Standard_residue_derivative . _Molecular_mass 16.023 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jul 14 16:09:34 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? HN1 HN1 H . 0 . ? HN2 HN2 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N HN1 ? ? SING N HN2 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $LqhIII 'Hebraeus yellow scorpion' 6884 Eukaryota Metazoa Leiurus quinquestriatus 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 $LqhIII 'purified from the natural source' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $LqhIII 2 mM . phosphate 100 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $LqhIII 2 mM . phosphate 100 mM . D2O 100 % . stop_ save_ ############################ # Computer software used # ############################ save_GIFA _Saveframe_category software _Name GIFA _Version 4.2 loop_ _Task 'data analysis' stop_ _Details . _Citation_label $ref_1 save_ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version NA loop_ _Task 'data collection' stop_ _Details Bruker save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.851 loop_ _Task 'structure solution' stop_ _Details Brunger save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'Avance DRX' _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_2D_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label . save_ save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.8 0.1 n/a temperature 311 0.1 K pressure 1 . atm 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 _Reference_correction_type H2O H 1 protons ppm 4.649 internal direct cylindrical internal parallel_to_Bo temperature 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details 'The chemical shifts listed concern the major conformer in solution' loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name LqhIII _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 VAL HA H 4.24 0.01 1 2 . 1 VAL HB H 1.73 0.01 1 3 . 1 VAL HG1 H 0.89 0.01 1 4 . 1 VAL HG2 H 0.83 0.01 1 5 . 2 ARG H H 8.99 0.01 1 6 . 2 ARG HA H 4.67 0.01 1 7 . 2 ARG HB2 H 1.80 0.01 1 8 . 2 ARG HB3 H 1.80 0.01 1 9 . 2 ARG HG2 H 1.48 0.01 1 10 . 2 ARG HG3 H 1.48 0.01 1 11 . 2 ARG HD2 H 3.10 0.01 2 12 . 2 ARG HD3 H 3.02 0.01 2 13 . 2 ARG HE H 7.64 0.01 1 14 . 3 ASP H H 8.07 0.01 1 15 . 3 ASP HA H 5.11 0.01 1 16 . 3 ASP HB2 H 2.85 0.01 1 17 . 3 ASP HB3 H 2.56 0.01 1 18 . 4 GLY H H 7.54 0.01 1 19 . 4 GLY HA2 H 3.55 0.01 1 20 . 4 GLY HA3 H 3.55 0.01 1 21 . 5 TYR H H 8.21 0.01 1 22 . 5 TYR HA H 4.96 0.01 1 23 . 5 TYR HB2 H 2.80 0.01 1 24 . 5 TYR HB3 H 2.56 0.01 1 25 . 5 TYR HD1 H 7.20 0.01 1 26 . 5 TYR HD2 H 7.20 0.01 1 27 . 5 TYR HE1 H 7.00 0.01 1 28 . 5 TYR HE2 H 7.00 0.01 1 29 . 6 ILE H H 6.87 0.01 1 30 . 6 ILE HA H 4.04 0.01 1 31 . 6 ILE HB H 1.67 0.01 1 32 . 6 ILE HG12 H 1.21 0.01 1 33 . 6 ILE HG13 H 1.21 0.01 1 34 . 6 ILE HG2 H 0.82 0.01 1 35 . 6 ILE HD1 H 0.64 0.01 1 36 . 7 ALA H H 7.55 0.01 1 37 . 7 ALA HA H 5.01 0.01 1 38 . 7 ALA HB H 0.88 0.01 1 39 . 8 GLN H H 9.52 0.01 1 40 . 8 GLN HA H 4.81 0.01 1 41 . 8 GLN HG2 H 1.53 0.01 1 42 . 8 GLN HG3 H 1.53 0.01 1 43 . 9 PRO HA H 4.41 0.01 1 44 . 9 PRO HB2 H 1.85 0.01 2 45 . 9 PRO HB3 H 2.33 0.01 2 46 . 9 PRO HG2 H 1.99 0.01 1 47 . 9 PRO HG3 H 1.99 0.01 1 48 . 9 PRO HD2 H 3.53 0.01 2 49 . 9 PRO HD3 H 3.83 0.01 2 50 . 10 GLU H H 7.48 0.01 1 51 . 10 GLU HA H 4.41 0.01 1 52 . 10 GLU HB2 H 1.73 0.01 1 53 . 10 GLU HB3 H 1.52 0.01 1 54 . 10 GLU HG2 H 2.15 0.01 1 55 . 10 GLU HG3 H 2.15 0.01 1 56 . 11 ASN H H 8.98 0.01 1 57 . 11 ASN HA H 3.91 0.01 1 58 . 11 ASN HB2 H 2.30 0.01 1 59 . 11 ASN HB3 H 2.30 0.01 1 60 . 11 ASN HD21 H 7.49 0.01 1 61 . 11 ASN HD22 H 6.94 0.01 1 62 . 12 CYS H H 8.33 0.01 1 63 . 12 CYS HA H 5.17 0.01 1 64 . 12 CYS HB2 H 3.17 0.01 1 65 . 12 CYS HB3 H 2.38 0.01 1 66 . 13 VAL H H 8.76 0.01 1 67 . 13 VAL HA H 4.32 0.01 1 68 . 13 VAL HB H 2.32 0.01 1 69 . 13 VAL HG1 H 0.49 0.01 1 70 . 13 VAL HG2 H 0.38 0.01 1 71 . 14 TYR H H 8.69 0.01 1 72 . 14 TYR HA H 4.40 0.01 1 73 . 14 TYR HB2 H 2.55 0.01 1 74 . 14 TYR HB3 H 2.67 0.01 1 75 . 14 TYR HD1 H 7.03 0.01 1 76 . 14 TYR HD2 H 7.03 0.01 1 77 . 14 TYR HE1 H 6.52 0.01 1 78 . 14 TYR HE2 H 6.52 0.01 1 79 . 15 HIS H H 8.56 0.01 1 80 . 15 HIS HA H 4.90 0.01 1 81 . 15 HIS HB2 H 3.16 0.01 1 82 . 15 HIS HB3 H 3.16 0.01 1 83 . 15 HIS HD2 H 7.35 0.01 1 84 . 15 HIS HE1 H 8.63 0.01 1 85 . 16 CYS H H 6.95 0.01 1 86 . 16 CYS HA H 4.81 0.01 1 87 . 16 CYS HB2 H 3.19 0.01 2 88 . 16 CYS HB3 H 2.91 0.01 2 89 . 17 PHE H H 8.18 0.01 1 90 . 17 PHE HA H 5.18 0.01 1 91 . 17 PHE HB2 H 3.18 0.01 2 92 . 17 PHE HB3 H 2.90 0.01 2 93 . 17 PHE HD1 H 7.34 0.01 1 94 . 17 PHE HD2 H 7.34 0.01 1 95 . 17 PHE HE1 H 7.42 0.01 1 96 . 17 PHE HE2 H 7.42 0.01 1 97 . 17 PHE HZ H 7.34 0.01 1 98 . 18 PRO HA H 4.34 0.01 1 99 . 18 PRO HB2 H 2.36 0.01 2 100 . 18 PRO HB3 H 1.98 0.01 2 101 . 18 PRO HG2 H 2.15 0.01 2 102 . 18 PRO HG3 H 1.91 0.01 2 103 . 18 PRO HD2 H 3.94 0.01 2 104 . 18 PRO HD3 H 3.66 0.01 2 105 . 19 GLY H H 8.72 0.01 1 106 . 19 GLY HA2 H 4.20 0.01 2 107 . 19 GLY HA3 H 3.87 0.01 2 108 . 20 SER H H 7.84 0.01 1 109 . 20 SER HA H 4.84 0.01 1 110 . 20 SER HB2 H 4.11 0.01 2 111 . 20 SER HB3 H 4.03 0.01 2 112 . 21 SER H H 8.96 0.01 1 113 . 21 SER HA H 4.01 0.01 1 114 . 21 SER HB2 H 4.24 0.01 2 115 . 21 SER HB3 H 4.06 0.01 2 116 . 22 GLY H H 8.46 0.01 1 117 . 22 GLY HA2 H 4.04 0.01 2 118 . 22 GLY HA3 H 3.88 0.01 2 119 . 23 CYS H H 8.67 0.01 1 120 . 23 CYS HA H 4.48 0.01 1 121 . 24 ASP H H 8.29 0.01 1 122 . 24 ASP HA H 3.95 0.01 1 123 . 24 ASP HB2 H 2.91 0.01 2 124 . 24 ASP HB3 H 2.72 0.01 2 125 . 25 THR H H 7.87 0.01 1 126 . 25 THR HA H 3.78 0.01 1 127 . 25 THR HB H 4.16 0.01 1 128 . 25 THR HG2 H 1.24 0.01 1 129 . 26 LEU H H 7.86 0.01 1 130 . 26 LEU HA H 4.03 0.01 1 131 . 26 LEU HB2 H 1.50 0.01 1 132 . 26 LEU HB3 H 1.77 0.01 1 133 . 26 LEU HG H 1.09 0.01 1 134 . 26 LEU HD1 H 0.54 0.01 2 135 . 26 LEU HD2 H 0.16 0.01 2 136 . 27 CYS H H 8.62 0.01 1 137 . 27 CYS HA H 3.92 0.01 1 138 . 27 CYS HB2 H 2.55 0.01 2 139 . 27 CYS HB3 H 2.41 0.01 2 140 . 28 LYS H H 7.86 0.01 1 141 . 28 LYS HA H 4.24 0.01 1 142 . 28 LYS HG2 H 1.32 0.01 1 143 . 28 LYS HG3 H 1.32 0.01 1 144 . 28 LYS HD2 H 1.22 0.01 1 145 . 28 LYS HD3 H 1.22 0.01 1 146 . 28 LYS HE2 H 3.00 0.01 1 147 . 28 LYS HE3 H 3.00 0.01 1 148 . 29 GLU H H 8.42 0.01 1 149 . 29 GLU HA H 4.01 0.01 1 150 . 29 GLU HB2 H 2.29 0.01 2 151 . 29 GLU HB3 H 2.15 0.01 2 152 . 29 GLU HG2 H 2.44 0.01 1 153 . 29 GLU HG3 H 2.44 0.01 1 154 . 30 LYS H H 7.53 0.01 1 155 . 30 LYS HA H 4.24 0.01 1 156 . 30 LYS HG2 H 1.55 0.01 2 157 . 30 LYS HG3 H 1.78 0.01 2 158 . 30 LYS HD2 H 1.25 0.01 1 159 . 30 LYS HD3 H 1.25 0.01 1 160 . 30 LYS HE2 H 2.85 0.01 1 161 . 30 LYS HE3 H 2.85 0.01 1 162 . 31 GLY H H 7.63 0.01 1 163 . 31 GLY HA2 H 4.29 0.01 2 164 . 31 GLY HA3 H 3.73 0.01 2 165 . 32 GLY H H 8.54 0.01 1 166 . 32 GLY HA2 H 4.77 0.01 2 167 . 32 GLY HA3 H 3.13 0.01 2 168 . 33 THR H H 8.26 0.01 1 169 . 33 THR HA H 4.32 0.01 1 170 . 33 THR HB H 4.16 0.01 1 171 . 33 THR HG2 H 1.24 0.01 1 172 . 34 SER H H 7.44 0.01 1 173 . 34 SER HA H 4.71 0.01 1 174 . 34 SER HB2 H 4.27 0.01 2 175 . 34 SER HB3 H 4.03 0.01 2 176 . 35 GLY HA2 H 5.05 0.01 2 177 . 35 GLY HA3 H 4.54 0.01 2 178 . 36 HIS H H 9.19 0.01 1 179 . 36 HIS HA H 5.08 0.01 1 180 . 36 HIS HD2 H 6.89 0.01 1 181 . 36 HIS HE1 H 7.90 0.01 1 182 . 37 CYS H H 9.38 0.01 1 183 . 37 CYS HA H 5.22 0.01 1 184 . 37 CYS HB2 H 3.18 0.01 2 185 . 37 CYS HB3 H 2.99 0.01 2 186 . 38 GLY H H 9.21 0.01 1 187 . 38 GLY HA2 H 4.79 0.01 2 188 . 38 GLY HA3 H 4.04 0.01 2 189 . 39 PHE H H 8.55 0.01 1 190 . 39 PHE HA H 4.69 0.01 1 191 . 39 PHE HB2 H 3.02 0.01 1 192 . 39 PHE HB3 H 2.92 0.01 1 193 . 39 PHE HD1 H 7.05 0.01 1 194 . 39 PHE HD2 H 7.05 0.01 1 195 . 39 PHE HE1 H 7.34 0.01 1 196 . 39 PHE HE2 H 7.34 0.01 1 197 . 39 PHE HZ H 7.05 0.01 1 198 . 40 LYS H H 8.12 0.01 1 199 . 40 LYS HA H 4.50 0.01 1 200 . 40 LYS HB2 H 1.36 0.01 1 201 . 40 LYS HB3 H 1.36 0.01 1 202 . 40 LYS HG2 H 1.20 0.01 1 203 . 40 LYS HG3 H 1.20 0.01 1 204 . 40 LYS HD2 H 0.82 0.01 1 205 . 40 LYS HD3 H 0.82 0.01 1 206 . 40 LYS HE2 H 2.80 0.01 2 207 . 40 LYS HE3 H 2.71 0.01 2 208 . 41 VAL H H 8.79 0.01 1 209 . 41 VAL HA H 3.67 0.01 1 210 . 41 VAL HB H 2.08 0.01 1 211 . 41 VAL HG1 H 1.20 0.01 2 212 . 41 VAL HG2 H 1.02 0.01 2 213 . 42 GLY H H 8.96 0.01 1 214 . 42 GLY HA2 H 4.24 0.01 2 215 . 42 GLY HA3 H 3.53 0.01 2 216 . 43 HIS H H 8.16 0.01 1 217 . 43 HIS HA H 4.59 0.01 1 218 . 43 HIS HB2 H 2.97 0.01 1 219 . 43 HIS HB3 H 2.39 0.01 1 220 . 43 HIS HD2 H 6.82 0.01 1 221 . 43 HIS HE1 H 8.07 0.01 1 222 . 44 GLY H H 8.13 0.01 1 223 . 44 GLY HA2 H 4.36 0.01 2 224 . 44 GLY HA3 H 3.26 0.01 2 225 . 45 LEU H H 8.47 0.01 1 226 . 45 LEU HA H 4.71 0.01 1 227 . 45 LEU HB2 H 1.89 0.01 2 228 . 45 LEU HB3 H 1.65 0.01 2 229 . 45 LEU HG H 1.89 0.01 1 230 . 45 LEU HD1 H 1.13 0.01 2 231 . 45 LEU HD2 H 1.02 0.01 2 232 . 46 ALA H H 8.97 0.01 1 233 . 46 ALA HA H 5.14 0.01 1 234 . 46 ALA HB H 1.12 0.01 1 235 . 47 CYS H H 8.26 0.01 1 236 . 47 CYS HA H 5.14 0.01 1 237 . 47 CYS HB2 H 2.64 0.01 1 238 . 47 CYS HB3 H 2.64 0.01 1 239 . 48 TRP H H 9.27 0.01 1 240 . 48 TRP HA H 4.32 0.01 1 241 . 48 TRP HB2 H 2.53 0.01 1 242 . 48 TRP HB3 H 2.53 0.01 1 243 . 48 TRP HD1 H 6.29 0.01 1 244 . 48 TRP HE1 H 9.67 0.01 1 245 . 48 TRP HE3 H 5.64 0.01 1 246 . 48 TRP HZ2 H 7.36 0.01 1 247 . 48 TRP HZ3 H 6.82 0.01 1 248 . 48 TRP HH2 H 7.11 0.01 1 249 . 49 CYS H H 8.21 0.01 1 250 . 49 CYS HA H 5.48 0.01 1 251 . 49 CYS HB2 H 2.80 0.01 1 252 . 49 CYS HB3 H 2.23 0.01 1 253 . 50 ASN H H 8.37 0.01 1 254 . 50 ASN HA H 4.95 0.01 1 255 . 50 ASN HB2 H 2.53 0.01 1 256 . 50 ASN HB3 H 2.53 0.01 1 257 . 50 ASN HD21 H 7.39 0.01 1 258 . 50 ASN HD22 H 7.09 0.01 1 259 . 51 ALA H H 9.64 0.01 1 260 . 51 ALA HA H 3.50 0.01 1 261 . 51 ALA HB H 1.34 0.01 1 262 . 52 LEU H H 8.58 0.01 1 263 . 52 LEU HA H 4.10 0.01 1 264 . 52 LEU HB2 H 1.71 0.01 2 265 . 52 LEU HB3 H 1.19 0.01 2 266 . 52 LEU HG H 1.33 0.01 1 267 . 52 LEU HD1 H 0.72 0.01 2 268 . 52 LEU HD2 H 0.46 0.01 2 269 . 53 PRO HA H 4.41 0.01 1 270 . 53 PRO HB2 H 2.45 0.01 2 271 . 53 PRO HB3 H 2.03 0.01 2 272 . 53 PRO HG2 H 2.27 0.01 2 273 . 53 PRO HG3 H 2.09 0.01 2 274 . 53 PRO HD2 H 3.59 0.01 2 275 . 53 PRO HD3 H 3.43 0.01 2 276 . 54 ASP H H 8.46 0.01 1 277 . 54 ASP HA H 4.09 0.01 1 278 . 54 ASP HB2 H 2.59 0.01 2 279 . 54 ASP HB3 H 2.44 0.01 2 280 . 55 ASN H H 7.92 0.01 1 281 . 55 ASN HA H 4.51 0.01 1 282 . 55 ASN HB2 H 2.98 0.01 2 283 . 55 ASN HB3 H 2.66 0.01 2 284 . 55 ASN HD21 H 7.50 0.01 1 285 . 55 ASN HD22 H 6.73 0.01 1 286 . 56 VAL H H 7.62 0.01 1 287 . 56 VAL HA H 3.95 0.01 1 288 . 56 VAL HB H 1.98 0.01 1 289 . 56 VAL HG1 H 1.03 0.01 1 290 . 56 VAL HG2 H 1.03 0.01 1 291 . 57 GLY H H 8.52 0.01 1 292 . 57 GLY HA2 H 3.86 0.01 2 293 . 57 GLY HA3 H 3.66 0.01 2 294 . 58 ILE H H 7.55 0.01 1 295 . 58 ILE HA H 4.84 0.01 1 296 . 58 ILE HG12 H 0.65 0.01 1 297 . 58 ILE HG13 H 0.65 0.01 1 298 . 58 ILE HG2 H 0.65 0.01 1 299 . 58 ILE HD1 H 0.45 0.01 1 300 . 59 ILE H H 6.26 0.01 1 301 . 59 ILE HA H 3.86 0.01 1 302 . 59 ILE HB H 1.79 0.01 1 303 . 59 ILE HG12 H 1.20 0.01 1 304 . 59 ILE HG13 H 1.20 0.01 1 305 . 59 ILE HG2 H 0.41 0.01 1 306 . 59 ILE HD1 H 0.15 0.01 1 307 . 60 VAL H H 9.33 0.01 1 308 . 60 VAL HA H 4.24 0.01 1 309 . 60 VAL HB H 2.01 0.01 1 310 . 60 VAL HG1 H 0.94 0.01 1 311 . 60 VAL HG2 H 0.94 0.01 1 312 . 61 GLU H H 8.74 0.01 1 313 . 61 GLU HA H 4.18 0.01 1 314 . 61 GLU HB2 H 1.96 0.01 1 315 . 61 GLU HB3 H 2.05 0.01 1 316 . 61 GLU HG2 H 2.40 0.01 1 317 . 61 GLU HG3 H 2.40 0.01 1 318 . 62 GLY H H 8.68 0.01 1 319 . 62 GLY HA2 H 4.16 0.01 2 320 . 62 GLY HA3 H 3.72 0.01 2 321 . 63 GLU H H 7.14 0.01 1 322 . 63 GLU HA H 4.63 0.01 1 323 . 63 GLU HB2 H 2.00 0.01 2 324 . 63 GLU HB3 H 1.79 0.01 2 325 . 63 GLU HG2 H 2.37 0.01 2 326 . 63 GLU HG3 H 2.26 0.01 2 327 . 64 LYS H H 8.69 0.01 1 328 . 64 LYS HA H 4.31 0.01 1 329 . 64 LYS HB2 H 1.65 0.01 1 330 . 64 LYS HB3 H 1.65 0.01 1 331 . 64 LYS HG2 H 1.43 0.01 1 332 . 64 LYS HG3 H 1.43 0.01 1 333 . 64 LYS HD2 H 1.80 0.01 1 334 . 64 LYS HD3 H 1.80 0.01 1 335 . 64 LYS HE2 H 2.98 0.01 1 336 . 64 LYS HE3 H 2.98 0.01 1 337 . 65 CYS H H 8.34 0.01 1 338 . 65 CYS HA H 5.12 0.01 1 339 . 65 CYS HB2 H 2.60 0.01 1 340 . 65 CYS HB3 H 3.97 0.01 1 341 . 66 HIS H H 8.93 0.01 1 342 . 66 HIS HA H 4.97 0.01 1 343 . 66 HIS HB2 H 3.26 0.01 1 344 . 66 HIS HB3 H 3.26 0.01 1 345 . 66 HIS HD2 H 7.32 0.01 1 346 . 66 HIS HE1 H 8.52 0.01 1 347 . 67 SER H H 8.48 0.01 1 348 . 67 SER HA H 4.48 0.01 1 349 . 67 SER HB2 H 3.83 0.01 1 350 . 67 SER HB3 H 3.83 0.01 1 351 . 68 NH2 HN1 H 7.10 0.01 1 352 . 68 NH2 HN2 H 7.57 0.01 1 stop_ save_