data_6499 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of antimicrobial peptide distinctin in water ; _BMRB_accession_number 6499 _BMRB_flat_file_name bmr6499.str _Entry_type original _Submission_date 2005-02-09 _Accession_date 2005-02-09 _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 Amodeo P. . . 2 Raimondo D. . . 3 Andreotti G. . . 4 Motta A. . . 5 Scaloni A. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 335 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-05-26 original BMRB . stop_ _Original_release_date 2005-02-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15840728 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Raimondo D. . . 2 Andreotti G. . . 3 Saint N. . . 4 Amodeo P. . . 5 Renzone G. . . 6 Sanseverino M. . . 7 Zocchi I. . . 8 Molle G. . . 9 Motta A. . . 10 Scaloni A. . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U. S. A.' _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 DISULFIDE 'FOUR-HELIX BUNDLE' HETERODIMER HOMODIMER 'NMR STRUCTURE' 'PORE-FORMING PEPTIDE' stop_ save_ ################################## # Molecular system description # ################################## save_system_distinctin _Saveframe_category molecular_system _Mol_system_name 'distinctin chain A/distinctin chain B' _Abbreviation_common distinctin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Distinctin chain A monomer 1' $Distinctin_chain_A 'Distinctin chain B monomer 1' $Distinctin_chain_B 'Distinctin chain A monomer 2' $Distinctin_chain_A 'Distinctin chain B monomer 2' $Distinctin_chain_B stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state tetramer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function antibiotic stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Distinctin_chain_A _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Distinctin chain A' _Abbreviation_common 'Distinctin chain A' _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 22 _Mol_residue_sequence ; ENREVPPGFTALIKTLRKCK II ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 ASN 3 ARG 4 GLU 5 VAL 6 PRO 7 PRO 8 GLY 9 PHE 10 THR 11 ALA 12 LEU 13 ILE 14 LYS 15 THR 16 LEU 17 ARG 18 LYS 19 CYS 20 LYS 21 ILE 22 ILE stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 1XKM 'Nmr Structure Of Antimicrobial Peptide Distinctin In Water' 100.00 22 100.00 100.00 7.45e-04 stop_ save_ save_Distinctin_chain_B _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Distinctin chain B' _Abbreviation_common 'Distinctin chain B' _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . _Residue_count 25 _Mol_residue_sequence ; NLVSGLIEARKYLEQLHRKL KNCKV ; loop_ _Residue_seq_code _Residue_label 1 ASN 2 LEU 3 VAL 4 SER 5 GLY 6 LEU 7 ILE 8 GLU 9 ALA 10 ARG 11 LYS 12 TYR 13 LEU 14 GLU 15 GLN 16 LEU 17 HIS 18 ARG 19 LYS 20 LEU 21 LYS 22 ASN 23 CYS 24 LYS 25 VAL stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 1XKM 'Nmr Structure Of Antimicrobial Peptide Distinctin In Water' 96.00 25 100.00 100.00 1.50e-04 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Tissue $Distinctin_chain_A 'tree frog' 164618 Eukaryota Metazoa Phyllomedusa distincta skin $Distinctin_chain_B 'tree frog' 164618 Eukaryota Metazoa Phyllomedusa distincta skin 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 $Distinctin_chain_A 'chemical synthesis' . . . . . $Distinctin_chain_B 'chemical synthesis' . . . . . 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 $Distinctin_chain_A . mM 0.05 3.8 . $Distinctin_chain_B . mM 0.05 3.8 . Phosphate 20 mM . . . NaCl 100 mM . . . stop_ save_ ############################ # Computer software used # ############################ save_AMBER _Saveframe_category software _Name AMBER _Version 5 loop_ _Task refinement 'structure solution' stop_ _Details 'Kollman, Case' save_ save_MolMol _Saveframe_category software _Name Molmol _Version 2K.2 loop_ _Task 'data analysis' stop_ _Details Koradi save_ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 3.5 loop_ _Task processing stop_ _Details Bruker save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 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_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.15 0.01 M pH 5.8 0.1 pH pressure 1 . atm temperature 300 0.5 K stop_ save_ save_sample_cond_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.15 0.01 M pH 6.8 0.1 pH pressure 1 . atm temperature 310 0.5 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 TSP H 1 'methyl protons' ppm 0.00 internal direct spherical internal parallel 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_chemical_shift_ch_A _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D NOESY' '2D TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Distinctin chain A monomer 1' _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 GLU HA H 4.80 . 1 2 . 1 GLU HB2 H 3.24 . 2 3 . 1 GLU HB3 H 3.20 . 2 4 . 1 GLU HG2 H 3.15 . 2 5 . 1 GLU HG3 H 3.05 . 2 6 . 2 ASN H H 7.42 . 1 7 . 2 ASN HA H 4.83 . 1 8 . 2 ASN HB2 H 2.89 . 2 9 . 2 ASN HB3 H 2.80 . 2 10 . 2 ASN HD21 H 7.69 . 2 11 . 2 ASN HD22 H 7.01 . 2 12 . 3 ARG H H 8.62 . 1 13 . 3 ARG HA H 4.43 . 1 14 . 3 ARG HB2 H 1.92 . 2 15 . 3 ARG HB3 H 1.76 . 2 16 . 3 ARG HG2 H 1.68 . 2 17 . 3 ARG HG3 H 1.66 . 2 18 . 3 ARG HD2 H 3.24 . 2 19 . 3 ARG HD3 H 3.22 . 2 20 . 3 ARG HE H 7.32 . 1 21 . 3 ARG HH11 H 7.18 . 1 22 . 3 ARG HH12 H 7.18 . 1 23 . 3 ARG HH21 H 6.73 . 1 24 . 3 ARG HH22 H 6.73 . 1 25 . 4 GLU H H 8.51 . 1 26 . 4 GLU HA H 4.35 . 1 27 . 4 GLU HB2 H 2.08 . 2 28 . 4 GLU HB3 H 1.99 . 2 29 . 4 GLU HG2 H 2.34 . 2 30 . 4 GLU HG3 H 2.30 . 2 31 . 5 VAL H H 8.23 . 1 32 . 5 VAL HA H 4.58 . 1 33 . 5 VAL HB H 2.11 . 1 34 . 5 VAL HG1 H 1.04 . 2 35 . 5 VAL HG2 H 0.95 . 2 36 . 6 PRO HA H 4.90 . 1 37 . 6 PRO HB2 H 2.69 . 2 38 . 6 PRO HB3 H 2.28 . 2 39 . 6 PRO HG2 H 2.13 . 1 40 . 6 PRO HG3 H 2.13 . 1 41 . 6 PRO HD2 H 4.15 . 2 42 . 6 PRO HD3 H 3.51 . 2 43 . 7 PRO HA H 4.47 . 1 44 . 7 PRO HB2 H 2.46 . 2 45 . 7 PRO HB3 H 2.24 . 2 46 . 7 PRO HG2 H 2.22 . 2 47 . 7 PRO HG3 H 2.20 . 2 48 . 7 PRO HD2 H 4.03 . 2 49 . 7 PRO HD3 H 3.91 . 2 50 . 8 GLY H H 8.99 . 1 51 . 8 GLY HA2 H 3.68 . 2 52 . 8 GLY HA3 H 3.39 . 2 53 . 9 PHE H H 7.80 . 1 54 . 9 PHE HA H 4.25 . 1 55 . 9 PHE HB2 H 3.42 . 2 56 . 9 PHE HB3 H 3.30 . 2 57 . 9 PHE HD1 H 7.43 . 1 58 . 9 PHE HD2 H 7.43 . 1 59 . 9 PHE HE1 H 7.22 . 1 60 . 9 PHE HE2 H 7.22 . 1 61 . 9 PHE HZ H 6.97 . 1 62 . 10 THR H H 7.94 . 1 63 . 10 THR HA H 3.84 . 1 64 . 10 THR HB H 4.27 . 1 65 . 10 THR HG2 H 1.29 . 1 66 . 11 ALA H H 8.04 . 1 67 . 11 ALA HA H 4.10 . 1 68 . 11 ALA HB H 1.44 . 1 69 . 12 LEU H H 7.66 . 1 70 . 12 LEU HA H 4.00 . 1 71 . 12 LEU HB2 H 2.22 . 2 72 . 12 LEU HB3 H 1.68 . 2 73 . 12 LEU HG H 1.47 . 1 74 . 12 LEU HD1 H 1.07 . 2 75 . 12 LEU HD2 H 0.88 . 2 76 . 13 ILE H H 8.16 . 1 77 . 13 ILE HA H 3.30 . 1 78 . 13 ILE HB H 1.98 . 1 79 . 13 ILE HG12 H 1.60 . 2 80 . 13 ILE HG13 H 0.81 . 2 81 . 13 ILE HG2 H 0.75 . 1 82 . 13 ILE HD1 H 0.40 . 1 83 . 14 LYS H H 7.84 . 1 84 . 14 LYS HA H 3.96 . 1 85 . 14 LYS HB2 H 1.97 . 2 86 . 14 LYS HB3 H 1.70 . 2 87 . 14 LYS HG2 H 1.44 . 2 88 . 14 LYS HG3 H 1.40 . 2 89 . 14 LYS HD2 H 1.44 . 2 90 . 14 LYS HD3 H 1.40 . 2 91 . 14 LYS HE2 H 2.97 . 1 92 . 14 LYS HE3 H 2.97 . 1 93 . 14 LYS HZ H 7.35 . 1 94 . 15 THR H H 8.18 . 1 95 . 15 THR HA H 3.88 . 1 96 . 15 THR HB H 4.19 . 1 97 . 15 THR HG2 H 1.14 . 1 98 . 16 LEU H H 8.91 . 1 99 . 16 LEU HA H 3.78 . 1 100 . 16 LEU HB2 H 2.04 . 2 101 . 16 LEU HB3 H 1.81 . 2 102 . 16 LEU HG H 1.19 . 1 103 . 16 LEU HD1 H 0.86 . 2 104 . 16 LEU HD2 H 0.84 . 2 105 . 17 ARG H H 8.47 . 1 106 . 17 ARG HA H 4.37 . 1 107 . 17 ARG HB2 H 1.89 . 2 108 . 17 ARG HB3 H 1.79 . 2 109 . 17 ARG HG2 H 1.63 . 1 110 . 17 ARG HG3 H 1.63 . 1 111 . 17 ARG HD2 H 3.22 . 2 112 . 17 ARG HD3 H 3.17 . 2 113 . 17 ARG HH11 H 7.10 . 1 114 . 17 ARG HH12 H 7.10 . 1 115 . 17 ARG HH21 H 6.43 . 1 116 . 17 ARG HH22 H 6.43 . 1 117 . 18 LYS H H 8.38 . 1 118 . 18 LYS HA H 4.16 . 1 119 . 18 LYS HB2 H 2.08 . 1 120 . 18 LYS HB3 H 2.08 . 1 121 . 18 LYS HG2 H 1.62 . 1 122 . 18 LYS HG3 H 1.62 . 1 123 . 18 LYS HD2 H 1.58 . 1 124 . 18 LYS HD3 H 1.58 . 1 125 . 18 LYS HE2 H 3.03 . 1 126 . 18 LYS HE3 H 3.03 . 1 127 . 18 LYS HZ H 7.26 . 1 128 . 19 CYS H H 7.95 . 1 129 . 19 CYS HA H 4.51 . 1 130 . 19 CYS HB2 H 3.26 . 2 131 . 19 CYS HB3 H 2.96 . 2 132 . 20 LYS H H 8.21 . 1 133 . 20 LYS HA H 4.09 . 1 134 . 20 LYS HB2 H 2.19 . 2 135 . 20 LYS HB3 H 1.81 . 2 136 . 20 LYS HG2 H 1.45 . 2 137 . 20 LYS HG3 H 1.42 . 2 138 . 20 LYS HD2 H 1.46 . 2 139 . 20 LYS HD3 H 1.44 . 2 140 . 20 LYS HE2 H 3.11 . 1 141 . 20 LYS HE3 H 3.11 . 1 142 . 20 LYS HZ H 7.16 . 1 143 . 21 ILE H H 8.34 . 1 144 . 21 ILE HA H 3.86 . 1 145 . 21 ILE HB H 1.63 . 1 146 . 21 ILE HG12 H 1.10 . 2 147 . 21 ILE HG13 H 0.98 . 2 148 . 21 ILE HG2 H 0.82 . 1 149 . 21 ILE HD1 H 0.82 . 1 150 . 22 ILE H H 6.88 . 1 151 . 22 ILE HA H 4.20 . 1 152 . 22 ILE HB H 1.82 . 1 153 . 22 ILE HG12 H 1.10 . 2 154 . 22 ILE HG13 H 0.73 . 2 155 . 22 ILE HG2 H 0.56 . 1 156 . 22 ILE HD1 H 0.41 . 1 stop_ save_ save_chemical_shift_ch_B _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D NOESY' '2D TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Distinctin chain B monomer 1' _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 ASN HA H 4.27 . 1 2 . 1 ASN HB2 H 2.99 . 1 3 . 1 ASN HB3 H 2.99 . 1 4 . 1 ASN HD21 H 7.76 . 2 5 . 1 ASN HD22 H 7.04 . 2 6 . 2 LEU H H 7.89 . 1 7 . 2 LEU HA H 4.46 . 1 8 . 2 LEU HB2 H 2.05 . 2 9 . 2 LEU HB3 H 1.70 . 2 10 . 2 LEU HG H 1.70 . 1 11 . 2 LEU HD1 H 1.00 . 2 12 . 2 LEU HD2 H 0.96 . 2 13 . 3 VAL H H 8.21 . 1 14 . 3 VAL HA H 4.09 . 1 15 . 3 VAL HB H 2.23 . 1 16 . 3 VAL HG1 H 1.04 . 2 17 . 3 VAL HG2 H 1.02 . 2 18 . 4 SER H H 8.36 . 1 19 . 4 SER HA H 4.40 . 1 20 . 4 SER HB2 H 4.02 . 2 21 . 4 SER HB3 H 3.95 . 2 22 . 5 GLY H H 8.63 . 1 23 . 5 GLY HA2 H 4.04 . 1 24 . 5 GLY HA3 H 4.04 . 1 25 . 6 LEU H H 8.11 . 1 26 . 6 LEU HA H 4.04 . 1 27 . 6 LEU HB2 H 1.74 . 2 28 . 6 LEU HB3 H 1.37 . 2 29 . 6 LEU HG H 1.23 . 1 30 . 6 LEU HD1 H 0.95 . 2 31 . 6 LEU HD2 H 0.84 . 2 32 . 7 ILE H H 7.93 . 1 33 . 7 ILE HA H 3.74 . 1 34 . 7 ILE HB H 2.04 . 1 35 . 7 ILE HG12 H 1.72 . 2 36 . 7 ILE HG13 H 1.70 . 2 37 . 7 ILE HG2 H 1.32 . 1 38 . 7 ILE HD1 H 1.00 . 1 39 . 8 GLU H H 8.44 . 1 40 . 8 GLU HA H 4.05 . 1 41 . 8 GLU HB2 H 2.19 . 2 42 . 8 GLU HB3 H 2.11 . 2 43 . 8 GLU HG2 H 2.51 . 2 44 . 8 GLU HG3 H 2.43 . 2 45 . 9 ALA H H 8.31 . 1 46 . 9 ALA HA H 4.37 . 1 47 . 9 ALA HB H 1.62 . 1 48 . 10 ARG H H 8.19 . 1 49 . 10 ARG HA H 3.87 . 1 50 . 10 ARG HB2 H 2.08 . 2 51 . 10 ARG HB3 H 1.84 . 2 52 . 10 ARG HG2 H 1.52 . 1 53 . 10 ARG HG3 H 1.52 . 1 54 . 10 ARG HD2 H 3.11 . 1 55 . 10 ARG HD3 H 3.11 . 1 56 . 10 ARG HH11 H 7.10 . 1 57 . 10 ARG HH12 H 7.10 . 1 58 . 10 ARG HH21 H 6.50 . 1 59 . 10 ARG HH22 H 6.50 . 1 60 . 11 LYS H H 8.11 . 1 61 . 11 LYS HA H 4.15 . 1 62 . 11 LYS HB2 H 2.01 . 2 63 . 11 LYS HB3 H 1.76 . 2 64 . 11 LYS HG2 H 1.57 . 1 65 . 11 LYS HG3 H 1.57 . 1 66 . 11 LYS HD2 H 1.55 . 1 67 . 11 LYS HD3 H 1.55 . 1 68 . 11 LYS HE2 H 3.00 . 1 69 . 11 LYS HE3 H 3.00 . 1 70 . 11 LYS HZ H 7.21 . 1 71 . 12 TYR H H 8.52 . 1 72 . 12 TYR HA H 4.39 . 1 73 . 12 TYR HB2 H 3.36 . 2 74 . 12 TYR HB3 H 3.13 . 2 75 . 12 TYR HD1 H 7.10 . 1 76 . 12 TYR HD2 H 7.10 . 1 77 . 12 TYR HE1 H 6.79 . 1 78 . 12 TYR HE2 H 6.79 . 1 79 . 13 LEU H H 8.59 . 1 80 . 13 LEU HA H 3.97 . 1 81 . 13 LEU HB2 H 2.12 . 2 82 . 13 LEU HB3 H 2.02 . 2 83 . 13 LEU HG H 1.67 . 1 84 . 13 LEU HD1 H 0.98 . 2 85 . 13 LEU HD2 H 0.84 . 2 86 . 14 GLU H H 8.10 . 1 87 . 14 GLU HA H 4.39 . 1 88 . 14 GLU HB2 H 2.34 . 1 89 . 14 GLU HB3 H 2.34 . 1 90 . 14 GLU HG2 H 2.31 . 2 91 . 14 GLU HG3 H 2.28 . 2 92 . 15 GLN H H 7.99 . 1 93 . 15 GLN HA H 4.15 . 1 94 . 15 GLN HB2 H 2.36 . 2 95 . 15 GLN HB3 H 2.22 . 2 96 . 15 GLN HG2 H 2.64 . 1 97 . 15 GLN HG3 H 2.64 . 1 98 . 15 GLN HE21 H 7.69 . 2 99 . 15 GLN HE22 H 7.01 . 2 100 . 16 LEU H H 8.37 . 1 101 . 16 LEU HA H 4.37 . 1 102 . 16 LEU HB2 H 1.74 . 2 103 . 16 LEU HB3 H 1.68 . 2 104 . 16 LEU HG H 1.24 . 1 105 . 16 LEU HD1 H 0.99 . 2 106 . 16 LEU HD2 H 0.82 . 2 107 . 17 HIS H H 8.40 . 1 108 . 17 HIS HA H 3.89 . 1 109 . 17 HIS HB2 H 3.27 . 2 110 . 17 HIS HB3 H 3.13 . 2 111 . 17 HIS HD2 H 7.07 . 1 112 . 17 HIS HE1 H 8.04 . 1 113 . 18 ARG H H 8.03 . 1 114 . 18 ARG HA H 3.99 . 1 115 . 18 ARG HB2 H 2.09 . 2 116 . 18 ARG HB3 H 2.00 . 2 117 . 18 ARG HG2 H 1.89 . 2 118 . 18 ARG HG3 H 1.71 . 2 119 . 18 ARG HD2 H 3.30 . 1 120 . 18 ARG HD3 H 3.30 . 1 121 . 18 ARG HH11 H 7.18 . 1 122 . 18 ARG HH12 H 7.18 . 1 123 . 18 ARG HH21 H 6.64 . 1 124 . 18 ARG HH22 H 6.64 . 1 125 . 19 LYS H H 8.14 . 1 126 . 19 LYS HA H 4.15 . 1 127 . 19 LYS HB2 H 1.87 . 2 128 . 19 LYS HB3 H 1.77 . 2 129 . 19 LYS HG2 H 1.58 . 1 130 . 19 LYS HG3 H 1.58 . 1 131 . 19 LYS HD2 H 1.55 . 1 132 . 19 LYS HD3 H 1.55 . 1 133 . 19 LYS HE2 H 3.02 . 1 134 . 19 LYS HE3 H 3.02 . 1 135 . 19 LYS HZ H 7.12 . 1 136 . 20 LEU H H 8.54 . 1 137 . 20 LEU HA H 3.98 . 1 138 . 20 LEU HB2 H 1.87 . 2 139 . 20 LEU HB3 H 1.69 . 2 140 . 20 LEU HG H 1.47 . 1 141 . 20 LEU HD1 H 0.99 . 2 142 . 20 LEU HD2 H 0.84 . 2 143 . 21 LYS H H 7.74 . 1 144 . 21 LYS HA H 3.94 . 1 145 . 21 LYS HB2 H 1.88 . 2 146 . 21 LYS HB3 H 1.65 . 2 147 . 21 LYS HG2 H 1.39 . 1 148 . 21 LYS HG3 H 1.39 . 1 149 . 21 LYS HD2 H 1.55 . 1 150 . 21 LYS HD3 H 1.55 . 1 151 . 21 LYS HE2 H 3.02 . 1 152 . 21 LYS HE3 H 3.02 . 1 153 . 21 LYS HZ H 7.12 . 1 154 . 22 ASN H H 7.26 . 1 155 . 22 ASN HA H 4.89 . 1 156 . 22 ASN HB2 H 3.08 . 1 157 . 22 ASN HB3 H 2.69 . 1 158 . 22 ASN HD21 H 7.62 . 2 159 . 22 ASN HD22 H 6.95 . 2 160 . 23 CYS H H 7.42 . 1 161 . 23 CYS HA H 4.54 . 1 162 . 23 CYS HB2 H 3.64 . 2 163 . 23 CYS HB3 H 3.06 . 2 164 . 24 LYS H H 8.62 . 1 165 . 24 LYS HA H 4.57 . 1 166 . 24 LYS HB2 H 1.91 . 2 167 . 24 LYS HB3 H 1.74 . 2 168 . 24 LYS HG2 H 1.47 . 1 169 . 24 LYS HG3 H 1.47 . 1 170 . 24 LYS HD2 H 1.49 . 1 171 . 24 LYS HD3 H 1.49 . 1 172 . 24 LYS HE2 H 3.05 . 1 173 . 24 LYS HE3 H 3.05 . 1 174 . 24 LYS HZ H 7.19 . 1 175 . 25 VAL H H 7.62 . 1 176 . 25 VAL HA H 4.16 . 1 177 . 25 VAL HB H 2.09 . 1 178 . 25 VAL HG1 H 0.93 . 1 179 . 25 VAL HG2 H 0.93 . 1 stop_ save_