data_5264 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of Human beta-Defensin 3 ; _BMRB_accession_number 5264 _BMRB_flat_file_name bmr5264.str _Entry_type original _Submission_date 2002-01-23 _Accession_date 2002-01-24 _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 Schibli D. J. . 2 Hunter H. N. . 3 Aseyev V. . . 4 Starner T. D. . 5 Wiencek J. M. . 6 McCray P. M. Jr. 7 Tack B. F. . 8 Vogel H. J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 241 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-06-13 original BMRB . stop_ _Original_release_date 2002-01-24 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The Solution Structures of the Human beta-Defensins lead to a Better Understanding of the Potent Bactericidal Activity of HBD3 against Staphylococcus aureus ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21864161 _PubMed_ID 11741980 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schibli D. J. . 2 Hunter H. N. . 3 Aseyev V. . . 4 Starner T. D. . 5 Wiencek J. M. . 6 McCray P. M. Jr. 7 Tack B. F. . 8 Vogel H. J. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 277 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 8279 _Page_last 8289 _Year 2002 _Details . loop_ _Keyword HBD3 'antimicrobial protein' beta-defensin defensin 'human beta-defensin 3' stop_ save_ ################################## # Molecular system description # ################################## save_system_HBD-3 _Saveframe_category molecular_system _Mol_system_name 'Human Beta-defensin 3' _Abbreviation_common HBD-3 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Beta-defensin 3' $HBD-3 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'antimicrobial protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HBD-3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Human beta-defensin 3' _Abbreviation_common HBD-3 _Molecular_mass 5168.9 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 45 _Mol_residue_sequence ; GIINTLQKYYCRVRGGRCAV LSCLPKEEQIGKCSTRGRKC CRRKK ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ILE 3 ILE 4 ASN 5 THR 6 LEU 7 GLN 8 LYS 9 TYR 10 TYR 11 CYS 12 ARG 13 VAL 14 ARG 15 GLY 16 GLY 17 ARG 18 CYS 19 ALA 20 VAL 21 LEU 22 SER 23 CYS 24 LEU 25 PRO 26 LYS 27 GLU 28 GLU 29 GLN 30 ILE 31 GLY 32 LYS 33 CYS 34 SER 35 THR 36 ARG 37 GLY 38 ARG 39 LYS 40 CYS 41 CYS 42 ARG 43 ARG 44 LYS 45 LYS 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 1KJ6 'Solution Structure Of Human Beta-Defensin 3' 100.00 45 100.00 100.00 1.68e-16 DBJ BAB40572 'defensin like protein [Homo sapiens]' 100.00 67 100.00 100.00 5.09e-17 EMBL CAC03097 'beta-defensin-3 [Homo sapiens]' 100.00 67 100.00 100.00 5.09e-17 EMBL CAL68919 'beta defensin 103 [Gorilla gorilla]' 100.00 67 100.00 100.00 5.45e-17 EMBL CAL68920 'beta defensin 103 [Pongo pygmaeus]' 100.00 67 100.00 100.00 5.09e-17 GenBank AAF73853 'beta defensin-3 [Homo sapiens]' 100.00 67 100.00 100.00 5.09e-17 GenBank AAG02237 'beta-defensin 3 [Homo sapiens]' 100.00 67 100.00 100.00 5.09e-17 GenBank AAG22030 'beta-defensin 3 [Homo sapiens]' 100.00 67 100.00 100.00 5.09e-17 GenBank AAI11597 'DEFB103A protein [synthetic construct]' 100.00 67 100.00 100.00 5.09e-17 GenBank AAI48675 'Defensin, beta 103B [synthetic construct]' 100.00 67 100.00 100.00 5.09e-17 REF NP_001075020 'beta-defensin 103B precursor [Homo sapiens]' 100.00 67 100.00 100.00 5.09e-17 REF NP_061131 'defensin, beta 103A precursor [Homo sapiens]' 100.00 67 100.00 100.00 5.09e-17 REF XP_001083420 'PREDICTED: defensin, beta 103A [Macaca mulatta]' 100.00 67 100.00 100.00 5.09e-17 SWISS-PROT A4H1Z9 'Beta-defensin 103A precursor (Defensin, beta 103A) (Defensin, beta 103)' 100.00 67 100.00 100.00 5.45e-17 SWISS-PROT A4H200 'Beta-defensin 103A precursor (Defensin, beta 103A) (Defensin, beta 103)' 100.00 67 100.00 100.00 5.09e-17 SWISS-PROT P81534 'Beta-defensin 103 precursor (Defensin, beta 103) (Beta-defensin 3) (BD-3) (hBD-3) (HBD3) (DEFB-3) (Defensin-like protein)' 100.00 67 100.00 100.00 5.09e-17 tpg|DAA01350.1| DAA01350 'TPA: TPA_exp: DEFB103-like protein [Papio anubis]' 100.00 67 100.00 100.00 4.61e-17 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ _Tissue $HBD-3 Human 9606 Eukaryota Metazoa Homo sapiens heart 'skeletal muscle; placenta; esophagus; trachea; oral mucosa; skin tissues' 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 _Details $HBD-3 'recombinant technology' . . . . . 'Produced by Peprotech (Rocky Hill, NJ).' 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 $HBD-3 0.36 mM . D2O 10 % . H2O 90 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HBD-3 0.36 mM . D2O 100 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.6 loop_ _Task collection stop_ _Details Bruker save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.8 loop_ _Task processing stop_ _Details 'Delaglio, G., Grzejiek, S., Vuister, G., Zhu, G., Pfeifer, J., Bax, A.' save_ save_NMRView _Saveframe_category software _Name NMRView _Version 4.1.3 loop_ _Task 'data analysis' stop_ _Details 'Johnson, B.A., Blevins, R.A.' save_ save_CNS _Saveframe_category software _Name CNS _Version 1.0 loop_ _Task refinement stop_ _Details ; A.T.Brunger, P.D.Adams, G.M.Clore, W.L.Delano, P.Gros, R.W.Grosse-Kunstleve, J.-S.Jiang, J.Kuszewski, M.Nilges, N.S.Pannu, R.J.Read, L.M.Rice, T.Simonson, G.L.Warren. ; save_ save_Aria _Saveframe_category software _Name Aria _Version 1.0 loop_ _Task refinement stop_ _Details "J.Linge, S.O'Donoghue, M.Nilges." save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _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_2D_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _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 pH 4.00 0.1 n/a pressure 1 . atm 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 internal 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D NOESY' '2D TOCSY' '2D DQF-COSY' 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 'Beta-defensin 3' _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 GLY HA3 H 3.873 . 2 2 . 2 ILE H H 8.530 . 1 3 . 2 ILE HA H 4.231 . 1 4 . 2 ILE HB H 1.839 . 1 5 . 2 ILE HG13 H 1.466 . 9 6 . 2 ILE HG12 H 1.199 . 9 7 . 2 ILE HD1 H 0.882 . 1 8 . 2 ILE HG2 H 0.908 . 4 9 . 3 ILE H H 8.364 . 1 10 . 3 ILE HA H 4.183 . 1 11 . 3 ILE HB H 1.868 . 1 12 . 3 ILE HG13 H 1.506 . 9 13 . 3 ILE HG12 H 1.215 . 9 14 . 3 ILE HD1 H 0.859 . 1 15 . 3 ILE HG2 H 0.854 . 4 16 . 4 ASN H H 8.595 . 1 17 . 4 ASN HA H 4.766 . 1 18 . 4 ASN HB3 H 2.834 . 2 19 . 4 ASN HD21 H 6.918 . 2 20 . 4 ASN HD22 H 7.641 . 2 21 . 5 THR H H 8.172 . 1 22 . 5 THR HA H 4.230 . 1 23 . 5 THR HB H 4.285 . 1 24 . 5 THR HG2 H 1.207 . 1 25 . 6 LEU H H 8.195 . 1 26 . 6 LEU HA H 4.329 . 1 27 . 6 LEU HB3 H 1.715 . 2 28 . 6 LEU HG H 1.622 . 1 29 . 6 LEU HD1 H 0.916 . 2 30 . 6 LEU HD2 H 0.848 . 2 31 . 7 GLN H H 8.166 . 1 32 . 7 GLN HA H 4.130 . 1 33 . 7 GLN HB3 H 2.082 . 2 34 . 7 GLN HB2 H 1.939 . 2 35 . 7 GLN HG3 H 2.335 . 2 36 . 7 GLN HE21 H 6.740 . 2 37 . 7 GLN HE22 H 7.442 . 2 38 . 8 LYS H H 8.160 . 1 39 . 8 LYS HA H 4.045 . 1 40 . 8 LYS HB3 H 1.707 . 2 41 . 8 LYS HG3 H 1.292 . 2 42 . 8 LYS HG2 H 1.187 . 2 43 . 8 LYS HD2 H 1.615 . 2 44 . 8 LYS HE2 H 2.924 . 2 45 . 9 TYR H H 7.994 . 1 46 . 9 TYR HA H 4.532 . 1 47 . 9 TYR HB3 H 2.986 . 2 48 . 9 TYR HB2 H 3.157 . 2 49 . 9 TYR HD1 H 6.981 . 2 50 . 9 TYR HE1 H 6.762 . 2 51 . 10 TYR H H 8.070 . 1 52 . 10 TYR HA H 4.291 . 1 53 . 10 TYR HB3 H 3.077 . 2 54 . 10 TYR HD1 H 7.099 . 2 55 . 10 TYR HE1 H 6.823 . 2 56 . 11 CYS H H 8.343 . 1 57 . 11 CYS HA H 4.255 . 1 58 . 11 CYS HB3 H 3.088 . 2 59 . 11 CYS HB2 H 2.971 . 2 60 . 12 ARG H H 7.958 . 1 61 . 12 ARG HA H 4.270 . 1 62 . 12 ARG HB3 H 1.949 . 2 63 . 12 ARG HG3 H 1.693 . 2 64 . 12 ARG HD3 H 3.210 . 2 65 . 12 ARG HE H 7.208 . 1 66 . 13 VAL H H 8.298 . 1 67 . 13 VAL HA H 3.904 . 1 68 . 13 VAL HB H 2.127 . 1 69 . 13 VAL HG2 H 0.919 . 2 70 . 13 VAL HG1 H 0.953 . 2 71 . 14 ARG H H 7.312 . 1 72 . 14 ARG HA H 4.303 . 1 73 . 14 ARG HB3 H 2.123 . 2 74 . 14 ARG HB2 H 1.936 . 2 75 . 14 ARG HG3 H 1.638 . 2 76 . 14 ARG HG2 H 1.531 . 2 77 . 14 ARG HD3 H 2.978 . 2 78 . 14 ARG HE H 6.879 . 1 79 . 15 GLY H H 8.009 . 1 80 . 15 GLY HA3 H 3.850 . 2 81 . 15 GLY HA2 H 4.217 . 2 82 . 16 GLY H H 8.176 . 1 83 . 16 GLY HA3 H 4.572 . 2 84 . 16 GLY HA2 H 3.306 . 2 85 . 17 ARG H H 8.843 . 1 86 . 17 ARG HA H 4.685 . 1 87 . 17 ARG HB3 H 1.741 . 2 88 . 17 ARG HB2 H 1.680 . 2 89 . 17 ARG HG3 H 1.535 . 2 90 . 17 ARG HG2 H 1.259 . 2 91 . 17 ARG HD3 H 3.184 . 2 92 . 17 ARG HD2 H 2.999 . 2 93 . 17 ARG HE H 9.220 . 1 94 . 17 ARG HH21 H 6.847 . 9 95 . 18 CYS H H 8.924 . 1 96 . 18 CYS HA H 5.362 . 1 97 . 18 CYS HB3 H 2.935 . 2 98 . 18 CYS HB2 H 2.720 . 2 99 . 19 ALA H H 9.365 . 1 100 . 19 ALA HA H 4.537 . 1 101 . 19 ALA HB H 1.323 . 1 102 . 20 VAL H H 8.640 . 1 103 . 20 VAL HA H 3.845 . 1 104 . 20 VAL HB H 2.034 . 1 105 . 20 VAL HG2 H 0.975 . 2 106 . 20 VAL HG1 H 1.012 . 2 107 . 21 LEU H H 8.345 . 1 108 . 21 LEU HA H 4.408 . 1 109 . 21 LEU HB3 H 1.718 . 2 110 . 21 LEU HG H 1.556 . 1 111 . 21 LEU HD1 H 0.951 . 2 112 . 21 LEU HD2 H 0.930 . 2 113 . 22 SER H H 8.189 . 1 114 . 22 SER HA H 4.484 . 1 115 . 22 SER HB3 H 3.795 . 2 116 . 22 SER HB2 H 3.881 . 2 117 . 23 CYS H H 8.581 . 1 118 . 23 CYS HA H 4.784 . 1 119 . 23 CYS HB3 H 3.399 . 2 120 . 23 CYS HB2 H 2.659 . 2 121 . 24 LEU H H 9.244 . 1 122 . 24 LEU HA H 4.500 . 1 123 . 24 LEU HB3 H 1.766 . 2 124 . 24 LEU HB2 H 1.305 . 2 125 . 24 LEU HG H 1.632 . 1 126 . 24 LEU HD1 H 0.958 . 4 127 . 24 LEU HD2 H 0.868 . 4 128 . 25 PRO HA H 4.354 . 1 129 . 25 PRO HB3 H 1.873 . 2 130 . 25 PRO HB2 H 2.431 . 2 131 . 25 PRO HG3 H 2.160 . 2 132 . 25 PRO HG2 H 2.056 . 2 133 . 25 PRO HD3 H 3.753 . 2 134 . 25 PRO HD2 H 3.819 . 2 135 . 26 LYS H H 7.828 . 1 136 . 26 LYS HA H 4.348 . 1 137 . 26 LYS HB3 H 1.868 . 2 138 . 26 LYS HB2 H 2.110 . 2 139 . 26 LYS HG3 H 1.419 . 2 140 . 26 LYS HD2 H 1.769 . 2 141 . 26 LYS HE2 H 2.982 . 2 142 . 27 GLU H H 8.122 . 1 143 . 27 GLU HA H 4.863 . 1 144 . 27 GLU HB3 H 1.821 . 2 145 . 27 GLU HB2 H 1.651 . 2 146 . 27 GLU HG3 H 2.520 . 2 147 . 27 GLU HG2 H 2.120 . 2 148 . 28 GLU H H 9.032 . 1 149 . 28 GLU HA H 4.755 . 1 150 . 28 GLU HB3 H 1.974 . 2 151 . 28 GLU HB2 H 1.869 . 2 152 . 28 GLU HG3 H 2.189 . 2 153 . 28 GLU HG2 H 2.123 . 2 154 . 29 GLN H H 9.027 . 1 155 . 29 GLN HA H 4.987 . 1 156 . 29 GLN HB3 H 2.088 . 2 157 . 29 GLN HG3 H 2.482 . 2 158 . 29 GLN HE21 H 7.099 . 2 159 . 29 GLN HE22 H 7.187 . 2 160 . 30 ILE H H 8.744 . 1 161 . 30 ILE HA H 4.717 . 1 162 . 30 ILE HB H 2.103 . 1 163 . 30 ILE HG13 H 0.966 . 1 164 . 30 ILE HD1 H 0.674 . 1 165 . 30 ILE HG2 H 0.824 . 4 166 . 31 GLY H H 7.629 . 1 167 . 31 GLY HA3 H 4.339 . 2 168 . 31 GLY HA2 H 4.055 . 2 169 . 32 LYS H H 8.947 . 1 170 . 32 LYS HA H 4.930 . 1 171 . 32 LYS HB3 H 1.966 . 2 172 . 32 LYS HG3 H 1.376 . 2 173 . 32 LYS HD2 H 1.665 . 2 174 . 32 LYS HE2 H 2.948 . 2 175 . 33 CYS H H 8.424 . 1 176 . 33 CYS HA H 4.840 . 1 177 . 33 CYS HB3 H 3.285 . 2 178 . 34 SER H H 8.202 . 1 179 . 34 SER HA H 4.364 . 1 180 . 34 SER HB3 H 3.895 . 2 181 . 34 SER HB2 H 4.076 . 2 182 . 35 THR H H 8.036 . 1 183 . 35 THR HA H 4.270 . 1 184 . 35 THR HB H 4.151 . 1 185 . 35 THR HG2 H 1.270 . 1 186 . 36 ARG H H 8.461 . 1 187 . 36 ARG HA H 4.213 . 1 188 . 36 ARG HB3 H 1.766 . 2 189 . 36 ARG HB2 H 1.987 . 2 190 . 36 ARG HG3 H 1.654 . 2 191 . 36 ARG HD3 H 3.208 . 2 192 . 37 GLY H H 8.166 . 1 193 . 37 GLY HA3 H 4.106 . 2 194 . 37 GLY HA2 H 3.780 . 2 195 . 38 ARG H H 7.625 . 1 196 . 38 ARG HA H 4.570 . 1 197 . 38 ARG HB3 H 1.756 . 2 198 . 38 ARG HG3 H 1.603 . 2 199 . 38 ARG HD3 H 3.024 . 2 200 . 38 ARG HE H 7.123 . 1 201 . 39 LYS H H 8.974 . 1 202 . 39 LYS HA H 4.317 . 1 203 . 39 LYS HB3 H 1.558 . 2 204 . 39 LYS HG3 H 1.350 . 2 205 . 39 LYS HD2 H 1.548 . 2 206 . 39 LYS HE2 H 3.039 . 2 207 . 40 CYS H H 8.311 . 1 208 . 40 CYS HA H 5.226 . 1 209 . 40 CYS HB3 H 2.494 . 2 210 . 40 CYS HB2 H 2.546 . 2 211 . 41 CYS H H 9.448 . 1 212 . 41 CYS HA H 5.468 . 1 213 . 41 CYS HB3 H 2.843 . 2 214 . 41 CYS HB2 H 2.553 . 2 215 . 42 ARG H H 9.430 . 1 216 . 42 ARG HA H 4.922 . 1 217 . 42 ARG HB3 H 1.922 . 2 218 . 42 ARG HB2 H 1.385 . 2 219 . 42 ARG HG3 H 1.801 . 2 220 . 42 ARG HD3 H 3.375 . 2 221 . 42 ARG HD2 H 2.939 . 2 222 . 42 ARG HE H 7.662 . 1 223 . 43 ARG H H 8.986 . 1 224 . 43 ARG HA H 4.235 . 1 225 . 43 ARG HB3 H 1.895 . 2 226 . 43 ARG HG3 H 1.736 . 2 227 . 43 ARG HD3 H 3.246 . 2 228 . 43 ARG HE H 7.346 . 1 229 . 44 LYS H H 8.604 . 1 230 . 44 LYS HA H 4.204 . 1 231 . 44 LYS HB3 H 1.829 . 2 232 . 44 LYS HG3 H 1.366 . 2 233 . 44 LYS HG2 H 1.309 . 2 234 . 44 LYS HD2 H 1.608 . 2 235 . 44 LYS HE2 H 2.933 . 2 236 . 45 LYS H H 8.243 . 1 237 . 45 LYS HA H 4.099 . 1 238 . 45 LYS HB3 H 1.783 . 2 239 . 45 LYS HG3 H 1.434 . 2 240 . 45 LYS HD2 H 1.713 . 2 241 . 45 LYS HE2 H 3.013 . 2 stop_ save_