data_18705 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of the Antimicrobial Peptide Human Defensin 5 ; _BMRB_accession_number 18705 _BMRB_flat_file_name bmr18705.str _Entry_type original _Submission_date 2012-09-10 _Accession_date 2012-09-10 _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 Wommack Andrew J. . 2 Robson Scott A. . 3 Wanniarahchi Yoshitha A. . 4 Wan Andrea . . 5 Turner Christopher J. . 6 Nolan Elizabeth M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 151 "13C chemical shifts" 96 "15N chemical shifts" 27 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-04-12 update BMRB 'update entry citation' 2012-11-27 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR solution structure and condition-dependent oligomerization of the antimicrobial peptide human defensin 5.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23163963 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wommack Andrew J. . 2 Robson Scott A. . 3 Wanniarachchi Yoshitha A. . 4 Wan Andrea . . 5 Turner Christopher J. . 6 Wagner Gerhard . . 7 Nolan Elizabeth M. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 51 _Journal_issue 48 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 9624 _Page_last 9637 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Antimicrobial Peptide Human Defensin 5' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Antimicrobial Peptide Human Defensin 5' $Human_Defensin_5 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Human_Defensin_5 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass 3594.227 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 32 _Mol_residue_sequence ; ATCYCRTGRCATRESLSGVC EISGRLYRLCCR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ALA 2 2 THR 3 3 CYS 4 4 TYR 5 5 CYS 6 6 ARG 7 7 THR 8 8 GLY 9 9 ARG 10 10 CYS 11 11 ALA 12 12 THR 13 13 ARG 14 14 GLU 15 15 SER 16 16 LEU 17 17 SER 18 18 GLY 19 19 VAL 20 20 CYS 21 21 GLU 22 22 ILE 23 23 SER 24 24 GLY 25 25 ARG 26 26 LEU 27 27 TYR 28 28 ARG 29 29 LEU 30 30 CYS 31 31 CYS 32 32 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-09-28 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 BMRB 19693 entity 100.00 32 100.00 100.00 1.41e-11 PDB 1ZMP "Crystal Structure Of Human Defensin-5" 100.00 32 100.00 100.00 1.41e-11 PDB 2LXZ "Solution Structure Of The Antimicrobial Peptide Human Defensin 5" 100.00 32 100.00 100.00 1.41e-11 PDB 2MIT "Solution Structure Of Oxidized Dimeric Form Of Human Defensin 5" 100.00 32 100.00 100.00 1.41e-11 EMBL CCD28566 "human alpha-defensin 5 proform [synthetic construct]" 100.00 94 100.00 100.00 8.98e-13 GB AAA35754 "defensin 5 [Homo sapiens]" 100.00 94 100.00 100.00 8.98e-13 GB AAH69690 "Defensin, alpha 5, Paneth cell-specific [Homo sapiens]" 100.00 94 100.00 100.00 8.98e-13 GB AAI07080 "Defensin, alpha 5, Paneth cell-specific [Homo sapiens]" 100.00 94 100.00 100.00 8.98e-13 GB AAT68886 "defensin, alpha 5, Paneth cell-specific [Homo sapiens]" 100.00 94 100.00 100.00 8.98e-13 GB ADQ32910 "defensin, alpha 5, Paneth cell-specific [synthetic construct]" 100.00 94 100.00 100.00 8.98e-13 REF NP_066290 "defensin-5 preproprotein [Homo sapiens]" 100.00 94 100.00 100.00 8.98e-13 SP Q01523 "RecName: Full=Defensin-5; AltName: Full=Defensin, alpha 5; AltName: Full=HD5(20-94); Contains: RecName: Full=HD5(23-94); Contai" 100.00 94 100.00 100.00 8.98e-13 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Human_Defensin_5 Human 9606 Eukaryota Metazoa Homo sapiens 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 $Human_Defensin_5 'recombinant technology' . Escherichia coli . pJ201-TEV-HD5 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 TFA . mM 0 1 'natural abundance' H2O 90 % . . 'natural abundance' D2O 10 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_1 save_ save_3D_HCACO_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCACO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.4 . mM pH 4 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 C 13 protons ppm 0 external indirect . . . 0.251449530 DSS H 1 protons ppm 0 external indirect . . . 1 DSS N 15 protons ppm 0 external indirect . . . 0.101329118 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D HNCO' '3D HNCA' '3D 1H-15N NOESY' '3D 1H-13C NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Antimicrobial Peptide Human Defensin 5' _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 1 ALA HA H 4.326 0.020 1 2 1 1 ALA HB H 1.513 0.020 1 3 1 1 ALA CA C 51.896 0.300 1 4 1 1 ALA CB C 19.720 0.300 1 5 2 2 THR H H 8.979 0.020 1 6 2 2 THR HA H 4.398 0.020 1 7 2 2 THR HB H 4.030 0.020 1 8 2 2 THR HG2 H 1.140 0.020 1 9 2 2 THR CA C 62.489 0.300 1 10 2 2 THR CB C 70.031 0.300 1 11 2 2 THR CG2 C 21.341 0.300 1 12 2 2 THR N N 118.310 0.300 1 13 3 3 CYS H H 8.541 0.020 1 14 3 3 CYS HA H 5.653 0.020 1 15 3 3 CYS HB2 H 2.600 0.020 1 16 3 3 CYS HB3 H 3.090 0.020 1 17 3 3 CYS C C 172.018 0.300 1 18 3 3 CYS CA C 55.069 0.300 1 19 3 3 CYS CB C 49.718 0.300 1 20 3 3 CYS N N 123.108 0.300 1 21 4 4 TYR HA H 4.609 0.020 1 22 4 4 TYR HB2 H 2.552 0.020 1 23 4 4 TYR HB3 H 3.008 0.020 1 24 4 4 TYR HD1 H 7.148 0.020 1 25 4 4 TYR HD2 H 7.148 0.020 1 26 4 4 TYR HE1 H 6.719 0.020 1 27 4 4 TYR HE2 H 6.719 0.020 1 28 4 4 TYR CA C 56.618 0.300 1 29 4 4 TYR CB C 42.182 0.300 1 30 5 5 CYS H H 9.195 0.020 1 31 5 5 CYS HA H 4.612 0.020 1 32 5 5 CYS HB2 H 2.551 0.020 1 33 5 5 CYS HB3 H 3.004 0.020 1 34 5 5 CYS CA C 56.553 0.300 1 35 5 5 CYS CB C 42.208 0.300 1 36 5 5 CYS N N 119.803 0.300 1 37 6 6 ARG H H 8.999 0.020 1 38 6 6 ARG HA H 5.333 0.020 1 39 6 6 ARG HB2 H 2.863 0.020 1 40 6 6 ARG HB3 H 2.863 0.020 1 41 6 6 ARG HG2 H 0.501 0.020 1 42 6 6 ARG HG3 H 0.501 0.020 1 43 6 6 ARG HD2 H 2.712 0.020 1 44 6 6 ARG HD3 H 2.712 0.020 1 45 6 6 ARG CA C 55.045 0.300 1 46 6 6 ARG CB C 40.925 0.300 1 47 6 6 ARG CG C 13.031 0.300 1 48 6 6 ARG CD C 40.966 0.300 1 49 6 6 ARG N N 123.484 0.300 1 50 7 7 THR H H 9.531 0.020 1 51 7 7 THR HA H 4.917 0.020 1 52 7 7 THR HB H 4.867 0.020 1 53 7 7 THR HG2 H 1.798 0.020 1 54 7 7 THR CA C 62.395 0.300 1 55 7 7 THR CB C 71.434 0.300 1 56 7 7 THR CG2 C 32.493 0.300 1 57 7 7 THR N N 126.371 0.300 1 58 8 8 GLY H H 8.004 0.020 1 59 8 8 GLY HA2 H 3.860 0.020 1 60 8 8 GLY HA3 H 4.239 0.020 1 61 8 8 GLY C C 172.685 0.300 1 62 8 8 GLY CA C 44.809 0.300 1 63 8 8 GLY N N 112.530 0.300 1 64 9 9 ARG H H 8.183 0.020 1 65 9 9 ARG HA H 4.283 0.020 1 66 9 9 ARG HB2 H 1.987 0.020 1 67 9 9 ARG HB3 H 1.987 0.020 1 68 9 9 ARG HG2 H 1.789 0.020 1 69 9 9 ARG HG3 H 1.789 0.020 1 70 9 9 ARG HD2 H 3.346 0.020 1 71 9 9 ARG HD3 H 3.346 0.020 1 72 9 9 ARG C C 176.627 0.300 1 73 9 9 ARG CA C 55.748 0.300 1 74 9 9 ARG CB C 31.418 0.300 1 75 9 9 ARG CG C 31.374 0.300 1 76 9 9 ARG CD C 43.461 0.300 1 77 9 9 ARG N N 119.486 0.300 1 78 10 10 CYS H H 8.595 0.020 1 79 10 10 CYS HA H 4.874 0.020 1 80 10 10 CYS HB2 H 2.788 0.020 1 81 10 10 CYS HB3 H 3.543 0.020 1 82 10 10 CYS C C 174.788 0.300 1 83 10 10 CYS CA C 52.737 0.300 1 84 10 10 CYS CB C 35.343 0.300 1 85 10 10 CYS N N 116.919 0.300 1 86 11 11 ALA H H 8.590 0.020 1 87 11 11 ALA HA H 4.433 0.020 1 88 11 11 ALA HB H 1.331 0.020 1 89 11 11 ALA C C 177.552 0.300 1 90 11 11 ALA CA C 51.381 0.300 1 91 11 11 ALA CB C 19.400 0.300 1 92 11 11 ALA N N 124.805 0.300 1 93 12 12 THR H H 8.238 0.020 1 94 12 12 THR HA H 4.002 0.020 1 95 12 12 THR HB H 4.107 0.020 1 96 12 12 THR HG2 H 1.330 0.020 1 97 12 12 THR C C 174.815 0.300 1 98 12 12 THR CA C 65.118 0.300 1 99 12 12 THR CB C 68.792 0.300 1 100 12 12 THR CG2 C 21.930 0.300 1 101 12 12 THR N N 114.885 0.300 1 102 13 13 ARG H H 8.518 0.020 1 103 13 13 ARG HA H 4.148 0.020 1 104 13 13 ARG HB3 H 2.089 0.020 1 105 13 13 ARG HG3 H 1.682 0.020 1 106 13 13 ARG HD3 H 3.244 0.020 1 107 13 13 ARG C C 175.566 0.300 1 108 13 13 ARG CA C 57.592 0.300 1 109 13 13 ARG CB C 28.486 0.300 1 110 13 13 ARG CG C 28.065 0.300 1 111 13 13 ARG CD C 43.463 0.300 1 112 13 13 ARG N N 116.842 0.300 1 113 14 14 GLU H H 7.855 0.020 1 114 14 14 GLU HA H 4.686 0.020 1 115 14 14 GLU HB2 H 1.697 0.020 1 116 14 14 GLU HB3 H 1.697 0.020 1 117 14 14 GLU HG2 H 2.438 0.020 1 118 14 14 GLU HG3 H 2.438 0.020 1 119 14 14 GLU C C 176.183 0.300 1 120 14 14 GLU CA C 54.645 0.300 1 121 14 14 GLU CB C 32.073 0.300 1 122 14 14 GLU CG C 32.225 0.300 1 123 14 14 GLU N N 117.264 0.300 1 124 15 15 SER H H 9.273 0.020 1 125 15 15 SER HA H 4.807 0.020 1 126 15 15 SER HB2 H 3.741 0.020 1 127 15 15 SER HB3 H 3.808 0.020 1 128 15 15 SER C C 174.427 0.300 1 129 15 15 SER CA C 56.875 0.300 1 130 15 15 SER CB C 65.036 0.300 1 131 15 15 SER N N 114.972 0.300 1 132 16 16 LEU H H 9.076 0.020 1 133 16 16 LEU HA H 4.791 0.020 1 134 16 16 LEU HB2 H 2.005 0.020 1 135 16 16 LEU HB3 H 2.005 0.020 1 136 16 16 LEU HG H 1.631 0.020 1 137 16 16 LEU HD1 H 1.203 0.020 1 138 16 16 LEU HD2 H 1.051 0.020 1 139 16 16 LEU C C 177.525 0.300 1 140 16 16 LEU CA C 56.384 0.300 1 141 16 16 LEU CB C 41.437 0.300 1 142 16 16 LEU CG C 41.331 0.300 1 143 16 16 LEU CD1 C 24.384 0.300 1 144 16 16 LEU CD2 C 21.600 0.300 1 145 16 16 LEU N N 129.724 0.300 1 146 17 17 SER H H 9.387 0.020 1 147 17 17 SER HA H 4.877 0.020 1 148 17 17 SER HB2 H 3.502 0.020 1 149 17 17 SER HB3 H 3.984 0.020 1 150 17 17 SER CA C 58.092 0.300 1 151 17 17 SER CB C 65.350 0.300 1 152 17 17 SER N N 123.451 0.300 1 153 18 18 GLY H H 7.608 0.020 1 154 18 18 GLY HA2 H 4.077 0.020 1 155 18 18 GLY HA3 H 4.532 0.020 1 156 18 18 GLY CA C 44.935 0.300 1 157 18 18 GLY N N 107.233 0.300 1 158 19 19 VAL H H 8.692 0.020 1 159 19 19 VAL HA H 5.065 0.020 1 160 19 19 VAL HB H 2.204 0.020 1 161 19 19 VAL HG1 H 1.068 0.020 1 162 19 19 VAL HG2 H 0.955 0.020 1 163 19 19 VAL CA C 60.314 0.300 1 164 19 19 VAL CB C 35.289 0.300 1 165 19 19 VAL CG1 C 25.633 0.300 1 166 19 19 VAL CG2 C 19.388 0.300 1 167 19 19 VAL N N 118.833 0.300 1 168 20 20 CYS H H 8.133 0.020 1 169 20 20 CYS HA H 4.892 0.020 1 170 20 20 CYS HB2 H 1.409 0.020 1 171 20 20 CYS HB3 H 1.661 0.020 1 172 20 20 CYS C C 176.328 0.300 1 173 20 20 CYS CA C 54.476 0.300 1 174 20 20 CYS CB C 43.178 0.300 1 175 20 20 CYS N N 121.714 0.300 1 176 22 22 ILE H H 8.865 0.020 1 177 22 22 ILE HA H 4.341 0.020 1 178 22 22 ILE HB H 1.830 0.020 1 179 22 22 ILE HG12 H 0.798 0.020 1 180 22 22 ILE HG13 H 0.798 0.020 1 181 22 22 ILE HG2 H 0.946 0.020 1 182 22 22 ILE HD1 H 0.503 0.020 1 183 22 22 ILE C C 176.380 0.300 1 184 22 22 ILE CA C 61.260 0.300 1 185 22 22 ILE CB C 40.877 0.300 1 186 22 22 ILE CG1 C 23.473 0.300 1 187 22 22 ILE CG2 C 17.053 0.300 1 188 22 22 ILE CD1 C 12.848 0.300 1 189 22 22 ILE N N 124.351 0.300 1 190 23 23 SER H H 9.633 0.020 1 191 23 23 SER HA H 4.108 0.020 1 192 23 23 SER HB2 H 3.927 0.020 1 193 23 23 SER HB3 H 4.256 0.020 1 194 23 23 SER CA C 58.444 0.300 1 195 23 23 SER CB C 62.226 0.300 1 196 23 23 SER N N 124.886 0.300 1 197 24 24 GLY H H 8.635 0.020 1 198 24 24 GLY HA2 H 3.698 0.020 1 199 24 24 GLY HA3 H 4.182 0.020 1 200 24 24 GLY C C 173.429 0.300 1 201 24 24 GLY CA C 45.233 0.300 1 202 24 24 GLY N N 104.151 0.300 1 203 25 25 ARG H H 7.969 0.020 1 204 25 25 ARG HA H 4.580 0.020 1 205 25 25 ARG HB2 H 1.884 0.020 1 206 25 25 ARG HB3 H 1.884 0.020 1 207 25 25 ARG HG2 H 1.500 0.020 1 208 25 25 ARG HG3 H 1.680 0.020 1 209 25 25 ARG HD2 H 3.239 0.020 1 210 25 25 ARG HD3 H 3.239 0.020 1 211 25 25 ARG HE H 7.132 0.020 1 212 25 25 ARG C C 174.701 0.300 1 213 25 25 ARG CA C 54.268 0.300 1 214 25 25 ARG CB C 32.556 0.300 1 215 25 25 ARG CG C 27.523 0.300 1 216 25 25 ARG CD C 43.268 0.300 1 217 25 25 ARG N N 121.072 0.300 1 218 26 26 LEU H H 8.161 0.020 1 219 26 26 LEU HA H 4.799 0.020 1 220 26 26 LEU HB2 H 1.522 0.020 1 221 26 26 LEU HB3 H 1.522 0.020 1 222 26 26 LEU HG H 1.368 0.020 1 223 26 26 LEU HD1 H 0.923 0.020 1 224 26 26 LEU HD2 H 0.923 0.020 1 225 26 26 LEU CA C 55.937 0.300 1 226 26 26 LEU CB C 42.847 0.300 1 227 26 26 LEU CG C 26.909 0.300 1 228 26 26 LEU CD1 C 24.744 0.300 1 229 26 26 LEU N N 124.251 0.300 1 230 27 27 TYR H H 9.173 0.020 1 231 27 27 TYR HA H 4.786 0.020 1 232 27 27 TYR HB2 H 2.502 0.020 1 233 27 27 TYR HB3 H 3.338 0.020 1 234 27 27 TYR HD1 H 6.971 0.020 1 235 27 27 TYR HD2 H 6.971 0.020 1 236 27 27 TYR HE1 H 6.838 0.020 1 237 27 27 TYR HE2 H 6.838 0.020 1 238 27 27 TYR CA C 54.099 0.300 1 239 27 27 TYR CB C 40.954 0.300 1 240 27 27 TYR N N 122.809 0.300 1 241 29 29 LEU HA H 4.612 0.020 1 242 29 29 LEU HB2 H 1.519 0.020 1 243 29 29 LEU HB3 H 1.519 0.020 1 244 29 29 LEU HG H 1.334 0.020 1 245 29 29 LEU HD1 H 0.761 0.020 1 246 29 29 LEU HD2 H 0.761 0.020 1 247 29 29 LEU CB C 42.860 0.300 1 248 30 30 CYS H H 9.020 0.020 1 249 30 30 CYS HA H 5.442 0.020 1 250 30 30 CYS HB2 H 2.862 0.020 1 251 30 30 CYS HB3 H 3.444 0.020 1 252 30 30 CYS CA C 53.458 0.300 1 253 30 30 CYS CB C 43.152 0.300 1 254 30 30 CYS N N 127.797 0.300 1 255 31 31 CYS H H 9.049 0.020 1 256 31 31 CYS HA H 5.767 0.020 1 257 31 31 CYS HB2 H 2.957 0.020 1 258 31 31 CYS HB3 H 3.111 0.020 1 259 31 31 CYS C C 173.200 0.300 1 260 31 31 CYS CA C 55.684 0.300 1 261 31 31 CYS CB C 49.066 0.300 1 262 31 31 CYS N N 120.526 0.300 1 263 32 32 ARG H H 8.969 0.020 1 264 32 32 ARG HA H 4.586 0.020 1 265 32 32 ARG HG2 H 1.817 0.020 1 266 32 32 ARG HG3 H 1.817 0.020 1 267 32 32 ARG HD2 H 3.281 0.020 1 268 32 32 ARG HD3 H 3.281 0.020 1 269 32 32 ARG C C 179.595 0.300 1 270 32 32 ARG CA C 57.317 0.300 1 271 32 32 ARG CB C 32.511 0.300 1 272 32 32 ARG CG C 27.216 0.300 1 273 32 32 ARG CD C 43.725 0.300 1 274 32 32 ARG N N 126.371 0.300 1 stop_ save_