data_26790 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H Chemical Shift Assignments for AvBD7 ; _BMRB_accession_number 26790 _BMRB_flat_file_name bmr26790.str _Entry_type original _Submission_date 2016-05-03 _Accession_date 2016-05-03 _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 Landon Celine . . 2 Meudal Herve . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 289 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-03-02 original BMRB . stop_ _Original_release_date 2016-05-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The Unusual Resistance of Avian Defensin AvBD7 to Proteolytic Enzymes Preserves Its Antibacterial Activity ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 27561012 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bailleul Geoffrey . . 2 Kravtzoff Amanda . . 3 Joulin-Giet Alix . . 4 Lecaille Fabien . . 5 Labas Valerie . . 6 Meudal Herve . . 7 Loth Karine . . 8 Teixeira-Gomes Ana-Paula P. . 9 Gilbert Florence B. . 10 Coquet Laurent . . 11 Jouenne Thierry . . 12 Bromme Dieter . . 13 Schouler Catherine . . 14 Landon Celine . . 15 Lalmanach Gilles . . 16 Lalmanach Anne-Christine C. . stop_ _Journal_abbreviation 'PLoS ONE' _Journal_name_full 'PloS one' _Journal_volume 11 _Journal_issue 8 _Journal_ISSN 1932-6203 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first e0161573 _Page_last e0161573 _Year 2016 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name AvBD7 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label AvBD7 $AvBD7 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_AvBD7 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common AvBD7 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 47 _Mol_residue_sequence ; XPFIPRPIDTCRLRNGICFP GICRRPYYWIGTCNNGIGSC CARGWRS ; loop_ _Residue_seq_code _Residue_label 1 PCA 2 PRO 3 PHE 4 ILE 5 PRO 6 ARG 7 PRO 8 ILE 9 ASP 10 THR 11 CYS 12 ARG 13 LEU 14 ARG 15 ASN 16 GLY 17 ILE 18 CYS 19 PHE 20 PRO 21 GLY 22 ILE 23 CYS 24 ARG 25 ARG 26 PRO 27 TYR 28 TYR 29 TRP 30 ILE 31 GLY 32 THR 33 CYS 34 ASN 35 ASN 36 GLY 37 ILE 38 GLY 39 SER 40 CYS 41 CYS 42 ALA 43 ARG 44 GLY 45 TRP 46 ARG 47 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_PCA _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common 'PYROGLUTAMIC ACID' _BMRB_code PCA _PDB_code PCA _Standard_residue_derivative . _Molecular_mass 129.114 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD CD C . 0 . ? OE OE O . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG2 HG2 H . 0 . ? HG3 HG3 H . 0 . ? HXT HXT 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 CA ? ? SING N CD ? ? SING N H ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG CD ? ? SING CG HG2 ? ? SING CG HG3 ? ? DOUB CD OE ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $AvBD7 chicken 9031 Eukaryota Metazoa Gallus gallus 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 $AvBD7 extracted . Gallus gallus . . 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 $AvBD7 0.23 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AvBD7 0.23 mM 'natural abundance' D2O 100 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_Ccpnmr _Saveframe_category software _Name Ccpnmr _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 950 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _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 pH 4.5 . 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 water H 1 protons ppm 4.77 internal direct . . . 1.000000000 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 '2D 1H-1H TOCSY' '2D 1H-1H NOESY' '2D DQF-COSY' 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 AvBD7 _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 PCA HA H 4.676 . . 2 1 1 PCA HB3 H 2.003 . . 3 1 1 PCA HB2 H 2.589 . . 4 1 1 PCA HG3 H 2.420 . . 5 1 1 PCA HG2 H 2.420 . . 6 2 2 PRO HA H 4.410 . . 7 2 2 PRO HB3 H 1.816 . . 8 2 2 PRO HB2 H 2.229 . . 9 2 2 PRO HG3 H 1.989 . . 10 2 2 PRO HG2 H 1.989 . . 11 2 2 PRO HD3 H 3.601 . . 12 2 2 PRO HD2 H 3.689 . . 13 3 3 PHE H H 8.178 . . 14 3 3 PHE HA H 4.609 . . 15 3 3 PHE HB3 H 2.990 . . 16 3 3 PHE HB2 H 3.124 . . 17 3 3 PHE HD1 H 7.208 . . 18 3 3 PHE HD2 H 7.208 . . 19 3 3 PHE HE1 H 7.300 . . 20 3 3 PHE HE2 H 7.300 . . 21 3 3 PHE HZ H 7.332 . . 22 4 4 ILE H H 7.916 . . 23 4 4 ILE HA H 4.371 . . 24 4 4 ILE HB H 1.726 . . 25 4 4 ILE HG12 H 1.081 . . 26 4 4 ILE HG13 H 1.418 . . 27 4 4 ILE HG2 H 0.828 . . 28 4 4 ILE HD1 H 0.828 . . 29 5 5 PRO HA H 4.279 . . 30 5 5 PRO HB3 H 1.872 . . 31 5 5 PRO HB2 H 2.287 . . 32 5 5 PRO HG3 H 1.992 . . 33 5 5 PRO HG2 H 1.991 . . 34 5 5 PRO HD3 H 3.627 . . 35 5 5 PRO HD2 H 3.670 . . 36 6 6 ARG H H 8.318 . . 37 6 6 ARG HA H 4.589 . . 38 6 6 ARG HB3 H 1.837 . . 39 6 6 ARG HB2 H 1.839 . . 40 6 6 ARG HG3 H 1.717 . . 41 6 6 ARG HG2 H 1.717 . . 42 6 6 ARG HD3 H 3.222 . . 43 6 6 ARG HD2 H 3.222 . . 44 6 6 ARG HE H 7.193 . . 45 7 7 PRO HA H 4.430 . . 46 7 7 PRO HB3 H 1.878 . . 47 7 7 PRO HB2 H 2.279 . . 48 7 7 PRO HG3 H 2.012 . . 49 7 7 PRO HG2 H 2.009 . . 50 7 7 PRO HD3 H 3.611 . . 51 7 7 PRO HD2 H 3.800 . . 52 8 8 ILE H H 8.240 . . 53 8 8 ILE HA H 4.085 . . 54 8 8 ILE HB H 1.808 . . 55 8 8 ILE HG12 H 1.210 . . 56 8 8 ILE HG13 H 1.500 . . 57 8 8 ILE HG2 H 0.884 . . 58 8 8 ILE HD1 H 0.884 . . 59 9 9 ASP H H 8.323 . . 60 9 9 ASP HA H 4.768 . . 61 9 9 ASP HB3 H 2.660 . . 62 9 9 ASP HB2 H 2.868 . . 63 10 10 THR H H 8.356 . . 64 10 10 THR HA H 3.974 . . 65 10 10 THR HB H 4.316 . . 66 10 10 THR HG2 H 1.239 . . 67 11 11 CYS H H 8.443 . . 68 11 11 CYS HA H 4.356 . . 69 11 11 CYS HB3 H 3.078 . . 70 11 11 CYS HB2 H 3.078 . . 71 12 12 ARG H H 8.024 . . 72 12 12 ARG HA H 4.204 . . 73 12 12 ARG HB3 H 1.841 . . 74 12 12 ARG HB2 H 1.838 . . 75 12 12 ARG HG3 H 1.660 . . 76 12 12 ARG HG2 H 1.722 . . 77 12 12 ARG HD3 H 3.229 . . 78 12 12 ARG HD2 H 3.276 . . 79 12 12 ARG HE H 7.294 . . 80 13 13 LEU H H 7.884 . . 81 13 13 LEU HA H 4.133 . . 82 13 13 LEU HB3 H 1.637 . . 83 13 13 LEU HB2 H 1.750 . . 84 13 13 LEU HG H 1.637 . . 85 13 13 LEU HD1 H 0.890 . . 86 13 13 LEU HD2 H 0.890 . . 87 14 14 ARG H H 7.239 . . 88 14 14 ARG HA H 4.353 . . 89 14 14 ARG HB3 H 1.599 . . 90 14 14 ARG HB2 H 2.056 . . 91 14 14 ARG HG3 H 1.741 . . 92 14 14 ARG HG2 H 1.741 . . 93 14 14 ARG HD3 H 3.109 . . 94 14 14 ARG HD2 H 3.109 . . 95 14 14 ARG HE H 6.998 . . 96 15 15 ASN H H 8.005 . . 97 15 15 ASN HA H 4.413 . . 98 15 15 ASN HB3 H 2.578 . . 99 15 15 ASN HB2 H 3.161 . . 100 15 15 ASN HD21 H 7.531 . . 101 15 15 ASN HD22 H 6.883 . . 102 16 16 GLY H H 8.007 . . 103 16 16 GLY HA3 H 3.233 . . 104 16 16 GLY HA2 H 4.507 . . 105 17 17 ILE H H 8.677 . . 106 17 17 ILE HA H 4.088 . . 107 17 17 ILE HB H 1.480 . . 108 17 17 ILE HG12 H 1.060 . . 109 17 17 ILE HG13 H 1.060 . . 110 17 17 ILE HG2 H 0.810 . . 111 17 17 ILE HD1 H 0.338 . . 112 18 18 CYS H H 8.571 . . 113 18 18 CYS HA H 5.223 . . 114 18 18 CYS HB3 H 2.843 . . 115 18 18 CYS HB2 H 2.843 . . 116 19 19 PHE H H 9.815 . . 117 19 19 PHE HA H 4.816 . . 118 19 19 PHE HB3 H 2.816 . . 119 19 19 PHE HB2 H 3.077 . . 120 19 19 PHE HD1 H 7.150 . . 121 19 19 PHE HD2 H 7.150 . . 122 19 19 PHE HE1 H 6.811 . . 123 19 19 PHE HE2 H 6.811 . . 124 19 19 PHE HZ H 6.477 . . 125 20 20 PRO HA H 4.679 . . 126 20 20 PRO HB3 H 2.167 . . 127 20 20 PRO HB2 H 2.167 . . 128 20 20 PRO HG3 H 2.067 . . 129 20 20 PRO HG2 H 2.067 . . 130 20 20 PRO HD3 H 3.706 . . 131 20 20 PRO HD2 H 3.781 . . 132 21 21 GLY H H 8.001 . . 133 21 21 GLY HA3 H 3.887 . . 134 21 21 GLY HA2 H 4.212 . . 135 22 22 ILE H H 7.837 . . 136 22 22 ILE HA H 4.424 . . 137 22 22 ILE HB H 1.931 . . 138 22 22 ILE HG12 H 1.165 . . 139 22 22 ILE HG13 H 1.313 . . 140 22 22 ILE HG2 H 0.941 . . 141 22 22 ILE HD1 H 0.849 . . 142 23 23 CYS H H 8.653 . . 143 23 23 CYS HA H 4.231 . . 144 23 23 CYS HB3 H 2.477 . . 145 23 23 CYS HB2 H 2.758 . . 146 24 24 ARG H H 7.975 . . 147 24 24 ARG HA H 4.563 . . 148 24 24 ARG HB3 H 1.814 . . 149 24 24 ARG HB2 H 1.814 . . 150 24 24 ARG HG3 H 1.597 . . 151 24 24 ARG HG2 H 1.597 . . 152 24 24 ARG HD3 H 3.183 . . 153 24 24 ARG HD2 H 3.183 . . 154 24 24 ARG HE H 7.190 . . 155 25 25 ARG HA H 4.291 . . 156 25 25 ARG HB3 H 1.743 . . 157 25 25 ARG HB2 H 1.743 . . 158 25 25 ARG HG3 H 1.567 . . 159 25 25 ARG HG2 H 1.567 . . 160 25 25 ARG HD3 H 3.091 . . 161 25 25 ARG HD2 H 3.091 . . 162 25 25 ARG HE H 7.134 . . 163 26 26 PRO HA H 4.448 . . 164 26 26 PRO HB3 H 2.096 . . 165 26 26 PRO HB2 H 2.288 . . 166 26 26 PRO HG3 H 1.079 . . 167 26 26 PRO HG2 H 2.097 . . 168 26 26 PRO HD3 H 3.510 . . 169 26 26 PRO HD2 H 3.511 . . 170 27 27 TYR H H 9.335 . . 171 27 27 TYR HA H 5.053 . . 172 27 27 TYR HB3 H 2.679 . . 173 27 27 TYR HB2 H 3.036 . . 174 27 27 TYR HD1 H 6.935 . . 175 27 27 TYR HD2 H 6.935 . . 176 27 27 TYR HE1 H 6.873 . . 177 27 27 TYR HE2 H 6.873 . . 178 28 28 TYR H H 9.094 . . 179 28 28 TYR HA H 4.893 . . 180 28 28 TYR HB3 H 2.964 . . 181 28 28 TYR HB2 H 3.077 . . 182 28 28 TYR HD1 H 6.993 . . 183 28 28 TYR HD2 H 6.993 . . 184 28 28 TYR HE1 H 6.586 . . 185 28 28 TYR HE2 H 6.586 . . 186 29 29 TRP H H 8.868 . . 187 29 29 TRP HA H 4.695 . . 188 29 29 TRP HB3 H 3.342 . . 189 29 29 TRP HB2 H 3.342 . . 190 29 29 TRP HD1 H 7.428 . . 191 29 29 TRP HE1 H 10.207 . . 192 29 29 TRP HE3 H 7.465 . . 193 29 29 TRP HZ2 H 7.356 . . 194 29 29 TRP HZ3 H 7.075 . . 195 29 29 TRP HH2 H 7.186 . . 196 30 30 ILE H H 8.622 . . 197 30 30 ILE HA H 4.561 . . 198 30 30 ILE HB H 1.945 . . 199 30 30 ILE HG12 H 0.831 . . 200 30 30 ILE HG13 H 0.831 . . 201 30 30 ILE HG2 H 0.605 . . 202 30 30 ILE HD1 H 0.511 . . 203 31 31 GLY H H 5.909 . . 204 31 31 GLY HA3 H 2.988 . . 205 31 31 GLY HA2 H 3.718 . . 206 32 32 THR H H 8.264 . . 207 32 32 THR HA H 4.955 . . 208 32 32 THR HB H 4.322 . . 209 32 32 THR HG2 H 1.550 . . 210 33 33 CYS H H 7.829 . . 211 33 33 CYS HA H 4.847 . . 212 33 33 CYS HB3 H 3.267 . . 213 33 33 CYS HB2 H 3.509 . . 214 34 34 ASN H H 9.219 . . 215 34 34 ASN HA H 4.388 . . 216 34 34 ASN HB3 H 2.592 . . 217 34 34 ASN HB2 H 3.024 . . 218 34 34 ASN HD21 H 7.499 . . 219 34 34 ASN HD22 H 6.884 . . 220 35 35 ASN H H 8.954 . . 221 35 35 ASN HA H 4.315 . . 222 35 35 ASN HB3 H 2.819 . . 223 35 35 ASN HB2 H 3.051 . . 224 35 35 ASN HD21 H 7.556 . . 225 35 35 ASN HD22 H 6.879 . . 226 36 36 GLY H H 7.799 . . 227 36 36 GLY HA3 H 3.611 . . 228 36 36 GLY HA2 H 4.370 . . 229 37 37 ILE H H 7.506 . . 230 37 37 ILE HA H 4.392 . . 231 37 37 ILE HB H 2.130 . . 232 37 37 ILE HG12 H 1.371 . . 233 37 37 ILE HG13 H 1.502 . . 234 37 37 ILE HG2 H 0.978 . . 235 37 37 ILE HD1 H 0.978 . . 236 38 38 GLY H H 8.245 . . 237 38 38 GLY HA3 H 3.690 . . 238 38 38 GLY HA2 H 4.628 . . 239 39 39 SER H H 8.964 . . 240 39 39 SER HA H 4.842 . . 241 39 39 SER HB3 H 3.963 . . 242 39 39 SER HB2 H 3.963 . . 243 39 39 SER HG H 5.758 . . 244 40 40 CYS H H 8.801 . . 245 40 40 CYS HA H 4.801 . . 246 40 40 CYS HB3 H 2.101 . . 247 40 40 CYS HB2 H 2.201 . . 248 41 41 CYS H H 9.247 . . 249 41 41 CYS HA H 5.532 . . 250 41 41 CYS HB3 H 2.697 . . 251 41 41 CYS HB2 H 3.001 . . 252 42 42 ALA H H 9.042 . . 253 42 42 ALA HA H 4.930 . . 254 42 42 ALA HB H 1.075 . . 255 43 43 ARG H H 8.710 . . 256 43 43 ARG HA H 4.161 . . 257 43 43 ARG HB3 H 1.492 . . 258 43 43 ARG HB2 H 1.492 . . 259 43 43 ARG HG3 H 1.072 . . 260 43 43 ARG HG2 H 1.279 . . 261 43 43 ARG HD3 H 2.751 . . 262 43 43 ARG HD2 H 2.816 . . 263 43 43 ARG HE H 7.071 . . 264 44 44 GLY H H 8.466 . . 265 44 44 GLY HA3 H 3.883 . . 266 44 44 GLY HA2 H 4.214 . . 267 45 45 TRP H H 8.144 . . 268 45 45 TRP HA H 4.597 . . 269 45 45 TRP HB3 H 3.228 . . 270 45 45 TRP HB2 H 3.228 . . 271 45 45 TRP HD1 H 7.222 . . 272 45 45 TRP HE1 H 10.085 . . 273 45 45 TRP HE3 H 7.568 . . 274 45 45 TRP HZ2 H 7.469 . . 275 45 45 TRP HZ3 H 7.068 . . 276 45 45 TRP HH2 H 7.201 . . 277 46 46 ARG H H 7.972 . . 278 46 46 ARG HA H 4.233 . . 279 46 46 ARG HB3 H 1.551 . . 280 46 46 ARG HB2 H 1.739 . . 281 46 46 ARG HG3 H 1.353 . . 282 46 46 ARG HG2 H 1.363 . . 283 46 46 ARG HD3 H 3.028 . . 284 46 46 ARG HD2 H 3.028 . . 285 46 46 ARG HE H 7.060 . . 286 47 47 SER H H 7.854 . . 287 47 47 SER HA H 4.162 . . 288 47 47 SER HB3 H 3.809 . . 289 47 47 SER HB2 H 3.809 . . stop_ save_