data_5966 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin binding requirements ; _BMRB_accession_number 5966 _BMRB_flat_file_name bmr5966.str _Entry_type original _Submission_date 2003-10-06 _Accession_date 2003-10-06 _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 Vermeulen Wim . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 230 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-17 update BMRB 'Updating non-standard residue' stop_ loop_ _Related_BMRB_accession_number _Relationship 5964 'human villin HP35' 5965 'human villin HP35 W64A mutant' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15096633 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vermeulen Wim . . 2 Vanhaesebrouck P. . . 3 'Van Troys' M. . . 4 Verschueren M. . . 5 Fant F. . . 6 Goethals M. . . 7 Ampe C. . . 8 Martins J.C. . . 9 Borremans F.A. . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_volume 13 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1276 _Page_last 1287 _Year 2004 _Details . loop_ _Keyword 'headpiece subdomain' villin advillin 'NMR structure' 'actin binding protein' stop_ save_ ################################## # Molecular system description # ################################## save_HP _Saveframe_category molecular_system _Mol_system_name 'headpiece subdomain' _Abbreviation_common HP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'human advillin HP36' $HAcHP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HAcHP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'human advillin C-terminal headpiece' _Abbreviation_common HAcHP _Molecular_mass . _Mol_thiol_state 'not present' _Details ; the subdomain is N-actetylated to avoid the artificial introduction of an N-terminal positive charge due to synthesis of the last 35 residues only ; ############################## # Polymer residue sequence # ############################## _Residue_count 37 _Mol_residue_sequence ; XYLSEQDFVSVFGITRGQFA ALPGWKQLQMKKEKGLF ; loop_ _Residue_seq_code _Residue_label 1 ACE 2 TYR 3 LEU 4 SER 5 GLU 6 GLN 7 ASP 8 PHE 9 VAL 10 SER 11 VAL 12 PHE 13 GLY 14 ILE 15 THR 16 ARG 17 GLY 18 GLN 19 PHE 20 ALA 21 ALA 22 LEU 23 PRO 24 GLY 25 TRP 26 LYS 27 GLN 28 LEU 29 GLN 30 MET 31 LYS 32 LYS 33 GLU 34 LYS 35 GLY 36 LEU 37 PHE 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 1UND "Solution Structure Of The Human Advillin C-Terminal Headpiece Subdomain" 97.22 37 100.00 100.00 2.99e-15 DBJ BAG36994 "unnamed protein product [Homo sapiens]" 97.22 819 100.00 100.00 1.17e-13 GB AAC25051 "advillin [Homo sapiens]" 97.22 819 100.00 100.00 1.18e-13 GB AAI11731 "AVIL protein [Homo sapiens]" 97.22 812 100.00 100.00 1.18e-13 GB AIC59667 "AVIL, partial [synthetic construct]" 97.22 812 100.00 100.00 1.18e-13 GB EAW97080 "advillin, isoform CRA_b [Homo sapiens]" 97.22 819 100.00 100.00 1.17e-13 GB EFB28896 "hypothetical protein PANDA_004141 [Ailuropoda melanoleuca]" 97.22 769 97.14 100.00 1.96e-13 REF NP_001179458 "advillin [Bos taurus]" 97.22 816 97.14 100.00 5.27e-13 REF NP_006567 "advillin [Homo sapiens]" 97.22 819 100.00 100.00 1.14e-13 REF XP_001101627 "PREDICTED: advillin-like [Macaca mulatta]" 97.22 839 100.00 100.00 1.38e-13 REF XP_001490278 "PREDICTED: advillin isoform 1 [Equus caballus]" 97.22 816 100.00 100.00 1.41e-13 REF XP_002823490 "PREDICTED: advillin [Pongo abelii]" 97.22 819 100.00 100.00 1.21e-13 SP O75366 "RecName: Full=Advillin; AltName: Full=p92 [Homo sapiens]" 97.22 819 100.00 100.00 1.14e-13 TPG DAA29655 "TPA: advillin [Bos taurus]" 97.22 816 97.14 100.00 5.27e-13 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_ACE _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'ACETYL GROUP' _BMRB_code . _PDB_code ACE _Standard_residue_derivative . _Molecular_mass 44.053 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jul 21 11:53:59 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . 0 . ? O O O . 0 . ? CH3 CH3 C . 0 . ? H H H . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 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 DOUB C O ? ? SING C CH3 ? ? SING C H ? ? SING CH3 H1 ? ? SING CH3 H2 ? ? SING CH3 H3 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HAcHP 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 $HAcHP '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 $HAcHP 2.0 mM 1.8 2.2 . stop_ save_ ############################ # Computer software used # ############################ save_Pronto _Saveframe_category software _Name Pronto _Version 19990506 loop_ _Task assignment stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label $sample_1 save_ save_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _Sample_label $sample_1 save_ save_1H-1H_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H DQF-COSY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_cond _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.2 0.05 n/a temperature 294 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'human advillin HP36' _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 ACE H2 H 1.97 0.02 1 2 . 2 TYR H H 8.28 0.02 1 3 . 2 TYR HA H 4.48 0.02 1 4 . 2 TYR HB3 H 2.93 0.02 2 5 . 2 TYR HB2 H 2.93 0.02 2 6 . 2 TYR HD2 H 7.08 0.02 3 7 . 2 TYR HE2 H 6.79 0.02 3 8 . 3 LEU H H 8.06 0.02 1 9 . 3 LEU HA H 4.41 0.02 1 10 . 3 LEU HB3 H 1.62 0.02 1 11 . 3 LEU HB2 H 1.62 0.02 1 12 . 3 LEU HG H 1.46 0.02 1 13 . 3 LEU HD1 H 0.77 0.02 1 14 . 3 LEU HD2 H 0.77 0.02 1 15 . 4 SER H H 8.99 0.02 1 16 . 4 SER HA H 4.44 0.02 1 17 . 4 SER HB3 H 4.33 0.02 2 18 . 4 SER HB2 H 4.09 0.02 2 19 . 5 GLU H H 8.94 0.02 1 20 . 5 GLU HA H 4.11 0.02 1 21 . 5 GLU HB3 H 2.45 0.02 1 22 . 5 GLU HB2 H 2.45 0.02 1 23 . 5 GLU HG3 H 2.12 0.02 1 24 . 5 GLU HG2 H 2.12 0.02 1 25 . 6 GLN H H 8.56 0.02 1 26 . 6 GLN HA H 4.13 0.02 1 27 . 6 GLN HB3 H 2.01 0.02 1 28 . 6 GLN HB2 H 2.09 0.02 1 29 . 6 GLN HG3 H 2.42 0.02 2 30 . 6 GLN HG2 H 2.45 0.02 2 31 . 6 GLN HE22 H 6.45 0.02 2 32 . 6 GLN HE21 H 7.20 0.02 2 33 . 7 ASP H H 8.04 0.02 1 34 . 7 ASP HA H 4.48 0.02 1 35 . 7 ASP HB3 H 2.68 0.02 1 36 . 7 ASP HB2 H 2.83 0.02 1 37 . 8 PHE H H 8.62 0.02 1 38 . 8 PHE HA H 3.85 0.02 1 39 . 8 PHE HB3 H 3.38 0.02 1 40 . 8 PHE HB2 H 2.94 0.02 1 41 . 8 PHE HD2 H 7.18 0.02 3 42 . 8 PHE HE2 H 6.58 0.02 3 43 . 8 PHE HZ H 5.75 0.02 1 44 . 9 VAL H H 7.98 0.02 1 45 . 9 VAL HA H 3.83 0.02 1 46 . 9 VAL HB H 2.13 0.02 1 47 . 9 VAL HG1 H 0.85 0.02 1 48 . 9 VAL HG2 H 1.04 0.02 1 49 . 10 SER H H 7.96 0.02 1 50 . 10 SER HA H 4.17 0.02 1 51 . 10 SER HB3 H 3.96 0.02 2 52 . 10 SER HB2 H 4.03 0.02 2 53 . 11 VAL H H 7.76 0.02 1 54 . 11 VAL HA H 3.60 0.02 1 55 . 11 VAL HB H 1.44 0.02 1 56 . 11 VAL HG1 H -0.13 0.02 1 57 . 11 VAL HG2 H 0.75 0.02 1 58 . 12 PHE H H 8.40 0.02 1 59 . 12 PHE HA H 4.34 0.02 1 60 . 12 PHE HB3 H 2.99 0.02 1 61 . 12 PHE HB2 H 2.59 0.02 1 62 . 12 PHE HD2 H 6.47 0.02 3 63 . 12 PHE HE2 H 6.61 0.02 3 64 . 12 PHE HZ H 6.80 0.02 1 65 . 13 GLY H H 8.59 0.02 1 66 . 13 GLY HA3 H 3.88 0.02 2 67 . 13 GLY HA2 H 4.20 0.02 2 68 . 14 ILE H H 7.33 0.02 1 69 . 14 ILE HA H 4.79 0.02 1 70 . 14 ILE HB H 2.21 0.02 1 71 . 14 ILE HG13 H 0.89 0.02 1 72 . 14 ILE HG12 H 0.89 0.02 1 73 . 14 ILE HG2 H 0.99 0.02 1 74 . 14 ILE HD1 H 1.56 0.02 1 75 . 15 THR H H 8.28 0.02 1 76 . 15 THR HA H 4.51 0.02 1 77 . 15 THR HB H 4.70 0.02 1 78 . 15 THR HG2 H 1.28 0.02 1 79 . 16 ARG H H 8.88 0.02 1 80 . 16 ARG HA H 3.09 0.02 1 81 . 16 ARG HB3 H 1.23 0.02 2 82 . 16 ARG HB2 H 1.37 0.02 2 83 . 16 ARG HG3 H 0.56 0.02 2 84 . 16 ARG HG2 H 0.93 0.02 2 85 . 16 ARG HD3 H 2.79 0.02 2 86 . 16 ARG HD2 H 2.93 0.02 2 87 . 17 GLY H H 8.67 0.02 1 88 . 17 GLY HA3 H 3.74 0.02 1 89 . 17 GLY HA2 H 3.74 0.02 1 90 . 18 GLN H H 7.76 0.02 1 91 . 18 GLN HA H 3.98 0.02 1 92 . 18 GLN HB3 H 2.40 0.02 1 93 . 18 GLN HB2 H 2.40 0.02 1 94 . 18 GLN HG3 H 1.92 0.02 1 95 . 18 GLN HG2 H 1.92 0.02 1 96 . 18 GLN HE22 H 6.92 0.02 1 97 . 18 GLN HE21 H 7.60 0.02 1 98 . 19 PHE H H 8.76 0.02 1 99 . 19 PHE HA H 3.87 0.02 1 100 . 19 PHE HB3 H 3.18 0.02 1 101 . 19 PHE HB2 H 2.94 0.02 1 102 . 19 PHE HD2 H 6.93 0.02 3 103 . 19 PHE HE2 H 7.03 0.02 3 104 . 19 PHE HZ H 7.03 0.02 1 105 . 20 ALA H H 8.12 0.02 1 106 . 20 ALA HA H 3.90 0.02 1 107 . 20 ALA HB H 1.45 0.02 1 108 . 21 ALA H H 6.97 0.02 1 109 . 21 ALA HA H 4.25 0.02 1 110 . 21 ALA HB H 1.39 0.02 1 111 . 22 LEU H H 7.29 0.02 1 112 . 22 LEU HA H 4.28 0.02 1 113 . 22 LEU HB3 H 0.76 0.02 1 114 . 22 LEU HB2 H 1.58 0.02 1 115 . 22 LEU HG H 1.89 0.02 1 116 . 22 LEU HD1 H 0.52 0.02 1 117 . 22 LEU HD2 H 0.72 0.02 1 118 . 23 PRO HA H 4.34 0.02 1 119 . 23 PRO HB3 H 2.38 0.02 1 120 . 23 PRO HB2 H 1.04 0.02 1 121 . 23 PRO HG3 H 2.07 0.02 1 122 . 23 PRO HG2 H 1.57 0.02 1 123 . 23 PRO HD3 H 3.76 0.02 2 124 . 23 PRO HD2 H 3.07 0.02 2 125 . 24 GLY H H 8.98 0.02 1 126 . 24 GLY HA3 H 3.50 0.02 2 127 . 24 GLY HA2 H 4.00 0.02 2 128 . 25 TRP H H 8.28 0.02 1 129 . 25 TRP HA H 4.39 0.02 1 130 . 25 TRP HB3 H 3.25 0.02 1 131 . 25 TRP HB2 H 3.49 0.02 1 132 . 25 TRP HD1 H 7.51 0.02 1 133 . 25 TRP HE1 H 10.55 0.02 1 134 . 25 TRP HE3 H 7.31 0.02 1 135 . 25 TRP HZ2 H 7.53 0.02 1 136 . 25 TRP HZ3 H 7.14 0.02 1 137 . 25 TRP HH2 H 7.26 0.02 1 138 . 26 LYS H H 6.18 0.02 1 139 . 26 LYS HA H 3.66 0.02 1 140 . 26 LYS HB3 H 1.21 0.02 1 141 . 26 LYS HB2 H 0.03 0.02 1 142 . 26 LYS HG3 H 0.80 0.02 1 143 . 26 LYS HG2 H 0.97 0.02 1 144 . 26 LYS HD3 H 1.39 0.02 2 145 . 26 LYS HD2 H 1.48 0.02 2 146 . 26 LYS HE3 H 2.83 0.02 1 147 . 26 LYS HE2 H 2.83 0.02 1 148 . 27 GLN H H 7.52 0.02 1 149 . 27 GLN HA H 3.42 0.02 1 150 . 27 GLN HB3 H 1.92 0.02 1 151 . 27 GLN HB2 H 1.86 0.02 1 152 . 27 GLN HG3 H 1.75 0.02 2 153 . 27 GLN HG2 H 0.83 0.02 2 154 . 27 GLN HE22 H 6.52 0.02 1 155 . 27 GLN HE21 H 7.28 0.02 1 156 . 28 LEU H H 7.77 0.02 1 157 . 28 LEU HA H 4.09 0.02 1 158 . 28 LEU HB3 H 1.79 0.02 1 159 . 28 LEU HB2 H 1.71 0.02 1 160 . 28 LEU HG H 1.75 0.02 1 161 . 28 LEU HD1 H 0.95 0.02 1 162 . 28 LEU HD2 H 0.95 0.02 1 163 . 29 GLN H H 7.74 0.02 1 164 . 29 GLN HA H 4.08 0.02 1 165 . 29 GLN HB3 H 2.40 0.02 1 166 . 29 GLN HB2 H 2.30 0.02 1 167 . 29 GLN HG3 H 2.69 0.02 1 168 . 29 GLN HG2 H 2.69 0.02 1 169 . 29 GLN HE22 H 7.04 0.02 1 170 . 29 GLN HE21 H 7.76 0.02 1 171 . 30 MET H H 8.40 0.02 1 172 . 30 MET HA H 4.22 0.02 1 173 . 30 MET HB3 H 2.32 0.02 1 174 . 30 MET HB2 H 2.32 0.02 1 175 . 30 MET HG3 H 2.64 0.02 2 176 . 30 MET HG2 H 2.81 0.02 2 177 . 30 MET HE H 2.20 0.02 1 178 . 31 LYS H H 8.24 0.02 1 179 . 31 LYS HA H 4.03 0.02 1 180 . 31 LYS HB3 H 1.93 0.02 1 181 . 31 LYS HB2 H 2.08 0.02 1 182 . 31 LYS HG3 H 1.37 0.02 2 183 . 31 LYS HG2 H 2.04 0.02 2 184 . 31 LYS HD3 H 1.77 0.02 1 185 . 31 LYS HD2 H 1.77 0.02 1 186 . 31 LYS HE3 H 2.89 0.02 1 187 . 31 LYS HE2 H 2.89 0.02 1 188 . 32 LYS H H 8.32 0.02 1 189 . 32 LYS HA H 4.12 0.02 1 190 . 32 LYS HB3 H 1.99 0.02 1 191 . 32 LYS HB2 H 1.99 0.02 1 192 . 32 LYS HG3 H 1.44 0.02 2 193 . 32 LYS HG2 H 1.58 0.02 2 194 . 32 LYS HD3 H 1.69 0.02 1 195 . 32 LYS HD2 H 1.69 0.02 1 196 . 32 LYS HE3 H 2.92 0.02 1 197 . 32 LYS HE2 H 2.92 0.02 1 198 . 33 GLU H H 8.31 0.02 1 199 . 33 GLU HA H 4.12 0.02 1 200 . 33 GLU HB3 H 2.31 0.02 1 201 . 33 GLU HB2 H 2.20 0.02 1 202 . 33 GLU HG3 H 2.48 0.02 2 203 . 33 GLU HG2 H 2.62 0.02 2 204 . 34 LYS H H 7.58 0.02 1 205 . 34 LYS HA H 4.38 0.02 1 206 . 34 LYS HB3 H 1.74 0.02 1 207 . 34 LYS HB2 H 1.65 0.02 1 208 . 34 LYS HG3 H 1.08 0.02 1 209 . 34 LYS HG2 H 1.08 0.02 1 210 . 34 LYS HD3 H 1.38 0.02 2 211 . 34 LYS HD2 H 1.51 0.02 2 212 . 34 LYS HE3 H 2.88 0.02 1 213 . 34 LYS HE2 H 2.88 0.02 1 214 . 35 GLY H H 7.89 0.02 1 215 . 35 GLY HA3 H 3.85 0.02 2 216 . 35 GLY HA2 H 3.96 0.02 2 217 . 36 LEU H H 7.91 0.02 1 218 . 36 LEU HA H 4.43 0.02 1 219 . 36 LEU HB3 H 1.46 0.02 1 220 . 36 LEU HB2 H 1.46 0.02 1 221 . 36 LEU HG H 1.62 0.02 1 222 . 36 LEU HD1 H 0.77 0.02 1 223 . 36 LEU HD2 H 0.77 0.02 1 224 . 37 PHE H H 7.69 0.02 1 225 . 37 PHE HA H 4.41 0.02 1 226 . 37 PHE HB3 H 2.92 0.02 2 227 . 37 PHE HB2 H 3.10 0.02 2 228 . 37 PHE HD2 H 7.22 0.02 3 229 . 37 PHE HE2 H 7.33 0.02 3 230 . 37 PHE HZ H 7.26 0.02 1 stop_ save_