data_5667 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the first zinc-finger domain from ZNF265 ; _BMRB_accession_number 5667 _BMRB_flat_file_name bmr5667.str _Entry_type original _Submission_date 2003-01-23 _Accession_date 2003-01-23 _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 Plambeck C. A. . 2 Kwan A. H.Y. . 3 Adams D. . . 4 Westman B. J. . 5 'van der Weyden' L . . 6 Medcalf R . . 7 Morris B. . . 8 Mackay J. P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 223 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-08-07 original author . stop_ _Original_release_date 2003-08-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The Structure of the Zinc Finger Domain from Human Splicing Factor ZNF265 Fold' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22692433 _PubMed_ID 12657633 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Plambeck C. A. . 2 Kwan A. H.Y. . 3 Adams D. J. . 4 Westman B. J. . 5 'van der Weyden' L. . . 6 Medcalf R. L. . 7 Morris B. J. . 8 Mackay J. P. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 278 _Journal_issue 25 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 22805 _Page_last 22811 _Year 2003 _Details . loop_ _Keyword 'RNA splicing' 'zinc finger' stop_ save_ ################################## # Molecular system description # ################################## save_system_znf265-F1 _Saveframe_category molecular_system _Mol_system_name 'First zinc finger of Zinc finger protein 265' _Abbreviation_common znf265-F1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'znf265-F1 monomer' $znf265-F1 'ZINC ION (II)' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all other bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_znf265-F1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'First zinc finger of Zinc finger protein 265' _Abbreviation_common znf265-F1 _Molecular_mass 4995.7 _Mol_thiol_state 'all other bound' _Details 'This mass refers to the apo-protein.' ############################## # Polymer residue sequence # ############################## _Residue_count 45 _Mol_residue_sequence ; GSMSTKNFRVSDGDWICPDK KCGNVNFARRTSCDRCGREK TTGPI ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 GLY 2 -1 SER 3 1 MET 4 2 SER 5 3 THR 6 4 LYS 7 5 ASN 8 6 PHE 9 7 ARG 10 8 VAL 11 9 SER 12 10 ASP 13 11 GLY 14 12 ASP 15 13 TRP 16 14 ILE 17 15 CYS 18 16 PRO 19 17 ASP 20 18 LYS 21 19 LYS 22 20 CYS 23 21 GLY 24 22 ASN 25 23 VAL 26 24 ASN 27 25 PHE 28 26 ALA 29 27 ARG 30 28 ARG 31 29 THR 32 30 SER 33 31 CYS 34 32 ASP 35 33 ARG 36 34 CYS 37 35 GLY 38 36 ARG 39 37 GLU 40 38 LYS 41 39 THR 42 40 THR 43 41 GLY 44 42 PRO 45 43 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 1N0Z 'Solution Structure Of The First Zinc-Finger Domain From Znf265' 100.00 45 100.00 100.00 4.97e-18 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jun 2 09:48:05 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $znf265-F1 Mouse 10090 Eukaryota Metazoa Mus musculus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $znf265-F1 'recombinant technology' 'E. coli' Escherichia coli DH5a plasmid 'pGEX 4t-3' 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 $znf265-F1 1 mM 0.7 1.3 . TCEP 2 mM . . . ZnZO4 1.7 mM . . . H2O 95 % . . . D2O 5 % . . . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 2.5 loop_ _Task processing stop_ _Details Bruker save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.13 loop_ _Task 'data analysis' stop_ _Details 'Bartels et al' save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task refinement stop_ _Details 'Guntert et al' save_ save_ARIA _Saveframe_category software _Name ARIA _Version 1.2 loop_ _Task 'structure solution' stop_ _Details 'Linge et al' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_1 save_ save_2D_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label $sample_1 save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $sample_1 save_ save_NOESY_Short_mixing_time_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'NOESY Short mixing time' _Sample_label $sample_1 save_ save_TOCSY_Short_mixing_time_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'TOCSY Short mixing time' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'NOESY Short mixing time' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'TOCSY Short mixing time' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.8 0.1 pH pressure 1 . atm temperature 298 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 _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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'znf265-F1 monomer' _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 . 3 MET H H 8.610 0.02 . 2 . 3 MET HA H 4.575 0.02 . 3 . 3 MET HB2 H 2.056 0.02 . 4 . 3 MET HB3 H 2.143 0.02 . 5 . 3 MET HG2 H 2.587 0.02 . 6 . 3 MET HG3 H 2.641 0.02 . 7 . 4 SER H H 8.402 0.02 . 8 . 4 SER HA H 4.523 0.02 . 9 . 4 SER HB2 H 3.885 0.02 . 10 . 4 SER HB3 H 3.921 0.02 . 11 . 5 THR H H 8.209 0.02 . 12 . 5 THR HA H 4.339 0.02 . 13 . 5 THR HB H 4.252 0.02 . 14 . 5 THR HG2 H 1.198 0.02 . 15 . 6 LYS H H 8.260 0.02 . 16 . 6 LYS HA H 4.264 0.02 . 17 . 6 LYS HB2 H 1.708 0.02 . 18 . 6 LYS HB3 H 1.653 0.02 . 19 . 6 LYS HG2 H 1.388 0.02 . 20 . 6 LYS HG3 H 1.337 0.02 . 21 . 6 LYS HE3 H 2.968 0.02 . 22 . 7 ASN H H 8.343 0.02 . 23 . 7 ASN HA H 4.691 0.02 . 24 . 7 ASN HB2 H 2.784 0.02 . 25 . 7 ASN HB3 H 2.687 0.02 . 26 . 7 ASN HD21 H 7.563 0.02 . 27 . 7 ASN HD22 H 6.898 0.02 . 28 . 8 PHE H H 8.087 0.02 . 29 . 8 PHE HA H 4.591 0.02 . 30 . 8 PHE HB2 H 3.026 0.02 . 31 . 8 PHE HB3 H 3.090 0.02 . 32 . 8 PHE HZ H 7.296 0.02 . 33 . 8 PHE HD1 H 7.201 0.02 . 34 . 8 PHE HE1 H 7.201 0.02 . 35 . 9 ARG H H 8.434 0.02 . 36 . 9 ARG HA H 4.379 0.02 . 37 . 9 ARG HB2 H 1.782 0.02 . 38 . 9 ARG HB3 H 1.708 0.02 . 39 . 9 ARG HG2 H 1.753 0.02 . 40 . 9 ARG HG3 H 1.539 0.02 . 41 . 9 ARG HD2 H 3.170 0.02 . 42 . 9 ARG HE H 7.266 0.02 . 43 . 10 VAL H H 8.292 0.02 . 44 . 10 VAL HA H 4.134 0.02 . 45 . 10 VAL HB H 2.107 0.02 . 46 . 10 VAL HG2 H 0.980 0.02 . 47 . 11 SER H H 8.581 0.02 . 48 . 11 SER HA H 4.514 0.02 . 49 . 11 SER HB2 H 3.881 0.02 . 50 . 12 ASP H H 8.266 0.02 . 51 . 12 ASP HA H 4.614 0.02 . 52 . 12 ASP HB2 H 2.685 0.02 . 53 . 12 ASP HB3 H 2.763 0.02 . 54 . 13 GLY H H 8.391 0.02 . 55 . 13 GLY HA2 H 3.982 0.02 . 56 . 13 GLY HA3 H 4.146 0.02 . 57 . 14 ASP H H 7.979 0.02 . 58 . 14 ASP HA H 4.846 0.02 . 59 . 14 ASP HB2 H 2.533 0.02 . 60 . 14 ASP HB3 H 2.579 0.02 . 61 . 15 TRP H H 8.808 0.02 . 62 . 15 TRP HA H 5.173 0.02 . 63 . 15 TRP HB2 H 3.102 0.02 . 64 . 15 TRP HB3 H 3.317 0.02 . 65 . 15 TRP HD1 H 7.191 0.02 . 66 . 15 TRP HE3 H 7.435 0.02 . 67 . 15 TRP HE1 H 9.667 0.02 . 68 . 15 TRP HZ3 H 7.074 0.02 . 69 . 15 TRP HZ2 H 6.735 0.02 . 70 . 15 TRP HH2 H 6.913 0.02 . 71 . 16 ILE H H 8.782 0.02 . 72 . 16 ILE HA H 4.252 0.02 . 73 . 16 ILE HB H 1.635 0.02 . 74 . 16 ILE HG2 H 0.612 0.02 . 75 . 16 ILE HG12 H 0.975 0.02 . 76 . 16 ILE HG13 H 1.520 0.02 . 77 . 16 ILE HD1 H 0.801 0.02 . 78 . 17 CYS H H 8.781 0.02 . 79 . 17 CYS HA H 4.594 0.02 . 80 . 17 CYS HB2 H 3.007 0.02 . 81 . 17 CYS HB3 H 2.846 0.02 . 82 . 18 PRO HA H 4.498 0.02 . 83 . 18 PRO HB2 H 2.365 0.02 . 84 . 18 PRO HB3 H 1.913 0.02 . 85 . 18 PRO HG2 H 2.232 0.02 . 86 . 18 PRO HG3 H 2.086 0.02 . 87 . 18 PRO HD2 H 4.265 0.02 . 88 . 18 PRO HD3 H 4.148 0.02 . 89 . 19 ASP H H 8.366 0.02 . 90 . 19 ASP HA H 4.680 0.02 . 91 . 19 ASP HB2 H 2.490 0.02 . 92 . 19 ASP HB3 H 3.348 0.02 . 93 . 20 LYS H H 8.939 0.02 . 94 . 20 LYS HA H 4.078 0.02 . 95 . 20 LYS HB2 H 1.888 0.02 . 96 . 20 LYS HG2 H 1.571 0.02 . 97 . 20 LYS HD2 H 1.750 0.02 . 98 . 21 LYS H H 8.418 0.02 . 99 . 21 LYS HA H 4.157 0.02 . 100 . 21 LYS HB2 H 1.862 0.02 . 101 . 21 LYS HG2 H 1.447 0.02 . 102 . 21 LYS HD2 H 1.709 0.02 . 103 . 21 LYS HE2 H 3.014 0.02 . 104 . 22 CYS H H 7.936 0.02 . 105 . 22 CYS HA H 4.405 0.02 . 106 . 22 CYS HB2 H 2.616 0.02 . 107 . 22 CYS HB3 H 3.392 0.02 . 108 . 23 GLY H H 7.756 0.02 . 109 . 23 GLY HA2 H 3.890 0.02 . 110 . 24 ASN H H 8.315 0.02 . 111 . 24 ASN HA H 4.246 0.02 . 112 . 24 ASN HB2 H 2.742 0.02 . 113 . 24 ASN HB3 H 2.491 0.02 . 114 . 24 ASN HD21 H 7.267 0.02 . 115 . 24 ASN HD22 H 6.685 0.02 . 116 . 25 VAL H H 7.763 0.02 . 117 . 25 VAL HA H 3.857 0.02 . 118 . 25 VAL HB H 1.753 0.02 . 119 . 25 VAL HG1 H 0.824 0.02 . 120 . 25 VAL HG2 H 0.611 0.02 . 121 . 26 ASN H H 8.779 0.02 . 122 . 26 ASN HA H 4.518 0.02 . 123 . 26 ASN HB2 H 1.538 0.02 . 124 . 26 ASN HB3 H 0.253 0.02 . 125 . 26 ASN HD21 H 4.282 0.02 . 126 . 26 ASN HD22 H 6.800 0.02 . 127 . 27 PHE H H 8.064 0.02 . 128 . 27 PHE HA H 4.752 0.02 . 129 . 27 PHE HB2 H 3.410 0.02 . 130 . 27 PHE HB3 H 2.920 0.02 . 131 . 27 PHE HZ H 7.439 0.02 . 132 . 27 PHE HD1 H 7.393 0.02 . 133 . 27 PHE HE1 H 7.393 0.02 . 134 . 28 ALA H H 8.794 0.02 . 135 . 28 ALA HA H 4.242 0.02 . 136 . 28 ALA HB H 1.441 0.02 . 137 . 29 ARG H H 7.525 0.02 . 138 . 29 ARG HA H 4.261 0.02 . 139 . 29 ARG HB2 H 1.957 0.02 . 140 . 29 ARG HG2 H 1.635 0.02 . 141 . 29 ARG HD2 H 3.218 0.02 . 142 . 30 ARG H H 8.389 0.02 . 143 . 30 ARG HA H 4.693 0.02 . 144 . 30 ARG HB2 H 2.359 0.02 . 145 . 30 ARG HB3 H 2.417 0.02 . 146 . 30 ARG HG2 H 2.110 0.02 . 147 . 30 ARG HG3 H 1.924 0.02 . 148 . 30 ARG HD2 H 3.476 0.02 . 149 . 30 ARG HE H 7.931 0.02 . 150 . 31 THR H H 8.891 0.02 . 151 . 31 THR HA H 4.260 0.02 . 152 . 31 THR HB H 4.570 0.02 . 153 . 31 THR HG2 H 1.224 0.02 . 154 . 32 SER H H 7.862 0.02 . 155 . 32 SER HA H 5.232 0.02 . 156 . 32 SER HB2 H 3.624 0.02 . 157 . 32 SER HB3 H 3.805 0.02 . 158 . 33 CYS H H 9.281 0.02 . 159 . 33 CYS HA H 4.082 0.02 . 160 . 33 CYS HB2 H 3.423 0.02 . 161 . 33 CYS HB3 H 3.115 0.02 . 162 . 34 ASP H H 8.555 0.02 . 163 . 34 ASP HA H 4.402 0.02 . 164 . 34 ASP HB2 H 2.606 0.02 . 165 . 35 ARG H H 8.955 0.02 . 166 . 35 ARG HA H 4.403 0.02 . 167 . 35 ARG HB2 H 1.765 0.02 . 168 . 35 ARG HG2 H 1.570 0.02 . 169 . 35 ARG HG3 H 1.518 0.02 . 170 . 35 ARG HD2 H 3.263 0.02 . 171 . 35 ARG HD3 H 3.344 0.02 . 172 . 36 CYS H H 8.170 0.02 . 173 . 36 CYS HA H 5.027 0.02 . 174 . 36 CYS HB2 H 2.864 0.02 . 175 . 36 CYS HB3 H 3.267 0.02 . 176 . 37 GLY H H 7.953 0.02 . 177 . 37 GLY HA2 H 3.927 0.02 . 178 . 37 GLY HA3 H 4.309 0.02 . 179 . 38 ARG H H 8.883 0.02 . 180 . 38 ARG HA H 4.247 0.02 . 181 . 38 ARG HB2 H 1.888 0.02 . 182 . 38 ARG HB3 H 2.112 0.02 . 183 . 38 ARG HG2 H 1.769 0.02 . 184 . 38 ARG HD2 H 3.303 0.02 . 185 . 38 ARG HD3 H 3.350 0.02 . 186 . 38 ARG HE H 7.641 0.02 . 187 . 39 GLU H H 8.908 0.02 . 188 . 39 GLU HA H 4.360 0.02 . 189 . 39 GLU HB2 H 2.077 0.02 . 190 . 39 GLU HB3 H 1.985 0.02 . 191 . 39 GLU HG2 H 2.408 0.02 . 192 . 39 GLU HG3 H 2.388 0.02 . 193 . 40 LYS H H 7.903 0.02 . 194 . 40 LYS HA H 3.398 0.02 . 195 . 40 LYS HB2 H 0.957 0.02 . 196 . 40 LYS HB3 H 0.485 0.02 . 197 . 40 LYS HG2 H 0.664 0.02 . 198 . 40 LYS HG3 H -0.133 0.02 . 199 . 40 LYS HD2 H 0.748 0.02 . 200 . 40 LYS HD3 H 0.465 0.02 . 201 . 40 LYS HE2 H 2.183 0.02 . 202 . 41 THR H H 7.772 0.02 . 203 . 41 THR HA H 4.362 0.02 . 204 . 41 THR HB H 4.215 0.02 . 205 . 41 THR HG2 H 1.175 0.02 . 206 . 42 THR H H 8.133 0.02 . 207 . 42 THR HA H 4.352 0.02 . 208 . 42 THR HB H 4.220 0.02 . 209 . 42 THR HG2 H 1.183 0.02 . 210 . 43 GLY H H 8.209 0.02 . 211 . 43 GLY HA2 H 4.185 0.02 . 212 . 43 GLY HA3 H 4.062 0.02 . 213 . 44 PRO HA H 4.463 0.02 . 214 . 44 PRO HB2 H 2.263 0.02 . 215 . 44 PRO HB3 H 1.992 0.02 . 216 . 44 PRO HG2 H 2.030 0.02 . 217 . 44 PRO HD2 H 3.632 0.02 . 218 . 45 ILE H H 7.767 0.02 . 219 . 45 ILE HA H 4.090 0.02 . 220 . 45 ILE HB H 1.831 0.02 . 221 . 45 ILE HG13 H 1.431 0.02 . 222 . 45 ILE HG12 H 1.148 0.02 . 223 . 45 ILE HD1 H 0.877 0.02 . stop_ save_