data_16436 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of intermediate IIa of Leech-derived tryptase inhibitor, LDTI ; _BMRB_accession_number 16436 _BMRB_flat_file_name bmr16436.str _Entry_type original _Submission_date 2009-08-03 _Accession_date 2009-08-03 _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 Pantoja-Uceda David . . 2 Santoro Jorge . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 222 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-01-20 update BMRB 'complete entry citation' 2009-11-18 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 16435 'LDTI, apo- form' 16437 'LDTI - IIb' 16438 'LDTI - IIc' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Deciphering the structural basis that guides the oxidative folding of leech-derived tryptase inhibitor.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19820233 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pantoja-Uceda David . . 2 Arolas Joan L. . 3 Aviles Francesc X. . 4 Santoro Jorge . . 5 Ventura Salvador . . 6 Sommerhoff Christian P. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 284 _Journal_issue 51 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 35612 _Page_last 35620 _Year 2009 _Details . loop_ _Keyword NMR 'protein folding' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name LDTI_-_IIa _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label LDTI_-_IIa $LDTI_-_IIa stop_ _System_molecular_weight . _System_physical_state intermediate _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'tryptase inhibitor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_LDTI_-_IIa _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common LDTI_-_IIa _Molecular_mass . _Mol_thiol_state 'free and disulfide bound' loop_ _Biological_function 'tryptase inhibitor' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 44 _Mol_residue_sequence ; KKVCACPKILKPVCGSDGRT YANSCIARCNGVSIKSEGSC PTGI ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 LYS 3 VAL 4 CYS 5 ALA 6 CYS 7 PRO 8 LYS 9 ILE 10 LEU 11 LYS 12 PRO 13 VAL 14 CYS 15 GLY 16 SER 17 ASP 18 GLY 19 ARG 20 THR 21 TYR 22 ALA 23 ASN 24 SER 25 CYS 26 ILE 27 ALA 28 ARG 29 CYS 30 ASN 31 GLY 32 VAL 33 SER 34 ILE 35 LYS 36 SER 37 GLU 38 GLY 39 SER 40 CYS 41 PRO 42 THR 43 GLY 44 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 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 16435 LDTI 100.00 44 100.00 100.00 3.83e-21 BMRB 16437 LDTI_-_IIb 100.00 44 100.00 100.00 3.83e-21 BMRB 16438 LDTI_-_IIc 100.00 44 100.00 100.00 3.83e-21 PDB 1AN1 "Leech-Derived Tryptase InhibitorTRYPSIN COMPLEX" 100.00 46 100.00 100.00 3.10e-21 PDB 1LDT "Complex Of Leech-Derived Tryptase Inhibitor With Porcine Trypsin" 100.00 46 100.00 100.00 3.10e-21 PDB 2KMO "Solution Structure Of Native Leech-Derived Tryptase Inhibitor, Ldti" 100.00 44 100.00 100.00 3.83e-21 PDB 2KMP "Solution Structure Of Intermeidate Iia Of Leeck-Derived Tryptase Inhibitor, Ldti." 100.00 44 100.00 100.00 3.83e-21 PDB 2KMQ "Solution Structure Of Intermediate Iib Of Leech-Derived Tryptase Inhibitor, Ldti." 100.00 44 100.00 100.00 3.83e-21 PDB 2KMR "Solution Structure Of Intermediate Iic Of Leech-Derived Tryptase Inhibitor, Ldti" 100.00 44 100.00 100.00 3.83e-21 GB AAB33769 "master cell tryptase inhibitor, LDTI [Hirudo medicinalis=medical leeches, Peptide, 46 aa]" 100.00 46 100.00 100.00 3.10e-21 SP P80424 "RecName: Full=Leech-derived tryptase inhibitor C; Short=LDTI-C; Contains: RecName: Full=Leech-derived tryptase inhibitor B; Sho" 100.00 46 100.00 100.00 3.10e-21 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $LDTI_-_IIa 'medicinal leech' 6421 Eukaryota Metazoa Hirudo medicinalis 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 $LDTI_-_IIa 'recombinant technology' . Escherichia coli . pVT102U/a 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 $LDTI_-_IIa 1.7 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $LDTI_-_IIa 1.7 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 1.3 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version 5.0.20 loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'data analysis' 'peak picking' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_AMBER _Saveframe_category software _Name AMBER _Version 9.0 loop_ _Vendor _Address _Electronic_address 'Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm' . . 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 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _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_COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H COSY' _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_2D_1H-1H_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 1.7 . pH pressure 1.0 . 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 4.7 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $NMRView stop_ loop_ _Experiment_label '2D 1H-1H TOCSY' '2D 1H-1H COSY' '2D 1H-1H NOESY' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name LDTI_-_IIa _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 LYS HA H 3.940 0.02 1 2 2 2 LYS H H 8.629 0.02 1 3 2 2 LYS HA H 4.345 0.02 1 4 2 2 LYS HB2 H 1.662 0.02 2 5 2 2 LYS HB3 H 1.743 0.02 2 6 2 2 LYS HG2 H 1.327 0.02 2 7 2 2 LYS HG3 H 1.361 0.02 2 8 3 3 VAL H H 8.359 0.02 1 9 3 3 VAL HA H 4.051 0.02 1 10 3 3 VAL HB H 1.969 0.02 1 11 3 3 VAL HG1 H 0.858 0.02 2 12 3 3 VAL HG2 H 0.880 0.02 2 13 4 4 CYS H H 8.384 0.02 1 14 4 4 CYS HA H 4.416 0.02 1 15 4 4 CYS HB2 H 2.833 0.02 2 16 4 4 CYS HB3 H 2.833 0.02 2 17 5 5 ALA H H 8.373 0.02 1 18 5 5 ALA HA H 4.400 0.02 1 19 5 5 ALA HB H 1.276 0.02 1 20 6 6 CYS H H 8.110 0.02 1 21 6 6 CYS HA H 5.098 0.02 1 22 6 6 CYS HB2 H 2.999 0.02 2 23 6 6 CYS HB3 H 2.628 0.02 2 24 7 7 PRO HA H 4.427 0.02 1 25 7 7 PRO HB2 H 1.732 0.02 2 26 7 7 PRO HB3 H 2.326 0.02 2 27 7 7 PRO HD2 H 3.480 0.02 2 28 7 7 PRO HD3 H 3.907 0.02 2 29 7 7 PRO HG2 H 1.959 0.02 2 30 7 7 PRO HG3 H 2.021 0.02 2 31 8 8 LYS H H 8.660 0.02 1 32 8 8 LYS HA H 4.229 0.02 1 33 8 8 LYS HB2 H 1.832 0.02 2 34 8 8 LYS HB3 H 1.597 0.02 2 35 8 8 LYS HD2 H 1.603 0.02 2 36 8 8 LYS HD3 H 1.603 0.02 2 37 8 8 LYS HE2 H 2.889 0.02 2 38 8 8 LYS HE3 H 2.889 0.02 2 39 8 8 LYS HG2 H 1.316 0.02 2 40 8 8 LYS HG3 H 1.408 0.02 2 41 9 9 ILE H H 6.860 0.02 1 42 9 9 ILE HA H 4.076 0.02 1 43 9 9 ILE HB H 1.603 0.02 1 44 9 9 ILE HD1 H 0.813 0.02 1 45 9 9 ILE HG12 H 1.351 0.02 2 46 9 9 ILE HG13 H 0.993 0.02 2 47 9 9 ILE HG2 H 0.803 0.02 1 48 10 10 LEU H H 8.603 0.02 1 49 10 10 LEU HA H 4.618 0.02 1 50 10 10 LEU HB2 H 1.747 0.02 2 51 10 10 LEU HB3 H 1.747 0.02 2 52 10 10 LEU HD1 H 0.941 0.02 2 53 10 10 LEU HD2 H 0.855 0.02 2 54 10 10 LEU HG H 1.417 0.02 1 55 11 11 LYS H H 8.814 0.02 1 56 11 11 LYS HA H 4.533 0.02 1 57 11 11 LYS HB2 H 1.559 0.02 2 58 11 11 LYS HB3 H 1.778 0.02 2 59 11 11 LYS HE2 H 2.929 0.02 2 60 11 11 LYS HE3 H 2.929 0.02 2 61 11 11 LYS HG2 H 1.351 0.02 2 62 11 11 LYS HG3 H 1.660 0.02 2 63 12 12 PRO HA H 4.570 0.02 1 64 12 12 PRO HB2 H 1.857 0.02 2 65 12 12 PRO HB3 H 1.820 0.02 2 66 12 12 PRO HD2 H 3.601 0.02 2 67 12 12 PRO HD3 H 3.328 0.02 2 68 12 12 PRO HG2 H 1.461 0.02 2 69 12 12 PRO HG3 H 2.007 0.02 2 70 13 13 VAL H H 8.283 0.02 1 71 13 13 VAL HA H 4.672 0.02 1 72 13 13 VAL HB H 2.118 0.02 1 73 13 13 VAL HG1 H 0.926 0.02 2 74 13 13 VAL HG2 H 0.533 0.02 2 75 14 14 CYS H H 8.695 0.02 1 76 14 14 CYS HA H 5.205 0.02 1 77 14 14 CYS HB2 H 2.555 0.02 2 78 14 14 CYS HB3 H 3.087 0.02 2 79 15 15 GLY H H 9.670 0.02 1 80 15 15 GLY HA2 H 4.754 0.02 2 81 15 15 GLY HA3 H 4.109 0.02 2 82 16 16 SER H H 9.001 0.02 1 83 16 16 SER HA H 3.982 0.02 1 84 16 16 SER HB2 H 3.756 0.02 2 85 16 16 SER HB3 H 3.756 0.02 2 86 17 17 ASP H H 8.114 0.02 1 87 17 17 ASP HA H 4.524 0.02 1 88 17 17 ASP HB2 H 3.089 0.02 2 89 17 17 ASP HB3 H 2.740 0.02 2 90 18 18 GLY H H 8.360 0.02 1 91 18 18 GLY HA2 H 3.698 0.02 2 92 18 18 GLY HA3 H 4.025 0.02 2 93 19 19 ARG H H 7.439 0.02 1 94 19 19 ARG HA H 4.398 0.02 1 95 19 19 ARG HB2 H 1.635 0.02 2 96 19 19 ARG HB3 H 1.300 0.02 2 97 19 19 ARG HD2 H 2.960 0.02 2 98 19 19 ARG HD3 H 2.991 0.02 2 99 19 19 ARG HG2 H 1.186 0.02 2 100 19 19 ARG HG3 H 1.186 0.02 2 101 20 20 THR H H 8.292 0.02 1 102 20 20 THR HA H 4.950 0.02 1 103 20 20 THR HB H 3.822 0.02 1 104 20 20 THR HG2 H 1.078 0.02 1 105 21 21 TYR H H 9.153 0.02 1 106 21 21 TYR HA H 4.548 0.02 1 107 21 21 TYR HB2 H 2.405 0.02 2 108 21 21 TYR HB3 H 2.813 0.02 2 109 21 21 TYR HD1 H 7.043 0.02 1 110 21 21 TYR HD2 H 7.043 0.02 1 111 21 21 TYR HE1 H 6.893 0.02 1 112 21 21 TYR HE2 H 6.893 0.02 1 113 22 22 ALA H H 8.884 0.02 1 114 22 22 ALA HA H 3.858 0.02 1 115 22 22 ALA HB H 1.382 0.02 1 116 23 23 ASN H H 7.112 0.02 1 117 23 23 ASN HA H 4.904 0.02 1 118 23 23 ASN HB2 H 2.988 0.02 2 119 23 23 ASN HB3 H 3.359 0.02 2 120 23 23 ASN HD21 H 6.861 0.02 2 121 23 23 ASN HD22 H 6.449 0.02 2 122 24 24 SER H H 9.338 0.02 1 123 24 24 SER HA H 3.904 0.02 1 124 25 25 CYS H H 8.018 0.02 1 125 25 25 CYS HA H 4.224 0.02 1 126 25 25 CYS HB2 H 3.038 0.02 2 127 25 25 CYS HB3 H 3.366 0.02 2 128 26 26 ILE H H 8.121 0.02 1 129 26 26 ILE HA H 3.555 0.02 1 130 26 26 ILE HB H 1.787 0.02 1 131 26 26 ILE HG12 H 1.123 0.02 2 132 26 26 ILE HG13 H 1.123 0.02 2 133 26 26 ILE HG2 H 0.906 0.02 1 134 27 27 ALA H H 7.235 0.02 1 135 27 27 ALA HA H 2.789 0.02 1 136 27 27 ALA HB H 0.871 0.02 1 137 28 28 ARG H H 7.934 0.02 1 138 28 28 ARG HA H 3.992 0.02 1 139 28 28 ARG HB2 H 1.939 0.02 2 140 28 28 ARG HB3 H 1.939 0.02 2 141 28 28 ARG HD2 H 3.151 0.02 2 142 28 28 ARG HD3 H 3.151 0.02 2 143 28 28 ARG HE H 7.120 0.02 1 144 28 28 ARG HG2 H 1.727 0.02 2 145 28 28 ARG HG3 H 1.606 0.02 2 146 29 29 CYS H H 8.485 0.02 1 147 29 29 CYS HA H 4.181 0.02 1 148 29 29 CYS HB2 H 3.013 0.02 2 149 29 29 CYS HB3 H 2.949 0.02 2 150 30 30 ASN H H 7.464 0.02 1 151 30 30 ASN HA H 4.667 0.02 1 152 30 30 ASN HB2 H 2.443 0.02 2 153 30 30 ASN HB3 H 2.815 0.02 2 154 30 30 ASN HD21 H 7.285 0.02 2 155 30 30 ASN HD22 H 7.424 0.02 2 156 31 31 GLY H H 7.884 0.02 1 157 31 31 GLY HA2 H 3.738 0.02 2 158 31 31 GLY HA3 H 3.929 0.02 2 159 32 32 VAL H H 7.270 0.02 1 160 32 32 VAL HA H 4.228 0.02 1 161 32 32 VAL HB H 1.876 0.02 1 162 32 32 VAL HG1 H 0.878 0.02 2 163 32 32 VAL HG2 H 0.612 0.02 2 164 33 33 SER H H 8.048 0.02 1 165 33 33 SER HA H 4.410 0.02 1 166 33 33 SER HB2 H 3.800 0.02 2 167 33 33 SER HB3 H 3.780 0.02 2 168 34 34 ILE H H 8.571 0.02 1 169 34 34 ILE HA H 3.879 0.02 1 170 34 34 ILE HB H 1.764 0.02 1 171 34 34 ILE HD1 H 0.658 0.02 1 172 34 34 ILE HG12 H 1.382 0.02 2 173 34 34 ILE HG13 H 0.940 0.02 2 174 34 34 ILE HG2 H 0.775 0.02 1 175 35 35 LYS H H 9.176 0.02 1 176 35 35 LYS HA H 4.251 0.02 1 177 35 35 LYS HB2 H 1.387 0.02 2 178 35 35 LYS HB3 H 1.595 0.02 2 179 35 35 LYS HD2 H 1.253 0.02 2 180 35 35 LYS HD3 H 1.297 0.02 2 181 36 36 SER H H 7.744 0.02 1 182 36 36 SER HA H 4.508 0.02 1 183 36 36 SER HB2 H 3.833 0.02 2 184 36 36 SER HB3 H 3.781 0.02 2 185 37 37 GLU H H 8.612 0.02 1 186 37 37 GLU HA H 4.314 0.02 1 187 37 37 GLU HB2 H 2.165 0.02 2 188 37 37 GLU HB3 H 1.925 0.02 2 189 37 37 GLU HG2 H 2.513 0.02 2 190 37 37 GLU HG3 H 2.417 0.02 2 191 38 38 GLY H H 8.008 0.02 1 192 38 38 GLY HA2 H 3.489 0.02 2 193 38 38 GLY HA3 H 4.234 0.02 2 194 39 39 SER H H 7.780 0.02 1 195 39 39 SER HA H 4.109 0.02 1 196 39 39 SER HB2 H 3.699 0.02 2 197 39 39 SER HB3 H 3.660 0.02 2 198 40 40 CYS H H 8.402 0.02 1 199 40 40 CYS HA H 4.627 0.02 1 200 40 40 CYS HB2 H 2.442 0.02 2 201 40 40 CYS HB3 H 3.040 0.02 2 202 41 41 PRO HA H 4.408 0.02 1 203 41 41 PRO HB2 H 2.226 0.02 2 204 41 41 PRO HB3 H 1.860 0.02 2 205 41 41 PRO HD2 H 3.591 0.02 2 206 41 41 PRO HD3 H 3.697 0.02 2 207 41 41 PRO HG2 H 1.959 0.02 2 208 41 41 PRO HG3 H 1.959 0.02 2 209 42 42 THR H H 8.192 0.02 1 210 42 42 THR HA H 4.182 0.02 1 211 42 42 THR HB H 4.110 0.02 1 212 42 42 THR HG2 H 1.126 0.02 1 213 43 43 GLY H H 8.302 0.02 1 214 43 43 GLY HA2 H 3.900 0.02 2 215 43 43 GLY HA3 H 3.900 0.02 2 216 44 44 ILE H H 7.939 0.02 1 217 44 44 ILE HA H 4.235 0.02 1 218 44 44 ILE HB H 1.847 0.02 1 219 44 44 ILE HD1 H 0.774 0.02 1 220 44 44 ILE HG12 H 1.343 0.02 2 221 44 44 ILE HG13 H 1.123 0.02 2 222 44 44 ILE HG2 H 0.845 0.02 1 stop_ save_