data_19701 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of the soluble A 17-34 peptide ; _BMRB_accession_number 19701 _BMRB_flat_file_name bmr19701.str _Entry_type original _Submission_date 2013-12-23 _Accession_date 2013-12-23 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'NMR structure of the soluble A 17-34 peptide' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Fonar Gennadiy . . 2 Samson Avraham O. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 84 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-11-03 original author . stop_ _Original_release_date 2014-11-03 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR structure of the water soluble Abeta17-34 peptide' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25284368 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Samson Avraham O. . 2 Fonar Gennadiy . . stop_ _Journal_abbreviation 'Biosci. Rep.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'soluble A 17-34 peptide' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'soluble A 17-34 peptide' $entity 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_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass 1851.147 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 18 _Mol_residue_sequence LVFFAEDVGSNKGAIIGL loop_ _Residue_seq_code _Residue_label 1 LEU 2 VAL 3 PHE 4 PHE 5 ALA 6 GLU 7 ASP 8 VAL 9 GLY 10 SER 11 ASN 12 LYS 13 GLY 14 ALA 15 ILE 16 ILE 17 GLY 18 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-18 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 11435 Amyloid-beta-(1-40) 100.00 40 100.00 100.00 4.75e-02 BMRB 15775 APP_C99 100.00 122 100.00 100.00 8.10e-03 BMRB 17159 Amyloid_beta-Peptide 100.00 40 100.00 100.00 4.75e-02 BMRB 17186 Abeta 100.00 40 100.00 100.00 4.75e-02 BMRB 17764 Abeta 100.00 40 100.00 100.00 4.75e-02 BMRB 17793 Abeta(1-42) 100.00 42 100.00 100.00 4.91e-02 BMRB 17794 Abeta(1-42) 100.00 42 100.00 100.00 4.91e-02 BMRB 17795 Abeta(1-40) 100.00 40 100.00 100.00 4.75e-02 BMRB 17796 Abeta40 100.00 40 100.00 100.00 4.75e-02 BMRB 18052 Pyroglutamate_Abeta 100.00 38 100.00 100.00 4.70e-02 BMRB 18080 entity 100.00 43 100.00 100.00 3.28e-02 BMRB 18127 beta-amyloid 100.00 40 100.00 100.00 4.75e-02 BMRB 18128 beta-amyloid 100.00 40 100.00 100.00 4.75e-02 BMRB 18129 beta-amyloid 100.00 40 100.00 100.00 4.75e-02 BMRB 18131 beta-amyloid 100.00 40 100.00 100.00 4.75e-02 BMRB 19009 beta-amyloid_peptide 100.00 40 100.00 100.00 4.75e-02 BMRB 19309 amyloid_peptide 100.00 40 100.00 100.00 4.75e-02 BMRB 25218 amyloid_peptide 100.00 42 100.00 100.00 4.91e-02 BMRB 25429 entity 100.00 42 100.00 100.00 4.91e-02 BMRB 26508 amyloid_B 100.00 40 100.00 100.00 4.75e-02 BMRB 26516 amyloid_B 100.00 40 100.00 100.00 4.75e-02 PDB 1AML "The Alzheimer`s Disease Amyloid A4 Peptide (Residues 1-40)" 100.00 40 100.00 100.00 4.75e-02 PDB 1BA4 "The Solution Structure Of Amyloid Beta-Peptide (1-40) In A Water-Micelle Environment. Is The Membrane-Spanning Domain Where We " 100.00 40 100.00 100.00 4.75e-02 PDB 1BA6 "Solution Structure Of The Methionine-Oxidized Amyloid Beta- Peptide (1-40). Does Oxidation Affect Conformational Switching? Nmr" 100.00 40 100.00 100.00 5.16e-02 PDB 1HZ3 "Alzheimer's Disease Amyloid-Beta Peptide (Residues 10-35)" 100.00 26 100.00 100.00 3.62e-02 PDB 1IYT "Solution Structure Of The Alzheimer's Disease Amyloid Beta- Peptide (1-42)" 100.00 42 100.00 100.00 4.91e-02 PDB 1Z0Q "Aqueous Solution Structure Of The Alzheimer's Disease Abeta Peptide (1-42)" 100.00 42 100.00 100.00 4.91e-02 PDB 2BEG "3d Structure Of Alzheimer's Abeta(1-42) Fibrils" 100.00 42 100.00 100.00 4.91e-02 PDB 2G47 "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-40)" 100.00 40 100.00 100.00 4.75e-02 PDB 2LFM "A Partially Folded Structure Of Amyloid-Beta(1 40) In An Aqueous Environment" 100.00 40 100.00 100.00 4.75e-02 PDB 2LLM "Structure Of Amyloid Precursor Protein's Transmembrane Domain" 100.00 43 100.00 100.00 3.28e-02 PDB 2LMN "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Positive Stagger" 100.00 40 100.00 100.00 4.75e-02 PDB 2LMO "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Negative Stagger" 100.00 40 100.00 100.00 4.75e-02 PDB 2LMP "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Positive Stagger" 100.00 40 100.00 100.00 4.75e-02 PDB 2LMQ "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Negative Stagger" 100.00 40 100.00 100.00 4.75e-02 PDB 2LOH "Dimeric Structure Of Transmembrane Domain Of Amyloid Precursor Protein In Micellar Environment" 100.00 43 100.00 100.00 3.28e-02 PDB 2LP1 "The Solution Nmr Structure Of The Transmembrane C-Terminal Domain Of The Amyloid Precursor Protein (C99)" 100.00 122 100.00 100.00 8.10e-03 PDB 2M4J "40-residue Beta-amyloid Fibril Derived From Alzheimer's Disease Brain" 100.00 40 100.00 100.00 4.75e-02 PDB 2M9R "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" 100.00 40 100.00 100.00 4.75e-02 PDB 2M9S "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" 100.00 40 100.00 100.00 4.75e-02 PDB 2MJ1 "Nmr Structure Of The Soluble A Beta 17-34 Peptide" 100.00 18 100.00 100.00 7.42e-02 PDB 2MXU "42-residue Beta Amyloid Fibril" 100.00 42 100.00 100.00 4.91e-02 PDB 2OTK "Structure Of Alzheimer Ab Peptide In Complex With An Engineered Binding Protein" 100.00 40 100.00 100.00 4.75e-02 PDB 2WK3 "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-42)" 100.00 42 100.00 100.00 4.91e-02 PDB 3IFN "X-ray Structure Of Amyloid Beta Peptide:antibody (abeta1-40:12a11) Complex" 100.00 40 100.00 100.00 4.75e-02 PDB 3MOQ "Amyloid Beta(18-41) Peptide Fusion With New Antigen Receptor Variable Domain From Sharks" 94.44 126 100.00 100.00 1.75e-01 PDB 4M1C "Crystal Structure Analysis Of Fab-bound Human Insulin Degrading Enzyme (ide) In Complex With Amyloid-beta (1-40)" 100.00 40 100.00 100.00 4.75e-02 PDB 4MVI "Crystal Structure Of An Engineered Lipocalin (anticalin Us7) In Complex With The Alzheimer Amyloid Peptide Abeta(1-40)" 100.00 40 100.00 100.00 4.75e-02 PDB 4MVL "Crystal Structure Of An Engineered Lipocalin (anticalin H1ga) In Complex With The Alzheimer Amyloid Peptide Abeta1-40" 100.00 40 100.00 100.00 4.75e-02 PDB 4NGE "Crystal Structure Of Human Presequence Protease In Complex With Amyloid-beta (1-40)" 100.00 40 100.00 100.00 4.75e-02 PDB 4ONG "Fab Fragment Of 3d6 In Complex With Amyloid Beta 1-40" 100.00 40 100.00 100.00 4.75e-02 PDB 5AEF "Electron Cryo-microscopy Of An Abeta(1-42)amyloid Fibril" 100.00 28 100.00 100.00 5.76e-02 DBJ BAA22264 "amyloid precursor protein [Homo sapiens]" 100.00 770 100.00 100.00 6.07e-02 DBJ BAA84580 "amyloid precursor protein [Sus scrofa]" 100.00 770 100.00 100.00 6.07e-02 DBJ BAB71958 "amyloid precursor protein [Homo sapiens]" 100.00 52 100.00 100.00 3.77e-02 DBJ BAC34997 "unnamed protein product [Mus musculus]" 100.00 218 100.00 100.00 2.67e-02 DBJ BAC36369 "unnamed protein product [Mus musculus]" 100.00 384 100.00 100.00 4.62e-02 EMBL CAA30050 "amyloid A4 protein [Homo sapiens]" 100.00 751 100.00 100.00 6.03e-02 EMBL CAA30488 "unnamed protein product [Rattus rattus]" 100.00 695 100.00 100.00 5.91e-02 EMBL CAA31830 "A4 amyloid protein precursor [Homo sapiens]" 100.00 695 100.00 100.00 5.91e-02 EMBL CAA39589 "amyloid precursor protein [Bos taurus]" 100.00 59 100.00 100.00 3.35e-02 EMBL CAA39590 "amyloid precursor protein [Canis lupus familiaris]" 100.00 58 100.00 100.00 3.43e-02 GB AAA35540 "amyloid protein, partial [Homo sapiens]" 100.00 97 100.00 100.00 2.25e-02 GB AAA36829 "amyloid b-protein precursor [Macaca fascicularis]" 100.00 695 100.00 100.00 5.91e-02 GB AAA37139 "beta-amyloid protein [Mus musculus]" 100.00 695 100.00 100.00 5.91e-02 GB AAA51564 "amyloid beta protein, partial [Homo sapiens]" 88.89 30 100.00 100.00 7.59e-01 GB AAA51722 "amyloid beta-protein precursor, partial [Homo sapiens]" 100.00 412 100.00 100.00 4.82e-02 PIR A60045 "Alzheimer's disease amyloid beta/A4 protein precursor - dog (fragment)" 100.00 57 100.00 100.00 3.38e-02 PIR D60045 "Alzheimer's disease amyloid beta/A4 protein precursor - bovine (fragment)" 100.00 57 100.00 100.00 3.38e-02 PIR E60045 "Alzheimer's disease amyloid beta/A4 protein precursor - sheep (fragment)" 100.00 57 100.00 100.00 3.38e-02 PIR G60045 "Alzheimer's disease amyloid beta/A4 protein precursor - guinea pig (fragment)" 100.00 57 100.00 100.00 3.38e-02 PIR PQ0438 "Alzheimer's disease amyloid A4 protein precursor - rabbit (fragment)" 100.00 82 100.00 100.00 2.36e-02 PRF 1303338A "amyloid A4 protein precursor" 100.00 695 100.00 100.00 5.91e-02 PRF 1403400A "amyloid protein A4" 100.00 751 100.00 100.00 6.03e-02 PRF 1405204A "amyloid protein" 100.00 42 100.00 100.00 4.91e-02 PRF 1507304A "beta amyloid peptide precursor" 100.00 412 100.00 100.00 4.82e-02 PRF 1507304B "beta amyloid peptide precursor" 100.00 574 100.00 100.00 5.58e-02 REF NP_000475 "amyloid beta A4 protein isoform a precursor [Homo sapiens]" 100.00 770 100.00 100.00 6.07e-02 REF NP_001006601 "amyloid beta A4 protein isoform APP-770 precursor [Canis lupus familiaris]" 100.00 770 100.00 100.00 6.07e-02 REF NP_001013036 "amyloid beta A4 protein precursor [Pan troglodytes]" 100.00 770 100.00 100.00 6.07e-02 REF NP_001070264 "amyloid beta A4 protein precursor [Bos taurus]" 100.00 695 100.00 100.00 5.91e-02 REF NP_001127014 "amyloid beta A4 protein precursor [Pongo abelii]" 100.00 695 100.00 100.00 5.91e-02 SP O73683 "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" 100.00 780 100.00 100.00 6.09e-02 SP P05067 "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; AltName: Full=APPI; Short=APP; AltName: Full=Alzheimer disease amylo" 100.00 770 100.00 100.00 6.07e-02 SP P08592 "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" 100.00 770 100.00 100.00 6.07e-02 SP P12023 "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" 100.00 770 100.00 100.00 6.07e-02 SP P53601 "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" 100.00 770 100.00 100.00 6.07e-02 TPG DAA33655 "TPA: amyloid beta A4 protein [Bos taurus]" 100.00 695 100.00 100.00 5.91e-02 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity 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 $entity 'obtained from a vendor' . . . . . 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 $entity . mM 'natural abundance' 'sodium phosphate' 50 mM 'natural abundance' 'sodium azide' 0.2 uM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CNS _Saveframe_category software _Name CNS _Version 1.3 loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.12 . mM pH 7 . pH pressure 1 . atm temperature 278 . 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 4.75 internal direct spherical 'insert at outer edge of experimental sample tube' parallel 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_ _Experiment_label '2D 1H-1H TOCSY' '2D 1H-1H 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 'soluble A 17-34 peptide' _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 LEU H H 8.307 0.01 . 2 1 1 LEU HA H 4.016 0.01 . 3 1 1 LEU HB2 H 2.003 0.01 . 4 1 1 LEU HB3 H 1.957 0.01 . 5 1 1 LEU HG H 1.777 0.01 . 6 1 1 LEU HD1 H 1.604 0.01 . 7 1 1 LEU HD1 H 1.132 0.01 . 8 1 1 LEU HD1 H 0.619 0.01 . 9 1 1 LEU HD2 H 0.54 0.01 . 10 2 2 VAL H H 7.894 0.01 . 11 2 2 VAL HA H 3.708 0.01 . 12 2 2 VAL HB H 1.581 0.01 . 13 2 2 VAL HG1 H 0.537 0.01 . 14 2 2 VAL HG2 H 0.435 0.01 . 15 3 3 PHE H H 8.109 0.01 . 16 3 3 PHE HA H 4.267 0.01 . 17 3 3 PHE HD1 H 0.603 0.01 . 18 3 3 PHE HD2 H 0.603 0.01 . 19 4 4 PHE H H 8.026 0.01 . 20 4 4 PHE HA H 4.24 0.01 . 21 4 4 PHE HB2 H 2.75 0.01 . 22 4 4 PHE HB3 H 2.613 0.01 . 23 4 4 PHE HD2 H 2.596 0.01 . 24 5 5 ALA H H 8.023 0.01 . 25 5 5 ALA HA H 3.901 0.01 . 26 5 5 ALA HB H 1.045 0.01 . 27 6 6 GLU H H 8.138 0.01 . 28 6 6 GLU HA H 3.87 0.01 . 29 6 6 GLU HB2 H 2.671 0.01 . 30 6 6 GLU HB3 H 2.617 0.01 . 31 6 6 GLU HG2 H 1.716 0.01 . 32 6 6 GLU HG3 H 1.589 0.01 . 33 7 7 ASP H H 8.231 0.01 . 34 7 7 ASP HA H 4.322 0.01 . 35 7 7 ASP HB2 H 2.442 0.01 . 36 7 7 ASP HB3 H 2.329 0.01 . 37 8 8 VAL H H 7.954 0.01 . 38 8 8 VAL HA H 3.822 0.01 . 39 8 8 VAL HB H 1.873 0.01 . 40 8 8 VAL HG1 H 1.051 0.01 . 41 8 8 VAL HG2 H 0.644 0.01 . 42 9 9 GLY H H 8.341 0.01 . 43 9 9 GLY HA2 H 3.668 0.01 . 44 9 9 GLY HA3 H 3.668 0.01 . 45 10 10 SER H H 7.94 0.01 . 46 10 10 SER HA H 4.127 0.01 . 47 10 10 SER HB2 H 3.586 0.01 . 48 10 10 SER HB3 H 3.545 0.01 . 49 11 11 ASN H H 7.809 0.01 . 50 11 11 ASN HA H 3.798 0.01 . 51 11 11 ASN HB2 H 1.877 0.01 . 52 11 11 ASN HB3 H 1.743 0.01 . 53 11 11 ASN HD21 H 1.712 0.01 . 54 11 11 ASN HD22 H 1.545 0.01 . 55 12 12 LYS H H 8.143 0.01 . 56 12 12 LYS HA H 3.959 0.01 . 57 12 12 LYS HB2 H 2.678 0.01 . 58 12 12 LYS HG2 H 1.956 0.01 . 59 12 12 LYS HG3 H 1.719 0.01 . 60 12 12 LYS HD2 H 1.623 0.01 . 61 13 13 GLY H H 8.205 0.01 . 62 13 13 GLY HA2 H 3.61 0.01 . 63 14 14 ALA H H 7.837 0.01 . 64 14 14 ALA HA H 3.993 0.01 . 65 14 14 ALA HB H 1.051 0.01 . 66 15 15 ILE H H 8.003 0.01 . 67 15 15 ILE HA H 3.836 0.01 . 68 15 15 ILE HG12 H 1.212 0.01 . 69 15 15 ILE HG13 H 0.88 0.01 . 70 15 15 ILE HD1 H 0.562 0.01 . 71 16 16 ILE H H 8.109 0.01 . 72 16 16 ILE HA H 3.86 0.01 . 73 16 16 ILE HB H 2.661 0.01 . 74 16 16 ILE HG12 H 2.61 0.01 . 75 16 16 ILE HG13 H 1.202 0.01 . 76 16 16 ILE HG2 H 0.908 0.01 . 77 17 17 GLY H H 8.351 0.01 . 78 17 17 GLY HA2 H 3.613 0.01 . 79 17 17 GLY HA3 H 3.613 0.01 . 80 18 18 LEU H H 7.921 0.01 . 81 18 18 LEU HA H 4.072 0.01 . 82 18 18 LEU HG H 1.298 0.01 . 83 18 18 LEU HD1 H 0.616 0.01 . 84 18 18 LEU HD2 H 0.565 0.01 . stop_ save_