data_19309 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 3D NMR structure of a complex between the amyloid beta peptide (1-40) and the polyphenol epsilon-viniferin glucoside ; _BMRB_accession_number 19309 _BMRB_flat_file_name bmr19309.str _Entry_type original _Submission_date 2013-06-19 _Accession_date 2013-06-19 _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 Monti Jean-Pierre . . 2 Richard Tristan . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 220 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-09-10 original author . stop_ _Original_release_date 2013-09-10 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title '3D NMR structure of a complex between the amyloid beta peptide (1-40) and the polyphenol epsilon-viniferin glucoside: Implications in Alzheimer's disease' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23830862 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Richard Tristan . . 2 Papastamoulis Yorgos . . 3 Pierre Waffo-Teguo . . 4 Monti Jean-Pierre . . stop_ _Journal_abbreviation 'Biochim. Biophys. Acta' _Journal_volume 1830 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5068 _Page_last 5074 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'complex between the amyloid beta peptide (1-40) and the polyphenol epsilon-viniferin glucoside' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'amyloid beta peptide' $amyloid_peptide EVG_1 $entity_EVG EVG_2 $entity_EVG EVG_3 $entity_EVG EVG_4 $entity_EVG EVG_5 $entity_EVG EVG_6 $entity_EVG EVG_7 $entity_EVG EVG_8 $entity_EVG EVG_9 $entity_EVG EVG_10 $entity_EVG EVG_11 $entity_EVG EVG_12 $entity_EVG 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_amyloid_peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common amyloid_peptide _Molecular_mass 4335.893 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 40 _Mol_residue_sequence ; DAEFRHDSGYEVHHQKLVFF AEDVGSNKGAIIGLMVGGVV ; loop_ _Residue_seq_code _Residue_label 1 ASP 2 ALA 3 GLU 4 PHE 5 ARG 6 HIS 7 ASP 8 SER 9 GLY 10 TYR 11 GLU 12 VAL 13 HIS 14 HIS 15 GLN 16 LYS 17 LEU 18 VAL 19 PHE 20 PHE 21 ALA 22 GLU 23 ASP 24 VAL 25 GLY 26 SER 27 ASN 28 LYS 29 GLY 30 ALA 31 ILE 32 ILE 33 GLY 34 LEU 35 MET 36 VAL 37 GLY 38 GLY 39 VAL 40 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 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 1.45e-18 BMRB 15775 APP_C99 100.00 122 100.00 100.00 1.17e-18 BMRB 17159 Amyloid_beta-Peptide 100.00 40 100.00 100.00 1.45e-18 BMRB 17186 Abeta 100.00 40 100.00 100.00 1.45e-18 BMRB 17764 Abeta 100.00 40 100.00 100.00 1.45e-18 BMRB 17793 Abeta(1-42) 100.00 42 100.00 100.00 1.25e-18 BMRB 17794 Abeta(1-42) 100.00 42 100.00 100.00 1.25e-18 BMRB 17795 Abeta(1-40) 100.00 40 100.00 100.00 1.45e-18 BMRB 17796 Abeta40 100.00 40 100.00 100.00 1.45e-18 BMRB 18052 Pyroglutamate_Abeta 92.50 38 100.00 100.00 2.67e-16 BMRB 18127 beta-amyloid 100.00 40 100.00 100.00 1.45e-18 BMRB 18128 beta-amyloid 100.00 40 100.00 100.00 1.45e-18 BMRB 18129 beta-amyloid 100.00 40 100.00 100.00 1.45e-18 BMRB 18131 beta-amyloid 100.00 40 100.00 100.00 1.45e-18 BMRB 19009 beta-amyloid_peptide 100.00 40 100.00 100.00 1.45e-18 BMRB 19393 Abeta 100.00 39 97.50 97.50 5.22e-16 BMRB 25218 amyloid_peptide 100.00 42 100.00 100.00 1.25e-18 BMRB 25289 amyloid_beta 100.00 39 97.50 97.50 5.22e-16 BMRB 25429 entity 100.00 42 100.00 100.00 1.25e-18 BMRB 26508 amyloid_B 100.00 40 100.00 100.00 1.45e-18 BMRB 26516 amyloid_B 100.00 40 100.00 100.00 1.45e-18 PDB 1AMB "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" 70.00 28 100.00 100.00 2.06e-10 PDB 1AMC "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" 70.00 28 100.00 100.00 2.06e-10 PDB 1AML "The Alzheimer`s Disease Amyloid A4 Peptide (Residues 1-40)" 100.00 40 100.00 100.00 1.45e-18 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 1.45e-18 PDB 1BA6 "Solution Structure Of The Methionine-Oxidized Amyloid Beta- Peptide (1-40). Does Oxidation Affect Conformational Switching? Nmr" 100.00 40 97.50 97.50 1.63e-17 PDB 1HZ3 "Alzheimer's Disease Amyloid-Beta Peptide (Residues 10-35)" 65.00 26 100.00 100.00 2.01e-08 PDB 1IYT "Solution Structure Of The Alzheimer's Disease Amyloid Beta- Peptide (1-42)" 100.00 42 100.00 100.00 1.25e-18 PDB 1Z0Q "Aqueous Solution Structure Of The Alzheimer's Disease Abeta Peptide (1-42)" 100.00 42 100.00 100.00 1.25e-18 PDB 2BEG "3d Structure Of Alzheimer's Abeta(1-42) Fibrils" 100.00 42 100.00 100.00 1.25e-18 PDB 2G47 "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-40)" 100.00 40 100.00 100.00 1.45e-18 PDB 2LFM "A Partially Folded Structure Of Amyloid-Beta(1 40) In An Aqueous Environment" 100.00 40 100.00 100.00 1.45e-18 PDB 2LMN "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Positive Stagger" 100.00 40 100.00 100.00 1.45e-18 PDB 2LMO "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Negative Stagger" 100.00 40 100.00 100.00 1.45e-18 PDB 2LMP "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Positive Stagger" 100.00 40 100.00 100.00 1.45e-18 PDB 2LMQ "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Negative Stagger" 100.00 40 100.00 100.00 1.45e-18 PDB 2LNQ "40-residue D23n Beta Amyloid Fibril" 100.00 40 97.50 100.00 4.98e-18 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 1.17e-18 PDB 2M4J "40-residue Beta-amyloid Fibril Derived From Alzheimer's Disease Brain" 100.00 40 100.00 100.00 1.45e-18 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 1.45e-18 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 1.45e-18 PDB 2MVX "Atomic-resolution 3d Structure Of Amyloid-beta Fibrils: The Osaka Mutation" 100.00 39 97.50 97.50 5.22e-16 PDB 2MXU "42-residue Beta Amyloid Fibril" 100.00 42 100.00 100.00 1.25e-18 PDB 2OTK "Structure Of Alzheimer Ab Peptide In Complex With An Engineered Binding Protein" 100.00 40 100.00 100.00 1.45e-18 PDB 2WK3 "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-42)" 100.00 42 100.00 100.00 1.25e-18 PDB 3BAE "Crystal Structure Of Fab Wo2 Bound To The N Terminal Domain Of Amyloid Beta Peptide (1-28)" 70.00 28 100.00 100.00 2.06e-10 PDB 3IFN "X-ray Structure Of Amyloid Beta Peptide:antibody (abeta1-40:12a11) Complex" 100.00 40 100.00 100.00 1.45e-18 PDB 4HIX "Crystal Structure Of A Humanised 3d6 Fab Bound To Amyloid Beta Peptide" 70.00 28 100.00 100.00 2.06e-10 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 1.45e-18 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 1.45e-18 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 1.45e-18 PDB 4NGE "Crystal Structure Of Human Presequence Protease In Complex With Amyloid-beta (1-40)" 100.00 40 100.00 100.00 1.45e-18 PDB 4ONG "Fab Fragment Of 3d6 In Complex With Amyloid Beta 1-40" 100.00 40 100.00 100.00 1.45e-18 PDB 5AEF "Electron Cryo-microscopy Of An Abeta(1-42)amyloid Fibril" 65.00 28 100.00 100.00 3.64e-07 DBJ BAA22264 "amyloid precursor protein [Homo sapiens]" 100.00 770 100.00 100.00 1.24e-18 DBJ BAA84580 "amyloid precursor protein [Sus scrofa]" 100.00 770 100.00 100.00 1.24e-18 DBJ BAB71958 "amyloid precursor protein [Homo sapiens]" 100.00 52 97.50 100.00 1.70e-18 DBJ BAD51938 "amyloid beta A4 precursor protein [Macaca fascicularis]" 100.00 696 100.00 100.00 1.11e-18 DBJ BAE01907 "unnamed protein product [Macaca fascicularis]" 100.00 751 100.00 100.00 1.39e-18 EMBL CAA30050 "amyloid A4 protein [Homo sapiens]" 100.00 751 100.00 100.00 1.21e-18 EMBL CAA31830 "A4 amyloid protein precursor [Homo sapiens]" 100.00 695 100.00 100.00 1.27e-18 EMBL CAA39589 "amyloid precursor protein [Bos taurus]" 100.00 59 100.00 100.00 3.47e-19 EMBL CAA39590 "amyloid precursor protein [Canis lupus familiaris]" 100.00 58 100.00 100.00 3.58e-19 EMBL CAA39591 "amyloid precursor protein [Cavia sp.]" 100.00 58 100.00 100.00 3.58e-19 GB AAA35540 "amyloid protein, partial [Homo sapiens]" 95.00 97 100.00 100.00 2.29e-17 GB AAA36829 "amyloid b-protein precursor [Macaca fascicularis]" 100.00 695 100.00 100.00 1.27e-18 GB AAA51564 "amyloid beta protein, partial [Homo sapiens]" 75.00 30 100.00 100.00 1.06e-11 GB AAA51722 "amyloid beta-protein precursor, partial [Homo sapiens]" 100.00 412 100.00 100.00 8.90e-19 GB AAA51726 "beta-amyloid A4, partial [Homo sapiens]" 100.00 264 100.00 100.00 1.69e-18 PIR A60045 "Alzheimer's disease amyloid beta/A4 protein precursor - dog (fragment)" 100.00 57 100.00 100.00 3.90e-19 PIR D60045 "Alzheimer's disease amyloid beta/A4 protein precursor - bovine (fragment)" 100.00 57 100.00 100.00 3.90e-19 PIR E60045 "Alzheimer's disease amyloid beta/A4 protein precursor - sheep (fragment)" 100.00 57 100.00 100.00 3.90e-19 PIR G60045 "Alzheimer's disease amyloid beta/A4 protein precursor - guinea pig (fragment)" 100.00 57 100.00 100.00 3.90e-19 PIR PQ0438 "Alzheimer's disease amyloid A4 protein precursor - rabbit (fragment)" 100.00 82 100.00 100.00 3.95e-19 PRF 1303338A "amyloid A4 protein precursor" 100.00 695 100.00 100.00 1.27e-18 PRF 1403400A "amyloid protein A4" 100.00 751 100.00 100.00 1.21e-18 PRF 1405204A "amyloid protein" 100.00 42 100.00 100.00 1.25e-18 PRF 1507304A "beta amyloid peptide precursor" 100.00 412 100.00 100.00 9.17e-19 PRF 1507304B "beta amyloid peptide precursor" 100.00 574 100.00 100.00 3.96e-18 REF NP_000475 "amyloid beta A4 protein isoform a precursor [Homo sapiens]" 100.00 770 100.00 100.00 1.24e-18 REF NP_001006601 "amyloid beta A4 protein isoform APP-770 precursor [Canis lupus familiaris]" 100.00 770 100.00 100.00 1.24e-18 REF NP_001013036 "amyloid beta A4 protein precursor [Pan troglodytes]" 100.00 770 100.00 100.00 1.24e-18 REF NP_001070264 "amyloid beta A4 protein precursor [Bos taurus]" 100.00 695 100.00 100.00 1.27e-18 REF NP_001127014 "amyloid beta A4 protein precursor [Pongo abelii]" 100.00 695 100.00 100.00 1.60e-18 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 1.24e-18 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 1.24e-18 SP P79307 "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 1.24e-18 SP P86906 "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" 100.00 40 97.50 100.00 5.37e-18 SP Q28053 "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" 100.00 59 100.00 100.00 3.47e-19 TPG DAA33655 "TPA: amyloid beta A4 protein [Bos taurus]" 100.00 695 100.00 100.00 1.27e-18 stop_ save_ ############# # Ligands # ############# save_EVG _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common furan-2-sulfonamide _BMRB_code EVG _PDB_code EVG _Molecular_mass 147.152 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons O O O . 0 . ? S S S . 0 . ? O1 O1 O . 0 . ? C2 C2 C . 0 . ? O2 O2 O . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? NH NH N . 0 . ? H3 H3 H . 0 . ? H4 H4 H . 0 . ? H5 H5 H . 0 . ? HNH HNH H . 0 . ? HNHA HNHA 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 C5 O ? ? SING C2 O ? ? SING C2 S ? ? DOUB O2 S ? ? DOUB S O1 ? ? SING S NH ? ? DOUB C3 C2 ? ? SING C4 C3 ? ? SING C3 H3 ? ? DOUB C4 C5 ? ? SING C4 H4 ? ? SING C5 H5 ? ? SING NH HNH ? ? SING NH HNHA ? ? 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 $amyloid_peptide 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 $amyloid_peptide 'chemical synthesis' . human human . . $entity_EVG 'purified from the natural source' . vitis vinifera . . 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 $amyloid_peptide 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_InsightII _Saveframe_category software _Name InsightII _Version . loop_ _Vendor _Address _Electronic_address 'Accelrys Software Inc.' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _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_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pressure 1 . atm temperature 300 . 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 DMSO-d6 H 1 'methyl protons' ppm 2.54 internal direct . . . 1 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' 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 'amyloid beta 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 ASP HA H 4.13 0.003 1 2 1 1 ASP HB2 H 2.70 0.001 1 3 1 1 ASP HB3 H 2.85 0.007 1 4 2 2 ALA H H 8.60 0.003 1 5 2 2 ALA HA H 4.34 0.004 1 6 2 2 ALA HB H 1.20 0.001 1 7 3 3 GLU H H 8.08 0.003 1 8 3 3 GLU HA H 4.24 0.007 1 9 3 3 GLU HB2 H 1.70 0.005 1 10 3 3 GLU HB3 H 1.85 0.004 1 11 3 3 GLU HG2 H 2.21 0.005 1 12 3 3 GLU HG3 H 2.21 0.005 1 13 4 4 PHE H H 7.92 0.004 1 14 4 4 PHE HA H 4.58 0.009 1 15 4 4 PHE HB2 H 2.79 0.008 1 16 4 4 PHE HB3 H 3.02 0.006 1 17 4 4 PHE HD1 H 7.20 0.010 1 18 4 4 PHE HD2 H 7.20 0.010 1 19 4 4 PHE HE1 H 7.25 0.002 1 20 4 4 PHE HE2 H 7.25 0.002 1 21 5 5 ARG H H 8.31 0.007 1 22 5 5 ARG HA H 4.29 0.005 1 23 5 5 ARG HB2 H 1.55 0.004 1 24 5 5 ARG HB3 H 1.70 0.004 1 25 5 5 ARG HG2 H 1.51 0.001 1 26 5 5 ARG HG3 H 1.51 0.001 1 27 5 5 ARG HD2 H 3.13 0.003 1 28 5 5 ARG HD3 H 3.13 0.003 1 29 5 5 ARG HE H 7.58 0.002 1 30 6 6 HIS H H 8.30 0.005 1 31 6 6 HIS HA H 4.63 0.007 1 32 6 6 HIS HB2 H 3.06 0.008 1 33 6 6 HIS HB3 H 2.95 0.004 1 34 6 6 HIS HD2 H 7.32 0.005 1 35 6 6 HIS HE1 H 8.94 0.001 1 36 7 7 ASP H H 8.42 0.006 1 37 7 7 ASP HA H 4.63 0.007 1 38 7 7 ASP HB2 H 2.52 0.001 1 39 7 7 ASP HB3 H 2.73 0.003 1 40 8 8 SER H H 8.10 0.007 1 41 8 8 SER HA H 4.29 0.006 1 42 8 8 SER HB2 H 3.60 0.002 1 43 8 8 SER HB3 H 3.53 0.001 1 44 9 9 GLY H H 8.07 0.006 1 45 9 9 GLY HA2 H 3.68 0.002 1 46 9 9 GLY HA3 H 3.75 0.007 1 47 10 10 TYR H H 8.01 0.002 1 48 10 10 TYR HA H 4.50 0.004 1 49 10 10 TYR HB2 H 2.85 0.005 1 50 10 10 TYR HB3 H 2.60 0.004 1 51 10 10 TYR HD1 H 6.98 0.005 1 52 10 10 TYR HD2 H 6.98 0.005 1 53 10 10 TYR HE1 H 6.61 0.003 1 54 10 10 TYR HE2 H 6.61 0.003 1 55 11 11 GLU H H 8.23 0.004 1 56 11 11 GLU HA H 4.34 0.004 1 57 11 11 GLU HB2 H 1.73 0.004 1 58 11 11 GLU HB3 H 1.86 0.005 1 59 11 11 GLU HG2 H 2.22 0.001 1 60 11 11 GLU HG3 H 2.22 0.001 1 61 12 12 VAL H H 7.78 0.003 1 62 12 12 VAL HA H 4.15 0.003 1 63 12 12 VAL HB H 1.90 0.003 1 64 12 12 VAL HG1 H 0.77 0.003 1 65 12 12 VAL HG2 H 0.77 0.003 1 66 13 13 HIS H H 8.37 0.004 1 67 13 13 HIS HA H 4.63 0.010 1 68 13 13 HIS HB2 H 2.94 0.006 1 69 13 13 HIS HB3 H 3.04 0.006 1 70 13 13 HIS HD2 H 7.32 0.005 1 71 13 13 HIS HE1 H 8.94 0.001 1 72 14 14 HIS H H 8.28 0.009 1 73 14 14 HIS HA H 4.63 0.010 1 74 14 14 HIS HB2 H 3.07 0.004 1 75 14 14 HIS HB3 H 2.96 0.004 1 76 14 14 HIS HD2 H 7.33 0.005 1 77 14 14 HIS HE1 H 8.95 0.001 1 78 15 15 GLN H H 8.30 0.005 1 79 15 15 GLN HA H 4.27 0.012 1 80 15 15 GLN HB2 H 1.73 0.003 1 81 15 15 GLN HB3 H 1.86 0.001 1 82 15 15 GLN HG2 H 2.10 0.001 1 83 15 15 GLN HG3 H 2.10 0.001 1 84 16 16 LYS H H 8.24 0.017 1 85 16 16 LYS HA H 4.28 0.010 1 86 16 16 LYS HB2 H 1.60 0.008 1 87 16 16 LYS HB3 H 1.60 0.008 1 88 16 16 LYS HG2 H 1.26 0.009 1 89 16 16 LYS HG3 H 1.26 0.009 1 90 16 16 LYS HD2 H 1.48 0.009 1 91 16 16 LYS HD3 H 1.48 0.009 1 92 16 16 LYS HE2 H 3.00 0.005 1 93 16 16 LYS HE3 H 3.00 0.005 1 94 17 17 LEU H H 8.02 0.005 1 95 17 17 LEU HA H 4.35 0.007 1 96 17 17 LEU HB2 H 1.37 0.018 1 97 17 17 LEU HB3 H 1.37 0.018 1 98 17 17 LEU HG H 1.38 0.006 1 99 17 17 LEU HD1 H 0.75 0.007 1 100 17 17 LEU HD2 H 0.75 0.007 1 101 18 18 VAL H H 7.74 0.004 1 102 18 18 VAL HA H 4.11 0.004 1 103 18 18 VAL HB H 1.82 0.004 1 104 18 18 VAL HG1 H 0.68 0.004 1 105 18 18 VAL HG2 H 0.68 0.004 1 106 19 19 PHE H H 7.93 0.007 1 107 19 19 PHE HA H 4.55 0.008 1 108 19 19 PHE HB2 H 2.92 0.009 1 109 19 19 PHE HB3 H 2.70 0.004 1 110 19 19 PHE HD1 H 7.14 0.005 1 111 19 19 PHE HD2 H 7.14 0.005 1 112 19 19 PHE HE1 H 7.19 0.004 1 113 19 19 PHE HE2 H 7.19 0.004 1 114 20 20 PHE H H 8.12 0.007 1 115 20 20 PHE HA H 4.59 0.005 1 116 20 20 PHE HB2 H 2.79 0.006 1 117 20 20 PHE HB3 H 2.99 0.005 1 118 20 20 PHE HD1 H 7.15 0.003 1 119 20 20 PHE HD2 H 7.15 0.003 1 120 20 20 PHE HE1 H 7.20 0.004 1 121 20 20 PHE HE2 H 7.20 0.004 1 122 21 21 ALA H H 8.19 0.004 1 123 21 21 ALA HA H 4.35 0.003 1 124 21 21 ALA HB H 1.19 0.004 1 125 22 22 GLU H H 8.03 0.003 1 126 22 22 GLU HA H 4.33 0.006 1 127 22 22 GLU HB2 H 1.73 0.006 1 128 22 22 GLU HB3 H 1.87 0.001 1 129 22 22 GLU HG2 H 2.21 0.001 1 130 22 22 GLU HG3 H 2.21 0.001 1 131 23 23 ASP H H 8.28 0.004 1 132 23 23 ASP HA H 4.63 0.004 1 133 23 23 ASP HB2 H 2.69 0.005 1 134 23 23 ASP HB3 H 2.49 0.004 1 135 24 24 VAL H H 7.68 0.003 1 136 24 24 VAL HA H 4.18 0.005 1 137 24 24 VAL HB H 1.95 0.007 1 138 24 24 VAL HG1 H 0.80 0.009 1 139 24 24 VAL HG2 H 0.80 0.009 1 140 25 25 GLY H H 8.15 0.004 1 141 25 25 GLY HA2 H 3.76 0.006 1 142 25 25 GLY HA3 H 3.83 0.004 1 143 26 26 SER H H 7.97 0.006 1 144 26 26 SER HA H 4.38 0.003 1 145 26 26 SER HB2 H 3.51 0.006 1 146 26 26 SER HB3 H 3.56 0.004 1 147 27 27 ASN H H 8.27 0.004 1 148 27 27 ASN HA H 4.58 0.011 1 149 27 27 ASN HB2 H 2.48 0.004 1 150 27 27 ASN HB3 H 2.57 0.005 1 151 27 27 ASN HD21 H 6.96 0.001 1 152 27 27 ASN HD22 H 7.41 0.001 1 153 28 28 LYS H H 8.00 0.006 1 154 28 28 LYS HA H 4.18 0.004 1 155 28 28 LYS HB2 H 1.69 0.006 1 156 28 28 LYS HB3 H 1.69 0.006 1 157 28 28 LYS HG2 H 1.30 0.008 1 158 28 28 LYS HG3 H 1.30 0.008 1 159 28 28 LYS HD2 H 1.50 0.006 1 160 28 28 LYS HD3 H 1.50 0.006 1 161 28 28 LYS HE2 H 2.74 0.004 1 162 28 28 LYS HE3 H 2.74 0.004 1 163 29 29 GLY H H 8.15 0.006 1 164 29 29 GLY HA2 H 3.71 0.008 1 165 29 29 GLY HA3 H 3.78 0.007 1 166 30 30 ALA H H 7.89 0.003 1 167 30 30 ALA HA H 4.36 0.005 1 168 30 30 ALA HB H 1.16 0.001 1 169 31 31 ILE H H 7.92 0.005 1 170 31 31 ILE HA H 4.19 0.004 1 171 31 31 ILE HB H 1.71 0.007 1 172 31 31 ILE HG12 H 1.04 0.005 1 173 31 31 ILE HG13 H 1.41 0.005 1 174 31 31 ILE HG2 H 0.78 0.012 1 175 31 31 ILE HD1 H 0.78 0.008 1 176 32 32 ILE H H 7.74 0.005 1 177 32 32 ILE HA H 4.19 0.001 1 178 32 32 ILE HB H 1.69 0.005 1 179 32 32 ILE HG12 H 1.41 0.008 1 180 32 32 ILE HG13 H 1.06 0.008 1 181 32 32 ILE HG2 H 0.80 0.004 1 182 32 32 ILE HD1 H 0.80 0.008 1 183 33 33 GLY H H 8.11 0.003 1 184 33 33 GLY HA2 H 3.68 0.006 1 185 33 33 GLY HA3 H 3.79 0.004 1 186 34 34 LEU H H 7.89 0.009 1 187 34 34 LEU HA H 4.36 0.001 1 188 34 34 LEU HB2 H 1.54 0.004 1 189 34 34 LEU HB3 H 1.54 0.004 1 190 34 34 LEU HG H 1.39 0.004 1 191 34 34 LEU HD1 H 0.81 0.001 1 192 34 34 LEU HD2 H 0.81 0.001 1 193 35 35 MET H H 8.18 0.005 1 194 35 35 MET HA H 4.39 0.011 1 195 35 35 MET HB2 H 1.89 0.003 1 196 35 35 MET HB3 H 1.77 0.006 1 197 35 35 MET HG2 H 2.43 0.001 1 198 35 35 MET HG3 H 2.36 0.001 1 199 35 35 MET HE H 1.81 0.001 1 200 36 36 VAL H H 7.66 0.008 1 201 36 36 VAL HA H 4.18 0.004 1 202 36 36 VAL HB H 1.94 0.005 1 203 36 36 VAL HG1 H 0.81 0.008 1 204 36 36 VAL HG2 H 0.81 0.008 1 205 37 37 GLY H H 8.22 0.004 1 206 37 37 GLY HA2 H 3.76 0.005 1 207 37 37 GLY HA3 H 3.76 0.005 1 208 38 38 GLY H H 8.05 0.006 1 209 38 38 GLY HA2 H 3.77 0.010 1 210 38 38 GLY HA3 H 3.83 0.010 1 211 39 39 VAL H H 7.81 0.006 1 212 39 39 VAL HA H 4.35 0.001 1 213 39 39 VAL HB H 1.94 0.001 1 214 39 39 VAL HG1 H 0.82 0.005 1 215 39 39 VAL HG2 H 0.82 0.005 1 216 40 40 VAL H H 8.04 0.001 1 217 40 40 VAL HA H 4.11 0.002 1 218 40 40 VAL HB H 2.02 0.001 1 219 40 40 VAL HG1 H 0.87 0.001 1 220 40 40 VAL HG2 H 0.87 0.001 1 stop_ save_