data_11435 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N Chemical Shift Assignments for amyloid-beta-(1-40) ; _BMRB_accession_number 11435 _BMRB_flat_file_name bmr11435.str _Entry_type original _Submission_date 2011-03-16 _Accession_date 2011-03-16 _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 Yamaguchi Takahiro . . 2 Matsuzaki Katsumi . . 3 Hoshino Masaru . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 168 "13C chemical shifts" 107 "15N chemical shifts" 39 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-06-07 original author . stop_ _Original_release_date 2011-06-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Transient formation of intermediate conformational states of amyloid-beta peptide revealed by heteronuclear magnetic resonance spectroscopy' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21402073 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yamaguchi Takahiro . . 2 Matsuzaki Katsumi . . 3 Hoshino Masaru . . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_volume 585 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1097 _Page_last 1102 _Year 2011 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Amyloid-beta-(1-40) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Amyloid beta-(1-40)' $Amyloid-beta-(1-40) stop_ _System_molecular_weight . _System_physical_state 'intrinsically disordered' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Amyloid-beta-(1-40) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Amyloid-beta-(1-40) _Molecular_mass . _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 2015-10-28 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 BMRB 15775 APP_C99 100.00 122 100.00 100.00 1.16e-18 BMRB 17159 Amyloid_beta-Peptide 100.00 40 100.00 100.00 1.44e-18 BMRB 17186 Abeta 100.00 40 100.00 100.00 1.44e-18 BMRB 17764 Abeta 100.00 40 100.00 100.00 1.44e-18 BMRB 17793 Abeta(1-42) 100.00 42 100.00 100.00 1.24e-18 BMRB 17794 Abeta(1-42) 100.00 42 100.00 100.00 1.24e-18 BMRB 17795 Abeta(1-40) 100.00 40 100.00 100.00 1.44e-18 BMRB 17796 Abeta40 100.00 40 100.00 100.00 1.44e-18 BMRB 18052 Pyroglutamate_Abeta 92.50 38 100.00 100.00 2.64e-16 BMRB 18127 beta-amyloid 100.00 40 100.00 100.00 1.44e-18 BMRB 18128 beta-amyloid 100.00 40 100.00 100.00 1.44e-18 BMRB 18129 beta-amyloid 100.00 40 100.00 100.00 1.44e-18 BMRB 18131 beta-amyloid 100.00 40 100.00 100.00 1.44e-18 BMRB 19009 beta-amyloid_peptide 100.00 40 100.00 100.00 1.44e-18 BMRB 19309 amyloid_peptide 100.00 40 100.00 100.00 1.44e-18 BMRB 19393 Abeta 100.00 39 97.50 97.50 5.18e-16 BMRB 25218 amyloid_peptide 100.00 42 100.00 100.00 1.24e-18 BMRB 25289 amyloid_beta 100.00 39 97.50 97.50 5.18e-16 BMRB 25429 entity 100.00 42 100.00 100.00 1.24e-18 BMRB 26508 amyloid_B 100.00 40 100.00 100.00 1.44e-18 BMRB 26516 amyloid_B 100.00 40 100.00 100.00 1.44e-18 PDB 1AMB "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" 70.00 28 100.00 100.00 2.04e-10 PDB 1AMC "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" 70.00 28 100.00 100.00 2.04e-10 PDB 1AML "The Alzheimer`s Disease Amyloid A4 Peptide (Residues 1-40)" 100.00 40 100.00 100.00 1.44e-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 1.44e-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 1.62e-17 PDB 1HZ3 "Alzheimer's Disease Amyloid-Beta Peptide (Residues 10-35)" 65.00 26 100.00 100.00 1.99e-08 PDB 1IYT "Solution Structure Of The Alzheimer's Disease Amyloid Beta- Peptide (1-42)" 100.00 42 100.00 100.00 1.24e-18 PDB 1Z0Q "Aqueous Solution Structure Of The Alzheimer's Disease Abeta Peptide (1-42)" 100.00 42 100.00 100.00 1.24e-18 PDB 2BEG "3d Structure Of Alzheimer's Abeta(1-42) Fibrils" 100.00 42 100.00 100.00 1.24e-18 PDB 2G47 "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-40)" 100.00 40 100.00 100.00 1.44e-18 PDB 2LFM "A Partially Folded Structure Of Amyloid-Beta(1 40) In An Aqueous Environment" 100.00 40 100.00 100.00 1.44e-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 1.44e-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 1.44e-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 1.44e-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 1.44e-18 PDB 2LNQ "40-residue D23n Beta Amyloid Fibril" 100.00 40 97.50 100.00 4.93e-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 1.16e-18 PDB 2M4J "40-residue Beta-amyloid Fibril Derived From Alzheimer's Disease Brain" 100.00 40 100.00 100.00 1.44e-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 1.44e-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 1.44e-18 PDB 2MVX "Atomic-resolution 3d Structure Of Amyloid-beta Fibrils: The Osaka Mutation" 100.00 39 97.50 97.50 5.18e-16 PDB 2MXU "42-residue Beta Amyloid Fibril" 100.00 42 100.00 100.00 1.24e-18 PDB 2OTK "Structure Of Alzheimer Ab Peptide In Complex With An Engineered Binding Protein" 100.00 40 100.00 100.00 1.44e-18 PDB 2WK3 "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-42)" 100.00 42 100.00 100.00 1.24e-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 2.04e-10 PDB 3IFN "X-ray Structure Of Amyloid Beta Peptide:antibody (abeta1-40:12a11) Complex" 100.00 40 100.00 100.00 1.44e-18 PDB 4HIX "Crystal Structure Of A Humanised 3d6 Fab Bound To Amyloid Beta Peptide" 70.00 28 100.00 100.00 2.04e-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 1.44e-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 1.44e-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 1.44e-18 PDB 4NGE "Crystal Structure Of Human Presequence Protease In Complex With Amyloid-beta (1-40)" 100.00 40 100.00 100.00 1.44e-18 PDB 4ONG "Fab Fragment Of 3d6 In Complex With Amyloid Beta 1-40" 100.00 40 100.00 100.00 1.44e-18 PDB 5AEF "Electron Cryo-microscopy Of An Abeta(1-42)amyloid Fibril" 65.00 28 100.00 100.00 3.61e-07 DBJ BAA22264 "amyloid precursor protein [Homo sapiens]" 100.00 770 100.00 100.00 1.23e-18 DBJ BAA84580 "amyloid precursor protein [Sus scrofa]" 100.00 770 100.00 100.00 1.23e-18 DBJ BAB71958 "amyloid precursor protein [Homo sapiens]" 100.00 52 97.50 100.00 1.69e-18 DBJ BAD51938 "amyloid beta A4 precursor protein [Macaca fascicularis]" 100.00 696 100.00 100.00 1.10e-18 DBJ BAE01907 "unnamed protein product [Macaca fascicularis]" 100.00 751 100.00 100.00 1.38e-18 EMBL CAA30050 "amyloid A4 protein [Homo sapiens]" 100.00 751 100.00 100.00 1.20e-18 EMBL CAA31830 "A4 amyloid protein precursor [Homo sapiens]" 100.00 695 100.00 100.00 1.26e-18 EMBL CAA39589 "amyloid precursor protein [Bos taurus]" 100.00 59 100.00 100.00 3.44e-19 EMBL CAA39590 "amyloid precursor protein [Canis lupus familiaris]" 100.00 58 100.00 100.00 3.55e-19 EMBL CAA39591 "amyloid precursor protein [Cavia sp.]" 100.00 58 100.00 100.00 3.55e-19 GB AAA35540 "amyloid protein, partial [Homo sapiens]" 95.00 97 100.00 100.00 2.27e-17 GB AAA36829 "amyloid b-protein precursor [Macaca fascicularis]" 100.00 695 100.00 100.00 1.26e-18 GB AAA51564 "amyloid beta protein, partial [Homo sapiens]" 75.00 30 100.00 100.00 1.05e-11 GB AAA51722 "amyloid beta-protein precursor, partial [Homo sapiens]" 100.00 412 100.00 100.00 8.82e-19 GB AAA51726 "beta-amyloid A4, partial [Homo sapiens]" 100.00 264 100.00 100.00 1.68e-18 PIR A60045 "Alzheimer's disease amyloid beta/A4 protein precursor - dog (fragment)" 100.00 57 100.00 100.00 3.87e-19 PIR D60045 "Alzheimer's disease amyloid beta/A4 protein precursor - bovine (fragment)" 100.00 57 100.00 100.00 3.87e-19 PIR E60045 "Alzheimer's disease amyloid beta/A4 protein precursor - sheep (fragment)" 100.00 57 100.00 100.00 3.87e-19 PIR G60045 "Alzheimer's disease amyloid beta/A4 protein precursor - guinea pig (fragment)" 100.00 57 100.00 100.00 3.87e-19 PIR PQ0438 "Alzheimer's disease amyloid A4 protein precursor - rabbit (fragment)" 100.00 82 100.00 100.00 3.91e-19 PRF 1303338A "amyloid A4 protein precursor" 100.00 695 100.00 100.00 1.26e-18 PRF 1403400A "amyloid protein A4" 100.00 751 100.00 100.00 1.20e-18 PRF 1405204A "amyloid protein" 100.00 42 100.00 100.00 1.24e-18 PRF 1507304A "beta amyloid peptide precursor" 100.00 412 100.00 100.00 9.10e-19 PRF 1507304B "beta amyloid peptide precursor" 100.00 574 100.00 100.00 3.93e-18 REF NP_000475 "amyloid beta A4 protein isoform a precursor [Homo sapiens]" 100.00 770 100.00 100.00 1.23e-18 REF NP_001006601 "amyloid beta A4 protein isoform APP-770 precursor [Canis lupus familiaris]" 100.00 770 100.00 100.00 1.23e-18 REF NP_001013036 "amyloid beta A4 protein precursor [Pan troglodytes]" 100.00 770 100.00 100.00 1.23e-18 REF NP_001070264 "amyloid beta A4 protein precursor [Bos taurus]" 100.00 695 100.00 100.00 1.26e-18 REF NP_001127014 "amyloid beta A4 protein precursor [Pongo abelii]" 100.00 695 100.00 100.00 1.59e-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 1.23e-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 1.23e-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 1.23e-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 5.32e-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 3.44e-19 TPG DAA33655 "TPA: amyloid beta A4 protein [Bos taurus]" 100.00 695 100.00 100.00 1.26e-18 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Amyloid-beta-(1-40) 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-beta-(1-40) 'recombinant technology' . Escherichia coli . pET28a 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-beta-(1-40) 50 uM [U-15N] 'sodium phosphate' 50 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Amyloid-beta-(1-40) 50 uM '[U-13C; U-15N]' 'sodium phosphate' 50 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' D2O 100 % 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Amyloid-beta-(1-40) 150 uM '[U-13C; U-15N]' 'sodium phosphate' 50 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_2 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_3 save_ save_3D_HCCH-TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_3 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . pH temperature 277 . 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 DSS C 13 'methyl carbons' ppm 0.00 external direct . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 external direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 external indirect . . . 0.101329118 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-15N HSQC' '2D 1H-13C HSQC' '3D HNCACB' '3D HCCH-TOCSY' stop_ loop_ _Sample_label $sample_1 $sample_2 $sample_3 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Amyloid beta-(1-40)' _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 4.23 0.01 1 2 1 1 ASP HB2 H 2.72 0.01 2 3 1 1 ASP HB3 H 2.84 0.01 2 4 1 1 ASP CA C 53.7 0.1 1 5 1 1 ASP CB C 40.0 0.1 1 6 2 2 ALA H H 8.79 0.01 1 7 2 2 ALA HA H 4.31 0.01 1 8 2 2 ALA HB H 1.37 0.01 1 9 2 2 ALA CA C 52.7 0.1 1 10 2 2 ALA CB C 19.1 0.1 1 11 2 2 ALA N N 124.3 0.1 1 12 3 3 GLU H H 8.57 0.01 1 13 3 3 GLU HA H 4.18 0.01 1 14 3 3 GLU HB2 H 1.92 0.01 5 15 3 3 GLU HB3 H 2.04 0.01 5 16 3 3 GLU HG2 H 2.14 0.01 5 17 3 3 GLU HG3 H 2.22 0.01 5 18 3 3 GLU CA C 56.6 0.1 1 19 3 3 GLU CB C 30.2 0.1 1 20 3 3 GLU CG C 36.2 0.1 5 21 3 3 GLU N N 121.0 0.1 1 22 4 4 PHE H H 8.44 0.01 1 23 4 4 PHE HA H 4.59 0.01 1 24 4 4 PHE HB2 H 3.02 0.01 2 25 4 4 PHE CA C 57.6 0.1 1 26 4 4 PHE CB C 39.5 0.1 1 27 4 4 PHE N N 122.1 0.1 1 28 5 5 ARG H H 8.30 0.01 1 29 5 5 ARG HA H 4.24 0.01 1 30 5 5 ARG HB2 H 1.64 0.01 2 31 5 5 ARG HB3 H 1.73 0.01 2 32 5 5 ARG HG2 H 1.48 0.01 2 33 5 5 ARG HD2 H 3.12 0.01 2 34 5 5 ARG CA C 55.7 0.1 1 35 5 5 ARG CB C 31.0 0.1 1 36 5 5 ARG CG C 27.0 0.1 1 37 5 5 ARG CD C 43.2 0.1 1 38 5 5 ARG N N 123.9 0.1 1 39 6 6 HIS H H 8.61 0.01 1 40 6 6 HIS HA H 4.59 0.01 1 41 6 6 HIS HB2 H 3.08 0.01 5 42 6 6 HIS HB3 H 3.16 0.01 5 43 6 6 HIS CA C 55.9 0.1 1 44 6 6 HIS CB C 30.0 0.1 1 45 6 6 HIS N N 121.4 0.1 1 46 7 7 ASP H H 8.53 0.01 1 47 7 7 ASP HA H 4.65 0.01 1 48 7 7 ASP HB2 H 2.70 0.01 5 49 7 7 ASP CA C 54.1 0.1 1 50 7 7 ASP CB C 41.2 0.1 1 51 7 7 ASP N N 122.1 0.1 1 52 8 8 SER H H 8.60 0.01 1 53 8 8 SER HA H 4.40 0.01 1 54 8 8 SER HB2 H 3.90 0.01 5 55 8 8 SER CA C 59.2 0.1 1 56 8 8 SER CB C 63.6 0.1 1 57 8 8 SER N N 117.1 0.1 1 58 9 9 GLY H H 8.68 0.01 1 59 9 9 GLY HA2 H 3.93 0.01 2 60 9 9 GLY CA C 45.4 0.1 1 61 9 9 GLY N N 111.2 0.1 1 62 10 10 TYR H H 8.07 0.01 1 63 10 10 TYR HA H 4.51 0.01 1 64 10 10 TYR HB2 H 2.97 0.01 2 65 10 10 TYR HB3 H 3.01 0.01 2 66 10 10 TYR CA C 58.4 0.1 1 67 10 10 TYR CB C 38.8 0.1 1 68 10 10 TYR N N 120.6 0.1 1 69 11 11 GLU H H 8.49 0.01 1 70 11 11 GLU HA H 4.21 0.01 1 71 11 11 GLU HB2 H 1.92 0.01 5 72 11 11 GLU HB3 H 2.04 0.01 5 73 11 11 GLU HG2 H 2.14 0.01 5 74 11 11 GLU HG3 H 2.22 0.01 5 75 11 11 GLU CA C 56.5 0.1 1 76 11 11 GLU CB C 30.3 0.1 1 77 11 11 GLU CG C 36.2 0.1 5 78 11 11 GLU N N 123.0 0.1 1 79 12 12 VAL H H 8.21 0.01 1 80 12 12 VAL HA H 3.93 0.01 1 81 12 12 VAL HB H 1.93 0.01 1 82 12 12 VAL HG1 H 0.77 0.01 2 83 12 12 VAL HG2 H 0.88 0.01 2 84 12 12 VAL CA C 62.8 0.1 1 85 12 12 VAL CB C 32.5 0.1 1 86 12 12 VAL CG1 C 20.8 0.1 2 87 12 12 VAL N N 121.8 0.1 1 88 13 13 HIS H H 8.49 0.01 1 89 13 13 HIS HA H 4.66 0.01 1 90 13 13 HIS HB2 H 3.05 0.01 2 91 13 13 HIS HB3 H 3.12 0.01 2 92 13 13 HIS CA C 55.7 0.1 1 93 13 13 HIS CB C 29.9 0.1 1 94 13 13 HIS N N 122.7 0.1 1 95 14 14 HIS H H 8.53 0.01 1 96 14 14 HIS HA H 4.60 0.01 1 97 14 14 HIS HB2 H 3.08 0.01 5 98 14 14 HIS HB3 H 3.16 0.01 5 99 14 14 HIS CA C 55.9 0.1 1 100 14 14 HIS CB C 29.9 0.1 1 101 14 14 HIS N N 121.3 0.1 1 102 15 15 GLN H H 8.62 0.01 1 103 15 15 GLN HA H 4.29 0.01 1 104 15 15 GLN HB2 H 1.98 0.01 2 105 15 15 GLN HB3 H 2.06 0.01 2 106 15 15 GLN HG2 H 2.35 0.01 2 107 15 15 GLN CA C 55.9 0.1 1 108 15 15 GLN CB C 29.5 0.1 1 109 15 15 GLN CG C 33.7 0.1 1 110 15 15 GLN N N 122.1 0.1 1 111 16 16 LYS H H 8.58 0.01 1 112 16 16 LYS HA H 4.29 0.01 1 113 16 16 LYS HB2 H 1.78 0.01 2 114 16 16 LYS HG2 H 1.40 0.01 5 115 16 16 LYS HG3 H 1.46 0.01 5 116 16 16 LYS HD2 H 1.68 0.01 5 117 16 16 LYS HD3 H 1.78 0.01 5 118 16 16 LYS HE2 H 2.98 0.01 5 119 16 16 LYS CA C 56.4 0.1 1 120 16 16 LYS CB C 33.0 0.1 1 121 16 16 LYS CG C 24.8 0.1 5 122 16 16 LYS CD C 29.1 0.1 5 123 16 16 LYS CE C 42.0 0.1 5 124 16 16 LYS N N 123.9 0.1 1 125 17 17 LEU H H 8.43 0.01 1 126 17 17 LEU HA H 4.34 0.01 1 127 17 17 LEU HB2 H 1.44 0.01 5 128 17 17 LEU HG H 1.60 0.01 5 129 17 17 LEU HD1 H 0.86 0.01 5 130 17 17 LEU HD2 H 0.92 0.01 5 131 17 17 LEU CA C 55.1 0.1 1 132 17 17 LEU CB C 42.3 0.1 1 133 17 17 LEU CG C 26.9 0.1 1 134 17 17 LEU CD1 C 23.6 0.1 5 135 17 17 LEU CD2 C 24.8 0.1 5 136 17 17 LEU N N 124.6 0.1 1 137 18 18 VAL H H 8.16 0.01 1 138 18 18 VAL HA H 4.04 0.01 1 139 18 18 VAL HB H 1.90 0.01 1 140 18 18 VAL HG1 H 0.75 0.01 2 141 18 18 VAL HG2 H 0.84 0.01 2 142 18 18 VAL CA C 62.0 0.1 1 143 18 18 VAL CB C 33.1 0.1 1 144 18 18 VAL CG1 C 21.2 0.1 2 145 18 18 VAL CG2 C 20.6 0.1 2 146 18 18 VAL N N 122.1 0.1 1 147 19 19 PHE H H 8.42 0.01 1 148 19 19 PHE HA H 4.60 0.01 1 149 19 19 PHE HB2 H 2.92 0.01 5 150 19 19 PHE HB3 H 3.07 0.01 5 151 19 19 PHE CA C 57.5 0.1 1 152 19 19 PHE CB C 40.2 0.1 1 153 19 19 PHE N N 125.0 0.1 1 154 20 20 PHE H H 8.36 0.01 1 155 20 20 PHE HA H 4.58 0.01 1 156 20 20 PHE HB2 H 2.92 0.01 5 157 20 20 PHE HB3 H 3.07 0.01 5 158 20 20 PHE CA C 57.4 0.1 1 159 20 20 PHE CB C 40.1 0.1 1 160 20 20 PHE N N 123.5 0.1 1 161 21 21 ALA H H 8.38 0.01 1 162 21 21 ALA HA H 4.23 0.01 1 163 21 21 ALA HB H 1.37 0.01 1 164 21 21 ALA CA C 52.4 0.1 1 165 21 21 ALA CB C 19.4 0.1 1 166 21 21 ALA N N 126.7 0.1 1 167 22 22 GLU H H 8.50 0.01 1 168 22 22 GLU HA H 4.21 0.01 1 169 22 22 GLU HB2 H 1.92 0.01 5 170 22 22 GLU HB3 H 2.04 0.01 5 171 22 22 GLU HG2 H 2.14 0.01 5 172 22 22 GLU HG3 H 2.22 0.01 5 173 22 22 GLU CA C 56.6 0.1 1 174 22 22 GLU CB C 30.3 0.1 1 175 22 22 GLU CG C 36.2 0.1 5 176 22 22 GLU N N 120.4 0.1 1 177 23 23 ASP H H 8.56 0.01 1 178 23 23 ASP HA H 4.66 0.01 1 179 23 23 ASP HB2 H 2.70 0.01 5 180 23 23 ASP CA C 54.2 0.1 1 181 23 23 ASP CB C 41.1 0.1 1 182 23 23 ASP N N 122.2 0.1 1 183 24 24 VAL H H 8.30 0.01 1 184 24 24 VAL HA H 4.15 0.01 1 185 24 24 VAL HB H 2.19 0.01 1 186 24 24 VAL HG1 H 0.95 0.01 5 187 24 24 VAL CA C 62.8 0.1 1 188 24 24 VAL CB C 32.3 0.1 1 189 24 24 VAL CG1 C 20.8 0.1 5 190 24 24 VAL N N 121.1 0.1 1 191 25 25 GLY H H 8.68 0.01 1 192 25 25 GLY HA2 H 3.99 0.01 2 193 25 25 GLY CA C 45.5 0.1 1 194 25 25 GLY N N 112.3 0.1 1 195 26 26 SER H H 8.30 0.01 1 196 26 26 SER HA H 4.43 0.01 1 197 26 26 SER HB2 H 3.90 0.01 5 198 26 26 SER CA C 58.6 0.1 1 199 26 26 SER CB C 63.7 0.1 1 200 26 26 SER N N 116.0 0.1 1 201 27 27 ASN H H 8.62 0.01 1 202 27 27 ASN HA H 4.75 0.01 1 203 27 27 ASN HB2 H 2.81 0.01 2 204 27 27 ASN HB3 H 2.87 0.01 2 205 27 27 ASN CA C 53.3 0.1 1 206 27 27 ASN CB C 38.5 0.1 1 207 27 27 ASN N N 121.0 0.1 1 208 28 28 LYS H H 8.49 0.01 1 209 28 28 LYS HA H 4.28 0.01 1 210 28 28 LYS HB2 H 1.89 0.01 2 211 28 28 LYS HG2 H 1.40 0.01 5 212 28 28 LYS HG3 H 1.46 0.01 5 213 28 28 LYS HD2 H 1.68 0.01 5 214 28 28 LYS HD3 H 1.78 0.01 5 215 28 28 LYS HE2 H 2.98 0.01 5 216 28 28 LYS CA C 56.8 0.1 1 217 28 28 LYS CB C 32.5 0.1 1 218 28 28 LYS CG C 24.8 0.1 5 219 28 28 LYS CD C 32.8 0.1 5 220 28 28 LYS CE C 42.0 0.1 5 221 28 28 LYS N N 122.2 0.1 1 222 29 29 GLY H H 8.56 0.01 1 223 29 29 GLY HA2 H 3.94 0.01 2 224 29 29 GLY CA C 45.2 0.1 1 225 29 29 GLY N N 110.0 0.1 1 226 30 30 ALA H H 8.16 0.01 1 227 30 30 ALA HA H 4.32 0.01 1 228 30 30 ALA HB H 1.36 0.01 1 229 30 30 ALA CA C 52.5 0.1 1 230 30 30 ALA CB C 19.3 0.1 1 231 30 30 ALA N N 124.0 0.1 1 232 31 31 ILE H H 8.33 0.01 1 233 31 31 ILE HA H 4.16 0.01 1 234 31 31 ILE HB H 1.86 0.01 5 235 31 31 ILE HG12 H 1.20 0.01 5 236 31 31 ILE HG13 H 1.51 0.01 5 237 31 31 ILE HG2 H 0.92 0.01 5 238 31 31 ILE HD1 H 0.87 0.01 5 239 31 31 ILE CA C 61.1 0.1 1 240 31 31 ILE CB C 38.4 0.1 1 241 31 31 ILE CG1 C 27.3 0.1 5 242 31 31 ILE CG2 C 17.4 0.1 5 243 31 31 ILE CD1 C 12.6 0.1 5 244 31 31 ILE N N 121.3 0.1 1 245 32 32 ILE H H 8.43 0.01 1 246 32 32 ILE HA H 4.17 0.01 1 247 32 32 ILE HB H 1.86 0.01 5 248 32 32 ILE HG12 H 1.20 0.01 5 249 32 32 ILE HG13 H 1.51 0.01 5 250 32 32 ILE HG2 H 0.92 0.01 5 251 32 32 ILE HD1 H 0.87 0.01 5 252 32 32 ILE CA C 61.2 0.1 1 253 32 32 ILE CB C 38.4 0.1 1 254 32 32 ILE CG1 C 27.3 0.1 5 255 32 32 ILE CG2 C 17.4 0.1 5 256 32 32 ILE CD1 C 12.6 0.1 5 257 32 32 ILE N N 126.8 0.1 1 258 33 33 GLY H H 8.62 0.01 1 259 33 33 GLY HA2 H 3.95 0.01 2 260 33 33 GLY CA C 45.2 0.1 1 261 33 33 GLY N N 113.6 0.1 1 262 34 34 LEU H H 8.19 0.01 1 263 34 34 LEU HA H 4.35 0.01 1 264 34 34 LEU HB2 H 1.44 0.01 5 265 34 34 LEU HG H 1.60 0.01 5 266 34 34 LEU HD1 H 0.86 0.01 5 267 34 34 LEU HD2 H 0.92 0.01 5 268 34 34 LEU CA C 55.2 0.1 1 269 34 34 LEU CB C 42.5 0.1 1 270 34 34 LEU CG C 26.9 0.1 1 271 34 34 LEU CD1 C 23.6 0.1 5 272 34 34 LEU CD2 C 24.8 0.1 5 273 34 34 LEU N N 122.1 0.1 1 274 35 35 MET H H 8.59 0.01 1 275 35 35 MET HA H 4.54 0.01 1 276 35 35 MET HB2 H 2.03 0.01 2 277 35 35 MET HG2 H 2.51 0.01 2 278 35 35 MET HG3 H 2.59 0.01 2 279 35 35 MET CA C 55.3 0.1 1 280 35 35 MET CB C 32.6 0.1 1 281 35 35 MET CG C 31.9 0.1 1 282 35 35 MET N N 122.4 0.1 1 283 36 36 VAL H H 8.39 0.01 1 284 36 36 VAL HA H 4.13 0.01 1 285 36 36 VAL HB H 2.08 0.01 1 286 36 36 VAL HG1 H 0.95 0.01 5 287 36 36 VAL CA C 62.7 0.1 1 288 36 36 VAL CB C 32.7 0.1 1 289 36 36 VAL CG1 C 20.8 0.1 5 290 36 36 VAL N N 123.0 0.1 1 291 37 37 GLY H H 8.75 0.01 1 292 37 37 GLY HA2 H 4.00 0.01 2 293 37 37 GLY CA C 45.2 0.1 1 294 37 37 GLY N N 113.7 0.1 1 295 38 38 GLY H H 8.39 0.01 1 296 38 38 GLY HA2 H 3.98 0.01 2 297 38 38 GLY CA C 45.1 0.1 1 298 38 38 GLY N N 109.1 0.1 1 299 39 39 VAL H H 8.22 0.01 1 300 39 39 VAL HA H 4.19 0.01 1 301 39 39 VAL HB H 2.09 0.01 1 302 39 39 VAL HG1 H 0.94 0.01 2 303 39 39 VAL CA C 62.5 0.1 1 304 39 39 VAL CB C 32.9 0.1 1 305 39 39 VAL CG1 C 20.9 0.1 2 306 39 39 VAL N N 120.3 0.1 1 307 40 40 VAL H H 7.97 0.01 1 308 40 40 VAL HB H 2.05 0.01 1 309 40 40 VAL HG1 H 0.90 0.01 2 310 40 40 VAL CA C 63.8 0.1 1 311 40 40 VAL CB C 33.2 0.1 1 312 40 40 VAL CG1 C 21.6 0.1 2 313 40 40 VAL CG2 C 20.2 0.1 2 314 40 40 VAL N N 128.9 0.1 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 14 '15,71,72,169,170' '16,17,73,74,171,172' '20,77,175' '41,42,97,98' '48,179' '54,197' '114,115,211,212' '116,117,213,214' '118,215' '121,218' '122,219' '123,220' '127,264' '128,265' '129,129,129,266,266,266' '130,130,130,267,267,267' '134,271' '135,272' '149,150,156,157' '186,186,186,286,286,286' '189,289' '234,247' '235,236,248,249' '237,237,237,250,250,250' '238,238,238,251,251,251' '241,254' '242,255' '243,256' stop_ save_