data_17794 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone chemical shift assignments for Ab42 with Met35 in its reduced state ; _BMRB_accession_number 17794 _BMRB_flat_file_name bmr17794.str _Entry_type original _Submission_date 2011-07-20 _Accession_date 2011-07-20 _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 Zagorski Michael . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 85 "13C chemical shifts" 77 "15N chemical shifts" 39 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-08-26 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 17793 'Abeta(1-42) oxidised' 17795 'Abeta(1-40) oxidised' 17796 'Abeta(1-40) reduced' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution NMR Studies of the Ab(1-40) and Ab(1-42) Peptides Establish that the Met35 Oxidation State Affects the Mechanism of Amyloid Formation' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14971932 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hou Liming . . 2 Shao Haiyan . . 3 Zhang Yongbo . . 4 Li Hua . . 5 Menon Nanda K. . 6 Neuhaus Elizabeth B. . 7 Brewer John M. . 8 Byeon In-Ja L. . 9 Ray Dale G. . 10 Vitek Michael P. . 11 Takashi Iwashita . . 12 Makula Ronald A. . 13 Przybyla Alan B. . 14 Zagorski Michael G. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_volume 126 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1992 _Page_last 2005 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Abeta(1-42) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Abeta(1-42) $Abeta(1-42) 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_Abeta(1-42) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Abeta(1-42) _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 42 _Mol_residue_sequence ; DAEFRHDSGYEVHHQKLVFF AEDVGSNKGAIIGLMVGGVV IA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ASP 2 2 ALA 3 3 GLU 4 4 PHE 5 5 ARG 6 6 HIS 7 7 ASP 8 8 SER 9 9 GLY 10 10 TYR 11 11 GLU 12 12 VAL 13 13 HIS 14 14 HIS 15 15 GLN 16 16 LYS 17 17 LEU 18 18 VAL 19 19 PHE 20 20 PHE 21 21 ALA 22 22 GLU 23 23 ASP 24 24 VAL 25 25 GLY 26 26 SER 27 27 ASN 28 28 LYS 29 29 GLY 30 30 ALA 31 31 ILE 32 32 ILE 33 33 GLY 34 34 LEU 35 35 MET 36 36 VAL 37 37 GLY 38 38 GLY 39 39 VAL 40 40 VAL 41 41 ILE 42 42 ALA 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) 95.24 40 100.00 100.00 1.31e-18 BMRB 15775 APP_C99 100.00 122 100.00 100.00 6.25e-20 BMRB 17159 Amyloid_beta-Peptide 95.24 40 100.00 100.00 1.31e-18 BMRB 17186 Abeta 95.24 40 100.00 100.00 1.31e-18 BMRB 17764 Abeta 95.24 40 100.00 100.00 1.31e-18 BMRB 17793 Abeta(1-42) 100.00 42 100.00 100.00 7.03e-20 BMRB 17795 Abeta(1-40) 95.24 40 100.00 100.00 1.31e-18 BMRB 17796 Abeta40 95.24 40 100.00 100.00 1.31e-18 BMRB 18052 Pyroglutamate_Abeta 88.10 38 100.00 100.00 2.54e-16 BMRB 18127 beta-amyloid 95.24 40 100.00 100.00 1.31e-18 BMRB 18128 beta-amyloid 95.24 40 100.00 100.00 1.31e-18 BMRB 18129 beta-amyloid 95.24 40 100.00 100.00 1.31e-18 BMRB 18131 beta-amyloid 95.24 40 100.00 100.00 1.31e-18 BMRB 19009 beta-amyloid_peptide 95.24 40 100.00 100.00 1.31e-18 BMRB 19309 amyloid_peptide 95.24 40 100.00 100.00 1.31e-18 BMRB 19393 Abeta 95.24 39 97.50 97.50 4.82e-16 BMRB 25218 amyloid_peptide 100.00 42 100.00 100.00 7.03e-20 BMRB 25289 amyloid_beta 95.24 39 97.50 97.50 4.82e-16 BMRB 25429 entity 100.00 42 100.00 100.00 7.03e-20 BMRB 26508 amyloid_B 95.24 40 100.00 100.00 1.31e-18 BMRB 26516 amyloid_B 95.24 40 100.00 100.00 1.31e-18 PDB 1AMB "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" 66.67 28 100.00 100.00 1.76e-10 PDB 1AMC "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" 66.67 28 100.00 100.00 1.76e-10 PDB 1AML "The Alzheimer`s Disease Amyloid A4 Peptide (Residues 1-40)" 95.24 40 100.00 100.00 1.31e-18 PDB 1BA4 "The Solution Structure Of Amyloid Beta-Peptide (1-40) In A Water-Micelle Environment. Is The Membrane-Spanning Domain Where We " 95.24 40 100.00 100.00 1.31e-18 PDB 1BA6 "Solution Structure Of The Methionine-Oxidized Amyloid Beta- Peptide (1-40). Does Oxidation Affect Conformational Switching? Nmr" 95.24 40 97.50 97.50 1.40e-17 PDB 1HZ3 "Alzheimer's Disease Amyloid-Beta Peptide (Residues 10-35)" 61.90 26 100.00 100.00 1.95e-08 PDB 1IYT "Solution Structure Of The Alzheimer's Disease Amyloid Beta- Peptide (1-42)" 100.00 42 100.00 100.00 7.03e-20 PDB 1Z0Q "Aqueous Solution Structure Of The Alzheimer's Disease Abeta Peptide (1-42)" 100.00 42 100.00 100.00 7.03e-20 PDB 2BEG "3d Structure Of Alzheimer's Abeta(1-42) Fibrils" 100.00 42 100.00 100.00 7.03e-20 PDB 2G47 "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-40)" 95.24 40 100.00 100.00 1.31e-18 PDB 2LFM "A Partially Folded Structure Of Amyloid-Beta(1 40) In An Aqueous Environment" 95.24 40 100.00 100.00 1.31e-18 PDB 2LMN "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Positive Stagger" 95.24 40 100.00 100.00 1.31e-18 PDB 2LMO "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Negative Stagger" 95.24 40 100.00 100.00 1.31e-18 PDB 2LMP "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Positive Stagger" 95.24 40 100.00 100.00 1.31e-18 PDB 2LMQ "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Negative Stagger" 95.24 40 100.00 100.00 1.31e-18 PDB 2LNQ "40-residue D23n Beta Amyloid Fibril" 95.24 40 97.50 100.00 4.49e-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 6.25e-20 PDB 2M4J "40-residue Beta-amyloid Fibril Derived From Alzheimer's Disease Brain" 95.24 40 100.00 100.00 1.31e-18 PDB 2M9R "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" 95.24 40 100.00 100.00 1.31e-18 PDB 2M9S "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" 95.24 40 100.00 100.00 1.31e-18 PDB 2MVX "Atomic-resolution 3d Structure Of Amyloid-beta Fibrils: The Osaka Mutation" 95.24 39 97.50 97.50 4.82e-16 PDB 2MXU "42-residue Beta Amyloid Fibril" 100.00 42 100.00 100.00 7.03e-20 PDB 2OTK "Structure Of Alzheimer Ab Peptide In Complex With An Engineered Binding Protein" 95.24 40 100.00 100.00 1.31e-18 PDB 2WK3 "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-42)" 100.00 42 100.00 100.00 7.03e-20 PDB 3BAE "Crystal Structure Of Fab Wo2 Bound To The N Terminal Domain Of Amyloid Beta Peptide (1-28)" 66.67 28 100.00 100.00 1.76e-10 PDB 3IFN "X-ray Structure Of Amyloid Beta Peptide:antibody (abeta1-40:12a11) Complex" 95.24 40 100.00 100.00 1.31e-18 PDB 4HIX "Crystal Structure Of A Humanised 3d6 Fab Bound To Amyloid Beta Peptide" 66.67 28 100.00 100.00 1.76e-10 PDB 4M1C "Crystal Structure Analysis Of Fab-bound Human Insulin Degrading Enzyme (ide) In Complex With Amyloid-beta (1-40)" 95.24 40 100.00 100.00 1.31e-18 PDB 4MVI "Crystal Structure Of An Engineered Lipocalin (anticalin Us7) In Complex With The Alzheimer Amyloid Peptide Abeta(1-40)" 95.24 40 100.00 100.00 1.31e-18 PDB 4MVL "Crystal Structure Of An Engineered Lipocalin (anticalin H1ga) In Complex With The Alzheimer Amyloid Peptide Abeta1-40" 95.24 40 100.00 100.00 1.31e-18 PDB 4NGE "Crystal Structure Of Human Presequence Protease In Complex With Amyloid-beta (1-40)" 95.24 40 100.00 100.00 1.31e-18 PDB 4ONG "Fab Fragment Of 3d6 In Complex With Amyloid Beta 1-40" 95.24 40 100.00 100.00 1.31e-18 PDB 5AEF "Electron Cryo-microscopy Of An Abeta(1-42)amyloid Fibril" 66.67 28 100.00 100.00 2.62e-08 DBJ BAA22264 "amyloid precursor protein [Homo sapiens]" 100.00 770 100.00 100.00 9.10e-20 DBJ BAA84580 "amyloid precursor protein [Sus scrofa]" 100.00 770 100.00 100.00 9.10e-20 DBJ BAB71958 "amyloid precursor protein [Homo sapiens]" 100.00 52 97.62 100.00 9.48e-20 DBJ BAD51938 "amyloid beta A4 precursor protein [Macaca fascicularis]" 100.00 696 100.00 100.00 8.02e-20 DBJ BAE01907 "unnamed protein product [Macaca fascicularis]" 100.00 751 100.00 100.00 8.84e-20 EMBL CAA30050 "amyloid A4 protein [Homo sapiens]" 100.00 751 100.00 100.00 8.84e-20 EMBL CAA31830 "A4 amyloid protein precursor [Homo sapiens]" 100.00 695 100.00 100.00 8.01e-20 EMBL CAA39589 "amyloid precursor protein [Bos taurus]" 100.00 59 100.00 100.00 1.89e-20 EMBL CAA39590 "amyloid precursor protein [Canis lupus familiaris]" 100.00 58 100.00 100.00 1.96e-20 EMBL CAA39591 "amyloid precursor protein [Cavia sp.]" 100.00 58 100.00 100.00 1.96e-20 GB AAA35540 "amyloid protein, partial [Homo sapiens]" 95.24 97 100.00 100.00 1.00e-18 GB AAA36829 "amyloid b-protein precursor [Macaca fascicularis]" 100.00 695 100.00 100.00 8.01e-20 GB AAA51564 "amyloid beta protein, partial [Homo sapiens]" 71.43 30 100.00 100.00 9.69e-12 GB AAA51722 "amyloid beta-protein precursor, partial [Homo sapiens]" 100.00 412 100.00 100.00 4.36e-20 GB AAA51726 "beta-amyloid A4, partial [Homo sapiens]" 100.00 264 100.00 100.00 9.30e-20 PIR A60045 "Alzheimer's disease amyloid beta/A4 protein precursor - dog (fragment)" 100.00 57 100.00 100.00 2.06e-20 PIR D60045 "Alzheimer's disease amyloid beta/A4 protein precursor - bovine (fragment)" 100.00 57 100.00 100.00 2.06e-20 PIR E60045 "Alzheimer's disease amyloid beta/A4 protein precursor - sheep (fragment)" 100.00 57 100.00 100.00 2.06e-20 PIR G60045 "Alzheimer's disease amyloid beta/A4 protein precursor - guinea pig (fragment)" 100.00 57 100.00 100.00 2.06e-20 PIR PQ0438 "Alzheimer's disease amyloid A4 protein precursor - rabbit (fragment)" 100.00 82 100.00 100.00 1.99e-20 PRF 1303338A "amyloid A4 protein precursor" 100.00 695 100.00 100.00 8.01e-20 PRF 1403400A "amyloid protein A4" 100.00 751 100.00 100.00 8.84e-20 PRF 1405204A "amyloid protein" 100.00 42 100.00 100.00 7.03e-20 PRF 1507304A "beta amyloid peptide precursor" 100.00 412 100.00 100.00 4.36e-20 PRF 1507304B "beta amyloid peptide precursor" 100.00 574 100.00 100.00 1.99e-19 REF NP_000475 "amyloid beta A4 protein isoform a precursor [Homo sapiens]" 100.00 770 100.00 100.00 9.10e-20 REF NP_001006601 "amyloid beta A4 protein isoform APP-770 precursor [Canis lupus familiaris]" 100.00 770 100.00 100.00 9.10e-20 REF NP_001013036 "amyloid beta A4 protein precursor [Pan troglodytes]" 100.00 770 100.00 100.00 9.10e-20 REF NP_001070264 "amyloid beta A4 protein precursor [Bos taurus]" 100.00 695 100.00 100.00 8.01e-20 REF NP_001127014 "amyloid beta A4 protein precursor [Pongo abelii]" 100.00 695 100.00 100.00 8.01e-20 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 9.10e-20 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 9.10e-20 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 9.10e-20 SP P86906 "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" 95.24 40 97.50 100.00 5.17e-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 1.89e-20 TPG DAA33655 "TPA: amyloid beta A4 protein [Bos taurus]" 100.00 695 100.00 100.00 8.01e-20 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Abeta(1-42) 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 $Abeta(1-42) 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Abeta(1-42) . mM 0.2 0.3 '[U-95% 15N]' H2O 90 % . . 'natural abundance' D2O 10 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNHA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _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 temperature 273 . K pH 7.2 . pH pressure 1 . atm 'ionic strength' 0.01 . M 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 H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS C 13 'methyl protons' ppm 0.00 n/a indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.00 n/a 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 '3D HNCACB' '3D HNHA' 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 Abeta(1-42) _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 4.19 . 1 2 1 1 ASP CA C 52.49 . 1 3 2 2 ALA H H 8.17 . 1 4 2 2 ALA HA H 4.29 . 1 5 2 2 ALA CA C 52.90 . 1 6 2 2 ALA CB C 19.27 . 1 7 2 2 ALA N N 123.70 . 1 8 3 3 GLU H H 8.60 . 1 9 3 3 GLU HA H 4.19 . 1 10 3 3 GLU CA C 56.72 . 1 11 3 3 GLU CB C 30.36 . 1 12 3 3 GLU N N 120.50 . 1 13 4 4 PHE H H 8.47 . 1 14 4 4 PHE HA H 4.56 . 1 15 4 4 PHE CA C 58.03 . 1 16 4 4 PHE CB C 39.67 . 1 17 4 4 PHE N N 122.10 . 1 18 5 5 ARG H H 8.28 . 1 19 5 5 ARG HA H 4.26 . 1 20 5 5 ARG CA C 55.65 . 1 21 5 5 ARG CB C 31.37 . 1 22 5 5 ARG N N 124.20 . 1 23 6 6 HIS CA C 56.96 . 1 24 6 6 HIS CB C 31.25 . 1 25 7 7 ASP H H 8.49 . 1 26 7 7 ASP HA H 4.63 . 1 27 7 7 ASP CA C 54.35 . 1 28 7 7 ASP CB C 41.22 . 1 29 7 7 ASP N N 121.80 . 1 30 8 8 SER H H 8.57 . 1 31 8 8 SER HA H 4.38 . 1 32 8 8 SER CA C 59.26 . 1 33 8 8 SER CB C 63.83 . 1 34 8 8 SER N N 116.80 . 1 35 9 9 GLY H H 8.67 . 1 36 9 9 GLY HA2 H 3.88 . . 37 9 9 GLY HA3 H 3.95 . 2 38 9 9 GLY CA C 45.33 . 1 39 9 9 GLY N N 110.80 . 1 40 10 10 TYR H H 8.07 . 1 41 10 10 TYR HA H 4.51 . 1 42 10 10 TYR CA C 58.30 . 1 43 10 10 TYR CB C 38.88 . 1 44 10 10 TYR N N 120.10 . 1 45 11 11 GLU H H 8.51 . 1 46 11 11 GLU HA H 4.17 . 1 47 11 11 GLU CA C 56.69 . 1 48 11 11 GLU CB C 30.44 . 1 49 11 11 GLU N N 122.70 . 1 50 12 12 VAL H H 8.23 . 1 51 12 12 VAL HA H 3.92 . 1 52 12 12 VAL CA C 63.05 . 1 53 12 12 VAL CB C 32.55 . 1 54 12 12 VAL N N 121.40 . 1 55 13 13 HIS H H 8.40 . 1 56 13 13 HIS HA H 4.59 . 1 57 13 13 HIS CA C 56.62 . 1 58 13 13 HIS CB C 31.09 . 1 59 13 13 HIS N N 122.80 . 1 60 14 14 HIS CA C 56.04 . 1 61 14 14 HIS CB C 30.66 . 1 62 15 15 GLN H H 8.53 . 1 63 15 15 GLN HA H 4.27 . 1 64 15 15 GLN CA C 56.27 . 1 65 15 15 GLN CB C 29.45 . 1 66 15 15 GLN N N 121.60 . 1 67 16 16 LYS H H 8.54 . 1 68 16 16 LYS HA H 4.27 . 1 69 16 16 LYS CA C 56.54 . 1 70 16 16 LYS CB C 33.11 . 1 71 16 16 LYS N N 123.30 . 1 72 17 17 LEU H H 8.43 . 1 73 17 17 LEU HA H 4.33 . 1 74 17 17 LEU CA C 55.23 . 1 75 17 17 LEU CB C 42.44 . 1 76 17 17 LEU N N 124.10 . 1 77 18 18 VAL H H 8.15 . 1 78 18 18 VAL HA H 4.03 . 1 79 18 18 VAL CA C 62.18 . 1 80 18 18 VAL CB C 33.24 . 1 81 18 18 VAL N N 121.80 . 1 82 19 19 PHE H H 8.43 . 1 83 19 19 PHE HA H 4.59 . 1 84 19 19 PHE CA C 57.73 . 1 85 19 19 PHE CB C 40.26 . 1 86 19 19 PHE N N 124.80 . 1 87 20 20 PHE H H 8.38 . 1 88 20 20 PHE HA H 4.57 . 1 89 20 20 PHE CA C 57.62 . 1 90 20 20 PHE CB C 40.18 . 1 91 20 20 PHE N N 123.30 . 1 92 21 21 ALA H H 8.39 . 1 93 21 21 ALA HA H 4.22 . 1 94 21 21 ALA CA C 52.61 . 1 95 21 21 ALA CB C 19.52 . 1 96 21 21 ALA N N 126.40 . 1 97 22 22 GLU H H 8.50 . 1 98 22 22 GLU HA H 4.19 . 1 99 22 22 GLU CA C 56.71 . 1 100 22 22 GLU CB C 30.48 . 1 101 22 22 GLU N N 120.30 . 1 102 23 23 ASP H H 8.58 . 1 103 23 23 ASP HA H 4.64 . 1 104 23 23 ASP CA C 54.35 . 1 105 23 23 ASP CB C 41.21 . 1 106 23 23 ASP N N 121.80 . 1 107 24 24 VAL H H 8.33 . 1 108 24 24 VAL HA H 4.15 . 1 109 24 24 VAL CA C 62.97 . 1 110 24 24 VAL CB C 32.28 . 1 111 24 24 VAL N N 121.10 . 1 112 25 25 GLY H H 8.70 . 1 113 25 25 GLY HA2 H 4.00 . . 114 25 25 GLY HA3 H 4.00 . 2 115 25 25 GLY CA C 45.57 . 1 116 25 25 GLY N N 111.90 . 1 117 26 26 SER H H 8.28 . 1 118 26 26 SER HA H 4.43 . 1 119 26 26 SER CA C 58.47 . 1 120 26 26 SER CB C 63.94 . 1 121 26 26 SER N N 115.60 . 1 122 27 27 ASN H H 8.63 . 1 123 27 27 ASN HA H 4.75 . 1 124 27 27 ASN CA C 53.39 . 1 125 27 27 ASN CB C 38.55 . 1 126 27 27 ASN N N 120.60 . 1 127 28 28 LYS H H 8.51 . 1 128 28 28 LYS HA H 4.28 . 1 129 28 28 LYS CA C 56.80 . 1 130 28 28 LYS CB C 32.64 . 1 131 28 28 LYS N N 122.00 . 1 132 29 29 GLY H H 8.57 . 1 133 29 29 GLY HA2 H 3.94 . . 134 29 29 GLY HA3 H 3.94 . 2 135 29 29 GLY CA C 45.25 . 1 136 29 29 GLY N N 109.70 . 1 137 30 30 ALA H H 8.17 . 1 138 30 30 ALA HA H 4.31 . 1 139 30 30 ALA CA C 52.69 . 1 140 30 30 ALA CB C 19.37 . 1 141 30 30 ALA N N 123.70 . 1 142 31 31 ILE H H 8.35 . 1 143 31 31 ILE HA H 4.16 . 1 144 31 31 ILE CA C 61.38 . 1 145 31 31 ILE CB C 38.46 . 1 146 31 31 ILE N N 121.10 . 1 147 32 32 ILE H H 8.49 . 1 148 32 32 ILE HA H 4.17 . 1 149 32 32 ILE CA C 61.19 . 1 150 32 32 ILE CB C 38.64 . 1 151 32 32 ILE N N 126.80 . 1 152 33 33 GLY H H 8.65 . 1 153 33 33 GLY HA2 H 3.94 . . 154 33 33 GLY HA3 H 3.94 . 2 155 33 33 GLY CA C 45.23 . 1 156 33 33 GLY N N 113.40 . 1 157 34 34 LEU H H 8.21 . 1 158 34 34 LEU HA H 4.37 . 1 159 34 34 LEU CA C 55.11 . 1 160 34 34 LEU CB C 42.87 . 1 161 34 34 LEU N N 121.90 . 1 162 35 35 MET H H 8.59 . 1 163 35 35 MET HA H 4.64 . 1 164 35 35 MET CA C 55.37 . 1 165 35 35 MET CB C 33.29 . 1 166 35 35 MET N N 121.80 . 1 167 36 36 VAL H H 8.51 . 1 168 36 36 VAL HA H 4.15 . 1 169 36 36 VAL CA C 62.84 . 1 170 36 36 VAL CB C 32.86 . 1 171 36 36 VAL N N 123.10 . 1 172 37 37 GLY H H 8.85 . 1 173 37 37 GLY HA2 H 3.98 . . 174 37 37 GLY HA3 H 3.98 . 2 175 37 37 GLY CA C 45.66 . 1 176 37 37 GLY N N 114.20 . 1 177 38 38 GLY H H 8.46 . 1 178 38 38 GLY HA2 H 3.96 . . 179 38 38 GLY HA3 H 3.96 . 2 180 38 38 GLY CA C 45.09 . 1 181 38 38 GLY N N 108.10 . 1 182 39 39 VAL H H 8.07 . 1 183 39 39 VAL HA H 4.17 . 1 184 39 39 VAL CA C 62.16 . 1 185 39 39 VAL CB C 33.31 . 1 186 39 39 VAL N N 119.70 . 1 187 40 40 VAL H H 8.57 . 1 188 40 40 VAL HA H 4.13 . 1 189 40 40 VAL CA C 62.73 . 1 190 40 40 VAL CB C 32.78 . 1 191 40 40 VAL N N 126.60 . 1 192 41 41 ILE H H 8.61 . 1 193 41 41 ILE HA H 4.17 . 1 194 41 41 ILE CA C 61.15 . 1 195 41 41 ILE CB C 38.50 . 1 196 41 41 ILE N N 128.00 . 1 197 42 42 ALA H H 8.21 . 1 198 42 42 ALA HA H 4.13 . 1 199 42 42 ALA CA C 54.04 . 1 200 42 42 ALA CB C 20.46 . 1 201 42 42 ALA N N 136.00 . 1 stop_ save_