data_25218 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shifts of amyloid beta (1-42) peptide in aqueous solution ; _BMRB_accession_number 25218 _BMRB_flat_file_name bmr25218.str _Entry_type original _Submission_date 2014-09-11 _Accession_date 2014-09-11 _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 Walti Marielle A. . 2 Orts Julien . . 3 Vogeli Beat . . 4 Campioni Silvia . . 5 Riek Roland . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 192 "13C chemical shifts" 78 "15N chemical shifts" 42 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-03-17 original author . stop_ _Original_release_date 2015-03-17 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution NMR Studies of Recombinant Abeta(1-42): From the Presence of a Micellar Entity to Residual Beta-Sheet Structure in the Soluble Species' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25676345 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Walti Marielle A. . 2 Orts Julien . . 3 Vogeli Beat . . 4 Campioni Silvia . . 5 Riek Roland . . stop_ _Journal_abbreviation Chembiochem. _Journal_volume 16 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 659 _Page_last 669 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'amyloid beta' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity $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 amyloid_peptide _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_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 41 ILE 42 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 1.35e-18 BMRB 15775 APP_C99 100.00 122 100.00 100.00 6.42e-20 BMRB 17159 Amyloid_beta-Peptide 95.24 40 100.00 100.00 1.35e-18 BMRB 17186 Abeta 95.24 40 100.00 100.00 1.35e-18 BMRB 17764 Abeta 95.24 40 100.00 100.00 1.35e-18 BMRB 17793 Abeta(1-42) 100.00 42 100.00 100.00 7.22e-20 BMRB 17794 Abeta(1-42) 100.00 42 100.00 100.00 7.22e-20 BMRB 17795 Abeta(1-40) 95.24 40 100.00 100.00 1.35e-18 BMRB 17796 Abeta40 95.24 40 100.00 100.00 1.35e-18 BMRB 18052 Pyroglutamate_Abeta 88.10 38 100.00 100.00 2.61e-16 BMRB 18127 beta-amyloid 95.24 40 100.00 100.00 1.35e-18 BMRB 18128 beta-amyloid 95.24 40 100.00 100.00 1.35e-18 BMRB 18129 beta-amyloid 95.24 40 100.00 100.00 1.35e-18 BMRB 18131 beta-amyloid 95.24 40 100.00 100.00 1.35e-18 BMRB 19009 beta-amyloid_peptide 95.24 40 100.00 100.00 1.35e-18 BMRB 19309 amyloid_peptide 95.24 40 100.00 100.00 1.35e-18 BMRB 19393 Abeta 95.24 39 97.50 97.50 4.95e-16 BMRB 25289 amyloid_beta 95.24 39 97.50 97.50 4.95e-16 BMRB 25429 entity 100.00 42 100.00 100.00 7.22e-20 BMRB 26508 amyloid_B 95.24 40 100.00 100.00 1.35e-18 BMRB 26516 amyloid_B 95.24 40 100.00 100.00 1.35e-18 PDB 1AMB "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" 66.67 28 100.00 100.00 1.81e-10 PDB 1AMC "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" 66.67 28 100.00 100.00 1.81e-10 PDB 1AML "The Alzheimer`s Disease Amyloid A4 Peptide (Residues 1-40)" 95.24 40 100.00 100.00 1.35e-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 1.35e-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 1.43e-17 PDB 1HZ3 "Alzheimer's Disease Amyloid-Beta Peptide (Residues 10-35)" 61.90 26 100.00 100.00 2.00e-08 PDB 1IYT "Solution Structure Of The Alzheimer's Disease Amyloid Beta- Peptide (1-42)" 100.00 42 100.00 100.00 7.22e-20 PDB 1Z0Q "Aqueous Solution Structure Of The Alzheimer's Disease Abeta Peptide (1-42)" 100.00 42 100.00 100.00 7.22e-20 PDB 2BEG "3d Structure Of Alzheimer's Abeta(1-42) Fibrils" 100.00 42 100.00 100.00 7.22e-20 PDB 2G47 "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-40)" 95.24 40 100.00 100.00 1.35e-18 PDB 2LFM "A Partially Folded Structure Of Amyloid-Beta(1 40) In An Aqueous Environment" 95.24 40 100.00 100.00 1.35e-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 1.35e-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 1.35e-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 1.35e-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 1.35e-18 PDB 2LNQ "40-residue D23n Beta Amyloid Fibril" 95.24 40 97.50 100.00 4.61e-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 6.42e-20 PDB 2M4J "40-residue Beta-amyloid Fibril Derived From Alzheimer's Disease Brain" 95.24 40 100.00 100.00 1.35e-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 1.35e-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 1.35e-18 PDB 2MVX "Atomic-resolution 3d Structure Of Amyloid-beta Fibrils: The Osaka Mutation" 95.24 39 97.50 97.50 4.95e-16 PDB 2MXU "42-residue Beta Amyloid Fibril" 100.00 42 100.00 100.00 7.22e-20 PDB 2OTK "Structure Of Alzheimer Ab Peptide In Complex With An Engineered Binding Protein" 95.24 40 100.00 100.00 1.35e-18 PDB 2WK3 "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-42)" 100.00 42 100.00 100.00 7.22e-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 1.81e-10 PDB 3IFN "X-ray Structure Of Amyloid Beta Peptide:antibody (abeta1-40:12a11) Complex" 95.24 40 100.00 100.00 1.35e-18 PDB 4HIX "Crystal Structure Of A Humanised 3d6 Fab Bound To Amyloid Beta Peptide" 66.67 28 100.00 100.00 1.81e-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 1.35e-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 1.35e-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 1.35e-18 PDB 4NGE "Crystal Structure Of Human Presequence Protease In Complex With Amyloid-beta (1-40)" 95.24 40 100.00 100.00 1.35e-18 PDB 4ONG "Fab Fragment Of 3d6 In Complex With Amyloid Beta 1-40" 95.24 40 100.00 100.00 1.35e-18 PDB 5AEF "Electron Cryo-microscopy Of An Abeta(1-42)amyloid Fibril" 66.67 28 100.00 100.00 2.69e-08 DBJ BAA22264 "amyloid precursor protein [Homo sapiens]" 100.00 770 100.00 100.00 9.34e-20 DBJ BAA84580 "amyloid precursor protein [Sus scrofa]" 100.00 770 100.00 100.00 9.34e-20 DBJ BAB71958 "amyloid precursor protein [Homo sapiens]" 100.00 52 97.62 100.00 9.73e-20 DBJ BAD51938 "amyloid beta A4 precursor protein [Macaca fascicularis]" 100.00 696 100.00 100.00 8.24e-20 DBJ BAE01907 "unnamed protein product [Macaca fascicularis]" 100.00 751 100.00 100.00 9.08e-20 EMBL CAA30050 "amyloid A4 protein [Homo sapiens]" 100.00 751 100.00 100.00 9.08e-20 EMBL CAA31830 "A4 amyloid protein precursor [Homo sapiens]" 100.00 695 100.00 100.00 8.22e-20 EMBL CAA39589 "amyloid precursor protein [Bos taurus]" 100.00 59 100.00 100.00 1.94e-20 EMBL CAA39590 "amyloid precursor protein [Canis lupus familiaris]" 100.00 58 100.00 100.00 2.01e-20 EMBL CAA39591 "amyloid precursor protein [Cavia sp.]" 100.00 58 100.00 100.00 2.01e-20 GB AAA35540 "amyloid protein, partial [Homo sapiens]" 95.24 97 100.00 100.00 1.03e-18 GB AAA36829 "amyloid b-protein precursor [Macaca fascicularis]" 100.00 695 100.00 100.00 8.22e-20 GB AAA51564 "amyloid beta protein, partial [Homo sapiens]" 71.43 30 100.00 100.00 9.95e-12 GB AAA51722 "amyloid beta-protein precursor, partial [Homo sapiens]" 100.00 412 100.00 100.00 4.48e-20 GB AAA51726 "beta-amyloid A4, partial [Homo sapiens]" 100.00 264 100.00 100.00 9.55e-20 PIR A60045 "Alzheimer's disease amyloid beta/A4 protein precursor - dog (fragment)" 100.00 57 100.00 100.00 2.12e-20 PIR D60045 "Alzheimer's disease amyloid beta/A4 protein precursor - bovine (fragment)" 100.00 57 100.00 100.00 2.12e-20 PIR E60045 "Alzheimer's disease amyloid beta/A4 protein precursor - sheep (fragment)" 100.00 57 100.00 100.00 2.12e-20 PIR G60045 "Alzheimer's disease amyloid beta/A4 protein precursor - guinea pig (fragment)" 100.00 57 100.00 100.00 2.12e-20 PIR PQ0438 "Alzheimer's disease amyloid A4 protein precursor - rabbit (fragment)" 100.00 82 100.00 100.00 2.05e-20 PRF 1303338A "amyloid A4 protein precursor" 100.00 695 100.00 100.00 8.22e-20 PRF 1403400A "amyloid protein A4" 100.00 751 100.00 100.00 9.08e-20 PRF 1405204A "amyloid protein" 100.00 42 100.00 100.00 7.22e-20 PRF 1507304A "beta amyloid peptide precursor" 100.00 412 100.00 100.00 4.48e-20 PRF 1507304B "beta amyloid peptide precursor" 100.00 574 100.00 100.00 2.04e-19 REF NP_000475 "amyloid beta A4 protein isoform a precursor [Homo sapiens]" 100.00 770 100.00 100.00 9.34e-20 REF NP_001006601 "amyloid beta A4 protein isoform APP-770 precursor [Canis lupus familiaris]" 100.00 770 100.00 100.00 9.34e-20 REF NP_001013036 "amyloid beta A4 protein precursor [Pan troglodytes]" 100.00 770 100.00 100.00 9.34e-20 REF NP_001070264 "amyloid beta A4 protein precursor [Bos taurus]" 100.00 695 100.00 100.00 8.22e-20 REF NP_001127014 "amyloid beta A4 protein precursor [Pongo abelii]" 100.00 695 100.00 100.00 8.22e-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 9.34e-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 9.34e-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 9.34e-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 5.31e-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 1.94e-20 TPG DAA33655 "TPA: amyloid beta A4 protein [Bos taurus]" 100.00 695 100.00 100.00 8.22e-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 $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 'recombinant technology' . Escherichia coli . pRSET 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 $entity . mM 0.5 0.7 '[U-13C; U-15N]' H2O 90 % . . 'natural abundance' D2O 10 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_ccpNMR _Saveframe_category software _Name ccpNMR _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_aliphatic_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY aliphatic' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _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 7.4 . pH pressure 1 . atm 'ionic strength' 20 . mM 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 na indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.00 na 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 HNCA' '3D HNCACB' '3D HN(CO)CA' '2D 1H-15N HSQC' '2D 1H-1H TOCSY' '2D 1H-1H NOESY' '3D 1H-15N NOESY' '3D 1H-15N TOCSY' '3D 1H-13C NOESY aliphatic' '3D HCCH-TOCSY' 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 entity _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 CA C 53.036 0.400 1 2 1 1 ASP CB C 38.622 0.400 1 3 1 1 ASP N N 117.609 0.400 1 4 2 2 ALA H H 7.958 0.020 1 5 2 2 ALA HA H 4.161 0.020 1 6 2 2 ALA HB H 1.267 0.020 1 7 2 2 ALA CA C 52.400 0.400 1 8 2 2 ALA CB C 19.112 0.400 1 9 2 2 ALA N N 123.781 0.400 1 10 3 3 GLU H H 8.459 0.020 1 11 3 3 GLU HA H 4.073 0.020 1 12 3 3 GLU HB2 H 1.801 0.020 2 13 3 3 GLU HB3 H 2.002 0.020 2 14 3 3 GLU HG2 H 2.108 0.020 2 15 3 3 GLU HG3 H 2.108 0.020 2 16 3 3 GLU CA C 56.497 0.400 1 17 3 3 GLU CB C 30.199 0.400 1 18 3 3 GLU N N 120.309 0.400 1 19 4 4 PHE H H 8.299 0.020 1 20 4 4 PHE HA H 4.438 0.020 1 21 4 4 PHE HB2 H 2.895 0.020 2 22 4 4 PHE HB3 H 2.895 0.020 2 23 4 4 PHE CA C 57.630 0.400 1 24 4 4 PHE CB C 39.487 0.400 1 25 4 4 PHE N N 121.733 0.400 1 26 5 5 ARG H H 8.112 0.020 1 27 5 5 ARG HA H 4.162 0.020 1 28 5 5 ARG HB2 H 1.620 0.020 2 29 5 5 ARG HB3 H 1.511 0.020 2 30 5 5 ARG HG2 H 1.380 0.020 2 31 5 5 ARG HG3 H 1.380 0.020 2 32 5 5 ARG HD2 H 3.011 0.020 2 33 5 5 ARG HD3 H 3.011 0.020 2 34 5 5 ARG CA C 55.312 0.400 1 35 5 5 ARG CB C 31.109 0.400 1 36 5 5 ARG N N 123.861 0.400 1 37 6 6 HIS H H 8.379 0.020 1 38 6 6 HIS HA H 4.401 0.020 1 39 6 6 HIS HB2 H 2.923 0.020 2 40 6 6 HIS HB3 H 2.923 0.020 2 41 6 6 HIS CA C 56.478 0.400 1 42 6 6 HIS CB C 30.743 0.400 1 43 6 6 HIS N N 122.416 0.400 1 44 7 7 ASP H H 8.332 0.020 1 45 7 7 ASP HA H 4.509 0.020 1 46 7 7 ASP HB2 H 2.558 0.020 2 47 7 7 ASP HB3 H 2.558 0.020 2 48 7 7 ASP CA C 53.908 0.400 1 49 7 7 ASP CB C 40.970 0.400 1 50 7 7 ASP N N 121.615 0.400 1 51 8 8 SER H H 8.406 0.020 1 52 8 8 SER HA H 4.268 0.020 1 53 8 8 SER HB2 H 3.770 0.020 2 54 8 8 SER HB3 H 3.789 0.020 2 55 8 8 SER CA C 58.890 0.400 1 56 8 8 SER CB C 63.605 0.400 1 57 8 8 SER N N 116.526 0.400 1 58 9 9 GLY H H 8.525 0.020 1 59 9 9 GLY HA3 H 3.781 0.020 2 60 9 9 GLY CA C 45.087 0.400 1 61 9 9 GLY N N 110.656 0.400 1 62 10 10 TYR H H 7.931 0.020 1 63 10 10 TYR HA H 4.413 0.020 1 64 10 10 TYR HB2 H 2.919 0.020 2 65 10 10 TYR HB3 H 2.842 0.020 2 66 10 10 TYR CA C 58.005 0.400 1 67 10 10 TYR CB C 38.722 0.400 1 68 10 10 TYR N N 119.973 0.400 1 69 11 11 GLU H H 8.378 0.020 1 70 11 11 GLU HA H 4.087 0.020 1 71 11 11 GLU HB2 H 1.721 0.020 2 72 11 11 GLU HB3 H 1.721 0.020 2 73 11 11 GLU HG2 H 2.075 0.020 2 74 11 11 GLU HG3 H 2.075 0.020 2 75 11 11 GLU CA C 56.468 0.400 1 76 11 11 GLU CB C 30.260 0.400 1 77 11 11 GLU N N 122.553 0.400 1 78 12 12 VAL H H 8.083 0.020 1 79 12 12 VAL HA H 3.825 0.020 1 80 12 12 VAL HB H 1.830 0.020 1 81 12 12 VAL HG1 H 0.669 0.020 2 82 12 12 VAL HG2 H 0.757 0.020 2 83 12 12 VAL CA C 62.786 0.400 1 84 12 12 VAL CB C 32.485 0.400 1 85 12 12 VAL N N 121.135 0.400 1 86 13 13 HIS H H 8.246 0.020 1 87 13 13 HIS HA H 4.475 0.020 1 88 13 13 HIS HB2 H 2.903 0.020 2 89 13 13 HIS HB3 H 2.910 0.020 2 90 13 13 HIS CA C 56.193 0.400 1 91 13 13 HIS CB C 30.727 0.400 1 92 13 13 HIS N N 122.697 0.400 1 93 14 14 HIS H H 8.142 0.020 1 94 14 14 HIS HA H 4.426 0.020 1 95 14 14 HIS HB2 H 2.899 0.020 2 96 14 14 HIS HB3 H 2.972 0.020 2 97 14 14 HIS CA C 56.489 0.400 1 98 14 14 HIS CB C 30.697 0.400 1 99 14 14 HIS N N 121.248 0.400 1 100 15 15 GLN H H 8.376 0.020 1 101 15 15 GLN HA H 4.150 0.020 1 102 15 15 GLN HB2 H 1.861 0.020 2 103 15 15 GLN HB3 H 1.950 0.020 2 104 15 15 GLN HG2 H 2.215 0.020 2 105 15 15 GLN HG3 H 2.215 0.020 2 106 15 15 GLN CA C 55.883 0.400 1 107 15 15 GLN CB C 29.386 0.400 1 108 15 15 GLN N N 121.474 0.400 1 109 16 16 LYS H H 8.381 0.020 1 110 16 16 LYS HA H 4.157 0.020 1 111 16 16 LYS HB2 H 1.653 0.020 2 112 16 16 LYS HB3 H 1.690 0.020 2 113 16 16 LYS HG2 H 1.277 0.020 2 114 16 16 LYS HG3 H 1.340 0.020 2 115 16 16 LYS CA C 56.177 0.400 1 116 16 16 LYS CB C 32.691 0.400 1 117 16 16 LYS N N 122.806 0.400 1 118 17 17 LEU H H 8.257 0.020 1 119 17 17 LEU HA H 4.215 0.020 1 120 17 17 LEU HB2 H 1.496 0.020 2 121 17 17 LEU HB3 H 1.496 0.020 2 122 17 17 LEU HG H 1.338 0.020 1 123 17 17 LEU HD1 H 0.811 0.020 2 124 17 17 LEU HD2 H 0.744 0.020 2 125 17 17 LEU CA C 55.129 0.400 1 126 17 17 LEU CB C 42.348 0.400 1 127 17 17 LEU N N 123.881 0.400 1 128 18 18 VAL H H 8.002 0.020 1 129 18 18 VAL HA H 3.920 0.020 1 130 18 18 VAL HB H 1.795 0.020 1 131 18 18 VAL HG1 H 0.643 0.020 2 132 18 18 VAL HG2 H 0.734 0.020 2 133 18 18 VAL CA C 61.860 0.400 1 134 18 18 VAL CB C 33.008 0.400 1 135 18 18 VAL N N 121.466 0.400 1 136 19 19 PHE H H 8.266 0.020 1 137 19 19 PHE HA H 4.471 0.020 1 138 19 19 PHE HB2 H 2.874 0.020 2 139 19 19 PHE HB3 H 2.817 0.020 2 140 19 19 PHE CA C 57.284 0.400 1 141 19 19 PHE CB C 40.024 0.400 1 142 19 19 PHE N N 124.337 0.400 1 143 20 20 PHE H H 8.240 0.020 1 144 20 20 PHE HA H 4.467 0.020 1 145 20 20 PHE HB2 H 2.969 0.020 2 146 20 20 PHE HB3 H 2.822 0.020 2 147 20 20 PHE CA C 57.240 0.400 1 148 20 20 PHE CB C 40.030 0.400 1 149 20 20 PHE N N 122.962 0.400 1 150 21 21 ALA H H 8.250 0.020 1 151 21 21 ALA HA H 4.114 0.020 1 152 21 21 ALA HB H 1.262 0.020 1 153 21 21 ALA CA C 52.257 0.400 1 154 21 21 ALA CB C 19.266 0.400 1 155 21 21 ALA N N 126.210 0.400 1 156 22 22 GLU H H 8.365 0.020 1 157 22 22 GLU HA H 4.090 0.020 1 158 22 22 GLU HB2 H 1.931 0.020 2 159 22 22 GLU HB3 H 1.814 0.020 2 160 22 22 GLU HG2 H 2.167 0.020 2 161 22 22 GLU HG3 H 2.167 0.020 2 162 22 22 GLU CA C 56.482 0.400 1 163 22 22 GLU CB C 30.240 0.400 1 164 22 22 GLU N N 119.907 0.400 1 165 23 23 ASP H H 8.430 0.020 1 166 23 23 ASP HA H 4.534 0.020 1 167 23 23 ASP HB2 H 2.533 0.020 2 168 23 23 ASP HB3 H 2.641 0.020 2 169 23 23 ASP CA C 54.008 0.400 1 170 23 23 ASP CB C 40.949 0.400 1 171 23 23 ASP N N 121.769 0.400 1 172 24 24 VAL H H 8.168 0.020 1 173 24 24 VAL HA H 4.027 0.020 1 174 24 24 VAL HB H 2.084 0.020 1 175 24 24 VAL HG1 H 0.850 0.020 2 176 24 24 VAL HG2 H 0.850 0.020 2 177 24 24 VAL CA C 62.644 0.400 1 178 24 24 VAL CB C 32.069 0.400 1 179 24 24 VAL N N 120.648 0.400 1 180 25 25 GLY H H 8.555 0.020 1 181 25 25 GLY HA2 H 3.866 0.020 2 182 25 25 GLY HA3 H 3.866 0.020 2 183 25 25 GLY CA C 45.241 0.400 1 184 25 25 GLY N N 111.702 0.400 1 185 26 26 SER H H 8.148 0.020 1 186 26 26 SER HA H 4.312 0.020 1 187 26 26 SER HB2 H 3.786 0.020 2 188 26 26 SER HB3 H 3.786 0.020 2 189 26 26 SER CA C 58.441 0.400 1 190 26 26 SER CB C 63.557 0.400 1 191 26 26 SER N N 115.416 0.400 1 192 27 27 ASN H H 8.481 0.020 1 193 27 27 ASN HA H 4.308 0.020 1 194 27 27 ASN HB2 H 2.764 0.020 2 195 27 27 ASN HB3 H 2.705 0.020 2 196 27 27 ASN CA C 53.166 0.400 1 197 27 27 ASN CB C 38.418 0.400 1 198 27 27 ASN N N 120.661 0.400 1 199 28 28 LYS H H 8.360 0.020 1 200 28 28 LYS HA H 4.161 0.020 1 201 28 28 LYS HB2 H 1.779 0.020 2 202 28 28 LYS HB3 H 1.669 0.020 2 203 28 28 LYS HG2 H 1.334 0.020 2 204 28 28 LYS HG3 H 1.334 0.020 2 205 28 28 LYS HD2 H 1.311 0.020 2 206 28 28 LYS HD3 H 1.311 0.020 2 207 28 28 LYS CA C 56.456 0.400 1 208 28 28 LYS CB C 32.523 0.400 1 209 28 28 LYS N N 121.692 0.400 1 210 29 29 GLY H H 8.424 0.020 1 211 29 29 GLY HA2 H 3.819 0.020 2 212 29 29 GLY HA3 H 3.819 0.020 2 213 29 29 GLY CA C 45.034 0.400 1 214 29 29 GLY N N 109.500 0.400 1 215 30 30 ALA H H 8.031 0.020 1 216 30 30 ALA HA H 4.194 0.020 1 217 30 30 ALA HB H 1.262 0.020 1 218 30 30 ALA CA C 52.379 0.400 1 219 30 30 ALA CB C 19.339 0.400 1 220 30 30 ALA N N 123.448 0.400 1 221 31 31 ILE H H 8.183 0.020 1 222 31 31 ILE HA H 4.045 0.020 1 223 31 31 ILE HB H 1.756 0.020 1 224 31 31 ILE HG12 H 1.400 0.020 2 225 31 31 ILE HG13 H 1.095 0.020 2 226 31 31 ILE HG2 H 0.814 0.020 1 227 31 31 ILE HD1 H 0.771 0.020 1 228 31 31 ILE CA C 60.988 0.400 1 229 31 31 ILE CB C 38.310 0.400 1 230 31 31 ILE N N 120.685 0.400 1 231 32 32 ILE H H 8.331 0.020 1 232 32 32 ILE HA H 4.045 0.020 1 233 32 32 ILE HB H 1.756 0.020 1 234 32 32 ILE HG12 H 1.395 0.020 2 235 32 32 ILE HG13 H 1.395 0.020 2 236 32 32 ILE HG2 H 1.102 0.020 1 237 32 32 ILE HD1 H 0.772 0.020 1 238 32 32 ILE CA C 61.005 0.400 1 239 32 32 ILE CB C 38.319 0.400 1 240 32 32 ILE N N 126.300 0.400 1 241 33 33 GLY H H 8.488 0.020 1 242 33 33 GLY HA2 H 3.824 0.020 2 243 33 33 GLY HA3 H 3.824 0.020 2 244 33 33 GLY CA C 45.022 0.400 1 245 33 33 GLY N N 113.019 0.400 1 246 34 34 LEU H H 8.062 0.020 1 247 34 34 LEU HA H 4.244 0.020 1 248 34 34 LEU HB2 H 1.503 0.020 2 249 34 34 LEU HB3 H 1.492 0.020 2 250 34 34 LEU HD1 H 0.816 0.020 2 251 34 34 LEU HD2 H 0.761 0.020 2 252 34 34 LEU CA C 54.906 0.400 1 253 34 34 LEU CB C 42.510 0.400 1 254 34 34 LEU N N 121.624 0.400 1 255 35 35 MET H H 8.434 0.020 1 256 35 35 MET HA H 4.522 0.020 1 257 35 35 MET HB2 H 1.900 0.020 2 258 35 35 MET HB3 H 1.900 0.020 2 259 35 35 MET HG2 H 2.351 0.020 2 260 35 35 MET HG3 H 2.443 0.020 2 261 35 35 MET CA C 54.987 0.400 1 262 35 35 MET CB C 33.026 0.400 1 263 35 35 MET N N 121.961 0.400 1 264 36 36 VAL H H 8.340 0.020 1 265 36 36 VAL HA H 4.028 0.020 1 266 36 36 VAL HB H 1.936 0.020 1 267 36 36 VAL HG1 H 0.837 0.020 2 268 36 36 VAL HG2 H 0.837 0.020 2 269 36 36 VAL CA C 62.497 0.400 1 270 36 36 VAL CB C 33.022 0.400 1 271 36 36 VAL N N 122.813 0.400 1 272 37 37 GLY H H 8.758 0.020 1 273 37 37 GLY HA2 H 3.856 0.020 2 274 37 37 GLY HA3 H 3.856 0.020 2 275 37 37 GLY CA C 45.249 0.400 1 276 37 37 GLY N N 114.223 0.400 1 277 38 38 GLY H H 8.326 0.020 1 278 38 38 GLY HA2 H 3.850 0.020 2 279 38 38 GLY HA3 H 3.850 0.020 2 280 38 38 GLY CA C 45.077 0.400 1 281 38 38 GLY N N 107.850 0.400 1 282 39 39 VAL H H 7.923 0.020 1 283 39 39 VAL HA H 4.054 0.020 1 284 39 39 VAL HB H 1.933 0.020 1 285 39 39 VAL HG1 H 0.818 0.020 2 286 39 39 VAL HG2 H 0.818 0.020 2 287 39 39 VAL CA C 61.855 0.400 1 288 39 39 VAL CB C 33.112 0.400 1 289 39 39 VAL N N 119.768 0.400 1 290 40 40 VAL H H 8.416 0.020 1 291 40 40 VAL HA H 4.042 0.020 1 292 40 40 VAL HB H 1.888 0.020 1 293 40 40 VAL HG1 H 0.824 0.020 2 294 40 40 VAL HG2 H 0.824 0.020 2 295 40 40 VAL CA C 62.473 0.400 1 296 40 40 VAL CB C 32.512 0.400 1 297 40 40 VAL N N 126.149 0.400 1 298 41 41 ILE H H 8.462 0.020 1 299 41 41 ILE HA H 4.023 0.020 1 300 41 41 ILE HB H 1.777 0.020 1 301 41 41 ILE HG12 H 1.385 0.020 2 302 41 41 ILE HG13 H 1.100 0.020 2 303 41 41 ILE HD1 H 0.782 0.020 1 304 41 41 ILE CA C 60.700 0.400 1 305 41 41 ILE CB C 38.287 0.400 1 306 41 41 ILE N N 127.666 0.400 1 307 42 42 ALA H H 8.045 0.020 1 308 42 42 ALA HA H 4.037 0.020 1 309 42 42 ALA HB H 1.231 0.020 1 310 42 42 ALA CA C 53.735 0.400 1 311 42 42 ALA CB C 20.211 0.400 1 312 42 42 ALA N N 134.150 0.400 1 stop_ save_