data_17159 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignment of the affibody-bound amyloid B-peptide ; _BMRB_accession_number 17159 _BMRB_flat_file_name bmr17159.str _Entry_type original _Submission_date 2010-08-31 _Accession_date 2010-08-31 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Amyloid B-peptide bound to the N-terminally truncated Affibody ZAB3' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lindgren Joel . . 2 Wahlstrom Anna . . 3 Danielsson Jens . . 4 Markova Natalia . . 5 Ekblad Caroline . . 6 Graslund Astrid . . 7 Abrahmsen Lars . . 8 Karlstrom Amelie . . 9 Warmlander Sebastian . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 35 "13C chemical shifts" 70 "15N chemical shifts" 35 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-12-01 update BMRB 'Update entry citation' 2010-10-05 update BMRB 'Update entry citation' 2010-09-16 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'N-terminal engineering of amyloid--binding Affibody molecules yields improved chemical synthesis and higher binding affinity.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20886513 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lindgren Joel . . 2 Wahlstrom Anna . . 3 Danielsson Jens . . 4 Markova Natalia . . 5 Ekblad Caroline . . 6 Graslund Astrid . . 7 Abrahmsen Lars . . 8 Karlstrom 'Amelie Eriksson' . . 9 Warmlander 'Sebastian K T S' . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein science : a publication of the Protein Society' _Journal_volume 19 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2319 _Page_last 2329 _Year 2010 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Affibody_Abeta _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Amyloid beta-Peptide' $Amyloid_beta-Peptide stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'Two affibody molecules bound to one Amyloid beta-peptide' save_ ######################## # Monomeric polymers # ######################## save_Amyloid_beta-Peptide _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Amyloid_beta-Peptide _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 11435 Amyloid-beta-(1-40) 100.00 40 100.00 100.00 1.44e-18 BMRB 15775 APP_C99 100.00 122 100.00 100.00 1.16e-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-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_beta-Peptide 'recombinant technology' . Escherichia coli . NA stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'Amyloid beta peptide bound to the Affibody ZAB3 molecule' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Amyloid_beta-Peptide 0.29 mM '[U-13C; U-15N]' 'sodium phosphate' 10 mM 'natural abundance' DSS 0.1 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 processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details 'equipped with a cryogenically cooled probehead' 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_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _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_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HCACO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCACO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 10 . mM pH 7.4 0.1 pH pressure 1 . atm temperature 298 1 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 protons' ppm 0 internal indirect . . . 0.25145 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0 internal indirect . . . 0.10133 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' '3D HNCO' '3D HN(CO)CA' '3D HNCA' '3D HCACO' 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 3 3 GLU H H 8.358 0.004 1 2 3 3 GLU C C 176.028 0.004 1 3 3 3 GLU CA C 56.674 0.003 1 4 3 3 GLU N N 120.146 0.009 1 5 4 4 PHE H H 8.180 0.000 1 6 4 4 PHE C C 175.254 0.021 1 7 4 4 PHE CA C 57.638 0.008 1 8 4 4 PHE N N 121.452 0.006 1 9 5 5 ARG H H 8.049 0.001 1 10 5 5 ARG C C 175.566 0.006 1 11 5 5 ARG CA C 55.586 0.006 1 12 5 5 ARG N N 123.404 0.033 1 13 7 7 ASP H H 8.266 0.001 1 14 7 7 ASP C C 175.053 0.021 1 15 7 7 ASP CA C 54.177 0.006 1 16 7 7 ASP N N 121.553 0.007 1 17 8 8 SER H H 8.279 0.002 1 18 8 8 SER C C 175.080 0.006 1 19 8 8 SER CA C 58.971 0.003 1 20 8 8 SER N N 116.252 0.008 1 21 9 9 GLY H H 8.422 0.004 1 22 9 9 GLY C C 173.923 0.014 1 23 9 9 GLY CA C 45.368 0.052 1 24 9 9 GLY N N 110.539 0.026 1 25 10 10 TYR H H 7.861 0.001 1 26 10 10 TYR C C 175.618 0.007 1 27 10 10 TYR CA C 58.002 0.020 1 28 10 10 TYR N N 119.831 0.009 1 29 11 11 GLU H H 8.276 0.001 1 30 11 11 GLU C C 176.039 0.025 1 31 11 11 GLU CA C 56.484 0.001 1 32 11 11 GLU N N 122.438 0.004 1 33 12 12 VAL H H 7.945 0.001 1 34 12 12 VAL C C 175.713 0.033 1 35 12 12 VAL CA C 62.483 0.008 1 36 12 12 VAL N N 120.612 0.024 1 37 13 13 HIS H H 8.187 0.007 1 38 13 13 HIS C C 174.969 0.006 1 39 13 13 HIS CA C 55.944 0.006 1 40 13 13 HIS N N 122.351 0.059 1 41 15 15 GLN H H 8.293 0.001 1 42 15 15 GLN C C 175.214 0.003 1 43 15 15 GLN CA C 55.701 0.001 1 44 15 15 GLN N N 120.993 0.057 1 45 16 16 LYS H H 8.371 0.001 1 46 16 16 LYS C C 175.207 0.005 1 47 16 16 LYS CA C 56.383 0.017 1 48 16 16 LYS N N 123.503 0.018 1 49 17 17 LEU H H 8.292 0.000 1 50 17 17 LEU C C 175.945 0.015 1 51 17 17 LEU CA C 54.487 0.005 1 52 17 17 LEU N N 124.409 0.030 1 53 18 18 VAL H H 8.350 0.001 1 54 18 18 VAL C C 174.868 0.000 1 55 18 18 VAL CA C 61.284 0.022 1 56 18 18 VAL N N 123.212 0.024 1 57 19 19 PHE H H 9.314 0.003 1 58 19 19 PHE C C 174.551 0.002 1 59 19 19 PHE CA C 59.134 0.007 1 60 19 19 PHE N N 127.548 0.050 1 61 20 20 PHE H H 8.659 0.004 1 62 20 20 PHE C C 171.764 0.016 1 63 20 20 PHE CA C 55.382 0.003 1 64 20 20 PHE N N 116.606 0.028 1 65 21 21 ALA H H 8.529 0.002 1 66 21 21 ALA C C 175.265 0.031 1 67 21 21 ALA CA C 49.588 0.016 1 68 21 21 ALA N N 119.144 0.065 1 69 22 22 GLU H H 9.360 0.002 1 70 22 22 GLU C C 175.224 0.010 1 71 22 22 GLU CA C 54.246 0.003 1 72 22 22 GLU N N 123.515 0.045 1 73 23 23 ASP H H 8.748 0.002 1 74 23 23 ASP C C 176.651 0.021 1 75 23 23 ASP CA C 54.227 0.007 1 76 23 23 ASP N N 126.602 0.027 1 77 24 24 VAL H H 8.420 0.002 1 78 24 24 VAL C C 177.062 0.006 1 79 24 24 VAL CA C 62.281 0.016 1 80 24 24 VAL N N 122.764 0.025 1 81 25 25 GLY H H 8.434 0.002 1 82 25 25 GLY C C 174.082 0.029 1 83 25 25 GLY CA C 45.234 0.012 1 84 25 25 GLY N N 110.653 0.030 1 85 26 26 SER H H 8.409 0.004 1 86 26 26 SER C C 174.709 0.000 1 87 26 26 SER CA C 58.476 0.000 1 88 26 26 SER N N 113.230 0.039 1 89 28 28 LYS H H 7.853 0.000 1 90 28 28 LYS C C 176.822 0.006 1 91 28 28 LYS CA C 56.203 0.001 1 92 28 28 LYS N N 117.651 0.011 1 93 29 29 GLY H H 8.138 0.001 1 94 29 29 GLY C C 172.297 0.003 1 95 29 29 GLY CA C 45.159 0.001 1 96 29 29 GLY N N 108.726 0.047 1 97 30 30 ALA H H 7.906 0.002 1 98 30 30 ALA C C 175.950 0.001 1 99 30 30 ALA CA C 51.226 0.014 1 100 30 30 ALA N N 121.726 0.014 1 101 31 31 ILE H H 8.607 0.002 1 102 31 31 ILE C C 174.248 0.009 1 103 31 31 ILE CA C 59.627 0.005 1 104 31 31 ILE N N 117.522 0.039 1 105 32 32 ILE H H 8.370 0.003 1 106 32 32 ILE C C 175.202 0.000 1 107 32 32 ILE CA C 57.213 0.003 1 108 32 32 ILE N N 123.855 0.061 1 109 33 33 GLY H H 7.595 0.003 1 110 33 33 GLY C C 169.339 0.018 1 111 33 33 GLY CA C 44.356 0.002 1 112 33 33 GLY N N 112.877 0.032 1 113 34 34 LEU H H 8.455 0.001 1 114 34 34 LEU C C 174.486 0.000 1 115 34 34 LEU CA C 53.585 0.001 1 116 34 34 LEU N N 116.284 0.019 1 117 35 35 MET H H 9.280 0.002 1 118 35 35 MET C C 175.119 0.003 1 119 35 35 MET CA C 53.772 0.047 1 120 35 35 MET N N 122.834 0.014 1 121 36 36 VAL H H 8.960 0.003 1 122 36 36 VAL C C 176.553 0.002 1 123 36 36 VAL CA C 61.502 0.007 1 124 36 36 VAL N N 127.341 0.017 1 125 37 37 GLY H H 8.771 0.002 1 126 37 37 GLY C C 173.834 0.006 1 127 37 37 GLY CA C 45.444 0.004 1 128 37 37 GLY N N 115.386 0.016 1 129 38 38 GLY H H 8.098 0.001 1 130 38 38 GLY C C 173.289 0.005 1 131 38 38 GLY CA C 44.794 0.002 1 132 38 38 GLY N N 107.275 0.005 1 133 39 39 VAL H H 7.924 0.001 1 134 39 39 VAL C C 175.162 0.003 1 135 39 39 VAL CA C 62.117 0.006 1 136 39 39 VAL N N 118.453 0.015 1 137 40 40 VAL H H 7.611 0.002 1 138 40 40 VAL C C 180.725 0.006 1 139 40 40 VAL CA C 63.745 0.006 1 140 40 40 VAL N N 127.502 0.011 1 stop_ save_