data_17764 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; A partially folded structure of amyloid-beta(1 40) in an aqueous environment ; _BMRB_accession_number 17764 _BMRB_flat_file_name bmr17764.str _Entry_type original _Submission_date 2011-07-06 _Accession_date 2011-07-06 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Folding mechanism of Abeta in aqueous environment' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vivekanandan Subramanian . . 2 Brender Jeffrey R. . 3 Lee Shirley Y. . 4 Ramamoorthy Ayyalusamy . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 210 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-08-19 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'A partially folded structure of amyloid-beta(1-40) in an aqueous environment.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21726530 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vivekanandan Subramanian . . 2 Brender Jeffrey R. . 3 Lee Shirley Y. . 4 Ramamoorthy Ayyalusamy . . stop_ _Journal_abbreviation 'Biochem. Biophys. Res. Commun.' _Journal_name_full 'Biochemical and biophysical research communications' _Journal_volume 411 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 312 _Page_last 316 _Year 2011 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Abeta _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Abeta $Abeta 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 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Abeta _Molecular_mass 4335.893 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 40 _Mol_residue_sequence ; DAEFRHDSGYEVHHQKLVFF AEDVGSNKGAIIGLMVGGVV ; loop_ _Residue_seq_code _Residue_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 stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 11435 Amyloid-beta-(1-40) 100.00 40 100.00 100.00 1.45e-18 BMRB 15775 APP_C99 100.00 122 100.00 100.00 1.17e-18 BMRB 17159 Amyloid_beta-Peptide 100.00 40 100.00 100.00 1.45e-18 BMRB 17186 Abeta 100.00 40 100.00 100.00 1.45e-18 BMRB 17793 Abeta(1-42) 100.00 42 100.00 100.00 1.25e-18 BMRB 17794 Abeta(1-42) 100.00 42 100.00 100.00 1.25e-18 BMRB 17795 Abeta(1-40) 100.00 40 100.00 100.00 1.45e-18 BMRB 17796 Abeta40 100.00 40 100.00 100.00 1.45e-18 BMRB 18052 Pyroglutamate_Abeta 92.50 38 100.00 100.00 2.67e-16 BMRB 18127 beta-amyloid 100.00 40 100.00 100.00 1.45e-18 BMRB 18128 beta-amyloid 100.00 40 100.00 100.00 1.45e-18 BMRB 18129 beta-amyloid 100.00 40 100.00 100.00 1.45e-18 BMRB 18131 beta-amyloid 100.00 40 100.00 100.00 1.45e-18 BMRB 19009 beta-amyloid_peptide 100.00 40 100.00 100.00 1.45e-18 BMRB 19309 amyloid_peptide 100.00 40 100.00 100.00 1.45e-18 BMRB 19393 Abeta 100.00 39 97.50 97.50 5.22e-16 BMRB 25218 amyloid_peptide 100.00 42 100.00 100.00 1.25e-18 BMRB 25289 amyloid_beta 100.00 39 97.50 97.50 5.22e-16 BMRB 25429 entity 100.00 42 100.00 100.00 1.25e-18 BMRB 26508 amyloid_B 100.00 40 100.00 100.00 1.45e-18 BMRB 26516 amyloid_B 100.00 40 100.00 100.00 1.45e-18 PDB 1AMB "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" 70.00 28 100.00 100.00 2.06e-10 PDB 1AMC "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" 70.00 28 100.00 100.00 2.06e-10 PDB 1AML "The Alzheimer`s Disease Amyloid A4 Peptide (Residues 1-40)" 100.00 40 100.00 100.00 1.45e-18 PDB 1BA4 "The Solution Structure Of Amyloid Beta-Peptide (1-40) In A Water-Micelle Environment. Is The Membrane-Spanning Domain Where We " 100.00 40 100.00 100.00 1.45e-18 PDB 1BA6 "Solution Structure Of The Methionine-Oxidized Amyloid Beta- Peptide (1-40). Does Oxidation Affect Conformational Switching? Nmr" 100.00 40 97.50 97.50 1.63e-17 PDB 1HZ3 "Alzheimer's Disease Amyloid-Beta Peptide (Residues 10-35)" 65.00 26 100.00 100.00 2.01e-08 PDB 1IYT "Solution Structure Of The Alzheimer's Disease Amyloid Beta- Peptide (1-42)" 100.00 42 100.00 100.00 1.25e-18 PDB 1Z0Q "Aqueous Solution Structure Of The Alzheimer's Disease Abeta Peptide (1-42)" 100.00 42 100.00 100.00 1.25e-18 PDB 2BEG "3d Structure Of Alzheimer's Abeta(1-42) Fibrils" 100.00 42 100.00 100.00 1.25e-18 PDB 2G47 "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-40)" 100.00 40 100.00 100.00 1.45e-18 PDB 2LFM "A Partially Folded Structure Of Amyloid-Beta(1 40) In An Aqueous Environment" 100.00 40 100.00 100.00 1.45e-18 PDB 2LMN "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Positive Stagger" 100.00 40 100.00 100.00 1.45e-18 PDB 2LMO "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Negative Stagger" 100.00 40 100.00 100.00 1.45e-18 PDB 2LMP "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Positive Stagger" 100.00 40 100.00 100.00 1.45e-18 PDB 2LMQ "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Negative Stagger" 100.00 40 100.00 100.00 1.45e-18 PDB 2LNQ "40-residue D23n Beta Amyloid Fibril" 100.00 40 97.50 100.00 4.98e-18 PDB 2LP1 "The Solution Nmr Structure Of The Transmembrane C-Terminal Domain Of The Amyloid Precursor Protein (C99)" 100.00 122 100.00 100.00 1.17e-18 PDB 2M4J "40-residue Beta-amyloid Fibril Derived From Alzheimer's Disease Brain" 100.00 40 100.00 100.00 1.45e-18 PDB 2M9R "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" 100.00 40 100.00 100.00 1.45e-18 PDB 2M9S "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" 100.00 40 100.00 100.00 1.45e-18 PDB 2MVX "Atomic-resolution 3d Structure Of Amyloid-beta Fibrils: The Osaka Mutation" 100.00 39 97.50 97.50 5.22e-16 PDB 2MXU "42-residue Beta Amyloid Fibril" 100.00 42 100.00 100.00 1.25e-18 PDB 2OTK "Structure Of Alzheimer Ab Peptide In Complex With An Engineered Binding Protein" 100.00 40 100.00 100.00 1.45e-18 PDB 2WK3 "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-42)" 100.00 42 100.00 100.00 1.25e-18 PDB 3BAE "Crystal Structure Of Fab Wo2 Bound To The N Terminal Domain Of Amyloid Beta Peptide (1-28)" 70.00 28 100.00 100.00 2.06e-10 PDB 3IFN "X-ray Structure Of Amyloid Beta Peptide:antibody (abeta1-40:12a11) Complex" 100.00 40 100.00 100.00 1.45e-18 PDB 4HIX "Crystal Structure Of A Humanised 3d6 Fab Bound To Amyloid Beta Peptide" 70.00 28 100.00 100.00 2.06e-10 PDB 4M1C "Crystal Structure Analysis Of Fab-bound Human Insulin Degrading Enzyme (ide) In Complex With Amyloid-beta (1-40)" 100.00 40 100.00 100.00 1.45e-18 PDB 4MVI "Crystal Structure Of An Engineered Lipocalin (anticalin Us7) In Complex With The Alzheimer Amyloid Peptide Abeta(1-40)" 100.00 40 100.00 100.00 1.45e-18 PDB 4MVL "Crystal Structure Of An Engineered Lipocalin (anticalin H1ga) In Complex With The Alzheimer Amyloid Peptide Abeta1-40" 100.00 40 100.00 100.00 1.45e-18 PDB 4NGE "Crystal Structure Of Human Presequence Protease In Complex With Amyloid-beta (1-40)" 100.00 40 100.00 100.00 1.45e-18 PDB 4ONG "Fab Fragment Of 3d6 In Complex With Amyloid Beta 1-40" 100.00 40 100.00 100.00 1.45e-18 PDB 5AEF "Electron Cryo-microscopy Of An Abeta(1-42)amyloid Fibril" 65.00 28 100.00 100.00 3.64e-07 DBJ BAA22264 "amyloid precursor protein [Homo sapiens]" 100.00 770 100.00 100.00 1.24e-18 DBJ BAA84580 "amyloid precursor protein [Sus scrofa]" 100.00 770 100.00 100.00 1.24e-18 DBJ BAB71958 "amyloid precursor protein [Homo sapiens]" 100.00 52 97.50 100.00 1.70e-18 DBJ BAD51938 "amyloid beta A4 precursor protein [Macaca fascicularis]" 100.00 696 100.00 100.00 1.11e-18 DBJ BAE01907 "unnamed protein product [Macaca fascicularis]" 100.00 751 100.00 100.00 1.39e-18 EMBL CAA30050 "amyloid A4 protein [Homo sapiens]" 100.00 751 100.00 100.00 1.21e-18 EMBL CAA31830 "A4 amyloid protein precursor [Homo sapiens]" 100.00 695 100.00 100.00 1.27e-18 EMBL CAA39589 "amyloid precursor protein [Bos taurus]" 100.00 59 100.00 100.00 3.47e-19 EMBL CAA39590 "amyloid precursor protein [Canis lupus familiaris]" 100.00 58 100.00 100.00 3.58e-19 EMBL CAA39591 "amyloid precursor protein [Cavia sp.]" 100.00 58 100.00 100.00 3.58e-19 GB AAA35540 "amyloid protein, partial [Homo sapiens]" 95.00 97 100.00 100.00 2.29e-17 GB AAA36829 "amyloid b-protein precursor [Macaca fascicularis]" 100.00 695 100.00 100.00 1.27e-18 GB AAA51564 "amyloid beta protein, partial [Homo sapiens]" 75.00 30 100.00 100.00 1.06e-11 GB AAA51722 "amyloid beta-protein precursor, partial [Homo sapiens]" 100.00 412 100.00 100.00 8.90e-19 GB AAA51726 "beta-amyloid A4, partial [Homo sapiens]" 100.00 264 100.00 100.00 1.69e-18 PIR A60045 "Alzheimer's disease amyloid beta/A4 protein precursor - dog (fragment)" 100.00 57 100.00 100.00 3.90e-19 PIR D60045 "Alzheimer's disease amyloid beta/A4 protein precursor - bovine (fragment)" 100.00 57 100.00 100.00 3.90e-19 PIR E60045 "Alzheimer's disease amyloid beta/A4 protein precursor - sheep (fragment)" 100.00 57 100.00 100.00 3.90e-19 PIR G60045 "Alzheimer's disease amyloid beta/A4 protein precursor - guinea pig (fragment)" 100.00 57 100.00 100.00 3.90e-19 PIR PQ0438 "Alzheimer's disease amyloid A4 protein precursor - rabbit (fragment)" 100.00 82 100.00 100.00 3.95e-19 PRF 1303338A "amyloid A4 protein precursor" 100.00 695 100.00 100.00 1.27e-18 PRF 1403400A "amyloid protein A4" 100.00 751 100.00 100.00 1.21e-18 PRF 1405204A "amyloid protein" 100.00 42 100.00 100.00 1.25e-18 PRF 1507304A "beta amyloid peptide precursor" 100.00 412 100.00 100.00 9.17e-19 PRF 1507304B "beta amyloid peptide precursor" 100.00 574 100.00 100.00 3.96e-18 REF NP_000475 "amyloid beta A4 protein isoform a precursor [Homo sapiens]" 100.00 770 100.00 100.00 1.24e-18 REF NP_001006601 "amyloid beta A4 protein isoform APP-770 precursor [Canis lupus familiaris]" 100.00 770 100.00 100.00 1.24e-18 REF NP_001013036 "amyloid beta A4 protein precursor [Pan troglodytes]" 100.00 770 100.00 100.00 1.24e-18 REF NP_001070264 "amyloid beta A4 protein precursor [Bos taurus]" 100.00 695 100.00 100.00 1.27e-18 REF NP_001127014 "amyloid beta A4 protein precursor [Pongo abelii]" 100.00 695 100.00 100.00 1.60e-18 SP P05067 "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; AltName: Full=APPI; Short=APP; AltName: Full=Alzheimer disease amylo" 100.00 770 100.00 100.00 1.24e-18 SP P53601 "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" 100.00 770 100.00 100.00 1.24e-18 SP P79307 "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" 100.00 770 100.00 100.00 1.24e-18 SP P86906 "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" 100.00 40 97.50 100.00 5.37e-18 SP Q28053 "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" 100.00 59 100.00 100.00 3.47e-19 TPG DAA33655 "TPA: amyloid beta A4 protein [Bos taurus]" 100.00 695 100.00 100.00 1.27e-18 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Abeta humans 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 _Details $Abeta 'chemical synthesis' . . . . . 'purchased from Anaspec' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '15C, 20 mM KPi, 50 mM NaCL, 77 uM Ab1-40' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling 'potassium phosphate' 20 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' $Abeta 77 uM '[U-10% 13C; U-100% 15N]' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Saveframe_category software _Name CYANA _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 288 . K pH 7.3 0.1 pH pressure 1 . atm 'ionic strength' 0.07 . 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 . . . 1.0 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H TOCSY' '2D 1H-1H NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name Abeta _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 4.035 0.002 1 2 1 1 ASP HB2 H 2.540 0.002 2 3 1 1 ASP HB3 H 2.668 0.000 2 4 2 2 ALA H H 7.931 0.000 1 5 2 2 ALA HA H 4.140 0.003 1 6 2 2 ALA HB H 1.203 0.003 1 7 3 3 GLU H H 8.354 0.002 1 8 3 3 GLU HA H 4.019 0.003 1 9 3 3 GLU HB2 H 1.769 0.000 2 10 3 3 GLU HB3 H 1.719 0.000 2 11 3 3 GLU HG2 H 2.058 0.000 2 12 3 3 GLU HG3 H 1.965 0.002 2 13 4 4 PHE H H 8.209 0.002 1 14 4 4 PHE HA H 4.403 0.003 1 15 4 4 PHE HB2 H 2.851 0.002 2 16 4 4 PHE HB3 H 2.851 0.002 2 17 4 4 PHE HD1 H 7.099 0.002 2 18 4 4 PHE HD2 H 7.099 0.002 2 19 4 4 PHE HE1 H 7.012 0.002 2 20 4 4 PHE HE2 H 7.012 0.002 2 21 5 5 ARG H H 8.067 0.002 1 22 5 5 ARG HA H 4.095 0.003 1 23 5 5 ARG HB2 H 1.328 0.005 2 24 5 5 ARG HB3 H 1.328 0.005 2 25 5 5 ARG HG2 H 1.576 0.002 2 26 5 5 ARG HG3 H 1.469 0.002 2 27 5 5 ARG HD2 H 2.965 0.004 2 28 5 5 ARG HD3 H 2.965 0.004 2 29 6 6 HIS HA H 4.396 0.004 1 30 6 6 HIS HB2 H 2.973 0.003 2 31 6 6 HIS HB3 H 2.903 0.003 2 32 6 6 HIS HD1 H 6.645 0.000 1 33 6 6 HIS HD2 H 6.923 0.001 1 34 7 7 ASP H H 8.281 0.002 1 35 7 7 ASP HA H 4.463 0.004 1 36 7 7 ASP HB2 H 2.516 0.001 2 37 7 7 ASP HB3 H 2.516 0.001 2 38 8 8 SER H H 8.333 0.003 1 39 8 8 SER HA H 4.223 0.004 1 40 8 8 SER HB2 H 3.754 0.003 2 41 8 8 SER HB3 H 3.713 0.003 2 42 9 9 GLY H H 8.445 0.001 1 43 9 9 GLY HA2 H 3.782 0.005 2 44 9 9 GLY HA3 H 3.721 0.003 2 45 10 10 TYR H H 7.860 0.002 1 46 10 10 TYR HA H 4.344 0.004 1 47 10 10 TYR HB2 H 2.862 0.002 2 48 10 10 TYR HB3 H 2.791 0.002 2 49 10 10 TYR HD1 H 6.893 0.001 3 50 10 10 TYR HD2 H 6.893 0.001 3 51 10 10 TYR HE1 H 6.612 0.001 3 52 10 10 TYR HE2 H 6.612 0.001 3 53 11 11 GLU H H 8.283 0.001 1 54 11 11 GLU HA H 4.037 0.004 1 55 11 11 GLU HB2 H 1.697 0.005 2 56 11 11 GLU HB3 H 1.773 0.002 2 57 11 11 GLU HG2 H 2.046 0.002 2 58 11 11 GLU HG3 H 1.995 0.001 2 59 12 12 VAL H H 7.970 0.001 1 60 12 12 VAL HA H 3.775 0.002 1 61 12 12 VAL HB H 1.774 0.002 1 62 12 12 VAL HG1 H 0.707 0.002 2 63 12 12 VAL HG2 H 0.611 0.002 2 64 13 13 HIS H H 7.760 0.002 1 65 13 13 HIS HA H 4.457 0.002 1 66 13 13 HIS HB2 H 2.920 0.002 2 67 13 13 HIS HB3 H 2.866 0.003 2 68 13 13 HIS HD1 H 6.610 0.000 1 69 13 13 HIS HD2 H 6.849 0.001 1 70 14 14 HIS H H 6.860 0.003 1 71 14 14 HIS HA H 4.396 0.003 1 72 14 14 HIS HB2 H 2.964 0.002 2 73 14 14 HIS HB3 H 2.861 0.002 2 74 15 15 GLN H H 8.336 0.002 1 75 15 15 GLN HA H 4.110 0.003 1 76 15 15 GLN HB2 H 1.905 0.002 2 77 15 15 GLN HB3 H 1.819 0.002 2 78 15 15 GLN HG2 H 2.173 0.002 2 79 15 15 GLN HG3 H 2.173 0.002 2 80 15 15 GLN HE21 H 7.475 0.000 2 81 15 15 GLN HE22 H 6.795 0.001 2 82 16 16 LYS H H 8.317 0.002 1 83 16 16 LYS HA H 4.116 0.003 1 84 16 16 LYS HB2 H 1.644 0.005 2 85 16 16 LYS HB3 H 1.584 0.002 2 86 16 16 LYS HG2 H 1.284 0.003 2 87 16 16 LYS HG3 H 1.214 0.005 2 88 16 16 LYS HD2 H 1.514 0.004 2 89 16 16 LYS HD3 H 1.514 0.004 2 90 16 16 LYS HE2 H 2.813 0.002 2 91 16 16 LYS HE3 H 2.813 0.002 2 92 17 17 LEU H H 8.169 0.003 1 93 17 17 LEU HA H 4.169 0.003 1 94 17 17 LEU HB2 H 1.443 0.002 2 95 17 17 LEU HB3 H 1.398 0.002 2 96 17 17 LEU HG H 1.281 0.004 1 97 17 17 LEU HD1 H 0.682 0.003 2 98 17 17 LEU HD2 H 0.749 0.003 2 99 18 18 VAL H H 7.902 0.002 1 100 18 18 VAL HA H 3.871 0.002 1 101 18 18 VAL HB H 1.742 0.003 1 102 18 18 VAL HG1 H 0.673 0.003 2 103 18 18 VAL HG2 H 0.587 0.002 2 104 19 19 PHE H H 8.160 0.001 1 105 19 19 PHE HA H 4.418 0.001 1 106 19 19 PHE HB2 H 2.821 0.006 2 107 19 19 PHE HB3 H 2.749 0.002 2 108 19 19 PHE HD1 H 7.005 0.002 2 109 19 19 PHE HD2 H 7.005 0.002 2 110 19 19 PHE HE1 H 7.144 0.001 2 111 19 19 PHE HE2 H 7.144 0.001 2 112 19 19 PHE HZ H 7.114 0.002 1 113 20 20 PHE H H 8.132 0.002 1 114 20 20 PHE HA H 4.422 0.003 1 115 20 20 PHE HB2 H 2.926 0.001 2 116 20 20 PHE HB3 H 2.773 0.001 2 117 20 20 PHE HD1 H 7.076 0.002 2 118 20 20 PHE HD2 H 7.076 0.002 2 119 20 20 PHE HE1 H 7.161 0.003 2 120 20 20 PHE HE2 H 7.161 0.003 2 121 21 21 ALA H H 8.154 0.001 1 122 21 21 ALA HA H 4.061 0.003 1 123 21 21 ALA HB H 1.206 0.002 1 124 22 22 GLU H H 8.269 0.003 1 125 22 22 GLU HA H 4.048 0.003 1 126 22 22 GLU HB2 H 1.762 0.004 2 127 22 22 GLU HB3 H 1.880 0.002 2 128 22 22 GLU HG2 H 2.108 0.010 2 129 22 22 GLU HG3 H 2.108 0.010 2 130 23 23 ASP H H 8.325 0.001 1 131 23 23 ASP HA H 4.487 0.002 1 132 23 23 ASP HB2 H 2.584 0.003 2 133 23 23 ASP HB3 H 2.480 0.004 2 134 24 24 VAL H H 8.053 0.001 1 135 24 24 VAL HA H 3.972 0.002 1 136 24 24 VAL HB H 2.025 0.003 1 137 24 24 VAL HG1 H 0.795 0.003 2 138 24 24 VAL HG2 H 0.795 0.003 2 139 25 25 GLY H H 8.451 0.001 1 140 25 25 GLY HA2 H 3.817 0.003 2 141 25 25 GLY HA3 H 3.817 0.003 2 142 26 26 SER H H 8.065 0.003 1 143 26 26 SER HA H 4.271 0.008 1 144 26 26 SER HB2 H 3.752 0.006 2 145 26 26 SER HB3 H 3.706 0.005 2 146 27 27 ASN H H 8.391 0.001 1 147 27 27 ASN HA H 4.575 0.003 1 148 27 27 ASN HB2 H 2.712 0.002 2 149 27 27 ASN HB3 H 2.645 0.003 2 150 27 27 ASN HD21 H 6.834 0.001 2 151 27 27 ASN HD22 H 7.545 0.001 2 152 28 28 LYS H H 8.252 0.002 1 153 28 28 LYS HA H 4.110 0.004 1 154 28 28 LYS HB2 H 1.724 0.005 2 155 28 28 LYS HB3 H 1.613 0.002 2 156 28 28 LYS HG2 H 1.316 0.008 2 157 28 28 LYS HG3 H 1.316 0.008 2 158 29 29 GLY H H 8.326 0.001 1 159 29 29 GLY HA2 H 3.763 0.002 2 160 29 29 GLY HA3 H 3.763 0.002 2 161 30 30 ALA H H 7.939 0.003 1 162 30 30 ALA HA H 4.155 0.003 1 163 30 30 ALA HB H 1.209 0.002 1 164 31 31 ILE H H 8.076 0.002 1 165 31 31 ILE HA H 3.995 0.002 1 166 31 31 ILE HB H 1.703 0.001 1 167 31 31 ILE HG12 H 1.339 0.003 2 168 31 31 ILE HG13 H 1.039 0.003 2 169 31 31 ILE HD1 H 0.709 0.000 1 170 32 32 ILE H H 8.177 0.005 1 171 32 32 ILE HA H 3.999 0.002 1 172 32 32 ILE HB H 1.705 0.002 1 173 32 32 ILE HG2 H 1.047 0.004 1 174 32 32 ILE HD1 H 0.703 0.003 1 175 33 33 GLY H H 8.369 0.001 1 176 33 33 GLY HA2 H 3.765 0.002 2 177 33 33 GLY HA3 H 3.765 0.002 2 178 34 34 LEU H H 7.953 0.002 1 179 34 34 LEU HA H 4.183 0.003 1 180 34 34 LEU HB2 H 1.438 0.001 2 181 34 34 LEU HB3 H 1.438 0.001 2 182 34 34 LEU HD1 H 0.765 0.004 2 183 34 34 LEU HD2 H 0.713 0.003 2 184 35 35 MET H H 8.350 0.003 1 185 35 35 MET HA H 4.367 0.001 1 186 35 35 MET HB2 H 1.918 0.003 2 187 35 35 MET HB3 H 1.859 0.003 2 188 35 35 MET HG2 H 2.431 0.002 2 189 35 35 MET HG3 H 2.354 0.002 2 190 36 36 VAL H H 8.135 0.002 1 191 36 36 VAL HA H 3.969 0.002 1 192 36 36 VAL HB H 1.924 0.003 1 193 36 36 VAL HG1 H 0.786 0.002 2 194 36 36 VAL HG2 H 0.786 0.002 2 195 37 37 GLY H H 8.496 0.001 1 196 37 37 GLY HA2 H 3.826 0.004 2 197 37 37 GLY HA3 H 3.826 0.004 2 198 38 38 GLY H H 8.166 0.002 1 199 38 38 GLY HA2 H 3.855 0.002 2 200 38 38 GLY HA3 H 3.789 0.003 2 201 39 39 VAL H H 7.981 0.004 1 202 39 39 VAL HA H 4.015 0.001 1 203 39 39 VAL HB H 1.927 0.003 1 204 39 39 VAL HG1 H 0.776 0.003 2 205 39 39 VAL HG2 H 0.776 0.003 2 206 40 40 VAL H H 7.718 0.001 1 207 40 40 VAL HA H 3.890 0.000 1 208 40 40 VAL HB H 1.898 0.003 1 209 40 40 VAL HG1 H 0.738 0.006 2 210 40 40 VAL HG2 H 0.738 0.006 2 stop_ save_