data_18052 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structural analysis of the pyroglutamate modified isoform of the Alzheimer's disease related beta-amyloid using NMR spectroscopy ; _BMRB_accession_number 18052 _BMRB_flat_file_name bmr18052.str _Entry_type original _Submission_date 2011-11-11 _Accession_date 2011-11-11 _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 Sun Na . . 2 Hartmann Rudolf . . 3 Lecher Justin . . 4 Stoldt Matthias . . 5 Willbold Dieter . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 185 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-10-29 original author . stop_ _Original_release_date 2012-10-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural analysis of the pyroglutamate modified isoform of the Alzheimer's disease related beta-amyloid using NMR spectroscopy' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23001756 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sun Na . . 2 Hartmann Rudolf . . 3 Lecher Justin . . 4 Stoldt Matthias . . 5 Funke 'Susanne Aileen' . . 6 Gremer Lothar . . 7 Ludwig Hans-Henning . . 8 Demuth Hans-Ulrich . . 9 Kleinschmi Martin . . 10 Willbold Dieter . . stop_ _Journal_abbreviation 'J. Pept. Sci.' _Journal_volume 18 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 691 _Page_last 695 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name MS2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label PyroAb $PyroAb stop_ _System_molecular_weight 4125.6626 _System_physical_state unfolded _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PyroAb _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Pyroglutamate_Abeta _Molecular_mass 4125.6626 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 38 _Mol_residue_sequence ; XFRHDSGYEVHHQKLVFFAE DVGSNKGAIIGLMVGGVV ; loop_ _Residue_seq_code _Residue_label 1 PCA 2 PHE 3 ARG 4 HIS 5 ASP 6 SER 7 GLY 8 TYR 9 GLU 10 VAL 11 HIS 12 HIS 13 GLN 14 LYS 15 LEU 16 VAL 17 PHE 18 PHE 19 ALA 20 GLU 21 ASP 22 VAL 23 GLY 24 SER 25 ASN 26 LYS 27 GLY 28 ALA 29 ILE 30 ILE 31 GLY 32 LEU 33 MET 34 VAL 35 GLY 36 GLY 37 VAL 38 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) 97.37 40 100.00 100.00 2.53e-16 BMRB 15775 APP_C99 97.37 122 100.00 100.00 2.51e-16 BMRB 17159 Amyloid_beta-Peptide 97.37 40 100.00 100.00 2.53e-16 BMRB 17186 Abeta 97.37 40 100.00 100.00 2.53e-16 BMRB 17764 Abeta 97.37 40 100.00 100.00 2.53e-16 BMRB 17793 Abeta(1-42) 97.37 42 100.00 100.00 2.30e-16 BMRB 17794 Abeta(1-42) 97.37 42 100.00 100.00 2.30e-16 BMRB 17795 Abeta(1-40) 97.37 40 100.00 100.00 2.53e-16 BMRB 17796 Abeta40 97.37 40 100.00 100.00 2.53e-16 BMRB 18127 beta-amyloid 97.37 40 100.00 100.00 2.53e-16 BMRB 18128 beta-amyloid 97.37 40 100.00 100.00 2.53e-16 BMRB 18129 beta-amyloid 97.37 40 100.00 100.00 2.53e-16 BMRB 18131 beta-amyloid 97.37 40 100.00 100.00 2.53e-16 BMRB 19009 beta-amyloid_peptide 97.37 40 100.00 100.00 2.53e-16 BMRB 19309 amyloid_peptide 97.37 40 100.00 100.00 2.53e-16 BMRB 19393 Abeta 97.37 39 97.30 97.30 1.09e-13 BMRB 25218 amyloid_peptide 97.37 42 100.00 100.00 2.30e-16 BMRB 25289 amyloid_beta 97.37 39 97.30 97.30 1.09e-13 BMRB 25429 entity 97.37 42 100.00 100.00 2.30e-16 BMRB 26508 amyloid_B 97.37 40 100.00 100.00 2.53e-16 BMRB 26516 amyloid_B 97.37 40 100.00 100.00 2.53e-16 PDB 1AMB "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" 65.79 28 100.00 100.00 2.61e-08 PDB 1AMC "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" 65.79 28 100.00 100.00 2.61e-08 PDB 1AML "The Alzheimer`s Disease Amyloid A4 Peptide (Residues 1-40)" 97.37 40 100.00 100.00 2.53e-16 PDB 1BA4 "The Solution Structure Of Amyloid Beta-Peptide (1-40) In A Water-Micelle Environment. Is The Membrane-Spanning Domain Where We " 97.37 40 100.00 100.00 2.53e-16 PDB 1BA6 "Solution Structure Of The Methionine-Oxidized Amyloid Beta- Peptide (1-40). Does Oxidation Affect Conformational Switching? Nmr" 97.37 40 97.30 97.30 2.77e-15 PDB 1HZ3 "Alzheimer's Disease Amyloid-Beta Peptide (Residues 10-35)" 68.42 26 100.00 100.00 2.13e-08 PDB 1IYT "Solution Structure Of The Alzheimer's Disease Amyloid Beta- Peptide (1-42)" 97.37 42 100.00 100.00 2.30e-16 PDB 1Z0Q "Aqueous Solution Structure Of The Alzheimer's Disease Abeta Peptide (1-42)" 97.37 42 100.00 100.00 2.30e-16 PDB 2BEG "3d Structure Of Alzheimer's Abeta(1-42) Fibrils" 97.37 42 100.00 100.00 2.30e-16 PDB 2G47 "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-40)" 97.37 40 100.00 100.00 2.53e-16 PDB 2LFM "A Partially Folded Structure Of Amyloid-Beta(1 40) In An Aqueous Environment" 97.37 40 100.00 100.00 2.53e-16 PDB 2LMN "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Positive Stagger" 97.37 40 100.00 100.00 2.53e-16 PDB 2LMO "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Negative Stagger" 97.37 40 100.00 100.00 2.53e-16 PDB 2LMP "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Positive Stagger" 97.37 40 100.00 100.00 2.53e-16 PDB 2LMQ "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Negative Stagger" 97.37 40 100.00 100.00 2.53e-16 PDB 2LNQ "40-residue D23n Beta Amyloid Fibril" 97.37 40 97.30 100.00 1.10e-15 PDB 2LP1 "The Solution Nmr Structure Of The Transmembrane C-Terminal Domain Of The Amyloid Precursor Protein (C99)" 97.37 122 100.00 100.00 2.51e-16 PDB 2M4J "40-residue Beta-amyloid Fibril Derived From Alzheimer's Disease Brain" 97.37 40 100.00 100.00 2.53e-16 PDB 2M9R "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" 97.37 40 100.00 100.00 2.53e-16 PDB 2M9S "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" 97.37 40 100.00 100.00 2.53e-16 PDB 2MVX "Atomic-resolution 3d Structure Of Amyloid-beta Fibrils: The Osaka Mutation" 97.37 39 97.30 97.30 1.09e-13 PDB 2MXU "42-residue Beta Amyloid Fibril" 97.37 42 100.00 100.00 2.30e-16 PDB 2OTK "Structure Of Alzheimer Ab Peptide In Complex With An Engineered Binding Protein" 97.37 40 100.00 100.00 2.53e-16 PDB 2WK3 "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-42)" 97.37 42 100.00 100.00 2.30e-16 PDB 3BAE "Crystal Structure Of Fab Wo2 Bound To The N Terminal Domain Of Amyloid Beta Peptide (1-28)" 65.79 28 100.00 100.00 2.61e-08 PDB 3IFN "X-ray Structure Of Amyloid Beta Peptide:antibody (abeta1-40:12a11) Complex" 97.37 40 100.00 100.00 2.53e-16 PDB 4HIX "Crystal Structure Of A Humanised 3d6 Fab Bound To Amyloid Beta Peptide" 65.79 28 100.00 100.00 2.61e-08 PDB 4M1C "Crystal Structure Analysis Of Fab-bound Human Insulin Degrading Enzyme (ide) In Complex With Amyloid-beta (1-40)" 97.37 40 100.00 100.00 2.53e-16 PDB 4MVI "Crystal Structure Of An Engineered Lipocalin (anticalin Us7) In Complex With The Alzheimer Amyloid Peptide Abeta(1-40)" 97.37 40 100.00 100.00 2.53e-16 PDB 4MVL "Crystal Structure Of An Engineered Lipocalin (anticalin H1ga) In Complex With The Alzheimer Amyloid Peptide Abeta1-40" 97.37 40 100.00 100.00 2.53e-16 PDB 4NGE "Crystal Structure Of Human Presequence Protease In Complex With Amyloid-beta (1-40)" 97.37 40 100.00 100.00 2.53e-16 PDB 4ONG "Fab Fragment Of 3d6 In Complex With Amyloid Beta 1-40" 97.37 40 100.00 100.00 2.53e-16 PDB 5AEF "Electron Cryo-microscopy Of An Abeta(1-42)amyloid Fibril" 68.42 28 100.00 100.00 4.08e-07 DBJ BAA22264 "amyloid precursor protein [Homo sapiens]" 97.37 770 100.00 100.00 1.64e-16 DBJ BAA84580 "amyloid precursor protein [Sus scrofa]" 97.37 770 100.00 100.00 1.64e-16 DBJ BAB71958 "amyloid precursor protein [Homo sapiens]" 97.37 52 97.30 100.00 4.63e-16 DBJ BAD51938 "amyloid beta A4 precursor protein [Macaca fascicularis]" 97.37 696 100.00 100.00 1.48e-16 DBJ BAE01907 "unnamed protein product [Macaca fascicularis]" 97.37 751 100.00 100.00 1.60e-16 EMBL CAA30050 "amyloid A4 protein [Homo sapiens]" 97.37 751 100.00 100.00 1.60e-16 EMBL CAA31830 "A4 amyloid protein precursor [Homo sapiens]" 97.37 695 100.00 100.00 1.48e-16 EMBL CAA39589 "amyloid precursor protein [Bos taurus]" 97.37 59 100.00 100.00 7.62e-17 EMBL CAA39590 "amyloid precursor protein [Canis lupus familiaris]" 97.37 58 100.00 100.00 7.46e-17 EMBL CAA39591 "amyloid precursor protein [Cavia sp.]" 97.37 58 100.00 100.00 7.46e-17 GB AAA35540 "amyloid protein, partial [Homo sapiens]" 97.37 97 100.00 100.00 1.29e-16 GB AAA36829 "amyloid b-protein precursor [Macaca fascicularis]" 97.37 695 100.00 100.00 1.48e-16 GB AAA51564 "amyloid beta protein, partial [Homo sapiens]" 76.32 30 100.00 100.00 5.28e-11 GB AAA51722 "amyloid beta-protein precursor, partial [Homo sapiens]" 97.37 412 100.00 100.00 5.28e-17 GB AAA51726 "beta-amyloid A4, partial [Homo sapiens]" 97.37 264 100.00 100.00 7.51e-17 PIR A60045 "Alzheimer's disease amyloid beta/A4 protein precursor - dog (fragment)" 97.37 57 100.00 100.00 7.96e-17 PIR D60045 "Alzheimer's disease amyloid beta/A4 protein precursor - bovine (fragment)" 97.37 57 100.00 100.00 7.96e-17 PIR E60045 "Alzheimer's disease amyloid beta/A4 protein precursor - sheep (fragment)" 97.37 57 100.00 100.00 7.96e-17 PIR G60045 "Alzheimer's disease amyloid beta/A4 protein precursor - guinea pig (fragment)" 97.37 57 100.00 100.00 7.96e-17 PIR PQ0438 "Alzheimer's disease amyloid A4 protein precursor - rabbit (fragment)" 97.37 82 100.00 100.00 9.39e-17 PRF 1303338A "amyloid A4 protein precursor" 97.37 695 100.00 100.00 1.48e-16 PRF 1403400A "amyloid protein A4" 97.37 751 100.00 100.00 1.60e-16 PRF 1405204A "amyloid protein" 97.37 42 100.00 100.00 2.30e-16 PRF 1507304A "beta amyloid peptide precursor" 97.37 412 100.00 100.00 5.28e-17 PRF 1507304B "beta amyloid peptide precursor" 97.37 574 100.00 100.00 1.15e-16 REF NP_000475 "amyloid beta A4 protein isoform a precursor [Homo sapiens]" 97.37 770 100.00 100.00 1.64e-16 REF NP_001006601 "amyloid beta A4 protein isoform APP-770 precursor [Canis lupus familiaris]" 97.37 770 100.00 100.00 1.64e-16 REF NP_001013036 "amyloid beta A4 protein precursor [Pan troglodytes]" 97.37 770 100.00 100.00 1.64e-16 REF NP_001070264 "amyloid beta A4 protein precursor [Bos taurus]" 97.37 695 100.00 100.00 1.48e-16 REF NP_001127014 "amyloid beta A4 protein precursor [Pongo abelii]" 97.37 695 100.00 100.00 1.48e-16 SP P05067 "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; AltName: Full=APPI; Short=APP; AltName: Full=Alzheimer disease amylo" 97.37 770 100.00 100.00 1.64e-16 SP P53601 "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" 97.37 770 100.00 100.00 1.64e-16 SP P79307 "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" 97.37 770 100.00 100.00 1.64e-16 SP P86906 "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" 97.37 40 97.30 100.00 1.05e-15 SP Q28053 "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" 97.37 59 100.00 100.00 7.62e-17 TPG DAA33655 "TPA: amyloid beta A4 protein [Bos taurus]" 97.37 695 100.00 100.00 1.48e-16 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_PCA _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common 'PYROGLUTAMIC ACID' _BMRB_code . _PDB_code PCA _Standard_residue_derivative . _Molecular_mass 129.114 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Nov 14 12:08:48 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD CD C . 0 . ? OE OE O . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG2 HG2 H . 0 . ? HG3 HG3 H . 0 . ? HXT HXT H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N CD ? ? SING N H ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG CD ? ? SING CG HG2 ? ? SING CG HG3 ? ? DOUB CD OE ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PyroAb 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 $PyroAb 'chemical synthesis' Synthetic Synthetic Synthetic . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PyroAb 0.1 mM 'natural abundance' Trifluoroethanol 40 % 'natural abundance' H2O 60 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CcpNmr_Analysis _Saveframe_category software _Name ANALYSIS _Version 2.1 loop_ _Vendor _Address _Electronic_address CCPN 'Department of Biochemistry, Cambridge CB2 1GA, UK' http://www.ccpn.ac.uk stop_ loop_ _Task assignment stop_ _Details 'The CCPN NMR assignment and data analysis application' save_ save_NmrPipe _Saveframe_category software _Name NMRPipe _Version 5.99.2011.242.16.23 loop_ _Vendor _Address _Electronic_address NIH 'Laboratory of Chemical Physics, NIDDK, NIH, USA' http://spin.niddk.nih.gov/NMRPipe/ stop_ loop_ _Task conversion processing stop_ _Details 'NMRPipe Spectral Processing and Analysis System' save_ save_VnmrJ _Saveframe_category software _Name VnmrJ _Version 2.3A loop_ _Vendor _Address _Electronic_address 'Agilent Technologies (formerly Varian)' 'Lake Forest, CA, USA' http://www.varianinc.com/cgi-bin/nav?products/nmr/software/vnmrj stop_ loop_ _Task 'data recording' 'spectrometer operation' stop_ _Details 'NMR acquisition and processing software' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model VNMRS _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 $1 save_ save_2D_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $1 save_ ####################### # Sample conditions # ####################### save_Standard _Saveframe_category sample_conditions _Details '40% TFE in water' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.050 . M pH 2.800 . pH pressure 1.000 . atm temperature 298.000 . 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 H 1 'methyl protons' ppm 0.0 external direct . 'capilary in NMR tube' . 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H TOCSY' '2D 1H-1H NOESY' stop_ loop_ _Sample_label $1 stop_ _Sample_conditions_label $Standard _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name PyroAb _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 1 139 1 PCA H H 7.759 0.03 1 2 140 1 PCA HA H 4.224 0.003 1 3 155 1 PCA HB2 H 2.147 0.03 2 4 154 1 PCA HB3 H 1.712 0.03 2 5 157 1 PCA HG2 H 2.429 0.004 2 6 156 1 PCA HG3 H 2.276 0.003 2 7 2 2 PHE H H 7.947 0.003 1 8 2 2 PHE HA H 4.713 0.015 1 9 2 2 PHE HB2 H 2.978 0.002 2 10 2 2 PHE HB3 H 3.229 0.004 2 11 2 2 PHE HD1 H 7.254 0.001 3 12 2 2 PHE HD2 H 7.254 0.001 3 13 2 2 PHE HE1 H 7.334 0.003 3 14 2 2 PHE HE2 H 7.334 0.003 3 15 3 3 ARG H H 8.281 0.003 1 16 3 3 ARG HA H 4.310 0.007 1 17 3 3 ARG HB2 H 1.762 0.005 2 18 3 3 ARG HB3 H 1.843 0.004 2 19 3 3 ARG HG2 H 1.577 0.003 2 20 3 3 ARG HG3 H 1.626 0.002 2 21 3 3 ARG HD3 H 3.200 0.002 1 22 3 3 ARG HE H 7.340 0.002 1 23 4 4 HIS H H 8.568 0.007 1 24 4 4 HIS HA H 4.724 0.013 1 25 4 4 HIS HB2 H 3.204 0.004 2 26 4 4 HIS HB3 H 3.299 0.002 2 27 4 4 HIS HD2 H 7.258 0.03 1 28 4 4 HIS HE1 H 8.569 0.03 1 29 5 5 ASP H H 8.453 0.001 1 30 5 5 ASP HA H 4.814 0.005 1 31 5 5 ASP HB2 H 2.917 0.002 1 32 6 6 SER H H 8.452 0.004 1 33 6 6 SER HA H 4.444 0.001 1 34 6 6 SER HB2 H 4.014 0.008 2 35 6 6 SER HB3 H 4.025 0.002 2 36 7 7 GLY H H 8.577 0.003 1 37 7 7 GLY HA2 H 3.932 0.003 1 38 8 8 TYR H H 8.066 0.002 1 39 8 8 TYR HA H 4.352 0.002 1 40 8 8 TYR HB2 H 3.166 0.003 2 41 8 8 TYR HB3 H 3.101 0.005 2 42 8 8 TYR HD1 H 7.089 0.001 3 43 8 8 TYR HD2 H 7.089 0.001 3 44 8 8 TYR HE1 H 6.767 0.002 3 45 8 8 TYR HE2 H 6.767 0.002 3 46 9 9 GLU H H 8.308 0.003 1 47 9 9 GLU HA H 4.150 0.001 1 48 9 9 GLU HB2 H 2.206 0.004 1 49 9 9 GLU HG3 H 2.537 0.004 1 50 10 10 VAL H H 8.127 0.004 1 51 10 10 VAL HA H 3.837 0.001 1 52 10 10 VAL HB H 2.083 0.002 1 53 10 10 VAL HG1 H 1.031 0.002 2 54 10 10 VAL HG2 H 0.907 0.006 2 55 11 11 HIS H H 8.109 0.003 1 56 11 11 HIS HA H 4.427 0.002 1 57 11 11 HIS HB2 H 3.270 0.003 1 58 11 11 HIS HD2 H 7.274 0.001 1 59 11 11 HIS HE1 H 8.598 0.001 1 60 12 12 HIS H H 8.485 0.002 1 61 12 12 HIS HA H 4.323 0.005 1 62 12 12 HIS HB2 H 3.298 0.005 2 63 12 12 HIS HB3 H 3.074 0.001 2 64 12 12 HIS HD2 H 7.221 0.001 1 65 12 12 HIS HE1 H 8.465 0.001 1 66 13 13 GLN H H 8.346 0.002 1 67 13 13 GLN HA H 4.012 0.002 1 68 13 13 GLN HB2 H 2.211 0.003 2 69 13 13 GLN HB3 H 2.141 0.007 2 70 13 13 GLN HG3 H 2.374 0.002 1 71 13 13 GLN HE21 H 6.626 0.002 1 72 13 13 GLN HE22 H 6.871 0.001 1 73 14 14 LYS H H 8.079 0.002 1 74 14 14 LYS HA H 4.127 0.002 1 75 15 15 LEU H H 7.687 0.003 1 76 15 15 LEU HA H 4.249 0.006 1 77 15 15 LEU HB3 H 1.754 0.002 1 78 15 15 LEU HG H 1.691 0.002 1 79 15 15 LEU HD1 H 0.887 0.002 2 80 15 15 LEU HD2 H 0.924 0.002 2 81 16 16 VAL H H 7.777 0.004 1 82 16 16 VAL HA H 3.672 0.002 1 83 16 16 VAL HB H 2.042 0.005 1 84 16 16 VAL HG2 H 0.862 0.003 1 85 17 17 PHE H H 8.019 0.002 1 86 17 17 PHE HA H 4.398 0.002 1 87 17 17 PHE HB2 H 3.200 0.004 1 88 17 17 PHE HD1 H 7.178 0.002 3 89 17 17 PHE HD2 H 7.178 0.002 3 90 17 17 PHE HE1 H 7.285 0.002 3 91 17 17 PHE HE2 H 7.285 0.002 3 92 18 18 PHE H H 8.329 0.004 1 93 18 18 PHE HA H 4.309 0.004 1 94 18 18 PHE HB2 H 3.285 0.011 1 95 18 18 PHE HD1 H 7.273 0.002 3 96 18 18 PHE HD2 H 7.273 0.002 3 97 18 18 PHE HE1 H 7.297 0.003 3 98 18 18 PHE HE2 H 7.297 0.003 3 99 18 18 PHE HZ H 7.244 0.03 1 100 19 19 ALA H H 8.582 0.005 1 101 19 19 ALA HA H 3.998 0.005 1 102 19 19 ALA HB H 1.533 0.002 1 103 20 20 GLU H H 8.326 0.003 1 104 20 20 GLU HA H 4.169 0.002 1 105 20 20 GLU HB2 H 2.185 0.004 2 106 20 20 GLU HB3 H 2.118 0.006 2 107 20 20 GLU HG2 H 2.645 0.001 2 108 20 20 GLU HG3 H 2.491 0.001 2 109 21 21 ASP H H 8.210 0.003 1 110 21 21 ASP HA H 4.572 0.001 1 111 21 21 ASP HB2 H 2.779 0.005 2 112 21 21 ASP HB3 H 2.809 0.002 2 113 22 22 VAL H H 8.091 0.005 1 114 22 22 VAL HA H 3.822 0.002 1 115 22 22 VAL HB H 1.949 0.002 1 116 22 22 VAL HG1 H 0.832 0.002 2 117 22 22 VAL HG2 H 0.753 0.003 2 118 23 23 GLY H H 8.165 0.002 1 119 23 23 GLY HA2 H 3.896 0.002 1 120 24 24 SER H H 7.913 0.003 1 121 24 24 SER HA H 4.447 0.001 1 122 24 24 SER HB2 H 4.022 0.002 2 123 24 24 SER HB3 H 3.974 0.005 2 124 25 25 ASN H H 8.094 0.003 1 125 25 25 ASN HA H 4.821 0.03 1 126 25 25 ASN HB2 H 2.960 0.002 2 127 25 25 ASN HB3 H 2.848 0.003 2 128 25 25 ASN HD21 H 6.729 0.002 1 129 25 25 ASN HD22 H 7.485 0.003 1 130 26 26 LYS H H 8.251 0.003 1 131 26 26 LYS HA H 4.141 0.002 1 132 26 26 LYS HB2 H 1.899 0.004 1 133 26 26 LYS HG2 H 1.485 0.005 2 134 26 26 LYS HG3 H 1.562 0.003 2 135 27 27 GLY H H 8.361 0.003 1 136 27 27 GLY HA2 H 3.901 0.003 2 137 27 27 GLY HA3 H 3.871 0.004 2 138 28 28 ALA H H 7.801 0.002 1 139 28 28 ALA HA H 4.241 0.002 1 140 28 28 ALA HB H 1.507 0.002 1 141 29 29 ILE H H 7.676 0.003 1 142 29 29 ILE HA H 3.926 0.003 1 143 29 29 ILE HB H 2.019 0.002 1 144 29 29 ILE HG12 H 0.979 0.002 2 145 29 29 ILE HG13 H 1.284 0.03 2 146 29 29 ILE HD1 H 0.902 0.002 1 147 30 30 ILE H H 7.897 0.005 1 148 30 30 ILE HA H 3.868 0.003 1 149 30 30 ILE HB H 1.947 0.003 1 150 30 30 ILE HG12 H 1.265 0.002 2 151 30 30 ILE HG13 H 0.941 0.002 2 152 31 31 GLY H H 7.991 0.001 1 153 31 31 GLY HA2 H 3.823 0.003 2 154 31 31 GLY HA3 H 3.859 0.004 2 155 32 32 LEU H H 7.847 0.003 1 156 32 32 LEU HA H 4.227 0.002 1 157 32 32 LEU HB2 H 1.980 0.002 2 158 32 32 LEU HB3 H 1.830 0.003 2 159 32 32 LEU HG H 1.594 0.002 1 160 32 32 LEU HD1 H 0.910 0.03 2 161 32 32 LEU HD2 H 0.881 0.002 2 162 33 33 MET H H 8.168 0.004 1 163 33 33 MET HA H 4.342 0.004 1 164 33 33 MET HB2 H 2.168 0.002 2 165 33 33 MET HB3 H 2.310 0.003 2 166 33 33 MET HG2 H 2.743 0.003 2 167 33 33 MET HG3 H 2.545 0.003 2 168 34 34 VAL H H 8.455 0.005 1 169 34 34 VAL HA H 4.028 0.002 1 170 34 34 VAL HB H 2.238 0.002 1 171 34 34 VAL HG1 H 1.050 0.003 2 172 34 34 VAL HG2 H 0.982 0.002 2 173 35 35 GLY H H 8.035 0.003 1 174 35 35 GLY HA2 H 3.919 0.006 2 175 35 35 GLY HA3 H 4.082 0.003 2 176 36 36 GLY H H 7.945 0.002 1 177 36 36 GLY HA2 H 4.010 0.002 1 178 37 37 VAL H H 7.883 0.003 1 179 37 37 VAL HA H 4.118 0.001 1 180 37 37 VAL HB H 2.135 0.003 1 181 37 37 VAL HG2 H 0.981 0.002 1 182 38 38 VAL H H 7.566 0.003 1 183 38 38 VAL HA H 4.319 0.004 1 184 38 38 VAL HB H 2.155 0.007 1 185 38 38 VAL HG2 H 0.947 0.006 1 stop_ save_