data_5057 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H Chemical Shift Assignments for Alzheimer peptide Ab(1-40) ; _BMRB_accession_number 5057 _BMRB_flat_file_name bmr5057.str _Entry_type original _Submission_date 2001-06-14 _Accession_date 2001-06-14 _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 Riek Roland . . 2 Guntert Peter . . 3 Dobeli Heinz . . 4 Wipf Beat . . 5 Wuthrich Kurt . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 212 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-29 update BMRB 'Updating non-standard residue' 2002-01-23 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR Studies in Aqueous Solution Fail to Identify Significant Conformational Differences between the Monomeric Forms of Two Alzheimer Peptides with Widely Different Plaque-competence, A beta(1-40)(ox) and A beta(1-42)(ox) ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21579731 _PubMed_ID 11722581 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Riek Roland . . 2 Guntert Peter . . 3 Dobeli Heinz . . 4 Wipf Beat . . 5 Wuthrich Kurt . . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_volume 268 _Journal_issue 22 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5930 _Page_last 5936 _Year 2001 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Dobeli H, Draeger N, Huber G, Jakob P, Schmidt D, Seilheimer B, Stuber D, Wipf B, Zulauf M. A biotechnological method provides access to aggregation competent monomeric Alzheimer's 1-42 residue amyloid peptide. Biotechnology (N Y). 1995 Sep;13(9):988-93. ; _Citation_title 'A biotechnological method provides access to aggregation competent monomeric Alzheimer's 1-42 residue amyloid peptide.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9636276 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Dobeli H. . . 2 Draeger N. . . 3 Huber G. . . 4 Jakob P. . . 5 Schmidt D. . . 6 Seilheimer B. . . 7 Stuber D. . . 8 Wipf B. . . 9 Zulauf M. . . stop_ _Journal_abbreviation 'Biotechnology (N.Y.)' _Journal_name_full 'Bio/technology (Nature Publishing Company)' _Journal_volume 13 _Journal_issue 9 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 988 _Page_last 993 _Year 1995 _Details ; Senile plaques, a neuropathological hallmark of Alzheimer's disease, consist primarily of insoluble aggregates of beta-amyloid peptide (A beta). A 42-residue peptide (A beta 1-42) appears to be the predominant form. In contrast to A beta 1-40, A beta 1-42 is characterized by its extreme tendency to aggregate into fibers or precipitate. A tailored biotechnological method prevents aggregation of A beta 1-42 monomers during its production. The method is based on a protein tail fused to the amino terminus of A beta. This tail leads to a high expression in E. coli, and a histidine affinity tag facilitates purification. Selective cleavage of the fusion tail is performed with cyanogen bromide by immobilizing the fusion protein on a reversed phase chromatography column. Cleavage then occurs only at the methionine positioned at the designed site but not at the methionine contained in the membrane anchor sequence of A beta. Furthermore, immobilization prevents aggregation of cleaved A beta. Elution from the HPLC column and all succeeding purification steps are optimized to preserve A beta 1-42 as a monomer. Solutions of monomeric A beta 1-42 spontaneously aggregate into fibers within hours. This permits the investigation of the transition of monomers into fibers and the correlation of physico-chemical properties with biological activities. Mutations of A beta 1-42 at position 35 influence the aggregation properties. Wild-type A beta 1-42 with methionine at position 35 has similar properties as A beta with a methionine sulfoxide residue. The fiber formation tendency, however, is reduced when position 35 is occupied by a glutamine, serine, leucine, or a glutamic acid residue. ; save_ ################################## # Molecular system description # ################################## save_system_Ab(1-40) _Saveframe_category molecular_system _Mol_system_name 'Alzheimer peptide Ab(1-40) of man' _Abbreviation_common Ab(1-40) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Ab(1-40) $Ab(1-40) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'Ab(1-40) is associated with Alzheimer disease' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Ab(1-40) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Ab _Name_variant Ab(1-40) _Abbreviation_common Ab(1-40) _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 40 _Mol_residue_sequence ; DAEFRHDSGYEVHHQKLVFF AEDVGSNKGAIIGLXVGGVV ; 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 SME 36 VAL 37 GLY 38 GLY 39 VAL 40 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 97.50 97.50 1.14e-17 BMRB 15775 APP_C99 100.00 122 97.50 97.50 8.35e-18 BMRB 17159 Amyloid_beta-Peptide 100.00 40 97.50 97.50 1.14e-17 BMRB 17186 Abeta 100.00 40 97.50 97.50 1.14e-17 BMRB 17764 Abeta 100.00 40 97.50 97.50 1.14e-17 BMRB 17793 Abeta(1-42) 100.00 42 97.50 97.50 9.29e-18 BMRB 17794 Abeta(1-42) 100.00 42 97.50 97.50 9.29e-18 BMRB 17795 Abeta(1-40) 100.00 40 97.50 97.50 1.14e-17 BMRB 17796 Abeta40 100.00 40 97.50 97.50 1.14e-17 BMRB 18052 Pyroglutamate_Abeta 92.50 38 97.30 97.30 2.04e-15 BMRB 18127 beta-amyloid 100.00 40 97.50 97.50 1.14e-17 BMRB 18128 beta-amyloid 100.00 40 97.50 97.50 1.14e-17 BMRB 18129 beta-amyloid 100.00 40 97.50 97.50 1.14e-17 BMRB 18131 beta-amyloid 100.00 40 97.50 97.50 1.14e-17 BMRB 19009 beta-amyloid_peptide 100.00 40 97.50 97.50 1.14e-17 BMRB 19309 amyloid_peptide 100.00 40 97.50 97.50 1.14e-17 BMRB 5400 Abeta1-42 100.00 42 97.50 97.50 9.29e-18 BMRB 6257 Abeta 100.00 40 97.50 97.50 1.14e-17 BMRB 6554 amyloid 100.00 42 97.50 97.50 9.29e-18 PDB 1AMB "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" 70.00 28 100.00 100.00 1.71e-10 PDB 1AMC "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" 70.00 28 100.00 100.00 1.71e-10 PDB 1AML "The Alzheimer`s Disease Amyloid A4 Peptide (Residues 1-40)" 100.00 40 97.50 97.50 1.14e-17 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 97.50 97.50 1.14e-17 PDB 1BA6 "Solution Structure Of The Methionine-Oxidized Amyloid Beta- Peptide (1-40). Does Oxidation Affect Conformational Switching? Nmr" 100.00 40 100.00 100.00 1.75e-17 PDB 1HZ3 "Alzheimer's Disease Amyloid-Beta Peptide (Residues 10-35)" 62.50 26 100.00 100.00 1.09e-07 PDB 1IYT "Solution Structure Of The Alzheimer's Disease Amyloid Beta- Peptide (1-42)" 100.00 42 97.50 97.50 9.29e-18 PDB 1Z0Q "Aqueous Solution Structure Of The Alzheimer's Disease Abeta Peptide (1-42)" 100.00 42 97.50 97.50 9.29e-18 PDB 2BEG "3d Structure Of Alzheimer's Abeta(1-42) Fibrils" 100.00 42 97.50 97.50 9.29e-18 PDB 2G47 "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-40)" 100.00 40 97.50 97.50 1.14e-17 PDB 2LFM "A Partially Folded Structure Of Amyloid-Beta(1 40) In An Aqueous Environment" 100.00 40 97.50 97.50 1.14e-17 PDB 2LMN "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Positive Stagger" 100.00 40 97.50 97.50 1.14e-17 PDB 2LMO "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Negative Stagger" 100.00 40 97.50 97.50 1.14e-17 PDB 2LMP "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Positive Stagger" 100.00 40 97.50 97.50 1.14e-17 PDB 2LMQ "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Negative Stagger" 100.00 40 97.50 97.50 1.14e-17 PDB 2LP1 "The Solution Nmr Structure Of The Transmembrane C-Terminal Domain Of The Amyloid Precursor Protein (C99)" 100.00 122 97.50 97.50 8.35e-18 PDB 2M4J "40-residue Beta-amyloid Fibril Derived From Alzheimer's Disease Brain" 100.00 40 97.50 97.50 1.14e-17 PDB 2M9R "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" 100.00 40 97.50 97.50 1.14e-17 PDB 2M9S "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" 100.00 40 97.50 97.50 1.14e-17 PDB 2OTK "Structure Of Alzheimer Ab Peptide In Complex With An Engineered Binding Protein" 100.00 40 97.50 97.50 1.14e-17 PDB 2WK3 "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-42)" 100.00 42 97.50 97.50 9.29e-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 1.71e-10 PDB 3IFN "X-ray Structure Of Amyloid Beta Peptide:antibody (abeta1-40:12a11) Complex" 100.00 40 97.50 97.50 1.14e-17 PDB 4HIX "Crystal Structure Of A Humanised 3d6 Fab Bound To Amyloid Beta Peptide" 70.00 28 100.00 100.00 1.71e-10 PDB 4M1C "Crystal Structure Analysis Of Fab-bound Human Insulin Degrading Enzyme (ide) In Complex With Amyloid-beta (1-40)" 100.00 40 97.50 97.50 1.14e-17 PDB 4NGE "Crystal Structure Of Human Presequence Protease In Complex With Amyloid-beta (1-40)" 100.00 40 97.50 97.50 1.14e-17 PDB 4ONG "Fab Fragment Of 3d6 In Complex With Amyloid Beta 1-40" 100.00 40 97.50 97.50 1.14e-17 DBJ BAA22264 "amyloid precursor protein [Homo sapiens]" 100.00 770 97.50 97.50 7.63e-18 DBJ BAA84580 "amyloid precursor protein [Sus scrofa]" 100.00 770 97.50 97.50 7.63e-18 DBJ BAD51938 "amyloid beta A4 precursor protein [Macaca fascicularis]" 100.00 696 97.50 97.50 6.85e-18 DBJ BAE01907 "unnamed protein product [Macaca fascicularis]" 100.00 751 97.50 97.50 9.04e-18 DBJ BAG10647 "amyloid beta A4 protein precursor [synthetic construct]" 100.00 770 97.50 97.50 7.63e-18 EMBL CAA30050 "amyloid A4 protein [Homo sapiens]" 100.00 751 97.50 97.50 8.53e-18 EMBL CAA31830 "A4 amyloid protein precursor [Homo sapiens]" 100.00 695 97.50 97.50 8.47e-18 EMBL CAA39589 "amyloid precursor protein [Bos taurus]" 100.00 59 97.50 97.50 2.03e-18 EMBL CAA39590 "amyloid precursor protein [Canis lupus familiaris]" 100.00 58 97.50 97.50 2.26e-18 EMBL CAA39591 "amyloid precursor protein [Cavia sp.]" 100.00 58 97.50 97.50 2.26e-18 GB AAA35540 "amyloid protein, partial [Homo sapiens]" 95.00 97 97.37 97.37 1.50e-16 GB AAA36829 "amyloid b-protein precursor [Macaca fascicularis]" 100.00 695 97.50 97.50 9.25e-18 GB AAA51564 "amyloid beta protein, partial [Homo sapiens]" 75.00 30 100.00 100.00 8.92e-12 GB AAA51722 "amyloid beta-protein precursor, partial [Homo sapiens]" 100.00 412 97.50 97.50 5.76e-18 GB AAA51726 "beta-amyloid A4, partial [Homo sapiens]" 100.00 264 97.50 97.50 8.67e-18 PIR A60045 "Alzheimer's disease amyloid beta/A4 protein precursor - dog (fragment)" 100.00 57 97.50 97.50 2.14e-18 PIR D60045 "Alzheimer's disease amyloid beta/A4 protein precursor - bovine (fragment)" 100.00 57 97.50 97.50 2.14e-18 PIR E60045 "Alzheimer's disease amyloid beta/A4 protein precursor - sheep (fragment)" 100.00 57 97.50 97.50 2.14e-18 PIR G60045 "Alzheimer's disease amyloid beta/A4 protein precursor - guinea pig (fragment)" 100.00 57 97.50 97.50 2.14e-18 PIR PQ0438 "Alzheimer's disease amyloid A4 protein precursor - rabbit (fragment)" 100.00 82 97.50 97.50 2.88e-18 PRF 1303338A "amyloid A4 protein precursor" 100.00 695 97.50 97.50 9.25e-18 PRF 1403400A "amyloid protein A4" 100.00 751 97.50 97.50 8.53e-18 PRF 1405204A "amyloid protein" 100.00 42 97.50 97.50 9.29e-18 PRF 1507304A "beta amyloid peptide precursor" 100.00 412 97.50 97.50 5.82e-18 PRF 1507304B "beta amyloid peptide precursor" 100.00 574 97.50 97.50 3.03e-17 REF NP_000475 "amyloid beta A4 protein isoform a precursor [Homo sapiens]" 100.00 770 97.50 97.50 7.63e-18 REF NP_001006601 "amyloid beta A4 protein isoform APP-770 precursor [Canis lupus familiaris]" 100.00 770 97.50 97.50 7.63e-18 REF NP_001013036 "amyloid beta A4 protein precursor [Pan troglodytes]" 100.00 770 97.50 97.50 7.63e-18 REF NP_001070264 "amyloid beta A4 protein precursor [Bos taurus]" 100.00 695 97.50 97.50 8.99e-18 REF NP_001127014 "amyloid beta A4 protein precursor [Pongo abelii]" 100.00 695 97.50 97.50 1.07e-17 SP P05067 "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; AltName: Full=APPI; Short=APP; AltName: Full=Alzheimer disease amylo" 100.00 770 97.50 97.50 7.63e-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 97.50 97.50 7.63e-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 97.50 97.50 7.63e-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 97.50 97.50 2.03e-18 SP Q28280 "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" 100.00 58 97.50 97.50 2.26e-18 TPG DAA33655 "TPA: amyloid beta A4 protein [Bos taurus]" 100.00 695 97.50 97.50 8.99e-18 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_SME _Saveframe_category polymer_residue _Mol_type 'L-peptide linking' _Name_common 'METHIONINE SULFOXIDE' _BMRB_code . _PDB_code SME _Standard_residue_derivative . _Molecular_mass 165.211 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jul 20 15:14:56 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 . ? S S S . 0 . ? OE OE O . 0 . ? CE CE C . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG2 HG2 H . 0 . ? HG3 HG3 H . 0 . ? HE1 HE1 H . 0 . ? HE2 HE2 H . 0 . ? HE3 HE3 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 H ? ? SING N H2 ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG S ? ? SING CG HG2 ? ? SING CG HG3 ? ? DOUB S OE ? ? SING S CE ? ? SING CE HE1 ? ? SING CE HE2 ? ? SING CE HE3 ? ? 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 $Ab(1-40) 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 _Details $Ab(1-40) 'recombinant technology' . . . . . 'Ab is expressed and purified on the basis of ref_1.' 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_max_value _Isotopic_labeling $Ab(1-40) . mM 1 . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 0.1 n/a temperature 281 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Ab(1-40) _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 ASP HA H 4.50 0.01 1 2 . 1 ASP HB2 H 2.55 0.01 2 3 . 1 ASP HB3 H 2.69 0.01 2 4 . 2 ALA H H 7.88 0.01 1 5 . 2 ALA HA H 4.09 0.01 1 6 . 2 ALA HB H 1.21 0.01 1 7 . 3 GLU H H 8.35 0.01 1 8 . 3 GLU HA H 4.01 0.01 1 9 . 3 GLU HB2 H 1.71 0.01 2 10 . 3 GLU HB3 H 1.76 0.01 2 11 . 3 GLU HG2 H 1.97 0.01 2 12 . 3 GLU HG3 H 2.05 0.01 2 13 . 4 PHE H H 8.23 0.01 1 14 . 4 PHE HA H 4.39 0.01 1 15 . 4 PHE HB2 H 2.84 0.01 1 16 . 4 PHE HB3 H 2.84 0.01 1 17 . 4 PHE HD1 H 7.00 0.01 1 18 . 4 PHE HD2 H 7.00 0.01 1 19 . 4 PHE HE1 H 7.09 0.01 1 20 . 4 PHE HE2 H 7.09 0.01 1 21 . 4 PHE HZ H 7.10 0.01 1 22 . 5 ARG H H 8.08 0.01 1 23 . 5 ARG HA H 4.08 0.01 1 24 . 5 ARG HB2 H 1.46 0.01 2 25 . 5 ARG HB3 H 1.57 0.01 2 26 . 5 ARG HG2 H 1.33 0.01 1 27 . 5 ARG HG3 H 1.33 0.01 1 28 . 5 ARG HD2 H 2.95 0.01 1 29 . 5 ARG HD3 H 2.95 0.01 1 30 . 7 ASP H H 8.30 0.01 1 31 . 7 ASP HA H 4.46 0.01 1 32 . 7 ASP HB2 H 2.51 0.01 1 33 . 7 ASP HB3 H 2.51 0.01 1 34 . 8 SER H H 8.35 0.01 1 35 . 8 SER HA H 4.21 0.01 1 36 . 8 SER HB2 H 3.75 0.01 2 37 . 8 SER HB3 H 3.70 0.01 2 38 . 9 GLY H H 8.45 0.01 1 39 . 9 GLY HA2 H 3.77 0.01 2 40 . 9 GLY HA3 H 3.71 0.01 2 41 . 10 TYR H H 7.86 0.01 1 42 . 10 TYR HA H 4.33 0.01 1 43 . 10 TYR HB2 H 2.85 0.01 2 44 . 10 TYR HB3 H 2.79 0.01 2 45 . 10 TYR HD1 H 6.88 0.01 1 46 . 10 TYR HD2 H 6.88 0.01 1 47 . 10 TYR HE1 H 6.59 0.01 1 48 . 10 TYR HE2 H 6.59 0.01 1 49 . 11 GLU H H 8.28 0.01 1 50 . 11 GLU HA H 4.03 0.01 1 51 . 11 GLU HB2 H 1.69 0.01 1 52 . 11 GLU HB3 H 1.69 0.01 1 53 . 11 GLU HG2 H 2.04 0.01 1 54 . 11 GLU HG3 H 2.04 0.01 1 55 . 12 VAL H H 7.97 0.01 1 56 . 12 VAL HA H 3.75 0.01 1 57 . 12 VAL HB H 1.76 0.01 1 58 . 12 VAL HG1 H 0.70 0.01 2 59 . 12 VAL HG2 H 0.59 0.01 2 60 . 13 HIS H H 8.22 0.01 1 61 . 13 HIS HA H 4.44 0.01 1 62 . 13 HIS HB2 H 2.91 0.01 2 63 . 13 HIS HB3 H 2.85 0.01 2 64 . 13 HIS HD1 H 6.86 0.01 1 65 . 14 HIS H H 8.29 0.01 1 66 . 14 HIS HA H 4.40 0.01 1 67 . 14 HIS HB2 H 2.96 0.01 2 68 . 14 HIS HB3 H 2.90 0.01 2 69 . 14 HIS HD1 H 6.87 0.01 1 70 . 15 GLN H H 8.35 0.01 1 71 . 15 GLN HA H 4.11 0.01 1 72 . 15 GLN HB2 H 1.81 0.01 2 73 . 15 GLN HB3 H 1.89 0.01 2 74 . 15 GLN HG2 H 2.17 0.01 1 75 . 15 GLN HG3 H 2.17 0.01 1 76 . 15 GLN HE21 H 6.80 0.01 2 77 . 15 GLN HE22 H 7.48 0.01 2 78 . 16 LYS H H 8.33 0.01 1 79 . 16 LYS HA H 4.11 0.01 1 80 . 16 LYS HB2 H 1.63 0.01 2 81 . 16 LYS HB3 H 1.58 0.01 2 82 . 16 LYS HG2 H 1.27 0.01 2 83 . 16 LYS HG3 H 1.20 0.01 2 84 . 16 LYS HD2 H 1.50 0.01 1 85 . 16 LYS HD3 H 1.50 0.01 1 86 . 16 LYS HE2 H 2.80 0.01 1 87 . 16 LYS HE3 H 2.80 0.01 1 88 . 17 LEU H H 8.19 0.01 1 89 . 17 LEU HA H 4.17 0.01 1 90 . 17 LEU HB2 H 1.43 0.01 1 91 . 17 LEU HB3 H 1.43 0.01 1 92 . 17 LEU HG H 1.27 0.01 1 93 . 17 LEU HD1 H 0.67 0.01 2 94 . 17 LEU HD2 H 0.74 0.01 2 95 . 18 VAL H H 7.92 0.01 1 96 . 18 VAL HA H 3.86 0.01 1 97 . 18 VAL HB H 1.73 0.01 1 98 . 18 VAL HG1 H 0.67 0.01 2 99 . 18 VAL HG2 H 0.58 0.01 2 100 . 19 PHE H H 8.18 0.01 1 101 . 19 PHE HA H 4.41 0.01 1 102 . 19 PHE HB2 H 2.81 0.01 2 103 . 19 PHE HB3 H 2.74 0.01 2 104 . 19 PHE HD1 H 6.99 0.01 1 105 . 19 PHE HD2 H 6.99 0.01 1 106 . 19 PHE HE1 H 7.14 0.01 1 107 . 19 PHE HE2 H 7.14 0.01 1 108 . 19 PHE HZ H 7.11 0.01 1 109 . 20 PHE H H 8.14 0.01 1 110 . 20 PHE HA H 4.40 0.01 1 111 . 20 PHE HB2 H 2.91 0.01 2 112 . 20 PHE HB3 H 2.76 0.01 2 113 . 20 PHE HD1 H 7.06 0.01 1 114 . 20 PHE HD2 H 7.06 0.01 1 115 . 20 PHE HE1 H 7.15 0.01 1 116 . 20 PHE HE2 H 7.15 0.01 1 117 . 20 PHE HZ H 7.11 0.01 1 118 . 21 ALA H H 8.16 0.01 1 119 . 21 ALA HA H 4.05 0.01 1 120 . 21 ALA HB H 1.20 0.01 1 121 . 22 GLU H H 8.28 0.01 1 122 . 22 GLU HA H 4.04 0.01 1 123 . 22 GLU HB2 H 1.75 0.01 2 124 . 22 GLU HB3 H 1.87 0.01 2 125 . 22 GLU HG2 H 2.10 0.01 1 126 . 22 GLU HG3 H 2.10 0.01 1 127 . 23 ASP H H 8.34 0.01 1 128 . 23 ASP HA H 4.47 0.01 1 129 . 23 ASP HB2 H 2.57 0.01 2 130 . 23 ASP HB3 H 2.46 0.01 2 131 . 24 VAL H H 8.07 0.01 1 132 . 24 VAL HA H 3.96 0.01 1 133 . 24 VAL HB H 2.02 0.01 1 134 . 24 VAL HG1 H 0.79 0.01 1 135 . 24 VAL HG2 H 0.79 0.01 1 136 . 25 GLY H H 8.46 0.01 1 137 . 25 GLY HA2 H 3.81 0.01 1 138 . 25 GLY HA3 H 3.81 0.01 1 139 . 26 SER H H 8.05 0.01 1 140 . 26 SER HA H 4.25 0.01 1 141 . 26 SER HB2 H 3.74 0.01 2 142 . 26 SER HB3 H 3.70 0.01 2 143 . 27 ASN H H 8.39 0.01 1 144 . 27 ASN HA H 4.57 0.01 1 145 . 27 ASN HB2 H 2.71 0.01 2 146 . 27 ASN HB3 H 2.63 0.01 2 147 . 27 ASN HD21 H 6.83 0.01 2 148 . 27 ASN HD22 H 7.55 0.01 2 149 . 28 LYS H H 8.26 0.01 1 150 . 28 LYS HA H 4.10 0.01 1 151 . 28 LYS HB2 H 1.60 0.01 2 152 . 28 LYS HB3 H 1.72 0.01 2 153 . 28 LYS HG2 H 1.30 0.01 2 154 . 28 LYS HG3 H 1.24 0.01 2 155 . 28 LYS HD2 H 1.50 0.01 2 156 . 28 LYS HE2 H 2.81 0.01 1 157 . 28 LYS HE3 H 2.81 0.01 1 158 . 29 GLY H H 8.33 0.01 1 159 . 29 GLY HA2 H 3.75 0.01 1 160 . 29 GLY HA3 H 3.75 0.01 1 161 . 30 ALA H H 7.95 0.01 1 162 . 30 ALA HA H 4.13 0.01 1 163 . 30 ALA HB H 1.20 0.01 1 164 . 31 ILE H H 8.10 0.01 1 165 . 31 ILE HA H 3.98 0.01 1 166 . 31 ILE HB H 1.69 0.01 1 167 . 31 ILE HG2 H 0.70 0.01 1 168 . 31 ILE HG12 H 1.03 0.01 2 169 . 31 ILE HG13 H 1.33 0.01 2 170 . 31 ILE HD1 H 0.70 0.01 1 171 . 32 ILE H H 8.21 0.01 1 172 . 32 ILE HA H 3.99 0.01 1 173 . 32 ILE HB H 1.69 0.01 1 174 . 32 ILE HG12 H 1.04 0.01 2 175 . 32 ILE HG13 H 1.33 0.01 2 176 . 32 ILE HD1 H 0.75 0.01 1 177 . 33 GLY H H 8.39 0.01 1 178 . 33 GLY HA2 H 3.80 0.01 2 179 . 33 GLY HA3 H 3.75 0.01 2 180 . 34 LEU H H 7.99 0.01 1 181 . 34 LEU HA H 4.17 0.01 1 182 . 34 LEU HB2 H 1.44 0.01 1 183 . 34 LEU HB3 H 1.44 0.01 1 184 . 34 LEU HG H 1.44 0.01 1 185 . 34 LEU HD1 H 0.71 0.01 2 186 . 34 LEU HD2 H 0.76 0.01 2 187 . 35 SME H H 8.54 0.01 1 188 . 35 SME HA H 4.42 0.01 1 189 . 35 SME HB2 H 2.08 0.01 2 190 . 35 SME HB3 H 2.00 0.01 2 191 . 35 SME HG2 H 2.79 0.01 2 192 . 35 SME HG3 H 2.79 0.01 2 193 . 36 VAL H H 8.29 0.01 1 194 . 36 VAL HA H 3.97 0.01 1 195 . 36 VAL HB H 1.92 0.01 1 196 . 36 VAL HG2 H 0.78 0.01 2 197 . 37 GLY H H 8.53 0.01 1 198 . 37 GLY HA2 H 3.82 0.01 1 199 . 37 GLY HA3 H 3.82 0.01 1 200 . 38 GLY H H 8.20 0.01 1 201 . 38 GLY HA2 H 3.85 0.01 2 202 . 38 GLY HA3 H 3.77 0.01 2 203 . 39 VAL H H 8.01 0.01 1 204 . 39 VAL HA H 4.00 0.01 1 205 . 39 VAL HB H 1.91 0.01 1 206 . 39 VAL HG1 H 0.77 0.01 1 207 . 39 VAL HG2 H 0.77 0.01 1 208 . 40 VAL H H 7.73 0.01 1 209 . 40 VAL HA H 4.01 0.01 1 210 . 40 VAL HB H 1.91 0.01 1 211 . 40 VAL HG1 H 0.77 0.01 2 212 . 40 VAL HG2 H 0.75 0.01 2 stop_ save_