data_18129
#######################
# Entry information #
#######################
save_entry_information
_Entry.Sf_category entry_information
_Entry.Sf_framecode entry_information
_Entry.ID 18129
_Entry.Title
;
Structural Model for a 40-residue Beta-Amyloid Fibril with Three-Fold Symmetry, Positive Stagger
;
_Entry.Type macromolecule
_Entry.Version_type original
_Entry.Submission_date 2011-12-08
_Entry.Accession_date 2011-12-08
_Entry.Last_release_date .
_Entry.Original_release_date .
_Entry.Origination author
_Entry.NMR_STAR_version 3.1.1.61
_Entry.Original_NMR_STAR_version 3.1
_Entry.Experimental_method NMR
_Entry.Experimental_method_subtype SOLID-STATE
_Entry.Details .
_Entry.BMRB_internal_directory_name .
loop_
_Entry_author.Ordinal
_Entry_author.Given_name
_Entry_author.Family_name
_Entry_author.First_initial
_Entry_author.Middle_initials
_Entry_author.Family_title
_Entry_author.Entry_ID
1 Robert Tycko . . . 18129
2 Anant Paravastu . . . 18129
stop_
loop_
_SG_project.SG_project_ID
_SG_project.Project_name
_SG_project.Full_name_of_center
_SG_project.Initial_of_center
_SG_project.Entry_ID
1 'not applicable' 'not applicable' . 18129
stop_
loop_
_Struct_keywords.Keywords
_Struct_keywords.Text
_Struct_keywords.Entry_ID
'Alzheimer's disease' . 18129
amyloid . 18129
'three-fold symmetry' . 18129
stop_
loop_
_Data_set.Type
_Data_set.Count
_Data_set.Entry_ID
assigned_chemical_shifts 1 18129
stop_
loop_
_Datum.Type
_Datum.Count
_Datum.Entry_ID
'13C chemical shifts' 90 18129
stop_
loop_
_Release.Release_number
_Release.Format_type
_Release.Format_version
_Release.Date
_Release.Submission_date
_Release.Type
_Release.Author
_Release.Detail
_Release.Entry_ID
2 . . 2012-01-11 2011-12-08 update author 'update chemical shifts' 18129
1 . . 2012-01-05 2011-12-08 original author 'original release' 18129
stop_
loop_
_Related_entries.Database_name
_Related_entries.Database_accession_code
_Related_entries.Relationship
_Related_entries.Entry_ID
BMRB 18127 '40-Residue Beta-Amyloid Fibril with Two-Fold Symmetry' 18129
BMRB 18128 '40-Residue Beta-Amyloid Fibril with Two-Fold Symmetry, Negative Stagger' 18129
BMRB 18131 '40-residue Beta-Amyloid Fibril with Three-Fold Symmetry, Negative Stagger' 18129
PDB 2LMP 'BMRB Entry Tracking System' 18129
stop_
save_
###############
# Citations #
###############
save_citation_1
_Citation.Sf_category citations
_Citation.Sf_framecode citation_1
_Citation.Entry_ID 18129
_Citation.ID 1
_Citation.Class 'entry citation'
_Citation.CAS_abstract_code .
_Citation.MEDLINE_UI_code .
_Citation.DOI .
_Citation.PubMed_ID 16401079
_Citation.Full_citation .
_Citation.Title 'Molecular structural basis for polymorphism in Alzheimer's beta-amyloid fibrils'
_Citation.Status published
_Citation.Type journal
_Citation.Journal_abbrev 'Proc. Natl. Acad. Sci. U.S.A.'
_Citation.Journal_name_full .
_Citation.Journal_volume 105
_Citation.Journal_issue 47
_Citation.Journal_ASTM .
_Citation.Journal_ISSN .
_Citation.Journal_CSD .
_Citation.Book_title .
_Citation.Book_chapter_title .
_Citation.Book_volume .
_Citation.Book_series .
_Citation.Book_publisher .
_Citation.Book_publisher_city .
_Citation.Book_ISBN .
_Citation.Conference_title .
_Citation.Conference_site .
_Citation.Conference_state_province .
_Citation.Conference_country .
_Citation.Conference_start_date .
_Citation.Conference_end_date .
_Citation.Conference_abstract_number .
_Citation.Thesis_institution .
_Citation.Thesis_institution_city .
_Citation.Thesis_institution_country .
_Citation.WWW_URL .
_Citation.Page_first 18349
_Citation.Page_last 18354
_Citation.Year 2008
_Citation.Details .
loop_
_Citation_author.Ordinal
_Citation_author.Given_name
_Citation_author.Family_name
_Citation_author.First_initial
_Citation_author.Middle_initials
_Citation_author.Family_title
_Citation_author.Entry_ID
_Citation_author.Citation_ID
1 Anant Paravastu . . . 18129 1
2 Richard Leapman . . . 18129 1
3 Wai-Ming Yau . . . 18129 1
4 Robert Tycko . . . 18129 1
stop_
save_
#############################################
# Molecular system (assembly) description #
#############################################
save_assembly
_Assembly.Sf_category assembly
_Assembly.Sf_framecode assembly
_Assembly.Entry_ID 18129
_Assembly.ID 1
_Assembly.Name '40-residue Beta-Amyloid Fibril with Three-Fold Symmetry, Positive Stagger'
_Assembly.BMRB_code .
_Assembly.Number_of_components 18
_Assembly.Organic_ligands .
_Assembly.Metal_ions .
_Assembly.Non_standard_bonds .
_Assembly.Ambiguous_conformational_states .
_Assembly.Ambiguous_chem_comp_sites .
_Assembly.Molecules_in_chemical_exchange .
_Assembly.Paramagnetic no
_Assembly.Thiol_state .
_Assembly.Molecular_mass .
_Assembly.Enzyme_commission_number .
_Assembly.Details .
_Assembly.DB_query_date .
_Assembly.DB_query_revised_last_date .
loop_
_Entity_assembly.ID
_Entity_assembly.Entity_assembly_name
_Entity_assembly.Entity_ID
_Entity_assembly.Entity_label
_Entity_assembly.Asym_ID
_Entity_assembly.PDB_chain_ID
_Entity_assembly.Experimental_data_reported
_Entity_assembly.Physical_state
_Entity_assembly.Conformational_isomer
_Entity_assembly.Chemical_exchange_state
_Entity_assembly.Magnetic_equivalence_group_code
_Entity_assembly.Role
_Entity_assembly.Details
_Entity_assembly.Entry_ID
_Entity_assembly.Assembly_ID
1 entity_1 1 $beta-amyloid A . yes native no no . . . 18129 1
2 entity_2 1 $beta-amyloid B . yes native no no . . . 18129 1
3 entity_3 1 $beta-amyloid C . yes native no no . . . 18129 1
4 entity_4 1 $beta-amyloid D . yes native no no . . . 18129 1
5 entity_5 1 $beta-amyloid E . yes native no no . . . 18129 1
6 entity_6 1 $beta-amyloid F . yes native no no . . . 18129 1
7 entity_7 1 $beta-amyloid G . yes native no no . . . 18129 1
8 entity_8 1 $beta-amyloid H . yes native no no . . . 18129 1
9 entity_9 1 $beta-amyloid I . yes native no no . . . 18129 1
10 entity_10 1 $beta-amyloid J . yes native no no . . . 18129 1
11 entity_11 1 $beta-amyloid K . yes native no no . . . 18129 1
12 entity_12 1 $beta-amyloid L . yes native no no . . . 18129 1
13 entity_13 1 $beta-amyloid M . yes native no no . . . 18129 1
14 entity_14 1 $beta-amyloid N . yes native no no . . . 18129 1
15 entity_15 1 $beta-amyloid O . yes native no no . . . 18129 1
16 entity_16 1 $beta-amyloid P . yes native no no . . . 18129 1
17 entity_17 1 $beta-amyloid Q . yes native no no . . . 18129 1
18 entity_18 1 $beta-amyloid R . yes native no no . . . 18129 1
stop_
save_
####################################
# Biological polymers and ligands #
####################################
save_beta-amyloid
_Entity.Sf_category entity
_Entity.Sf_framecode beta-amyloid
_Entity.Entry_ID 18129
_Entity.ID 1
_Entity.BMRB_code .
_Entity.Name beta-amyloid
_Entity.Type polymer
_Entity.Polymer_common_type .
_Entity.Polymer_type polypeptide(L)
_Entity.Polymer_type_details .
_Entity.Polymer_strand_ID A-R
_Entity.Polymer_seq_one_letter_code_can .
_Entity.Polymer_seq_one_letter_code
;
DAEFRHDSGYEVHHQKLVFF
AEDVGSNKGAIIGLMVGGVV
;
_Entity.Target_identifier .
_Entity.Polymer_author_defined_seq .
_Entity.Polymer_author_seq_details .
_Entity.Ambiguous_conformational_states no
_Entity.Ambiguous_chem_comp_sites no
_Entity.Nstd_monomer no
_Entity.Nstd_chirality no
_Entity.Nstd_linkage no
_Entity.Nonpolymer_comp_ID .
_Entity.Nonpolymer_comp_label .
_Entity.Number_of_monomers 40
_Entity.Number_of_nonpolymer_components .
_Entity.Paramagnetic no
_Entity.Thiol_state 'not present'
_Entity.Src_method man
_Entity.Parent_entity_ID .
_Entity.Fragment .
_Entity.Mutation .
_Entity.EC_number .
_Entity.Calc_isoelectric_point .
_Entity.Formula_weight 3375.924
_Entity.Formula_weight_exptl .
_Entity.Formula_weight_exptl_meth .
_Entity.Details .
_Entity.DB_query_date .
_Entity.DB_query_revised_last_date 2015-11-25
loop_
_Entity_db_link.Ordinal
_Entity_db_link.Author_supplied
_Entity_db_link.Database_code
_Entity_db_link.Accession_code
_Entity_db_link.Entry_mol_code
_Entity_db_link.Entry_mol_name
_Entity_db_link.Entry_experimental_method
_Entity_db_link.Entry_structure_resolution
_Entity_db_link.Entry_relation_type
_Entity_db_link.Entry_details
_Entity_db_link.Chimera_segment_ID
_Entity_db_link.Seq_query_to_submitted_percent
_Entity_db_link.Seq_subject_length
_Entity_db_link.Seq_identity
_Entity_db_link.Seq_positive
_Entity_db_link.Seq_homology_expectation_val
_Entity_db_link.Seq_align_begin
_Entity_db_link.Seq_align_end
_Entity_db_link.Seq_difference_details
_Entity_db_link.Seq_alignment_details
_Entity_db_link.Entry_ID
_Entity_db_link.Entity_ID
1 no BMRB 11435 . Amyloid-beta-(1-40) . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
2 no BMRB 15775 . APP_C99 . . . . . 100.00 122 100.00 100.00 1.20e-18 . . . . 18129 1
3 no BMRB 17159 . Amyloid_beta-Peptide . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
4 no BMRB 17186 . Abeta . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
5 no BMRB 17764 . Abeta . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
6 no BMRB 17793 . Abeta(1-42) . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 18129 1
7 no BMRB 17794 . Abeta(1-42) . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 18129 1
8 no BMRB 17795 . Abeta(1-40) . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
9 no BMRB 17796 . Abeta40 . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
10 no BMRB 18052 . Pyroglutamate_Abeta . . . . . 92.50 38 100.00 100.00 2.74e-16 . . . . 18129 1
11 no BMRB 18127 . beta-amyloid . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
12 no BMRB 18128 . beta-amyloid . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
13 no BMRB 18131 . beta-amyloid . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
14 no BMRB 19009 . beta-amyloid_peptide . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
15 no BMRB 19309 . amyloid_peptide . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
16 no BMRB 19393 . Abeta . . . . . 100.00 39 97.50 97.50 5.36e-16 . . . . 18129 1
17 no BMRB 25218 . amyloid_peptide . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 18129 1
18 no BMRB 25289 . amyloid_beta . . . . . 100.00 39 97.50 97.50 5.36e-16 . . . . 18129 1
19 no BMRB 25429 . entity . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 18129 1
20 no BMRB 26508 . amyloid_B . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
21 no BMRB 26516 . amyloid_B . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
22 no PDB 1AMB . "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" . . . . . 70.00 28 100.00 100.00 2.11e-10 . . . . 18129 1
23 no PDB 1AMC . "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" . . . . . 70.00 28 100.00 100.00 2.11e-10 . . . . 18129 1
24 no PDB 1AML . "The Alzheimer`s Disease Amyloid A4 Peptide (Residues 1-40)" . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
25 no 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 1.49e-18 . . . . 18129 1
26 no 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 1.67e-17 . . . . 18129 1
27 no PDB 1HZ3 . "Alzheimer's Disease Amyloid-Beta Peptide (Residues 10-35)" . . . . . 65.00 26 100.00 100.00 2.06e-08 . . . . 18129 1
28 no PDB 1IYT . "Solution Structure Of The Alzheimer's Disease Amyloid Beta- Peptide (1-42)" . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 18129 1
29 no PDB 1Z0Q . "Aqueous Solution Structure Of The Alzheimer's Disease Abeta Peptide (1-42)" . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 18129 1
30 no PDB 2BEG . "3d Structure Of Alzheimer's Abeta(1-42) Fibrils" . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 18129 1
31 no PDB 2G47 . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-40)" . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
32 no PDB 2LFM . "A Partially Folded Structure Of Amyloid-Beta(1 40) In An Aqueous Environment" . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
33 no PDB 2LMN . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Positive Stagger" . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
34 no PDB 2LMO . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Negative Stagger" . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
35 no PDB 2LMP . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Positive Stagger" . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
36 no PDB 2LMQ . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Negative Stagger" . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
37 no PDB 2LNQ . "40-residue D23n Beta Amyloid Fibril" . . . . . 100.00 40 97.50 100.00 5.11e-18 . . . . 18129 1
38 no 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 1.20e-18 . . . . 18129 1
39 no PDB 2M4J . "40-residue Beta-amyloid Fibril Derived From Alzheimer's Disease Brain" . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
40 no 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 1.49e-18 . . . . 18129 1
41 no 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 1.49e-18 . . . . 18129 1
42 no PDB 2MVX . "Atomic-resolution 3d Structure Of Amyloid-beta Fibrils: The Osaka Mutation" . . . . . 100.00 39 97.50 97.50 5.36e-16 . . . . 18129 1
43 no PDB 2MXU . "42-residue Beta Amyloid Fibril" . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 18129 1
44 no PDB 2OTK . "Structure Of Alzheimer Ab Peptide In Complex With An Engineered Binding Protein" . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
45 no PDB 2WK3 . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-42)" . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 18129 1
46 no 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 2.11e-10 . . . . 18129 1
47 no PDB 3IFN . "X-ray Structure Of Amyloid Beta Peptide:antibody (abeta1-40:12a11) Complex" . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
48 no PDB 4HIX . "Crystal Structure Of A Humanised 3d6 Fab Bound To Amyloid Beta Peptide" . . . . . 70.00 28 100.00 100.00 2.11e-10 . . . . 18129 1
49 no 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 1.49e-18 . . . . 18129 1
50 no 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 1.49e-18 . . . . 18129 1
51 no 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 1.49e-18 . . . . 18129 1
52 no PDB 4NGE . "Crystal Structure Of Human Presequence Protease In Complex With Amyloid-beta (1-40)" . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
53 no PDB 4ONG . "Fab Fragment Of 3d6 In Complex With Amyloid Beta 1-40" . . . . . 100.00 40 100.00 100.00 1.49e-18 . . . . 18129 1
54 no PDB 5AEF . "Electron Cryo-microscopy Of An Abeta(1-42)amyloid Fibril" . . . . . 65.00 28 100.00 100.00 3.73e-07 . . . . 18129 1
55 no DBJ BAA22264 . "amyloid precursor protein [Homo sapiens]" . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 18129 1
56 no DBJ BAA84580 . "amyloid precursor protein [Sus scrofa]" . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 18129 1
57 no DBJ BAB71958 . "amyloid precursor protein [Homo sapiens]" . . . . . 100.00 52 97.50 100.00 1.74e-18 . . . . 18129 1
58 no DBJ BAD51938 . "amyloid beta A4 precursor protein [Macaca fascicularis]" . . . . . 100.00 696 100.00 100.00 1.14e-18 . . . . 18129 1
59 no DBJ BAE01907 . "unnamed protein product [Macaca fascicularis]" . . . . . 100.00 751 100.00 100.00 1.43e-18 . . . . 18129 1
60 no EMBL CAA30050 . "amyloid A4 protein [Homo sapiens]" . . . . . 100.00 751 100.00 100.00 1.25e-18 . . . . 18129 1
61 no EMBL CAA31830 . "A4 amyloid protein precursor [Homo sapiens]" . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 18129 1
62 no EMBL CAA39589 . "amyloid precursor protein [Bos taurus]" . . . . . 100.00 59 100.00 100.00 3.56e-19 . . . . 18129 1
63 no EMBL CAA39590 . "amyloid precursor protein [Canis lupus familiaris]" . . . . . 100.00 58 100.00 100.00 3.68e-19 . . . . 18129 1
64 no EMBL CAA39591 . "amyloid precursor protein [Cavia sp.]" . . . . . 100.00 58 100.00 100.00 3.68e-19 . . . . 18129 1
65 no GB AAA35540 . "amyloid protein, partial [Homo sapiens]" . . . . . 95.00 97 100.00 100.00 2.36e-17 . . . . 18129 1
66 no GB AAA36829 . "amyloid b-protein precursor [Macaca fascicularis]" . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 18129 1
67 no GB AAA51564 . "amyloid beta protein, partial [Homo sapiens]" . . . . . 75.00 30 100.00 100.00 1.09e-11 . . . . 18129 1
68 no GB AAA51722 . "amyloid beta-protein precursor, partial [Homo sapiens]" . . . . . 100.00 412 100.00 100.00 9.13e-19 . . . . 18129 1
69 no GB AAA51726 . "beta-amyloid A4, partial [Homo sapiens]" . . . . . 100.00 264 100.00 100.00 1.74e-18 . . . . 18129 1
70 no PIR A60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - dog (fragment)" . . . . . 100.00 57 100.00 100.00 4.01e-19 . . . . 18129 1
71 no PIR D60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - bovine (fragment)" . . . . . 100.00 57 100.00 100.00 4.01e-19 . . . . 18129 1
72 no PIR E60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - sheep (fragment)" . . . . . 100.00 57 100.00 100.00 4.01e-19 . . . . 18129 1
73 no PIR G60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - guinea pig (fragment)" . . . . . 100.00 57 100.00 100.00 4.01e-19 . . . . 18129 1
74 no PIR PQ0438 . "Alzheimer's disease amyloid A4 protein precursor - rabbit (fragment)" . . . . . 100.00 82 100.00 100.00 4.05e-19 . . . . 18129 1
75 no PRF 1303338A . "amyloid A4 protein precursor" . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 18129 1
76 no PRF 1403400A . "amyloid protein A4" . . . . . 100.00 751 100.00 100.00 1.25e-18 . . . . 18129 1
77 no PRF 1405204A . "amyloid protein" . . . . . 100.00 42 100.00 100.00 1.28e-18 . . . . 18129 1
78 no PRF 1507304A . "beta amyloid peptide precursor" . . . . . 100.00 412 100.00 100.00 9.42e-19 . . . . 18129 1
79 no PRF 1507304B . "beta amyloid peptide precursor" . . . . . 100.00 574 100.00 100.00 4.07e-18 . . . . 18129 1
80 no REF NP_000475 . "amyloid beta A4 protein isoform a precursor [Homo sapiens]" . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 18129 1
81 no REF NP_001006601 . "amyloid beta A4 protein isoform APP-770 precursor [Canis lupus familiaris]" . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 18129 1
82 no REF NP_001013036 . "amyloid beta A4 protein precursor [Pan troglodytes]" . . . . . 100.00 770 100.00 100.00 1.28e-18 . . . . 18129 1
83 no REF NP_001070264 . "amyloid beta A4 protein precursor [Bos taurus]" . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 18129 1
84 no REF NP_001127014 . "amyloid beta A4 protein precursor [Pongo abelii]" . . . . . 100.00 695 100.00 100.00 1.65e-18 . . . . 18129 1
85 no 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 1.28e-18 . . . . 18129 1
86 no 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 1.28e-18 . . . . 18129 1
87 no 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 1.28e-18 . . . . 18129 1
88 no 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 5.51e-18 . . . . 18129 1
89 no 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 3.56e-19 . . . . 18129 1
90 no TPG DAA33655 . "TPA: amyloid beta A4 protein [Bos taurus]" . . . . . 100.00 695 100.00 100.00 1.30e-18 . . . . 18129 1
stop_
loop_
_Entity_comp_index.ID
_Entity_comp_index.Auth_seq_ID
_Entity_comp_index.Comp_ID
_Entity_comp_index.Comp_label
_Entity_comp_index.Entry_ID
_Entity_comp_index.Entity_ID
1 . ASP . 18129 1
2 . ALA . 18129 1
3 . GLU . 18129 1
4 . PHE . 18129 1
5 . ARG . 18129 1
6 . HIS . 18129 1
7 . ASP . 18129 1
8 . SER . 18129 1
9 . GLY . 18129 1
10 . TYR . 18129 1
11 . GLU . 18129 1
12 . VAL . 18129 1
13 . HIS . 18129 1
14 . HIS . 18129 1
15 . GLN . 18129 1
16 . LYS . 18129 1
17 . LEU . 18129 1
18 . VAL . 18129 1
19 . PHE . 18129 1
20 . PHE . 18129 1
21 . ALA . 18129 1
22 . GLU . 18129 1
23 . ASP . 18129 1
24 . VAL . 18129 1
25 . GLY . 18129 1
26 . SER . 18129 1
27 . ASN . 18129 1
28 . LYS . 18129 1
29 . GLY . 18129 1
30 . ALA . 18129 1
31 . ILE . 18129 1
32 . ILE . 18129 1
33 . GLY . 18129 1
34 . LEU . 18129 1
35 . MET . 18129 1
36 . VAL . 18129 1
37 . GLY . 18129 1
38 . GLY . 18129 1
39 . VAL . 18129 1
40 . VAL . 18129 1
stop_
loop_
_Entity_poly_seq.Hetero
_Entity_poly_seq.Mon_ID
_Entity_poly_seq.Num
_Entity_poly_seq.Comp_index_ID
_Entity_poly_seq.Entry_ID
_Entity_poly_seq.Entity_ID
. ASP 1 1 18129 1
. ALA 2 2 18129 1
. GLU 3 3 18129 1
. PHE 4 4 18129 1
. ARG 5 5 18129 1
. HIS 6 6 18129 1
. ASP 7 7 18129 1
. SER 8 8 18129 1
. GLY 9 9 18129 1
. TYR 10 10 18129 1
. GLU 11 11 18129 1
. VAL 12 12 18129 1
. HIS 13 13 18129 1
. HIS 14 14 18129 1
. GLN 15 15 18129 1
. LYS 16 16 18129 1
. LEU 17 17 18129 1
. VAL 18 18 18129 1
. PHE 19 19 18129 1
. PHE 20 20 18129 1
. ALA 21 21 18129 1
. GLU 22 22 18129 1
. ASP 23 23 18129 1
. VAL 24 24 18129 1
. GLY 25 25 18129 1
. SER 26 26 18129 1
. ASN 27 27 18129 1
. LYS 28 28 18129 1
. GLY 29 29 18129 1
. ALA 30 30 18129 1
. ILE 31 31 18129 1
. ILE 32 32 18129 1
. GLY 33 33 18129 1
. LEU 34 34 18129 1
. MET 35 35 18129 1
. VAL 36 36 18129 1
. GLY 37 37 18129 1
. GLY 38 38 18129 1
. VAL 39 39 18129 1
. VAL 40 40 18129 1
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Entity_natural_src_list.Sf_category natural_source
_Entity_natural_src_list.Sf_framecode natural_source
_Entity_natural_src_list.Entry_ID 18129
_Entity_natural_src_list.ID 1
loop_
_Entity_natural_src.ID
_Entity_natural_src.Entity_ID
_Entity_natural_src.Entity_label
_Entity_natural_src.Entity_chimera_segment_ID
_Entity_natural_src.NCBI_taxonomy_ID
_Entity_natural_src.Type
_Entity_natural_src.Common
_Entity_natural_src.Organism_name_scientific
_Entity_natural_src.Organism_name_common
_Entity_natural_src.Organism_acronym
_Entity_natural_src.ICTVdb_decimal_code
_Entity_natural_src.Superkingdom
_Entity_natural_src.Kingdom
_Entity_natural_src.Genus
_Entity_natural_src.Species
_Entity_natural_src.Strain
_Entity_natural_src.Variant
_Entity_natural_src.Subvariant
_Entity_natural_src.Organ
_Entity_natural_src.Tissue
_Entity_natural_src.Tissue_fraction
_Entity_natural_src.Cell_line
_Entity_natural_src.Cell_type
_Entity_natural_src.ATCC_number
_Entity_natural_src.Organelle
_Entity_natural_src.Cellular_location
_Entity_natural_src.Fragment
_Entity_natural_src.Fraction
_Entity_natural_src.Secretion
_Entity_natural_src.Plasmid
_Entity_natural_src.Plasmid_details
_Entity_natural_src.Gene_mnemonic
_Entity_natural_src.Dev_stage
_Entity_natural_src.Details
_Entity_natural_src.Citation_ID
_Entity_natural_src.Citation_label
_Entity_natural_src.Entry_ID
_Entity_natural_src.Entity_natural_src_list_ID
1 1 $beta-amyloid . 9606 organism . 'Homo sapiens' human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 18129 1
stop_
save_
#########################
# Experimental source #
#########################
save_experimental_source
_Entity_experimental_src_list.Sf_category experimental_source
_Entity_experimental_src_list.Sf_framecode experimental_source
_Entity_experimental_src_list.Entry_ID 18129
_Entity_experimental_src_list.ID 1
loop_
_Entity_experimental_src.ID
_Entity_experimental_src.Entity_ID
_Entity_experimental_src.Entity_label
_Entity_experimental_src.Entity_chimera_segment_ID
_Entity_experimental_src.Production_method
_Entity_experimental_src.Host_org_scientific_name
_Entity_experimental_src.Host_org_name_common
_Entity_experimental_src.Host_org_details
_Entity_experimental_src.Host_org_NCBI_taxonomy_ID
_Entity_experimental_src.Host_org_genus
_Entity_experimental_src.Host_org_species
_Entity_experimental_src.Host_org_strain
_Entity_experimental_src.Host_org_variant
_Entity_experimental_src.Host_org_subvariant
_Entity_experimental_src.Host_org_organ
_Entity_experimental_src.Host_org_tissue
_Entity_experimental_src.Host_org_tissue_fraction
_Entity_experimental_src.Host_org_cell_line
_Entity_experimental_src.Host_org_cell_type
_Entity_experimental_src.Host_org_cellular_location
_Entity_experimental_src.Host_org_organelle
_Entity_experimental_src.Host_org_gene
_Entity_experimental_src.Host_org_culture_collection
_Entity_experimental_src.Host_org_ATCC_number
_Entity_experimental_src.Vector_type
_Entity_experimental_src.PDBview_host_org_vector_name
_Entity_experimental_src.PDBview_plasmid_name
_Entity_experimental_src.Vector_name
_Entity_experimental_src.Vector_details
_Entity_experimental_src.Vendor_name
_Entity_experimental_src.Host_org_dev_stage
_Entity_experimental_src.Details
_Entity_experimental_src.Citation_ID
_Entity_experimental_src.Citation_label
_Entity_experimental_src.Entry_ID
_Entity_experimental_src.Entity_experimental_src_list_ID
1 1 $beta-amyloid . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 18129 1
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Sample.Sf_category sample
_Sample.Sf_framecode sample_1
_Sample.Entry_ID 18129
_Sample.ID 1
_Sample.Type 'amyloid fibril'
_Sample.Sub_type .
_Sample.Details 'Grown quiescently at room temperature, 1 mg/ml peptide, pH 7.4. Structurally purified by multiple rounds of seeded growth.'
_Sample.Aggregate_sample_number .
_Sample.Solvent_system '10 mM phosphate buffer'
_Sample.Preparation_date .
_Sample.Preparation_expiration_date .
_Sample.Polycrystallization_protocol .
_Sample.Single_crystal_protocol .
_Sample.Crystal_grow_apparatus .
_Sample.Crystal_grow_atmosphere .
_Sample.Crystal_grow_details .
_Sample.Crystal_grow_method .
_Sample.Crystal_grow_method_cit_ID .
_Sample.Crystal_grow_pH .
_Sample.Crystal_grow_pH_range .
_Sample.Crystal_grow_pressure .
_Sample.Crystal_grow_pressure_esd .
_Sample.Crystal_grow_seeding .
_Sample.Crystal_grow_seeding_cit_ID .
_Sample.Crystal_grow_temp .
_Sample.Crystal_grow_temp_details .
_Sample.Crystal_grow_temp_esd .
_Sample.Crystal_grow_time .
_Sample.Oriented_sample_prep_protocol .
_Sample.Lyophilization_cryo_protectant .
_Sample.Storage_protocol .
loop_
_Sample_component.ID
_Sample_component.Mol_common_name
_Sample_component.Isotopic_labeling
_Sample_component.Assembly_ID
_Sample_component.Assembly_label
_Sample_component.Entity_ID
_Sample_component.Entity_label
_Sample_component.Product_ID
_Sample_component.Type
_Sample_component.Concentration_val
_Sample_component.Concentration_val_min
_Sample_component.Concentration_val_max
_Sample_component.Concentration_val_units
_Sample_component.Concentration_val_err
_Sample_component.Vendor
_Sample_component.Vendor_product_name
_Sample_component.Vendor_product_code
_Sample_component.Entry_ID
_Sample_component.Sample_ID
1 beta-amyloid 'selective 13C and 15N' . . 1 $beta-amyloid . . 1 . . mg/mL . . . . 18129 1
2 'phosphate buffer' 'natural abundance' . . . . . . 10 . . mM . . . . 18129 1
stop_
save_
#######################
# Sample conditions #
#######################
save_sample_conditions_1
_Sample_condition_list.Sf_category sample_conditions
_Sample_condition_list.Sf_framecode sample_conditions_1
_Sample_condition_list.Entry_ID 18129
_Sample_condition_list.ID 1
_Sample_condition_list.Details .
loop_
_Sample_condition_variable.Type
_Sample_condition_variable.Val
_Sample_condition_variable.Val_err
_Sample_condition_variable.Val_units
_Sample_condition_variable.Entry_ID
_Sample_condition_variable.Sample_condition_list_ID
'ionic strength' 10 . mM 18129 1
pH 7.4 . pH 18129 1
pressure 1 . atm 18129 1
temperature 300 . K 18129 1
stop_
save_
############################
# Computer software used #
############################
save_X-PLOR_NIH
_Software.Sf_category software
_Software.Sf_framecode X-PLOR_NIH
_Software.Entry_ID 18129
_Software.ID 1
_Software.Name 'X-PLOR NIH'
_Software.Version .
_Software.Details .
loop_
_Vendor.Name
_Vendor.Address
_Vendor.Electronic_address
_Vendor.Entry_ID
_Vendor.Software_ID
'Schwieters, Kuszewski, Tjandra and Clore' . . 18129 1
stop_
loop_
_Task.Task
_Task.Entry_ID
_Task.Software_ID
'structure solution' 18129 1
stop_
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_1
_NMR_spectrometer.Sf_category NMR_spectrometer
_NMR_spectrometer.Sf_framecode spectrometer_1
_NMR_spectrometer.Entry_ID 18129
_NMR_spectrometer.ID 1
_NMR_spectrometer.Details .
_NMR_spectrometer.Manufacturer Varian
_NMR_spectrometer.Model Infinity
_NMR_spectrometer.Serial_number .
_NMR_spectrometer.Field_strength 400
save_
save_spectrometer_2
_NMR_spectrometer.Sf_category NMR_spectrometer
_NMR_spectrometer.Sf_framecode spectrometer_2
_NMR_spectrometer.Entry_ID 18129
_NMR_spectrometer.ID 2
_NMR_spectrometer.Details .
_NMR_spectrometer.Manufacturer Varian
_NMR_spectrometer.Model Infinity
_NMR_spectrometer.Serial_number .
_NMR_spectrometer.Field_strength 600
save_
save_NMR_spectrometer_list
_NMR_spectrometer_list.Sf_category NMR_spectrometer_list
_NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list
_NMR_spectrometer_list.Entry_ID 18129
_NMR_spectrometer_list.ID 1
loop_
_NMR_spectrometer_view.ID
_NMR_spectrometer_view.Name
_NMR_spectrometer_view.Manufacturer
_NMR_spectrometer_view.Model
_NMR_spectrometer_view.Serial_number
_NMR_spectrometer_view.Field_strength
_NMR_spectrometer_view.Details
_NMR_spectrometer_view.Citation_ID
_NMR_spectrometer_view.Citation_label
_NMR_spectrometer_view.Entry_ID
_NMR_spectrometer_view.NMR_spectrometer_list_ID
1 spectrometer_1 Varian Infinity . 400 . . . 18129 1
2 spectrometer_2 Varian Infinity . 600 . . . 18129 1
stop_
save_
#############################
# NMR applied experiments #
#############################
save_experiment_list
_Experiment_list.Sf_category experiment_list
_Experiment_list.Sf_framecode experiment_list
_Experiment_list.Entry_ID 18129
_Experiment_list.ID 1
_Experiment_list.Details .
loop_
_Experiment.ID
_Experiment.Name
_Experiment.Raw_data_flag
_Experiment.NMR_spec_expt_ID
_Experiment.NMR_spec_expt_label
_Experiment.MS_expt_ID
_Experiment.MS_expt_label
_Experiment.SAXS_expt_ID
_Experiment.SAXS_expt_label
_Experiment.FRET_expt_ID
_Experiment.FRET_expt_label
_Experiment.EMR_expt_ID
_Experiment.EMR_expt_label
_Experiment.Sample_ID
_Experiment.Sample_label
_Experiment.Sample_state
_Experiment.Sample_volume
_Experiment.Sample_volume_units
_Experiment.Sample_condition_list_ID
_Experiment.Sample_condition_list_label
_Experiment.Sample_spinning_rate
_Experiment.Sample_angle
_Experiment.NMR_tube_type
_Experiment.NMR_spectrometer_ID
_Experiment.NMR_spectrometer_label
_Experiment.NMR_spectrometer_probe_ID
_Experiment.NMR_spectrometer_probe_label
_Experiment.NMR_spectral_processing_ID
_Experiment.NMR_spectral_processing_label
_Experiment.Mass_spectrometer_ID
_Experiment.Mass_spectrometer_label
_Experiment.Xray_instrument_ID
_Experiment.Xray_instrument_label
_Experiment.Fluorescence_instrument_ID
_Experiment.Fluorescence_instrument_label
_Experiment.EMR_instrument_ID
_Experiment.EMR_instrument_label
_Experiment.Chromatographic_system_ID
_Experiment.Chromatographic_system_label
_Experiment.Chromatographic_column_ID
_Experiment.Chromatographic_column_label
_Experiment.Entry_ID
_Experiment.Experiment_list_ID
1 '2D fpRFDR' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18129 1
2 '2D RAD' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18129 1
3 '2D TEDOR' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18129 1
4 fsREDOR no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18129 1
5 15N-BARE no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18129 1
6 13C-BARE no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18129 1
7 PITHIRDS-CT no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18129 1
8 '2D NCACX' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 18129 1
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference_1
_Chem_shift_reference.Sf_category chem_shift_reference
_Chem_shift_reference.Sf_framecode chemical_shift_reference_1
_Chem_shift_reference.Entry_ID 18129
_Chem_shift_reference.ID 1
_Chem_shift_reference.Details 'DSS reference for 13C shifts.'
loop_
_Chem_shift_ref.Atom_type
_Chem_shift_ref.Atom_isotope_number
_Chem_shift_ref.Mol_common_name
_Chem_shift_ref.Atom_group
_Chem_shift_ref.Concentration_val
_Chem_shift_ref.Concentration_units
_Chem_shift_ref.Solvent
_Chem_shift_ref.Rank
_Chem_shift_ref.Chem_shift_units
_Chem_shift_ref.Chem_shift_val
_Chem_shift_ref.Ref_method
_Chem_shift_ref.Ref_type
_Chem_shift_ref.Indirect_shift_ratio
_Chem_shift_ref.External_ref_loc
_Chem_shift_ref.External_ref_sample_geometry
_Chem_shift_ref.External_ref_axis
_Chem_shift_ref.Indirect_shift_ratio_cit_ID
_Chem_shift_ref.Indirect_shift_ratio_cit_label
_Chem_shift_ref.Ref_correction_type
_Chem_shift_ref.Correction_val
_Chem_shift_ref.Correction_val_cit_ID
_Chem_shift_ref.Correction_val_cit_label
_Chem_shift_ref.Entry_ID
_Chem_shift_ref.Chem_shift_reference_ID
C 13 DSS 'methyl carbons' . . . . ppm 0 external direct 1.0 . . . . . . . . . 18129 1
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
_Assigned_chem_shift_list.Sf_category assigned_chemical_shifts
_Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1
_Assigned_chem_shift_list.Entry_ID 18129
_Assigned_chem_shift_list.ID 1
_Assigned_chem_shift_list.Sample_condition_list_ID 1
_Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1
_Assigned_chem_shift_list.Chem_shift_reference_ID 1
_Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1
_Assigned_chem_shift_list.Chem_shift_1H_err .
_Assigned_chem_shift_list.Chem_shift_13C_err .
_Assigned_chem_shift_list.Chem_shift_15N_err .
_Assigned_chem_shift_list.Chem_shift_31P_err .
_Assigned_chem_shift_list.Chem_shift_2H_err .
_Assigned_chem_shift_list.Chem_shift_19F_err .
_Assigned_chem_shift_list.Error_derivation_method .
_Assigned_chem_shift_list.Details .
_Assigned_chem_shift_list.Text_data_format .
_Assigned_chem_shift_list.Text_data .
loop_
_Chem_shift_experiment.Experiment_ID
_Chem_shift_experiment.Experiment_name
_Chem_shift_experiment.Sample_ID
_Chem_shift_experiment.Sample_label
_Chem_shift_experiment.Sample_state
_Chem_shift_experiment.Entry_ID
_Chem_shift_experiment.Assigned_chem_shift_list_ID
1 '2D fpRFDR' . . . 18129 1
stop_
loop_
_Atom_chem_shift.ID
_Atom_chem_shift.Assembly_atom_ID
_Atom_chem_shift.Entity_assembly_ID
_Atom_chem_shift.Entity_ID
_Atom_chem_shift.Comp_index_ID
_Atom_chem_shift.Seq_ID
_Atom_chem_shift.Comp_ID
_Atom_chem_shift.Atom_ID
_Atom_chem_shift.Atom_type
_Atom_chem_shift.Atom_isotope_number
_Atom_chem_shift.Val
_Atom_chem_shift.Val_err
_Atom_chem_shift.Assign_fig_of_merit
_Atom_chem_shift.Ambiguity_code
_Atom_chem_shift.Occupancy
_Atom_chem_shift.Resonance_ID
_Atom_chem_shift.Auth_entity_assembly_ID
_Atom_chem_shift.Auth_asym_ID
_Atom_chem_shift.Auth_seq_ID
_Atom_chem_shift.Auth_comp_ID
_Atom_chem_shift.Auth_atom_ID
_Atom_chem_shift.Details
_Atom_chem_shift.Entry_ID
_Atom_chem_shift.Assigned_chem_shift_list_ID
1 . 1 1 9 9 GLY C C 13 172.2 0.3 . 1 . . . A 9 GLY C . 18129 1
2 . 1 1 9 9 GLY CA C 13 46.2 0.3 . 1 . . . A 9 GLY CA . 18129 1
3 . 1 1 10 10 TYR C C 13 173.7 0.3 . 1 . . . A 10 TYR C . 18129 1
4 . 1 1 10 10 TYR CA C 13 54.2 0.3 . 1 . . . A 10 TYR CA . 18129 1
5 . 1 1 10 10 TYR CB C 13 37.7 0.3 . 1 . . . A 10 TYR CB . 18129 1
6 . 1 1 11 11 GLU C C 13 173.2 0.3 . 1 . . . A 11 GLU C . 18129 1
7 . 1 1 11 11 GLU CA C 13 54.5 0.3 . 1 . . . A 11 GLU CA . 18129 1
8 . 1 1 11 11 GLU CB C 13 31.4 0.3 . 1 . . . A 11 GLU CB . 18129 1
9 . 1 1 12 12 VAL C C 13 174.1 0.3 . 1 . . . A 12 VAL C . 18129 1
10 . 1 1 12 12 VAL CA C 13 61 0.3 . 1 . . . A 12 VAL CA . 18129 1
11 . 1 1 12 12 VAL CB C 13 35.4 0.3 . 1 . . . A 12 VAL CB . 18129 1
12 . 1 1 13 13 HIS C C 13 172.9 0.3 . 1 . . . A 13 HIS C . 18129 1
13 . 1 1 13 13 HIS CA C 13 54.2 0.3 . 1 . . . A 13 HIS CA . 18129 1
14 . 1 1 13 13 HIS CB C 13 31.2 0.3 . 1 . . . A 13 HIS CB . 18129 1
15 . 1 1 14 14 HIS C C 13 171.9 0.3 . 1 . . . A 14 HIS C . 18129 1
16 . 1 1 14 14 HIS CA C 13 53.7 0.3 . 1 . . . A 14 HIS CA . 18129 1
17 . 1 1 14 14 HIS CB C 13 35.4 0.3 . 1 . . . A 14 HIS CB . 18129 1
18 . 1 1 15 15 GLN C C 13 173.4 0.3 . 1 . . . A 15 GLN C . 18129 1
19 . 1 1 15 15 GLN CA C 13 54.6 0.3 . 1 . . . A 15 GLN CA . 18129 1
20 . 1 1 15 15 GLN CB C 13 33.7 0.3 . 1 . . . A 15 GLN CB . 18129 1
21 . 1 1 16 16 LYS C C 13 173.5 0.3 . 1 . . . A 16 LYS C . 18129 1
22 . 1 1 16 16 LYS CA C 13 54.3 0.3 . 1 . . . A 16 LYS CA . 18129 1
23 . 1 1 16 16 LYS CB C 13 36.2 0.3 . 1 . . . A 16 LYS CB . 18129 1
24 . 1 1 17 17 LEU C C 13 174.7 0.3 . 1 . . . A 17 LEU C . 18129 1
25 . 1 1 17 17 LEU CA C 13 53.9 0.3 . 1 . . . A 17 LEU CA . 18129 1
26 . 1 1 17 17 LEU CB C 13 44.9 0.3 . 1 . . . A 17 LEU CB . 18129 1
27 . 1 1 18 18 VAL C C 13 174.1 0.3 . 1 . . . A 18 VAL C . 18129 1
28 . 1 1 18 18 VAL CA C 13 60.6 0.3 . 1 . . . A 18 VAL CA . 18129 1
29 . 1 1 18 18 VAL CB C 13 35.3 0.3 . 1 . . . A 18 VAL CB . 18129 1
30 . 1 1 19 19 PHE C C 13 172.7 0.3 . 1 . . . A 19 PHE C . 18129 1
31 . 1 1 19 19 PHE CA C 13 56.1 0.3 . 1 . . . A 19 PHE CA . 18129 1
32 . 1 1 19 19 PHE CB C 13 42.2 0.3 . 1 . . . A 19 PHE CB . 18129 1
33 . 1 1 20 20 PHE C C 13 172.3 0.3 . 1 . . . A 20 PHE C . 18129 1
34 . 1 1 20 20 PHE CA C 13 56.0 0.3 . 1 . . . A 20 PHE CA . 18129 1
35 . 1 1 20 20 PHE CB C 13 42.9 0.3 . 1 . . . A 20 PHE CB . 18129 1
36 . 1 1 21 21 ALA C C 13 175.1 0.3 . 1 . . . A 21 ALA C . 18129 1
37 . 1 1 21 21 ALA CA C 13 49.7 0.3 . 1 . . . A 21 ALA CA . 18129 1
38 . 1 1 21 21 ALA CB C 13 22.1 0.3 . 1 . . . A 21 ALA CB . 18129 1
39 . 1 1 22 22 GLU C C 13 176 0.3 . 1 . . . A 22 GLU C . 18129 1
40 . 1 1 22 22 GLU CA C 13 54.4 0.3 . 1 . . . A 22 GLU CA . 18129 1
41 . 1 1 22 22 GLU CB C 13 33.9 0.3 . 1 . . . A 22 GLU CB . 18129 1
42 . 1 1 23 23 ASP C C 13 174.4 0.3 . 1 . . . A 23 ASP C . 18129 1
43 . 1 1 23 23 ASP CA C 13 56.5 0.3 . 1 . . . A 23 ASP CA . 18129 1
44 . 1 1 23 23 ASP CB C 13 39.1 0.3 . 1 . . . A 23 ASP CB . 18129 1
45 . 1 1 24 24 VAL C C 13 176.8 0.3 . 1 . . . A 24 VAL C . 18129 1
46 . 1 1 24 24 VAL CA C 13 60.1 0.3 . 1 . . . A 24 VAL CA . 18129 1
47 . 1 1 24 24 VAL CB C 13 32.7 0.3 . 1 . . . A 24 VAL CB . 18129 1
48 . 1 1 25 25 GLY C C 13 171.5 0.3 . 1 . . . A 25 GLY C . 18129 1
49 . 1 1 25 25 GLY CA C 13 46.5 0.3 . 1 . . . A 25 GLY CA . 18129 1
50 . 1 1 26 26 SER C C 13 173.8 0.3 . 1 . . . A 26 SER C . 18129 1
51 . 1 1 26 26 SER CA C 13 55.7 0.3 . 1 . . . A 26 SER CA . 18129 1
52 . 1 1 26 26 SER CB C 13 65.3 0.3 . 1 . . . A 26 SER CB . 18129 1
53 . 1 1 27 27 ASN C C 13 174.3 0.3 . 1 . . . A 27 ASN C . 18129 1
54 . 1 1 27 27 ASN CA C 13 53.1 0.3 . 1 . . . A 27 ASN CA . 18129 1
55 . 1 1 27 27 ASN CB C 13 40.8 0.3 . 1 . . . A 27 ASN CB . 18129 1
56 . 1 1 28 28 LYS C C 13 175.3 0.3 . 1 . . . A 28 LYS C . 18129 1
57 . 1 1 28 28 LYS CA C 13 55.5 0.3 . 1 . . . A 28 LYS CA . 18129 1
58 . 1 1 28 28 LYS CB C 13 35.5 0.3 . 1 . . . A 28 LYS CB . 18129 1
59 . 1 1 29 29 GLY C C 13 171.7 0.3 . 1 . . . A 29 GLY C . 18129 1
60 . 1 1 29 29 GLY CA C 13 43.5 0.3 . 1 . . . A 29 GLY CA . 18129 1
61 . 1 1 30 30 ALA C C 13 175.2 0.3 . 1 . . . A 30 ALA C . 18129 1
62 . 1 1 30 30 ALA CA C 13 49.8 0.3 . 1 . . . A 30 ALA CA . 18129 1
63 . 1 1 30 30 ALA CB C 13 21.3 0.3 . 1 . . . A 30 ALA CB . 18129 1
64 . 1 1 31 31 ILE C C 13 173.6 0.3 . 1 . . . A 31 ILE C . 18129 1
65 . 1 1 31 31 ILE CA C 13 60.8 0.3 . 1 . . . A 31 ILE CA . 18129 1
66 . 1 1 31 31 ILE CB C 13 39.9 0.3 . 1 . . . A 31 ILE CB . 18129 1
67 . 1 1 32 32 ILE C C 13 175.7 0.3 . 1 . . . A 32 ILE C . 18129 1
68 . 1 1 32 32 ILE CA C 13 57.2 0.3 . 1 . . . A 32 ILE CA . 18129 1
69 . 1 1 32 32 ILE CB C 13 42.2 0.3 . 1 . . . A 32 ILE CB . 18129 1
70 . 1 1 33 33 GLY C C 13 171.7 0.3 . 1 . . . A 33 GLY C . 18129 1
71 . 1 1 33 33 GLY CA C 13 48.1 0.3 . 1 . . . A 33 GLY CA . 18129 1
72 . 1 1 34 34 LEU C C 13 173.2 0.3 . 1 . . . A 34 LEU C . 18129 1
73 . 1 1 34 34 LEU CA C 13 54.2 0.3 . 1 . . . A 34 LEU CA . 18129 1
74 . 1 1 34 34 LEU CB C 13 45.8 0.3 . 1 . . . A 34 LEU CB . 18129 1
75 . 1 1 35 35 MET C C 13 172.9 0.3 . 1 . . . A 35 MET C . 18129 1
76 . 1 1 35 35 MET CA C 13 54.1 0.3 . 1 . . . A 35 MET CA . 18129 1
77 . 1 1 35 35 MET CB C 13 36.4 0.3 . 1 . . . A 35 MET CB . 18129 1
78 . 1 1 36 36 VAL C C 13 175.4 0.3 . 1 . . . A 36 VAL C . 18129 1
79 . 1 1 36 36 VAL CA C 13 58.9 0.3 . 1 . . . A 36 VAL CA . 18129 1
80 . 1 1 36 36 VAL CB C 13 35.1 0.3 . 1 . . . A 36 VAL CB . 18129 1
81 . 1 1 37 37 GLY C C 13 172.3 0.3 . 1 . . . A 37 GLY C . 18129 1
82 . 1 1 37 37 GLY CA C 13 48.3 0.3 . 1 . . . A 37 GLY CA . 18129 1
83 . 1 1 38 38 GLY C C 13 171.3 0.3 . 1 . . . A 38 GLY C . 18129 1
84 . 1 1 38 38 GLY CA C 13 44.1 0.3 . 1 . . . A 38 GLY CA . 18129 1
85 . 1 1 39 39 VAL C C 13 173.5 0.3 . 1 . . . A 39 VAL C . 18129 1
86 . 1 1 39 39 VAL CA C 13 60.6 0.3 . 1 . . . A 39 VAL CA . 18129 1
87 . 1 1 39 39 VAL CB C 13 34.1 0.3 . 1 . . . A 39 VAL CB . 18129 1
88 . 1 1 40 40 VAL C C 13 179.6 0.3 . 1 . . . A 40 VAL C . 18129 1
89 . 1 1 40 40 VAL CA C 13 60.7 0.3 . 1 . . . A 40 VAL CA . 18129 1
90 . 1 1 40 40 VAL CB C 13 34.9 0.3 . 1 . . . A 40 VAL CB . 18129 1
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