data_25429
#######################
# Entry information #
#######################
save_entry_information
_Entry.Sf_category entry_information
_Entry.Sf_framecode entry_information
_Entry.ID 25429
_Entry.Title
;
42-Residue Beta Amyloid Fibril
;
_Entry.Type macromolecule
_Entry.Version_type original
_Entry.Submission_date 2015-01-14
_Entry.Accession_date 2015-01-14
_Entry.Last_release_date 2015-05-04
_Entry.Original_release_date 2015-05-04
_Entry.Origination author
_Entry.NMR_STAR_version 3.1.1.77
_Entry.Original_NMR_STAR_version 3.1
_Entry.Experimental_method NMR
_Entry.Experimental_method_subtype SOLID-STATE
_Entry.Details 'Amyloid Beta 42 Structural Model'
_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 Yiling Xiao . . . 25429
2 Buyong Ma . . . 25429
3 Dan McElheny . . . 25429
4 Sudhakar Parthasarathy . . . 25429
5 Fei Long . . . 25429
6 Minako Hoshi . . . 25429
7 Ruth Nussinov . . . 25429
8 Yoshitaka Ishii . . . 25429
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' . 25429
stop_
loop_
_Struct_keywords.Keywords
_Struct_keywords.Text
_Struct_keywords.Entry_ID
'Amyloid Fibril' . 25429
'Protein Fibril' . 25429
stop_
loop_
_Data_set.Type
_Data_set.Count
_Data_set.Entry_ID
assigned_chemical_shifts 1 25429
stop_
loop_
_Datum.Type
_Datum.Count
_Datum.Entry_ID
'13C chemical shifts' 78 25429
'15N chemical shifts' 25 25429
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
1 . . 2015-05-04 . original BMRB . 25429
stop_
loop_
_Related_entries.Database_name
_Related_entries.Database_accession_code
_Related_entries.Relationship
_Related_entries.Entry_ID
PDB 2MXU 'BMRB Entry Tracking System' 25429
stop_
save_
###############
# Citations #
###############
save_entry_citation
_Citation.Sf_category citations
_Citation.Sf_framecode entry_citation
_Citation.Entry_ID 25429
_Citation.ID 1
_Citation.Class 'entry citation'
_Citation.CAS_abstract_code .
_Citation.MEDLINE_UI_code .
_Citation.DOI .
_Citation.PubMed_ID .
_Citation.Full_citation .
_Citation.Title
;
A (1-42) Fibril Structure Illuminates Self-recognition and Replication Machinery of Amyloid in Alzheimer's
;
_Citation.Status 'in preparation'
_Citation.Type journal
_Citation.Journal_abbrev 'Nat. Struct. Biol.'
_Citation.Journal_name_full .
_Citation.Journal_volume .
_Citation.Journal_issue .
_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 .
_Citation.Page_last .
_Citation.Year .
_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 Yiling Xiao . . . 25429 1
2 Buyong Ma . . . 25429 1
3 Dan McElheny . . . 25429 1
4 Sudhakar Parthasarathy . . . 25429 1
5 Fei Long . . . 25429 1
6 Minako Hoshi . . . 25429 1
7 Ruth Nussinov . . . 25429 1
8 Yoshitaka Ishii . . . 25429 1
stop_
save_
#############################################
# Molecular system (assembly) description #
#############################################
save_assembly
_Assembly.Sf_category assembly
_Assembly.Sf_framecode assembly
_Assembly.Entry_ID 25429
_Assembly.ID 1
_Assembly.Name '42-Residue Beta Amyloid Fibril'
_Assembly.BMRB_code .
_Assembly.Number_of_components 12
_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 $entity A . yes native no no . . . 25429 1
2 entity_2 1 $entity B . yes native no no . . . 25429 1
3 entity_3 1 $entity C . yes native no no . . . 25429 1
4 entity_4 1 $entity D . yes native no no . . . 25429 1
5 entity_5 1 $entity E . yes native no no . . . 25429 1
6 entity_6 1 $entity F . yes native no no . . . 25429 1
7 entity_7 1 $entity G . yes native no no . . . 25429 1
8 entity_8 1 $entity H . yes native no no . . . 25429 1
9 entity_9 1 $entity I . yes native no no . . . 25429 1
10 entity_10 1 $entity J . yes native no no . . . 25429 1
11 entity_11 1 $entity K . yes native no no . . . 25429 1
12 entity_12 1 $entity L . yes native no no . . . 25429 1
stop_
save_
####################################
# Biological polymers and ligands #
####################################
save_entity
_Entity.Sf_category entity
_Entity.Sf_framecode entity
_Entity.Entry_ID 25429
_Entity.ID 1
_Entity.BMRB_code .
_Entity.Name entity
_Entity.Type polymer
_Entity.Polymer_common_type .
_Entity.Polymer_type polypeptide(L)
_Entity.Polymer_type_details .
_Entity.Polymer_strand_ID ABCDEFGHIJKL
_Entity.Polymer_seq_one_letter_code_can .
_Entity.Polymer_seq_one_letter_code
;
DAEFRHDSGYEVHHQKLVFF
AEDVGSNKGAIIGLMVGGVV
IA
;
_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 42
_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 3339.934
_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) . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
2 no BMRB 15775 . APP_C99 . . . . . 100.00 122 100.00 100.00 6.42e-20 . . . . 25429 1
3 no BMRB 17159 . Amyloid_beta-Peptide . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
4 no BMRB 17186 . Abeta . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
5 no BMRB 17764 . Abeta . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
6 no BMRB 17793 . Abeta(1-42) . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25429 1
7 no BMRB 17794 . Abeta(1-42) . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25429 1
8 no BMRB 17795 . Abeta(1-40) . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
9 no BMRB 17796 . Abeta40 . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
10 no BMRB 18052 . Pyroglutamate_Abeta . . . . . 88.10 38 100.00 100.00 2.61e-16 . . . . 25429 1
11 no BMRB 18127 . beta-amyloid . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
12 no BMRB 18128 . beta-amyloid . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
13 no BMRB 18129 . beta-amyloid . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
14 no BMRB 18131 . beta-amyloid . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
15 no BMRB 19009 . beta-amyloid_peptide . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
16 no BMRB 19309 . amyloid_peptide . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
17 no BMRB 19393 . Abeta . . . . . 95.24 39 97.50 97.50 4.95e-16 . . . . 25429 1
18 no BMRB 25218 . amyloid_peptide . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25429 1
19 no BMRB 25289 . amyloid_beta . . . . . 95.24 39 97.50 97.50 4.95e-16 . . . . 25429 1
20 no BMRB 26508 . amyloid_B . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
21 no BMRB 26516 . amyloid_B . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
22 no PDB 1AMB . "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" . . . . . 66.67 28 100.00 100.00 1.81e-10 . . . . 25429 1
23 no PDB 1AMC . "Solution Structure Of Residues 1-28 Of The Amyloid Beta- Peptide" . . . . . 66.67 28 100.00 100.00 1.81e-10 . . . . 25429 1
24 no PDB 1AML . "The Alzheimer`s Disease Amyloid A4 Peptide (Residues 1-40)" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 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 " . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
26 no PDB 1BA6 . "Solution Structure Of The Methionine-Oxidized Amyloid Beta- Peptide (1-40). Does Oxidation Affect Conformational Switching? Nmr" . . . . . 95.24 40 97.50 97.50 1.43e-17 . . . . 25429 1
27 no PDB 1HZ3 . "Alzheimer's Disease Amyloid-Beta Peptide (Residues 10-35)" . . . . . 61.90 26 100.00 100.00 2.00e-08 . . . . 25429 1
28 no PDB 1IYT . "Solution Structure Of The Alzheimer's Disease Amyloid Beta- Peptide (1-42)" . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25429 1
29 no PDB 1Z0Q . "Aqueous Solution Structure Of The Alzheimer's Disease Abeta Peptide (1-42)" . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25429 1
30 no PDB 2BEG . "3d Structure Of Alzheimer's Abeta(1-42) Fibrils" . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25429 1
31 no PDB 2G47 . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-40)" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
32 no PDB 2LFM . "A Partially Folded Structure Of Amyloid-Beta(1 40) In An Aqueous Environment" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
33 no PDB 2LMN . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Positive Stagger" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
34 no PDB 2LMO . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Negative Stagger" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
35 no PDB 2LMP . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Positive Stagger" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
36 no PDB 2LMQ . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Negative Stagger" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
37 no PDB 2LNQ . "40-residue D23n Beta Amyloid Fibril" . . . . . 95.24 40 97.50 100.00 4.61e-18 . . . . 25429 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 6.42e-20 . . . . 25429 1
39 no PDB 2M4J . "40-residue Beta-amyloid Fibril Derived From Alzheimer's Disease Brain" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
40 no PDB 2M9R . "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
41 no PDB 2M9S . "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
42 no PDB 2MVX . "Atomic-resolution 3d Structure Of Amyloid-beta Fibrils: The Osaka Mutation" . . . . . 95.24 39 97.50 97.50 4.95e-16 . . . . 25429 1
43 no PDB 2MXU . "42-residue Beta Amyloid Fibril" . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25429 1
44 no PDB 2OTK . "Structure Of Alzheimer Ab Peptide In Complex With An Engineered Binding Protein" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 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 7.22e-20 . . . . 25429 1
46 no PDB 3BAE . "Crystal Structure Of Fab Wo2 Bound To The N Terminal Domain Of Amyloid Beta Peptide (1-28)" . . . . . 66.67 28 100.00 100.00 1.81e-10 . . . . 25429 1
47 no PDB 3IFN . "X-ray Structure Of Amyloid Beta Peptide:antibody (abeta1-40:12a11) Complex" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
48 no PDB 4HIX . "Crystal Structure Of A Humanised 3d6 Fab Bound To Amyloid Beta Peptide" . . . . . 66.67 28 100.00 100.00 1.81e-10 . . . . 25429 1
49 no PDB 4M1C . "Crystal Structure Analysis Of Fab-bound Human Insulin Degrading Enzyme (ide) In Complex With Amyloid-beta (1-40)" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
50 no PDB 4MVI . "Crystal Structure Of An Engineered Lipocalin (anticalin Us7) In Complex With The Alzheimer Amyloid Peptide Abeta(1-40)" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
51 no PDB 4MVL . "Crystal Structure Of An Engineered Lipocalin (anticalin H1ga) In Complex With The Alzheimer Amyloid Peptide Abeta1-40" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
52 no PDB 4NGE . "Crystal Structure Of Human Presequence Protease In Complex With Amyloid-beta (1-40)" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
53 no PDB 4ONG . "Fab Fragment Of 3d6 In Complex With Amyloid Beta 1-40" . . . . . 95.24 40 100.00 100.00 1.35e-18 . . . . 25429 1
54 no PDB 5AEF . "Electron Cryo-microscopy Of An Abeta(1-42)amyloid Fibril" . . . . . 66.67 28 100.00 100.00 2.69e-08 . . . . 25429 1
55 no DBJ BAA22264 . "amyloid precursor protein [Homo sapiens]" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25429 1
56 no DBJ BAA84580 . "amyloid precursor protein [Sus scrofa]" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25429 1
57 no DBJ BAB71958 . "amyloid precursor protein [Homo sapiens]" . . . . . 100.00 52 97.62 100.00 9.73e-20 . . . . 25429 1
58 no DBJ BAD51938 . "amyloid beta A4 precursor protein [Macaca fascicularis]" . . . . . 100.00 696 100.00 100.00 8.24e-20 . . . . 25429 1
59 no DBJ BAE01907 . "unnamed protein product [Macaca fascicularis]" . . . . . 100.00 751 100.00 100.00 9.08e-20 . . . . 25429 1
60 no EMBL CAA30050 . "amyloid A4 protein [Homo sapiens]" . . . . . 100.00 751 100.00 100.00 9.08e-20 . . . . 25429 1
61 no EMBL CAA31830 . "A4 amyloid protein precursor [Homo sapiens]" . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25429 1
62 no EMBL CAA39589 . "amyloid precursor protein [Bos taurus]" . . . . . 100.00 59 100.00 100.00 1.94e-20 . . . . 25429 1
63 no EMBL CAA39590 . "amyloid precursor protein [Canis lupus familiaris]" . . . . . 100.00 58 100.00 100.00 2.01e-20 . . . . 25429 1
64 no EMBL CAA39591 . "amyloid precursor protein [Cavia sp.]" . . . . . 100.00 58 100.00 100.00 2.01e-20 . . . . 25429 1
65 no GB AAA35540 . "amyloid protein, partial [Homo sapiens]" . . . . . 95.24 97 100.00 100.00 1.03e-18 . . . . 25429 1
66 no GB AAA36829 . "amyloid b-protein precursor [Macaca fascicularis]" . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25429 1
67 no GB AAA51564 . "amyloid beta protein, partial [Homo sapiens]" . . . . . 71.43 30 100.00 100.00 9.95e-12 . . . . 25429 1
68 no GB AAA51722 . "amyloid beta-protein precursor, partial [Homo sapiens]" . . . . . 100.00 412 100.00 100.00 4.48e-20 . . . . 25429 1
69 no GB AAA51726 . "beta-amyloid A4, partial [Homo sapiens]" . . . . . 100.00 264 100.00 100.00 9.55e-20 . . . . 25429 1
70 no PIR A60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - dog (fragment)" . . . . . 100.00 57 100.00 100.00 2.12e-20 . . . . 25429 1
71 no PIR D60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - bovine (fragment)" . . . . . 100.00 57 100.00 100.00 2.12e-20 . . . . 25429 1
72 no PIR E60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - sheep (fragment)" . . . . . 100.00 57 100.00 100.00 2.12e-20 . . . . 25429 1
73 no PIR G60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - guinea pig (fragment)" . . . . . 100.00 57 100.00 100.00 2.12e-20 . . . . 25429 1
74 no PIR PQ0438 . "Alzheimer's disease amyloid A4 protein precursor - rabbit (fragment)" . . . . . 100.00 82 100.00 100.00 2.05e-20 . . . . 25429 1
75 no PRF 1303338A . "amyloid A4 protein precursor" . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25429 1
76 no PRF 1403400A . "amyloid protein A4" . . . . . 100.00 751 100.00 100.00 9.08e-20 . . . . 25429 1
77 no PRF 1405204A . "amyloid protein" . . . . . 100.00 42 100.00 100.00 7.22e-20 . . . . 25429 1
78 no PRF 1507304A . "beta amyloid peptide precursor" . . . . . 100.00 412 100.00 100.00 4.48e-20 . . . . 25429 1
79 no PRF 1507304B . "beta amyloid peptide precursor" . . . . . 100.00 574 100.00 100.00 2.04e-19 . . . . 25429 1
80 no REF NP_000475 . "amyloid beta A4 protein isoform a precursor [Homo sapiens]" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25429 1
81 no REF NP_001006601 . "amyloid beta A4 protein isoform APP-770 precursor [Canis lupus familiaris]" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25429 1
82 no REF NP_001013036 . "amyloid beta A4 protein precursor [Pan troglodytes]" . . . . . 100.00 770 100.00 100.00 9.34e-20 . . . . 25429 1
83 no REF NP_001070264 . "amyloid beta A4 protein precursor [Bos taurus]" . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25429 1
84 no REF NP_001127014 . "amyloid beta A4 protein precursor [Pongo abelii]" . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25429 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 9.34e-20 . . . . 25429 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 9.34e-20 . . . . 25429 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 9.34e-20 . . . . 25429 1
88 no SP P86906 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 95.24 40 97.50 100.00 5.31e-18 . . . . 25429 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 1.94e-20 . . . . 25429 1
90 no TPG DAA33655 . "TPA: amyloid beta A4 protein [Bos taurus]" . . . . . 100.00 695 100.00 100.00 8.22e-20 . . . . 25429 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 . 25429 1
2 . ALA . 25429 1
3 . GLU . 25429 1
4 . PHE . 25429 1
5 . ARG . 25429 1
6 . HIS . 25429 1
7 . ASP . 25429 1
8 . SER . 25429 1
9 . GLY . 25429 1
10 . TYR . 25429 1
11 . GLU . 25429 1
12 . VAL . 25429 1
13 . HIS . 25429 1
14 . HIS . 25429 1
15 . GLN . 25429 1
16 . LYS . 25429 1
17 . LEU . 25429 1
18 . VAL . 25429 1
19 . PHE . 25429 1
20 . PHE . 25429 1
21 . ALA . 25429 1
22 . GLU . 25429 1
23 . ASP . 25429 1
24 . VAL . 25429 1
25 . GLY . 25429 1
26 . SER . 25429 1
27 . ASN . 25429 1
28 . LYS . 25429 1
29 . GLY . 25429 1
30 . ALA . 25429 1
31 . ILE . 25429 1
32 . ILE . 25429 1
33 . GLY . 25429 1
34 . LEU . 25429 1
35 . MET . 25429 1
36 . VAL . 25429 1
37 . GLY . 25429 1
38 . GLY . 25429 1
39 . VAL . 25429 1
40 . VAL . 25429 1
41 . ILE . 25429 1
42 . ALA . 25429 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 25429 1
. ALA 2 2 25429 1
. GLU 3 3 25429 1
. PHE 4 4 25429 1
. ARG 5 5 25429 1
. HIS 6 6 25429 1
. ASP 7 7 25429 1
. SER 8 8 25429 1
. GLY 9 9 25429 1
. TYR 10 10 25429 1
. GLU 11 11 25429 1
. VAL 12 12 25429 1
. HIS 13 13 25429 1
. HIS 14 14 25429 1
. GLN 15 15 25429 1
. LYS 16 16 25429 1
. LEU 17 17 25429 1
. VAL 18 18 25429 1
. PHE 19 19 25429 1
. PHE 20 20 25429 1
. ALA 21 21 25429 1
. GLU 22 22 25429 1
. ASP 23 23 25429 1
. VAL 24 24 25429 1
. GLY 25 25 25429 1
. SER 26 26 25429 1
. ASN 27 27 25429 1
. LYS 28 28 25429 1
. GLY 29 29 25429 1
. ALA 30 30 25429 1
. ILE 31 31 25429 1
. ILE 32 32 25429 1
. GLY 33 33 25429 1
. LEU 34 34 25429 1
. MET 35 35 25429 1
. VAL 36 36 25429 1
. GLY 37 37 25429 1
. GLY 38 38 25429 1
. VAL 39 39 25429 1
. VAL 40 40 25429 1
. ILE 41 41 25429 1
. ALA 42 42 25429 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 25429
_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.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.Secretion
_Entity_natural_src.Plasmid
_Entity_natural_src.Gene_mnemonic
_Entity_natural_src.Details
_Entity_natural_src.Entry_ID
_Entity_natural_src.Entity_natural_src_list_ID
1 1 $entity . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . 25429 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 25429
_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_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.Details
_Entity_experimental_src.Entry_ID
_Entity_experimental_src.Entity_experimental_src_list_ID
1 1 $entity . 'chemical synthesis' . . . . . . . . . . . . . . .
;
hemically synthesized by an Applied Biosystems model 433A automated peptide synthesizer with Fmoc protected 13C- and 15N-labeled amino acids at selected sites
; 25429 1
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Sample.Sf_category sample
_Sample.Sf_framecode sample_1
_Sample.Entry_ID 25429
_Sample.ID 1
_Sample.Type solid
_Sample.Sub_type .
_Sample.Details .
_Sample.Aggregate_sample_number .
_Sample.Solvent_system '90% H2O/10% D2O'
_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 AB42 '[U-100% 13C; U-100% 15N]' . . 1 $entity . . 50 . . uM . . . . 25429 1
2 'sodium phosphate' 'natural abundance' . . . . . . 10 . . mM . . . . 25429 1
3 H2O 'natural abundance' . . . . . . 90 . . % . . . . 25429 1
4 D2O 'natural abundance' . . . . . . 10 . . % . . . . 25429 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 25429
_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
pH 7.4 0.1 pH 25429 1
pressure 1 . atm 25429 1
temperature 283 1 K 25429 1
stop_
save_
############################
# Computer software used #
############################
save_CYANA
_Software.Sf_category software
_Software.Sf_framecode CYANA
_Software.Entry_ID 25429
_Software.ID 1
_Software.Name CYANA
_Software.Version 2.1
_Software.Details 'The Fold was initially determined within CYANA 2.1, Further annealing was done within AMBER12 however.'
loop_
_Task.Task
_Task.Entry_ID
_Task.Software_ID
'chemical shift assignment' 25429 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 25429
_NMR_spectrometer.ID 1
_NMR_spectrometer.Details .
_NMR_spectrometer.Manufacturer Bruker
_NMR_spectrometer.Model Avance
_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 25429
_NMR_spectrometer.ID 2
_NMR_spectrometer.Details .
_NMR_spectrometer.Manufacturer Varian
_NMR_spectrometer.Model UnityPlus
_NMR_spectrometer.Serial_number .
_NMR_spectrometer.Field_strength 400
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 25429
_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 Bruker Avance . 400 . . . 25429 1
2 spectrometer_2 Varian UnityPlus . 400 . . . 25429 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 25429
_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 13C-13C DARR (50 ms)' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25429 1
2 '2D 13C-13C DARR (200 ms)' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25429 1
3 '2D 13C-15N correlation' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25429 1
4 '1D 13C-13C fpRFDR-CT' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25429 1
5 '1D 13C-15N REDOR' no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 25429 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 25429
_Chem_shift_reference.ID 1
_Chem_shift_reference.Details .
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 TMS 'methyl carbon' . . . . ppm 0 external direct 1 . . . . . . . . . 25429 1
N 15 TMS 'methyl carbon' . . . . ppm 0 external indirect 1 . . . . . . . . . 25429 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 25429
_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 1
_Assigned_chem_shift_list.Chem_shift_13C_err 1
_Assigned_chem_shift_list.Chem_shift_15N_err 1
_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 13C-13C DARR (50 ms)' . . . 25429 1
3 '2D 13C-15N correlation' . . . 25429 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 2 2 ALA C C 13 173.600 1 . 1 . . . . 2 ALA C . 25429 1
2 . 1 1 2 2 ALA CA C 13 50.500 1 . 1 . . . . 2 ALA CA . 25429 1
3 . 1 1 2 2 ALA CB C 13 17.600 1 . 1 . . . . 2 ALA CB . 25429 1
4 . 1 1 4 4 PHE C C 13 173.000 1 . 1 . . . . 4 PHE C . 25429 1
5 . 1 1 4 4 PHE CA C 13 55.000 1 . 1 . . . . 4 PHE CA . 25429 1
6 . 1 1 4 4 PHE CB C 13 40.000 1 . 1 . . . . 4 PHE CB . 25429 1
7 . 1 1 4 4 PHE N N 15 123.600 1 . 1 . . . . 4 PHE N . 25429 1
8 . 1 1 9 9 GLY C C 13 170.500 1 . 1 . . . . 9 GLY C . 25429 1
9 . 1 1 9 9 GLY CA C 13 43.300 1 . 1 . . . . 9 GLY CA . 25429 1
10 . 1 1 9 9 GLY N N 15 109.120 1 . 1 . . . . 9 GLY N . 25429 1
11 . 1 1 12 12 VAL C C 13 172.300 1 . 1 . . . A 12 VAL C . 25429 1
12 . 1 1 12 12 VAL CA C 13 59.000 1 . 1 . . . A 12 VAL CA . 25429 1
13 . 1 1 12 12 VAL CB C 13 33.600 1 . 1 . . . A 12 VAL CB . 25429 1
14 . 1 1 12 12 VAL N N 15 125.300 1 . 1 . . . A 12 VAL N . 25429 1
15 . 1 1 13 13 HIS C C 13 171.900 1 . 1 . . . A 13 HIS C . 25429 1
16 . 1 1 13 13 HIS CA C 13 52.400 1 . 1 . . . A 13 HIS CA . 25429 1
17 . 1 1 13 13 HIS CB C 13 30.000 1 . 1 . . . A 13 HIS CB . 25429 1
18 . 1 1 17 17 LEU C C 13 172.900 1 . 1 . . . A 17 LEU C . 25429 1
19 . 1 1 17 17 LEU CA C 13 52.900 1 . 1 . . . A 17 LEU CA . 25429 1
20 . 1 1 17 17 LEU CB C 13 43.200 1 . 1 . . . A 17 LEU CB . 25429 1
21 . 1 1 17 17 LEU N N 15 132.300 1 . 1 . . . A 17 LEU N . 25429 1
22 . 1 1 18 18 VAL C C 13 171.900 1 . 1 . . . A 18 VAL C . 25429 1
23 . 1 1 18 18 VAL CA C 13 57.600 1 . 1 . . . A 18 VAL CA . 25429 1
24 . 1 1 18 18 VAL CB C 13 33.500 1 . 1 . . . A 18 VAL CB . 25429 1
25 . 1 1 18 18 VAL N N 15 125.200 1 . 1 . . . A 18 VAL N . 25429 1
26 . 1 1 19 19 PHE C C 13 172.900 1 . 1 . . . A 19 PHE C . 25429 1
27 . 1 1 19 19 PHE CA C 13 58.800 1 . 1 . . . A 19 PHE CA . 25429 1
28 . 1 1 19 19 PHE CB C 13 39.100 1 . 1 . . . A 19 PHE CB . 25429 1
29 . 1 1 19 19 PHE N N 15 130.200 1 . 1 . . . A 19 PHE N . 25429 1
30 . 1 1 20 20 PHE C C 13 172.600 1 . 1 . . . A 20 PHE C . 25429 1
31 . 1 1 20 20 PHE CA C 13 55.200 1 . 1 . . . A 20 PHE CA . 25429 1
32 . 1 1 20 20 PHE CB C 13 38.500 1 . 1 . . . A 20 PHE CB . 25429 1
33 . 1 1 20 20 PHE N N 15 117.900 1 . 1 . . . A 20 PHE N . 25429 1
34 . 1 1 21 21 ALA C C 13 175.300 1 . 1 . . . A 21 ALA C . 25429 1
35 . 1 1 21 21 ALA CA C 13 51.200 1 . 1 . . . A 21 ALA CA . 25429 1
36 . 1 1 21 21 ALA CB C 13 18.800 1 . 1 . . . A 21 ALA CB . 25429 1
37 . 1 1 21 21 ALA N N 15 124.150 1 . 1 . . . A 21 ALA N . 25429 1
38 . 1 1 23 23 ASP C C 13 173.600 1 . 1 . . . A 23 ASP C . 25429 1
39 . 1 1 23 23 ASP CA C 13 53.800 1 . 1 . . . A 23 ASP CA . 25429 1
40 . 1 1 23 23 ASP CB C 13 39.600 1 . 1 . . . A 23 ASP CB . 25429 1
41 . 1 1 23 23 ASP N N 15 122.150 1 . 1 . . . A 23 ASP N . 25429 1
42 . 1 1 24 24 VAL C C 13 175.000 1 . 1 . . . A 24 VAL C . 25429 1
43 . 1 1 24 24 VAL CA C 13 57.600 1 . 1 . . . A 24 VAL CA . 25429 1
44 . 1 1 24 24 VAL CB C 13 34.100 1 . 1 . . . A 24 VAL CB . 25429 1
45 . 1 1 24 24 VAL N N 15 118.550 1 . 1 . . . A 24 VAL N . 25429 1
46 . 1 1 25 25 GLY C C 13 172.200 1 . 1 . . . A 25 GLY C . 25429 1
47 . 1 1 25 25 GLY CA C 13 46.500 1 . 1 . . . A 25 GLY CA . 25429 1
48 . 1 1 25 25 GLY N N 15 115.540 1 . 1 . . . A 25 GLY N . 25429 1
49 . 1 1 26 26 SER C C 13 170.300 1 . 1 . . . A 26 SER C . 25429 1
50 . 1 1 26 26 SER CA C 13 54.400 1 . 1 . . . A 26 SER CA . 25429 1
51 . 1 1 26 26 SER CB C 13 63.800 1 . 1 . . . A 26 SER CB . 25429 1
52 . 1 1 26 26 SER N N 15 115.000 1 . 1 . . . A 26 SER N . 25429 1
53 . 1 1 28 28 LYS C C 13 173.200 1 . 1 . . . A 28 LYS C . 25429 1
54 . 1 1 28 28 LYS CA C 13 52.600 1 . 1 . . . A 28 LYS CA . 25429 1
55 . 1 1 28 28 LYS CB C 13 33.300 1 . 1 . . . A 28 LYS CB . 25429 1
56 . 1 1 28 28 LYS N N 15 129.300 1 . 1 . . . A 28 LYS N . 25429 1
57 . 1 1 29 29 GLY C C 13 169.400 1 . 1 . . . A 29 GLY C . 25429 1
58 . 1 1 29 29 GLY CA C 13 46.600 1 . 1 . . . A 29 GLY CA . 25429 1
59 . 1 1 29 29 GLY N N 15 113.600 1 . 1 . . . A 29 GLY N . 25429 1
60 . 1 1 30 30 ALA C C 13 173.900 1 . 1 . . . A 30 ALA C . 25429 1
61 . 1 1 30 30 ALA CA C 13 49.000 1 . 1 . . . A 30 ALA CA . 25429 1
62 . 1 1 30 30 ALA CB C 13 20.000 1 . 1 . . . A 30 ALA CB . 25429 1
63 . 1 1 30 30 ALA N N 15 126.000 1 . 1 . . . A 30 ALA N . 25429 1
64 . 1 1 31 31 ILE C C 13 171.900 1 . 1 . . . A 31 ILE C . 25429 1
65 . 1 1 31 31 ILE CA C 13 58.200 1 . 1 . . . A 31 ILE CA . 25429 1
66 . 1 1 31 31 ILE CB C 13 42.600 1 . 1 . . . A 31 ILE CB . 25429 1
67 . 1 1 31 31 ILE N N 15 121.700 1 . 1 . . . A 31 ILE N . 25429 1
68 . 1 1 32 32 ILE C C 13 172.300 1 . 1 . . . A 32 ILE C . 25429 1
69 . 1 1 32 32 ILE CA C 13 58.300 1 . 1 . . . A 32 ILE CA . 25429 1
70 . 1 1 32 32 ILE CB C 13 39.500 1 . 1 . . . A 32 ILE CB . 25429 1
71 . 1 1 32 32 ILE N N 15 126.520 1 . 1 . . . A 32 ILE N . 25429 1
72 . 1 1 33 33 GLY C C 13 170.600 1 . 1 . . . A 33 GLY C . 25429 1
73 . 1 1 33 33 GLY CA C 13 44.400 1 . 1 . . . A 33 GLY CA . 25429 1
74 . 1 1 33 33 GLY N N 15 111.280 1 . 1 . . . A 33 GLY N . 25429 1
75 . 1 1 34 34 LEU C C 13 176.600 1 . 1 . . . A 34 LEU C . 25429 1
76 . 1 1 34 34 LEU CA C 13 55.400 1 . 1 . . . A 34 LEU CA . 25429 1
77 . 1 1 34 34 LEU CB C 13 40.100 1 . 1 . . . A 34 LEU CB . 25429 1
78 . 1 1 34 34 LEU N N 15 111.460 1 . 1 . . . A 34 LEU N . 25429 1
79 . 1 1 36 36 VAL C C 13 173.200 1 . 1 . . . A 36 VAL C . 25429 1
80 . 1 1 36 36 VAL CA C 13 58.900 1 . 1 . . . A 36 VAL CA . 25429 1
81 . 1 1 36 36 VAL CB C 13 32.800 1 . 1 . . . A 36 VAL CB . 25429 1
82 . 1 1 36 36 VAL N N 15 124.360 1 . 1 . . . A 36 VAL N . 25429 1
83 . 1 1 37 37 GLY C C 13 170.500 1 . 1 . . . A 37 GLY C . 25429 1
84 . 1 1 37 37 GLY CA C 13 43.600 1 . 1 . . . A 37 GLY CA . 25429 1
85 . 1 1 37 37 GLY N N 15 116.240 1 . 1 . . . A 37 GLY N . 25429 1
86 . 1 1 38 38 GLY C C 13 171.500 1 . 1 . . . A 38 GLY C . 25429 1
87 . 1 1 38 38 GLY CA C 13 46.800 1 . 1 . . . A 38 GLY CA . 25429 1
88 . 1 1 38 38 GLY N N 15 113.600 1 . 1 . . . A 38 GLY N . 25429 1
89 . 1 1 39 39 VAL C C 13 171.900 1 . 1 . . . A 39 VAL C . 25429 1
90 . 1 1 39 39 VAL CA C 13 58.300 1 . 1 . . . A 39 VAL CA . 25429 1
91 . 1 1 39 39 VAL CB C 13 34.000 1 . 1 . . . A 39 VAL CB . 25429 1
92 . 1 1 39 39 VAL N N 15 120.300 1 . 1 . . . A 39 VAL N . 25429 1
93 . 1 1 40 40 VAL C C 13 171.800 1 . 1 . . . A 40 VAL C . 25429 1
94 . 1 1 40 40 VAL CA C 13 59.100 1 . 1 . . . A 40 VAL CA . 25429 1
95 . 1 1 40 40 VAL CB C 13 33.300 1 . 1 . . . A 40 VAL CB . 25429 1
96 . 1 1 40 40 VAL N N 15 127.600 1 . 1 . . . A 40 VAL N . 25429 1
97 . 1 1 41 41 ILE C C 13 171.200 1 . 1 . . . A 41 ILE C . 25429 1
98 . 1 1 41 41 ILE CA C 13 58.300 1 . 1 . . . A 41 ILE CA . 25429 1
99 . 1 1 41 41 ILE CB C 13 37.800 1 . 1 . . . A 41 ILE CB . 25429 1
100 . 1 1 41 41 ILE N N 15 128.600 1 . 1 . . . A 41 ILE N . 25429 1
101 . 1 1 42 42 ALA C C 13 180.000 1 . 1 . . . A 42 ALA C . 25429 1
102 . 1 1 42 42 ALA CA C 13 50.800 1 . 1 . . . A 42 ALA CA . 25429 1
103 . 1 1 42 42 ALA CB C 13 19.300 1 . 1 . . . A 42 ALA CB . 25429 1
stop_
save_