data_25289
#######################
# Entry information #
#######################
save_entry_information
_Entry.Sf_category entry_information
_Entry.Sf_framecode entry_information
_Entry.ID 25289
_Entry.Title
;
Atomic-resolution 3D structure of amyloid-beta fibrils: the Osaka mutation
;
_Entry.Type macromolecule
_Entry.Version_type original
_Entry.Submission_date 2014-10-17
_Entry.Accession_date 2014-10-17
_Entry.Last_release_date 2015-08-25
_Entry.Original_release_date 2015-08-25
_Entry.Origination author
_Entry.NMR_STAR_version 3.1.1.81
_Entry.Original_NMR_STAR_version 3.1
_Entry.Experimental_method NMR
_Entry.Experimental_method_subtype 'NMR, 20 STRUCTURES'
_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 Anne Schuetz . K. . 25289
2 Toni Vagt . . . 25289
3 Matthias Huber . . . 25289
4 Oxana Ovchinnikova . Y. . 25289
5 Riccardo Cadalbert . . . 25289
6 Joseph Wall . . . 25289
7 Peter Guentert . . . 25289
8 Anja Bockmann . . . 25289
9 Rudi Glockshuber . . . 25289
10 Beat Meier . H. . 25289
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' . 25289
stop_
loop_
_Struct_keywords.Keywords
_Struct_keywords.Text
_Struct_keywords.Entry_ID
'Osaka mutation' . 25289
'amyloid beta' . 25289
'amyloid fibrils' . 25289
'solid-state NMR' . 25289
stop_
loop_
_Data_set.Type
_Data_set.Count
_Data_set.Entry_ID
assigned_chemical_shifts 3 25289
stop_
loop_
_Datum.Type
_Datum.Count
_Datum.Entry_ID
'13C chemical shifts' 477 25289
'15N chemical shifts' 91 25289
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 . . 2015-08-25 2014-10-17 update BMRB 'update entry citation' 25289
1 . . 2014-11-24 2014-10-17 original author 'original release' 25289
stop_
loop_
_Related_entries.Database_name
_Related_entries.Database_accession_code
_Related_entries.Relationship
_Related_entries.Entry_ID
PDB 2MVX 'BMRB Entry Tracking System' 25289
stop_
save_
###############
# Citations #
###############
save_entry_citation
_Citation.Sf_category citations
_Citation.Sf_framecode entry_citation
_Citation.Entry_ID 25289
_Citation.ID 1
_Citation.Class 'entry citation'
_Citation.CAS_abstract_code .
_Citation.MEDLINE_UI_code .
_Citation.DOI .
_Citation.PubMed_ID 25395337
_Citation.Full_citation .
_Citation.Title
;
Atomic-Resolution Three-Dimensional Structure of Amyloid beta Fibrils Bearing the Osaka Mutation
;
_Citation.Status published
_Citation.Type journal
_Citation.Journal_abbrev 'Angew. Chem. Int. Ed. Engl.'
_Citation.Journal_name_full .
_Citation.Journal_volume 54
_Citation.Journal_issue 1
_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 331
_Citation.Page_last 335
_Citation.Year 2015
_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 Anne Schuetz . K. . 25289 1
2 Toni Vagt . . . 25289 1
3 Matthias Huber . . . 25289 1
4 Oxana Ovchinnikova . Y. . 25289 1
5 Riccardo Cadalbert . . . 25289 1
6 Joseph Wall . . . 25289 1
7 Peter Guentert . . . 25289 1
8 Anja Bockmann . . . 25289 1
9 Rudi Glockshuber . . . 25289 1
10 Beat Meier . H. . 25289 1
stop_
save_
#############################################
# Molecular system (assembly) description #
#############################################
save_assembly
_Assembly.Sf_category assembly
_Assembly.Sf_framecode assembly
_Assembly.Entry_ID 25289
_Assembly.ID 1
_Assembly.Name 'amyloid-beta fibrils: the Osaka mutation'
_Assembly.BMRB_code .
_Assembly.Number_of_components 10
_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 $amyloid_beta A . yes native no no . . . 25289 1
2 entity_2 1 $amyloid_beta B . yes native no no . . . 25289 1
3 entity_3 1 $amyloid_beta C . yes native no no . . . 25289 1
4 entity_4 1 $amyloid_beta D . yes native no no . . . 25289 1
5 entity_5 1 $amyloid_beta E . yes native no no . . . 25289 1
6 entity_6 1 $amyloid_beta F . yes native no no . . . 25289 1
7 entity_7 1 $amyloid_beta G . yes native no no . . . 25289 1
8 entity_8 1 $amyloid_beta H . yes native no no . . . 25289 1
9 entity_9 1 $amyloid_beta I . yes native no no . . . 25289 1
10 entity_10 1 $amyloid_beta J . yes native no no . . . 25289 1
stop_
save_
####################################
# Biological polymers and ligands #
####################################
save_amyloid_beta
_Entity.Sf_category entity
_Entity.Sf_framecode amyloid_beta
_Entity.Entry_ID 25289
_Entity.ID 1
_Entity.BMRB_code .
_Entity.Name amyloid_beta
_Entity.Type polymer
_Entity.Polymer_common_type .
_Entity.Polymer_type polypeptide(L)
_Entity.Polymer_type_details .
_Entity.Polymer_strand_ID ABCDEFGHIJ
_Entity.Polymer_seq_one_letter_code_can .
_Entity.Polymer_seq_one_letter_code
;
DAEFRHDSGYEVHHQKLVFF
ADVGSNKGAIIGLMVGGVV
;
_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 39
_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 'Osaka mutation E22Delta'
_Entity.EC_number .
_Entity.Calc_isoelectric_point .
_Entity.Formula_weight 4206.777
_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) . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
2 no BMRB 15775 . APP_C99 . . . . . 102.56 122 97.50 97.50 3.93e-16 . . . . 25289 1
3 no BMRB 17159 . Amyloid_beta-Peptide . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
4 no BMRB 17186 . Abeta . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
5 no BMRB 17764 . Abeta . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
6 no BMRB 17793 . Abeta(1-42) . . . . . 102.56 42 97.50 97.50 4.60e-16 . . . . 25289 1
7 no BMRB 17794 . Abeta(1-42) . . . . . 102.56 42 97.50 97.50 4.60e-16 . . . . 25289 1
8 no BMRB 17795 . Abeta(1-40) . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
9 no BMRB 17796 . Abeta40 . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
10 no BMRB 18052 . Pyroglutamate_Abeta . . . . . 94.87 38 97.30 97.30 1.15e-13 . . . . 25289 1
11 no BMRB 18127 . beta-amyloid . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
12 no BMRB 18128 . beta-amyloid . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
13 no BMRB 18129 . beta-amyloid . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
14 no BMRB 18131 . beta-amyloid . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
15 no BMRB 19009 . beta-amyloid_peptide . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
16 no BMRB 19309 . amyloid_peptide . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
17 no BMRB 19393 . Abeta . . . . . 100.00 39 100.00 100.00 9.32e-18 . . . . 25289 1
18 no BMRB 25218 . amyloid_peptide . . . . . 102.56 42 97.50 97.50 4.60e-16 . . . . 25289 1
19 no BMRB 25429 . entity . . . . . 102.56 42 97.50 97.50 4.60e-16 . . . . 25289 1
20 no BMRB 26508 . amyloid_B . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
21 no BMRB 26516 . amyloid_B . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
22 no PDB 1AML . "The Alzheimer`s Disease Amyloid A4 Peptide (Residues 1-40)" . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
23 no PDB 1BA4 . "The Solution Structure Of Amyloid Beta-Peptide (1-40) In A Water-Micelle Environment. Is The Membrane-Spanning Domain Where We " . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
24 no PDB 1IYT . "Solution Structure Of The Alzheimer's Disease Amyloid Beta- Peptide (1-42)" . . . . . 102.56 42 97.50 97.50 4.60e-16 . . . . 25289 1
25 no PDB 1Z0Q . "Aqueous Solution Structure Of The Alzheimer's Disease Abeta Peptide (1-42)" . . . . . 102.56 42 97.50 97.50 4.60e-16 . . . . 25289 1
26 no PDB 2BEG . "3d Structure Of Alzheimer's Abeta(1-42) Fibrils" . . . . . 102.56 42 97.50 97.50 4.60e-16 . . . . 25289 1
27 no PDB 2G47 . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-40)" . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
28 no PDB 2LFM . "A Partially Folded Structure Of Amyloid-Beta(1 40) In An Aqueous Environment" . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
29 no PDB 2LMN . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Positive Stagger" . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
30 no PDB 2LMO . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Two-Fold Symmetry, Negative Stagger" . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
31 no PDB 2LMP . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Positive Stagger" . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
32 no PDB 2LMQ . "Structural Model For A 40-Residue Beta-Amyloid Fibril With Three-Fold Symmetry, Negative Stagger" . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
33 no PDB 2LP1 . "The Solution Nmr Structure Of The Transmembrane C-Terminal Domain Of The Amyloid Precursor Protein (C99)" . . . . . 102.56 122 97.50 97.50 3.93e-16 . . . . 25289 1
34 no PDB 2M4J . "40-residue Beta-amyloid Fibril Derived From Alzheimer's Disease Brain" . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
35 no PDB 2M9R . "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
36 no PDB 2M9S . "3d Nmr Structure Of A Complex Between The Amyloid Beta Peptide (1-40) And The Polyphenol Epsilon-viniferin Glucoside" . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
37 no PDB 2MVX . "Atomic-resolution 3d Structure Of Amyloid-beta Fibrils: The Osaka Mutation" . . . . . 100.00 39 100.00 100.00 9.32e-18 . . . . 25289 1
38 no PDB 2MXU . "42-residue Beta Amyloid Fibril" . . . . . 102.56 42 97.50 97.50 4.60e-16 . . . . 25289 1
39 no PDB 2OTK . "Structure Of Alzheimer Ab Peptide In Complex With An Engineered Binding Protein" . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
40 no PDB 2WK3 . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Amyloid-Beta (1-42)" . . . . . 102.56 42 97.50 97.50 4.60e-16 . . . . 25289 1
41 no PDB 3IFN . "X-ray Structure Of Amyloid Beta Peptide:antibody (abeta1-40:12a11) Complex" . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
42 no PDB 4M1C . "Crystal Structure Analysis Of Fab-bound Human Insulin Degrading Enzyme (ide) In Complex With Amyloid-beta (1-40)" . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
43 no PDB 4MVI . "Crystal Structure Of An Engineered Lipocalin (anticalin Us7) In Complex With The Alzheimer Amyloid Peptide Abeta(1-40)" . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
44 no PDB 4MVL . "Crystal Structure Of An Engineered Lipocalin (anticalin H1ga) In Complex With The Alzheimer Amyloid Peptide Abeta1-40" . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
45 no PDB 4NGE . "Crystal Structure Of Human Presequence Protease In Complex With Amyloid-beta (1-40)" . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
46 no PDB 4ONG . "Fab Fragment Of 3d6 In Complex With Amyloid Beta 1-40" . . . . . 102.56 40 97.50 97.50 5.23e-16 . . . . 25289 1
47 no DBJ BAA22264 . "amyloid precursor protein [Homo sapiens]" . . . . . 102.56 770 97.50 97.50 2.71e-16 . . . . 25289 1
48 no DBJ BAA84580 . "amyloid precursor protein [Sus scrofa]" . . . . . 102.56 770 97.50 97.50 2.71e-16 . . . . 25289 1
49 no DBJ BAD51938 . "amyloid beta A4 precursor protein [Macaca fascicularis]" . . . . . 102.56 696 97.50 97.50 2.46e-16 . . . . 25289 1
50 no DBJ BAE01907 . "unnamed protein product [Macaca fascicularis]" . . . . . 102.56 751 97.50 97.50 2.65e-16 . . . . 25289 1
51 no DBJ BAG10647 . "amyloid beta A4 protein precursor [synthetic construct]" . . . . . 102.56 770 97.50 97.50 2.71e-16 . . . . 25289 1
52 no EMBL CAA30050 . "amyloid A4 protein [Homo sapiens]" . . . . . 102.56 751 97.50 97.50 2.65e-16 . . . . 25289 1
53 no EMBL CAA31830 . "A4 amyloid protein precursor [Homo sapiens]" . . . . . 102.56 695 97.50 97.50 2.46e-16 . . . . 25289 1
54 no EMBL CAA39589 . "amyloid precursor protein [Bos taurus]" . . . . . 102.56 59 97.50 97.50 1.31e-16 . . . . 25289 1
55 no EMBL CAA39590 . "amyloid precursor protein [Canis lupus familiaris]" . . . . . 102.56 58 97.50 97.50 1.32e-16 . . . . 25289 1
56 no EMBL CAA39591 . "amyloid precursor protein [Cavia sp.]" . . . . . 102.56 58 97.50 97.50 1.32e-16 . . . . 25289 1
57 no GB AAA35540 . "amyloid protein, partial [Homo sapiens]" . . . . . 97.44 97 97.37 97.37 6.86e-15 . . . . 25289 1
58 no GB AAA36829 . "amyloid b-protein precursor [Macaca fascicularis]" . . . . . 102.56 695 97.50 97.50 2.46e-16 . . . . 25289 1
59 no GB AAA51722 . "amyloid beta-protein precursor, partial [Homo sapiens]" . . . . . 102.56 412 97.50 97.50 8.95e-17 . . . . 25289 1
60 no GB AAA51726 . "beta-amyloid A4, partial [Homo sapiens]" . . . . . 102.56 264 97.50 97.50 1.67e-16 . . . . 25289 1
61 no GB AAA51727 . "amyloid-beta protein, partial [Homo sapiens]" . . . . . 102.56 82 97.50 97.50 1.40e-16 . . . . 25289 1
62 no PIR A60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - dog (fragment)" . . . . . 102.56 57 97.50 97.50 1.41e-16 . . . . 25289 1
63 no PIR D60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - bovine (fragment)" . . . . . 102.56 57 97.50 97.50 1.41e-16 . . . . 25289 1
64 no PIR E60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - sheep (fragment)" . . . . . 102.56 57 97.50 97.50 1.41e-16 . . . . 25289 1
65 no PIR G60045 . "Alzheimer's disease amyloid beta/A4 protein precursor - guinea pig (fragment)" . . . . . 102.56 57 97.50 97.50 1.41e-16 . . . . 25289 1
66 no PIR PQ0438 . "Alzheimer's disease amyloid A4 protein precursor - rabbit (fragment)" . . . . . 102.56 82 97.50 97.50 1.40e-16 . . . . 25289 1
67 no PRF 1303338A . "amyloid A4 protein precursor" . . . . . 102.56 695 97.50 97.50 2.46e-16 . . . . 25289 1
68 no PRF 1403400A . "amyloid protein A4" . . . . . 102.56 751 97.50 97.50 2.65e-16 . . . . 25289 1
69 no PRF 1405204A . "amyloid protein" . . . . . 102.56 42 97.50 97.50 4.60e-16 . . . . 25289 1
70 no PRF 1507304A . "beta amyloid peptide precursor" . . . . . 102.56 412 97.50 97.50 8.95e-17 . . . . 25289 1
71 no PRF 1507304B . "beta amyloid peptide precursor" . . . . . 102.56 574 97.50 97.50 1.92e-16 . . . . 25289 1
72 no REF NP_000475 . "amyloid beta A4 protein isoform a precursor [Homo sapiens]" . . . . . 102.56 770 97.50 97.50 2.71e-16 . . . . 25289 1
73 no REF NP_001006601 . "amyloid beta A4 protein isoform APP-770 precursor [Canis lupus familiaris]" . . . . . 102.56 770 97.50 97.50 2.71e-16 . . . . 25289 1
74 no REF NP_001013036 . "amyloid beta A4 protein precursor [Pan troglodytes]" . . . . . 102.56 770 97.50 97.50 2.71e-16 . . . . 25289 1
75 no REF NP_001070264 . "amyloid beta A4 protein precursor [Bos taurus]" . . . . . 102.56 695 97.50 97.50 2.46e-16 . . . . 25289 1
76 no REF NP_001127014 . "amyloid beta A4 protein precursor [Pongo abelii]" . . . . . 102.56 695 97.50 97.50 2.46e-16 . . . . 25289 1
77 no SP P05067 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; AltName: Full=APPI; Short=APP; AltName: Full=Alzheimer disease amylo" . . . . . 102.56 770 97.50 97.50 2.71e-16 . . . . 25289 1
78 no SP P53601 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 102.56 770 97.50 97.50 2.71e-16 . . . . 25289 1
79 no SP P79307 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 102.56 770 97.50 97.50 2.71e-16 . . . . 25289 1
80 no SP Q28053 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 102.56 59 97.50 97.50 1.31e-16 . . . . 25289 1
81 no SP Q28280 . "RecName: Full=Amyloid beta A4 protein; AltName: Full=ABPP; Short=APP; AltName: Full=Alzheimer disease amyloid A4 protein homolo" . . . . . 102.56 58 97.50 97.50 1.32e-16 . . . . 25289 1
82 no TPG DAA33655 . "TPA: amyloid beta A4 protein [Bos taurus]" . . . . . 102.56 695 97.50 97.50 2.46e-16 . . . . 25289 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 . 25289 1
2 . ALA . 25289 1
3 . GLU . 25289 1
4 . PHE . 25289 1
5 . ARG . 25289 1
6 . HIS . 25289 1
7 . ASP . 25289 1
8 . SER . 25289 1
9 . GLY . 25289 1
10 . TYR . 25289 1
11 . GLU . 25289 1
12 . VAL . 25289 1
13 . HIS . 25289 1
14 . HIS . 25289 1
15 . GLN . 25289 1
16 . LYS . 25289 1
17 . LEU . 25289 1
18 . VAL . 25289 1
19 . PHE . 25289 1
20 . PHE . 25289 1
21 . ALA . 25289 1
22 . ASP . 25289 1
23 . VAL . 25289 1
24 . GLY . 25289 1
25 . SER . 25289 1
26 . ASN . 25289 1
27 . LYS . 25289 1
28 . GLY . 25289 1
29 . ALA . 25289 1
30 . ILE . 25289 1
31 . ILE . 25289 1
32 . GLY . 25289 1
33 . LEU . 25289 1
34 . MET . 25289 1
35 . VAL . 25289 1
36 . GLY . 25289 1
37 . GLY . 25289 1
38 . VAL . 25289 1
39 . VAL . 25289 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 25289 1
. ALA 2 2 25289 1
. GLU 3 3 25289 1
. PHE 4 4 25289 1
. ARG 5 5 25289 1
. HIS 6 6 25289 1
. ASP 7 7 25289 1
. SER 8 8 25289 1
. GLY 9 9 25289 1
. TYR 10 10 25289 1
. GLU 11 11 25289 1
. VAL 12 12 25289 1
. HIS 13 13 25289 1
. HIS 14 14 25289 1
. GLN 15 15 25289 1
. LYS 16 16 25289 1
. LEU 17 17 25289 1
. VAL 18 18 25289 1
. PHE 19 19 25289 1
. PHE 20 20 25289 1
. ALA 21 21 25289 1
. ASP 22 22 25289 1
. VAL 23 23 25289 1
. GLY 24 24 25289 1
. SER 25 25 25289 1
. ASN 26 26 25289 1
. LYS 27 27 25289 1
. GLY 28 28 25289 1
. ALA 29 29 25289 1
. ILE 30 30 25289 1
. ILE 31 31 25289 1
. GLY 32 32 25289 1
. LEU 33 33 25289 1
. MET 34 34 25289 1
. VAL 35 35 25289 1
. GLY 36 36 25289 1
. GLY 37 37 25289 1
. VAL 38 38 25289 1
. VAL 39 39 25289 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 25289
_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 $amyloid_beta . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . 25289 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 25289
_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 $amyloid_beta . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli BL21 DE3 . . . . 'pET T7' . . . 25289 1
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_uniform_13C15N
_Sample.Sf_category sample
_Sample.Sf_framecode uniform_13C15N
_Sample.Entry_ID 25289
_Sample.ID 1
_Sample.Type solid
_Sample.Sub_type .
_Sample.Details .
_Sample.Aggregate_sample_number .
_Sample.Solvent_system '100% H2O'
_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 'amyloid beta' '[U-100% 13C; U-100% 15N]' . . 1 $amyloid_beta . . 15 . . mg . . . . 25289 1
stop_
save_
save_uniform_13C
_Sample.Sf_category sample
_Sample.Sf_framecode uniform_13C
_Sample.Entry_ID 25289
_Sample.ID 2
_Sample.Type solid
_Sample.Sub_type .
_Sample.Details .
_Sample.Aggregate_sample_number .
_Sample.Solvent_system '100% H2O'
_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 'amyloid beta' '[U-100% 13C]' . . 1 $amyloid_beta . . 15 . . mg . . . . 25289 2
stop_
save_
save_mixed_13C-15N
_Sample.Sf_category sample
_Sample.Sf_framecode mixed_13C-15N
_Sample.Entry_ID 25289
_Sample.ID 3
_Sample.Type solid
_Sample.Sub_type .
_Sample.Details 'Selectively 13C and 15N labeled monomers were mixed before fibrillation in a 1/1 ratio.'
_Sample.Aggregate_sample_number .
_Sample.Solvent_system '100% H2O'
_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 'amyloid beta' '[U-100% 13C; U-100% 15N]' . . 1 $amyloid_beta . . 15 . . mg . . . . 25289 3
stop_
save_
save_2-13C-glucose
_Sample.Sf_category sample
_Sample.Sf_framecode 2-13C-glucose
_Sample.Entry_ID 25289
_Sample.ID 4
_Sample.Type solid
_Sample.Sub_type .
_Sample.Details .
_Sample.Aggregate_sample_number .
_Sample.Solvent_system '100% H2O'
_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 'amyloid beta' '[U-100% 2-13C-glucose; U-100% 15N]' . . 1 $amyloid_beta . . 15 . . mg . . . . 25289 4
stop_
save_
save_diluted
_Sample.Sf_category sample
_Sample.Sf_framecode diluted
_Sample.Entry_ID 25289
_Sample.ID 5
_Sample.Type solid
_Sample.Sub_type .
_Sample.Details 'Selectively [13C,15N} and natural abundance monomers were mixed before fibrillation in a 1/4 ratio.'
_Sample.Aggregate_sample_number .
_Sample.Solvent_system '100% H2O'
_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 'amyloid beta' '[U-100% 13C; U-100% 15N]/natural abundance' . . 1 $amyloid_beta . . 15 . . mg . . . . 25289 5
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 25289
_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' 0 . M 25289 1
pH 7 . pH 25289 1
pressure 1 . atm 25289 1
temperature 273 . K 25289 1
stop_
save_
############################
# Computer software used #
############################
save_CYANA
_Software.Sf_category software
_Software.Sf_framecode CYANA
_Software.Entry_ID 25289
_Software.ID 1
_Software.Name CYANA
_Software.Version 3.9.6
_Software.Details .
loop_
_Vendor.Name
_Vendor.Address
_Vendor.Electronic_address
_Vendor.Entry_ID
_Vendor.Software_ID
'Guntert, Mumenthaler and Wuthrich' . . 25289 1
stop_
loop_
_Task.Task
_Task.Entry_ID
_Task.Software_ID
'structure solution' 25289 1
stop_
save_
save_CcpNMR
_Software.Sf_category software
_Software.Sf_framecode CcpNMR
_Software.Entry_ID 25289
_Software.ID 2
_Software.Name CcpNMR
_Software.Version 2.2.2
_Software.Details .
loop_
_Vendor.Name
_Vendor.Address
_Vendor.Electronic_address
_Vendor.Entry_ID
_Vendor.Software_ID
CCPN . . 25289 2
stop_
loop_
_Task.Task
_Task.Entry_ID
_Task.Software_ID
'chemical shift assignment' 25289 2
'data analysis' 25289 2
'peak picking' 25289 2
stop_
save_
save_TALOS+
_Software.Sf_category software
_Software.Sf_framecode TALOS+
_Software.Entry_ID 25289
_Software.ID 3
_Software.Name TALOS+
_Software.Version 2.1
_Software.Details .
loop_
_Vendor.Name
_Vendor.Address
_Vendor.Electronic_address
_Vendor.Entry_ID
_Vendor.Software_ID
'Cornilescu, Delaglio and Bax' . . 25289 3
stop_
loop_
_Task.Task
_Task.Entry_ID
_Task.Software_ID
'dihedral angle prediction' 25289 3
stop_
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_850_MHz
_NMR_spectrometer.Sf_category NMR_spectrometer
_NMR_spectrometer.Sf_framecode 850_MHz
_NMR_spectrometer.Entry_ID 25289
_NMR_spectrometer.ID 1
_NMR_spectrometer.Details
;
widebore magnet
Bruker triple resonance 3.2 mm MAS probe
;
_NMR_spectrometer.Manufacturer Bruker
_NMR_spectrometer.Model Avance
_NMR_spectrometer.Serial_number .
_NMR_spectrometer.Field_strength 850
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 25289
_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
1 850_MHz Bruker Avance . 850
;
widebore magnet
Bruker triple resonance 3.2 mm MAS probe
; . . 25289 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 25289
_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 NCA no . . . . . . . . . . 1 $uniform_13C15N solid . . 1 $sample_conditions_1 . . . 1 $850_MHz . . . . . . . . . . . . . . . . 25289 1
2 NCO no . . . . . . . . . . 1 $uniform_13C15N solid . . 1 $sample_conditions_1 . . . 1 $850_MHz . . . . . . . . . . . . . . . . 25289 1
3 'DARR 15 ms' no . . . . . . . . . . 2 $uniform_13C solid . . 1 $sample_conditions_1 . . . 1 $850_MHz . . . . . . . . . . . . . . . . 25289 1
4 'PAIN 6 ms' no . . . . . . . . . . 1 $uniform_13C15N solid . . 1 $sample_conditions_1 . . . 1 $850_MHz . . . . . . . . . . . . . . . . 25289 1
5 'PAIN 6 ms' no . . . . . . . . . . 3 $mixed_13C-15N solid . . 1 $sample_conditions_1 . . . 1 $850_MHz . . . . . . . . . . . . . . . . 25289 1
6 'DARR 400 ms' no . . . . . . . . . . 2 $uniform_13C solid . . 1 $sample_conditions_1 . . . 1 $850_MHz . . . . . . . . . . . . . . . . 25289 1
7 'DARR 400 ms' no . . . . . . . . . . 5 $diluted solid . . 1 $sample_conditions_1 . . . 1 $850_MHz . . . . . . . . . . . . . . . . 25289 1
8 'PAR 8 ms' no . . . . . . . . . . 2 $uniform_13C solid . . 1 $sample_conditions_1 . . . 1 $850_MHz . . . . . . . . . . . . . . . . 25289 1
9 'PAR 8 ms' no . . . . . . . . . . 5 $diluted solid . . 1 $sample_conditions_1 . . . 1 $850_MHz . . . . . . . . . . . . . . . . 25289 1
10 'CHHC 500 us' no . . . . . . . . . . 2 $uniform_13C solid . . 1 $sample_conditions_1 . . . 1 $850_MHz . . . . . . . . . . . . . . . . 25289 1
11 'CHHC 500 us' no . . . . . . . . . . 5 $diluted solid . . 1 $sample_conditions_1 . . . 1 $850_MHz . . . . . . . . . . . . . . . . 25289 1
12 'PDSD 4 s' no . . . . . . . . . . 4 $2-13C-glucose solid . . 1 $sample_conditions_1 . . . 1 $850_MHz . . . . . . . . . . . . . . . . 25289 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 25289
_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 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.251449530 . . . . . . . . . 25289 1
N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . . . . . 25289 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_chemical_shift_uniform_13C15N
_Assigned_chem_shift_list.Sf_category assigned_chemical_shifts
_Assigned_chem_shift_list.Sf_framecode assigned_chemical_shift_uniform_13C15N
_Assigned_chem_shift_list.Entry_ID 25289
_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 0.2
_Assigned_chem_shift_list.Chem_shift_15N_err 0.2
_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 NCA . . . 25289 1
2 NCO . . . 25289 1
4 'PAIN 6 ms' . . . 25289 1
stop_
loop_
_Chem_shift_software.Software_ID
_Chem_shift_software.Software_label
_Chem_shift_software.Method_ID
_Chem_shift_software.Method_label
_Chem_shift_software.Entry_ID
_Chem_shift_software.Assigned_chem_shift_list_ID
2 $CcpNMR . . 25289 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 1 1 ASP C C 13 173.601 0.20 . 1 . . . A 1 ASP C . 25289 1
2 . 1 1 1 1 ASP CA C 13 54.174 0.20 . 1 . . . A 1 ASP CA . 25289 1
3 . 1 1 1 1 ASP CB C 13 40.915 0.20 . 1 . . . A 1 ASP CB . 25289 1
4 . 1 1 1 1 ASP CG C 13 179.615 0.20 . 1 . . . A 1 ASP CG . 25289 1
5 . 1 1 1 1 ASP N N 15 37.421 0.20 . 1 . . . A 1 ASP N . 25289 1
6 . 1 1 2 2 ALA C C 13 177.737 0.20 . 1 . . . A 2 ALA C . 25289 1
7 . 1 1 2 2 ALA CA C 13 51.880 0.20 . 1 . . . A 2 ALA CA . 25289 1
8 . 1 1 2 2 ALA CB C 13 15.692 0.20 . 1 . . . A 2 ALA CB . 25289 1
9 . 1 1 2 2 ALA N N 15 118.014 0.20 . 1 . . . A 2 ALA N . 25289 1
10 . 1 1 3 3 GLU C C 13 176.622 0.20 . 1 . . . A 3 GLU C . 25289 1
11 . 1 1 3 3 GLU CA C 13 62.504 0.20 . 1 . . . A 3 GLU CA . 25289 1
12 . 1 1 3 3 GLU CB C 13 29.623 0.20 . 1 . . . A 3 GLU CB . 25289 1
13 . 1 1 3 3 GLU CG C 13 39.104 0.20 . 1 . . . A 3 GLU CG . 25289 1
14 . 1 1 3 3 GLU CD C 13 183.635 0.20 . 1 . . . A 3 GLU CD . 25289 1
15 . 1 1 3 3 GLU N N 15 121.987 0.20 . 1 . . . A 3 GLU N . 25289 1
16 . 1 1 4 4 PHE C C 13 175.867 0.20 . 1 . . . A 4 PHE C . 25289 1
17 . 1 1 4 4 PHE CA C 13 57.984 0.20 . 1 . . . A 4 PHE CA . 25289 1
18 . 1 1 4 4 PHE CB C 13 41.700 0.20 . 1 . . . A 4 PHE CB . 25289 1
19 . 1 1 4 4 PHE CG C 13 137.488 0.20 . 1 . . . A 4 PHE CG . 25289 1
20 . 1 1 4 4 PHE CD1 C 13 133.089 0.20 . 3 . . . A 4 PHE CD1 . 25289 1
21 . 1 1 4 4 PHE CE1 C 13 131.573 0.20 . 3 . . . A 4 PHE CE1 . 25289 1
22 . 1 1 4 4 PHE CZ C 13 128.840 0.20 . 1 . . . A 4 PHE CZ . 25289 1
23 . 1 1 4 4 PHE N N 15 114.820 0.20 . 1 . . . A 4 PHE N . 25289 1
24 . 1 1 5 5 ARG C C 13 173.318 0.20 . 1 . . . A 5 ARG C . 25289 1
25 . 1 1 5 5 ARG CA C 13 54.636 0.20 . 1 . . . A 5 ARG CA . 25289 1
26 . 1 1 5 5 ARG CB C 13 33.723 0.20 . 1 . . . A 5 ARG CB . 25289 1
27 . 1 1 5 5 ARG CG C 13 27.366 0.20 . 1 . . . A 5 ARG CG . 25289 1
28 . 1 1 5 5 ARG CD C 13 43.795 0.20 . 1 . . . A 5 ARG CD . 25289 1
29 . 1 1 5 5 ARG CZ C 13 159.541 0.20 . 1 . . . A 5 ARG CZ . 25289 1
30 . 1 1 5 5 ARG N N 15 132.201 0.20 . 1 . . . A 5 ARG N . 25289 1
31 . 1 1 5 5 ARG NE N 15 86.247 0.20 . 1 . . . A 5 ARG NE . 25289 1
32 . 1 1 6 6 HIS C C 13 171.847 0.20 . 1 . . . A 6 HIS C . 25289 1
33 . 1 1 6 6 HIS CA C 13 51.169 0.20 . 1 . . . A 6 HIS CA . 25289 1
34 . 1 1 6 6 HIS CB C 13 32.337 0.20 . 1 . . . A 6 HIS CB . 25289 1
35 . 1 1 6 6 HIS CG C 13 131.413 0.20 . 1 . . . A 6 HIS CG . 25289 1
36 . 1 1 6 6 HIS CD2 C 13 117.236 0.20 . 1 . . . A 6 HIS CD2 . 25289 1
37 . 1 1 6 6 HIS CE1 C 13 137.079 0.20 . 1 . . . A 6 HIS CE1 . 25289 1
38 . 1 1 6 6 HIS N N 15 126.106 0.20 . 1 . . . A 6 HIS N . 25289 1
39 . 1 1 6 6 HIS ND1 N 15 175.541 0.20 . 1 . . . A 6 HIS ND1 . 25289 1
40 . 1 1 6 6 HIS NE2 N 15 182.448 0.20 . 1 . . . A 6 HIS NE2 . 25289 1
41 . 1 1 7 7 ASP C C 13 173.950 0.20 . 1 . . . A 7 ASP C . 25289 1
42 . 1 1 7 7 ASP CA C 13 52.423 0.20 . 1 . . . A 7 ASP CA . 25289 1
43 . 1 1 7 7 ASP CB C 13 42.024 0.20 . 1 . . . A 7 ASP CB . 25289 1
44 . 1 1 7 7 ASP CG C 13 180.007 0.20 . 1 . . . A 7 ASP CG . 25289 1
45 . 1 1 7 7 ASP N N 15 129.834 0.20 . 1 . . . A 7 ASP N . 25289 1
46 . 1 1 8 8 SER C C 13 175.357 0.20 . 1 . . . A 8 SER C . 25289 1
47 . 1 1 8 8 SER CA C 13 55.033 0.20 . 1 . . . A 8 SER CA . 25289 1
48 . 1 1 8 8 SER CB C 13 66.184 0.20 . 1 . . . A 8 SER CB . 25289 1
49 . 1 1 8 8 SER N N 15 116.727 0.20 . 1 . . . A 8 SER N . 25289 1
50 . 1 1 9 9 GLY C C 13 173.834 0.20 . 1 . . . A 9 GLY C . 25289 1
51 . 1 1 9 9 GLY CA C 13 47.196 0.20 . 1 . . . A 9 GLY CA . 25289 1
52 . 1 1 9 9 GLY N N 15 112.188 0.20 . 1 . . . A 9 GLY N . 25289 1
53 . 1 1 10 10 TYR C C 13 172.647 0.20 . 1 . . . A 10 TYR C . 25289 1
54 . 1 1 10 10 TYR CA C 13 58.031 0.20 . 1 . . . A 10 TYR CA . 25289 1
55 . 1 1 10 10 TYR CB C 13 42.069 0.20 . 1 . . . A 10 TYR CB . 25289 1
56 . 1 1 10 10 TYR CD1 C 13 133.269 0.20 . 3 . . . A 10 TYR CD1 . 25289 1
57 . 1 1 10 10 TYR CE1 C 13 118.435 0.20 . 3 . . . A 10 TYR CE1 . 25289 1
58 . 1 1 10 10 TYR CZ C 13 156.561 0.20 . 1 . . . A 10 TYR CZ . 25289 1
59 . 1 1 10 10 TYR N N 15 126.552 0.20 . 1 . . . A 10 TYR N . 25289 1
60 . 1 1 11 11 GLU CA C 13 54.828 0.20 . 1 . . . A 11 GLU CA . 25289 1
61 . 1 1 11 11 GLU CB C 13 32.332 0.20 . 1 . . . A 11 GLU CB . 25289 1
62 . 1 1 11 11 GLU CG C 13 38.077 0.20 . 1 . . . A 11 GLU CG . 25289 1
63 . 1 1 11 11 GLU CD C 13 183.706 0.20 . 1 . . . A 11 GLU CD . 25289 1
64 . 1 1 11 11 GLU N N 15 130.897 0.20 . 1 . . . A 11 GLU N . 25289 1
65 . 1 1 12 12 VAL C C 13 175.777 0.20 . 1 . . . A 12 VAL C . 25289 1
66 . 1 1 12 12 VAL CA C 13 60.552 0.20 . 1 . . . A 12 VAL CA . 25289 1
67 . 1 1 12 12 VAL CB C 13 34.866 0.20 . 1 . . . A 12 VAL CB . 25289 1
68 . 1 1 12 12 VAL CG1 C 13 21.287 0.20 . 2 . . . A 12 VAL CG1 . 25289 1
69 . 1 1 12 12 VAL CG2 C 13 21.636 0.20 . 2 . . . A 12 VAL CG2 . 25289 1
70 . 1 1 12 12 VAL N N 15 126.150 0.20 . 1 . . . A 12 VAL N . 25289 1
71 . 1 1 13 13 HIS C C 13 173.570 0.20 . 1 . . . A 13 HIS C . 25289 1
72 . 1 1 13 13 HIS CA C 13 50.444 0.20 . 1 . . . A 13 HIS CA . 25289 1
73 . 1 1 13 13 HIS CB C 13 33.390 0.20 . 1 . . . A 13 HIS CB . 25289 1
74 . 1 1 13 13 HIS CG C 13 133.014 0.20 . 1 . . . A 13 HIS CG . 25289 1
75 . 1 1 13 13 HIS CD2 C 13 113.907 0.20 . 1 . . . A 13 HIS CD2 . 25289 1
76 . 1 1 13 13 HIS CE1 C 13 139.890 0.20 . 1 . . . A 13 HIS CE1 . 25289 1
77 . 1 1 13 13 HIS N N 15 125.956 0.20 . 1 . . . A 13 HIS N . 25289 1
78 . 1 1 13 13 HIS ND1 N 15 191.995 0.20 . 1 . . . A 13 HIS ND1 . 25289 1
79 . 1 1 13 13 HIS NE2 N 15 170.461 0.20 . 1 . . . A 13 HIS NE2 . 25289 1
80 . 1 1 14 14 HIS C C 13 173.557 0.20 . 1 . . . A 14 HIS C . 25289 1
81 . 1 1 14 14 HIS CA C 13 54.898 0.20 . 1 . . . A 14 HIS CA . 25289 1
82 . 1 1 14 14 HIS CB C 13 31.969 0.20 . 1 . . . A 14 HIS CB . 25289 1
83 . 1 1 14 14 HIS CG C 13 135.867 0.20 . 1 . . . A 14 HIS CG . 25289 1
84 . 1 1 14 14 HIS CD2 C 13 118.277 0.20 . 1 . . . A 14 HIS CD2 . 25289 1
85 . 1 1 14 14 HIS CE1 C 13 138.211 0.20 . 1 . . . A 14 HIS CE1 . 25289 1
86 . 1 1 14 14 HIS N N 15 118.068 0.20 . 1 . . . A 14 HIS N . 25289 1
87 . 1 1 15 15 GLN C C 13 175.161 0.20 . 1 . . . A 15 GLN C . 25289 1
88 . 1 1 15 15 GLN CA C 13 54.735 0.20 . 1 . . . A 15 GLN CA . 25289 1
89 . 1 1 15 15 GLN CB C 13 33.033 0.20 . 1 . . . A 15 GLN CB . 25289 1
90 . 1 1 15 15 GLN CG C 13 30.555 0.20 . 1 . . . A 15 GLN CG . 25289 1
91 . 1 1 15 15 GLN CD C 13 176.363 0.20 . 1 . . . A 15 GLN CD . 25289 1
92 . 1 1 15 15 GLN N N 15 108.832 0.20 . 1 . . . A 15 GLN N . 25289 1
93 . 1 1 15 15 GLN NE2 N 15 108.865 0.20 . 1 . . . A 15 GLN NE2 . 25289 1
94 . 1 1 16 16 LYS C C 13 174.135 0.20 . 1 . . . A 16 LYS C . 25289 1
95 . 1 1 16 16 LYS CA C 13 55.161 0.20 . 1 . . . A 16 LYS CA . 25289 1
96 . 1 1 16 16 LYS CB C 13 36.677 0.20 . 1 . . . A 16 LYS CB . 25289 1
97 . 1 1 16 16 LYS CG C 13 25.731 0.20 . 1 . . . A 16 LYS CG . 25289 1
98 . 1 1 16 16 LYS CD C 13 30.434 0.20 . 1 . . . A 16 LYS CD . 25289 1
99 . 1 1 16 16 LYS CE C 13 42.115 0.20 . 1 . . . A 16 LYS CE . 25289 1
100 . 1 1 16 16 LYS N N 15 120.134 0.20 . 1 . . . A 16 LYS N . 25289 1
101 . 1 1 16 16 LYS NZ N 15 34.330 0.20 . 1 . . . A 16 LYS NZ . 25289 1
102 . 1 1 17 17 LEU C C 13 174.949 0.20 . 1 . . . A 17 LEU C . 25289 1
103 . 1 1 17 17 LEU CA C 13 54.624 0.20 . 1 . . . A 17 LEU CA . 25289 1
104 . 1 1 17 17 LEU CB C 13 44.696 0.20 . 1 . . . A 17 LEU CB . 25289 1
105 . 1 1 17 17 LEU CG C 13 30.366 0.20 . 1 . . . A 17 LEU CG . 25289 1
106 . 1 1 17 17 LEU CD1 C 13 22.788 0.20 . 2 . . . A 17 LEU CD1 . 25289 1
107 . 1 1 17 17 LEU CD2 C 13 25.012 0.20 . 2 . . . A 17 LEU CD2 . 25289 1
108 . 1 1 17 17 LEU N N 15 128.053 0.20 . 1 . . . A 17 LEU N . 25289 1
109 . 1 1 18 18 VAL C C 13 172.776 0.20 . 1 . . . A 18 VAL C . 25289 1
110 . 1 1 18 18 VAL CA C 13 61.757 0.20 . 1 . . . A 18 VAL CA . 25289 1
111 . 1 1 18 18 VAL CB C 13 33.817 0.20 . 1 . . . A 18 VAL CB . 25289 1
112 . 1 1 18 18 VAL CG1 C 13 22.087 0.20 . 2 . . . A 18 VAL CG1 . 25289 1
113 . 1 1 18 18 VAL CG2 C 13 20.269 0.20 . 2 . . . A 18 VAL CG2 . 25289 1
114 . 1 1 18 18 VAL N N 15 123.642 0.20 . 1 . . . A 18 VAL N . 25289 1
115 . 1 1 19 19 PHE C C 13 174.192 0.20 . 1 . . . A 19 PHE C . 25289 1
116 . 1 1 19 19 PHE CA C 13 55.575 0.20 . 1 . . . A 19 PHE CA . 25289 1
117 . 1 1 19 19 PHE CB C 13 42.431 0.20 . 1 . . . A 19 PHE CB . 25289 1
118 . 1 1 19 19 PHE CG C 13 142.602 0.20 . 1 . . . A 19 PHE CG . 25289 1
119 . 1 1 19 19 PHE CD1 C 13 130.619 0.20 . 3 . . . A 19 PHE CD1 . 25289 1
120 . 1 1 19 19 PHE CE1 C 13 131.501 0.20 . 3 . . . A 19 PHE CE1 . 25289 1
121 . 1 1 19 19 PHE CZ C 13 128.881 0.20 . 1 . . . A 19 PHE CZ . 25289 1
122 . 1 1 19 19 PHE N N 15 129.487 0.20 . 1 . . . A 19 PHE N . 25289 1
123 . 1 1 20 20 PHE C C 13 170.932 0.20 . 1 . . . A 20 PHE C . 25289 1
124 . 1 1 20 20 PHE CA C 13 58.679 0.20 . 1 . . . A 20 PHE CA . 25289 1
125 . 1 1 20 20 PHE CB C 13 32.923 0.20 . 1 . . . A 20 PHE CB . 25289 1
126 . 1 1 20 20 PHE CG C 13 142.426 0.20 . 1 . . . A 20 PHE CG . 25289 1
127 . 1 1 20 20 PHE CD1 C 13 131.333 0.20 . 3 . . . A 20 PHE CD1 . 25289 1
128 . 1 1 20 20 PHE CE1 C 13 134.117 0.20 . 3 . . . A 20 PHE CE1 . 25289 1
129 . 1 1 20 20 PHE CZ C 13 129.282 0.20 . 1 . . . A 20 PHE CZ . 25289 1
130 . 1 1 20 20 PHE N N 15 117.543 0.20 . 1 . . . A 20 PHE N . 25289 1
131 . 1 1 21 21 ALA C C 13 177.230 0.20 . 1 . . . A 21 ALA C . 25289 1
132 . 1 1 21 21 ALA CA C 13 48.992 0.20 . 1 . . . A 21 ALA CA . 25289 1
133 . 1 1 21 21 ALA CB C 13 23.188 0.20 . 1 . . . A 21 ALA CB . 25289 1
134 . 1 1 21 21 ALA N N 15 115.079 0.20 . 1 . . . A 21 ALA N . 25289 1
135 . 1 1 22 22 ASP CA C 13 55.469 0.20 . 1 . . . A 22 ASP CA . 25289 1
136 . 1 1 22 22 ASP CB C 13 39.067 0.20 . 1 . . . A 22 ASP CB . 25289 1
137 . 1 1 22 22 ASP CG C 13 182.421 0.20 . 1 . . . A 22 ASP CG . 25289 1
138 . 1 1 22 22 ASP N N 15 118.083 0.20 . 1 . . . A 22 ASP N . 25289 1
139 . 1 1 23 23 VAL C C 13 177.102 0.20 . 1 . . . A 23 VAL C . 25289 1
140 . 1 1 23 23 VAL CA C 13 58.358 0.20 . 1 . . . A 23 VAL CA . 25289 1
141 . 1 1 23 23 VAL CB C 13 36.811 0.20 . 1 . . . A 23 VAL CB . 25289 1
142 . 1 1 23 23 VAL CG1 C 13 21.933 0.20 . 2 . . . A 23 VAL CG1 . 25289 1
143 . 1 1 23 23 VAL CG2 C 13 23.155 0.20 . 2 . . . A 23 VAL CG2 . 25289 1
144 . 1 1 23 23 VAL N N 15 118.167 0.20 . 1 . . . A 23 VAL N . 25289 1
145 . 1 1 24 24 GLY C C 13 175.652 0.20 . 1 . . . A 24 GLY C . 25289 1
146 . 1 1 24 24 GLY CA C 13 48.862 0.20 . 1 . . . A 24 GLY CA . 25289 1
147 . 1 1 24 24 GLY N N 15 116.706 0.20 . 1 . . . A 24 GLY N . 25289 1
148 . 1 1 25 25 SER C C 13 171.430 0.20 . 1 . . . A 25 SER C . 25289 1
149 . 1 1 25 25 SER CA C 13 57.801 0.20 . 1 . . . A 25 SER CA . 25289 1
150 . 1 1 25 25 SER CB C 13 66.227 0.20 . 1 . . . A 25 SER CB . 25289 1
151 . 1 1 25 25 SER N N 15 114.116 0.20 . 1 . . . A 25 SER N . 25289 1
152 . 1 1 26 26 ASN C C 13 174.397 0.20 . 1 . . . A 26 ASN C . 25289 1
153 . 1 1 26 26 ASN CA C 13 52.749 0.20 . 1 . . . A 26 ASN CA . 25289 1
154 . 1 1 26 26 ASN CB C 13 40.826 0.20 . 1 . . . A 26 ASN CB . 25289 1
155 . 1 1 26 26 ASN CG C 13 174.453 0.20 . 1 . . . A 26 ASN CG . 25289 1
156 . 1 1 26 26 ASN N N 15 124.399 0.20 . 1 . . . A 26 ASN N . 25289 1
157 . 1 1 26 26 ASN ND2 N 15 113.249 0.20 . 1 . . . A 26 ASN ND2 . 25289 1
158 . 1 1 27 27 LYS C C 13 174.254 0.20 . 1 . . . A 27 LYS C . 25289 1
159 . 1 1 27 27 LYS CA C 13 54.790 0.20 . 1 . . . A 27 LYS CA . 25289 1
160 . 1 1 27 27 LYS CB C 13 39.371 0.20 . 1 . . . A 27 LYS CB . 25289 1
161 . 1 1 27 27 LYS CG C 13 25.378 0.20 . 1 . . . A 27 LYS CG . 25289 1
162 . 1 1 27 27 LYS CD C 13 30.702 0.20 . 1 . . . A 27 LYS CD . 25289 1
163 . 1 1 27 27 LYS CE C 13 41.763 0.20 . 1 . . . A 27 LYS CE . 25289 1
164 . 1 1 27 27 LYS N N 15 119.929 0.20 . 1 . . . A 27 LYS N . 25289 1
165 . 1 1 27 27 LYS NZ N 15 34.346 0.20 . 1 . . . A 27 LYS NZ . 25289 1
166 . 1 1 28 28 GLY C C 13 170.924 0.20 . 1 . . . A 28 GLY C . 25289 1
167 . 1 1 28 28 GLY CA C 13 44.986 0.20 . 1 . . . A 28 GLY CA . 25289 1
168 . 1 1 28 28 GLY N N 15 110.364 0.20 . 1 . . . A 28 GLY N . 25289 1
169 . 1 1 29 29 ALA C C 13 174.741 0.20 . 1 . . . A 29 ALA C . 25289 1
170 . 1 1 29 29 ALA CA C 13 50.157 0.20 . 1 . . . A 29 ALA CA . 25289 1
171 . 1 1 29 29 ALA CB C 13 20.182 0.20 . 1 . . . A 29 ALA CB . 25289 1
172 . 1 1 29 29 ALA N N 15 131.126 0.20 . 1 . . . A 29 ALA N . 25289 1
173 . 1 1 30 30 ILE C C 13 174.412 0.20 . 1 . . . A 30 ILE C . 25289 1
174 . 1 1 30 30 ILE CA C 13 57.752 0.20 . 1 . . . A 30 ILE CA . 25289 1
175 . 1 1 30 30 ILE CB C 13 38.797 0.20 . 1 . . . A 30 ILE CB . 25289 1
176 . 1 1 30 30 ILE CG1 C 13 27.145 0.20 . 1 . . . A 30 ILE CG1 . 25289 1
177 . 1 1 30 30 ILE CG2 C 13 18.450 0.20 . 1 . . . A 30 ILE CG2 . 25289 1
178 . 1 1 30 30 ILE CD1 C 13 12.376 0.20 . 1 . . . A 30 ILE CD1 . 25289 1
179 . 1 1 30 30 ILE N N 15 124.057 0.20 . 1 . . . A 30 ILE N . 25289 1
180 . 1 1 31 31 ILE C C 13 175.726 0.20 . 1 . . . A 31 ILE C . 25289 1
181 . 1 1 31 31 ILE CA C 13 58.438 0.20 . 1 . . . A 31 ILE CA . 25289 1
182 . 1 1 31 31 ILE CB C 13 41.749 0.20 . 1 . . . A 31 ILE CB . 25289 1
183 . 1 1 31 31 ILE CG1 C 13 27.369 0.20 . 1 . . . A 31 ILE CG1 . 25289 1
184 . 1 1 31 31 ILE CG2 C 13 17.222 0.20 . 1 . . . A 31 ILE CG2 . 25289 1
185 . 1 1 31 31 ILE CD1 C 13 14.256 0.20 . 1 . . . A 31 ILE CD1 . 25289 1
186 . 1 1 31 31 ILE N N 15 125.346 0.20 . 1 . . . A 31 ILE N . 25289 1
187 . 1 1 32 32 GLY C C 13 171.545 0.20 . 1 . . . A 32 GLY C . 25289 1
188 . 1 1 32 32 GLY CA C 13 48.711 0.20 . 1 . . . A 32 GLY CA . 25289 1
189 . 1 1 32 32 GLY N N 15 114.247 0.20 . 1 . . . A 32 GLY N . 25289 1
190 . 1 1 33 33 LEU C C 13 173.806 0.20 . 1 . . . A 33 LEU C . 25289 1
191 . 1 1 33 33 LEU CA C 13 54.124 0.20 . 1 . . . A 33 LEU CA . 25289 1
192 . 1 1 33 33 LEU CB C 13 45.854 0.20 . 1 . . . A 33 LEU CB . 25289 1
193 . 1 1 33 33 LEU CG C 13 28.148 0.20 . 1 . . . A 33 LEU CG . 25289 1
194 . 1 1 33 33 LEU CD1 C 13 24.915 0.20 . 2 . . . A 33 LEU CD1 . 25289 1
195 . 1 1 33 33 LEU CD2 C 13 25.579 0.20 . 2 . . . A 33 LEU CD2 . 25289 1
196 . 1 1 33 33 LEU N N 15 125.458 0.20 . 1 . . . A 33 LEU N . 25289 1
197 . 1 1 34 34 MET C C 13 173.609 0.20 . 1 . . . A 34 MET C . 25289 1
198 . 1 1 34 34 MET CA C 13 53.644 0.20 . 1 . . . A 34 MET CA . 25289 1
199 . 1 1 34 34 MET CB C 13 37.230 0.20 . 1 . . . A 34 MET CB . 25289 1
200 . 1 1 34 34 MET CG C 13 32.208 0.20 . 1 . . . A 34 MET CG . 25289 1
201 . 1 1 34 34 MET CE C 13 18.522 0.20 . 1 . . . A 34 MET CE . 25289 1
202 . 1 1 34 34 MET N N 15 126.372 0.20 . 1 . . . A 34 MET N . 25289 1
203 . 1 1 35 35 VAL C C 13 176.204 0.20 . 1 . . . A 35 VAL C . 25289 1
204 . 1 1 35 35 VAL CA C 13 58.717 0.20 . 1 . . . A 35 VAL CA . 25289 1
205 . 1 1 35 35 VAL CB C 13 36.067 0.20 . 1 . . . A 35 VAL CB . 25289 1
206 . 1 1 35 35 VAL CG1 C 13 21.709 0.20 . 2 . . . A 35 VAL CG1 . 25289 1
207 . 1 1 35 35 VAL N N 15 125.387 0.20 . 1 . . . A 35 VAL N . 25289 1
208 . 1 1 36 36 GLY C C 13 173.838 0.20 . 1 . . . A 36 GLY C . 25289 1
209 . 1 1 36 36 GLY CA C 13 48.353 0.20 . 1 . . . A 36 GLY CA . 25289 1
210 . 1 1 36 36 GLY N N 15 117.182 0.20 . 1 . . . A 36 GLY N . 25289 1
211 . 1 1 37 37 GLY C C 13 169.824 0.20 . 1 . . . A 37 GLY C . 25289 1
212 . 1 1 37 37 GLY CA C 13 44.974 0.20 . 1 . . . A 37 GLY CA . 25289 1
213 . 1 1 37 37 GLY N N 15 105.656 0.20 . 1 . . . A 37 GLY N . 25289 1
214 . 1 1 38 38 VAL C C 13 172.917 0.20 . 1 . . . A 38 VAL C . 25289 1
215 . 1 1 38 38 VAL CA C 13 60.545 0.20 . 1 . . . A 38 VAL CA . 25289 1
216 . 1 1 38 38 VAL CB C 13 36.733 0.20 . 1 . . . A 38 VAL CB . 25289 1
217 . 1 1 38 38 VAL CG1 C 13 22.966 0.20 . 2 . . . A 38 VAL CG1 . 25289 1
218 . 1 1 38 38 VAL CG2 C 13 22.291 0.20 . 2 . . . A 38 VAL CG2 . 25289 1
219 . 1 1 38 38 VAL N N 15 118.585 0.20 . 1 . . . A 38 VAL N . 25289 1
220 . 1 1 39 39 VAL C C 13 179.187 0.20 . 1 . . . A 39 VAL C . 25289 1
221 . 1 1 39 39 VAL CA C 13 59.865 0.20 . 1 . . . A 39 VAL CA . 25289 1
222 . 1 1 39 39 VAL CB C 13 33.467 0.20 . 1 . . . A 39 VAL CB . 25289 1
223 . 1 1 39 39 VAL CG1 C 13 21.829 0.20 . 2 . . . A 39 VAL CG1 . 25289 1
224 . 1 1 39 39 VAL N N 15 128.178 0.20 . 1 . . . A 39 VAL N . 25289 1
stop_
save_
save_assigned_chemical_shift_uniform_13C
_Assigned_chem_shift_list.Sf_category assigned_chemical_shifts
_Assigned_chem_shift_list.Sf_framecode assigned_chemical_shift_uniform_13C
_Assigned_chem_shift_list.Entry_ID 25289
_Assigned_chem_shift_list.ID 2
_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 0.2
_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
3 'DARR 15 ms' . . . 25289 2
6 'DARR 400 ms' . . . 25289 2
8 'PAR 8 ms' . . . 25289 2
10 'CHHC 500 us' . . . 25289 2
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 1 1 ASP C C 13 173.631 0.20 . 1 . . . A 1 ASP C . 25289 2
2 . 1 1 1 1 ASP CA C 13 54.171 0.20 . 1 . . . A 1 ASP CA . 25289 2
3 . 1 1 1 1 ASP CB C 13 40.992 0.20 . 1 . . . A 1 ASP CB . 25289 2
4 . 1 1 1 1 ASP CG C 13 179.634 0.20 . 1 . . . A 1 ASP CG . 25289 2
5 . 1 1 2 2 ALA C C 13 177.746 0.20 . 1 . . . A 2 ALA C . 25289 2
6 . 1 1 2 2 ALA CA C 13 51.922 0.20 . 1 . . . A 2 ALA CA . 25289 2
7 . 1 1 2 2 ALA CB C 13 15.681 0.20 . 1 . . . A 2 ALA CB . 25289 2
8 . 1 1 3 3 GLU C C 13 176.745 0.20 . 1 . . . A 3 GLU C . 25289 2
9 . 1 1 3 3 GLU CA C 13 62.552 0.20 . 1 . . . A 3 GLU CA . 25289 2
10 . 1 1 3 3 GLU CB C 13 29.718 0.20 . 1 . . . A 3 GLU CB . 25289 2
11 . 1 1 3 3 GLU CG C 13 38.967 0.20 . 1 . . . A 3 GLU CG . 25289 2
12 . 1 1 3 3 GLU CD C 13 183.703 0.20 . 1 . . . A 3 GLU CD . 25289 2
13 . 1 1 4 4 PHE C C 13 176.035 0.20 . 1 . . . A 4 PHE C . 25289 2
14 . 1 1 4 4 PHE CA C 13 58.038 0.20 . 1 . . . A 4 PHE CA . 25289 2
15 . 1 1 4 4 PHE CB C 13 41.672 0.20 . 1 . . . A 4 PHE CB . 25289 2
16 . 1 1 4 4 PHE CG C 13 137.781 0.20 . 1 . . . A 4 PHE CG . 25289 2
17 . 1 1 4 4 PHE CD1 C 13 133.253 0.20 . 3 . . . A 4 PHE CD1 . 25289 2
18 . 1 1 4 4 PHE CE1 C 13 131.573 0.20 . 3 . . . A 4 PHE CE1 . 25289 2
19 . 1 1 4 4 PHE CZ C 13 128.584 0.20 . 1 . . . A 4 PHE CZ . 25289 2
20 . 1 1 5 5 ARG C C 13 173.397 0.20 . 1 . . . A 5 ARG C . 25289 2
21 . 1 1 5 5 ARG CA C 13 54.679 0.20 . 1 . . . A 5 ARG CA . 25289 2
22 . 1 1 5 5 ARG CB C 13 33.762 0.20 . 1 . . . A 5 ARG CB . 25289 2
23 . 1 1 5 5 ARG CG C 13 27.320 0.20 . 1 . . . A 5 ARG CG . 25289 2
24 . 1 1 5 5 ARG CD C 13 43.841 0.20 . 1 . . . A 5 ARG CD . 25289 2
25 . 1 1 5 5 ARG CZ C 13 159.588 0.20 . 1 . . . A 5 ARG CZ . 25289 2
26 . 1 1 6 6 HIS C C 13 171.874 0.20 . 1 . . . A 6 HIS C . 25289 2
27 . 1 1 6 6 HIS CA C 13 51.166 0.20 . 1 . . . A 6 HIS CA . 25289 2
28 . 1 1 6 6 HIS CB C 13 32.330 0.20 . 1 . . . A 6 HIS CB . 25289 2
29 . 1 1 6 6 HIS CG C 13 131.242 0.20 . 1 . . . A 6 HIS CG . 25289 2
30 . 1 1 6 6 HIS CD2 C 13 117.407 0.20 . 1 . . . A 6 HIS CD2 . 25289 2
31 . 1 1 6 6 HIS CE1 C 13 137.350 0.20 . 1 . . . A 6 HIS CE1 . 25289 2
32 . 1 1 7 7 ASP C C 13 173.858 0.20 . 1 . . . A 7 ASP C . 25289 2
33 . 1 1 7 7 ASP CA C 13 52.555 0.20 . 1 . . . A 7 ASP CA . 25289 2
34 . 1 1 7 7 ASP CB C 13 42.074 0.20 . 1 . . . A 7 ASP CB . 25289 2
35 . 1 1 7 7 ASP CG C 13 180.099 0.20 . 1 . . . A 7 ASP CG . 25289 2
36 . 1 1 8 8 SER C C 13 175.425 0.20 . 1 . . . A 8 SER C . 25289 2
37 . 1 1 8 8 SER CA C 13 55.135 0.20 . 1 . . . A 8 SER CA . 25289 2
38 . 1 1 8 8 SER CB C 13 66.211 0.20 . 1 . . . A 8 SER CB . 25289 2
39 . 1 1 9 9 GLY C C 13 173.792 0.20 . 1 . . . A 9 GLY C . 25289 2
40 . 1 1 9 9 GLY CA C 13 47.190 0.20 . 1 . . . A 9 GLY CA . 25289 2
41 . 1 1 10 10 TYR C C 13 172.773 0.20 . 1 . . . A 10 TYR C . 25289 2
42 . 1 1 10 10 TYR CA C 13 58.114 0.20 . 1 . . . A 10 TYR CA . 25289 2
43 . 1 1 10 10 TYR CB C 13 42.089 0.20 . 1 . . . A 10 TYR CB . 25289 2
44 . 1 1 10 10 TYR CG C 13 128.426 0.20 . 1 . . . A 10 TYR CG . 25289 2
45 . 1 1 10 10 TYR CD1 C 13 133.238 0.20 . 3 . . . A 10 TYR CD1 . 25289 2
46 . 1 1 10 10 TYR CE1 C 13 118.511 0.20 . 3 . . . A 10 TYR CE1 . 25289 2
47 . 1 1 10 10 TYR CZ C 13 156.538 0.20 . 1 . . . A 10 TYR CZ . 25289 2
48 . 1 1 11 11 GLU C C 13 173.432 0.20 . 1 . . . A 11 GLU C . 25289 2
49 . 1 1 11 11 GLU CA C 13 54.816 0.20 . 1 . . . A 11 GLU CA . 25289 2
50 . 1 1 11 11 GLU CB C 13 32.367 0.20 . 1 . . . A 11 GLU CB . 25289 2
51 . 1 1 11 11 GLU CG C 13 38.072 0.20 . 1 . . . A 11 GLU CG . 25289 2
52 . 1 1 11 11 GLU CD C 13 183.723 0.20 . 1 . . . A 11 GLU CD . 25289 2
53 . 1 1 12 12 VAL C C 13 175.822 0.20 . 1 . . . A 12 VAL C . 25289 2
54 . 1 1 12 12 VAL CA C 13 60.564 0.20 . 1 . . . A 12 VAL CA . 25289 2
55 . 1 1 12 12 VAL CB C 13 34.924 0.20 . 1 . . . A 12 VAL CB . 25289 2
56 . 1 1 12 12 VAL CG1 C 13 21.331 0.20 . 2 . . . A 12 VAL CG1 . 25289 2
57 . 1 1 13 13 HIS C C 13 173.620 0.20 . 1 . . . A 13 HIS C . 25289 2
58 . 1 1 13 13 HIS CA C 13 50.401 0.20 . 1 . . . A 13 HIS CA . 25289 2
59 . 1 1 13 13 HIS CB C 13 33.381 0.20 . 1 . . . A 13 HIS CB . 25289 2
60 . 1 1 13 13 HIS CG C 13 132.978 0.20 . 1 . . . A 13 HIS CG . 25289 2
61 . 1 1 13 13 HIS CD2 C 13 113.942 0.20 . 1 . . . A 13 HIS CD2 . 25289 2
62 . 1 1 13 13 HIS CE1 C 13 139.841 0.20 . 1 . . . A 13 HIS CE1 . 25289 2
63 . 1 1 14 14 HIS C C 13 173.528 0.20 . 1 . . . A 14 HIS C . 25289 2
64 . 1 1 14 14 HIS CA C 13 54.915 0.20 . 1 . . . A 14 HIS CA . 25289 2
65 . 1 1 14 14 HIS CB C 13 31.919 0.20 . 1 . . . A 14 HIS CB . 25289 2
66 . 1 1 14 14 HIS CG C 13 135.568 0.20 . 1 . . . A 14 HIS CG . 25289 2
67 . 1 1 14 14 HIS CD2 C 13 118.611 0.20 . 1 . . . A 14 HIS CD2 . 25289 2
68 . 1 1 14 14 HIS CE1 C 13 138.347 0.20 . 1 . . . A 14 HIS CE1 . 25289 2
69 . 1 1 15 15 GLN C C 13 175.127 0.20 . 1 . . . A 15 GLN C . 25289 2
70 . 1 1 15 15 GLN CA C 13 54.693 0.20 . 1 . . . A 15 GLN CA . 25289 2
71 . 1 1 15 15 GLN CB C 13 33.038 0.20 . 1 . . . A 15 GLN CB . 25289 2
72 . 1 1 15 15 GLN CG C 13 30.554 0.20 . 1 . . . A 15 GLN CG . 25289 2
73 . 1 1 15 15 GLN CD C 13 176.448 0.20 . 1 . . . A 15 GLN CD . 25289 2
74 . 1 1 16 16 LYS C C 13 174.242 0.20 . 1 . . . A 16 LYS C . 25289 2
75 . 1 1 16 16 LYS CA C 13 55.183 0.20 . 1 . . . A 16 LYS CA . 25289 2
76 . 1 1 16 16 LYS CB C 13 36.663 0.20 . 1 . . . A 16 LYS CB . 25289 2
77 . 1 1 16 16 LYS CG C 13 25.750 0.20 . 1 . . . A 16 LYS CG . 25289 2
78 . 1 1 16 16 LYS CD C 13 30.228 0.20 . 1 . . . A 16 LYS CD . 25289 2
79 . 1 1 16 16 LYS CE C 13 42.000 0.20 . 1 . . . A 16 LYS CE . 25289 2
80 . 1 1 17 17 LEU C C 13 174.992 0.20 . 1 . . . A 17 LEU C . 25289 2
81 . 1 1 17 17 LEU CA C 13 54.585 0.20 . 1 . . . A 17 LEU CA . 25289 2
82 . 1 1 17 17 LEU CB C 13 44.687 0.20 . 1 . . . A 17 LEU CB . 25289 2
83 . 1 1 17 17 LEU CG C 13 30.333 0.20 . 1 . . . A 17 LEU CG . 25289 2
84 . 1 1 17 17 LEU CD1 C 13 22.817 0.20 . 2 . . . A 17 LEU CD1 . 25289 2
85 . 1 1 17 17 LEU CD2 C 13 25.049 0.20 . 2 . . . A 17 LEU CD2 . 25289 2
86 . 1 1 18 18 VAL C C 13 172.891 0.20 . 1 . . . A 18 VAL C . 25289 2
87 . 1 1 18 18 VAL CA C 13 61.826 0.20 . 1 . . . A 18 VAL CA . 25289 2
88 . 1 1 18 18 VAL CB C 13 33.830 0.20 . 1 . . . A 18 VAL CB . 25289 2
89 . 1 1 18 18 VAL CG1 C 13 22.111 0.20 . 2 . . . A 18 VAL CG1 . 25289 2
90 . 1 1 18 18 VAL CG2 C 13 20.208 0.20 . 2 . . . A 18 VAL CG2 . 25289 2
91 . 1 1 19 19 PHE C C 13 174.272 0.20 . 1 . . . A 19 PHE C . 25289 2
92 . 1 1 19 19 PHE CA C 13 55.581 0.20 . 1 . . . A 19 PHE CA . 25289 2
93 . 1 1 19 19 PHE CB C 13 42.475 0.20 . 1 . . . A 19 PHE CB . 25289 2
94 . 1 1 19 19 PHE CG C 13 142.752 0.20 . 1 . . . A 19 PHE CG . 25289 2
95 . 1 1 19 19 PHE CD1 C 13 130.619 0.20 . 3 . . . A 19 PHE CD1 . 25289 2
96 . 1 1 19 19 PHE CE1 C 13 131.445 0.20 . 3 . . . A 19 PHE CE1 . 25289 2
97 . 1 1 19 19 PHE CZ C 13 128.858 0.20 . 1 . . . A 19 PHE CZ . 25289 2
98 . 1 1 20 20 PHE C C 13 171.025 0.20 . 1 . . . A 20 PHE C . 25289 2
99 . 1 1 20 20 PHE CA C 13 58.689 0.20 . 1 . . . A 20 PHE CA . 25289 2
100 . 1 1 20 20 PHE CB C 13 32.976 0.20 . 1 . . . A 20 PHE CB . 25289 2
101 . 1 1 20 20 PHE CG C 13 142.475 0.20 . 1 . . . A 20 PHE CG . 25289 2
102 . 1 1 20 20 PHE CD1 C 13 131.528 0.20 . 3 . . . A 20 PHE CD1 . 25289 2
103 . 1 1 20 20 PHE CE1 C 13 134.073 0.20 . 3 . . . A 20 PHE CE1 . 25289 2
104 . 1 1 20 20 PHE CZ C 13 129.236 0.20 . 1 . . . A 20 PHE CZ . 25289 2
105 . 1 1 21 21 ALA C C 13 177.234 0.20 . 1 . . . A 21 ALA C . 25289 2
106 . 1 1 21 21 ALA CA C 13 49.067 0.20 . 1 . . . A 21 ALA CA . 25289 2
107 . 1 1 21 21 ALA CB C 13 23.224 0.20 . 1 . . . A 21 ALA CB . 25289 2
108 . 1 1 22 22 ASP C C 13 174.335 0.20 . 1 . . . A 22 ASP C . 25289 2
109 . 1 1 22 22 ASP CA C 13 55.335 0.20 . 1 . . . A 22 ASP CA . 25289 2
110 . 1 1 22 22 ASP CB C 13 38.744 0.20 . 1 . . . A 22 ASP CB . 25289 2
111 . 1 1 22 22 ASP CG C 13 182.076 0.20 . 1 . . . A 22 ASP CG . 25289 2
112 . 1 1 23 23 VAL C C 13 177.082 0.20 . 1 . . . A 23 VAL C . 25289 2
113 . 1 1 23 23 VAL CA C 13 58.390 0.20 . 1 . . . A 23 VAL CA . 25289 2
114 . 1 1 23 23 VAL CB C 13 36.941 0.20 . 1 . . . A 23 VAL CB . 25289 2
115 . 1 1 23 23 VAL CG1 C 13 21.997 0.20 . 2 . . . A 23 VAL CG1 . 25289 2
116 . 1 1 23 23 VAL CG2 C 13 23.103 0.20 . 2 . . . A 23 VAL CG2 . 25289 2
117 . 1 1 24 24 GLY C C 13 175.476 0.20 . 1 . . . A 24 GLY C . 25289 2
118 . 1 1 24 24 GLY CA C 13 48.889 0.20 . 1 . . . A 24 GLY CA . 25289 2
119 . 1 1 25 25 SER C C 13 171.562 0.20 . 1 . . . A 25 SER C . 25289 2
120 . 1 1 25 25 SER CA C 13 57.842 0.20 . 1 . . . A 25 SER CA . 25289 2
121 . 1 1 25 25 SER CB C 13 66.249 0.20 . 1 . . . A 25 SER CB . 25289 2
122 . 1 1 26 26 ASN C C 13 174.457 0.20 . 1 . . . A 26 ASN C . 25289 2
123 . 1 1 26 26 ASN CA C 13 52.691 0.20 . 1 . . . A 26 ASN CA . 25289 2
124 . 1 1 26 26 ASN CB C 13 40.755 0.20 . 1 . . . A 26 ASN CB . 25289 2
125 . 1 1 26 26 ASN CG C 13 174.453 0.20 . 1 . . . A 26 ASN CG . 25289 2
126 . 1 1 27 27 LYS C C 13 174.290 0.20 . 1 . . . A 27 LYS C . 25289 2
127 . 1 1 27 27 LYS CA C 13 54.794 0.20 . 1 . . . A 27 LYS CA . 25289 2
128 . 1 1 27 27 LYS CB C 13 39.374 0.20 . 1 . . . A 27 LYS CB . 25289 2
129 . 1 1 27 27 LYS CG C 13 25.319 0.20 . 1 . . . A 27 LYS CG . 25289 2
130 . 1 1 27 27 LYS CD C 13 30.728 0.20 . 1 . . . A 27 LYS CD . 25289 2
131 . 1 1 27 27 LYS CE C 13 41.764 0.20 . 1 . . . A 27 LYS CE . 25289 2
132 . 1 1 28 28 GLY C C 13 170.707 0.20 . 1 . . . A 28 GLY C . 25289 2
133 . 1 1 28 28 GLY CA C 13 45.121 0.20 . 1 . . . A 28 GLY CA . 25289 2
134 . 1 1 29 29 ALA C C 13 174.306 0.20 . 1 . . . A 29 ALA C . 25289 2
135 . 1 1 29 29 ALA CA C 13 49.957 0.20 . 1 . . . A 29 ALA CA . 25289 2
136 . 1 1 29 29 ALA CB C 13 21.242 0.20 . 1 . . . A 29 ALA CB . 25289 2
137 . 1 1 30 30 ILE C C 13 174.786 0.20 . 1 . . . A 30 ILE C . 25289 2
138 . 1 1 30 30 ILE CA C 13 57.811 0.20 . 1 . . . A 30 ILE CA . 25289 2
139 . 1 1 30 30 ILE CB C 13 40.838 0.20 . 1 . . . A 30 ILE CB . 25289 2
140 . 1 1 30 30 ILE CG1 C 13 27.083 0.20 . 1 . . . A 30 ILE CG1 . 25289 2
141 . 1 1 30 30 ILE CG2 C 13 18.222 0.20 . 1 . . . A 30 ILE CG2 . 25289 2
142 . 1 1 30 30 ILE CD1 C 13 13.351 0.20 . 1 . . . A 30 ILE CD1 . 25289 2
143 . 1 1 31 31 ILE C C 13 176.149 0.20 . 1 . . . A 31 ILE C . 25289 2
144 . 1 1 31 31 ILE CA C 13 57.982 0.20 . 1 . . . A 31 ILE CA . 25289 2
145 . 1 1 31 31 ILE CB C 13 41.665 0.20 . 1 . . . A 31 ILE CB . 25289 2
146 . 1 1 31 31 ILE CG1 C 13 27.099 0.20 . 1 . . . A 31 ILE CG1 . 25289 2
147 . 1 1 31 31 ILE CG2 C 13 17.276 0.20 . 1 . . . A 31 ILE CG2 . 25289 2
148 . 1 1 31 31 ILE CD1 C 13 14.826 0.20 . 1 . . . A 31 ILE CD1 . 25289 2
149 . 1 1 32 32 GLY C C 13 171.818 0.20 . 1 . . . A 32 GLY C . 25289 2
150 . 1 1 32 32 GLY CA C 13 48.834 0.20 . 1 . . . A 32 GLY CA . 25289 2
151 . 1 1 33 33 LEU C C 13 173.617 0.20 . 1 . . . A 33 LEU C . 25289 2
152 . 1 1 33 33 LEU CA C 13 54.171 0.20 . 1 . . . A 33 LEU CA . 25289 2
153 . 1 1 33 33 LEU CB C 13 45.938 0.20 . 1 . . . A 33 LEU CB . 25289 2
154 . 1 1 33 33 LEU CG C 13 28.143 0.20 . 1 . . . A 33 LEU CG . 25289 2
155 . 1 1 33 33 LEU CD1 C 13 24.916 0.20 . 2 . . . A 33 LEU CD1 . 25289 2
156 . 1 1 33 33 LEU CD2 C 13 25.627 0.20 . 2 . . . A 33 LEU CD2 . 25289 2
157 . 1 1 34 34 MET C C 13 173.585 0.20 . 1 . . . A 34 MET C . 25289 2
158 . 1 1 34 34 MET CA C 13 53.826 0.20 . 1 . . . A 34 MET CA . 25289 2
159 . 1 1 34 34 MET CB C 13 37.292 0.20 . 1 . . . A 34 MET CB . 25289 2
160 . 1 1 34 34 MET CG C 13 32.466 0.20 . 1 . . . A 34 MET CG . 25289 2
161 . 1 1 34 34 MET CE C 13 18.732 0.20 . 1 . . . A 34 MET CE . 25289 2
162 . 1 1 35 35 VAL C C 13 176.295 0.20 . 1 . . . A 35 VAL C . 25289 2
163 . 1 1 35 35 VAL CA C 13 58.815 0.20 . 1 . . . A 35 VAL CA . 25289 2
164 . 1 1 35 35 VAL CB C 13 36.143 0.20 . 1 . . . A 35 VAL CB . 25289 2
165 . 1 1 35 35 VAL CG1 C 13 21.738 0.20 . 2 . . . A 35 VAL CG1 . 25289 2
166 . 1 1 36 36 GLY C C 13 174.029 0.20 . 1 . . . A 36 GLY C . 25289 2
167 . 1 1 36 36 GLY CA C 13 48.373 0.20 . 1 . . . A 36 GLY CA . 25289 2
168 . 1 1 37 37 GLY C C 13 169.855 0.20 . 1 . . . A 37 GLY C . 25289 2
169 . 1 1 37 37 GLY CA C 13 45.057 0.20 . 1 . . . A 37 GLY CA . 25289 2
170 . 1 1 38 38 VAL C C 13 173.131 0.20 . 1 . . . A 38 VAL C . 25289 2
171 . 1 1 38 38 VAL CA C 13 60.589 0.20 . 1 . . . A 38 VAL CA . 25289 2
172 . 1 1 38 38 VAL CB C 13 36.787 0.20 . 1 . . . A 38 VAL CB . 25289 2
173 . 1 1 38 38 VAL CG1 C 13 22.781 0.20 . 2 . . . A 38 VAL CG1 . 25289 2
174 . 1 1 38 38 VAL CG2 C 13 22.493 0.20 . 2 . . . A 38 VAL CG2 . 25289 2
175 . 1 1 39 39 VAL C C 13 179.129 0.20 . 1 . . . A 39 VAL C . 25289 2
176 . 1 1 39 39 VAL CA C 13 59.835 0.20 . 1 . . . A 39 VAL CA . 25289 2
177 . 1 1 39 39 VAL CB C 13 33.404 0.20 . 1 . . . A 39 VAL CB . 25289 2
178 . 1 1 39 39 VAL CG1 C 13 21.948 0.20 . 2 . . . A 39 VAL CG1 . 25289 2
stop_
save_
save_assigned_chemical_shift_2-13C-glucose
_Assigned_chem_shift_list.Sf_category assigned_chemical_shifts
_Assigned_chem_shift_list.Sf_framecode assigned_chemical_shift_2-13C-glucose
_Assigned_chem_shift_list.Entry_ID 25289
_Assigned_chem_shift_list.ID 3
_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 0.2
_Assigned_chem_shift_list.Chem_shift_15N_err 0.2
_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
12 'PDSD 4 s' . . . 25289 3
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 1 1 ASP C C 13 173.491 0.20 . 1 . . . A 1 ASP C . 25289 3
2 . 1 1 1 1 ASP CA C 13 54.092 0.20 . 1 . . . A 1 ASP CA . 25289 3
3 . 1 1 1 1 ASP CB C 13 40.984 0.20 . 1 . . . A 1 ASP CB . 25289 3
4 . 1 1 1 1 ASP CG C 13 179.402 0.20 . 1 . . . A 1 ASP CG . 25289 3
5 . 1 1 1 1 ASP N N 15 36.933 0.20 . 1 . . . A 1 ASP N . 25289 3
6 . 1 1 2 2 ALA CA C 13 51.921 0.20 . 1 . . . A 2 ALA CA . 25289 3
7 . 1 1 2 2 ALA N N 15 117.772 0.20 . 1 . . . A 2 ALA N . 25289 3
8 . 1 1 3 3 GLU C C 13 176.478 0.20 . 1 . . . A 3 GLU C . 25289 3
9 . 1 1 3 3 GLU CA C 13 62.518 0.20 . 1 . . . A 3 GLU CA . 25289 3
10 . 1 1 3 3 GLU CB C 13 29.578 0.20 . 1 . . . A 3 GLU CB . 25289 3
11 . 1 1 3 3 GLU CD C 13 183.579 0.20 . 1 . . . A 3 GLU CD . 25289 3
12 . 1 1 3 3 GLU N N 15 121.758 0.20 . 1 . . . A 3 GLU N . 25289 3
13 . 1 1 4 4 PHE C C 13 175.844 0.20 . 1 . . . A 4 PHE C . 25289 3
14 . 1 1 4 4 PHE CA C 13 58.035 0.20 . 1 . . . A 4 PHE CA . 25289 3
15 . 1 1 4 4 PHE CB C 13 41.712 0.20 . 1 . . . A 4 PHE CB . 25289 3
16 . 1 1 4 4 PHE CG C 13 137.149 0.20 . 1 . . . A 4 PHE CG . 25289 3
17 . 1 1 4 4 PHE CD1 C 13 133.015 0.20 . 3 . . . A 4 PHE CD1 . 25289 3
18 . 1 1 4 4 PHE CE1 C 13 132.106 0.20 . 3 . . . A 4 PHE CE1 . 25289 3
19 . 1 1 4 4 PHE CZ C 13 129.133 0.20 . 1 . . . A 4 PHE CZ . 25289 3
20 . 1 1 4 4 PHE N N 15 114.612 0.20 . 1 . . . A 4 PHE N . 25289 3
21 . 1 1 5 5 ARG C C 13 173.144 0.20 . 1 . . . A 5 ARG C . 25289 3
22 . 1 1 5 5 ARG CA C 13 54.569 0.20 . 1 . . . A 5 ARG CA . 25289 3
23 . 1 1 5 5 ARG CB C 13 33.604 0.20 . 1 . . . A 5 ARG CB . 25289 3
24 . 1 1 5 5 ARG CG C 13 27.443 0.20 . 1 . . . A 5 ARG CG . 25289 3
25 . 1 1 5 5 ARG CD C 13 43.646 0.20 . 1 . . . A 5 ARG CD . 25289 3
26 . 1 1 5 5 ARG N N 15 132.057 0.20 . 1 . . . A 5 ARG N . 25289 3
27 . 1 1 6 6 HIS CA C 13 51.156 0.20 . 1 . . . A 6 HIS CA . 25289 3
28 . 1 1 6 6 HIS CB C 13 32.343 0.20 . 1 . . . A 6 HIS CB . 25289 3
29 . 1 1 6 6 HIS CG C 13 131.164 0.20 . 1 . . . A 6 HIS CG . 25289 3
30 . 1 1 6 6 HIS CD2 C 13 117.231 0.20 . 1 . . . A 6 HIS CD2 . 25289 3
31 . 1 1 6 6 HIS CE1 C 13 137.067 0.20 . 1 . . . A 6 HIS CE1 . 25289 3
32 . 1 1 6 6 HIS N N 15 125.775 0.20 . 1 . . . A 6 HIS N . 25289 3
33 . 1 1 6 6 HIS ND1 N 15 181.912 0.20 . 1 . . . A 6 HIS ND1 . 25289 3
34 . 1 1 7 7 ASP C C 13 173.860 0.20 . 1 . . . A 7 ASP C . 25289 3
35 . 1 1 7 7 ASP CA C 13 52.525 0.20 . 1 . . . A 7 ASP CA . 25289 3
36 . 1 1 7 7 ASP N N 15 129.788 0.20 . 1 . . . A 7 ASP N . 25289 3
37 . 1 1 8 8 SER CA C 13 55.122 0.20 . 1 . . . A 8 SER CA . 25289 3
38 . 1 1 8 8 SER N N 15 116.505 0.20 . 1 . . . A 8 SER N . 25289 3
39 . 1 1 9 9 GLY C C 13 173.781 0.20 . 1 . . . A 9 GLY C . 25289 3
40 . 1 1 9 9 GLY CA C 13 47.253 0.20 . 1 . . . A 9 GLY CA . 25289 3
41 . 1 1 9 9 GLY N N 15 111.731 0.20 . 1 . . . A 9 GLY N . 25289 3
42 . 1 1 10 10 TYR CA C 13 58.068 0.20 . 1 . . . A 10 TYR CA . 25289 3
43 . 1 1 11 11 GLU CD C 13 183.541 0.20 . 1 . . . A 11 GLU CD . 25289 3
44 . 1 1 12 12 VAL C C 13 176.263 0.20 . 1 . . . A 12 VAL C . 25289 3
45 . 1 1 12 12 VAL CA C 13 60.535 0.20 . 1 . . . A 12 VAL CA . 25289 3
46 . 1 1 12 12 VAL CB C 13 34.863 0.20 . 1 . . . A 12 VAL CB . 25289 3
47 . 1 1 12 12 VAL N N 15 125.989 0.20 . 1 . . . A 12 VAL N . 25289 3
48 . 1 1 13 13 HIS CA C 13 50.399 0.20 . 1 . . . A 13 HIS CA . 25289 3
49 . 1 1 13 13 HIS CG C 13 132.808 0.20 . 1 . . . A 13 HIS CG . 25289 3
50 . 1 1 13 13 HIS CD2 C 13 113.890 0.20 . 1 . . . A 13 HIS CD2 . 25289 3
51 . 1 1 13 13 HIS CE1 C 13 139.721 0.20 . 1 . . . A 13 HIS CE1 . 25289 3
52 . 1 1 13 13 HIS N N 15 125.789 0.20 . 1 . . . A 13 HIS N . 25289 3
53 . 1 1 13 13 HIS ND1 N 15 191.224 0.20 . 1 . . . A 13 HIS ND1 . 25289 3
54 . 1 1 13 13 HIS NE2 N 15 170.128 0.20 . 1 . . . A 13 HIS NE2 . 25289 3
55 . 1 1 14 14 HIS CA C 13 54.927 0.20 . 1 . . . A 14 HIS CA . 25289 3
56 . 1 1 14 14 HIS CG C 13 135.875 0.20 . 1 . . . A 14 HIS CG . 25289 3
57 . 1 1 14 14 HIS CE1 C 13 138.006 0.20 . 1 . . . A 14 HIS CE1 . 25289 3
58 . 1 1 14 14 HIS N N 15 118.026 0.20 . 1 . . . A 14 HIS N . 25289 3
59 . 1 1 15 15 GLN CA C 13 54.770 0.20 . 1 . . . A 15 GLN CA . 25289 3
60 . 1 1 15 15 GLN CB C 13 33.077 0.20 . 1 . . . A 15 GLN CB . 25289 3
61 . 1 1 15 15 GLN CG C 13 30.410 0.20 . 1 . . . A 15 GLN CG . 25289 3
62 . 1 1 15 15 GLN CD C 13 176.309 0.20 . 1 . . . A 15 GLN CD . 25289 3
63 . 1 1 15 15 GLN N N 15 108.924 0.20 . 1 . . . A 15 GLN N . 25289 3
64 . 1 1 15 15 GLN NE2 N 15 108.571 0.20 . 1 . . . A 15 GLN NE2 . 25289 3
65 . 1 1 16 16 LYS C C 13 173.925 0.20 . 1 . . . A 16 LYS C . 25289 3
66 . 1 1 16 16 LYS CA C 13 55.140 0.20 . 1 . . . A 16 LYS CA . 25289 3
67 . 1 1 16 16 LYS CB C 13 36.672 0.20 . 1 . . . A 16 LYS CB . 25289 3
68 . 1 1 16 16 LYS CG C 13 25.817 0.20 . 1 . . . A 16 LYS CG . 25289 3
69 . 1 1 16 16 LYS CE C 13 42.101 0.20 . 1 . . . A 16 LYS CE . 25289 3
70 . 1 1 16 16 LYS N N 15 119.524 0.20 . 1 . . . A 16 LYS N . 25289 3
71 . 1 1 16 16 LYS NZ N 15 33.385 0.20 . 1 . . . A 16 LYS NZ . 25289 3
72 . 1 1 17 17 LEU C C 13 174.899 0.20 . 1 . . . A 17 LEU C . 25289 3
73 . 1 1 17 17 LEU CA C 13 54.471 0.20 . 1 . . . A 17 LEU CA . 25289 3
74 . 1 1 17 17 LEU CB C 13 44.654 0.20 . 1 . . . A 17 LEU CB . 25289 3
75 . 1 1 17 17 LEU CG C 13 30.412 0.20 . 1 . . . A 17 LEU CG . 25289 3
76 . 1 1 17 17 LEU CD1 C 13 24.987 0.20 . 2 . . . A 17 LEU CD1 . 25289 3
77 . 1 1 17 17 LEU N N 15 127.791 0.20 . 1 . . . A 17 LEU N . 25289 3
78 . 1 1 18 18 VAL C C 13 172.704 0.20 . 1 . . . A 18 VAL C . 25289 3
79 . 1 1 18 18 VAL CA C 13 61.741 0.20 . 1 . . . A 18 VAL CA . 25289 3
80 . 1 1 18 18 VAL CB C 13 33.885 0.20 . 1 . . . A 18 VAL CB . 25289 3
81 . 1 1 18 18 VAL N N 15 123.123 0.20 . 1 . . . A 18 VAL N . 25289 3
82 . 1 1 19 19 PHE C C 13 174.296 0.20 . 1 . . . A 19 PHE C . 25289 3
83 . 1 1 19 19 PHE CA C 13 55.556 0.20 . 1 . . . A 19 PHE CA . 25289 3
84 . 1 1 19 19 PHE CG C 13 142.561 0.20 . 1 . . . A 19 PHE CG . 25289 3
85 . 1 1 19 19 PHE N N 15 129.279 0.20 . 1 . . . A 19 PHE N . 25289 3
86 . 1 1 20 20 PHE CA C 13 58.692 0.20 . 1 . . . A 20 PHE CA . 25289 3
87 . 1 1 20 20 PHE CG C 13 142.304 0.20 . 1 . . . A 20 PHE CG . 25289 3
88 . 1 1 20 20 PHE CD1 C 13 131.752 0.20 . 3 . . . A 20 PHE CD1 . 25289 3
89 . 1 1 20 20 PHE CD2 C 13 131.870 0.20 . 3 . . . A 20 PHE CD2 . 25289 3
90 . 1 1 20 20 PHE CZ C 13 129.180 0.20 . 1 . . . A 20 PHE CZ . 25289 3
91 . 1 1 20 20 PHE N N 15 117.565 0.20 . 1 . . . A 20 PHE N . 25289 3
92 . 1 1 21 21 ALA CA C 13 48.935 0.20 . 1 . . . A 21 ALA CA . 25289 3
93 . 1 1 21 21 ALA N N 15 114.797 0.20 . 1 . . . A 21 ALA N . 25289 3
94 . 1 1 23 23 VAL CA C 13 58.370 0.20 . 1 . . . A 23 VAL CA . 25289 3
95 . 1 1 23 23 VAL CB C 13 36.845 0.20 . 1 . . . A 23 VAL CB . 25289 3
96 . 1 1 23 23 VAL N N 15 118.036 0.20 . 1 . . . A 23 VAL N . 25289 3
97 . 1 1 24 24 GLY C C 13 175.720 0.20 . 1 . . . A 24 GLY C . 25289 3
98 . 1 1 24 24 GLY CA C 13 48.897 0.20 . 1 . . . A 24 GLY CA . 25289 3
99 . 1 1 24 24 GLY N N 15 116.516 0.20 . 1 . . . A 24 GLY N . 25289 3
100 . 1 1 25 25 SER CA C 13 57.815 0.20 . 1 . . . A 25 SER CA . 25289 3
101 . 1 1 25 25 SER N N 15 113.850 0.20 . 1 . . . A 25 SER N . 25289 3
102 . 1 1 26 26 ASN C C 13 174.303 0.20 . 1 . . . A 26 ASN C . 25289 3
103 . 1 1 26 26 ASN CA C 13 52.712 0.20 . 1 . . . A 26 ASN CA . 25289 3
104 . 1 1 26 26 ASN CB C 13 40.725 0.20 . 1 . . . A 26 ASN CB . 25289 3
105 . 1 1 26 26 ASN CG C 13 174.159 0.20 . 1 . . . A 26 ASN CG . 25289 3
106 . 1 1 26 26 ASN N N 15 124.195 0.20 . 1 . . . A 26 ASN N . 25289 3
107 . 1 1 26 26 ASN ND2 N 15 112.972 0.20 . 1 . . . A 26 ASN ND2 . 25289 3
108 . 1 1 27 27 LYS C C 13 174.333 0.20 . 1 . . . A 27 LYS C . 25289 3
109 . 1 1 27 27 LYS CA C 13 54.781 0.20 . 1 . . . A 27 LYS CA . 25289 3
110 . 1 1 27 27 LYS CB C 13 39.365 0.20 . 1 . . . A 27 LYS CB . 25289 3
111 . 1 1 27 27 LYS CG C 13 25.323 0.20 . 1 . . . A 27 LYS CG . 25289 3
112 . 1 1 27 27 LYS CE C 13 41.676 0.20 . 1 . . . A 27 LYS CE . 25289 3
113 . 1 1 27 27 LYS N N 15 119.572 0.20 . 1 . . . A 27 LYS N . 25289 3
114 . 1 1 27 27 LYS NZ N 15 33.768 0.20 . 1 . . . A 27 LYS NZ . 25289 3
115 . 1 1 28 28 GLY C C 13 170.751 0.20 . 1 . . . A 28 GLY C . 25289 3
116 . 1 1 28 28 GLY CA C 13 45.086 0.20 . 1 . . . A 28 GLY CA . 25289 3
117 . 1 1 28 28 GLY N N 15 110.001 0.20 . 1 . . . A 28 GLY N . 25289 3
118 . 1 1 29 29 ALA CA C 13 50.064 0.20 . 1 . . . A 29 ALA CA . 25289 3
119 . 1 1 29 29 ALA N N 15 131.032 0.20 . 1 . . . A 29 ALA N . 25289 3
120 . 1 1 30 30 ILE C C 13 174.388 0.20 . 1 . . . A 30 ILE C . 25289 3
121 . 1 1 30 30 ILE CA C 13 57.734 0.20 . 1 . . . A 30 ILE CA . 25289 3
122 . 1 1 30 30 ILE CD1 C 13 12.703 0.20 . 1 . . . A 30 ILE CD1 . 25289 3
123 . 1 1 30 30 ILE N N 15 123.344 0.20 . 1 . . . A 30 ILE N . 25289 3
124 . 1 1 31 31 ILE C C 13 175.833 0.20 . 1 . . . A 31 ILE C . 25289 3
125 . 1 1 31 31 ILE CA C 13 58.152 0.20 . 1 . . . A 31 ILE CA . 25289 3
126 . 1 1 31 31 ILE CB C 13 41.730 0.20 . 1 . . . A 31 ILE CB . 25289 3
127 . 1 1 31 31 ILE CG1 C 13 27.163 0.20 . 1 . . . A 31 ILE CG1 . 25289 3
128 . 1 1 31 31 ILE CG2 C 13 17.180 0.20 . 1 . . . A 31 ILE CG2 . 25289 3
129 . 1 1 31 31 ILE CD1 C 13 14.274 0.20 . 1 . . . A 31 ILE CD1 . 25289 3
130 . 1 1 31 31 ILE N N 15 124.839 0.20 . 1 . . . A 31 ILE N . 25289 3
131 . 1 1 32 32 GLY C C 13 171.518 0.20 . 1 . . . A 32 GLY C . 25289 3
132 . 1 1 32 32 GLY CA C 13 48.750 0.20 . 1 . . . A 32 GLY CA . 25289 3
133 . 1 1 32 32 GLY N N 15 113.865 0.20 . 1 . . . A 32 GLY N . 25289 3
134 . 1 1 33 33 LEU C C 13 173.634 0.20 . 1 . . . A 33 LEU C . 25289 3
135 . 1 1 33 33 LEU CA C 13 54.140 0.20 . 1 . . . A 33 LEU CA . 25289 3
136 . 1 1 33 33 LEU CB C 13 45.841 0.20 . 1 . . . A 33 LEU CB . 25289 3
137 . 1 1 33 33 LEU CG C 13 28.153 0.20 . 1 . . . A 33 LEU CG . 25289 3
138 . 1 1 33 33 LEU CD1 C 13 24.873 0.20 . 2 . . . A 33 LEU CD1 . 25289 3
139 . 1 1 33 33 LEU CD2 C 13 25.534 0.20 . 2 . . . A 33 LEU CD2 . 25289 3
140 . 1 1 33 33 LEU N N 15 125.287 0.20 . 1 . . . A 33 LEU N . 25289 3
141 . 1 1 34 34 MET C C 13 173.567 0.20 . 1 . . . A 34 MET C . 25289 3
142 . 1 1 34 34 MET CA C 13 53.659 0.20 . 1 . . . A 34 MET CA . 25289 3
143 . 1 1 34 34 MET CB C 13 37.251 0.20 . 1 . . . A 34 MET CB . 25289 3
144 . 1 1 34 34 MET CG C 13 32.448 0.20 . 1 . . . A 34 MET CG . 25289 3
145 . 1 1 34 34 MET CE C 13 18.523 0.20 . 1 . . . A 34 MET CE . 25289 3
146 . 1 1 34 34 MET N N 15 126.605 0.20 . 1 . . . A 34 MET N . 25289 3
147 . 1 1 35 35 VAL C C 13 176.291 0.20 . 1 . . . A 35 VAL C . 25289 3
148 . 1 1 35 35 VAL CA C 13 58.731 0.20 . 1 . . . A 35 VAL CA . 25289 3
149 . 1 1 35 35 VAL CB C 13 36.095 0.20 . 1 . . . A 35 VAL CB . 25289 3
150 . 1 1 35 35 VAL CG1 C 13 21.661 0.20 . 2 . . . A 35 VAL CG1 . 25289 3
151 . 1 1 35 35 VAL N N 15 125.094 0.20 . 1 . . . A 35 VAL N . 25289 3
152 . 1 1 36 36 GLY C C 13 173.978 0.20 . 1 . . . A 36 GLY C . 25289 3
153 . 1 1 36 36 GLY CA C 13 48.367 0.20 . 1 . . . A 36 GLY CA . 25289 3
154 . 1 1 36 36 GLY N N 15 117.127 0.20 . 1 . . . A 36 GLY N . 25289 3
155 . 1 1 37 37 GLY C C 13 169.671 0.20 . 1 . . . A 37 GLY C . 25289 3
156 . 1 1 37 37 GLY CA C 13 44.978 0.20 . 1 . . . A 37 GLY CA . 25289 3
157 . 1 1 37 37 GLY N N 15 105.300 0.20 . 1 . . . A 37 GLY N . 25289 3
158 . 1 1 38 38 VAL C C 13 173.132 0.20 . 1 . . . A 38 VAL C . 25289 3
159 . 1 1 38 38 VAL CA C 13 60.610 0.20 . 1 . . . A 38 VAL CA . 25289 3
160 . 1 1 38 38 VAL CB C 13 36.694 0.20 . 1 . . . A 38 VAL CB . 25289 3
161 . 1 1 38 38 VAL CG1 C 13 22.864 0.20 . 2 . . . A 38 VAL CG1 . 25289 3
162 . 1 1 38 38 VAL N N 15 118.391 0.20 . 1 . . . A 38 VAL N . 25289 3
163 . 1 1 39 39 VAL CA C 13 59.881 0.20 . 1 . . . A 39 VAL CA . 25289 3
164 . 1 1 39 39 VAL CB C 13 33.436 0.20 . 1 . . . A 39 VAL CB . 25289 3
165 . 1 1 39 39 VAL CG1 C 13 21.817 0.20 . 2 . . . A 39 VAL CG1 . 25289 3
166 . 1 1 39 39 VAL N N 15 127.547 0.20 . 1 . . . A 39 VAL N . 25289 3
stop_
save_