data_5101
#######################
# Entry information #
#######################
save_entry_information
_Entry.Sf_category entry_information
_Entry.Sf_framecode entry_information
_Entry.ID 5101
_Entry.Title
;
Structure and Properties of a Dimeric N-terminal Fragment of Human Ubiquitin
;
_Entry.Type macromolecule
_Entry.Version_type original
_Entry.Submission_date 2001-08-06
_Entry.Accession_date 2001-08-06
_Entry.Last_release_date 2002-01-25
_Entry.Original_release_date 2002-01-25
_Entry.Origination author
_Entry.NMR_STAR_version 3.1.1.61
_Entry.Original_NMR_STAR_version 2.1
_Entry.Experimental_method NMR
_Entry.Experimental_method_subtype .
_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 David Bolton . . . 5101
2 Philip Evans . A. . 5101
3 Katherine Stott . . . 5101
4 Richard Broadhurst . W. . 5101
stop_
loop_
_Data_set.Type
_Data_set.Count
_Data_set.Entry_ID
assigned_chemical_shifts 1 5101
stop_
loop_
_Datum.Type
_Datum.Count
_Datum.Entry_ID
'1H chemical shifts' 390 5101
'13C chemical shifts' 174 5101
'15N chemical shifts' 49 5101
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 . . 2002-01-25 2001-08-06 original author . 5101
stop_
save_
###############
# Citations #
###############
save_entry_citation
_Citation.Sf_category citations
_Citation.Sf_framecode entry_citation
_Citation.Entry_ID 5101
_Citation.ID 1
_Citation.Class 'entry citation'
_Citation.CAS_abstract_code .
_Citation.MEDLINE_UI_code 21592562
_Citation.DOI .
_Citation.PubMed_ID 117733996
_Citation.Full_citation .
_Citation.Title 'Structure and Properties of a Dimeric N-terminal Fragment of Human Ubiquitin'
_Citation.Status published
_Citation.Type journal
_Citation.Journal_abbrev 'J. Mol. Biol.'
_Citation.Journal_name_full .
_Citation.Journal_volume 314
_Citation.Journal_issue 4
_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 773
_Citation.Page_last 787
_Citation.Year 2001
_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 David Bolton . . . 5101 1
2 Philip Evans . A. . 5101 1
3 Katherine Stott . . . 5101 1
4 Richard Broadhurst . W. . 5101 1
stop_
loop_
_Citation_keyword.Keyword
_Citation_keyword.Entry_ID
_Citation_keyword.Citation_ID
ubiquitin 5101 1
dimer 5101 1
'protein dissection' 5101 1
'structural specificity' 5101 1
'NMR spectroscopy' 5101 1
stop_
save_
#############################################
# Molecular system (assembly) description #
#############################################
save_system_UQ(1-51)
_Assembly.Sf_category assembly
_Assembly.Sf_framecode system_UQ(1-51)
_Assembly.Entry_ID 5101
_Assembly.ID 1
_Assembly.Name 'ubiquitin fragment'
_Assembly.BMRB_code .
_Assembly.Number_of_components .
_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 'not present'
_Assembly.Molecular_mass .
_Assembly.Enzyme_commission_number .
_Assembly.Details .
_Assembly.DB_query_date .
_Assembly.DB_query_revised_last_date .
loop_
_Assembly_type.Type
_Assembly_type.Entry_ID
_Assembly_type.Assembly_ID
dimer 5101 1
stop_
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 'uq1_51 subunit A' 1 $uq1_51 . . . native . . 1 . . 5101 1
2 'uq1_51 subunit B' 1 $uq1_51 . . . native . . 1 . . 5101 1
stop_
loop_
_Assembly_common_name.Name
_Assembly_common_name.Type
_Assembly_common_name.Entry_ID
_Assembly_common_name.Assembly_ID
'ubiquitin fragment' system 5101 1
UQ(1-51) abbreviation 5101 1
stop_
save_
####################################
# Biological polymers and ligands #
####################################
save_uq1_51
_Entity.Sf_category entity
_Entity.Sf_framecode uq1_51
_Entity.Entry_ID 5101
_Entity.ID 1
_Entity.BMRB_code .
_Entity.Name Ubiquitin
_Entity.Type polymer
_Entity.Polymer_common_type .
_Entity.Polymer_type polypeptide(L)
_Entity.Polymer_type_details .
_Entity.Polymer_strand_ID .
_Entity.Polymer_seq_one_letter_code_can .
_Entity.Polymer_seq_one_letter_code
;
GSMQIFVKTLTGKTITLEVE
PSDTIENVKAKIQDKEGIPP
DQQRLIFAGKQLE
;
_Entity.Target_identifier .
_Entity.Polymer_author_defined_seq .
_Entity.Polymer_author_seq_details .
_Entity.Ambiguous_conformational_states .
_Entity.Ambiguous_chem_comp_sites .
_Entity.Nstd_monomer .
_Entity.Nstd_chirality .
_Entity.Nstd_linkage .
_Entity.Nonpolymer_comp_ID .
_Entity.Nonpolymer_comp_label .
_Entity.Number_of_monomers 53
_Entity.Number_of_nonpolymer_components .
_Entity.Paramagnetic .
_Entity.Thiol_state 'not present'
_Entity.Src_method .
_Entity.Parent_entity_ID .
_Entity.Fragment .
_Entity.Mutation .
_Entity.EC_number .
_Entity.Calc_isoelectric_point .
_Entity.Formula_weight .
_Entity.Formula_weight_exptl .
_Entity.Formula_weight_exptl_meth .
_Entity.Details .
_Entity.DB_query_date .
_Entity.DB_query_revised_last_date 2015-01-28
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 11505 . entity . . . . . 96.23 76 98.04 98.04 6.84e-26 . . . . 5101 1
2 no BMRB 11547 . ubiquitin . . . . . 96.23 76 98.04 98.04 6.84e-26 . . . . 5101 1
3 no BMRB 15047 . denatured_ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
4 no BMRB 15410 . Ubi . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
5 no BMRB 15689 . UBB . . . . . 100.00 103 100.00 100.00 7.26e-28 . . . . 5101 1
6 no BMRB 15866 . ubiquitin . . . . . 96.23 76 100.00 100.00 1.27e-26 . . . . 5101 1
7 no BMRB 15907 . Ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
8 no BMRB 16228 . ubiquitin . . . . . 96.23 76 98.04 98.04 1.31e-25 . . . . 5101 1
9 no BMRB 16582 . Ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
10 no BMRB 16626 . Ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
11 no BMRB 16763 . ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
12 no BMRB 16880 . Ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
13 no BMRB 16885 . Ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
14 no BMRB 16895 . UBB+1 . . . . . 100.00 103 100.00 100.00 7.26e-28 . . . . 5101 1
15 no BMRB 17059 . ubiquitin . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1
16 no BMRB 17181 . ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
17 no BMRB 17239 . ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
18 no BMRB 17333 . UB . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
19 no BMRB 17439 . ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
20 no BMRB 17769 . Ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
21 no BMRB 17919 . entity . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
22 no BMRB 18582 . ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
23 no BMRB 18583 . ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
24 no BMRB 18584 . ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
25 no BMRB 18610 . Ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
26 no BMRB 18611 . Ubiquitin_A_state . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
27 no BMRB 18737 . UBIQUITIN . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
28 no BMRB 19394 . ubiquitin . . . . . 98.11 79 98.08 98.08 1.27e-26 . . . . 5101 1
29 no BMRB 19399 . Ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
30 no BMRB 19406 . entity . . . . . 96.23 152 100.00 100.00 1.06e-25 . . . . 5101 1
31 no BMRB 19412 . entity . . . . . 96.23 152 100.00 100.00 1.06e-25 . . . . 5101 1
32 no BMRB 19447 . Ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
33 no BMRB 25070 . Ubiquitin . . . . . 98.11 79 98.08 98.08 1.27e-26 . . . . 5101 1
34 no BMRB 25230 . Ubiquitin . . . . . 98.11 78 98.08 98.08 1.13e-26 . . . . 5101 1
35 no BMRB 4245 . ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
36 no BMRB 4375 . Ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
37 no BMRB 5387 . ubq . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
38 no BMRB 6457 . Ub . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
39 no BMRB 6466 . Ub . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
40 no BMRB 6470 . Ub . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
41 no BMRB 6488 . Ub . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
42 no BMRB 68 . ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
43 no BMRB 7111 . human_ubiquitin . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
44 no PDB 1AAR . "Structure Of A Diubiquitin Conjugate And A Model For Interaction With Ubiquitin Conjugating Enzyme (E2)" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
45 no PDB 1CMX . "Structural Basis For The Specificity Of Ubiquitin C- Terminal Hydrolases" . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1
46 no PDB 1D3Z . "Ubiquitin Nmr Structure" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
47 no PDB 1F9J . "Structure Of A New Crystal Form Of Tetraubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
48 no PDB 1FXT . "Structure Of A Conjugating Enzyme-Ubiquitin Thiolester Complex" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
49 no PDB 1G6J . "Structure Of Recombinant Human Ubiquitin In Aot Reverse Micelles" . . . . . 94.34 76 100.00 100.00 1.52e-25 . . . . 5101 1
50 no PDB 1GJZ . "Solution Structure Of A Dimeric N-Terminal Fragment Of Human Ubiquitin" . . . . . 100.00 53 100.00 100.00 4.76e-28 . . . . 5101 1
51 no PDB 1NBF . "Crystal Structure Of A Ubp-Family Deubiquitinating Enzyme In Isolation And In Complex With Ubiquitin Aldehyde" . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1
52 no PDB 1OGW . "Synthetic Ubiquitin With Fluoro-Leu At 50 And 67" . . . . . 96.23 76 98.04 98.04 1.01e-25 . . . . 5101 1
53 no PDB 1P3Q . "Mechanism Of Ubiquitin Recognition By The Cue Domain Of Vps9" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
54 no PDB 1Q5W . "Ubiquitin Recognition By Npl4 Zinc-Fingers" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
55 no PDB 1S1Q . "Tsg101(Uev) Domain In Complex With Ubiquitin" . . . . . 94.34 76 100.00 100.00 1.52e-25 . . . . 5101 1
56 no PDB 1TBE . "Structure Of Tetraubiquitin Shows How Multiubiquitin Chains Can Be Formed" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
57 no PDB 1UBI . "Synthetic Structural And Biological Studies Of The Ubiquitin System. Part 1" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
58 no PDB 1UBQ . "Structure Of Ubiquitin Refined At 1.8 Angstroms Resolution" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
59 no PDB 1UZX . "A Complex Of The Vps23 Uev With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
60 no PDB 1V80 . "Solution Structures Of Ubiquitin At 30 Bar And 3 Kbar" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
61 no PDB 1V81 . "Solution Structures Of Ubiquitin At 30 Bar And 3 Kbar" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
62 no PDB 1VX7 . "Cryo-em Structure Of The Plasmodium Falciparum 80s Ribosome Bound To The Anti-protozoan Drug Emetine, Large Subunit (protein On" . . . . . 96.23 128 98.04 100.00 5.03e-26 . . . . 5101 1
63 no PDB 1WR6 . "Crystal Structure Of Gga3 Gat Domain In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
64 no PDB 1WRD . "Crystal Structure Of Tom1 Gat Domain In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
65 no PDB 1XD3 . "Crystal Structure Of Uchl3-Ubvme Complex" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1
66 no PDB 1XQQ . "Simultaneous Determination Of Protein Structure And Dynamics" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
67 no PDB 1YD8 . "Complex Of Human Gga3 Gat Domain And Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
68 no PDB 1YIW . "X-Ray Crystal Structure Of A Chemically Synthesized Ubiquitin" . . . . . 96.23 76 98.04 100.00 5.57e-26 . . . . 5101 1
69 no PDB 1YX5 . "Solution Structure Of S5a Uim-1UBIQUITIN COMPLEX" . . . . . 96.23 98 100.00 100.00 4.75e-27 . . . . 5101 1
70 no PDB 1YX6 . "Solution Structure Of S5a Uim-2UBIQUITIN COMPLEX" . . . . . 96.23 98 100.00 100.00 4.75e-27 . . . . 5101 1
71 no PDB 1ZGU . "Solution Structure Of The Human Mms2-Ubiquitin Complex" . . . . . 96.23 76 98.04 100.00 2.70e-26 . . . . 5101 1
72 no PDB 2AYO . "Structure Of Usp14 Bound To Ubquitin Aldehyde" . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1
73 no PDB 2BGF . "Nmr Structure Of Lys48-Linked Di-Ubiquitin Using Chemical Shift Perturbation Data Together With Rdcs And 15n- Relaxation Data" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
74 no PDB 2C7M . "Human Rabex-5 Residues 1-74 In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
75 no PDB 2C7N . "Human Rabex-5 Residues 1-74 In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
76 no PDB 2D3G . "Double Sided Ubiquitin Binding Of Hrs-Uim" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
77 no PDB 2DEN . "Solution Structure Of The Ubiquitin-Associated Domain Of Human Bmsc-Ubp And Its Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
78 no PDB 2DX5 . "The Complex Structure Between The Mouse Eap45-Glue Domain And Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
79 no PDB 2FCQ . "X-Ray Crystal Structure Of A Chemically Synthesized Ubiquitin With A Cubic Space Group" . . . . . 96.23 76 98.04 100.00 5.57e-26 . . . . 5101 1
80 no PDB 2FID . "Crystal Structure Of A Bovine Rabex-5 Fragment Complexed With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
81 no PDB 2FIF . "Crystal Structure Of A Bovine Rabex-5 Fragment Complexed With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
82 no PDB 2FUH . "Solution Structure Of The Ubch5cUB NON-Covalent Complex" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
83 no PDB 2G45 . "Co-Crystal Structure Of Znf Ubp Domain From The Deubiquitinating Enzyme Isopeptidase T (Isot) In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
84 no PDB 2GMI . Mms2UBC13~UBIQUITIN . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
85 no PDB 2HD5 . "Usp2 In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
86 no PDB 2HTH . "Structural Basis For Ubiquitin Recognition By The Human Eap45ESCRT-Ii Glue Domain" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
87 no PDB 2IBI . "Covalent Ubiquitin-Usp2 Complex" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1
88 no PDB 2J7Q . "Crystal Structure Of The Ubiquitin-Specific Protease Encoded By Murine Cytomegalovirus Tegument Protein M48 In Complex With A U" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1
89 no PDB 2JF5 . "Crystal Structure Of Lys63-Linked Di-Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
90 no PDB 2JRI . "Solution Structure Of The Josephin Domain Of Ataxin-3 In Complex With Ubiquitin Molecule." . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
91 no PDB 2JY6 . "Solution Structure Of The Complex Of Ubiquitin And Ubiquilin 1 Uba Domain" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
92 no PDB 2JZZ . "Solid-State Nmr Structure Of Microcrystalline Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
93 no PDB 2K25 . "Automated Nmr Structure Of The Ubb By Fapsy" . . . . . 100.00 103 100.00 100.00 7.26e-28 . . . . 5101 1
94 no PDB 2K39 . "Recognition Dynamics Up To Microseconds Revealed From Rdc Derived Ubiquitin Ensemble In Solution" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
95 no PDB 2K6D . "Cin85 Sh3-C Domain In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.27e-26 . . . . 5101 1
96 no PDB 2K8B . "Solution Structure Of Plaa Family Ubiquitin Binding Domain (Pfuc) Cis Isomer In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
97 no PDB 2K8C . "Solution Structure Of Plaa Family Ubiquitin Binding Domain (Pfuc) Trans Isomer In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
98 no PDB 2KDE . "Nmr Structure Of Major S5a (196-306):k48 Linked Diubiquitin Species" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
99 no PDB 2KDF . "Nmr Structure Of Minor S5a (196-306):k48 Linked Diubiquitin Species" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
100 no PDB 2KHW . "Solution Structure Of The Human Polymerase Iota Ubm2- Ubiquitin Complex" . . . . . 98.11 79 98.08 98.08 1.27e-26 . . . . 5101 1
101 no PDB 2KJH . "Nmr Based Structural Model Of The Ubch8-Ubiquitin Complex" . . . . . 96.23 76 100.00 100.00 1.27e-26 . . . . 5101 1
102 no PDB 2KLG . "Pere Nmr Structure Of Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
103 no PDB 2KN5 . "A Correspondence Between Solution-State Dynamics Of An Individual Protein And The Sequence And Conformational Diversity Of Its " . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
104 no PDB 2KOX . "Nmr Residual Dipolar Couplings Identify Long Range Correlated Motions In The Backbone Of The Protein Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
105 no PDB 2KTF . "Solution Nmr Structure Of Human Polymerase Iota Ubm2 In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
106 no PDB 2KWU . "Solution Structure Of Ubm2 Of Murine Polymerase Iota In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
107 no PDB 2KWV . "Solution Structure Of Ubm1 Of Murine Polymerase Iota In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
108 no PDB 2KX0 . "The Solution Structure Of Ubb+1, Frameshift Mutant Of Ubiquitin B" . . . . . 100.00 103 100.00 100.00 7.26e-28 . . . . 5101 1
109 no PDB 2L0F . "Solution Nmr Structure Of Human Polymerase Iota Ubm2 (P692a Mutant) In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
110 no PDB 2L0T . "Solution Structure Of The Complex Of Ubiquitin And The Vhs Domain Of Stam2" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
111 no PDB 2L3Z . "Proton-Detected 4d Dream Solid-State Nmr Structure Of Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
112 no PDB 2LD9 . "Backbone Structure Of Ubiquitin Determined Using Backbone Amide Noes And Backbone N-H And N-C Rdcs" . . . . . 96.23 77 100.00 100.00 1.56e-26 . . . . 5101 1
113 no PDB 2LJ5 . "Description Of The Structural Fluctuations Of Proteins From Structure- Based Calculations Of Residual Dipolar Couplings" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
114 no PDB 2LVO . "Structure Of The Gp78cue Domain Bound To Monubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
115 no PDB 2LVP . "Gp78cue Domain Bound To The Distal Ubiquitin Of K48-Linked Diubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
116 no PDB 2LVQ . "Gp78cue Domain Bound To The Proximal Ubiquitin Of K48-Linked Diubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
117 no PDB 2LZ6 . "Distinct Ubiquitin Binding Modes Exhibited By Sh3 Domains: Molecular Determinants And Functional Implications" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
118 no PDB 2MBB . "Solution Structure Of The Human Polymerase Iota Ubm1-ubiquitin Complex" . . . . . 98.11 78 98.08 98.08 1.13e-26 . . . . 5101 1
119 no PDB 2MBH . "Nmr Structure Of Eklf(22-40)/ubiquitin Complex" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
120 no PDB 2MBO . "K11-linked Diubiquitin Average Solution Structure At Ph 6.8, 0 Mm Nacl" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
121 no PDB 2MBQ . "K11-linked Diubiquitin Average Solution Structure At Ph 6.8, 150 Mm Nacl" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
122 no PDB 2MCN . "Distinct Ubiquitin Binding Modes Exhibited By Sh3 Domains: Molecular Determinants And Functional Implications" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
123 no PDB 2MJ5 . "Structure Of The Uba Domain Of Human Nbr1 In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
124 no PDB 2MJB . "Solution Nmr Structure Of Ubiquitin Refined Against Dipolar Couplings In 4 Media" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
125 no PDB 2MOR . "A Tensor-free Method For The Structural And Dynamical Refinement Of Proteins Using Residual Dipolar Couplings" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
126 no PDB 2MRE . "Nmr Structure Of The Rad18-ubz/ubiquitin Complex" . . . . . 98.11 79 98.08 98.08 1.27e-26 . . . . 5101 1
127 no PDB 2MUR . "Solution Structure Of The Human Faap20 Ubz-ubiquitin Complex" . . . . . 98.11 78 98.08 98.08 1.13e-26 . . . . 5101 1
128 no PDB 2NR2 . "The Mumo (Minimal Under-Restraining Minimal Over- Restraining) Method For The Determination Of Native States Ensembles Of Prote" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
129 no PDB 2O6V . "Crystal Structure And Solution Nmr Studies Of Lys48-Linked Tetraubiquitin At Neutral Ph" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
130 no PDB 2OJR . "Structure Of Ubiquitin Solved By Sad Using The Lanthanide- Binding Tag" . . . . . 98.11 111 98.08 100.00 2.03e-26 . . . . 5101 1
131 no PDB 2OOB . "Crystal Structure Of The Uba Domain From Cbl-B Ubiquitin Ligase In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
132 no PDB 2PE9 . "Nmr Based Structure Of The Open Conformation Of Lys48- Linked Di-Ubiquitin Using Experimental Global Rotational Diffusion Tenso" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
133 no PDB 2PEA . "Nmr Based Structure Of The Closed Conformation Of Lys48- Linked Di-Ubiquitin Using Experimental Global Rotational Diffusion Ten" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
134 no PDB 2QHO . "Crystal Structure Of The Uba Domain From Edd Ubiquitin Ligase In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
135 no PDB 2RR9 . "The Solution Structure Of The K63-Ub2:tuims Complex" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
136 no PDB 2RSU . "Alternative Structure Of Ubiquitin" . . . . . 96.23 76 98.04 98.04 6.84e-26 . . . . 5101 1
137 no PDB 2RU6 . "The Pure Alternative State Of Ubiquitin" . . . . . 96.23 76 98.04 98.04 6.84e-26 . . . . 5101 1
138 no PDB 2W9N . "Crystal Structure Of Linear Di-Ubiquitin" . . . . . 94.34 152 100.00 100.00 9.10e-25 . . . . 5101 1
139 no PDB 2WDT . "Crystal Structure Of Plasmodium Falciparum Uchl3 In Complex With The Suicide Inhibitor Ubvme" . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1
140 no PDB 2WWZ . "Tab2 Nzf Domain In Complex With Lys63-Linked Di-Ubiquitin, P212121" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
141 no PDB 2WX0 . "Tab2 Nzf Domain In Complex With Lys63-Linked Di-Ubiquitin, P21" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
142 no PDB 2WX1 . "Tab2 Nzf Domain In Complex With Lys63-Linked Tri-Ubiquitin, P212121" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
143 no PDB 2XBB . "Nedd4 Hect:ub Complex" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
144 no PDB 2XEW . "Crystal Structure Of K11-Linked Diubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
145 no PDB 2XK5 . "Crystal Structure Of K6-Linked Diubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
146 no PDB 2Y5B . "Structure Of Usp21 In Complex With Linear Diubiquitin-Aldehyde" . . . . . 96.23 152 100.00 100.00 8.44e-26 . . . . 5101 1
147 no PDB 2Z59 . "Complex Structures Of Mouse Rpn13 (22-130aa) And Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
148 no PDB 2ZCC . "Ubiquitin Crystallized Under High Pressure" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
149 no PDB 2ZNV . "Crystal Structure Of Human Amsh-Lp Dub Domain In Complex With Lys63-Linked Ubiquitin Dimer" . . . . . 96.23 76 100.00 100.00 1.39e-26 . . . . 5101 1
150 no PDB 2ZVN . "Nemo Cozi Domain Incomplex With Diubiquitin In P212121 Space Group" . . . . . 100.00 154 98.11 98.11 1.39e-26 . . . . 5101 1
151 no PDB 2ZVO . "Nemo Cozi Domain In Complex With Diubiquitin In C2 Space Group" . . . . . 100.00 154 98.11 98.11 1.39e-26 . . . . 5101 1
152 no PDB 3A1Q . "Crystal Structure Of The Mouse Rap80 Uims In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.39e-26 . . . . 5101 1
153 no PDB 3A33 . "Ubch5b~ubiquitin Conjugate" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
154 no PDB 3A9J . "Crystal Structure Of The Mouse Tab2-Nzf In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.39e-26 . . . . 5101 1
155 no PDB 3A9K . "Crystal Structure Of The Mouse Tab3-Nzf In Complex With Lys63-Linked Di-Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.39e-26 . . . . 5101 1
156 no PDB 3AI5 . "Crystal Structure Of Yeast Enhanced Green Fluorescent Protein- Ubiquitin Fusion Protein" . . . . . 100.00 307 100.00 100.00 3.41e-26 . . . . 5101 1
157 no PDB 3ALB . "Cyclic Lys48-Linked Tetraubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
158 no PDB 3AUL . "Crystal Structure Of Wild-Type Lys48-Linked Diubiquitin In An Open Conformation" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
159 no PDB 3AXC . "Crystal Structure Of Linear Diubiquitin" . . . . . 100.00 154 98.11 98.11 1.39e-26 . . . . 5101 1
160 no PDB 3B08 . "Crystal Structure Of The Mouse Hoil1-l-nzf In Complex With Linear Di- Ubiquitin" . . . . . 96.23 152 100.00 100.00 1.06e-25 . . . . 5101 1
161 no PDB 3B0A . "Crystal Structure Of The Mouse Hoil1-l-nzf In Complex With Linear Di- Ubiquitin" . . . . . 96.23 152 100.00 100.00 1.06e-25 . . . . 5101 1
162 no PDB 3BY4 . "Structure Of Ovarian Tumor (Otu) Domain In Complex With Ubiquitin" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1
163 no PDB 3C0R . "Structure Of Ovarian Tumor (Otu) Domain In Complex With Ubiquitin" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1
164 no PDB 3DVG . "Crystal Structure Of K63-Specific Fab Apu.3a8 Bound To K63-Linked Di- Ubiquitin" . . . . . 98.11 79 98.08 98.08 1.10e-26 . . . . 5101 1
165 no PDB 3DVN . "Crystal Structure Of K63-specific Fab Apu2.16 Bound To K63-linked Di- Ubiquitin" . . . . . 98.11 79 98.08 98.08 1.10e-26 . . . . 5101 1
166 no PDB 3EEC . "X-Ray Structure Of Human Ubiquitin Cd(Ii) Adduct" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
167 no PDB 3EFU . "X-Ray Structure Of Human Ubiquitin-Hg(Ii) Adduct" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
168 no PDB 3EHV . "X-Ray Structure Of Human Ubiquitin Zn(Ii) Adduct" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
169 no PDB 3H1U . "Structure Of Ubiquitin In Complex With Cd Ions" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
170 no PDB 3H7P . "Crystal Structure Of K63-Linked Di-Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.39e-26 . . . . 5101 1
171 no PDB 3H7S . "Crystal Structures Of K63-Linked Di- And Tri-Ubiquitin Reveal A Highly Extended Chain Architecture" . . . . . 96.23 76 100.00 100.00 1.15e-26 . . . . 5101 1
172 no PDB 3HM3 . "The Structure And Conformation Of Lys-63 Linked Tetra-Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
173 no PDB 3I3T . "Crystal Structure Of Covalent Ubiquitin-usp21 Complex" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1
174 no PDB 3IFW . "Crystal Structure Of The S18y Variant Of Ubiquitin Carboxy T Hydrolase L1 Bound To Ubiquitin Vinylmethylester." . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1
175 no PDB 3IHP . "Covalent Ubiquitin-Usp5 Complex" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1
176 no PDB 3JSV . "Crystal Structure Of Mouse Nemo Cozi In Complex With Lys63- Linked Di-Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.39e-26 . . . . 5101 1
177 no PDB 3JVZ . E2~ubiquitin-Hect . . . . . 100.00 81 100.00 100.00 4.22e-28 . . . . 5101 1
178 no PDB 3JW0 . E2~ubiquitin-Hect . . . . . 100.00 81 100.00 100.00 4.22e-28 . . . . 5101 1
179 no PDB 3K9O . "The Crystal Structure Of E2-25k And Ubb+1 Complex" . . . . . 96.23 96 100.00 100.00 2.31e-26 . . . . 5101 1
180 no PDB 3K9P . "The Crystal Structure Of E2-25k And Ubiquitin Complex" . . . . . 98.11 79 98.08 98.08 1.27e-26 . . . . 5101 1
181 no PDB 3KVF . "Crystal Structure Of The I93m Mutant Of Ubiquitin Carboxy Te Hydrolase L1 Bound To Ubiquitin Vinylmethylester" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1
182 no PDB 3KW5 . "Crystal Structure Of Ubiquitin Carboxy Terminal Hydrolase L1 Ubiquitin Vinylmethylester" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1
183 no PDB 3LDZ . "Crystal Structure Of Human Stam1 Vhs Domain In Complex With Ubiquitin" . . . . . 96.23 73 100.00 100.00 1.19e-26 . . . . 5101 1
184 no PDB 3M3J . "A New Crystal Form Of Lys48-Linked Diubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
185 no PDB 3MHS . "Structure Of The Saga Ubp8SGF11SUS1SGF73 DUB MODULE BOUND Ubiquitin Aldehyde" . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1
186 no PDB 3MTN . "Usp21 In Complex With A Ubiquitin-based, Usp21-specific Inhibitor" . . . . . 96.23 85 100.00 100.00 1.61e-26 . . . . 5101 1
187 no PDB 3N30 . "Crystal Structure Of Cubic Zn3-Hub (Human Ubiquitin) Adduct" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
188 no PDB 3N32 . "The Crystal Structure Of Human Ubiquitin Adduct With Zeise's Salt" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
189 no PDB 3NHE . "High Resolution Structure (1.26a) Of Usp2a In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
190 no PDB 3NOB . "Structure Of K11-linked Di-ubiquitin" . . . . . 98.11 78 98.08 98.08 1.13e-26 . . . . 5101 1
191 no PDB 3NS8 . "Crystal Structure Of An Open Conformation Of Lys48-Linked Diubiquitin At Ph 7.5" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
192 no PDB 3O65 . "Crystal Structure Of A Josephin-Ubiquitin Complex: Evolutionary Restraints On Ataxin-3 Deubiquitinating Activity" . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1
193 no PDB 3OFI . "Crystal Structure Of Human Insulin-Degrading Enzyme In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
194 no PDB 3OJ3 . "Crystal Structure Of The A20 Znf4 And Ubiquitin Complex" . . . . . 98.11 79 98.08 98.08 1.27e-26 . . . . 5101 1
195 no PDB 3OJ4 . "Crystal Structure Of The A20 Znf4, Ubiquitin And Ubch5a Complex" . . . . . 98.11 79 98.08 98.08 1.27e-26 . . . . 5101 1
196 no PDB 3ONS . "Crystal Structure Of Human Ubiquitin In A New Crystal Form" . . . . . 96.23 72 100.00 100.00 1.10e-26 . . . . 5101 1
197 no PDB 3PHD . "Crystal Structure Of Human Hdac6 In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
198 no PDB 3PHW . "Otu Domain Of Crimean Congo Hemorrhagic Fever Virus In Complex With Ubiquitin" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1
199 no PDB 3PRM . "Structural Analysis Of A Viral Otu Domain Protease From The Crimean- Congo Hemorrhagic Fever Virus In Complex With Human Ubiqui" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1
200 no PDB 3PRP . "Structural Analysis Of A Viral Otu Domain Protease From The Crimean- Congo Hemorrhagic Fever Virus In Complex With Human Ubiqui" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1
201 no PDB 3PT2 . "Structure Of A Viral Otu Domain Protease Bound To Ubiquitin" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1
202 no PDB 3PTF . "X-Ray Structure Of The Non-Covalent Complex Between Ubch5a And Ubiquitin" . . . . . 98.11 79 98.08 98.08 1.27e-26 . . . . 5101 1
203 no PDB 3Q3F . "Engineering Domain-Swapped Binding Interfaces By Mutually Exclusive Folding: Insertion Of Ubiquitin Into Position 103 Of Barnas" . . . . . 94.34 189 100.00 100.00 5.85e-25 . . . . 5101 1
204 no PDB 3RUL . "New Strategy To Analyze Structures Of Glycopeptide-Target Complexes" . . . . . 96.23 79 100.00 100.00 1.41e-26 . . . . 5101 1
205 no PDB 3TBL . "Structure Of Mono-ubiquitinated Pcna: Implications For Dna Polymerase Switching And Okazaki Fragment Maturation" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
206 no PDB 3TMP . "The Catalytic Domain Of Human Deubiquitinase Duba In Complex With Ubiquitin Aldehyde" . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1
207 no PDB 3U30 . "Crystal Structure Of A Linear-Specific Ubiquitin Fab Bound To Linear Ubiquitin" . . . . . 98.11 172 98.08 98.08 6.45e-26 . . . . 5101 1
208 no PDB 3UGB . "Ubch5c~ubiquitin Conjugate" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
209 no PDB 3VDZ . "Tailoring Encodable Lanthanide-Binding Tags As Mri Contrast Agents: Xq-Dse3-Ubiquitin At 2.4 Angstroms" . . . . . 98.11 111 98.08 100.00 1.11e-26 . . . . 5101 1
210 no PDB 3VFK . "The Structure Of Monodechloro-teicoplanin In Complex With Its Ligand, Using Ubiquitin As A Ligand Carrier" . . . . . 96.23 79 100.00 100.00 1.41e-26 . . . . 5101 1
211 no PDB 3VHT . "Crystal Structure Of Gfp-Wrnip1 Ubz Domain Fusion Protein In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
212 no PDB 3VUW . "Crystal Structure Of A20 Zf7 In Complex With Linear Ubiquitin, Form I" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
213 no PDB 3VUX . "Crystal Structure Of A20 Zf7 In Complex With Linear Ubiquitin, Form Ii" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
214 no PDB 3VUY . "Crystal Structure Of A20 Zf7 In Complex With Linear Tetraubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
215 no PDB 3ZLZ . "Lys6-linked Tri-ubiquitin" . . . . . 96.23 76 98.04 100.00 2.70e-26 . . . . 5101 1
216 no PDB 3ZNH . "Crimean Congo Hemorrhagic Fever Virus Otu Domain In Complex With Ubiquitin-propargyl." . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1
217 no PDB 3ZNI . "Structure Of Phosphotyr363-cbl-b - Ubch5b-ub - Zap-70 Peptide Complex" . . . . . 100.00 81 100.00 100.00 4.22e-28 . . . . 5101 1
218 no PDB 3ZNZ . "Crystal Structure Of Otulin Otu Domain (c129a) In Complex With Met1-di Ubiquitin" . . . . . 96.23 152 100.00 100.00 1.06e-25 . . . . 5101 1
219 no PDB 4AP4 . "Rnf4 - Ubch5a - Ubiquitin Heterotrimeric Complex" . . . . . 98.11 80 98.08 98.08 1.42e-26 . . . . 5101 1
220 no PDB 4AUQ . "Structure Of Birc7-Ubch5b-Ub Complex." . . . . . 100.00 81 100.00 100.00 4.22e-28 . . . . 5101 1
221 no PDB 4BBN . "Nedd4 Hect-ub:ub Complex" . . . . . 96.23 76 100.00 100.00 1.27e-26 . . . . 5101 1
222 no PDB 4BOS . "Structure Of Otud2 Otu Domain In Complex With Ubiquitin K11- Linked Peptide" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
223 no PDB 4BOZ . "Structure Of Otud2 Otu Domain In Complex With K11-linked Di Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
224 no PDB 4BVU . "Structure Of Shigella Effector Ospg In Complex With Host Ubch5c-ubiquitin Conjugate" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
225 no PDB 4CXC . "Regulation Of The Mammalian Elongation Cycle By 40s Subunit Rolling: A Eukaryotic-specific Ribosome Rearrangement" . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1
226 no PDB 4CXD . "Regulation Of The Mammalian Elongation Cycle By 40s Subunit Rolling: A Eukaryotic-specific Ribosome Rearrangement" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1
227 no PDB 4DDG . "Crystal Structure Of Human Otub1UBCH5B~UBUB" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
228 no PDB 4DDI . "Crystal Structure Of Human Otub1UBCH5B~UBUB" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
229 no PDB 4DHJ . "The Structure Of A Ceotub1 Ubiquitin Aldehyde Ubc13~ub Complex" . . . . . 96.23 76 100.00 100.00 1.27e-26 . . . . 5101 1
230 no PDB 4DHZ . "The Structure Of HCEOTUB1-Ubiquitin Aldehyde-Ubc13~ub" . . . . . 96.23 76 100.00 100.00 1.27e-26 . . . . 5101 1
231 no PDB 4HXD . "Diversity Of Ubiquitin And Isg15 Specificity Amongst Nairoviruses Viral Ovarian Tumor Domain Proteases" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1
232 no PDB 4I6N . "Crystal Structure Of Trichinella Spiralis Uch37 Catalytic Domain Bound To Ubiquitin Vinyl Methyl Ester" . . . . . 94.34 75 100.00 100.00 1.28e-25 . . . . 5101 1
233 no PDB 4IG7 . "Crystal Structure Of Trichinella Spiralis Uch37 Bound To Ubiquitin Vinyl Methyl Ester" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1
234 no PDB 4IUM . "Equine Arteritis Virus Papain-like Protease 2 (plp2) Covalently Bound To Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1
235 no PDB 4JIO . "Bro1 V Domain And Ubiquitin" . . . . . 96.23 76 98.04 98.04 9.07e-26 . . . . 5101 1
236 no PDB 4JQW . "Crystal Structure Of A Complex Of Nod1 Card And Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
237 no PDB 4K1R . "Crystal Structure Of Schizosaccharomyces Pombe Sst2 Catalytic Domain And Ubiquitin" . . . . . 100.00 81 100.00 100.00 6.23e-28 . . . . 5101 1
238 no PDB 4K7S . "Crystal Structure Of Zn2-hub (human Ubiquitin) Adduct From A Solution 35 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
239 no PDB 4K7U . "Crystal Structure Of Zn2.3-hub (human Ubiquitin) Adduct From A Solution 70 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
240 no PDB 4K7W . "Crystal Structure Of Zn3-hub(human Ubiquitin) Adduct From A Solution 100 Mm Zinc Acetate/1.3 Mm Hub" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
241 no PDB 4KSK . "Gumby/fam105b In Complex With Ubiquitin" . . . . . 98.11 80 98.08 98.08 1.42e-26 . . . . 5101 1
242 no PDB 4KSL . "Gumby/fam105b In Complex With Linear Di-ubiquitin" . . . . . 96.23 156 100.00 100.00 1.14e-25 . . . . 5101 1
243 no PDB 4KZX . "Rabbit 40s Ribosomal Subunit In Complex With Eif1." . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1
244 no PDB 4KZY . "Rabbit 40s Ribosomal Subunit In Complex With Eif1 And Eif1a." . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1
245 no PDB 4KZZ . "Rabbit 40s Ribosomal Subunit In Complex With Mrna, Initiator Trna And Eif1a" . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1
246 no PDB 4LCD . "Structure Of An Rsp5xubxsna3 Complex: Mechanism Of Ubiquitin Ligation And Lysine Prioritization By A Hect E3" . . . . . 98.11 83 98.08 98.08 3.66e-27 . . . . 5101 1
247 no PDB 4LDT . "The Structure Of H/ceotub1-ubiquitin Aldehyde-ubch5b~ub" . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1
248 no PDB 4LJO . "Structure Of An Active Ligase (hoip)/ubiquitin Transfer Complex" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
249 no PDB 4LJP . "Structure Of An Active Ligase (hoip-h889a)/ubiquitin Transfer Complex" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
250 no PDB 4M0W . "Crystal Structure Of Sars-cov Papain-like Protease C112s Mutant In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
251 no PDB 4MDK . "Cdc34-ubiquitin-cc0651 Complex" . . . . . 98.11 80 98.08 98.08 1.42e-26 . . . . 5101 1
252 no PDB 4MM3 . "Crystal Structure Of Sars-cov Papain-like Protease Plpro In Complex With Ubiquitin Aldehyde" . . . . . 96.23 76 100.00 100.00 1.34e-26 . . . . 5101 1
253 no PDB 4MSM . "Crystal Structure Of Schizosaccharomyces Pombe Amsh-like Protease Sst2 E286a Mutant Bound To Ubiquitin" . . . . . 100.00 81 100.00 100.00 6.23e-28 . . . . 5101 1
254 no PDB 4MSQ . "Crystal Structure Of Schizosaccharomyces Pombe Amsh-like Protease Sst2 Catalytic Domain Bound To Ubiquitin" . . . . . 100.00 81 100.00 100.00 6.23e-28 . . . . 5101 1
255 no PDB 4NQK . "Structure Of An Ubiquitin Complex" . . . . . 98.11 79 98.08 98.08 2.27e-26 . . . . 5101 1
256 no PDB 4NQL . "The Crystal Structure Of The Dub Domain Of Amsh Orthologue, Sst2 From S. Pombe, In Complex With Lysine 63-linked Diubiquitin" . . . . . 96.23 76 100.00 100.00 1.39e-26 . . . . 5101 1
257 no PDB 4P4H . "Caught-in-action Signaling Complex Of Rig-i 2card Domain And Mavs Card Domain" . . . . . 98.11 79 98.08 98.08 2.27e-26 . . . . 5101 1
258 no PDB 4PIG . "Crystal Structure Of The Ubiquitin K11s Mutant" . . . . . 96.23 76 98.04 98.04 6.28e-26 . . . . 5101 1
259 no PDB 4PIH . "X-ray Crystal Structure Of The K33s Mutant Of Ubiquitin" . . . . . 96.23 76 98.04 98.04 6.28e-26 . . . . 5101 1
260 no PDB 4PIJ . "X-ray Crystal Structure Of The K11s/k63s Double Mutant Of Ubiquitin" . . . . . 96.23 75 98.04 98.04 4.52e-26 . . . . 5101 1
261 no PDB 4PQT . "Insights Into The Mechanism Of Deubiquitination By Jamm Deubiquitinases From Co-crystal Structures Of Enzyme With Substrate And" . . . . . 100.00 81 100.00 100.00 6.23e-28 . . . . 5101 1
262 no PDB 4RF0 . "Crystal Structure Of The Middle-east Respiratory Syndrome Coronavirus Papain-like Protease In Complex With Ubiquitin (space Gro" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1
263 no PDB 4RF1 . "Crystal Structure Of The Middle-east Respiratory Syndrome Coronavirus Papain-like Protease In Complex With Ubiquitin (space Gro" . . . . . 96.23 75 100.00 100.00 1.30e-26 . . . . 5101 1
264 no PDB 4UN2 . "Crystal Structure Of The Uba Domain Of Dsk2 In Complex With Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
265 no PDB 4UPX . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Pre-like State" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1
266 no PDB 4UQ1 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Post-like State" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1
267 no PDB 4UQ4 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Post-like State" . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1
268 no PDB 4UQ5 . "Mammalian 80s Hcv-ires Initiation Complex With Eif5b Pre-like State" . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1
269 no PDB 4W20 . "Structure Of The Mammalian 60s Ribosomal Subunit (this Entry Contains The Large Ribosomal Proteins)" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1
270 no PDB 4W22 . "Structure Of The 80s Mammalian Ribosome Bound To Eef2 (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1
271 no PDB 4W23 . "Structure Of The 80s Mammalian Ribosome Bound To Eef2 (this Entry Contains The Small Ribosomal Subunit)" . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1
272 no PDB 4W25 . "Structure Of The Idle Mammalian Ribosome-sec61 Complex (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1
273 no PDB 4W27 . "Structure Of The Translating Mammalian Ribosome-sec61 Complex (this Entry Contains The Large Ribosomal Subunit Proteins)" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1
274 no PDB 4W28 . "Structure Of The Translating Mammalian Ribosome-sec61 Complex (this Entry Contains The Small Ribosomal Subunit)" . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1
275 no PDB 4WUR . "The Crystal Structure Of The Mers-cov Papain-like Protease (c111s) With Human Ubiquitin" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
276 no PDB 4WZP . "Ser65 Phosphorylated Ubiquitin, Major Conformation" . . . . . 96.23 76 100.00 100.00 1.93e-26 . . . . 5101 1
277 no DBJ BAA03983 . "polyubiquitin [Rattus norvegicus]" . . . . . 96.23 305 100.00 100.00 1.37e-24 . . . . 5101 1
278 no DBJ BAA11389 . "putative ubiquitin extension protein [Brassica rapa]" . . . . . 66.04 112 97.14 97.14 5.41e-14 . . . . 5101 1
279 no DBJ BAA11842 . "ubiquitin [Cavia porcellus]" . . . . . 96.23 311 100.00 100.00 1.53e-24 . . . . 5101 1
280 no DBJ BAA11843 . "ubiquitin extention protein [Cavia porcellus]" . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1
281 no DBJ BAA23486 . "polyubiquitin [Homo sapiens]" . . . . . 96.23 609 100.00 100.00 1.25e-23 . . . . 5101 1
282 no EMBL CAA28495 . "ubiquitin [Homo sapiens]" . . . . . 96.23 229 100.00 100.00 6.13e-25 . . . . 5101 1
283 no EMBL CAA30815 . "unnamed protein product [Cricetulus sp.]" . . . . . 96.23 223 100.00 100.00 4.80e-25 . . . . 5101 1
284 no EMBL CAA33466 . "unnamed protein product [Chlamydomonas reinhardtii]" . . . . . 96.23 128 98.04 98.04 1.75e-25 . . . . 5101 1
285 no EMBL CAA35999 . "ubiquitin [Mus musculus]" . . . . . 96.23 305 100.00 100.00 1.37e-24 . . . . 5101 1
286 no EMBL CAA37227 . "unnamed protein product [Drosophila melanogaster]" . . . . . 96.23 128 100.00 100.00 1.52e-26 . . . . 5101 1
287 no GB AAA02769 . "polyprotein [Bovine viral diarrhea virus 1-Osloss]" . . . . . 96.23 3975 98.04 100.00 2.19e-23 . . . . 5101 1
288 no GB AAA28153 . "ubiquitin A, partial [Caenorhabditis elegans]" . . . . . 69.81 37 97.30 97.30 1.29e-14 . . . . 5101 1
289 no GB AAA28154 . "polyubiquitin [Caenorhabditis elegans]" . . . . . 96.23 838 98.04 98.04 1.14e-22 . . . . 5101 1
290 no GB AAA28997 . "ubiquitin [Drosophila melanogaster]" . . . . . 96.23 231 100.00 100.00 5.26e-25 . . . . 5101 1
291 no GB AAA28998 . "ubiquitin-hybrid protein precursor [Drosophila melanogaster]" . . . . . 96.23 156 100.00 100.00 2.71e-26 . . . . 5101 1
292 no PIR I50437 . "polyubiquitin 4 - chicken [Gallus gallus]" . . . . . 96.23 305 100.00 100.00 1.37e-24 . . . . 5101 1
293 no PIR I51568 . "polyubiquitin - African clawed frog (fragment)" . . . . . 100.00 167 98.11 98.11 1.45e-26 . . . . 5101 1
294 no PIR I65237 . "ubiquitin / ribosomal protein L40, cytosolic [validated] - rat" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1
295 no PIR JN0790 . "ubiquitin/ribosomal protein CEP52 fusion protein - Leishmania major" . . . . . 96.23 128 98.04 98.04 3.27e-26 . . . . 5101 1
296 no PIR S13928 . "ubiquitin precursor - chicken [Gallus gallus]" . . . . . 96.23 229 100.00 100.00 5.18e-25 . . . . 5101 1
297 no PRF 0412265A . ubiquitin . . . . . 96.23 75 98.04 98.04 6.19e-26 . . . . 5101 1
298 no PRF 1212243A . "ubiquitin S1" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
299 no PRF 1212243B . "ubiquitin S5" . . . . . 96.23 77 98.04 98.04 6.10e-26 . . . . 5101 1
300 no PRF 1212243C . "ubiquitin S3" . . . . . 96.23 76 100.00 100.00 1.49e-26 . . . . 5101 1
301 no PRF 1212243D . "ubiquitin S2" . . . . . 96.23 77 98.04 98.04 7.99e-26 . . . . 5101 1
302 no REF NP_001005123 . "ubiquitin A-52 residue ribosomal protein fusion product 1 [Xenopus (Silurana) tropicalis]" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1
303 no REF NP_001006688 . "ubiquitin C [Xenopus (Silurana) tropicalis]" . . . . . 96.23 609 100.00 100.00 1.25e-23 . . . . 5101 1
304 no REF NP_001009117 . "polyubiquitin-B [Pan troglodytes]" . . . . . 96.23 229 100.00 100.00 6.13e-25 . . . . 5101 1
305 no REF NP_001009202 . "polyubiquitin-B [Ovis aries]" . . . . . 96.23 305 100.00 100.00 1.66e-24 . . . . 5101 1
306 no REF NP_001009286 . "ubiquitin-60S ribosomal protein L40 [Ovis aries]" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1
307 no SP P0C273 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1
308 no SP P0C275 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1
309 no SP P0C276 . "RecName: Full=Ubiquitin-60S ribosomal protein L40; AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1; Con" . . . . . 96.23 128 100.00 100.00 1.44e-26 . . . . 5101 1
310 no SP P0CG47 . "RecName: Full=Polyubiquitin-B; Contains: RecName: Full=Ubiquitin; Flags: Precursor [Homo sapiens]" . . . . . 96.23 229 100.00 100.00 6.13e-25 . . . . 5101 1
311 no SP P0CG48 . "RecName: Full=Polyubiquitin-C; Contains: RecName: Full=Ubiquitin; Flags: Precursor [Homo sapiens]" . . . . . 96.23 685 100.00 100.00 1.59e-23 . . . . 5101 1
312 no TPG DAA18802 . "TPA: polyubiquitin [Bos taurus]" . . . . . 96.23 305 100.00 100.00 1.69e-24 . . . . 5101 1
313 no TPG DAA20663 . "TPA: ubiquitin C [Bos taurus]" . . . . . 96.23 314 98.04 98.04 6.82e-24 . . . . 5101 1
314 no TPG DAA20672 . "TPA: ubiquitin B-like [Bos taurus]" . . . . . 96.23 77 98.04 98.04 1.05e-25 . . . . 5101 1
315 no TPG DAA24675 . "TPA: 40S ribosomal protein S27a [Bos taurus]" . . . . . 96.23 156 100.00 100.00 2.12e-26 . . . . 5101 1
316 no TPG DAA26453 . "TPA: ubiquitin and ribosomal protein S27a-like [Bos taurus]" . . . . . 96.23 156 98.04 100.00 2.80e-26 . . . . 5101 1
stop_
loop_
_Entity_common_name.Name
_Entity_common_name.Type
_Entity_common_name.Entry_ID
_Entity_common_name.Entity_ID
Ubiquitin common 5101 1
uq1_51 abbreviation 5101 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 -1 GLY . 5101 1
2 0 SER . 5101 1
3 1 MET . 5101 1
4 2 GLN . 5101 1
5 3 ILE . 5101 1
6 4 PHE . 5101 1
7 5 VAL . 5101 1
8 6 LYS . 5101 1
9 7 THR . 5101 1
10 8 LEU . 5101 1
11 9 THR . 5101 1
12 10 GLY . 5101 1
13 11 LYS . 5101 1
14 12 THR . 5101 1
15 13 ILE . 5101 1
16 14 THR . 5101 1
17 15 LEU . 5101 1
18 16 GLU . 5101 1
19 17 VAL . 5101 1
20 18 GLU . 5101 1
21 19 PRO . 5101 1
22 20 SER . 5101 1
23 21 ASP . 5101 1
24 22 THR . 5101 1
25 23 ILE . 5101 1
26 24 GLU . 5101 1
27 25 ASN . 5101 1
28 26 VAL . 5101 1
29 27 LYS . 5101 1
30 28 ALA . 5101 1
31 29 LYS . 5101 1
32 30 ILE . 5101 1
33 31 GLN . 5101 1
34 32 ASP . 5101 1
35 33 LYS . 5101 1
36 34 GLU . 5101 1
37 35 GLY . 5101 1
38 36 ILE . 5101 1
39 37 PRO . 5101 1
40 38 PRO . 5101 1
41 39 ASP . 5101 1
42 40 GLN . 5101 1
43 41 GLN . 5101 1
44 42 ARG . 5101 1
45 43 LEU . 5101 1
46 44 ILE . 5101 1
47 45 PHE . 5101 1
48 46 ALA . 5101 1
49 47 GLY . 5101 1
50 48 LYS . 5101 1
51 49 GLN . 5101 1
52 50 LEU . 5101 1
53 51 GLU . 5101 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
. GLY 1 1 5101 1
. SER 2 2 5101 1
. MET 3 3 5101 1
. GLN 4 4 5101 1
. ILE 5 5 5101 1
. PHE 6 6 5101 1
. VAL 7 7 5101 1
. LYS 8 8 5101 1
. THR 9 9 5101 1
. LEU 10 10 5101 1
. THR 11 11 5101 1
. GLY 12 12 5101 1
. LYS 13 13 5101 1
. THR 14 14 5101 1
. ILE 15 15 5101 1
. THR 16 16 5101 1
. LEU 17 17 5101 1
. GLU 18 18 5101 1
. VAL 19 19 5101 1
. GLU 20 20 5101 1
. PRO 21 21 5101 1
. SER 22 22 5101 1
. ASP 23 23 5101 1
. THR 24 24 5101 1
. ILE 25 25 5101 1
. GLU 26 26 5101 1
. ASN 27 27 5101 1
. VAL 28 28 5101 1
. LYS 29 29 5101 1
. ALA 30 30 5101 1
. LYS 31 31 5101 1
. ILE 32 32 5101 1
. GLN 33 33 5101 1
. ASP 34 34 5101 1
. LYS 35 35 5101 1
. GLU 36 36 5101 1
. GLY 37 37 5101 1
. ILE 38 38 5101 1
. PRO 39 39 5101 1
. PRO 40 40 5101 1
. ASP 41 41 5101 1
. GLN 42 42 5101 1
. GLN 43 43 5101 1
. ARG 44 44 5101 1
. LEU 45 45 5101 1
. ILE 46 46 5101 1
. PHE 47 47 5101 1
. ALA 48 48 5101 1
. GLY 49 49 5101 1
. LYS 50 50 5101 1
. GLN 51 51 5101 1
. LEU 52 52 5101 1
. GLU 53 53 5101 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 5101
_Entity_natural_src_list.ID 1
loop_
_Entity_natural_src.ID
_Entity_natural_src.Entity_ID
_Entity_natural_src.Entity_label
_Entity_natural_src.Entity_chimera_segment_ID
_Entity_natural_src.NCBI_taxonomy_ID
_Entity_natural_src.Type
_Entity_natural_src.Common
_Entity_natural_src.Organism_name_scientific
_Entity_natural_src.Organism_name_common
_Entity_natural_src.Organism_acronym
_Entity_natural_src.ICTVdb_decimal_code
_Entity_natural_src.Superkingdom
_Entity_natural_src.Kingdom
_Entity_natural_src.Genus
_Entity_natural_src.Species
_Entity_natural_src.Strain
_Entity_natural_src.Variant
_Entity_natural_src.Subvariant
_Entity_natural_src.Organ
_Entity_natural_src.Tissue
_Entity_natural_src.Tissue_fraction
_Entity_natural_src.Cell_line
_Entity_natural_src.Cell_type
_Entity_natural_src.ATCC_number
_Entity_natural_src.Organelle
_Entity_natural_src.Cellular_location
_Entity_natural_src.Fragment
_Entity_natural_src.Fraction
_Entity_natural_src.Secretion
_Entity_natural_src.Plasmid
_Entity_natural_src.Plasmid_details
_Entity_natural_src.Gene_mnemonic
_Entity_natural_src.Dev_stage
_Entity_natural_src.Details
_Entity_natural_src.Citation_ID
_Entity_natural_src.Citation_label
_Entity_natural_src.Entry_ID
_Entity_natural_src.Entity_natural_src_list_ID
1 1 $uq1_51 . 9606 . . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 5101 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 5101
_Entity_experimental_src_list.ID 1
loop_
_Entity_experimental_src.ID
_Entity_experimental_src.Entity_ID
_Entity_experimental_src.Entity_label
_Entity_experimental_src.Entity_chimera_segment_ID
_Entity_experimental_src.Production_method
_Entity_experimental_src.Host_org_scientific_name
_Entity_experimental_src.Host_org_name_common
_Entity_experimental_src.Host_org_details
_Entity_experimental_src.Host_org_NCBI_taxonomy_ID
_Entity_experimental_src.Host_org_genus
_Entity_experimental_src.Host_org_species
_Entity_experimental_src.Host_org_strain
_Entity_experimental_src.Host_org_variant
_Entity_experimental_src.Host_org_subvariant
_Entity_experimental_src.Host_org_organ
_Entity_experimental_src.Host_org_tissue
_Entity_experimental_src.Host_org_tissue_fraction
_Entity_experimental_src.Host_org_cell_line
_Entity_experimental_src.Host_org_cell_type
_Entity_experimental_src.Host_org_cellular_location
_Entity_experimental_src.Host_org_organelle
_Entity_experimental_src.Host_org_gene
_Entity_experimental_src.Host_org_culture_collection
_Entity_experimental_src.Host_org_ATCC_number
_Entity_experimental_src.Vector_type
_Entity_experimental_src.PDBview_host_org_vector_name
_Entity_experimental_src.PDBview_plasmid_name
_Entity_experimental_src.Vector_name
_Entity_experimental_src.Vector_details
_Entity_experimental_src.Vendor_name
_Entity_experimental_src.Host_org_dev_stage
_Entity_experimental_src.Details
_Entity_experimental_src.Citation_ID
_Entity_experimental_src.Citation_label
_Entity_experimental_src.Entry_ID
_Entity_experimental_src.Entity_experimental_src_list_ID
1 1 $uq1_51 . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli BL21 . . . . . . . . . . . . plasmid . . pGEX-4T3 . . . 'Peptide was expressed as a fusion to GST and then cleaved with thrombin.' . . 5101 1
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Sample.Sf_category sample
_Sample.Sf_framecode sample_1
_Sample.Entry_ID 5101
_Sample.ID 1
_Sample.Type solution
_Sample.Sub_type .
_Sample.Details .
_Sample.Aggregate_sample_number .
_Sample.Solvent_system .
_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 Ubiquitin '[U-100% 13C; U-100% 15N]' . . 1 $uq1_51 . . 1.0 . . mM . . . . 5101 1
2 'sodium sulphate' . . . . . . . 0.8 . . M . . . . 5101 1
stop_
save_
save_sample_2
_Sample.Sf_category sample
_Sample.Sf_framecode sample_2
_Sample.Entry_ID 5101
_Sample.ID 2
_Sample.Type solution
_Sample.Sub_type .
_Sample.Details .
_Sample.Aggregate_sample_number .
_Sample.Solvent_system .
_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 Ubiquitin . . . 1 $uq1_51 . . 1.0 . . mM . . . . 5101 2
2 'sodium sulphate' . . . . . . . 0.8 . . M . . . . 5101 2
stop_
save_
#######################
# Sample conditions #
#######################
save_conditions_1
_Sample_condition_list.Sf_category sample_conditions
_Sample_condition_list.Sf_framecode conditions_1
_Sample_condition_list.Entry_ID 5101
_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 7.0 0.2 na 5101 1
temperature 298 1 K 5101 1
'ionic strength' 0.8 0.1 M 5101 1
pressure 1 0.1 atm 5101 1
stop_
save_
############################
# Computer software used #
############################
save_AZARA
_Software.Sf_category software
_Software.Sf_framecode AZARA
_Software.Entry_ID 5101
_Software.ID 1
_Software.Name AZARA
_Software.Version .
_Software.Details .
loop_
_Task.Task
_Task.Entry_ID
_Task.Software_ID
'data processing' 5101 1
stop_
save_
save_ANSIG
_Software.Sf_category software
_Software.Sf_framecode ANSIG
_Software.Entry_ID 5101
_Software.ID 2
_Software.Name ANSIG
_Software.Version 3.3
_Software.Details .
loop_
_Task.Task
_Task.Entry_ID
_Task.Software_ID
assignment 5101 2
stop_
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer
_NMR_spectrometer.Sf_category NMR_spectrometer
_NMR_spectrometer.Sf_framecode NMR_spectrometer
_NMR_spectrometer.Entry_ID 5101
_NMR_spectrometer.ID 1
_NMR_spectrometer.Details .
_NMR_spectrometer.Manufacturer Bruker
_NMR_spectrometer.Model DRX
_NMR_spectrometer.Serial_number .
_NMR_spectrometer.Field_strength 500
save_
save_spectrometer_list
_NMR_spectrometer_list.Sf_category NMR_spectrometer_list
_NMR_spectrometer_list.Sf_framecode spectrometer_list
_NMR_spectrometer_list.Entry_ID 5101
_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 NMR_spectrometer Bruker DRX . 500 . . . 5101 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 5101
_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 '3D 1H-1H-15N NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5101 1
2 '3D 1H-1H-15N TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5101 1
3 '3D 13C-1H-1H NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5101 1
4 '3D 1H-13C-1H HCCH-TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5101 1
5 '3D CBCA(CO)NH' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5101 1
6 '3D HNCA' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5101 1
7 '3D HN(CO)CA' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5101 1
stop_
save_
save_NMR_spec_expt__0_1
_NMR_spec_expt.Sf_category NMR_spectrometer_expt
_NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1
_NMR_spec_expt.Entry_ID 5101
_NMR_spec_expt.ID 1
_NMR_spec_expt.Name '3D 1H-1H-15N NOESY'
_NMR_spec_expt.Type .
_NMR_spec_expt.Sample_volume .
_NMR_spec_expt.Sample_volume_units .
_NMR_spec_expt.NMR_tube_type .
_NMR_spec_expt.Sample_spinning_rate .
_NMR_spec_expt.Sample_angle .
_NMR_spec_expt.NMR_spectrometer_ID .
_NMR_spec_expt.NMR_spectrometer_label .
_NMR_spec_expt.NMR_spectrometer_probe_ID .
_NMR_spec_expt.NMR_spectrometer_probe_label .
_NMR_spec_expt.Carrier_freq_switch_time .
_NMR_spec_expt.Software_ID .
_NMR_spec_expt.Software_label .
_NMR_spec_expt.Method_ID .
_NMR_spec_expt.Method_label .
_NMR_spec_expt.Pulse_seq_accession_BMRB_code .
_NMR_spec_expt.Details .
save_
save_NMR_spec_expt__0_2
_NMR_spec_expt.Sf_category NMR_spectrometer_expt
_NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2
_NMR_spec_expt.Entry_ID 5101
_NMR_spec_expt.ID 2
_NMR_spec_expt.Name '3D 1H-1H-15N TOCSY'
_NMR_spec_expt.Type .
_NMR_spec_expt.Sample_volume .
_NMR_spec_expt.Sample_volume_units .
_NMR_spec_expt.NMR_tube_type .
_NMR_spec_expt.Sample_spinning_rate .
_NMR_spec_expt.Sample_angle .
_NMR_spec_expt.NMR_spectrometer_ID .
_NMR_spec_expt.NMR_spectrometer_label .
_NMR_spec_expt.NMR_spectrometer_probe_ID .
_NMR_spec_expt.NMR_spectrometer_probe_label .
_NMR_spec_expt.Carrier_freq_switch_time .
_NMR_spec_expt.Software_ID .
_NMR_spec_expt.Software_label .
_NMR_spec_expt.Method_ID .
_NMR_spec_expt.Method_label .
_NMR_spec_expt.Pulse_seq_accession_BMRB_code .
_NMR_spec_expt.Details .
save_
save_NMR_spec_expt__0_3
_NMR_spec_expt.Sf_category NMR_spectrometer_expt
_NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3
_NMR_spec_expt.Entry_ID 5101
_NMR_spec_expt.ID 3
_NMR_spec_expt.Name '3D 13C-1H-1H NOESY'
_NMR_spec_expt.Type .
_NMR_spec_expt.Sample_volume .
_NMR_spec_expt.Sample_volume_units .
_NMR_spec_expt.NMR_tube_type .
_NMR_spec_expt.Sample_spinning_rate .
_NMR_spec_expt.Sample_angle .
_NMR_spec_expt.NMR_spectrometer_ID .
_NMR_spec_expt.NMR_spectrometer_label .
_NMR_spec_expt.NMR_spectrometer_probe_ID .
_NMR_spec_expt.NMR_spectrometer_probe_label .
_NMR_spec_expt.Carrier_freq_switch_time .
_NMR_spec_expt.Software_ID .
_NMR_spec_expt.Software_label .
_NMR_spec_expt.Method_ID .
_NMR_spec_expt.Method_label .
_NMR_spec_expt.Pulse_seq_accession_BMRB_code .
_NMR_spec_expt.Details .
save_
save_NMR_spec_expt__0_4
_NMR_spec_expt.Sf_category NMR_spectrometer_expt
_NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4
_NMR_spec_expt.Entry_ID 5101
_NMR_spec_expt.ID 4
_NMR_spec_expt.Name '3D 1H-13C-1H HCCH-TOCSY'
_NMR_spec_expt.Type .
_NMR_spec_expt.Sample_volume .
_NMR_spec_expt.Sample_volume_units .
_NMR_spec_expt.NMR_tube_type .
_NMR_spec_expt.Sample_spinning_rate .
_NMR_spec_expt.Sample_angle .
_NMR_spec_expt.NMR_spectrometer_ID .
_NMR_spec_expt.NMR_spectrometer_label .
_NMR_spec_expt.NMR_spectrometer_probe_ID .
_NMR_spec_expt.NMR_spectrometer_probe_label .
_NMR_spec_expt.Carrier_freq_switch_time .
_NMR_spec_expt.Software_ID .
_NMR_spec_expt.Software_label .
_NMR_spec_expt.Method_ID .
_NMR_spec_expt.Method_label .
_NMR_spec_expt.Pulse_seq_accession_BMRB_code .
_NMR_spec_expt.Details .
save_
save_NMR_spec_expt__0_5
_NMR_spec_expt.Sf_category NMR_spectrometer_expt
_NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5
_NMR_spec_expt.Entry_ID 5101
_NMR_spec_expt.ID 5
_NMR_spec_expt.Name '3D CBCA(CO)NH'
_NMR_spec_expt.Type .
_NMR_spec_expt.Sample_volume .
_NMR_spec_expt.Sample_volume_units .
_NMR_spec_expt.NMR_tube_type .
_NMR_spec_expt.Sample_spinning_rate .
_NMR_spec_expt.Sample_angle .
_NMR_spec_expt.NMR_spectrometer_ID .
_NMR_spec_expt.NMR_spectrometer_label .
_NMR_spec_expt.NMR_spectrometer_probe_ID .
_NMR_spec_expt.NMR_spectrometer_probe_label .
_NMR_spec_expt.Carrier_freq_switch_time .
_NMR_spec_expt.Software_ID .
_NMR_spec_expt.Software_label .
_NMR_spec_expt.Method_ID .
_NMR_spec_expt.Method_label .
_NMR_spec_expt.Pulse_seq_accession_BMRB_code .
_NMR_spec_expt.Details .
save_
save_NMR_spec_expt__0_6
_NMR_spec_expt.Sf_category NMR_spectrometer_expt
_NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6
_NMR_spec_expt.Entry_ID 5101
_NMR_spec_expt.ID 6
_NMR_spec_expt.Name '3D HNCA'
_NMR_spec_expt.Type .
_NMR_spec_expt.Sample_volume .
_NMR_spec_expt.Sample_volume_units .
_NMR_spec_expt.NMR_tube_type .
_NMR_spec_expt.Sample_spinning_rate .
_NMR_spec_expt.Sample_angle .
_NMR_spec_expt.NMR_spectrometer_ID .
_NMR_spec_expt.NMR_spectrometer_label .
_NMR_spec_expt.NMR_spectrometer_probe_ID .
_NMR_spec_expt.NMR_spectrometer_probe_label .
_NMR_spec_expt.Carrier_freq_switch_time .
_NMR_spec_expt.Software_ID .
_NMR_spec_expt.Software_label .
_NMR_spec_expt.Method_ID .
_NMR_spec_expt.Method_label .
_NMR_spec_expt.Pulse_seq_accession_BMRB_code .
_NMR_spec_expt.Details .
save_
save_NMR_spec_expt__0_7
_NMR_spec_expt.Sf_category NMR_spectrometer_expt
_NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7
_NMR_spec_expt.Entry_ID 5101
_NMR_spec_expt.ID 7
_NMR_spec_expt.Name '3D HN(CO)CA'
_NMR_spec_expt.Type .
_NMR_spec_expt.Sample_volume .
_NMR_spec_expt.Sample_volume_units .
_NMR_spec_expt.NMR_tube_type .
_NMR_spec_expt.Sample_spinning_rate .
_NMR_spec_expt.Sample_angle .
_NMR_spec_expt.NMR_spectrometer_ID .
_NMR_spec_expt.NMR_spectrometer_label .
_NMR_spec_expt.NMR_spectrometer_probe_ID .
_NMR_spec_expt.NMR_spectrometer_probe_label .
_NMR_spec_expt.Carrier_freq_switch_time .
_NMR_spec_expt.Software_ID .
_NMR_spec_expt.Software_label .
_NMR_spec_expt.Method_ID .
_NMR_spec_expt.Method_label .
_NMR_spec_expt.Pulse_seq_accession_BMRB_code .
_NMR_spec_expt.Details .
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference
_Chem_shift_reference.Sf_category chem_shift_reference
_Chem_shift_reference.Sf_framecode chemical_shift_reference
_Chem_shift_reference.Entry_ID 5101
_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
H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.000000000 . . . . . . . . . 5101 1
N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5101 1
C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5101 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_shift_set_1
_Assigned_chem_shift_list.Sf_category assigned_chemical_shifts
_Assigned_chem_shift_list.Sf_framecode shift_set_1
_Assigned_chem_shift_list.Entry_ID 5101
_Assigned_chem_shift_list.ID 1
_Assigned_chem_shift_list.Sample_condition_list_ID 1
_Assigned_chem_shift_list.Sample_condition_list_label $conditions_1
_Assigned_chem_shift_list.Chem_shift_reference_ID 1
_Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference
_Assigned_chem_shift_list.Chem_shift_1H_err .
_Assigned_chem_shift_list.Chem_shift_13C_err .
_Assigned_chem_shift_list.Chem_shift_15N_err .
_Assigned_chem_shift_list.Chem_shift_31P_err .
_Assigned_chem_shift_list.Chem_shift_2H_err .
_Assigned_chem_shift_list.Chem_shift_19F_err .
_Assigned_chem_shift_list.Error_derivation_method .
_Assigned_chem_shift_list.Details .
_Assigned_chem_shift_list.Text_data_format .
_Assigned_chem_shift_list.Text_data .
loop_
_Chem_shift_experiment.Experiment_ID
_Chem_shift_experiment.Experiment_name
_Chem_shift_experiment.Sample_ID
_Chem_shift_experiment.Sample_label
_Chem_shift_experiment.Sample_state
_Chem_shift_experiment.Entry_ID
_Chem_shift_experiment.Assigned_chem_shift_list_ID
1 '3D 1H-1H-15N NOESY' . . . 5101 1
2 '3D 1H-1H-15N TOCSY' . . . 5101 1
3 '3D 13C-1H-1H NOESY' . . . 5101 1
4 '3D 1H-13C-1H HCCH-TOCSY' . . . 5101 1
5 '3D CBCA(CO)NH' . . . 5101 1
6 '3D HNCA' . . . 5101 1
7 '3D HN(CO)CA' . . . 5101 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 GLY CA C 13 43.61 0.05 . 1 . . . . -1 . . . 5101 1
2 . 1 1 1 1 GLY HA2 H 1 3.89 0.01 . 2 . . . . -1 . . . 5101 1
3 . 1 1 1 1 GLY HA3 H 1 3.76 0.01 . 2 . . . . -1 . . . 5101 1
4 . 1 1 2 2 SER CA C 13 58.41 0.05 . 1 . . . . 0 . . . 5101 1
5 . 1 1 2 2 SER CB C 13 64.28 0.05 . 1 . . . . 0 . . . 5101 1
6 . 1 1 2 2 SER HA H 1 4.58 0.01 . 1 . . . . 0 . . . 5101 1
7 . 1 1 2 2 SER HB2 H 1 3.82 0.01 . 1 . . . . 0 . . . 5101 1
8 . 1 1 2 2 SER HB3 H 1 3.82 0.01 . 1 . . . . 0 . . . 5101 1
9 . 1 1 2 2 SER N N 15 115.16 0.05 . 1 . . . . 0 . . . 5101 1
10 . 1 1 3 3 MET CB C 13 35.66 0.05 . 1 . . . . 1 . . . 5101 1
11 . 1 1 3 3 MET CE C 13 17.70 0.05 . 1 . . . . 1 . . . 5101 1
12 . 1 1 3 3 MET CG C 13 31.17 0.05 . 1 . . . . 1 . . . 5101 1
13 . 1 1 3 3 MET HA H 1 4.72 0.01 . 1 . . . . 1 . . . 5101 1
14 . 1 1 3 3 MET HB2 H 1 1.93 0.01 . 1 . . . . 1 . . . 5101 1
15 . 1 1 3 3 MET HB3 H 1 1.93 0.01 . 1 . . . . 1 . . . 5101 1
16 . 1 1 3 3 MET HE1 H 1 1.97 0.01 . 1 . . . . 1 . . . 5101 1
17 . 1 1 3 3 MET HE2 H 1 1.97 0.01 . 1 . . . . 1 . . . 5101 1
18 . 1 1 3 3 MET HE3 H 1 1.97 0.01 . 1 . . . . 1 . . . 5101 1
19 . 1 1 3 3 MET HG2 H 1 2.31 0.01 . 1 . . . . 1 . . . 5101 1
20 . 1 1 3 3 MET HG3 H 1 2.31 0.01 . 1 . . . . 1 . . . 5101 1
21 . 1 1 3 3 MET H H 1 8.94 0.01 . 1 . . . . 1 . . . 5101 1
22 . 1 1 3 3 MET N N 15 121.26 0.05 . 1 . . . . 1 . . . 5101 1
23 . 1 1 4 4 GLN CA C 13 55.30 0.05 . 1 . . . . 2 . . . 5101 1
24 . 1 1 4 4 GLN CB C 13 30.59 0.05 . 1 . . . . 2 . . . 5101 1
25 . 1 1 4 4 GLN CG C 13 34.45 0.05 . 1 . . . . 2 . . . 5101 1
26 . 1 1 4 4 GLN HA H 1 4.88 0.01 . 1 . . . . 2 . . . 5101 1
27 . 1 1 4 4 GLN HB2 H 1 1.83 0.01 . 2 . . . . 2 . . . 5101 1
28 . 1 1 4 4 GLN HB3 H 1 1.60 0.01 . 2 . . . . 2 . . . 5101 1
29 . 1 1 4 4 GLN HE21 H 1 6.78 0.01 . 2 . . . . 2 . . . 5101 1
30 . 1 1 4 4 GLN HE22 H 1 7.46 0.01 . 2 . . . . 2 . . . 5101 1
31 . 1 1 4 4 GLN HG2 H 1 2.17 0.01 . 2 . . . . 2 . . . 5101 1
32 . 1 1 4 4 GLN HG3 H 1 1.90 0.01 . 2 . . . . 2 . . . 5101 1
33 . 1 1 4 4 GLN H H 1 8.42 0.01 . 1 . . . . 2 . . . 5101 1
34 . 1 1 4 4 GLN N N 15 121.47 0.05 . 1 . . . . 2 . . . 5101 1
35 . 1 1 5 5 ILE CA C 13 58.80 0.05 . 1 . . . . 3 . . . 5101 1
36 . 1 1 5 5 ILE CB C 13 40.81 0.05 . 1 . . . . 3 . . . 5101 1
37 . 1 1 5 5 ILE CD1 C 13 15.37 0.05 . 2 . . . . 3 . . . 5101 1
38 . 1 1 5 5 ILE CG1 C 13 20.70 0.05 . 2 . . . . 3 . . . 5101 1
39 . 1 1 5 5 ILE CG2 C 13 20.10 0.05 . 1 . . . . 3 . . . 5101 1
40 . 1 1 5 5 ILE HA H 1 4.58 0.01 . 1 . . . . 3 . . . 5101 1
41 . 1 1 5 5 ILE HB H 1 1.88 0.01 . 1 . . . . 3 . . . 5101 1
42 . 1 1 5 5 ILE HD11 H 1 0.44 0.01 . 1 . . . . 3 . . . 5101 1
43 . 1 1 5 5 ILE HD12 H 1 0.44 0.01 . 1 . . . . 3 . . . 5101 1
44 . 1 1 5 5 ILE HD13 H 1 0.44 0.01 . 1 . . . . 3 . . . 5101 1
45 . 1 1 5 5 ILE HG12 H 1 1.19 0.01 . 2 . . . . 3 . . . 5101 1
46 . 1 1 5 5 ILE HG13 H 1 0.87 0.01 . 2 . . . . 3 . . . 5101 1
47 . 1 1 5 5 ILE HG21 H 1 0.84 0.01 . 1 . . . . 3 . . . 5101 1
48 . 1 1 5 5 ILE HG22 H 1 0.84 0.01 . 1 . . . . 3 . . . 5101 1
49 . 1 1 5 5 ILE HG23 H 1 0.84 0.01 . 1 . . . . 3 . . . 5101 1
50 . 1 1 5 5 ILE H H 1 8.67 0.01 . 1 . . . . 3 . . . 5101 1
51 . 1 1 5 5 ILE N N 15 117.51 0.05 . 1 . . . . 3 . . . 5101 1
52 . 1 1 6 6 PHE CA C 13 56.40 0.05 . 1 . . . . 4 . . . 5101 1
53 . 1 1 6 6 PHE CB C 13 41.38 0.05 . 1 . . . . 4 . . . 5101 1
54 . 1 1 6 6 PHE CD1 C 13 130.70 0.05 . 1 . . . . 4 . . . 5101 1
55 . 1 1 6 6 PHE CD2 C 13 130.70 0.05 . 1 . . . . 4 . . . 5101 1
56 . 1 1 6 6 PHE CE1 C 13 130.79 0.05 . 1 . . . . 4 . . . 5101 1
57 . 1 1 6 6 PHE CE2 C 13 130.79 0.05 . 1 . . . . 4 . . . 5101 1
58 . 1 1 6 6 PHE HA H 1 5.26 0.01 . 1 . . . . 4 . . . 5101 1
59 . 1 1 6 6 PHE HB2 H 1 2.78 0.01 . 2 . . . . 4 . . . 5101 1
60 . 1 1 6 6 PHE HB3 H 1 3.01 0.01 . 2 . . . . 4 . . . 5101 1
61 . 1 1 6 6 PHE HD1 H 1 7.12 0.01 . 1 . . . . 4 . . . 5101 1
62 . 1 1 6 6 PHE HD2 H 1 7.12 0.01 . 1 . . . . 4 . . . 5101 1
63 . 1 1 6 6 PHE HE1 H 1 7.24 0.01 . 1 . . . . 4 . . . 5101 1
64 . 1 1 6 6 PHE HE2 H 1 7.24 0.01 . 1 . . . . 4 . . . 5101 1
65 . 1 1 6 6 PHE H H 1 8.51 0.01 . 1 . . . . 4 . . . 5101 1
66 . 1 1 6 6 PHE N N 15 119.86 0.05 . 1 . . . . 4 . . . 5101 1
67 . 1 1 7 7 VAL CA C 13 60.28 0.05 . 1 . . . . 5 . . . 5101 1
68 . 1 1 7 7 VAL CB C 13 34.16 0.05 . 1 . . . . 5 . . . 5101 1
69 . 1 1 7 7 VAL CG1 C 13 21.13 0.05 . 1 . . . . 5 . . . 5101 1
70 . 1 1 7 7 VAL CG2 C 13 21.13 0.05 . 1 . . . . 5 . . . 5101 1
71 . 1 1 7 7 VAL HA H 1 5.00 0.01 . 1 . . . . 5 . . . 5101 1
72 . 1 1 7 7 VAL HB H 1 1.90 0.01 . 1 . . . . 5 . . . 5101 1
73 . 1 1 7 7 VAL HG11 H 1 0.66 0.01 . 1 . . . . 5 . . . 5101 1
74 . 1 1 7 7 VAL HG12 H 1 0.66 0.01 . 1 . . . . 5 . . . 5101 1
75 . 1 1 7 7 VAL HG13 H 1 0.66 0.01 . 1 . . . . 5 . . . 5101 1
76 . 1 1 7 7 VAL HG21 H 1 0.66 0.01 . 1 . . . . 5 . . . 5101 1
77 . 1 1 7 7 VAL HG22 H 1 0.66 0.01 . 1 . . . . 5 . . . 5101 1
78 . 1 1 7 7 VAL HG23 H 1 0.66 0.01 . 1 . . . . 5 . . . 5101 1
79 . 1 1 7 7 VAL H H 1 9.26 0.01 . 1 . . . . 5 . . . 5101 1
80 . 1 1 7 7 VAL N N 15 122.14 0.05 . 1 . . . . 5 . . . 5101 1
81 . 1 1 8 8 LYS CA C 13 54.65 0.05 . 1 . . . . 6 . . . 5101 1
82 . 1 1 8 8 LYS CB C 13 32.84 0.05 . 1 . . . . 6 . . . 5101 1
83 . 1 1 8 8 LYS CD C 13 28.98 0.05 . 1 . . . . 6 . . . 5101 1
84 . 1 1 8 8 LYS CG C 13 24.98 0.05 . 1 . . . . 6 . . . 5101 1
85 . 1 1 8 8 LYS HA H 1 5.09 0.01 . 1 . . . . 6 . . . 5101 1
86 . 1 1 8 8 LYS HB2 H 1 1.85 0.01 . 2 . . . . 6 . . . 5101 1
87 . 1 1 8 8 LYS HB3 H 1 1.65 0.01 . 2 . . . . 6 . . . 5101 1
88 . 1 1 8 8 LYS HD2 H 1 1.59 0.01 . 1 . . . . 6 . . . 5101 1
89 . 1 1 8 8 LYS HD3 H 1 1.59 0.01 . 1 . . . . 6 . . . 5101 1
90 . 1 1 8 8 LYS HE2 H 1 2.83 0.01 . 1 . . . . 6 . . . 5101 1
91 . 1 1 8 8 LYS HE3 H 1 2.83 0.01 . 1 . . . . 6 . . . 5101 1
92 . 1 1 8 8 LYS HG2 H 1 1.39 0.01 . 1 . . . . 6 . . . 5101 1
93 . 1 1 8 8 LYS HG3 H 1 1.39 0.01 . 1 . . . . 6 . . . 5101 1
94 . 1 1 8 8 LYS H H 1 8.71 0.01 . 1 . . . . 6 . . . 5101 1
95 . 1 1 8 8 LYS N N 15 127.14 0.05 . 1 . . . . 6 . . . 5101 1
96 . 1 1 9 9 THR CA C 13 61.12 0.05 . 1 . . . . 7 . . . 5101 1
97 . 1 1 9 9 THR CG2 C 13 22.88 0.05 . 1 . . . . 7 . . . 5101 1
98 . 1 1 9 9 THR HA H 1 4.33 0.01 . 1 . . . . 7 . . . 5101 1
99 . 1 1 9 9 THR HB H 1 4.70 0.01 . 1 . . . . 7 . . . 5101 1
100 . 1 1 9 9 THR HG21 H 1 1.15 0.01 . 1 . . . . 7 . . . 5101 1
101 . 1 1 9 9 THR HG22 H 1 1.15 0.01 . 1 . . . . 7 . . . 5101 1
102 . 1 1 9 9 THR HG23 H 1 1.15 0.01 . 1 . . . . 7 . . . 5101 1
103 . 1 1 9 9 THR H H 1 8.75 0.01 . 1 . . . . 7 . . . 5101 1
104 . 1 1 9 9 THR N N 15 114.88 0.05 . 1 . . . . 7 . . . 5101 1
105 . 1 1 10 10 LEU CA C 13 57.45 0.05 . 1 . . . . 8 . . . 5101 1
106 . 1 1 10 10 LEU CB C 13 41.10 0.05 . 1 . . . . 8 . . . 5101 1
107 . 1 1 10 10 LEU CD1 C 13 25.15 0.05 . 2 . . . . 8 . . . 5101 1
108 . 1 1 10 10 LEU CD2 C 13 23.03 0.05 . 2 . . . . 8 . . . 5101 1
109 . 1 1 10 10 LEU CG C 13 27.53 0.05 . 1 . . . . 8 . . . 5101 1
110 . 1 1 10 10 LEU HA H 1 4.17 0.01 . 1 . . . . 8 . . . 5101 1
111 . 1 1 10 10 LEU HB2 H 1 1.82 0.01 . 2 . . . . 8 . . . 5101 1
112 . 1 1 10 10 LEU HB3 H 1 1.65 0.01 . 2 . . . . 8 . . . 5101 1
113 . 1 1 10 10 LEU HD11 H 1 0.93 0.01 . 2 . . . . 8 . . . 5101 1
114 . 1 1 10 10 LEU HD12 H 1 0.93 0.01 . 2 . . . . 8 . . . 5101 1
115 . 1 1 10 10 LEU HD13 H 1 0.93 0.01 . 2 . . . . 8 . . . 5101 1
116 . 1 1 10 10 LEU HD21 H 1 0.84 0.01 . 2 . . . . 8 . . . 5101 1
117 . 1 1 10 10 LEU HD22 H 1 0.84 0.01 . 2 . . . . 8 . . . 5101 1
118 . 1 1 10 10 LEU HD23 H 1 0.84 0.01 . 2 . . . . 8 . . . 5101 1
119 . 1 1 10 10 LEU HG H 1 1.67 0.01 . 1 . . . . 8 . . . 5101 1
120 . 1 1 10 10 LEU H H 1 9.03 0.01 . 1 . . . . 8 . . . 5101 1
121 . 1 1 10 10 LEU N N 15 119.50 0.05 . 1 . . . . 8 . . . 5101 1
122 . 1 1 11 11 THR CA C 13 61.41 0.05 . 1 . . . . 9 . . . 5101 1
123 . 1 1 11 11 THR CB C 13 69.21 0.05 . 1 . . . . 9 . . . 5101 1
124 . 1 1 11 11 THR CG2 C 13 22.08 0.05 . 1 . . . . 9 . . . 5101 1
125 . 1 1 11 11 THR HA H 1 4.39 0.01 . 1 . . . . 9 . . . 5101 1
126 . 1 1 11 11 THR HB H 1 4.52 0.01 . 1 . . . . 9 . . . 5101 1
127 . 1 1 11 11 THR HG21 H 1 1.21 0.01 . 1 . . . . 9 . . . 5101 1
128 . 1 1 11 11 THR HG22 H 1 1.21 0.01 . 1 . . . . 9 . . . 5101 1
129 . 1 1 11 11 THR HG23 H 1 1.21 0.01 . 1 . . . . 9 . . . 5101 1
130 . 1 1 11 11 THR H H 1 7.57 0.01 . 1 . . . . 9 . . . 5101 1
131 . 1 1 11 11 THR N N 15 105.51 0.05 . 1 . . . . 9 . . . 5101 1
132 . 1 1 12 12 GLY CA C 13 45.90 0.05 . 1 . . . . 10 . . . 5101 1
133 . 1 1 12 12 GLY HA2 H 1 4.27 0.01 . 2 . . . . 10 . . . 5101 1
134 . 1 1 12 12 GLY HA3 H 1 3.60 0.01 . 2 . . . . 10 . . . 5101 1
135 . 1 1 12 12 GLY H H 1 7.78 0.01 . 1 . . . . 10 . . . 5101 1
136 . 1 1 12 12 GLY N N 15 109.47 0.05 . 1 . . . . 10 . . . 5101 1
137 . 1 1 13 13 LYS CA C 13 55.58 0.05 . 1 . . . . 11 . . . 5101 1
138 . 1 1 13 13 LYS CB C 13 33.79 0.05 . 1 . . . . 11 . . . 5101 1
139 . 1 1 13 13 LYS CD C 13 29.12 0.05 . 1 . . . . 11 . . . 5101 1
140 . 1 1 13 13 LYS CG C 13 24.95 0.05 . 1 . . . . 11 . . . 5101 1
141 . 1 1 13 13 LYS HA H 1 4.44 0.01 . 1 . . . . 11 . . . 5101 1
142 . 1 1 13 13 LYS HB2 H 1 1.66 0.01 . 1 . . . . 11 . . . 5101 1
143 . 1 1 13 13 LYS HB3 H 1 1.66 0.01 . 1 . . . . 11 . . . 5101 1
144 . 1 1 13 13 LYS HD2 H 1 1.60 0.01 . 1 . . . . 11 . . . 5101 1
145 . 1 1 13 13 LYS HD3 H 1 1.60 0.01 . 1 . . . . 11 . . . 5101 1
146 . 1 1 13 13 LYS HE2 H 1 2.92 0.01 . 1 . . . . 11 . . . 5101 1
147 . 1 1 13 13 LYS HE3 H 1 2.92 0.01 . 1 . . . . 11 . . . 5101 1
148 . 1 1 13 13 LYS HG2 H 1 1.27 0.01 . 1 . . . . 11 . . . 5101 1
149 . 1 1 13 13 LYS HG3 H 1 1.27 0.01 . 1 . . . . 11 . . . 5101 1
150 . 1 1 13 13 LYS H H 1 7.31 0.01 . 1 . . . . 11 . . . 5101 1
151 . 1 1 13 13 LYS N N 15 120.59 0.05 . 1 . . . . 11 . . . 5101 1
152 . 1 1 14 14 THR CA C 13 62.33 0.05 . 1 . . . . 12 . . . 5101 1
153 . 1 1 14 14 THR CB C 13 69.60 0.05 . 1 . . . . 12 . . . 5101 1
154 . 1 1 14 14 THR CG2 C 13 21.98 0.05 . 1 . . . . 12 . . . 5101 1
155 . 1 1 14 14 THR HA H 1 5.33 0.01 . 1 . . . . 12 . . . 5101 1
156 . 1 1 14 14 THR HB H 1 3.97 0.01 . 1 . . . . 12 . . . 5101 1
157 . 1 1 14 14 THR HG21 H 1 1.14 0.01 . 1 . . . . 12 . . . 5101 1
158 . 1 1 14 14 THR HG22 H 1 1.14 0.01 . 1 . . . . 12 . . . 5101 1
159 . 1 1 14 14 THR HG23 H 1 1.14 0.01 . 1 . . . . 12 . . . 5101 1
160 . 1 1 14 14 THR H H 1 8.65 0.01 . 1 . . . . 12 . . . 5101 1
161 . 1 1 14 14 THR N N 15 119.66 0.05 . 1 . . . . 12 . . . 5101 1
162 . 1 1 15 15 ILE CB C 13 41.78 0.05 . 1 . . . . 13 . . . 5101 1
163 . 1 1 15 15 ILE CD1 C 13 14.37 0.05 . 1 . . . . 13 . . . 5101 1
164 . 1 1 15 15 ILE CG1 C 13 26.93 0.05 . 1 . . . . 13 . . . 5101 1
165 . 1 1 15 15 ILE CG2 C 13 18.82 0.05 . 1 . . . . 13 . . . 5101 1
166 . 1 1 15 15 ILE HA H 1 4.72 0.01 . 1 . . . . 13 . . . 5101 1
167 . 1 1 15 15 ILE HB H 1 1.93 0.01 . 1 . . . . 13 . . . 5101 1
168 . 1 1 15 15 ILE HD11 H 1 0.68 0.01 . 1 . . . . 13 . . . 5101 1
169 . 1 1 15 15 ILE HD12 H 1 0.68 0.01 . 1 . . . . 13 . . . 5101 1
170 . 1 1 15 15 ILE HD13 H 1 0.68 0.01 . 1 . . . . 13 . . . 5101 1
171 . 1 1 15 15 ILE HG12 H 1 1.23 0.01 . 2 . . . . 13 . . . 5101 1
172 . 1 1 15 15 ILE HG13 H 1 1.07 0.01 . 2 . . . . 13 . . . 5101 1
173 . 1 1 15 15 ILE HG21 H 1 0.83 0.01 . 1 . . . . 13 . . . 5101 1
174 . 1 1 15 15 ILE HG22 H 1 0.83 0.01 . 1 . . . . 13 . . . 5101 1
175 . 1 1 15 15 ILE HG23 H 1 0.83 0.01 . 1 . . . . 13 . . . 5101 1
176 . 1 1 15 15 ILE H H 1 9.24 0.01 . 1 . . . . 13 . . . 5101 1
177 . 1 1 15 15 ILE N N 15 124.29 0.05 . 1 . . . . 13 . . . 5101 1
178 . 1 1 16 16 THR CA C 13 60.19 0.05 . 1 . . . . 14 . . . 5101 1
179 . 1 1 16 16 THR CB C 13 70.87 0.05 . 1 . . . . 14 . . . 5101 1
180 . 1 1 16 16 THR CG2 C 13 22.97 0.05 . 1 . . . . 14 . . . 5101 1
181 . 1 1 16 16 THR HA H 1 5.15 0.01 . 1 . . . . 14 . . . 5101 1
182 . 1 1 16 16 THR HB H 1 3.83 0.01 . 1 . . . . 14 . . . 5101 1
183 . 1 1 16 16 THR HG21 H 1 0.79 0.01 . 1 . . . . 14 . . . 5101 1
184 . 1 1 16 16 THR HG22 H 1 0.79 0.01 . 1 . . . . 14 . . . 5101 1
185 . 1 1 16 16 THR HG23 H 1 0.79 0.01 . 1 . . . . 14 . . . 5101 1
186 . 1 1 16 16 THR H H 1 8.26 0.01 . 1 . . . . 14 . . . 5101 1
187 . 1 1 16 16 THR N N 15 113.92 0.05 . 1 . . . . 14 . . . 5101 1
188 . 1 1 17 17 LEU CA C 13 53.68 0.05 . 1 . . . . 15 . . . 5101 1
189 . 1 1 17 17 LEU CB C 13 46.03 0.05 . 1 . . . . 15 . . . 5101 1
190 . 1 1 17 17 LEU CD1 C 13 24.82 0.05 . 2 . . . . 15 . . . 5101 1
191 . 1 1 17 17 LEU CD2 C 13 25.62 0.05 . 2 . . . . 15 . . . 5101 1
192 . 1 1 17 17 LEU CG C 13 27.30 0.05 . 1 . . . . 15 . . . 5101 1
193 . 1 1 17 17 LEU HA H 1 4.58 0.01 . 1 . . . . 15 . . . 5101 1
194 . 1 1 17 17 LEU HB2 H 1 1.35 0.01 . 2 . . . . 15 . . . 5101 1
195 . 1 1 17 17 LEU HB3 H 1 1.14 0.01 . 2 . . . . 15 . . . 5101 1
196 . 1 1 17 17 LEU HD11 H 1 0.66 0.01 . 2 . . . . 15 . . . 5101 1
197 . 1 1 17 17 LEU HD12 H 1 0.66 0.01 . 2 . . . . 15 . . . 5101 1
198 . 1 1 17 17 LEU HD13 H 1 0.66 0.01 . 2 . . . . 15 . . . 5101 1
199 . 1 1 17 17 LEU HD21 H 1 0.62 0.01 . 2 . . . . 15 . . . 5101 1
200 . 1 1 17 17 LEU HD22 H 1 0.62 0.01 . 2 . . . . 15 . . . 5101 1
201 . 1 1 17 17 LEU HD23 H 1 0.62 0.01 . 2 . . . . 15 . . . 5101 1
202 . 1 1 17 17 LEU HG H 1 1.38 0.01 . 1 . . . . 15 . . . 5101 1
203 . 1 1 17 17 LEU H H 1 8.30 0.01 . 1 . . . . 15 . . . 5101 1
204 . 1 1 17 17 LEU N N 15 123.19 0.05 . 1 . . . . 15 . . . 5101 1
205 . 1 1 18 18 GLU CA C 13 55.48 0.05 . 1 . . . . 16 . . . 5101 1
206 . 1 1 18 18 GLU CB C 13 30.83 0.05 . 1 . . . . 16 . . . 5101 1
207 . 1 1 18 18 GLU CG C 13 36.62 0.05 . 1 . . . . 16 . . . 5101 1
208 . 1 1 18 18 GLU HA H 1 5.03 0.01 . 1 . . . . 16 . . . 5101 1
209 . 1 1 18 18 GLU HB2 H 1 1.83 0.01 . 1 . . . . 16 . . . 5101 1
210 . 1 1 18 18 GLU HB3 H 1 1.83 0.01 . 1 . . . . 16 . . . 5101 1
211 . 1 1 18 18 GLU HG2 H 1 2.17 0.01 . 2 . . . . 16 . . . 5101 1
212 . 1 1 18 18 GLU HG3 H 1 2.04 0.01 . 2 . . . . 16 . . . 5101 1
213 . 1 1 18 18 GLU H H 1 8.30 0.01 . 1 . . . . 16 . . . 5101 1
214 . 1 1 18 18 GLU N N 15 121.07 0.05 . 1 . . . . 16 . . . 5101 1
215 . 1 1 19 19 VAL CB C 13 34.62 0.05 . 1 . . . . 17 . . . 5101 1
216 . 1 1 19 19 VAL CG1 C 13 32.27 0.05 . 2 . . . . 17 . . . 5101 1
217 . 1 1 19 19 VAL CG2 C 13 19.29 0.05 . 2 . . . . 17 . . . 5101 1
218 . 1 1 19 19 VAL HA H 1 4.69 0.01 . 1 . . . . 17 . . . 5101 1
219 . 1 1 19 19 VAL HB H 1 2.53 0.01 . 1 . . . . 17 . . . 5101 1
220 . 1 1 19 19 VAL HG11 H 1 0.72 0.01 . 2 . . . . 17 . . . 5101 1
221 . 1 1 19 19 VAL HG12 H 1 0.72 0.01 . 2 . . . . 17 . . . 5101 1
222 . 1 1 19 19 VAL HG13 H 1 0.72 0.01 . 2 . . . . 17 . . . 5101 1
223 . 1 1 19 19 VAL HG21 H 1 0.58 0.01 . 2 . . . . 17 . . . 5101 1
224 . 1 1 19 19 VAL HG22 H 1 0.58 0.01 . 2 . . . . 17 . . . 5101 1
225 . 1 1 19 19 VAL HG23 H 1 0.58 0.01 . 2 . . . . 17 . . . 5101 1
226 . 1 1 19 19 VAL H H 1 8.65 0.01 . 1 . . . . 17 . . . 5101 1
227 . 1 1 19 19 VAL N N 15 116.00 0.05 . 1 . . . . 17 . . . 5101 1
228 . 1 1 20 20 GLU CA C 13 53.03 0.05 . 1 . . . . 18 . . . 5101 1
229 . 1 1 20 20 GLU CB C 13 30.68 0.05 . 1 . . . . 18 . . . 5101 1
230 . 1 1 20 20 GLU CG C 13 35.63 0.05 . 1 . . . . 18 . . . 5101 1
231 . 1 1 20 20 GLU HA H 1 4.91 0.01 . 1 . . . . 18 . . . 5101 1
232 . 1 1 20 20 GLU HB2 H 1 2.04 0.01 . 2 . . . . 18 . . . 5101 1
233 . 1 1 20 20 GLU HB3 H 1 1.74 0.01 . 2 . . . . 18 . . . 5101 1
234 . 1 1 20 20 GLU HG2 H 1 2.31 0.01 . 1 . . . . 18 . . . 5101 1
235 . 1 1 20 20 GLU HG3 H 1 2.31 0.01 . 1 . . . . 18 . . . 5101 1
236 . 1 1 20 20 GLU H H 1 8.55 0.01 . 2 . . . . 18 . . . 5101 1
237 . 1 1 20 20 GLU N N 15 120.16 0.05 . 1 . . . . 18 . . . 5101 1
238 . 1 1 21 21 PRO CA C 13 64.73 0.05 . 1 . . . . 19 . . . 5101 1
239 . 1 1 21 21 PRO CB C 13 32.06 0.05 . 1 . . . . 19 . . . 5101 1
240 . 1 1 21 21 PRO CD C 13 50.73 0.05 . 1 . . . . 19 . . . 5101 1
241 . 1 1 21 21 PRO CG C 13 27.79 0.05 . 1 . . . . 19 . . . 5101 1
242 . 1 1 21 21 PRO HA H 1 4.18 0.01 . 1 . . . . 19 . . . 5101 1
243 . 1 1 21 21 PRO HB2 H 1 2.05 0.01 . 2 . . . . 19 . . . 5101 1
244 . 1 1 21 21 PRO HB3 H 1 2.32 0.01 . 2 . . . . 19 . . . 5101 1
245 . 1 1 21 21 PRO HD2 H 1 3.74 0.01 . 2 . . . . 19 . . . 5101 1
246 . 1 1 21 21 PRO HD3 H 1 3.73 0.01 . 2 . . . . 19 . . . 5101 1
247 . 1 1 21 21 PRO HG2 H 1 2.18 0.01 . 2 . . . . 19 . . . 5101 1
248 . 1 1 21 21 PRO HG3 H 1 1.97 0.01 . 2 . . . . 19 . . . 5101 1
249 . 1 1 22 22 SER CA C 13 57.48 0.05 . 1 . . . . 20 . . . 5101 1
250 . 1 1 22 22 SER CB C 13 63.29 0.05 . 1 . . . . 20 . . . 5101 1
251 . 1 1 22 22 SER HA H 1 4.35 0.01 . 1 . . . . 20 . . . 5101 1
252 . 1 1 22 22 SER HB2 H 1 4.16 0.01 . 2 . . . . 20 . . . 5101 1
253 . 1 1 22 22 SER HB3 H 1 3.78 0.01 . 2 . . . . 20 . . . 5101 1
254 . 1 1 22 22 SER H H 1 7.12 0.01 . 1 . . . . 20 . . . 5101 1
255 . 1 1 22 22 SER N N 15 104.57 0.05 . 1 . . . . 20 . . . 5101 1
256 . 1 1 23 23 ASP CB C 13 41.12 0.05 . 1 . . . . 21 . . . 5101 1
257 . 1 1 23 23 ASP HA H 1 4.74 0.01 . 1 . . . . 21 . . . 5101 1
258 . 1 1 23 23 ASP HB2 H 1 2.88 0.01 . 2 . . . . 21 . . . 5101 1
259 . 1 1 23 23 ASP HB3 H 1 2.50 0.01 . 2 . . . . 21 . . . 5101 1
260 . 1 1 23 23 ASP H H 1 7.89 0.01 . 1 . . . . 21 . . . 5101 1
261 . 1 1 23 23 ASP N N 15 123.85 0.05 . 1 . . . . 21 . . . 5101 1
262 . 1 1 24 24 THR CA C 13 59.61 0.05 . 1 . . . . 22 . . . 5101 1
263 . 1 1 24 24 THR CB C 13 71.08 0.05 . 1 . . . . 22 . . . 5101 1
264 . 1 1 24 24 THR CG2 C 13 22.47 0.05 . 1 . . . . 22 . . . 5101 1
265 . 1 1 24 24 THR HA H 1 4.84 0.01 . 1 . . . . 22 . . . 5101 1
266 . 1 1 24 24 THR HB H 1 4.60 0.01 . 1 . . . . 22 . . . 5101 1
267 . 1 1 24 24 THR HG21 H 1 1.23 0.01 . 1 . . . . 22 . . . 5101 1
268 . 1 1 24 24 THR HG22 H 1 1.23 0.01 . 1 . . . . 22 . . . 5101 1
269 . 1 1 24 24 THR HG23 H 1 1.23 0.01 . 1 . . . . 22 . . . 5101 1
270 . 1 1 24 24 THR H H 1 8.17 0.01 . 1 . . . . 22 . . . 5101 1
271 . 1 1 24 24 THR N N 15 109.09 0.05 . 1 . . . . 22 . . . 5101 1
272 . 1 1 25 25 ILE CA C 13 65.13 0.05 . 1 . . . . 23 . . . 5101 1
273 . 1 1 25 25 ILE CB C 13 36.70 0.05 . 1 . . . . 23 . . . 5101 1
274 . 1 1 25 25 ILE CD1 C 13 11.93 0.05 . 1 . . . . 23 . . . 5101 1
275 . 1 1 25 25 ILE CG1 C 13 28.50 0.05 . 1 . . . . 23 . . . 5101 1
276 . 1 1 25 25 ILE CG2 C 13 18.23 0.05 . 1 . . . . 23 . . . 5101 1
277 . 1 1 25 25 ILE HA H 1 3.62 0.01 . 1 . . . . 23 . . . 5101 1
278 . 1 1 25 25 ILE HB H 1 2.21 0.01 . 1 . . . . 23 . . . 5101 1
279 . 1 1 25 25 ILE HD11 H 1 0.83 0.01 . 1 . . . . 23 . . . 5101 1
280 . 1 1 25 25 ILE HD12 H 1 0.83 0.01 . 1 . . . . 23 . . . 5101 1
281 . 1 1 25 25 ILE HD13 H 1 0.83 0.01 . 1 . . . . 23 . . . 5101 1
282 . 1 1 25 25 ILE HG12 H 1 1.27 0.01 . 2 . . . . 23 . . . 5101 1
283 . 1 1 25 25 ILE HG13 H 1 1.60 0.01 . 2 . . . . 23 . . . 5101 1
284 . 1 1 25 25 ILE HG21 H 1 0.91 0.01 . 1 . . . . 23 . . . 5101 1
285 . 1 1 25 25 ILE HG22 H 1 0.91 0.01 . 1 . . . . 23 . . . 5101 1
286 . 1 1 25 25 ILE HG23 H 1 0.91 0.01 . 1 . . . . 23 . . . 5101 1
287 . 1 1 25 25 ILE H H 1 8.48 0.01 . 1 . . . . 23 . . . 5101 1
288 . 1 1 25 25 ILE N N 15 120.45 0.05 . 1 . . . . 23 . . . 5101 1
289 . 1 1 26 26 GLU CA C 13 59.41 0.05 . 1 . . . . 24 . . . 5101 1
290 . 1 1 26 26 GLU CB C 13 29.43 0.05 . 1 . . . . 24 . . . 5101 1
291 . 1 1 26 26 GLU CG C 13 35.16 0.05 . 1 . . . . 24 . . . 5101 1
292 . 1 1 26 26 GLU HA H 1 3.95 0.01 . 1 . . . . 24 . . . 5101 1
293 . 1 1 26 26 GLU HB2 H 1 2.01 0.01 . 2 . . . . 24 . . . 5101 1
294 . 1 1 26 26 GLU HB3 H 1 1.87 0.01 . 2 . . . . 24 . . . 5101 1
295 . 1 1 26 26 GLU HG2 H 1 2.17 0.01 . 1 . . . . 24 . . . 5101 1
296 . 1 1 26 26 GLU HG3 H 1 2.17 0.01 . 1 . . . . 24 . . . 5101 1
297 . 1 1 26 26 GLU H H 1 8.69 0.01 . 1 . . . . 24 . . . 5101 1
298 . 1 1 26 26 GLU N N 15 116.72 0.05 . 1 . . . . 24 . . . 5101 1
299 . 1 1 27 27 ASN CA C 13 55.97 0.05 . 1 . . . . 25 . . . 5101 1
300 . 1 1 27 27 ASN CB C 13 38.53 0.05 . 1 . . . . 25 . . . 5101 1
301 . 1 1 27 27 ASN HA H 1 4.51 0.01 . 1 . . . . 25 . . . 5101 1
302 . 1 1 27 27 ASN HB2 H 1 3.06 0.01 . 2 . . . . 25 . . . 5101 1
303 . 1 1 27 27 ASN HB3 H 1 2.81 0.01 . 2 . . . . 25 . . . 5101 1
304 . 1 1 27 27 ASN HD22 H 1 8.02 0.01 . 2 . . . . 25 . . . 5101 1
305 . 1 1 27 27 ASN H H 1 7.87 0.01 . 1 . . . . 25 . . . 5101 1
306 . 1 1 27 27 ASN N N 15 120.19 0.05 . 1 . . . . 25 . . . 5101 1
307 . 1 1 28 28 VAL CA C 13 67.00 0.05 . 1 . . . . 26 . . . 5101 1
308 . 1 1 28 28 VAL CB C 13 31.16 0.05 . 1 . . . . 26 . . . 5101 1
309 . 1 1 28 28 VAL CG1 C 13 23.67 0.05 . 2 . . . . 26 . . . 5101 1
310 . 1 1 28 28 VAL CG2 C 13 23.71 0.05 . 2 . . . . 26 . . . 5101 1
311 . 1 1 28 28 VAL HA H 1 3.50 0.01 . 1 . . . . 26 . . . 5101 1
312 . 1 1 28 28 VAL HB H 1 2.14 0.01 . 1 . . . . 26 . . . 5101 1
313 . 1 1 28 28 VAL HG11 H 1 1.06 0.01 . 2 . . . . 26 . . . 5101 1
314 . 1 1 28 28 VAL HG12 H 1 1.06 0.01 . 2 . . . . 26 . . . 5101 1
315 . 1 1 28 28 VAL HG13 H 1 1.06 0.01 . 2 . . . . 26 . . . 5101 1
316 . 1 1 28 28 VAL HG21 H 1 0.52 0.01 . 2 . . . . 26 . . . 5101 1
317 . 1 1 28 28 VAL HG22 H 1 0.52 0.01 . 2 . . . . 26 . . . 5101 1
318 . 1 1 28 28 VAL HG23 H 1 0.52 0.01 . 2 . . . . 26 . . . 5101 1
319 . 1 1 28 28 VAL H H 1 8.47 0.01 . 1 . . . . 26 . . . 5101 1
320 . 1 1 28 28 VAL N N 15 122.87 0.05 . 1 . . . . 26 . . . 5101 1
321 . 1 1 29 29 LYS CA C 13 59.67 0.05 . 1 . . . . 27 . . . 5101 1
322 . 1 1 29 29 LYS CB C 13 33.71 0.05 . 1 . . . . 27 . . . 5101 1
323 . 1 1 29 29 LYS CE C 13 42.72 0.05 . 1 . . . . 27 . . . 5101 1
324 . 1 1 29 29 LYS CG C 13 25.90 0.05 . 1 . . . . 27 . . . 5101 1
325 . 1 1 29 29 LYS HA H 1 4.48 0.01 . 1 . . . . 27 . . . 5101 1
326 . 1 1 29 29 LYS HB2 H 1 2.03 0.01 . 2 . . . . 27 . . . 5101 1
327 . 1 1 29 29 LYS HB3 H 1 1.46 0.01 . 2 . . . . 27 . . . 5101 1
328 . 1 1 29 29 LYS HD2 H 1 1.66 0.01 . 1 . . . . 27 . . . 5101 1
329 . 1 1 29 29 LYS HD3 H 1 1.66 0.01 . 1 . . . . 27 . . . 5101 1
330 . 1 1 29 29 LYS HE2 H 1 2.83 0.01 . 1 . . . . 27 . . . 5101 1
331 . 1 1 29 29 LYS HE3 H 1 2.83 0.01 . 1 . . . . 27 . . . 5101 1
332 . 1 1 29 29 LYS HG2 H 1 1.86 0.01 . 2 . . . . 27 . . . 5101 1
333 . 1 1 29 29 LYS HG3 H 1 1.70 0.01 . 2 . . . . 27 . . . 5101 1
334 . 1 1 29 29 LYS H H 1 8.65 0.01 . 1 . . . . 27 . . . 5101 1
335 . 1 1 29 29 LYS N N 15 117.95 0.05 . 1 . . . . 27 . . . 5101 1
336 . 1 1 30 30 ALA CA C 13 55.15 0.05 . 1 . . . . 28 . . . 5101 1
337 . 1 1 30 30 ALA CB C 13 18.13 0.05 . 1 . . . . 28 . . . 5101 1
338 . 1 1 30 30 ALA HA H 1 4.12 0.01 . 1 . . . . 28 . . . 5101 1
339 . 1 1 30 30 ALA HB1 H 1 1.53 0.01 . 1 . . . . 28 . . . 5101 1
340 . 1 1 30 30 ALA HB2 H 1 1.53 0.01 . 1 . . . . 28 . . . 5101 1
341 . 1 1 30 30 ALA HB3 H 1 1.53 0.01 . 1 . . . . 28 . . . 5101 1
342 . 1 1 30 30 ALA H H 1 7.78 0.01 . 1 . . . . 28 . . . 5101 1
343 . 1 1 30 30 ALA N N 15 121.61 0.05 . 1 . . . . 28 . . . 5101 1
344 . 1 1 31 31 LYS CA C 13 59.27 0.05 . 1 . . . . 29 . . . 5101 1
345 . 1 1 31 31 LYS CB C 13 32.20 0.05 . 1 . . . . 29 . . . 5101 1
346 . 1 1 31 31 LYS CD C 13 29.69 0.05 . 1 . . . . 29 . . . 5101 1
347 . 1 1 31 31 LYS CG C 13 25.84 0.05 . 1 . . . . 29 . . . 5101 1
348 . 1 1 31 31 LYS HA H 1 4.09 0.01 . 1 . . . . 29 . . . 5101 1
349 . 1 1 31 31 LYS HB2 H 1 1.83 0.01 . 2 . . . . 29 . . . 5101 1
350 . 1 1 31 31 LYS HB3 H 1 1.95 0.01 . 2 . . . . 29 . . . 5101 1
351 . 1 1 31 31 LYS HD2 H 1 1.54 0.01 . 1 . . . . 29 . . . 5101 1
352 . 1 1 31 31 LYS HD3 H 1 1.54 0.01 . 1 . . . . 29 . . . 5101 1
353 . 1 1 31 31 LYS HE2 H 1 2.92 0.01 . 1 . . . . 29 . . . 5101 1
354 . 1 1 31 31 LYS HE3 H 1 2.92 0.01 . 1 . . . . 29 . . . 5101 1
355 . 1 1 31 31 LYS HG2 H 1 1.60 0.01 . 2 . . . . 29 . . . 5101 1
356 . 1 1 31 31 LYS HG3 H 1 1.35 0.01 . 2 . . . . 29 . . . 5101 1
357 . 1 1 31 31 LYS H H 1 7.80 0.01 . 1 . . . . 29 . . . 5101 1
358 . 1 1 31 31 LYS N N 15 121.20 0.05 . 1 . . . . 29 . . . 5101 1
359 . 1 1 32 32 ILE CA C 13 65.69 0.05 . 1 . . . . 30 . . . 5101 1
360 . 1 1 32 32 ILE CB C 13 37.03 0.05 . 1 . . . . 30 . . . 5101 1
361 . 1 1 32 32 ILE CD1 C 13 14.39 0.05 . 1 . . . . 30 . . . 5101 1
362 . 1 1 32 32 ILE CG1 C 13 30.19 0.05 . 1 . . . . 30 . . . 5101 1
363 . 1 1 32 32 ILE CG2 C 13 17.68 0.05 . 1 . . . . 30 . . . 5101 1
364 . 1 1 32 32 ILE HA H 1 3.26 0.01 . 1 . . . . 30 . . . 5101 1
365 . 1 1 32 32 ILE HB H 1 1.81 0.01 . 1 . . . . 30 . . . 5101 1
366 . 1 1 32 32 ILE HD11 H 1 -0.03 0.01 . 1 . . . . 30 . . . 5101 1
367 . 1 1 32 32 ILE HD12 H 1 -0.03 0.01 . 1 . . . . 30 . . . 5101 1
368 . 1 1 32 32 ILE HD13 H 1 -0.03 0.01 . 1 . . . . 30 . . . 5101 1
369 . 1 1 32 32 ILE HG12 H 1 0.37 0.01 . 2 . . . . 30 . . . 5101 1
370 . 1 1 32 32 ILE HG13 H 1 1.27 0.01 . 2 . . . . 30 . . . 5101 1
371 . 1 1 32 32 ILE HG21 H 1 0.52 0.01 . 1 . . . . 30 . . . 5101 1
372 . 1 1 32 32 ILE HG22 H 1 0.52 0.01 . 1 . . . . 30 . . . 5101 1
373 . 1 1 32 32 ILE HG23 H 1 0.52 0.01 . 1 . . . . 30 . . . 5101 1
374 . 1 1 32 32 ILE H H 1 8.10 0.01 . 1 . . . . 30 . . . 5101 1
375 . 1 1 32 32 ILE N N 15 120.42 0.05 . 1 . . . . 30 . . . 5101 1
376 . 1 1 33 33 GLN CA C 13 59.79 0.05 . 1 . . . . 31 . . . 5101 1
377 . 1 1 33 33 GLN CB C 13 28.02 0.05 . 1 . . . . 31 . . . 5101 1
378 . 1 1 33 33 GLN CG C 13 33.67 0.05 . 1 . . . . 31 . . . 5101 1
379 . 1 1 33 33 GLN HA H 1 3.74 0.01 . 1 . . . . 31 . . . 5101 1
380 . 1 1 33 33 GLN HB2 H 1 2.27 0.01 . 2 . . . . 31 . . . 5101 1
381 . 1 1 33 33 GLN HB3 H 1 1.85 0.01 . 2 . . . . 31 . . . 5101 1
382 . 1 1 33 33 GLN HE21 H 1 6.84 0.01 . 2 . . . . 31 . . . 5101 1
383 . 1 1 33 33 GLN HE22 H 1 7.60 0.01 . 2 . . . . 31 . . . 5101 1
384 . 1 1 33 33 GLN HG2 H 1 1.96 0.01 . 1 . . . . 31 . . . 5101 1
385 . 1 1 33 33 GLN HG3 H 1 1.96 0.01 . 1 . . . . 31 . . . 5101 1
386 . 1 1 33 33 GLN H H 1 8.19 0.01 . 1 . . . . 31 . . . 5101 1
387 . 1 1 33 33 GLN N N 15 122.43 0.05 . 1 . . . . 31 . . . 5101 1
388 . 1 1 34 34 ASP CA C 13 57.22 0.05 . 1 . . . . 32 . . . 5101 1
389 . 1 1 34 34 ASP CB C 13 41.58 0.05 . 1 . . . . 32 . . . 5101 1
390 . 1 1 34 34 ASP HA H 1 4.25 0.01 . 1 . . . . 32 . . . 5101 1
391 . 1 1 34 34 ASP HB2 H 1 2.74 0.01 . 2 . . . . 32 . . . 5101 1
392 . 1 1 34 34 ASP HB3 H 1 2.68 0.01 . 2 . . . . 32 . . . 5101 1
393 . 1 1 34 34 ASP H H 1 8.08 0.01 . 1 . . . . 32 . . . 5101 1
394 . 1 1 34 34 ASP N N 15 119.95 0.05 . 1 . . . . 32 . . . 5101 1
395 . 1 1 35 35 LYS CA C 13 58.42 0.05 . 1 . . . . 33 . . . 5101 1
396 . 1 1 35 35 LYS CB C 13 33.74 0.05 . 1 . . . . 33 . . . 5101 1
397 . 1 1 35 35 LYS CD C 13 28.70 0.05 . 1 . . . . 33 . . . 5101 1
398 . 1 1 35 35 LYS CE C 13 42.38 0.05 . 1 . . . . 33 . . . 5101 1
399 . 1 1 35 35 LYS CG C 13 25.16 0.05 . 1 . . . . 33 . . . 5101 1
400 . 1 1 35 35 LYS HA H 1 4.19 0.01 . 1 . . . . 33 . . . 5101 1
401 . 1 1 35 35 LYS HB2 H 1 1.85 0.01 . 1 . . . . 33 . . . 5101 1
402 . 1 1 35 35 LYS HB3 H 1 1.85 0.01 . 1 . . . . 33 . . . 5101 1
403 . 1 1 35 35 LYS HD2 H 1 1.59 0.01 . 1 . . . . 33 . . . 5101 1
404 . 1 1 35 35 LYS HD3 H 1 1.59 0.01 . 1 . . . . 33 . . . 5101 1
405 . 1 1 35 35 LYS HE2 H 1 2.96 0.01 . 1 . . . . 33 . . . 5101 1
406 . 1 1 35 35 LYS HE3 H 1 2.96 0.01 . 1 . . . . 33 . . . 5101 1
407 . 1 1 35 35 LYS HG2 H 1 1.51 0.01 . 1 . . . . 33 . . . 5101 1
408 . 1 1 35 35 LYS HG3 H 1 1.51 0.01 . 1 . . . . 33 . . . 5101 1
409 . 1 1 35 35 LYS H H 1 8.05 0.01 . 1 . . . . 33 . . . 5101 1
410 . 1 1 35 35 LYS N N 15 115.80 0.05 . 1 . . . . 33 . . . 5101 1
411 . 1 1 36 36 GLU CB C 13 32.10 0.05 . 1 . . . . 34 . . . 5101 1
412 . 1 1 36 36 GLU HA H 1 4.61 0.01 . 1 . . . . 34 . . . 5101 1
413 . 1 1 36 36 GLU HB2 H 1 2.30 0.01 . 2 . . . . 34 . . . 5101 1
414 . 1 1 36 36 GLU HB3 H 1 1.58 0.01 . 2 . . . . 34 . . . 5101 1
415 . 1 1 36 36 GLU HG2 H 1 2.01 0.01 . 1 . . . . 34 . . . 5101 1
416 . 1 1 36 36 GLU HG3 H 1 2.01 0.01 . 1 . . . . 34 . . . 5101 1
417 . 1 1 36 36 GLU H H 1 8.46 0.01 . 1 . . . . 34 . . . 5101 1
418 . 1 1 36 36 GLU N N 15 113.62 0.05 . 1 . . . . 34 . . . 5101 1
419 . 1 1 37 37 GLY CA C 13 46.47 0.05 . 1 . . . . 35 . . . 5101 1
420 . 1 1 37 37 GLY HA2 H 1 4.04 0.01 . 2 . . . . 35 . . . 5101 1
421 . 1 1 37 37 GLY HA3 H 1 3.92 0.01 . 2 . . . . 35 . . . 5101 1
422 . 1 1 37 37 GLY H H 1 8.00 0.01 . 1 . . . . 35 . . . 5101 1
423 . 1 1 37 37 GLY N N 15 108.68 0.05 . 1 . . . . 35 . . . 5101 1
424 . 1 1 38 38 ILE CA C 13 58.81 0.05 . 1 . . . . 36 . . . 5101 1
425 . 1 1 38 38 ILE CB C 13 39.70 0.05 . 1 . . . . 36 . . . 5101 1
426 . 1 1 38 38 ILE CD1 C 13 13.38 0.05 . 1 . . . . 36 . . . 5101 1
427 . 1 1 38 38 ILE CG1 C 13 27.58 0.05 . 1 . . . . 36 . . . 5101 1
428 . 1 1 38 38 ILE CG2 C 13 18.60 0.05 . 1 . . . . 36 . . . 5101 1
429 . 1 1 38 38 ILE HA H 1 4.35 0.01 . 1 . . . . 36 . . . 5101 1
430 . 1 1 38 38 ILE HB H 1 1.42 0.01 . 1 . . . . 36 . . . 5101 1
431 . 1 1 38 38 ILE HD11 H 1 0.69 0.01 . 1 . . . . 36 . . . 5101 1
432 . 1 1 38 38 ILE HD12 H 1 0.69 0.01 . 1 . . . . 36 . . . 5101 1
433 . 1 1 38 38 ILE HD13 H 1 0.69 0.01 . 1 . . . . 36 . . . 5101 1
434 . 1 1 38 38 ILE HG12 H 1 1.40 0.01 . 2 . . . . 36 . . . 5101 1
435 . 1 1 38 38 ILE HG13 H 1 0.94 0.01 . 2 . . . . 36 . . . 5101 1
436 . 1 1 38 38 ILE HG21 H 1 0.89 0.01 . 1 . . . . 36 . . . 5101 1
437 . 1 1 38 38 ILE HG22 H 1 0.89 0.01 . 1 . . . . 36 . . . 5101 1
438 . 1 1 38 38 ILE HG23 H 1 0.89 0.01 . 1 . . . . 36 . . . 5101 1
439 . 1 1 38 38 ILE H H 1 6.29 0.01 . 1 . . . . 36 . . . 5101 1
440 . 1 1 38 38 ILE N N 15 119.43 0.05 . 1 . . . . 36 . . . 5101 1
441 . 1 1 39 39 PRO CA C 13 61.75 0.05 . 1 . . . . 37 . . . 5101 1
442 . 1 1 39 39 PRO CB C 13 31.75 0.05 . 1 . . . . 37 . . . 5101 1
443 . 1 1 39 39 PRO CD C 13 51.03 0.05 . 1 . . . . 37 . . . 5101 1
444 . 1 1 39 39 PRO CG C 13 28.45 0.05 . 1 . . . . 37 . . . 5101 1
445 . 1 1 39 39 PRO HA H 1 4.53 0.01 . 1 . . . . 37 . . . 5101 1
446 . 1 1 39 39 PRO HB2 H 1 2.39 0.01 . 2 . . . . 37 . . . 5101 1
447 . 1 1 39 39 PRO HB3 H 1 1.84 0.01 . 2 . . . . 37 . . . 5101 1
448 . 1 1 39 39 PRO HD2 H 1 3.48 0.01 . 2 . . . . 37 . . . 5101 1
449 . 1 1 39 39 PRO HD3 H 1 4.27 0.01 . 2 . . . . 37 . . . 5101 1
450 . 1 1 39 39 PRO HG2 H 1 2.01 0.01 . 1 . . . . 37 . . . 5101 1
451 . 1 1 39 39 PRO HG3 H 1 2.01 0.01 . 1 . . . . 37 . . . 5101 1
452 . 1 1 40 40 PRO CA C 13 66.14 0.05 . 1 . . . . 38 . . . 5101 1
453 . 1 1 40 40 PRO CB C 13 32.66 0.05 . 1 . . . . 38 . . . 5101 1
454 . 1 1 40 40 PRO CD C 13 50.86 0.05 . 1 . . . . 38 . . . 5101 1
455 . 1 1 40 40 PRO CG C 13 27.60 0.05 . 1 . . . . 38 . . . 5101 1
456 . 1 1 40 40 PRO HA H 1 4.160 0.01 . 1 . . . . 38 . . . 5101 1
457 . 1 1 40 40 PRO HB2 H 1 2.03 0.01 . 2 . . . . 38 . . . 5101 1
458 . 1 1 40 40 PRO HB3 H 1 2.21 0.01 . 2 . . . . 38 . . . 5101 1
459 . 1 1 40 40 PRO HD2 H 1 3.72 0.01 . 1 . . . . 38 . . . 5101 1
460 . 1 1 40 40 PRO HD3 H 1 3.72 0.01 . 1 . . . . 38 . . . 5101 1
461 . 1 1 40 40 PRO HG2 H 1 2.15 0.01 . 2 . . . . 38 . . . 5101 1
462 . 1 1 40 40 PRO HG3 H 1 1.71 0.01 . 2 . . . . 38 . . . 5101 1
463 . 1 1 41 41 ASP CA C 13 55.90 0.05 . 1 . . . . 39 . . . 5101 1
464 . 1 1 41 41 ASP CB C 13 39.83 0.05 . 1 . . . . 39 . . . 5101 1
465 . 1 1 41 41 ASP HA H 1 4.46 0.01 . 1 . . . . 39 . . . 5101 1
466 . 1 1 41 41 ASP HB2 H 1 2.71 0.01 . 1 . . . . 39 . . . 5101 1
467 . 1 1 41 41 ASP HB3 H 1 2.71 0.01 . 1 . . . . 39 . . . 5101 1
468 . 1 1 41 41 ASP H H 1 8.68 0.01 . 1 . . . . 39 . . . 5101 1
469 . 1 1 41 41 ASP N N 15 114.55 0.05 . 1 . . . . 39 . . . 5101 1
470 . 1 1 42 42 GLN CA C 13 54.96 0.05 . 1 . . . . 40 . . . 5101 1
471 . 1 1 42 42 GLN CB C 13 30.03 0.05 . 1 . . . . 40 . . . 5101 1
472 . 1 1 42 42 GLN CG C 13 34.47 0.05 . 1 . . . . 40 . . . 5101 1
473 . 1 1 42 42 GLN HA H 1 4.35 0.01 . 1 . . . . 40 . . . 5101 1
474 . 1 1 42 42 GLN HB2 H 1 2.57 0.01 . 2 . . . . 40 . . . 5101 1
475 . 1 1 42 42 GLN HB3 H 1 1.79 0.01 . 2 . . . . 40 . . . 5101 1
476 . 1 1 42 42 GLN HE21 H 1 7.69 0.01 . 2 . . . . 40 . . . 5101 1
477 . 1 1 42 42 GLN HE22 H 1 6.81 0.01 . 2 . . . . 40 . . . 5101 1
478 . 1 1 42 42 GLN HG2 H 1 2.32 0.01 . 1 . . . . 40 . . . 5101 1
479 . 1 1 42 42 GLN HG3 H 1 2.32 0.01 . 1 . . . . 40 . . . 5101 1
480 . 1 1 42 42 GLN H H 1 7.96 0.01 . 1 . . . . 40 . . . 5101 1
481 . 1 1 42 42 GLN N N 15 117.05 0.05 . 1 . . . . 40 . . . 5101 1
482 . 1 1 43 43 GLN CA C 13 55.62 0.05 . 1 . . . . 41 . . . 5101 1
483 . 1 1 43 43 GLN HA H 1 4.57 0.01 . 1 . . . . 41 . . . 5101 1
484 . 1 1 43 43 GLN HB2 H 1 2.00 0.01 . 1 . . . . 41 . . . 5101 1
485 . 1 1 43 43 GLN HB3 H 1 2.00 0.01 . 1 . . . . 41 . . . 5101 1
486 . 1 1 43 43 GLN HE21 H 1 6.74 0.01 . 2 . . . . 41 . . . 5101 1
487 . 1 1 43 43 GLN HE22 H 1 6.54 0.01 . 2 . . . . 41 . . . 5101 1
488 . 1 1 43 43 GLN H H 1 7.18 0.01 . 1 . . . . 41 . . . 5101 1
489 . 1 1 43 43 GLN N N 15 117.97 0.05 . 1 . . . . 41 . . . 5101 1
490 . 1 1 44 44 ARG CA C 13 54.67 0.05 . 1 . . . . 42 . . . 5101 1
491 . 1 1 44 44 ARG CB C 13 32.37 0.05 . 1 . . . . 42 . . . 5101 1
492 . 1 1 44 44 ARG CD C 13 43.27 0.05 . 1 . . . . 42 . . . 5101 1
493 . 1 1 44 44 ARG CG C 13 27.31 0.05 . 1 . . . . 42 . . . 5101 1
494 . 1 1 44 44 ARG HA H 1 4.59 0.01 . 1 . . . . 42 . . . 5101 1
495 . 1 1 44 44 ARG HB2 H 1 1.65 0.01 . 1 . . . . 42 . . . 5101 1
496 . 1 1 44 44 ARG HB3 H 1 1.65 0.01 . 1 . . . . 42 . . . 5101 1
497 . 1 1 44 44 ARG HD2 H 1 2.79 0.01 . 1 . . . . 42 . . . 5101 1
498 . 1 1 44 44 ARG HD3 H 1 2.79 0.01 . 1 . . . . 42 . . . 5101 1
499 . 1 1 44 44 ARG HG2 H 1 1.52 0.01 . 2 . . . . 42 . . . 5101 1
500 . 1 1 44 44 ARG HG3 H 1 1.42 0.01 . 2 . . . . 42 . . . 5101 1
501 . 1 1 44 44 ARG H H 1 9.14 0.01 . 1 . . . . 42 . . . 5101 1
502 . 1 1 44 44 ARG N N 15 125.09 0.05 . 1 . . . . 42 . . . 5101 1
503 . 1 1 45 45 LEU CA C 13 55.50 0.05 . 1 . . . . 43 . . . 5101 1
504 . 1 1 45 45 LEU CB C 13 42.86 0.05 . 1 . . . . 43 . . . 5101 1
505 . 1 1 45 45 LEU CD1 C 13 23.25 0.05 . 2 . . . . 43 . . . 5101 1
506 . 1 1 45 45 LEU CD2 C 13 26.70 0.05 . 2 . . . . 43 . . . 5101 1
507 . 1 1 45 45 LEU CG C 13 28.50 0.05 . 1 . . . . 43 . . . 5101 1
508 . 1 1 45 45 LEU HA H 1 4.58 0.01 . 1 . . . . 43 . . . 5101 1
509 . 1 1 45 45 LEU HB2 H 1 1.48 0.01 . 2 . . . . 43 . . . 5101 1
510 . 1 1 45 45 LEU HB3 H 1 1.23 0.01 . 2 . . . . 43 . . . 5101 1
511 . 1 1 45 45 LEU HD11 H 1 0.19 0.01 . 2 . . . . 43 . . . 5101 1
512 . 1 1 45 45 LEU HD12 H 1 0.19 0.01 . 2 . . . . 43 . . . 5101 1
513 . 1 1 45 45 LEU HD13 H 1 0.19 0.01 . 2 . . . . 43 . . . 5101 1
514 . 1 1 45 45 LEU HD21 H 1 0.67 0.01 . 2 . . . . 43 . . . 5101 1
515 . 1 1 45 45 LEU HD22 H 1 0.67 0.01 . 2 . . . . 43 . . . 5101 1
516 . 1 1 45 45 LEU HD23 H 1 0.67 0.01 . 2 . . . . 43 . . . 5101 1
517 . 1 1 45 45 LEU HG H 1 0.87 0.01 . 1 . . . . 43 . . . 5101 1
518 . 1 1 45 45 LEU H H 1 8.74 0.01 . 1 . . . . 43 . . . 5101 1
519 . 1 1 45 45 LEU N N 15 127.01 0.05 . 1 . . . . 43 . . . 5101 1
520 . 1 1 46 46 ILE CA C 13 59.79 0.05 . 1 . . . . 44 . . . 5101 1
521 . 1 1 46 46 ILE CB C 13 41.60 0.05 . 1 . . . . 44 . . . 5101 1
522 . 1 1 46 46 ILE CD1 C 13 15.24 0.05 . 1 . . . . 44 . . . 5101 1
523 . 1 1 46 46 ILE CG1 C 13 28.49 0.05 . 1 . . . . 44 . . . 5101 1
524 . 1 1 46 46 ILE CG2 C 13 18.10 0.05 . 1 . . . . 44 . . . 5101 1
525 . 1 1 46 46 ILE HA H 1 5.00 0.01 . 1 . . . . 44 . . . 5101 1
526 . 1 1 46 46 ILE HB H 1 1.70 0.01 . 1 . . . . 44 . . . 5101 1
527 . 1 1 46 46 ILE HD11 H 1 0.67 0.01 . 1 . . . . 44 . . . 5101 1
528 . 1 1 46 46 ILE HD12 H 1 0.67 0.01 . 1 . . . . 44 . . . 5101 1
529 . 1 1 46 46 ILE HD13 H 1 0.67 0.01 . 1 . . . . 44 . . . 5101 1
530 . 1 1 46 46 ILE HG12 H 1 0.86 0.01 . 2 . . . . 44 . . . 5101 1
531 . 1 1 46 46 ILE HG13 H 1 1.40 0.01 . 2 . . . . 44 . . . 5101 1
532 . 1 1 46 46 ILE HG21 H 1 0.75 0.01 . 1 . . . . 44 . . . 5101 1
533 . 1 1 46 46 ILE HG22 H 1 0.75 0.01 . 1 . . . . 44 . . . 5101 1
534 . 1 1 46 46 ILE HG23 H 1 0.75 0.01 . 1 . . . . 44 . . . 5101 1
535 . 1 1 46 46 ILE H H 1 9.13 0.01 . 1 . . . . 44 . . . 5101 1
536 . 1 1 46 46 ILE N N 15 125.22 0.05 . 1 . . . . 44 . . . 5101 1
537 . 1 1 47 47 PHE CA C 13 55.96 0.05 . 1 . . . . 45 . . . 5101 1
538 . 1 1 47 47 PHE CB C 13 41.23 0.05 . 1 . . . . 45 . . . 5101 1
539 . 1 1 47 47 PHE CD1 C 13 131.70 0.05 . 1 . . . . 45 . . . 5101 1
540 . 1 1 47 47 PHE CD2 C 13 131.70 0.05 . 1 . . . . 45 . . . 5101 1
541 . 1 1 47 47 PHE CE1 C 13 129.99 0.05 . 1 . . . . 45 . . . 5101 1
542 . 1 1 47 47 PHE CE2 C 13 129.99 0.05 . 1 . . . . 45 . . . 5101 1
543 . 1 1 47 47 PHE CZ C 13 127.33 0.05 . 1 . . . . 45 . . . 5101 1
544 . 1 1 47 47 PHE HA H 1 5.26 0.01 . 1 . . . . 45 . . . 5101 1
545 . 1 1 47 47 PHE HB2 H 1 2.53 0.01 . 2 . . . . 45 . . . 5101 1
546 . 1 1 47 47 PHE HB3 H 1 3.00 0.01 . 2 . . . . 45 . . . 5101 1
547 . 1 1 47 47 PHE HD1 H 1 7.20 0.01 . 1 . . . . 45 . . . 5101 1
548 . 1 1 47 47 PHE HD2 H 1 7.20 0.01 . 1 . . . . 45 . . . 5101 1
549 . 1 1 47 47 PHE HE1 H 1 6.92 0.01 . 1 . . . . 45 . . . 5101 1
550 . 1 1 47 47 PHE HE2 H 1 6.92 0.01 . 1 . . . . 45 . . . 5101 1
551 . 1 1 47 47 PHE H H 1 9.29 0.01 . 1 . . . . 45 . . . 5101 1
552 . 1 1 47 47 PHE HZ H 1 6.87 0.01 . 1 . . . . 45 . . . 5101 1
553 . 1 1 47 47 PHE N N 15 125.99 0.05 . 1 . . . . 45 . . . 5101 1
554 . 1 1 48 48 ALA CA C 13 50.30 0.05 . 1 . . . . 46 . . . 5101 1
555 . 1 1 48 48 ALA CB C 13 22.09 0.05 . 1 . . . . 46 . . . 5101 1
556 . 1 1 48 48 ALA HA H 1 4.87 0.01 . 1 . . . . 46 . . . 5101 1
557 . 1 1 48 48 ALA HB1 H 1 1.30 0.01 . 1 . . . . 46 . . . 5101 1
558 . 1 1 48 48 ALA HB2 H 1 1.30 0.01 . 1 . . . . 46 . . . 5101 1
559 . 1 1 48 48 ALA HB3 H 1 1.30 0.01 . 1 . . . . 46 . . . 5101 1
560 . 1 1 48 48 ALA H H 1 9.19 0.01 . 1 . . . . 46 . . . 5101 1
561 . 1 1 48 48 ALA N N 15 125.08 0.05 . 1 . . . . 46 . . . 5101 1
562 . 1 1 49 49 GLY CA C 13 45.04 0.05 . 1 . . . . 47 . . . 5101 1
563 . 1 1 49 49 GLY HA2 H 1 4.59 0.01 . 2 . . . . 47 . . . 5101 1
564 . 1 1 49 49 GLY HA3 H 1 3.45 0.01 . 2 . . . . 47 . . . 5101 1
565 . 1 1 49 49 GLY H H 1 8.69 0.01 . 1 . . . . 47 . . . 5101 1
566 . 1 1 49 49 GLY N N 15 108.53 0.05 . 1 . . . . 47 . . . 5101 1
567 . 1 1 50 50 LYS CA C 13 56.01 0.05 . 1 . . . . 48 . . . 5101 1
568 . 1 1 50 50 LYS CB C 13 33.56 0.05 . 1 . . . . 48 . . . 5101 1
569 . 1 1 50 50 LYS CD C 13 29.42 0.05 . 1 . . . . 48 . . . 5101 1
570 . 1 1 50 50 LYS CG C 13 24.73 0.05 . 1 . . . . 48 . . . 5101 1
571 . 1 1 50 50 LYS HA H 1 4.27 0.01 . 1 . . . . 48 . . . 5101 1
572 . 1 1 50 50 LYS HB2 H 1 1.60 0.01 . 2 . . . . 48 . . . 5101 1
573 . 1 1 50 50 LYS HB3 H 1 1.73 0.01 . 2 . . . . 48 . . . 5101 1
574 . 1 1 50 50 LYS HD2 H 1 1.63 0.01 . 1 . . . . 48 . . . 5101 1
575 . 1 1 50 50 LYS HD3 H 1 1.63 0.01 . 1 . . . . 48 . . . 5101 1
576 . 1 1 50 50 LYS HE2 H 1 2.92 0.01 . 1 . . . . 48 . . . 5101 1
577 . 1 1 50 50 LYS HE3 H 1 2.92 0.01 . 1 . . . . 48 . . . 5101 1
578 . 1 1 50 50 LYS HG2 H 1 1.31 0.01 . 1 . . . . 48 . . . 5101 1
579 . 1 1 50 50 LYS HG3 H 1 1.31 0.01 . 1 . . . . 48 . . . 5101 1
580 . 1 1 50 50 LYS H H 1 8.43 0.01 . 1 . . . . 48 . . . 5101 1
581 . 1 1 50 50 LYS N N 15 122.94 0.05 . 1 . . . . 48 . . . 5101 1
582 . 1 1 51 51 GLN CA C 13 55.97 0.05 . 1 . . . . 49 . . . 5101 1
583 . 1 1 51 51 GLN CB C 13 29.47 0.05 . 1 . . . . 49 . . . 5101 1
584 . 1 1 51 51 GLN CG C 13 33.81 0.05 . 1 . . . . 49 . . . 5101 1
585 . 1 1 51 51 GLN HA H 1 4.22 0.01 . 1 . . . . 49 . . . 5101 1
586 . 1 1 51 51 GLN HB2 H 1 2.04 0.01 . 2 . . . . 49 . . . 5101 1
587 . 1 1 51 51 GLN HB3 H 1 1.92 0.01 . 2 . . . . 49 . . . 5101 1
588 . 1 1 51 51 GLN HG2 H 1 2.33 0.01 . 1 . . . . 49 . . . 5101 1
589 . 1 1 51 51 GLN HG3 H 1 2.33 0.01 . 1 . . . . 49 . . . 5101 1
590 . 1 1 51 51 GLN H H 1 8.51 0.01 . 1 . . . . 49 . . . 5101 1
591 . 1 1 51 51 GLN N N 15 121.27 0.05 . 1 . . . . 49 . . . 5101 1
592 . 1 1 52 52 LEU CA C 13 55.33 0.05 . 1 . . . . 50 . . . 5101 1
593 . 1 1 52 52 LEU CB C 13 42.18 0.05 . 1 . . . . 50 . . . 5101 1
594 . 1 1 52 52 LEU CD1 C 13 24.00 0.05 . 2 . . . . 50 . . . 5101 1
595 . 1 1 52 52 LEU CD2 C 13 24.73 0.05 . 2 . . . . 50 . . . 5101 1
596 . 1 1 52 52 LEU HA H 1 4.28 0.01 . 1 . . . . 50 . . . 5101 1
597 . 1 1 52 52 LEU HB2 H 1 1.57 0.01 . 1 . . . . 50 . . . 5101 1
598 . 1 1 52 52 LEU HB3 H 1 1.57 0.01 . 1 . . . . 50 . . . 5101 1
599 . 1 1 52 52 LEU HD11 H 1 0.79 0.01 . 2 . . . . 50 . . . 5101 1
600 . 1 1 52 52 LEU HD12 H 1 0.79 0.01 . 2 . . . . 50 . . . 5101 1
601 . 1 1 52 52 LEU HD13 H 1 0.79 0.01 . 2 . . . . 50 . . . 5101 1
602 . 1 1 52 52 LEU HD21 H 1 0.81 0.01 . 2 . . . . 50 . . . 5101 1
603 . 1 1 52 52 LEU HD22 H 1 0.81 0.01 . 2 . . . . 50 . . . 5101 1
604 . 1 1 52 52 LEU HD23 H 1 0.81 0.01 . 2 . . . . 50 . . . 5101 1
605 . 1 1 52 52 LEU H H 1 8.27 0.01 . 1 . . . . 50 . . . 5101 1
606 . 1 1 52 52 LEU N N 15 124.03 0.05 . 1 . . . . 50 . . . 5101 1
607 . 1 1 53 53 GLU CA C 13 57.97 0.05 . 1 . . . . 51 . . . 5101 1
608 . 1 1 53 53 GLU CG C 13 36.99 0.05 . 1 . . . . 51 . . . 5101 1
609 . 1 1 53 53 GLU HA H 1 4.06 0.01 . 1 . . . . 51 . . . 5101 1
610 . 1 1 53 53 GLU HG2 H 1 2.14 0.01 . 1 . . . . 51 . . . 5101 1
611 . 1 1 53 53 GLU HG3 H 1 2.14 0.01 . 1 . . . . 51 . . . 5101 1
612 . 1 1 53 53 GLU H H 1 7.87 0.01 . 1 . . . . 51 . . . 5101 1
613 . 1 1 53 53 GLU N N 15 126.04 0.05 . 1 . . . . 51 . . . 5101 1
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