data_15013
#######################
# Entry information #
#######################
save_entry_information
_Entry.Sf_category entry_information
_Entry.Sf_framecode entry_information
_Entry.ID 15013
_Entry.Title
;
Chimer between Spc-SH3 and P41
;
_Entry.Type macromolecule
_Entry.Version_type original
_Entry.Submission_date 2006-11-02
_Entry.Accession_date 2006-11-02
_Entry.Last_release_date 2007-05-10
_Entry.Original_release_date 2007-05-10
_Entry.Origination author
_Entry.NMR_STAR_version 3.1.1.61
_Entry.Original_NMR_STAR_version .
_Entry.Experimental_method NMR
_Entry.Experimental_method_subtype solution
_Entry.Details 'Chimer between Spc-SH3 and decapeptide P41 starting from circular permutant S19P20s'
_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 Nico 'van Nuland' . A.J. . 15013
2 Adela Candel . M. . 15013
3 Jose Martinez . C. . 15013
4 Francisco Conejero-Lara . . . 15013
5 Marta Bruix . . . 15013
stop_
loop_
_SG_project.SG_project_ID
_SG_project.Project_name
_SG_project.Full_name_of_center
_SG_project.Initial_of_center
_SG_project.Entry_ID
1 'not applicable' 'not applicable' . 15013
stop_
loop_
_Struct_keywords.Keywords
_Struct_keywords.Text
_Struct_keywords.Entry_ID
chimer . 15013
P41 . 15013
Spc-SH3 . 15013
stop_
loop_
_Data_set.Type
_Data_set.Count
_Data_set.Entry_ID
assigned_chemical_shifts 1 15013
stop_
loop_
_Datum.Type
_Datum.Count
_Datum.Entry_ID
'13C chemical shifts' 282 15013
'15N chemical shifts' 78 15013
'1H chemical shifts' 527 15013
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 . . 2007-05-10 2006-11-02 original author . 15013
stop_
loop_
_Related_entries.Database_name
_Related_entries.Database_accession_code
_Related_entries.Relationship
_Related_entries.Entry_ID
PDB 1TUC . 15013
PDB 2JMA . 15013
PDB 2JMC 'BMRB Entry Tracking System' 15013
stop_
save_
###############
# Citations #
###############
save_entry_citation
_Citation.Sf_category citations
_Citation.Sf_framecode entry_citation
_Citation.Entry_ID 15013
_Citation.ID 1
_Citation.Class 'entry citation'
_Citation.CAS_abstract_code .
_Citation.MEDLINE_UI_code .
_Citation.DOI .
_Citation.PubMed_ID 17275816
_Citation.Full_citation .
_Citation.Title 'The high-resolution NMR structure of a single-chain chimeric protein mimicking a SH3-peptide complex.'
_Citation.Status published
_Citation.Type journal
_Citation.Journal_abbrev 'FEBS Lett.'
_Citation.Journal_name_full .
_Citation.Journal_volume 581
_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 687
_Citation.Page_last 692
_Citation.Year 2007
_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 Adela Candel . M. . 15013 1
2 Francisco Conejero-Lara . . . 15013 1
3 Jose Martinez . C. . 15013 1
4 Nico 'van Nuland' . A.J. . 15013 1
5 Marta Bruix . . . 15013 1
stop_
loop_
_Citation_keyword.Keyword
_Citation_keyword.Entry_ID
_Citation_keyword.Citation_ID
'chimeric protein' 15013 1
NMR 15013 1
'proline-rich peptide' 15013 1
'protein structure' 15013 1
SH3 15013 1
stop_
save_
#############################################
# Molecular system (assembly) description #
#############################################
save_assembly
_Assembly.Sf_category assembly
_Assembly.Sf_framecode assembly
_Assembly.Entry_ID 15013
_Assembly.ID 1
_Assembly.Name 'SPCp41 monomer'
_Assembly.BMRB_code .
_Assembly.Number_of_components 1
_Assembly.Organic_ligands 0
_Assembly.Metal_ions 0
_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_
_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 SPCp41 1 $SPCp41 A . yes native no no . . . 15013 1
stop_
loop_
_Assembly_db_link.Author_supplied
_Assembly_db_link.Database_code
_Assembly_db_link.Accession_code
_Assembly_db_link.Entry_mol_code
_Assembly_db_link.Entry_mol_name
_Assembly_db_link.Entry_experimental_method
_Assembly_db_link.Entry_structure_resolution
_Assembly_db_link.Entry_relation_type
_Assembly_db_link.Entry_details
_Assembly_db_link.Entry_ID
_Assembly_db_link.Assembly_ID
yes PDB 1TUC . . X-ray . . . 15013 1
yes PDB 2JMA . . 'solution NMR' . . . 15013 1
stop_
save_
####################################
# Biological polymers and ligands #
####################################
save_SPCp41
_Entity.Sf_category entity
_Entity.Sf_framecode SPCp41
_Entity.Entry_ID 15013
_Entity.ID 1
_Entity.BMRB_code .
_Entity.Name SPCp41
_Entity.Type polymer
_Entity.Polymer_common_type .
_Entity.Polymer_type polypeptide(L)
_Entity.Polymer_type_details .
_Entity.Polymer_strand_ID A
_Entity.Polymer_seq_one_letter_code_can .
_Entity.Polymer_seq_one_letter_code
;
GAMGPREVTMKKGDILTLLN
STNKDWWKVEVNDRQGFVPA
AYVKKLDSGTGKELVLALYD
YQESGDNAPSYSPPPPP
;
_Entity.Target_identifier .
_Entity.Polymer_author_defined_seq .
_Entity.Polymer_author_seq_details .
_Entity.Ambiguous_conformational_states no
_Entity.Ambiguous_chem_comp_sites no
_Entity.Nstd_monomer no
_Entity.Nstd_chirality no
_Entity.Nstd_linkage no
_Entity.Nonpolymer_comp_ID .
_Entity.Nonpolymer_comp_label .
_Entity.Number_of_monomers 77
_Entity.Number_of_nonpolymer_components .
_Entity.Paramagnetic no
_Entity.Thiol_state 'not present'
_Entity.Src_method man
_Entity.Parent_entity_ID 1
_Entity.Fragment .
_Entity.Mutation .
_Entity.EC_number .
_Entity.Calc_isoelectric_point .
_Entity.Formula_weight 8470.656
_Entity.Formula_weight_exptl .
_Entity.Formula_weight_exptl_meth .
_Entity.Details .
_Entity.DB_query_date .
_Entity.DB_query_revised_last_date 2015-11-26
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 15144 . SH3_domain_from_chicken_alpha-spectrin . . . . . 57.14 62 97.73 97.73 7.34e-22 . . . . 15013 1
2 no BMRB 17915 . SH3 . . . . . 57.14 62 97.73 97.73 7.34e-22 . . . . 15013 1
3 no PDB 1AEY . "Alpha-Spectrin Src Homology 3 Domain, Solution Nmr, 15 Structures" . . . . . 57.14 62 97.73 97.73 7.34e-22 . . . . 15013 1
4 no PDB 1M8M . "Solid-State Mas Nmr Structure Of The A-Spectrin Sh3 Domain" . . . . . 57.14 62 97.73 97.73 7.34e-22 . . . . 15013 1
5 no PDB 1NEG . "Crystal Structure Analysis Of N-And C-Terminal Labeled Sh3- Domain Of Alpha-Chicken Spectrin" . . . . . 54.55 83 100.00 100.00 5.77e-21 . . . . 15013 1
6 no PDB 1QKW . "Alpha-Spectrin Src Homology 3 Domain, N47g Mutant In The Distal Loop" . . . . . 55.84 62 97.67 97.67 1.02e-20 . . . . 15013 1
7 no PDB 1SHG . "Crystal Structure Of A Src-Homology 3 (Sh3) Domain" . . . . . 57.14 62 97.73 97.73 7.34e-22 . . . . 15013 1
8 no PDB 1TUC . "Alpha-Spectrin Src Homology 3 Domain, Circular Permutant, Cut At S19-P20" . . . . . 79.22 63 100.00 100.00 1.04e-35 . . . . 15013 1
9 no PDB 1U06 . "Crystal Structure Of Chicken Alpha-Spectrin Sh3 Domain" . . . . . 57.14 62 97.73 97.73 7.34e-22 . . . . 15013 1
10 no PDB 2F2V . "Alpha-Spectrin Sh3 Domain A56g Mutant" . . . . . 55.84 62 97.67 97.67 4.64e-21 . . . . 15013 1
11 no PDB 2F2X . "Alpha-Spectrin Sh3 Domain R21g Mutant" . . . . . 55.84 62 97.67 97.67 1.96e-20 . . . . 15013 1
12 no PDB 2JMC . "Chimer Between Spc-Sh3 And P41" . . . . . 100.00 77 100.00 100.00 1.13e-47 . . . . 15013 1
13 no PDB 2LJ3 . "Pfbd: High-Throughput Strategy Of Backbone Fold Determination For Small Well-Folded Proteins In Less Than A Day" . . . . . 57.14 63 97.73 97.73 7.51e-22 . . . . 15013 1
14 no PDB 2NUZ . "Crystal Structure Of Alpha Spectrin Sh3 Domain Measured At Room Temperature" . . . . . 57.14 62 97.73 97.73 7.34e-22 . . . . 15013 1
15 no PDB 4F16 . "Crystal Structure Of The Alpha Spectrin Sh3 Domain At Ph 5" . . . . . 57.14 62 97.73 97.73 7.34e-22 . . . . 15013 1
16 no PDB 4F17 . "Crystal Structure Of The Alpha Spectrin Sh3 Domain At Ph 9" . . . . . 57.14 62 97.73 97.73 7.34e-22 . . . . 15013 1
17 no DBJ BAD52438 . "non-erythrocytic spectrin alpha [Homo sapiens]" . . . . . 55.84 2452 100.00 100.00 1.34e-20 . . . . 15013 1
18 no DBJ BAD93097 . "spectrin, alpha, non-erythrocytic 1 (alpha-fodrin) variant [Homo sapiens]" . . . . . 55.84 2506 100.00 100.00 1.77e-20 . . . . 15013 1
19 no DBJ BAG57892 . "unnamed protein product [Homo sapiens]" . . . . . 55.84 1312 100.00 100.00 1.65e-20 . . . . 15013 1
20 no DBJ BAG62120 . "unnamed protein product [Homo sapiens]" . . . . . 55.84 1176 100.00 100.00 1.03e-20 . . . . 15013 1
21 no DBJ BAG72795 . "spectrin, alpha, non-erythrocytic 1 [synthetic construct]" . . . . . 55.84 2472 100.00 100.00 1.28e-20 . . . . 15013 1
22 no EMBL CAA29435 . "unnamed protein product [Xenopus laevis]" . . . . . 50.65 454 100.00 100.00 2.29e-17 . . . . 15013 1
23 no EMBL CAA32663 . "spectrin alpha chain, partial [Gallus gallus]" . . . . . 55.84 2449 100.00 100.00 1.40e-20 . . . . 15013 1
24 no EMBL CAF90367 . "unnamed protein product [Tetraodon nigroviridis]" . . . . . 55.84 1589 97.67 97.67 8.03e-19 . . . . 15013 1
25 no EMBL CDQ79062 . "unnamed protein product [Oncorhynchus mykiss]" . . . . . 55.84 2460 100.00 100.00 2.36e-20 . . . . 15013 1
26 no GB AAA51702 . "alpha-fodrin, partial [Homo sapiens]" . . . . . 55.84 920 100.00 100.00 2.62e-20 . . . . 15013 1
27 no GB AAA51790 . "nonerythroid alpha-spectrin [Homo sapiens]" . . . . . 55.84 2472 100.00 100.00 1.28e-20 . . . . 15013 1
28 no GB AAA52468 . "alpha-fodrin, partial [Homo sapiens]" . . . . . 55.84 920 100.00 100.00 2.62e-20 . . . . 15013 1
29 no GB AAB41498 . "alpha II spectrin [Homo sapiens]" . . . . . 55.84 2477 100.00 100.00 1.28e-20 . . . . 15013 1
30 no GB AAB60364 . "alpha II spectrin, partial [Homo sapiens]" . . . . . 55.84 719 100.00 100.00 1.79e-20 . . . . 15013 1
31 no REF NP_001036003 . "spectrin alpha chain, non-erythrocytic 1 [Gallus gallus]" . . . . . 55.84 2477 100.00 100.00 1.45e-20 . . . . 15013 1
32 no REF NP_001090674 . "spectrin alpha chain, non-erythrocytic 1 [Xenopus (Silurana) tropicalis]" . . . . . 55.84 2471 100.00 100.00 1.56e-20 . . . . 15013 1
33 no REF NP_001091958 . "spectrin alpha chain, non-erythrocytic 1 [Danio rerio]" . . . . . 55.84 2480 100.00 100.00 1.87e-20 . . . . 15013 1
34 no REF NP_001123910 . "spectrin alpha chain, non-erythrocytic 1 isoform 1 [Homo sapiens]" . . . . . 55.84 2477 100.00 100.00 1.28e-20 . . . . 15013 1
35 no REF NP_001182461 . "spectrin alpha chain, non-erythrocytic 1 isoform 3 [Homo sapiens]" . . . . . 55.84 2452 100.00 100.00 1.34e-20 . . . . 15013 1
36 no SP P07751 . "RecName: Full=Spectrin alpha chain, non-erythrocytic 1; AltName: Full=Alpha-II spectrin; AltName: Full=Fodrin alpha chain" . . . . . 55.84 2477 100.00 100.00 1.45e-20 . . . . 15013 1
37 no SP Q13813 . "RecName: Full=Spectrin alpha chain, non-erythrocytic 1; AltName: Full=Alpha-II spectrin; AltName: Full=Fodrin alpha chain; AltN" . . . . . 55.84 2472 100.00 100.00 1.28e-20 . . . . 15013 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 . GLY . 15013 1
2 . ALA . 15013 1
3 . MET . 15013 1
4 . GLY . 15013 1
5 . PRO . 15013 1
6 . ARG . 15013 1
7 . GLU . 15013 1
8 . VAL . 15013 1
9 . THR . 15013 1
10 . MET . 15013 1
11 . LYS . 15013 1
12 . LYS . 15013 1
13 . GLY . 15013 1
14 . ASP . 15013 1
15 . ILE . 15013 1
16 . LEU . 15013 1
17 . THR . 15013 1
18 . LEU . 15013 1
19 . LEU . 15013 1
20 . ASN . 15013 1
21 . SER . 15013 1
22 . THR . 15013 1
23 . ASN . 15013 1
24 . LYS . 15013 1
25 . ASP . 15013 1
26 . TRP . 15013 1
27 . TRP . 15013 1
28 . LYS . 15013 1
29 . VAL . 15013 1
30 . GLU . 15013 1
31 . VAL . 15013 1
32 . ASN . 15013 1
33 . ASP . 15013 1
34 . ARG . 15013 1
35 . GLN . 15013 1
36 . GLY . 15013 1
37 . PHE . 15013 1
38 . VAL . 15013 1
39 . PRO . 15013 1
40 . ALA . 15013 1
41 . ALA . 15013 1
42 . TYR . 15013 1
43 . VAL . 15013 1
44 . LYS . 15013 1
45 . LYS . 15013 1
46 . LEU . 15013 1
47 . ASP . 15013 1
48 . SER . 15013 1
49 . GLY . 15013 1
50 . THR . 15013 1
51 . GLY . 15013 1
52 . LYS . 15013 1
53 . GLU . 15013 1
54 . LEU . 15013 1
55 . VAL . 15013 1
56 . LEU . 15013 1
57 . ALA . 15013 1
58 . LEU . 15013 1
59 . TYR . 15013 1
60 . ASP . 15013 1
61 . TYR . 15013 1
62 . GLN . 15013 1
63 . GLU . 15013 1
64 . SER . 15013 1
65 . GLY . 15013 1
66 . ASP . 15013 1
67 . ASN . 15013 1
68 . ALA . 15013 1
69 . PRO . 15013 1
70 . SER . 15013 1
71 . TYR . 15013 1
72 . SER . 15013 1
73 . PRO . 15013 1
74 . PRO . 15013 1
75 . PRO . 15013 1
76 . PRO . 15013 1
77 . PRO . 15013 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 15013 1
. ALA 2 2 15013 1
. MET 3 3 15013 1
. GLY 4 4 15013 1
. PRO 5 5 15013 1
. ARG 6 6 15013 1
. GLU 7 7 15013 1
. VAL 8 8 15013 1
. THR 9 9 15013 1
. MET 10 10 15013 1
. LYS 11 11 15013 1
. LYS 12 12 15013 1
. GLY 13 13 15013 1
. ASP 14 14 15013 1
. ILE 15 15 15013 1
. LEU 16 16 15013 1
. THR 17 17 15013 1
. LEU 18 18 15013 1
. LEU 19 19 15013 1
. ASN 20 20 15013 1
. SER 21 21 15013 1
. THR 22 22 15013 1
. ASN 23 23 15013 1
. LYS 24 24 15013 1
. ASP 25 25 15013 1
. TRP 26 26 15013 1
. TRP 27 27 15013 1
. LYS 28 28 15013 1
. VAL 29 29 15013 1
. GLU 30 30 15013 1
. VAL 31 31 15013 1
. ASN 32 32 15013 1
. ASP 33 33 15013 1
. ARG 34 34 15013 1
. GLN 35 35 15013 1
. GLY 36 36 15013 1
. PHE 37 37 15013 1
. VAL 38 38 15013 1
. PRO 39 39 15013 1
. ALA 40 40 15013 1
. ALA 41 41 15013 1
. TYR 42 42 15013 1
. VAL 43 43 15013 1
. LYS 44 44 15013 1
. LYS 45 45 15013 1
. LEU 46 46 15013 1
. ASP 47 47 15013 1
. SER 48 48 15013 1
. GLY 49 49 15013 1
. THR 50 50 15013 1
. GLY 51 51 15013 1
. LYS 52 52 15013 1
. GLU 53 53 15013 1
. LEU 54 54 15013 1
. VAL 55 55 15013 1
. LEU 56 56 15013 1
. ALA 57 57 15013 1
. LEU 58 58 15013 1
. TYR 59 59 15013 1
. ASP 60 60 15013 1
. TYR 61 61 15013 1
. GLN 62 62 15013 1
. GLU 63 63 15013 1
. SER 64 64 15013 1
. GLY 65 65 15013 1
. ASP 66 66 15013 1
. ASN 67 67 15013 1
. ALA 68 68 15013 1
. PRO 69 69 15013 1
. SER 70 70 15013 1
. TYR 71 71 15013 1
. SER 72 72 15013 1
. PRO 73 73 15013 1
. PRO 74 74 15013 1
. PRO 75 75 15013 1
. PRO 76 76 15013 1
. PRO 77 77 15013 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 15013
_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 $SPCp41 . . 'no natural source' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 15013 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 15013
_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 $SPCp41 . 'recombinant technology' 'Escherichia coli' . . . . . . . . . . . . . . . . . . . . . pETM11 . . . . . . 15013 1
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Sample.Sf_category sample
_Sample.Sf_framecode sample_1
_Sample.Entry_ID 15013
_Sample.ID 1
_Sample.Type solution
_Sample.Sub_type .
_Sample.Details .
_Sample.Aggregate_sample_number .
_Sample.Solvent_system '90% H2O/10% D2O'
_Sample.Preparation_date .
_Sample.Preparation_expiration_date .
_Sample.Polycrystallization_protocol .
_Sample.Single_crystal_protocol .
_Sample.Crystal_grow_apparatus .
_Sample.Crystal_grow_atmosphere .
_Sample.Crystal_grow_details .
_Sample.Crystal_grow_method .
_Sample.Crystal_grow_method_cit_ID .
_Sample.Crystal_grow_pH .
_Sample.Crystal_grow_pH_range .
_Sample.Crystal_grow_pressure .
_Sample.Crystal_grow_pressure_esd .
_Sample.Crystal_grow_seeding .
_Sample.Crystal_grow_seeding_cit_ID .
_Sample.Crystal_grow_temp .
_Sample.Crystal_grow_temp_details .
_Sample.Crystal_grow_temp_esd .
_Sample.Crystal_grow_time .
_Sample.Oriented_sample_prep_protocol .
_Sample.Lyophilization_cryo_protectant .
_Sample.Storage_protocol .
loop_
_Sample_component.ID
_Sample_component.Mol_common_name
_Sample_component.Isotopic_labeling
_Sample_component.Assembly_ID
_Sample_component.Assembly_label
_Sample_component.Entity_ID
_Sample_component.Entity_label
_Sample_component.Product_ID
_Sample_component.Type
_Sample_component.Concentration_val
_Sample_component.Concentration_val_min
_Sample_component.Concentration_val_max
_Sample_component.Concentration_val_units
_Sample_component.Concentration_val_err
_Sample_component.Vendor
_Sample_component.Vendor_product_name
_Sample_component.Vendor_product_code
_Sample_component.Entry_ID
_Sample_component.Sample_ID
1 SPCp41 '[U-98% 13C; U-98% 15N]' . . 1 $SPCp41 . . 1 . . mM . . . . 15013 1
2 glycine . . . . . . . 20 . . mM . . . . 15013 1
3 H2O . . . . . . . 90 . . % . . . . 15013 1
4 D2O . . . . . . . 10 . . % . . . . 15013 1
stop_
save_
save_sample_2
_Sample.Sf_category sample
_Sample.Sf_framecode sample_2
_Sample.Entry_ID 15013
_Sample.ID 2
_Sample.Type solution
_Sample.Sub_type .
_Sample.Details .
_Sample.Aggregate_sample_number .
_Sample.Solvent_system '90% H2O/10% D2O'
_Sample.Preparation_date .
_Sample.Preparation_expiration_date .
_Sample.Polycrystallization_protocol .
_Sample.Single_crystal_protocol .
_Sample.Crystal_grow_apparatus .
_Sample.Crystal_grow_atmosphere .
_Sample.Crystal_grow_details .
_Sample.Crystal_grow_method .
_Sample.Crystal_grow_method_cit_ID .
_Sample.Crystal_grow_pH .
_Sample.Crystal_grow_pH_range .
_Sample.Crystal_grow_pressure .
_Sample.Crystal_grow_pressure_esd .
_Sample.Crystal_grow_seeding .
_Sample.Crystal_grow_seeding_cit_ID .
_Sample.Crystal_grow_temp .
_Sample.Crystal_grow_temp_details .
_Sample.Crystal_grow_temp_esd .
_Sample.Crystal_grow_time .
_Sample.Oriented_sample_prep_protocol .
_Sample.Lyophilization_cryo_protectant .
_Sample.Storage_protocol .
loop_
_Sample_component.ID
_Sample_component.Mol_common_name
_Sample_component.Isotopic_labeling
_Sample_component.Assembly_ID
_Sample_component.Assembly_label
_Sample_component.Entity_ID
_Sample_component.Entity_label
_Sample_component.Product_ID
_Sample_component.Type
_Sample_component.Concentration_val
_Sample_component.Concentration_val_min
_Sample_component.Concentration_val_max
_Sample_component.Concentration_val_units
_Sample_component.Concentration_val_err
_Sample_component.Vendor
_Sample_component.Vendor_product_name
_Sample_component.Vendor_product_code
_Sample_component.Entry_ID
_Sample_component.Sample_ID
1 SPCp41 '[U-98% 15N]' . . 1 $SPCp41 . . 1 . . mM . . . . 15013 2
2 glycine . . . . . . . 20 . . mM . . . . 15013 2
3 H2O . . . . . . . 90 . . % . . . . 15013 2
4 D2O . . . . . . . 10 . . % . . . . 15013 2
stop_
save_
save_sample_3
_Sample.Sf_category sample
_Sample.Sf_framecode sample_3
_Sample.Entry_ID 15013
_Sample.ID 3
_Sample.Type solution
_Sample.Sub_type .
_Sample.Details .
_Sample.Aggregate_sample_number .
_Sample.Solvent_system '90% H2O/10% D2O'
_Sample.Preparation_date .
_Sample.Preparation_expiration_date .
_Sample.Polycrystallization_protocol .
_Sample.Single_crystal_protocol .
_Sample.Crystal_grow_apparatus .
_Sample.Crystal_grow_atmosphere .
_Sample.Crystal_grow_details .
_Sample.Crystal_grow_method .
_Sample.Crystal_grow_method_cit_ID .
_Sample.Crystal_grow_pH .
_Sample.Crystal_grow_pH_range .
_Sample.Crystal_grow_pressure .
_Sample.Crystal_grow_pressure_esd .
_Sample.Crystal_grow_seeding .
_Sample.Crystal_grow_seeding_cit_ID .
_Sample.Crystal_grow_temp .
_Sample.Crystal_grow_temp_details .
_Sample.Crystal_grow_temp_esd .
_Sample.Crystal_grow_time .
_Sample.Oriented_sample_prep_protocol .
_Sample.Lyophilization_cryo_protectant .
_Sample.Storage_protocol .
loop_
_Sample_component.ID
_Sample_component.Mol_common_name
_Sample_component.Isotopic_labeling
_Sample_component.Assembly_ID
_Sample_component.Assembly_label
_Sample_component.Entity_ID
_Sample_component.Entity_label
_Sample_component.Product_ID
_Sample_component.Type
_Sample_component.Concentration_val
_Sample_component.Concentration_val_min
_Sample_component.Concentration_val_max
_Sample_component.Concentration_val_units
_Sample_component.Concentration_val_err
_Sample_component.Vendor
_Sample_component.Vendor_product_name
_Sample_component.Vendor_product_code
_Sample_component.Entry_ID
_Sample_component.Sample_ID
1 SPCp41 . . . 1 $SPCp41 . . 1 . . mM . . . . 15013 3
2 glycine . . . . . . . 20 . . mM . . . . 15013 3
3 H2O . . . . . . . 90 . . % . . . . 15013 3
4 D2O . . . . . . . 10 . . % . . . . 15013 3
stop_
save_
#######################
# Sample conditions #
#######################
save_sample_conditions_1
_Sample_condition_list.Sf_category sample_conditions
_Sample_condition_list.Sf_framecode sample_conditions_1
_Sample_condition_list.Entry_ID 15013
_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 3.5 . pH 15013 1
pressure 1 . atm 15013 1
temperature 303 . K 15013 1
stop_
save_
############################
# Computer software used #
############################
save_SPARKY
_Software.Sf_category software
_Software.Sf_framecode SPARKY
_Software.Entry_ID 15013
_Software.ID 1
_Software.Name SPARKY
_Software.Version .
_Software.Details .
loop_
_Vendor.Name
_Vendor.Address
_Vendor.Electronic_address
_Vendor.Entry_ID
_Vendor.Software_ID
'T Goddard' . . 15013 1
stop_
loop_
_Task.Task
_Task.Entry_ID
_Task.Software_ID
'chemical shift assignment' 15013 1
'data analysis' 15013 1
'peak picking' 15013 1
stop_
save_
save_CYANA
_Software.Sf_category software
_Software.Sf_framecode CYANA
_Software.Entry_ID 15013
_Software.ID 2
_Software.Name CYANA
_Software.Version .
_Software.Details .
loop_
_Vendor.Name
_Vendor.Address
_Vendor.Electronic_address
_Vendor.Entry_ID
_Vendor.Software_ID
'P Guntert, C Mumenthaler and K Wuthrich' . . 15013 2
stop_
loop_
_Task.Task
_Task.Entry_ID
_Task.Software_ID
'structure solution' 15013 2
stop_
save_
save_xwinnmr
_Software.Sf_category software
_Software.Sf_framecode xwinnmr
_Software.Entry_ID 15013
_Software.ID 3
_Software.Name xwinnmr
_Software.Version .
_Software.Details .
loop_
_Vendor.Name
_Vendor.Address
_Vendor.Electronic_address
_Vendor.Entry_ID
_Vendor.Software_ID
'Bruker Biospin' . . 15013 3
stop_
loop_
_Task.Task
_Task.Entry_ID
_Task.Software_ID
collection 15013 3
processing 15013 3
stop_
save_
save_TOPSPIN
_Software.Sf_category software
_Software.Sf_framecode TOPSPIN
_Software.Entry_ID 15013
_Software.ID 4
_Software.Name TOPSPIN
_Software.Version .
_Software.Details .
loop_
_Vendor.Name
_Vendor.Address
_Vendor.Electronic_address
_Vendor.Entry_ID
_Vendor.Software_ID
'Bruker Biospin' . . 15013 4
stop_
loop_
_Task.Task
_Task.Entry_ID
_Task.Software_ID
collection 15013 4
processing 15013 4
stop_
save_
save_VNMRJ
_Software.Sf_category software
_Software.Sf_framecode VNMRJ
_Software.Entry_ID 15013
_Software.ID 5
_Software.Name VNMRJ
_Software.Version .
_Software.Details .
loop_
_Vendor.Name
_Vendor.Address
_Vendor.Electronic_address
_Vendor.Entry_ID
_Vendor.Software_ID
Varian . . 15013 5
stop_
loop_
_Task.Task
_Task.Entry_ID
_Task.Software_ID
collection 15013 5
stop_
save_
save_NMRPipe
_Software.Sf_category software
_Software.Sf_framecode NMRPipe
_Software.Entry_ID 15013
_Software.ID 6
_Software.Name NMRPipe
_Software.Version .
_Software.Details .
loop_
_Vendor.Name
_Vendor.Address
_Vendor.Electronic_address
_Vendor.Entry_ID
_Vendor.Software_ID
'F Delaglio, S Grzesiek, GW Vuister, G Zhu, J Pfeifer and A Bax' . . 15013 6
stop_
loop_
_Task.Task
_Task.Entry_ID
_Task.Software_ID
processing 15013 6
stop_
save_
save_NMRView
_Software.Sf_category software
_Software.Sf_framecode NMRView
_Software.Entry_ID 15013
_Software.ID 7
_Software.Name NMRView
_Software.Version .
_Software.Details .
loop_
_Vendor.Name
_Vendor.Address
_Vendor.Electronic_address
_Vendor.Entry_ID
_Vendor.Software_ID
'B Johnson, One Moon Scientific' . . 15013 7
stop_
loop_
_Task.Task
_Task.Entry_ID
_Task.Software_ID
'chemical shift assignment' 15013 7
'data analysis' 15013 7
'peak picking' 15013 7
stop_
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_1
_NMR_spectrometer.Sf_category NMR_spectrometer
_NMR_spectrometer.Sf_framecode spectrometer_1
_NMR_spectrometer.Entry_ID 15013
_NMR_spectrometer.ID 1
_NMR_spectrometer.Details .
_NMR_spectrometer.Manufacturer Varian
_NMR_spectrometer.Model 'Varian NMR System'
_NMR_spectrometer.Serial_number .
_NMR_spectrometer.Field_strength 600
save_
save_spectrometer_2
_NMR_spectrometer.Sf_category NMR_spectrometer
_NMR_spectrometer.Sf_framecode spectrometer_2
_NMR_spectrometer.Entry_ID 15013
_NMR_spectrometer.ID 2
_NMR_spectrometer.Details .
_NMR_spectrometer.Manufacturer Bruker
_NMR_spectrometer.Model Avance
_NMR_spectrometer.Serial_number .
_NMR_spectrometer.Field_strength 800
save_
save_NMR_spectrometer_list
_NMR_spectrometer_list.Sf_category NMR_spectrometer_list
_NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list
_NMR_spectrometer_list.Entry_ID 15013
_NMR_spectrometer_list.ID 1
loop_
_NMR_spectrometer_view.ID
_NMR_spectrometer_view.Name
_NMR_spectrometer_view.Manufacturer
_NMR_spectrometer_view.Model
_NMR_spectrometer_view.Serial_number
_NMR_spectrometer_view.Field_strength
_NMR_spectrometer_view.Details
_NMR_spectrometer_view.Citation_ID
_NMR_spectrometer_view.Citation_label
_NMR_spectrometer_view.Entry_ID
_NMR_spectrometer_view.NMR_spectrometer_list_ID
1 spectrometer_2 Bruker Avance . 800 . . . 15013 1
2 spectrometer_1 Varian 'Varian NMR System' . 600 . . . 15013 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 15013
_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 CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15013 1
2 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15013 1
3 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15013 1
4 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15013 1
5 '3D HN(CO)CA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15013 1
6 '3D 1H-15N NOESY' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15013 1
7 '3D 1H-15N TOCSY' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15013 1
8 '2D 1H-1H NOESY' no . . . . . . . . . . 3 $sample_3 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15013 1
9 '2D 1H-15N HSQC' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15013 1
10 '2D 1H-15N HSQC' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 15013 1
11 '3D HCCH-TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15013 1
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference_1
_Chem_shift_reference.Sf_category chem_shift_reference
_Chem_shift_reference.Sf_framecode chemical_shift_reference_1
_Chem_shift_reference.Entry_ID 15013
_Chem_shift_reference.ID 1
_Chem_shift_reference.Details .
loop_
_Chem_shift_ref.Atom_type
_Chem_shift_ref.Atom_isotope_number
_Chem_shift_ref.Mol_common_name
_Chem_shift_ref.Atom_group
_Chem_shift_ref.Concentration_val
_Chem_shift_ref.Concentration_units
_Chem_shift_ref.Solvent
_Chem_shift_ref.Rank
_Chem_shift_ref.Chem_shift_units
_Chem_shift_ref.Chem_shift_val
_Chem_shift_ref.Ref_method
_Chem_shift_ref.Ref_type
_Chem_shift_ref.Indirect_shift_ratio
_Chem_shift_ref.External_ref_loc
_Chem_shift_ref.External_ref_sample_geometry
_Chem_shift_ref.External_ref_axis
_Chem_shift_ref.Indirect_shift_ratio_cit_ID
_Chem_shift_ref.Indirect_shift_ratio_cit_label
_Chem_shift_ref.Ref_correction_type
_Chem_shift_ref.Correction_val
_Chem_shift_ref.Correction_val_cit_ID
_Chem_shift_ref.Correction_val_cit_label
_Chem_shift_ref.Entry_ID
_Chem_shift_ref.Chem_shift_reference_ID
C 13 DSS 'methyl protons' . . . . ppm 0 . indirect 0.251449530 . . . 1 $entry_citation . . 1 $entry_citation 15013 1
H 1 DSS 'methyl protons' . . . . ppm 0 internal direct 1.0 . . . 1 $entry_citation . . 1 $entry_citation 15013 1
N 15 DSS 'methyl protons' . . . . ppm 0 . indirect 0.101329118 . . . 1 $entry_citation . . 1 $entry_citation 15013 1
stop_
save_
###################################
# Assigned chemical shift lists #
###################################
###################################################################
# Chemical Shift Ambiguity Index Value Definitions #
# #
# The values other than 1 are used for those atoms with different #
# chemical shifts that cannot be assigned to stereospecific atoms #
# or to specific residues or chains. #
# #
# Index Value Definition #
# #
# 1 Unique (including isolated methyl protons, #
# geminal atoms, and geminal methyl #
# groups with identical chemical shifts) #
# (e.g. ILE HD11, HD12, HD13 protons) #
# 2 Ambiguity of geminal atoms or geminal methyl #
# proton groups (e.g. ASP HB2 and HB3 #
# protons, LEU CD1 and CD2 carbons, or #
# LEU HD11, HD12, HD13 and HD21, HD22, #
# HD23 methyl protons) #
# 3 Aromatic atoms on opposite sides of #
# symmetrical rings (e.g. TYR HE1 and HE2 #
# protons) #
# 4 Intraresidue ambiguities (e.g. LYS HG and #
# HD protons or TRP HZ2 and HZ3 protons) #
# 5 Interresidue ambiguities (LYS 12 vs. LYS 27) #
# 6 Intermolecular ambiguities (e.g. ASP 31 CA #
# in monomer 1 and ASP 31 CA in monomer 2 #
# of an asymmetrical homodimer, duplex #
# DNA assignments, or other assignments #
# that may apply to atoms in one or more #
# molecule in the molecular assembly) #
# 9 Ambiguous, specific ambiguity not defined #
# #
###################################################################
save_assigned_chem_shift_list_1
_Assigned_chem_shift_list.Sf_category assigned_chemical_shifts
_Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1
_Assigned_chem_shift_list.Entry_ID 15013
_Assigned_chem_shift_list.ID 1
_Assigned_chem_shift_list.Sample_condition_list_ID 1
_Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1
_Assigned_chem_shift_list.Chem_shift_reference_ID 1
_Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1
_Assigned_chem_shift_list.Chem_shift_1H_err .
_Assigned_chem_shift_list.Chem_shift_13C_err .
_Assigned_chem_shift_list.Chem_shift_15N_err .
_Assigned_chem_shift_list.Chem_shift_31P_err .
_Assigned_chem_shift_list.Chem_shift_2H_err .
_Assigned_chem_shift_list.Chem_shift_19F_err .
_Assigned_chem_shift_list.Error_derivation_method .
_Assigned_chem_shift_list.Details .
_Assigned_chem_shift_list.Text_data_format .
_Assigned_chem_shift_list.Text_data .
loop_
_Chem_shift_experiment.Experiment_ID
_Chem_shift_experiment.Experiment_name
_Chem_shift_experiment.Sample_ID
_Chem_shift_experiment.Sample_label
_Chem_shift_experiment.Sample_state
_Chem_shift_experiment.Entry_ID
_Chem_shift_experiment.Assigned_chem_shift_list_ID
2 '3D HNCACB' . . . 15013 1
3 '3D HNCO' . . . 15013 1
8 '2D 1H-1H NOESY' . . . 15013 1
11 '3D HCCH-TOCSY' . . . 15013 1
stop_
loop_
_Chem_shift_software.Software_ID
_Chem_shift_software.Software_label
_Chem_shift_software.Method_ID
_Chem_shift_software.Method_label
_Chem_shift_software.Entry_ID
_Chem_shift_software.Assigned_chem_shift_list_ID
1 $SPARKY . . 15013 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 HA2 H 1 3.849 0.02 . . . . . . 1 GLY HA2 . 15013 1
2 . 1 1 1 1 GLY HA3 H 1 3.849 0.02 . . . . . . 1 GLY HA3 . 15013 1
3 . 1 1 2 2 ALA H H 1 8.587 0.002 . . . . . . 2 ALA H . 15013 1
4 . 1 1 2 2 ALA HA H 1 4.359 0.001 . . . . . . 2 ALA HA . 15013 1
5 . 1 1 2 2 ALA HB1 H 1 1.387 0.02 . . . . . . 2 ALA HB1 . 15013 1
6 . 1 1 2 2 ALA HB2 H 1 1.387 0.02 . . . . . . 2 ALA HB2 . 15013 1
7 . 1 1 2 2 ALA HB3 H 1 1.387 0.02 . . . . . . 2 ALA HB3 . 15013 1
8 . 1 1 2 2 ALA N N 15 123.863 0.05 . . . . . . 2 ALA N . 15013 1
9 . 1 1 3 3 MET H H 1 8.460 0.02 . . . . . . 3 MET H . 15013 1
10 . 1 1 3 3 MET HA H 1 4.534 0.02 . . . . . . 3 MET HA . 15013 1
11 . 1 1 3 3 MET HB2 H 1 2.015 0.002 . . . . . . 3 MET HB2 . 15013 1
12 . 1 1 3 3 MET HB3 H 1 2.101 0.02 . . . . . . 3 MET HB3 . 15013 1
13 . 1 1 3 3 MET HG2 H 1 2.568 0.02 . . . . . . 3 MET HG2 . 15013 1
14 . 1 1 3 3 MET HG3 H 1 2.621 0.02 . . . . . . 3 MET HG3 . 15013 1
15 . 1 1 3 3 MET C C 13 172.802 0.05 . . . . . . 3 MET C . 15013 1
16 . 1 1 3 3 MET CA C 13 55.423 0.05 . . . . . . 3 MET CA . 15013 1
17 . 1 1 3 3 MET CB C 13 32.969 0.05 . . . . . . 3 MET CB . 15013 1
18 . 1 1 3 3 MET CG C 13 31.107 0.041 . . . . . . 3 MET CG . 15013 1
19 . 1 1 3 3 MET N N 15 119.757 0.05 . . . . . . 3 MET N . 15013 1
20 . 1 1 4 4 GLY H H 1 8.472 0.178 . . . . . . 4 GLY H . 15013 1
21 . 1 1 4 4 GLY HA2 H 1 4.034 0.02 . . . . . . 4 GLY HA2 . 15013 1
22 . 1 1 4 4 GLY HA3 H 1 4.162 0.02 . . . . . . 4 GLY HA3 . 15013 1
23 . 1 1 4 4 GLY CA C 13 44.822 0.05 . . . . . . 4 GLY CA . 15013 1
24 . 1 1 4 4 GLY N N 15 112.111 0.008 . . . . . . 4 GLY N . 15013 1
25 . 1 1 5 5 PRO HA H 1 4.458 0.02 . . . . . . 5 PRO HA . 15013 1
26 . 1 1 5 5 PRO HB2 H 1 1.926 0.02 . . . . . . 5 PRO HB2 . 15013 1
27 . 1 1 5 5 PRO HB3 H 1 2.282 0.002 . . . . . . 5 PRO HB3 . 15013 1
28 . 1 1 5 5 PRO HG2 H 1 1.990 0.02 . . . . . . 5 PRO HG2 . 15013 1
29 . 1 1 5 5 PRO HG3 H 1 1.990 0.02 . . . . . . 5 PRO HG3 . 15013 1
30 . 1 1 5 5 PRO HD2 H 1 3.612 0.001 . . . . . . 5 PRO HD2 . 15013 1
31 . 1 1 5 5 PRO HD3 H 1 3.612 0.001 . . . . . . 5 PRO HD3 . 15013 1
32 . 1 1 5 5 PRO C C 13 177.247 0.05 . . . . . . 5 PRO C . 15013 1
33 . 1 1 5 5 PRO CA C 13 63.418 0.05 . . . . . . 5 PRO CA . 15013 1
34 . 1 1 5 5 PRO CB C 13 32.457 0.05 . . . . . . 5 PRO CB . 15013 1
35 . 1 1 5 5 PRO CG C 13 27.389 0.054 . . . . . . 5 PRO CG . 15013 1
36 . 1 1 5 5 PRO CD C 13 50.152 0.042 . . . . . . 5 PRO CD . 15013 1
37 . 1 1 6 6 ARG H H 1 8.495 0.003 . . . . . . 6 ARG H . 15013 1
38 . 1 1 6 6 ARG HA H 1 4.383 0.001 . . . . . . 6 ARG HA . 15013 1
39 . 1 1 6 6 ARG HB2 H 1 1.795 0.02 . . . . . . 6 ARG HB2 . 15013 1
40 . 1 1 6 6 ARG HB3 H 1 1.913 0.005 . . . . . . 6 ARG HB3 . 15013 1
41 . 1 1 6 6 ARG HG2 H 1 1.654 0.02 . . . . . . 6 ARG HG2 . 15013 1
42 . 1 1 6 6 ARG HG3 H 1 1.715 0.02 . . . . . . 6 ARG HG3 . 15013 1
43 . 1 1 6 6 ARG HD2 H 1 3.220 0.004 . . . . . . 6 ARG HD2 . 15013 1
44 . 1 1 6 6 ARG HD3 H 1 3.220 0.004 . . . . . . 6 ARG HD3 . 15013 1
45 . 1 1 6 6 ARG HE H 1 7.183 0.006 . . . . . . 6 ARG HE . 15013 1
46 . 1 1 6 6 ARG C C 13 176.122 0.05 . . . . . . 6 ARG C . 15013 1
47 . 1 1 6 6 ARG CA C 13 56.200 0.003 . . . . . . 6 ARG CA . 15013 1
48 . 1 1 6 6 ARG CB C 13 30.942 0.013 . . . . . . 6 ARG CB . 15013 1
49 . 1 1 6 6 ARG CG C 13 27.187 0.021 . . . . . . 6 ARG CG . 15013 1
50 . 1 1 6 6 ARG CD C 13 43.673 0.036 . . . . . . 6 ARG CD . 15013 1
51 . 1 1 6 6 ARG N N 15 120.801 0.032 . . . . . . 6 ARG N . 15013 1
52 . 1 1 6 6 ARG NE N 15 115.328 0.013 . . . . . . 6 ARG NE . 15013 1
53 . 1 1 7 7 GLU H H 1 8.078 0.001 . . . . . . 7 GLU H . 15013 1
54 . 1 1 7 7 GLU HA H 1 4.593 0.02 . . . . . . 7 GLU HA . 15013 1
55 . 1 1 7 7 GLU HB2 H 1 1.950 0.02 . . . . . . 7 GLU HB2 . 15013 1
56 . 1 1 7 7 GLU HB3 H 1 2.084 0.02 . . . . . . 7 GLU HB3 . 15013 1
57 . 1 1 7 7 GLU HG2 H 1 2.393 0.02 . . . . . . 7 GLU HG2 . 15013 1
58 . 1 1 7 7 GLU HG3 H 1 2.393 0.02 . . . . . . 7 GLU HG3 . 15013 1
59 . 1 1 7 7 GLU C C 13 176.109 0.05 . . . . . . 7 GLU C . 15013 1
60 . 1 1 7 7 GLU CA C 13 55.792 0.005 . . . . . . 7 GLU CA . 15013 1
61 . 1 1 7 7 GLU CB C 13 30.050 0.001 . . . . . . 7 GLU CB . 15013 1
62 . 1 1 7 7 GLU CG C 13 33.743 0.013 . . . . . . 7 GLU CG . 15013 1
63 . 1 1 7 7 GLU N N 15 120.603 0.033 . . . . . . 7 GLU N . 15013 1
64 . 1 1 8 8 VAL H H 1 8.296 0.005 . . . . . . 8 VAL H . 15013 1
65 . 1 1 8 8 VAL HA H 1 4.096 0.001 . . . . . . 8 VAL HA . 15013 1
66 . 1 1 8 8 VAL HB H 1 1.920 0.02 . . . . . . 8 VAL HB . 15013 1
67 . 1 1 8 8 VAL HG11 H 1 0.753 0.02 . . . . . . 8 VAL HG11 . 15013 1
68 . 1 1 8 8 VAL HG12 H 1 0.753 0.02 . . . . . . 8 VAL HG12 . 15013 1
69 . 1 1 8 8 VAL HG13 H 1 0.753 0.02 . . . . . . 8 VAL HG13 . 15013 1
70 . 1 1 8 8 VAL HG21 H 1 0.828 0.02 . . . . . . 8 VAL HG21 . 15013 1
71 . 1 1 8 8 VAL HG22 H 1 0.828 0.02 . . . . . . 8 VAL HG22 . 15013 1
72 . 1 1 8 8 VAL HG23 H 1 0.828 0.02 . . . . . . 8 VAL HG23 . 15013 1
73 . 1 1 8 8 VAL C C 13 174.660 0.05 . . . . . . 8 VAL C . 15013 1
74 . 1 1 8 8 VAL CA C 13 62.866 0.001 . . . . . . 8 VAL CA . 15013 1
75 . 1 1 8 8 VAL CB C 13 33.474 0.003 . . . . . . 8 VAL CB . 15013 1
76 . 1 1 8 8 VAL CG1 C 13 21.125 0.099 . . . . . . 8 VAL CG1 . 15013 1
77 . 1 1 8 8 VAL CG2 C 13 21.861 0.079 . . . . . . 8 VAL CG2 . 15013 1
78 . 1 1 8 8 VAL N N 15 121.939 0.016 . . . . . . 8 VAL N . 15013 1
79 . 1 1 9 9 THR H H 1 7.972 0.023 . . . . . . 9 THR H . 15013 1
80 . 1 1 9 9 THR HA H 1 4.803 0.02 . . . . . . 9 THR HA . 15013 1
81 . 1 1 9 9 THR HB H 1 4.063 0.001 . . . . . . 9 THR HB . 15013 1
82 . 1 1 9 9 THR HG21 H 1 1.136 0.02 . . . . . . 9 THR HG21 . 15013 1
83 . 1 1 9 9 THR HG22 H 1 1.136 0.02 . . . . . . 9 THR HG22 . 15013 1
84 . 1 1 9 9 THR HG23 H 1 1.136 0.02 . . . . . . 9 THR HG23 . 15013 1
85 . 1 1 9 9 THR C C 13 173.345 0.05 . . . . . . 9 THR C . 15013 1
86 . 1 1 9 9 THR CA C 13 61.409 0.010 . . . . . . 9 THR CA . 15013 1
87 . 1 1 9 9 THR CB C 13 70.989 0.002 . . . . . . 9 THR CB . 15013 1
88 . 1 1 9 9 THR CG2 C 13 24.631 0.05 . . . . . . 9 THR CG2 . 15013 1
89 . 1 1 9 9 THR N N 15 120.018 0.036 . . . . . . 9 THR N . 15013 1
90 . 1 1 10 10 MET H H 1 9.097 0.023 . . . . . . 10 MET H . 15013 1
91 . 1 1 10 10 MET HA H 1 4.667 0.006 . . . . . . 10 MET HA . 15013 1
92 . 1 1 10 10 MET HB2 H 1 1.992 0.009 . . . . . . 10 MET HB2 . 15013 1
93 . 1 1 10 10 MET HB3 H 1 2.240 0.022 . . . . . . 10 MET HB3 . 15013 1
94 . 1 1 10 10 MET HG2 H 1 2.458 0.02 . . . . . . 10 MET HG2 . 15013 1
95 . 1 1 10 10 MET HG3 H 1 2.655 0.002 . . . . . . 10 MET HG3 . 15013 1
96 . 1 1 10 10 MET C C 13 173.829 0.05 . . . . . . 10 MET C . 15013 1
97 . 1 1 10 10 MET CA C 13 55.224 0.031 . . . . . . 10 MET CA . 15013 1
98 . 1 1 10 10 MET CB C 13 36.409 0.05 . . . . . . 10 MET CB . 15013 1
99 . 1 1 10 10 MET CG C 13 32.477 0.030 . . . . . . 10 MET CG . 15013 1
100 . 1 1 10 10 MET N N 15 122.967 0.038 . . . . . . 10 MET N . 15013 1
101 . 1 1 11 11 LYS H H 1 8.688 0.059 . . . . . . 11 LYS H . 15013 1
102 . 1 1 11 11 LYS HA H 1 4.871 0.001 . . . . . . 11 LYS HA . 15013 1
103 . 1 1 11 11 LYS HB2 H 1 1.671 0.02 . . . . . . 11 LYS HB2 . 15013 1
104 . 1 1 11 11 LYS HB3 H 1 1.704 0.02 . . . . . . 11 LYS HB3 . 15013 1
105 . 1 1 11 11 LYS HG2 H 1 1.382 0.02 . . . . . . 11 LYS HG2 . 15013 1
106 . 1 1 11 11 LYS HG3 H 1 1.406 0.02 . . . . . . 11 LYS HG3 . 15013 1
107 . 1 1 11 11 LYS C C 13 175.497 0.05 . . . . . . 11 LYS C . 15013 1
108 . 1 1 11 11 LYS CA C 13 53.481 0.025 . . . . . . 11 LYS CA . 15013 1
109 . 1 1 11 11 LYS CB C 13 34.507 0.007 . . . . . . 11 LYS CB . 15013 1
110 . 1 1 11 11 LYS CG C 13 24.763 0.041 . . . . . . 11 LYS CG . 15013 1
111 . 1 1 11 11 LYS CD C 13 29.089 0.030 . . . . . . 11 LYS CD . 15013 1
112 . 1 1 11 11 LYS CE C 13 41.979 0.026 . . . . . . 11 LYS CE . 15013 1
113 . 1 1 11 11 LYS N N 15 126.398 0.032 . . . . . . 11 LYS N . 15013 1
114 . 1 1 12 12 LYS H H 1 8.501 0.022 . . . . . . 12 LYS H . 15013 1
115 . 1 1 12 12 LYS HA H 1 3.295 0.002 . . . . . . 12 LYS HA . 15013 1
116 . 1 1 12 12 LYS HB2 H 1 1.456 0.02 . . . . . . 12 LYS HB2 . 15013 1
117 . 1 1 12 12 LYS HB3 H 1 1.610 0.02 . . . . . . 12 LYS HB3 . 15013 1
118 . 1 1 12 12 LYS HG2 H 1 1.100 0.02 . . . . . . 12 LYS HG2 . 15013 1
119 . 1 1 12 12 LYS HG3 H 1 1.166 0.02 . . . . . . 12 LYS HG3 . 15013 1
120 . 1 1 12 12 LYS HD2 H 1 1.654 0.02 . . . . . . 12 LYS HD2 . 15013 1
121 . 1 1 12 12 LYS HD3 H 1 1.654 0.02 . . . . . . 12 LYS HD3 . 15013 1
122 . 1 1 12 12 LYS C C 13 177.341 0.05 . . . . . . 12 LYS C . 15013 1
123 . 1 1 12 12 LYS CA C 13 58.620 0.016 . . . . . . 12 LYS CA . 15013 1
124 . 1 1 12 12 LYS CB C 13 32.722 0.014 . . . . . . 12 LYS CB . 15013 1
125 . 1 1 12 12 LYS CG C 13 24.545 0.032 . . . . . . 12 LYS CG . 15013 1
126 . 1 1 12 12 LYS CD C 13 29.750 0.060 . . . . . . 12 LYS CD . 15013 1
127 . 1 1 12 12 LYS CE C 13 42.320 0.050 . . . . . . 12 LYS CE . 15013 1
128 . 1 1 12 12 LYS N N 15 121.424 0.030 . . . . . . 12 LYS N . 15013 1
129 . 1 1 13 13 GLY H H 1 8.834 0.005 . . . . . . 13 GLY H . 15013 1
130 . 1 1 13 13 GLY HA2 H 1 3.522 0.001 . . . . . . 13 GLY HA2 . 15013 1
131 . 1 1 13 13 GLY HA3 H 1 4.482 0.001 . . . . . . 13 GLY HA3 . 15013 1
132 . 1 1 13 13 GLY C C 13 174.350 0.05 . . . . . . 13 GLY C . 15013 1
133 . 1 1 13 13 GLY CA C 13 45.024 0.002 . . . . . . 13 GLY CA . 15013 1
134 . 1 1 13 13 GLY N N 15 115.551 0.021 . . . . . . 13 GLY N . 15013 1
135 . 1 1 14 14 ASP H H 1 8.489 0.007 . . . . . . 14 ASP H . 15013 1
136 . 1 1 14 14 ASP HA H 1 4.564 0.001 . . . . . . 14 ASP HA . 15013 1
137 . 1 1 14 14 ASP HB2 H 1 2.615 0.02 . . . . . . 14 ASP HB2 . 15013 1
138 . 1 1 14 14 ASP HB3 H 1 2.857 0.02 . . . . . . 14 ASP HB3 . 15013 1
139 . 1 1 14 14 ASP C C 13 174.595 0.05 . . . . . . 14 ASP C . 15013 1
140 . 1 1 14 14 ASP CA C 13 55.453 0.003 . . . . . . 14 ASP CA . 15013 1
141 . 1 1 14 14 ASP CB C 13 41.349 0.004 . . . . . . 14 ASP CB . 15013 1
142 . 1 1 14 14 ASP N N 15 121.772 0.019 . . . . . . 14 ASP N . 15013 1
143 . 1 1 15 15 ILE H H 1 8.118 0.018 . . . . . . 15 ILE H . 15013 1
144 . 1 1 15 15 ILE HA H 1 5.071 0.02 . . . . . . 15 ILE HA . 15013 1
145 . 1 1 15 15 ILE HB H 1 1.766 0.02 . . . . . . 15 ILE HB . 15013 1
146 . 1 1 15 15 ILE HG12 H 1 1.103 0.02 . . . . . . 15 ILE HG12 . 15013 1
147 . 1 1 15 15 ILE HG13 H 1 1.669 0.02 . . . . . . 15 ILE HG13 . 15013 1
148 . 1 1 15 15 ILE HG21 H 1 0.888 0.02 . . . . . . 15 ILE HG21 . 15013 1
149 . 1 1 15 15 ILE HG22 H 1 0.888 0.02 . . . . . . 15 ILE HG22 . 15013 1
150 . 1 1 15 15 ILE HG23 H 1 0.888 0.02 . . . . . . 15 ILE HG23 . 15013 1
151 . 1 1 15 15 ILE HD11 H 1 0.847 0.02 . . . . . . 15 ILE HD11 . 15013 1
152 . 1 1 15 15 ILE HD12 H 1 0.847 0.02 . . . . . . 15 ILE HD12 . 15013 1
153 . 1 1 15 15 ILE HD13 H 1 0.847 0.02 . . . . . . 15 ILE HD13 . 15013 1
154 . 1 1 15 15 ILE C C 13 176.683 0.05 . . . . . . 15 ILE C . 15013 1
155 . 1 1 15 15 ILE CA C 13 60.407 0.012 . . . . . . 15 ILE CA . 15013 1
156 . 1 1 15 15 ILE CB C 13 38.623 0.020 . . . . . . 15 ILE CB . 15013 1
157 . 1 1 15 15 ILE CG1 C 13 28.160 0.051 . . . . . . 15 ILE CG1 . 15013 1
158 . 1 1 15 15 ILE CG2 C 13 19.021 0.034 . . . . . . 15 ILE CG2 . 15013 1
159 . 1 1 15 15 ILE CD1 C 13 12.954 0.05 . . . . . . 15 ILE CD1 . 15013 1
160 . 1 1 15 15 ILE N N 15 120.153 0.034 . . . . . . 15 ILE N . 15013 1
161 . 1 1 16 16 LEU H H 1 9.280 0.007 . . . . . . 16 LEU H . 15013 1
162 . 1 1 16 16 LEU HA H 1 4.996 0.001 . . . . . . 16 LEU HA . 15013 1
163 . 1 1 16 16 LEU HB2 H 1 1.425 0.02 . . . . . . 16 LEU HB2 . 15013 1
164 . 1 1 16 16 LEU HB3 H 1 1.645 0.02 . . . . . . 16 LEU HB3 . 15013 1
165 . 1 1 16 16 LEU HG H 1 1.584 0.02 . . . . . . 16 LEU HG . 15013 1
166 . 1 1 16 16 LEU HD11 H 1 0.865 0.02 . . . . . . 16 LEU HD11 . 15013 1
167 . 1 1 16 16 LEU HD12 H 1 0.865 0.02 . . . . . . 16 LEU HD12 . 15013 1
168 . 1 1 16 16 LEU HD13 H 1 0.865 0.02 . . . . . . 16 LEU HD13 . 15013 1
169 . 1 1 16 16 LEU HD21 H 1 0.893 0.02 . . . . . . 16 LEU HD21 . 15013 1
170 . 1 1 16 16 LEU HD22 H 1 0.893 0.02 . . . . . . 16 LEU HD22 . 15013 1
171 . 1 1 16 16 LEU HD23 H 1 0.893 0.02 . . . . . . 16 LEU HD23 . 15013 1
172 . 1 1 16 16 LEU C C 13 175.911 0.05 . . . . . . 16 LEU C . 15013 1
173 . 1 1 16 16 LEU CA C 13 54.216 0.038 . . . . . . 16 LEU CA . 15013 1
174 . 1 1 16 16 LEU CB C 13 44.419 0.006 . . . . . . 16 LEU CB . 15013 1
175 . 1 1 16 16 LEU CG C 13 28.602 0.018 . . . . . . 16 LEU CG . 15013 1
176 . 1 1 16 16 LEU CD2 C 13 27.891 0.05 . . . . . . 16 LEU CD2 . 15013 1
177 . 1 1 16 16 LEU N N 15 126.959 0.018 . . . . . . 16 LEU N . 15013 1
178 . 1 1 17 17 THR H H 1 8.477 0.002 . . . . . . 17 THR H . 15013 1
179 . 1 1 17 17 THR HA H 1 4.569 0.001 . . . . . . 17 THR HA . 15013 1
180 . 1 1 17 17 THR HB H 1 4.099 0.003 . . . . . . 17 THR HB . 15013 1
181 . 1 1 17 17 THR HG21 H 1 1.154 0.02 . . . . . . 17 THR HG21 . 15013 1
182 . 1 1 17 17 THR HG22 H 1 1.154 0.02 . . . . . . 17 THR HG22 . 15013 1
183 . 1 1 17 17 THR HG23 H 1 1.154 0.02 . . . . . . 17 THR HG23 . 15013 1
184 . 1 1 17 17 THR C C 13 173.933 0.05 . . . . . . 17 THR C . 15013 1
185 . 1 1 17 17 THR CA C 13 63.734 0.018 . . . . . . 17 THR CA . 15013 1
186 . 1 1 17 17 THR CB C 13 69.962 0.005 . . . . . . 17 THR CB . 15013 1
187 . 1 1 17 17 THR N N 15 117.328 0.005 . . . . . . 17 THR N . 15013 1
188 . 1 1 18 18 LEU H H 1 8.787 0.004 . . . . . . 18 LEU H . 15013 1
189 . 1 1 18 18 LEU HA H 1 4.407 0.002 . . . . . . 18 LEU HA . 15013 1
190 . 1 1 18 18 LEU HB2 H 1 1.122 0.02 . . . . . . 18 LEU HB2 . 15013 1
191 . 1 1 18 18 LEU HB3 H 1 1.770 0.02 . . . . . . 18 LEU HB3 . 15013 1
192 . 1 1 18 18 LEU HG H 1 1.146 0.02 . . . . . . 18 LEU HG . 15013 1
193 . 1 1 18 18 LEU HD11 H 1 0.391 0.02 . . . . . . 18 LEU HD11 . 15013 1
194 . 1 1 18 18 LEU HD12 H 1 0.391 0.02 . . . . . . 18 LEU HD12 . 15013 1
195 . 1 1 18 18 LEU HD13 H 1 0.391 0.02 . . . . . . 18 LEU HD13 . 15013 1
196 . 1 1 18 18 LEU HD21 H 1 0.682 0.02 . . . . . . 18 LEU HD21 . 15013 1
197 . 1 1 18 18 LEU HD22 H 1 0.682 0.02 . . . . . . 18 LEU HD22 . 15013 1
198 . 1 1 18 18 LEU HD23 H 1 0.682 0.02 . . . . . . 18 LEU HD23 . 15013 1
199 . 1 1 18 18 LEU C C 13 174.874 0.05 . . . . . . 18 LEU C . 15013 1
200 . 1 1 18 18 LEU CA C 13 54.703 0.016 . . . . . . 18 LEU CA . 15013 1
201 . 1 1 18 18 LEU CB C 13 43.415 0.028 . . . . . . 18 LEU CB . 15013 1
202 . 1 1 18 18 LEU CG C 13 26.964 0.030 . . . . . . 18 LEU CG . 15013 1
203 . 1 1 18 18 LEU CD1 C 13 25.507 0.049 . . . . . . 18 LEU CD1 . 15013 1
204 . 1 1 18 18 LEU CD2 C 13 24.015 0.041 . . . . . . 18 LEU CD2 . 15013 1
205 . 1 1 18 18 LEU N N 15 129.268 0.022 . . . . . . 18 LEU N . 15013 1
206 . 1 1 19 19 LEU H H 1 8.973 0.003 . . . . . . 19 LEU H . 15013 1
207 . 1 1 19 19 LEU HA H 1 4.494 0.001 . . . . . . 19 LEU HA . 15013 1
208 . 1 1 19 19 LEU HB2 H 1 1.155 0.02 . . . . . . 19 LEU HB2 . 15013 1
209 . 1 1 19 19 LEU HB3 H 1 1.411 0.02 . . . . . . 19 LEU HB3 . 15013 1
210 . 1 1 19 19 LEU HG H 1 1.407 0.001 . . . . . . 19 LEU HG . 15013 1
211 . 1 1 19 19 LEU HD11 H 1 0.746 0.02 . . . . . . 19 LEU HD11 . 15013 1
212 . 1 1 19 19 LEU HD12 H 1 0.746 0.02 . . . . . . 19 LEU HD12 . 15013 1
213 . 1 1 19 19 LEU HD13 H 1 0.746 0.02 . . . . . . 19 LEU HD13 . 15013 1
214 . 1 1 19 19 LEU HD21 H 1 0.704 0.02 . . . . . . 19 LEU HD21 . 15013 1
215 . 1 1 19 19 LEU HD22 H 1 0.704 0.02 . . . . . . 19 LEU HD22 . 15013 1
216 . 1 1 19 19 LEU HD23 H 1 0.704 0.02 . . . . . . 19 LEU HD23 . 15013 1
217 . 1 1 19 19 LEU C C 13 177.750 0.05 . . . . . . 19 LEU C . 15013 1
218 . 1 1 19 19 LEU CA C 13 55.406 0.035 . . . . . . 19 LEU CA . 15013 1
219 . 1 1 19 19 LEU CB C 13 43.213 0.017 . . . . . . 19 LEU CB . 15013 1
220 . 1 1 19 19 LEU CG C 13 27.092 0.028 . . . . . . 19 LEU CG . 15013 1
221 . 1 1 19 19 LEU CD1 C 13 25.978 0.027 . . . . . . 19 LEU CD1 . 15013 1
222 . 1 1 19 19 LEU CD2 C 13 22.292 0.045 . . . . . . 19 LEU CD2 . 15013 1
223 . 1 1 19 19 LEU N N 15 126.111 0.069 . . . . . . 19 LEU N . 15013 1
224 . 1 1 20 20 ASN H H 1 7.526 0.003 . . . . . . 20 ASN H . 15013 1
225 . 1 1 20 20 ASN HA H 1 4.710 0.02 . . . . . . 20 ASN HA . 15013 1
226 . 1 1 20 20 ASN HB2 H 1 2.651 0.02 . . . . . . 20 ASN HB2 . 15013 1
227 . 1 1 20 20 ASN HB3 H 1 2.795 0.02 . . . . . . 20 ASN HB3 . 15013 1
228 . 1 1 20 20 ASN HD21 H 1 7.184 0.02 . . . . . . 20 ASN HD21 . 15013 1
229 . 1 1 20 20 ASN HD22 H 1 7.916 0.02 . . . . . . 20 ASN HD22 . 15013 1
230 . 1 1 20 20 ASN C C 13 174.573 0.05 . . . . . . 20 ASN C . 15013 1
231 . 1 1 20 20 ASN CA C 13 54.701 0.015 . . . . . . 20 ASN CA . 15013 1
232 . 1 1 20 20 ASN CB C 13 41.354 0.021 . . . . . . 20 ASN CB . 15013 1
233 . 1 1 20 20 ASN N N 15 114.046 0.012 . . . . . . 20 ASN N . 15013 1
234 . 1 1 20 20 ASN ND2 N 15 114.763 0.05 . . . . . . 20 ASN ND2 . 15013 1
235 . 1 1 21 21 SER H H 1 9.063 0.006 . . . . . . 21 SER H . 15013 1
236 . 1 1 21 21 SER HA H 1 3.950 0.001 . . . . . . 21 SER HA . 15013 1
237 . 1 1 21 21 SER HB2 H 1 2.032 0.02 . . . . . . 21 SER HB2 . 15013 1
238 . 1 1 21 21 SER HB3 H 1 2.878 0.02 . . . . . . 21 SER HB3 . 15013 1
239 . 1 1 21 21 SER C C 13 173.723 0.05 . . . . . . 21 SER C . 15013 1
240 . 1 1 21 21 SER CA C 13 57.066 0.005 . . . . . . 21 SER CA . 15013 1
241 . 1 1 21 21 SER CB C 13 62.415 0.053 . . . . . . 21 SER CB . 15013 1
242 . 1 1 21 21 SER N N 15 123.165 0.024 . . . . . . 21 SER N . 15013 1
243 . 1 1 22 22 THR H H 1 8.166 0.011 . . . . . . 22 THR H . 15013 1
244 . 1 1 22 22 THR HA H 1 3.973 0.001 . . . . . . 22 THR HA . 15013 1
245 . 1 1 22 22 THR HB H 1 4.273 0.02 . . . . . . 22 THR HB . 15013 1
246 . 1 1 22 22 THR HG21 H 1 1.307 0.02 . . . . . . 22 THR HG21 . 15013 1
247 . 1 1 22 22 THR HG22 H 1 1.307 0.02 . . . . . . 22 THR HG22 . 15013 1
248 . 1 1 22 22 THR HG23 H 1 1.307 0.02 . . . . . . 22 THR HG23 . 15013 1
249 . 1 1 22 22 THR C C 13 175.474 0.05 . . . . . . 22 THR C . 15013 1
250 . 1 1 22 22 THR CA C 13 65.615 0.008 . . . . . . 22 THR CA . 15013 1
251 . 1 1 22 22 THR CB C 13 69.709 0.026 . . . . . . 22 THR CB . 15013 1
252 . 1 1 22 22 THR N N 15 115.378 0.007 . . . . . . 22 THR N . 15013 1
253 . 1 1 23 23 ASN H H 1 8.622 0.009 . . . . . . 23 ASN H . 15013 1
254 . 1 1 23 23 ASN HA H 1 4.832 0.001 . . . . . . 23 ASN HA . 15013 1
255 . 1 1 23 23 ASN HB2 H 1 2.853 0.02 . . . . . . 23 ASN HB2 . 15013 1
256 . 1 1 23 23 ASN HB3 H 1 3.832 0.001 . . . . . . 23 ASN HB3 . 15013 1
257 . 1 1 23 23 ASN HD21 H 1 7.484 0.02 . . . . . . 23 ASN HD21 . 15013 1
258 . 1 1 23 23 ASN HD22 H 1 7.930 0.02 . . . . . . 23 ASN HD22 . 15013 1
259 . 1 1 23 23 ASN C C 13 174.922 0.05 . . . . . . 23 ASN C . 15013 1
260 . 1 1 23 23 ASN CA C 13 53.471 0.005 . . . . . . 23 ASN CA . 15013 1
261 . 1 1 23 23 ASN CB C 13 40.374 0.016 . . . . . . 23 ASN CB . 15013 1
262 . 1 1 23 23 ASN N N 15 122.914 0.019 . . . . . . 23 ASN N . 15013 1
263 . 1 1 23 23 ASN ND2 N 15 114.775 0.05 . . . . . . 23 ASN ND2 . 15013 1
264 . 1 1 24 24 LYS H H 1 8.485 0.006 . . . . . . 24 LYS H . 15013 1
265 . 1 1 24 24 LYS HA H 1 4.265 0.02 . . . . . . 24 LYS HA . 15013 1
266 . 1 1 24 24 LYS HB2 H 1 1.796 0.02 . . . . . . 24 LYS HB2 . 15013 1
267 . 1 1 24 24 LYS HB3 H 1 1.841 0.02 . . . . . . 24 LYS HB3 . 15013 1
268 . 1 1 24 24 LYS HG2 H 1 1.442 0.001 . . . . . . 24 LYS HG2 . 15013 1
269 . 1 1 24 24 LYS HG3 H 1 1.442 0.001 . . . . . . 24 LYS HG3 . 15013 1
270 . 1 1 24 24 LYS HD2 H 1 1.695 0.02 . . . . . . 24 LYS HD2 . 15013 1
271 . 1 1 24 24 LYS HD3 H 1 1.695 0.02 . . . . . . 24 LYS HD3 . 15013 1
272 . 1 1 24 24 LYS HE2 H 1 3.037 0.02 . . . . . . 24 LYS HE2 . 15013 1
273 . 1 1 24 24 LYS HE3 H 1 3.037 0.02 . . . . . . 24 LYS HE3 . 15013 1
274 . 1 1 24 24 LYS C C 13 176.547 0.05 . . . . . . 24 LYS C . 15013 1
275 . 1 1 24 24 LYS CA C 13 58.469 0.022 . . . . . . 24 LYS CA . 15013 1
276 . 1 1 24 24 LYS CB C 13 32.784 0.002 . . . . . . 24 LYS CB . 15013 1
277 . 1 1 24 24 LYS CG C 13 24.519 0.030 . . . . . . 24 LYS CG . 15013 1
278 . 1 1 24 24 LYS CD C 13 29.544 0.061 . . . . . . 24 LYS CD . 15013 1
279 . 1 1 24 24 LYS CE C 13 42.422 0.053 . . . . . . 24 LYS CE . 15013 1
280 . 1 1 24 24 LYS N N 15 121.275 0.020 . . . . . . 24 LYS N . 15013 1
281 . 1 1 25 25 ASP H H 1 8.326 0.017 . . . . . . 25 ASP H . 15013 1
282 . 1 1 25 25 ASP HA H 1 4.524 0.002 . . . . . . 25 ASP HA . 15013 1
283 . 1 1 25 25 ASP HB2 H 1 1.955 0.02 . . . . . . 25 ASP HB2 . 15013 1
284 . 1 1 25 25 ASP HB3 H 1 2.801 0.001 . . . . . . 25 ASP HB3 . 15013 1
285 . 1 1 25 25 ASP C C 13 176.916 0.05 . . . . . . 25 ASP C . 15013 1
286 . 1 1 25 25 ASP CA C 13 55.596 0.015 . . . . . . 25 ASP CA . 15013 1
287 . 1 1 25 25 ASP CB C 13 43.386 0.002 . . . . . . 25 ASP CB . 15013 1
288 . 1 1 25 25 ASP N N 15 115.342 0.011 . . . . . . 25 ASP N . 15013 1
289 . 1 1 26 26 TRP H H 1 8.104 0.005 . . . . . . 26 TRP H . 15013 1
290 . 1 1 26 26 TRP HA H 1 5.132 0.02 . . . . . . 26 TRP HA . 15013 1
291 . 1 1 26 26 TRP HB2 H 1 2.865 0.001 . . . . . . 26 TRP HB2 . 15013 1
292 . 1 1 26 26 TRP HB3 H 1 2.972 0.02 . . . . . . 26 TRP HB3 . 15013 1
293 . 1 1 26 26 TRP HD1 H 1 7.139 0.02 . . . . . . 26 TRP HD1 . 15013 1
294 . 1 1 26 26 TRP HE1 H 1 9.925 0.02 . . . . . . 26 TRP HE1 . 15013 1
295 . 1 1 26 26 TRP HE3 H 1 6.950 0.02 . . . . . . 26 TRP HE3 . 15013 1
296 . 1 1 26 26 TRP HZ2 H 1 7.057 0.02 . . . . . . 26 TRP HZ2 . 15013 1
297 . 1 1 26 26 TRP HZ3 H 1 6.756 0.02 . . . . . . 26 TRP HZ3 . 15013 1
298 . 1 1 26 26 TRP HH2 H 1 7.235 0.001 . . . . . . 26 TRP HH2 . 15013 1
299 . 1 1 26 26 TRP C C 13 174.490 0.05 . . . . . . 26 TRP C . 15013 1
300 . 1 1 26 26 TRP CA C 13 55.890 0.052 . . . . . . 26 TRP CA . 15013 1
301 . 1 1 26 26 TRP CB C 13 33.085 0.045 . . . . . . 26 TRP CB . 15013 1
302 . 1 1 26 26 TRP N N 15 121.794 0.025 . . . . . . 26 TRP N . 15013 1
303 . 1 1 26 26 TRP NE1 N 15 128.806 0.05 . . . . . . 26 TRP NE1 . 15013 1
304 . 1 1 27 27 TRP H H 1 9.530 0.004 . . . . . . 27 TRP H . 15013 1
305 . 1 1 27 27 TRP HA H 1 5.511 0.002 . . . . . . 27 TRP HA . 15013 1
306 . 1 1 27 27 TRP HB2 H 1 2.804 0.002 . . . . . . 27 TRP HB2 . 15013 1
307 . 1 1 27 27 TRP HB3 H 1 2.967 0.02 . . . . . . 27 TRP HB3 . 15013 1
308 . 1 1 27 27 TRP HD1 H 1 7.555 0.02 . . . . . . 27 TRP HD1 . 15013 1
309 . 1 1 27 27 TRP HE1 H 1 9.272 0.02 . . . . . . 27 TRP HE1 . 15013 1
310 . 1 1 27 27 TRP HE3 H 1 7.091 0.002 . . . . . . 27 TRP HE3 . 15013 1
311 . 1 1 27 27 TRP HZ2 H 1 7.547 0.02 . . . . . . 27 TRP HZ2 . 15013 1
312 . 1 1 27 27 TRP HZ3 H 1 6.715 0.02 . . . . . . 27 TRP HZ3 . 15013 1
313 . 1 1 27 27 TRP HH2 H 1 7.211 0.02 . . . . . . 27 TRP HH2 . 15013 1
314 . 1 1 27 27 TRP C C 13 174.485 0.05 . . . . . . 27 TRP C . 15013 1
315 . 1 1 27 27 TRP CA C 13 54.170 0.004 . . . . . . 27 TRP CA . 15013 1
316 . 1 1 27 27 TRP CB C 13 31.848 0.001 . . . . . . 27 TRP CB . 15013 1
317 . 1 1 27 27 TRP N N 15 124.771 0.023 . . . . . . 27 TRP N . 15013 1
318 . 1 1 27 27 TRP NE1 N 15 129.396 0.05 . . . . . . 27 TRP NE1 . 15013 1
319 . 1 1 28 28 LYS H H 1 8.723 0.002 . . . . . . 28 LYS H . 15013 1
320 . 1 1 28 28 LYS HA H 1 4.415 0.001 . . . . . . 28 LYS HA . 15013 1
321 . 1 1 28 28 LYS HB2 H 1 1.104 0.02 . . . . . . 28 LYS HB2 . 15013 1
322 . 1 1 28 28 LYS HB3 H 1 1.498 0.002 . . . . . . 28 LYS HB3 . 15013 1
323 . 1 1 28 28 LYS HG2 H 1 0.305 0.001 . . . . . . 28 LYS HG2 . 15013 1
324 . 1 1 28 28 LYS HG3 H 1 0.948 0.02 . . . . . . 28 LYS HG3 . 15013 1
325 . 1 1 28 28 LYS HD2 H 1 1.394 0.02 . . . . . . 28 LYS HD2 . 15013 1
326 . 1 1 28 28 LYS HD3 H 1 1.394 0.02 . . . . . . 28 LYS HD3 . 15013 1
327 . 1 1 28 28 LYS HE2 H 1 2.614 0.02 . . . . . . 28 LYS HE2 . 15013 1
328 . 1 1 28 28 LYS HE3 H 1 2.684 0.02 . . . . . . 28 LYS HE3 . 15013 1
329 . 1 1 28 28 LYS C C 13 175.913 0.05 . . . . . . 28 LYS C . 15013 1
330 . 1 1 28 28 LYS CA C 13 55.430 0.004 . . . . . . 28 LYS CA . 15013 1
331 . 1 1 28 28 LYS CB C 13 34.684 0.017 . . . . . . 28 LYS CB . 15013 1
332 . 1 1 28 28 LYS CG C 13 25.991 0.060 . . . . . . 28 LYS CG . 15013 1
333 . 1 1 28 28 LYS CD C 13 29.562 0.052 . . . . . . 28 LYS CD . 15013 1
334 . 1 1 28 28 LYS N N 15 124.270 0.061 . . . . . . 28 LYS N . 15013 1
335 . 1 1 29 29 VAL H H 1 9.176 0.004 . . . . . . 29 VAL H . 15013 1
336 . 1 1 29 29 VAL HA H 1 5.334 0.02 . . . . . . 29 VAL HA . 15013 1
337 . 1 1 29 29 VAL HB H 1 2.114 0.02 . . . . . . 29 VAL HB . 15013 1
338 . 1 1 29 29 VAL HG11 H 1 0.753 0.02 . . . . . . 29 VAL HG11 . 15013 1
339 . 1 1 29 29 VAL HG12 H 1 0.753 0.02 . . . . . . 29 VAL HG12 . 15013 1
340 . 1 1 29 29 VAL HG13 H 1 0.753 0.02 . . . . . . 29 VAL HG13 . 15013 1
341 . 1 1 29 29 VAL HG21 H 1 0.835 0.02 . . . . . . 29 VAL HG21 . 15013 1
342 . 1 1 29 29 VAL HG22 H 1 0.835 0.02 . . . . . . 29 VAL HG22 . 15013 1
343 . 1 1 29 29 VAL HG23 H 1 0.835 0.02 . . . . . . 29 VAL HG23 . 15013 1
344 . 1 1 29 29 VAL C C 13 173.995 0.05 . . . . . . 29 VAL C . 15013 1
345 . 1 1 29 29 VAL CA C 13 59.048 0.013 . . . . . . 29 VAL CA . 15013 1
346 . 1 1 29 29 VAL CB C 13 36.757 0.008 . . . . . . 29 VAL CB . 15013 1
347 . 1 1 29 29 VAL CG1 C 13 18.876 0.028 . . . . . . 29 VAL CG1 . 15013 1
348 . 1 1 29 29 VAL CG2 C 13 21.878 0.021 . . . . . . 29 VAL CG2 . 15013 1
349 . 1 1 29 29 VAL N N 15 121.453 0.035 . . . . . . 29 VAL N . 15013 1
350 . 1 1 30 30 GLU H H 1 8.666 0.003 . . . . . . 30 GLU H . 15013 1
351 . 1 1 30 30 GLU HA H 1 5.332 0.02 . . . . . . 30 GLU HA . 15013 1
352 . 1 1 30 30 GLU HB2 H 1 1.861 0.02 . . . . . . 30 GLU HB2 . 15013 1
353 . 1 1 30 30 GLU HB3 H 1 1.861 0.02 . . . . . . 30 GLU HB3 . 15013 1
354 . 1 1 30 30 GLU HG2 H 1 2.292 0.02 . . . . . . 30 GLU HG2 . 15013 1
355 . 1 1 30 30 GLU HG3 H 1 2.292 0.02 . . . . . . 30 GLU HG3 . 15013 1
356 . 1 1 30 30 GLU C C 13 174.821 0.05 . . . . . . 30 GLU C . 15013 1
357 . 1 1 30 30 GLU CA C 13 54.514 0.035 . . . . . . 30 GLU CA . 15013 1
358 . 1 1 30 30 GLU CB C 13 32.215 0.040 . . . . . . 30 GLU CB . 15013 1
359 . 1 1 30 30 GLU CG C 13 33.431 0.05 . . . . . . 30 GLU CG . 15013 1
360 . 1 1 30 30 GLU N N 15 118.996 0.047 . . . . . . 30 GLU N . 15013 1
361 . 1 1 31 31 VAL H H 1 8.657 0.008 . . . . . . 31 VAL H . 15013 1
362 . 1 1 31 31 VAL HA H 1 4.453 0.02 . . . . . . 31 VAL HA . 15013 1
363 . 1 1 31 31 VAL HB H 1 2.115 0.001 . . . . . . 31 VAL HB . 15013 1
364 . 1 1 31 31 VAL HG11 H 1 0.929 0.02 . . . . . . 31 VAL HG11 . 15013 1
365 . 1 1 31 31 VAL HG12 H 1 0.929 0.02 . . . . . . 31 VAL HG12 . 15013 1
366 . 1 1 31 31 VAL HG13 H 1 0.929 0.02 . . . . . . 31 VAL HG13 . 15013 1
367 . 1 1 31 31 VAL HG21 H 1 1.045 0.02 . . . . . . 31 VAL HG21 . 15013 1
368 . 1 1 31 31 VAL HG22 H 1 1.045 0.02 . . . . . . 31 VAL HG22 . 15013 1
369 . 1 1 31 31 VAL HG23 H 1 1.045 0.02 . . . . . . 31 VAL HG23 . 15013 1
370 . 1 1 31 31 VAL C C 13 174.801 0.05 . . . . . . 31 VAL C . 15013 1
371 . 1 1 31 31 VAL CA C 13 61.217 0.002 . . . . . . 31 VAL CA . 15013 1
372 . 1 1 31 31 VAL CB C 13 33.928 0.005 . . . . . . 31 VAL CB . 15013 1
373 . 1 1 31 31 VAL CG1 C 13 19.733 0.050 . . . . . . 31 VAL CG1 . 15013 1
374 . 1 1 31 31 VAL CG2 C 13 21.563 0.019 . . . . . . 31 VAL CG2 . 15013 1
375 . 1 1 31 31 VAL N N 15 124.548 0.045 . . . . . . 31 VAL N . 15013 1
376 . 1 1 32 32 ASN H H 1 9.425 0.011 . . . . . . 32 ASN H . 15013 1
377 . 1 1 32 32 ASN HA H 1 4.334 0.02 . . . . . . 32 ASN HA . 15013 1
378 . 1 1 32 32 ASN HB2 H 1 2.861 0.02 . . . . . . 32 ASN HB2 . 15013 1
379 . 1 1 32 32 ASN HB3 H 1 3.063 0.02 . . . . . . 32 ASN HB3 . 15013 1
380 . 1 1 32 32 ASN HD21 H 1 7.042 0.02 . . . . . . 32 ASN HD21 . 15013 1
381 . 1 1 32 32 ASN HD22 H 1 7.586 0.02 . . . . . . 32 ASN HD22 . 15013 1
382 . 1 1 32 32 ASN C C 13 174.402 0.05 . . . . . . 32 ASN C . 15013 1
383 . 1 1 32 32 ASN CA C 13 55.247 0.007 . . . . . . 32 ASN CA . 15013 1
384 . 1 1 32 32 ASN CB C 13 37.740 0.014 . . . . . . 32 ASN CB . 15013 1
385 . 1 1 32 32 ASN N N 15 126.251 0.038 . . . . . . 32 ASN N . 15013 1
386 . 1 1 32 32 ASN ND2 N 15 113.211 0.05 . . . . . . 32 ASN ND2 . 15013 1
387 . 1 1 33 33 ASP H H 1 8.748 0.008 . . . . . . 33 ASP H . 15013 1
388 . 1 1 33 33 ASP HA H 1 4.418 0.003 . . . . . . 33 ASP HA . 15013 1
389 . 1 1 33 33 ASP HB2 H 1 2.960 0.02 . . . . . . 33 ASP HB2 . 15013 1
390 . 1 1 33 33 ASP HB3 H 1 3.077 0.02 . . . . . . 33 ASP HB3 . 15013 1
391 . 1 1 33 33 ASP C C 13 174.748 0.05 . . . . . . 33 ASP C . 15013 1
392 . 1 1 33 33 ASP CA C 13 54.934 0.014 . . . . . . 33 ASP CA . 15013 1
393 . 1 1 33 33 ASP CB C 13 38.682 0.006 . . . . . . 33 ASP CB . 15013 1
394 . 1 1 33 33 ASP N N 15 112.100 0.032 . . . . . . 33 ASP N . 15013 1
395 . 1 1 34 34 ARG H H 1 8.106 0.004 . . . . . . 34 ARG H . 15013 1
396 . 1 1 34 34 ARG HA H 1 4.691 0.001 . . . . . . 34 ARG HA . 15013 1
397 . 1 1 34 34 ARG HB2 H 1 1.795 0.02 . . . . . . 34 ARG HB2 . 15013 1
398 . 1 1 34 34 ARG HB3 H 1 1.917 0.02 . . . . . . 34 ARG HB3 . 15013 1
399 . 1 1 34 34 ARG HG2 H 1 1.654 0.02 . . . . . . 34 ARG HG2 . 15013 1
400 . 1 1 34 34 ARG HG3 H 1 1.716 0.02 . . . . . . 34 ARG HG3 . 15013 1
401 . 1 1 34 34 ARG HD2 H 1 3.218 0.001 . . . . . . 34 ARG HD2 . 15013 1
402 . 1 1 34 34 ARG HD3 H 1 3.218 0.001 . . . . . . 34 ARG HD3 . 15013 1
403 . 1 1 34 34 ARG HE H 1 7.199 0.004 . . . . . . 34 ARG HE . 15013 1
404 . 1 1 34 34 ARG C C 13 175.030 0.05 . . . . . . 34 ARG C . 15013 1
405 . 1 1 34 34 ARG CA C 13 55.131 0.007 . . . . . . 34 ARG CA . 15013 1
406 . 1 1 34 34 ARG CB C 13 32.315 0.012 . . . . . . 34 ARG CB . 15013 1
407 . 1 1 34 34 ARG CG C 13 27.393 0.009 . . . . . . 34 ARG CG . 15013 1
408 . 1 1 34 34 ARG CD C 13 43.617 0.05 . . . . . . 34 ARG CD . 15013 1
409 . 1 1 34 34 ARG N N 15 119.743 0.047 . . . . . . 34 ARG N . 15013 1
410 . 1 1 34 34 ARG NE N 15 114.751 0.001 . . . . . . 34 ARG NE . 15013 1
411 . 1 1 35 35 GLN H H 1 8.465 0.010 . . . . . . 35 GLN H . 15013 1
412 . 1 1 35 35 GLN HA H 1 5.333 0.001 . . . . . . 35 GLN HA . 15013 1
413 . 1 1 35 35 GLN HB2 H 1 1.739 0.02 . . . . . . 35 GLN HB2 . 15013 1
414 . 1 1 35 35 GLN HB3 H 1 1.890 0.02 . . . . . . 35 GLN HB3 . 15013 1
415 . 1 1 35 35 GLN HG2 H 1 2.109 0.02 . . . . . . 35 GLN HG2 . 15013 1
416 . 1 1 35 35 GLN HG3 H 1 2.253 0.038 . . . . . . 35 GLN HG3 . 15013 1
417 . 1 1 35 35 GLN HE21 H 1 6.713 0.02 . . . . . . 35 GLN HE21 . 15013 1
418 . 1 1 35 35 GLN HE22 H 1 7.304 0.02 . . . . . . 35 GLN HE22 . 15013 1
419 . 1 1 35 35 GLN C C 13 175.915 0.05 . . . . . . 35 GLN C . 15013 1
420 . 1 1 35 35 GLN CA C 13 54.287 0.05 . . . . . . 35 GLN CA . 15013 1
421 . 1 1 35 35 GLN CB C 13 31.572 0.002 . . . . . . 35 GLN CB . 15013 1
422 . 1 1 35 35 GLN CG C 13 33.845 0.032 . . . . . . 35 GLN CG . 15013 1
423 . 1 1 35 35 GLN N N 15 119.853 0.022 . . . . . . 35 GLN N . 15013 1
424 . 1 1 35 35 GLN NE2 N 15 110.590 0.05 . . . . . . 35 GLN NE2 . 15013 1
425 . 1 1 36 36 GLY H H 1 8.434 0.004 . . . . . . 36 GLY H . 15013 1
426 . 1 1 36 36 GLY HA2 H 1 4.129 0.001 . . . . . . 36 GLY HA2 . 15013 1
427 . 1 1 36 36 GLY HA3 H 1 4.129 0.001 . . . . . . 36 GLY HA3 . 15013 1
428 . 1 1 36 36 GLY C C 13 170.828 0.05 . . . . . . 36 GLY C . 15013 1
429 . 1 1 36 36 GLY CA C 13 45.554 0.012 . . . . . . 36 GLY CA . 15013 1
430 . 1 1 36 36 GLY N N 15 107.483 0.049 . . . . . . 36 GLY N . 15013 1
431 . 1 1 37 37 PHE H H 1 8.492 0.014 . . . . . . 37 PHE H . 15013 1
432 . 1 1 37 37 PHE HA H 1 5.592 0.02 . . . . . . 37 PHE HA . 15013 1
433 . 1 1 37 37 PHE HB2 H 1 2.761 0.02 . . . . . . 37 PHE HB2 . 15013 1
434 . 1 1 37 37 PHE HB3 H 1 2.761 0.02 . . . . . . 37 PHE HB3 . 15013 1
435 . 1 1 37 37 PHE HD1 H 1 7.024 0.001 . . . . . . 37 PHE HD1 . 15013 1
436 . 1 1 37 37 PHE HD2 H 1 7.024 0.001 . . . . . . 37 PHE HD2 . 15013 1
437 . 1 1 37 37 PHE HE1 H 1 7.387 0.02 . . . . . . 37 PHE HE1 . 15013 1
438 . 1 1 37 37 PHE HE2 H 1 7.387 0.02 . . . . . . 37 PHE HE2 . 15013 1
439 . 1 1 37 37 PHE C C 13 175.924 0.05 . . . . . . 37 PHE C . 15013 1
440 . 1 1 37 37 PHE CA C 13 57.997 0.027 . . . . . . 37 PHE CA . 15013 1
441 . 1 1 37 37 PHE CB C 13 42.204 0.002 . . . . . . 37 PHE CB . 15013 1
442 . 1 1 37 37 PHE N N 15 117.750 0.011 . . . . . . 37 PHE N . 15013 1
443 . 1 1 38 38 VAL H H 1 9.262 0.001 . . . . . . 38 VAL H . 15013 1
444 . 1 1 38 38 VAL HA H 1 4.919 0.001 . . . . . . 38 VAL HA . 15013 1
445 . 1 1 38 38 VAL HB H 1 1.825 0.02 . . . . . . 38 VAL HB . 15013 1
446 . 1 1 38 38 VAL HG11 H 1 0.711 0.02 . . . . . . 38 VAL HG11 . 15013 1
447 . 1 1 38 38 VAL HG12 H 1 0.711 0.02 . . . . . . 38 VAL HG12 . 15013 1
448 . 1 1 38 38 VAL HG13 H 1 0.711 0.02 . . . . . . 38 VAL HG13 . 15013 1
449 . 1 1 38 38 VAL HG21 H 1 1.048 0.02 . . . . . . 38 VAL HG21 . 15013 1
450 . 1 1 38 38 VAL HG22 H 1 1.048 0.02 . . . . . . 38 VAL HG22 . 15013 1
451 . 1 1 38 38 VAL HG23 H 1 1.048 0.02 . . . . . . 38 VAL HG23 . 15013 1
452 . 1 1 38 38 VAL CA C 13 57.311 0.05 . . . . . . 38 VAL CA . 15013 1
453 . 1 1 38 38 VAL CB C 13 33.096 0.05 . . . . . . 38 VAL CB . 15013 1
454 . 1 1 38 38 VAL CG1 C 13 17.975 0.079 . . . . . . 38 VAL CG1 . 15013 1
455 . 1 1 38 38 VAL CG2 C 13 21.538 0.103 . . . . . . 38 VAL CG2 . 15013 1
456 . 1 1 38 38 VAL N N 15 113.319 0.043 . . . . . . 38 VAL N . 15013 1
457 . 1 1 39 39 PRO HA H 1 3.846 0.001 . . . . . . 39 PRO HA . 15013 1
458 . 1 1 39 39 PRO HB2 H 1 1.045 0.02 . . . . . . 39 PRO HB2 . 15013 1
459 . 1 1 39 39 PRO HB3 H 1 1.327 0.02 . . . . . . 39 PRO HB3 . 15013 1
460 . 1 1 39 39 PRO HG2 H 1 0.104 0.001 . . . . . . 39 PRO HG2 . 15013 1
461 . 1 1 39 39 PRO HG3 H 1 0.715 0.02 . . . . . . 39 PRO HG3 . 15013 1
462 . 1 1 39 39 PRO HD2 H 1 2.097 0.02 . . . . . . 39 PRO HD2 . 15013 1
463 . 1 1 39 39 PRO HD3 H 1 2.391 0.002 . . . . . . 39 PRO HD3 . 15013 1
464 . 1 1 39 39 PRO C C 13 177.902 0.05 . . . . . . 39 PRO C . 15013 1
465 . 1 1 39 39 PRO CA C 13 61.946 0.05 . . . . . . 39 PRO CA . 15013 1
466 . 1 1 39 39 PRO CB C 13 31.143 0.05 . . . . . . 39 PRO CB . 15013 1
467 . 1 1 39 39 PRO CG C 13 27.733 0.051 . . . . . . 39 PRO CG . 15013 1
468 . 1 1 39 39 PRO CD C 13 50.297 0.042 . . . . . . 39 PRO CD . 15013 1
469 . 1 1 40 40 ALA H H 1 7.651 0.002 . . . . . . 40 ALA H . 15013 1
470 . 1 1 40 40 ALA HA H 1 2.629 0.004 . . . . . . 40 ALA HA . 15013 1
471 . 1 1 40 40 ALA HB1 H 1 -0.068 0.02 . . . . . . 40 ALA HB1 . 15013 1
472 . 1 1 40 40 ALA HB2 H 1 -0.068 0.02 . . . . . . 40 ALA HB2 . 15013 1
473 . 1 1 40 40 ALA HB3 H 1 -0.068 0.02 . . . . . . 40 ALA HB3 . 15013 1
474 . 1 1 40 40 ALA C C 13 178.861 0.05 . . . . . . 40 ALA C . 15013 1
475 . 1 1 40 40 ALA CA C 13 55.137 0.034 . . . . . . 40 ALA CA . 15013 1
476 . 1 1 40 40 ALA CB C 13 16.049 0.007 . . . . . . 40 ALA CB . 15013 1
477 . 1 1 40 40 ALA N N 15 130.254 0.031 . . . . . . 40 ALA N . 15013 1
478 . 1 1 41 41 ALA H H 1 8.148 0.003 . . . . . . 41 ALA H . 15013 1
479 . 1 1 41 41 ALA HA H 1 4.113 0.002 . . . . . . 41 ALA HA . 15013 1
480 . 1 1 41 41 ALA HB1 H 1 1.323 0.02 . . . . . . 41 ALA HB1 . 15013 1
481 . 1 1 41 41 ALA HB2 H 1 1.323 0.02 . . . . . . 41 ALA HB2 . 15013 1
482 . 1 1 41 41 ALA HB3 H 1 1.323 0.02 . . . . . . 41 ALA HB3 . 15013 1
483 . 1 1 41 41 ALA C C 13 177.864 0.05 . . . . . . 41 ALA C . 15013 1
484 . 1 1 41 41 ALA CA C 13 52.897 0.003 . . . . . . 41 ALA CA . 15013 1
485 . 1 1 41 41 ALA CB C 13 18.002 0.003 . . . . . . 41 ALA CB . 15013 1
486 . 1 1 41 41 ALA N N 15 113.328 0.031 . . . . . . 41 ALA N . 15013 1
487 . 1 1 42 42 TYR H H 1 7.920 0.006 . . . . . . 42 TYR H . 15013 1
488 . 1 1 42 42 TYR HA H 1 4.793 0.003 . . . . . . 42 TYR HA . 15013 1
489 . 1 1 42 42 TYR HB2 H 1 3.163 0.003 . . . . . . 42 TYR HB2 . 15013 1
490 . 1 1 42 42 TYR HB3 H 1 3.336 0.02 . . . . . . 42 TYR HB3 . 15013 1
491 . 1 1 42 42 TYR HD1 H 1 6.830 0.02 . . . . . . 42 TYR HD1 . 15013 1
492 . 1 1 42 42 TYR HD2 H 1 6.830 0.02 . . . . . . 42 TYR HD2 . 15013 1
493 . 1 1 42 42 TYR HE1 H 1 6.754 0.02 . . . . . . 42 TYR HE1 . 15013 1
494 . 1 1 42 42 TYR HE2 H 1 6.754 0.02 . . . . . . 42 TYR HE2 . 15013 1
495 . 1 1 42 42 TYR C C 13 174.736 0.05 . . . . . . 42 TYR C . 15013 1
496 . 1 1 42 42 TYR CA C 13 57.157 0.027 . . . . . . 42 TYR CA . 15013 1
497 . 1 1 42 42 TYR CB C 13 37.725 0.002 . . . . . . 42 TYR CB . 15013 1
498 . 1 1 42 42 TYR N N 15 116.511 0.003 . . . . . . 42 TYR N . 15013 1
499 . 1 1 43 43 VAL H H 1 7.472 0.001 . . . . . . 43 VAL H . 15013 1
500 . 1 1 43 43 VAL HA H 1 5.483 0.001 . . . . . . 43 VAL HA . 15013 1
501 . 1 1 43 43 VAL HB H 1 1.937 0.02 . . . . . . 43 VAL HB . 15013 1
502 . 1 1 43 43 VAL HG11 H 1 0.775 0.02 . . . . . . 43 VAL HG11 . 15013 1
503 . 1 1 43 43 VAL HG12 H 1 0.775 0.02 . . . . . . 43 VAL HG12 . 15013 1
504 . 1 1 43 43 VAL HG13 H 1 0.775 0.02 . . . . . . 43 VAL HG13 . 15013 1
505 . 1 1 43 43 VAL HG21 H 1 0.794 0.02 . . . . . . 43 VAL HG21 . 15013 1
506 . 1 1 43 43 VAL HG22 H 1 0.794 0.02 . . . . . . 43 VAL HG22 . 15013 1
507 . 1 1 43 43 VAL HG23 H 1 0.794 0.02 . . . . . . 43 VAL HG23 . 15013 1
508 . 1 1 43 43 VAL C C 13 173.648 0.05 . . . . . . 43 VAL C . 15013 1
509 . 1 1 43 43 VAL CA C 13 58.391 0.016 . . . . . . 43 VAL CA . 15013 1
510 . 1 1 43 43 VAL CB C 13 36.427 0.019 . . . . . . 43 VAL CB . 15013 1
511 . 1 1 43 43 VAL CG2 C 13 22.828 0.019 . . . . . . 43 VAL CG2 . 15013 1
512 . 1 1 43 43 VAL N N 15 110.912 0.039 . . . . . . 43 VAL N . 15013 1
513 . 1 1 44 44 LYS H H 1 8.739 0.002 . . . . . . 44 LYS H . 15013 1
514 . 1 1 44 44 LYS HA H 1 4.835 0.002 . . . . . . 44 LYS HA . 15013 1
515 . 1 1 44 44 LYS HB2 H 1 1.720 0.02 . . . . . . 44 LYS HB2 . 15013 1
516 . 1 1 44 44 LYS HB3 H 1 1.720 0.02 . . . . . . 44 LYS HB3 . 15013 1
517 . 1 1 44 44 LYS HG2 H 1 1.373 0.004 . . . . . . 44 LYS HG2 . 15013 1
518 . 1 1 44 44 LYS HG3 H 1 1.459 0.02 . . . . . . 44 LYS HG3 . 15013 1
519 . 1 1 44 44 LYS HD2 H 1 1.642 0.02 . . . . . . 44 LYS HD2 . 15013 1
520 . 1 1 44 44 LYS HD3 H 1 1.642 0.02 . . . . . . 44 LYS HD3 . 15013 1
521 . 1 1 44 44 LYS HE2 H 1 2.958 0.02 . . . . . . 44 LYS HE2 . 15013 1
522 . 1 1 44 44 LYS HE3 H 1 2.958 0.02 . . . . . . 44 LYS HE3 . 15013 1
523 . 1 1 44 44 LYS C C 13 176.280 0.05 . . . . . . 44 LYS C . 15013 1
524 . 1 1 44 44 LYS CA C 13 54.240 0.005 . . . . . . 44 LYS CA . 15013 1
525 . 1 1 44 44 LYS CB C 13 37.042 0.020 . . . . . . 44 LYS CB . 15013 1
526 . 1 1 44 44 LYS CD C 13 30.018 0.058 . . . . . . 44 LYS CD . 15013 1
527 . 1 1 44 44 LYS N N 15 118.908 0.023 . . . . . . 44 LYS N . 15013 1
528 . 1 1 45 45 LYS H H 1 9.190 0.012 . . . . . . 45 LYS H . 15013 1
529 . 1 1 45 45 LYS HA H 1 4.500 0.001 . . . . . . 45 LYS HA . 15013 1
530 . 1 1 45 45 LYS HB2 H 1 1.838 0.02 . . . . . . 45 LYS HB2 . 15013 1
531 . 1 1 45 45 LYS HB3 H 1 1.997 0.02 . . . . . . 45 LYS HB3 . 15013 1
532 . 1 1 45 45 LYS HG2 H 1 1.433 0.001 . . . . . . 45 LYS HG2 . 15013 1
533 . 1 1 45 45 LYS HG3 H 1 1.712 0.006 . . . . . . 45 LYS HG3 . 15013 1
534 . 1 1 45 45 LYS HD2 H 1 1.642 0.001 . . . . . . 45 LYS HD2 . 15013 1
535 . 1 1 45 45 LYS HD3 H 1 1.719 0.02 . . . . . . 45 LYS HD3 . 15013 1
536 . 1 1 45 45 LYS HE2 H 1 2.758 0.001 . . . . . . 45 LYS HE2 . 15013 1
537 . 1 1 45 45 LYS HE3 H 1 2.846 0.003 . . . . . . 45 LYS HE3 . 15013 1
538 . 1 1 45 45 LYS CA C 13 58.683 0.017 . . . . . . 45 LYS CA . 15013 1
539 . 1 1 45 45 LYS CB C 13 33.291 0.007 . . . . . . 45 LYS CB . 15013 1
540 . 1 1 45 45 LYS CG C 13 26.100 0.048 . . . . . . 45 LYS CG . 15013 1
541 . 1 1 45 45 LYS CD C 13 29.649 0.05 . . . . . . 45 LYS CD . 15013 1
542 . 1 1 45 45 LYS N N 15 126.137 0.051 . . . . . . 45 LYS N . 15013 1
543 . 1 1 46 46 LEU H H 1 8.320 0.004 . . . . . . 46 LEU H . 15013 1
544 . 1 1 46 46 LEU HA H 1 4.573 0.002 . . . . . . 46 LEU HA . 15013 1
545 . 1 1 46 46 LEU HB2 H 1 1.498 0.02 . . . . . . 46 LEU HB2 . 15013 1
546 . 1 1 46 46 LEU HB3 H 1 1.565 0.02 . . . . . . 46 LEU HB3 . 15013 1
547 . 1 1 46 46 LEU HG H 1 1.643 0.02 . . . . . . 46 LEU HG . 15013 1
548 . 1 1 46 46 LEU HD11 H 1 0.867 0.02 . . . . . . 46 LEU HD11 . 15013 1
549 . 1 1 46 46 LEU HD12 H 1 0.867 0.02 . . . . . . 46 LEU HD12 . 15013 1
550 . 1 1 46 46 LEU HD13 H 1 0.867 0.02 . . . . . . 46 LEU HD13 . 15013 1
551 . 1 1 46 46 LEU HD21 H 1 0.867 0.02 . . . . . . 46 LEU HD21 . 15013 1
552 . 1 1 46 46 LEU HD22 H 1 0.867 0.02 . . . . . . 46 LEU HD22 . 15013 1
553 . 1 1 46 46 LEU HD23 H 1 0.867 0.02 . . . . . . 46 LEU HD23 . 15013 1
554 . 1 1 46 46 LEU C C 13 176.707 0.322 . . . . . . 46 LEU C . 15013 1
555 . 1 1 46 46 LEU CA C 13 54.088 0.019 . . . . . . 46 LEU CA . 15013 1
556 . 1 1 46 46 LEU CB C 13 43.729 0.027 . . . . . . 46 LEU CB . 15013 1
557 . 1 1 46 46 LEU CG C 13 27.201 0.066 . . . . . . 46 LEU CG . 15013 1
558 . 1 1 46 46 LEU CD1 C 13 25.963 0.061 . . . . . . 46 LEU CD1 . 15013 1
559 . 1 1 46 46 LEU CD2 C 13 25.963 0.061 . . . . . . 46 LEU CD2 . 15013 1
560 . 1 1 46 46 LEU N N 15 125.332 0.039 . . . . . . 46 LEU N . 15013 1
561 . 1 1 47 47 ASP H H 1 8.619 0.020 . . . . . . 47 ASP H . 15013 1
562 . 1 1 47 47 ASP HA H 1 4.832 0.02 . . . . . . 47 ASP HA . 15013 1
563 . 1 1 47 47 ASP HB2 H 1 2.747 0.02 . . . . . . 47 ASP HB2 . 15013 1
564 . 1 1 47 47 ASP HB3 H 1 2.881 0.02 . . . . . . 47 ASP HB3 . 15013 1
565 . 1 1 47 47 ASP C C 13 175.795 0.05 . . . . . . 47 ASP C . 15013 1
566 . 1 1 47 47 ASP CA C 13 53.777 0.009 . . . . . . 47 ASP CA . 15013 1
567 . 1 1 47 47 ASP CB C 13 39.717 0.001 . . . . . . 47 ASP CB . 15013 1
568 . 1 1 47 47 ASP N N 15 121.309 0.040 . . . . . . 47 ASP N . 15013 1
569 . 1 1 48 48 SER H H 1 8.312 0.007 . . . . . . 48 SER H . 15013 1
570 . 1 1 48 48 SER HA H 1 4.560 0.003 . . . . . . 48 SER HA . 15013 1
571 . 1 1 48 48 SER HB2 H 1 3.817 0.02 . . . . . . 48 SER HB2 . 15013 1
572 . 1 1 48 48 SER HB3 H 1 3.951 0.02 . . . . . . 48 SER HB3 . 15013 1
573 . 1 1 48 48 SER C C 13 175.436 0.05 . . . . . . 48 SER C . 15013 1
574 . 1 1 48 48 SER CA C 13 58.373 0.015 . . . . . . 48 SER CA . 15013 1
575 . 1 1 48 48 SER CB C 13 64.689 0.042 . . . . . . 48 SER CB . 15013 1
576 . 1 1 48 48 SER N N 15 116.622 0.006 . . . . . . 48 SER N . 15013 1
577 . 1 1 49 49 GLY H H 1 8.587 0.005 . . . . . . 49 GLY H . 15013 1
578 . 1 1 49 49 GLY HA2 H 1 4.071 0.002 . . . . . . 49 GLY HA2 . 15013 1
579 . 1 1 49 49 GLY HA3 H 1 4.071 0.002 . . . . . . 49 GLY HA3 . 15013 1
580 . 1 1 49 49 GLY C C 13 174.886 0.05 . . . . . . 49 GLY C . 15013 1
581 . 1 1 49 49 GLY CA C 13 45.844 0.012 . . . . . . 49 GLY CA . 15013 1
582 . 1 1 49 49 GLY N N 15 111.630 0.046 . . . . . . 49 GLY N . 15013 1
583 . 1 1 50 50 THR H H 1 8.145 0.004 . . . . . . 50 THR H . 15013 1
584 . 1 1 50 50 THR HA H 1 4.408 0.02 . . . . . . 50 THR HA . 15013 1
585 . 1 1 50 50 THR HB H 1 4.364 0.02 . . . . . . 50 THR HB . 15013 1
586 . 1 1 50 50 THR HG21 H 1 1.196 0.02 . . . . . . 50 THR HG21 . 15013 1
587 . 1 1 50 50 THR HG22 H 1 1.196 0.02 . . . . . . 50 THR HG22 . 15013 1
588 . 1 1 50 50 THR HG23 H 1 1.196 0.02 . . . . . . 50 THR HG23 . 15013 1
589 . 1 1 50 50 THR C C 13 175.580 0.05 . . . . . . 50 THR C . 15013 1
590 . 1 1 50 50 THR CA C 13 61.973 0.001 . . . . . . 50 THR CA . 15013 1
591 . 1 1 50 50 THR CB C 13 70.121 0.012 . . . . . . 50 THR CB . 15013 1
592 . 1 1 50 50 THR N N 15 112.104 0.012 . . . . . . 50 THR N . 15013 1
593 . 1 1 51 51 GLY H H 1 8.424 0.003 . . . . . . 51 GLY H . 15013 1
594 . 1 1 51 51 GLY HA2 H 1 3.853 0.003 . . . . . . 51 GLY HA2 . 15013 1
595 . 1 1 51 51 GLY HA3 H 1 4.085 0.001 . . . . . . 51 GLY HA3 . 15013 1
596 . 1 1 51 51 GLY C C 13 174.068 0.05 . . . . . . 51 GLY C . 15013 1
597 . 1 1 51 51 GLY CA C 13 45.602 0.002 . . . . . . 51 GLY CA . 15013 1
598 . 1 1 51 51 GLY N N 15 110.990 0.027 . . . . . . 51 GLY N . 15013 1
599 . 1 1 52 52 LYS H H 1 7.724 0.011 . . . . . . 52 LYS H . 15013 1
600 . 1 1 52 52 LYS HA H 1 4.343 0.002 . . . . . . 52 LYS HA . 15013 1
601 . 1 1 52 52 LYS HB2 H 1 1.649 0.02 . . . . . . 52 LYS HB2 . 15013 1
602 . 1 1 52 52 LYS HB3 H 1 1.722 0.02 . . . . . . 52 LYS HB3 . 15013 1
603 . 1 1 52 52 LYS HG2 H 1 1.344 0.02 . . . . . . 52 LYS HG2 . 15013 1
604 . 1 1 52 52 LYS HG3 H 1 1.381 0.02 . . . . . . 52 LYS HG3 . 15013 1
605 . 1 1 52 52 LYS HD2 H 1 1.628 0.02 . . . . . . 52 LYS HD2 . 15013 1
606 . 1 1 52 52 LYS HD3 H 1 1.628 0.02 . . . . . . 52 LYS HD3 . 15013 1
607 . 1 1 52 52 LYS HE2 H 1 2.965 0.02 . . . . . . 52 LYS HE2 . 15013 1
608 . 1 1 52 52 LYS HE3 H 1 2.965 0.02 . . . . . . 52 LYS HE3 . 15013 1
609 . 1 1 52 52 LYS C C 13 175.851 0.05 . . . . . . 52 LYS C . 15013 1
610 . 1 1 52 52 LYS CA C 13 55.855 0.038 . . . . . . 52 LYS CA . 15013 1
611 . 1 1 52 52 LYS CB C 13 33.698 0.006 . . . . . . 52 LYS CB . 15013 1
612 . 1 1 52 52 LYS CD C 13 29.452 0.062 . . . . . . 52 LYS CD . 15013 1
613 . 1 1 52 52 LYS CE C 13 42.530 0.05 . . . . . . 52 LYS CE . 15013 1
614 . 1 1 52 52 LYS N N 15 120.068 0.009 . . . . . . 52 LYS N . 15013 1
615 . 1 1 53 53 GLU H H 1 8.649 0.010 . . . . . . 53 GLU H . 15013 1
616 . 1 1 53 53 GLU HA H 1 4.534 0.001 . . . . . . 53 GLU HA . 15013 1
617 . 1 1 53 53 GLU HB2 H 1 2.010 0.010 . . . . . . 53 GLU HB2 . 15013 1
618 . 1 1 53 53 GLU HB3 H 1 2.122 0.02 . . . . . . 53 GLU HB3 . 15013 1
619 . 1 1 53 53 GLU HG2 H 1 2.350 0.02 . . . . . . 53 GLU HG2 . 15013 1
620 . 1 1 53 53 GLU HG3 H 1 2.461 0.02 . . . . . . 53 GLU HG3 . 15013 1
621 . 1 1 53 53 GLU C C 13 174.641 0.05 . . . . . . 53 GLU C . 15013 1
622 . 1 1 53 53 GLU CA C 13 55.780 0.05 . . . . . . 53 GLU CA . 15013 1
623 . 1 1 53 53 GLU CB C 13 29.538 0.011 . . . . . . 53 GLU CB . 15013 1
624 . 1 1 53 53 GLU CG C 13 33.837 0.012 . . . . . . 53 GLU CG . 15013 1
625 . 1 1 53 53 GLU N N 15 122.758 0.025 . . . . . . 53 GLU N . 15013 1
626 . 1 1 54 54 LEU H H 1 8.438 0.008 . . . . . . 54 LEU H . 15013 1
627 . 1 1 54 54 LEU HA H 1 5.412 0.001 . . . . . . 54 LEU HA . 15013 1
628 . 1 1 54 54 LEU HB2 H 1 1.375 0.02 . . . . . . 54 LEU HB2 . 15013 1
629 . 1 1 54 54 LEU HB3 H 1 1.671 0.02 . . . . . . 54 LEU HB3 . 15013 1
630 . 1 1 54 54 LEU HG H 1 1.566 0.02 . . . . . . 54 LEU HG . 15013 1
631 . 1 1 54 54 LEU HD11 H 1 0.795 0.02 . . . . . . 54 LEU HD11 . 15013 1
632 . 1 1 54 54 LEU HD12 H 1 0.795 0.02 . . . . . . 54 LEU HD12 . 15013 1
633 . 1 1 54 54 LEU HD13 H 1 0.795 0.02 . . . . . . 54 LEU HD13 . 15013 1
634 . 1 1 54 54 LEU HD21 H 1 0.837 0.02 . . . . . . 54 LEU HD21 . 15013 1
635 . 1 1 54 54 LEU HD22 H 1 0.837 0.02 . . . . . . 54 LEU HD22 . 15013 1
636 . 1 1 54 54 LEU HD23 H 1 0.837 0.02 . . . . . . 54 LEU HD23 . 15013 1
637 . 1 1 54 54 LEU C C 13 177.384 0.05 . . . . . . 54 LEU C . 15013 1
638 . 1 1 54 54 LEU CA C 13 53.436 0.017 . . . . . . 54 LEU CA . 15013 1
639 . 1 1 54 54 LEU CB C 13 46.225 0.025 . . . . . . 54 LEU CB . 15013 1
640 . 1 1 54 54 LEU CD1 C 13 23.625 0.048 . . . . . . 54 LEU CD1 . 15013 1
641 . 1 1 54 54 LEU CD2 C 13 25.645 0.035 . . . . . . 54 LEU CD2 . 15013 1
642 . 1 1 54 54 LEU N N 15 124.029 0.037 . . . . . . 54 LEU N . 15013 1
643 . 1 1 55 55 VAL H H 1 9.106 0.002 . . . . . . 55 VAL H . 15013 1
644 . 1 1 55 55 VAL HA H 1 5.239 0.001 . . . . . . 55 VAL HA . 15013 1
645 . 1 1 55 55 VAL HB H 1 2.008 0.02 . . . . . . 55 VAL HB . 15013 1
646 . 1 1 55 55 VAL HG11 H 1 0.804 0.02 . . . . . . 55 VAL HG11 . 15013 1
647 . 1 1 55 55 VAL HG12 H 1 0.804 0.02 . . . . . . 55 VAL HG12 . 15013 1
648 . 1 1 55 55 VAL HG13 H 1 0.804 0.02 . . . . . . 55 VAL HG13 . 15013 1
649 . 1 1 55 55 VAL HG21 H 1 1.057 0.02 . . . . . . 55 VAL HG21 . 15013 1
650 . 1 1 55 55 VAL HG22 H 1 1.057 0.02 . . . . . . 55 VAL HG22 . 15013 1
651 . 1 1 55 55 VAL HG23 H 1 1.057 0.02 . . . . . . 55 VAL HG23 . 15013 1
652 . 1 1 55 55 VAL C C 13 172.848 0.05 . . . . . . 55 VAL C . 15013 1
653 . 1 1 55 55 VAL CA C 13 58.106 0.002 . . . . . . 55 VAL CA . 15013 1
654 . 1 1 55 55 VAL CB C 13 36.203 0.006 . . . . . . 55 VAL CB . 15013 1
655 . 1 1 55 55 VAL CG1 C 13 20.140 0.023 . . . . . . 55 VAL CG1 . 15013 1
656 . 1 1 55 55 VAL CG2 C 13 24.276 0.011 . . . . . . 55 VAL CG2 . 15013 1
657 . 1 1 55 55 VAL N N 15 111.440 0.013 . . . . . . 55 VAL N . 15013 1
658 . 1 1 56 56 LEU H H 1 9.015 0.002 . . . . . . 56 LEU H . 15013 1
659 . 1 1 56 56 LEU HA H 1 5.106 0.001 . . . . . . 56 LEU HA . 15013 1
660 . 1 1 56 56 LEU HB2 H 1 1.388 0.02 . . . . . . 56 LEU HB2 . 15013 1
661 . 1 1 56 56 LEU HB3 H 1 1.726 0.02 . . . . . . 56 LEU HB3 . 15013 1
662 . 1 1 56 56 LEU HG H 1 1.264 0.02 . . . . . . 56 LEU HG . 15013 1
663 . 1 1 56 56 LEU HD11 H 1 0.803 0.02 . . . . . . 56 LEU HD11 . 15013 1
664 . 1 1 56 56 LEU HD12 H 1 0.803 0.02 . . . . . . 56 LEU HD12 . 15013 1
665 . 1 1 56 56 LEU HD13 H 1 0.803 0.02 . . . . . . 56 LEU HD13 . 15013 1
666 . 1 1 56 56 LEU HD21 H 1 0.846 0.02 . . . . . . 56 LEU HD21 . 15013 1
667 . 1 1 56 56 LEU HD22 H 1 0.846 0.02 . . . . . . 56 LEU HD22 . 15013 1
668 . 1 1 56 56 LEU HD23 H 1 0.846 0.02 . . . . . . 56 LEU HD23 . 15013 1
669 . 1 1 56 56 LEU C C 13 176.869 0.05 . . . . . . 56 LEU C . 15013 1
670 . 1 1 56 56 LEU CA C 13 52.793 0.097 . . . . . . 56 LEU CA . 15013 1
671 . 1 1 56 56 LEU CB C 13 46.801 0.001 . . . . . . 56 LEU CB . 15013 1
672 . 1 1 56 56 LEU CD1 C 13 26.541 0.097 . . . . . . 56 LEU CD1 . 15013 1
673 . 1 1 56 56 LEU CD2 C 13 24.357 0.057 . . . . . . 56 LEU CD2 . 15013 1
674 . 1 1 56 56 LEU N N 15 123.355 0.036 . . . . . . 56 LEU N . 15013 1
675 . 1 1 57 57 ALA H H 1 9.214 0.003 . . . . . . 57 ALA H . 15013 1
676 . 1 1 57 57 ALA HA H 1 4.549 0.001 . . . . . . 57 ALA HA . 15013 1
677 . 1 1 57 57 ALA HB1 H 1 1.611 0.02 . . . . . . 57 ALA HB1 . 15013 1
678 . 1 1 57 57 ALA HB2 H 1 1.611 0.02 . . . . . . 57 ALA HB2 . 15013 1
679 . 1 1 57 57 ALA HB3 H 1 1.611 0.02 . . . . . . 57 ALA HB3 . 15013 1
680 . 1 1 57 57 ALA C C 13 178.476 0.05 . . . . . . 57 ALA C . 15013 1
681 . 1 1 57 57 ALA CA C 13 52.957 0.05 . . . . . . 57 ALA CA . 15013 1
682 . 1 1 57 57 ALA CB C 13 19.754 0.046 . . . . . . 57 ALA CB . 15013 1
683 . 1 1 57 57 ALA N N 15 127.357 0.016 . . . . . . 57 ALA N . 15013 1
684 . 1 1 58 58 LEU H H 1 9.238 0.006 . . . . . . 58 LEU H . 15013 1
685 . 1 1 58 58 LEU HA H 1 3.912 0.001 . . . . . . 58 LEU HA . 15013 1
686 . 1 1 58 58 LEU HB2 H 1 0.526 0.02 . . . . . . 58 LEU HB2 . 15013 1
687 . 1 1 58 58 LEU HB3 H 1 1.076 0.02 . . . . . . 58 LEU HB3 . 15013 1
688 . 1 1 58 58 LEU HG H 1 1.324 0.02 . . . . . . 58 LEU HG . 15013 1
689 . 1 1 58 58 LEU HD11 H 1 0.593 0.02 . . . . . . 58 LEU HD11 . 15013 1
690 . 1 1 58 58 LEU HD12 H 1 0.593 0.02 . . . . . . 58 LEU HD12 . 15013 1
691 . 1 1 58 58 LEU HD13 H 1 0.593 0.02 . . . . . . 58 LEU HD13 . 15013 1
692 . 1 1 58 58 LEU HD21 H 1 0.648 0.02 . . . . . . 58 LEU HD21 . 15013 1
693 . 1 1 58 58 LEU HD22 H 1 0.648 0.02 . . . . . . 58 LEU HD22 . 15013 1
694 . 1 1 58 58 LEU HD23 H 1 0.648 0.02 . . . . . . 58 LEU HD23 . 15013 1
695 . 1 1 58 58 LEU C C 13 175.258 0.05 . . . . . . 58 LEU C . 15013 1
696 . 1 1 58 58 LEU CA C 13 55.756 0.028 . . . . . . 58 LEU CA . 15013 1
697 . 1 1 58 58 LEU CB C 13 43.079 0.003 . . . . . . 58 LEU CB . 15013 1
698 . 1 1 58 58 LEU CD1 C 13 21.950 0.065 . . . . . . 58 LEU CD1 . 15013 1
699 . 1 1 58 58 LEU CD2 C 13 25.551 0.045 . . . . . . 58 LEU CD2 . 15013 1
700 . 1 1 58 58 LEU N N 15 126.607 0.014 . . . . . . 58 LEU N . 15013 1
701 . 1 1 59 59 TYR H H 1 7.033 0.001 . . . . . . 59 TYR H . 15013 1
702 . 1 1 59 59 TYR HA H 1 4.691 0.001 . . . . . . 59 TYR HA . 15013 1
703 . 1 1 59 59 TYR HB2 H 1 2.082 0.02 . . . . . . 59 TYR HB2 . 15013 1
704 . 1 1 59 59 TYR HB3 H 1 3.075 0.002 . . . . . . 59 TYR HB3 . 15013 1
705 . 1 1 59 59 TYR HD1 H 1 6.640 0.02 . . . . . . 59 TYR HD1 . 15013 1
706 . 1 1 59 59 TYR HD2 H 1 6.640 0.02 . . . . . . 59 TYR HD2 . 15013 1
707 . 1 1 59 59 TYR HE1 H 1 6.586 0.02 . . . . . . 59 TYR HE1 . 15013 1
708 . 1 1 59 59 TYR HE2 H 1 6.586 0.02 . . . . . . 59 TYR HE2 . 15013 1
709 . 1 1 59 59 TYR C C 13 173.398 0.05 . . . . . . 59 TYR C . 15013 1
710 . 1 1 59 59 TYR CA C 13 54.556 0.015 . . . . . . 59 TYR CA . 15013 1
711 . 1 1 59 59 TYR CB C 13 43.302 0.047 . . . . . . 59 TYR CB . 15013 1
712 . 1 1 59 59 TYR N N 15 111.462 0.023 . . . . . . 59 TYR N . 15013 1
713 . 1 1 60 60 ASP H H 1 8.281 0.026 . . . . . . 60 ASP H . 15013 1
714 . 1 1 60 60 ASP HA H 1 4.920 0.02 . . . . . . 60 ASP HA . 15013 1
715 . 1 1 60 60 ASP HB2 H 1 2.742 0.02 . . . . . . 60 ASP HB2 . 15013 1
716 . 1 1 60 60 ASP HB3 H 1 2.888 0.02 . . . . . . 60 ASP HB3 . 15013 1
717 . 1 1 60 60 ASP C C 13 176.991 0.05 . . . . . . 60 ASP C . 15013 1
718 . 1 1 60 60 ASP CA C 13 54.128 0.026 . . . . . . 60 ASP CA . 15013 1
719 . 1 1 60 60 ASP CB C 13 41.044 0.008 . . . . . . 60 ASP CB . 15013 1
720 . 1 1 60 60 ASP N N 15 117.786 0.015 . . . . . . 60 ASP N . 15013 1
721 . 1 1 61 61 TYR H H 1 8.877 0.002 . . . . . . 61 TYR H . 15013 1
722 . 1 1 61 61 TYR HA H 1 4.732 0.02 . . . . . . 61 TYR HA . 15013 1
723 . 1 1 61 61 TYR HB2 H 1 2.751 0.001 . . . . . . 61 TYR HB2 . 15013 1
724 . 1 1 61 61 TYR HB3 H 1 3.354 0.001 . . . . . . 61 TYR HB3 . 15013 1
725 . 1 1 61 61 TYR HD1 H 1 7.125 0.02 . . . . . . 61 TYR HD1 . 15013 1
726 . 1 1 61 61 TYR HD2 H 1 7.125 0.02 . . . . . . 61 TYR HD2 . 15013 1
727 . 1 1 61 61 TYR HE1 H 1 6.987 0.02 . . . . . . 61 TYR HE1 . 15013 1
728 . 1 1 61 61 TYR HE2 H 1 6.987 0.02 . . . . . . 61 TYR HE2 . 15013 1
729 . 1 1 61 61 TYR C C 13 173.155 0.05 . . . . . . 61 TYR C . 15013 1
730 . 1 1 61 61 TYR CA C 13 60.027 0.023 . . . . . . 61 TYR CA . 15013 1
731 . 1 1 61 61 TYR CB C 13 43.365 0.006 . . . . . . 61 TYR CB . 15013 1
732 . 1 1 61 61 TYR N N 15 119.377 0.011 . . . . . . 61 TYR N . 15013 1
733 . 1 1 62 62 GLN H H 1 7.660 0.003 . . . . . . 62 GLN H . 15013 1
734 . 1 1 62 62 GLN HA H 1 4.673 0.003 . . . . . . 62 GLN HA . 15013 1
735 . 1 1 62 62 GLN HB2 H 1 1.916 0.02 . . . . . . 62 GLN HB2 . 15013 1
736 . 1 1 62 62 GLN HB3 H 1 1.916 0.02 . . . . . . 62 GLN HB3 . 15013 1
737 . 1 1 62 62 GLN HG2 H 1 1.994 0.02 . . . . . . 62 GLN HG2 . 15013 1
738 . 1 1 62 62 GLN HG3 H 1 1.994 0.02 . . . . . . 62 GLN HG3 . 15013 1
739 . 1 1 62 62 GLN HE21 H 1 6.759 0.02 . . . . . . 62 GLN HE21 . 15013 1
740 . 1 1 62 62 GLN HE22 H 1 7.432 0.02 . . . . . . 62 GLN HE22 . 15013 1
741 . 1 1 62 62 GLN C C 13 173.764 0.05 . . . . . . 62 GLN C . 15013 1
742 . 1 1 62 62 GLN CA C 13 54.838 0.001 . . . . . . 62 GLN CA . 15013 1
743 . 1 1 62 62 GLN CB C 13 30.599 0.001 . . . . . . 62 GLN CB . 15013 1
744 . 1 1 62 62 GLN N N 15 126.124 0.054 . . . . . . 62 GLN N . 15013 1
745 . 1 1 62 62 GLN NE2 N 15 112.103 0.05 . . . . . . 62 GLN NE2 . 15013 1
746 . 1 1 63 63 GLU H H 1 8.180 0.033 . . . . . . 63 GLU H . 15013 1
747 . 1 1 63 63 GLU HA H 1 4.380 0.001 . . . . . . 63 GLU HA . 15013 1
748 . 1 1 63 63 GLU HB2 H 1 2.145 0.02 . . . . . . 63 GLU HB2 . 15013 1
749 . 1 1 63 63 GLU HB3 H 1 2.236 0.02 . . . . . . 63 GLU HB3 . 15013 1
750 . 1 1 63 63 GLU HG2 H 1 2.575 0.02 . . . . . . 63 GLU HG2 . 15013 1
751 . 1 1 63 63 GLU HG3 H 1 2.652 0.02 . . . . . . 63 GLU HG3 . 15013 1
752 . 1 1 63 63 GLU C C 13 175.621 0.05 . . . . . . 63 GLU C . 15013 1
753 . 1 1 63 63 GLU CA C 13 56.131 0.007 . . . . . . 63 GLU CA . 15013 1
754 . 1 1 63 63 GLU CB C 13 30.130 0.035 . . . . . . 63 GLU CB . 15013 1
755 . 1 1 63 63 GLU CG C 13 33.383 0.047 . . . . . . 63 GLU CG . 15013 1
756 . 1 1 63 63 GLU N N 15 122.776 0.036 . . . . . . 63 GLU N . 15013 1
757 . 1 1 64 64 SER H H 1 8.453 0.008 . . . . . . 64 SER H . 15013 1
758 . 1 1 64 64 SER HA H 1 4.668 0.002 . . . . . . 64 SER HA . 15013 1
759 . 1 1 64 64 SER HB2 H 1 3.869 0.02 . . . . . . 64 SER HB2 . 15013 1
760 . 1 1 64 64 SER HB3 H 1 3.869 0.02 . . . . . . 64 SER HB3 . 15013 1
761 . 1 1 64 64 SER C C 13 174.943 0.05 . . . . . . 64 SER C . 15013 1
762 . 1 1 64 64 SER CA C 13 58.191 0.009 . . . . . . 64 SER CA . 15013 1
763 . 1 1 64 64 SER CB C 13 64.582 0.025 . . . . . . 64 SER CB . 15013 1
764 . 1 1 64 64 SER N N 15 117.598 0.011 . . . . . . 64 SER N . 15013 1
765 . 1 1 65 65 GLY H H 1 8.360 0.002 . . . . . . 65 GLY H . 15013 1
766 . 1 1 65 65 GLY HA2 H 1 4.063 0.001 . . . . . . 65 GLY HA2 . 15013 1
767 . 1 1 65 65 GLY HA3 H 1 4.220 0.001 . . . . . . 65 GLY HA3 . 15013 1
768 . 1 1 65 65 GLY C C 13 173.929 0.05 . . . . . . 65 GLY C . 15013 1
769 . 1 1 65 65 GLY CA C 13 45.286 0.05 . . . . . . 65 GLY CA . 15013 1
770 . 1 1 65 65 GLY N N 15 111.496 0.031 . . . . . . 65 GLY N . 15013 1
771 . 1 1 66 66 ASP H H 1 8.435 0.016 . . . . . . 66 ASP H . 15013 1
772 . 1 1 66 66 ASP HA H 1 4.890 0.02 . . . . . . 66 ASP HA . 15013 1
773 . 1 1 66 66 ASP HB2 H 1 2.812 0.001 . . . . . . 66 ASP HB2 . 15013 1
774 . 1 1 66 66 ASP HB3 H 1 2.812 0.001 . . . . . . 66 ASP HB3 . 15013 1
775 . 1 1 66 66 ASP C C 13 175.372 0.05 . . . . . . 66 ASP C . 15013 1
776 . 1 1 66 66 ASP CA C 13 53.966 0.019 . . . . . . 66 ASP CA . 15013 1
777 . 1 1 66 66 ASP CB C 13 40.248 0.004 . . . . . . 66 ASP CB . 15013 1
778 . 1 1 66 66 ASP N N 15 117.852 0.013 . . . . . . 66 ASP N . 15013 1
779 . 1 1 67 67 ASN H H 1 8.053 0.006 . . . . . . 67 ASN H . 15013 1
780 . 1 1 67 67 ASN HA H 1 4.723 0.02 . . . . . . 67 ASN HA . 15013 1
781 . 1 1 67 67 ASN HB2 H 1 2.566 0.02 . . . . . . 67 ASN HB2 . 15013 1
782 . 1 1 67 67 ASN HB3 H 1 2.620 0.02 . . . . . . 67 ASN HB3 . 15013 1
783 . 1 1 67 67 ASN HD21 H 1 6.856 0.02 . . . . . . 67 ASN HD21 . 15013 1
784 . 1 1 67 67 ASN HD22 H 1 7.432 0.02 . . . . . . 67 ASN HD22 . 15013 1
785 . 1 1 67 67 ASN C C 13 174.159 0.05 . . . . . . 67 ASN C . 15013 1
786 . 1 1 67 67 ASN CA C 13 52.331 0.004 . . . . . . 67 ASN CA . 15013 1
787 . 1 1 67 67 ASN CB C 13 40.204 0.060 . . . . . . 67 ASN CB . 15013 1
788 . 1 1 67 67 ASN N N 15 117.060 0.006 . . . . . . 67 ASN N . 15013 1
789 . 1 1 67 67 ASN ND2 N 15 113.444 0.05 . . . . . . 67 ASN ND2 . 15013 1
790 . 1 1 68 68 ALA H H 1 7.960 0.013 . . . . . . 68 ALA H . 15013 1
791 . 1 1 68 68 ALA HA H 1 3.151 0.02 . . . . . . 68 ALA HA . 15013 1
792 . 1 1 68 68 ALA HB1 H 1 0.708 0.02 . . . . . . 68 ALA HB1 . 15013 1
793 . 1 1 68 68 ALA HB2 H 1 0.708 0.02 . . . . . . 68 ALA HB2 . 15013 1
794 . 1 1 68 68 ALA HB3 H 1 0.708 0.02 . . . . . . 68 ALA HB3 . 15013 1
795 . 1 1 68 68 ALA CA C 13 50.551 0.05 . . . . . . 68 ALA CA . 15013 1
796 . 1 1 68 68 ALA CB C 13 17.177 0.05 . . . . . . 68 ALA CB . 15013 1
797 . 1 1 68 68 ALA N N 15 125.697 0.025 . . . . . . 68 ALA N . 15013 1
798 . 1 1 69 69 PRO HA H 1 3.716 0.001 . . . . . . 69 PRO HA . 15013 1
799 . 1 1 69 69 PRO HB2 H 1 0.415 0.02 . . . . . . 69 PRO HB2 . 15013 1
800 . 1 1 69 69 PRO HB3 H 1 1.027 0.02 . . . . . . 69 PRO HB3 . 15013 1
801 . 1 1 69 69 PRO HG2 H 1 0.901 0.02 . . . . . . 69 PRO HG2 . 15013 1
802 . 1 1 69 69 PRO HG3 H 1 0.901 0.02 . . . . . . 69 PRO HG3 . 15013 1
803 . 1 1 69 69 PRO C C 13 176.218 0.05 . . . . . . 69 PRO C . 15013 1
804 . 1 1 69 69 PRO CA C 13 62.623 0.05 . . . . . . 69 PRO CA . 15013 1
805 . 1 1 69 69 PRO CB C 13 31.648 0.05 . . . . . . 69 PRO CB . 15013 1
806 . 1 1 69 69 PRO CG C 13 27.569 0.075 . . . . . . 69 PRO CG . 15013 1
807 . 1 1 69 69 PRO CD C 13 49.121 0.040 . . . . . . 69 PRO CD . 15013 1
808 . 1 1 70 70 SER H H 1 8.067 0.016 . . . . . . 70 SER H . 15013 1
809 . 1 1 70 70 SER HA H 1 4.316 0.02 . . . . . . 70 SER HA . 15013 1
810 . 1 1 70 70 SER HB2 H 1 3.745 0.002 . . . . . . 70 SER HB2 . 15013 1
811 . 1 1 70 70 SER HB3 H 1 3.888 0.001 . . . . . . 70 SER HB3 . 15013 1
812 . 1 1 70 70 SER C C 13 173.872 0.05 . . . . . . 70 SER C . 15013 1
813 . 1 1 70 70 SER CA C 13 58.165 0.012 . . . . . . 70 SER CA . 15013 1
814 . 1 1 70 70 SER CB C 13 63.753 0.005 . . . . . . 70 SER CB . 15013 1
815 . 1 1 70 70 SER N N 15 114.298 0.017 . . . . . . 70 SER N . 15013 1
816 . 1 1 71 71 TYR H H 1 6.883 0.007 . . . . . . 71 TYR H . 15013 1
817 . 1 1 71 71 TYR HA H 1 4.866 0.001 . . . . . . 71 TYR HA . 15013 1
818 . 1 1 71 71 TYR HB2 H 1 3.043 0.001 . . . . . . 71 TYR HB2 . 15013 1
819 . 1 1 71 71 TYR HB3 H 1 3.253 0.003 . . . . . . 71 TYR HB3 . 15013 1
820 . 1 1 71 71 TYR HD1 H 1 7.196 0.02 . . . . . . 71 TYR HD1 . 15013 1
821 . 1 1 71 71 TYR HD2 H 1 7.196 0.02 . . . . . . 71 TYR HD2 . 15013 1
822 . 1 1 71 71 TYR HE1 H 1 6.844 0.02 . . . . . . 71 TYR HE1 . 15013 1
823 . 1 1 71 71 TYR HE2 H 1 6.844 0.02 . . . . . . 71 TYR HE2 . 15013 1
824 . 1 1 71 71 TYR C C 13 174.887 0.05 . . . . . . 71 TYR C . 15013 1
825 . 1 1 71 71 TYR CA C 13 55.083 0.019 . . . . . . 71 TYR CA . 15013 1
826 . 1 1 71 71 TYR CB C 13 39.672 0.007 . . . . . . 71 TYR CB . 15013 1
827 . 1 1 71 71 TYR N N 15 118.415 0.014 . . . . . . 71 TYR N . 15013 1
828 . 1 1 72 72 SER H H 1 8.554 0.014 . . . . . . 72 SER H . 15013 1
829 . 1 1 72 72 SER HA H 1 4.719 0.02 . . . . . . 72 SER HA . 15013 1
830 . 1 1 72 72 SER HB2 H 1 3.817 0.02 . . . . . . 72 SER HB2 . 15013 1
831 . 1 1 72 72 SER HB3 H 1 3.941 0.02 . . . . . . 72 SER HB3 . 15013 1
832 . 1 1 72 72 SER CA C 13 57.367 0.05 . . . . . . 72 SER CA . 15013 1
833 . 1 1 72 72 SER CB C 13 62.951 0.05 . . . . . . 72 SER CB . 15013 1
834 . 1 1 72 72 SER N N 15 116.950 0.019 . . . . . . 72 SER N . 15013 1
835 . 1 1 73 73 PRO HA H 1 4.532 0.02 . . . . . . 73 PRO HA . 15013 1
836 . 1 1 73 73 PRO HB2 H 1 0.661 0.007 . . . . . . 73 PRO HB2 . 15013 1
837 . 1 1 73 73 PRO HB3 H 1 1.322 0.02 . . . . . . 73 PRO HB3 . 15013 1
838 . 1 1 73 73 PRO HG2 H 1 1.161 0.02 . . . . . . 73 PRO HG2 . 15013 1
839 . 1 1 73 73 PRO HG3 H 1 1.686 0.02 . . . . . . 73 PRO HG3 . 15013 1
840 . 1 1 73 73 PRO HD2 H 1 3.302 0.001 . . . . . . 73 PRO HD2 . 15013 1
841 . 1 1 73 73 PRO HD3 H 1 3.567 0.001 . . . . . . 73 PRO HD3 . 15013 1
842 . 1 1 73 73 PRO CA C 13 61.507 0.088 . . . . . . 73 PRO CA . 15013 1
843 . 1 1 73 73 PRO CB C 13 29.776 0.049 . . . . . . 73 PRO CB . 15013 1
844 . 1 1 73 73 PRO CG C 13 26.859 0.054 . . . . . . 73 PRO CG . 15013 1
845 . 1 1 73 73 PRO CD C 13 50.001 0.079 . . . . . . 73 PRO CD . 15013 1
846 . 1 1 74 74 PRO HA H 1 4.741 0.02 . . . . . . 74 PRO HA . 15013 1
847 . 1 1 74 74 PRO HB2 H 1 1.999 0.02 . . . . . . 74 PRO HB2 . 15013 1
848 . 1 1 74 74 PRO HB3 H 1 2.330 0.001 . . . . . . 74 PRO HB3 . 15013 1
849 . 1 1 74 74 PRO HG2 H 1 2.001 0.02 . . . . . . 74 PRO HG2 . 15013 1
850 . 1 1 74 74 PRO HG3 H 1 2.196 0.002 . . . . . . 74 PRO HG3 . 15013 1
851 . 1 1 74 74 PRO HD2 H 1 3.189 0.002 . . . . . . 74 PRO HD2 . 15013 1
852 . 1 1 74 74 PRO HD3 H 1 3.871 0.001 . . . . . . 74 PRO HD3 . 15013 1
853 . 1 1 74 74 PRO CA C 13 61.690 0.041 . . . . . . 74 PRO CA . 15013 1
854 . 1 1 74 74 PRO CB C 13 30.166 0.010 . . . . . . 74 PRO CB . 15013 1
855 . 1 1 74 74 PRO CG C 13 27.776 0.031 . . . . . . 74 PRO CG . 15013 1
856 . 1 1 74 74 PRO CD C 13 50.617 0.035 . . . . . . 74 PRO CD . 15013 1
857 . 1 1 75 75 PRO HA H 1 4.659 0.02 . . . . . . 75 PRO HA . 15013 1
858 . 1 1 75 75 PRO HB2 H 1 1.839 0.02 . . . . . . 75 PRO HB2 . 15013 1
859 . 1 1 75 75 PRO HB3 H 1 2.274 0.004 . . . . . . 75 PRO HB3 . 15013 1
860 . 1 1 75 75 PRO HG2 H 1 1.938 0.02 . . . . . . 75 PRO HG2 . 15013 1
861 . 1 1 75 75 PRO HG3 H 1 2.001 0.02 . . . . . . 75 PRO HG3 . 15013 1
862 . 1 1 75 75 PRO HD2 H 1 3.607 0.003 . . . . . . 75 PRO HD2 . 15013 1
863 . 1 1 75 75 PRO HD3 H 1 3.731 0.02 . . . . . . 75 PRO HD3 . 15013 1
864 . 1 1 75 75 PRO CA C 13 61.405 0.05 . . . . . . 75 PRO CA . 15013 1
865 . 1 1 75 75 PRO CB C 13 30.547 0.015 . . . . . . 75 PRO CB . 15013 1
866 . 1 1 75 75 PRO CD C 13 50.256 0.011 . . . . . . 75 PRO CD . 15013 1
867 . 1 1 76 76 PRO HA H 1 3.906 0.001 . . . . . . 76 PRO HA . 15013 1
868 . 1 1 76 76 PRO HB2 H 1 1.401 0.001 . . . . . . 76 PRO HB2 . 15013 1
869 . 1 1 76 76 PRO HB3 H 1 1.504 0.02 . . . . . . 76 PRO HB3 . 15013 1
870 . 1 1 76 76 PRO HG2 H 1 1.672 0.001 . . . . . . 76 PRO HG2 . 15013 1
871 . 1 1 76 76 PRO HG3 H 1 1.965 0.001 . . . . . . 76 PRO HG3 . 15013 1
872 . 1 1 76 76 PRO HD2 H 1 3.494 0.002 . . . . . . 76 PRO HD2 . 15013 1
873 . 1 1 76 76 PRO HD3 H 1 3.703 0.001 . . . . . . 76 PRO HD3 . 15013 1
874 . 1 1 76 76 PRO CA C 13 61.578 0.086 . . . . . . 76 PRO CA . 15013 1
875 . 1 1 76 76 PRO CB C 13 30.252 0.051 . . . . . . 76 PRO CB . 15013 1
876 . 1 1 76 76 PRO CG C 13 27.719 0.056 . . . . . . 76 PRO CG . 15013 1
877 . 1 1 76 76 PRO CD C 13 50.441 0.080 . . . . . . 76 PRO CD . 15013 1
878 . 1 1 77 77 PRO HA H 1 4.225 0.02 . . . . . . 77 PRO HA . 15013 1
879 . 1 1 77 77 PRO HB2 H 1 1.875 0.02 . . . . . . 77 PRO HB2 . 15013 1
880 . 1 1 77 77 PRO HB3 H 1 2.153 0.02 . . . . . . 77 PRO HB3 . 15013 1
881 . 1 1 77 77 PRO HG2 H 1 1.725 0.02 . . . . . . 77 PRO HG2 . 15013 1
882 . 1 1 77 77 PRO HG3 H 1 1.877 0.02 . . . . . . 77 PRO HG3 . 15013 1
883 . 1 1 77 77 PRO HD2 H 1 2.055 0.02 . . . . . . 77 PRO HD2 . 15013 1
884 . 1 1 77 77 PRO HD3 H 1 3.019 0.001 . . . . . . 77 PRO HD3 . 15013 1
885 . 1 1 77 77 PRO CB C 13 31.700 0.009 . . . . . . 77 PRO CB . 15013 1
886 . 1 1 77 77 PRO CG C 13 26.906 0.086 . . . . . . 77 PRO CG . 15013 1
887 . 1 1 77 77 PRO CD C 13 50.136 0.059 . . . . . . 77 PRO CD . 15013 1
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