data_4655
#######################
# Entry information #
#######################
save_entry_information
_Entry.Sf_category entry_information
_Entry.Sf_framecode entry_information
_Entry.ID 4655
_Entry.Title
;
Solution Structure of Intradiskal Loop 1 of Bovine Rhodopsin (Rhodopsin Residues
93-123)
;
_Entry.Type macromolecule
_Entry.Version_type original
_Entry.Submission_date 2000-01-28
_Entry.Accession_date 2001-03-16
_Entry.Last_release_date 2001-05-10
_Entry.Original_release_date 2001-05-10
_Entry.Origination author
_Entry.NMR_STAR_version 3.1.1.61
_Entry.Original_NMR_STAR_version 2.1
_Entry.Experimental_method NMR
_Entry.Experimental_method_subtype .
_Entry.Details .
_Entry.BMRB_internal_directory_name .
loop_
_Entry_author.Ordinal
_Entry_author.Given_name
_Entry_author.Family_name
_Entry_author.First_initial
_Entry_author.Middle_initials
_Entry_author.Family_title
_Entry_author.Entry_ID
1 P. Yeagle . L. . 4655
2 A. Salloum . . . 4655
3 A. Chopra . . . 4655
4 N. Bhawsar . . . 4655
5 L. Ali . . . 4655
stop_
loop_
_Data_set.Type
_Data_set.Count
_Data_set.Entry_ID
assigned_chemical_shifts 1 4655
stop_
loop_
_Datum.Type
_Datum.Count
_Datum.Entry_ID
'1H chemical shifts' 157 4655
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 . . 2001-05-10 2000-01-28 original author . 4655
stop_
save_
###############
# Citations #
###############
save_entry_citation
_Citation.Sf_category citations
_Citation.Sf_framecode entry_citation
_Citation.Entry_ID 4655
_Citation.ID 1
_Citation.Class 'entry citation'
_Citation.CAS_abstract_code .
_Citation.MEDLINE_UI_code .
_Citation.DOI .
_Citation.PubMed_ID 10888202
_Citation.Full_citation .
_Citation.Title
;
Structures of the intradiskal loops and amino terminus of the G-protein
receptor, rhodopsin
;
_Citation.Status published
_Citation.Type journal
_Citation.Journal_abbrev 'J. Pept. Res.'
_Citation.Journal_name_full .
_Citation.Journal_volume 55
_Citation.Journal_issue 6
_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 455
_Citation.Page_last 465
_Citation.Year 2000
_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 P. Yeagle . L. . 4655 1
2 A. Salloum . . . 4655 1
3 A. Chopra . . . 4655 1
4 N. Bhawsar . . . 4655 1
5 L. Ali . . . 4655 1
6 G. Kuzmanovski . . . 4655 1
7 J. Alderfer . L. . 4655 1
8 A. Albert . D. . 4655 1
stop_
loop_
_Citation_keyword.Keyword
_Citation_keyword.Entry_ID
_Citation_keyword.Citation_ID
helix 4655 1
stop_
save_
#############################################
# Molecular system (assembly) description #
#############################################
save_system_RHODOPSIN
_Assembly.Sf_category assembly
_Assembly.Sf_framecode system_RHODOPSIN
_Assembly.Entry_ID 4655
_Assembly.ID 1
_Assembly.Name 'First intradiskal loop of RHODOPSIN (residues 93-123)'
_Assembly.BMRB_code .
_Assembly.Number_of_components .
_Assembly.Organic_ligands .
_Assembly.Metal_ions .
_Assembly.Non_standard_bonds .
_Assembly.Ambiguous_conformational_states .
_Assembly.Ambiguous_chem_comp_sites .
_Assembly.Molecules_in_chemical_exchange .
_Assembly.Paramagnetic no
_Assembly.Thiol_state 'all free'
_Assembly.Molecular_mass .
_Assembly.Enzyme_commission_number .
_Assembly.Details .
_Assembly.DB_query_date .
_Assembly.DB_query_revised_last_date .
loop_
_Assembly_type.Type
_Assembly_type.Entry_ID
_Assembly_type.Assembly_ID
monomer 4655 1
stop_
loop_
_Entity_assembly.ID
_Entity_assembly.Entity_assembly_name
_Entity_assembly.Entity_ID
_Entity_assembly.Entity_label
_Entity_assembly.Asym_ID
_Entity_assembly.PDB_chain_ID
_Entity_assembly.Experimental_data_reported
_Entity_assembly.Physical_state
_Entity_assembly.Conformational_isomer
_Entity_assembly.Chemical_exchange_state
_Entity_assembly.Magnetic_equivalence_group_code
_Entity_assembly.Role
_Entity_assembly.Details
_Entity_assembly.Entry_ID
_Entity_assembly.Assembly_ID
1 RHODOPSIN 1 $RHODOPSIN . . . native . . . . . 4655 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
. PDB 1EDS . . . . . . 4655 1
stop_
loop_
_Assembly_common_name.Name
_Assembly_common_name.Type
_Assembly_common_name.Entry_ID
_Assembly_common_name.Assembly_ID
'First intradiskal loop of RHODOPSIN (residues 93-123)' system 4655 1
RHODOPSIN abbreviation 4655 1
stop_
save_
####################################
# Biological polymers and ligands #
####################################
save_RHODOPSIN
_Entity.Sf_category entity
_Entity.Sf_framecode RHODOPSIN
_Entity.Entry_ID 4655
_Entity.ID 1
_Entity.BMRB_code .
_Entity.Name RHODOPSIN
_Entity.Type polymer
_Entity.Polymer_common_type .
_Entity.Polymer_type polypeptide(L)
_Entity.Polymer_type_details .
_Entity.Polymer_strand_ID .
_Entity.Polymer_seq_one_letter_code_can .
_Entity.Polymer_seq_one_letter_code
;
TTLYTSLHGYFVFGPTGCNL
EGFFATLGGEI
;
_Entity.Target_identifier .
_Entity.Polymer_author_defined_seq .
_Entity.Polymer_author_seq_details .
_Entity.Ambiguous_conformational_states .
_Entity.Ambiguous_chem_comp_sites .
_Entity.Nstd_monomer .
_Entity.Nstd_chirality .
_Entity.Nstd_linkage .
_Entity.Nonpolymer_comp_ID .
_Entity.Nonpolymer_comp_label .
_Entity.Number_of_monomers 31
_Entity.Number_of_nonpolymer_components .
_Entity.Paramagnetic .
_Entity.Thiol_state 'all free'
_Entity.Src_method .
_Entity.Parent_entity_ID 1
_Entity.Fragment .
_Entity.Mutation .
_Entity.EC_number .
_Entity.Calc_isoelectric_point .
_Entity.Formula_weight .
_Entity.Formula_weight_exptl .
_Entity.Formula_weight_exptl_meth .
_Entity.Details .
_Entity.DB_query_date .
_Entity.DB_query_revised_last_date 2015-11-24
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 PDB 1EDS . "Solution Structure Of Intradiskal Loop 1 Of Bovine Rhodopsin (Rhodopsin Residues 92-123)" . . . . . 100.00 31 100.00 100.00 1.41e-11 . . . . 4655 1
2 no PDB 1F88 . "Crystal Structure Of Bovine Rhodopsin" . . . . . 100.00 348 100.00 100.00 4.83e-11 . . . . 4655 1
3 no PDB 1GZM . "Structure Of Bovine Rhodopsin In A Trigonal Crystal Form" . . . . . 100.00 349 100.00 100.00 4.87e-11 . . . . 4655 1
4 no PDB 1HZX . "Crystal Structure Of Bovine Rhodopsin" . . . . . 100.00 349 100.00 100.00 4.87e-11 . . . . 4655 1
5 no PDB 1JFP . "Structure Of Bovine Rhodopsin (Dark Adapted)" . . . . . 100.00 348 100.00 100.00 4.83e-11 . . . . 4655 1
6 no PDB 1L9H . "Crystal Structure Of Bovine Rhodopsin At 2.6 Angstroms Resolution" . . . . . 100.00 349 100.00 100.00 4.87e-11 . . . . 4655 1
7 no PDB 1LN6 . "Structure Of Bovine Rhodopsin (Metarhodopsin Ii)" . . . . . 100.00 348 100.00 100.00 4.83e-11 . . . . 4655 1
8 no PDB 1U19 . "Crystal Structure Of Bovine Rhodopsin At 2.2 Angstroms Resolution" . . . . . 100.00 349 100.00 100.00 4.87e-11 . . . . 4655 1
9 no PDB 2G87 . "Crystallographic Model Of Bathorhodopsin" . . . . . 100.00 349 100.00 100.00 4.87e-11 . . . . 4655 1
10 no PDB 2HPY . "Crystallographic Model Of Lumirhodopsin" . . . . . 100.00 349 100.00 100.00 4.87e-11 . . . . 4655 1
11 no PDB 2I35 . "Crystal Structure Of Rhombohedral Crystal Form Of Ground-State Rhodopsin" . . . . . 100.00 349 100.00 100.00 4.87e-11 . . . . 4655 1
12 no PDB 2I36 . "Crystal Structure Of Trigonal Crystal Form Of Ground-State Rhodopsin" . . . . . 100.00 349 100.00 100.00 4.87e-11 . . . . 4655 1
13 no PDB 2I37 . "Crystal Structure Of A Photoactivated Rhodopsin" . . . . . 100.00 349 100.00 100.00 4.87e-11 . . . . 4655 1
14 no PDB 2J4Y . "Crystal Structure Of A Rhodopsin Stabilizing Mutant Expressed In Mammalian Cells" . . . . . 100.00 349 100.00 100.00 5.22e-11 . . . . 4655 1
15 no PDB 2PED . "Crystallographic Model Of 9-Cis-Rhodopsin" . . . . . 100.00 349 100.00 100.00 4.87e-11 . . . . 4655 1
16 no PDB 3C9L . "Structure Of Ground-State Bovine Rhodospin In A Hexagonal Crystal Form" . . . . . 100.00 348 100.00 100.00 4.83e-11 . . . . 4655 1
17 no PDB 3C9M . "Structure Of A Mutant Bovine Rhodopsin In Hexagonal Crystal Form" . . . . . 100.00 348 100.00 100.00 5.18e-11 . . . . 4655 1
18 no PDB 3CAP . "Crystal Structure Of Native Opsin: The G Protein-Coupled Receptor Rhodopsin In Its Ligand-Free State" . . . . . 100.00 348 100.00 100.00 4.83e-11 . . . . 4655 1
19 no PDB 3DQB . "Crystal Structure Of The Active G-protein-coupled Receptor Opsin In Complex With A C-terminal Peptide Derived From The Galpha S" . . . . . 100.00 348 100.00 100.00 4.83e-11 . . . . 4655 1
20 no PDB 3OAX . "Crystal Structure Of Bovine Rhodopsin With Beta-Ionone" . . . . . 100.00 349 100.00 100.00 4.87e-11 . . . . 4655 1
21 no PDB 3PQR . "Crystal Structure Of Metarhodopsin Ii In Complex With A C-Terminal Peptide Derived From The Galpha Subunit Of Transducin" . . . . . 100.00 348 100.00 100.00 4.83e-11 . . . . 4655 1
22 no PDB 3PXO . "Crystal Structure Of Metarhodopsin Ii" . . . . . 100.00 348 100.00 100.00 4.83e-11 . . . . 4655 1
23 no PDB 4A4M . "Crystal Structure Of The Light-Activated Constitutively Active N2c,M257y,D282c Rhodopsin Mutant In Complex With A Peptide Resem" . . . . . 100.00 349 100.00 100.00 5.44e-11 . . . . 4655 1
24 no PDB 4BEY . "Night Blindness Causing G90d Rhodopsin In Complex With Gact2 Peptide" . . . . . 100.00 349 100.00 100.00 5.22e-11 . . . . 4655 1
25 no PDB 4BEZ . "Night Blindness Causing G90d Rhodopsin In The Active Conformation" . . . . . 100.00 349 100.00 100.00 5.22e-11 . . . . 4655 1
26 no PDB 4J4Q . "Crystal Structure Of Active Conformation Of Gpcr Opsin Stabilized By Octylglucoside" . . . . . 100.00 348 100.00 100.00 4.83e-11 . . . . 4655 1
27 no PDB 4PXF . "Crystal Structure Of The Active G-protein-coupled Receptor Opsin In Complex With The Finger-loop Peptide Derived From The Full-" . . . . . 100.00 348 100.00 100.00 4.83e-11 . . . . 4655 1
28 no PDB 4X1H . "Opsin/g(alpha) Peptide Complex Stabilized By Nonyl-glucoside" . . . . . 100.00 348 100.00 100.00 4.83e-11 . . . . 4655 1
29 no DBJ BAB83621 . "rhodopsin [synthetic construct]" . . . . . 100.00 348 100.00 100.00 4.83e-11 . . . . 4655 1
30 no DBJ BAC31871 . "unnamed protein product [Mus musculus]" . . . . . 100.00 348 100.00 100.00 4.36e-11 . . . . 4655 1
31 no DBJ BAC31908 . "unnamed protein product [Mus musculus]" . . . . . 100.00 348 100.00 100.00 4.36e-11 . . . . 4655 1
32 no DBJ BAD02408 . "rod visual pigment [Otolemur crassicaudatus]" . . . . . 100.00 348 100.00 100.00 5.18e-11 . . . . 4655 1
33 no DBJ BAD02410 . "rod visual pigment [Otolemur crassicaudatus]" . . . . . 100.00 348 100.00 100.00 5.18e-11 . . . . 4655 1
34 no EMBL CAA43398 . "opsin [Cricetulus griseus]" . . . . . 100.00 348 100.00 100.00 4.98e-11 . . . . 4655 1
35 no EMBL CAA87081 . "rhodopsin [Rattus norvegicus]" . . . . . 100.00 348 100.00 100.00 4.73e-11 . . . . 4655 1
36 no EMBL CAD10144 . "opsin [Felis catus]" . . . . . 100.00 348 100.00 100.00 4.69e-11 . . . . 4655 1
37 no GB AAA30674 . "rhodopsin [Bos taurus]" . . . . . 100.00 348 100.00 100.00 4.83e-11 . . . . 4655 1
38 no GB AAA30675 . "rhodopsin, partial [Bos taurus]" . . . . . 100.00 343 100.00 100.00 4.79e-11 . . . . 4655 1
39 no GB AAA39861 . "opsin [Mus musculus]" . . . . . 100.00 348 100.00 100.00 4.45e-11 . . . . 4655 1
40 no GB AAA63392 . "opsin [Mus musculus]" . . . . . 100.00 348 100.00 100.00 4.45e-11 . . . . 4655 1
41 no GB AAA84439 . "opsin [Rattus norvegicus]" . . . . . 100.00 348 100.00 100.00 4.54e-11 . . . . 4655 1
42 no PRF 0811197A . rhodopsin . . . . . 100.00 347 100.00 100.00 4.51e-11 . . . . 4655 1
43 no PRF 0901188A . rhodopsin . . . . . 100.00 348 100.00 100.00 4.83e-11 . . . . 4655 1
44 no PRF 0901212A . rhodopsin . . . . . 100.00 348 100.00 100.00 4.83e-11 . . . . 4655 1
45 no PRF 1001148A . rhodopsin . . . . . 100.00 348 100.00 100.00 4.83e-11 . . . . 4655 1
46 no REF NP_001009242 . "rhodopsin [Felis catus]" . . . . . 100.00 348 100.00 100.00 4.69e-11 . . . . 4655 1
47 no REF NP_001014890 . "rhodopsin [Bos taurus]" . . . . . 100.00 348 100.00 100.00 4.83e-11 . . . . 4655 1
48 no REF NP_001231336 . "rhodopsin [Cricetulus griseus]" . . . . . 100.00 348 100.00 100.00 4.98e-11 . . . . 4655 1
49 no REF NP_254276 . "rhodopsin [Rattus norvegicus]" . . . . . 100.00 348 100.00 100.00 4.73e-11 . . . . 4655 1
50 no REF NP_663358 . "rhodopsin [Mus musculus]" . . . . . 100.00 348 100.00 100.00 4.36e-11 . . . . 4655 1
51 no SP O18766 . "RecName: Full=Rhodopsin" . . . . . 100.00 348 100.00 100.00 4.50e-11 . . . . 4655 1
52 no SP O62794 . "RecName: Full=Rhodopsin" . . . . . 100.00 348 100.00 100.00 4.23e-11 . . . . 4655 1
53 no SP O62795 . "RecName: Full=Rhodopsin" . . . . . 100.00 348 100.00 100.00 4.23e-11 . . . . 4655 1
54 no SP P02699 . "RecName: Full=Rhodopsin" . . . . . 100.00 348 100.00 100.00 4.83e-11 . . . . 4655 1
55 no SP P02700 . "RecName: Full=Rhodopsin" . . . . . 100.00 348 100.00 100.00 4.23e-11 . . . . 4655 1
56 no TPG DAA16827 . "TPA: rhodopsin [Bos taurus]" . . . . . 100.00 348 100.00 100.00 4.83e-11 . . . . 4655 1
stop_
loop_
_Entity_common_name.Name
_Entity_common_name.Type
_Entity_common_name.Entry_ID
_Entity_common_name.Entity_ID
RHODOPSIN common 4655 1
RHODOPSIN abbreviation 4655 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 93 THR . 4655 1
2 94 THR . 4655 1
3 95 LEU . 4655 1
4 96 TYR . 4655 1
5 97 THR . 4655 1
6 98 SER . 4655 1
7 99 LEU . 4655 1
8 100 HIS . 4655 1
9 101 GLY . 4655 1
10 102 TYR . 4655 1
11 103 PHE . 4655 1
12 104 VAL . 4655 1
13 105 PHE . 4655 1
14 106 GLY . 4655 1
15 107 PRO . 4655 1
16 108 THR . 4655 1
17 109 GLY . 4655 1
18 110 CYS . 4655 1
19 111 ASN . 4655 1
20 112 LEU . 4655 1
21 113 GLU . 4655 1
22 114 GLY . 4655 1
23 115 PHE . 4655 1
24 116 PHE . 4655 1
25 117 ALA . 4655 1
26 118 THR . 4655 1
27 119 LEU . 4655 1
28 120 GLY . 4655 1
29 121 GLY . 4655 1
30 122 GLU . 4655 1
31 123 ILE . 4655 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
. THR 1 1 4655 1
. THR 2 2 4655 1
. LEU 3 3 4655 1
. TYR 4 4 4655 1
. THR 5 5 4655 1
. SER 6 6 4655 1
. LEU 7 7 4655 1
. HIS 8 8 4655 1
. GLY 9 9 4655 1
. TYR 10 10 4655 1
. PHE 11 11 4655 1
. VAL 12 12 4655 1
. PHE 13 13 4655 1
. GLY 14 14 4655 1
. PRO 15 15 4655 1
. THR 16 16 4655 1
. GLY 17 17 4655 1
. CYS 18 18 4655 1
. ASN 19 19 4655 1
. LEU 20 20 4655 1
. GLU 21 21 4655 1
. GLY 22 22 4655 1
. PHE 23 23 4655 1
. PHE 24 24 4655 1
. ALA 25 25 4655 1
. THR 26 26 4655 1
. LEU 27 27 4655 1
. GLY 28 28 4655 1
. GLY 29 29 4655 1
. GLU 30 30 4655 1
. ILE 31 31 4655 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 4655
_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 $RHODOPSIN . 9913 organism . 'Bos taurus' cow . . Eukaryota Metazoa Bos taurus . . . . . . . . . . . . . . . . . . . . . 4655 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 4655
_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 $RHODOPSIN . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4655 1
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Sample.Sf_category sample
_Sample.Sf_framecode sample_1
_Sample.Entry_ID 4655
_Sample.ID 1
_Sample.Type solution
_Sample.Sub_type .
_Sample.Details .
_Sample.Aggregate_sample_number .
_Sample.Solvent_system .
_Sample.Preparation_date .
_Sample.Preparation_expiration_date .
_Sample.Polycrystallization_protocol .
_Sample.Single_crystal_protocol .
_Sample.Crystal_grow_apparatus .
_Sample.Crystal_grow_atmosphere .
_Sample.Crystal_grow_details .
_Sample.Crystal_grow_method .
_Sample.Crystal_grow_method_cit_ID .
_Sample.Crystal_grow_pH .
_Sample.Crystal_grow_pH_range .
_Sample.Crystal_grow_pressure .
_Sample.Crystal_grow_pressure_esd .
_Sample.Crystal_grow_seeding .
_Sample.Crystal_grow_seeding_cit_ID .
_Sample.Crystal_grow_temp .
_Sample.Crystal_grow_temp_details .
_Sample.Crystal_grow_temp_esd .
_Sample.Crystal_grow_time .
_Sample.Oriented_sample_prep_protocol .
_Sample.Lyophilization_cryo_protectant .
_Sample.Storage_protocol .
loop_
_Sample_component.ID
_Sample_component.Mol_common_name
_Sample_component.Isotopic_labeling
_Sample_component.Assembly_ID
_Sample_component.Assembly_label
_Sample_component.Entity_ID
_Sample_component.Entity_label
_Sample_component.Product_ID
_Sample_component.Type
_Sample_component.Concentration_val
_Sample_component.Concentration_val_min
_Sample_component.Concentration_val_max
_Sample_component.Concentration_val_units
_Sample_component.Concentration_val_err
_Sample_component.Vendor
_Sample_component.Vendor_product_name
_Sample_component.Vendor_product_code
_Sample_component.Entry_ID
_Sample_component.Sample_ID
1 RHODOPSIN . . . 1 $RHODOPSIN . . 2 . . mM . . . . 4655 1
2 DMSO . . . . . . . . . . % . . . . 4655 1
stop_
save_
#######################
# Sample conditions #
#######################
save_sample_cond_1
_Sample_condition_list.Sf_category sample_conditions
_Sample_condition_list.Sf_framecode sample_cond_1
_Sample_condition_list.Entry_ID 4655
_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
temperature 303 . K 4655 1
pressure 1 . atm 4655 1
stop_
save_
############################
# Computer software used #
############################
save_FELIX
_Software.Sf_category software
_Software.Sf_framecode FELIX
_Software.Entry_ID 4655
_Software.ID 1
_Software.Name FELIX
_Software.Version .
_Software.Details .
loop_
_Task.Task
_Task.Entry_ID
_Task.Software_ID
'data analysis' 4655 1
stop_
save_
save_DIANA
_Software.Sf_category software
_Software.Sf_framecode DIANA
_Software.Entry_ID 4655
_Software.ID 2
_Software.Name DIANA
_Software.Version .
_Software.Details .
loop_
_Task.Task
_Task.Entry_ID
_Task.Software_ID
refinement 4655 2
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 4655
_NMR_spectrometer.ID 1
_NMR_spectrometer.Details .
_NMR_spectrometer.Manufacturer Bruker
_NMR_spectrometer.Model AMX
_NMR_spectrometer.Serial_number .
_NMR_spectrometer.Field_strength 600
save_
save_spectrometer_list
_NMR_spectrometer_list.Sf_category NMR_spectrometer_list
_NMR_spectrometer_list.Sf_framecode spectrometer_list
_NMR_spectrometer_list.Entry_ID 4655
_NMR_spectrometer_list.ID 1
loop_
_NMR_spectrometer_view.ID
_NMR_spectrometer_view.Name
_NMR_spectrometer_view.Manufacturer
_NMR_spectrometer_view.Model
_NMR_spectrometer_view.Serial_number
_NMR_spectrometer_view.Field_strength
_NMR_spectrometer_view.Details
_NMR_spectrometer_view.Citation_ID
_NMR_spectrometer_view.Citation_label
_NMR_spectrometer_view.Entry_ID
_NMR_spectrometer_view.NMR_spectrometer_list_ID
1 spectrometer_1 Bruker AMX . 600 . . . 4655 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 4655
_Experiment_list.ID 1
_Experiment_list.Details .
loop_
_Experiment.ID
_Experiment.Name
_Experiment.Raw_data_flag
_Experiment.NMR_spec_expt_ID
_Experiment.NMR_spec_expt_label
_Experiment.MS_expt_ID
_Experiment.MS_expt_label
_Experiment.SAXS_expt_ID
_Experiment.SAXS_expt_label
_Experiment.FRET_expt_ID
_Experiment.FRET_expt_label
_Experiment.EMR_expt_ID
_Experiment.EMR_expt_label
_Experiment.Sample_ID
_Experiment.Sample_label
_Experiment.Sample_state
_Experiment.Sample_volume
_Experiment.Sample_volume_units
_Experiment.Sample_condition_list_ID
_Experiment.Sample_condition_list_label
_Experiment.Sample_spinning_rate
_Experiment.Sample_angle
_Experiment.NMR_tube_type
_Experiment.NMR_spectrometer_ID
_Experiment.NMR_spectrometer_label
_Experiment.NMR_spectrometer_probe_ID
_Experiment.NMR_spectrometer_probe_label
_Experiment.NMR_spectral_processing_ID
_Experiment.NMR_spectral_processing_label
_Experiment.Mass_spectrometer_ID
_Experiment.Mass_spectrometer_label
_Experiment.Xray_instrument_ID
_Experiment.Xray_instrument_label
_Experiment.Fluorescence_instrument_ID
_Experiment.Fluorescence_instrument_label
_Experiment.EMR_instrument_ID
_Experiment.EMR_instrument_label
_Experiment.Chromatographic_system_ID
_Experiment.Chromatographic_system_label
_Experiment.Chromatographic_column_ID
_Experiment.Chromatographic_column_label
_Experiment.Entry_ID
_Experiment.Experiment_list_ID
1 '2D NOESY' . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4655 1
2 DQF-COSY . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 4655 1
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_ref_1
_Chem_shift_reference.Sf_category chem_shift_reference
_Chem_shift_reference.Sf_framecode chemical_shift_ref_1
_Chem_shift_reference.Entry_ID 4655
_Chem_shift_reference.ID 1
_Chem_shift_reference.Details .
loop_
_Chem_shift_ref.Atom_type
_Chem_shift_ref.Atom_isotope_number
_Chem_shift_ref.Mol_common_name
_Chem_shift_ref.Atom_group
_Chem_shift_ref.Concentration_val
_Chem_shift_ref.Concentration_units
_Chem_shift_ref.Solvent
_Chem_shift_ref.Rank
_Chem_shift_ref.Chem_shift_units
_Chem_shift_ref.Chem_shift_val
_Chem_shift_ref.Ref_method
_Chem_shift_ref.Ref_type
_Chem_shift_ref.Indirect_shift_ratio
_Chem_shift_ref.External_ref_loc
_Chem_shift_ref.External_ref_sample_geometry
_Chem_shift_ref.External_ref_axis
_Chem_shift_ref.Indirect_shift_ratio_cit_ID
_Chem_shift_ref.Indirect_shift_ratio_cit_label
_Chem_shift_ref.Ref_correction_type
_Chem_shift_ref.Correction_val
_Chem_shift_ref.Correction_val_cit_ID
_Chem_shift_ref.Correction_val_cit_label
_Chem_shift_ref.Entry_ID
_Chem_shift_ref.Chem_shift_reference_ID
H 1 . . . . . . ppm . . . . . . . 1 $entry_citation . . 1 $entry_citation 4655 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_chemical_shift_set_1
_Assigned_chem_shift_list.Sf_category assigned_chemical_shifts
_Assigned_chem_shift_list.Sf_framecode chemical_shift_set_1
_Assigned_chem_shift_list.Entry_ID 4655
_Assigned_chem_shift_list.ID 1
_Assigned_chem_shift_list.Sample_condition_list_ID 1
_Assigned_chem_shift_list.Sample_condition_list_label $sample_cond_1
_Assigned_chem_shift_list.Chem_shift_reference_ID 1
_Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_ref_1
_Assigned_chem_shift_list.Chem_shift_1H_err .
_Assigned_chem_shift_list.Chem_shift_13C_err .
_Assigned_chem_shift_list.Chem_shift_15N_err .
_Assigned_chem_shift_list.Chem_shift_31P_err .
_Assigned_chem_shift_list.Chem_shift_2H_err .
_Assigned_chem_shift_list.Chem_shift_19F_err .
_Assigned_chem_shift_list.Error_derivation_method .
_Assigned_chem_shift_list.Details .
_Assigned_chem_shift_list.Text_data_format .
_Assigned_chem_shift_list.Text_data .
loop_
_Chem_shift_experiment.Experiment_ID
_Chem_shift_experiment.Experiment_name
_Chem_shift_experiment.Sample_ID
_Chem_shift_experiment.Sample_label
_Chem_shift_experiment.Sample_state
_Chem_shift_experiment.Entry_ID
_Chem_shift_experiment.Assigned_chem_shift_list_ID
. . 1 $sample_1 . 4655 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 THR HA H 1 4.01 . . . . . . . . . . . 4655 1
2 . 1 1 1 1 THR HB H 1 3.375 . . . . . . . . . . . 4655 1
3 . 1 1 1 1 THR HG21 H 1 1.05 . . . . . . . . . . . 4655 1
4 . 1 1 1 1 THR HG22 H 1 1.05 . . . . . . . . . . . 4655 1
5 . 1 1 1 1 THR HG23 H 1 1.05 . . . . . . . . . . . 4655 1
6 . 1 1 2 2 THR H H 1 8.46 . . . . . . . . . . . 4655 1
7 . 1 1 2 2 THR HA H 1 4.405 . . . . . . . . . . . 4655 1
8 . 1 1 2 2 THR HB H 1 3.96 . . . . . . . . . . . 4655 1
9 . 1 1 2 2 THR HG21 H 1 1.13 . . . . . . . . . . . 4655 1
10 . 1 1 2 2 THR HG22 H 1 1.13 . . . . . . . . . . . 4655 1
11 . 1 1 2 2 THR HG23 H 1 1.13 . . . . . . . . . . . 4655 1
12 . 1 1 3 3 LEU H H 1 7.74 . . . . . . . . . . . 4655 1
13 . 1 1 3 3 LEU HA H 1 4.37 . . . . . . . . . . . 4655 1
14 . 1 1 4 4 TYR H H 1 7.78 . . . . . . . . . . . 4655 1
15 . 1 1 4 4 TYR HA H 1 4.47 . . . . . . . . . . . 4655 1
16 . 1 1 4 4 TYR HB2 H 1 2.66 . . . . . . . . . . . 4655 1
17 . 1 1 4 4 TYR HB3 H 1 2.87 . . . . . . . . . . . 4655 1
18 . 1 1 4 4 TYR HD1 H 1 6.975 . . . . . . . . . . . 4655 1
19 . 1 1 4 4 TYR HD2 H 1 6.975 . . . . . . . . . . . 4655 1
20 . 1 1 4 4 TYR HE1 H 1 7.31 . . . . . . . . . . . 4655 1
21 . 1 1 4 4 TYR HE2 H 1 7.31 . . . . . . . . . . . 4655 1
22 . 1 1 5 5 THR H H 1 7.83 . . . . . . . . . . . 4655 1
23 . 1 1 5 5 THR HA H 1 4.22 . . . . . . . . . . . 4655 1
24 . 1 1 5 5 THR HB H 1 3.99 . . . . . . . . . . . 4655 1
25 . 1 1 5 5 THR HG21 H 1 1.01 . . . . . . . . . . . 4655 1
26 . 1 1 5 5 THR HG22 H 1 1.01 . . . . . . . . . . . 4655 1
27 . 1 1 5 5 THR HG23 H 1 1.01 . . . . . . . . . . . 4655 1
28 . 1 1 6 6 SER H H 1 8.33 . . . . . . . . . . . 4655 1
29 . 1 1 6 6 SER HA H 1 4.52 . . . . . . . . . . . 4655 1
30 . 1 1 6 6 SER HB2 H 1 3.76 . . . . . . . . . . . 4655 1
31 . 1 1 6 6 SER HB3 H 1 3.76 . . . . . . . . . . . 4655 1
32 . 1 1 7 7 LEU H H 1 7.91 . . . . . . . . . . . 4655 1
33 . 1 1 7 7 LEU HA H 1 4.16 . . . . . . . . . . . 4655 1
34 . 1 1 7 7 LEU HB2 H 1 1.44 . . . . . . . . . . . 4655 1
35 . 1 1 7 7 LEU HB3 H 1 1.44 . . . . . . . . . . . 4655 1
36 . 1 1 7 7 LEU HG H 1 1.72 . . . . . . . . . . . 4655 1
37 . 1 1 7 7 LEU HD11 H 1 0.76 . . . . . . . . . . . 4655 1
38 . 1 1 7 7 LEU HD12 H 1 0.76 . . . . . . . . . . . 4655 1
39 . 1 1 7 7 LEU HD13 H 1 0.76 . . . . . . . . . . . 4655 1
40 . 1 1 7 7 LEU HD21 H 1 0.76 . . . . . . . . . . . 4655 1
41 . 1 1 7 7 LEU HD22 H 1 0.76 . . . . . . . . . . . 4655 1
42 . 1 1 7 7 LEU HD23 H 1 0.76 . . . . . . . . . . . 4655 1
43 . 1 1 8 8 HIS H H 1 8.03 . . . . . . . . . . . 4655 1
44 . 1 1 8 8 HIS HA H 1 4.54 . . . . . . . . . . . 4655 1
45 . 1 1 8 8 HIS HB2 H 1 3.05 . . . . . . . . . . . 4655 1
46 . 1 1 8 8 HIS HB3 H 1 3.05 . . . . . . . . . . . 4655 1
47 . 1 1 9 9 GLY H H 1 8.00 . . . . . . . . . . . 4655 1
48 . 1 1 9 9 GLY HA2 H 1 3.64 . . . . . . . . . . . 4655 1
49 . 1 1 9 9 GLY HA3 H 1 3.64 . . . . . . . . . . . 4655 1
50 . 1 1 10 10 TYR H H 1 7.985 . . . . . . . . . . . 4655 1
51 . 1 1 10 10 TYR HA H 1 4.395 . . . . . . . . . . . 4655 1
52 . 1 1 10 10 TYR HB2 H 1 2.56 . . . . . . . . . . . 4655 1
53 . 1 1 10 10 TYR HB3 H 1 2.83 . . . . . . . . . . . 4655 1
54 . 1 1 10 10 TYR HD1 H 1 6.931 . . . . . . . . . . . 4655 1
55 . 1 1 10 10 TYR HD2 H 1 6.931 . . . . . . . . . . . 4655 1
56 . 1 1 10 10 TYR HE1 H 1 7.13 . . . . . . . . . . . 4655 1
57 . 1 1 10 10 TYR HE2 H 1 7.13 . . . . . . . . . . . 4655 1
58 . 1 1 11 11 PHE H H 1 8.16 . . . . . . . . . . . 4655 1
59 . 1 1 11 11 PHE HA H 1 4.57 . . . . . . . . . . . 4655 1
60 . 1 1 12 12 VAL H H 1 7.70 . . . . . . . . . . . 4655 1
61 . 1 1 12 12 VAL HA H 1 4.12 . . . . . . . . . . . 4655 1
62 . 1 1 12 12 VAL HB H 1 1.8 . . . . . . . . . . . 4655 1
63 . 1 1 12 12 VAL HG21 H 1 0.74 . . . . . . . . . . . 4655 1
64 . 1 1 12 12 VAL HG22 H 1 0.74 . . . . . . . . . . . 4655 1
65 . 1 1 12 12 VAL HG23 H 1 0.74 . . . . . . . . . . . 4655 1
66 . 1 1 13 13 PHE H H 1 8.005 . . . . . . . . . . . 4655 1
67 . 1 1 13 13 PHE HA H 1 4.59 . . . . . . . . . . . 4655 1
68 . 1 1 13 13 PHE HB2 H 1 2.75 . . . . . . . . . . . 4655 1
69 . 1 1 13 13 PHE HB3 H 1 2.98 . . . . . . . . . . . 4655 1
70 . 1 1 13 13 PHE HD1 H 1 7.185 . . . . . . . . . . . 4655 1
71 . 1 1 13 13 PHE HD2 H 1 7.185 . . . . . . . . . . . 4655 1
72 . 1 1 14 14 GLY H H 1 8.01 . . . . . . . . . . . 4655 1
73 . 1 1 14 14 GLY HA2 H 1 3.73 . . . . . . . . . . . 4655 1
74 . 1 1 14 14 GLY HA3 H 1 3.73 . . . . . . . . . . . 4655 1
75 . 1 1 15 15 PRO HA H 1 4.44 . . . . . . . . . . . 4655 1
76 . 1 1 15 15 PRO HB2 H 1 2.0 . . . . . . . . . . . 4655 1
77 . 1 1 15 15 PRO HB3 H 1 1.85 . . . . . . . . . . . 4655 1
78 . 1 1 15 15 PRO HG2 H 1 3.44 . . . . . . . . . . . 4655 1
79 . 1 1 15 15 PRO HG3 H 1 3.44 . . . . . . . . . . . 4655 1
80 . 1 1 16 16 THR H H 1 7.85 . . . . . . . . . . . 4655 1
81 . 1 1 16 16 THR HA H 1 4.16 . . . . . . . . . . . 4655 1
82 . 1 1 16 16 THR HG21 H 1 1.04 . . . . . . . . . . . 4655 1
83 . 1 1 16 16 THR HG22 H 1 1.04 . . . . . . . . . . . 4655 1
84 . 1 1 16 16 THR HG23 H 1 1.04 . . . . . . . . . . . 4655 1
85 . 1 1 17 17 GLY H H 1 7.84 . . . . . . . . . . . 4655 1
86 . 1 1 17 17 GLY HA2 H 1 3.58 . . . . . . . . . . . 4655 1
87 . 1 1 17 17 GLY HA3 H 1 3.58 . . . . . . . . . . . 4655 1
88 . 1 1 18 18 CYS H H 1 8.19 . . . . . . . . . . . 4655 1
89 . 1 1 18 18 CYS HB2 H 1 2.77 . . . . . . . . . . . 4655 1
90 . 1 1 18 18 CYS HB3 H 1 3.04 . . . . . . . . . . . 4655 1
91 . 1 1 19 19 ASN H H 1 8.25 . . . . . . . . . . . 4655 1
92 . 1 1 19 19 ASN HA H 1 4.53 . . . . . . . . . . . 4655 1
93 . 1 1 19 19 ASN HB2 H 1 2.41 . . . . . . . . . . . 4655 1
94 . 1 1 19 19 ASN HB3 H 1 2.56 . . . . . . . . . . . 4655 1
95 . 1 1 19 19 ASN HD21 H 1 6.872 . . . . . . . . . . . 4655 1
96 . 1 1 19 19 ASN HD22 H 1 7.36 . . . . . . . . . . . 4655 1
97 . 1 1 20 20 LEU H H 1 8.07 . . . . . . . . . . . 4655 1
98 . 1 1 20 20 LEU HA H 1 4.08 . . . . . . . . . . . 4655 1
99 . 1 1 21 21 GLU H H 1 7.66 . . . . . . . . . . . 4655 1
100 . 1 1 21 21 GLU HA H 1 4.165 . . . . . . . . . . . 4655 1
101 . 1 1 21 21 GLU HB2 H 1 1.88 . . . . . . . . . . . 4655 1
102 . 1 1 21 21 GLU HB3 H 1 1.74 . . . . . . . . . . . 4655 1
103 . 1 1 21 21 GLU HG2 H 1 2.20 . . . . . . . . . . . 4655 1
104 . 1 1 21 21 GLU HG3 H 1 2.20 . . . . . . . . . . . 4655 1
105 . 1 1 22 22 GLY H H 1 7.95 . . . . . . . . . . . 4655 1
106 . 1 1 22 22 GLY HA2 H 1 3.59 . . . . . . . . . . . 4655 1
107 . 1 1 22 22 GLY HA3 H 1 3.59 . . . . . . . . . . . 4655 1
108 . 1 1 23 23 PHE H H 1 7.875 . . . . . . . . . . . 4655 1
109 . 1 1 23 23 PHE HA H 1 4.46 . . . . . . . . . . . 4655 1
110 . 1 1 23 23 PHE HB2 H 1 2.92 . . . . . . . . . . . 4655 1
111 . 1 1 23 23 PHE HB3 H 1 2.67 . . . . . . . . . . . 4655 1
112 . 1 1 23 23 PHE HD1 H 1 7.135 . . . . . . . . . . . 4655 1
113 . 1 1 23 23 PHE HD2 H 1 7.135 . . . . . . . . . . . 4655 1
114 . 1 1 23 23 PHE HE1 H 1 6.97 . . . . . . . . . . . 4655 1
115 . 1 1 23 23 PHE HE2 H 1 6.97 . . . . . . . . . . . 4655 1
116 . 1 1 24 24 PHE H H 1 8.12 . . . . . . . . . . . 4655 1
117 . 1 1 24 24 PHE HA H 1 4.49 . . . . . . . . . . . 4655 1
118 . 1 1 24 24 PHE HB2 H 1 3.0 . . . . . . . . . . . 4655 1
119 . 1 1 24 24 PHE HB3 H 1 2.78 . . . . . . . . . . . 4655 1
120 . 1 1 24 24 PHE HD1 H 1 7.2 . . . . . . . . . . . 4655 1
121 . 1 1 24 24 PHE HD2 H 1 7.2 . . . . . . . . . . . 4655 1
122 . 1 1 25 25 ALA H H 1 8.105 . . . . . . . . . . . 4655 1
123 . 1 1 25 25 ALA HA H 1 4.38 . . . . . . . . . . . 4655 1
124 . 1 1 25 25 ALA HB1 H 1 1.21 . . . . . . . . . . . 4655 1
125 . 1 1 25 25 ALA HB2 H 1 1.21 . . . . . . . . . . . 4655 1
126 . 1 1 25 25 ALA HB3 H 1 1.21 . . . . . . . . . . . 4655 1
127 . 1 1 26 26 THR H H 1 7.71 . . . . . . . . . . . 4655 1
128 . 1 1 26 26 THR HA H 1 4.21 . . . . . . . . . . . 4655 1
129 . 1 1 26 26 THR HB H 1 3.99 . . . . . . . . . . . 4655 1
130 . 1 1 26 26 THR HG21 H 1 1.02 . . . . . . . . . . . 4655 1
131 . 1 1 26 26 THR HG22 H 1 1.02 . . . . . . . . . . . 4655 1
132 . 1 1 26 26 THR HG23 H 1 1.02 . . . . . . . . . . . 4655 1
133 . 1 1 27 27 LEU H H 1 7.814 . . . . . . . . . . . 4655 1
134 . 1 1 27 27 LEU HA H 1 4.28 . . . . . . . . . . . 4655 1
135 . 1 1 27 27 LEU HB2 H 1 1.47 . . . . . . . . . . . 4655 1
136 . 1 1 27 27 LEU HB3 H 1 1.47 . . . . . . . . . . . 4655 1
137 . 1 1 27 27 LEU HG H 1 0.8 . . . . . . . . . . . 4655 1
138 . 1 1 28 28 GLY H H 1 8.105 . . . . . . . . . . . 4655 1
139 . 1 1 28 28 GLY HA2 H 1 3.67 . . . . . . . . . . . 4655 1
140 . 1 1 28 28 GLY HA3 H 1 3.67 . . . . . . . . . . . 4655 1
141 . 1 1 29 29 GLY H H 1 7.94 . . . . . . . . . . . 4655 1
142 . 1 1 29 29 GLY HA2 H 1 3.74 . . . . . . . . . . . 4655 1
143 . 1 1 29 29 GLY HA3 H 1 3.74 . . . . . . . . . . . 4655 1
144 . 1 1 30 30 GLU H H 1 7.91 . . . . . . . . . . . 4655 1
145 . 1 1 30 30 GLU HA H 1 4.60 . . . . . . . . . . . 4655 1
146 . 1 1 30 30 GLU HB2 H 1 1.97 . . . . . . . . . . . 4655 1
147 . 1 1 30 30 GLU HB3 H 1 1.86 . . . . . . . . . . . 4655 1
148 . 1 1 30 30 GLU HG2 H 1 2.17 . . . . . . . . . . . 4655 1
149 . 1 1 30 30 GLU HG3 H 1 2.17 . . . . . . . . . . . 4655 1
150 . 1 1 31 31 ILE H H 1 7.85 . . . . . . . . . . . 4655 1
151 . 1 1 31 31 ILE HA H 1 4.27 . . . . . . . . . . . 4655 1
152 . 1 1 31 31 ILE HB H 1 1.75 . . . . . . . . . . . 4655 1
153 . 1 1 31 31 ILE HG12 H 1 1.35 . . . . . . . . . . . 4655 1
154 . 1 1 31 31 ILE HG13 H 1 1.0 . . . . . . . . . . . 4655 1
155 . 1 1 31 31 ILE HD11 H 1 2.82 . . . . . . . . . . . 4655 1
156 . 1 1 31 31 ILE HD12 H 1 2.82 . . . . . . . . . . . 4655 1
157 . 1 1 31 31 ILE HD13 H 1 2.82 . . . . . . . . . . . 4655 1
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