data_1162 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 1162 _Entry.Title ; Sequence-specific 1H-NMR assignment and conformation of proteolytic fragment 163-231 of bacterioopsin ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1995-07-31 _Entry.Accession_date 1996-03-25 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination BMRB _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 Igor Barsukov . L. . 1162 2 Galina Abdulaeva . V. . 1162 3 Alexander Arseniev . S. . 1162 4 Vladimir Bystrov . F. . 1162 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 1162 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 440 1162 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 4 . . 2010-06-14 . revision BMRB 'Complete natural source information' 1162 3 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1162 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1162 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 1162 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 1162 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Barsukov, Igor L., Abdulaeva, Galina V., Arseniev, Alexander S., Bystrov, Vladimir F., "Sequence-specific 1H-NMR assignment and conformation of proteolytic fragment 163-231 of bacterioopsin," Eur. J. Biochem. 192, 321-327 (1990). ; _Citation.Title ; Sequence-specific 1H-NMR assignment and conformation of proteolytic fragment 163-231 of bacterioopsin ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Eur. J. Biochem.' _Citation.Journal_name_full . _Citation.Journal_volume 192 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 321 _Citation.Page_last 327 _Citation.Year 1990 _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 Igor Barsukov . L. . 1162 1 2 Galina Abdulaeva . V. . 1162 1 3 Alexander Arseniev . S. . 1162 1 4 Vladimir Bystrov . F. . 1162 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_bacteriorhodopsin _Assembly.Sf_category assembly _Assembly.Sf_framecode system_bacteriorhodopsin _Assembly.Entry_ID 1162 _Assembly.ID 1 _Assembly.Name bacteriorhodopsin _Assembly.BMRB_code . _Assembly.Number_of_components 1 _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 . _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 bacteriorhodopsin 1 $bacteriorhodopsin . . . . . . . . . 1162 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID bacteriorhodopsin system 1162 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_bacteriorhodopsin _Entity.Sf_category entity _Entity.Sf_framecode bacteriorhodopsin _Entity.Entry_ID 1162 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name bacteriorhodopsin _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 ; MRPQVASTFKVLRNVTVVLW SAYPVVWLIGSEGAGIVPLN IETLLFMVLDVSAKVGFGLI LLRSRAIFG ; _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 69 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _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 2015-11-26 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 17361 . bR . . . . . 100.00 249 98.55 100.00 9.29e-37 . . . . 1162 1 2 no PDB 1AP9 . "X-Ray Structure Of Bacteriorhodopsin From Microcrystals Grown In Lipidic Cubic Phases" . . . . . 100.00 248 98.55 100.00 9.58e-37 . . . . 1162 1 3 no PDB 1AT9 . "Structure Of Bacteriorhodopsin At 3.0 Angstrom Determined By Electron Crystallography" . . . . . 100.00 248 98.55 100.00 9.68e-37 . . . . 1162 1 4 no PDB 1BCT . "Three-Dimensional Structure Of Proteolytic Fragment 163-231 Of Bacterioopsin Determined From Nuclear Magnetic Resonance Data In" . . . . . 100.00 69 98.55 100.00 1.84e-38 . . . . 1162 1 5 no PDB 1BM1 . "Crystal Structure Of Bacteriorhodopsin In The Light-adapted State" . . . . . 100.00 248 98.55 100.00 9.68e-37 . . . . 1162 1 6 no PDB 1BRD . "Model For The Structure Of Bacteriorhodopsin Based On High-R Electron Cryo-Microscopy" . . . . . 100.00 248 98.55 100.00 9.68e-37 . . . . 1162 1 7 no PDB 1BRR . "X-Ray Structure Of The Bacteriorhodopsin TrimerLIPID COMPLEX" . . . . . 100.00 247 98.55 100.00 9.36e-37 . . . . 1162 1 8 no PDB 1BRX . "BacteriorhodopsinLIPID COMPLEX" . . . . . 100.00 248 98.55 100.00 9.68e-37 . . . . 1162 1 9 no PDB 1C3W . "BacteriorhodopsinLIPID COMPLEX AT 1.55 A RESOLUTION" . . . . . 100.00 222 98.55 100.00 7.48e-37 . . . . 1162 1 10 no PDB 1C8R . "Bacteriorhodopsin D96n Br State At 2.0 A Resolution" . . . . . 100.00 249 98.55 100.00 9.70e-37 . . . . 1162 1 11 no PDB 1C8S . "Bacteriorhodopsin D96n Late M State Intermediate" . . . . . 72.46 196 98.00 98.00 8.27e-22 . . . . 1162 1 12 no PDB 1CWQ . "M Intermediate Structure Of The Wild Type Bacteriorhodopsin In Combination With The Ground State Structure" . . . . . 100.00 248 98.55 100.00 8.61e-37 . . . . 1162 1 13 no PDB 1DZE . "Structure Of The M Intermediate Of Bacteriorhodopsin Trapped At 100k" . . . . . 100.00 248 98.55 100.00 9.58e-37 . . . . 1162 1 14 no PDB 1E0P . "L Intermediate Of Bacteriorhodopsin" . . . . . 100.00 228 98.55 100.00 7.78e-37 . . . . 1162 1 15 no PDB 1F4Z . "Bacteriorhodopsin-M Photointermediate State Of The E204q Mutant At 1.8 Angstrom Resolution" . . . . . 100.00 227 97.10 100.00 2.47e-36 . . . . 1162 1 16 no PDB 1F50 . "Bacteriorhodopsin-br State Of The E204q Mutant At 1.7 Angstrom Resolution" . . . . . 100.00 227 97.10 100.00 2.47e-36 . . . . 1162 1 17 no PDB 1FBB . "Crystal Structure Of Native Conformation Of Bacteriorhodopsin" . . . . . 100.00 248 98.55 100.00 9.58e-37 . . . . 1162 1 18 no PDB 1IW6 . "Crystal Structure Of The Ground State Of Bacteriorhodopsin" . . . . . 100.00 248 98.55 100.00 9.58e-37 . . . . 1162 1 19 no PDB 1IW9 . "Crystal Structure Of The M Intermediate Of Bacteriorhodopsin" . . . . . 100.00 248 98.55 100.00 9.58e-37 . . . . 1162 1 20 no PDB 1IXF . "Crystal Structure Of The K Intermediate Of Bacteriorhodopsin" . . . . . 100.00 248 98.55 100.00 9.58e-37 . . . . 1162 1 21 no PDB 1JV6 . "Bacteriorhodopsin D85sF219L DOUBLE MUTANT AT 2.00 ANGSTROM Resolution" . . . . . 100.00 249 97.10 98.55 7.69e-36 . . . . 1162 1 22 no PDB 1JV7 . "Bacteriorhodopsin O-like Intermediate State Of The D85s Mutant At 2.25 Angstrom Resolution" . . . . . 100.00 249 98.55 100.00 9.29e-37 . . . . 1162 1 23 no PDB 1KG8 . "X-Ray Structure Of An Early-M Intermediate Of Bacteriorhodopsin" . . . . . 100.00 231 98.55 100.00 8.28e-37 . . . . 1162 1 24 no PDB 1KG9 . 'Structure Of A "mock-Trapped" Early-M Intermediate Of Bacteriorhosopsin' . . . . . 100.00 231 98.55 100.00 8.28e-37 . . . . 1162 1 25 no PDB 1KGB . "Structure Of Ground-State Bacteriorhodopsin" . . . . . 100.00 231 98.55 100.00 8.28e-37 . . . . 1162 1 26 no PDB 1KME . "Crystal Structure Of Bacteriorhodopsin Crystallized From Bicelles" . . . . . 100.00 231 98.55 100.00 8.28e-37 . . . . 1162 1 27 no PDB 1L0M . "Solution Structure Of Bacteriorhodopsin" . . . . . 81.16 212 98.21 100.00 9.46e-28 . . . . 1162 1 28 no PDB 1M0K . "Bacteriorhodopsin K Intermediate At 1.43 A Resolution" . . . . . 100.00 262 98.55 100.00 1.18e-36 . . . . 1162 1 29 no PDB 1M0L . "BacteriorhodopsinLIPID COMPLEX AT 1.47 A RESOLUTION" . . . . . 100.00 262 98.55 100.00 1.18e-36 . . . . 1162 1 30 no PDB 1M0M . "Bacteriorhodopsin M1 Intermediate At 1.43 A Resolution" . . . . . 100.00 262 98.55 100.00 1.18e-36 . . . . 1162 1 31 no PDB 1MGY . "Structure Of The D85s Mutant Of Bacteriorhodopsin With Bromide Bound" . . . . . 100.00 249 98.55 100.00 9.29e-37 . . . . 1162 1 32 no PDB 1O0A . "Bacteriorhodopsin L Intermediate At 1.62 A Resolution" . . . . . 100.00 249 98.55 100.00 9.29e-37 . . . . 1162 1 33 no PDB 1P8H . "Bacteriorhodopsin M1 Intermediate Produced At Room Temperature" . . . . . 100.00 249 98.55 100.00 9.29e-37 . . . . 1162 1 34 no PDB 1P8I . "F219l Bacteriorhodopsin Mutant" . . . . . 100.00 249 97.10 98.55 8.20e-36 . . . . 1162 1 35 no PDB 1P8U . "Bacteriorhodopsin N' Intermediate At 1.62 A Resolution" . . . . . 100.00 249 98.55 100.00 9.10e-37 . . . . 1162 1 36 no PDB 1PXR . "Structure Of Pro50ala Mutant Of Bacteriorhodopsin" . . . . . 100.00 249 98.55 100.00 7.59e-37 . . . . 1162 1 37 no PDB 1PXS . "Structure Of Met56ala Mutant Of Bacteriorhodopsin" . . . . . 100.00 249 98.55 100.00 8.90e-37 . . . . 1162 1 38 no PDB 1PY6 . "Bacteriorhodopsin Crystallized From Bicells" . . . . . 100.00 249 98.55 100.00 9.29e-37 . . . . 1162 1 39 no PDB 1Q5I . "Crystal Structure Of Bacteriorhodopsin Mutant P186a Crystallized From Bicelles" . . . . . 100.00 249 97.10 98.55 1.49e-35 . . . . 1162 1 40 no PDB 1Q5J . "Crystal Structure Of Bacteriorhodopsin Mutant P91a Crystallized From Bicelles" . . . . . 100.00 249 98.55 100.00 7.59e-37 . . . . 1162 1 41 no PDB 1QHJ . "X-Ray Structure Of Bacteriorhodopsin Grown In Lipidic Cubic Phases" . . . . . 100.00 248 98.55 100.00 9.58e-37 . . . . 1162 1 42 no PDB 1QKO . "High Resolution X-Ray Structure Of An Early Intermediate In The Bacteriorhodopsin Photocycle" . . . . . 100.00 248 98.55 100.00 9.58e-37 . . . . 1162 1 43 no PDB 1QKP . "High Resolution X-Ray Structure Of An Early Intermediate In The Bacteriorhodopsin Photocycle" . . . . . 100.00 248 98.55 100.00 9.58e-37 . . . . 1162 1 44 no PDB 1QM8 . "Structure Of Bacteriorhodopsin At 100 K" . . . . . 100.00 248 98.55 100.00 9.58e-37 . . . . 1162 1 45 no PDB 1R2N . "Nmr Structure Of The All-trans Retinal In Dark-adapted Bacteriorhodopsin" . . . . . 100.00 249 98.55 100.00 9.29e-37 . . . . 1162 1 46 no PDB 1R84 . "Nmr Structure Of The 13-cis-15-syn Retinal In Dark_adapted Bacteriorhodopsin" . . . . . 100.00 232 98.55 100.00 7.95e-37 . . . . 1162 1 47 no PDB 1S51 . "Thr24ser Bacteriorhodopsin" . . . . . 100.00 227 98.55 100.00 7.84e-37 . . . . 1162 1 48 no PDB 1S52 . "Thr24val Bacteriorhodopsin" . . . . . 100.00 227 98.55 100.00 7.59e-37 . . . . 1162 1 49 no PDB 1S53 . "Thr46ser Bacteriorhodopsin" . . . . . 100.00 227 98.55 100.00 7.84e-37 . . . . 1162 1 50 no PDB 1S54 . "Thr24ala Bacteriorhodopsin" . . . . . 100.00 227 98.55 100.00 8.19e-37 . . . . 1162 1 51 no PDB 1S8J . "Nitrate-Bound D85s Mutant Of Bacteriorhodopsin" . . . . . 100.00 249 98.55 100.00 9.29e-37 . . . . 1162 1 52 no PDB 1S8L . "Anion-Free Form Of The D85s Mutant Of Bacteriorhodopsin From Crystals Grown In The Presence Of Halide" . . . . . 100.00 249 98.55 100.00 9.29e-37 . . . . 1162 1 53 no PDB 1TN0 . "Structure Of Bacterorhodopsin Mutant A51p" . . . . . 100.00 249 98.55 100.00 1.15e-36 . . . . 1162 1 54 no PDB 1TN5 . "Structure Of Bacterorhodopsin Mutant K41p" . . . . . 100.00 249 98.55 100.00 1.00e-36 . . . . 1162 1 55 no PDB 1UCQ . "Crystal Structure Of The L Intermediate Of Bacteriorhodopsin" . . . . . 100.00 249 98.55 100.00 9.29e-37 . . . . 1162 1 56 no PDB 1VJM . "Deformation Of Helix C In The Low-Temperature L-Intermediate Of Bacteriorhodopsin" . . . . . 100.00 249 98.55 100.00 9.29e-37 . . . . 1162 1 57 no PDB 1X0I . "Crystal Structure Of The Acid Blue Form Of Bacteriorhodopsin" . . . . . 100.00 248 98.55 100.00 9.58e-37 . . . . 1162 1 58 no PDB 1X0K . "Crystal Structure Of Bacteriorhodopsin At Ph 10" . . . . . 100.00 248 98.55 100.00 9.58e-37 . . . . 1162 1 59 no PDB 1X0S . "Crystal Structure Of The 13-Cis Isomer Of Bacteriorhodopsin" . . . . . 100.00 248 98.55 100.00 9.58e-37 . . . . 1162 1 60 no PDB 1XJI . "Bacteriorhodopsin Crystallized In Bicelles At Room Temperature" . . . . . 100.00 247 98.55 100.00 9.46e-37 . . . . 1162 1 61 no PDB 2AT9 . "Structure Of Bacteriorhodopsin At 3.0 Angstrom By Electron Crystallography" . . . . . 100.00 248 98.55 100.00 9.68e-37 . . . . 1162 1 62 no PDB 2BRD . "Crystal Structure Of Bacteriorhodopsin In Purple Membrane" . . . . . 100.00 248 98.55 100.00 9.68e-37 . . . . 1162 1 63 no PDB 2I1X . "BacteriorhodopsinLIPID COMPLEX, D96A MUTANT" . . . . . 100.00 249 98.55 100.00 9.10e-37 . . . . 1162 1 64 no PDB 2I20 . "BacteriorhodopsinLIPID COMPLEX, M STATE OF D96A MUTANT" . . . . . 100.00 249 98.55 100.00 9.10e-37 . . . . 1162 1 65 no PDB 2I21 . "BacteriorhodopsinLIPID COMPLEX, T46V MUTANT" . . . . . 100.00 249 98.55 100.00 1.01e-36 . . . . 1162 1 66 no PDB 2NTU . "Bacteriorhodopsin, Wild Type, Before Illumination" . . . . . 100.00 249 98.55 100.00 9.29e-37 . . . . 1162 1 67 no PDB 2NTW . "Bacteriorhodopsin, Wild Type, After Illumination To Produce The L Intermediate" . . . . . 100.00 249 98.55 100.00 9.29e-37 . . . . 1162 1 68 no PDB 2WJK . "Bacteriorhodopsin Mutant E204d" . . . . . 100.00 249 97.10 100.00 2.85e-36 . . . . 1162 1 69 no PDB 2WJL . "Bacteriorhodopsin Mutant E194d" . . . . . 100.00 249 97.10 100.00 2.85e-36 . . . . 1162 1 70 no PDB 2ZFE . "Crystal Structure Of Bacteriorhodopsin-Xenon Complex" . . . . . 100.00 262 98.55 100.00 1.18e-36 . . . . 1162 1 71 no PDB 2ZZL . "Structure Of Bacteriorhodopsin's M Intermediate At Ph 7" . . . . . 100.00 262 98.55 100.00 1.18e-36 . . . . 1162 1 72 no PDB 3COC . "Crystal Structure Of D115a Mutant Of Bacteriorhodopsin" . . . . . 100.00 249 98.55 100.00 9.10e-37 . . . . 1162 1 73 no PDB 3COD . "Crystal Structure Of T90aD115A MUTANT OF BACTERIORHODOPSIN" . . . . . 100.00 249 98.55 100.00 8.90e-37 . . . . 1162 1 74 no PDB 3HAN . "Crystal Structure Of Bacteriorhodopsin Mutant V49a Crystallized From Bicelles" . . . . . 100.00 249 98.55 100.00 9.10e-37 . . . . 1162 1 75 no PDB 3HAO . "Crystal Structure Of Bacteriorhodopsin Mutant L94a Crystallized From Bicelles" . . . . . 100.00 249 98.55 100.00 8.72e-37 . . . . 1162 1 76 no PDB 3HAP . "Crystal Structure Of Bacteriorhodopsin Mutant L111a Crystallized From Bicelles" . . . . . 100.00 249 98.55 100.00 8.72e-37 . . . . 1162 1 77 no PDB 3HAQ . "Crystal Structure Of Bacteriorhodopsin Mutant I148a Crystallized From Bicelles" . . . . . 100.00 249 98.55 100.00 8.72e-37 . . . . 1162 1 78 no PDB 3HAR . "Crystal Structure Of Bacteriorhodopsin Mutant I148v Crystallized From Bicelles" . . . . . 100.00 249 98.55 100.00 8.81e-37 . . . . 1162 1 79 no PDB 3HAS . "Crystal Structure Of Bacteriorhodopsin Mutant L152a Crystallized From Bicelles" . . . . . 100.00 249 98.55 100.00 8.72e-37 . . . . 1162 1 80 no PDB 3MBV . "Structure Of Bacterirhodopsin Crystallized In Betta-Xyloc(16+4) Meso Phase" . . . . . 100.00 248 98.55 100.00 9.58e-37 . . . . 1162 1 81 no PDB 3NS0 . "X-Ray Structure Of Bacteriorhodopsin" . . . . . 100.00 248 98.55 100.00 9.58e-37 . . . . 1162 1 82 no PDB 3NSB . "Structure Of Bacteriorhodopsin Ground State Before And After X-Ray Modification" . . . . . 100.00 248 98.55 100.00 9.58e-37 . . . . 1162 1 83 no PDB 3T45 . "Crystal Structure Of Bacteriorhodopsin Mutant A215t, A Phototaxis Signaling Mutant At 3.0 A Resolution" . . . . . 100.00 225 97.10 98.55 3.35e-36 . . . . 1162 1 84 no PDB 3UTV . "Crystal Structure Of Bacteriorhodopsin Mutant Y57f" . . . . . 100.00 249 98.55 100.00 9.91e-37 . . . . 1162 1 85 no PDB 3UTW . "Crystal Structure Of Bacteriorhodopsin Mutant P50a/y57f" . . . . . 100.00 249 98.55 100.00 8.62e-37 . . . . 1162 1 86 no PDB 3UTX . "Crystal Structure Of Bacteriorhodopsin Mutant T46a" . . . . . 100.00 249 98.55 100.00 9.49e-37 . . . . 1162 1 87 no PDB 3UTY . "Crystal Structure Of Bacteriorhodopsin Mutant P50a/t46a" . . . . . 100.00 249 98.55 100.00 7.83e-37 . . . . 1162 1 88 no PDB 3VHZ . "Crystal Structure Of The Trans Isomer Of The L93a Mutant Of Bacteriorhodopsin" . . . . . 100.00 262 98.55 100.00 9.47e-37 . . . . 1162 1 89 no PDB 3VI0 . "Crystal Structure Of The O Intermediate Of The L93a Mutant Of Bacteriorhodopsin" . . . . . 100.00 262 98.55 100.00 9.47e-37 . . . . 1162 1 90 no PDB 4HWL . "Crystal Structure Analysis Of The Bacteriorhodopsin In Facial Amphiphile-7 Dmpc Bicelle" . . . . . 100.00 262 98.55 100.00 1.18e-36 . . . . 1162 1 91 no PDB 4HYX . "Crystal Structure Analysis Of The Bacteriorhodopsin In Facial Amphiphile-4 Dmpc Bicelle" . . . . . 100.00 262 98.55 100.00 1.18e-36 . . . . 1162 1 92 no PDB 4MD1 . "Orange Species Of Bacteriorhodopsin From Halobacterium Salinarum" . . . . . 100.00 248 98.55 100.00 9.58e-37 . . . . 1162 1 93 no PDB 4MD2 . "Ground State Of Bacteriorhodopsin From Halobacterium Salinarum" . . . . . 100.00 248 98.55 100.00 9.58e-37 . . . . 1162 1 94 no PDB 4X31 . "Room Temperature Structure Of Bacteriorhodopsin From Lipidic Cubic Phase Obtained With Serial Millisecond Crystallography Using" . . . . . 100.00 229 98.55 100.00 7.72e-37 . . . . 1162 1 95 no PDB 4X32 . "Bacteriorhodopsin Ground State Structure Collected In Cryo Conditions From Crystals Obtained In Lcp With Peg As A Precipitant" . . . . . 100.00 228 98.55 100.00 7.78e-37 . . . . 1162 1 96 no PDB 4XXJ . "Crystal Structure Of Escherichia Coli-expressed Halobacterium Salinarum Bacteriorhodopsin In The Trimeric Form" . . . . . 100.00 269 97.10 98.55 9.99e-36 . . . . 1162 1 97 no PDB 5A44 . "Structure Of Bacteriorhodopsin Obtained From 20um Crystals By Multi Crystal Data Collection" . . . . . 100.00 248 98.55 100.00 9.58e-37 . . . . 1162 1 98 no PDB 5A45 . "Structure Of Bacteriorhodopsin Obtained From 5um Crystals By Multi Crystal Data Collection" . . . . . 100.00 248 98.55 100.00 9.58e-37 . . . . 1162 1 99 no EMBL CAA23744 . "unnamed protein product [Halobacterium salinarum]" . . . . . 100.00 262 98.55 100.00 1.18e-36 . . . . 1162 1 100 no EMBL CAA49762 . "bacterioopsin [synthetic construct]" . . . . . 100.00 259 98.55 100.00 1.77e-36 . . . . 1162 1 101 no EMBL CAA49774 . "bacterio-opsin [Halobacterium sp. GRB]" . . . . . 100.00 262 98.55 100.00 1.18e-36 . . . . 1162 1 102 no EMBL CAP14056 . "bacteriorhodopsin [Halobacterium salinarum R1]" . . . . . 100.00 262 98.55 100.00 1.18e-36 . . . . 1162 1 103 no GB AAA72184 . "bacteriorhodopsin [synthetic construct]" . . . . . 100.00 249 98.55 100.00 9.39e-37 . . . . 1162 1 104 no GB AAA72504 . "bacteriorhodopsin [Halobacterium salinarum]" . . . . . 100.00 262 98.55 100.00 1.18e-36 . . . . 1162 1 105 no GB AAA72603 . "bacteriorhodopsin [synthetic construct]" . . . . . 100.00 249 98.55 100.00 9.39e-37 . . . . 1162 1 106 no GB AAG19772 . "bacteriorhodopsin [Halobacterium sp. NRC-1]" . . . . . 100.00 262 98.55 100.00 1.18e-36 . . . . 1162 1 107 no GB AER29833 . "ChR2-EYFP-betabR [synthetic construct]" . . . . . 100.00 906 98.55 100.00 1.55e-34 . . . . 1162 1 108 no PRF 0501217A . bacteriorhodopsin . . . . . 100.00 247 97.10 98.55 3.96e-36 . . . . 1162 1 109 no PRF 0712242A . "bacteriorhodopsin precursor" . . . . . 100.00 262 97.10 98.55 2.49e-35 . . . . 1162 1 110 no REF WP_049892510 . "rhodopsin [Halobacterium salinarum]" . . . . . 100.00 230 98.55 100.00 4.39e-37 . . . . 1162 1 111 no SP P02945 . "RecName: Full=Bacteriorhodopsin; Short=BR; AltName: Full=Bacterioopsin; Short=BO; Flags: Precursor" . . . . . 100.00 262 98.55 100.00 1.18e-36 . . . . 1162 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID bacteriorhodopsin common 1162 1 'residues 163-231' variant 1162 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 . MET . 1162 1 2 . ARG . 1162 1 3 . PRO . 1162 1 4 . GLN . 1162 1 5 . VAL . 1162 1 6 . ALA . 1162 1 7 . SER . 1162 1 8 . THR . 1162 1 9 . PHE . 1162 1 10 . LYS . 1162 1 11 . VAL . 1162 1 12 . LEU . 1162 1 13 . ARG . 1162 1 14 . ASN . 1162 1 15 . VAL . 1162 1 16 . THR . 1162 1 17 . VAL . 1162 1 18 . VAL . 1162 1 19 . LEU . 1162 1 20 . TRP . 1162 1 21 . SER . 1162 1 22 . ALA . 1162 1 23 . TYR . 1162 1 24 . PRO . 1162 1 25 . VAL . 1162 1 26 . VAL . 1162 1 27 . TRP . 1162 1 28 . LEU . 1162 1 29 . ILE . 1162 1 30 . GLY . 1162 1 31 . SER . 1162 1 32 . GLU . 1162 1 33 . GLY . 1162 1 34 . ALA . 1162 1 35 . GLY . 1162 1 36 . ILE . 1162 1 37 . VAL . 1162 1 38 . PRO . 1162 1 39 . LEU . 1162 1 40 . ASN . 1162 1 41 . ILE . 1162 1 42 . GLU . 1162 1 43 . THR . 1162 1 44 . LEU . 1162 1 45 . LEU . 1162 1 46 . PHE . 1162 1 47 . MET . 1162 1 48 . VAL . 1162 1 49 . LEU . 1162 1 50 . ASP . 1162 1 51 . VAL . 1162 1 52 . SER . 1162 1 53 . ALA . 1162 1 54 . LYS . 1162 1 55 . VAL . 1162 1 56 . GLY . 1162 1 57 . PHE . 1162 1 58 . GLY . 1162 1 59 . LEU . 1162 1 60 . ILE . 1162 1 61 . LEU . 1162 1 62 . LEU . 1162 1 63 . ARG . 1162 1 64 . SER . 1162 1 65 . ARG . 1162 1 66 . ALA . 1162 1 67 . ILE . 1162 1 68 . PHE . 1162 1 69 . GLY . 1162 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 . MET 1 1 1162 1 . ARG 2 2 1162 1 . PRO 3 3 1162 1 . GLN 4 4 1162 1 . VAL 5 5 1162 1 . ALA 6 6 1162 1 . SER 7 7 1162 1 . THR 8 8 1162 1 . PHE 9 9 1162 1 . LYS 10 10 1162 1 . VAL 11 11 1162 1 . LEU 12 12 1162 1 . ARG 13 13 1162 1 . ASN 14 14 1162 1 . VAL 15 15 1162 1 . THR 16 16 1162 1 . VAL 17 17 1162 1 . VAL 18 18 1162 1 . LEU 19 19 1162 1 . TRP 20 20 1162 1 . SER 21 21 1162 1 . ALA 22 22 1162 1 . TYR 23 23 1162 1 . PRO 24 24 1162 1 . VAL 25 25 1162 1 . VAL 26 26 1162 1 . TRP 27 27 1162 1 . LEU 28 28 1162 1 . ILE 29 29 1162 1 . GLY 30 30 1162 1 . SER 31 31 1162 1 . GLU 32 32 1162 1 . GLY 33 33 1162 1 . ALA 34 34 1162 1 . GLY 35 35 1162 1 . ILE 36 36 1162 1 . VAL 37 37 1162 1 . PRO 38 38 1162 1 . LEU 39 39 1162 1 . ASN 40 40 1162 1 . ILE 41 41 1162 1 . GLU 42 42 1162 1 . THR 43 43 1162 1 . LEU 44 44 1162 1 . LEU 45 45 1162 1 . PHE 46 46 1162 1 . MET 47 47 1162 1 . VAL 48 48 1162 1 . LEU 49 49 1162 1 . ASP 50 50 1162 1 . VAL 51 51 1162 1 . SER 52 52 1162 1 . ALA 53 53 1162 1 . LYS 54 54 1162 1 . VAL 55 55 1162 1 . GLY 56 56 1162 1 . PHE 57 57 1162 1 . GLY 58 58 1162 1 . LEU 59 59 1162 1 . ILE 60 60 1162 1 . LEU 61 61 1162 1 . LEU 62 62 1162 1 . ARG 63 63 1162 1 . SER 64 64 1162 1 . ARG 65 65 1162 1 . ALA 66 66 1162 1 . ILE 67 67 1162 1 . PHE 68 68 1162 1 . GLY 69 69 1162 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 1162 _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 $bacteriorhodopsin . 2242 organism . 'Halobacterium halobium' . . . Bacteria . Halobacterium halobium R1M1 . . . . . . . . . . . 'purple membrane' . . . . . . . . 1162 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 1162 _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 $bacteriorhodopsin . 'not available' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1162 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 1162 _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 . save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_condition_set_one _Sample_condition_list.Entry_ID 1162 _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 8 . na 1162 1 temperature 303 . K 1162 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 1162 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 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 1162 _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 unknown unknown . 0 'spectrometer information not available' . . 1162 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 1162 _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 . . . . . . . . . . . . 1 $sample_one . . . 1 $sample_condition_set_one . . . 1 $spectrometer_list . . . . . . . . . . . . . . . . 1162 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_par_set_one _Chem_shift_reference.Entry_ID 1162 _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 . TMS . . . . . ppm 0 . . . . . . . . . . . . 1162 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_assignment_data_set_one _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode 'chemical_shift_assignment_data_set_one' _Assigned_chem_shift_list.Entry_ID 1162 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_condition_set_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_par_set_one _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_one . 1162 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 6 6 ALA H H 1 7.82 . . 1 . . . . . . . . 1162 1 2 . 1 1 6 6 ALA HA H 1 4.05 . . 1 . . . . . . . . 1162 1 3 . 1 1 6 6 ALA HB1 H 1 1.15 . . 1 . . . . . . . . 1162 1 4 . 1 1 6 6 ALA HB2 H 1 1.15 . . 1 . . . . . . . . 1162 1 5 . 1 1 6 6 ALA HB3 H 1 1.15 . . 1 . . . . . . . . 1162 1 6 . 1 1 7 7 SER H H 1 7.28 . . 1 . . . . . . . . 1162 1 7 . 1 1 7 7 SER HA H 1 3.94 . . 1 . . . . . . . . 1162 1 8 . 1 1 8 8 THR H H 1 7.79 . . 1 . . . . . . . . 1162 1 9 . 1 1 8 8 THR HA H 1 3.57 . . 1 . . . . . . . . 1162 1 10 . 1 1 8 8 THR HB H 1 4.02 . . 1 . . . . . . . . 1162 1 11 . 1 1 8 8 THR HG21 H 1 .96 . . 1 . . . . . . . . 1162 1 12 . 1 1 8 8 THR HG22 H 1 .96 . . 1 . . . . . . . . 1162 1 13 . 1 1 8 8 THR HG23 H 1 .96 . . 1 . . . . . . . . 1162 1 14 . 1 1 9 9 PHE H H 1 7.88 . . 1 . . . . . . . . 1162 1 15 . 1 1 9 9 PHE HA H 1 3.9 . . 1 . . . . . . . . 1162 1 16 . 1 1 9 9 PHE HB2 H 1 2.94 . . 1 . . . . . . . . 1162 1 17 . 1 1 9 9 PHE HB3 H 1 2.94 . . 1 . . . . . . . . 1162 1 18 . 1 1 10 10 LYS H H 1 7.79 . . 1 . . . . . . . . 1162 1 19 . 1 1 10 10 LYS HA H 1 3.56 . . 1 . . . . . . . . 1162 1 20 . 1 1 10 10 LYS HB2 H 1 1.45 . . 2 . . . . . . . . 1162 1 21 . 1 1 10 10 LYS HB3 H 1 1.74 . . 2 . . . . . . . . 1162 1 22 . 1 1 11 11 VAL H H 1 7.73 . . 1 . . . . . . . . 1162 1 23 . 1 1 11 11 VAL HA H 1 3.37 . . 1 . . . . . . . . 1162 1 24 . 1 1 11 11 VAL HB H 1 1.97 . . 1 . . . . . . . . 1162 1 25 . 1 1 11 11 VAL HG11 H 1 .72 . . 2 . . . . . . . . 1162 1 26 . 1 1 11 11 VAL HG12 H 1 .72 . . 2 . . . . . . . . 1162 1 27 . 1 1 11 11 VAL HG13 H 1 .72 . . 2 . . . . . . . . 1162 1 28 . 1 1 11 11 VAL HG21 H 1 .86 . . 2 . . . . . . . . 1162 1 29 . 1 1 11 11 VAL HG22 H 1 .86 . . 2 . . . . . . . . 1162 1 30 . 1 1 11 11 VAL HG23 H 1 .86 . . 2 . . . . . . . . 1162 1 31 . 1 1 12 12 LEU H H 1 7.88 . . 1 . . . . . . . . 1162 1 32 . 1 1 12 12 LEU HA H 1 3.7 . . 1 . . . . . . . . 1162 1 33 . 1 1 12 12 LEU HB2 H 1 1.29 . . 2 . . . . . . . . 1162 1 34 . 1 1 12 12 LEU HB3 H 1 1.53 . . 2 . . . . . . . . 1162 1 35 . 1 1 12 12 LEU HG H 1 .85 . . 1 . . . . . . . . 1162 1 36 . 1 1 12 12 LEU HD11 H 1 .6 . . 2 . . . . . . . . 1162 1 37 . 1 1 12 12 LEU HD12 H 1 .6 . . 2 . . . . . . . . 1162 1 38 . 1 1 12 12 LEU HD13 H 1 .6 . . 2 . . . . . . . . 1162 1 39 . 1 1 12 12 LEU HD21 H 1 .71 . . 2 . . . . . . . . 1162 1 40 . 1 1 12 12 LEU HD22 H 1 .71 . . 2 . . . . . . . . 1162 1 41 . 1 1 12 12 LEU HD23 H 1 .71 . . 2 . . . . . . . . 1162 1 42 . 1 1 13 13 ARG H H 1 8.38 . . 1 . . . . . . . . 1162 1 43 . 1 1 13 13 ARG HA H 1 3.57 . . 1 . . . . . . . . 1162 1 44 . 1 1 13 13 ARG HB2 H 1 1.51 . . 2 . . . . . . . . 1162 1 45 . 1 1 13 13 ARG HB3 H 1 1.73 . . 2 . . . . . . . . 1162 1 46 . 1 1 13 13 ARG HG2 H 1 1.22 . . 1 . . . . . . . . 1162 1 47 . 1 1 13 13 ARG HG3 H 1 1.22 . . 1 . . . . . . . . 1162 1 48 . 1 1 13 13 ARG HD2 H 1 2.73 . . 2 . . . . . . . . 1162 1 49 . 1 1 13 13 ARG HD3 H 1 2.9 . . 2 . . . . . . . . 1162 1 50 . 1 1 14 14 ASN H H 1 8.06 . . 1 . . . . . . . . 1162 1 51 . 1 1 14 14 ASN HA H 1 4.07 . . 1 . . . . . . . . 1162 1 52 . 1 1 14 14 ASN HB2 H 1 2.86 . . 2 . . . . . . . . 1162 1 53 . 1 1 14 14 ASN HB3 H 1 2.46 . . 2 . . . . . . . . 1162 1 54 . 1 1 14 14 ASN HD21 H 1 6.45 . . 2 . . . . . . . . 1162 1 55 . 1 1 14 14 ASN HD22 H 1 7.14 . . 2 . . . . . . . . 1162 1 56 . 1 1 15 15 VAL H H 1 8.46 . . 1 . . . . . . . . 1162 1 57 . 1 1 15 15 VAL HA H 1 3.31 . . 1 . . . . . . . . 1162 1 58 . 1 1 15 15 VAL HB H 1 1.92 . . 1 . . . . . . . . 1162 1 59 . 1 1 15 15 VAL HG11 H 1 .71 . . 2 . . . . . . . . 1162 1 60 . 1 1 15 15 VAL HG12 H 1 .71 . . 2 . . . . . . . . 1162 1 61 . 1 1 15 15 VAL HG13 H 1 .71 . . 2 . . . . . . . . 1162 1 62 . 1 1 15 15 VAL HG21 H 1 .85 . . 2 . . . . . . . . 1162 1 63 . 1 1 15 15 VAL HG22 H 1 .85 . . 2 . . . . . . . . 1162 1 64 . 1 1 15 15 VAL HG23 H 1 .85 . . 2 . . . . . . . . 1162 1 65 . 1 1 16 16 THR H H 1 7.61 . . 1 . . . . . . . . 1162 1 66 . 1 1 16 16 THR HA H 1 3.49 . . 1 . . . . . . . . 1162 1 67 . 1 1 16 16 THR HB H 1 4.04 . . 1 . . . . . . . . 1162 1 68 . 1 1 16 16 THR HG1 H 1 4.83 . . 1 . . . . . . . . 1162 1 69 . 1 1 16 16 THR HG21 H 1 .73 . . 1 . . . . . . . . 1162 1 70 . 1 1 16 16 THR HG22 H 1 .73 . . 1 . . . . . . . . 1162 1 71 . 1 1 16 16 THR HG23 H 1 .73 . . 1 . . . . . . . . 1162 1 72 . 1 1 17 17 VAL H H 1 7.72 . . 1 . . . . . . . . 1162 1 73 . 1 1 17 17 VAL HA H 1 3.41 . . 1 . . . . . . . . 1162 1 74 . 1 1 17 17 VAL HB H 1 2.02 . . 1 . . . . . . . . 1162 1 75 . 1 1 17 17 VAL HG11 H 1 .75 . . 2 . . . . . . . . 1162 1 76 . 1 1 17 17 VAL HG12 H 1 .75 . . 2 . . . . . . . . 1162 1 77 . 1 1 17 17 VAL HG13 H 1 .75 . . 2 . . . . . . . . 1162 1 78 . 1 1 17 17 VAL HG21 H 1 .84 . . 2 . . . . . . . . 1162 1 79 . 1 1 17 17 VAL HG22 H 1 .84 . . 2 . . . . . . . . 1162 1 80 . 1 1 17 17 VAL HG23 H 1 .84 . . 2 . . . . . . . . 1162 1 81 . 1 1 18 18 VAL H H 1 7.73 . . 1 . . . . . . . . 1162 1 82 . 1 1 18 18 VAL HA H 1 3.39 . . 1 . . . . . . . . 1162 1 83 . 1 1 18 18 VAL HB H 1 2.02 . . 1 . . . . . . . . 1162 1 84 . 1 1 18 18 VAL HG11 H 1 .72 . . 2 . . . . . . . . 1162 1 85 . 1 1 18 18 VAL HG12 H 1 .72 . . 2 . . . . . . . . 1162 1 86 . 1 1 18 18 VAL HG13 H 1 .72 . . 2 . . . . . . . . 1162 1 87 . 1 1 18 18 VAL HG21 H 1 .86 . . 2 . . . . . . . . 1162 1 88 . 1 1 18 18 VAL HG22 H 1 .86 . . 2 . . . . . . . . 1162 1 89 . 1 1 18 18 VAL HG23 H 1 .86 . . 2 . . . . . . . . 1162 1 90 . 1 1 19 19 LEU H H 1 2.15 . . 1 . . . . . . . . 1162 1 91 . 1 1 19 19 LEU HA H 1 3.81 . . 1 . . . . . . . . 1162 1 92 . 1 1 19 19 LEU HB2 H 1 1.62 . . 2 . . . . . . . . 1162 1 93 . 1 1 19 19 LEU HB3 H 1 1.7 . . 2 . . . . . . . . 1162 1 94 . 1 1 19 19 LEU HG H 1 .86 . . 1 . . . . . . . . 1162 1 95 . 1 1 19 19 LEU HD11 H 1 .62 . . 2 . . . . . . . . 1162 1 96 . 1 1 19 19 LEU HD12 H 1 .62 . . 2 . . . . . . . . 1162 1 97 . 1 1 19 19 LEU HD13 H 1 .62 . . 2 . . . . . . . . 1162 1 98 . 1 1 19 19 LEU HD21 H 1 .72 . . 2 . . . . . . . . 1162 1 99 . 1 1 19 19 LEU HD22 H 1 .72 . . 2 . . . . . . . . 1162 1 100 . 1 1 19 19 LEU HD23 H 1 .72 . . 2 . . . . . . . . 1162 1 101 . 1 1 20 20 TRP H H 1 8.32 . . 1 . . . . . . . . 1162 1 102 . 1 1 20 20 TRP HA H 1 4.18 . . 1 . . . . . . . . 1162 1 103 . 1 1 20 20 TRP HB2 H 1 3.1 . . 2 . . . . . . . . 1162 1 104 . 1 1 20 20 TRP HB3 H 1 3.16 . . 2 . . . . . . . . 1162 1 105 . 1 1 20 20 TRP HD1 H 1 6.95 . . 1 . . . . . . . . 1162 1 106 . 1 1 20 20 TRP HE1 H 1 9.68 . . 1 . . . . . . . . 1162 1 107 . 1 1 20 20 TRP HE3 H 1 7.3 . . 1 . . . . . . . . 1162 1 108 . 1 1 20 20 TRP HZ2 H 1 7.03 . . 1 . . . . . . . . 1162 1 109 . 1 1 20 20 TRP HZ3 H 1 6.62 . . 1 . . . . . . . . 1162 1 110 . 1 1 20 20 TRP HH2 H 1 6.77 . . 1 . . . . . . . . 1162 1 111 . 1 1 21 21 SER H H 1 7.9 . . 1 . . . . . . . . 1162 1 112 . 1 1 21 21 SER HA H 1 4 . . 1 . . . . . . . . 1162 1 113 . 1 1 21 21 SER HB2 H 1 3.78 . . 2 . . . . . . . . 1162 1 114 . 1 1 21 21 SER HB3 H 1 3.88 . . 2 . . . . . . . . 1162 1 115 . 1 1 21 21 SER HG H 1 5.12 . . 1 . . . . . . . . 1162 1 116 . 1 1 22 22 ALA H H 1 4.1 . . 1 . . . . . . . . 1162 1 117 . 1 1 22 22 ALA HA H 1 1.24 . . 1 . . . . . . . . 1162 1 118 . 1 1 23 23 TYR H H 1 7.65 . . 1 . . . . . . . . 1162 1 119 . 1 1 23 23 TYR HA H 1 4.1 . . 1 . . . . . . . . 1162 1 120 . 1 1 23 23 TYR HB2 H 1 2.79 . . 2 . . . . . . . . 1162 1 121 . 1 1 23 23 TYR HB3 H 1 2.95 . . 2 . . . . . . . . 1162 1 122 . 1 1 23 23 TYR HD1 H 1 6.4 . . 1 . . . . . . . . 1162 1 123 . 1 1 23 23 TYR HD2 H 1 6.4 . . 1 . . . . . . . . 1162 1 124 . 1 1 23 23 TYR HE1 H 1 6.75 . . 1 . . . . . . . . 1162 1 125 . 1 1 23 23 TYR HE2 H 1 6.75 . . 1 . . . . . . . . 1162 1 126 . 1 1 24 24 PRO HA H 1 3.84 . . 1 . . . . . . . . 1162 1 127 . 1 1 24 24 PRO HB2 H 1 1.85 . . 2 . . . . . . . . 1162 1 128 . 1 1 24 24 PRO HB3 H 1 2.06 . . 2 . . . . . . . . 1162 1 129 . 1 1 24 24 PRO HG2 H 1 1.34 . . 2 . . . . . . . . 1162 1 130 . 1 1 24 24 PRO HG3 H 1 1.59 . . 2 . . . . . . . . 1162 1 131 . 1 1 24 24 PRO HD2 H 1 3.44 . . 2 . . . . . . . . 1162 1 132 . 1 1 24 24 PRO HD3 H 1 3.51 . . 2 . . . . . . . . 1162 1 133 . 1 1 25 25 VAL H H 1 6.94 . . 1 . . . . . . . . 1162 1 134 . 1 1 25 25 VAL HA H 1 3.42 . . 1 . . . . . . . . 1162 1 135 . 1 1 25 25 VAL HB H 1 2.01 . . 1 . . . . . . . . 1162 1 136 . 1 1 25 25 VAL HG11 H 1 .74 . . 2 . . . . . . . . 1162 1 137 . 1 1 25 25 VAL HG12 H 1 .74 . . 2 . . . . . . . . 1162 1 138 . 1 1 25 25 VAL HG13 H 1 .74 . . 2 . . . . . . . . 1162 1 139 . 1 1 25 25 VAL HG21 H 1 .83 . . 2 . . . . . . . . 1162 1 140 . 1 1 25 25 VAL HG22 H 1 .83 . . 2 . . . . . . . . 1162 1 141 . 1 1 25 25 VAL HG23 H 1 .83 . . 2 . . . . . . . . 1162 1 142 . 1 1 26 26 VAL H H 1 7.5 . . 1 . . . . . . . . 1162 1 143 . 1 1 26 26 VAL HA H 1 3.26 . . 1 . . . . . . . . 1162 1 144 . 1 1 26 26 VAL HB H 1 1.86 . . 1 . . . . . . . . 1162 1 145 . 1 1 26 26 VAL HG11 H 1 .63 . . 2 . . . . . . . . 1162 1 146 . 1 1 26 26 VAL HG12 H 1 .63 . . 2 . . . . . . . . 1162 1 147 . 1 1 26 26 VAL HG13 H 1 .63 . . 2 . . . . . . . . 1162 1 148 . 1 1 26 26 VAL HG21 H 1 .74 . . 2 . . . . . . . . 1162 1 149 . 1 1 26 26 VAL HG22 H 1 .74 . . 2 . . . . . . . . 1162 1 150 . 1 1 26 26 VAL HG23 H 1 .74 . . 2 . . . . . . . . 1162 1 151 . 1 1 27 27 TRP H H 1 7.84 . . 1 . . . . . . . . 1162 1 152 . 1 1 27 27 TRP HA H 1 3.92 . . 1 . . . . . . . . 1162 1 153 . 1 1 27 27 TRP HB2 H 1 2.79 . . 2 . . . . . . . . 1162 1 154 . 1 1 27 27 TRP HB3 H 1 3 . . 2 . . . . . . . . 1162 1 155 . 1 1 27 27 TRP HD1 H 1 6.73 . . 1 . . . . . . . . 1162 1 156 . 1 1 27 27 TRP HE1 H 1 9.46 . . 1 . . . . . . . . 1162 1 157 . 1 1 27 27 TRP HE3 H 1 7.23 . . 1 . . . . . . . . 1162 1 158 . 1 1 27 27 TRP HZ2 H 1 7.07 . . 1 . . . . . . . . 1162 1 159 . 1 1 27 27 TRP HZ3 H 1 6.74 . . 1 . . . . . . . . 1162 1 160 . 1 1 27 27 TRP HH2 H 1 6.81 . . 1 . . . . . . . . 1162 1 161 . 1 1 28 28 LEU H H 1 7.8 . . 1 . . . . . . . . 1162 1 162 . 1 1 28 28 LEU HA H 1 3.69 . . 1 . . . . . . . . 1162 1 163 . 1 1 28 28 LEU HB2 H 1 1.53 . . 2 . . . . . . . . 1162 1 164 . 1 1 28 28 LEU HB3 H 1 1.64 . . 2 . . . . . . . . 1162 1 165 . 1 1 28 28 LEU HD11 H 1 .69 . . 1 . . . . . . . . 1162 1 166 . 1 1 28 28 LEU HD12 H 1 .69 . . 1 . . . . . . . . 1162 1 167 . 1 1 28 28 LEU HD13 H 1 .69 . . 1 . . . . . . . . 1162 1 168 . 1 1 28 28 LEU HD21 H 1 .69 . . 1 . . . . . . . . 1162 1 169 . 1 1 28 28 LEU HD22 H 1 .69 . . 1 . . . . . . . . 1162 1 170 . 1 1 28 28 LEU HD23 H 1 .69 . . 1 . . . . . . . . 1162 1 171 . 1 1 29 29 ILE H H 1 8.01 . . 1 . . . . . . . . 1162 1 172 . 1 1 29 29 ILE HA H 1 3.48 . . 1 . . . . . . . . 1162 1 173 . 1 1 29 29 ILE HB H 1 1.64 . . 1 . . . . . . . . 1162 1 174 . 1 1 29 29 ILE HG12 H 1 .92 . . 2 . . . . . . . . 1162 1 175 . 1 1 29 29 ILE HG13 H 1 1.52 . . 2 . . . . . . . . 1162 1 176 . 1 1 29 29 ILE HG21 H 1 .65 . . 1 . . . . . . . . 1162 1 177 . 1 1 29 29 ILE HG22 H 1 .65 . . 1 . . . . . . . . 1162 1 178 . 1 1 29 29 ILE HG23 H 1 .65 . . 1 . . . . . . . . 1162 1 179 . 1 1 29 29 ILE HD11 H 1 .57 . . 1 . . . . . . . . 1162 1 180 . 1 1 29 29 ILE HD12 H 1 .57 . . 1 . . . . . . . . 1162 1 181 . 1 1 29 29 ILE HD13 H 1 .57 . . 1 . . . . . . . . 1162 1 182 . 1 1 30 30 GLY H H 1 8.35 . . 1 . . . . . . . . 1162 1 183 . 1 1 30 30 GLY HA2 H 1 3.49 . . 2 . . . . . . . . 1162 1 184 . 1 1 30 30 GLY HA3 H 1 3.57 . . 2 . . . . . . . . 1162 1 185 . 1 1 31 31 SER H H 1 7.79 . . 1 . . . . . . . . 1162 1 186 . 1 1 31 31 SER HA H 1 3.85 . . 1 . . . . . . . . 1162 1 187 . 1 1 31 31 SER HB2 H 1 3.37 . . 2 . . . . . . . . 1162 1 188 . 1 1 31 31 SER HB3 H 1 3.55 . . 2 . . . . . . . . 1162 1 189 . 1 1 32 32 GLU H H 1 7.99 . . 1 . . . . . . . . 1162 1 190 . 1 1 32 32 GLU HA H 1 3.92 . . 1 . . . . . . . . 1162 1 191 . 1 1 32 32 GLU HB2 H 1 1.8 . . 2 . . . . . . . . 1162 1 192 . 1 1 32 32 GLU HB3 H 1 1.9 . . 2 . . . . . . . . 1162 1 193 . 1 1 33 33 GLY H H 1 8.03 . . 1 . . . . . . . . 1162 1 194 . 1 1 33 33 GLY HA2 H 1 3.59 . . 1 . . . . . . . . 1162 1 195 . 1 1 33 33 GLY HA3 H 1 3.59 . . 1 . . . . . . . . 1162 1 196 . 1 1 34 34 ALA H H 1 7.67 . . 1 . . . . . . . . 1162 1 197 . 1 1 34 34 ALA HA H 1 3.91 . . 1 . . . . . . . . 1162 1 198 . 1 1 34 34 ALA HB1 H 1 1.22 . . 1 . . . . . . . . 1162 1 199 . 1 1 34 34 ALA HB2 H 1 1.22 . . 1 . . . . . . . . 1162 1 200 . 1 1 34 34 ALA HB3 H 1 1.22 . . 1 . . . . . . . . 1162 1 201 . 1 1 35 35 GLY H H 1 7.73 . . 1 . . . . . . . . 1162 1 202 . 1 1 35 35 GLY HA2 H 1 3.58 . . 1 . . . . . . . . 1162 1 203 . 1 1 35 35 GLY HA3 H 1 3.58 . . 1 . . . . . . . . 1162 1 204 . 1 1 36 36 ILE H H 1 7.44 . . 1 . . . . . . . . 1162 1 205 . 1 1 36 36 ILE HA H 1 3.82 . . 1 . . . . . . . . 1162 1 206 . 1 1 36 36 ILE HB H 1 1.7 . . 1 . . . . . . . . 1162 1 207 . 1 1 36 36 ILE HG12 H 1 1.03 . . 2 . . . . . . . . 1162 1 208 . 1 1 36 36 ILE HG13 H 1 1.32 . . 2 . . . . . . . . 1162 1 209 . 1 1 36 36 ILE HG21 H 1 .7 . . 1 . . . . . . . . 1162 1 210 . 1 1 36 36 ILE HG22 H 1 .7 . . 1 . . . . . . . . 1162 1 211 . 1 1 36 36 ILE HG23 H 1 .7 . . 1 . . . . . . . . 1162 1 212 . 1 1 36 36 ILE HD11 H 1 .64 . . 1 . . . . . . . . 1162 1 213 . 1 1 36 36 ILE HD12 H 1 .64 . . 1 . . . . . . . . 1162 1 214 . 1 1 36 36 ILE HD13 H 1 .64 . . 1 . . . . . . . . 1162 1 215 . 1 1 37 37 VAL H H 1 7.43 . . 1 . . . . . . . . 1162 1 216 . 1 1 37 37 VAL HA H 1 3.83 . . 1 . . . . . . . . 1162 1 217 . 1 1 37 37 VAL HB H 1 2.02 . . 1 . . . . . . . . 1162 1 218 . 1 1 37 37 VAL HG11 H 1 .71 . . 2 . . . . . . . . 1162 1 219 . 1 1 37 37 VAL HG12 H 1 .71 . . 2 . . . . . . . . 1162 1 220 . 1 1 37 37 VAL HG13 H 1 .71 . . 2 . . . . . . . . 1162 1 221 . 1 1 37 37 VAL HG21 H 1 .82 . . 2 . . . . . . . . 1162 1 222 . 1 1 37 37 VAL HG22 H 1 .82 . . 2 . . . . . . . . 1162 1 223 . 1 1 37 37 VAL HG23 H 1 .82 . . 2 . . . . . . . . 1162 1 224 . 1 1 38 38 PRO HA H 1 4.04 . . 1 . . . . . . . . 1162 1 225 . 1 1 38 38 PRO HB2 H 1 1.72 . . 2 . . . . . . . . 1162 1 226 . 1 1 38 38 PRO HB3 H 1 2.01 . . 2 . . . . . . . . 1162 1 227 . 1 1 39 39 LEU H H 1 7.28 . . 1 . . . . . . . . 1162 1 228 . 1 1 39 39 LEU HA H 1 3.93 . . 1 . . . . . . . . 1162 1 229 . 1 1 39 39 LEU HB2 H 1 1.44 . . 1 . . . . . . . . 1162 1 230 . 1 1 39 39 LEU HB3 H 1 1.44 . . 1 . . . . . . . . 1162 1 231 . 1 1 39 39 LEU HD11 H 1 .66 . . 2 . . . . . . . . 1162 1 232 . 1 1 39 39 LEU HD12 H 1 .66 . . 2 . . . . . . . . 1162 1 233 . 1 1 39 39 LEU HD13 H 1 .66 . . 2 . . . . . . . . 1162 1 234 . 1 1 39 39 LEU HD21 H 1 .74 . . 2 . . . . . . . . 1162 1 235 . 1 1 39 39 LEU HD22 H 1 .74 . . 2 . . . . . . . . 1162 1 236 . 1 1 39 39 LEU HD23 H 1 .74 . . 2 . . . . . . . . 1162 1 237 . 1 1 40 40 ASN H H 1 7.98 . . 1 . . . . . . . . 1162 1 238 . 1 1 40 40 ASN HA H 1 4.28 . . 1 . . . . . . . . 1162 1 239 . 1 1 40 40 ASN HB2 H 1 2.53 . . 2 . . . . . . . . 1162 1 240 . 1 1 40 40 ASN HB3 H 1 2.81 . . 2 . . . . . . . . 1162 1 241 . 1 1 40 40 ASN HD21 H 1 6.26 . . 2 . . . . . . . . 1162 1 242 . 1 1 40 40 ASN HD22 H 1 7.22 . . 2 . . . . . . . . 1162 1 243 . 1 1 41 41 ILE H H 1 7.94 . . 1 . . . . . . . . 1162 1 244 . 1 1 41 41 ILE HA H 1 3.48 . . 1 . . . . . . . . 1162 1 245 . 1 1 41 41 ILE HB H 1 1.69 . . 1 . . . . . . . . 1162 1 246 . 1 1 41 41 ILE HG12 H 1 1.28 . . 2 . . . . . . . . 1162 1 247 . 1 1 41 41 ILE HG13 H 1 1.44 . . 2 . . . . . . . . 1162 1 248 . 1 1 41 41 ILE HG21 H 1 .69 . . 1 . . . . . . . . 1162 1 249 . 1 1 41 41 ILE HG22 H 1 .69 . . 1 . . . . . . . . 1162 1 250 . 1 1 41 41 ILE HG23 H 1 .69 . . 1 . . . . . . . . 1162 1 251 . 1 1 41 41 ILE HD11 H 1 .6 . . 1 . . . . . . . . 1162 1 252 . 1 1 41 41 ILE HD12 H 1 .6 . . 1 . . . . . . . . 1162 1 253 . 1 1 41 41 ILE HD13 H 1 .6 . . 1 . . . . . . . . 1162 1 254 . 1 1 42 42 GLU H H 1 8.44 . . 1 . . . . . . . . 1162 1 255 . 1 1 42 42 GLU HA H 1 3.65 . . 1 . . . . . . . . 1162 1 256 . 1 1 42 42 GLU HB2 H 1 1.84 . . 2 . . . . . . . . 1162 1 257 . 1 1 42 42 GLU HB3 H 1 1.97 . . 2 . . . . . . . . 1162 1 258 . 1 1 42 42 GLU HG2 H 1 2.09 . . 2 . . . . . . . . 1162 1 259 . 1 1 42 42 GLU HG3 H 1 2.17 . . 2 . . . . . . . . 1162 1 260 . 1 1 43 43 THR H H 1 7.69 . . 1 . . . . . . . . 1162 1 261 . 1 1 43 43 THR HA H 1 3.67 . . 1 . . . . . . . . 1162 1 262 . 1 1 43 43 THR HB H 1 4.06 . . 1 . . . . . . . . 1162 1 263 . 1 1 43 43 THR HG1 H 1 4.68 . . 1 . . . . . . . . 1162 1 264 . 1 1 43 43 THR HG21 H 1 1.05 . . 1 . . . . . . . . 1162 1 265 . 1 1 43 43 THR HG22 H 1 1.05 . . 1 . . . . . . . . 1162 1 266 . 1 1 43 43 THR HG23 H 1 1.05 . . 1 . . . . . . . . 1162 1 267 . 1 1 44 44 LEU H H 1 7.62 . . 1 . . . . . . . . 1162 1 268 . 1 1 44 44 LEU HA H 1 3.87 . . 1 . . . . . . . . 1162 1 269 . 1 1 44 44 LEU HB2 H 1 1.49 . . 2 . . . . . . . . 1162 1 270 . 1 1 44 44 LEU HB3 H 1 1.55 . . 2 . . . . . . . . 1162 1 271 . 1 1 44 44 LEU HD11 H 1 .61 . . 2 . . . . . . . . 1162 1 272 . 1 1 44 44 LEU HD12 H 1 .61 . . 2 . . . . . . . . 1162 1 273 . 1 1 44 44 LEU HD13 H 1 .61 . . 2 . . . . . . . . 1162 1 274 . 1 1 44 44 LEU HD21 H 1 .69 . . 2 . . . . . . . . 1162 1 275 . 1 1 44 44 LEU HD22 H 1 .69 . . 2 . . . . . . . . 1162 1 276 . 1 1 44 44 LEU HD23 H 1 .69 . . 2 . . . . . . . . 1162 1 277 . 1 1 45 45 LEU H H 1 8.04 . . 1 . . . . . . . . 1162 1 278 . 1 1 45 45 LEU HA H 1 3.74 . . 1 . . . . . . . . 1162 1 279 . 1 1 45 45 LEU HB2 H 1 1.39 . . 2 . . . . . . . . 1162 1 280 . 1 1 45 45 LEU HB3 H 1 1.54 . . 2 . . . . . . . . 1162 1 281 . 1 1 45 45 LEU HD11 H 1 .63 . . 2 . . . . . . . . 1162 1 282 . 1 1 45 45 LEU HD12 H 1 .63 . . 2 . . . . . . . . 1162 1 283 . 1 1 45 45 LEU HD13 H 1 .63 . . 2 . . . . . . . . 1162 1 284 . 1 1 45 45 LEU HD21 H 1 .68 . . 2 . . . . . . . . 1162 1 285 . 1 1 45 45 LEU HD22 H 1 .68 . . 2 . . . . . . . . 1162 1 286 . 1 1 45 45 LEU HD23 H 1 .68 . . 2 . . . . . . . . 1162 1 287 . 1 1 46 46 PHE H H 1 8.03 . . 1 . . . . . . . . 1162 1 288 . 1 1 46 46 PHE HA H 1 3.86 . . 1 . . . . . . . . 1162 1 289 . 1 1 46 46 PHE HB2 H 1 2.95 . . 2 . . . . . . . . 1162 1 290 . 1 1 46 46 PHE HB3 H 1 3.03 . . 2 . . . . . . . . 1162 1 291 . 1 1 47 47 MET H H 1 8.05 . . 1 . . . . . . . . 1162 1 292 . 1 1 47 47 MET HA H 1 3.76 . . 1 . . . . . . . . 1162 1 293 . 1 1 47 47 MET HB2 H 1 2.16 . . 2 . . . . . . . . 1162 1 294 . 1 1 47 47 MET HB3 H 1 1.93 . . 2 . . . . . . . . 1162 1 295 . 1 1 47 47 MET HG2 H 1 2.68 . . 2 . . . . . . . . 1162 1 296 . 1 1 47 47 MET HG3 H 1 3.32 . . 2 . . . . . . . . 1162 1 297 . 1 1 48 48 VAL H H 1 8.08 . . 1 . . . . . . . . 1162 1 298 . 1 1 48 48 VAL HA H 1 3.33 . . 1 . . . . . . . . 1162 1 299 . 1 1 48 48 VAL HB H 1 2.02 . . 1 . . . . . . . . 1162 1 300 . 1 1 48 48 VAL HG11 H 1 .7 . . 2 . . . . . . . . 1162 1 301 . 1 1 48 48 VAL HG12 H 1 .7 . . 2 . . . . . . . . 1162 1 302 . 1 1 48 48 VAL HG13 H 1 .7 . . 2 . . . . . . . . 1162 1 303 . 1 1 48 48 VAL HG21 H 1 .86 . . 2 . . . . . . . . 1162 1 304 . 1 1 48 48 VAL HG22 H 1 .86 . . 2 . . . . . . . . 1162 1 305 . 1 1 48 48 VAL HG23 H 1 .86 . . 2 . . . . . . . . 1162 1 306 . 1 1 49 49 LEU H H 1 8.09 . . 1 . . . . . . . . 1162 1 307 . 1 1 49 49 LEU HA H 1 3.7 . . 1 . . . . . . . . 1162 1 308 . 1 1 49 49 LEU HB2 H 1 1.54 . . 2 . . . . . . . . 1162 1 309 . 1 1 49 49 LEU HB3 H 1 1.59 . . 2 . . . . . . . . 1162 1 310 . 1 1 49 49 LEU HD11 H 1 .53 . . 2 . . . . . . . . 1162 1 311 . 1 1 49 49 LEU HD12 H 1 .53 . . 2 . . . . . . . . 1162 1 312 . 1 1 49 49 LEU HD13 H 1 .53 . . 2 . . . . . . . . 1162 1 313 . 1 1 49 49 LEU HD21 H 1 .62 . . 2 . . . . . . . . 1162 1 314 . 1 1 49 49 LEU HD22 H 1 .62 . . 2 . . . . . . . . 1162 1 315 . 1 1 49 49 LEU HD23 H 1 .62 . . 2 . . . . . . . . 1162 1 316 . 1 1 50 50 ASP H H 1 8.23 . . 1 . . . . . . . . 1162 1 317 . 1 1 50 50 ASP HA H 1 4.03 . . 1 . . . . . . . . 1162 1 318 . 1 1 50 50 ASP HB2 H 1 2.12 . . 2 . . . . . . . . 1162 1 319 . 1 1 50 50 ASP HB3 H 1 2.41 . . 2 . . . . . . . . 1162 1 320 . 1 1 51 51 VAL H H 1 8.27 . . 1 . . . . . . . . 1162 1 321 . 1 1 51 51 VAL HA H 1 3.31 . . 1 . . . . . . . . 1162 1 322 . 1 1 51 51 VAL HB H 1 1.9 . . 1 . . . . . . . . 1162 1 323 . 1 1 51 51 VAL HG11 H 1 .72 . . 2 . . . . . . . . 1162 1 324 . 1 1 51 51 VAL HG12 H 1 .72 . . 2 . . . . . . . . 1162 1 325 . 1 1 51 51 VAL HG13 H 1 .72 . . 2 . . . . . . . . 1162 1 326 . 1 1 51 51 VAL HG21 H 1 .89 . . 2 . . . . . . . . 1162 1 327 . 1 1 51 51 VAL HG22 H 1 .89 . . 2 . . . . . . . . 1162 1 328 . 1 1 51 51 VAL HG23 H 1 .89 . . 2 . . . . . . . . 1162 1 329 . 1 1 52 52 SER H H 1 7.83 . . 1 . . . . . . . . 1162 1 330 . 1 1 52 52 SER HA H 1 3.84 . . 1 . . . . . . . . 1162 1 331 . 1 1 52 52 SER HB2 H 1 3.63 . . 2 . . . . . . . . 1162 1 332 . 1 1 52 52 SER HB3 H 1 3.7 . . 2 . . . . . . . . 1162 1 333 . 1 1 52 52 SER HG H 1 4.28 . . 1 . . . . . . . . 1162 1 334 . 1 1 53 53 ALA H H 1 8.19 . . 1 . . . . . . . . 1162 1 335 . 1 1 53 53 ALA HA H 1 3.85 . . 1 . . . . . . . . 1162 1 336 . 1 1 53 53 ALA HB1 H 1 1.28 . . 1 . . . . . . . . 1162 1 337 . 1 1 53 53 ALA HB2 H 1 1.28 . . 1 . . . . . . . . 1162 1 338 . 1 1 53 53 ALA HB3 H 1 1.28 . . 1 . . . . . . . . 1162 1 339 . 1 1 54 54 LYS H H 1 7.88 . . 1 . . . . . . . . 1162 1 340 . 1 1 54 54 LYS HA H 1 3.74 . . 1 . . . . . . . . 1162 1 341 . 1 1 54 54 LYS HB2 H 1 1.63 . . 2 . . . . . . . . 1162 1 342 . 1 1 54 54 LYS HB3 H 1 1.81 . . 2 . . . . . . . . 1162 1 343 . 1 1 54 54 LYS HG2 H 1 1.1 . . 2 . . . . . . . . 1162 1 344 . 1 1 54 54 LYS HG3 H 1 1.55 . . 2 . . . . . . . . 1162 1 345 . 1 1 54 54 LYS HD2 H 1 1.32 . . 1 . . . . . . . . 1162 1 346 . 1 1 54 54 LYS HD3 H 1 1.32 . . 1 . . . . . . . . 1162 1 347 . 1 1 54 54 LYS HE2 H 1 2.63 . . 1 . . . . . . . . 1162 1 348 . 1 1 54 54 LYS HE3 H 1 2.63 . . 1 . . . . . . . . 1162 1 349 . 1 1 55 55 VAL H H 1 8.53 . . 1 . . . . . . . . 1162 1 350 . 1 1 55 55 VAL HA H 1 3.46 . . 1 . . . . . . . . 1162 1 351 . 1 1 55 55 VAL HB H 1 1.93 . . 1 . . . . . . . . 1162 1 352 . 1 1 55 55 VAL HG11 H 1 .69 . . 2 . . . . . . . . 1162 1 353 . 1 1 55 55 VAL HG12 H 1 .69 . . 2 . . . . . . . . 1162 1 354 . 1 1 55 55 VAL HG13 H 1 .69 . . 2 . . . . . . . . 1162 1 355 . 1 1 55 55 VAL HG21 H 1 .84 . . 2 . . . . . . . . 1162 1 356 . 1 1 55 55 VAL HG22 H 1 .84 . . 2 . . . . . . . . 1162 1 357 . 1 1 55 55 VAL HG23 H 1 .84 . . 2 . . . . . . . . 1162 1 358 . 1 1 56 56 GLY H H 1 8.2 . . 1 . . . . . . . . 1162 1 359 . 1 1 56 56 GLY HA2 H 1 3.48 . . 2 . . . . . . . . 1162 1 360 . 1 1 56 56 GLY HA3 H 1 3.57 . . 2 . . . . . . . . 1162 1 361 . 1 1 57 57 PHE H H 1 8.33 . . 1 . . . . . . . . 1162 1 362 . 1 1 57 57 PHE HA H 1 4.08 . . 1 . . . . . . . . 1162 1 363 . 1 1 57 57 PHE HB2 H 1 2.95 . . 2 . . . . . . . . 1162 1 364 . 1 1 57 57 PHE HB3 H 1 3.04 . . 2 . . . . . . . . 1162 1 365 . 1 1 58 58 GLY H H 1 8.09 . . 1 . . . . . . . . 1162 1 366 . 1 1 58 58 GLY HA2 H 1 3.45 . . 2 . . . . . . . . 1162 1 367 . 1 1 58 58 GLY HA3 H 1 3.64 . . 2 . . . . . . . . 1162 1 368 . 1 1 59 59 LEU H H 1 8.1 . . 1 . . . . . . . . 1162 1 369 . 1 1 59 59 LEU HA H 1 3.7 . . 1 . . . . . . . . 1162 1 370 . 1 1 59 59 LEU HB2 H 1 1.56 . . 1 . . . . . . . . 1162 1 371 . 1 1 59 59 LEU HB3 H 1 1.56 . . 1 . . . . . . . . 1162 1 372 . 1 1 59 59 LEU HD11 H 1 .64 . . 1 . . . . . . . . 1162 1 373 . 1 1 59 59 LEU HD12 H 1 .64 . . 1 . . . . . . . . 1162 1 374 . 1 1 59 59 LEU HD13 H 1 .64 . . 1 . . . . . . . . 1162 1 375 . 1 1 59 59 LEU HD21 H 1 .64 . . 1 . . . . . . . . 1162 1 376 . 1 1 59 59 LEU HD22 H 1 .64 . . 1 . . . . . . . . 1162 1 377 . 1 1 59 59 LEU HD23 H 1 .64 . . 1 . . . . . . . . 1162 1 378 . 1 1 60 60 ILE H H 1 7.68 . . 1 . . . . . . . . 1162 1 379 . 1 1 60 60 ILE HA H 1 3.35 . . 1 . . . . . . . . 1162 1 380 . 1 1 60 60 ILE HB H 1 1.78 . . 1 . . . . . . . . 1162 1 381 . 1 1 60 60 ILE HG12 H 1 .8 . . 2 . . . . . . . . 1162 1 382 . 1 1 60 60 ILE HG13 H 1 1.52 . . 2 . . . . . . . . 1162 1 383 . 1 1 60 60 ILE HG21 H 1 .63 . . 1 . . . . . . . . 1162 1 384 . 1 1 60 60 ILE HG22 H 1 .63 . . 1 . . . . . . . . 1162 1 385 . 1 1 60 60 ILE HG23 H 1 .63 . . 1 . . . . . . . . 1162 1 386 . 1 1 61 61 LEU H H 1 8.01 . . 1 . . . . . . . . 1162 1 387 . 1 1 61 61 LEU HA H 1 3.65 . . 1 . . . . . . . . 1162 1 388 . 1 1 61 61 LEU HB2 H 1 1.28 . . 2 . . . . . . . . 1162 1 389 . 1 1 61 61 LEU HB3 H 1 1.52 . . 2 . . . . . . . . 1162 1 390 . 1 1 61 61 LEU HD11 H 1 .54 . . 2 . . . . . . . . 1162 1 391 . 1 1 61 61 LEU HD12 H 1 .54 . . 2 . . . . . . . . 1162 1 392 . 1 1 61 61 LEU HD13 H 1 .54 . . 2 . . . . . . . . 1162 1 393 . 1 1 61 61 LEU HD21 H 1 .64 . . 2 . . . . . . . . 1162 1 394 . 1 1 61 61 LEU HD22 H 1 .64 . . 2 . . . . . . . . 1162 1 395 . 1 1 61 61 LEU HD23 H 1 .64 . . 2 . . . . . . . . 1162 1 396 . 1 1 63 63 ARG H H 1 8.17 . . 1 . . . . . . . . 1162 1 397 . 1 1 63 63 ARG HA H 1 3.71 . . 1 . . . . . . . . 1162 1 398 . 1 1 63 63 ARG HB2 H 1 1.58 . . 2 . . . . . . . . 1162 1 399 . 1 1 63 63 ARG HB3 H 1 1.69 . . 2 . . . . . . . . 1162 1 400 . 1 1 63 63 ARG HG2 H 1 1.41 . . 2 . . . . . . . . 1162 1 401 . 1 1 63 63 ARG HG3 H 1 1.53 . . 2 . . . . . . . . 1162 1 402 . 1 1 63 63 ARG HD2 H 1 2.88 . . 2 . . . . . . . . 1162 1 403 . 1 1 63 63 ARG HD3 H 1 2.92 . . 2 . . . . . . . . 1162 1 404 . 1 1 63 63 ARG HE H 1 6.67 . . 1 . . . . . . . . 1162 1 405 . 1 1 64 64 SER H H 1 7.84 . . 1 . . . . . . . . 1162 1 406 . 1 1 64 64 SER HA H 1 3.89 . . 1 . . . . . . . . 1162 1 407 . 1 1 64 64 SER HB2 H 1 3.63 . . 1 . . . . . . . . 1162 1 408 . 1 1 64 64 SER HB3 H 1 3.63 . . 1 . . . . . . . . 1162 1 409 . 1 1 65 65 ARG H H 1 8.09 . . 1 . . . . . . . . 1162 1 410 . 1 1 65 65 ARG HA H 1 3.83 . . 1 . . . . . . . . 1162 1 411 . 1 1 65 65 ARG HB2 H 1 1.52 . . 2 . . . . . . . . 1162 1 412 . 1 1 65 65 ARG HB3 H 1 1.79 . . 2 . . . . . . . . 1162 1 413 . 1 1 65 65 ARG HG2 H 1 1.27 . . 2 . . . . . . . . 1162 1 414 . 1 1 65 65 ARG HG3 H 1 1.42 . . 2 . . . . . . . . 1162 1 415 . 1 1 65 65 ARG HD2 H 1 2.86 . . 2 . . . . . . . . 1162 1 416 . 1 1 65 65 ARG HD3 H 1 2.95 . . 2 . . . . . . . . 1162 1 417 . 1 1 65 65 ARG HE H 1 7.04 . . 1 . . . . . . . . 1162 1 418 . 1 1 66 66 ALA H H 1 7.69 . . 1 . . . . . . . . 1162 1 419 . 1 1 66 66 ALA HA H 1 3.88 . . 1 . . . . . . . . 1162 1 420 . 1 1 66 66 ALA HB1 H 1 1.25 . . 1 . . . . . . . . 1162 1 421 . 1 1 66 66 ALA HB2 H 1 1.25 . . 1 . . . . . . . . 1162 1 422 . 1 1 66 66 ALA HB3 H 1 1.25 . . 1 . . . . . . . . 1162 1 423 . 1 1 67 67 ILE H H 1 7.53 . . 1 . . . . . . . . 1162 1 424 . 1 1 67 67 ILE HA H 1 3.55 . . 1 . . . . . . . . 1162 1 425 . 1 1 67 67 ILE HB H 1 1.44 . . 1 . . . . . . . . 1162 1 426 . 1 1 67 67 ILE HG12 H 1 1.26 . . 1 . . . . . . . . 1162 1 427 . 1 1 67 67 ILE HG13 H 1 1.26 . . 1 . . . . . . . . 1162 1 428 . 1 1 67 67 ILE HG21 H 1 .24 . . 1 . . . . . . . . 1162 1 429 . 1 1 67 67 ILE HG22 H 1 .24 . . 1 . . . . . . . . 1162 1 430 . 1 1 67 67 ILE HG23 H 1 .24 . . 1 . . . . . . . . 1162 1 431 . 1 1 67 67 ILE HD11 H 1 .48 . . 1 . . . . . . . . 1162 1 432 . 1 1 67 67 ILE HD12 H 1 .48 . . 1 . . . . . . . . 1162 1 433 . 1 1 67 67 ILE HD13 H 1 .48 . . 1 . . . . . . . . 1162 1 434 . 1 1 68 68 PHE H H 1 7.68 . . 1 . . . . . . . . 1162 1 435 . 1 1 68 68 PHE HA H 1 4.28 . . 1 . . . . . . . . 1162 1 436 . 1 1 68 68 PHE HB2 H 1 2.72 . . 2 . . . . . . . . 1162 1 437 . 1 1 68 68 PHE HB3 H 1 3.03 . . 2 . . . . . . . . 1162 1 438 . 1 1 69 69 GLY H H 1 7.74 . . 1 . . . . . . . . 1162 1 439 . 1 1 69 69 GLY HA2 H 1 3.54 . . 2 . . . . . . . . 1162 1 440 . 1 1 69 69 GLY HA3 H 1 3.69 . . 2 . . . . . . . . 1162 1 stop_ save_