data_17361 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 17361 _Entry.Title ; The Conformation of Bacteriorhodopsin Loops in Purple Membranes resolved by Solid-state MAS-NMR ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2010-12-14 _Entry.Accession_date 2010-12-14 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype SOLID-STATE _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 Victoria Higman . A. . 17361 2 Krisztina Varga . . . 17361 3 Lubica Aslimovska . . . 17361 4 Peter Judge . J. . 17361 5 Lindsay Sperling . J. . 17361 6 Chad Rienstra . M. . 17361 7 Anthony Watts . . . 17361 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 17361 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 204 17361 '15N chemical shifts' 51 17361 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 3 . . 2013-01-28 2010-12-14 update BMRB 'update entry citation' 17361 2 . . 2012-03-12 2010-12-14 update BMRB 'update entry citation' 17361 1 . . 2011-08-03 2010-12-14 original author 'original release' 17361 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 17361 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 21770003 _Citation.Full_citation . _Citation.Title 'The conformation of bacteriorhodopsin loops in purple membranes resolved by solid-state MAS NMR spectroscopy.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Angew. Chem. Int. Ed. Engl.' _Citation.Journal_name_full 'Angewandte Chemie (International ed. in English)' _Citation.Journal_volume 50 _Citation.Journal_issue 36 _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 8432 _Citation.Page_last 8435 _Citation.Year 2011 _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 Victoria Higman . A. . 17361 1 2 Krisztina Varga . . . 17361 1 3 Lubica Aslimovska . . . 17361 1 4 Peter Judge . J. . 17361 1 5 Lindsay Sperling . J. . 17361 1 6 Chad Rienstra . M. . 17361 1 7 Anthony Watts . . . 17361 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 17361 _Assembly.ID 1 _Assembly.Name bR/PM _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds no _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details 'bacteriorhodopsin in purple membranes' _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 bR 1 $bR A . yes native no no . . . 17361 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_bR _Entity.Sf_category entity _Entity.Sf_framecode bR _Entity.Entry_ID 17361 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name bR _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 ; QAQITGRPEWIWLALGTALM GLGTLYFLVKGMGVSDPDAK KFYAITTLVPAIAFTMYLSM LLGYGLTMVPFGGEQNPIYW ARYADWLFTTPLLLLDLALL VDADQGTILALVGADGIMIG TGLVGALTKVYSYRFVWWAI STAAMLYILYVLFFGFTSKA ESMRPEVASTFKVLRNVTVV LWSAYPVVWLIGSEGAGIVP LNIETLLFMVLDVSAKVGFG LILLRSRAIFGEAEAPEPSA GDGAAATSD ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 249 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _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 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 1AP9 . "X-Ray Structure Of Bacteriorhodopsin From Microcrystals Grown In Lipidic Cubic Phases" . . . . . 99.60 248 100.00 100.00 1.43e-171 . . . . 17361 1 2 no PDB 1AT9 . "Structure Of Bacteriorhodopsin At 3.0 Angstrom Determined By Electron Crystallography" . . . . . 99.20 248 100.00 100.00 1.38e-170 . . . . 17361 1 3 no PDB 1BM1 . "Crystal Structure Of Bacteriorhodopsin In The Light-adapted State" . . . . . 99.20 248 100.00 100.00 1.38e-170 . . . . 17361 1 4 no PDB 1BRD . "Model For The Structure Of Bacteriorhodopsin Based On High-R Electron Cryo-Microscopy" . . . . . 99.20 248 100.00 100.00 1.38e-170 . . . . 17361 1 5 no PDB 1BRR . "X-Ray Structure Of The Bacteriorhodopsin TrimerLIPID COMPLEX" . . . . . 99.20 247 99.60 99.60 4.52e-168 . . . . 17361 1 6 no PDB 1BRX . "BacteriorhodopsinLIPID COMPLEX" . . . . . 99.20 248 100.00 100.00 1.38e-170 . . . . 17361 1 7 no PDB 1C3W . "BacteriorhodopsinLIPID COMPLEX AT 1.55 A RESOLUTION" . . . . . 91.16 222 97.80 97.80 8.85e-149 . . . . 17361 1 8 no PDB 1C8R . "Bacteriorhodopsin D96n Br State At 2.0 A Resolution" . . . . . 100.00 249 99.60 100.00 7.45e-172 . . . . 17361 1 9 no PDB 1CWQ . "M Intermediate Structure Of The Wild Type Bacteriorhodopsin In Combination With The Ground State Structure" . . . . . 99.60 248 99.60 99.60 4.71e-169 . . . . 17361 1 10 no PDB 1DZE . "Structure Of The M Intermediate Of Bacteriorhodopsin Trapped At 100k" . . . . . 99.60 248 100.00 100.00 1.43e-171 . . . . 17361 1 11 no PDB 1E0P . "L Intermediate Of Bacteriorhodopsin" . . . . . 91.57 228 100.00 100.00 4.11e-156 . . . . 17361 1 12 no PDB 1F4Z . "Bacteriorhodopsin-M Photointermediate State Of The E204q Mutant At 1.8 Angstrom Resolution" . . . . . 91.16 227 99.56 100.00 1.07e-154 . . . . 17361 1 13 no PDB 1F50 . "Bacteriorhodopsin-br State Of The E204q Mutant At 1.7 Angstrom Resolution" . . . . . 91.16 227 99.56 100.00 1.07e-154 . . . . 17361 1 14 no PDB 1FBB . "Crystal Structure Of Native Conformation Of Bacteriorhodopsin" . . . . . 99.60 248 100.00 100.00 1.43e-171 . . . . 17361 1 15 no PDB 1FBK . "Crystal Structure Of Cytoplasmically Open Conformation Of Bacteriorhodopsin" . . . . . 99.60 248 98.79 98.79 1.23e-168 . . . . 17361 1 16 no PDB 1IW6 . "Crystal Structure Of The Ground State Of Bacteriorhodopsin" . . . . . 99.60 248 100.00 100.00 1.43e-171 . . . . 17361 1 17 no PDB 1IW9 . "Crystal Structure Of The M Intermediate Of Bacteriorhodopsin" . . . . . 99.60 248 100.00 100.00 1.43e-171 . . . . 17361 1 18 no PDB 1IXF . "Crystal Structure Of The K Intermediate Of Bacteriorhodopsin" . . . . . 99.60 248 100.00 100.00 1.43e-171 . . . . 17361 1 19 no PDB 1JV6 . "Bacteriorhodopsin D85sF219L DOUBLE MUTANT AT 2.00 ANGSTROM Resolution" . . . . . 100.00 249 99.20 99.20 1.12e-170 . . . . 17361 1 20 no PDB 1JV7 . "Bacteriorhodopsin O-like Intermediate State Of The D85s Mutant At 2.25 Angstrom Resolution" . . . . . 100.00 249 99.60 99.60 1.45e-171 . . . . 17361 1 21 no PDB 1KG8 . "X-Ray Structure Of An Early-M Intermediate Of Bacteriorhodopsin" . . . . . 92.77 231 100.00 100.00 1.71e-158 . . . . 17361 1 22 no PDB 1KG9 . 'Structure Of A "mock-Trapped" Early-M Intermediate Of Bacteriorhosopsin' . . . . . 92.77 231 100.00 100.00 1.71e-158 . . . . 17361 1 23 no PDB 1KGB . "Structure Of Ground-State Bacteriorhodopsin" . . . . . 92.77 231 100.00 100.00 1.71e-158 . . . . 17361 1 24 no PDB 1KME . "Crystal Structure Of Bacteriorhodopsin Crystallized From Bicelles" . . . . . 92.77 231 100.00 100.00 1.71e-158 . . . . 17361 1 25 no PDB 1L0M . "Solution Structure Of Bacteriorhodopsin" . . . . . 85.14 212 100.00 100.00 2.91e-144 . . . . 17361 1 26 no PDB 1M0K . "Bacteriorhodopsin K Intermediate At 1.43 A Resolution" . . . . . 100.00 262 100.00 100.00 1.07e-172 . . . . 17361 1 27 no PDB 1M0L . "BacteriorhodopsinLIPID COMPLEX AT 1.47 A RESOLUTION" . . . . . 100.00 262 100.00 100.00 1.07e-172 . . . . 17361 1 28 no PDB 1M0M . "Bacteriorhodopsin M1 Intermediate At 1.43 A Resolution" . . . . . 100.00 262 100.00 100.00 1.07e-172 . . . . 17361 1 29 no PDB 1MGY . "Structure Of The D85s Mutant Of Bacteriorhodopsin With Bromide Bound" . . . . . 100.00 249 99.60 99.60 1.45e-171 . . . . 17361 1 30 no PDB 1O0A . "Bacteriorhodopsin L Intermediate At 1.62 A Resolution" . . . . . 100.00 249 100.00 100.00 1.61e-172 . . . . 17361 1 31 no PDB 1P8H . "Bacteriorhodopsin M1 Intermediate Produced At Room Temperature" . . . . . 100.00 249 100.00 100.00 1.61e-172 . . . . 17361 1 32 no PDB 1P8I . "F219l Bacteriorhodopsin Mutant" . . . . . 100.00 249 99.60 99.60 1.47e-171 . . . . 17361 1 33 no PDB 1P8U . "Bacteriorhodopsin N' Intermediate At 1.62 A Resolution" . . . . . 100.00 249 99.60 99.60 6.82e-172 . . . . 17361 1 34 no PDB 1PXR . "Structure Of Pro50ala Mutant Of Bacteriorhodopsin" . . . . . 100.00 249 99.60 99.60 1.71e-171 . . . . 17361 1 35 no PDB 1PXS . "Structure Of Met56ala Mutant Of Bacteriorhodopsin" . . . . . 100.00 249 99.60 99.60 1.55e-171 . . . . 17361 1 36 no PDB 1PY6 . "Bacteriorhodopsin Crystallized From Bicells" . . . . . 100.00 249 100.00 100.00 1.61e-172 . . . . 17361 1 37 no PDB 1Q5I . "Crystal Structure Of Bacteriorhodopsin Mutant P186a Crystallized From Bicelles" . . . . . 100.00 249 99.60 99.60 1.71e-171 . . . . 17361 1 38 no PDB 1Q5J . "Crystal Structure Of Bacteriorhodopsin Mutant P91a Crystallized From Bicelles" . . . . . 100.00 249 99.60 99.60 1.71e-171 . . . . 17361 1 39 no PDB 1QHJ . "X-Ray Structure Of Bacteriorhodopsin Grown In Lipidic Cubic Phases" . . . . . 99.60 248 100.00 100.00 1.43e-171 . . . . 17361 1 40 no PDB 1QKO . "High Resolution X-Ray Structure Of An Early Intermediate In The Bacteriorhodopsin Photocycle" . . . . . 99.60 248 100.00 100.00 1.43e-171 . . . . 17361 1 41 no PDB 1QKP . "High Resolution X-Ray Structure Of An Early Intermediate In The Bacteriorhodopsin Photocycle" . . . . . 99.60 248 100.00 100.00 1.43e-171 . . . . 17361 1 42 no PDB 1QM8 . "Structure Of Bacteriorhodopsin At 100 K" . . . . . 99.60 248 100.00 100.00 1.43e-171 . . . . 17361 1 43 no PDB 1R2N . "Nmr Structure Of The All-trans Retinal In Dark-adapted Bacteriorhodopsin" . . . . . 100.00 249 100.00 100.00 1.61e-172 . . . . 17361 1 44 no PDB 1R84 . "Nmr Structure Of The 13-cis-15-syn Retinal In Dark_adapted Bacteriorhodopsin" . . . . . 93.17 232 100.00 100.00 2.17e-159 . . . . 17361 1 45 no PDB 1S51 . "Thr24ser Bacteriorhodopsin" . . . . . 91.16 227 99.56 100.00 1.05e-154 . . . . 17361 1 46 no PDB 1S52 . "Thr24val Bacteriorhodopsin" . . . . . 91.16 227 99.56 99.56 2.37e-154 . . . . 17361 1 47 no PDB 1S53 . "Thr46ser Bacteriorhodopsin" . . . . . 91.16 227 99.56 100.00 1.05e-154 . . . . 17361 1 48 no PDB 1S54 . "Thr24ala Bacteriorhodopsin" . . . . . 91.16 227 99.56 99.56 2.24e-154 . . . . 17361 1 49 no PDB 1S8J . "Nitrate-Bound D85s Mutant Of Bacteriorhodopsin" . . . . . 100.00 249 99.60 99.60 1.45e-171 . . . . 17361 1 50 no PDB 1S8L . "Anion-Free Form Of The D85s Mutant Of Bacteriorhodopsin From Crystals Grown In The Presence Of Halide" . . . . . 100.00 249 99.60 99.60 1.45e-171 . . . . 17361 1 51 no PDB 1TN0 . "Structure Of Bacterorhodopsin Mutant A51p" . . . . . 100.00 249 99.60 99.60 1.26e-171 . . . . 17361 1 52 no PDB 1TN5 . "Structure Of Bacterorhodopsin Mutant K41p" . . . . . 100.00 249 99.60 99.60 2.48e-171 . . . . 17361 1 53 no PDB 1UCQ . "Crystal Structure Of The L Intermediate Of Bacteriorhodopsin" . . . . . 100.00 249 100.00 100.00 1.61e-172 . . . . 17361 1 54 no PDB 1VJM . "Deformation Of Helix C In The Low-Temperature L-Intermediate Of Bacteriorhodopsin" . . . . . 100.00 249 100.00 100.00 1.61e-172 . . . . 17361 1 55 no PDB 1X0I . "Crystal Structure Of The Acid Blue Form Of Bacteriorhodopsin" . . . . . 99.60 248 100.00 100.00 1.43e-171 . . . . 17361 1 56 no PDB 1X0K . "Crystal Structure Of Bacteriorhodopsin At Ph 10" . . . . . 99.60 248 100.00 100.00 1.43e-171 . . . . 17361 1 57 no PDB 1X0S . "Crystal Structure Of The 13-Cis Isomer Of Bacteriorhodopsin" . . . . . 99.60 248 100.00 100.00 1.43e-171 . . . . 17361 1 58 no PDB 1XJI . "Bacteriorhodopsin Crystallized In Bicelles At Room Temperature" . . . . . 99.20 247 100.00 100.00 1.33e-170 . . . . 17361 1 59 no PDB 2AT9 . "Structure Of Bacteriorhodopsin At 3.0 Angstrom By Electron Crystallography" . . . . . 99.20 248 100.00 100.00 1.38e-170 . . . . 17361 1 60 no PDB 2BRD . "Crystal Structure Of Bacteriorhodopsin In Purple Membrane" . . . . . 99.20 248 100.00 100.00 1.38e-170 . . . . 17361 1 61 no PDB 2I1X . "BacteriorhodopsinLIPID COMPLEX, D96A MUTANT" . . . . . 100.00 249 99.60 99.60 2.20e-171 . . . . 17361 1 62 no PDB 2I20 . "BacteriorhodopsinLIPID COMPLEX, M STATE OF D96A MUTANT" . . . . . 100.00 249 99.60 99.60 2.20e-171 . . . . 17361 1 63 no PDB 2I21 . "BacteriorhodopsinLIPID COMPLEX, T46V MUTANT" . . . . . 100.00 249 99.60 99.60 8.97e-172 . . . . 17361 1 64 no PDB 2NTU . "Bacteriorhodopsin, Wild Type, Before Illumination" . . . . . 100.00 249 100.00 100.00 1.61e-172 . . . . 17361 1 65 no PDB 2NTW . "Bacteriorhodopsin, Wild Type, After Illumination To Produce The L Intermediate" . . . . . 100.00 249 100.00 100.00 1.61e-172 . . . . 17361 1 66 no PDB 2WJK . "Bacteriorhodopsin Mutant E204d" . . . . . 100.00 249 99.60 100.00 8.77e-172 . . . . 17361 1 67 no PDB 2WJL . "Bacteriorhodopsin Mutant E194d" . . . . . 100.00 249 99.60 100.00 8.77e-172 . . . . 17361 1 68 no PDB 2ZFE . "Crystal Structure Of Bacteriorhodopsin-Xenon Complex" . . . . . 100.00 262 100.00 100.00 1.07e-172 . . . . 17361 1 69 no PDB 2ZZL . "Structure Of Bacteriorhodopsin's M Intermediate At Ph 7" . . . . . 100.00 262 100.00 100.00 1.07e-172 . . . . 17361 1 70 no PDB 3COC . "Crystal Structure Of D115a Mutant Of Bacteriorhodopsin" . . . . . 100.00 249 99.60 99.60 2.20e-171 . . . . 17361 1 71 no PDB 3COD . "Crystal Structure Of T90aD115A MUTANT OF BACTERIORHODOPSIN" . . . . . 100.00 249 99.20 99.20 1.09e-170 . . . . 17361 1 72 no PDB 3HAN . "Crystal Structure Of Bacteriorhodopsin Mutant V49a Crystallized From Bicelles" . . . . . 100.00 249 99.60 99.60 6.82e-172 . . . . 17361 1 73 no PDB 3HAO . "Crystal Structure Of Bacteriorhodopsin Mutant L94a Crystallized From Bicelles" . . . . . 100.00 249 99.60 99.60 6.75e-172 . . . . 17361 1 74 no PDB 3HAP . "Crystal Structure Of Bacteriorhodopsin Mutant L111a Crystallized From Bicelles" . . . . . 100.00 249 99.60 99.60 6.75e-172 . . . . 17361 1 75 no PDB 3HAQ . "Crystal Structure Of Bacteriorhodopsin Mutant I148a Crystallized From Bicelles" . . . . . 100.00 249 99.60 99.60 1.10e-171 . . . . 17361 1 76 no PDB 3HAR . "Crystal Structure Of Bacteriorhodopsin Mutant I148v Crystallized From Bicelles" . . . . . 100.00 249 99.60 100.00 2.78e-172 . . . . 17361 1 77 no PDB 3HAS . "Crystal Structure Of Bacteriorhodopsin Mutant L152a Crystallized From Bicelles" . . . . . 100.00 249 99.60 99.60 6.75e-172 . . . . 17361 1 78 no PDB 3MBV . "Structure Of Bacterirhodopsin Crystallized In Betta-Xyloc(16+4) Meso Phase" . . . . . 99.60 248 100.00 100.00 1.43e-171 . . . . 17361 1 79 no PDB 3NS0 . "X-Ray Structure Of Bacteriorhodopsin" . . . . . 99.60 248 100.00 100.00 1.43e-171 . . . . 17361 1 80 no PDB 3NSB . "Structure Of Bacteriorhodopsin Ground State Before And After X-Ray Modification" . . . . . 99.60 248 100.00 100.00 1.43e-171 . . . . 17361 1 81 no PDB 3T45 . "Crystal Structure Of Bacteriorhodopsin Mutant A215t, A Phototaxis Signaling Mutant At 3.0 A Resolution" . . . . . 90.36 225 99.56 99.56 4.46e-153 . . . . 17361 1 82 no PDB 3UTV . "Crystal Structure Of Bacteriorhodopsin Mutant Y57f" . . . . . 100.00 249 99.60 100.00 5.48e-172 . . . . 17361 1 83 no PDB 3UTW . "Crystal Structure Of Bacteriorhodopsin Mutant P50a/y57f" . . . . . 100.00 249 99.20 99.60 6.15e-171 . . . . 17361 1 84 no PDB 3UTX . "Crystal Structure Of Bacteriorhodopsin Mutant T46a" . . . . . 100.00 249 99.60 99.60 7.36e-172 . . . . 17361 1 85 no PDB 3UTY . "Crystal Structure Of Bacteriorhodopsin Mutant P50a/t46a" . . . . . 100.00 249 99.20 99.20 9.84e-171 . . . . 17361 1 86 no PDB 3VHZ . "Crystal Structure Of The Trans Isomer Of The L93a Mutant Of Bacteriorhodopsin" . . . . . 100.00 262 99.60 99.60 1.04e-171 . . . . 17361 1 87 no PDB 3VI0 . "Crystal Structure Of The O Intermediate Of The L93a Mutant Of Bacteriorhodopsin" . . . . . 100.00 262 99.60 99.60 1.04e-171 . . . . 17361 1 88 no PDB 4FPD . "Deprotonation Of D96 In Bacteriorhodopsin Opens The Proton Uptake Pathway" . . . . . 100.00 262 98.80 98.80 9.77e-170 . . . . 17361 1 89 no PDB 4HWL . "Crystal Structure Analysis Of The Bacteriorhodopsin In Facial Amphiphile-7 Dmpc Bicelle" . . . . . 100.00 262 100.00 100.00 1.07e-172 . . . . 17361 1 90 no PDB 4HYX . "Crystal Structure Analysis Of The Bacteriorhodopsin In Facial Amphiphile-4 Dmpc Bicelle" . . . . . 100.00 262 100.00 100.00 1.07e-172 . . . . 17361 1 91 no PDB 4MD1 . "Orange Species Of Bacteriorhodopsin From Halobacterium Salinarum" . . . . . 99.60 248 100.00 100.00 1.43e-171 . . . . 17361 1 92 no PDB 4MD2 . "Ground State Of Bacteriorhodopsin From Halobacterium Salinarum" . . . . . 99.60 248 100.00 100.00 1.43e-171 . . . . 17361 1 93 no PDB 4X31 . "Room Temperature Structure Of Bacteriorhodopsin From Lipidic Cubic Phase Obtained With Serial Millisecond Crystallography Using" . . . . . 91.97 229 100.00 100.00 9.52e-157 . . . . 17361 1 94 no PDB 4X32 . "Bacteriorhodopsin Ground State Structure Collected In Cryo Conditions From Crystals Obtained In Lcp With Peg As A Precipitant" . . . . . 91.57 228 100.00 100.00 4.11e-156 . . . . 17361 1 95 no PDB 4XXJ . "Crystal Structure Of Escherichia Coli-expressed Halobacterium Salinarum Bacteriorhodopsin In The Trimeric Form" . . . . . 100.00 269 99.60 99.60 4.31e-172 . . . . 17361 1 96 no PDB 5A44 . "Structure Of Bacteriorhodopsin Obtained From 20um Crystals By Multi Crystal Data Collection" . . . . . 99.60 248 100.00 100.00 1.43e-171 . . . . 17361 1 97 no PDB 5A45 . "Structure Of Bacteriorhodopsin Obtained From 5um Crystals By Multi Crystal Data Collection" . . . . . 99.60 248 100.00 100.00 1.43e-171 . . . . 17361 1 98 no EMBL CAA23744 . "unnamed protein product [Halobacterium salinarum]" . . . . . 100.00 262 100.00 100.00 1.07e-172 . . . . 17361 1 99 no EMBL CAA49762 . "bacterioopsin [synthetic construct]" . . . . . 100.00 259 99.60 100.00 2.37e-171 . . . . 17361 1 100 no EMBL CAA49774 . "bacterio-opsin [Halobacterium sp. GRB]" . . . . . 100.00 262 100.00 100.00 1.07e-172 . . . . 17361 1 101 no EMBL CAP14056 . "bacteriorhodopsin [Halobacterium salinarum R1]" . . . . . 100.00 262 100.00 100.00 1.07e-172 . . . . 17361 1 102 no GB AAA72184 . "bacteriorhodopsin [synthetic construct]" . . . . . 99.60 249 100.00 100.00 1.48e-171 . . . . 17361 1 103 no GB AAA72504 . "bacteriorhodopsin [Halobacterium salinarum]" . . . . . 100.00 262 100.00 100.00 1.07e-172 . . . . 17361 1 104 no GB AAA72603 . "bacteriorhodopsin [synthetic construct]" . . . . . 99.60 249 100.00 100.00 1.48e-171 . . . . 17361 1 105 no GB AAG19772 . "bacteriorhodopsin [Halobacterium sp. NRC-1]" . . . . . 100.00 262 100.00 100.00 1.07e-172 . . . . 17361 1 106 no PRF 0501217A . bacteriorhodopsin . . . . . 99.60 247 97.18 98.79 7.04e-165 . . . . 17361 1 107 no PRF 0712242A . "bacteriorhodopsin precursor" . . . . . 100.00 262 99.60 99.60 2.03e-171 . . . . 17361 1 108 no REF WP_049892510 . "rhodopsin [Halobacterium salinarum]" . . . . . 92.37 230 100.00 100.00 1.26e-157 . . . . 17361 1 109 no SP P02945 . "RecName: Full=Bacteriorhodopsin; Short=BR; AltName: Full=Bacterioopsin; Short=BO; Flags: Precursor" . . . . . 100.00 262 100.00 100.00 1.07e-172 . . . . 17361 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 . GLN . 17361 1 2 . ALA . 17361 1 3 . GLN . 17361 1 4 . ILE . 17361 1 5 . THR . 17361 1 6 . GLY . 17361 1 7 . ARG . 17361 1 8 . PRO . 17361 1 9 . GLU . 17361 1 10 . TRP . 17361 1 11 . ILE . 17361 1 12 . TRP . 17361 1 13 . LEU . 17361 1 14 . ALA . 17361 1 15 . LEU . 17361 1 16 . GLY . 17361 1 17 . THR . 17361 1 18 . ALA . 17361 1 19 . LEU . 17361 1 20 . MET . 17361 1 21 . GLY . 17361 1 22 . LEU . 17361 1 23 . GLY . 17361 1 24 . THR . 17361 1 25 . LEU . 17361 1 26 . TYR . 17361 1 27 . PHE . 17361 1 28 . LEU . 17361 1 29 . VAL . 17361 1 30 . LYS . 17361 1 31 . GLY . 17361 1 32 . MET . 17361 1 33 . GLY . 17361 1 34 . VAL . 17361 1 35 . SER . 17361 1 36 . ASP . 17361 1 37 . PRO . 17361 1 38 . ASP . 17361 1 39 . ALA . 17361 1 40 . LYS . 17361 1 41 . LYS . 17361 1 42 . PHE . 17361 1 43 . TYR . 17361 1 44 . ALA . 17361 1 45 . ILE . 17361 1 46 . THR . 17361 1 47 . THR . 17361 1 48 . LEU . 17361 1 49 . VAL . 17361 1 50 . PRO . 17361 1 51 . ALA . 17361 1 52 . ILE . 17361 1 53 . ALA . 17361 1 54 . PHE . 17361 1 55 . THR . 17361 1 56 . MET . 17361 1 57 . TYR . 17361 1 58 . LEU . 17361 1 59 . SER . 17361 1 60 . MET . 17361 1 61 . LEU . 17361 1 62 . LEU . 17361 1 63 . GLY . 17361 1 64 . TYR . 17361 1 65 . GLY . 17361 1 66 . LEU . 17361 1 67 . THR . 17361 1 68 . MET . 17361 1 69 . VAL . 17361 1 70 . PRO . 17361 1 71 . PHE . 17361 1 72 . GLY . 17361 1 73 . GLY . 17361 1 74 . GLU . 17361 1 75 . GLN . 17361 1 76 . ASN . 17361 1 77 . PRO . 17361 1 78 . ILE . 17361 1 79 . TYR . 17361 1 80 . TRP . 17361 1 81 . ALA . 17361 1 82 . ARG . 17361 1 83 . TYR . 17361 1 84 . ALA . 17361 1 85 . ASP . 17361 1 86 . TRP . 17361 1 87 . LEU . 17361 1 88 . PHE . 17361 1 89 . THR . 17361 1 90 . THR . 17361 1 91 . PRO . 17361 1 92 . LEU . 17361 1 93 . LEU . 17361 1 94 . LEU . 17361 1 95 . LEU . 17361 1 96 . ASP . 17361 1 97 . LEU . 17361 1 98 . ALA . 17361 1 99 . LEU . 17361 1 100 . LEU . 17361 1 101 . VAL . 17361 1 102 . ASP . 17361 1 103 . ALA . 17361 1 104 . ASP . 17361 1 105 . GLN . 17361 1 106 . GLY . 17361 1 107 . THR . 17361 1 108 . ILE . 17361 1 109 . LEU . 17361 1 110 . ALA . 17361 1 111 . LEU . 17361 1 112 . VAL . 17361 1 113 . GLY . 17361 1 114 . ALA . 17361 1 115 . ASP . 17361 1 116 . GLY . 17361 1 117 . ILE . 17361 1 118 . MET . 17361 1 119 . ILE . 17361 1 120 . GLY . 17361 1 121 . THR . 17361 1 122 . GLY . 17361 1 123 . LEU . 17361 1 124 . VAL . 17361 1 125 . GLY . 17361 1 126 . ALA . 17361 1 127 . LEU . 17361 1 128 . THR . 17361 1 129 . LYS . 17361 1 130 . VAL . 17361 1 131 . TYR . 17361 1 132 . SER . 17361 1 133 . TYR . 17361 1 134 . ARG . 17361 1 135 . PHE . 17361 1 136 . VAL . 17361 1 137 . TRP . 17361 1 138 . TRP . 17361 1 139 . ALA . 17361 1 140 . ILE . 17361 1 141 . SER . 17361 1 142 . THR . 17361 1 143 . ALA . 17361 1 144 . ALA . 17361 1 145 . MET . 17361 1 146 . LEU . 17361 1 147 . TYR . 17361 1 148 . ILE . 17361 1 149 . LEU . 17361 1 150 . TYR . 17361 1 151 . VAL . 17361 1 152 . LEU . 17361 1 153 . PHE . 17361 1 154 . PHE . 17361 1 155 . GLY . 17361 1 156 . PHE . 17361 1 157 . THR . 17361 1 158 . SER . 17361 1 159 . LYS . 17361 1 160 . ALA . 17361 1 161 . GLU . 17361 1 162 . SER . 17361 1 163 . MET . 17361 1 164 . ARG . 17361 1 165 . PRO . 17361 1 166 . GLU . 17361 1 167 . VAL . 17361 1 168 . ALA . 17361 1 169 . SER . 17361 1 170 . THR . 17361 1 171 . PHE . 17361 1 172 . LYS . 17361 1 173 . VAL . 17361 1 174 . LEU . 17361 1 175 . ARG . 17361 1 176 . ASN . 17361 1 177 . VAL . 17361 1 178 . THR . 17361 1 179 . VAL . 17361 1 180 . VAL . 17361 1 181 . LEU . 17361 1 182 . TRP . 17361 1 183 . SER . 17361 1 184 . ALA . 17361 1 185 . TYR . 17361 1 186 . PRO . 17361 1 187 . VAL . 17361 1 188 . VAL . 17361 1 189 . TRP . 17361 1 190 . LEU . 17361 1 191 . ILE . 17361 1 192 . GLY . 17361 1 193 . SER . 17361 1 194 . GLU . 17361 1 195 . GLY . 17361 1 196 . ALA . 17361 1 197 . GLY . 17361 1 198 . ILE . 17361 1 199 . VAL . 17361 1 200 . PRO . 17361 1 201 . LEU . 17361 1 202 . ASN . 17361 1 203 . ILE . 17361 1 204 . GLU . 17361 1 205 . THR . 17361 1 206 . LEU . 17361 1 207 . LEU . 17361 1 208 . PHE . 17361 1 209 . MET . 17361 1 210 . VAL . 17361 1 211 . LEU . 17361 1 212 . ASP . 17361 1 213 . VAL . 17361 1 214 . SER . 17361 1 215 . ALA . 17361 1 216 . LYS . 17361 1 217 . VAL . 17361 1 218 . GLY . 17361 1 219 . PHE . 17361 1 220 . GLY . 17361 1 221 . LEU . 17361 1 222 . ILE . 17361 1 223 . LEU . 17361 1 224 . LEU . 17361 1 225 . ARG . 17361 1 226 . SER . 17361 1 227 . ARG . 17361 1 228 . ALA . 17361 1 229 . ILE . 17361 1 230 . PHE . 17361 1 231 . GLY . 17361 1 232 . GLU . 17361 1 233 . ALA . 17361 1 234 . GLU . 17361 1 235 . ALA . 17361 1 236 . PRO . 17361 1 237 . GLU . 17361 1 238 . PRO . 17361 1 239 . SER . 17361 1 240 . ALA . 17361 1 241 . GLY . 17361 1 242 . ASP . 17361 1 243 . GLY . 17361 1 244 . ALA . 17361 1 245 . ALA . 17361 1 246 . ALA . 17361 1 247 . THR . 17361 1 248 . SER . 17361 1 249 . ASP . 17361 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 . GLN 1 1 17361 1 . ALA 2 2 17361 1 . GLN 3 3 17361 1 . ILE 4 4 17361 1 . THR 5 5 17361 1 . GLY 6 6 17361 1 . ARG 7 7 17361 1 . PRO 8 8 17361 1 . GLU 9 9 17361 1 . TRP 10 10 17361 1 . ILE 11 11 17361 1 . TRP 12 12 17361 1 . LEU 13 13 17361 1 . ALA 14 14 17361 1 . LEU 15 15 17361 1 . GLY 16 16 17361 1 . THR 17 17 17361 1 . ALA 18 18 17361 1 . LEU 19 19 17361 1 . MET 20 20 17361 1 . GLY 21 21 17361 1 . LEU 22 22 17361 1 . GLY 23 23 17361 1 . THR 24 24 17361 1 . LEU 25 25 17361 1 . TYR 26 26 17361 1 . PHE 27 27 17361 1 . LEU 28 28 17361 1 . VAL 29 29 17361 1 . LYS 30 30 17361 1 . GLY 31 31 17361 1 . MET 32 32 17361 1 . GLY 33 33 17361 1 . VAL 34 34 17361 1 . SER 35 35 17361 1 . ASP 36 36 17361 1 . PRO 37 37 17361 1 . ASP 38 38 17361 1 . ALA 39 39 17361 1 . LYS 40 40 17361 1 . LYS 41 41 17361 1 . PHE 42 42 17361 1 . TYR 43 43 17361 1 . ALA 44 44 17361 1 . ILE 45 45 17361 1 . THR 46 46 17361 1 . THR 47 47 17361 1 . LEU 48 48 17361 1 . VAL 49 49 17361 1 . PRO 50 50 17361 1 . ALA 51 51 17361 1 . ILE 52 52 17361 1 . ALA 53 53 17361 1 . PHE 54 54 17361 1 . THR 55 55 17361 1 . MET 56 56 17361 1 . TYR 57 57 17361 1 . LEU 58 58 17361 1 . SER 59 59 17361 1 . MET 60 60 17361 1 . LEU 61 61 17361 1 . LEU 62 62 17361 1 . GLY 63 63 17361 1 . TYR 64 64 17361 1 . GLY 65 65 17361 1 . LEU 66 66 17361 1 . THR 67 67 17361 1 . MET 68 68 17361 1 . VAL 69 69 17361 1 . PRO 70 70 17361 1 . PHE 71 71 17361 1 . GLY 72 72 17361 1 . GLY 73 73 17361 1 . GLU 74 74 17361 1 . GLN 75 75 17361 1 . ASN 76 76 17361 1 . PRO 77 77 17361 1 . ILE 78 78 17361 1 . TYR 79 79 17361 1 . TRP 80 80 17361 1 . ALA 81 81 17361 1 . ARG 82 82 17361 1 . TYR 83 83 17361 1 . ALA 84 84 17361 1 . ASP 85 85 17361 1 . TRP 86 86 17361 1 . LEU 87 87 17361 1 . PHE 88 88 17361 1 . THR 89 89 17361 1 . THR 90 90 17361 1 . PRO 91 91 17361 1 . LEU 92 92 17361 1 . LEU 93 93 17361 1 . LEU 94 94 17361 1 . LEU 95 95 17361 1 . ASP 96 96 17361 1 . LEU 97 97 17361 1 . ALA 98 98 17361 1 . LEU 99 99 17361 1 . LEU 100 100 17361 1 . VAL 101 101 17361 1 . ASP 102 102 17361 1 . ALA 103 103 17361 1 . ASP 104 104 17361 1 . GLN 105 105 17361 1 . GLY 106 106 17361 1 . THR 107 107 17361 1 . ILE 108 108 17361 1 . LEU 109 109 17361 1 . ALA 110 110 17361 1 . LEU 111 111 17361 1 . VAL 112 112 17361 1 . GLY 113 113 17361 1 . ALA 114 114 17361 1 . ASP 115 115 17361 1 . GLY 116 116 17361 1 . ILE 117 117 17361 1 . MET 118 118 17361 1 . ILE 119 119 17361 1 . GLY 120 120 17361 1 . THR 121 121 17361 1 . GLY 122 122 17361 1 . LEU 123 123 17361 1 . VAL 124 124 17361 1 . GLY 125 125 17361 1 . ALA 126 126 17361 1 . LEU 127 127 17361 1 . THR 128 128 17361 1 . LYS 129 129 17361 1 . VAL 130 130 17361 1 . TYR 131 131 17361 1 . SER 132 132 17361 1 . TYR 133 133 17361 1 . ARG 134 134 17361 1 . PHE 135 135 17361 1 . VAL 136 136 17361 1 . TRP 137 137 17361 1 . TRP 138 138 17361 1 . ALA 139 139 17361 1 . ILE 140 140 17361 1 . SER 141 141 17361 1 . THR 142 142 17361 1 . ALA 143 143 17361 1 . ALA 144 144 17361 1 . MET 145 145 17361 1 . LEU 146 146 17361 1 . TYR 147 147 17361 1 . ILE 148 148 17361 1 . LEU 149 149 17361 1 . TYR 150 150 17361 1 . VAL 151 151 17361 1 . LEU 152 152 17361 1 . PHE 153 153 17361 1 . PHE 154 154 17361 1 . GLY 155 155 17361 1 . PHE 156 156 17361 1 . THR 157 157 17361 1 . SER 158 158 17361 1 . LYS 159 159 17361 1 . ALA 160 160 17361 1 . GLU 161 161 17361 1 . SER 162 162 17361 1 . MET 163 163 17361 1 . ARG 164 164 17361 1 . PRO 165 165 17361 1 . GLU 166 166 17361 1 . VAL 167 167 17361 1 . ALA 168 168 17361 1 . SER 169 169 17361 1 . THR 170 170 17361 1 . PHE 171 171 17361 1 . LYS 172 172 17361 1 . VAL 173 173 17361 1 . LEU 174 174 17361 1 . ARG 175 175 17361 1 . ASN 176 176 17361 1 . VAL 177 177 17361 1 . THR 178 178 17361 1 . VAL 179 179 17361 1 . VAL 180 180 17361 1 . LEU 181 181 17361 1 . TRP 182 182 17361 1 . SER 183 183 17361 1 . ALA 184 184 17361 1 . TYR 185 185 17361 1 . PRO 186 186 17361 1 . VAL 187 187 17361 1 . VAL 188 188 17361 1 . TRP 189 189 17361 1 . LEU 190 190 17361 1 . ILE 191 191 17361 1 . GLY 192 192 17361 1 . SER 193 193 17361 1 . GLU 194 194 17361 1 . GLY 195 195 17361 1 . ALA 196 196 17361 1 . GLY 197 197 17361 1 . ILE 198 198 17361 1 . VAL 199 199 17361 1 . PRO 200 200 17361 1 . LEU 201 201 17361 1 . ASN 202 202 17361 1 . ILE 203 203 17361 1 . GLU 204 204 17361 1 . THR 205 205 17361 1 . LEU 206 206 17361 1 . LEU 207 207 17361 1 . PHE 208 208 17361 1 . MET 209 209 17361 1 . VAL 210 210 17361 1 . LEU 211 211 17361 1 . ASP 212 212 17361 1 . VAL 213 213 17361 1 . SER 214 214 17361 1 . ALA 215 215 17361 1 . LYS 216 216 17361 1 . VAL 217 217 17361 1 . GLY 218 218 17361 1 . PHE 219 219 17361 1 . GLY 220 220 17361 1 . LEU 221 221 17361 1 . ILE 222 222 17361 1 . LEU 223 223 17361 1 . LEU 224 224 17361 1 . ARG 225 225 17361 1 . SER 226 226 17361 1 . ARG 227 227 17361 1 . ALA 228 228 17361 1 . ILE 229 229 17361 1 . PHE 230 230 17361 1 . GLY 231 231 17361 1 . GLU 232 232 17361 1 . ALA 233 233 17361 1 . GLU 234 234 17361 1 . ALA 235 235 17361 1 . PRO 236 236 17361 1 . GLU 237 237 17361 1 . PRO 238 238 17361 1 . SER 239 239 17361 1 . ALA 240 240 17361 1 . GLY 241 241 17361 1 . ASP 242 242 17361 1 . GLY 243 243 17361 1 . ALA 244 244 17361 1 . ALA 245 245 17361 1 . ALA 246 246 17361 1 . THR 247 247 17361 1 . SER 248 248 17361 1 . ASP 249 249 17361 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 17361 _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 $bR . 2242 organism . 'Halobacterium salinarum' 'Halobacterium salinarum' . . Archaea . Halobacterium salinarum . . . . . . . . . . . . . . . . . . . . . 17361 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 17361 _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 $bR . 'purified from the natural source' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 17361 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 17361 _Sample.ID 1 _Sample.Type membrane _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '95% H2O/5% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 bR '[U-100% 13C; U-100% 15N]' . . 1 $bR . . 18 . . mg . . . . 17361 1 2 'sodium citrate' 'natural abundance' . . . . . . 20 . . mM . . . . 17361 1 3 'sodium azide' 'natural abundance' . . . . . . 0.01 . . % . . . . 17361 1 4 H2O 'natural abundance' . . . . . . 95 . . % . . . . 17361 1 5 D2O 'natural abundance' . . . . . . 5 . . % . . . . 17361 1 6 'purple membrane lipids' '[U-100% 13C; U-100% 15N]' . . . . . . 6 . . mg . . . . 17361 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 17361 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.2 . mM 17361 1 pH 6.0 . pH 17361 1 pressure 1 . atm 17361 1 temperature 278 5 K 17361 1 stop_ save_ save_sample_conditions_2 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_2 _Sample_condition_list.Entry_ID 17361 _Sample_condition_list.ID 2 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.2 . mM 17361 2 pH 6.0 . pH 17361 2 pressure 1 . atm 17361 2 temperature 263 5 K 17361 2 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 17361 _Software.ID 1 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 17361 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 17361 1 stop_ save_ save_Analysis _Software.Sf_category software _Software.Sf_framecode Analysis _Software.Entry_ID 17361 _Software.ID 2 _Software.Name Analysis _Software.Version 2.1.15 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID CCPN . . 17361 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 17361 2 'peak picking' 17361 2 stop_ save_ save_Spinsight _Software.Sf_category software _Software.Sf_framecode Spinsight _Software.Entry_ID 17361 _Software.ID 3 _Software.Name Spinsight _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Chemagnetics/Varian . . 17361 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 17361 3 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 17361 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model 'Infinity Plus' _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 17361 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model 'Infinity Plus' _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 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 17361 _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 Varian 'Infinity Plus' . 800 . . . 17361 1 2 spectrometer_2 Varian 'Infinity Plus' . 500 . . . 17361 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 17361 _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 DARR no . . . . . . . . . . 1 $sample_1 solid . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17361 1 2 NCACX no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17361 1 3 NCOCX no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 17361 1 4 CANCO no . . . . . . . . . . 1 $sample_1 isotropic . . 2 $sample_conditions_2 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 17361 1 5 CANCOCX no . . . . . . . . . . 1 $sample_1 isotropic . . 2 $sample_conditions_2 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 17361 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 17361 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 adamantane 'methylene carbons' . . . . ppm 40.48 external direct 1.0 . . . 1 $entry_citation . . 1 $entry_citation 17361 1 N 15 adamantane 'methylene carbons' . . . . ppm 40.48 external indirect 0.402979946 . . . 1 $entry_citation . . 1 $entry_citation 17361 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 17361 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 DARR . . . 17361 1 2 NCACX . . . 17361 1 3 NCOCX . . . 17361 1 4 CANCO . . . 17361 1 5 CANCOCX . . . 17361 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 19 19 LEU C C 13 179.667 0.029 . 1 . . . . 19 LEU C . 17361 1 2 . 1 1 19 19 LEU CA C 13 58.510 0.000 . 1 . . . . 19 LEU CA . 17361 1 3 . 1 1 19 19 LEU CB C 13 42.084 0.014 . 1 . . . . 19 LEU CB . 17361 1 4 . 1 1 19 19 LEU CG C 13 27.379 0.000 . 1 . . . . 19 LEU CG . 17361 1 5 . 1 1 19 19 LEU CD1 C 13 22.755 0.000 . 2 . . . . 19 LEU CD1 . 17361 1 6 . 1 1 19 19 LEU CD2 C 13 26.430 0.000 . 2 . . . . 19 LEU CD2 . 17361 1 7 . 1 1 20 20 MET C C 13 180.804 0.059 . 1 . . . . 20 MET C . 17361 1 8 . 1 1 20 20 MET CA C 13 57.400 0.138 . 1 . . . . 20 MET CA . 17361 1 9 . 1 1 20 20 MET CB C 13 34.211 0.054 . 1 . . . . 20 MET CB . 17361 1 10 . 1 1 20 20 MET CG C 13 30.656 0.083 . 1 . . . . 20 MET CG . 17361 1 11 . 1 1 20 20 MET N N 15 115.577 0.101 . 1 . . . . 20 MET N . 17361 1 12 . 1 1 21 21 GLY C C 13 173.946 0.000 . 1 . . . . 21 GLY C . 17361 1 13 . 1 1 21 21 GLY CA C 13 47.925 0.044 . 1 . . . . 21 GLY CA . 17361 1 14 . 1 1 21 21 GLY N N 15 109.977 0.138 . 1 . . . . 21 GLY N . 17361 1 15 . 1 1 34 34 VAL C C 13 175.438 0.047 . 1 . . . . 34 VAL C . 17361 1 16 . 1 1 34 34 VAL CA C 13 63.121 0.036 . 1 . . . . 34 VAL CA . 17361 1 17 . 1 1 34 34 VAL CB C 13 32.176 0.081 . 1 . . . . 34 VAL CB . 17361 1 18 . 1 1 34 34 VAL CG1 C 13 21.796 0.023 . 2 . . . . 34 VAL CG1 . 17361 1 19 . 1 1 34 34 VAL CG2 C 13 22.018 0.000 . 2 . . . . 34 VAL CG2 . 17361 1 20 . 1 1 34 34 VAL N N 15 122.009 0.034 . 1 . . . . 34 VAL N . 17361 1 21 . 1 1 35 35 SER C C 13 174.813 0.063 . 1 . . . . 35 SER C . 17361 1 22 . 1 1 35 35 SER CA C 13 57.936 0.025 . 1 . . . . 35 SER CA . 17361 1 23 . 1 1 35 35 SER CB C 13 64.901 0.032 . 1 . . . . 35 SER CB . 17361 1 24 . 1 1 35 35 SER N N 15 120.905 0.147 . 1 . . . . 35 SER N . 17361 1 25 . 1 1 36 36 ASP C C 13 174.789 0.200 . 1 . . . . 36 ASP C . 17361 1 26 . 1 1 36 36 ASP CA C 13 52.546 0.068 . 1 . . . . 36 ASP CA . 17361 1 27 . 1 1 36 36 ASP CB C 13 43.577 0.082 . 1 . . . . 36 ASP CB . 17361 1 28 . 1 1 36 36 ASP CG C 13 179.410 0.017 . 1 . . . . 36 ASP CG . 17361 1 29 . 1 1 36 36 ASP N N 15 126.512 0.085 . 1 . . . . 36 ASP N . 17361 1 30 . 1 1 37 37 PRO C C 13 179.593 0.098 . 1 . . . . 37 PRO C . 17361 1 31 . 1 1 37 37 PRO CA C 13 65.393 0.081 . 1 . . . . 37 PRO CA . 17361 1 32 . 1 1 37 37 PRO CB C 13 32.285 0.052 . 1 . . . . 37 PRO CB . 17361 1 33 . 1 1 37 37 PRO CG C 13 27.795 0.039 . 1 . . . . 37 PRO CG . 17361 1 34 . 1 1 37 37 PRO CD C 13 51.219 0.026 . 1 . . . . 37 PRO CD . 17361 1 35 . 1 1 37 37 PRO N N 15 139.092 0.196 . 1 . . . . 37 PRO N . 17361 1 36 . 1 1 67 67 THR C C 13 176.629 0.101 . 1 . . . . 67 THR C . 17361 1 37 . 1 1 67 67 THR CA C 13 66.113 0.058 . 1 . . . . 67 THR CA . 17361 1 38 . 1 1 67 67 THR CB C 13 68.444 0.028 . 1 . . . . 67 THR CB . 17361 1 39 . 1 1 67 67 THR CG2 C 13 23.516 0.026 . 1 . . . . 67 THR CG2 . 17361 1 40 . 1 1 67 67 THR N N 15 110.547 0.027 . 1 . . . . 67 THR N . 17361 1 41 . 1 1 68 68 MET C C 13 176.675 0.139 . 1 . . . . 68 MET C . 17361 1 42 . 1 1 68 68 MET CA C 13 52.738 0.039 . 1 . . . . 68 MET CA . 17361 1 43 . 1 1 68 68 MET CB C 13 33.124 0.036 . 1 . . . . 68 MET CB . 17361 1 44 . 1 1 68 68 MET CG C 13 32.348 0.044 . 1 . . . . 68 MET CG . 17361 1 45 . 1 1 68 68 MET CE C 13 17.375 0.005 . 1 . . . . 68 MET CE . 17361 1 46 . 1 1 68 68 MET N N 15 121.788 0.196 . 1 . . . . 68 MET N . 17361 1 47 . 1 1 69 69 VAL C C 13 174.691 0.034 . 1 . . . . 69 VAL C . 17361 1 48 . 1 1 69 69 VAL CA C 13 58.713 0.062 . 1 . . . . 69 VAL CA . 17361 1 49 . 1 1 69 69 VAL CB C 13 35.985 0.005 . 1 . . . . 69 VAL CB . 17361 1 50 . 1 1 69 69 VAL CG1 C 13 22.693 0.050 . 2 . . . . 69 VAL CG1 . 17361 1 51 . 1 1 69 69 VAL CG2 C 13 21.062 0.025 . 2 . . . . 69 VAL CG2 . 17361 1 52 . 1 1 69 69 VAL N N 15 126.001 0.095 . 1 . . . . 69 VAL N . 17361 1 53 . 1 1 70 70 PRO C C 13 176.885 0.076 . 1 . . . . 70 PRO C . 17361 1 54 . 1 1 70 70 PRO CA C 13 61.666 0.041 . 1 . . . . 70 PRO CA . 17361 1 55 . 1 1 70 70 PRO CB C 13 31.471 0.052 . 1 . . . . 70 PRO CB . 17361 1 56 . 1 1 70 70 PRO CG C 13 27.138 0.041 . 1 . . . . 70 PRO CG . 17361 1 57 . 1 1 70 70 PRO CD C 13 51.303 0.078 . 1 . . . . 70 PRO CD . 17361 1 58 . 1 1 70 70 PRO N N 15 143.503 0.104 . 1 . . . . 70 PRO N . 17361 1 59 . 1 1 71 71 PHE C C 13 177.574 0.133 . 1 . . . . 71 PHE C . 17361 1 60 . 1 1 71 71 PHE CA C 13 58.928 0.078 . 1 . . . . 71 PHE CA . 17361 1 61 . 1 1 71 71 PHE CB C 13 40.305 0.045 . 1 . . . . 71 PHE CB . 17361 1 62 . 1 1 71 71 PHE N N 15 114.767 0.127 . 1 . . . . 71 PHE N . 17361 1 63 . 1 1 72 72 GLY C C 13 175.199 0.097 . 1 . . . . 72 GLY C . 17361 1 64 . 1 1 72 72 GLY CA C 13 46.464 0.128 . 1 . . . . 72 GLY CA . 17361 1 65 . 1 1 72 72 GLY N N 15 110.164 0.185 . 1 . . . . 72 GLY N . 17361 1 66 . 1 1 73 73 GLY C C 13 173.614 0.086 . 1 . . . . 73 GLY C . 17361 1 67 . 1 1 73 73 GLY CA C 13 45.001 0.153 . 1 . . . . 73 GLY CA . 17361 1 68 . 1 1 73 73 GLY N N 15 106.204 0.185 . 1 . . . . 73 GLY N . 17361 1 69 . 1 1 74 74 GLU C C 13 174.853 0.104 . 1 . . . . 74 GLU C . 17361 1 70 . 1 1 74 74 GLU CA C 13 53.703 0.104 . 1 . . . . 74 GLU CA . 17361 1 71 . 1 1 74 74 GLU CB C 13 33.101 0.036 . 1 . . . . 74 GLU CB . 17361 1 72 . 1 1 74 74 GLU N N 15 118.139 0.036 . 1 . . . . 74 GLU N . 17361 1 73 . 1 1 75 75 GLN C C 13 175.096 0.077 . 1 . . . . 75 GLN C . 17361 1 74 . 1 1 75 75 GLN CA C 13 55.296 0.061 . 1 . . . . 75 GLN CA . 17361 1 75 . 1 1 75 75 GLN CB C 13 29.046 0.163 . 1 . . . . 75 GLN CB . 17361 1 76 . 1 1 75 75 GLN CG C 13 33.014 0.070 . 1 . . . . 75 GLN CG . 17361 1 77 . 1 1 75 75 GLN N N 15 119.249 0.101 . 1 . . . . 75 GLN N . 17361 1 78 . 1 1 76 76 ASN C C 13 172.439 0.062 . 1 . . . . 76 ASN C . 17361 1 79 . 1 1 76 76 ASN CA C 13 51.393 0.024 . 1 . . . . 76 ASN CA . 17361 1 80 . 1 1 76 76 ASN CB C 13 41.051 0.033 . 1 . . . . 76 ASN CB . 17361 1 81 . 1 1 76 76 ASN CG C 13 175.304 0.029 . 1 . . . . 76 ASN CG . 17361 1 82 . 1 1 76 76 ASN N N 15 122.741 0.130 . 1 . . . . 76 ASN N . 17361 1 83 . 1 1 77 77 PRO C C 13 175.799 0.083 . 1 . . . . 77 PRO C . 17361 1 84 . 1 1 77 77 PRO CA C 13 62.420 0.025 . 1 . . . . 77 PRO CA . 17361 1 85 . 1 1 77 77 PRO CB C 13 32.006 0.058 . 1 . . . . 77 PRO CB . 17361 1 86 . 1 1 77 77 PRO CG C 13 28.031 0.056 . 1 . . . . 77 PRO CG . 17361 1 87 . 1 1 77 77 PRO CD C 13 50.850 0.126 . 1 . . . . 77 PRO CD . 17361 1 88 . 1 1 77 77 PRO N N 15 137.630 0.103 . 1 . . . . 77 PRO N . 17361 1 89 . 1 1 78 78 ILE C C 13 176.422 0.032 . 1 . . . . 78 ILE C . 17361 1 90 . 1 1 78 78 ILE CA C 13 56.870 0.121 . 1 . . . . 78 ILE CA . 17361 1 91 . 1 1 78 78 ILE CB C 13 38.640 0.078 . 1 . . . . 78 ILE CB . 17361 1 92 . 1 1 78 78 ILE CG1 C 13 25.613 0.046 . 1 . . . . 78 ILE CG1 . 17361 1 93 . 1 1 78 78 ILE CG2 C 13 15.958 0.040 . 1 . . . . 78 ILE CG2 . 17361 1 94 . 1 1 78 78 ILE CD1 C 13 10.506 0.028 . 1 . . . . 78 ILE CD1 . 17361 1 95 . 1 1 78 78 ILE N N 15 126.041 0.143 . 1 . . . . 78 ILE N . 17361 1 96 . 1 1 79 79 TYR C C 13 176.539 0.072 . 1 . . . . 79 TYR C . 17361 1 97 . 1 1 79 79 TYR CA C 13 58.356 0.064 . 1 . . . . 79 TYR CA . 17361 1 98 . 1 1 79 79 TYR CB C 13 37.603 0.004 . 1 . . . . 79 TYR CB . 17361 1 99 . 1 1 79 79 TYR N N 15 128.222 0.105 . 1 . . . . 79 TYR N . 17361 1 100 . 1 1 116 116 GLY C C 13 176.323 0.083 . 1 . . . . 116 GLY C . 17361 1 101 . 1 1 116 116 GLY CA C 13 47.719 0.089 . 1 . . . . 116 GLY CA . 17361 1 102 . 1 1 116 116 GLY N N 15 107.717 0.126 . 1 . . . . 116 GLY N . 17361 1 103 . 1 1 117 117 ILE C C 13 178.731 0.038 . 1 . . . . 117 ILE C . 17361 1 104 . 1 1 117 117 ILE CA C 13 65.845 0.083 . 1 . . . . 117 ILE CA . 17361 1 105 . 1 1 117 117 ILE CB C 13 37.426 0.105 . 1 . . . . 117 ILE CB . 17361 1 106 . 1 1 117 117 ILE CG1 C 13 29.849 0.014 . 1 . . . . 117 ILE CG1 . 17361 1 107 . 1 1 117 117 ILE CG2 C 13 16.877 0.064 . 1 . . . . 117 ILE CG2 . 17361 1 108 . 1 1 117 117 ILE CD1 C 13 13.601 0.072 . 1 . . . . 117 ILE CD1 . 17361 1 109 . 1 1 117 117 ILE N N 15 121.341 0.140 . 1 . . . . 117 ILE N . 17361 1 110 . 1 1 118 118 MET C C 13 178.682 0.026 . 1 . . . . 118 MET C . 17361 1 111 . 1 1 118 118 MET CA C 13 59.215 0.066 . 1 . . . . 118 MET CA . 17361 1 112 . 1 1 118 118 MET CB C 13 34.179 0.074 . 1 . . . . 118 MET CB . 17361 1 113 . 1 1 118 118 MET CG C 13 29.922 0.016 . 1 . . . . 118 MET CG . 17361 1 114 . 1 1 118 118 MET N N 15 124.788 0.114 . 1 . . . . 118 MET N . 17361 1 115 . 1 1 119 119 ILE C C 13 178.153 0.019 . 1 . . . . 119 ILE C . 17361 1 116 . 1 1 119 119 ILE CA C 13 61.752 0.035 . 1 . . . . 119 ILE CA . 17361 1 117 . 1 1 119 119 ILE CB C 13 34.206 0.070 . 1 . . . . 119 ILE CB . 17361 1 118 . 1 1 119 119 ILE CG1 C 13 25.841 0.057 . 1 . . . . 119 ILE CG1 . 17361 1 119 . 1 1 119 119 ILE CG2 C 13 19.773 0.038 . 1 . . . . 119 ILE CG2 . 17361 1 120 . 1 1 119 119 ILE CD1 C 13 9.821 0.034 . 1 . . . . 119 ILE CD1 . 17361 1 121 . 1 1 119 119 ILE N N 15 117.783 0.054 . 1 . . . . 119 ILE N . 17361 1 122 . 1 1 120 120 GLY C C 13 175.178 0.073 . 1 . . . . 120 GLY C . 17361 1 123 . 1 1 120 120 GLY CA C 13 47.855 0.068 . 1 . . . . 120 GLY CA . 17361 1 124 . 1 1 120 120 GLY N N 15 107.897 0.055 . 1 . . . . 120 GLY N . 17361 1 125 . 1 1 121 121 THR C C 13 177.715 0.072 . 1 . . . . 121 THR C . 17361 1 126 . 1 1 121 121 THR CA C 13 65.643 0.077 . 1 . . . . 121 THR CA . 17361 1 127 . 1 1 121 121 THR CB C 13 68.843 0.124 . 1 . . . . 121 THR CB . 17361 1 128 . 1 1 121 121 THR N N 15 109.662 0.144 . 1 . . . . 121 THR N . 17361 1 129 . 1 1 122 122 GLY C C 13 174.036 0.057 . 1 . . . . 122 GLY C . 17361 1 130 . 1 1 122 122 GLY CA C 13 47.913 0.064 . 1 . . . . 122 GLY CA . 17361 1 131 . 1 1 122 122 GLY N N 15 111.526 0.144 . 1 . . . . 122 GLY N . 17361 1 132 . 1 1 129 129 LYS C C 13 175.602 0.021 . 1 . . . . 129 LYS C . 17361 1 133 . 1 1 129 129 LYS CA C 13 58.069 0.103 . 1 . . . . 129 LYS CA . 17361 1 134 . 1 1 129 129 LYS CB C 13 33.918 0.041 . 1 . . . . 129 LYS CB . 17361 1 135 . 1 1 129 129 LYS CG C 13 25.815 0.005 . 1 . . . . 129 LYS CG . 17361 1 136 . 1 1 129 129 LYS CD C 13 29.942 0.055 . 1 . . . . 129 LYS CD . 17361 1 137 . 1 1 129 129 LYS CE C 13 42.265 0.000 . 1 . . . . 129 LYS CE . 17361 1 138 . 1 1 129 129 LYS N N 15 125.478 0.052 . 1 . . . . 129 LYS N . 17361 1 139 . 1 1 130 130 VAL C C 13 176.690 0.086 . 1 . . . . 130 VAL C . 17361 1 140 . 1 1 130 130 VAL CA C 13 61.415 0.094 . 1 . . . . 130 VAL CA . 17361 1 141 . 1 1 130 130 VAL CB C 13 33.243 0.055 . 1 . . . . 130 VAL CB . 17361 1 142 . 1 1 130 130 VAL CG2 C 13 20.114 0.057 . 1 . . . . 130 VAL CG2 . 17361 1 143 . 1 1 130 130 VAL N N 15 119.376 0.152 . 1 . . . . 130 VAL N . 17361 1 144 . 1 1 131 131 TYR C C 13 176.891 0.093 . 1 . . . . 131 TYR C . 17361 1 145 . 1 1 131 131 TYR CA C 13 62.388 0.126 . 1 . . . . 131 TYR CA . 17361 1 146 . 1 1 131 131 TYR CB C 13 38.948 0.075 . 1 . . . . 131 TYR CB . 17361 1 147 . 1 1 131 131 TYR N N 15 129.029 0.091 . 1 . . . . 131 TYR N . 17361 1 148 . 1 1 132 132 SER C C 13 176.452 0.063 . 1 . . . . 132 SER C . 17361 1 149 . 1 1 132 132 SER CA C 13 62.385 0.105 . 1 . . . . 132 SER CA . 17361 1 150 . 1 1 132 132 SER CB C 13 62.956 0.044 . 1 . . . . 132 SER CB . 17361 1 151 . 1 1 132 132 SER N N 15 110.521 0.107 . 1 . . . . 132 SER N . 17361 1 152 . 1 1 156 156 PHE C C 13 177.923 0.079 . 1 . . . . 156 PHE C . 17361 1 153 . 1 1 156 156 PHE CA C 13 58.935 0.117 . 1 . . . . 156 PHE CA . 17361 1 154 . 1 1 156 156 PHE CB C 13 42.436 0.113 . 1 . . . . 156 PHE CB . 17361 1 155 . 1 1 156 156 PHE N N 15 107.817 0.131 . 1 . . . . 156 PHE N . 17361 1 156 . 1 1 157 157 THR C C 13 177.771 0.040 . 1 . . . . 157 THR C . 17361 1 157 . 1 1 157 157 THR CA C 13 65.718 0.053 . 1 . . . . 157 THR CA . 17361 1 158 . 1 1 157 157 THR CB C 13 69.733 0.084 . 1 . . . . 157 THR CB . 17361 1 159 . 1 1 157 157 THR CG2 C 13 24.699 0.095 . 1 . . . . 157 THR CG2 . 17361 1 160 . 1 1 157 157 THR N N 15 109.237 0.097 . 1 . . . . 157 THR N . 17361 1 161 . 1 1 158 158 SER CA C 13 58.264 0.134 . 1 . . . . 158 SER CA . 17361 1 162 . 1 1 158 158 SER CB C 13 64.270 0.027 . 1 . . . . 158 SER CB . 17361 1 163 . 1 1 158 158 SER N N 15 112.663 0.173 . 1 . . . . 158 SER N . 17361 1 164 . 1 1 167 167 VAL C C 13 176.838 0.055 . 1 . . . . 167 VAL C . 17361 1 165 . 1 1 167 167 VAL CA C 13 66.006 0.120 . 1 . . . . 167 VAL CA . 17361 1 166 . 1 1 167 167 VAL CB C 13 31.531 0.045 . 1 . . . . 167 VAL CB . 17361 1 167 . 1 1 167 167 VAL CG1 C 13 21.740 0.048 . 2 . . . . 167 VAL CG1 . 17361 1 168 . 1 1 167 167 VAL CG2 C 13 23.092 0.012 . 2 . . . . 167 VAL CG2 . 17361 1 169 . 1 1 167 167 VAL N N 15 120.878 0.058 . 1 . . . . 167 VAL N . 17361 1 170 . 1 1 168 168 ALA C C 13 180.199 0.057 . 1 . . . . 168 ALA C . 17361 1 171 . 1 1 168 168 ALA CA C 13 56.232 0.091 . 1 . . . . 168 ALA CA . 17361 1 172 . 1 1 168 168 ALA CB C 13 18.530 0.011 . 1 . . . . 168 ALA CB . 17361 1 173 . 1 1 168 168 ALA N N 15 121.818 0.127 . 1 . . . . 168 ALA N . 17361 1 174 . 1 1 169 169 SER C C 13 177.299 0.037 . 1 . . . . 169 SER C . 17361 1 175 . 1 1 169 169 SER CA C 13 61.545 0.094 . 1 . . . . 169 SER CA . 17361 1 176 . 1 1 169 169 SER CB C 13 62.724 0.054 . 1 . . . . 169 SER CB . 17361 1 177 . 1 1 169 169 SER N N 15 111.415 0.115 . 1 . . . . 169 SER N . 17361 1 178 . 1 1 170 170 THR C C 13 175.394 0.001 . 1 . . . . 170 THR C . 17361 1 179 . 1 1 170 170 THR CA C 13 66.897 0.025 . 1 . . . . 170 THR CA . 17361 1 180 . 1 1 170 170 THR CB C 13 67.974 0.065 . 1 . . . . 170 THR CB . 17361 1 181 . 1 1 170 170 THR CG2 C 13 22.070 0.000 . 1 . . . . 170 THR CG2 . 17361 1 182 . 1 1 170 170 THR N N 15 119.214 0.063 . 1 . . . . 170 THR N . 17361 1 183 . 1 1 189 189 TRP C C 13 177.596 0.034 . 1 . . . . 189 TRP C . 17361 1 184 . 1 1 189 189 TRP CA C 13 61.914 0.058 . 1 . . . . 189 TRP CA . 17361 1 185 . 1 1 189 189 TRP CB C 13 33.713 0.006 . 1 . . . . 189 TRP CB . 17361 1 186 . 1 1 189 189 TRP N N 15 118.020 0.003 . 1 . . . . 189 TRP N . 17361 1 187 . 1 1 190 190 LEU C C 13 178.686 0.034 . 1 . . . . 190 LEU C . 17361 1 188 . 1 1 190 190 LEU CA C 13 58.738 0.076 . 1 . . . . 190 LEU CA . 17361 1 189 . 1 1 190 190 LEU CB C 13 43.055 0.019 . 1 . . . . 190 LEU CB . 17361 1 190 . 1 1 190 190 LEU CG C 13 26.330 0.053 . 1 . . . . 190 LEU CG . 17361 1 191 . 1 1 190 190 LEU CD1 C 13 25.237 0.007 . 2 . . . . 190 LEU CD1 . 17361 1 192 . 1 1 190 190 LEU CD2 C 13 23.192 0.043 . 2 . . . . 190 LEU CD2 . 17361 1 193 . 1 1 190 190 LEU N N 15 113.408 0.055 . 1 . . . . 190 LEU N . 17361 1 194 . 1 1 191 191 ILE C C 13 176.113 0.070 . 1 . . . . 191 ILE C . 17361 1 195 . 1 1 191 191 ILE CA C 13 62.010 0.088 . 1 . . . . 191 ILE CA . 17361 1 196 . 1 1 191 191 ILE CB C 13 38.498 0.048 . 1 . . . . 191 ILE CB . 17361 1 197 . 1 1 191 191 ILE CG1 C 13 24.443 0.073 . 1 . . . . 191 ILE CG1 . 17361 1 198 . 1 1 191 191 ILE CG2 C 13 17.240 0.031 . 1 . . . . 191 ILE CG2 . 17361 1 199 . 1 1 191 191 ILE CD1 C 13 14.127 0.019 . 1 . . . . 191 ILE CD1 . 17361 1 200 . 1 1 191 191 ILE N N 15 107.020 0.102 . 1 . . . . 191 ILE N . 17361 1 201 . 1 1 192 192 GLY C C 13 175.083 0.048 . 1 . . . . 192 GLY C . 17361 1 202 . 1 1 192 192 GLY CA C 13 43.521 0.124 . 1 . . . . 192 GLY CA . 17361 1 203 . 1 1 192 192 GLY N N 15 113.426 0.136 . 1 . . . . 192 GLY N . 17361 1 204 . 1 1 193 193 SER CA C 13 61.829 0.045 . 1 . . . . 193 SER CA . 17361 1 205 . 1 1 193 193 SER CB C 13 63.802 0.010 . 1 . . . . 193 SER CB . 17361 1 206 . 1 1 193 193 SER N N 15 117.253 0.165 . 1 . . . . 193 SER N . 17361 1 207 . 1 1 194 194 GLU C C 13 174.676 0.051 . 1 . . . . 194 GLU C . 17361 1 208 . 1 1 194 194 GLU CA C 13 58.500 0.021 . 1 . . . . 194 GLU CA . 17361 1 209 . 1 1 195 195 GLY C C 13 174.381 0.053 . 1 . . . . 195 GLY C . 17361 1 210 . 1 1 195 195 GLY CA C 13 44.623 0.155 . 1 . . . . 195 GLY CA . 17361 1 211 . 1 1 195 195 GLY N N 15 106.547 0.102 . 1 . . . . 195 GLY N . 17361 1 212 . 1 1 196 196 ALA C C 13 178.703 0.056 . 1 . . . . 196 ALA C . 17361 1 213 . 1 1 196 196 ALA CA C 13 53.020 0.118 . 1 . . . . 196 ALA CA . 17361 1 214 . 1 1 196 196 ALA CB C 13 20.328 0.033 . 1 . . . . 196 ALA CB . 17361 1 215 . 1 1 196 196 ALA N N 15 129.655 0.102 . 1 . . . . 196 ALA N . 17361 1 216 . 1 1 197 197 GLY C C 13 175.249 0.073 . 1 . . . . 197 GLY C . 17361 1 217 . 1 1 197 197 GLY CA C 13 47.405 0.081 . 1 . . . . 197 GLY CA . 17361 1 218 . 1 1 197 197 GLY N N 15 106.594 0.200 . 1 . . . . 197 GLY N . 17361 1 219 . 1 1 198 198 ILE C C 13 176.332 0.055 . 1 . . . . 198 ILE C . 17361 1 220 . 1 1 198 198 ILE CA C 13 62.753 0.091 . 1 . . . . 198 ILE CA . 17361 1 221 . 1 1 198 198 ILE CB C 13 39.020 0.013 . 1 . . . . 198 ILE CB . 17361 1 222 . 1 1 198 198 ILE CG1 C 13 28.162 0.056 . 1 . . . . 198 ILE CG1 . 17361 1 223 . 1 1 198 198 ILE CG2 C 13 18.066 0.045 . 1 . . . . 198 ILE CG2 . 17361 1 224 . 1 1 198 198 ILE CD1 C 13 13.924 0.036 . 1 . . . . 198 ILE CD1 . 17361 1 225 . 1 1 198 198 ILE N N 15 118.780 0.106 . 1 . . . . 198 ILE N . 17361 1 226 . 1 1 203 203 ILE C C 13 177.634 0.095 . 1 . . . . 203 ILE C . 17361 1 227 . 1 1 203 203 ILE CA C 13 62.142 0.070 . 1 . . . . 203 ILE CA . 17361 1 228 . 1 1 203 203 ILE CB C 13 36.451 0.067 . 1 . . . . 203 ILE CB . 17361 1 229 . 1 1 203 203 ILE CG1 C 13 28.007 0.086 . 1 . . . . 203 ILE CG1 . 17361 1 230 . 1 1 203 203 ILE CG2 C 13 17.355 0.053 . 1 . . . . 203 ILE CG2 . 17361 1 231 . 1 1 203 203 ILE CD1 C 13 10.848 0.083 . 1 . . . . 203 ILE CD1 . 17361 1 232 . 1 1 203 203 ILE N N 15 119.356 0.083 . 1 . . . . 203 ILE N . 17361 1 233 . 1 1 204 204 GLU C C 13 176.915 0.031 . 1 . . . . 204 GLU C . 17361 1 234 . 1 1 204 204 GLU CA C 13 59.482 0.070 . 1 . . . . 204 GLU CA . 17361 1 235 . 1 1 204 204 GLU CB C 13 28.731 0.044 . 1 . . . . 204 GLU CB . 17361 1 236 . 1 1 204 204 GLU CG C 13 33.963 0.058 . 1 . . . . 204 GLU CG . 17361 1 237 . 1 1 204 204 GLU N N 15 121.594 0.063 . 1 . . . . 204 GLU N . 17361 1 238 . 1 1 205 205 THR C C 13 176.663 0.024 . 1 . . . . 205 THR C . 17361 1 239 . 1 1 205 205 THR CA C 13 67.619 0.090 . 1 . . . . 205 THR CA . 17361 1 240 . 1 1 205 205 THR CB C 13 67.935 0.001 . 1 . . . . 205 THR CB . 17361 1 241 . 1 1 205 205 THR CG2 C 13 22.615 0.016 . 1 . . . . 205 THR CG2 . 17361 1 242 . 1 1 205 205 THR N N 15 113.841 0.125 . 1 . . . . 205 THR N . 17361 1 243 . 1 1 206 206 LEU C C 13 177.148 0.073 . 1 . . . . 206 LEU C . 17361 1 244 . 1 1 206 206 LEU CA C 13 59.252 0.073 . 1 . . . . 206 LEU CA . 17361 1 245 . 1 1 206 206 LEU CB C 13 39.870 0.092 . 1 . . . . 206 LEU CB . 17361 1 246 . 1 1 206 206 LEU CG C 13 26.843 0.054 . 1 . . . . 206 LEU CG . 17361 1 247 . 1 1 206 206 LEU CD1 C 13 22.359 0.027 . 2 . . . . 206 LEU CD1 . 17361 1 248 . 1 1 206 206 LEU CD2 C 13 25.551 0.082 . 2 . . . . 206 LEU CD2 . 17361 1 249 . 1 1 206 206 LEU N N 15 126.908 0.109 . 1 . . . . 206 LEU N . 17361 1 250 . 1 1 207 207 LEU CA C 13 58.376 0.048 . 1 . . . . 207 LEU CA . 17361 1 251 . 1 1 207 207 LEU CB C 13 41.087 0.000 . 1 . . . . 207 LEU CB . 17361 1 252 . 1 1 207 207 LEU CG C 13 26.465 0.000 . 1 . . . . 207 LEU CG . 17361 1 253 . 1 1 207 207 LEU CD1 C 13 22.846 0.000 . 2 . . . . 207 LEU CD1 . 17361 1 254 . 1 1 207 207 LEU CD2 C 13 25.743 0.000 . 2 . . . . 207 LEU CD2 . 17361 1 255 . 1 1 207 207 LEU N N 15 118.121 0.026 . 1 . . . . 207 LEU N . 17361 1 stop_ save_