data_5650 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5650 _Entry.Title ; NMR structure of the ribosomal protein L23 from Thermus Thermophilus ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2002-12-22 _Entry.Accession_date 2002-12-23 _Entry.Last_release_date 2003-04-29 _Entry.Original_release_date 2003-04-29 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Ahman Anders . . . 5650 2 Alexey Rak . . . 5650 3 Maria Dontsova . . . 5650 4 Maria Garber . B. . 5650 5 Torleif Hard . . . 5650 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5650 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 717 5650 '13C chemical shifts' 413 5650 '15N chemical shifts' 100 5650 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2003-04-29 2002-12-22 original author . 5650 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5650 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title 'NMR structure of the ribosomal protein L23 from Thermus Thermophilus' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 26 _Citation.Journal_issue 2 _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 131 _Citation.Page_last 137 _Citation.Year 2003 _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 Ahman Anders . . . 5650 1 2 Alexey Rak . . . 5650 1 3 Maria Dontsova . . . 5650 1 4 Maria Garber . B. . 5650 1 5 Torleif Hard . . . 5650 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'NMR spectroscopy' 5650 1 'protein structure' 5650 1 L23 5650 1 ribosome 5650 1 translation 5650 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_L23_(L25) _Assembly.Sf_category assembly _Assembly.Sf_framecode system_L23_(L25) _Assembly.Entry_ID 5650 _Assembly.ID 1 _Assembly.Name L23 _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'not present' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5650 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 L23 1 $L23 . . . native . . . . . 5650 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1N88 . . . . . . 5650 1 yes EMBL Q9RA57 . . . . . . 5650 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID L23 system 5650 1 'L23 (L25)' abbreviation 5650 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'A ribosomal protein.' 5650 1 'A chaperone docking site on the ribosome.' 5650 1 'Anchors the SRP to the ribosome.' 5650 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_L23 _Entity.Sf_category entity _Entity.Sf_framecode L23 _Entity.Entry_ID 5650 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name L23 _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 ; MKTAYDVILAPVLSEKAYAG FAEGKYTFWVHPKATKTEIK NAVETAFKVKVVKVNTLHVR GKKKRLGRYLGKRPDRKKAI VQVAPGQKIEALEGLI ; _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 96 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 10737 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 1N88 . "Nmr Structure Of The Ribosomal Protein L23 From Thermus Thermophilus." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 2 no PDB 1VSA . "Crystal Structure Of A 70s Ribosome-Trna Complex Reveals Functional Interactions And Rearrangements. This File, 1vsa, Contains " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 3 no PDB 1VSP . "Interactions And Dynamics Of The Shine-Dalgarno Helix In The 70s Ribosome. This File, 1vsp, Contains The 50s Ribosome Subunit. " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 4 no PDB 1VVM . "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-u On The Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 5 no PDB 1VVO . "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-u On The Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 6 no PDB 1VVQ . "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-a On The Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 7 no PDB 1VVS . "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-a On The Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 8 no PDB 1VVU . "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccg-g On The Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 9 no PDB 1VVW . "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccg-g On The Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 10 no PDB 1VVY . "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-u In The Absence Of Paromomycin" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 11 no PDB 1VW0 . "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-u In The Absence Of Paromomycin" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 12 no PDB 1VX9 . "Crystal Structure Of Trna Proline (cgg) Bound To Codon Ccc-u On The Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 13 no PDB 1VXJ . "Crystal Structure Of Trna Proline (cgg) Bound To Codon Ccc-u On The Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 14 no PDB 1VXL . "Crystal Structure Of Trna Proline (cgg) Bound To Codon Ccg-g On The Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 15 no PDB 1VXN . "Crystal Structure Of Trna Proline (cgg) Bound To Codon Ccg-g On The Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 16 no PDB 1VXQ . "Crystal Structure Of Trna Proline (cgg) Bound To Codon Ccc-g On The Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 17 no PDB 1VXT . "Crystal Structure Of Trna Proline (cgg) Bound To Codon Ccc-g On The Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 18 no PDB 1VY1 . "Crystal Structure Of Unmodified Trna Proline (cgg) Bound To Codon Ccg On The Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 19 no PDB 1VY3 . "Crystal Structure Of Unmodified Trna Proline (cgg) Bound To Codon Ccg On The Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 20 no PDB 2HGJ . "Crystal Structure Of The 70s Thermus Thermophilus Ribosome Showing How The 16s 3'-End Mimicks Mrna E And P Codons. This Entry 2" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 21 no PDB 2HGQ . "Crystal Structure Of The 70s Thermus Thermophilus Ribosome With Translocated And Rotated Shine-Dalgarno Duplex. This Entry 2hgq" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 22 no PDB 2HGU . "70s T.Th. Ribosome Functional Complex With Mrna And E- And P-Site Trnas At 4.5a. This Entry 2hgu Contains 50s Ribosomal Subunit" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 23 no PDB 2J01 . "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Mrna, Trna And Paromomycin (Part 2 Of 4). This File Contains " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 24 no PDB 2J03 . "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Mrna, Trna And Paromomycin (Part 4 Of 4). This File Contains " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 25 no PDB 2V47 . "Structure Of The Ribosome Recycling Factor Bound To The Thermus Thermophilus 70s Ribosome With Mrna, Asl-Phe And Trna-Fmet (Par" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 26 no PDB 2V49 . "Structure Of The Ribosome Recycling Factor Bound To The Thermus Thermophilus 70s Ribosome With Mrna, Asl-Phe And Trna-Fmet (Par" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 27 no PDB 2WDI . "Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Mrna, Paromomycin, Acylated A-Site Trna, Deacylated P-Site T" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 28 no PDB 2WDJ . "Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Mrna, Paromomycin, Acylated A-Site Trna, Deacylated P-Site T" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 29 no PDB 2WDL . "Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Mrna, Paromomycin, Acylated A- And P-Site Trnas, And E-Site " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 30 no PDB 2WDN . "Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Mrna, Paromomycin, Acylated A- And P-Site Trnas, And E-Site " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 31 no PDB 2WH2 . "Insights Into Translational Termination From The Structure Of Rf2 Bound To The Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 32 no PDB 2WH4 . "Insights Into Translational Termination From The Structure Of Rf2 Bound To The Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 33 no PDB 2WRJ . "The Structure Of The Ribosome With Elongation Factor G Trapped In The Post-Translocational State (Part 2 Of 4)." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 34 no PDB 2WRL . "The Structure Of The Ribosome With Elongation Factor G Trapped In The Post-Translocational State. (Part 4 Of 4)." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 35 no PDB 2WRO . "The Crystal Structure Of The 70s Ribosome Bound To Ef-Tu And Trna (Part 2 Of 4)." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 36 no PDB 2WRR . "The Crystal Structure Of The 70s Ribosome Bound To Ef-Tu And Trna (Part 4 Of 4)." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 37 no PDB 2X9S . "Structure Of The 70s Ribosome Bound To Release Factor 2 And A Substrate Analog Provides Insights Into Catalysis Of Peptide Rele" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 38 no PDB 2X9U . "Structure Of The 70s Ribosome Bound To Release Factor 2 And A Substrate Analog Provides Insights Into Catalysis Of Peptide Rele" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 39 no PDB 2XG0 . "Structure Of Cytotoxic Domain Of Colicin E3 Bound To The 70s Ribosome (part 2 Of 4)" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 40 no PDB 2XG2 . "Structure Of Cytotoxic Domain Of Colicin E3 Bound To The 70s Ribosome (part 4 Of 4)" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 41 no PDB 2XQE . "The Structure Of Ef-Tu And Aminoacyl-Trna Bound To The 70s Ribosome With A Gtp Analog" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 42 no PDB 2XTG . "Trna Tranlocation On The 70s Ribosome: The Pre- Translocational Translocation Intermediate Ti(Pre)" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 43 no PDB 2XUX . "Trna Translocation On The 70s Ribosome: The Post- Translocational Translocation Intermediate Ti(Post)" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 44 no PDB 2Y0V . "The Crystal Structure Of Ef-Tu And A9c-Trna-Trp Bound To A Near-Cognate Codon On The 70s Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 45 no PDB 2Y0X . "The Crystal Structure Of Ef-Tu And A9c-Trna-Trp Bound To A Near-Cognate Codon On The 70s Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 46 no PDB 2Y0Z . "The Crystal Structure Of Ef-Tu And G24a-Trna-Trp Bound To A Near-Cognate Codon On The 70s Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 47 no PDB 2Y11 . "The Crystal Structure Of Ef-Tu And Trp-Trna-Trp Bound To A Cognate Codon On The 70s Ribosome." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 48 no PDB 2Y13 . "The Crystal Structure Of Ef-Tu And G24a-Trna-Trp Bound To A Near-Cognate Codon On The 70s Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 49 no PDB 2Y15 . "The Crystal Structure Of Ef-Tu And G24a-Trna-Trp Bound To A Cognate Codon On The 70s Ribosome." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 50 no PDB 2Y17 . "Ef-Tu Complex 3" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 51 no PDB 2Y19 . "The Crystal Structure Of Ef-Tu And Trp-Trna-Trp Bound To A Cognate Codon On The 70s Ribosome." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 52 no PDB 3D5B . "Structural Basis For Translation Termination On The 70s Ribosome. This File Contains The 50s Subunit Of One 70s Ribosome. The E" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 53 no PDB 3D5D . "Structural Basis For Translation Termination On The 70s Ribosome. This File Contains The 50s Subunit Of The Second 70s Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 54 no PDB 3F1F . "Crystal Structure Of A Translation Termination Complex Formed With Release Factor Rf2. This File Contains The 50s Subunit Of On" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 55 no PDB 3F1H . "Crystal Structure Of A Translation Termination Complex Formed With Release Factor Rf2. This File Contains The 50s Subunit Of Th" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 56 no PDB 3FIN . "T. Thermophilus 70s Ribosome In Complex With Mrna, Trnas And Ef- Tu.Gdp.Kirromycin Ternary Complex, Fitted To A 6.4 A Cryo-Em M" . . . . . 96.88 93 100.00 100.00 3.03e-58 . . . . 5650 1 57 no PDB 3HUX . "Structure Of Ef-P Bound To The 70s Ribosome; This File Contains The 50s Subunit For Molecule I." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 58 no PDB 3HUZ . "Structure Of Ef-p Bound To The 70s Ribosome; This File Contains The 50s Subunit For Molecule Ii." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 59 no PDB 3I8F . "Elongation Complex Of The 70s Ribosome With Three Trnas And Entry 3i8f Contains 50s Ribosomal Subunit. The 30s Ribosoma Can Be " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 60 no PDB 3I8I . "Elongation Complex Of The 70s Ribosome With Three Trnas And Entry 3i8i Contains 50s Ribosomal Subnit. The 30s Ribosomal Can Be " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 61 no PDB 3I9C . "Initiation Complex Of 70s Ribosome With Two Trnas And Mrna. 3i9c Contains 50s Ribosomal Subunit Of Molecule B. The 30s Subunit " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 62 no PDB 3I9E . "Initiation Complex Of 70s Ribosome With Two Trnas And Mrna. 3i9e Contains 50s Ribosomal Subunit Of Molecule A. The 30s Subunit " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 63 no PDB 3KIR . "Structure Of Rele Nuclease Bound To The 70s Ribosome (Precleavage State; Part 2 Of 4)" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 64 no PDB 3KIT . "Structure Of Rele Nuclease Bound To The 70s Ribosome (Precleavage State; Part 4 Of 4)" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 65 no PDB 3KIW . "Structure Of Rele Nuclease Bound To The 70s Ribosome (Postcleavage State; Part 2 Of 4)" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 66 no PDB 3KIY . "Structure Of Rele Nuclease Bound To The 70s Ribosome (Postcleavage State; Part 4 Of 4)" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 67 no PDB 3KNI . "The Structures Of Viomycin Bound To The 70s Ribosome. This File Contains The 50s Subunit For Molecule I" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 68 no PDB 3KNK . "The Structures Of Viomycin Bound To The 70s Ribosome. This File Contains The 50s Subunit For Molecule Ii." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 69 no PDB 3KNM . "The Structures Of Capreomycin Bound To The 70s Ribosome. This File Contains The 50s Subunit For Molecule I." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 70 no PDB 3KNO . "The Structures Of Capreomycin Bound To The 70s Ribosome. This File Contains The 50s Subunit For Molecule Ii" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 71 no PDB 3MRZ . "Recognition Of The Amber Stop Codon By Release Factor Rf1. This Entry 3mrz Contains 50s Ribosomal Subunit. The 30s Ribosomal Su" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 72 no PDB 3MS1 . "Recognition Of The Amber Stop Codon By Release Factor Rf1. This Entry 3ms1 Contains 50s Ribosomal Subunit. The 30s Ribosomal Su" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 73 no PDB 3OH5 . "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Chloramphenicol. This File Contains The 50s Subunit Of One 70" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 74 no PDB 3OH7 . "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Chloramphenicol. This File Contains The 50s Subunit Of One 70" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 75 no PDB 3OHJ . "Structure Of The Thermus Thermophilus Ribosome Complexed With Erythromycin. This File Contains The 50s Subunit Of One 70s Ribos" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 76 no PDB 3OHK . "Structure Of The Thermus Thermophilus Ribosome Complexed With Erythromycin. This File Contains The 50s Subunit Of One 70s Ribos" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 77 no PDB 3OHZ . "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Azithromycin. This File Contains The 50s Subunit Of One 70s R" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 78 no PDB 3OI1 . "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Azithromycin. This File Contains The 50s Subunit Of One 70s R" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 79 no PDB 3OI3 . "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Telithromycin. This File Contains The 50s Subunit Of One 70s " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 80 no PDB 3OI5 . "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Telithromycin. This File Contains The 50s Subunit Of One 70s " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 81 no PDB 3PYO . "Crystal Structure Of A Complex Containing Domain 3 From The Psiv Igr Ires Rna Bound To The 70s Ribosome. This File Contains The" . . . . . 95.83 92 100.00 100.00 1.43e-57 . . . . 5650 1 82 no PDB 3PYR . "Crystal Structure Of A Complex Containing Domain 3 From The Psiv Igr Ires Rna Bound To The 70s Ribosome. This File Contains The" . . . . . 95.83 92 100.00 100.00 1.43e-57 . . . . 5650 1 83 no PDB 3PYT . "Crystal Structure Of A Complex Containing Domain 3 Of Crpv Igr Ires Rna Bound To The 70s Ribosome. This File Contains The 50s S" . . . . . 95.83 92 100.00 100.00 1.43e-57 . . . . 5650 1 84 no PDB 3PYV . "Crystal Structure Of A Complex Containing Domain 3 Of Crpv Igr Ires Rna Bound To The 70s Ribosome. This File Contains The 50s S" . . . . . 95.83 92 100.00 100.00 1.43e-57 . . . . 5650 1 85 no PDB 3TVE . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" . . . . . 95.83 92 100.00 100.00 1.43e-57 . . . . 5650 1 86 no PDB 3TVH . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s Molecule In T" . . . . . 95.83 92 100.00 100.00 1.43e-57 . . . . 5650 1 87 no PDB 3UXQ . "The Structure Of Thermorubin In Complex With The 70s Ribosome From Thermus Thermophilus. This File Contains The 50s Subunit Of " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 88 no PDB 3UXR . "The Structure Of Thermorubin In Complex With The 70s Ribosome From Thermus Thermophilus. This File Contains The 50s Subunit Of " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 89 no PDB 3UYE . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 90 no PDB 3UYG . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 91 no PDB 3UZ1 . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 92 no PDB 3UZ2 . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s Molecule In T" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 93 no PDB 3UZ8 . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s Molecule In T" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 94 no PDB 3UZ9 . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 95 no PDB 3UZF . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 96 no PDB 3UZH . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s Molecule In T" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 97 no PDB 3UZK . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 98 no PDB 3UZN . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s Molecule In T" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 99 no PDB 3V23 . "Crystal Structure Of Rmf Bound To The 70s Ribosome. This Pdb Entry Contains Coordinates For The 50s Subunit Of The 1st Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 100 no PDB 3V25 . "Crystal Structure Of Rmf Bound To The 70s Ribosome. This Pdb Entry Contains Coordinates For The 50s Subunit Of The 2nd Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 101 no PDB 3V27 . "Crystal Structure Of Hpf Bound To The 70s Ribosome. This Pdb Entry Contains Coordinates For The 50s Subunit Of The 1st Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 102 no PDB 3V29 . "Crystal Structure Of Hpf Bound To The 70s Ribosome. This Entry Contains The 50s Subunit Of The 2nd Molecule In The Asu." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 103 no PDB 3V2D . "Crystal Structure Of Yfia Bound To The 70s Ribosome. This Pdb Entry Contains Coordinates For The 50s Subunit Of The 1st Ribosom" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 104 no PDB 3V2F . "Crystal Structure Of Yfia Bound To The 70s Ribosome. This Pdb Entry Contains Coordinates For The 50s Subunit Of The 2nd Ribosom" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 105 no PDB 3V6W . "Crystal Structure Of The Bacterial Ribosome Ram Mutation G347u. This Entry Contains The 50s Ribosomal Subunit Of The First 70s " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 106 no PDB 3V6X . "Crystal Structure Of The Bacterial Ribosome Ram Mutation G347u. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 107 no PDB 3ZN9 . "The Crystal Structure Of Agmatidine Trna-ile2 Bound To The 70s Ribosome In The A And P Site." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 108 no PDB 3ZNE . "The Crystal Structure Of Agmatidine Trna-ile2 Bound To The 70s Ribosome In The A And P Site." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 109 no PDB 3ZVP . "Crystal Structure Of The Hybrid State Of Ribosome In Complex With The Guanosine Triphosphatase Release Factor 3" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 110 no PDB 4ABS . "Complex Of Smpb, A Tmrna Fragment And Ef-Tu-Gdp-Kirromycin With The 70s Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 111 no PDB 4B8G . "Crystal Structure Of 70s Ribosome With Both Cognate Trnas In The E And P Sites Representing An Authentic Elongation Complex." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 112 no PDB 4B8I . "Crystal Structure Of 70s Ribosome With Both Cognate Trnas In The E And P Sites Representing An Authentic Elongation Complex." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 113 no PDB 4BTD . "Thermus Thermophilus Ribosome" . . . . . 98.96 95 100.00 100.00 1.66e-59 . . . . 5650 1 114 no PDB 4BYC . "Structure Of Thermus Thermophilus 50s Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 115 no PDB 4BYE . "Structure Of Thermus Thermophilus 50s Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 116 no PDB 4DHA . "Crystal Structure Of Yaej Bound To The 70s Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 117 no PDB 4DHC . "Crystal Structure Of Yaej Bound To The 70s Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 118 no PDB 4EJB . "Crystal Structure Of The Bacterial Ribosome Ram Mutation G299a.this Entry Contains The 50s Ribosomal Subunit Of The First 70s M" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 119 no PDB 4EJC . "Crystal Structure Of The Bacterial Ribosome Ram Mutation G299a. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 120 no PDB 4G5L . "Crystal Structure Of The 70s Ribosome With Tetracycline. This Entry Contains The 50s Subunit Of Molecule A." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 121 no PDB 4G5N . "Crystal Structure Of The 70s Ribosome With Tetracycline. This Entry Contains The 50s Subunit Of Molecule B." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 122 no PDB 4G5U . "Crystal Structure Of The 70s Ribosome With Tigecycline. This Entry Contains The 50s Subunit Of Molecule A." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 123 no PDB 4G5W . "Crystal Structure Of The 70s Ribosome With Tigecycline. This Entry Contains The 50s Subunit Of Molecule B." . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 124 no PDB 4JUX . "Crystal Structure Of The Ribosome Bound To Elongation Factor G In The Guanosine Triphosphatase State (this File Contains The 50" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 125 no PDB 4K0M . "Crystal Structure Of Thermus Thermophilus 70s Containing Trnas And Mrna Stop Codon With Pseudouridine" . . . . . 95.83 92 100.00 100.00 1.43e-57 . . . . 5650 1 126 no PDB 4K0Q . "Crystal Structure Of Thermus Thermophilus 70s Containing Trnas And Mrna Stop Codon With Pseudouridine" . . . . . 95.83 92 100.00 100.00 1.43e-57 . . . . 5650 1 127 no PDB 4KBU . "70s Ribosome Translocation Intermediate Gdpnp-ii Containing Elongation Factor Efg/gdpnp, Mrna, And Trna Bound In The Pe*/e Stat" . . . . . 96.88 93 100.00 100.00 3.03e-58 . . . . 5650 1 128 no PDB 4KBW . "70s Ribosome Translocation Intermediate Gdpnp-ii Containing Elongation Factor Efg/gdpnp, Mrna, And Trna Bound In The Pe*/e Stat" . . . . . 96.88 93 100.00 100.00 3.03e-58 . . . . 5650 1 129 no PDB 4KCZ . "70s Ribosome Translocation Intermediate Gdpnp-i Containing Elongation Factor Efg/gdpnp, Mrna, And Trna Bound In The Pe*/e State" . . . . . 96.88 93 100.00 100.00 3.03e-58 . . . . 5650 1 130 no PDB 4KD2 . "70s Ribosome Translocation Intermediate Gdpnp-i Containing Elongation Factor Efg/gdpnp, Mrna, And Trna Bound In The Pe*/e State" . . . . . 96.88 93 100.00 100.00 3.03e-58 . . . . 5650 1 131 no PDB 4KD9 . "70s Ribosome Translocation Intermediate Fa-3.6a Containing Elongation Factor Efg/fusidic Acid/gdp, Mrna, And Trna Bound In The " . . . . . 96.88 93 100.00 100.00 3.03e-58 . . . . 5650 1 132 no PDB 4KDB . "70s Ribosome Translocation Intermediate Fa-3.6a Containing Elongation Factor Efg/fusidic Acid/gdp, Mrna, And Trna Bound In The " . . . . . 96.88 93 100.00 100.00 3.03e-58 . . . . 5650 1 133 no PDB 4KDH . "70s Ribosome Translocation Intermediate Fa-4.2a Containing Elongation Factor Efg/fusidic Acid/gdp, Mrna, And Trna Bound In The " . . . . . 96.88 93 100.00 100.00 3.03e-58 . . . . 5650 1 134 no PDB 4KDK . "70s Ribosome Translocation Intermediate Fa-4.2a Containing Elongation Factor Efg/fusidic Acid/gdp, Mrna, And Trna Bound In The " . . . . . 96.88 93 100.00 100.00 3.03e-58 . . . . 5650 1 135 no PDB 4KFI . "Crystal Structure Of The 70s Ribosome Bound With The Q253p Mutant Of Release Factor Rf2. 50s Of The A Subunit" . . . . . 95.83 92 100.00 100.00 1.43e-57 . . . . 5650 1 136 no PDB 4KFL . "Crystal Structure Of The 70s Ribosome Bound With The Q253p Mutant Of Release Factor Rf2. 50s Of The B Subunit" . . . . . 95.83 92 100.00 100.00 1.43e-57 . . . . 5650 1 137 no PDB 4KX0 . "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-g On The Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 138 no PDB 4KX2 . "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-g On The Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 139 no PDB 4L6J . "Crystal Structure Of Blasticidin S Bound To Thermus Thermophilus 70s Ribosome. This File Contains The 50s Subunit And Blasticid" . . . . . 95.83 92 100.00 100.00 1.43e-57 . . . . 5650 1 140 no PDB 4L6L . "Crystal Structure Of Blasticidin S Bound To Thermus Thermophilus 70s Ribosome. This File Contains The 50s Subunit And Blasticid" . . . . . 95.83 92 100.00 100.00 1.43e-57 . . . . 5650 1 141 no PDB 4NVV . "Crystal Structure Of Antibiotic Dityromycin Bound To 70s Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 142 no PDB 4NVX . "Crystal Structure Of Antibiotic Dityromycin Bound To 70s Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 143 no PDB 4NVZ . "Crystal Structure Of Antibiotic Ge82832 Bound To 70s Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 144 no PDB 4NW1 . "Crystal Structure Of Antibiotic Ge82832 Bound To 70s Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 145 no PDB 4QCN . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Pre- Attack State Of Peptide Bond Formation Containing Acylat" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 146 no PDB 4QCP . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Pre- Attack State Of Peptide Bond Formation Containing Acylat" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 147 no PDB 4QCR . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Post-catalysis State Of Peptide Bond Formation Containing Dip" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 148 no PDB 4QCT . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Post-catalysis State Of Peptide Bond Formation Containing Dip" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 149 no PDB 4QCV . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Pre- Attack State Of Peptide Bond Formation Containing Short " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 150 no PDB 4QCX . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Pre- Attack State Of Peptide Bond Formation Containing Short " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 151 no PDB 4QCZ . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Pre- Attack State Of Peptide Bond Formation Containing Short " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 152 no PDB 4QD1 . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Pre- Attack State Of Peptide Bond Formation Containing Short " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 153 no PDB 4QJS . "Crystal Structure Of Elongation Factor 4 (ef4/lepa) Bound To The Thermus Thermophilus 70s Ribosome, 50s Subunit Of The 70s Ribo" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 154 no PDB 4RB6 . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Amicoumacin, Mrna And Three Deacylated Trnas In The " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 155 no PDB 4RB8 . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Amicoumacin, Mrna And Three Deacylated Trnas In The " . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 156 no PDB 4RBA . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Pactamycin (soaked), Mrna And Three Deacylated Trnas" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 157 no PDB 4RBC . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Pactamycin (soaked), Mrna And Three Deacylated Trnas" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 158 no PDB 4RBE . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Pactamycin (co-crystallized), Mrna And Deacylated Tr" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 159 no PDB 4RBG . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Pactamycin (co-crystallized), Mrna And Deacylated Tr" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 160 no PDB 4RBI . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Negamycin, Mrna And Three Deacylated Trnas In The A," . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 161 no PDB 4RBK . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Negamycin, Mrna And Three Deacylated Trnas In The A," . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 162 no PDB 4W2B . "Crystal Structure Of The Peptolide 12c Bound To Bacterial Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 163 no PDB 4W2D . "Crystal Structure Of The Peptolide 12c Bound To Bacterial Ribosome" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 164 no DBJ BAD71513 . "50S ribosomal protein L23 [Thermus thermophilus HB8]" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 165 no GB AAD55971 . "ribosomal protein L23 [Thermus thermophilus]" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 166 no GB AAS81668 . "LSU ribosomal protein L23P [Thermus thermophilus HB27]" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 167 no GB AEG34103 . "Ribosomal protein L25/L23 [Thermus thermophilus SG0.5JP17-16]" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 168 no GB AFH38264 . "ribosomal protein L23 [Thermus thermophilus JL-18]" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 169 no GB EIA38549 . "50S ribosomal protein L23 [Thermus sp. RL]" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 170 no REF WP_008633421 . "MULTISPECIES: 50S ribosomal protein L23 [Thermus]" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 171 no REF YP_005295 . "50S ribosomal protein L23 [Thermus thermophilus HB27]" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 172 no REF YP_005641230 . "50S ribosomal protein L25 [Thermus thermophilus SG0.5JP17-16]" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 173 no REF YP_006058050 . "50S ribosomal protein L23 [Thermus thermophilus JL-18]" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 174 no REF YP_144956 . "50S ribosomal protein L23 [Thermus thermophilus HB8]" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 175 no SP Q5SHP0 . "RecName: Full=50S ribosomal protein L23 [Thermus thermophilus HB8]" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 176 no SP Q72I06 . "RecName: Full=50S ribosomal protein L23 [Thermus thermophilus HB27]" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 177 no SP Q9RA57 . "RecName: Full=50S ribosomal protein L23; Short=L*23 [Thermus thermophilus]" . . . . . 100.00 96 100.00 100.00 1.33e-60 . . . . 5650 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID L23 common 5650 1 L23 abbreviation 5650 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 . 5650 1 2 . LYS . 5650 1 3 . THR . 5650 1 4 . ALA . 5650 1 5 . TYR . 5650 1 6 . ASP . 5650 1 7 . VAL . 5650 1 8 . ILE . 5650 1 9 . LEU . 5650 1 10 . ALA . 5650 1 11 . PRO . 5650 1 12 . VAL . 5650 1 13 . LEU . 5650 1 14 . SER . 5650 1 15 . GLU . 5650 1 16 . LYS . 5650 1 17 . ALA . 5650 1 18 . TYR . 5650 1 19 . ALA . 5650 1 20 . GLY . 5650 1 21 . PHE . 5650 1 22 . ALA . 5650 1 23 . GLU . 5650 1 24 . GLY . 5650 1 25 . LYS . 5650 1 26 . TYR . 5650 1 27 . THR . 5650 1 28 . PHE . 5650 1 29 . TRP . 5650 1 30 . VAL . 5650 1 31 . HIS . 5650 1 32 . PRO . 5650 1 33 . LYS . 5650 1 34 . ALA . 5650 1 35 . THR . 5650 1 36 . LYS . 5650 1 37 . THR . 5650 1 38 . GLU . 5650 1 39 . ILE . 5650 1 40 . LYS . 5650 1 41 . ASN . 5650 1 42 . ALA . 5650 1 43 . VAL . 5650 1 44 . GLU . 5650 1 45 . THR . 5650 1 46 . ALA . 5650 1 47 . PHE . 5650 1 48 . LYS . 5650 1 49 . VAL . 5650 1 50 . LYS . 5650 1 51 . VAL . 5650 1 52 . VAL . 5650 1 53 . LYS . 5650 1 54 . VAL . 5650 1 55 . ASN . 5650 1 56 . THR . 5650 1 57 . LEU . 5650 1 58 . HIS . 5650 1 59 . VAL . 5650 1 60 . ARG . 5650 1 61 . GLY . 5650 1 62 . LYS . 5650 1 63 . LYS . 5650 1 64 . LYS . 5650 1 65 . ARG . 5650 1 66 . LEU . 5650 1 67 . GLY . 5650 1 68 . ARG . 5650 1 69 . TYR . 5650 1 70 . LEU . 5650 1 71 . GLY . 5650 1 72 . LYS . 5650 1 73 . ARG . 5650 1 74 . PRO . 5650 1 75 . ASP . 5650 1 76 . ARG . 5650 1 77 . LYS . 5650 1 78 . LYS . 5650 1 79 . ALA . 5650 1 80 . ILE . 5650 1 81 . VAL . 5650 1 82 . GLN . 5650 1 83 . VAL . 5650 1 84 . ALA . 5650 1 85 . PRO . 5650 1 86 . GLY . 5650 1 87 . GLN . 5650 1 88 . LYS . 5650 1 89 . ILE . 5650 1 90 . GLU . 5650 1 91 . ALA . 5650 1 92 . LEU . 5650 1 93 . GLU . 5650 1 94 . GLY . 5650 1 95 . LEU . 5650 1 96 . ILE . 5650 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 5650 1 . LYS 2 2 5650 1 . THR 3 3 5650 1 . ALA 4 4 5650 1 . TYR 5 5 5650 1 . ASP 6 6 5650 1 . VAL 7 7 5650 1 . ILE 8 8 5650 1 . LEU 9 9 5650 1 . ALA 10 10 5650 1 . PRO 11 11 5650 1 . VAL 12 12 5650 1 . LEU 13 13 5650 1 . SER 14 14 5650 1 . GLU 15 15 5650 1 . LYS 16 16 5650 1 . ALA 17 17 5650 1 . TYR 18 18 5650 1 . ALA 19 19 5650 1 . GLY 20 20 5650 1 . PHE 21 21 5650 1 . ALA 22 22 5650 1 . GLU 23 23 5650 1 . GLY 24 24 5650 1 . LYS 25 25 5650 1 . TYR 26 26 5650 1 . THR 27 27 5650 1 . PHE 28 28 5650 1 . TRP 29 29 5650 1 . VAL 30 30 5650 1 . HIS 31 31 5650 1 . PRO 32 32 5650 1 . LYS 33 33 5650 1 . ALA 34 34 5650 1 . THR 35 35 5650 1 . LYS 36 36 5650 1 . THR 37 37 5650 1 . GLU 38 38 5650 1 . ILE 39 39 5650 1 . LYS 40 40 5650 1 . ASN 41 41 5650 1 . ALA 42 42 5650 1 . VAL 43 43 5650 1 . GLU 44 44 5650 1 . THR 45 45 5650 1 . ALA 46 46 5650 1 . PHE 47 47 5650 1 . LYS 48 48 5650 1 . VAL 49 49 5650 1 . LYS 50 50 5650 1 . VAL 51 51 5650 1 . VAL 52 52 5650 1 . LYS 53 53 5650 1 . VAL 54 54 5650 1 . ASN 55 55 5650 1 . THR 56 56 5650 1 . LEU 57 57 5650 1 . HIS 58 58 5650 1 . VAL 59 59 5650 1 . ARG 60 60 5650 1 . GLY 61 61 5650 1 . LYS 62 62 5650 1 . LYS 63 63 5650 1 . LYS 64 64 5650 1 . ARG 65 65 5650 1 . LEU 66 66 5650 1 . GLY 67 67 5650 1 . ARG 68 68 5650 1 . TYR 69 69 5650 1 . LEU 70 70 5650 1 . GLY 71 71 5650 1 . LYS 72 72 5650 1 . ARG 73 73 5650 1 . PRO 74 74 5650 1 . ASP 75 75 5650 1 . ARG 76 76 5650 1 . LYS 77 77 5650 1 . LYS 78 78 5650 1 . ALA 79 79 5650 1 . ILE 80 80 5650 1 . VAL 81 81 5650 1 . GLN 82 82 5650 1 . VAL 83 83 5650 1 . ALA 84 84 5650 1 . PRO 85 85 5650 1 . GLY 86 86 5650 1 . GLN 87 87 5650 1 . LYS 88 88 5650 1 . ILE 89 89 5650 1 . GLU 90 90 5650 1 . ALA 91 91 5650 1 . LEU 92 92 5650 1 . GLU 93 93 5650 1 . GLY 94 94 5650 1 . LEU 95 95 5650 1 . ILE 96 96 5650 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 5650 _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 $L23 . 274 . . 'Thermus thermophilus' 'Thermus thermophilus' . . Eubacteria . Thermus thermophilus . . . . . . . . . . . . . . . . . . . . . 5650 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 5650 _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 $L23 . 'recombinant technology' 'Echerichia coli' 'E. coli' . . Echerichia coli . . . . . . . . . . . . . plasmid . . pET11c . . . . . . 5650 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Sample_1 _Sample.Sf_category sample _Sample.Sf_framecode Sample_1 _Sample.Entry_ID 5650 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 L23 '[U-13C; U-15N]' . . 1 $L23 . . 0.8 . . mM . . . . 5650 1 stop_ save_ save_Sample_2 _Sample.Sf_category sample _Sample.Sf_framecode Sample_2 _Sample.Entry_ID 5650 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 L23 [U-15N] . . 1 $L23 . . 0.8 . . mM . . . . 5650 2 stop_ save_ ####################### # Sample conditions # ####################### save_Condition_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Condition_1 _Sample_condition_list.Entry_ID 5650 _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 5.1 0.1 na 5650 1 temperature 308 0.5 K 5650 1 'ionic strength' 0.65 0.01 M 5650 1 stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Software.Sf_category software _Software.Sf_framecode XWINNMR _Software.Entry_ID 5650 _Software.ID 1 _Software.Name XWINNMR _Software.Version 2.6 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data collection' 5650 1 processing 5650 1 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 5650 _Software.ID 2 _Software.Name NMRPipe _Software.Version 2.1 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 5650 2 stop_ save_ save_Ansig_for_Windows _Software.Sf_category software _Software.Sf_framecode Ansig_for_Windows _Software.Entry_ID 5650 _Software.ID 3 _Software.Name 'Ansig for Windows' _Software.Version 1.02 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 5650 3 assignment 5650 3 stop_ save_ save_Talos _Software.Sf_category software _Software.Sf_framecode Talos _Software.Entry_ID 5650 _Software.ID 4 _Software.Name Talos _Software.Version 1999.019.15.47 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 5650 4 stop_ save_ save_Aqua _Software.Sf_category software _Software.Sf_framecode Aqua _Software.Entry_ID 5650 _Software.ID 5 _Software.Name Aqua _Software.Version 3.2 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 5650 5 stop_ save_ save_XPLOR _Software.Sf_category software _Software.Sf_framecode XPLOR _Software.Entry_ID 5650 _Software.ID 6 _Software.Name XPLOR _Software.Version 3.851 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure calculation' 5650 6 'structure analysis' 5650 6 stop_ save_ save_MOLMOL _Software.Sf_category software _Software.Sf_framecode MOLMOL _Software.Entry_ID 5650 _Software.ID 7 _Software.Name MOLMOL _Software.Version 2K.1 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data and structure analysis' 5650 7 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 5650 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AVANCE _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 5650 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AVANCE _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_3 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_3 _NMR_spectrometer.Entry_ID 5650 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5650 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer_1 Bruker AVANCE . 600 . . . 5650 1 2 NMR_spectrometer_2 Bruker AVANCE . 500 . . . 5650 1 3 NMR_spectrometer_3 Varian INOVA . 800 . . . 5650 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 5650 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 15N-HSQC' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5650 1 2 '3D 15N-DIPSI-HSQC' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5650 1 3 '3D 15N-NOESY-HSQC' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5650 1 4 '3D CBCANH' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5650 1 5 CBCA(CO)NH . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5650 1 6 HNCO . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5650 1 7 HNCA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5650 1 8 HN(CO)CA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5650 1 9 '3D C(CO)NH' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5650 1 10 HC(CO)NH . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5650 1 11 HCCH-COSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5650 1 12 HCCH-TOCSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5650 1 13 '3D 13C-edited NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5650 1 14 '2D DQF-COSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5650 1 15 clean-TOCSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5650 1 16 NOESY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5650 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 5650 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '2D 15N-HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 5650 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '3D 15N-DIPSI-HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 5650 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name '3D 15N-NOESY-HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 5650 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name '3D CBCANH' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 5650 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name CBCA(CO)NH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 5650 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name HNCO _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_7 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7 _NMR_spec_expt.Entry_ID 5650 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name HNCA _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_8 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_8 _NMR_spec_expt.Entry_ID 5650 _NMR_spec_expt.ID 8 _NMR_spec_expt.Name HN(CO)CA _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_9 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_9 _NMR_spec_expt.Entry_ID 5650 _NMR_spec_expt.ID 9 _NMR_spec_expt.Name '3D C(CO)NH' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_10 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_10 _NMR_spec_expt.Entry_ID 5650 _NMR_spec_expt.ID 10 _NMR_spec_expt.Name HC(CO)NH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_11 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_11 _NMR_spec_expt.Entry_ID 5650 _NMR_spec_expt.ID 11 _NMR_spec_expt.Name HCCH-COSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_12 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_12 _NMR_spec_expt.Entry_ID 5650 _NMR_spec_expt.ID 12 _NMR_spec_expt.Name HCCH-TOCSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_13 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_13 _NMR_spec_expt.Entry_ID 5650 _NMR_spec_expt.ID 13 _NMR_spec_expt.Name '3D 13C-edited NOESY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_14 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_14 _NMR_spec_expt.Entry_ID 5650 _NMR_spec_expt.ID 14 _NMR_spec_expt.Name '2D DQF-COSY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_15 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_15 _NMR_spec_expt.Entry_ID 5650 _NMR_spec_expt.ID 15 _NMR_spec_expt.Name clean-TOCSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_16 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_16 _NMR_spec_expt.Entry_ID 5650 _NMR_spec_expt.ID 16 _NMR_spec_expt.Name NOESY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5650 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.000000000 . . . . . . . . . 5650 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5650 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5650 1 H 2 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.153506088 . . . . . . . . . 5650 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_CSS_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode CSS_1 _Assigned_chem_shift_list.Entry_ID 5650 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Condition_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 15N-HSQC' . . . 5650 1 2 '3D 15N-DIPSI-HSQC' . . . 5650 1 3 '3D 15N-NOESY-HSQC' . . . 5650 1 4 '3D CBCANH' . . . 5650 1 5 CBCA(CO)NH . . . 5650 1 6 HNCO . . . 5650 1 7 HNCA . . . 5650 1 8 HN(CO)CA . . . 5650 1 9 '3D C(CO)NH' . . . 5650 1 10 HC(CO)NH . . . 5650 1 11 HCCH-COSY . . . 5650 1 12 HCCH-TOCSY . . . 5650 1 13 '3D 13C-edited NOESY' . . . 5650 1 14 '2D DQF-COSY' . . . 5650 1 15 clean-TOCSY . . . 5650 1 16 NOESY . . . 5650 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 MET CA C 13 53.028 0.050 . 1 . . . . . . . . 5650 1 2 . 1 1 1 1 MET HA H 1 4.185 0.005 . 1 . . . . . . . . 5650 1 3 . 1 1 1 1 MET C C 13 180.016 0.050 . 1 . . . . . . . . 5650 1 4 . 1 1 1 1 MET CB C 13 30.926 0.050 . 1 . . . . . . . . 5650 1 5 . 1 1 1 1 MET CG C 13 28.711 0.050 . 1 . . . . . . . . 5650 1 6 . 1 1 1 1 MET HB2 H 1 2.193 0.005 . 1 . . . . . . . . 5650 1 7 . 1 1 1 1 MET HB3 H 1 2.193 0.005 . 1 . . . . . . . . 5650 1 8 . 1 1 1 1 MET HG2 H 1 2.596 0.005 . 1 . . . . . . . . 5650 1 9 . 1 1 1 1 MET HG3 H 1 2.596 0.005 . 1 . . . . . . . . 5650 1 10 . 1 1 2 2 LYS N N 15 124.455 0.050 . 1 . . . . . . . . 5650 1 11 . 1 1 2 2 LYS H H 1 8.819 0.005 . 1 . . . . . . . . 5650 1 12 . 1 1 2 2 LYS CA C 13 54.400 0.050 . 1 . . . . . . . . 5650 1 13 . 1 1 2 2 LYS HA H 1 4.520 0.005 . 1 . . . . . . . . 5650 1 14 . 1 1 2 2 LYS C C 13 175.902 0.050 . 1 . . . . . . . . 5650 1 15 . 1 1 2 2 LYS CB C 13 31.295 0.050 . 1 . . . . . . . . 5650 1 16 . 1 1 2 2 LYS HB2 H 1 1.767 0.005 . 2 . . . . . . . . 5650 1 17 . 1 1 2 2 LYS HB3 H 1 1.845 0.005 . 2 . . . . . . . . 5650 1 18 . 1 1 2 2 LYS CG C 13 22.737 0.050 . 1 . . . . . . . . 5650 1 19 . 1 1 2 2 LYS HG2 H 1 1.435 0.005 . 2 . . . . . . . . 5650 1 20 . 1 1 2 2 LYS HG3 H 1 1.505 0.005 . 2 . . . . . . . . 5650 1 21 . 1 1 2 2 LYS CD C 13 27.053 0.050 . 1 . . . . . . . . 5650 1 22 . 1 1 2 2 LYS CE C 13 39.883 0.050 . 1 . . . . . . . . 5650 1 23 . 1 1 2 2 LYS HD3 H 1 1.638 0.005 . 1 . . . . . . . . 5650 1 24 . 1 1 2 2 LYS HE3 H 1 2.937 0.005 . 1 . . . . . . . . 5650 1 25 . 1 1 2 2 LYS HD2 H 1 1.638 0.005 . 1 . . . . . . . . 5650 1 26 . 1 1 2 2 LYS HE2 H 1 2.937 0.005 . 1 . . . . . . . . 5650 1 27 . 1 1 3 3 THR N N 15 114.534 0.050 . 1 . . . . . . . . 5650 1 28 . 1 1 3 3 THR H H 1 8.467 0.005 . 1 . . . . . . . . 5650 1 29 . 1 1 3 3 THR CA C 13 58.848 0.050 . 1 . . . . . . . . 5650 1 30 . 1 1 3 3 THR HA H 1 4.447 0.005 . 1 . . . . . . . . 5650 1 31 . 1 1 3 3 THR C C 13 177.297 0.050 . 1 . . . . . . . . 5650 1 32 . 1 1 3 3 THR CB C 13 68.692 0.050 . 1 . . . . . . . . 5650 1 33 . 1 1 3 3 THR HB H 1 4.244 0.005 . 1 . . . . . . . . 5650 1 34 . 1 1 3 3 THR CG2 C 13 19.485 0.050 . 1 . . . . . . . . 5650 1 35 . 1 1 3 3 THR HG21 H 1 1.191 0.005 . 1 . . . . . . . . 5650 1 36 . 1 1 3 3 THR HG22 H 1 1.191 0.005 . 1 . . . . . . . . 5650 1 37 . 1 1 3 3 THR HG23 H 1 1.191 0.005 . 1 . . . . . . . . 5650 1 38 . 1 1 4 4 ALA N N 15 123.963 0.050 . 1 . . . . . . . . 5650 1 39 . 1 1 4 4 ALA H H 1 8.449 0.005 . 1 . . . . . . . . 5650 1 40 . 1 1 4 4 ALA CA C 13 51.700 0.050 . 1 . . . . . . . . 5650 1 41 . 1 1 4 4 ALA HA H 1 4.133 0.005 . 1 . . . . . . . . 5650 1 42 . 1 1 4 4 ALA C C 13 174.508 0.050 . 1 . . . . . . . . 5650 1 43 . 1 1 4 4 ALA CB C 13 16.851 0.050 . 1 . . . . . . . . 5650 1 44 . 1 1 4 4 ALA HB1 H 1 1.229 0.005 . 1 . . . . . . . . 5650 1 45 . 1 1 4 4 ALA HB2 H 1 1.229 0.005 . 1 . . . . . . . . 5650 1 46 . 1 1 4 4 ALA HB3 H 1 1.229 0.005 . 1 . . . . . . . . 5650 1 47 . 1 1 5 5 TYR N N 15 115.624 0.050 . 1 . . . . . . . . 5650 1 48 . 1 1 5 5 TYR H H 1 7.470 0.005 . 1 . . . . . . . . 5650 1 49 . 1 1 5 5 TYR CA C 13 55.163 0.050 . 1 . . . . . . . . 5650 1 50 . 1 1 5 5 TYR HA H 1 4.700 0.005 . 1 . . . . . . . . 5650 1 51 . 1 1 5 5 TYR C C 13 176.978 0.050 . 1 . . . . . . . . 5650 1 52 . 1 1 5 5 TYR CB C 13 35.993 0.050 . 1 . . . . . . . . 5650 1 53 . 1 1 5 5 TYR HB2 H 1 2.656 0.005 . 2 . . . . . . . . 5650 1 54 . 1 1 5 5 TYR HB3 H 1 3.059 0.005 . 2 . . . . . . . . 5650 1 55 . 1 1 5 5 TYR HD1 H 1 6.892 0.005 . 1 . . . . . . . . 5650 1 56 . 1 1 5 5 TYR HE1 H 1 6.585 0.005 . 1 . . . . . . . . 5650 1 57 . 1 1 5 5 TYR HD2 H 1 6.892 0.005 . 1 . . . . . . . . 5650 1 58 . 1 1 5 5 TYR HE2 H 1 6.585 0.005 . 1 . . . . . . . . 5650 1 59 . 1 1 6 6 ASP N N 15 118.532 0.050 . 1 . . . . . . . . 5650 1 60 . 1 1 6 6 ASP H H 1 7.919 0.005 . 1 . . . . . . . . 5650 1 61 . 1 1 6 6 ASP CA C 13 52.732 0.050 . 1 . . . . . . . . 5650 1 62 . 1 1 6 6 ASP HA H 1 4.660 0.005 . 1 . . . . . . . . 5650 1 63 . 1 1 6 6 ASP C C 13 176.566 0.050 . 1 . . . . . . . . 5650 1 64 . 1 1 6 6 ASP CB C 13 39.027 0.050 . 1 . . . . . . . . 5650 1 65 . 1 1 6 6 ASP HB2 H 1 2.713 0.005 . 1 . . . . . . . . 5650 1 66 . 1 1 6 6 ASP HB3 H 1 2.713 0.005 . 1 . . . . . . . . 5650 1 67 . 1 1 7 7 VAL N N 15 117.686 0.050 . 1 . . . . . . . . 5650 1 68 . 1 1 7 7 VAL H H 1 7.652 0.005 . 1 . . . . . . . . 5650 1 69 . 1 1 7 7 VAL CA C 13 63.165 0.050 . 1 . . . . . . . . 5650 1 70 . 1 1 7 7 VAL HA H 1 3.873 0.005 . 1 . . . . . . . . 5650 1 71 . 1 1 7 7 VAL C C 13 176.866 0.050 . 1 . . . . . . . . 5650 1 72 . 1 1 7 7 VAL CB C 13 31.308 0.050 . 1 . . . . . . . . 5650 1 73 . 1 1 7 7 VAL HB H 1 1.913 0.005 . 1 . . . . . . . . 5650 1 74 . 1 1 7 7 VAL CG1 C 13 19.855 0.050 . 2 . . . . . . . . 5650 1 75 . 1 1 7 7 VAL HG11 H 1 0.817 0.005 . 2 . . . . . . . . 5650 1 76 . 1 1 7 7 VAL HG12 H 1 0.817 0.005 . 2 . . . . . . . . 5650 1 77 . 1 1 7 7 VAL HG13 H 1 0.817 0.005 . 2 . . . . . . . . 5650 1 78 . 1 1 7 7 VAL CG2 C 13 20.022 0.050 . 2 . . . . . . . . 5650 1 79 . 1 1 7 7 VAL HG21 H 1 0.914 0.005 . 2 . . . . . . . . 5650 1 80 . 1 1 7 7 VAL HG22 H 1 0.914 0.005 . 2 . . . . . . . . 5650 1 81 . 1 1 7 7 VAL HG23 H 1 0.914 0.005 . 2 . . . . . . . . 5650 1 82 . 1 1 8 8 ILE N N 15 116.966 0.050 . 1 . . . . . . . . 5650 1 83 . 1 1 8 8 ILE H H 1 8.189 0.005 . 1 . . . . . . . . 5650 1 84 . 1 1 8 8 ILE CA C 13 58.460 0.050 . 1 . . . . . . . . 5650 1 85 . 1 1 8 8 ILE HA H 1 4.111 0.005 . 1 . . . . . . . . 5650 1 86 . 1 1 8 8 ILE C C 13 177.389 0.050 . 1 . . . . . . . . 5650 1 87 . 1 1 8 8 ILE CB C 13 35.297 0.050 . 1 . . . . . . . . 5650 1 88 . 1 1 8 8 ILE HB H 1 1.897 0.005 . 1 . . . . . . . . 5650 1 89 . 1 1 8 8 ILE CG1 C 13 24.630 0.050 . 1 . . . . . . . . 5650 1 90 . 1 1 8 8 ILE HG12 H 1 0.820 0.005 . 2 . . . . . . . . 5650 1 91 . 1 1 8 8 ILE HG13 H 1 1.354 0.005 . 2 . . . . . . . . 5650 1 92 . 1 1 8 8 ILE CG2 C 13 16.190 0.050 . 1 . . . . . . . . 5650 1 93 . 1 1 8 8 ILE HG21 H 1 0.732 0.005 . 1 . . . . . . . . 5650 1 94 . 1 1 8 8 ILE HG22 H 1 0.732 0.005 . 1 . . . . . . . . 5650 1 95 . 1 1 8 8 ILE HG23 H 1 0.732 0.005 . 1 . . . . . . . . 5650 1 96 . 1 1 8 8 ILE CD1 C 13 10.262 0.050 . 1 . . . . . . . . 5650 1 97 . 1 1 8 8 ILE HD11 H 1 0.375 0.005 . 1 . . . . . . . . 5650 1 98 . 1 1 8 8 ILE HD12 H 1 0.375 0.005 . 1 . . . . . . . . 5650 1 99 . 1 1 8 8 ILE HD13 H 1 0.375 0.005 . 1 . . . . . . . . 5650 1 100 . 1 1 9 9 LEU N N 15 126.055 0.050 . 1 . . . . . . . . 5650 1 101 . 1 1 9 9 LEU H H 1 8.842 0.005 . 1 . . . . . . . . 5650 1 102 . 1 1 9 9 LEU CA C 13 54.353 0.050 . 1 . . . . . . . . 5650 1 103 . 1 1 9 9 LEU HA H 1 4.580 0.005 . 1 . . . . . . . . 5650 1 104 . 1 1 9 9 LEU CB C 13 40.134 0.050 . 1 . . . . . . . . 5650 1 105 . 1 1 9 9 LEU HB2 H 1 1.594 0.005 . 2 . . . . . . . . 5650 1 106 . 1 1 9 9 LEU HB3 H 1 1.713 0.005 . 2 . . . . . . . . 5650 1 107 . 1 1 9 9 LEU CG C 13 25.585 0.050 . 1 . . . . . . . . 5650 1 108 . 1 1 9 9 LEU HG H 1 1.651 0.005 . 1 . . . . . . . . 5650 1 109 . 1 1 9 9 LEU CD1 C 13 20.609 0.050 . 1 . . . . . . . . 5650 1 110 . 1 1 9 9 LEU HD11 H 1 0.899 0.005 . 1 . . . . . . . . 5650 1 111 . 1 1 9 9 LEU HD12 H 1 0.899 0.005 . 1 . . . . . . . . 5650 1 112 . 1 1 9 9 LEU HD13 H 1 0.899 0.005 . 1 . . . . . . . . 5650 1 113 . 1 1 9 9 LEU CD2 C 13 20.609 0.050 . 1 . . . . . . . . 5650 1 114 . 1 1 9 9 LEU HD21 H 1 0.899 0.005 . 1 . . . . . . . . 5650 1 115 . 1 1 9 9 LEU HD22 H 1 0.899 0.005 . 1 . . . . . . . . 5650 1 116 . 1 1 9 9 LEU HD23 H 1 0.899 0.005 . 1 . . . . . . . . 5650 1 117 . 1 1 10 10 ALA H H 1 7.837 0.005 . 1 . . . . . . . . 5650 1 118 . 1 1 10 10 ALA CA C 13 49.346 0.050 . 1 . . . . . . . . 5650 1 119 . 1 1 10 10 ALA HA H 1 5.087 0.005 . 1 . . . . . . . . 5650 1 120 . 1 1 10 10 ALA CB C 13 19.121 0.050 . 1 . . . . . . . . 5650 1 121 . 1 1 10 10 ALA HB1 H 1 1.786 0.005 . 1 . . . . . . . . 5650 1 122 . 1 1 10 10 ALA HB2 H 1 1.786 0.005 . 1 . . . . . . . . 5650 1 123 . 1 1 10 10 ALA HB3 H 1 1.786 0.005 . 1 . . . . . . . . 5650 1 124 . 1 1 11 11 PRO CA C 13 60.529 0.050 . 1 . . . . . . . . 5650 1 125 . 1 1 11 11 PRO HA H 1 4.840 0.005 . 1 . . . . . . . . 5650 1 126 . 1 1 11 11 PRO C C 13 177.438 0.050 . 1 . . . . . . . . 5650 1 127 . 1 1 11 11 PRO CB C 13 29.966 0.050 . 1 . . . . . . . . 5650 1 128 . 1 1 11 11 PRO HB2 H 1 1.877 0.005 . 2 . . . . . . . . 5650 1 129 . 1 1 11 11 PRO HB3 H 1 2.181 0.005 . 2 . . . . . . . . 5650 1 130 . 1 1 11 11 PRO CG C 13 25.417 0.050 . 1 . . . . . . . . 5650 1 131 . 1 1 11 11 PRO HG2 H 1 2.252 0.005 . 2 . . . . . . . . 5650 1 132 . 1 1 11 11 PRO HG3 H 1 2.437 0.005 . 2 . . . . . . . . 5650 1 133 . 1 1 11 11 PRO CD C 13 48.503 0.050 . 1 . . . . . . . . 5650 1 134 . 1 1 11 11 PRO HD2 H 1 4.021 0.005 . 2 . . . . . . . . 5650 1 135 . 1 1 11 11 PRO HD3 H 1 4.287 0.005 . 2 . . . . . . . . 5650 1 136 . 1 1 12 12 VAL N N 15 121.817 0.050 . 1 . . . . . . . . 5650 1 137 . 1 1 12 12 VAL H H 1 7.731 0.005 . 1 . . . . . . . . 5650 1 138 . 1 1 12 12 VAL CA C 13 60.558 0.050 . 1 . . . . . . . . 5650 1 139 . 1 1 12 12 VAL HA H 1 3.979 0.005 . 1 . . . . . . . . 5650 1 140 . 1 1 12 12 VAL C C 13 177.564 0.050 . 1 . . . . . . . . 5650 1 141 . 1 1 12 12 VAL CB C 13 29.032 0.050 . 1 . . . . . . . . 5650 1 142 . 1 1 12 12 VAL HB H 1 1.411 0.005 . 1 . . . . . . . . 5650 1 143 . 1 1 12 12 VAL CG1 C 13 18.363 0.050 . 2 . . . . . . . . 5650 1 144 . 1 1 12 12 VAL HG11 H 1 -0.078 0.005 . 2 . . . . . . . . 5650 1 145 . 1 1 12 12 VAL HG12 H 1 -0.078 0.005 . 2 . . . . . . . . 5650 1 146 . 1 1 12 12 VAL HG13 H 1 -0.078 0.005 . 2 . . . . . . . . 5650 1 147 . 1 1 12 12 VAL CG2 C 13 19.016 0.050 . 2 . . . . . . . . 5650 1 148 . 1 1 12 12 VAL HG21 H 1 0.755 0.005 . 2 . . . . . . . . 5650 1 149 . 1 1 12 12 VAL HG22 H 1 0.755 0.005 . 2 . . . . . . . . 5650 1 150 . 1 1 12 12 VAL HG23 H 1 0.755 0.005 . 2 . . . . . . . . 5650 1 151 . 1 1 13 13 LEU N N 15 127.792 0.050 . 1 . . . . . . . . 5650 1 152 . 1 1 13 13 LEU H H 1 8.465 0.005 . 1 . . . . . . . . 5650 1 153 . 1 1 13 13 LEU CA C 13 51.106 0.050 . 1 . . . . . . . . 5650 1 154 . 1 1 13 13 LEU HA H 1 4.681 0.005 . 1 . . . . . . . . 5650 1 155 . 1 1 13 13 LEU C C 13 176.690 0.050 . 1 . . . . . . . . 5650 1 156 . 1 1 13 13 LEU CB C 13 38.542 0.050 . 1 . . . . . . . . 5650 1 157 . 1 1 13 13 LEU HB2 H 1 1.696 0.005 . 2 . . . . . . . . 5650 1 158 . 1 1 13 13 LEU HB3 H 1 1.851 0.005 . 2 . . . . . . . . 5650 1 159 . 1 1 13 13 LEU CG C 13 24.623 0.050 . 1 . . . . . . . . 5650 1 160 . 1 1 13 13 LEU HG H 1 1.709 0.005 . 1 . . . . . . . . 5650 1 161 . 1 1 13 13 LEU CD1 C 13 21.197 0.050 . 2 . . . . . . . . 5650 1 162 . 1 1 13 13 LEU HD11 H 1 1.000 0.005 . 2 . . . . . . . . 5650 1 163 . 1 1 13 13 LEU HD12 H 1 1.000 0.005 . 2 . . . . . . . . 5650 1 164 . 1 1 13 13 LEU HD13 H 1 1.000 0.005 . 2 . . . . . . . . 5650 1 165 . 1 1 13 13 LEU CD2 C 13 23.955 0.050 . 2 . . . . . . . . 5650 1 166 . 1 1 13 13 LEU HD21 H 1 1.085 0.005 . 2 . . . . . . . . 5650 1 167 . 1 1 13 13 LEU HD22 H 1 1.085 0.005 . 2 . . . . . . . . 5650 1 168 . 1 1 13 13 LEU HD23 H 1 1.085 0.005 . 2 . . . . . . . . 5650 1 169 . 1 1 14 14 SER N N 15 115.050 0.050 . 1 . . . . . . . . 5650 1 170 . 1 1 14 14 SER H H 1 6.870 0.005 . 1 . . . . . . . . 5650 1 171 . 1 1 14 14 SER CA C 13 54.092 0.050 . 1 . . . . . . . . 5650 1 172 . 1 1 14 14 SER HA H 1 4.596 0.005 . 1 . . . . . . . . 5650 1 173 . 1 1 14 14 SER C C 13 178.668 0.050 . 1 . . . . . . . . 5650 1 174 . 1 1 14 14 SER CB C 13 63.436 0.050 . 1 . . . . . . . . 5650 1 175 . 1 1 14 14 SER HB2 H 1 3.869 0.005 . 2 . . . . . . . . 5650 1 176 . 1 1 14 14 SER HB3 H 1 4.211 0.005 . 2 . . . . . . . . 5650 1 177 . 1 1 15 15 GLU N N 15 121.318 0.050 . 1 . . . . . . . . 5650 1 178 . 1 1 15 15 GLU H H 1 8.941 0.005 . 1 . . . . . . . . 5650 1 179 . 1 1 15 15 GLU CA C 13 57.544 0.050 . 1 . . . . . . . . 5650 1 180 . 1 1 15 15 GLU HA H 1 3.898 0.005 . 1 . . . . . . . . 5650 1 181 . 1 1 15 15 GLU C C 13 173.629 0.050 . 1 . . . . . . . . 5650 1 182 . 1 1 15 15 GLU CB C 13 26.846 0.050 . 1 . . . . . . . . 5650 1 183 . 1 1 15 15 GLU CG C 13 33.796 0.050 . 1 . . . . . . . . 5650 1 184 . 1 1 15 15 GLU HG2 H 1 2.345 0.005 . 2 . . . . . . . . 5650 1 185 . 1 1 15 15 GLU HG3 H 1 2.406 0.005 . 2 . . . . . . . . 5650 1 186 . 1 1 15 15 GLU HB2 H 1 2.067 0.005 . 1 . . . . . . . . 5650 1 187 . 1 1 15 15 GLU HB3 H 1 2.067 0.005 . 1 . . . . . . . . 5650 1 188 . 1 1 16 16 LYS N N 15 118.370 0.050 . 1 . . . . . . . . 5650 1 189 . 1 1 16 16 LYS H H 1 8.163 0.005 . 1 . . . . . . . . 5650 1 190 . 1 1 16 16 LYS CA C 13 56.420 0.050 . 1 . . . . . . . . 5650 1 191 . 1 1 16 16 LYS HA H 1 4.015 0.005 . 1 . . . . . . . . 5650 1 192 . 1 1 16 16 LYS C C 13 173.617 0.050 . 1 . . . . . . . . 5650 1 193 . 1 1 16 16 LYS CB C 13 30.012 0.050 . 1 . . . . . . . . 5650 1 194 . 1 1 16 16 LYS HB2 H 1 1.687 0.005 . 2 . . . . . . . . 5650 1 195 . 1 1 16 16 LYS HB3 H 1 1.737 0.005 . 2 . . . . . . . . 5650 1 196 . 1 1 16 16 LYS CG C 13 22.894 0.050 . 1 . . . . . . . . 5650 1 197 . 1 1 16 16 LYS HG2 H 1 1.361 0.005 . 2 . . . . . . . . 5650 1 198 . 1 1 16 16 LYS HG3 H 1 1.453 0.005 . 2 . . . . . . . . 5650 1 199 . 1 1 16 16 LYS CD C 13 26.741 0.050 . 1 . . . . . . . . 5650 1 200 . 1 1 16 16 LYS CE C 13 39.966 0.050 . 1 . . . . . . . . 5650 1 201 . 1 1 16 16 LYS HD3 H 1 1.703 0.005 . 1 . . . . . . . . 5650 1 202 . 1 1 16 16 LYS HE3 H 1 2.988 0.005 . 1 . . . . . . . . 5650 1 203 . 1 1 16 16 LYS HD2 H 1 1.703 0.005 . 1 . . . . . . . . 5650 1 204 . 1 1 16 16 LYS HE2 H 1 2.988 0.005 . 1 . . . . . . . . 5650 1 205 . 1 1 17 17 ALA N N 15 122.035 0.050 . 1 . . . . . . . . 5650 1 206 . 1 1 17 17 ALA H H 1 7.661 0.005 . 1 . . . . . . . . 5650 1 207 . 1 1 17 17 ALA CA C 13 52.308 0.050 . 1 . . . . . . . . 5650 1 208 . 1 1 17 17 ALA HA H 1 3.974 0.005 . 1 . . . . . . . . 5650 1 209 . 1 1 17 17 ALA C C 13 171.839 0.050 . 1 . . . . . . . . 5650 1 210 . 1 1 17 17 ALA CB C 13 16.286 0.050 . 1 . . . . . . . . 5650 1 211 . 1 1 17 17 ALA HB1 H 1 1.288 0.005 . 1 . . . . . . . . 5650 1 212 . 1 1 17 17 ALA HB2 H 1 1.288 0.005 . 1 . . . . . . . . 5650 1 213 . 1 1 17 17 ALA HB3 H 1 1.288 0.005 . 1 . . . . . . . . 5650 1 214 . 1 1 18 18 TYR N N 15 118.066 0.050 . 1 . . . . . . . . 5650 1 215 . 1 1 18 18 TYR H H 1 8.160 0.005 . 1 . . . . . . . . 5650 1 216 . 1 1 18 18 TYR CA C 13 56.303 0.050 . 1 . . . . . . . . 5650 1 217 . 1 1 18 18 TYR HA H 1 3.101 0.005 . 1 . . . . . . . . 5650 1 218 . 1 1 18 18 TYR C C 13 174.108 0.050 . 1 . . . . . . . . 5650 1 219 . 1 1 18 18 TYR CB C 13 35.203 0.050 . 1 . . . . . . . . 5650 1 220 . 1 1 18 18 TYR HB2 H 1 2.841 0.005 . 1 . . . . . . . . 5650 1 221 . 1 1 18 18 TYR HD1 H 1 6.829 0.005 . 1 . . . . . . . . 5650 1 222 . 1 1 18 18 TYR HE1 H 1 7.215 0.005 . 1 . . . . . . . . 5650 1 223 . 1 1 18 18 TYR HB3 H 1 2.841 0.005 . 1 . . . . . . . . 5650 1 224 . 1 1 18 18 TYR HD2 H 1 6.829 0.005 . 1 . . . . . . . . 5650 1 225 . 1 1 18 18 TYR HE2 H 1 7.215 0.005 . 1 . . . . . . . . 5650 1 226 . 1 1 19 19 ALA N N 15 120.965 0.050 . 1 . . . . . . . . 5650 1 227 . 1 1 19 19 ALA H H 1 7.519 0.005 . 1 . . . . . . . . 5650 1 228 . 1 1 19 19 ALA CA C 13 52.215 0.050 . 1 . . . . . . . . 5650 1 229 . 1 1 19 19 ALA HA H 1 4.049 0.005 . 1 . . . . . . . . 5650 1 230 . 1 1 19 19 ALA C C 13 172.756 0.050 . 1 . . . . . . . . 5650 1 231 . 1 1 19 19 ALA CB C 13 15.881 0.050 . 1 . . . . . . . . 5650 1 232 . 1 1 19 19 ALA HB1 H 1 1.435 0.005 . 1 . . . . . . . . 5650 1 233 . 1 1 19 19 ALA HB2 H 1 1.435 0.005 . 1 . . . . . . . . 5650 1 234 . 1 1 19 19 ALA HB3 H 1 1.435 0.005 . 1 . . . . . . . . 5650 1 235 . 1 1 20 20 GLY N N 15 103.206 0.050 . 1 . . . . . . . . 5650 1 236 . 1 1 20 20 GLY H H 1 7.512 0.005 . 1 . . . . . . . . 5650 1 237 . 1 1 20 20 GLY CA C 13 44.268 0.050 . 1 . . . . . . . . 5650 1 238 . 1 1 20 20 GLY HA2 H 1 3.742 0.005 . 1 . . . . . . . . 5650 1 239 . 1 1 20 20 GLY HA3 H 1 4.023 0.005 . 1 . . . . . . . . 5650 1 240 . 1 1 20 20 GLY C C 13 175.974 0.050 . 1 . . . . . . . . 5650 1 241 . 1 1 21 21 PHE N N 15 122.045 0.050 . 1 . . . . . . . . 5650 1 242 . 1 1 21 21 PHE H H 1 7.791 0.005 . 1 . . . . . . . . 5650 1 243 . 1 1 21 21 PHE CA C 13 56.067 0.050 . 1 . . . . . . . . 5650 1 244 . 1 1 21 21 PHE HA H 1 3.855 0.005 . 1 . . . . . . . . 5650 1 245 . 1 1 21 21 PHE C C 13 172.786 0.050 . 1 . . . . . . . . 5650 1 246 . 1 1 21 21 PHE CB C 13 34.161 0.050 . 1 . . . . . . . . 5650 1 247 . 1 1 21 21 PHE HB2 H 1 3.166 0.005 . 2 . . . . . . . . 5650 1 248 . 1 1 21 21 PHE HB3 H 1 3.299 0.005 . 2 . . . . . . . . 5650 1 249 . 1 1 21 21 PHE HD1 H 1 7.109 0.005 . 1 . . . . . . . . 5650 1 250 . 1 1 21 21 PHE HE1 H 1 7.406 0.005 . 1 . . . . . . . . 5650 1 251 . 1 1 21 21 PHE HD2 H 1 7.109 0.005 . 1 . . . . . . . . 5650 1 252 . 1 1 21 21 PHE HE2 H 1 7.406 0.005 . 1 . . . . . . . . 5650 1 253 . 1 1 22 22 ALA N N 15 120.496 0.050 . 1 . . . . . . . . 5650 1 254 . 1 1 22 22 ALA H H 1 7.846 0.005 . 1 . . . . . . . . 5650 1 255 . 1 1 22 22 ALA CA C 13 52.306 0.050 . 1 . . . . . . . . 5650 1 256 . 1 1 22 22 ALA HA H 1 4.209 0.005 . 1 . . . . . . . . 5650 1 257 . 1 1 22 22 ALA C C 13 173.606 0.050 . 1 . . . . . . . . 5650 1 258 . 1 1 22 22 ALA CB C 13 16.446 0.050 . 1 . . . . . . . . 5650 1 259 . 1 1 22 22 ALA HB1 H 1 1.510 0.005 . 1 . . . . . . . . 5650 1 260 . 1 1 22 22 ALA HB2 H 1 1.510 0.005 . 1 . . . . . . . . 5650 1 261 . 1 1 22 22 ALA HB3 H 1 1.510 0.005 . 1 . . . . . . . . 5650 1 262 . 1 1 23 23 GLU N N 15 114.703 0.050 . 1 . . . . . . . . 5650 1 263 . 1 1 23 23 GLU H H 1 7.616 0.005 . 1 . . . . . . . . 5650 1 264 . 1 1 23 23 GLU CA C 13 52.715 0.050 . 1 . . . . . . . . 5650 1 265 . 1 1 23 23 GLU HA H 1 4.563 0.005 . 1 . . . . . . . . 5650 1 266 . 1 1 23 23 GLU C C 13 175.922 0.050 . 1 . . . . . . . . 5650 1 267 . 1 1 23 23 GLU CB C 13 28.259 0.050 . 1 . . . . . . . . 5650 1 268 . 1 1 23 23 GLU HB2 H 1 2.004 0.005 . 2 . . . . . . . . 5650 1 269 . 1 1 23 23 GLU HB3 H 1 2.323 0.005 . 2 . . . . . . . . 5650 1 270 . 1 1 23 23 GLU CG C 13 33.670 0.050 . 1 . . . . . . . . 5650 1 271 . 1 1 23 23 GLU HG2 H 1 2.290 0.005 . 2 . . . . . . . . 5650 1 272 . 1 1 23 23 GLU HG3 H 1 2.338 0.005 . 2 . . . . . . . . 5650 1 273 . 1 1 24 24 GLY N N 15 109.307 0.050 . 1 . . . . . . . . 5650 1 274 . 1 1 24 24 GLY H H 1 8.108 0.005 . 1 . . . . . . . . 5650 1 275 . 1 1 24 24 GLY CA C 13 44.447 0.050 . 1 . . . . . . . . 5650 1 276 . 1 1 24 24 GLY HA2 H 1 3.824 0.005 . 1 . . . . . . . . 5650 1 277 . 1 1 24 24 GLY HA3 H 1 4.252 0.005 . 1 . . . . . . . . 5650 1 278 . 1 1 24 24 GLY C C 13 179.788 0.050 . 1 . . . . . . . . 5650 1 279 . 1 1 25 25 LYS N N 15 117.804 0.050 . 1 . . . . . . . . 5650 1 280 . 1 1 25 25 LYS H H 1 7.464 0.005 . 1 . . . . . . . . 5650 1 281 . 1 1 25 25 LYS CA C 13 52.638 0.050 . 1 . . . . . . . . 5650 1 282 . 1 1 25 25 LYS HA H 1 5.077 0.005 . 1 . . . . . . . . 5650 1 283 . 1 1 25 25 LYS C C 13 177.011 0.050 . 1 . . . . . . . . 5650 1 284 . 1 1 25 25 LYS CB C 13 32.042 0.050 . 1 . . . . . . . . 5650 1 285 . 1 1 25 25 LYS HB2 H 1 1.322 0.005 . 2 . . . . . . . . 5650 1 286 . 1 1 25 25 LYS HB3 H 1 1.503 0.005 . 2 . . . . . . . . 5650 1 287 . 1 1 25 25 LYS CG C 13 23.324 0.050 . 1 . . . . . . . . 5650 1 288 . 1 1 25 25 LYS HG2 H 1 1.008 0.005 . 2 . . . . . . . . 5650 1 289 . 1 1 25 25 LYS HG3 H 1 1.274 0.005 . 2 . . . . . . . . 5650 1 290 . 1 1 25 25 LYS CD C 13 27.698 0.050 . 1 . . . . . . . . 5650 1 291 . 1 1 25 25 LYS HD2 H 1 1.538 0.005 . 2 . . . . . . . . 5650 1 292 . 1 1 25 25 LYS HD3 H 1 1.586 0.005 . 2 . . . . . . . . 5650 1 293 . 1 1 25 25 LYS CE C 13 40.132 0.050 . 1 . . . . . . . . 5650 1 294 . 1 1 25 25 LYS HE3 H 1 2.888 0.005 . 1 . . . . . . . . 5650 1 295 . 1 1 25 25 LYS HE2 H 1 2.888 0.005 . 1 . . . . . . . . 5650 1 296 . 1 1 26 26 TYR N N 15 122.352 0.050 . 1 . . . . . . . . 5650 1 297 . 1 1 26 26 TYR H H 1 9.072 0.005 . 1 . . . . . . . . 5650 1 298 . 1 1 26 26 TYR CA C 13 55.419 0.050 . 1 . . . . . . . . 5650 1 299 . 1 1 26 26 TYR HA H 1 4.527 0.005 . 1 . . . . . . . . 5650 1 300 . 1 1 26 26 TYR C C 13 178.084 0.050 . 1 . . . . . . . . 5650 1 301 . 1 1 26 26 TYR CB C 13 39.712 0.050 . 1 . . . . . . . . 5650 1 302 . 1 1 26 26 TYR HB2 H 1 2.464 0.005 . 1 . . . . . . . . 5650 1 303 . 1 1 26 26 TYR HD1 H 1 6.605 0.005 . 1 . . . . . . . . 5650 1 304 . 1 1 26 26 TYR HE1 H 1 6.219 0.005 . 1 . . . . . . . . 5650 1 305 . 1 1 26 26 TYR HB3 H 1 2.464 0.005 . 1 . . . . . . . . 5650 1 306 . 1 1 26 26 TYR HD2 H 1 6.605 0.005 . 1 . . . . . . . . 5650 1 307 . 1 1 26 26 TYR HE2 H 1 6.219 0.005 . 1 . . . . . . . . 5650 1 308 . 1 1 27 27 THR N N 15 118.730 0.050 . 1 . . . . . . . . 5650 1 309 . 1 1 27 27 THR H H 1 7.824 0.005 . 1 . . . . . . . . 5650 1 310 . 1 1 27 27 THR CA C 13 59.912 0.050 . 1 . . . . . . . . 5650 1 311 . 1 1 27 27 THR HA H 1 5.356 0.005 . 1 . . . . . . . . 5650 1 312 . 1 1 27 27 THR C C 13 178.470 0.050 . 1 . . . . . . . . 5650 1 313 . 1 1 27 27 THR CB C 13 67.505 0.050 . 1 . . . . . . . . 5650 1 314 . 1 1 27 27 THR HB H 1 3.790 0.005 . 1 . . . . . . . . 5650 1 315 . 1 1 27 27 THR CG2 C 13 18.682 0.050 . 1 . . . . . . . . 5650 1 316 . 1 1 27 27 THR HG21 H 1 0.907 0.005 . 1 . . . . . . . . 5650 1 317 . 1 1 27 27 THR HG22 H 1 0.907 0.005 . 1 . . . . . . . . 5650 1 318 . 1 1 27 27 THR HG23 H 1 0.907 0.005 . 1 . . . . . . . . 5650 1 319 . 1 1 28 28 PHE N N 15 123.604 0.050 . 1 . . . . . . . . 5650 1 320 . 1 1 28 28 PHE H H 1 9.461 0.005 . 1 . . . . . . . . 5650 1 321 . 1 1 28 28 PHE CA C 13 54.905 0.050 . 1 . . . . . . . . 5650 1 322 . 1 1 28 28 PHE HA H 1 5.155 0.005 . 1 . . . . . . . . 5650 1 323 . 1 1 28 28 PHE C C 13 176.826 0.050 . 1 . . . . . . . . 5650 1 324 . 1 1 28 28 PHE CB C 13 41.759 0.050 . 1 . . . . . . . . 5650 1 325 . 1 1 28 28 PHE HB2 H 1 2.432 0.005 . 2 . . . . . . . . 5650 1 326 . 1 1 28 28 PHE HB3 H 1 3.195 0.005 . 2 . . . . . . . . 5650 1 327 . 1 1 28 28 PHE HD1 H 1 6.998 0.005 . 1 . . . . . . . . 5650 1 328 . 1 1 28 28 PHE HE1 H 1 7.018 0.005 . 1 . . . . . . . . 5650 1 329 . 1 1 28 28 PHE HD2 H 1 6.998 0.005 . 1 . . . . . . . . 5650 1 330 . 1 1 28 28 PHE HE2 H 1 7.018 0.005 . 1 . . . . . . . . 5650 1 331 . 1 1 29 29 TRP N N 15 122.190 0.050 . 1 . . . . . . . . 5650 1 332 . 1 1 29 29 TRP H H 1 9.534 0.005 . 1 . . . . . . . . 5650 1 333 . 1 1 29 29 TRP CA C 13 54.751 0.050 . 1 . . . . . . . . 5650 1 334 . 1 1 29 29 TRP HA H 1 5.540 0.005 . 1 . . . . . . . . 5650 1 335 . 1 1 29 29 TRP C C 13 175.184 0.050 . 1 . . . . . . . . 5650 1 336 . 1 1 29 29 TRP CB C 13 29.165 0.050 . 1 . . . . . . . . 5650 1 337 . 1 1 29 29 TRP HD1 H 1 7.018 0.005 . 2 . . . . . . . . 5650 1 338 . 1 1 29 29 TRP NE1 N 15 129.383 0.050 . 1 . . . . . . . . 5650 1 339 . 1 1 29 29 TRP HE1 H 1 10.507 0.005 . 1 . . . . . . . . 5650 1 340 . 1 1 29 29 TRP HE3 H 1 7.712 0.005 . 1 . . . . . . . . 5650 1 341 . 1 1 29 29 TRP HZ2 H 1 7.581 0.005 . 1 . . . . . . . . 5650 1 342 . 1 1 29 29 TRP HZ3 H 1 6.828 0.005 . 1 . . . . . . . . 5650 1 343 . 1 1 29 29 TRP HH2 H 1 7.227 0.005 . 1 . . . . . . . . 5650 1 344 . 1 1 29 29 TRP HB2 H 1 3.372 0.005 . 1 . . . . . . . . 5650 1 345 . 1 1 29 29 TRP HB3 H 1 3.372 0.005 . 1 . . . . . . . . 5650 1 346 . 1 1 30 30 VAL N N 15 115.651 0.050 . 1 . . . . . . . . 5650 1 347 . 1 1 30 30 VAL H H 1 9.286 0.005 . 1 . . . . . . . . 5650 1 348 . 1 1 30 30 VAL CA C 13 56.046 0.050 . 1 . . . . . . . . 5650 1 349 . 1 1 30 30 VAL HA H 1 5.580 0.005 . 1 . . . . . . . . 5650 1 350 . 1 1 30 30 VAL C C 13 177.730 0.050 . 1 . . . . . . . . 5650 1 351 . 1 1 30 30 VAL CB C 13 33.807 0.050 . 1 . . . . . . . . 5650 1 352 . 1 1 30 30 VAL HB H 1 2.339 0.005 . 1 . . . . . . . . 5650 1 353 . 1 1 30 30 VAL CG1 C 13 16.426 0.050 . 2 . . . . . . . . 5650 1 354 . 1 1 30 30 VAL HG11 H 1 0.732 0.005 . 2 . . . . . . . . 5650 1 355 . 1 1 30 30 VAL HG12 H 1 0.732 0.005 . 2 . . . . . . . . 5650 1 356 . 1 1 30 30 VAL HG13 H 1 0.732 0.005 . 2 . . . . . . . . 5650 1 357 . 1 1 30 30 VAL CG2 C 13 20.636 0.050 . 2 . . . . . . . . 5650 1 358 . 1 1 30 30 VAL HG21 H 1 0.907 0.005 . 2 . . . . . . . . 5650 1 359 . 1 1 30 30 VAL HG22 H 1 0.907 0.005 . 2 . . . . . . . . 5650 1 360 . 1 1 30 30 VAL HG23 H 1 0.907 0.005 . 2 . . . . . . . . 5650 1 361 . 1 1 31 31 HIS N N 15 122.679 0.050 . 1 . . . . . . . . 5650 1 362 . 1 1 31 31 HIS H H 1 8.702 0.005 . 1 . . . . . . . . 5650 1 363 . 1 1 31 31 HIS CA C 13 54.622 0.050 . 1 . . . . . . . . 5650 1 364 . 1 1 31 31 HIS HA H 1 4.433 0.005 . 1 . . . . . . . . 5650 1 365 . 1 1 31 31 HIS CB C 13 29.231 0.050 . 1 . . . . . . . . 5650 1 366 . 1 1 31 31 HIS HB2 H 1 3.046 0.005 . 2 . . . . . . . . 5650 1 367 . 1 1 31 31 HIS HB3 H 1 3.495 0.005 . 2 . . . . . . . . 5650 1 368 . 1 1 31 31 HIS HD2 H 1 7.276 0.005 . 2 . . . . . . . . 5650 1 369 . 1 1 32 32 PRO CA C 13 63.462 0.050 . 1 . . . . . . . . 5650 1 370 . 1 1 32 32 PRO HA H 1 4.144 0.005 . 1 . . . . . . . . 5650 1 371 . 1 1 32 32 PRO C C 13 173.910 0.050 . 1 . . . . . . . . 5650 1 372 . 1 1 32 32 PRO CB C 13 30.358 0.050 . 1 . . . . . . . . 5650 1 373 . 1 1 32 32 PRO HB2 H 1 1.979 0.005 . 2 . . . . . . . . 5650 1 374 . 1 1 32 32 PRO HB3 H 1 2.269 0.005 . 2 . . . . . . . . 5650 1 375 . 1 1 32 32 PRO CG C 13 25.854 0.050 . 1 . . . . . . . . 5650 1 376 . 1 1 32 32 PRO HG2 H 1 1.847 0.005 . 2 . . . . . . . . 5650 1 377 . 1 1 32 32 PRO HG3 H 1 1.934 0.005 . 2 . . . . . . . . 5650 1 378 . 1 1 32 32 PRO CD C 13 48.528 0.050 . 1 . . . . . . . . 5650 1 379 . 1 1 32 32 PRO HD2 H 1 2.746 0.005 . 2 . . . . . . . . 5650 1 380 . 1 1 32 32 PRO HD3 H 1 3.750 0.005 . 2 . . . . . . . . 5650 1 381 . 1 1 33 33 LYS N N 15 118.566 0.050 . 1 . . . . . . . . 5650 1 382 . 1 1 33 33 LYS H H 1 10.290 0.005 . 1 . . . . . . . . 5650 1 383 . 1 1 33 33 LYS CA C 13 53.327 0.050 . 1 . . . . . . . . 5650 1 384 . 1 1 33 33 LYS HA H 1 4.508 0.005 . 1 . . . . . . . . 5650 1 385 . 1 1 33 33 LYS C C 13 174.646 0.050 . 1 . . . . . . . . 5650 1 386 . 1 1 33 33 LYS CB C 13 30.091 0.050 . 1 . . . . . . . . 5650 1 387 . 1 1 33 33 LYS HB2 H 1 1.799 0.005 . 2 . . . . . . . . 5650 1 388 . 1 1 33 33 LYS HB3 H 1 2.078 0.005 . 2 . . . . . . . . 5650 1 389 . 1 1 33 33 LYS CG C 13 23.294 0.050 . 1 . . . . . . . . 5650 1 390 . 1 1 33 33 LYS HG2 H 1 1.518 0.005 . 2 . . . . . . . . 5650 1 391 . 1 1 33 33 LYS HG3 H 1 1.639 0.005 . 2 . . . . . . . . 5650 1 392 . 1 1 33 33 LYS CD C 13 26.700 0.050 . 1 . . . . . . . . 5650 1 393 . 1 1 33 33 LYS CE C 13 40.008 0.050 . 1 . . . . . . . . 5650 1 394 . 1 1 33 33 LYS HZ1 H 1 7.736 0.005 . 1 . . . . . . . . 5650 1 395 . 1 1 33 33 LYS HZ2 H 1 7.736 0.005 . 1 . . . . . . . . 5650 1 396 . 1 1 33 33 LYS HZ3 H 1 7.736 0.005 . 1 . . . . . . . . 5650 1 397 . 1 1 33 33 LYS HD3 H 1 1.756 0.005 . 1 . . . . . . . . 5650 1 398 . 1 1 33 33 LYS HE3 H 1 3.078 0.005 . 1 . . . . . . . . 5650 1 399 . 1 1 33 33 LYS HD2 H 1 1.756 0.005 . 1 . . . . . . . . 5650 1 400 . 1 1 33 33 LYS HE2 H 1 3.078 0.005 . 1 . . . . . . . . 5650 1 401 . 1 1 34 34 ALA N N 15 122.791 0.050 . 1 . . . . . . . . 5650 1 402 . 1 1 34 34 ALA H H 1 8.050 0.005 . 1 . . . . . . . . 5650 1 403 . 1 1 34 34 ALA CA C 13 50.495 0.050 . 1 . . . . . . . . 5650 1 404 . 1 1 34 34 ALA HA H 1 4.624 0.005 . 1 . . . . . . . . 5650 1 405 . 1 1 34 34 ALA C C 13 173.993 0.050 . 1 . . . . . . . . 5650 1 406 . 1 1 34 34 ALA CB C 13 17.967 0.050 . 1 . . . . . . . . 5650 1 407 . 1 1 34 34 ALA HB1 H 1 1.523 0.005 . 1 . . . . . . . . 5650 1 408 . 1 1 34 34 ALA HB2 H 1 1.523 0.005 . 1 . . . . . . . . 5650 1 409 . 1 1 34 34 ALA HB3 H 1 1.523 0.005 . 1 . . . . . . . . 5650 1 410 . 1 1 35 35 THR N N 15 114.382 0.050 . 1 . . . . . . . . 5650 1 411 . 1 1 35 35 THR H H 1 8.745 0.005 . 1 . . . . . . . . 5650 1 412 . 1 1 35 35 THR CA C 13 57.785 0.050 . 1 . . . . . . . . 5650 1 413 . 1 1 35 35 THR HA H 1 4.689 0.005 . 1 . . . . . . . . 5650 1 414 . 1 1 35 35 THR C C 13 176.245 0.050 . 1 . . . . . . . . 5650 1 415 . 1 1 35 35 THR CB C 13 69.224 0.050 . 1 . . . . . . . . 5650 1 416 . 1 1 35 35 THR HB H 1 4.882 0.005 . 1 . . . . . . . . 5650 1 417 . 1 1 35 35 THR CG2 C 13 19.570 0.050 . 1 . . . . . . . . 5650 1 418 . 1 1 35 35 THR HG21 H 1 1.416 0.005 . 1 . . . . . . . . 5650 1 419 . 1 1 35 35 THR HG22 H 1 1.416 0.005 . 1 . . . . . . . . 5650 1 420 . 1 1 35 35 THR HG23 H 1 1.416 0.005 . 1 . . . . . . . . 5650 1 421 . 1 1 36 36 LYS N N 15 119.663 0.050 . 1 . . . . . . . . 5650 1 422 . 1 1 36 36 LYS H H 1 9.190 0.005 . 1 . . . . . . . . 5650 1 423 . 1 1 36 36 LYS CA C 13 59.627 0.050 . 1 . . . . . . . . 5650 1 424 . 1 1 36 36 LYS HA H 1 3.823 0.005 . 1 . . . . . . . . 5650 1 425 . 1 1 36 36 LYS C C 13 173.102 0.050 . 1 . . . . . . . . 5650 1 426 . 1 1 36 36 LYS CB C 13 30.008 0.050 . 1 . . . . . . . . 5650 1 427 . 1 1 36 36 LYS HB2 H 1 1.813 0.005 . 2 . . . . . . . . 5650 1 428 . 1 1 36 36 LYS HB3 H 1 2.026 0.005 . 2 . . . . . . . . 5650 1 429 . 1 1 36 36 LYS CG C 13 24.782 0.050 . 1 . . . . . . . . 5650 1 430 . 1 1 36 36 LYS HG2 H 1 1.244 0.005 . 2 . . . . . . . . 5650 1 431 . 1 1 36 36 LYS HG3 H 1 1.859 0.005 . 2 . . . . . . . . 5650 1 432 . 1 1 36 36 LYS CD C 13 27.477 0.050 . 1 . . . . . . . . 5650 1 433 . 1 1 36 36 LYS HD2 H 1 1.862 0.005 . 2 . . . . . . . . 5650 1 434 . 1 1 36 36 LYS HD3 H 1 1.955 0.005 . 2 . . . . . . . . 5650 1 435 . 1 1 36 36 LYS CE C 13 40.216 0.050 . 1 . . . . . . . . 5650 1 436 . 1 1 36 36 LYS HE3 H 1 3.209 0.005 . 1 . . . . . . . . 5650 1 437 . 1 1 36 36 LYS HE2 H 1 3.209 0.005 . 1 . . . . . . . . 5650 1 438 . 1 1 37 37 THR N N 15 114.693 0.050 . 1 . . . . . . . . 5650 1 439 . 1 1 37 37 THR H H 1 8.202 0.005 . 1 . . . . . . . . 5650 1 440 . 1 1 37 37 THR CA C 13 64.590 0.050 . 1 . . . . . . . . 5650 1 441 . 1 1 37 37 THR HA H 1 3.895 0.005 . 1 . . . . . . . . 5650 1 442 . 1 1 37 37 THR C C 13 176.285 0.050 . 1 . . . . . . . . 5650 1 443 . 1 1 37 37 THR CB C 13 66.441 0.050 . 1 . . . . . . . . 5650 1 444 . 1 1 37 37 THR HB H 1 4.079 0.005 . 1 . . . . . . . . 5650 1 445 . 1 1 37 37 THR CG2 C 13 19.933 0.050 . 1 . . . . . . . . 5650 1 446 . 1 1 37 37 THR HG21 H 1 1.269 0.005 . 1 . . . . . . . . 5650 1 447 . 1 1 37 37 THR HG22 H 1 1.269 0.005 . 1 . . . . . . . . 5650 1 448 . 1 1 37 37 THR HG23 H 1 1.269 0.005 . 1 . . . . . . . . 5650 1 449 . 1 1 38 38 GLU N N 15 121.755 0.050 . 1 . . . . . . . . 5650 1 450 . 1 1 38 38 GLU H H 1 7.698 0.005 . 1 . . . . . . . . 5650 1 451 . 1 1 38 38 GLU CA C 13 57.209 0.050 . 1 . . . . . . . . 5650 1 452 . 1 1 38 38 GLU HA H 1 4.021 0.005 . 1 . . . . . . . . 5650 1 453 . 1 1 38 38 GLU C C 13 172.180 0.050 . 1 . . . . . . . . 5650 1 454 . 1 1 38 38 GLU CB C 13 27.650 0.050 . 1 . . . . . . . . 5650 1 455 . 1 1 38 38 GLU HB2 H 1 1.939 0.005 . 2 . . . . . . . . 5650 1 456 . 1 1 38 38 GLU HB3 H 1 2.455 0.005 . 2 . . . . . . . . 5650 1 457 . 1 1 38 38 GLU CG C 13 35.151 0.050 . 1 . . . . . . . . 5650 1 458 . 1 1 38 38 GLU HG2 H 1 2.330 0.005 . 2 . . . . . . . . 5650 1 459 . 1 1 38 38 GLU HG3 H 1 2.439 0.005 . 2 . . . . . . . . 5650 1 460 . 1 1 39 39 ILE N N 15 120.388 0.050 . 1 . . . . . . . . 5650 1 461 . 1 1 39 39 ILE H H 1 8.492 0.005 . 1 . . . . . . . . 5650 1 462 . 1 1 39 39 ILE CA C 13 63.654 0.050 . 1 . . . . . . . . 5650 1 463 . 1 1 39 39 ILE HA H 1 3.421 0.005 . 1 . . . . . . . . 5650 1 464 . 1 1 39 39 ILE C C 13 175.826 0.050 . 1 . . . . . . . . 5650 1 465 . 1 1 39 39 ILE CB C 13 36.267 0.050 . 1 . . . . . . . . 5650 1 466 . 1 1 39 39 ILE HB H 1 1.813 0.005 . 1 . . . . . . . . 5650 1 467 . 1 1 39 39 ILE CG1 C 13 27.256 0.050 . 1 . . . . . . . . 5650 1 468 . 1 1 39 39 ILE HG12 H 1 0.538 0.005 . 2 . . . . . . . . 5650 1 469 . 1 1 39 39 ILE HG13 H 1 1.880 0.005 . 2 . . . . . . . . 5650 1 470 . 1 1 39 39 ILE CG2 C 13 15.338 0.050 . 1 . . . . . . . . 5650 1 471 . 1 1 39 39 ILE HG21 H 1 0.625 0.005 . 1 . . . . . . . . 5650 1 472 . 1 1 39 39 ILE HG22 H 1 0.625 0.005 . 1 . . . . . . . . 5650 1 473 . 1 1 39 39 ILE HG23 H 1 0.625 0.005 . 1 . . . . . . . . 5650 1 474 . 1 1 39 39 ILE CD1 C 13 12.967 0.050 . 1 . . . . . . . . 5650 1 475 . 1 1 39 39 ILE HD11 H 1 0.655 0.005 . 1 . . . . . . . . 5650 1 476 . 1 1 39 39 ILE HD12 H 1 0.655 0.005 . 1 . . . . . . . . 5650 1 477 . 1 1 39 39 ILE HD13 H 1 0.655 0.005 . 1 . . . . . . . . 5650 1 478 . 1 1 40 40 LYS N N 15 119.454 0.050 . 1 . . . . . . . . 5650 1 479 . 1 1 40 40 LYS H H 1 8.254 0.005 . 1 . . . . . . . . 5650 1 480 . 1 1 40 40 LYS CA C 13 58.575 0.050 . 1 . . . . . . . . 5650 1 481 . 1 1 40 40 LYS HA H 1 3.588 0.005 . 1 . . . . . . . . 5650 1 482 . 1 1 40 40 LYS C C 13 174.862 0.050 . 1 . . . . . . . . 5650 1 483 . 1 1 40 40 LYS CB C 13 30.575 0.050 . 1 . . . . . . . . 5650 1 484 . 1 1 40 40 LYS HB2 H 1 1.830 0.005 . 2 . . . . . . . . 5650 1 485 . 1 1 40 40 LYS HB3 H 1 2.079 0.005 . 2 . . . . . . . . 5650 1 486 . 1 1 40 40 LYS CG C 13 22.289 0.050 . 1 . . . . . . . . 5650 1 487 . 1 1 40 40 LYS CD C 13 27.801 0.050 . 1 . . . . . . . . 5650 1 488 . 1 1 40 40 LYS CE C 13 40.060 0.050 . 1 . . . . . . . . 5650 1 489 . 1 1 40 40 LYS HG2 H 1 1.254 0.005 . 1 . . . . . . . . 5650 1 490 . 1 1 40 40 LYS HD3 H 1 1.670 0.005 . 1 . . . . . . . . 5650 1 491 . 1 1 40 40 LYS HE3 H 1 3.091 0.005 . 1 . . . . . . . . 5650 1 492 . 1 1 40 40 LYS HG3 H 1 1.254 0.005 . 1 . . . . . . . . 5650 1 493 . 1 1 40 40 LYS HD2 H 1 1.670 0.005 . 1 . . . . . . . . 5650 1 494 . 1 1 40 40 LYS HE2 H 1 3.091 0.005 . 1 . . . . . . . . 5650 1 495 . 1 1 41 41 ASN N N 15 114.978 0.050 . 1 . . . . . . . . 5650 1 496 . 1 1 41 41 ASN H H 1 8.288 0.005 . 1 . . . . . . . . 5650 1 497 . 1 1 41 41 ASN CA C 13 54.088 0.050 . 1 . . . . . . . . 5650 1 498 . 1 1 41 41 ASN HA H 1 4.485 0.005 . 1 . . . . . . . . 5650 1 499 . 1 1 41 41 ASN C C 13 174.312 0.050 . 1 . . . . . . . . 5650 1 500 . 1 1 41 41 ASN CB C 13 36.238 0.050 . 1 . . . . . . . . 5650 1 501 . 1 1 41 41 ASN ND2 N 15 111.424 0.050 . 1 . . . . . . . . 5650 1 502 . 1 1 41 41 ASN HD21 H 1 6.922 0.005 . 1 . . . . . . . . 5650 1 503 . 1 1 41 41 ASN HD22 H 1 7.633 0.005 . 1 . . . . . . . . 5650 1 504 . 1 1 41 41 ASN HB2 H 1 2.828 0.005 . 1 . . . . . . . . 5650 1 505 . 1 1 41 41 ASN HB3 H 1 2.828 0.005 . 1 . . . . . . . . 5650 1 506 . 1 1 42 42 ALA N N 15 123.106 0.050 . 1 . . . . . . . . 5650 1 507 . 1 1 42 42 ALA H H 1 8.356 0.005 . 1 . . . . . . . . 5650 1 508 . 1 1 42 42 ALA CA C 13 53.152 0.050 . 1 . . . . . . . . 5650 1 509 . 1 1 42 42 ALA HA H 1 4.081 0.005 . 1 . . . . . . . . 5650 1 510 . 1 1 42 42 ALA C C 13 172.871 0.050 . 1 . . . . . . . . 5650 1 511 . 1 1 42 42 ALA CB C 13 16.660 0.050 . 1 . . . . . . . . 5650 1 512 . 1 1 42 42 ALA HB1 H 1 1.489 0.005 . 1 . . . . . . . . 5650 1 513 . 1 1 42 42 ALA HB2 H 1 1.489 0.005 . 1 . . . . . . . . 5650 1 514 . 1 1 42 42 ALA HB3 H 1 1.489 0.005 . 1 . . . . . . . . 5650 1 515 . 1 1 43 43 VAL N N 15 117.721 0.050 . 1 . . . . . . . . 5650 1 516 . 1 1 43 43 VAL H H 1 8.165 0.005 . 1 . . . . . . . . 5650 1 517 . 1 1 43 43 VAL CA C 13 64.300 0.050 . 1 . . . . . . . . 5650 1 518 . 1 1 43 43 VAL HA H 1 3.494 0.005 . 1 . . . . . . . . 5650 1 519 . 1 1 43 43 VAL C C 13 174.466 0.050 . 1 . . . . . . . . 5650 1 520 . 1 1 43 43 VAL CB C 13 29.560 0.050 . 1 . . . . . . . . 5650 1 521 . 1 1 43 43 VAL HB H 1 2.037 0.005 . 1 . . . . . . . . 5650 1 522 . 1 1 43 43 VAL CG1 C 13 21.370 0.050 . 2 . . . . . . . . 5650 1 523 . 1 1 43 43 VAL HG11 H 1 0.692 0.005 . 2 . . . . . . . . 5650 1 524 . 1 1 43 43 VAL HG12 H 1 0.692 0.005 . 2 . . . . . . . . 5650 1 525 . 1 1 43 43 VAL HG13 H 1 0.692 0.005 . 2 . . . . . . . . 5650 1 526 . 1 1 43 43 VAL CG2 C 13 19.520 0.050 . 2 . . . . . . . . 5650 1 527 . 1 1 43 43 VAL HG21 H 1 0.788 0.005 . 2 . . . . . . . . 5650 1 528 . 1 1 43 43 VAL HG22 H 1 0.788 0.005 . 2 . . . . . . . . 5650 1 529 . 1 1 43 43 VAL HG23 H 1 0.788 0.005 . 2 . . . . . . . . 5650 1 530 . 1 1 44 44 GLU N N 15 117.889 0.050 . 1 . . . . . . . . 5650 1 531 . 1 1 44 44 GLU H H 1 8.401 0.005 . 1 . . . . . . . . 5650 1 532 . 1 1 44 44 GLU CA C 13 58.714 0.050 . 1 . . . . . . . . 5650 1 533 . 1 1 44 44 GLU HA H 1 4.197 0.005 . 1 . . . . . . . . 5650 1 534 . 1 1 44 44 GLU C C 13 171.754 0.050 . 1 . . . . . . . . 5650 1 535 . 1 1 44 44 GLU CB C 13 27.262 0.050 . 1 . . . . . . . . 5650 1 536 . 1 1 44 44 GLU HB2 H 1 2.090 0.005 . 2 . . . . . . . . 5650 1 537 . 1 1 44 44 GLU HB3 H 1 2.206 0.005 . 2 . . . . . . . . 5650 1 538 . 1 1 44 44 GLU CG C 13 35.379 0.050 . 1 . . . . . . . . 5650 1 539 . 1 1 44 44 GLU HG2 H 1 2.804 0.005 . 2 . . . . . . . . 5650 1 540 . 1 1 44 44 GLU HG3 H 1 2.872 0.005 . 2 . . . . . . . . 5650 1 541 . 1 1 45 45 THR N N 15 112.743 0.050 . 1 . . . . . . . . 5650 1 542 . 1 1 45 45 THR H H 1 8.131 0.005 . 1 . . . . . . . . 5650 1 543 . 1 1 45 45 THR CA C 13 63.639 0.050 . 1 . . . . . . . . 5650 1 544 . 1 1 45 45 THR HA H 1 3.993 0.005 . 1 . . . . . . . . 5650 1 545 . 1 1 45 45 THR C C 13 176.578 0.050 . 1 . . . . . . . . 5650 1 546 . 1 1 45 45 THR CB C 13 66.955 0.050 . 1 . . . . . . . . 5650 1 547 . 1 1 45 45 THR HB H 1 4.121 0.005 . 1 . . . . . . . . 5650 1 548 . 1 1 45 45 THR CG2 C 13 19.100 0.050 . 1 . . . . . . . . 5650 1 549 . 1 1 45 45 THR HG21 H 1 1.231 0.005 . 1 . . . . . . . . 5650 1 550 . 1 1 45 45 THR HG22 H 1 1.231 0.005 . 1 . . . . . . . . 5650 1 551 . 1 1 45 45 THR HG23 H 1 1.231 0.005 . 1 . . . . . . . . 5650 1 552 . 1 1 46 46 ALA N N 15 121.222 0.050 . 1 . . . . . . . . 5650 1 553 . 1 1 46 46 ALA H H 1 7.943 0.005 . 1 . . . . . . . . 5650 1 554 . 1 1 46 46 ALA CA C 13 52.507 0.050 . 1 . . . . . . . . 5650 1 555 . 1 1 46 46 ALA HA H 1 3.799 0.005 . 1 . . . . . . . . 5650 1 556 . 1 1 46 46 ALA C C 13 172.820 0.050 . 1 . . . . . . . . 5650 1 557 . 1 1 46 46 ALA CB C 13 15.927 0.050 . 1 . . . . . . . . 5650 1 558 . 1 1 46 46 ALA HB1 H 1 0.541 0.005 . 1 . . . . . . . . 5650 1 559 . 1 1 46 46 ALA HB2 H 1 0.541 0.005 . 1 . . . . . . . . 5650 1 560 . 1 1 46 46 ALA HB3 H 1 0.541 0.005 . 1 . . . . . . . . 5650 1 561 . 1 1 47 47 PHE N N 15 110.562 0.050 . 1 . . . . . . . . 5650 1 562 . 1 1 47 47 PHE H H 1 7.922 0.005 . 1 . . . . . . . . 5650 1 563 . 1 1 47 47 PHE CA C 13 54.905 0.050 . 1 . . . . . . . . 5650 1 564 . 1 1 47 47 PHE HA H 1 4.901 0.005 . 1 . . . . . . . . 5650 1 565 . 1 1 47 47 PHE C C 13 177.412 0.050 . 1 . . . . . . . . 5650 1 566 . 1 1 47 47 PHE CB C 13 37.971 0.050 . 1 . . . . . . . . 5650 1 567 . 1 1 47 47 PHE HB2 H 1 2.740 0.005 . 2 . . . . . . . . 5650 1 568 . 1 1 47 47 PHE HB3 H 1 3.381 0.005 . 2 . . . . . . . . 5650 1 569 . 1 1 47 47 PHE HD1 H 1 7.329 0.005 . 1 . . . . . . . . 5650 1 570 . 1 1 47 47 PHE HE1 H 1 7.078 0.005 . 1 . . . . . . . . 5650 1 571 . 1 1 47 47 PHE HD2 H 1 7.329 0.005 . 1 . . . . . . . . 5650 1 572 . 1 1 47 47 PHE HE2 H 1 7.078 0.005 . 1 . . . . . . . . 5650 1 573 . 1 1 48 48 LYS N N 15 116.500 0.050 . 1 . . . . . . . . 5650 1 574 . 1 1 48 48 LYS H H 1 7.743 0.005 . 1 . . . . . . . . 5650 1 575 . 1 1 48 48 LYS CA C 13 55.128 0.050 . 1 . . . . . . . . 5650 1 576 . 1 1 48 48 LYS HA H 1 4.154 0.005 . 1 . . . . . . . . 5650 1 577 . 1 1 48 48 LYS C C 13 176.879 0.050 . 1 . . . . . . . . 5650 1 578 . 1 1 48 48 LYS CB C 13 26.186 0.050 . 1 . . . . . . . . 5650 1 579 . 1 1 48 48 LYS HB2 H 1 1.970 0.005 . 2 . . . . . . . . 5650 1 580 . 1 1 48 48 LYS HB3 H 1 2.132 0.005 . 2 . . . . . . . . 5650 1 581 . 1 1 48 48 LYS CG C 13 22.891 0.050 . 1 . . . . . . . . 5650 1 582 . 1 1 48 48 LYS CD C 13 26.862 0.050 . 1 . . . . . . . . 5650 1 583 . 1 1 48 48 LYS CE C 13 40.432 0.050 . 1 . . . . . . . . 5650 1 584 . 1 1 48 48 LYS HG2 H 1 1.390 0.005 . 1 . . . . . . . . 5650 1 585 . 1 1 48 48 LYS HD3 H 1 1.735 0.005 . 1 . . . . . . . . 5650 1 586 . 1 1 48 48 LYS HE3 H 1 3.103 0.005 . 1 . . . . . . . . 5650 1 587 . 1 1 48 48 LYS HG3 H 1 1.390 0.005 . 1 . . . . . . . . 5650 1 588 . 1 1 48 48 LYS HD2 H 1 1.735 0.005 . 1 . . . . . . . . 5650 1 589 . 1 1 48 48 LYS HE2 H 1 3.103 0.005 . 1 . . . . . . . . 5650 1 590 . 1 1 49 49 VAL N N 15 108.589 0.050 . 1 . . . . . . . . 5650 1 591 . 1 1 49 49 VAL H H 1 6.880 0.005 . 1 . . . . . . . . 5650 1 592 . 1 1 49 49 VAL CA C 13 56.086 0.050 . 1 . . . . . . . . 5650 1 593 . 1 1 49 49 VAL HA H 1 4.705 0.005 . 1 . . . . . . . . 5650 1 594 . 1 1 49 49 VAL C C 13 177.965 0.050 . 1 . . . . . . . . 5650 1 595 . 1 1 49 49 VAL CB C 13 33.301 0.050 . 1 . . . . . . . . 5650 1 596 . 1 1 49 49 VAL HB H 1 2.143 0.005 . 1 . . . . . . . . 5650 1 597 . 1 1 49 49 VAL CG1 C 13 16.366 0.050 . 2 . . . . . . . . 5650 1 598 . 1 1 49 49 VAL HG11 H 1 0.571 0.005 . 2 . . . . . . . . 5650 1 599 . 1 1 49 49 VAL HG12 H 1 0.571 0.005 . 2 . . . . . . . . 5650 1 600 . 1 1 49 49 VAL HG13 H 1 0.571 0.005 . 2 . . . . . . . . 5650 1 601 . 1 1 49 49 VAL CG2 C 13 19.980 0.050 . 2 . . . . . . . . 5650 1 602 . 1 1 49 49 VAL HG21 H 1 0.819 0.005 . 2 . . . . . . . . 5650 1 603 . 1 1 49 49 VAL HG22 H 1 0.819 0.005 . 2 . . . . . . . . 5650 1 604 . 1 1 49 49 VAL HG23 H 1 0.819 0.005 . 2 . . . . . . . . 5650 1 605 . 1 1 50 50 LYS N N 15 122.045 0.050 . 1 . . . . . . . . 5650 1 606 . 1 1 50 50 LYS H H 1 9.044 0.005 . 1 . . . . . . . . 5650 1 607 . 1 1 50 50 LYS CA C 13 52.654 0.050 . 1 . . . . . . . . 5650 1 608 . 1 1 50 50 LYS HA H 1 4.628 0.005 . 1 . . . . . . . . 5650 1 609 . 1 1 50 50 LYS C C 13 176.627 0.050 . 1 . . . . . . . . 5650 1 610 . 1 1 50 50 LYS CB C 13 31.293 0.050 . 1 . . . . . . . . 5650 1 611 . 1 1 50 50 LYS HB2 H 1 1.743 0.005 . 2 . . . . . . . . 5650 1 612 . 1 1 50 50 LYS HB3 H 1 1.781 0.005 . 2 . . . . . . . . 5650 1 613 . 1 1 50 50 LYS CG C 13 22.654 0.050 . 1 . . . . . . . . 5650 1 614 . 1 1 50 50 LYS HG2 H 1 1.268 0.005 . 2 . . . . . . . . 5650 1 615 . 1 1 50 50 LYS HG3 H 1 1.444 0.005 . 2 . . . . . . . . 5650 1 616 . 1 1 50 50 LYS CD C 13 26.706 0.050 . 1 . . . . . . . . 5650 1 617 . 1 1 50 50 LYS CE C 13 40.012 0.050 . 1 . . . . . . . . 5650 1 618 . 1 1 50 50 LYS HD3 H 1 1.682 0.005 . 1 . . . . . . . . 5650 1 619 . 1 1 50 50 LYS HE3 H 1 2.988 0.005 . 1 . . . . . . . . 5650 1 620 . 1 1 50 50 LYS HD2 H 1 1.682 0.005 . 1 . . . . . . . . 5650 1 621 . 1 1 50 50 LYS HE2 H 1 2.988 0.005 . 1 . . . . . . . . 5650 1 622 . 1 1 51 51 VAL N N 15 126.431 0.050 . 1 . . . . . . . . 5650 1 623 . 1 1 51 51 VAL H H 1 9.828 0.005 . 1 . . . . . . . . 5650 1 624 . 1 1 51 51 VAL CA C 13 60.165 0.050 . 1 . . . . . . . . 5650 1 625 . 1 1 51 51 VAL HA H 1 4.280 0.005 . 1 . . . . . . . . 5650 1 626 . 1 1 51 51 VAL C C 13 176.193 0.050 . 1 . . . . . . . . 5650 1 627 . 1 1 51 51 VAL CB C 13 30.829 0.050 . 1 . . . . . . . . 5650 1 628 . 1 1 51 51 VAL HB H 1 2.082 0.005 . 1 . . . . . . . . 5650 1 629 . 1 1 51 51 VAL CG1 C 13 20.706 0.050 . 2 . . . . . . . . 5650 1 630 . 1 1 51 51 VAL HG11 H 1 0.881 0.005 . 2 . . . . . . . . 5650 1 631 . 1 1 51 51 VAL HG12 H 1 0.881 0.005 . 2 . . . . . . . . 5650 1 632 . 1 1 51 51 VAL HG13 H 1 0.881 0.005 . 2 . . . . . . . . 5650 1 633 . 1 1 51 51 VAL CG2 C 13 21.215 0.050 . 2 . . . . . . . . 5650 1 634 . 1 1 51 51 VAL HG21 H 1 0.962 0.005 . 2 . . . . . . . . 5650 1 635 . 1 1 51 51 VAL HG22 H 1 0.962 0.005 . 2 . . . . . . . . 5650 1 636 . 1 1 51 51 VAL HG23 H 1 0.962 0.005 . 2 . . . . . . . . 5650 1 637 . 1 1 52 52 VAL N N 15 120.634 0.050 . 1 . . . . . . . . 5650 1 638 . 1 1 52 52 VAL H H 1 8.989 0.005 . 1 . . . . . . . . 5650 1 639 . 1 1 52 52 VAL CA C 13 59.767 0.050 . 1 . . . . . . . . 5650 1 640 . 1 1 52 52 VAL HA H 1 4.442 0.005 . 1 . . . . . . . . 5650 1 641 . 1 1 52 52 VAL C C 13 176.177 0.050 . 1 . . . . . . . . 5650 1 642 . 1 1 52 52 VAL CB C 13 30.741 0.050 . 1 . . . . . . . . 5650 1 643 . 1 1 52 52 VAL HB H 1 2.148 0.005 . 1 . . . . . . . . 5650 1 644 . 1 1 52 52 VAL CG1 C 13 16.988 0.050 . 2 . . . . . . . . 5650 1 645 . 1 1 52 52 VAL HG11 H 1 0.792 0.005 . 2 . . . . . . . . 5650 1 646 . 1 1 52 52 VAL HG12 H 1 0.792 0.005 . 2 . . . . . . . . 5650 1 647 . 1 1 52 52 VAL HG13 H 1 0.792 0.005 . 2 . . . . . . . . 5650 1 648 . 1 1 52 52 VAL CG2 C 13 19.108 0.050 . 2 . . . . . . . . 5650 1 649 . 1 1 52 52 VAL HG21 H 1 0.931 0.005 . 2 . . . . . . . . 5650 1 650 . 1 1 52 52 VAL HG22 H 1 0.931 0.005 . 2 . . . . . . . . 5650 1 651 . 1 1 52 52 VAL HG23 H 1 0.931 0.005 . 2 . . . . . . . . 5650 1 652 . 1 1 53 53 LYS N N 15 120.016 0.050 . 1 . . . . . . . . 5650 1 653 . 1 1 53 53 LYS H H 1 7.591 0.005 . 1 . . . . . . . . 5650 1 654 . 1 1 53 53 LYS CA C 13 54.555 0.050 . 1 . . . . . . . . 5650 1 655 . 1 1 53 53 LYS HA H 1 4.623 0.005 . 1 . . . . . . . . 5650 1 656 . 1 1 53 53 LYS C C 13 178.419 0.050 . 1 . . . . . . . . 5650 1 657 . 1 1 53 53 LYS CB C 13 34.460 0.050 . 1 . . . . . . . . 5650 1 658 . 1 1 53 53 LYS CG C 13 22.878 0.050 . 1 . . . . . . . . 5650 1 659 . 1 1 53 53 LYS CD C 13 27.072 0.050 . 1 . . . . . . . . 5650 1 660 . 1 1 53 53 LYS CE C 13 39.940 0.050 . 1 . . . . . . . . 5650 1 661 . 1 1 53 53 LYS HB2 H 1 1.847 0.005 . 1 . . . . . . . . 5650 1 662 . 1 1 53 53 LYS HG2 H 1 1.447 0.005 . 1 . . . . . . . . 5650 1 663 . 1 1 53 53 LYS HD3 H 1 1.735 0.005 . 1 . . . . . . . . 5650 1 664 . 1 1 53 53 LYS HE3 H 1 3.050 0.005 . 1 . . . . . . . . 5650 1 665 . 1 1 53 53 LYS HB3 H 1 1.847 0.005 . 1 . . . . . . . . 5650 1 666 . 1 1 53 53 LYS HG3 H 1 1.447 0.005 . 1 . . . . . . . . 5650 1 667 . 1 1 53 53 LYS HD2 H 1 1.735 0.005 . 1 . . . . . . . . 5650 1 668 . 1 1 53 53 LYS HE2 H 1 3.050 0.005 . 1 . . . . . . . . 5650 1 669 . 1 1 54 54 VAL N N 15 122.708 0.050 . 1 . . . . . . . . 5650 1 670 . 1 1 54 54 VAL H H 1 8.527 0.005 . 1 . . . . . . . . 5650 1 671 . 1 1 54 54 VAL CA C 13 59.444 0.050 . 1 . . . . . . . . 5650 1 672 . 1 1 54 54 VAL HA H 1 4.724 0.005 . 1 . . . . . . . . 5650 1 673 . 1 1 54 54 VAL C C 13 178.363 0.050 . 1 . . . . . . . . 5650 1 674 . 1 1 54 54 VAL CB C 13 33.230 0.050 . 1 . . . . . . . . 5650 1 675 . 1 1 54 54 VAL HB H 1 1.943 0.005 . 1 . . . . . . . . 5650 1 676 . 1 1 54 54 VAL CG1 C 13 19.798 0.050 . 2 . . . . . . . . 5650 1 677 . 1 1 54 54 VAL HG11 H 1 0.907 0.005 . 2 . . . . . . . . 5650 1 678 . 1 1 54 54 VAL HG12 H 1 0.907 0.005 . 2 . . . . . . . . 5650 1 679 . 1 1 54 54 VAL HG13 H 1 0.907 0.005 . 2 . . . . . . . . 5650 1 680 . 1 1 54 54 VAL CG2 C 13 19.615 0.050 . 2 . . . . . . . . 5650 1 681 . 1 1 54 54 VAL HG21 H 1 0.959 0.005 . 2 . . . . . . . . 5650 1 682 . 1 1 54 54 VAL HG22 H 1 0.959 0.005 . 2 . . . . . . . . 5650 1 683 . 1 1 54 54 VAL HG23 H 1 0.959 0.005 . 2 . . . . . . . . 5650 1 684 . 1 1 55 55 ASN N N 15 124.136 0.050 . 1 . . . . . . . . 5650 1 685 . 1 1 55 55 ASN H H 1 8.877 0.005 . 1 . . . . . . . . 5650 1 686 . 1 1 55 55 ASN CA C 13 50.131 0.050 . 1 . . . . . . . . 5650 1 687 . 1 1 55 55 ASN HA H 1 5.264 0.005 . 1 . . . . . . . . 5650 1 688 . 1 1 55 55 ASN C C 13 177.583 0.050 . 1 . . . . . . . . 5650 1 689 . 1 1 55 55 ASN CB C 13 40.001 0.050 . 1 . . . . . . . . 5650 1 690 . 1 1 55 55 ASN HB2 H 1 2.615 0.005 . 2 . . . . . . . . 5650 1 691 . 1 1 55 55 ASN HB3 H 1 2.865 0.005 . 2 . . . . . . . . 5650 1 692 . 1 1 55 55 ASN ND2 N 15 111.437 0.050 . 1 . . . . . . . . 5650 1 693 . 1 1 55 55 ASN HD21 H 1 6.938 0.005 . 1 . . . . . . . . 5650 1 694 . 1 1 55 55 ASN HD22 H 1 7.572 0.005 . 1 . . . . . . . . 5650 1 695 . 1 1 56 56 THR N N 15 112.778 0.050 . 1 . . . . . . . . 5650 1 696 . 1 1 56 56 THR H H 1 8.781 0.005 . 1 . . . . . . . . 5650 1 697 . 1 1 56 56 THR CA C 13 57.694 0.050 . 1 . . . . . . . . 5650 1 698 . 1 1 56 56 THR HA H 1 5.276 0.005 . 1 . . . . . . . . 5650 1 699 . 1 1 56 56 THR C C 13 178.558 0.050 . 1 . . . . . . . . 5650 1 700 . 1 1 56 56 THR CB C 13 68.993 0.050 . 1 . . . . . . . . 5650 1 701 . 1 1 56 56 THR HB H 1 4.079 0.005 . 1 . . . . . . . . 5650 1 702 . 1 1 56 56 THR CG2 C 13 20.199 0.050 . 1 . . . . . . . . 5650 1 703 . 1 1 56 56 THR HG21 H 1 1.045 0.005 . 1 . . . . . . . . 5650 1 704 . 1 1 56 56 THR HG22 H 1 1.045 0.005 . 1 . . . . . . . . 5650 1 705 . 1 1 56 56 THR HG23 H 1 1.045 0.005 . 1 . . . . . . . . 5650 1 706 . 1 1 57 57 LEU N N 15 121.451 0.050 . 1 . . . . . . . . 5650 1 707 . 1 1 57 57 LEU H H 1 8.729 0.005 . 1 . . . . . . . . 5650 1 708 . 1 1 57 57 LEU CA C 13 52.385 0.050 . 1 . . . . . . . . 5650 1 709 . 1 1 57 57 LEU HA H 1 4.727 0.005 . 1 . . . . . . . . 5650 1 710 . 1 1 57 57 LEU C C 13 176.290 0.050 . 1 . . . . . . . . 5650 1 711 . 1 1 57 57 LEU CB C 13 42.372 0.050 . 1 . . . . . . . . 5650 1 712 . 1 1 57 57 LEU HB2 H 1 1.530 0.005 . 2 . . . . . . . . 5650 1 713 . 1 1 57 57 LEU HB3 H 1 1.668 0.005 . 2 . . . . . . . . 5650 1 714 . 1 1 57 57 LEU CG C 13 24.984 0.050 . 1 . . . . . . . . 5650 1 715 . 1 1 57 57 LEU HG H 1 1.550 0.005 . 1 . . . . . . . . 5650 1 716 . 1 1 57 57 LEU CD1 C 13 22.868 0.050 . 1 . . . . . . . . 5650 1 717 . 1 1 57 57 LEU HD11 H 1 0.873 0.005 . 1 . . . . . . . . 5650 1 718 . 1 1 57 57 LEU HD12 H 1 0.873 0.005 . 1 . . . . . . . . 5650 1 719 . 1 1 57 57 LEU HD13 H 1 0.873 0.005 . 1 . . . . . . . . 5650 1 720 . 1 1 57 57 LEU CD2 C 13 22.868 0.050 . 1 . . . . . . . . 5650 1 721 . 1 1 57 57 LEU HD21 H 1 0.873 0.005 . 1 . . . . . . . . 5650 1 722 . 1 1 57 57 LEU HD22 H 1 0.873 0.005 . 1 . . . . . . . . 5650 1 723 . 1 1 57 57 LEU HD23 H 1 0.873 0.005 . 1 . . . . . . . . 5650 1 724 . 1 1 58 58 HIS N N 15 121.464 0.050 . 1 . . . . . . . . 5650 1 725 . 1 1 58 58 HIS H H 1 8.990 0.005 . 1 . . . . . . . . 5650 1 726 . 1 1 58 58 HIS CA C 13 53.572 0.050 . 1 . . . . . . . . 5650 1 727 . 1 1 58 58 HIS HA H 1 4.996 0.005 . 1 . . . . . . . . 5650 1 728 . 1 1 58 58 HIS C C 13 177.649 0.050 . 1 . . . . . . . . 5650 1 729 . 1 1 58 58 HIS CB C 13 27.220 0.050 . 1 . . . . . . . . 5650 1 730 . 1 1 58 58 HIS HB2 H 1 3.266 0.005 . 2 . . . . . . . . 5650 1 731 . 1 1 58 58 HIS HB3 H 1 3.343 0.005 . 2 . . . . . . . . 5650 1 732 . 1 1 58 58 HIS HD2 H 1 6.274 0.005 . 1 . . . . . . . . 5650 1 733 . 1 1 59 59 VAL N N 15 123.265 0.050 . 1 . . . . . . . . 5650 1 734 . 1 1 59 59 VAL H H 1 8.582 0.005 . 1 . . . . . . . . 5650 1 735 . 1 1 59 59 VAL CA C 13 59.746 0.050 . 1 . . . . . . . . 5650 1 736 . 1 1 59 59 VAL HA H 1 4.335 0.005 . 1 . . . . . . . . 5650 1 737 . 1 1 59 59 VAL C C 13 176.840 0.050 . 1 . . . . . . . . 5650 1 738 . 1 1 59 59 VAL CB C 13 31.507 0.050 . 1 . . . . . . . . 5650 1 739 . 1 1 59 59 VAL HB H 1 2.142 0.005 . 1 . . . . . . . . 5650 1 740 . 1 1 59 59 VAL CG1 C 13 18.777 0.050 . 2 . . . . . . . . 5650 1 741 . 1 1 59 59 VAL HG11 H 1 1.063 0.005 . 2 . . . . . . . . 5650 1 742 . 1 1 59 59 VAL HG12 H 1 1.063 0.005 . 2 . . . . . . . . 5650 1 743 . 1 1 59 59 VAL HG13 H 1 1.063 0.005 . 2 . . . . . . . . 5650 1 744 . 1 1 59 59 VAL CG2 C 13 19.320 0.050 . 2 . . . . . . . . 5650 1 745 . 1 1 59 59 VAL HG21 H 1 1.099 0.005 . 2 . . . . . . . . 5650 1 746 . 1 1 59 59 VAL HG22 H 1 1.099 0.005 . 2 . . . . . . . . 5650 1 747 . 1 1 59 59 VAL HG23 H 1 1.099 0.005 . 2 . . . . . . . . 5650 1 748 . 1 1 60 60 ARG N N 15 126.064 0.050 . 1 . . . . . . . . 5650 1 749 . 1 1 60 60 ARG H H 1 8.699 0.005 . 1 . . . . . . . . 5650 1 750 . 1 1 60 60 ARG CA C 13 53.976 0.050 . 1 . . . . . . . . 5650 1 751 . 1 1 60 60 ARG HA H 1 4.528 0.005 . 1 . . . . . . . . 5650 1 752 . 1 1 60 60 ARG C C 13 175.217 0.050 . 1 . . . . . . . . 5650 1 753 . 1 1 60 60 ARG CB C 13 28.895 0.050 . 1 . . . . . . . . 5650 1 754 . 1 1 60 60 ARG HB2 H 1 1.886 0.005 . 2 . . . . . . . . 5650 1 755 . 1 1 60 60 ARG HB3 H 1 1.935 0.005 . 2 . . . . . . . . 5650 1 756 . 1 1 60 60 ARG CG C 13 25.053 0.050 . 1 . . . . . . . . 5650 1 757 . 1 1 60 60 ARG CD C 13 41.333 0.050 . 1 . . . . . . . . 5650 1 758 . 1 1 60 60 ARG NE N 15 116.745 0.050 . 1 . . . . . . . . 5650 1 759 . 1 1 60 60 ARG HE H 1 7.390 0.005 . 1 . . . . . . . . 5650 1 760 . 1 1 60 60 ARG HG2 H 1 1.760 0.005 . 1 . . . . . . . . 5650 1 761 . 1 1 60 60 ARG HD2 H 1 3.262 0.005 . 1 . . . . . . . . 5650 1 762 . 1 1 60 60 ARG HG3 H 1 1.760 0.005 . 1 . . . . . . . . 5650 1 763 . 1 1 60 60 ARG HD3 H 1 3.262 0.005 . 1 . . . . . . . . 5650 1 764 . 1 1 61 61 GLY N N 15 110.199 0.050 . 1 . . . . . . . . 5650 1 765 . 1 1 61 61 GLY H H 1 8.669 0.005 . 1 . . . . . . . . 5650 1 766 . 1 1 61 61 GLY CA C 13 43.112 0.050 . 1 . . . . . . . . 5650 1 767 . 1 1 61 61 GLY HA2 H 1 3.908 0.005 . 1 . . . . . . . . 5650 1 768 . 1 1 61 61 GLY HA3 H 1 4.083 0.005 . 1 . . . . . . . . 5650 1 769 . 1 1 61 61 GLY C C 13 178.407 0.050 . 1 . . . . . . . . 5650 1 770 . 1 1 62 62 LYS N N 15 120.829 0.050 . 1 . . . . . . . . 5650 1 771 . 1 1 62 62 LYS H H 1 8.393 0.005 . 1 . . . . . . . . 5650 1 772 . 1 1 62 62 LYS CA C 13 54.241 0.050 . 1 . . . . . . . . 5650 1 773 . 1 1 62 62 LYS C C 13 175.427 0.050 . 1 . . . . . . . . 5650 1 774 . 1 1 62 62 LYS CB C 13 31.118 0.050 . 1 . . . . . . . . 5650 1 775 . 1 1 62 62 LYS CG C 13 22.675 0.050 . 1 . . . . . . . . 5650 1 776 . 1 1 62 62 LYS CD C 13 26.868 0.050 . 1 . . . . . . . . 5650 1 777 . 1 1 63 63 LYS N N 15 121.324 0.050 . 1 . . . . . . . . 5650 1 778 . 1 1 63 63 LYS H H 1 8.406 0.005 . 1 . . . . . . . . 5650 1 779 . 1 1 63 63 LYS CA C 13 54.306 0.050 . 1 . . . . . . . . 5650 1 780 . 1 1 63 63 LYS HA H 1 4.359 0.005 . 1 . . . . . . . . 5650 1 781 . 1 1 63 63 LYS C C 13 175.651 0.050 . 1 . . . . . . . . 5650 1 782 . 1 1 63 63 LYS CB C 13 30.975 0.050 . 1 . . . . . . . . 5650 1 783 . 1 1 63 63 LYS CG C 13 22.858 0.050 . 1 . . . . . . . . 5650 1 784 . 1 1 63 63 LYS CD C 13 27.011 0.050 . 1 . . . . . . . . 5650 1 785 . 1 1 63 63 LYS CE C 13 39.988 0.050 . 1 . . . . . . . . 5650 1 786 . 1 1 63 63 LYS HG2 H 1 1.466 0.005 . 1 . . . . . . . . 5650 1 787 . 1 1 63 63 LYS HE3 H 1 3.036 0.005 . 1 . . . . . . . . 5650 1 788 . 1 1 63 63 LYS HG3 H 1 1.466 0.005 . 1 . . . . . . . . 5650 1 789 . 1 1 63 63 LYS HE2 H 1 3.036 0.005 . 1 . . . . . . . . 5650 1 790 . 1 1 64 64 LYS N N 15 122.002 0.050 . 1 . . . . . . . . 5650 1 791 . 1 1 64 64 LYS H H 1 8.315 0.005 . 1 . . . . . . . . 5650 1 792 . 1 1 64 64 LYS CA C 13 54.519 0.050 . 1 . . . . . . . . 5650 1 793 . 1 1 64 64 LYS HA H 1 4.313 0.005 . 1 . . . . . . . . 5650 1 794 . 1 1 64 64 LYS C C 13 175.874 0.050 . 1 . . . . . . . . 5650 1 795 . 1 1 64 64 LYS CB C 13 31.001 0.050 . 1 . . . . . . . . 5650 1 796 . 1 1 64 64 LYS CG C 13 22.665 0.050 . 1 . . . . . . . . 5650 1 797 . 1 1 64 64 LYS CD C 13 26.941 0.050 . 1 . . . . . . . . 5650 1 798 . 1 1 64 64 LYS CE C 13 39.982 0.050 . 1 . . . . . . . . 5650 1 799 . 1 1 64 64 LYS HB2 H 1 1.837 0.005 . 1 . . . . . . . . 5650 1 800 . 1 1 64 64 LYS HB3 H 1 1.837 0.005 . 1 . . . . . . . . 5650 1 801 . 1 1 65 65 ARG N N 15 121.785 0.050 . 1 . . . . . . . . 5650 1 802 . 1 1 65 65 ARG H H 1 8.400 0.005 . 1 . . . . . . . . 5650 1 803 . 1 1 65 65 ARG CA C 13 54.068 0.050 . 1 . . . . . . . . 5650 1 804 . 1 1 65 65 ARG HA H 1 4.391 0.005 . 1 . . . . . . . . 5650 1 805 . 1 1 65 65 ARG C C 13 176.226 0.050 . 1 . . . . . . . . 5650 1 806 . 1 1 65 65 ARG CB C 13 28.772 0.050 . 1 . . . . . . . . 5650 1 807 . 1 1 65 65 ARG HB2 H 1 1.806 0.005 . 2 . . . . . . . . 5650 1 808 . 1 1 65 65 ARG HB3 H 1 1.889 0.005 . 2 . . . . . . . . 5650 1 809 . 1 1 65 65 ARG CG C 13 25.045 0.050 . 1 . . . . . . . . 5650 1 810 . 1 1 65 65 ARG HG2 H 1 1.621 0.005 . 2 . . . . . . . . 5650 1 811 . 1 1 65 65 ARG HG3 H 1 1.661 0.005 . 2 . . . . . . . . 5650 1 812 . 1 1 65 65 ARG CD C 13 41.265 0.050 . 1 . . . . . . . . 5650 1 813 . 1 1 65 65 ARG NE N 15 116.496 0.050 . 1 . . . . . . . . 5650 1 814 . 1 1 65 65 ARG HE H 1 7.412 0.005 . 1 . . . . . . . . 5650 1 815 . 1 1 65 65 ARG HD2 H 1 3.198 0.005 . 1 . . . . . . . . 5650 1 816 . 1 1 65 65 ARG HD3 H 1 3.198 0.005 . 1 . . . . . . . . 5650 1 817 . 1 1 66 66 LEU N N 15 122.812 0.050 . 1 . . . . . . . . 5650 1 818 . 1 1 66 66 LEU H H 1 8.377 0.005 . 1 . . . . . . . . 5650 1 819 . 1 1 66 66 LEU CA C 13 53.112 0.050 . 1 . . . . . . . . 5650 1 820 . 1 1 66 66 LEU HA H 1 4.398 0.005 . 1 . . . . . . . . 5650 1 821 . 1 1 66 66 LEU C C 13 174.698 0.050 . 1 . . . . . . . . 5650 1 822 . 1 1 66 66 LEU CB C 13 40.250 0.050 . 1 . . . . . . . . 5650 1 823 . 1 1 66 66 LEU HB2 H 1 1.641 0.005 . 2 . . . . . . . . 5650 1 824 . 1 1 66 66 LEU HB3 H 1 1.710 0.005 . 2 . . . . . . . . 5650 1 825 . 1 1 66 66 LEU CG C 13 24.832 0.050 . 1 . . . . . . . . 5650 1 826 . 1 1 66 66 LEU HG H 1 1.641 0.005 . 1 . . . . . . . . 5650 1 827 . 1 1 66 66 LEU CD1 C 13 21.480 0.050 . 2 . . . . . . . . 5650 1 828 . 1 1 66 66 LEU HD11 H 1 0.909 0.005 . 2 . . . . . . . . 5650 1 829 . 1 1 66 66 LEU HD12 H 1 0.909 0.005 . 2 . . . . . . . . 5650 1 830 . 1 1 66 66 LEU HD13 H 1 0.909 0.005 . 2 . . . . . . . . 5650 1 831 . 1 1 66 66 LEU CD2 C 13 22.928 0.050 . 2 . . . . . . . . 5650 1 832 . 1 1 66 66 LEU HD21 H 1 0.944 0.005 . 2 . . . . . . . . 5650 1 833 . 1 1 66 66 LEU HD22 H 1 0.944 0.005 . 2 . . . . . . . . 5650 1 834 . 1 1 66 66 LEU HD23 H 1 0.944 0.005 . 2 . . . . . . . . 5650 1 835 . 1 1 67 67 GLY N N 15 108.985 0.050 . 1 . . . . . . . . 5650 1 836 . 1 1 67 67 GLY H H 1 8.385 0.005 . 1 . . . . . . . . 5650 1 837 . 1 1 67 67 GLY CA C 13 43.482 0.050 . 1 . . . . . . . . 5650 1 838 . 1 1 67 67 GLY HA2 H 1 3.893 0.005 . 1 . . . . . . . . 5650 1 839 . 1 1 67 67 GLY HA3 H 1 4.036 0.005 . 1 . . . . . . . . 5650 1 840 . 1 1 67 67 GLY C C 13 177.941 0.050 . 1 . . . . . . . . 5650 1 841 . 1 1 68 68 ARG N N 15 120.571 0.050 . 1 . . . . . . . . 5650 1 842 . 1 1 68 68 ARG H H 1 8.244 0.005 . 1 . . . . . . . . 5650 1 843 . 1 1 68 68 ARG CA C 13 54.327 0.050 . 1 . . . . . . . . 5650 1 844 . 1 1 68 68 ARG HA H 1 4.289 0.005 . 1 . . . . . . . . 5650 1 845 . 1 1 68 68 ARG C C 13 176.180 0.050 . 1 . . . . . . . . 5650 1 846 . 1 1 68 68 ARG CB C 13 28.627 0.050 . 1 . . . . . . . . 5650 1 847 . 1 1 68 68 ARG CG C 13 24.763 0.050 . 1 . . . . . . . . 5650 1 848 . 1 1 68 68 ARG CD C 13 41.259 0.050 . 1 . . . . . . . . 5650 1 849 . 1 1 68 68 ARG NE N 15 116.552 0.050 . 1 . . . . . . . . 5650 1 850 . 1 1 68 68 ARG HE H 1 7.248 0.005 . 1 . . . . . . . . 5650 1 851 . 1 1 68 68 ARG HB2 H 1 1.706 0.005 . 1 . . . . . . . . 5650 1 852 . 1 1 68 68 ARG HG2 H 1 1.487 0.005 . 1 . . . . . . . . 5650 1 853 . 1 1 68 68 ARG HD2 H 1 3.158 0.005 . 1 . . . . . . . . 5650 1 854 . 1 1 68 68 ARG HB3 H 1 1.706 0.005 . 1 . . . . . . . . 5650 1 855 . 1 1 68 68 ARG HG3 H 1 1.487 0.005 . 1 . . . . . . . . 5650 1 856 . 1 1 68 68 ARG HD3 H 1 3.158 0.005 . 1 . . . . . . . . 5650 1 857 . 1 1 69 69 TYR N N 15 120.039 0.050 . 1 . . . . . . . . 5650 1 858 . 1 1 69 69 TYR H H 1 8.224 0.005 . 1 . . . . . . . . 5650 1 859 . 1 1 69 69 TYR CA C 13 55.728 0.050 . 1 . . . . . . . . 5650 1 860 . 1 1 69 69 TYR HA H 1 4.644 0.005 . 1 . . . . . . . . 5650 1 861 . 1 1 69 69 TYR C C 13 176.679 0.050 . 1 . . . . . . . . 5650 1 862 . 1 1 69 69 TYR CB C 13 36.487 0.050 . 1 . . . . . . . . 5650 1 863 . 1 1 69 69 TYR HB2 H 1 2.977 0.005 . 2 . . . . . . . . 5650 1 864 . 1 1 69 69 TYR HB3 H 1 3.115 0.005 . 2 . . . . . . . . 5650 1 865 . 1 1 69 69 TYR HD1 H 1 7.158 0.005 . 1 . . . . . . . . 5650 1 866 . 1 1 69 69 TYR HE1 H 1 6.855 0.005 . 1 . . . . . . . . 5650 1 867 . 1 1 69 69 TYR HD2 H 1 7.158 0.005 . 1 . . . . . . . . 5650 1 868 . 1 1 69 69 TYR HE2 H 1 6.855 0.005 . 1 . . . . . . . . 5650 1 869 . 1 1 70 70 LEU N N 15 123.571 0.050 . 1 . . . . . . . . 5650 1 870 . 1 1 70 70 LEU H H 1 8.186 0.005 . 1 . . . . . . . . 5650 1 871 . 1 1 70 70 LEU CA C 13 53.005 0.050 . 1 . . . . . . . . 5650 1 872 . 1 1 70 70 LEU HA H 1 4.362 0.005 . 1 . . . . . . . . 5650 1 873 . 1 1 70 70 LEU C C 13 174.936 0.050 . 1 . . . . . . . . 5650 1 874 . 1 1 70 70 LEU CB C 13 40.259 0.050 . 1 . . . . . . . . 5650 1 875 . 1 1 70 70 LEU HB2 H 1 1.603 0.005 . 2 . . . . . . . . 5650 1 876 . 1 1 70 70 LEU HB3 H 1 1.633 0.005 . 2 . . . . . . . . 5650 1 877 . 1 1 70 70 LEU CG C 13 24.720 0.050 . 1 . . . . . . . . 5650 1 878 . 1 1 70 70 LEU HG H 1 1.574 0.005 . 1 . . . . . . . . 5650 1 879 . 1 1 70 70 LEU CD1 C 13 21.410 0.050 . 2 . . . . . . . . 5650 1 880 . 1 1 70 70 LEU HD11 H 1 0.869 0.005 . 2 . . . . . . . . 5650 1 881 . 1 1 70 70 LEU HD12 H 1 0.869 0.005 . 2 . . . . . . . . 5650 1 882 . 1 1 70 70 LEU HD13 H 1 0.869 0.005 . 2 . . . . . . . . 5650 1 883 . 1 1 70 70 LEU CD2 C 13 22.913 0.050 . 2 . . . . . . . . 5650 1 884 . 1 1 70 70 LEU HD21 H 1 0.921 0.005 . 2 . . . . . . . . 5650 1 885 . 1 1 70 70 LEU HD22 H 1 0.921 0.005 . 2 . . . . . . . . 5650 1 886 . 1 1 70 70 LEU HD23 H 1 0.921 0.005 . 2 . . . . . . . . 5650 1 887 . 1 1 71 71 GLY N N 15 108.580 0.050 . 1 . . . . . . . . 5650 1 888 . 1 1 71 71 GLY H H 1 7.925 0.005 . 1 . . . . . . . . 5650 1 889 . 1 1 71 71 GLY CA C 13 42.945 0.050 . 1 . . . . . . . . 5650 1 890 . 1 1 71 71 GLY C C 13 178.689 0.050 . 1 . . . . . . . . 5650 1 891 . 1 1 71 71 GLY HA2 H 1 3.958 0.005 . 1 . . . . . . . . 5650 1 892 . 1 1 71 71 GLY HA3 H 1 3.958 0.005 . 1 . . . . . . . . 5650 1 893 . 1 1 72 72 LYS N N 15 120.051 0.050 . 1 . . . . . . . . 5650 1 894 . 1 1 72 72 LYS H H 1 8.170 0.005 . 1 . . . . . . . . 5650 1 895 . 1 1 72 72 LYS CA C 13 54.165 0.050 . 1 . . . . . . . . 5650 1 896 . 1 1 72 72 LYS HA H 1 4.374 0.005 . 1 . . . . . . . . 5650 1 897 . 1 1 72 72 LYS C C 13 175.766 0.050 . 1 . . . . . . . . 5650 1 898 . 1 1 72 72 LYS CB C 13 31.296 0.050 . 1 . . . . . . . . 5650 1 899 . 1 1 72 72 LYS HB2 H 1 1.780 0.005 . 2 . . . . . . . . 5650 1 900 . 1 1 72 72 LYS HB3 H 1 1.880 0.005 . 2 . . . . . . . . 5650 1 901 . 1 1 72 72 LYS CG C 13 22.458 0.050 . 1 . . . . . . . . 5650 1 902 . 1 1 72 72 LYS CD C 13 26.865 0.050 . 1 . . . . . . . . 5650 1 903 . 1 1 72 72 LYS CE C 13 40.005 0.050 . 1 . . . . . . . . 5650 1 904 . 1 1 72 72 LYS HG2 H 1 1.441 0.005 . 1 . . . . . . . . 5650 1 905 . 1 1 72 72 LYS HD3 H 1 1.767 0.005 . 1 . . . . . . . . 5650 1 906 . 1 1 72 72 LYS HE3 H 1 3.042 0.005 . 1 . . . . . . . . 5650 1 907 . 1 1 72 72 LYS HG3 H 1 1.441 0.005 . 1 . . . . . . . . 5650 1 908 . 1 1 72 72 LYS HD2 H 1 1.767 0.005 . 1 . . . . . . . . 5650 1 909 . 1 1 72 72 LYS HE2 H 1 3.042 0.005 . 1 . . . . . . . . 5650 1 910 . 1 1 73 73 ARG N N 15 123.310 0.050 . 1 . . . . . . . . 5650 1 911 . 1 1 73 73 ARG H H 1 8.445 0.005 . 1 . . . . . . . . 5650 1 912 . 1 1 73 73 ARG CA C 13 51.693 0.050 . 1 . . . . . . . . 5650 1 913 . 1 1 73 73 ARG HA H 1 4.581 0.005 . 1 . . . . . . . . 5650 1 914 . 1 1 73 73 ARG CB C 13 28.038 0.050 . 1 . . . . . . . . 5650 1 915 . 1 1 73 73 ARG HB2 H 1 1.746 0.005 . 2 . . . . . . . . 5650 1 916 . 1 1 73 73 ARG HB3 H 1 1.866 0.005 . 2 . . . . . . . . 5650 1 917 . 1 1 73 73 ARG CG C 13 24.944 0.050 . 1 . . . . . . . . 5650 1 918 . 1 1 73 73 ARG HG2 H 1 1.652 0.005 . 2 . . . . . . . . 5650 1 919 . 1 1 73 73 ARG HG3 H 1 1.683 0.005 . 2 . . . . . . . . 5650 1 920 . 1 1 73 73 ARG CD C 13 41.167 0.050 . 1 . . . . . . . . 5650 1 921 . 1 1 73 73 ARG NE N 15 116.565 0.050 . 1 . . . . . . . . 5650 1 922 . 1 1 73 73 ARG HE H 1 7.369 0.005 . 1 . . . . . . . . 5650 1 923 . 1 1 73 73 ARG HD2 H 1 3.181 0.005 . 1 . . . . . . . . 5650 1 924 . 1 1 73 73 ARG HD3 H 1 3.181 0.005 . 1 . . . . . . . . 5650 1 925 . 1 1 74 74 PRO CA C 13 60.851 0.050 . 1 . . . . . . . . 5650 1 926 . 1 1 74 74 PRO HA H 1 4.462 0.005 . 1 . . . . . . . . 5650 1 927 . 1 1 74 74 PRO C C 13 175.973 0.050 . 1 . . . . . . . . 5650 1 928 . 1 1 74 74 PRO CB C 13 30.024 0.050 . 1 . . . . . . . . 5650 1 929 . 1 1 74 74 PRO HB2 H 1 1.910 0.005 . 2 . . . . . . . . 5650 1 930 . 1 1 74 74 PRO HB3 H 1 2.286 0.005 . 2 . . . . . . . . 5650 1 931 . 1 1 74 74 PRO CG C 13 25.229 0.050 . 1 . . . . . . . . 5650 1 932 . 1 1 74 74 PRO CD C 13 48.464 0.050 . 1 . . . . . . . . 5650 1 933 . 1 1 74 74 PRO HD2 H 1 3.593 0.005 . 2 . . . . . . . . 5650 1 934 . 1 1 74 74 PRO HD3 H 1 3.778 0.005 . 2 . . . . . . . . 5650 1 935 . 1 1 74 74 PRO HG2 H 1 2.000 0.005 . 1 . . . . . . . . 5650 1 936 . 1 1 74 74 PRO HG3 H 1 2.000 0.005 . 1 . . . . . . . . 5650 1 937 . 1 1 75 75 ASP N N 15 120.741 0.050 . 1 . . . . . . . . 5650 1 938 . 1 1 75 75 ASP H H 1 8.422 0.005 . 1 . . . . . . . . 5650 1 939 . 1 1 75 75 ASP CA C 13 52.125 0.050 . 1 . . . . . . . . 5650 1 940 . 1 1 75 75 ASP HA H 1 4.673 0.005 . 1 . . . . . . . . 5650 1 941 . 1 1 75 75 ASP C C 13 176.898 0.050 . 1 . . . . . . . . 5650 1 942 . 1 1 75 75 ASP CB C 13 39.117 0.050 . 1 . . . . . . . . 5650 1 943 . 1 1 75 75 ASP HB2 H 1 2.679 0.005 . 2 . . . . . . . . 5650 1 944 . 1 1 75 75 ASP HB3 H 1 2.722 0.005 . 2 . . . . . . . . 5650 1 945 . 1 1 76 76 ARG N N 15 117.880 0.050 . 1 . . . . . . . . 5650 1 946 . 1 1 76 76 ARG H H 1 8.152 0.005 . 1 . . . . . . . . 5650 1 947 . 1 1 76 76 ARG CA C 13 52.877 0.050 . 1 . . . . . . . . 5650 1 948 . 1 1 76 76 ARG HA H 1 4.701 0.005 . 1 . . . . . . . . 5650 1 949 . 1 1 76 76 ARG C C 13 177.602 0.050 . 1 . . . . . . . . 5650 1 950 . 1 1 76 76 ARG CB C 13 31.887 0.050 . 1 . . . . . . . . 5650 1 951 . 1 1 76 76 ARG HB2 H 1 1.714 0.005 . 2 . . . . . . . . 5650 1 952 . 1 1 76 76 ARG HB3 H 1 2.014 0.005 . 2 . . . . . . . . 5650 1 953 . 1 1 76 76 ARG CG C 13 24.008 0.050 . 1 . . . . . . . . 5650 1 954 . 1 1 76 76 ARG HG2 H 1 1.433 0.005 . 2 . . . . . . . . 5650 1 955 . 1 1 76 76 ARG HG3 H 1 1.502 0.005 . 2 . . . . . . . . 5650 1 956 . 1 1 76 76 ARG CD C 13 41.228 0.050 . 1 . . . . . . . . 5650 1 957 . 1 1 76 76 ARG HD2 H 1 2.288 0.005 . 2 . . . . . . . . 5650 1 958 . 1 1 76 76 ARG HD3 H 1 2.596 0.005 . 2 . . . . . . . . 5650 1 959 . 1 1 76 76 ARG NE N 15 115.982 0.050 . 1 . . . . . . . . 5650 1 960 . 1 1 76 76 ARG HE H 1 6.642 0.005 . 1 . . . . . . . . 5650 1 961 . 1 1 77 77 LYS N N 15 122.640 0.050 . 1 . . . . . . . . 5650 1 962 . 1 1 77 77 LYS H H 1 9.520 0.005 . 1 . . . . . . . . 5650 1 963 . 1 1 77 77 LYS CA C 13 53.678 0.050 . 1 . . . . . . . . 5650 1 964 . 1 1 77 77 LYS HA H 1 5.111 0.005 . 1 . . . . . . . . 5650 1 965 . 1 1 77 77 LYS C C 13 178.785 0.050 . 1 . . . . . . . . 5650 1 966 . 1 1 77 77 LYS CB C 13 34.755 0.050 . 1 . . . . . . . . 5650 1 967 . 1 1 77 77 LYS HB2 H 1 1.590 0.005 . 2 . . . . . . . . 5650 1 968 . 1 1 77 77 LYS HB3 H 1 1.912 0.005 . 2 . . . . . . . . 5650 1 969 . 1 1 77 77 LYS CG C 13 22.892 0.050 . 1 . . . . . . . . 5650 1 970 . 1 1 77 77 LYS HG2 H 1 1.151 0.005 . 2 . . . . . . . . 5650 1 971 . 1 1 77 77 LYS HG3 H 1 1.247 0.005 . 2 . . . . . . . . 5650 1 972 . 1 1 77 77 LYS CD C 13 28.362 0.050 . 1 . . . . . . . . 5650 1 973 . 1 1 77 77 LYS HD2 H 1 1.627 0.005 . 2 . . . . . . . . 5650 1 974 . 1 1 77 77 LYS HD3 H 1 1.776 0.005 . 2 . . . . . . . . 5650 1 975 . 1 1 77 77 LYS CE C 13 39.937 0.050 . 1 . . . . . . . . 5650 1 976 . 1 1 77 77 LYS HE2 H 1 2.699 0.005 . 1 . . . . . . . . 5650 1 977 . 1 1 77 77 LYS HE3 H 1 3.068 0.005 . 1 . . . . . . . . 5650 1 978 . 1 1 78 78 LYS N N 15 124.748 0.050 . 1 . . . . . . . . 5650 1 979 . 1 1 78 78 LYS H H 1 8.897 0.005 . 1 . . . . . . . . 5650 1 980 . 1 1 78 78 LYS CA C 13 52.524 0.050 . 1 . . . . . . . . 5650 1 981 . 1 1 78 78 LYS HA H 1 5.227 0.005 . 1 . . . . . . . . 5650 1 982 . 1 1 78 78 LYS C C 13 177.212 0.050 . 1 . . . . . . . . 5650 1 983 . 1 1 78 78 LYS CB C 13 34.162 0.050 . 1 . . . . . . . . 5650 1 984 . 1 1 78 78 LYS CG C 13 23.307 0.050 . 1 . . . . . . . . 5650 1 985 . 1 1 78 78 LYS HG2 H 1 0.684 0.005 . 2 . . . . . . . . 5650 1 986 . 1 1 78 78 LYS HG3 H 1 0.764 0.005 . 2 . . . . . . . . 5650 1 987 . 1 1 78 78 LYS CD C 13 27.414 0.050 . 1 . . . . . . . . 5650 1 988 . 1 1 78 78 LYS HD2 H 1 1.117 0.005 . 2 . . . . . . . . 5650 1 989 . 1 1 78 78 LYS HD3 H 1 1.157 0.005 . 2 . . . . . . . . 5650 1 990 . 1 1 78 78 LYS CE C 13 39.399 0.050 . 1 . . . . . . . . 5650 1 991 . 1 1 78 78 LYS HE2 H 1 2.076 0.005 . 1 . . . . . . . . 5650 1 992 . 1 1 78 78 LYS HE3 H 1 2.303 0.005 . 1 . . . . . . . . 5650 1 993 . 1 1 78 78 LYS HB2 H 1 1.436 0.005 . 1 . . . . . . . . 5650 1 994 . 1 1 78 78 LYS HB3 H 1 1.436 0.005 . 1 . . . . . . . . 5650 1 995 . 1 1 79 79 ALA N N 15 123.021 0.050 . 1 . . . . . . . . 5650 1 996 . 1 1 79 79 ALA H H 1 9.490 0.005 . 1 . . . . . . . . 5650 1 997 . 1 1 79 79 ALA CA C 13 47.873 0.050 . 1 . . . . . . . . 5650 1 998 . 1 1 79 79 ALA HA H 1 5.363 0.005 . 1 . . . . . . . . 5650 1 999 . 1 1 79 79 ALA C C 13 177.170 0.050 . 1 . . . . . . . . 5650 1 1000 . 1 1 79 79 ALA CB C 13 21.614 0.050 . 1 . . . . . . . . 5650 1 1001 . 1 1 79 79 ALA HB1 H 1 1.295 0.005 . 1 . . . . . . . . 5650 1 1002 . 1 1 79 79 ALA HB2 H 1 1.295 0.005 . 1 . . . . . . . . 5650 1 1003 . 1 1 79 79 ALA HB3 H 1 1.295 0.005 . 1 . . . . . . . . 5650 1 1004 . 1 1 80 80 ILE N N 15 122.894 0.050 . 1 . . . . . . . . 5650 1 1005 . 1 1 80 80 ILE H H 1 9.173 0.005 . 1 . . . . . . . . 5650 1 1006 . 1 1 80 80 ILE CA C 13 58.967 0.050 . 1 . . . . . . . . 5650 1 1007 . 1 1 80 80 ILE HA H 1 4.731 0.005 . 1 . . . . . . . . 5650 1 1008 . 1 1 80 80 ILE C C 13 176.134 0.050 . 1 . . . . . . . . 5650 1 1009 . 1 1 80 80 ILE CB C 13 37.374 0.050 . 1 . . . . . . . . 5650 1 1010 . 1 1 80 80 ILE HB H 1 1.726 0.005 . 1 . . . . . . . . 5650 1 1011 . 1 1 80 80 ILE CG1 C 13 25.974 0.050 . 1 . . . . . . . . 5650 1 1012 . 1 1 80 80 ILE HG12 H 1 1.192 0.005 . 2 . . . . . . . . 5650 1 1013 . 1 1 80 80 ILE HG13 H 1 1.409 0.005 . 2 . . . . . . . . 5650 1 1014 . 1 1 80 80 ILE CG2 C 13 16.271 0.050 . 1 . . . . . . . . 5650 1 1015 . 1 1 80 80 ILE HG21 H 1 0.777 0.005 . 1 . . . . . . . . 5650 1 1016 . 1 1 80 80 ILE HG22 H 1 0.777 0.005 . 1 . . . . . . . . 5650 1 1017 . 1 1 80 80 ILE HG23 H 1 0.777 0.005 . 1 . . . . . . . . 5650 1 1018 . 1 1 80 80 ILE CD1 C 13 12.075 0.050 . 1 . . . . . . . . 5650 1 1019 . 1 1 80 80 ILE HD11 H 1 0.790 0.005 . 1 . . . . . . . . 5650 1 1020 . 1 1 80 80 ILE HD12 H 1 0.790 0.005 . 1 . . . . . . . . 5650 1 1021 . 1 1 80 80 ILE HD13 H 1 0.790 0.005 . 1 . . . . . . . . 5650 1 1022 . 1 1 81 81 VAL N N 15 127.144 0.050 . 1 . . . . . . . . 5650 1 1023 . 1 1 81 81 VAL H H 1 9.634 0.005 . 1 . . . . . . . . 5650 1 1024 . 1 1 81 81 VAL CA C 13 58.236 0.050 . 1 . . . . . . . . 5650 1 1025 . 1 1 81 81 VAL HA H 1 4.906 0.005 . 1 . . . . . . . . 5650 1 1026 . 1 1 81 81 VAL C C 13 178.773 0.050 . 1 . . . . . . . . 5650 1 1027 . 1 1 81 81 VAL CB C 13 31.868 0.050 . 1 . . . . . . . . 5650 1 1028 . 1 1 81 81 VAL HB H 1 2.400 0.005 . 1 . . . . . . . . 5650 1 1029 . 1 1 81 81 VAL CG1 C 13 20.548 0.050 . 2 . . . . . . . . 5650 1 1030 . 1 1 81 81 VAL HG11 H 1 1.063 0.005 . 2 . . . . . . . . 5650 1 1031 . 1 1 81 81 VAL HG12 H 1 1.063 0.005 . 2 . . . . . . . . 5650 1 1032 . 1 1 81 81 VAL HG13 H 1 1.063 0.005 . 2 . . . . . . . . 5650 1 1033 . 1 1 81 81 VAL CG2 C 13 18.981 0.050 . 2 . . . . . . . . 5650 1 1034 . 1 1 81 81 VAL HG21 H 1 1.120 0.005 . 2 . . . . . . . . 5650 1 1035 . 1 1 81 81 VAL HG22 H 1 1.120 0.005 . 2 . . . . . . . . 5650 1 1036 . 1 1 81 81 VAL HG23 H 1 1.120 0.005 . 2 . . . . . . . . 5650 1 1037 . 1 1 82 82 GLN N N 15 126.481 0.050 . 1 . . . . . . . . 5650 1 1038 . 1 1 82 82 GLN H H 1 8.977 0.005 . 1 . . . . . . . . 5650 1 1039 . 1 1 82 82 GLN CA C 13 51.523 0.050 . 1 . . . . . . . . 5650 1 1040 . 1 1 82 82 GLN HA H 1 5.493 0.005 . 1 . . . . . . . . 5650 1 1041 . 1 1 82 82 GLN C C 13 175.711 0.050 . 1 . . . . . . . . 5650 1 1042 . 1 1 82 82 GLN CB C 13 29.263 0.050 . 1 . . . . . . . . 5650 1 1043 . 1 1 82 82 GLN HB2 H 1 1.879 0.005 . 2 . . . . . . . . 5650 1 1044 . 1 1 82 82 GLN HB3 H 1 2.118 0.005 . 2 . . . . . . . . 5650 1 1045 . 1 1 82 82 GLN CG C 13 31.480 0.050 . 1 . . . . . . . . 5650 1 1046 . 1 1 82 82 GLN HG2 H 1 2.271 0.005 . 2 . . . . . . . . 5650 1 1047 . 1 1 82 82 GLN HG3 H 1 2.454 0.005 . 2 . . . . . . . . 5650 1 1048 . 1 1 82 82 GLN NE2 N 15 112.314 0.050 . 1 . . . . . . . . 5650 1 1049 . 1 1 82 82 GLN HE21 H 1 7.173 0.005 . 1 . . . . . . . . 5650 1 1050 . 1 1 82 82 GLN HE22 H 1 7.719 0.005 . 1 . . . . . . . . 5650 1 1051 . 1 1 83 83 VAL N N 15 122.038 0.050 . 1 . . . . . . . . 5650 1 1052 . 1 1 83 83 VAL H H 1 9.069 0.005 . 1 . . . . . . . . 5650 1 1053 . 1 1 83 83 VAL CA C 13 57.974 0.050 . 1 . . . . . . . . 5650 1 1054 . 1 1 83 83 VAL HA H 1 5.272 0.005 . 1 . . . . . . . . 5650 1 1055 . 1 1 83 83 VAL C C 13 176.892 0.050 . 1 . . . . . . . . 5650 1 1056 . 1 1 83 83 VAL CB C 13 31.129 0.050 . 1 . . . . . . . . 5650 1 1057 . 1 1 83 83 VAL HB H 1 2.581 0.005 . 1 . . . . . . . . 5650 1 1058 . 1 1 83 83 VAL CG1 C 13 20.159 0.050 . 2 . . . . . . . . 5650 1 1059 . 1 1 83 83 VAL HG11 H 1 0.944 0.005 . 2 . . . . . . . . 5650 1 1060 . 1 1 83 83 VAL HG12 H 1 0.944 0.005 . 2 . . . . . . . . 5650 1 1061 . 1 1 83 83 VAL HG13 H 1 0.944 0.005 . 2 . . . . . . . . 5650 1 1062 . 1 1 83 83 VAL CG2 C 13 17.958 0.050 . 2 . . . . . . . . 5650 1 1063 . 1 1 83 83 VAL HG21 H 1 1.177 0.005 . 2 . . . . . . . . 5650 1 1064 . 1 1 83 83 VAL HG22 H 1 1.177 0.005 . 2 . . . . . . . . 5650 1 1065 . 1 1 83 83 VAL HG23 H 1 1.177 0.005 . 2 . . . . . . . . 5650 1 1066 . 1 1 84 84 ALA N N 15 123.975 0.050 . 1 . . . . . . . . 5650 1 1067 . 1 1 84 84 ALA H H 1 8.089 0.005 . 1 . . . . . . . . 5650 1 1068 . 1 1 84 84 ALA CA C 13 48.949 0.050 . 1 . . . . . . . . 5650 1 1069 . 1 1 84 84 ALA HA H 1 4.258 0.005 . 1 . . . . . . . . 5650 1 1070 . 1 1 84 84 ALA CB C 13 15.114 0.050 . 1 . . . . . . . . 5650 1 1071 . 1 1 84 84 ALA HB1 H 1 1.332 0.005 . 1 . . . . . . . . 5650 1 1072 . 1 1 84 84 ALA HB2 H 1 1.332 0.005 . 1 . . . . . . . . 5650 1 1073 . 1 1 84 84 ALA HB3 H 1 1.332 0.005 . 1 . . . . . . . . 5650 1 1074 . 1 1 85 85 PRO CA C 13 61.945 0.050 . 1 . . . . . . . . 5650 1 1075 . 1 1 85 85 PRO HA H 1 4.422 0.005 . 1 . . . . . . . . 5650 1 1076 . 1 1 85 85 PRO C C 13 174.156 0.050 . 1 . . . . . . . . 5650 1 1077 . 1 1 85 85 PRO CB C 13 29.498 0.050 . 1 . . . . . . . . 5650 1 1078 . 1 1 85 85 PRO HB2 H 1 1.944 0.005 . 2 . . . . . . . . 5650 1 1079 . 1 1 85 85 PRO HB3 H 1 2.374 0.005 . 2 . . . . . . . . 5650 1 1080 . 1 1 85 85 PRO CG C 13 25.612 0.050 . 1 . . . . . . . . 5650 1 1081 . 1 1 85 85 PRO HG2 H 1 2.112 0.005 . 2 . . . . . . . . 5650 1 1082 . 1 1 85 85 PRO HG3 H 1 2.193 0.005 . 2 . . . . . . . . 5650 1 1083 . 1 1 85 85 PRO CD C 13 48.398 0.050 . 1 . . . . . . . . 5650 1 1084 . 1 1 85 85 PRO HD2 H 1 3.656 0.005 . 2 . . . . . . . . 5650 1 1085 . 1 1 85 85 PRO HD3 H 1 3.860 0.005 . 2 . . . . . . . . 5650 1 1086 . 1 1 86 86 GLY N N 15 112.042 0.050 . 1 . . . . . . . . 5650 1 1087 . 1 1 86 86 GLY H H 1 8.734 0.005 . 1 . . . . . . . . 5650 1 1088 . 1 1 86 86 GLY CA C 13 43.224 0.050 . 1 . . . . . . . . 5650 1 1089 . 1 1 86 86 GLY HA2 H 1 3.744 0.005 . 1 . . . . . . . . 5650 1 1090 . 1 1 86 86 GLY HA3 H 1 4.319 0.005 . 1 . . . . . . . . 5650 1 1091 . 1 1 86 86 GLY C C 13 177.756 0.050 . 1 . . . . . . . . 5650 1 1092 . 1 1 87 87 GLN N N 15 119.084 0.050 . 1 . . . . . . . . 5650 1 1093 . 1 1 87 87 GLN H H 1 8.003 0.005 . 1 . . . . . . . . 5650 1 1094 . 1 1 87 87 GLN CA C 13 53.253 0.050 . 1 . . . . . . . . 5650 1 1095 . 1 1 87 87 GLN HA H 1 4.672 0.005 . 1 . . . . . . . . 5650 1 1096 . 1 1 87 87 GLN C C 13 177.457 0.050 . 1 . . . . . . . . 5650 1 1097 . 1 1 87 87 GLN CB C 13 27.699 0.050 . 1 . . . . . . . . 5650 1 1098 . 1 1 87 87 GLN HB2 H 1 2.039 0.005 . 2 . . . . . . . . 5650 1 1099 . 1 1 87 87 GLN HB3 H 1 2.357 0.005 . 2 . . . . . . . . 5650 1 1100 . 1 1 87 87 GLN CG C 13 32.532 0.050 . 1 . . . . . . . . 5650 1 1101 . 1 1 87 87 GLN NE2 N 15 108.520 0.050 . 1 . . . . . . . . 5650 1 1102 . 1 1 87 87 GLN HE21 H 1 6.395 0.005 . 1 . . . . . . . . 5650 1 1103 . 1 1 87 87 GLN HE22 H 1 7.448 0.005 . 1 . . . . . . . . 5650 1 1104 . 1 1 87 87 GLN HG2 H 1 2.360 0.005 . 1 . . . . . . . . 5650 1 1105 . 1 1 87 87 GLN HG3 H 1 2.360 0.005 . 1 . . . . . . . . 5650 1 1106 . 1 1 88 88 LYS N N 15 116.597 0.050 . 1 . . . . . . . . 5650 1 1107 . 1 1 88 88 LYS H H 1 8.297 0.005 . 1 . . . . . . . . 5650 1 1108 . 1 1 88 88 LYS CA C 13 52.594 0.050 . 1 . . . . . . . . 5650 1 1109 . 1 1 88 88 LYS HA H 1 4.696 0.005 . 1 . . . . . . . . 5650 1 1110 . 1 1 88 88 LYS C C 13 177.424 0.050 . 1 . . . . . . . . 5650 1 1111 . 1 1 88 88 LYS CB C 13 33.991 0.050 . 1 . . . . . . . . 5650 1 1112 . 1 1 88 88 LYS HB2 H 1 1.661 0.005 . 2 . . . . . . . . 5650 1 1113 . 1 1 88 88 LYS HB3 H 1 1.734 0.005 . 2 . . . . . . . . 5650 1 1114 . 1 1 88 88 LYS CG C 13 21.769 0.050 . 1 . . . . . . . . 5650 1 1115 . 1 1 88 88 LYS HG2 H 1 1.299 0.005 . 2 . . . . . . . . 5650 1 1116 . 1 1 88 88 LYS HG3 H 1 1.379 0.005 . 2 . . . . . . . . 5650 1 1117 . 1 1 88 88 LYS CD C 13 27.036 0.050 . 1 . . . . . . . . 5650 1 1118 . 1 1 88 88 LYS CE C 13 40.077 0.050 . 1 . . . . . . . . 5650 1 1119 . 1 1 88 88 LYS HD3 H 1 1.684 0.005 . 1 . . . . . . . . 5650 1 1120 . 1 1 88 88 LYS HE3 H 1 2.974 0.005 . 1 . . . . . . . . 5650 1 1121 . 1 1 88 88 LYS HD2 H 1 1.684 0.005 . 1 . . . . . . . . 5650 1 1122 . 1 1 88 88 LYS HE2 H 1 2.974 0.005 . 1 . . . . . . . . 5650 1 1123 . 1 1 89 89 ILE N N 15 118.419 0.050 . 1 . . . . . . . . 5650 1 1124 . 1 1 89 89 ILE H H 1 7.343 0.005 . 1 . . . . . . . . 5650 1 1125 . 1 1 89 89 ILE CA C 13 58.371 0.050 . 1 . . . . . . . . 5650 1 1126 . 1 1 89 89 ILE HA H 1 4.066 0.005 . 1 . . . . . . . . 5650 1 1127 . 1 1 89 89 ILE C C 13 176.119 0.050 . 1 . . . . . . . . 5650 1 1128 . 1 1 89 89 ILE CB C 13 33.850 0.050 . 1 . . . . . . . . 5650 1 1129 . 1 1 89 89 ILE HB H 1 0.678 0.005 . 1 . . . . . . . . 5650 1 1130 . 1 1 89 89 ILE CG1 C 13 25.131 0.050 . 1 . . . . . . . . 5650 1 1131 . 1 1 89 89 ILE HG12 H 1 0.407 0.005 . 2 . . . . . . . . 5650 1 1132 . 1 1 89 89 ILE HG13 H 1 0.808 0.005 . 2 . . . . . . . . 5650 1 1133 . 1 1 89 89 ILE CG2 C 13 15.931 0.050 . 1 . . . . . . . . 5650 1 1134 . 1 1 89 89 ILE HG21 H 1 0.207 0.005 . 1 . . . . . . . . 5650 1 1135 . 1 1 89 89 ILE HG22 H 1 0.207 0.005 . 1 . . . . . . . . 5650 1 1136 . 1 1 89 89 ILE HG23 H 1 0.207 0.005 . 1 . . . . . . . . 5650 1 1137 . 1 1 89 89 ILE CD1 C 13 9.757 0.050 . 1 . . . . . . . . 5650 1 1138 . 1 1 89 89 ILE HD11 H 1 -0.152 0.005 . 1 . . . . . . . . 5650 1 1139 . 1 1 89 89 ILE HD12 H 1 -0.152 0.005 . 1 . . . . . . . . 5650 1 1140 . 1 1 89 89 ILE HD13 H 1 -0.152 0.005 . 1 . . . . . . . . 5650 1 1141 . 1 1 90 90 GLU N N 15 128.594 0.050 . 1 . . . . . . . . 5650 1 1142 . 1 1 90 90 GLU H H 1 8.507 0.005 . 1 . . . . . . . . 5650 1 1143 . 1 1 90 90 GLU CA C 13 57.630 0.050 . 1 . . . . . . . . 5650 1 1144 . 1 1 90 90 GLU HA H 1 3.909 0.005 . 1 . . . . . . . . 5650 1 1145 . 1 1 90 90 GLU C C 13 173.762 0.050 . 1 . . . . . . . . 5650 1 1146 . 1 1 90 90 GLU CB C 13 27.093 0.050 . 1 . . . . . . . . 5650 1 1147 . 1 1 90 90 GLU CG C 13 33.679 0.050 . 1 . . . . . . . . 5650 1 1148 . 1 1 90 90 GLU HG2 H 1 2.337 0.005 . 2 . . . . . . . . 5650 1 1149 . 1 1 90 90 GLU HG3 H 1 2.378 0.005 . 2 . . . . . . . . 5650 1 1150 . 1 1 90 90 GLU HB2 H 1 2.075 0.005 . 1 . . . . . . . . 5650 1 1151 . 1 1 90 90 GLU HB3 H 1 2.075 0.005 . 1 . . . . . . . . 5650 1 1152 . 1 1 91 91 ALA N N 15 119.713 0.050 . 1 . . . . . . . . 5650 1 1153 . 1 1 91 91 ALA H H 1 8.830 0.005 . 1 . . . . . . . . 5650 1 1154 . 1 1 91 91 ALA CA C 13 52.275 0.050 . 1 . . . . . . . . 5650 1 1155 . 1 1 91 91 ALA HA H 1 4.181 0.005 . 1 . . . . . . . . 5650 1 1156 . 1 1 91 91 ALA C C 13 173.749 0.050 . 1 . . . . . . . . 5650 1 1157 . 1 1 91 91 ALA CB C 13 16.853 0.050 . 1 . . . . . . . . 5650 1 1158 . 1 1 91 91 ALA HB1 H 1 1.522 0.005 . 1 . . . . . . . . 5650 1 1159 . 1 1 91 91 ALA HB2 H 1 1.522 0.005 . 1 . . . . . . . . 5650 1 1160 . 1 1 91 91 ALA HB3 H 1 1.522 0.005 . 1 . . . . . . . . 5650 1 1161 . 1 1 92 92 LEU N N 15 113.256 0.050 . 1 . . . . . . . . 5650 1 1162 . 1 1 92 92 LEU H H 1 6.800 0.005 . 1 . . . . . . . . 5650 1 1163 . 1 1 92 92 LEU CA C 13 53.384 0.050 . 1 . . . . . . . . 5650 1 1164 . 1 1 92 92 LEU HA H 1 4.363 0.005 . 1 . . . . . . . . 5650 1 1165 . 1 1 92 92 LEU C C 13 174.657 0.050 . 1 . . . . . . . . 5650 1 1166 . 1 1 92 92 LEU CB C 13 39.691 0.050 . 1 . . . . . . . . 5650 1 1167 . 1 1 92 92 LEU HB2 H 1 1.321 0.005 . 2 . . . . . . . . 5650 1 1168 . 1 1 92 92 LEU HB3 H 1 1.558 0.005 . 2 . . . . . . . . 5650 1 1169 . 1 1 92 92 LEU CG C 13 25.840 0.050 . 1 . . . . . . . . 5650 1 1170 . 1 1 92 92 LEU HG H 1 1.359 0.005 . 1 . . . . . . . . 5650 1 1171 . 1 1 92 92 LEU CD1 C 13 23.223 0.050 . 2 . . . . . . . . 5650 1 1172 . 1 1 92 92 LEU HD11 H 1 0.586 0.005 . 2 . . . . . . . . 5650 1 1173 . 1 1 92 92 LEU HD12 H 1 0.586 0.005 . 2 . . . . . . . . 5650 1 1174 . 1 1 92 92 LEU HD13 H 1 0.586 0.005 . 2 . . . . . . . . 5650 1 1175 . 1 1 92 92 LEU CD2 C 13 21.412 0.050 . 2 . . . . . . . . 5650 1 1176 . 1 1 92 92 LEU HD21 H 1 0.814 0.005 . 2 . . . . . . . . 5650 1 1177 . 1 1 92 92 LEU HD22 H 1 0.814 0.005 . 2 . . . . . . . . 5650 1 1178 . 1 1 92 92 LEU HD23 H 1 0.814 0.005 . 2 . . . . . . . . 5650 1 1179 . 1 1 93 93 GLU N N 15 117.272 0.050 . 1 . . . . . . . . 5650 1 1180 . 1 1 93 93 GLU H H 1 7.554 0.005 . 1 . . . . . . . . 5650 1 1181 . 1 1 93 93 GLU CA C 13 56.344 0.050 . 1 . . . . . . . . 5650 1 1182 . 1 1 93 93 GLU HA H 1 4.167 0.005 . 1 . . . . . . . . 5650 1 1183 . 1 1 93 93 GLU C C 13 174.302 0.050 . 1 . . . . . . . . 5650 1 1184 . 1 1 93 93 GLU CB C 13 27.124 0.050 . 1 . . . . . . . . 5650 1 1185 . 1 1 93 93 GLU HB2 H 1 2.014 0.005 . 2 . . . . . . . . 5650 1 1186 . 1 1 93 93 GLU HB3 H 1 2.223 0.005 . 2 . . . . . . . . 5650 1 1187 . 1 1 93 93 GLU CG C 13 33.757 0.050 . 1 . . . . . . . . 5650 1 1188 . 1 1 93 93 GLU HG2 H 1 2.196 0.005 . 2 . . . . . . . . 5650 1 1189 . 1 1 93 93 GLU HG3 H 1 2.391 0.005 . 2 . . . . . . . . 5650 1 1190 . 1 1 94 94 GLY N N 15 104.531 0.050 . 1 . . . . . . . . 5650 1 1191 . 1 1 94 94 GLY H H 1 8.024 0.005 . 1 . . . . . . . . 5650 1 1192 . 1 1 94 94 GLY CA C 13 43.426 0.050 . 1 . . . . . . . . 5650 1 1193 . 1 1 94 94 GLY HA2 H 1 3.910 0.005 . 1 . . . . . . . . 5650 1 1194 . 1 1 94 94 GLY HA3 H 1 4.090 0.005 . 1 . . . . . . . . 5650 1 1195 . 1 1 94 94 GLY C C 13 177.850 0.050 . 1 . . . . . . . . 5650 1 1196 . 1 1 95 95 LEU N N 15 119.193 0.050 . 1 . . . . . . . . 5650 1 1197 . 1 1 95 95 LEU H H 1 7.561 0.005 . 1 . . . . . . . . 5650 1 1198 . 1 1 95 95 LEU CA C 13 53.169 0.050 . 1 . . . . . . . . 5650 1 1199 . 1 1 95 95 LEU HA H 1 4.162 0.005 . 1 . . . . . . . . 5650 1 1200 . 1 1 95 95 LEU C C 13 176.171 0.050 . 1 . . . . . . . . 5650 1 1201 . 1 1 95 95 LEU CB C 13 40.537 0.050 . 1 . . . . . . . . 5650 1 1202 . 1 1 95 95 LEU HB2 H 1 1.439 0.005 . 2 . . . . . . . . 5650 1 1203 . 1 1 95 95 LEU HB3 H 1 1.799 0.005 . 2 . . . . . . . . 5650 1 1204 . 1 1 95 95 LEU CG C 13 24.401 0.050 . 1 . . . . . . . . 5650 1 1205 . 1 1 95 95 LEU HG H 1 1.767 0.005 . 1 . . . . . . . . 5650 1 1206 . 1 1 95 95 LEU CD1 C 13 20.486 0.050 . 2 . . . . . . . . 5650 1 1207 . 1 1 95 95 LEU HD11 H 1 0.712 0.005 . 2 . . . . . . . . 5650 1 1208 . 1 1 95 95 LEU HD12 H 1 0.712 0.005 . 2 . . . . . . . . 5650 1 1209 . 1 1 95 95 LEU HD13 H 1 0.712 0.005 . 2 . . . . . . . . 5650 1 1210 . 1 1 95 95 LEU CD2 C 13 23.835 0.050 . 2 . . . . . . . . 5650 1 1211 . 1 1 95 95 LEU HD21 H 1 0.970 0.005 . 2 . . . . . . . . 5650 1 1212 . 1 1 95 95 LEU HD22 H 1 0.970 0.005 . 2 . . . . . . . . 5650 1 1213 . 1 1 95 95 LEU HD23 H 1 0.970 0.005 . 2 . . . . . . . . 5650 1 1214 . 1 1 96 96 ILE N N 15 121.144 0.050 . 1 . . . . . . . . 5650 1 1215 . 1 1 96 96 ILE H H 1 7.088 0.005 . 1 . . . . . . . . 5650 1 1216 . 1 1 96 96 ILE CA C 13 60.318 0.050 . 1 . . . . . . . . 5650 1 1217 . 1 1 96 96 ILE HA H 1 3.942 0.005 . 1 . . . . . . . . 5650 1 1218 . 1 1 96 96 ILE CB C 13 37.386 0.050 . 1 . . . . . . . . 5650 1 1219 . 1 1 96 96 ILE HB H 1 1.711 0.005 . 1 . . . . . . . . 5650 1 1220 . 1 1 96 96 ILE CG1 C 13 25.186 0.050 . 1 . . . . . . . . 5650 1 1221 . 1 1 96 96 ILE HG12 H 1 1.034 0.005 . 2 . . . . . . . . 5650 1 1222 . 1 1 96 96 ILE HG13 H 1 1.377 0.005 . 2 . . . . . . . . 5650 1 1223 . 1 1 96 96 ILE CG2 C 13 15.880 0.050 . 1 . . . . . . . . 5650 1 1224 . 1 1 96 96 ILE HG21 H 1 0.711 0.005 . 1 . . . . . . . . 5650 1 1225 . 1 1 96 96 ILE HG22 H 1 0.711 0.005 . 1 . . . . . . . . 5650 1 1226 . 1 1 96 96 ILE HG23 H 1 0.711 0.005 . 1 . . . . . . . . 5650 1 1227 . 1 1 96 96 ILE CD1 C 13 11.758 0.050 . 1 . . . . . . . . 5650 1 1228 . 1 1 96 96 ILE HD11 H 1 0.779 0.005 . 1 . . . . . . . . 5650 1 1229 . 1 1 96 96 ILE HD12 H 1 0.779 0.005 . 1 . . . . . . . . 5650 1 1230 . 1 1 96 96 ILE HD13 H 1 0.779 0.005 . 1 . . . . . . . . 5650 1 stop_ save_