data_5231 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5231 _Entry.Title ; Resonance assignments for stromelysin complexed with a beta-sulfonyl hydroxamate inhibitor ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2001-12-12 _Entry.Accession_date 2001-12-12 _Entry.Last_release_date . _Entry.Original_release_date . _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 Parag Sahasrabudhe . V. . 5231 2 Brian Stockman . J. . 5231 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5231 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 482 5231 '13C chemical shifts' 477 5231 '15N chemical shifts' 134 5231 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 2 . . 2010-01-12 2001-12-12 update BMRB 'complete entry citation' 5231 1 . . 2003-06-09 2001-12-12 original author 'original release' 5231 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5231 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 19888686 _Citation.Full_citation . _Citation.Title 'Resonance assignments for stromelysin complexed with a beta-sulfonyl hydroxamate inhibitor' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biomol. NMR Assignments' _Citation.Journal_name_full . _Citation.Journal_volume 3 _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 183 _Citation.Page_last 186 _Citation.Year 2009 _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 Parag Sahasrabudhe . V. . 5231 1 2 Brian Stockman . J. . 5231 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5231 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8520220 _Citation.Full_citation ; Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93. ; _Citation.Title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 6 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0925-2738 _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 277 _Citation.Page_last 293 _Citation.Year 1995 _Citation.Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; 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 F. Delaglio F. . . 5231 2 2 S. Grzesiek S. . . 5231 2 3 'G. W.' Vuister G. W. . 5231 2 4 G. Zhu G. . . 5231 2 5 J. Pfeifer J. . . 5231 2 6 A. Bax A. . . 5231 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 5231 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11462827 _Citation.Full_citation ; Moseley HN, Monleon D, Montelione GT. Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data. Methods Enzymol. 2001;339:91-108. ; _Citation.Title 'Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Meth. Enzymol.' _Citation.Journal_name_full 'Methods in enzymology' _Citation.Journal_volume 339 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN 0076-6879 _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 91 _Citation.Page_last 108 _Citation.Year 2001 _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 'H. N.' Moseley H. N. . 5231 3 2 D. Monleon D. . . 5231 3 3 'G. T.' Montelione G. T. . 5231 3 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_stromelysin _Assembly.Sf_category assembly _Assembly.Sf_framecode system_stromelysin _Assembly.Entry_ID 5231 _Assembly.ID 1 _Assembly.Name 'Stromelysin complex with a ligand' _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 3.4.24.17 _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 5231 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 stromelysin 1 $stromelysin . . . native . . . . . 5231 1 2 'beta-hydroxamate inhibitor' 2 $HYIN . . . native . . . . . 5231 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Stromelysin complex with a ligand' system 5231 1 stromelysin abbreviation 5231 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'matrix metalloproteinase' 5231 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_stromelysin _Entity.Sf_category entity _Entity.Sf_framecode stromelysin _Entity.Entry_ID 5231 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name stromelysin _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 ; FRTFPGIPKWRKTHLTYRIV NYTPDLPKDAVDSAVEKALK VWEEVTPLTFSRLYEGEADI MISFAVREHGDFYPFDGPGN VLAHAYAPGPGINGDAHFDD DEQWTKDTTGTNLFLVAAHE IGHSLGLFHSANTEALMYPL YHSLTDLTRFRLSQDDINGI QSLYGPPPDSPET ; _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 173 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 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 BMRB 15120 . MMP3 . . . . . 93.06 161 100.00 100.00 8.49e-114 . . . . 5231 1 2 no BMRB 15395 . MMP3 . . . . . 93.06 161 99.38 99.38 1.89e-112 . . . . 5231 1 3 no BMRB 15396 . MMP3 . . . . . 93.06 161 99.38 99.38 1.89e-112 . . . . 5231 1 4 no BMRB 4173 . SLN . . . . . 100.00 173 100.00 100.00 3.06e-123 . . . . 5231 1 5 no BMRB 4364 . stromelysin . . . . . 95.95 166 99.40 99.40 1.46e-116 . . . . 5231 1 6 no BMRB 4365 . stromelysin . . . . . 95.95 166 99.40 99.40 1.46e-116 . . . . 5231 1 7 no BMRB 4366 . stromelysin . . . . . 95.95 166 99.40 99.40 1.46e-116 . . . . 5231 1 8 no BMRB 5099 . MMP-3 . . . . . 100.00 173 99.42 100.00 7.58e-123 . . . . 5231 1 9 no BMRB 5153 . MMP-3 . . . . . 100.00 173 99.42 100.00 7.58e-123 . . . . 5231 1 10 no PDB 1B3D . Stromelysin-1 . . . . . 100.00 173 100.00 100.00 3.06e-123 . . . . 5231 1 11 no PDB 1B8Y . "X-Ray Structure Of Human Stromelysin Catalytic Domain Complexed With Non-Peptide Inhibitors: Implications For Inhibitor Selecti" . . . . . 96.53 167 100.00 100.00 7.97e-119 . . . . 5231 1 12 no PDB 1BIW . "Design And Synthesis Of Conformationally-Constrained Mmp Inhibitors" . . . . . 100.00 173 100.00 100.00 3.06e-123 . . . . 5231 1 13 no PDB 1BM6 . "Solution Structure Of The Catalytic Domain Of Human Stromelysin-1 Complexed To A Potent Non-Peptidic Inhibitor, Nmr, 20 Structu" . . . . . 100.00 173 100.00 100.00 3.06e-123 . . . . 5231 1 14 no PDB 1BQO . "Discovery Of Potent, Achiral Matrix Metalloproteinase Inhibitors" . . . . . 100.00 173 100.00 100.00 3.06e-123 . . . . 5231 1 15 no PDB 1C3I . "Human Stromelysin-1 Catalytic Domain Complexed With Ro-26-2812" . . . . . 100.00 173 100.00 100.00 3.06e-123 . . . . 5231 1 16 no PDB 1C8T . "Human Stromelysin-1 (E202q) Catalytic Domain Complexed With Ro-26-2812" . . . . . 95.95 167 99.40 100.00 1.98e-117 . . . . 5231 1 17 no PDB 1CAQ . "X-Ray Structure Of Human Stromelysin Catalytic Domain Complexes With Non-Peptide Inhibitors: Implication For Inhibitor Selectiv" . . . . . 97.11 168 100.00 100.00 1.17e-119 . . . . 5231 1 18 no PDB 1CIZ . "X-ray Structure Of Human Stromelysin Catalytic Domain Complexes With Non-peptide Inhibitors: Implication For Inhibitor Selectiv" . . . . . 97.11 168 100.00 100.00 1.17e-119 . . . . 5231 1 19 no PDB 1CQR . "Crystal Structure Of The Stromelysin Catalytic Domain At 2.0 A Resolution" . . . . . 100.00 173 100.00 100.00 3.06e-123 . . . . 5231 1 20 no PDB 1D5J . "Crystal Structure Of Mmp3 Complexed With A Thiazepine Based Inhibitor." . . . . . 100.00 173 100.00 100.00 3.06e-123 . . . . 5231 1 21 no PDB 1D7X . "Crystal Structure Of Mmp3 Complexed With A Modified Proline Scaffold Based Inhibitor." . . . . . 100.00 173 100.00 100.00 3.06e-123 . . . . 5231 1 22 no PDB 1D8F . "Crystal Structure Of Mmp3 Complexed With A Piperazine Based Inhibitor." . . . . . 100.00 173 100.00 100.00 3.06e-123 . . . . 5231 1 23 no PDB 1D8M . "Crystal Structure Of Mmp3 Complexed With A Heterocycle- Based Inhibitor" . . . . . 100.00 173 100.00 100.00 3.06e-123 . . . . 5231 1 24 no PDB 1G05 . "Heterocycle-Based Mmp Inhibitor With P2'substituents" . . . . . 100.00 173 100.00 100.00 3.06e-123 . . . . 5231 1 25 no PDB 1G49 . "A Carboxylic Acid Based Inhibitor In Complex With Mmp3" . . . . . 100.00 173 100.00 100.00 3.06e-123 . . . . 5231 1 26 no PDB 1G4K . "X-ray Structure Of A Novel Matrix Metalloproteinase Inhibitor Complexed To Stromelysin" . . . . . 97.11 168 100.00 100.00 1.17e-119 . . . . 5231 1 27 no PDB 1HFS . "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The N-Carboxy-Alkyl Inhibitor L-764," . . . . . 92.49 160 100.00 100.00 4.82e-113 . . . . 5231 1 28 no PDB 1HY7 . "A Carboxylic Acid Based Inhibitor In Complex With Mmp3" . . . . . 100.00 173 100.00 100.00 3.06e-123 . . . . 5231 1 29 no PDB 1OO9 . "Orientation In Solution Of Mmp-3 Catalytic Domain And N- Timp-1 From Residual Dipolar Couplings" . . . . . 97.11 168 100.00 100.00 1.17e-119 . . . . 5231 1 30 no PDB 1QIA . "Crystal Structure Of Stromelysin Catalytic Domain" . . . . . 93.64 162 100.00 100.00 1.05e-114 . . . . 5231 1 31 no PDB 1QIC . "Crystal Structure Of Stromelysin Catalytic Domain" . . . . . 93.06 161 100.00 100.00 6.46e-114 . . . . 5231 1 32 no PDB 1SLM . "Crystal Structure Of Fibroblast Stromelysin-1: The C-Truncated Human Proenzyme" . . . . . 100.00 255 100.00 100.00 2.09e-123 . . . . 5231 1 33 no PDB 1SLN . "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The N-Carboxy-Alkyl Inhibitor L-702," . . . . . 100.00 173 100.00 100.00 3.06e-123 . . . . 5231 1 34 no PDB 1UEA . "Mmp-3TIMP-1 Complex" . . . . . 100.00 173 98.84 98.84 3.88e-121 . . . . 5231 1 35 no PDB 1UMS . "Stromelysin-1 Catalytic Domain With Hydrophobic Inhibitor Bound, Ph 7.0, 32oc, 20 Mm Cacl2, 15% Acetonitrile; Nmr Ensemble Of 2" . . . . . 100.00 174 100.00 100.00 4.30e-123 . . . . 5231 1 36 no PDB 1UMT . "Stromelysin-1 Catalytic Domain With Hydrophobic Inhibitor Bound, Ph 7.0, 32oc, 20 Mm Cacl2, 15% Acetonitrile; Nmr Average Of 20" . . . . . 100.00 174 100.00 100.00 4.30e-123 . . . . 5231 1 37 no PDB 1USN . "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With Thiadiazole Inhibitor Pnu-142372" . . . . . 95.38 165 100.00 100.00 3.45e-117 . . . . 5231 1 38 no PDB 2D1O . "Stromelysin-1 (Mmp-3) Complexed To A Hydroxamic Acid Inhibitor" . . . . . 98.84 171 100.00 100.00 7.84e-122 . . . . 5231 1 39 no PDB 2JNP . "Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3) In The Presence Of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]glycyl Hydro" . . . . . 93.06 161 100.00 100.00 8.49e-114 . . . . 5231 1 40 no PDB 2JT5 . "Solution Structure Of Matrix Metalloproteinase 3 (mmp-3) In The Presence Of N-hydroxy-2-[n-(2-hydroxyethyl)biphenyl-4- Sulfonam" . . . . . 93.06 161 100.00 100.00 8.49e-114 . . . . 5231 1 41 no PDB 2JT6 . "Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3) In The Presence Of 3-4'-Cyanobyphenyl-4-Yloxy)-N- Hdydroxypropionamide" . . . . . 93.06 161 100.00 100.00 8.49e-114 . . . . 5231 1 42 no PDB 2SRT . "Catalytic Domain Of Human Stromelysin-1 At Ph 5.5 And 40oc Complexed With Inhibitor" . . . . . 100.00 173 100.00 100.00 3.06e-123 . . . . 5231 1 43 no PDB 2USN . "Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With Thiadiazole Inhibitor Pnu-141803" . . . . . 95.38 165 100.00 100.00 3.45e-117 . . . . 5231 1 44 no PDB 3OHL . "Catalytic Domain Of Stromelysin-1 In Complex With N-Hydroxy-2-(4- Methoxy-N-(Pyridine-3-Ylmethyl)phenylsulfonamido)acetamide" . . . . . 96.53 167 100.00 100.00 7.97e-119 . . . . 5231 1 45 no PDB 3OHO . "Catalytic Domain Of Stromelysin-1 In Complex With N-Hydroxy-2-(4- Methylphenylsulfonamido)acetamide" . . . . . 97.69 169 100.00 100.00 2.61e-120 . . . . 5231 1 46 no PDB 3USN . "Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The Thiadiazole Inhibitor Ipnu-107859, Nmr, " . . . . . 97.11 168 100.00 100.00 1.17e-119 . . . . 5231 1 47 no PDB 4DPE . "Structure Of Mmp3 Complexed With A Platinum-based Inhibitor." . . . . . 100.00 173 100.00 100.00 3.06e-123 . . . . 5231 1 48 no PDB 4G9L . "Structure Of Mmp3 Complexed With Nngh Inhibitor" . . . . . 100.00 173 100.00 100.00 3.06e-123 . . . . 5231 1 49 no PDB 4JA1 . "Structure Of Mmp3 Complexed With A Platinum-based Inhibitor" . . . . . 100.00 173 100.00 100.00 3.06e-123 . . . . 5231 1 50 no DBJ BAD97003 . "matrix metalloproteinase 3 preproprotein variant [Homo sapiens]" . . . . . 100.00 477 100.00 100.00 4.32e-120 . . . . 5231 1 51 no DBJ BAD97011 . "matrix metalloproteinase 3 preproprotein variant [Homo sapiens]" . . . . . 100.00 477 100.00 100.00 4.32e-120 . . . . 5231 1 52 no DBJ BAG36115 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 477 100.00 100.00 3.48e-120 . . . . 5231 1 53 no EMBL CAA28859 . "preprostromelysin [Homo sapiens]" . . . . . 100.00 477 100.00 100.00 3.48e-120 . . . . 5231 1 54 no GB AAA00036 . "prostromelysin=matrix metalloproteinase [human, Peptide, 477 aa]" . . . . . 100.00 477 100.00 100.00 4.32e-120 . . . . 5231 1 55 no GB AAA36321 . "matrix metalloproteinase-3 [Homo sapiens]" . . . . . 100.00 477 100.00 100.00 4.32e-120 . . . . 5231 1 56 no GB AAB36942 . "stromelysin [Homo sapiens]" . . . . . 100.00 477 100.00 100.00 4.32e-120 . . . . 5231 1 57 no GB AAD45887 . "stromelysin catalytic domain [synthetic construct]" . . . . . 100.00 174 100.00 100.00 4.30e-123 . . . . 5231 1 58 no GB AAH69676 . "Matrix metallopeptidase 3 (stromelysin 1, progelatinase) [Homo sapiens]" . . . . . 100.00 477 100.00 100.00 4.32e-120 . . . . 5231 1 59 no REF NP_002413 . "stromelysin-1 preproprotein [Homo sapiens]" . . . . . 100.00 477 100.00 100.00 3.48e-120 . . . . 5231 1 60 no REF XP_002822450 . "PREDICTED: stromelysin-1 [Pongo abelii]" . . . . . 100.00 477 98.84 100.00 1.36e-119 . . . . 5231 1 61 no REF XP_003253099 . "PREDICTED: stromelysin-1 [Nomascus leucogenys]" . . . . . 100.00 477 99.42 100.00 2.65e-120 . . . . 5231 1 62 no REF XP_003828425 . "PREDICTED: stromelysin-1 [Pan paniscus]" . . . . . 100.00 477 100.00 100.00 2.09e-120 . . . . 5231 1 63 no REF XP_004052086 . "PREDICTED: stromelysin-1 [Gorilla gorilla gorilla]" . . . . . 100.00 477 98.84 99.42 1.06e-118 . . . . 5231 1 64 no SP P08254 . "RecName: Full=Stromelysin-1; Short=SL-1; AltName: Full=Matrix metalloproteinase-3; Short=MMP-3; AltName: Full=Transin-1; Flags:" . . . . . 100.00 477 100.00 100.00 3.48e-120 . . . . 5231 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID stromelysin common 5231 1 stromelysin abbreviation 5231 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 . PHE . 5231 1 2 . ARG . 5231 1 3 . THR . 5231 1 4 . PHE . 5231 1 5 . PRO . 5231 1 6 . GLY . 5231 1 7 . ILE . 5231 1 8 . PRO . 5231 1 9 . LYS . 5231 1 10 . TRP . 5231 1 11 . ARG . 5231 1 12 . LYS . 5231 1 13 . THR . 5231 1 14 . HIS . 5231 1 15 . LEU . 5231 1 16 . THR . 5231 1 17 . TYR . 5231 1 18 . ARG . 5231 1 19 . ILE . 5231 1 20 . VAL . 5231 1 21 . ASN . 5231 1 22 . TYR . 5231 1 23 . THR . 5231 1 24 . PRO . 5231 1 25 . ASP . 5231 1 26 . LEU . 5231 1 27 . PRO . 5231 1 28 . LYS . 5231 1 29 . ASP . 5231 1 30 . ALA . 5231 1 31 . VAL . 5231 1 32 . ASP . 5231 1 33 . SER . 5231 1 34 . ALA . 5231 1 35 . VAL . 5231 1 36 . GLU . 5231 1 37 . LYS . 5231 1 38 . ALA . 5231 1 39 . LEU . 5231 1 40 . LYS . 5231 1 41 . VAL . 5231 1 42 . TRP . 5231 1 43 . GLU . 5231 1 44 . GLU . 5231 1 45 . VAL . 5231 1 46 . THR . 5231 1 47 . PRO . 5231 1 48 . LEU . 5231 1 49 . THR . 5231 1 50 . PHE . 5231 1 51 . SER . 5231 1 52 . ARG . 5231 1 53 . LEU . 5231 1 54 . TYR . 5231 1 55 . GLU . 5231 1 56 . GLY . 5231 1 57 . GLU . 5231 1 58 . ALA . 5231 1 59 . ASP . 5231 1 60 . ILE . 5231 1 61 . MET . 5231 1 62 . ILE . 5231 1 63 . SER . 5231 1 64 . PHE . 5231 1 65 . ALA . 5231 1 66 . VAL . 5231 1 67 . ARG . 5231 1 68 . GLU . 5231 1 69 . HIS . 5231 1 70 . GLY . 5231 1 71 . ASP . 5231 1 72 . PHE . 5231 1 73 . TYR . 5231 1 74 . PRO . 5231 1 75 . PHE . 5231 1 76 . ASP . 5231 1 77 . GLY . 5231 1 78 . PRO . 5231 1 79 . GLY . 5231 1 80 . ASN . 5231 1 81 . VAL . 5231 1 82 . LEU . 5231 1 83 . ALA . 5231 1 84 . HIS . 5231 1 85 . ALA . 5231 1 86 . TYR . 5231 1 87 . ALA . 5231 1 88 . PRO . 5231 1 89 . GLY . 5231 1 90 . PRO . 5231 1 91 . GLY . 5231 1 92 . ILE . 5231 1 93 . ASN . 5231 1 94 . GLY . 5231 1 95 . ASP . 5231 1 96 . ALA . 5231 1 97 . HIS . 5231 1 98 . PHE . 5231 1 99 . ASP . 5231 1 100 . ASP . 5231 1 101 . ASP . 5231 1 102 . GLU . 5231 1 103 . GLN . 5231 1 104 . TRP . 5231 1 105 . THR . 5231 1 106 . LYS . 5231 1 107 . ASP . 5231 1 108 . THR . 5231 1 109 . THR . 5231 1 110 . GLY . 5231 1 111 . THR . 5231 1 112 . ASN . 5231 1 113 . LEU . 5231 1 114 . PHE . 5231 1 115 . LEU . 5231 1 116 . VAL . 5231 1 117 . ALA . 5231 1 118 . ALA . 5231 1 119 . HIS . 5231 1 120 . GLU . 5231 1 121 . ILE . 5231 1 122 . GLY . 5231 1 123 . HIS . 5231 1 124 . SER . 5231 1 125 . LEU . 5231 1 126 . GLY . 5231 1 127 . LEU . 5231 1 128 . PHE . 5231 1 129 . HIS . 5231 1 130 . SER . 5231 1 131 . ALA . 5231 1 132 . ASN . 5231 1 133 . THR . 5231 1 134 . GLU . 5231 1 135 . ALA . 5231 1 136 . LEU . 5231 1 137 . MET . 5231 1 138 . TYR . 5231 1 139 . PRO . 5231 1 140 . LEU . 5231 1 141 . TYR . 5231 1 142 . HIS . 5231 1 143 . SER . 5231 1 144 . LEU . 5231 1 145 . THR . 5231 1 146 . ASP . 5231 1 147 . LEU . 5231 1 148 . THR . 5231 1 149 . ARG . 5231 1 150 . PHE . 5231 1 151 . ARG . 5231 1 152 . LEU . 5231 1 153 . SER . 5231 1 154 . GLN . 5231 1 155 . ASP . 5231 1 156 . ASP . 5231 1 157 . ILE . 5231 1 158 . ASN . 5231 1 159 . GLY . 5231 1 160 . ILE . 5231 1 161 . GLN . 5231 1 162 . SER . 5231 1 163 . LEU . 5231 1 164 . TYR . 5231 1 165 . GLY . 5231 1 166 . PRO . 5231 1 167 . PRO . 5231 1 168 . PRO . 5231 1 169 . ASP . 5231 1 170 . SER . 5231 1 171 . PRO . 5231 1 172 . GLU . 5231 1 173 . THR . 5231 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 . PHE 1 1 5231 1 . ARG 2 2 5231 1 . THR 3 3 5231 1 . PHE 4 4 5231 1 . PRO 5 5 5231 1 . GLY 6 6 5231 1 . ILE 7 7 5231 1 . PRO 8 8 5231 1 . LYS 9 9 5231 1 . TRP 10 10 5231 1 . ARG 11 11 5231 1 . LYS 12 12 5231 1 . THR 13 13 5231 1 . HIS 14 14 5231 1 . LEU 15 15 5231 1 . THR 16 16 5231 1 . TYR 17 17 5231 1 . ARG 18 18 5231 1 . ILE 19 19 5231 1 . VAL 20 20 5231 1 . ASN 21 21 5231 1 . TYR 22 22 5231 1 . THR 23 23 5231 1 . PRO 24 24 5231 1 . ASP 25 25 5231 1 . LEU 26 26 5231 1 . PRO 27 27 5231 1 . LYS 28 28 5231 1 . ASP 29 29 5231 1 . ALA 30 30 5231 1 . VAL 31 31 5231 1 . ASP 32 32 5231 1 . SER 33 33 5231 1 . ALA 34 34 5231 1 . VAL 35 35 5231 1 . GLU 36 36 5231 1 . LYS 37 37 5231 1 . ALA 38 38 5231 1 . LEU 39 39 5231 1 . LYS 40 40 5231 1 . VAL 41 41 5231 1 . TRP 42 42 5231 1 . GLU 43 43 5231 1 . GLU 44 44 5231 1 . VAL 45 45 5231 1 . THR 46 46 5231 1 . PRO 47 47 5231 1 . LEU 48 48 5231 1 . THR 49 49 5231 1 . PHE 50 50 5231 1 . SER 51 51 5231 1 . ARG 52 52 5231 1 . LEU 53 53 5231 1 . TYR 54 54 5231 1 . GLU 55 55 5231 1 . GLY 56 56 5231 1 . GLU 57 57 5231 1 . ALA 58 58 5231 1 . ASP 59 59 5231 1 . ILE 60 60 5231 1 . MET 61 61 5231 1 . ILE 62 62 5231 1 . SER 63 63 5231 1 . PHE 64 64 5231 1 . ALA 65 65 5231 1 . VAL 66 66 5231 1 . ARG 67 67 5231 1 . GLU 68 68 5231 1 . HIS 69 69 5231 1 . GLY 70 70 5231 1 . ASP 71 71 5231 1 . PHE 72 72 5231 1 . TYR 73 73 5231 1 . PRO 74 74 5231 1 . PHE 75 75 5231 1 . ASP 76 76 5231 1 . GLY 77 77 5231 1 . PRO 78 78 5231 1 . GLY 79 79 5231 1 . ASN 80 80 5231 1 . VAL 81 81 5231 1 . LEU 82 82 5231 1 . ALA 83 83 5231 1 . HIS 84 84 5231 1 . ALA 85 85 5231 1 . TYR 86 86 5231 1 . ALA 87 87 5231 1 . PRO 88 88 5231 1 . GLY 89 89 5231 1 . PRO 90 90 5231 1 . GLY 91 91 5231 1 . ILE 92 92 5231 1 . ASN 93 93 5231 1 . GLY 94 94 5231 1 . ASP 95 95 5231 1 . ALA 96 96 5231 1 . HIS 97 97 5231 1 . PHE 98 98 5231 1 . ASP 99 99 5231 1 . ASP 100 100 5231 1 . ASP 101 101 5231 1 . GLU 102 102 5231 1 . GLN 103 103 5231 1 . TRP 104 104 5231 1 . THR 105 105 5231 1 . LYS 106 106 5231 1 . ASP 107 107 5231 1 . THR 108 108 5231 1 . THR 109 109 5231 1 . GLY 110 110 5231 1 . THR 111 111 5231 1 . ASN 112 112 5231 1 . LEU 113 113 5231 1 . PHE 114 114 5231 1 . LEU 115 115 5231 1 . VAL 116 116 5231 1 . ALA 117 117 5231 1 . ALA 118 118 5231 1 . HIS 119 119 5231 1 . GLU 120 120 5231 1 . ILE 121 121 5231 1 . GLY 122 122 5231 1 . HIS 123 123 5231 1 . SER 124 124 5231 1 . LEU 125 125 5231 1 . GLY 126 126 5231 1 . LEU 127 127 5231 1 . PHE 128 128 5231 1 . HIS 129 129 5231 1 . SER 130 130 5231 1 . ALA 131 131 5231 1 . ASN 132 132 5231 1 . THR 133 133 5231 1 . GLU 134 134 5231 1 . ALA 135 135 5231 1 . LEU 136 136 5231 1 . MET 137 137 5231 1 . TYR 138 138 5231 1 . PRO 139 139 5231 1 . LEU 140 140 5231 1 . TYR 141 141 5231 1 . HIS 142 142 5231 1 . SER 143 143 5231 1 . LEU 144 144 5231 1 . THR 145 145 5231 1 . ASP 146 146 5231 1 . LEU 147 147 5231 1 . THR 148 148 5231 1 . ARG 149 149 5231 1 . PHE 150 150 5231 1 . ARG 151 151 5231 1 . LEU 152 152 5231 1 . SER 153 153 5231 1 . GLN 154 154 5231 1 . ASP 155 155 5231 1 . ASP 156 156 5231 1 . ILE 157 157 5231 1 . ASN 158 158 5231 1 . GLY 159 159 5231 1 . ILE 160 160 5231 1 . GLN 161 161 5231 1 . SER 162 162 5231 1 . LEU 163 163 5231 1 . TYR 164 164 5231 1 . GLY 165 165 5231 1 . PRO 166 166 5231 1 . PRO 167 167 5231 1 . PRO 168 168 5231 1 . ASP 169 169 5231 1 . SER 170 170 5231 1 . PRO 171 171 5231 1 . GLU 172 172 5231 1 . THR 173 173 5231 1 stop_ save_ save_HYIN _Entity.Sf_category entity _Entity.Sf_framecode HYIN _Entity.Entry_ID 5231 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name 'beta-hydroxamate inhibitor' _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID HYIN _Entity.Nonpolymer_comp_label $chem_comp_HYIN _Entity.Number_of_monomers 1 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 2 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'beta-hydroxamate inhibitor' common 5231 2 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 . HYIN . 5231 2 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 . HYIN 1 1 5231 2 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 5231 _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 $stromelysin . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 5231 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 5231 _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 $stromelysin . ; Stromelysin was prepared by overexpression in E.coli strain BL21(DE3)(pLyseE) transformed with pstro255 expression vector. ; . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5231 1 2 2 $HYIN . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5231 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_HYIN _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_HYIN _Chem_comp.Entry_ID 5231 _Chem_comp.ID HYIN _Chem_comp.Provenance BMRB _Chem_comp.Name 'beta-hydroxamate inhibitor' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code HYIN _Chem_comp.PDB_code . _Chem_comp.Ambiguous_flag . _Chem_comp.Initial_date . _Chem_comp.Modified_date . _Chem_comp.Release_status . _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code . _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic no _Chem_comp.Aromatic yes _Chem_comp.Formula C18H39O8N1S2 _Chem_comp.Formula_weight . _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag . _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag . _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site . _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details . _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_common_name.Name _Chem_comp_common_name.Type _Chem_comp_common_name.Entry_ID _Chem_comp_common_name.Comp_ID 'beta-hydroxamate inhibitor' common 5231 HYIN stop_ loop_ _Chem_comp_systematic_name.Name _Chem_comp_systematic_name.Naming_system _Chem_comp_systematic_name.Entry_ID _Chem_comp_systematic_name.Comp_ID N-hydroxy-3-[(4-methoxyphenyl)sulfonyl]-2-{[(4-methoxyphenyl)sulfonyl]methyl}propanamide IUPAC 5231 HYIN stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID N1 . . . . N . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN S1 . . . . S . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN S2 . . . . S . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN O1 . . . . O . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN O2 . . . . O . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN O3 . . . . O . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN O4 . . . . O . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN O5 . . . . O . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN O6 . . . . O . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN O7 . . . . O . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN O8 . . . . O . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN C1 . . . . C . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN C2 . . . . C . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN C3 . . . . C . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN C4 . . . . C . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN C5 . . . . C . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN C6 . . . . C . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN C7 . . . . C . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN C8 . . . . C . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN C9 . . . . C . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN C10 . . . . C . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN C11 . . . . C . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN C12 . . . . C . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN C13 . . . . C . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN C14 . . . . C . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN C15 . . . . C . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN C16 . . . . C . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN C17 . . . . C . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN C18 . . . . C . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN HO . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN HN . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN H2 . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN H3A . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN H3B . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN H4A . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN H4B . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN H6 . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN H7 . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN H9 . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN H10 . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN H13 . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN H14 . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN H16 . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN H17 . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN H11A . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN H11B . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN H11C . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN H18A . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN H18B . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN H18C . . . . H . . . 0 . . . . . . . . . . . . . . . . . . . . . 5231 HYIN stop_ loop_ _Atom_nomenclature.Atom_ID _Atom_nomenclature.Atom_name _Atom_nomenclature.Naming_system _Atom_nomenclature.Entry_ID _Atom_nomenclature.Comp_ID . N1 . 5231 HYIN . S1 . 5231 HYIN . S2 . 5231 HYIN . O1 . 5231 HYIN . O2 . 5231 HYIN . O3 . 5231 HYIN . O4 . 5231 HYIN . O5 . 5231 HYIN . O6 . 5231 HYIN . O7 . 5231 HYIN . O8 . 5231 HYIN . C1 . 5231 HYIN . C2 . 5231 HYIN . C3 . 5231 HYIN . C4 . 5231 HYIN . C5 . 5231 HYIN . C6 . 5231 HYIN . C7 . 5231 HYIN . C8 . 5231 HYIN . C9 . 5231 HYIN . C10 . 5231 HYIN . C11 . 5231 HYIN . C12 . 5231 HYIN . C13 . 5231 HYIN . C14 . 5231 HYIN . C15 . 5231 HYIN . C16 . 5231 HYIN . C17 . 5231 HYIN . C18 . 5231 HYIN . HO . 5231 HYIN . HN . 5231 HYIN . H2 . 5231 HYIN . H3A . 5231 HYIN . H3B . 5231 HYIN . H4A . 5231 HYIN . H4B . 5231 HYIN . H6 . 5231 HYIN . H7 . 5231 HYIN . H9 . 5231 HYIN . H10 . 5231 HYIN . H13 . 5231 HYIN . H14 . 5231 HYIN . H16 . 5231 HYIN . H17 . 5231 HYIN . H11A . 5231 HYIN . H11B . 5231 HYIN . H11C . 5231 HYIN . H18A . 5231 HYIN . H18B . 5231 HYIN . H18C . 5231 HYIN stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING HO O1 . . . . 5231 HYIN 2 . SING O1 N1 . . . . 5231 HYIN 3 . SING N1 HN . . . . 5231 HYIN 4 . SING N1 C1 . . . . 5231 HYIN 5 . SING C1 C2 . . . . 5231 HYIN 6 . SING C2 C3 . . . . 5231 HYIN 7 . SING C2 C4 . . . . 5231 HYIN 8 . SING C2 H2 . . . . 5231 HYIN 9 . SING C3 H3A . . . . 5231 HYIN 10 . SING C3 H3B . . . . 5231 HYIN 11 . SING C3 S1 . . . . 5231 HYIN 12 . SING S1 C5 . . . . 5231 HYIN 13 . SING C5 C6 . . . . 5231 HYIN 14 . SING C6 H6 . . . . 5231 HYIN 15 . SING C7 H7 . . . . 5231 HYIN 16 . SING C7 C8 . . . . 5231 HYIN 17 . SING C8 O5 . . . . 5231 HYIN 18 . SING C9 H9 . . . . 5231 HYIN 19 . SING C9 C10 . . . . 5231 HYIN 20 . SING C10 H10 . . . . 5231 HYIN 21 . SING O5 C11 . . . . 5231 HYIN 22 . SING C11 H11A . . . . 5231 HYIN 23 . SING C11 H11B . . . . 5231 HYIN 24 . SING C11 H11C . . . . 5231 HYIN 25 . SING C4 H4A . . . . 5231 HYIN 26 . SING C4 H4B . . . . 5231 HYIN 27 . SING C4 S2 . . . . 5231 HYIN 28 . SING S2 C12 . . . . 5231 HYIN 29 . SING C12 C13 . . . . 5231 HYIN 30 . SING C13 H13 . . . . 5231 HYIN 31 . SING C14 H14 . . . . 5231 HYIN 32 . SING C14 C15 . . . . 5231 HYIN 33 . SING C15 O8 . . . . 5231 HYIN 34 . SING C16 H16 . . . . 5231 HYIN 35 . SING C16 C17 . . . . 5231 HYIN 36 . SING C17 H17 . . . . 5231 HYIN 37 . SING O8 C18 . . . . 5231 HYIN 38 . SING C18 H18A . . . . 5231 HYIN 39 . SING C18 H18B . . . . 5231 HYIN 40 . SING C18 H18C . . . . 5231 HYIN 41 . DOUB C1 O2 . . . . 5231 HYIN 42 . DOUB S1 O3 . . . . 5231 HYIN 43 . DOUB S1 O4 . . . . 5231 HYIN 44 . DOUB C5 C6 . . . . 5231 HYIN 45 . DOUB C7 C8 . . . . 5231 HYIN 46 . DOUB C9 C10 . . . . 5231 HYIN 47 . DOUB S2 O6 . . . . 5231 HYIN 48 . DOUB S2 O7 . . . . 5231 HYIN 49 . DOUB C12 C13 . . . . 5231 HYIN 50 . DOUB C14 C15 . . . . 5231 HYIN 51 . DOUB C16 C17 . . . . 5231 HYIN stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5231 _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 stromelysin '[U-100% 13C; U-100% 15N]' . . 1 $stromelysin . . 0.9 . . mM . . . . 5231 1 2 'beta-hydroxamate inhibitor' . . . 2 $HYIN . . 1 . . mM . . . . 5231 1 3 d-imidazole . . . . . . . 10 . . mM . . . . 5231 1 4 CaCl2 . . . . . . . 2.5 . . mM . . . . 5231 1 5 ZnCl2 . . . . . . . 5 . . uM . . . . 5231 1 6 NaN3 . . . . . . . 0.02 . . % . . . . 5231 1 stop_ save_ ####################### # Sample conditions # ####################### save_stromelysin_condition_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode stromelysin_condition_1 _Sample_condition_list.Entry_ID 5231 _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 6.6 0.1 pH 5231 1 temperature 300 0.1 K 5231 1 stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Software.Sf_category software _Software.Sf_framecode XWINNMR _Software.Entry_ID 5231 _Software.ID 1 _Software.Name XWINNMR _Software.Version 2.6 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data acquisition' 5231 1 stop_ save_ save_NMRPIPE _Software.Sf_category software _Software.Sf_framecode NMRPIPE _Software.Entry_ID 5231 _Software.ID 2 _Software.Name NMRPIPE _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data processing' 5231 2 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 2 $ref_1 5231 2 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 5231 _Software.ID 3 _Software.Name SPARKY _Software.Version . _Software.Details 'Goddard and Kneller, University of California, San Francisco.' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'peak picking' 5231 3 'peak management' 5231 3 stop_ save_ save_AUTOASSIGN _Software.Sf_category software _Software.Sf_framecode AUTOASSIGN _Software.Entry_ID 5231 _Software.ID 4 _Software.Name AUTOASSIGN _Software.Version . _Software.Details 'Licensed from Geneformatics (http://www.geneformatics.com).' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Automated resonance assignment' 5231 4 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 3 $ref_2 5231 4 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 5231 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5231 _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 Bruker DRX . 600 . . . 5231 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 5231 _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 '1H-15N HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $stromelysin_condition_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5231 1 2 HNCO . . . . . . . . . . . 1 $sample_1 . . . 1 $stromelysin_condition_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5231 1 3 HNCA . . . . . . . . . . . 1 $sample_1 . . . 1 $stromelysin_condition_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5231 1 4 HN(CO)CA . . . . . . . . . . . 1 $sample_1 . . . 1 $stromelysin_condition_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5231 1 5 CBCA(CO)NH . . . . . . . . . . . 1 $sample_1 . . . 1 $stromelysin_condition_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5231 1 6 CBCANH . . . . . . . . . . . 1 $sample_1 . . . 1 $stromelysin_condition_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5231 1 7 HBHA(CO)NH . . . . . . . . . . . 1 $sample_1 . . . 1 $stromelysin_condition_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5231 1 8 (H)CC(CO)NH-TOCSY . . . . . . . . . . . 1 $sample_1 . . . 1 $stromelysin_condition_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5231 1 9 H(CC)(CO)NH-TOCSY . . . . . . . . . . . 1 $sample_1 . . . 1 $stromelysin_condition_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5231 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 5231 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '1H-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 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _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 5231 _NMR_spec_expt.ID 2 _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 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _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 5231 _NMR_spec_expt.ID 3 _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 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _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 5231 _NMR_spec_expt.ID 4 _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 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _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 5231 _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 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _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 5231 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name 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 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _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 5231 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name HBHA(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 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _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 5231 _NMR_spec_expt.ID 8 _NMR_spec_expt.Name (H)CC(CO)NH-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 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _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 5231 _NMR_spec_expt.ID 9 _NMR_spec_expt.Name H(CC)(CO)NH-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 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _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 5231 _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 H2O protons . . . . ppm 4.70 internal direct . internal cylindrical parallel . . . . . . 5231 1 C 13 H2O protons . . . . ppm 4.70 internal indirect 0.251449530 internal cylindrical parallel . . . . . . 5231 1 N 15 H2O protons . . . . ppm 4.70 internal indirect 0.101329118 internal cylindrical parallel . . . . . . 5231 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_stromelysin_CS _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode stromelysin_CS _Assigned_chem_shift_list.Entry_ID 5231 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $stromelysin_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 $sample_1 . 5231 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 2 2 ARG HA H 1 4.879 0.02 . 1 . . . . . . . . 5231 1 2 . 1 1 2 2 ARG C C 13 175.4 0.1 . 1 . . . . . . . . 5231 1 3 . 1 1 2 2 ARG CA C 13 55.74 0.1 . 1 . . . . . . . . 5231 1 4 . 1 1 2 2 ARG CB C 13 35.74 0.1 . 1 . . . . . . . . 5231 1 5 . 1 1 2 2 ARG CG C 13 31.56 0.1 . 1 . . . . . . . . 5231 1 6 . 1 1 3 3 THR H H 1 8.36 0.02 . 1 . . . . . . . . 5231 1 7 . 1 1 3 3 THR CA C 13 60.38 0.1 . 1 . . . . . . . . 5231 1 8 . 1 1 3 3 THR N N 15 112.5 0.1 . 1 . . . . . . . . 5231 1 9 . 1 1 11 11 ARG HA H 1 4.648 0.02 . 1 . . . . . . . . 5231 1 10 . 1 1 11 11 ARG HB2 H 1 2.268 0.02 . 2 . . . . . . . . 5231 1 11 . 1 1 11 11 ARG HG2 H 1 1.889 0.02 . 2 . . . . . . . . 5231 1 12 . 1 1 11 11 ARG HD2 H 1 3.295 0.02 . 2 . . . . . . . . 5231 1 13 . 1 1 11 11 ARG C C 13 174.8 0.1 . 1 . . . . . . . . 5231 1 14 . 1 1 11 11 ARG CA C 13 55.39 0.1 . 1 . . . . . . . . 5231 1 15 . 1 1 11 11 ARG CB C 13 29.06 0.1 . 1 . . . . . . . . 5231 1 16 . 1 1 11 11 ARG CG C 13 27.98 0.1 . 1 . . . . . . . . 5231 1 17 . 1 1 11 11 ARG CD C 13 43.51 0.1 . 1 . . . . . . . . 5231 1 18 . 1 1 12 12 LYS H H 1 7.50 0.02 . 1 . . . . . . . . 5231 1 19 . 1 1 12 12 LYS HA H 1 4.822 0.02 . 1 . . . . . . . . 5231 1 20 . 1 1 12 12 LYS HB2 H 1 2.077 0.02 . 2 . . . . . . . . 5231 1 21 . 1 1 12 12 LYS C C 13 174.3 0.1 . 1 . . . . . . . . 5231 1 22 . 1 1 12 12 LYS CA C 13 54.36 0.1 . 1 . . . . . . . . 5231 1 23 . 1 1 12 12 LYS CB C 13 34.58 0.1 . 1 . . . . . . . . 5231 1 24 . 1 1 12 12 LYS N N 15 116.7 0.1 . 1 . . . . . . . . 5231 1 25 . 1 1 13 13 THR H H 1 7.99 0.02 . 1 . . . . . . . . 5231 1 26 . 1 1 13 13 THR HA H 1 4.396 0.02 . 1 . . . . . . . . 5231 1 27 . 1 1 13 13 THR HG21 H 1 1.175 0.02 . 1 . . . . . . . . 5231 1 28 . 1 1 13 13 THR HG22 H 1 1.175 0.02 . 1 . . . . . . . . 5231 1 29 . 1 1 13 13 THR HG23 H 1 1.175 0.02 . 1 . . . . . . . . 5231 1 30 . 1 1 13 13 THR C C 13 172.6 0.1 . 1 . . . . . . . . 5231 1 31 . 1 1 13 13 THR CA C 13 61.29 0.1 . 1 . . . . . . . . 5231 1 32 . 1 1 13 13 THR CB C 13 69.49 0.1 . 1 . . . . . . . . 5231 1 33 . 1 1 13 13 THR CG2 C 13 21.84 0.1 . 1 . . . . . . . . 5231 1 34 . 1 1 13 13 THR N N 15 105.4 0.1 . 1 . . . . . . . . 5231 1 35 . 1 1 14 14 HIS H H 1 7.01 0.02 . 1 . . . . . . . . 5231 1 36 . 1 1 14 14 HIS HA H 1 5.181 0.02 . 1 . . . . . . . . 5231 1 37 . 1 1 14 14 HIS HB2 H 1 3.471 0.02 . 1 . . . . . . . . 5231 1 38 . 1 1 14 14 HIS HB3 H 1 3.124 0.02 . 1 . . . . . . . . 5231 1 39 . 1 1 14 14 HIS C C 13 173.8 0.1 . 1 . . . . . . . . 5231 1 40 . 1 1 14 14 HIS CA C 13 54.17 0.1 . 1 . . . . . . . . 5231 1 41 . 1 1 14 14 HIS CB C 13 29.76 0.1 . 1 . . . . . . . . 5231 1 42 . 1 1 14 14 HIS N N 15 119.7 0.1 . 1 . . . . . . . . 5231 1 43 . 1 1 15 15 LEU H H 1 8.21 0.02 . 1 . . . . . . . . 5231 1 44 . 1 1 15 15 LEU HA H 1 4.551 0.02 . 1 . . . . . . . . 5231 1 45 . 1 1 15 15 LEU HB2 H 1 1.381 0.02 . 2 . . . . . . . . 5231 1 46 . 1 1 15 15 LEU HG H 1 1.255 0.02 . 1 . . . . . . . . 5231 1 47 . 1 1 15 15 LEU HD11 H 1 0.781 0.02 . 2 . . . . . . . . 5231 1 48 . 1 1 15 15 LEU HD12 H 1 0.781 0.02 . 2 . . . . . . . . 5231 1 49 . 1 1 15 15 LEU HD13 H 1 0.781 0.02 . 2 . . . . . . . . 5231 1 50 . 1 1 15 15 LEU C C 13 176.3 0.1 . 1 . . . . . . . . 5231 1 51 . 1 1 15 15 LEU CA C 13 53.12 0.1 . 1 . . . . . . . . 5231 1 52 . 1 1 15 15 LEU CB C 13 45.28 0.1 . 1 . . . . . . . . 5231 1 53 . 1 1 15 15 LEU N N 15 128.0 0.1 . 1 . . . . . . . . 5231 1 54 . 1 1 16 16 THR H H 1 9.16 0.02 . 1 . . . . . . . . 5231 1 55 . 1 1 16 16 THR HA H 1 5.809 0.02 . 1 . . . . . . . . 5231 1 56 . 1 1 16 16 THR HG21 H 1 1.192 0.02 . 1 . . . . . . . . 5231 1 57 . 1 1 16 16 THR HG22 H 1 1.192 0.02 . 1 . . . . . . . . 5231 1 58 . 1 1 16 16 THR HG23 H 1 1.192 0.02 . 1 . . . . . . . . 5231 1 59 . 1 1 16 16 THR C C 13 174.5 0.1 . 1 . . . . . . . . 5231 1 60 . 1 1 16 16 THR CA C 13 58.31 0.1 . 1 . . . . . . . . 5231 1 61 . 1 1 16 16 THR CB C 13 73.3 0.1 . 1 . . . . . . . . 5231 1 62 . 1 1 16 16 THR CG2 C 13 22.29 0.1 . 1 . . . . . . . . 5231 1 63 . 1 1 16 16 THR N N 15 110.5 0.1 . 1 . . . . . . . . 5231 1 64 . 1 1 17 17 TYR H H 1 8.58 0.02 . 1 . . . . . . . . 5231 1 65 . 1 1 17 17 TYR CA C 13 54.97 0.1 . 1 . . . . . . . . 5231 1 66 . 1 1 17 17 TYR CB C 13 42.34 0.1 . 1 . . . . . . . . 5231 1 67 . 1 1 17 17 TYR N N 15 117.8 0.1 . 1 . . . . . . . . 5231 1 68 . 1 1 18 18 ARG HA H 1 4.412 0.02 . 1 . . . . . . . . 5231 1 69 . 1 1 18 18 ARG C C 13 174.0 0.1 . 1 . . . . . . . . 5231 1 70 . 1 1 18 18 ARG CA C 13 55.15 0.1 . 1 . . . . . . . . 5231 1 71 . 1 1 18 18 ARG CB C 13 34.91 0.1 . 1 . . . . . . . . 5231 1 72 . 1 1 18 18 ARG CG C 13 27.44 0.1 . 1 . . . . . . . . 5231 1 73 . 1 1 19 19 ILE H H 1 8.37 0.02 . 1 . . . . . . . . 5231 1 74 . 1 1 19 19 ILE HA H 1 4.369 0.02 . 1 . . . . . . . . 5231 1 75 . 1 1 19 19 ILE HG21 H 1 1.241 0.02 . 1 . . . . . . . . 5231 1 76 . 1 1 19 19 ILE HG22 H 1 1.241 0.02 . 1 . . . . . . . . 5231 1 77 . 1 1 19 19 ILE HG23 H 1 1.241 0.02 . 1 . . . . . . . . 5231 1 78 . 1 1 19 19 ILE C C 13 175.5 0.1 . 1 . . . . . . . . 5231 1 79 . 1 1 19 19 ILE CA C 13 61.76 0.1 . 1 . . . . . . . . 5231 1 80 . 1 1 19 19 ILE CB C 13 37.39 0.1 . 1 . . . . . . . . 5231 1 81 . 1 1 19 19 ILE N N 15 128.2 0.1 . 1 . . . . . . . . 5231 1 82 . 1 1 20 20 VAL H H 1 9.50 0.02 . 1 . . . . . . . . 5231 1 83 . 1 1 20 20 VAL HA H 1 3.465 0.02 . 1 . . . . . . . . 5231 1 84 . 1 1 20 20 VAL HB H 1 2.143 0.02 . 1 . . . . . . . . 5231 1 85 . 1 1 20 20 VAL HG11 H 1 1.051 0.02 . 2 . . . . . . . . 5231 1 86 . 1 1 20 20 VAL HG12 H 1 1.051 0.02 . 2 . . . . . . . . 5231 1 87 . 1 1 20 20 VAL HG13 H 1 1.051 0.02 . 2 . . . . . . . . 5231 1 88 . 1 1 20 20 VAL C C 13 175.4 0.1 . 1 . . . . . . . . 5231 1 89 . 1 1 20 20 VAL CA C 13 66.29 0.1 . 1 . . . . . . . . 5231 1 90 . 1 1 20 20 VAL CB C 13 32.86 0.1 . 1 . . . . . . . . 5231 1 91 . 1 1 20 20 VAL CG1 C 13 24.01 0.1 . 1 . . . . . . . . 5231 1 92 . 1 1 20 20 VAL CG2 C 13 21.42 0.1 . 1 . . . . . . . . 5231 1 93 . 1 1 20 20 VAL N N 15 129.9 0.1 . 1 . . . . . . . . 5231 1 94 . 1 1 21 21 ASN H H 1 7.63 0.02 . 1 . . . . . . . . 5231 1 95 . 1 1 21 21 ASN HA H 1 4.757 0.02 . 1 . . . . . . . . 5231 1 96 . 1 1 21 21 ASN C C 13 169.9 0.1 . 1 . . . . . . . . 5231 1 97 . 1 1 21 21 ASN CA C 13 51.49 0.1 . 1 . . . . . . . . 5231 1 98 . 1 1 21 21 ASN CB C 13 39.81 0.1 . 1 . . . . . . . . 5231 1 99 . 1 1 21 21 ASN N N 15 116.2 0.1 . 1 . . . . . . . . 5231 1 100 . 1 1 22 22 TYR H H 1 8.05 0.02 . 1 . . . . . . . . 5231 1 101 . 1 1 22 22 TYR HA H 1 4.504 0.02 . 1 . . . . . . . . 5231 1 102 . 1 1 22 22 TYR HB2 H 1 3.121 0.02 . 1 . . . . . . . . 5231 1 103 . 1 1 22 22 TYR HB3 H 1 2.864 0.02 . 1 . . . . . . . . 5231 1 104 . 1 1 22 22 TYR C C 13 177.5 0.1 . 1 . . . . . . . . 5231 1 105 . 1 1 22 22 TYR CA C 13 58.76 0.1 . 1 . . . . . . . . 5231 1 106 . 1 1 22 22 TYR CB C 13 41.61 0.1 . 1 . . . . . . . . 5231 1 107 . 1 1 22 22 TYR N N 15 112.0 0.1 . 1 . . . . . . . . 5231 1 108 . 1 1 23 23 THR H H 1 8.56 0.02 . 1 . . . . . . . . 5231 1 109 . 1 1 23 23 THR CA C 13 60.87 0.1 . 1 . . . . . . . . 5231 1 110 . 1 1 23 23 THR N N 15 123.8 0.1 . 1 . . . . . . . . 5231 1 111 . 1 1 24 24 PRO HA H 1 4.668 0.02 . 1 . . . . . . . . 5231 1 112 . 1 1 24 24 PRO C C 13 177.4 0.1 . 1 . . . . . . . . 5231 1 113 . 1 1 24 24 PRO CA C 13 63.34 0.1 . 1 . . . . . . . . 5231 1 114 . 1 1 24 24 PRO CB C 13 32.03 0.1 . 1 . . . . . . . . 5231 1 115 . 1 1 25 25 ASP H H 1 8.83 0.02 . 1 . . . . . . . . 5231 1 116 . 1 1 25 25 ASP HA H 1 4.157 0.02 . 1 . . . . . . . . 5231 1 117 . 1 1 25 25 ASP HB2 H 1 3.32 0.02 . 2 . . . . . . . . 5231 1 118 . 1 1 25 25 ASP C C 13 175.4 0.1 . 1 . . . . . . . . 5231 1 119 . 1 1 25 25 ASP CA C 13 56.06 0.1 . 1 . . . . . . . . 5231 1 120 . 1 1 25 25 ASP CB C 13 41.63 0.1 . 1 . . . . . . . . 5231 1 121 . 1 1 25 25 ASP N N 15 121.8 0.1 . 1 . . . . . . . . 5231 1 122 . 1 1 26 26 LEU H H 1 6.94 0.02 . 1 . . . . . . . . 5231 1 123 . 1 1 26 26 LEU CA C 13 51.36 0.1 . 1 . . . . . . . . 5231 1 124 . 1 1 26 26 LEU CB C 13 47.6 0.1 . 1 . . . . . . . . 5231 1 125 . 1 1 26 26 LEU N N 15 116.4 0.1 . 1 . . . . . . . . 5231 1 126 . 1 1 27 27 PRO HA H 1 4.563 0.02 . 1 . . . . . . . . 5231 1 127 . 1 1 27 27 PRO C C 13 177.7 0.1 . 1 . . . . . . . . 5231 1 128 . 1 1 27 27 PRO CA C 13 62.32 0.1 . 1 . . . . . . . . 5231 1 129 . 1 1 27 27 PRO CB C 13 32.65 0.1 . 1 . . . . . . . . 5231 1 130 . 1 1 28 28 LYS H H 1 8.60 0.02 . 1 . . . . . . . . 5231 1 131 . 1 1 28 28 LYS HA H 1 3.793 0.02 . 1 . . . . . . . . 5231 1 132 . 1 1 28 28 LYS HG2 H 1 1.302 0.02 . 2 . . . . . . . . 5231 1 133 . 1 1 28 28 LYS C C 13 178.2 0.1 . 1 . . . . . . . . 5231 1 134 . 1 1 28 28 LYS CA C 13 60.61 0.1 . 1 . . . . . . . . 5231 1 135 . 1 1 28 28 LYS CB C 13 32.74 0.1 . 1 . . . . . . . . 5231 1 136 . 1 1 28 28 LYS CG C 13 24.94 0.1 . 1 . . . . . . . . 5231 1 137 . 1 1 28 28 LYS N N 15 123.8 0.1 . 1 . . . . . . . . 5231 1 138 . 1 1 29 29 ASP H H 1 8.45 0.02 . 1 . . . . . . . . 5231 1 139 . 1 1 29 29 ASP HA H 1 4.411 0.02 . 1 . . . . . . . . 5231 1 140 . 1 1 29 29 ASP HB2 H 1 2.732 0.02 . 2 . . . . . . . . 5231 1 141 . 1 1 29 29 ASP C C 13 178.4 0.1 . 1 . . . . . . . . 5231 1 142 . 1 1 29 29 ASP CA C 13 56.8 0.1 . 1 . . . . . . . . 5231 1 143 . 1 1 29 29 ASP CB C 13 40.15 0.1 . 1 . . . . . . . . 5231 1 144 . 1 1 29 29 ASP N N 15 113.7 0.1 . 1 . . . . . . . . 5231 1 145 . 1 1 30 30 ALA H H 1 7.28 0.02 . 1 . . . . . . . . 5231 1 146 . 1 1 30 30 ALA HA H 1 4.368 0.02 . 1 . . . . . . . . 5231 1 147 . 1 1 30 30 ALA HB1 H 1 1.643 0.02 . 1 . . . . . . . . 5231 1 148 . 1 1 30 30 ALA HB2 H 1 1.643 0.02 . 1 . . . . . . . . 5231 1 149 . 1 1 30 30 ALA HB3 H 1 1.643 0.02 . 1 . . . . . . . . 5231 1 150 . 1 1 30 30 ALA C C 13 180.6 0.1 . 1 . . . . . . . . 5231 1 151 . 1 1 30 30 ALA CA C 13 54.34 0.1 . 1 . . . . . . . . 5231 1 152 . 1 1 30 30 ALA CB C 13 19.4 0.1 . 1 . . . . . . . . 5231 1 153 . 1 1 30 30 ALA N N 15 122.7 0.1 . 1 . . . . . . . . 5231 1 154 . 1 1 31 31 VAL H H 1 7.48 0.02 . 1 . . . . . . . . 5231 1 155 . 1 1 31 31 VAL HA H 1 3.606 0.02 . 1 . . . . . . . . 5231 1 156 . 1 1 31 31 VAL HB H 1 2.794 0.02 . 1 . . . . . . . . 5231 1 157 . 1 1 31 31 VAL HG11 H 1 0.982 0.02 . 2 . . . . . . . . 5231 1 158 . 1 1 31 31 VAL HG12 H 1 0.982 0.02 . 2 . . . . . . . . 5231 1 159 . 1 1 31 31 VAL HG13 H 1 0.982 0.02 . 2 . . . . . . . . 5231 1 160 . 1 1 31 31 VAL C C 13 176.9 0.1 . 1 . . . . . . . . 5231 1 161 . 1 1 31 31 VAL CA C 13 66.46 0.1 . 1 . . . . . . . . 5231 1 162 . 1 1 31 31 VAL CB C 13 31.6 0.1 . 1 . . . . . . . . 5231 1 163 . 1 1 31 31 VAL CG1 C 13 24.56 0.1 . 2 . . . . . . . . 5231 1 164 . 1 1 31 31 VAL N N 15 121.8 0.1 . 1 . . . . . . . . 5231 1 165 . 1 1 32 32 ASP H H 1 8.52 0.02 . 1 . . . . . . . . 5231 1 166 . 1 1 32 32 ASP HA H 1 4.681 0.02 . 1 . . . . . . . . 5231 1 167 . 1 1 32 32 ASP HB2 H 1 3.086 0.02 . 2 . . . . . . . . 5231 1 168 . 1 1 32 32 ASP C C 13 178.6 0.1 . 1 . . . . . . . . 5231 1 169 . 1 1 32 32 ASP CA C 13 58.18 0.1 . 1 . . . . . . . . 5231 1 170 . 1 1 32 32 ASP CB C 13 40.16 0.1 . 1 . . . . . . . . 5231 1 171 . 1 1 32 32 ASP N N 15 119.6 0.1 . 1 . . . . . . . . 5231 1 172 . 1 1 33 33 SER H H 1 8.00 0.02 . 1 . . . . . . . . 5231 1 173 . 1 1 33 33 SER HA H 1 4.299 0.02 . 1 . . . . . . . . 5231 1 174 . 1 1 33 33 SER HB2 H 1 4.04 0.02 . 2 . . . . . . . . 5231 1 175 . 1 1 33 33 SER C C 13 176.5 0.1 . 1 . . . . . . . . 5231 1 176 . 1 1 33 33 SER CA C 13 61.7 0.1 . 1 . . . . . . . . 5231 1 177 . 1 1 33 33 SER CB C 13 63.52 0.1 . 1 . . . . . . . . 5231 1 178 . 1 1 33 33 SER N N 15 112.4 0.1 . 1 . . . . . . . . 5231 1 179 . 1 1 34 34 ALA H H 1 7.63 0.02 . 1 . . . . . . . . 5231 1 180 . 1 1 34 34 ALA HA H 1 4.252 0.02 . 1 . . . . . . . . 5231 1 181 . 1 1 34 34 ALA HB1 H 1 1.531 0.02 . 1 . . . . . . . . 5231 1 182 . 1 1 34 34 ALA HB2 H 1 1.531 0.02 . 1 . . . . . . . . 5231 1 183 . 1 1 34 34 ALA HB3 H 1 1.531 0.02 . 1 . . . . . . . . 5231 1 184 . 1 1 34 34 ALA C C 13 179.3 0.1 . 1 . . . . . . . . 5231 1 185 . 1 1 34 34 ALA CA C 13 55.92 0.1 . 1 . . . . . . . . 5231 1 186 . 1 1 34 34 ALA CB C 13 18.49 0.1 . 1 . . . . . . . . 5231 1 187 . 1 1 34 34 ALA N N 15 124.0 0.1 . 1 . . . . . . . . 5231 1 188 . 1 1 35 35 VAL H H 1 7.97 0.02 . 1 . . . . . . . . 5231 1 189 . 1 1 35 35 VAL HA H 1 3.314 0.02 . 1 . . . . . . . . 5231 1 190 . 1 1 35 35 VAL HB H 1 2.149 0.02 . 1 . . . . . . . . 5231 1 191 . 1 1 35 35 VAL HG11 H 1 0.784 0.02 . 2 . . . . . . . . 5231 1 192 . 1 1 35 35 VAL HG12 H 1 0.784 0.02 . 2 . . . . . . . . 5231 1 193 . 1 1 35 35 VAL HG13 H 1 0.784 0.02 . 2 . . . . . . . . 5231 1 194 . 1 1 35 35 VAL C C 13 176.9 0.1 . 1 . . . . . . . . 5231 1 195 . 1 1 35 35 VAL CA C 13 67.24 0.1 . 1 . . . . . . . . 5231 1 196 . 1 1 35 35 VAL CB C 13 31.51 0.1 . 1 . . . . . . . . 5231 1 197 . 1 1 35 35 VAL CG1 C 13 22.37 0.1 . 2 . . . . . . . . 5231 1 198 . 1 1 35 35 VAL N N 15 116.0 0.1 . 1 . . . . . . . . 5231 1 199 . 1 1 36 36 GLU H H 1 8.39 0.02 . 1 . . . . . . . . 5231 1 200 . 1 1 36 36 GLU HA H 1 3.764 0.02 . 1 . . . . . . . . 5231 1 201 . 1 1 36 36 GLU HB2 H 1 2.274 0.02 . 2 . . . . . . . . 5231 1 202 . 1 1 36 36 GLU HG2 H 1 2.556 0.02 . 2 . . . . . . . . 5231 1 203 . 1 1 36 36 GLU C C 13 179.6 0.1 . 1 . . . . . . . . 5231 1 204 . 1 1 36 36 GLU CA C 13 60.5 0.1 . 1 . . . . . . . . 5231 1 205 . 1 1 36 36 GLU CB C 13 29.8 0.1 . 1 . . . . . . . . 5231 1 206 . 1 1 36 36 GLU CG C 13 37.46 0.1 . 1 . . . . . . . . 5231 1 207 . 1 1 36 36 GLU N N 15 118.2 0.1 . 1 . . . . . . . . 5231 1 208 . 1 1 37 37 LYS H H 1 8.25 0.02 . 1 . . . . . . . . 5231 1 209 . 1 1 37 37 LYS HA H 1 4.018 0.02 . 1 . . . . . . . . 5231 1 210 . 1 1 37 37 LYS HB2 H 1 1.953 0.02 . 1 . . . . . . . . 5231 1 211 . 1 1 37 37 LYS HB3 H 1 1.762 0.02 . 1 . . . . . . . . 5231 1 212 . 1 1 37 37 LYS HG2 H 1 1.399 0.02 . 2 . . . . . . . . 5231 1 213 . 1 1 37 37 LYS C C 13 178.7 0.1 . 1 . . . . . . . . 5231 1 214 . 1 1 37 37 LYS CA C 13 59.87 0.1 . 1 . . . . . . . . 5231 1 215 . 1 1 37 37 LYS CB C 13 32.67 0.1 . 1 . . . . . . . . 5231 1 216 . 1 1 37 37 LYS CG C 13 26.26 0.1 . 1 . . . . . . . . 5231 1 217 . 1 1 37 37 LYS N N 15 119.2 0.1 . 1 . . . . . . . . 5231 1 218 . 1 1 38 38 ALA H H 1 8.05 0.02 . 1 . . . . . . . . 5231 1 219 . 1 1 38 38 ALA HA H 1 4.09 0.02 . 1 . . . . . . . . 5231 1 220 . 1 1 38 38 ALA HB1 H 1 1.501 0.02 . 1 . . . . . . . . 5231 1 221 . 1 1 38 38 ALA HB2 H 1 1.501 0.02 . 1 . . . . . . . . 5231 1 222 . 1 1 38 38 ALA HB3 H 1 1.501 0.02 . 1 . . . . . . . . 5231 1 223 . 1 1 38 38 ALA C C 13 177.8 0.1 . 1 . . . . . . . . 5231 1 224 . 1 1 38 38 ALA CA C 13 55.88 0.1 . 1 . . . . . . . . 5231 1 225 . 1 1 38 38 ALA CB C 13 18.47 0.1 . 1 . . . . . . . . 5231 1 226 . 1 1 38 38 ALA N N 15 123.5 0.1 . 1 . . . . . . . . 5231 1 227 . 1 1 39 39 LEU H H 1 7.66 0.02 . 1 . . . . . . . . 5231 1 228 . 1 1 39 39 LEU HA H 1 3.77 0.02 . 1 . . . . . . . . 5231 1 229 . 1 1 39 39 LEU HB2 H 1 1.699 0.02 . 1 . . . . . . . . 5231 1 230 . 1 1 39 39 LEU HB3 H 1 1.566 0.02 . 1 . . . . . . . . 5231 1 231 . 1 1 39 39 LEU C C 13 179.7 0.1 . 1 . . . . . . . . 5231 1 232 . 1 1 39 39 LEU CA C 13 57.86 0.1 . 1 . . . . . . . . 5231 1 233 . 1 1 39 39 LEU CB C 13 41.1 0.1 . 1 . . . . . . . . 5231 1 234 . 1 1 39 39 LEU N N 15 115.3 0.1 . 1 . . . . . . . . 5231 1 235 . 1 1 40 40 LYS H H 1 7.77 0.02 . 1 . . . . . . . . 5231 1 236 . 1 1 40 40 LYS HA H 1 4.196 0.02 . 1 . . . . . . . . 5231 1 237 . 1 1 40 40 LYS HB2 H 1 2.078 0.02 . 2 . . . . . . . . 5231 1 238 . 1 1 40 40 LYS HG2 H 1 1.38 0.02 . 2 . . . . . . . . 5231 1 239 . 1 1 40 40 LYS HD2 H 1 1.685 0.02 . 2 . . . . . . . . 5231 1 240 . 1 1 40 40 LYS HE2 H 1 2.751 0.02 . 2 . . . . . . . . 5231 1 241 . 1 1 40 40 LYS C C 13 178.6 0.1 . 1 . . . . . . . . 5231 1 242 . 1 1 40 40 LYS CA C 13 58.77 0.1 . 1 . . . . . . . . 5231 1 243 . 1 1 40 40 LYS CB C 13 32.39 0.1 . 1 . . . . . . . . 5231 1 244 . 1 1 40 40 LYS CG C 13 25.49 0.1 . 1 . . . . . . . . 5231 1 245 . 1 1 40 40 LYS CD C 13 28.98 0.1 . 1 . . . . . . . . 5231 1 246 . 1 1 40 40 LYS N N 15 119.0 0.1 . 1 . . . . . . . . 5231 1 247 . 1 1 41 41 VAL H H 1 7.41 0.02 . 1 . . . . . . . . 5231 1 248 . 1 1 41 41 VAL HA H 1 3.89 0.02 . 1 . . . . . . . . 5231 1 249 . 1 1 41 41 VAL HB H 1 2.14 0.02 . 1 . . . . . . . . 5231 1 250 . 1 1 41 41 VAL HG11 H 1 0.969 0.02 . 1 . . . . . . . . 5231 1 251 . 1 1 41 41 VAL HG12 H 1 0.969 0.02 . 1 . . . . . . . . 5231 1 252 . 1 1 41 41 VAL HG13 H 1 0.969 0.02 . 1 . . . . . . . . 5231 1 253 . 1 1 41 41 VAL HG21 H 1 0.716 0.02 . 1 . . . . . . . . 5231 1 254 . 1 1 41 41 VAL HG22 H 1 0.716 0.02 . 1 . . . . . . . . 5231 1 255 . 1 1 41 41 VAL HG23 H 1 0.716 0.02 . 1 . . . . . . . . 5231 1 256 . 1 1 41 41 VAL C C 13 177.2 0.1 . 1 . . . . . . . . 5231 1 257 . 1 1 41 41 VAL CA C 13 65.4 0.1 . 1 . . . . . . . . 5231 1 258 . 1 1 41 41 VAL CB C 13 31.64 0.1 . 1 . . . . . . . . 5231 1 259 . 1 1 41 41 VAL CG1 C 13 22.03 0.1 . 2 . . . . . . . . 5231 1 260 . 1 1 41 41 VAL N N 15 114.3 0.1 . 1 . . . . . . . . 5231 1 261 . 1 1 42 42 TRP H H 1 6.65 0.02 . 1 . . . . . . . . 5231 1 262 . 1 1 42 42 TRP HA H 1 4.795 0.02 . 1 . . . . . . . . 5231 1 263 . 1 1 42 42 TRP HB2 H 1 3.924 0.02 . 2 . . . . . . . . 5231 1 264 . 1 1 42 42 TRP C C 13 180.1 0.1 . 1 . . . . . . . . 5231 1 265 . 1 1 42 42 TRP CA C 13 57.97 0.1 . 1 . . . . . . . . 5231 1 266 . 1 1 42 42 TRP CB C 13 30.72 0.1 . 1 . . . . . . . . 5231 1 267 . 1 1 42 42 TRP N N 15 117.6 0.1 . 1 . . . . . . . . 5231 1 268 . 1 1 43 43 GLU H H 1 8.47 0.02 . 1 . . . . . . . . 5231 1 269 . 1 1 43 43 GLU HA H 1 4.064 0.02 . 1 . . . . . . . . 5231 1 270 . 1 1 43 43 GLU HB2 H 1 2.408 0.02 . 2 . . . . . . . . 5231 1 271 . 1 1 43 43 GLU HG2 H 1 2.529 0.02 . 2 . . . . . . . . 5231 1 272 . 1 1 43 43 GLU C C 13 178.2 0.1 . 1 . . . . . . . . 5231 1 273 . 1 1 43 43 GLU CA C 13 59.85 0.1 . 1 . . . . . . . . 5231 1 274 . 1 1 43 43 GLU CB C 13 31.37 0.1 . 1 . . . . . . . . 5231 1 275 . 1 1 43 43 GLU CG C 13 36.81 0.1 . 1 . . . . . . . . 5231 1 276 . 1 1 43 43 GLU N N 15 122.9 0.1 . 1 . . . . . . . . 5231 1 277 . 1 1 44 44 GLU H H 1 7.74 0.02 . 1 . . . . . . . . 5231 1 278 . 1 1 44 44 GLU HA H 1 4.209 0.02 . 1 . . . . . . . . 5231 1 279 . 1 1 44 44 GLU HB2 H 1 1.824 0.02 . 2 . . . . . . . . 5231 1 280 . 1 1 44 44 GLU HG2 H 1 2.676 0.02 . 1 . . . . . . . . 5231 1 281 . 1 1 44 44 GLU HG3 H 1 2.435 0.02 . 1 . . . . . . . . 5231 1 282 . 1 1 44 44 GLU C C 13 177.9 0.1 . 1 . . . . . . . . 5231 1 283 . 1 1 44 44 GLU CA C 13 58.88 0.1 . 1 . . . . . . . . 5231 1 284 . 1 1 44 44 GLU CB C 13 31.14 0.1 . 1 . . . . . . . . 5231 1 285 . 1 1 44 44 GLU CG C 13 37.32 0.1 . 1 . . . . . . . . 5231 1 286 . 1 1 44 44 GLU N N 15 111.4 0.1 . 1 . . . . . . . . 5231 1 287 . 1 1 45 45 VAL H H 1 7.02 0.02 . 1 . . . . . . . . 5231 1 288 . 1 1 45 45 VAL HA H 1 4.766 0.02 . 1 . . . . . . . . 5231 1 289 . 1 1 45 45 VAL HB H 1 2.747 0.02 . 1 . . . . . . . . 5231 1 290 . 1 1 45 45 VAL HG11 H 1 1.235 0.02 . 1 . . . . . . . . 5231 1 291 . 1 1 45 45 VAL HG12 H 1 1.235 0.02 . 1 . . . . . . . . 5231 1 292 . 1 1 45 45 VAL HG13 H 1 1.235 0.02 . 1 . . . . . . . . 5231 1 293 . 1 1 45 45 VAL HG21 H 1 0.986 0.02 . 1 . . . . . . . . 5231 1 294 . 1 1 45 45 VAL HG22 H 1 0.986 0.02 . 1 . . . . . . . . 5231 1 295 . 1 1 45 45 VAL HG23 H 1 0.986 0.02 . 1 . . . . . . . . 5231 1 296 . 1 1 45 45 VAL C C 13 174.5 0.1 . 1 . . . . . . . . 5231 1 297 . 1 1 45 45 VAL CA C 13 60.4 0.1 . 1 . . . . . . . . 5231 1 298 . 1 1 45 45 VAL CB C 13 32.78 0.1 . 1 . . . . . . . . 5231 1 299 . 1 1 45 45 VAL CG1 C 13 21.8 0.1 . 1 . . . . . . . . 5231 1 300 . 1 1 45 45 VAL CG2 C 13 19.45 0.1 . 1 . . . . . . . . 5231 1 301 . 1 1 45 45 VAL N N 15 104.8 0.1 . 1 . . . . . . . . 5231 1 302 . 1 1 46 46 THR H H 1 7.59 0.02 . 1 . . . . . . . . 5231 1 303 . 1 1 46 46 THR CA C 13 60.43 0.1 . 1 . . . . . . . . 5231 1 304 . 1 1 46 46 THR CB C 13 72.42 0.1 . 1 . . . . . . . . 5231 1 305 . 1 1 46 46 THR N N 15 111.6 0.1 . 1 . . . . . . . . 5231 1 306 . 1 1 47 47 PRO HA H 1 5.01 0.02 . 1 . . . . . . . . 5231 1 307 . 1 1 47 47 PRO HB2 H 1 2.654 0.02 . 1 . . . . . . . . 5231 1 308 . 1 1 47 47 PRO HB3 H 1 1.75 0.02 . 1 . . . . . . . . 5231 1 309 . 1 1 47 47 PRO HG2 H 1 2.167 0.02 . 2 . . . . . . . . 5231 1 310 . 1 1 47 47 PRO C C 13 176.7 0.1 . 1 . . . . . . . . 5231 1 311 . 1 1 47 47 PRO CA C 13 62.27 0.1 . 1 . . . . . . . . 5231 1 312 . 1 1 47 47 PRO CB C 13 31.95 0.1 . 1 . . . . . . . . 5231 1 313 . 1 1 48 48 LEU H H 1 7.35 0.02 . 1 . . . . . . . . 5231 1 314 . 1 1 48 48 LEU HA H 1 4.575 0.02 . 1 . . . . . . . . 5231 1 315 . 1 1 48 48 LEU HG H 1 1.427 0.02 . 1 . . . . . . . . 5231 1 316 . 1 1 48 48 LEU C C 13 176.8 0.1 . 1 . . . . . . . . 5231 1 317 . 1 1 48 48 LEU CA C 13 55.17 0.1 . 1 . . . . . . . . 5231 1 318 . 1 1 48 48 LEU CB C 13 43.11 0.1 . 1 . . . . . . . . 5231 1 319 . 1 1 48 48 LEU CG C 13 26.98 0.1 . 1 . . . . . . . . 5231 1 320 . 1 1 48 48 LEU N N 15 117.8 0.1 . 1 . . . . . . . . 5231 1 321 . 1 1 49 49 THR H H 1 8.11 0.02 . 1 . . . . . . . . 5231 1 322 . 1 1 49 49 THR HA H 1 4.633 0.02 . 1 . . . . . . . . 5231 1 323 . 1 1 49 49 THR HB H 1 4.234 0.02 . 1 . . . . . . . . 5231 1 324 . 1 1 49 49 THR HG21 H 1 1.144 0.02 . 1 . . . . . . . . 5231 1 325 . 1 1 49 49 THR HG22 H 1 1.144 0.02 . 1 . . . . . . . . 5231 1 326 . 1 1 49 49 THR HG23 H 1 1.144 0.02 . 1 . . . . . . . . 5231 1 327 . 1 1 49 49 THR C C 13 172.5 0.1 . 1 . . . . . . . . 5231 1 328 . 1 1 49 49 THR CA C 13 59.9 0.1 . 1 . . . . . . . . 5231 1 329 . 1 1 49 49 THR CB C 13 72.84 0.1 . 1 . . . . . . . . 5231 1 330 . 1 1 49 49 THR CG2 C 13 22.43 0.1 . 1 . . . . . . . . 5231 1 331 . 1 1 49 49 THR N N 15 110.2 0.1 . 1 . . . . . . . . 5231 1 332 . 1 1 50 50 PHE H H 1 8.24 0.02 . 1 . . . . . . . . 5231 1 333 . 1 1 50 50 PHE HA H 1 5.795 0.02 . 1 . . . . . . . . 5231 1 334 . 1 1 50 50 PHE HB2 H 1 2.882 0.02 . 2 . . . . . . . . 5231 1 335 . 1 1 50 50 PHE C C 13 176.9 0.1 . 1 . . . . . . . . 5231 1 336 . 1 1 50 50 PHE CA C 13 56.4 0.1 . 1 . . . . . . . . 5231 1 337 . 1 1 50 50 PHE CB C 13 43.66 0.1 . 1 . . . . . . . . 5231 1 338 . 1 1 50 50 PHE N N 15 117.1 0.1 . 1 . . . . . . . . 5231 1 339 . 1 1 51 51 SER H H 1 8.67 0.02 . 1 . . . . . . . . 5231 1 340 . 1 1 51 51 SER HA H 1 4.994 0.02 . 1 . . . . . . . . 5231 1 341 . 1 1 51 51 SER HB2 H 1 3.97 0.02 . 1 . . . . . . . . 5231 1 342 . 1 1 51 51 SER HB3 H 1 3.76 0.02 . 1 . . . . . . . . 5231 1 343 . 1 1 51 51 SER C C 13 171.4 0.1 . 1 . . . . . . . . 5231 1 344 . 1 1 51 51 SER CA C 13 57.78 0.1 . 1 . . . . . . . . 5231 1 345 . 1 1 51 51 SER CB C 13 65.85 0.1 . 1 . . . . . . . . 5231 1 346 . 1 1 51 51 SER N N 15 116.5 0.1 . 1 . . . . . . . . 5231 1 347 . 1 1 52 52 ARG H H 1 8.54 0.02 . 1 . . . . . . . . 5231 1 348 . 1 1 52 52 ARG HA H 1 3.592 0.02 . 1 . . . . . . . . 5231 1 349 . 1 1 52 52 ARG HB2 H 1 1.962 0.02 . 2 . . . . . . . . 5231 1 350 . 1 1 52 52 ARG C C 13 175.7 0.1 . 1 . . . . . . . . 5231 1 351 . 1 1 52 52 ARG CA C 13 55.75 0.1 . 1 . . . . . . . . 5231 1 352 . 1 1 52 52 ARG CB C 13 32.15 0.1 . 1 . . . . . . . . 5231 1 353 . 1 1 52 52 ARG N N 15 125.1 0.1 . 1 . . . . . . . . 5231 1 354 . 1 1 53 53 LEU H H 1 8.54 0.02 . 1 . . . . . . . . 5231 1 355 . 1 1 53 53 LEU HA H 1 4.746 0.02 . 1 . . . . . . . . 5231 1 356 . 1 1 53 53 LEU HB2 H 1 1.734 0.02 . 2 . . . . . . . . 5231 1 357 . 1 1 53 53 LEU C C 13 176.9 0.1 . 1 . . . . . . . . 5231 1 358 . 1 1 53 53 LEU CA C 13 53.16 0.1 . 1 . . . . . . . . 5231 1 359 . 1 1 53 53 LEU CB C 13 45.75 0.1 . 1 . . . . . . . . 5231 1 360 . 1 1 53 53 LEU N N 15 125.3 0.1 . 1 . . . . . . . . 5231 1 361 . 1 1 54 54 TYR H H 1 9.20 0.02 . 1 . . . . . . . . 5231 1 362 . 1 1 54 54 TYR HA H 1 4.439 0.02 . 1 . . . . . . . . 5231 1 363 . 1 1 54 54 TYR HB2 H 1 2.759 0.02 . 2 . . . . . . . . 5231 1 364 . 1 1 54 54 TYR C C 13 174.1 0.1 . 1 . . . . . . . . 5231 1 365 . 1 1 54 54 TYR CA C 13 58.91 0.1 . 1 . . . . . . . . 5231 1 366 . 1 1 54 54 TYR CB C 13 39.72 0.1 . 1 . . . . . . . . 5231 1 367 . 1 1 54 54 TYR N N 15 119.0 0.1 . 1 . . . . . . . . 5231 1 368 . 1 1 55 55 GLU H H 1 7.45 0.02 . 1 . . . . . . . . 5231 1 369 . 1 1 55 55 GLU HA H 1 4.466 0.02 . 1 . . . . . . . . 5231 1 370 . 1 1 55 55 GLU HB2 H 1 2.149 0.02 . 1 . . . . . . . . 5231 1 371 . 1 1 55 55 GLU HB3 H 1 1.985 0.02 . 1 . . . . . . . . 5231 1 372 . 1 1 55 55 GLU HG2 H 1 2.213 0.02 . 2 . . . . . . . . 5231 1 373 . 1 1 55 55 GLU C C 13 174.7 0.1 . 1 . . . . . . . . 5231 1 374 . 1 1 55 55 GLU CA C 13 54.79 0.1 . 1 . . . . . . . . 5231 1 375 . 1 1 55 55 GLU CB C 13 33.2 0.1 . 1 . . . . . . . . 5231 1 376 . 1 1 55 55 GLU CG C 13 35.63 0.1 . 1 . . . . . . . . 5231 1 377 . 1 1 55 55 GLU N N 15 116.7 0.1 . 1 . . . . . . . . 5231 1 378 . 1 1 56 56 GLY H H 1 8.49 0.02 . 1 . . . . . . . . 5231 1 379 . 1 1 56 56 GLY HA2 H 1 4.104 0.02 . 1 . . . . . . . . 5231 1 380 . 1 1 56 56 GLY HA3 H 1 3.831 0.02 . 1 . . . . . . . . 5231 1 381 . 1 1 56 56 GLY C C 13 172.3 0.1 . 1 . . . . . . . . 5231 1 382 . 1 1 56 56 GLY CA C 13 44.69 0.1 . 1 . . . . . . . . 5231 1 383 . 1 1 56 56 GLY N N 15 108.5 0.1 . 1 . . . . . . . . 5231 1 384 . 1 1 57 57 GLU H H 1 8.18 0.02 . 1 . . . . . . . . 5231 1 385 . 1 1 57 57 GLU HA H 1 4.421 0.02 . 1 . . . . . . . . 5231 1 386 . 1 1 57 57 GLU HB2 H 1 1.978 0.02 . 2 . . . . . . . . 5231 1 387 . 1 1 57 57 GLU HG2 H 1 2.225 0.02 . 2 . . . . . . . . 5231 1 388 . 1 1 57 57 GLU C C 13 175.5 0.1 . 1 . . . . . . . . 5231 1 389 . 1 1 57 57 GLU CA C 13 56.1 0.1 . 1 . . . . . . . . 5231 1 390 . 1 1 57 57 GLU CB C 13 30.14 0.1 . 1 . . . . . . . . 5231 1 391 . 1 1 57 57 GLU CG C 13 36.35 0.1 . 1 . . . . . . . . 5231 1 392 . 1 1 57 57 GLU N N 15 119.2 0.1 . 1 . . . . . . . . 5231 1 393 . 1 1 58 58 ALA H H 1 7.99 0.02 . 1 . . . . . . . . 5231 1 394 . 1 1 58 58 ALA HA H 1 4.457 0.02 . 1 . . . . . . . . 5231 1 395 . 1 1 58 58 ALA HB1 H 1 2.014 0.02 . 1 . . . . . . . . 5231 1 396 . 1 1 58 58 ALA HB2 H 1 2.014 0.02 . 1 . . . . . . . . 5231 1 397 . 1 1 58 58 ALA HB3 H 1 2.014 0.02 . 1 . . . . . . . . 5231 1 398 . 1 1 58 58 ALA C C 13 176.7 0.1 . 1 . . . . . . . . 5231 1 399 . 1 1 58 58 ALA CA C 13 49.77 0.1 . 1 . . . . . . . . 5231 1 400 . 1 1 58 58 ALA CB C 13 22.22 0.1 . 1 . . . . . . . . 5231 1 401 . 1 1 58 58 ALA N N 15 131.6 0.1 . 1 . . . . . . . . 5231 1 402 . 1 1 59 59 ASP H H 1 8.30 0.02 . 1 . . . . . . . . 5231 1 403 . 1 1 59 59 ASP CA C 13 59.7 0.1 . 1 . . . . . . . . 5231 1 404 . 1 1 59 59 ASP CB C 13 41.36 0.1 . 1 . . . . . . . . 5231 1 405 . 1 1 59 59 ASP N N 15 122.2 0.1 . 1 . . . . . . . . 5231 1 406 . 1 1 60 60 ILE HA H 1 4.309 0.02 . 1 . . . . . . . . 5231 1 407 . 1 1 60 60 ILE HB H 1 1.56 0.02 . 1 . . . . . . . . 5231 1 408 . 1 1 60 60 ILE HG12 H 1 1.791 0.02 . 2 . . . . . . . . 5231 1 409 . 1 1 60 60 ILE HG21 H 1 1.048 0.02 . 1 . . . . . . . . 5231 1 410 . 1 1 60 60 ILE HG22 H 1 1.048 0.02 . 1 . . . . . . . . 5231 1 411 . 1 1 60 60 ILE HG23 H 1 1.048 0.02 . 1 . . . . . . . . 5231 1 412 . 1 1 60 60 ILE C C 13 174.5 0.1 . 1 . . . . . . . . 5231 1 413 . 1 1 60 60 ILE CA C 13 60.96 0.1 . 1 . . . . . . . . 5231 1 414 . 1 1 60 60 ILE CB C 13 39.56 0.1 . 1 . . . . . . . . 5231 1 415 . 1 1 61 61 MET H H 1 7.19 0.02 . 1 . . . . . . . . 5231 1 416 . 1 1 61 61 MET C C 13 177.0 0.1 . 1 . . . . . . . . 5231 1 417 . 1 1 61 61 MET CA C 13 54.05 0.1 . 1 . . . . . . . . 5231 1 418 . 1 1 61 61 MET CG C 13 32.61 0.1 . 1 . . . . . . . . 5231 1 419 . 1 1 61 61 MET N N 15 126.5 0.1 . 1 . . . . . . . . 5231 1 420 . 1 1 62 62 ILE H H 1 9.20 0.02 . 1 . . . . . . . . 5231 1 421 . 1 1 62 62 ILE HA H 1 5.464 0.02 . 1 . . . . . . . . 5231 1 422 . 1 1 62 62 ILE C C 13 174.1 0.1 . 1 . . . . . . . . 5231 1 423 . 1 1 62 62 ILE CA C 13 61.19 0.1 . 1 . . . . . . . . 5231 1 424 . 1 1 62 62 ILE CB C 13 40.21 0.1 . 1 . . . . . . . . 5231 1 425 . 1 1 62 62 ILE CG1 C 13 17.1 0.1 . 2 . . . . . . . . 5231 1 426 . 1 1 62 62 ILE N N 15 128.7 0.1 . 1 . . . . . . . . 5231 1 427 . 1 1 63 63 SER H H 1 8.58 0.02 . 1 . . . . . . . . 5231 1 428 . 1 1 63 63 SER HA H 1 5.124 0.02 . 1 . . . . . . . . 5231 1 429 . 1 1 63 63 SER HB2 H 1 3.837 0.02 . 2 . . . . . . . . 5231 1 430 . 1 1 63 63 SER C C 13 172.0 0.1 . 1 . . . . . . . . 5231 1 431 . 1 1 63 63 SER CA C 13 57.0 0.1 . 1 . . . . . . . . 5231 1 432 . 1 1 63 63 SER CB C 13 66.79 0.1 . 1 . . . . . . . . 5231 1 433 . 1 1 63 63 SER N N 15 118.5 0.1 . 1 . . . . . . . . 5231 1 434 . 1 1 64 64 PHE H H 1 9.47 0.02 . 1 . . . . . . . . 5231 1 435 . 1 1 64 64 PHE HA H 1 5.405 0.02 . 1 . . . . . . . . 5231 1 436 . 1 1 64 64 PHE HB2 H 1 1.164 0.02 . 2 . . . . . . . . 5231 1 437 . 1 1 64 64 PHE C C 13 176.0 0.1 . 1 . . . . . . . . 5231 1 438 . 1 1 64 64 PHE CA C 13 56.78 0.1 . 1 . . . . . . . . 5231 1 439 . 1 1 64 64 PHE CB C 13 42.13 0.1 . 1 . . . . . . . . 5231 1 440 . 1 1 64 64 PHE N N 15 120.2 0.1 . 1 . . . . . . . . 5231 1 441 . 1 1 65 65 ALA H H 1 9.29 0.02 . 1 . . . . . . . . 5231 1 442 . 1 1 65 65 ALA HA H 1 4.954 0.02 . 1 . . . . . . . . 5231 1 443 . 1 1 65 65 ALA HB1 H 1 1.164 0.02 . 1 . . . . . . . . 5231 1 444 . 1 1 65 65 ALA HB2 H 1 1.164 0.02 . 1 . . . . . . . . 5231 1 445 . 1 1 65 65 ALA HB3 H 1 1.164 0.02 . 1 . . . . . . . . 5231 1 446 . 1 1 65 65 ALA C C 13 175.1 0.1 . 1 . . . . . . . . 5231 1 447 . 1 1 65 65 ALA CA C 13 51.31 0.1 . 1 . . . . . . . . 5231 1 448 . 1 1 65 65 ALA CB C 13 23.77 0.1 . 1 . . . . . . . . 5231 1 449 . 1 1 65 65 ALA N N 15 125.6 0.1 . 1 . . . . . . . . 5231 1 450 . 1 1 66 66 VAL H H 1 8.16 0.02 . 1 . . . . . . . . 5231 1 451 . 1 1 66 66 VAL HA H 1 4.544 0.02 . 1 . . . . . . . . 5231 1 452 . 1 1 66 66 VAL C C 13 176.3 0.1 . 1 . . . . . . . . 5231 1 453 . 1 1 66 66 VAL CA C 13 59.33 0.1 . 1 . . . . . . . . 5231 1 454 . 1 1 66 66 VAL CB C 13 29.52 0.1 . 1 . . . . . . . . 5231 1 455 . 1 1 66 66 VAL N N 15 111.8 0.1 . 1 . . . . . . . . 5231 1 456 . 1 1 67 67 ARG H H 1 9.18 0.02 . 1 . . . . . . . . 5231 1 457 . 1 1 67 67 ARG HA H 1 3.87 0.02 . 1 . . . . . . . . 5231 1 458 . 1 1 67 67 ARG HB2 H 1 1.134 0.02 . 2 . . . . . . . . 5231 1 459 . 1 1 67 67 ARG C C 13 177.4 0.1 . 1 . . . . . . . . 5231 1 460 . 1 1 67 67 ARG CA C 13 56.77 0.1 . 1 . . . . . . . . 5231 1 461 . 1 1 67 67 ARG CB C 13 28.86 0.1 . 1 . . . . . . . . 5231 1 462 . 1 1 67 67 ARG N N 15 117.3 0.1 . 1 . . . . . . . . 5231 1 463 . 1 1 68 68 GLU H H 1 8.29 0.02 . 1 . . . . . . . . 5231 1 464 . 1 1 68 68 GLU C C 13 175.2 0.1 . 1 . . . . . . . . 5231 1 465 . 1 1 68 68 GLU CA C 13 58.34 0.1 . 1 . . . . . . . . 5231 1 466 . 1 1 68 68 GLU CB C 13 29.14 0.1 . 1 . . . . . . . . 5231 1 467 . 1 1 68 68 GLU CG C 13 36.82 0.1 . 1 . . . . . . . . 5231 1 468 . 1 1 68 68 GLU N N 15 128.4 0.1 . 1 . . . . . . . . 5231 1 469 . 1 1 69 69 HIS H H 1 9.10 0.02 . 1 . . . . . . . . 5231 1 470 . 1 1 69 69 HIS CA C 13 54.86 0.1 . 1 . . . . . . . . 5231 1 471 . 1 1 69 69 HIS CB C 13 29.13 0.1 . 1 . . . . . . . . 5231 1 472 . 1 1 69 69 HIS N N 15 121.3 0.1 . 1 . . . . . . . . 5231 1 473 . 1 1 70 70 GLY HA2 H 1 4.181 0.02 . 1 . . . . . . . . 5231 1 474 . 1 1 70 70 GLY HA3 H 1 3.62 0.02 . 1 . . . . . . . . 5231 1 475 . 1 1 70 70 GLY C C 13 173.7 0.1 . 1 . . . . . . . . 5231 1 476 . 1 1 70 70 GLY CA C 13 46.17 0.1 . 1 . . . . . . . . 5231 1 477 . 1 1 71 71 ASP H H 1 6.92 0.02 . 1 . . . . . . . . 5231 1 478 . 1 1 71 71 ASP CA C 13 51.27 0.1 . 1 . . . . . . . . 5231 1 479 . 1 1 71 71 ASP CB C 13 41.38 0.1 . 1 . . . . . . . . 5231 1 480 . 1 1 71 71 ASP N N 15 117.3 0.1 . 1 . . . . . . . . 5231 1 481 . 1 1 72 72 PHE CA C 13 58.62 0.1 . 1 . . . . . . . . 5231 1 482 . 1 1 72 72 PHE CB C 13 38.15 0.1 . 1 . . . . . . . . 5231 1 483 . 1 1 73 73 TYR H H 1 6.77 0.02 . 1 . . . . . . . . 5231 1 484 . 1 1 73 73 TYR CA C 13 54.65 0.1 . 1 . . . . . . . . 5231 1 485 . 1 1 73 73 TYR CB C 13 39.91 0.1 . 1 . . . . . . . . 5231 1 486 . 1 1 73 73 TYR N N 15 116.9 0.1 . 1 . . . . . . . . 5231 1 487 . 1 1 75 75 PHE C C 13 175.6 0.1 . 1 . . . . . . . . 5231 1 488 . 1 1 75 75 PHE CB C 13 39.02 0.1 . 1 . . . . . . . . 5231 1 489 . 1 1 76 76 ASP H H 1 7.96 0.02 . 1 . . . . . . . . 5231 1 490 . 1 1 76 76 ASP HA H 1 4.758 0.02 . 1 . . . . . . . . 5231 1 491 . 1 1 76 76 ASP HB2 H 1 2.738 0.02 . 2 . . . . . . . . 5231 1 492 . 1 1 76 76 ASP C C 13 178.0 0.1 . 1 . . . . . . . . 5231 1 493 . 1 1 76 76 ASP CA C 13 53.67 0.1 . 1 . . . . . . . . 5231 1 494 . 1 1 76 76 ASP CB C 13 41.97 0.1 . 1 . . . . . . . . 5231 1 495 . 1 1 76 76 ASP N N 15 116.0 0.1 . 1 . . . . . . . . 5231 1 496 . 1 1 77 77 GLY H H 1 8.91 0.02 . 1 . . . . . . . . 5231 1 497 . 1 1 77 77 GLY CA C 13 44.51 0.1 . 1 . . . . . . . . 5231 1 498 . 1 1 77 77 GLY N N 15 110.5 0.1 . 1 . . . . . . . . 5231 1 499 . 1 1 78 78 PRO HA H 1 3.948 0.02 . 1 . . . . . . . . 5231 1 500 . 1 1 78 78 PRO HB2 H 1 2.277 0.02 . 2 . . . . . . . . 5231 1 501 . 1 1 78 78 PRO C C 13 178.0 0.1 . 1 . . . . . . . . 5231 1 502 . 1 1 78 78 PRO CA C 13 64.21 0.1 . 1 . . . . . . . . 5231 1 503 . 1 1 78 78 PRO CB C 13 31.77 0.1 . 1 . . . . . . . . 5231 1 504 . 1 1 78 78 PRO CG C 13 25.86 0.1 . 1 . . . . . . . . 5231 1 505 . 1 1 79 79 GLY H H 1 11.33 0.02 . 1 . . . . . . . . 5231 1 506 . 1 1 79 79 GLY HA2 H 1 4.094 0.02 . 1 . . . . . . . . 5231 1 507 . 1 1 79 79 GLY HA3 H 1 3.446 0.02 . 1 . . . . . . . . 5231 1 508 . 1 1 79 79 GLY C C 13 173.8 0.1 . 1 . . . . . . . . 5231 1 509 . 1 1 79 79 GLY CA C 13 43.71 0.1 . 1 . . . . . . . . 5231 1 510 . 1 1 79 79 GLY N N 15 119.7 0.1 . 1 . . . . . . . . 5231 1 511 . 1 1 80 80 ASN H H 1 8.80 0.02 . 1 . . . . . . . . 5231 1 512 . 1 1 80 80 ASN HA H 1 4.032 0.02 . 1 . . . . . . . . 5231 1 513 . 1 1 80 80 ASN HB2 H 1 3.188 0.02 . 1 . . . . . . . . 5231 1 514 . 1 1 80 80 ASN HB3 H 1 2.911 0.02 . 1 . . . . . . . . 5231 1 515 . 1 1 80 80 ASN C C 13 175.0 0.1 . 1 . . . . . . . . 5231 1 516 . 1 1 80 80 ASN CA C 13 56.15 0.1 . 1 . . . . . . . . 5231 1 517 . 1 1 80 80 ASN CB C 13 38.42 0.1 . 1 . . . . . . . . 5231 1 518 . 1 1 80 80 ASN N N 15 117.9 0.1 . 1 . . . . . . . . 5231 1 519 . 1 1 81 81 VAL H H 1 10.24 0.02 . 1 . . . . . . . . 5231 1 520 . 1 1 81 81 VAL CA C 13 67.03 0.1 . 1 . . . . . . . . 5231 1 521 . 1 1 81 81 VAL CG1 C 13 24.09 0.1 . 2 . . . . . . . . 5231 1 522 . 1 1 81 81 VAL N N 15 127.5 0.1 . 1 . . . . . . . . 5231 1 523 . 1 1 82 82 LEU H H 1 8.54 0.02 . 1 . . . . . . . . 5231 1 524 . 1 1 82 82 LEU HA H 1 4.568 0.02 . 1 . . . . . . . . 5231 1 525 . 1 1 82 82 LEU HB2 H 1 1.493 0.02 . 2 . . . . . . . . 5231 1 526 . 1 1 82 82 LEU C C 13 176.0 0.1 . 1 . . . . . . . . 5231 1 527 . 1 1 82 82 LEU CA C 13 55.45 0.1 . 1 . . . . . . . . 5231 1 528 . 1 1 82 82 LEU CB C 13 43.49 0.1 . 1 . . . . . . . . 5231 1 529 . 1 1 82 82 LEU N N 15 128.9 0.1 . 1 . . . . . . . . 5231 1 530 . 1 1 83 83 ALA H H 1 7.57 0.02 . 1 . . . . . . . . 5231 1 531 . 1 1 83 83 ALA HA H 1 4.695 0.02 . 1 . . . . . . . . 5231 1 532 . 1 1 83 83 ALA HB1 H 1 1.244 0.02 . 1 . . . . . . . . 5231 1 533 . 1 1 83 83 ALA HB2 H 1 1.244 0.02 . 1 . . . . . . . . 5231 1 534 . 1 1 83 83 ALA HB3 H 1 1.244 0.02 . 1 . . . . . . . . 5231 1 535 . 1 1 83 83 ALA C C 13 175.3 0.1 . 1 . . . . . . . . 5231 1 536 . 1 1 83 83 ALA CA C 13 51.87 0.1 . 1 . . . . . . . . 5231 1 537 . 1 1 83 83 ALA CB C 13 22.8 0.1 . 1 . . . . . . . . 5231 1 538 . 1 1 83 83 ALA N N 15 114.5 0.1 . 1 . . . . . . . . 5231 1 539 . 1 1 84 84 HIS H H 1 9.17 0.02 . 1 . . . . . . . . 5231 1 540 . 1 1 84 84 HIS CA C 13 54.33 0.1 . 1 . . . . . . . . 5231 1 541 . 1 1 84 84 HIS CB C 13 31.6 0.1 . 1 . . . . . . . . 5231 1 542 . 1 1 84 84 HIS N N 15 115.1 0.1 . 1 . . . . . . . . 5231 1 543 . 1 1 88 88 PRO C C 13 174.5 0.1 . 1 . . . . . . . . 5231 1 544 . 1 1 88 88 PRO CA C 13 64.37 0.1 . 1 . . . . . . . . 5231 1 545 . 1 1 88 88 PRO CB C 13 32.46 0.1 . 1 . . . . . . . . 5231 1 546 . 1 1 89 89 GLY H H 1 5.47 0.02 . 1 . . . . . . . . 5231 1 547 . 1 1 89 89 GLY CA C 13 44.23 0.1 . 1 . . . . . . . . 5231 1 548 . 1 1 89 89 GLY N N 15 108.3 0.1 . 1 . . . . . . . . 5231 1 549 . 1 1 90 90 PRO HA H 1 4.754 0.02 . 1 . . . . . . . . 5231 1 550 . 1 1 90 90 PRO HB2 H 1 2.079 0.02 . 2 . . . . . . . . 5231 1 551 . 1 1 90 90 PRO HG2 H 1 1.832 0.02 . 2 . . . . . . . . 5231 1 552 . 1 1 90 90 PRO C C 13 177.7 0.1 . 1 . . . . . . . . 5231 1 553 . 1 1 90 90 PRO CA C 13 62.94 0.1 . 1 . . . . . . . . 5231 1 554 . 1 1 90 90 PRO CB C 13 33.51 0.1 . 1 . . . . . . . . 5231 1 555 . 1 1 90 90 PRO CG C 13 26.97 0.1 . 1 . . . . . . . . 5231 1 556 . 1 1 91 91 GLY H H 1 8.74 0.02 . 1 . . . . . . . . 5231 1 557 . 1 1 91 91 GLY HA2 H 1 4.055 0.02 . 2 . . . . . . . . 5231 1 558 . 1 1 91 91 GLY C C 13 175.2 0.1 . 1 . . . . . . . . 5231 1 559 . 1 1 91 91 GLY CA C 13 46.97 0.1 . 1 . . . . . . . . 5231 1 560 . 1 1 91 91 GLY N N 15 109.9 0.1 . 1 . . . . . . . . 5231 1 561 . 1 1 92 92 ILE H H 1 8.89 0.02 . 1 . . . . . . . . 5231 1 562 . 1 1 92 92 ILE HA H 1 4.248 0.02 . 1 . . . . . . . . 5231 1 563 . 1 1 92 92 ILE HB H 1 1.621 0.02 . 1 . . . . . . . . 5231 1 564 . 1 1 92 92 ILE C C 13 174.3 0.1 . 1 . . . . . . . . 5231 1 565 . 1 1 92 92 ILE CA C 13 62.07 0.1 . 1 . . . . . . . . 5231 1 566 . 1 1 92 92 ILE CB C 13 37.78 0.1 . 1 . . . . . . . . 5231 1 567 . 1 1 92 92 ILE CG1 C 13 16.65 0.1 . 2 . . . . . . . . 5231 1 568 . 1 1 92 92 ILE N N 15 131.8 0.1 . 1 . . . . . . . . 5231 1 569 . 1 1 93 93 ASN H H 1 7.13 0.02 . 1 . . . . . . . . 5231 1 570 . 1 1 93 93 ASN HA H 1 4.239 0.02 . 1 . . . . . . . . 5231 1 571 . 1 1 93 93 ASN C C 13 175.4 0.1 . 1 . . . . . . . . 5231 1 572 . 1 1 93 93 ASN CA C 13 56.18 0.1 . 1 . . . . . . . . 5231 1 573 . 1 1 93 93 ASN CB C 13 36.0 0.1 . 1 . . . . . . . . 5231 1 574 . 1 1 93 93 ASN N N 15 118.4 0.1 . 1 . . . . . . . . 5231 1 575 . 1 1 94 94 GLY H H 1 7.60 0.02 . 1 . . . . . . . . 5231 1 576 . 1 1 94 94 GLY HA2 H 1 3.905 0.02 . 2 . . . . . . . . 5231 1 577 . 1 1 94 94 GLY C C 13 171.6 0.1 . 1 . . . . . . . . 5231 1 578 . 1 1 94 94 GLY CA C 13 46.02 0.1 . 1 . . . . . . . . 5231 1 579 . 1 1 94 94 GLY N N 15 119.0 0.1 . 1 . . . . . . . . 5231 1 580 . 1 1 95 95 ASP H H 1 7.88 0.02 . 1 . . . . . . . . 5231 1 581 . 1 1 95 95 ASP HA H 1 4.767 0.02 . 1 . . . . . . . . 5231 1 582 . 1 1 95 95 ASP HB2 H 1 2.153 0.02 . 2 . . . . . . . . 5231 1 583 . 1 1 95 95 ASP C C 13 173.8 0.1 . 1 . . . . . . . . 5231 1 584 . 1 1 95 95 ASP CA C 13 55.55 0.1 . 1 . . . . . . . . 5231 1 585 . 1 1 95 95 ASP CB C 13 40.81 0.1 . 1 . . . . . . . . 5231 1 586 . 1 1 95 95 ASP N N 15 121.8 0.1 . 1 . . . . . . . . 5231 1 587 . 1 1 96 96 ALA H H 1 8.07 0.02 . 1 . . . . . . . . 5231 1 588 . 1 1 96 96 ALA HA H 1 5.029 0.02 . 1 . . . . . . . . 5231 1 589 . 1 1 96 96 ALA HB1 H 1 1.185 0.02 . 1 . . . . . . . . 5231 1 590 . 1 1 96 96 ALA HB2 H 1 1.185 0.02 . 1 . . . . . . . . 5231 1 591 . 1 1 96 96 ALA HB3 H 1 1.185 0.02 . 1 . . . . . . . . 5231 1 592 . 1 1 96 96 ALA CA C 13 51.44 0.1 . 1 . . . . . . . . 5231 1 593 . 1 1 96 96 ALA CB C 13 22.46 0.1 . 1 . . . . . . . . 5231 1 594 . 1 1 96 96 ALA N N 15 118.2 0.1 . 1 . . . . . . . . 5231 1 595 . 1 1 97 97 HIS H H 1 9.20 0.02 . 1 . . . . . . . . 5231 1 596 . 1 1 97 97 HIS HB2 H 1 3.265 0.02 . 2 . . . . . . . . 5231 1 597 . 1 1 97 97 HIS C C 13 173.4 0.1 . 1 . . . . . . . . 5231 1 598 . 1 1 97 97 HIS CA C 13 51.12 0.1 . 1 . . . . . . . . 5231 1 599 . 1 1 97 97 HIS CB C 13 34.72 0.1 . 1 . . . . . . . . 5231 1 600 . 1 1 97 97 HIS N N 15 120.5 0.1 . 1 . . . . . . . . 5231 1 601 . 1 1 98 98 PHE H H 1 8.85 0.02 . 1 . . . . . . . . 5231 1 602 . 1 1 98 98 PHE HA H 1 4.352 0.02 . 1 . . . . . . . . 5231 1 603 . 1 1 98 98 PHE HB2 H 1 2.231 0.02 . 2 . . . . . . . . 5231 1 604 . 1 1 98 98 PHE C C 13 173.9 0.1 . 1 . . . . . . . . 5231 1 605 . 1 1 98 98 PHE CA C 13 56.99 0.1 . 1 . . . . . . . . 5231 1 606 . 1 1 98 98 PHE CB C 13 41.81 0.1 . 1 . . . . . . . . 5231 1 607 . 1 1 98 98 PHE N N 15 122.6 0.1 . 1 . . . . . . . . 5231 1 608 . 1 1 99 99 ASP H H 1 8.15 0.02 . 1 . . . . . . . . 5231 1 609 . 1 1 99 99 ASP HA H 1 4.442 0.02 . 1 . . . . . . . . 5231 1 610 . 1 1 99 99 ASP HB2 H 1 3.187 0.02 . 2 . . . . . . . . 5231 1 611 . 1 1 99 99 ASP C C 13 179.4 0.1 . 1 . . . . . . . . 5231 1 612 . 1 1 99 99 ASP CA C 13 54.03 0.1 . 1 . . . . . . . . 5231 1 613 . 1 1 99 99 ASP CB C 13 40.73 0.1 . 1 . . . . . . . . 5231 1 614 . 1 1 99 99 ASP N N 15 123.5 0.1 . 1 . . . . . . . . 5231 1 615 . 1 1 100 100 ASP H H 1 9.83 0.02 . 1 . . . . . . . . 5231 1 616 . 1 1 100 100 ASP HA H 1 5.583 0.02 . 1 . . . . . . . . 5231 1 617 . 1 1 100 100 ASP HB2 H 1 2.959 0.02 . 2 . . . . . . . . 5231 1 618 . 1 1 100 100 ASP C C 13 179.0 0.1 . 1 . . . . . . . . 5231 1 619 . 1 1 100 100 ASP CA C 13 53.38 0.1 . 1 . . . . . . . . 5231 1 620 . 1 1 100 100 ASP CB C 13 40.95 0.1 . 1 . . . . . . . . 5231 1 621 . 1 1 100 100 ASP N N 15 128.4 0.1 . 1 . . . . . . . . 5231 1 622 . 1 1 101 101 ASP H H 1 9.26 0.02 . 1 . . . . . . . . 5231 1 623 . 1 1 101 101 ASP HA H 1 5.021 0.02 . 1 . . . . . . . . 5231 1 624 . 1 1 101 101 ASP HB2 H 1 2.705 0.02 . 2 . . . . . . . . 5231 1 625 . 1 1 101 101 ASP C C 13 177.1 0.1 . 1 . . . . . . . . 5231 1 626 . 1 1 101 101 ASP CA C 13 56.72 0.1 . 1 . . . . . . . . 5231 1 627 . 1 1 101 101 ASP CB C 13 39.08 0.1 . 1 . . . . . . . . 5231 1 628 . 1 1 101 101 ASP N N 15 124.1 0.1 . 1 . . . . . . . . 5231 1 629 . 1 1 102 102 GLU H H 1 7.19 0.02 . 1 . . . . . . . . 5231 1 630 . 1 1 102 102 GLU HA H 1 4.559 0.02 . 1 . . . . . . . . 5231 1 631 . 1 1 102 102 GLU C C 13 175.5 0.1 . 1 . . . . . . . . 5231 1 632 . 1 1 102 102 GLU CA C 13 53.53 0.1 . 1 . . . . . . . . 5231 1 633 . 1 1 102 102 GLU CB C 13 26.2 0.1 . 1 . . . . . . . . 5231 1 634 . 1 1 102 102 GLU CG C 13 35.61 0.1 . 1 . . . . . . . . 5231 1 635 . 1 1 102 102 GLU N N 15 115.8 0.1 . 1 . . . . . . . . 5231 1 636 . 1 1 103 103 GLN H H 1 8.34 0.02 . 1 . . . . . . . . 5231 1 637 . 1 1 103 103 GLN HA H 1 4.431 0.02 . 1 . . . . . . . . 5231 1 638 . 1 1 103 103 GLN HB2 H 1 1.97 0.02 . 2 . . . . . . . . 5231 1 639 . 1 1 103 103 GLN HG2 H 1 2.271 0.02 . 2 . . . . . . . . 5231 1 640 . 1 1 103 103 GLN C C 13 173.3 0.1 . 1 . . . . . . . . 5231 1 641 . 1 1 103 103 GLN CA C 13 53.67 0.1 . 1 . . . . . . . . 5231 1 642 . 1 1 103 103 GLN CB C 13 27.63 0.1 . 1 . . . . . . . . 5231 1 643 . 1 1 103 103 GLN CG C 13 33.56 0.1 . 1 . . . . . . . . 5231 1 644 . 1 1 103 103 GLN N N 15 126.5 0.1 . 1 . . . . . . . . 5231 1 645 . 1 1 104 104 TRP H H 1 9.57 0.02 . 1 . . . . . . . . 5231 1 646 . 1 1 104 104 TRP HA H 1 5.118 0.02 . 1 . . . . . . . . 5231 1 647 . 1 1 104 104 TRP HB2 H 1 3.097 0.02 . 2 . . . . . . . . 5231 1 648 . 1 1 104 104 TRP C C 13 177.6 0.1 . 1 . . . . . . . . 5231 1 649 . 1 1 104 104 TRP CA C 13 57.31 0.1 . 1 . . . . . . . . 5231 1 650 . 1 1 104 104 TRP CB C 13 30.49 0.1 . 1 . . . . . . . . 5231 1 651 . 1 1 104 104 TRP N N 15 131.1 0.1 . 1 . . . . . . . . 5231 1 652 . 1 1 105 105 THR H H 1 8.79 0.02 . 1 . . . . . . . . 5231 1 653 . 1 1 105 105 THR HA H 1 4.951 0.02 . 1 . . . . . . . . 5231 1 654 . 1 1 105 105 THR HB H 1 4.548 0.02 . 1 . . . . . . . . 5231 1 655 . 1 1 105 105 THR C C 13 175.7 0.1 . 1 . . . . . . . . 5231 1 656 . 1 1 105 105 THR CA C 13 60.3 0.1 . 1 . . . . . . . . 5231 1 657 . 1 1 105 105 THR CB C 13 73.25 0.1 . 1 . . . . . . . . 5231 1 658 . 1 1 105 105 THR CG2 C 13 21.25 0.1 . 1 . . . . . . . . 5231 1 659 . 1 1 105 105 THR N N 15 111.1 0.1 . 1 . . . . . . . . 5231 1 660 . 1 1 106 106 LYS H H 1 9.04 0.02 . 1 . . . . . . . . 5231 1 661 . 1 1 106 106 LYS HA H 1 4.587 0.02 . 1 . . . . . . . . 5231 1 662 . 1 1 106 106 LYS HB2 H 1 2.028 0.02 . 2 . . . . . . . . 5231 1 663 . 1 1 106 106 LYS HG2 H 1 1.566 0.02 . 2 . . . . . . . . 5231 1 664 . 1 1 106 106 LYS C C 13 176.1 0.1 . 1 . . . . . . . . 5231 1 665 . 1 1 106 106 LYS CA C 13 56.83 0.1 . 1 . . . . . . . . 5231 1 666 . 1 1 106 106 LYS CB C 13 33.61 0.1 . 1 . . . . . . . . 5231 1 667 . 1 1 106 106 LYS CG C 13 24.71 0.1 . 1 . . . . . . . . 5231 1 668 . 1 1 106 106 LYS CD C 13 29.95 0.1 . 1 . . . . . . . . 5231 1 669 . 1 1 106 106 LYS CE C 13 42.09 0.1 . 1 . . . . . . . . 5231 1 670 . 1 1 106 106 LYS N N 15 119.8 0.1 . 1 . . . . . . . . 5231 1 671 . 1 1 107 107 ASP H H 1 7.46 0.02 . 1 . . . . . . . . 5231 1 672 . 1 1 107 107 ASP HA H 1 4.767 0.02 . 1 . . . . . . . . 5231 1 673 . 1 1 107 107 ASP HB2 H 1 2.738 0.02 . 1 . . . . . . . . 5231 1 674 . 1 1 107 107 ASP HB3 H 1 2.593 0.02 . 1 . . . . . . . . 5231 1 675 . 1 1 107 107 ASP C C 13 175.5 0.1 . 1 . . . . . . . . 5231 1 676 . 1 1 107 107 ASP CA C 13 52.66 0.1 . 1 . . . . . . . . 5231 1 677 . 1 1 107 107 ASP CB C 13 42.1 0.1 . 1 . . . . . . . . 5231 1 678 . 1 1 107 107 ASP N N 15 120.8 0.1 . 1 . . . . . . . . 5231 1 679 . 1 1 108 108 THR H H 1 7.74 0.02 . 1 . . . . . . . . 5231 1 680 . 1 1 108 108 THR HA H 1 4.949 0.02 . 1 . . . . . . . . 5231 1 681 . 1 1 108 108 THR HB H 1 4.646 0.02 . 1 . . . . . . . . 5231 1 682 . 1 1 108 108 THR HG21 H 1 1.343 0.02 . 1 . . . . . . . . 5231 1 683 . 1 1 108 108 THR HG22 H 1 1.343 0.02 . 1 . . . . . . . . 5231 1 684 . 1 1 108 108 THR HG23 H 1 1.343 0.02 . 1 . . . . . . . . 5231 1 685 . 1 1 108 108 THR C C 13 174.9 0.1 . 1 . . . . . . . . 5231 1 686 . 1 1 108 108 THR CA C 13 61.96 0.1 . 1 . . . . . . . . 5231 1 687 . 1 1 108 108 THR CB C 13 68.03 0.1 . 1 . . . . . . . . 5231 1 688 . 1 1 108 108 THR CG2 C 13 22.21 0.1 . 1 . . . . . . . . 5231 1 689 . 1 1 108 108 THR N N 15 109.3 0.1 . 1 . . . . . . . . 5231 1 690 . 1 1 109 109 THR H H 1 8.20 0.02 . 1 . . . . . . . . 5231 1 691 . 1 1 109 109 THR HA H 1 4.277 0.02 . 1 . . . . . . . . 5231 1 692 . 1 1 109 109 THR HB H 1 4.272 0.02 . 1 . . . . . . . . 5231 1 693 . 1 1 109 109 THR HG21 H 1 1.328 0.02 . 1 . . . . . . . . 5231 1 694 . 1 1 109 109 THR HG22 H 1 1.328 0.02 . 1 . . . . . . . . 5231 1 695 . 1 1 109 109 THR HG23 H 1 1.328 0.02 . 1 . . . . . . . . 5231 1 696 . 1 1 109 109 THR C C 13 175.4 0.1 . 1 . . . . . . . . 5231 1 697 . 1 1 109 109 THR CA C 13 64.35 0.1 . 1 . . . . . . . . 5231 1 698 . 1 1 109 109 THR CB C 13 70.08 0.1 . 1 . . . . . . . . 5231 1 699 . 1 1 109 109 THR CG2 C 13 22.51 0.1 . 1 . . . . . . . . 5231 1 700 . 1 1 109 109 THR N N 15 115.2 0.1 . 1 . . . . . . . . 5231 1 701 . 1 1 110 110 GLY H H 1 7.33 0.02 . 1 . . . . . . . . 5231 1 702 . 1 1 110 110 GLY HA2 H 1 4.305 0.02 . 1 . . . . . . . . 5231 1 703 . 1 1 110 110 GLY HA3 H 1 3.56 0.02 . 1 . . . . . . . . 5231 1 704 . 1 1 110 110 GLY C C 13 173.5 0.1 . 1 . . . . . . . . 5231 1 705 . 1 1 110 110 GLY CA C 13 45.52 0.1 . 1 . . . . . . . . 5231 1 706 . 1 1 110 110 GLY N N 15 112.1 0.1 . 1 . . . . . . . . 5231 1 707 . 1 1 111 111 THR H H 1 8.50 0.02 . 1 . . . . . . . . 5231 1 708 . 1 1 111 111 THR HA H 1 3.903 0.02 . 1 . . . . . . . . 5231 1 709 . 1 1 111 111 THR HB H 1 3.714 0.02 . 1 . . . . . . . . 5231 1 710 . 1 1 111 111 THR HG21 H 1 1.282 0.02 . 1 . . . . . . . . 5231 1 711 . 1 1 111 111 THR HG22 H 1 1.282 0.02 . 1 . . . . . . . . 5231 1 712 . 1 1 111 111 THR HG23 H 1 1.282 0.02 . 1 . . . . . . . . 5231 1 713 . 1 1 111 111 THR C C 13 172.8 0.1 . 1 . . . . . . . . 5231 1 714 . 1 1 111 111 THR CA C 13 62.79 0.1 . 1 . . . . . . . . 5231 1 715 . 1 1 111 111 THR CB C 13 67.93 0.1 . 1 . . . . . . . . 5231 1 716 . 1 1 111 111 THR CG2 C 13 24.98 0.1 . 1 . . . . . . . . 5231 1 717 . 1 1 111 111 THR N N 15 123.7 0.1 . 1 . . . . . . . . 5231 1 718 . 1 1 112 112 ASN H H 1 8.33 0.02 . 1 . . . . . . . . 5231 1 719 . 1 1 112 112 ASN HA H 1 4.431 0.02 . 1 . . . . . . . . 5231 1 720 . 1 1 112 112 ASN HB2 H 1 2.766 0.02 . 2 . . . . . . . . 5231 1 721 . 1 1 112 112 ASN C C 13 174.8 0.1 . 1 . . . . . . . . 5231 1 722 . 1 1 112 112 ASN CA C 13 55.94 0.1 . 1 . . . . . . . . 5231 1 723 . 1 1 112 112 ASN CB C 13 41.4 0.1 . 1 . . . . . . . . 5231 1 724 . 1 1 112 112 ASN N N 15 126.8 0.1 . 1 . . . . . . . . 5231 1 725 . 1 1 113 113 LEU H H 1 8.00 0.02 . 1 . . . . . . . . 5231 1 726 . 1 1 113 113 LEU HA H 1 4.578 0.02 . 1 . . . . . . . . 5231 1 727 . 1 1 113 113 LEU HB2 H 1 1.759 0.02 . 2 . . . . . . . . 5231 1 728 . 1 1 113 113 LEU C C 13 176.4 0.1 . 1 . . . . . . . . 5231 1 729 . 1 1 113 113 LEU CA C 13 58.22 0.1 . 1 . . . . . . . . 5231 1 730 . 1 1 113 113 LEU CB C 13 41.72 0.1 . 1 . . . . . . . . 5231 1 731 . 1 1 113 113 LEU CG C 13 29.21 0.1 . 1 . . . . . . . . 5231 1 732 . 1 1 113 113 LEU N N 15 128.3 0.1 . 1 . . . . . . . . 5231 1 733 . 1 1 114 114 PHE H H 1 8.36 0.02 . 1 . . . . . . . . 5231 1 734 . 1 1 114 114 PHE HA H 1 4.114 0.02 . 1 . . . . . . . . 5231 1 735 . 1 1 114 114 PHE HB2 H 1 3.284 0.02 . 2 . . . . . . . . 5231 1 736 . 1 1 114 114 PHE C C 13 175.2 0.1 . 1 . . . . . . . . 5231 1 737 . 1 1 114 114 PHE CA C 13 61.41 0.1 . 1 . . . . . . . . 5231 1 738 . 1 1 114 114 PHE CB C 13 37.77 0.1 . 1 . . . . . . . . 5231 1 739 . 1 1 114 114 PHE N N 15 119.3 0.1 . 1 . . . . . . . . 5231 1 740 . 1 1 115 115 LEU H H 1 8.67 0.02 . 1 . . . . . . . . 5231 1 741 . 1 1 115 115 LEU HA H 1 4.731 0.02 . 1 . . . . . . . . 5231 1 742 . 1 1 115 115 LEU HB2 H 1 2.10 0.02 . 2 . . . . . . . . 5231 1 743 . 1 1 115 115 LEU C C 13 178.0 0.1 . 1 . . . . . . . . 5231 1 744 . 1 1 115 115 LEU CA C 13 57.86 0.1 . 1 . . . . . . . . 5231 1 745 . 1 1 115 115 LEU CB C 13 44.1 0.1 . 1 . . . . . . . . 5231 1 746 . 1 1 115 115 LEU N N 15 120.0 0.1 . 1 . . . . . . . . 5231 1 747 . 1 1 116 116 VAL H H 1 7.85 0.02 . 1 . . . . . . . . 5231 1 748 . 1 1 116 116 VAL HA H 1 4.113 0.02 . 1 . . . . . . . . 5231 1 749 . 1 1 116 116 VAL HB H 1 2.464 0.02 . 1 . . . . . . . . 5231 1 750 . 1 1 116 116 VAL HG11 H 1 1.265 0.02 . 2 . . . . . . . . 5231 1 751 . 1 1 116 116 VAL HG12 H 1 1.265 0.02 . 2 . . . . . . . . 5231 1 752 . 1 1 116 116 VAL HG13 H 1 1.265 0.02 . 2 . . . . . . . . 5231 1 753 . 1 1 116 116 VAL C C 13 179.0 0.1 . 1 . . . . . . . . 5231 1 754 . 1 1 116 116 VAL CA C 13 66.02 0.1 . 1 . . . . . . . . 5231 1 755 . 1 1 116 116 VAL CB C 13 32.62 0.1 . 1 . . . . . . . . 5231 1 756 . 1 1 116 116 VAL CG1 C 13 26.12 0.1 . 1 . . . . . . . . 5231 1 757 . 1 1 116 116 VAL CG2 C 13 23.82 0.1 . 1 . . . . . . . . 5231 1 758 . 1 1 116 116 VAL N N 15 119.8 0.1 . 1 . . . . . . . . 5231 1 759 . 1 1 117 117 ALA H H 1 9.51 0.02 . 1 . . . . . . . . 5231 1 760 . 1 1 117 117 ALA HA H 1 4.17 0.02 . 1 . . . . . . . . 5231 1 761 . 1 1 117 117 ALA HB1 H 1 1.284 0.02 . 1 . . . . . . . . 5231 1 762 . 1 1 117 117 ALA HB2 H 1 1.284 0.02 . 1 . . . . . . . . 5231 1 763 . 1 1 117 117 ALA HB3 H 1 1.284 0.02 . 1 . . . . . . . . 5231 1 764 . 1 1 117 117 ALA C C 13 178.4 0.1 . 1 . . . . . . . . 5231 1 765 . 1 1 117 117 ALA CA C 13 56.16 0.1 . 1 . . . . . . . . 5231 1 766 . 1 1 117 117 ALA CB C 13 16.81 0.1 . 1 . . . . . . . . 5231 1 767 . 1 1 117 117 ALA N N 15 122.3 0.1 . 1 . . . . . . . . 5231 1 768 . 1 1 118 118 ALA H H 1 8.85 0.02 . 1 . . . . . . . . 5231 1 769 . 1 1 118 118 ALA HA H 1 4.054 0.02 . 1 . . . . . . . . 5231 1 770 . 1 1 118 118 ALA HB1 H 1 1.126 0.02 . 1 . . . . . . . . 5231 1 771 . 1 1 118 118 ALA HB2 H 1 1.126 0.02 . 1 . . . . . . . . 5231 1 772 . 1 1 118 118 ALA HB3 H 1 1.126 0.02 . 1 . . . . . . . . 5231 1 773 . 1 1 118 118 ALA C C 13 179.9 0.1 . 1 . . . . . . . . 5231 1 774 . 1 1 118 118 ALA CA C 13 56.82 0.1 . 1 . . . . . . . . 5231 1 775 . 1 1 118 118 ALA CB C 13 17.14 0.1 . 1 . . . . . . . . 5231 1 776 . 1 1 118 118 ALA N N 15 120.8 0.1 . 1 . . . . . . . . 5231 1 777 . 1 1 119 119 HIS H H 1 7.60 0.02 . 1 . . . . . . . . 5231 1 778 . 1 1 119 119 HIS C C 13 174.4 0.1 . 1 . . . . . . . . 5231 1 779 . 1 1 119 119 HIS CA C 13 59.34 0.1 . 1 . . . . . . . . 5231 1 780 . 1 1 119 119 HIS CB C 13 29.34 0.1 . 1 . . . . . . . . 5231 1 781 . 1 1 119 119 HIS N N 15 119.5 0.1 . 1 . . . . . . . . 5231 1 782 . 1 1 120 120 GLU H H 1 9.56 0.02 . 1 . . . . . . . . 5231 1 783 . 1 1 120 120 GLU HA H 1 4.085 0.02 . 1 . . . . . . . . 5231 1 784 . 1 1 120 120 GLU HB2 H 1 1.615 0.02 . 2 . . . . . . . . 5231 1 785 . 1 1 120 120 GLU C C 13 178.1 0.1 . 1 . . . . . . . . 5231 1 786 . 1 1 120 120 GLU CA C 13 58.8 0.1 . 1 . . . . . . . . 5231 1 787 . 1 1 120 120 GLU CB C 13 28.48 0.1 . 1 . . . . . . . . 5231 1 788 . 1 1 120 120 GLU CG C 13 33.46 0.1 . 1 . . . . . . . . 5231 1 789 . 1 1 120 120 GLU N N 15 117.5 0.1 . 1 . . . . . . . . 5231 1 790 . 1 1 121 121 ILE H H 1 9.01 0.02 . 1 . . . . . . . . 5231 1 791 . 1 1 121 121 ILE HA H 1 3.917 0.02 . 1 . . . . . . . . 5231 1 792 . 1 1 121 121 ILE HB H 1 2.057 0.02 . 1 . . . . . . . . 5231 1 793 . 1 1 121 121 ILE C C 13 177.3 0.1 . 1 . . . . . . . . 5231 1 794 . 1 1 121 121 ILE CA C 13 61.99 0.1 . 1 . . . . . . . . 5231 1 795 . 1 1 121 121 ILE CB C 13 36.08 0.1 . 1 . . . . . . . . 5231 1 796 . 1 1 121 121 ILE CG1 C 13 18.99 0.1 . 2 . . . . . . . . 5231 1 797 . 1 1 121 121 ILE N N 15 117.9 0.1 . 1 . . . . . . . . 5231 1 798 . 1 1 122 122 GLY H H 1 7.48 0.02 . 1 . . . . . . . . 5231 1 799 . 1 1 122 122 GLY HA2 H 1 4.095 0.02 . 1 . . . . . . . . 5231 1 800 . 1 1 122 122 GLY HA3 H 1 2.471 0.02 . 1 . . . . . . . . 5231 1 801 . 1 1 122 122 GLY C C 13 177.0 0.1 . 1 . . . . . . . . 5231 1 802 . 1 1 122 122 GLY CA C 13 48.71 0.1 . 1 . . . . . . . . 5231 1 803 . 1 1 122 122 GLY N N 15 108.9 0.1 . 1 . . . . . . . . 5231 1 804 . 1 1 123 123 HIS H H 1 7.20 0.02 . 1 . . . . . . . . 5231 1 805 . 1 1 123 123 HIS HA H 1 5.664 0.02 . 1 . . . . . . . . 5231 1 806 . 1 1 123 123 HIS C C 13 178.6 0.1 . 1 . . . . . . . . 5231 1 807 . 1 1 123 123 HIS CA C 13 57.6 0.1 . 1 . . . . . . . . 5231 1 808 . 1 1 123 123 HIS CB C 13 28.98 0.1 . 1 . . . . . . . . 5231 1 809 . 1 1 123 123 HIS N N 15 119.9 0.1 . 1 . . . . . . . . 5231 1 810 . 1 1 124 124 SER H H 1 8.50 0.02 . 1 . . . . . . . . 5231 1 811 . 1 1 124 124 SER C C 13 175.8 0.1 . 1 . . . . . . . . 5231 1 812 . 1 1 124 124 SER CA C 13 62.75 0.1 . 1 . . . . . . . . 5231 1 813 . 1 1 124 124 SER CB C 13 63.68 0.1 . 1 . . . . . . . . 5231 1 814 . 1 1 124 124 SER N N 15 118.3 0.1 . 1 . . . . . . . . 5231 1 815 . 1 1 125 125 LEU H H 1 7.73 0.02 . 1 . . . . . . . . 5231 1 816 . 1 1 125 125 LEU HA H 1 4.635 0.02 . 1 . . . . . . . . 5231 1 817 . 1 1 125 125 LEU C C 13 178.4 0.1 . 1 . . . . . . . . 5231 1 818 . 1 1 125 125 LEU CA C 13 55.45 0.1 . 1 . . . . . . . . 5231 1 819 . 1 1 125 125 LEU CB C 13 43.63 0.1 . 1 . . . . . . . . 5231 1 820 . 1 1 125 125 LEU N N 15 108.5 0.1 . 1 . . . . . . . . 5231 1 821 . 1 1 126 126 GLY H H 1 8.53 0.02 . 1 . . . . . . . . 5231 1 822 . 1 1 126 126 GLY C C 13 173.3 0.1 . 1 . . . . . . . . 5231 1 823 . 1 1 126 126 GLY CA C 13 45.2 0.1 . 1 . . . . . . . . 5231 1 824 . 1 1 126 126 GLY N N 15 108.5 0.1 . 1 . . . . . . . . 5231 1 825 . 1 1 127 127 LEU H H 1 8.86 0.02 . 1 . . . . . . . . 5231 1 826 . 1 1 127 127 LEU CA C 13 54.29 0.1 . 1 . . . . . . . . 5231 1 827 . 1 1 127 127 LEU CB C 13 42.53 0.1 . 1 . . . . . . . . 5231 1 828 . 1 1 127 127 LEU N N 15 120.1 0.1 . 1 . . . . . . . . 5231 1 829 . 1 1 129 129 HIS HA H 1 4.966 0.02 . 1 . . . . . . . . 5231 1 830 . 1 1 129 129 HIS HB2 H 1 3.511 0.02 . 2 . . . . . . . . 5231 1 831 . 1 1 129 129 HIS C C 13 173.7 0.1 . 1 . . . . . . . . 5231 1 832 . 1 1 129 129 HIS CA C 13 55.62 0.1 . 1 . . . . . . . . 5231 1 833 . 1 1 129 129 HIS CB C 13 29.57 0.1 . 1 . . . . . . . . 5231 1 834 . 1 1 130 130 SER H H 1 6.54 0.02 . 1 . . . . . . . . 5231 1 835 . 1 1 130 130 SER CA C 13 56.8 0.1 . 1 . . . . . . . . 5231 1 836 . 1 1 130 130 SER N N 15 115.7 0.1 . 1 . . . . . . . . 5231 1 837 . 1 1 131 131 ALA HA H 1 4.681 0.02 . 1 . . . . . . . . 5231 1 838 . 1 1 131 131 ALA HB1 H 1 1.517 0.02 . 1 . . . . . . . . 5231 1 839 . 1 1 131 131 ALA HB2 H 1 1.517 0.02 . 1 . . . . . . . . 5231 1 840 . 1 1 131 131 ALA HB3 H 1 1.517 0.02 . 1 . . . . . . . . 5231 1 841 . 1 1 131 131 ALA C C 13 176.8 0.1 . 1 . . . . . . . . 5231 1 842 . 1 1 131 131 ALA CA C 13 52.46 0.1 . 1 . . . . . . . . 5231 1 843 . 1 1 131 131 ALA CB C 13 19.52 0.1 . 1 . . . . . . . . 5231 1 844 . 1 1 132 132 ASN H H 1 8.75 0.02 . 1 . . . . . . . . 5231 1 845 . 1 1 132 132 ASN HA H 1 4.615 0.02 . 1 . . . . . . . . 5231 1 846 . 1 1 132 132 ASN HB2 H 1 2.687 0.02 . 2 . . . . . . . . 5231 1 847 . 1 1 132 132 ASN C C 13 175.6 0.1 . 1 . . . . . . . . 5231 1 848 . 1 1 132 132 ASN CA C 13 53.64 0.1 . 1 . . . . . . . . 5231 1 849 . 1 1 132 132 ASN CB C 13 37.44 0.1 . 1 . . . . . . . . 5231 1 850 . 1 1 132 132 ASN N N 15 120.7 0.1 . 1 . . . . . . . . 5231 1 851 . 1 1 133 133 THR H H 1 8.00 0.02 . 1 . . . . . . . . 5231 1 852 . 1 1 133 133 THR HA H 1 3.85 0.02 . 1 . . . . . . . . 5231 1 853 . 1 1 133 133 THR HB H 1 2.453 0.02 . 1 . . . . . . . . 5231 1 854 . 1 1 133 133 THR HG21 H 1 0.977 0.02 . 1 . . . . . . . . 5231 1 855 . 1 1 133 133 THR HG22 H 1 0.977 0.02 . 1 . . . . . . . . 5231 1 856 . 1 1 133 133 THR HG23 H 1 0.977 0.02 . 1 . . . . . . . . 5231 1 857 . 1 1 133 133 THR C C 13 175.4 0.1 . 1 . . . . . . . . 5231 1 858 . 1 1 133 133 THR CA C 13 63.91 0.1 . 1 . . . . . . . . 5231 1 859 . 1 1 133 133 THR CB C 13 68.55 0.1 . 1 . . . . . . . . 5231 1 860 . 1 1 133 133 THR CG2 C 13 22.18 0.1 . 1 . . . . . . . . 5231 1 861 . 1 1 133 133 THR N N 15 116.9 0.1 . 1 . . . . . . . . 5231 1 862 . 1 1 134 134 GLU H H 1 8.94 0.02 . 1 . . . . . . . . 5231 1 863 . 1 1 134 134 GLU HA H 1 4.417 0.02 . 1 . . . . . . . . 5231 1 864 . 1 1 134 134 GLU HB2 H 1 2.123 0.02 . 2 . . . . . . . . 5231 1 865 . 1 1 134 134 GLU HG2 H 1 2.416 0.02 . 2 . . . . . . . . 5231 1 866 . 1 1 134 134 GLU C C 13 176.2 0.1 . 1 . . . . . . . . 5231 1 867 . 1 1 134 134 GLU CA C 13 56.19 0.1 . 1 . . . . . . . . 5231 1 868 . 1 1 134 134 GLU CB C 13 29.23 0.1 . 1 . . . . . . . . 5231 1 869 . 1 1 134 134 GLU CG C 13 36.22 0.1 . 1 . . . . . . . . 5231 1 870 . 1 1 134 134 GLU N N 15 120.4 0.1 . 1 . . . . . . . . 5231 1 871 . 1 1 135 135 ALA H H 1 7.68 0.02 . 1 . . . . . . . . 5231 1 872 . 1 1 135 135 ALA HA H 1 4.636 0.02 . 1 . . . . . . . . 5231 1 873 . 1 1 135 135 ALA HB1 H 1 1.848 0.02 . 1 . . . . . . . . 5231 1 874 . 1 1 135 135 ALA HB2 H 1 1.848 0.02 . 1 . . . . . . . . 5231 1 875 . 1 1 135 135 ALA HB3 H 1 1.848 0.02 . 1 . . . . . . . . 5231 1 876 . 1 1 135 135 ALA C C 13 179.0 0.1 . 1 . . . . . . . . 5231 1 877 . 1 1 135 135 ALA CA C 13 52.0 0.1 . 1 . . . . . . . . 5231 1 878 . 1 1 135 135 ALA CB C 13 19.59 0.1 . 1 . . . . . . . . 5231 1 879 . 1 1 135 135 ALA N N 15 124.4 0.1 . 1 . . . . . . . . 5231 1 880 . 1 1 136 136 LEU H H 1 11.47 0.02 . 1 . . . . . . . . 5231 1 881 . 1 1 136 136 LEU HA H 1 4.596 0.02 . 1 . . . . . . . . 5231 1 882 . 1 1 136 136 LEU C C 13 180.5 0.1 . 1 . . . . . . . . 5231 1 883 . 1 1 136 136 LEU CA C 13 58.06 0.1 . 1 . . . . . . . . 5231 1 884 . 1 1 136 136 LEU CB C 13 42.0 0.1 . 1 . . . . . . . . 5231 1 885 . 1 1 136 136 LEU N N 15 131.7 0.1 . 1 . . . . . . . . 5231 1 886 . 1 1 137 137 MET H H 1 7.93 0.02 . 1 . . . . . . . . 5231 1 887 . 1 1 137 137 MET HA H 1 4.55 0.02 . 1 . . . . . . . . 5231 1 888 . 1 1 137 137 MET C C 13 177.2 0.1 . 1 . . . . . . . . 5231 1 889 . 1 1 137 137 MET CA C 13 53.36 0.1 . 1 . . . . . . . . 5231 1 890 . 1 1 137 137 MET CB C 13 27.31 0.1 . 1 . . . . . . . . 5231 1 891 . 1 1 137 137 MET N N 15 110.9 0.1 . 1 . . . . . . . . 5231 1 892 . 1 1 138 138 TYR H H 1 8.03 0.02 . 1 . . . . . . . . 5231 1 893 . 1 1 138 138 TYR CA C 13 57.45 0.1 . 1 . . . . . . . . 5231 1 894 . 1 1 138 138 TYR CB C 13 39.38 0.1 . 1 . . . . . . . . 5231 1 895 . 1 1 138 138 TYR N N 15 128.5 0.1 . 1 . . . . . . . . 5231 1 896 . 1 1 142 142 HIS H H 1 8.20 0.02 . 1 . . . . . . . . 5231 1 897 . 1 1 142 142 HIS HA H 1 4.16 0.02 . 1 . . . . . . . . 5231 1 898 . 1 1 142 142 HIS HB2 H 1 2.442 0.02 . 2 . . . . . . . . 5231 1 899 . 1 1 142 142 HIS C C 13 177.8 0.1 . 1 . . . . . . . . 5231 1 900 . 1 1 142 142 HIS CA C 13 56.97 0.1 . 1 . . . . . . . . 5231 1 901 . 1 1 142 142 HIS CB C 13 37.3 0.1 . 1 . . . . . . . . 5231 1 902 . 1 1 142 142 HIS N N 15 127.6 0.1 . 1 . . . . . . . . 5231 1 903 . 1 1 143 143 SER H H 1 7.44 0.02 . 1 . . . . . . . . 5231 1 904 . 1 1 143 143 SER HA H 1 4.65 0.02 . 1 . . . . . . . . 5231 1 905 . 1 1 143 143 SER HB2 H 1 3.338 0.02 . 2 . . . . . . . . 5231 1 906 . 1 1 143 143 SER C C 13 174.9 0.1 . 1 . . . . . . . . 5231 1 907 . 1 1 143 143 SER CA C 13 59.23 0.1 . 1 . . . . . . . . 5231 1 908 . 1 1 143 143 SER CB C 13 61.86 0.1 . 1 . . . . . . . . 5231 1 909 . 1 1 143 143 SER N N 15 112.9 0.1 . 1 . . . . . . . . 5231 1 910 . 1 1 144 144 LEU H H 1 6.63 0.02 . 1 . . . . . . . . 5231 1 911 . 1 1 144 144 LEU CA C 13 56.88 0.1 . 1 . . . . . . . . 5231 1 912 . 1 1 144 144 LEU CB C 13 44.13 0.1 . 1 . . . . . . . . 5231 1 913 . 1 1 144 144 LEU N N 15 120.5 0.1 . 1 . . . . . . . . 5231 1 914 . 1 1 146 146 ASP HA H 1 4.827 0.02 . 1 . . . . . . . . 5231 1 915 . 1 1 146 146 ASP HB2 H 1 2.874 0.02 . 1 . . . . . . . . 5231 1 916 . 1 1 146 146 ASP HB3 H 1 2.667 0.02 . 1 . . . . . . . . 5231 1 917 . 1 1 146 146 ASP C C 13 177.0 0.1 . 1 . . . . . . . . 5231 1 918 . 1 1 146 146 ASP CA C 13 53.1 0.1 . 1 . . . . . . . . 5231 1 919 . 1 1 146 146 ASP CB C 13 41.33 0.1 . 1 . . . . . . . . 5231 1 920 . 1 1 147 147 LEU H H 1 8.85 0.02 . 1 . . . . . . . . 5231 1 921 . 1 1 147 147 LEU HA H 1 4.223 0.02 . 1 . . . . . . . . 5231 1 922 . 1 1 147 147 LEU HB2 H 1 1.691 0.02 . 2 . . . . . . . . 5231 1 923 . 1 1 147 147 LEU C C 13 179.1 0.1 . 1 . . . . . . . . 5231 1 924 . 1 1 147 147 LEU CA C 13 57.24 0.1 . 1 . . . . . . . . 5231 1 925 . 1 1 147 147 LEU CB C 13 42.26 0.1 . 1 . . . . . . . . 5231 1 926 . 1 1 147 147 LEU N N 15 126.3 0.1 . 1 . . . . . . . . 5231 1 927 . 1 1 148 148 THR H H 1 8.37 0.02 . 1 . . . . . . . . 5231 1 928 . 1 1 148 148 THR HA H 1 4.233 0.02 . 1 . . . . . . . . 5231 1 929 . 1 1 148 148 THR HB H 1 4.341 0.02 . 1 . . . . . . . . 5231 1 930 . 1 1 148 148 THR HG21 H 1 1.35 0.02 . 1 . . . . . . . . 5231 1 931 . 1 1 148 148 THR HG22 H 1 1.35 0.02 . 1 . . . . . . . . 5231 1 932 . 1 1 148 148 THR HG23 H 1 1.35 0.02 . 1 . . . . . . . . 5231 1 933 . 1 1 148 148 THR C C 13 175.7 0.1 . 1 . . . . . . . . 5231 1 934 . 1 1 148 148 THR CA C 13 64.7 0.1 . 1 . . . . . . . . 5231 1 935 . 1 1 148 148 THR CB C 13 69.18 0.1 . 1 . . . . . . . . 5231 1 936 . 1 1 148 148 THR CG2 C 13 22.21 0.1 . 1 . . . . . . . . 5231 1 937 . 1 1 148 148 THR N N 15 111.9 0.1 . 1 . . . . . . . . 5231 1 938 . 1 1 149 149 ARG H H 1 7.37 0.02 . 1 . . . . . . . . 5231 1 939 . 1 1 149 149 ARG HA H 1 4.493 0.02 . 1 . . . . . . . . 5231 1 940 . 1 1 149 149 ARG HB2 H 1 2.098 0.02 . 1 . . . . . . . . 5231 1 941 . 1 1 149 149 ARG HB3 H 1 1.688 0.02 . 1 . . . . . . . . 5231 1 942 . 1 1 149 149 ARG HG2 H 1 1.694 0.02 . 2 . . . . . . . . 5231 1 943 . 1 1 149 149 ARG HD2 H 1 3.20 0.02 . 2 . . . . . . . . 5231 1 944 . 1 1 149 149 ARG C C 13 175.6 0.1 . 1 . . . . . . . . 5231 1 945 . 1 1 149 149 ARG CA C 13 55.06 0.1 . 1 . . . . . . . . 5231 1 946 . 1 1 149 149 ARG CB C 13 30.7 0.1 . 1 . . . . . . . . 5231 1 947 . 1 1 149 149 ARG CG C 13 27.8 0.1 . 1 . . . . . . . . 5231 1 948 . 1 1 149 149 ARG CD C 13 43.67 0.1 . 1 . . . . . . . . 5231 1 949 . 1 1 149 149 ARG N N 15 119.5 0.1 . 1 . . . . . . . . 5231 1 950 . 1 1 150 150 PHE H H 1 7.32 0.02 . 1 . . . . . . . . 5231 1 951 . 1 1 150 150 PHE HA H 1 4.277 0.02 . 1 . . . . . . . . 5231 1 952 . 1 1 150 150 PHE HB2 H 1 2.971 0.02 . 2 . . . . . . . . 5231 1 953 . 1 1 150 150 PHE C C 13 174.7 0.1 . 1 . . . . . . . . 5231 1 954 . 1 1 150 150 PHE CA C 13 60.49 0.1 . 1 . . . . . . . . 5231 1 955 . 1 1 150 150 PHE CB C 13 39.88 0.1 . 1 . . . . . . . . 5231 1 956 . 1 1 150 150 PHE N N 15 121.1 0.1 . 1 . . . . . . . . 5231 1 957 . 1 1 151 151 ARG H H 1 6.97 0.02 . 1 . . . . . . . . 5231 1 958 . 1 1 151 151 ARG HA H 1 4.037 0.02 . 1 . . . . . . . . 5231 1 959 . 1 1 151 151 ARG HB2 H 1 1.766 0.02 . 2 . . . . . . . . 5231 1 960 . 1 1 151 151 ARG HG2 H 1 1.502 0.02 . 2 . . . . . . . . 5231 1 961 . 1 1 151 151 ARG HD2 H 1 3.172 0.02 . 2 . . . . . . . . 5231 1 962 . 1 1 151 151 ARG C C 13 174.7 0.1 . 1 . . . . . . . . 5231 1 963 . 1 1 151 151 ARG CA C 13 54.32 0.1 . 1 . . . . . . . . 5231 1 964 . 1 1 151 151 ARG CB C 13 33.46 0.1 . 1 . . . . . . . . 5231 1 965 . 1 1 151 151 ARG CG C 13 26.68 0.1 . 1 . . . . . . . . 5231 1 966 . 1 1 151 151 ARG CD C 13 43.81 0.1 . 1 . . . . . . . . 5231 1 967 . 1 1 151 151 ARG N N 15 126.4 0.1 . 1 . . . . . . . . 5231 1 968 . 1 1 152 152 LEU H H 1 8.43 0.02 . 1 . . . . . . . . 5231 1 969 . 1 1 152 152 LEU HA H 1 3.906 0.02 . 1 . . . . . . . . 5231 1 970 . 1 1 152 152 LEU HB2 H 1 1.494 0.02 . 2 . . . . . . . . 5231 1 971 . 1 1 152 152 LEU HG H 1 1.404 0.02 . 1 . . . . . . . . 5231 1 972 . 1 1 152 152 LEU C C 13 177.1 0.1 . 1 . . . . . . . . 5231 1 973 . 1 1 152 152 LEU CA C 13 55.31 0.1 . 1 . . . . . . . . 5231 1 974 . 1 1 152 152 LEU CB C 13 43.39 0.1 . 1 . . . . . . . . 5231 1 975 . 1 1 152 152 LEU CG C 13 27.3 0.1 . 1 . . . . . . . . 5231 1 976 . 1 1 152 152 LEU N N 15 122.2 0.1 . 1 . . . . . . . . 5231 1 977 . 1 1 153 153 SER H H 1 8.24 0.02 . 1 . . . . . . . . 5231 1 978 . 1 1 153 153 SER HA H 1 4.559 0.02 . 1 . . . . . . . . 5231 1 979 . 1 1 153 153 SER HB2 H 1 4.175 0.02 . 2 . . . . . . . . 5231 1 980 . 1 1 153 153 SER C C 13 175.2 0.1 . 1 . . . . . . . . 5231 1 981 . 1 1 153 153 SER CA C 13 58.63 0.1 . 1 . . . . . . . . 5231 1 982 . 1 1 153 153 SER CB C 13 66.07 0.1 . 1 . . . . . . . . 5231 1 983 . 1 1 153 153 SER N N 15 117.9 0.1 . 1 . . . . . . . . 5231 1 984 . 1 1 154 154 GLN H H 1 9.01 0.02 . 1 . . . . . . . . 5231 1 985 . 1 1 154 154 GLN HA H 1 3.939 0.02 . 1 . . . . . . . . 5231 1 986 . 1 1 154 154 GLN HB2 H 1 2.104 0.02 . 2 . . . . . . . . 5231 1 987 . 1 1 154 154 GLN HG2 H 1 2.537 0.02 . 2 . . . . . . . . 5231 1 988 . 1 1 154 154 GLN C C 13 177.4 0.1 . 1 . . . . . . . . 5231 1 989 . 1 1 154 154 GLN CA C 13 58.6 0.1 . 1 . . . . . . . . 5231 1 990 . 1 1 154 154 GLN CB C 13 28.33 0.1 . 1 . . . . . . . . 5231 1 991 . 1 1 154 154 GLN CG C 13 34.3 0.1 . 1 . . . . . . . . 5231 1 992 . 1 1 154 154 GLN N N 15 122.2 0.1 . 1 . . . . . . . . 5231 1 993 . 1 1 155 155 ASP H H 1 8.19 0.02 . 1 . . . . . . . . 5231 1 994 . 1 1 155 155 ASP HA H 1 4.588 0.02 . 1 . . . . . . . . 5231 1 995 . 1 1 155 155 ASP HB2 H 1 3.548 0.02 . 2 . . . . . . . . 5231 1 996 . 1 1 155 155 ASP C C 13 177.9 0.1 . 1 . . . . . . . . 5231 1 997 . 1 1 155 155 ASP CA C 13 58.97 0.1 . 1 . . . . . . . . 5231 1 998 . 1 1 155 155 ASP CB C 13 43.54 0.1 . 1 . . . . . . . . 5231 1 999 . 1 1 155 155 ASP N N 15 118.0 0.1 . 1 . . . . . . . . 5231 1 1000 . 1 1 156 156 ASP H H 1 7.35 0.02 . 1 . . . . . . . . 5231 1 1001 . 1 1 156 156 ASP HA H 1 4.844 0.02 . 1 . . . . . . . . 5231 1 1002 . 1 1 156 156 ASP HB2 H 1 2.742 0.02 . 2 . . . . . . . . 5231 1 1003 . 1 1 156 156 ASP C C 13 176.2 0.1 . 1 . . . . . . . . 5231 1 1004 . 1 1 156 156 ASP CA C 13 57.69 0.1 . 1 . . . . . . . . 5231 1 1005 . 1 1 156 156 ASP CB C 13 39.05 0.1 . 1 . . . . . . . . 5231 1 1006 . 1 1 156 156 ASP N N 15 116.3 0.1 . 1 . . . . . . . . 5231 1 1007 . 1 1 157 157 ILE H H 1 7.92 0.02 . 1 . . . . . . . . 5231 1 1008 . 1 1 157 157 ILE HA H 1 3.645 0.02 . 1 . . . . . . . . 5231 1 1009 . 1 1 157 157 ILE HB H 1 3.651 0.02 . 1 . . . . . . . . 5231 1 1010 . 1 1 157 157 ILE HG21 H 1 0.934 0.02 . 1 . . . . . . . . 5231 1 1011 . 1 1 157 157 ILE HG22 H 1 0.934 0.02 . 1 . . . . . . . . 5231 1 1012 . 1 1 157 157 ILE HG23 H 1 0.934 0.02 . 1 . . . . . . . . 5231 1 1013 . 1 1 157 157 ILE C C 13 177.6 0.1 . 1 . . . . . . . . 5231 1 1014 . 1 1 157 157 ILE CA C 13 66.0 0.1 . 1 . . . . . . . . 5231 1 1015 . 1 1 157 157 ILE CB C 13 38.73 0.1 . 1 . . . . . . . . 5231 1 1016 . 1 1 157 157 ILE CG1 C 13 17.48 0.1 . 2 . . . . . . . . 5231 1 1017 . 1 1 157 157 ILE N N 15 116.1 0.1 . 1 . . . . . . . . 5231 1 1018 . 1 1 158 158 ASN H H 1 9.15 0.02 . 1 . . . . . . . . 5231 1 1019 . 1 1 158 158 ASN HA H 1 4.357 0.02 . 1 . . . . . . . . 5231 1 1020 . 1 1 158 158 ASN HB2 H 1 3.134 0.02 . 2 . . . . . . . . 5231 1 1021 . 1 1 158 158 ASN C C 13 178.9 0.1 . 1 . . . . . . . . 5231 1 1022 . 1 1 158 158 ASN CA C 13 55.32 0.1 . 1 . . . . . . . . 5231 1 1023 . 1 1 158 158 ASN CB C 13 37.46 0.1 . 1 . . . . . . . . 5231 1 1024 . 1 1 158 158 ASN N N 15 118.7 0.1 . 1 . . . . . . . . 5231 1 1025 . 1 1 159 159 GLY H H 1 8.09 0.02 . 1 . . . . . . . . 5231 1 1026 . 1 1 159 159 GLY C C 13 176.1 0.1 . 1 . . . . . . . . 5231 1 1027 . 1 1 159 159 GLY CA C 13 46.36 0.1 . 1 . . . . . . . . 5231 1 1028 . 1 1 159 159 GLY N N 15 109.3 0.1 . 1 . . . . . . . . 5231 1 1029 . 1 1 160 160 ILE H H 1 8.66 0.02 . 1 . . . . . . . . 5231 1 1030 . 1 1 160 160 ILE HA H 1 4.345 0.02 . 1 . . . . . . . . 5231 1 1031 . 1 1 160 160 ILE C C 13 178.3 0.1 . 1 . . . . . . . . 5231 1 1032 . 1 1 160 160 ILE CA C 13 61.15 0.1 . 1 . . . . . . . . 5231 1 1033 . 1 1 160 160 ILE CB C 13 39.06 0.1 . 1 . . . . . . . . 5231 1 1034 . 1 1 160 160 ILE N N 15 125.5 0.1 . 1 . . . . . . . . 5231 1 1035 . 1 1 161 161 GLN H H 1 8.55 0.02 . 1 . . . . . . . . 5231 1 1036 . 1 1 161 161 GLN HA H 1 4.297 0.02 . 1 . . . . . . . . 5231 1 1037 . 1 1 161 161 GLN C C 13 179.8 0.1 . 1 . . . . . . . . 5231 1 1038 . 1 1 161 161 GLN CA C 13 58.54 0.1 . 1 . . . . . . . . 5231 1 1039 . 1 1 161 161 GLN CB C 13 26.84 0.1 . 1 . . . . . . . . 5231 1 1040 . 1 1 161 161 GLN N N 15 122.1 0.1 . 1 . . . . . . . . 5231 1 1041 . 1 1 162 162 SER H H 1 7.78 0.02 . 1 . . . . . . . . 5231 1 1042 . 1 1 162 162 SER CA C 13 61.82 0.1 . 1 . . . . . . . . 5231 1 1043 . 1 1 162 162 SER N N 15 119.5 0.1 . 1 . . . . . . . . 5231 1 1044 . 1 1 164 164 TYR HA H 1 4.864 0.02 . 1 . . . . . . . . 5231 1 1045 . 1 1 164 164 TYR HB2 H 1 3.495 0.02 . 2 . . . . . . . . 5231 1 1046 . 1 1 164 164 TYR C C 13 175.7 0.1 . 1 . . . . . . . . 5231 1 1047 . 1 1 164 164 TYR CA C 13 58.97 0.1 . 1 . . . . . . . . 5231 1 1048 . 1 1 164 164 TYR CB C 13 41.73 0.1 . 1 . . . . . . . . 5231 1 1049 . 1 1 165 165 GLY H H 1 8.29 0.02 . 1 . . . . . . . . 5231 1 1050 . 1 1 165 165 GLY CA C 13 44.44 0.1 . 1 . . . . . . . . 5231 1 1051 . 1 1 165 165 GLY N N 15 109.0 0.1 . 1 . . . . . . . . 5231 1 1052 . 1 1 168 168 PRO HA H 1 4.477 0.02 . 1 . . . . . . . . 5231 1 1053 . 1 1 168 168 PRO HB2 H 1 2.351 0.02 . 1 . . . . . . . . 5231 1 1054 . 1 1 168 168 PRO HB3 H 1 2.012 0.02 . 1 . . . . . . . . 5231 1 1055 . 1 1 168 168 PRO C C 13 176.5 0.1 . 1 . . . . . . . . 5231 1 1056 . 1 1 168 168 PRO CA C 13 63.13 0.1 . 1 . . . . . . . . 5231 1 1057 . 1 1 168 168 PRO CB C 13 32.3 0.1 . 1 . . . . . . . . 5231 1 1058 . 1 1 168 168 PRO CG C 13 27.82 0.1 . 1 . . . . . . . . 5231 1 1059 . 1 1 168 168 PRO CD C 13 50.69 0.1 . 1 . . . . . . . . 5231 1 1060 . 1 1 169 169 ASP H H 1 8.28 0.02 . 1 . . . . . . . . 5231 1 1061 . 1 1 169 169 ASP HA H 1 4.619 0.02 . 1 . . . . . . . . 5231 1 1062 . 1 1 169 169 ASP HB2 H 1 2.675 0.02 . 2 . . . . . . . . 5231 1 1063 . 1 1 169 169 ASP C C 13 176.0 0.1 . 1 . . . . . . . . 5231 1 1064 . 1 1 169 169 ASP CA C 13 54.53 0.1 . 1 . . . . . . . . 5231 1 1065 . 1 1 169 169 ASP CB C 13 41.31 0.1 . 1 . . . . . . . . 5231 1 1066 . 1 1 169 169 ASP N N 15 120.2 0.1 . 1 . . . . . . . . 5231 1 1067 . 1 1 170 170 SER H H 1 8.10 0.02 . 1 . . . . . . . . 5231 1 1068 . 1 1 170 170 SER CA C 13 56.38 0.1 . 1 . . . . . . . . 5231 1 1069 . 1 1 170 170 SER CB C 13 63.89 0.1 . 1 . . . . . . . . 5231 1 1070 . 1 1 170 170 SER N N 15 116.7 0.1 . 1 . . . . . . . . 5231 1 1071 . 1 1 171 171 PRO HA H 1 4.496 0.02 . 1 . . . . . . . . 5231 1 1072 . 1 1 171 171 PRO HB2 H 1 2.359 0.02 . 1 . . . . . . . . 5231 1 1073 . 1 1 171 171 PRO HB3 H 1 2.024 0.02 . 1 . . . . . . . . 5231 1 1074 . 1 1 171 171 PRO HG2 H 1 2.804 0.02 . 2 . . . . . . . . 5231 1 1075 . 1 1 171 171 PRO HD2 H 1 3.826 0.02 . 2 . . . . . . . . 5231 1 1076 . 1 1 171 171 PRO C C 13 176.8 0.1 . 1 . . . . . . . . 5231 1 1077 . 1 1 171 171 PRO CA C 13 63.45 0.1 . 1 . . . . . . . . 5231 1 1078 . 1 1 171 171 PRO CB C 13 32.47 0.1 . 1 . . . . . . . . 5231 1 1079 . 1 1 171 171 PRO CG C 13 27.81 0.1 . 1 . . . . . . . . 5231 1 1080 . 1 1 171 171 PRO CD C 13 51.06 0.1 . 1 . . . . . . . . 5231 1 1081 . 1 1 172 172 GLU H H 1 8.43 0.02 . 1 . . . . . . . . 5231 1 1082 . 1 1 172 172 GLU HA H 1 4.376 0.02 . 1 . . . . . . . . 5231 1 1083 . 1 1 172 172 GLU HB2 H 1 2.159 0.02 . 1 . . . . . . . . 5231 1 1084 . 1 1 172 172 GLU HB3 H 1 2.017 0.02 . 1 . . . . . . . . 5231 1 1085 . 1 1 172 172 GLU C C 13 176.0 0.1 . 1 . . . . . . . . 5231 1 1086 . 1 1 172 172 GLU CA C 13 57.03 0.1 . 1 . . . . . . . . 5231 1 1087 . 1 1 172 172 GLU CB C 13 30.59 0.1 . 1 . . . . . . . . 5231 1 1088 . 1 1 172 172 GLU CG C 13 36.74 0.1 . 1 . . . . . . . . 5231 1 1089 . 1 1 172 172 GLU N N 15 121.5 0.1 . 1 . . . . . . . . 5231 1 1090 . 1 1 173 173 THR H H 1 7.69 0.02 . 1 . . . . . . . . 5231 1 1091 . 1 1 173 173 THR CA C 13 63.27 0.1 . 1 . . . . . . . . 5231 1 1092 . 1 1 173 173 THR CB C 13 71.11 0.1 . 1 . . . . . . . . 5231 1 1093 . 1 1 173 173 THR N N 15 120.2 0.1 . 1 . . . . . . . . 5231 1 stop_ save_