data_5099 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5099 _Entry.Title ; Backbone and side chain 1H, 13C, and 15N Chemical Shift Assignments for N-TIMP-1 in N-TIMP-1/MMP-3(E202Q) Complex ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2001-08-03 _Entry.Accession_date 2001-08-03 _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 S. Arumugam . . . 5099 2 Steven 'Van Doren' . R. . 5099 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5099 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 488 5099 '13C chemical shifts' 327 5099 '15N chemical shifts' 113 5099 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2003-05-20 . update author 'correction of chemical shifts' 5099 2 . . 2003-05-20 . update author 'addition of side chain assignmnets' 5099 3 . . 2002-08-22 . original author 'original release' 5099 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5099 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 12634064 _Citation.Full_citation . _Citation.Title ; Increased backbone mobility in Beta-barrel enhances entropy gain driving binding of N-TIMP-1 to MMP-3 ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full . _Citation.Journal_volume 327 _Citation.Journal_issue 3 _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 719 _Citation.Page_last 734 _Citation.Year 2003 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 S. Arumugam . . . 5099 1 2 G. Gao . . . 5099 1 3 B. Patton . . . 5099 1 4 V. Semenchenko . . . 5099 1 5 K. Brew . . . 5099 1 6 Steven 'Van Doren' . R. . 5099 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'TIMP-1/MMP-3(E202Q) complex' 5099 1 'tissue inhibitor of matrix metalloproteinases' 5099 1 'NMR assignments' 5099 1 'matrix metalloproteinase-3' 5099 1 stop_ save_ save_entry_reference_1 _Citation.Sf_category citations _Citation.Sf_framecode entry_reference_1 _Citation.Entry_ID 5099 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Global Orientation of Bound MMP-3 and N-TIMP-1 in Solution via Residual Dipolar Couplings ; _Citation.Status . _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _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 S. Arumugam . . . 5099 2 2 Steven 'Van Doren' . R. . 5099 2 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'protein-protein interactions' 5099 2 docking 5099 2 'residual dipolar couplings' 5099 2 NMR 5099 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_N-TIMP-1_MMP-3(deltaC)_complex _Assembly.Sf_category assembly _Assembly.Sf_framecode system_N-TIMP-1_MMP-3(deltaC)_complex _Assembly.Entry_ID 5099 _Assembly.ID 1 _Assembly.Name 'N-terminus of Tissue Inhibitor of Metalloproteinases-1/Matrix MetalloProteinase-3(E202Q)(deltaC) complex' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'all disulfide bound' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details ; Present system contains only the N-terminal 2/3 of the Tissue Inhibitor of Metalloproteinase, whereas the related system is full-length. In addition, the present system has been studied in solution as a complex with a mutant matrix metalloproteinase-3(E202Q). The system of PDB 1D2B has been studied in solution as a complex with a mutant matrix metalloproteinase-3(E202Q). ; _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5099 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 'N-TIMP-1, inhibitor' 1 $N-TIMP-1 . . . native . . . . . 5099 1 2 'MMP-3, metalloproteinase' 2 $MMP-3 . . . native . . . . . 5099 1 3 'CALCIUM (II) ION' 3 $CA . . . native . . . . . 5099 1 4 'ZINC (II) ION' 4 $ZN . . . native . . . . . 5099 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 1 1 SG . 1 . 1 CYS 70 70 SG . . . . . . . . . . 5099 1 2 disulfide single . 1 . 1 CYS 3 3 SG . 1 . 1 CYS 99 99 SG . . . . . . . . . . 5099 1 3 disulfide single . 1 . 1 CYS 13 13 SG . 1 . 1 CYS 124 124 SG . . . . . . . . . . 5099 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1UEA . . . . . ; Present system contains only the N-terminal 2/3 of the Tissue Inhibitor of Metalloproteinase, whereas the related system is full-length. In addition, the present system has been studied in solution as a complex with a mutant matrix metalloproteinase-3(E202Q). ; 5099 1 yes PDB 1D2B . 'free N-TIMP-1' . . . . 5099 1 yes PDB 1UEA . 'MMP-3 bound TIMP-1' . . . ; The present system has been studied in solution as a complex with a mutant matrix metalloproteinase-3(E202Q). ; 5099 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'N-terminus of Tissue Inhibitor of Metalloproteinases-1/Matrix MetalloProteinase-3(E202Q)(deltaC) complex' system 5099 1 'N-TIMP-1/MMP-3(deltaC) complex' abbreviation 5099 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'N-TIMP-1 inhibits the enzymatic activity of matrix metalloproteinases-1,-2, &-3 with Ki values less than 2.0 nM.' 5099 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_N-TIMP-1 _Entity.Sf_category entity _Entity.Sf_framecode N-TIMP-1 _Entity.Entry_ID 5099 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'N-terminus of Tissue Inhibitor of Metalloproteinases-1/Matrix MetalloProteinases-3(catalytic domain) complex' _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 ; CTCVPPHPQTAFCNSDLVIR AKFVGTPEVNQTTLYQRYEI KMTKMYKGFQALGDAADIRF VYTPAMESVCGYFHRSHNRS EEFLIAGKLQDGLLHITTCS FVAPWNSLSLAQRRGFTKTY TVGCEE ; _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 126 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _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 99.38 100.00 1.87e-113 . . . . 5099 1 2 no BMRB 15395 . MMP3 . . . . . 93.06 161 98.76 99.38 4.49e-112 . . . . 5099 1 3 no BMRB 15396 . MMP3 . . . . . 93.06 161 98.76 99.38 4.49e-112 . . . . 5099 1 4 no BMRB 4173 . SLN . . . . . 100.00 173 99.42 100.00 7.58e-123 . . . . 5099 1 5 no BMRB 4364 . stromelysin . . . . . 95.95 166 98.80 99.40 3.43e-116 . . . . 5099 1 6 no BMRB 4365 . stromelysin . . . . . 95.95 166 98.80 99.40 3.43e-116 . . . . 5099 1 7 no BMRB 4366 . stromelysin . . . . . 95.95 166 98.80 99.40 3.43e-116 . . . . 5099 1 8 no BMRB 5153 . MMP-3 . . . . . 100.00 173 100.00 100.00 1.66e-123 . . . . 5099 1 9 no BMRB 5231 . stromelysin . . . . . 100.00 173 99.42 100.00 7.58e-123 . . . . 5099 1 10 no PDB 1B3D . Stromelysin-1 . . . . . 100.00 173 99.42 100.00 7.58e-123 . . . . 5099 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 99.40 100.00 2.08e-118 . . . . 5099 1 12 no PDB 1BIW . "Design And Synthesis Of Conformationally-Constrained Mmp Inhibitors" . . . . . 100.00 173 99.42 100.00 7.58e-123 . . . . 5099 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 99.42 100.00 7.58e-123 . . . . 5099 1 14 no PDB 1BQO . "Discovery Of Potent, Achiral Matrix Metalloproteinase Inhibitors" . . . . . 100.00 173 99.42 100.00 7.58e-123 . . . . 5099 1 15 no PDB 1C3I . "Human Stromelysin-1 Catalytic Domain Complexed With Ro-26-2812" . . . . . 100.00 173 99.42 100.00 7.58e-123 . . . . 5099 1 16 no PDB 1C8T . "Human Stromelysin-1 (E202q) Catalytic Domain Complexed With Ro-26-2812" . . . . . 95.95 167 100.00 100.00 5.70e-118 . . . . 5099 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 99.40 100.00 3.12e-119 . . . . 5099 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 99.40 100.00 3.12e-119 . . . . 5099 1 19 no PDB 1CQR . "Crystal Structure Of The Stromelysin Catalytic Domain At 2.0 A Resolution" . . . . . 100.00 173 99.42 100.00 7.58e-123 . . . . 5099 1 20 no PDB 1D5J . "Crystal Structure Of Mmp3 Complexed With A Thiazepine Based Inhibitor." . . . . . 100.00 173 99.42 100.00 7.58e-123 . . . . 5099 1 21 no PDB 1D7X . "Crystal Structure Of Mmp3 Complexed With A Modified Proline Scaffold Based Inhibitor." . . . . . 100.00 173 99.42 100.00 7.58e-123 . . . . 5099 1 22 no PDB 1D8F . "Crystal Structure Of Mmp3 Complexed With A Piperazine Based Inhibitor." . . . . . 100.00 173 99.42 100.00 7.58e-123 . . . . 5099 1 23 no PDB 1D8M . "Crystal Structure Of Mmp3 Complexed With A Heterocycle- Based Inhibitor" . . . . . 100.00 173 99.42 100.00 7.58e-123 . . . . 5099 1 24 no PDB 1G05 . "Heterocycle-Based Mmp Inhibitor With P2'substituents" . . . . . 100.00 173 99.42 100.00 7.58e-123 . . . . 5099 1 25 no PDB 1G49 . "A Carboxylic Acid Based Inhibitor In Complex With Mmp3" . . . . . 100.00 173 99.42 100.00 7.58e-123 . . . . 5099 1 26 no PDB 1G4K . "X-ray Structure Of A Novel Matrix Metalloproteinase Inhibitor Complexed To Stromelysin" . . . . . 97.11 168 99.40 100.00 3.12e-119 . . . . 5099 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 99.38 100.00 1.28e-112 . . . . 5099 1 28 no PDB 1HY7 . "A Carboxylic Acid Based Inhibitor In Complex With Mmp3" . . . . . 100.00 173 99.42 100.00 7.58e-123 . . . . 5099 1 29 no PDB 1OO9 . "Orientation In Solution Of Mmp-3 Catalytic Domain And N- Timp-1 From Residual Dipolar Couplings" . . . . . 97.11 168 99.40 100.00 3.12e-119 . . . . 5099 1 30 no PDB 1QIA . "Crystal Structure Of Stromelysin Catalytic Domain" . . . . . 93.64 162 99.38 100.00 2.50e-114 . . . . 5099 1 31 no PDB 1QIC . "Crystal Structure Of Stromelysin Catalytic Domain" . . . . . 93.06 161 99.38 100.00 1.58e-113 . . . . 5099 1 32 no PDB 1SLM . "Crystal Structure Of Fibroblast Stromelysin-1: The C-Truncated Human Proenzyme" . . . . . 100.00 255 99.42 100.00 5.95e-123 . . . . 5099 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 99.42 100.00 7.58e-123 . . . . 5099 1 34 no PDB 1UEA . "Mmp-3TIMP-1 Complex" . . . . . 100.00 173 98.27 98.84 9.83e-121 . . . . 5099 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 99.42 100.00 8.29e-123 . . . . 5099 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 99.42 100.00 8.29e-123 . . . . 5099 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 99.39 100.00 9.12e-117 . . . . 5099 1 38 no PDB 2D1O . "Stromelysin-1 (Mmp-3) Complexed To A Hydroxamic Acid Inhibitor" . . . . . 98.84 171 99.42 100.00 2.05e-121 . . . . 5099 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 99.38 100.00 1.87e-113 . . . . 5099 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 99.38 100.00 1.87e-113 . . . . 5099 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 99.38 100.00 1.87e-113 . . . . 5099 1 42 no PDB 2SRT . "Catalytic Domain Of Human Stromelysin-1 At Ph 5.5 And 40oc Complexed With Inhibitor" . . . . . 100.00 173 99.42 100.00 7.58e-123 . . . . 5099 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 99.39 100.00 9.12e-117 . . . . 5099 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 99.40 100.00 2.08e-118 . . . . 5099 1 45 no PDB 3OHO . "Catalytic Domain Of Stromelysin-1 In Complex With N-Hydroxy-2-(4- Methylphenylsulfonamido)acetamide" . . . . . 97.69 169 99.41 100.00 6.83e-120 . . . . 5099 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 99.40 100.00 3.12e-119 . . . . 5099 1 47 no PDB 4DPE . "Structure Of Mmp3 Complexed With A Platinum-based Inhibitor." . . . . . 100.00 173 99.42 100.00 7.58e-123 . . . . 5099 1 48 no PDB 4G9L . "Structure Of Mmp3 Complexed With Nngh Inhibitor" . . . . . 100.00 173 99.42 100.00 7.58e-123 . . . . 5099 1 49 no PDB 4JA1 . "Structure Of Mmp3 Complexed With A Platinum-based Inhibitor" . . . . . 100.00 173 99.42 100.00 7.58e-123 . . . . 5099 1 50 no DBJ BAD97003 . "matrix metalloproteinase 3 preproprotein variant [Homo sapiens]" . . . . . 100.00 477 99.42 100.00 8.11e-120 . . . . 5099 1 51 no DBJ BAD97011 . "matrix metalloproteinase 3 preproprotein variant [Homo sapiens]" . . . . . 100.00 477 99.42 100.00 8.11e-120 . . . . 5099 1 52 no DBJ BAG36115 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 477 99.42 100.00 8.11e-120 . . . . 5099 1 53 no EMBL CAA28859 . "preprostromelysin [Homo sapiens]" . . . . . 100.00 477 99.42 100.00 8.11e-120 . . . . 5099 1 54 no GB AAA00036 . "prostromelysin=matrix metalloproteinase [human, Peptide, 477 aa]" . . . . . 100.00 477 99.42 100.00 8.11e-120 . . . . 5099 1 55 no GB AAA36321 . "matrix metalloproteinase-3 [Homo sapiens]" . . . . . 100.00 477 99.42 100.00 8.11e-120 . . . . 5099 1 56 no GB AAB36942 . "stromelysin [Homo sapiens]" . . . . . 100.00 477 99.42 100.00 8.11e-120 . . . . 5099 1 57 no GB AAD45887 . "stromelysin catalytic domain [synthetic construct]" . . . . . 100.00 174 99.42 100.00 8.29e-123 . . . . 5099 1 58 no GB AAH69676 . "Matrix metallopeptidase 3 (stromelysin 1, progelatinase) [Homo sapiens]" . . . . . 100.00 477 99.42 100.00 8.11e-120 . . . . 5099 1 59 no REF NP_002413 . "stromelysin-1 preproprotein [Homo sapiens]" . . . . . 100.00 477 99.42 100.00 8.11e-120 . . . . 5099 1 60 no REF XP_002822450 . "PREDICTED: stromelysin-1 [Pongo abelii]" . . . . . 100.00 477 98.27 100.00 3.25e-119 . . . . 5099 1 61 no REF XP_003253099 . "PREDICTED: stromelysin-1 [Nomascus leucogenys]" . . . . . 100.00 477 98.84 100.00 6.18e-120 . . . . 5099 1 62 no REF XP_003828425 . "PREDICTED: stromelysin-1 [Pan paniscus]" . . . . . 100.00 477 99.42 100.00 5.03e-120 . . . . 5099 1 63 no REF XP_004052086 . "PREDICTED: stromelysin-1 [Gorilla gorilla gorilla]" . . . . . 100.00 477 98.27 99.42 2.67e-118 . . . . 5099 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 99.42 100.00 8.11e-120 . . . . 5099 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'N-terminus of Tissue Inhibitor of Metalloproteinases-1/Matrix MetalloProteinases-3(catalytic domain) complex' common 5099 1 'N-TIMP-1/MMP-3(deltaC) complex' abbreviation 5099 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 . CYS . 5099 1 2 . THR . 5099 1 3 . CYS . 5099 1 4 . VAL . 5099 1 5 . PRO . 5099 1 6 . PRO . 5099 1 7 . HIS . 5099 1 8 . PRO . 5099 1 9 . GLN . 5099 1 10 . THR . 5099 1 11 . ALA . 5099 1 12 . PHE . 5099 1 13 . CYS . 5099 1 14 . ASN . 5099 1 15 . SER . 5099 1 16 . ASP . 5099 1 17 . LEU . 5099 1 18 . VAL . 5099 1 19 . ILE . 5099 1 20 . ARG . 5099 1 21 . ALA . 5099 1 22 . LYS . 5099 1 23 . PHE . 5099 1 24 . VAL . 5099 1 25 . GLY . 5099 1 26 . THR . 5099 1 27 . PRO . 5099 1 28 . GLU . 5099 1 29 . VAL . 5099 1 30 . ASN . 5099 1 31 . GLN . 5099 1 32 . THR . 5099 1 33 . THR . 5099 1 34 . LEU . 5099 1 35 . TYR . 5099 1 36 . GLN . 5099 1 37 . ARG . 5099 1 38 . TYR . 5099 1 39 . GLU . 5099 1 40 . ILE . 5099 1 41 . LYS . 5099 1 42 . MET . 5099 1 43 . THR . 5099 1 44 . LYS . 5099 1 45 . MET . 5099 1 46 . TYR . 5099 1 47 . LYS . 5099 1 48 . GLY . 5099 1 49 . PHE . 5099 1 50 . GLN . 5099 1 51 . ALA . 5099 1 52 . LEU . 5099 1 53 . GLY . 5099 1 54 . ASP . 5099 1 55 . ALA . 5099 1 56 . ALA . 5099 1 57 . ASP . 5099 1 58 . ILE . 5099 1 59 . ARG . 5099 1 60 . PHE . 5099 1 61 . VAL . 5099 1 62 . TYR . 5099 1 63 . THR . 5099 1 64 . PRO . 5099 1 65 . ALA . 5099 1 66 . MET . 5099 1 67 . GLU . 5099 1 68 . SER . 5099 1 69 . VAL . 5099 1 70 . CYS . 5099 1 71 . GLY . 5099 1 72 . TYR . 5099 1 73 . PHE . 5099 1 74 . HIS . 5099 1 75 . ARG . 5099 1 76 . SER . 5099 1 77 . HIS . 5099 1 78 . ASN . 5099 1 79 . ARG . 5099 1 80 . SER . 5099 1 81 . GLU . 5099 1 82 . GLU . 5099 1 83 . PHE . 5099 1 84 . LEU . 5099 1 85 . ILE . 5099 1 86 . ALA . 5099 1 87 . GLY . 5099 1 88 . LYS . 5099 1 89 . LEU . 5099 1 90 . GLN . 5099 1 91 . ASP . 5099 1 92 . GLY . 5099 1 93 . LEU . 5099 1 94 . LEU . 5099 1 95 . HIS . 5099 1 96 . ILE . 5099 1 97 . THR . 5099 1 98 . THR . 5099 1 99 . CYS . 5099 1 100 . SER . 5099 1 101 . PHE . 5099 1 102 . VAL . 5099 1 103 . ALA . 5099 1 104 . PRO . 5099 1 105 . TRP . 5099 1 106 . ASN . 5099 1 107 . SER . 5099 1 108 . LEU . 5099 1 109 . SER . 5099 1 110 . LEU . 5099 1 111 . ALA . 5099 1 112 . GLN . 5099 1 113 . ARG . 5099 1 114 . ARG . 5099 1 115 . GLY . 5099 1 116 . PHE . 5099 1 117 . THR . 5099 1 118 . LYS . 5099 1 119 . THR . 5099 1 120 . TYR . 5099 1 121 . THR . 5099 1 122 . VAL . 5099 1 123 . GLY . 5099 1 124 . CYS . 5099 1 125 . GLU . 5099 1 126 . GLU . 5099 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 . CYS 1 1 5099 1 . THR 2 2 5099 1 . CYS 3 3 5099 1 . VAL 4 4 5099 1 . PRO 5 5 5099 1 . PRO 6 6 5099 1 . HIS 7 7 5099 1 . PRO 8 8 5099 1 . GLN 9 9 5099 1 . THR 10 10 5099 1 . ALA 11 11 5099 1 . PHE 12 12 5099 1 . CYS 13 13 5099 1 . ASN 14 14 5099 1 . SER 15 15 5099 1 . ASP 16 16 5099 1 . LEU 17 17 5099 1 . VAL 18 18 5099 1 . ILE 19 19 5099 1 . ARG 20 20 5099 1 . ALA 21 21 5099 1 . LYS 22 22 5099 1 . PHE 23 23 5099 1 . VAL 24 24 5099 1 . GLY 25 25 5099 1 . THR 26 26 5099 1 . PRO 27 27 5099 1 . GLU 28 28 5099 1 . VAL 29 29 5099 1 . ASN 30 30 5099 1 . GLN 31 31 5099 1 . THR 32 32 5099 1 . THR 33 33 5099 1 . LEU 34 34 5099 1 . TYR 35 35 5099 1 . GLN 36 36 5099 1 . ARG 37 37 5099 1 . TYR 38 38 5099 1 . GLU 39 39 5099 1 . ILE 40 40 5099 1 . LYS 41 41 5099 1 . MET 42 42 5099 1 . THR 43 43 5099 1 . LYS 44 44 5099 1 . MET 45 45 5099 1 . TYR 46 46 5099 1 . LYS 47 47 5099 1 . GLY 48 48 5099 1 . PHE 49 49 5099 1 . GLN 50 50 5099 1 . ALA 51 51 5099 1 . LEU 52 52 5099 1 . GLY 53 53 5099 1 . ASP 54 54 5099 1 . ALA 55 55 5099 1 . ALA 56 56 5099 1 . ASP 57 57 5099 1 . ILE 58 58 5099 1 . ARG 59 59 5099 1 . PHE 60 60 5099 1 . VAL 61 61 5099 1 . TYR 62 62 5099 1 . THR 63 63 5099 1 . PRO 64 64 5099 1 . ALA 65 65 5099 1 . MET 66 66 5099 1 . GLU 67 67 5099 1 . SER 68 68 5099 1 . VAL 69 69 5099 1 . CYS 70 70 5099 1 . GLY 71 71 5099 1 . TYR 72 72 5099 1 . PHE 73 73 5099 1 . HIS 74 74 5099 1 . ARG 75 75 5099 1 . SER 76 76 5099 1 . HIS 77 77 5099 1 . ASN 78 78 5099 1 . ARG 79 79 5099 1 . SER 80 80 5099 1 . GLU 81 81 5099 1 . GLU 82 82 5099 1 . PHE 83 83 5099 1 . LEU 84 84 5099 1 . ILE 85 85 5099 1 . ALA 86 86 5099 1 . GLY 87 87 5099 1 . LYS 88 88 5099 1 . LEU 89 89 5099 1 . GLN 90 90 5099 1 . ASP 91 91 5099 1 . GLY 92 92 5099 1 . LEU 93 93 5099 1 . LEU 94 94 5099 1 . HIS 95 95 5099 1 . ILE 96 96 5099 1 . THR 97 97 5099 1 . THR 98 98 5099 1 . CYS 99 99 5099 1 . SER 100 100 5099 1 . PHE 101 101 5099 1 . VAL 102 102 5099 1 . ALA 103 103 5099 1 . PRO 104 104 5099 1 . TRP 105 105 5099 1 . ASN 106 106 5099 1 . SER 107 107 5099 1 . LEU 108 108 5099 1 . SER 109 109 5099 1 . LEU 110 110 5099 1 . ALA 111 111 5099 1 . GLN 112 112 5099 1 . ARG 113 113 5099 1 . ARG 114 114 5099 1 . GLY 115 115 5099 1 . PHE 116 116 5099 1 . THR 117 117 5099 1 . LYS 118 118 5099 1 . THR 119 119 5099 1 . TYR 120 120 5099 1 . THR 121 121 5099 1 . VAL 122 122 5099 1 . GLY 123 123 5099 1 . CYS 124 124 5099 1 . GLU 125 125 5099 1 . GLU 126 126 5099 1 stop_ save_ save_MMP-3 _Entity.Sf_category entity _Entity.Sf_framecode MMP-3 _Entity.Entry_ID 5099 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name 'Metalloproteinases-1/Matrix MetalloProteinase-3(catalytic domain, residue 83-255)' _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 DEQWTKDTTGTNLFLVAAHQ 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 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 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 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 . . SWISS-PROT P08254 . 'Stromelysin-1 precursor (SL-1) (Matrix metalloproteinase-3) (MMP-3) (Transin-1)' . . . . . 100.00 477 99.42 100.00 4.94e-98 . . . . 5099 2 . . REF XP_508723 . 'PREDICTED: matrix metalloproteinase 3 isoform 4 [Pan troglodytes]' . . . . . 100.00 477 99.42 100.00 3.42e-98 . . . . 5099 2 . . REF XP_001154004 . 'PREDICTED: matrix metalloproteinase 3 isoform 2 [Pan troglodytes]' . . . . . 100.00 410 99.42 100.00 4.15e-98 . . . . 5099 2 . . REF XP_001153941 . 'PREDICTED: matrix metalloproteinase 3 isoform 1 [Pan troglodytes]' . . . . . 100.00 447 99.42 100.00 7.82e-98 . . . . 5099 2 . . REF NP_002413 . 'matrix metalloproteinase 3 preproprotein [Homo sapiens]' . . . . . 100.00 477 99.42 100.00 4.94e-98 . . . . 5099 2 . . GenBank AAH69676 . 'Matrix metallopeptidase 3 (stromelysin 1, progelatinase) [Homo sapiens]' . . . . . 100.00 477 99.42 100.00 4.94e-98 . . . . 5099 2 . . GenBank AAD45887 . 'stromelysin catalytic domain [synthetic construct]' . . . . . 100.00 174 99.42 100.00 5.51e-97 . . . . 5099 2 . . GenBank AAB36942 . 'stromelysin [Homo sapiens]' . . . . . 100.00 477 99.42 100.00 4.94e-98 . . . . 5099 2 . . GenBank AAA36321 . 'matrix metalloproteinase-3' . . . . . 100.00 477 99.42 100.00 4.94e-98 . . . . 5099 2 . . GenBank AAA00036 . 'prostromelysin=matrix metalloproteinase [human, Peptide, 477 aa]' . . . . . 100.00 477 99.42 100.00 4.94e-98 . . . . 5099 2 . . EMBL CAA28859 . 'preprostromelysin [Homo sapiens]' . . . . . 100.00 477 99.42 100.00 4.94e-98 . . . . 5099 2 . . DBJ BAG36115 . 'unnamed protein product [Homo sapiens]' . . . . . 100.00 477 99.42 100.00 4.94e-98 . . . . 5099 2 . . DBJ BAD97011 . 'matrix metalloproteinase 3 preproprotein variant [Homo sapiens]' . . . . . 100.00 477 99.42 100.00 4.94e-98 . . . . 5099 2 . . DBJ BAD97003 . 'matrix metalloproteinase 3 preproprotein variant [Homo sapiens]' . . . . . 100.00 477 99.42 100.00 4.94e-98 . . . . 5099 2 . . PDB 3USN . 'Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1' . . . . . 97.11 168 99.40 100.00 3.46e-94 . . . . 5099 2 . . PDB 2USN . 'Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With Thiadiazole Inhibitor Pnu-141803' . . . . . 95.38 165 99.39 100.00 2.85e-92 . . . . 5099 2 . . PDB 2SRT . 'Catalytic Domain Of Human Stromelysin-1 At Ph 5.5 And 40oc Complexed With Inhibitor' . . . . . 100.00 173 99.42 100.00 5.28e-97 . . . . 5099 2 . . PDB 2JT6 . 'Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3) In The Presence Of 3-4'-Cyanobyphenyl-4-Yloxy)-N- Hdydroxypropionamide (Mmp-3 Inhibitor Vii)' . . . . . 93.06 161 99.38 100.00 1.07e-89 . . . . 5099 2 . . PDB 2JT5 . 'Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3) In The Presence Of N-Hydroxy-2-[n-(2-Hydroxyethyl)biphenyl-4- Sulfonamide] Hydroxamic Acid (Mlc88)' . . . . . 93.06 161 99.38 100.00 1.07e-89 . . . . 5099 2 . . PDB 2JNP . 'Solution Structure Of Matrix Metalloproteinase 3 (Mmp-3) In The Presence Of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]glycyl Hydroxamic Acid (Nngh)' . . . . . 93.06 161 99.38 100.00 1.07e-89 . . . . 5099 2 . . PDB 2D1O . 'Stromelysin-1 (Mmp-3) Complexed To A Hydroxamic Acid Inhibitor' . . . . . 98.84 171 99.42 100.00 6.90e-96 . . . . 5099 2 . . PDB 1USN . 'Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With Thiadiazole Inhibitor Pnu-142372' . . . . . 95.38 165 99.39 100.00 2.85e-92 . . . . 5099 2 . . PDB 1UMT . 'Stromelysin-1 Catalytic Domain With Hydrophobic Inhibitor Bound, Ph 7.0, 32oc, 20 Mm Cacl2, 15% Acetonitrile; Nmr Average Of 20 Structures Minimized With Restraints' . . . . . 100.00 174 99.42 100.00 5.51e-97 . . . . 5099 2 . . PDB 1UMS . 'Stromelysin-1 Catalytic Domain With Hydrophobic Inhibitor Bound, Ph 7.0, 32oc, 20 Mm Cacl2, 15% Acetonitrile; Nmr Ensemble Of 20 Structures' . . . . . 100.00 174 99.42 100.00 5.51e-97 . . . . 5099 2 . . PDB 1UEA . 'Mmp-3TIMP-1 Complex' . . . . . 100.00 173 98.27 98.84 2.16e-95 . . . . 5099 2 . . PDB 1SLN . 'Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The N-Carboxy- Alkyl Inhibitor L-702,842' . . . . . 99.42 173 99.42 100.00 2.16e-96 . . . . 5099 2 . . PDB 1SLM . 'Crystal Structure Of Fibroblast Stromelysin-1: The C- Truncated Human Proenzyme' . . . . . 100.00 255 99.42 100.00 5.02e-98 . . . . 5099 2 . . PDB 1QIC . 'Crystal Structure Of Stromelysin Catalytic Domain' . . . . . 93.06 161 99.38 100.00 9.41e-90 . . . . 5099 2 . . PDB 1QIA . 'Crystal Structure Of Stromelysin Catalytic Domain' . . . . . 93.64 162 99.38 100.00 2.24e-90 . . . . 5099 2 . . PDB 1OO9 . 'Orientation In Solution Of Mmp-3 Catalytic Domain And N- Timp-1 From Residual Dipolar Couplings' . . . . . 97.11 168 99.40 100.00 3.46e-94 . . . . 5099 2 . . PDB 1HY7 . 'A Carboxylic Acid Based Inhibitor In Complex With Mmp3' . . . . . 100.00 173 99.42 100.00 5.28e-97 . . . . 5099 2 . . PDB 1HFS . 'Crystal Structure Of The Catalytic Domain Of Human Fibroblast Stromelysin-1 Inhibited With The N-Carboxy- Alkyl Inhibitor L-764,004' . . . . . 92.49 160 99.38 100.00 4.75e-89 . . . . 5099 2 . . PDB 1G4K . 'X-Ray Structure Of A Novel Matrix Metalloproteinase Inhibitor Complexed To Stromelysin' . . . . . 97.11 168 99.40 100.00 3.46e-94 . . . . 5099 2 . . PDB 1G49 . 'A Carboxylic Acid Based Inhibitor In Complex With Mmp3' . . . . . 100.00 173 99.42 100.00 5.28e-97 . . . . 5099 2 . . PDB 1G05 . 'Heterocycle-Based Mmp Inhibitor With P2'substituents' . . . . . 100.00 173 99.42 100.00 5.28e-97 . . . . 5099 2 . . PDB 1D8M . 'Crystal Structure Of Mmp3 Complexed With A Heterocycle- Based Inhibitor' . . . . . 100.00 173 99.42 100.00 5.28e-97 . . . . 5099 2 . . PDB 1D8F . 'Crystal Structure Of Mmp3 Complexed With A Piperazine Based Inhibitor.' . . . . . 100.00 173 99.42 100.00 5.28e-97 . . . . 5099 2 . . PDB 1D7X . 'Crystal Structure Of Mmp3 Complexed With A Modified Proline Scaffold Based Inhibitor.' . . . . . 100.00 173 99.42 100.00 5.28e-97 . . . . 5099 2 . . PDB 1D5J . 'Crystal Structure Of Mmp3 Complexed With A Thiazepine Based Inhibitor.' . . . . . 100.00 173 99.42 100.00 5.28e-97 . . . . 5099 2 . . PDB 1CQR . 'Crystal Structure Of The Stromelysin Catalytic Domain At 2.0 A Resolution' . . . . . 100.00 173 99.42 100.00 5.28e-97 . . . . 5099 2 . . PDB 1CIZ . 'X-Ray Structure Of Human Stromelysin Catalytic Domain Complexes With Non-Peptide Inhibitors: Implication For Inhibitor Selectivity' . . . . . 97.11 168 99.40 100.00 3.46e-94 . . . . 5099 2 . . PDB 1CAQ . 'X-Ray Structure Of Human Stromelysin Catalytic Domain Complexes With Non-Peptide Inhibitors: Implication For Inhibitor Selectivity' . . . . . 97.11 168 99.40 100.00 3.46e-94 . . . . 5099 2 . . PDB 1C8T . 'Human Stromelysin-1 (E202q) Catalytic Domain Complexed With Ro-26-2812' . . . . . 95.95 167 100.00 100.00 3.26e-93 . . . . 5099 2 . . PDB 1C3I . 'Human Stromelysin-1 Catalytic Domain Complexed With Ro-26- 2812' . . . . . 100.00 173 99.42 100.00 5.28e-97 . . . . 5099 2 . . PDB 1BQO . 'Discovery Of Potent, Achiral Matrix Metalloproteinase Inhibitors' . . . . . 100.00 173 99.42 100.00 5.28e-97 . . . . 5099 2 . . PDB 1BM6 . 'Solution Structure Of The Catalytic Domain Of Human Stromelysin-1 Complexed To A Potent Non-Peptidic Inhibitor, Nmr, 20 Structures' . . . . . 100.00 173 99.42 100.00 5.28e-97 . . . . 5099 2 . . PDB 1BIW . 'Design And Synthesis Of Conformationally-Constrained Mmp Inhibitors' . . . . . 100.00 173 99.42 100.00 5.28e-97 . . . . 5099 2 . . PDB 1B8Y . 'X-Ray Structure Of Human Stromelysin Catalytic Domain Complexed With Non-Peptide Inhibitors: Implications For Inhibitor Selectivity' . . . . . 96.53 167 99.40 100.00 1.51e-93 . . . . 5099 2 . . PDB 1B3D . Stromelysin-1 . . . . . 100.00 173 99.42 100.00 5.28e-97 . . . . 5099 2 . . BMRB 5785 . 'Matrix MetalloProteinases-3 or stromelysin 1' . . . . . 100.00 173 100.00 100.00 1.66e-97 . . . . 5099 2 . . BMRB 5231 . stromelysin . . . . . 100.00 173 99.42 100.00 5.28e-97 . . . . 5099 2 . . BMRB 5153 . 'MatrixMetalloProteinases-3(catalytic domain)' . . . . . 100.00 173 100.00 100.00 1.66e-97 . . . . 5099 2 . . BMRB 4366 . stromelysin . . . . . 95.95 166 98.80 99.40 7.64e-92 . . . . 5099 2 . . BMRB 4365 . stromelysin . . . . . 95.95 166 98.80 99.40 7.64e-92 . . . . 5099 2 . . BMRB 4364 . stromelysin . . . . . 95.95 166 98.80 99.40 7.64e-92 . . . . 5099 2 . . BMRB 4173 . STROMELYSIN-1 . . . . . 100.00 173 99.42 100.00 5.28e-97 . . . . 5099 2 . . BMRB 15396 . MMP3 . . . . . 93.06 161 99.38 100.00 1.07e-89 . . . . 5099 2 . . BMRB 15395 . MMP3 . . . . . 93.06 161 99.38 100.00 1.07e-89 . . . . 5099 2 . . BMRB 15120 . entity_1 . . . . . 93.06 161 99.38 100.00 1.07e-89 . . . . 5099 2 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Metalloproteinases-1/Matrix MetalloProteinase-3(catalytic domain, residue 83-255)' common 5099 2 'N-TIMP-1/MMP-3(deltaC) complex' abbreviation 5099 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 . PHE . 5099 2 2 . ARG . 5099 2 3 . THR . 5099 2 4 . PHE . 5099 2 5 . PRO . 5099 2 6 . GLY . 5099 2 7 . ILE . 5099 2 8 . PRO . 5099 2 9 . LYS . 5099 2 10 . TRP . 5099 2 11 . ARG . 5099 2 12 . LYS . 5099 2 13 . THR . 5099 2 14 . HIS . 5099 2 15 . LEU . 5099 2 16 . THR . 5099 2 17 . TYR . 5099 2 18 . ARG . 5099 2 19 . ILE . 5099 2 20 . VAL . 5099 2 21 . ASN . 5099 2 22 . TYR . 5099 2 23 . THR . 5099 2 24 . PRO . 5099 2 25 . ASP . 5099 2 26 . LEU . 5099 2 27 . PRO . 5099 2 28 . LYS . 5099 2 29 . ASP . 5099 2 30 . ALA . 5099 2 31 . VAL . 5099 2 32 . ASP . 5099 2 33 . SER . 5099 2 34 . ALA . 5099 2 35 . VAL . 5099 2 36 . GLU . 5099 2 37 . LYS . 5099 2 38 . ALA . 5099 2 39 . LEU . 5099 2 40 . LYS . 5099 2 41 . VAL . 5099 2 42 . TRP . 5099 2 43 . GLU . 5099 2 44 . GLU . 5099 2 45 . VAL . 5099 2 46 . THR . 5099 2 47 . PRO . 5099 2 48 . LEU . 5099 2 49 . THR . 5099 2 50 . PHE . 5099 2 51 . SER . 5099 2 52 . ARG . 5099 2 53 . LEU . 5099 2 54 . TYR . 5099 2 55 . GLU . 5099 2 56 . GLY . 5099 2 57 . GLU . 5099 2 58 . ALA . 5099 2 59 . ASP . 5099 2 60 . ILE . 5099 2 61 . MET . 5099 2 62 . ILE . 5099 2 63 . SER . 5099 2 64 . PHE . 5099 2 65 . ALA . 5099 2 66 . VAL . 5099 2 67 . ARG . 5099 2 68 . GLU . 5099 2 69 . HIS . 5099 2 70 . GLY . 5099 2 71 . ASP . 5099 2 72 . PHE . 5099 2 73 . TYR . 5099 2 74 . PRO . 5099 2 75 . PHE . 5099 2 76 . ASP . 5099 2 77 . GLY . 5099 2 78 . PRO . 5099 2 79 . GLY . 5099 2 80 . ASN . 5099 2 81 . VAL . 5099 2 82 . LEU . 5099 2 83 . ALA . 5099 2 84 . HIS . 5099 2 85 . ALA . 5099 2 86 . TYR . 5099 2 87 . ALA . 5099 2 88 . PRO . 5099 2 89 . GLY . 5099 2 90 . PRO . 5099 2 91 . GLY . 5099 2 92 . ILE . 5099 2 93 . ASN . 5099 2 94 . GLY . 5099 2 95 . ASP . 5099 2 96 . ALA . 5099 2 97 . HIS . 5099 2 98 . PHE . 5099 2 99 . ASP . 5099 2 100 . ASP . 5099 2 101 . ASP . 5099 2 102 . GLU . 5099 2 103 . GLN . 5099 2 104 . TRP . 5099 2 105 . THR . 5099 2 106 . LYS . 5099 2 107 . ASP . 5099 2 108 . THR . 5099 2 109 . THR . 5099 2 110 . GLY . 5099 2 111 . THR . 5099 2 112 . ASN . 5099 2 113 . LEU . 5099 2 114 . PHE . 5099 2 115 . LEU . 5099 2 116 . VAL . 5099 2 117 . ALA . 5099 2 118 . ALA . 5099 2 119 . HIS . 5099 2 120 . GLN . 5099 2 121 . ILE . 5099 2 122 . GLY . 5099 2 123 . HIS . 5099 2 124 . SER . 5099 2 125 . LEU . 5099 2 126 . GLY . 5099 2 127 . LEU . 5099 2 128 . PHE . 5099 2 129 . HIS . 5099 2 130 . SER . 5099 2 131 . ALA . 5099 2 132 . ASN . 5099 2 133 . THR . 5099 2 134 . GLU . 5099 2 135 . ALA . 5099 2 136 . LEU . 5099 2 137 . MET . 5099 2 138 . TYR . 5099 2 139 . PRO . 5099 2 140 . LEU . 5099 2 141 . TYR . 5099 2 142 . HIS . 5099 2 143 . SER . 5099 2 144 . LEU . 5099 2 145 . THR . 5099 2 146 . ASP . 5099 2 147 . LEU . 5099 2 148 . THR . 5099 2 149 . ARG . 5099 2 150 . PHE . 5099 2 151 . ARG . 5099 2 152 . LEU . 5099 2 153 . SER . 5099 2 154 . GLN . 5099 2 155 . ASP . 5099 2 156 . ASP . 5099 2 157 . ILE . 5099 2 158 . ASN . 5099 2 159 . GLY . 5099 2 160 . ILE . 5099 2 161 . GLN . 5099 2 162 . SER . 5099 2 163 . LEU . 5099 2 164 . TYR . 5099 2 165 . GLY . 5099 2 166 . PRO . 5099 2 167 . PRO . 5099 2 168 . PRO . 5099 2 169 . ASP . 5099 2 170 . SER . 5099 2 171 . PRO . 5099 2 172 . GLU . 5099 2 173 . THR . 5099 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 . PHE 1 1 5099 2 . ARG 2 2 5099 2 . THR 3 3 5099 2 . PHE 4 4 5099 2 . PRO 5 5 5099 2 . GLY 6 6 5099 2 . ILE 7 7 5099 2 . PRO 8 8 5099 2 . LYS 9 9 5099 2 . TRP 10 10 5099 2 . ARG 11 11 5099 2 . LYS 12 12 5099 2 . THR 13 13 5099 2 . HIS 14 14 5099 2 . LEU 15 15 5099 2 . THR 16 16 5099 2 . TYR 17 17 5099 2 . ARG 18 18 5099 2 . ILE 19 19 5099 2 . VAL 20 20 5099 2 . ASN 21 21 5099 2 . TYR 22 22 5099 2 . THR 23 23 5099 2 . PRO 24 24 5099 2 . ASP 25 25 5099 2 . LEU 26 26 5099 2 . PRO 27 27 5099 2 . LYS 28 28 5099 2 . ASP 29 29 5099 2 . ALA 30 30 5099 2 . VAL 31 31 5099 2 . ASP 32 32 5099 2 . SER 33 33 5099 2 . ALA 34 34 5099 2 . VAL 35 35 5099 2 . GLU 36 36 5099 2 . LYS 37 37 5099 2 . ALA 38 38 5099 2 . LEU 39 39 5099 2 . LYS 40 40 5099 2 . VAL 41 41 5099 2 . TRP 42 42 5099 2 . GLU 43 43 5099 2 . GLU 44 44 5099 2 . VAL 45 45 5099 2 . THR 46 46 5099 2 . PRO 47 47 5099 2 . LEU 48 48 5099 2 . THR 49 49 5099 2 . PHE 50 50 5099 2 . SER 51 51 5099 2 . ARG 52 52 5099 2 . LEU 53 53 5099 2 . TYR 54 54 5099 2 . GLU 55 55 5099 2 . GLY 56 56 5099 2 . GLU 57 57 5099 2 . ALA 58 58 5099 2 . ASP 59 59 5099 2 . ILE 60 60 5099 2 . MET 61 61 5099 2 . ILE 62 62 5099 2 . SER 63 63 5099 2 . PHE 64 64 5099 2 . ALA 65 65 5099 2 . VAL 66 66 5099 2 . ARG 67 67 5099 2 . GLU 68 68 5099 2 . HIS 69 69 5099 2 . GLY 70 70 5099 2 . ASP 71 71 5099 2 . PHE 72 72 5099 2 . TYR 73 73 5099 2 . PRO 74 74 5099 2 . PHE 75 75 5099 2 . ASP 76 76 5099 2 . GLY 77 77 5099 2 . PRO 78 78 5099 2 . GLY 79 79 5099 2 . ASN 80 80 5099 2 . VAL 81 81 5099 2 . LEU 82 82 5099 2 . ALA 83 83 5099 2 . HIS 84 84 5099 2 . ALA 85 85 5099 2 . TYR 86 86 5099 2 . ALA 87 87 5099 2 . PRO 88 88 5099 2 . GLY 89 89 5099 2 . PRO 90 90 5099 2 . GLY 91 91 5099 2 . ILE 92 92 5099 2 . ASN 93 93 5099 2 . GLY 94 94 5099 2 . ASP 95 95 5099 2 . ALA 96 96 5099 2 . HIS 97 97 5099 2 . PHE 98 98 5099 2 . ASP 99 99 5099 2 . ASP 100 100 5099 2 . ASP 101 101 5099 2 . GLU 102 102 5099 2 . GLN 103 103 5099 2 . TRP 104 104 5099 2 . THR 105 105 5099 2 . LYS 106 106 5099 2 . ASP 107 107 5099 2 . THR 108 108 5099 2 . THR 109 109 5099 2 . GLY 110 110 5099 2 . THR 111 111 5099 2 . ASN 112 112 5099 2 . LEU 113 113 5099 2 . PHE 114 114 5099 2 . LEU 115 115 5099 2 . VAL 116 116 5099 2 . ALA 117 117 5099 2 . ALA 118 118 5099 2 . HIS 119 119 5099 2 . GLN 120 120 5099 2 . ILE 121 121 5099 2 . GLY 122 122 5099 2 . HIS 123 123 5099 2 . SER 124 124 5099 2 . LEU 125 125 5099 2 . GLY 126 126 5099 2 . LEU 127 127 5099 2 . PHE 128 128 5099 2 . HIS 129 129 5099 2 . SER 130 130 5099 2 . ALA 131 131 5099 2 . ASN 132 132 5099 2 . THR 133 133 5099 2 . GLU 134 134 5099 2 . ALA 135 135 5099 2 . LEU 136 136 5099 2 . MET 137 137 5099 2 . TYR 138 138 5099 2 . PRO 139 139 5099 2 . LEU 140 140 5099 2 . TYR 141 141 5099 2 . HIS 142 142 5099 2 . SER 143 143 5099 2 . LEU 144 144 5099 2 . THR 145 145 5099 2 . ASP 146 146 5099 2 . LEU 147 147 5099 2 . THR 148 148 5099 2 . ARG 149 149 5099 2 . PHE 150 150 5099 2 . ARG 151 151 5099 2 . LEU 152 152 5099 2 . SER 153 153 5099 2 . GLN 154 154 5099 2 . ASP 155 155 5099 2 . ASP 156 156 5099 2 . ILE 157 157 5099 2 . ASN 158 158 5099 2 . GLY 159 159 5099 2 . ILE 160 160 5099 2 . GLN 161 161 5099 2 . SER 162 162 5099 2 . LEU 163 163 5099 2 . TYR 164 164 5099 2 . GLY 165 165 5099 2 . PRO 166 166 5099 2 . PRO 167 167 5099 2 . PRO 168 168 5099 2 . ASP 169 169 5099 2 . SER 170 170 5099 2 . PRO 171 171 5099 2 . GLU 172 172 5099 2 . THR 173 173 5099 2 stop_ save_ save_CA _Entity.Sf_category entity _Entity.Sf_framecode CA _Entity.Entry_ID 5099 _Entity.ID 3 _Entity.BMRB_code . _Entity.Name CA _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 no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID CA _Entity.Nonpolymer_comp_label $chem_comp_CA _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 3 _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_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 . CA . 5099 3 stop_ save_ save_ZN _Entity.Sf_category entity _Entity.Sf_framecode ZN _Entity.Entry_ID 5099 _Entity.ID 4 _Entity.BMRB_code . _Entity.Name ZN _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 no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID ZN _Entity.Nonpolymer_comp_label $chem_comp_ZN _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 4 _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_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 . ZN . 5099 4 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 5099 _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 $N-TIMP-1 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 5099 1 2 2 $MMP-3 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 5099 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 5099 _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 $N-TIMP-1 . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli 'BL21 (DE3)' . . . . . . . . . . . . 'T7 expression' . . pET3a . . . . . . 5099 1 2 2 $MMP-3 . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli 'BL21 (DE3)' . . . . . . . . . . . . 'T7 expression' . . pET3a . . . . . . 5099 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_CA _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_CA _Chem_comp.Entry_ID 5099 _Chem_comp.ID CA _Chem_comp.Provenance . _Chem_comp.Name 'CALCIUM ION' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code CA _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2011-06-04 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code CA _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 2 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula Ca _Chem_comp.Formula_weight 40.078 _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 no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jun 13 13:55:41 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID [Ca+2] SMILES ACDLabs 10.04 5099 CA [Ca++] SMILES_CANONICAL CACTVS 3.341 5099 CA [Ca++] SMILES CACTVS 3.341 5099 CA [Ca+2] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 5099 CA [Ca+2] SMILES 'OpenEye OEToolkits' 1.5.0 5099 CA InChI=1S/Ca/q+2 InChI InChI 1.03 5099 CA BHPQYMZQTOCNFJ-UHFFFAOYSA-N InChIKey InChI 1.03 5099 CA stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID calcium 'SYSTEMATIC NAME' ACDLabs 10.04 5099 CA 'calcium(+2) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 5099 CA 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 CA . CA . . CA . . N 2 . . . . no no . . . . 0.000 . 0.000 . 0.000 . 0.000 0.000 0.000 1 . 5099 CA stop_ save_ save_chem_comp_ZN _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_ZN _Chem_comp.Entry_ID 5099 _Chem_comp.ID ZN _Chem_comp.Provenance . _Chem_comp.Name 'ZINC ION' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code ZN _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2011-06-04 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code ZN _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 2 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula Zn _Chem_comp.Formula_weight 65.409 _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 no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jun 13 14:00:03 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID [Zn+2] SMILES ACDLabs 10.04 5099 ZN [Zn++] SMILES_CANONICAL CACTVS 3.341 5099 ZN [Zn++] SMILES CACTVS 3.341 5099 ZN [Zn+2] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 5099 ZN [Zn+2] SMILES 'OpenEye OEToolkits' 1.5.0 5099 ZN InChI=1S/Zn/q+2 InChI InChI 1.03 5099 ZN PTFCDOFLOPIGGS-UHFFFAOYSA-N InChIKey InChI 1.03 5099 ZN stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID zinc 'SYSTEMATIC NAME' ACDLabs 10.04 5099 ZN 'zinc(+2) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 5099 ZN 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 ZN . ZN . . ZN . . N 2 . . . . no no . . . . 0.000 . 0.000 . 0.000 . 0.000 0.000 0.000 1 . 5099 ZN stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5099 _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 'N-terminus of Tissue Inhibitor of Metalloproteinases-1/Matrix MetalloProteinases-3(catalytic domain) complex' '[U-13C; U-15N]' . . 1 $N-TIMP-1 . . 0.66 . . mM . . . . 5099 1 2 'Metalloproteinases-1/Matrix MetalloProteinase-3(catalytic domain, residue 83-255)' . . . 2 $MMP-3 . . 0.66 . . mM . . . . 5099 1 3 Tris [U-2H] . . . . . . 20 . . mM . . . . 5099 1 4 NaCl . . . . . . . 125 . . mM . . . . 5099 1 5 CaCl2 . . . . . . . 10 . . mM . . . . 5099 1 6 NaN3 . . . . . . . 1 . . mM . . . . 5099 1 7 ZnCl2 . . . . . . . 50 . . uM . . . . 5099 1 8 D2O . . . . . . . 7 . . % . . . . 5099 1 9 H2O . . . . . . . 93 . . % . . . . 5099 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 5099 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'N-terminus of Tissue Inhibitor of Metalloproteinases-1/Matrix MetalloProteinases-3(catalytic domain) complex' '[U-50% 2H; U-13C; U-15N]' . . 1 $N-TIMP-1 . . 0.52 . . mM . . . . 5099 2 2 'Metalloproteinases-1/Matrix MetalloProteinase-3(catalytic domain, residue 83-255)' . . . 2 $MMP-3 . . 0.52 . . mM . . . . 5099 2 3 Tris [U-2H] . . . . . . 20 . . mM . . . . 5099 2 4 NaCl . . . . . . . 125 . . mM . . . . 5099 2 5 CaCl2 . . . . . . . 10 . . mM . . . . 5099 2 6 NaN3 . . . . . . . 1 . . mM . . . . 5099 2 7 ZnCl2 . . . . . . . 50 . . uM . . . . 5099 2 8 D2O . . . . . . . 7 . . % . . . . 5099 2 9 H2O . . . . . . . 93 . . % . . . . 5099 2 stop_ save_ save_sample_3 _Sample.Sf_category sample _Sample.Sf_framecode sample_3 _Sample.Entry_ID 5099 _Sample.ID 3 _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 'N-terminus of Tissue Inhibitor of Metalloproteinases-1/Matrix MetalloProteinases-3(catalytic domain) complex' '[U-2H; U-13C; U-15N]' . . 1 $N-TIMP-1 . . 0.30 . . mM . . . . 5099 3 2 'Metalloproteinases-1/Matrix MetalloProteinase-3(catalytic domain, residue 83-255)' . . . 2 $MMP-3 . . 0.30 . . mM . . . . 5099 3 3 Tris [U-2H] . . . . . . 20 . . mM . . . . 5099 3 4 NaCl . . . . . . . 125 . . mM . . . . 5099 3 5 CaCl2 . . . . . . . 10 . . mM . . . . 5099 3 6 NaN3 . . . . . . . 1 . . mM . . . . 5099 3 7 ZnCl2 . . . . . . . 50 . . uM . . . . 5099 3 8 D2O . . . . . . . 7 . . % . . . . 5099 3 9 H2O . . . . . . . 93 . . % . . . . 5099 3 stop_ save_ ####################### # Sample conditions # ####################### save_EX-COND-1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode EX-COND-1 _Sample_condition_list.Entry_ID 5099 _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 6.22 0.05 n/a 5099 1 temperature 307 0.5 K 5099 1 'ionic strength' 0.186 0.02 M 5099 1 stop_ save_ ############################ # Computer software used # ############################ save_SYBYL_TRIAD _Software.Sf_category software _Software.Sf_framecode SYBYL_TRIAD _Software.Entry_ID 5099 _Software.ID 1 _Software.Name 'SYBYL TRIAD' _Software.Version '6.2, 6.3, 6.6' _Software.Details ; At times, use of NMRPIPE software for an intermediate data conversion was necessary before processing with Sybyl. ; loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'process NMR spectra' 5099 1 'interpret NMR spectra' 5099 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 5099 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 5099 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_3 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_3 _NMR_spectrometer.Entry_ID 5099 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model Inova _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_4 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_4 _NMR_spectrometer.Entry_ID 5099 _NMR_spectrometer.ID 4 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model UnityPlus _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 720 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5099 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer_1 Bruker DRX . 750 . . . 5099 1 2 NMR_spectrometer_2 Bruker DRX . 500 . . . 5099 1 3 NMR_spectrometer_3 Varian Inova . 600 . . . 5099 1 4 NMR_spectrometer_4 Varian UnityPlus . 720 . . . 5099 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 5099 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 15N HSQC' . . . . . . . . . . . . . . . . 1 $EX-COND-1 . . . . . . . . . . . . . . . . . . . . . 5099 1 2 '3D HNCA' . . . . . . . . . . . . . . . . 1 $EX-COND-1 . . . . . . . . . . . . . . . . . . . . . 5099 1 3 '3D HN(CO)CA' . . . . . . . . . . . . . . . . 1 $EX-COND-1 . . . . . . . . . . . . . . . . . . . . . 5099 1 4 '3D HNCO' . . . . . . . . . . . . . . . . 1 $EX-COND-1 . . . . . . . . . . . . . . . . . . . . . 5099 1 5 '3D TROSY-HNCA' . . . . . . . . . . . . . . . . 1 $EX-COND-1 . . . . . . . . . . . . . . . . . . . . . 5099 1 6 NOESY-HSQC . . . . . . . . . . . . . . . . 1 $EX-COND-1 . . . . . . . . . . . . . . . . . . . . . 5099 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 5099 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '2D 15N HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID 1 _NMR_spec_expt.Software_label $SYBYL_TRIAD _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 5099 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '3D HNCA' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID 1 _NMR_spec_expt.Software_label $SYBYL_TRIAD _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 5099 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name '3D HN(CO)CA' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID 1 _NMR_spec_expt.Software_label $SYBYL_TRIAD _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 5099 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name '3D HNCO' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID 1 _NMR_spec_expt.Software_label $SYBYL_TRIAD _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 5099 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name '3D TROSY-HNCA' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID 1 _NMR_spec_expt.Software_label $SYBYL_TRIAD _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 5099 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name NOESY-HSQC _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID 1 _NMR_spec_expt.Software_label $SYBYL_TRIAD _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 5099 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 5099 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5099 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5099 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_timpcpxshifts08022001 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode timpcpxshifts08022001 _Assigned_chem_shift_list.Entry_ID 5099 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $EX-COND-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 . 5099 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 CYS C C 13 177.1 0.12 . 1 . . . . . . . . 5099 1 2 . 1 1 1 1 CYS HB2 H 1 2.94 0.01 . 2 . . . . . . . . 5099 1 3 . 1 1 2 2 THR H H 1 7.83 0.01 . 1 . . . . . . . . 5099 1 4 . 1 1 2 2 THR HG21 H 1 1.16 0.01 . 1 . . . . . . . . 5099 1 5 . 1 1 2 2 THR HG22 H 1 1.16 0.01 . 1 . . . . . . . . 5099 1 6 . 1 1 2 2 THR HG23 H 1 1.16 0.01 . 1 . . . . . . . . 5099 1 7 . 1 1 2 2 THR C C 13 176.18 0.12 . 1 . . . . . . . . 5099 1 8 . 1 1 2 2 THR CA C 13 62.68 0.12 . 1 . . . . . . . . 5099 1 9 . 1 1 2 2 THR N N 15 128.39 0.12 . 1 . . . . . . . . 5099 1 10 . 1 1 3 3 CYS H H 1 8.85 0.01 . 1 . . . . . . . . 5099 1 11 . 1 1 3 3 CYS HA H 1 4.95 0.01 . 1 . . . . . . . . 5099 1 12 . 1 1 3 3 CYS HB2 H 1 3.46 0.01 . 2 . . . . . . . . 5099 1 13 . 1 1 3 3 CYS C C 13 176.17 0.12 . 1 . . . . . . . . 5099 1 14 . 1 1 3 3 CYS CA C 13 52.71 0.12 . 1 . . . . . . . . 5099 1 15 . 1 1 3 3 CYS N N 15 124.99 0.12 . 1 . . . . . . . . 5099 1 16 . 1 1 4 4 VAL H H 1 8.29 0.01 . 1 . . . . . . . . 5099 1 17 . 1 1 4 4 VAL HB H 1 1.94 0.01 . 1 . . . . . . . . 5099 1 18 . 1 1 4 4 VAL HG11 H 1 1.10 0.01 . 1 . . . . . . . . 5099 1 19 . 1 1 4 4 VAL HG12 H 1 1.10 0.01 . 1 . . . . . . . . 5099 1 20 . 1 1 4 4 VAL HG13 H 1 1.10 0.01 . 1 . . . . . . . . 5099 1 21 . 1 1 4 4 VAL CA C 13 62.46 0.12 . 1 . . . . . . . . 5099 1 22 . 1 1 4 4 VAL N N 15 124.61 0.12 . 1 . . . . . . . . 5099 1 23 . 1 1 6 6 PRO HA H 1 4.32 0.01 . 1 . . . . . . . . 5099 1 24 . 1 1 6 6 PRO CA C 13 59.03 0.12 . 1 . . . . . . . . 5099 1 25 . 1 1 7 7 HIS H H 1 8.31 0.01 . 1 . . . . . . . . 5099 1 26 . 1 1 7 7 HIS CA C 13 55.43 0.12 . 1 . . . . . . . . 5099 1 27 . 1 1 7 7 HIS N N 15 120.48 0.12 . 1 . . . . . . . . 5099 1 28 . 1 1 8 8 PRO C C 13 176.58 0.12 . 1 . . . . . . . . 5099 1 29 . 1 1 8 8 PRO CA C 13 66.39 0.12 . 1 . . . . . . . . 5099 1 30 . 1 1 9 9 GLN H H 1 8.38 0.01 . 1 . . . . . . . . 5099 1 31 . 1 1 9 9 GLN HB2 H 1 2.55 0.01 . 9 . . . . . . . . 5099 1 32 . 1 1 9 9 GLN HB3 H 1 2.15 0.01 . 9 . . . . . . . . 5099 1 33 . 1 1 9 9 GLN HG2 H 1 1.90 0.01 . 2 . . . . . . . . 5099 1 34 . 1 1 9 9 GLN HG3 H 1 1.65 0.01 . 2 . . . . . . . . 5099 1 35 . 1 1 9 9 GLN C C 13 178.29 0.12 . 1 . . . . . . . . 5099 1 36 . 1 1 9 9 GLN CA C 13 59.19 0.12 . 1 . . . . . . . . 5099 1 37 . 1 1 9 9 GLN CG C 13 33.87 0.12 . 1 . . . . . . . . 5099 1 38 . 1 1 9 9 GLN N N 15 117.68 0.12 . 1 . . . . . . . . 5099 1 39 . 1 1 10 10 THR H H 1 7.17 0.12 . 1 . . . . . . . . 5099 1 40 . 1 1 10 10 THR HA H 1 3.66 0.01 . 1 . . . . . . . . 5099 1 41 . 1 1 10 10 THR HB H 1 4.07 0.01 . 1 . . . . . . . . 5099 1 42 . 1 1 10 10 THR HG21 H 1 1.02 0.01 . 1 . . . . . . . . 5099 1 43 . 1 1 10 10 THR HG22 H 1 1.02 0.01 . 1 . . . . . . . . 5099 1 44 . 1 1 10 10 THR HG23 H 1 1.02 0.01 . 1 . . . . . . . . 5099 1 45 . 1 1 10 10 THR C C 13 176.92 0.12 . 1 . . . . . . . . 5099 1 46 . 1 1 10 10 THR CA C 13 65.78 0.12 . 1 . . . . . . . . 5099 1 47 . 1 1 10 10 THR CB C 13 63.98 0.12 . 9 . . . . . . . . 5099 1 48 . 1 1 10 10 THR CG2 C 13 22.48 0.12 . 1 . . . . . . . . 5099 1 49 . 1 1 10 10 THR N N 15 115.01 0.12 . 1 . . . . . . . . 5099 1 50 . 1 1 11 11 ALA H H 1 8.72 0.01 . 1 . . . . . . . . 5099 1 51 . 1 1 11 11 ALA HA H 1 3.89 0.01 . 1 . . . . . . . . 5099 1 52 . 1 1 11 11 ALA HB1 H 1 1.32 0.01 . 1 . . . . . . . . 5099 1 53 . 1 1 11 11 ALA HB2 H 1 1.32 0.01 . 1 . . . . . . . . 5099 1 54 . 1 1 11 11 ALA HB3 H 1 1.32 0.01 . 1 . . . . . . . . 5099 1 55 . 1 1 11 11 ALA C C 13 180.89 0.12 . 1 . . . . . . . . 5099 1 56 . 1 1 11 11 ALA CA C 13 55.21 0.12 . 1 . . . . . . . . 5099 1 57 . 1 1 11 11 ALA CB C 13 19.27 0.12 . 1 . . . . . . . . 5099 1 58 . 1 1 11 11 ALA N N 15 124.11 0.12 . 1 . . . . . . . . 5099 1 59 . 1 1 12 12 PHE H H 1 8.23 0.01 . 1 . . . . . . . . 5099 1 60 . 1 1 12 12 PHE C C 13 177.04 0.12 . 1 . . . . . . . . 5099 1 61 . 1 1 12 12 PHE CA C 13 62.62 0.12 . 1 . . . . . . . . 5099 1 62 . 1 1 12 12 PHE N N 15 119.9 0.12 . 1 . . . . . . . . 5099 1 63 . 1 1 13 13 CYS H H 1 7.92 0.01 . 1 . . . . . . . . 5099 1 64 . 1 1 13 13 CYS HA H 1 4.26 0.01 . 1 . . . . . . . . 5099 1 65 . 1 1 13 13 CYS HB2 H 1 3.17 0.01 . 2 . . . . . . . . 5099 1 66 . 1 1 13 13 CYS HB3 H 1 2.66 0.01 . 2 . . . . . . . . 5099 1 67 . 1 1 13 13 CYS C C 13 176.43 0.12 . 1 . . . . . . . . 5099 1 68 . 1 1 13 13 CYS CA C 13 56.93 0.12 . 1 . . . . . . . . 5099 1 69 . 1 1 13 13 CYS CB C 13 37.04 0.12 . 1 . . . . . . . . 5099 1 70 . 1 1 13 13 CYS N N 15 114.57 0.12 . 1 . . . . . . . . 5099 1 71 . 1 1 14 14 ASN H H 1 8.27 0.12 . 1 . . . . . . . . 5099 1 72 . 1 1 14 14 ASN HA H 1 4.54 0.12 . 1 . . . . . . . . 5099 1 73 . 1 1 14 14 ASN HB2 H 1 2.67 0.01 . 2 . . . . . . . . 5099 1 74 . 1 1 14 14 ASN HB3 H 1 2.62 0.01 . 2 . . . . . . . . 5099 1 75 . 1 1 14 14 ASN C C 13 175.82 0.12 . 1 . . . . . . . . 5099 1 76 . 1 1 14 14 ASN CA C 13 54.24 0.12 . 1 . . . . . . . . 5099 1 77 . 1 1 14 14 ASN N N 15 116.21 0.12 . 1 . . . . . . . . 5099 1 78 . 1 1 15 15 SER H H 1 7.21 0.01 . 1 . . . . . . . . 5099 1 79 . 1 1 15 15 SER C C 13 172.4 0.01 . 1 . . . . . . . . 5099 1 80 . 1 1 15 15 SER CA C 13 60.04 0.12 . 1 . . . . . . . . 5099 1 81 . 1 1 15 15 SER N N 15 116.23 0.12 . 1 . . . . . . . . 5099 1 82 . 1 1 16 16 ASP H H 1 8.06 0.01 . 1 . . . . . . . . 5099 1 83 . 1 1 16 16 ASP HA H 1 4.5 0.01 . 1 . . . . . . . . 5099 1 84 . 1 1 16 16 ASP HB2 H 1 2.27 0.01 . 2 . . . . . . . . 5099 1 85 . 1 1 16 16 ASP HB3 H 1 2.51 0.01 . 2 . . . . . . . . 5099 1 86 . 1 1 16 16 ASP C C 13 175.47 0.12 . 1 . . . . . . . . 5099 1 87 . 1 1 16 16 ASP CA C 13 56.61 0.12 . 1 . . . . . . . . 5099 1 88 . 1 1 16 16 ASP CB C 13 43.4 0.12 . 1 . . . . . . . . 5099 1 89 . 1 1 16 16 ASP N N 15 120.1 0.12 . 1 . . . . . . . . 5099 1 90 . 1 1 17 17 LEU H H 1 7.41 0.01 . 1 . . . . . . . . 5099 1 91 . 1 1 17 17 LEU HA H 1 4.57 0.01 . 1 . . . . . . . . 5099 1 92 . 1 1 17 17 LEU HB2 H 1 1.15 0.01 . 2 . . . . . . . . 5099 1 93 . 1 1 17 17 LEU HG H 1 1.44 0.01 . 1 . . . . . . . . 5099 1 94 . 1 1 17 17 LEU HD11 H 1 0.7 0.01 . 2 . . . . . . . . 5099 1 95 . 1 1 17 17 LEU HD12 H 1 0.7 0.01 . 2 . . . . . . . . 5099 1 96 . 1 1 17 17 LEU HD13 H 1 0.7 0.01 . 2 . . . . . . . . 5099 1 97 . 1 1 17 17 LEU C C 13 175.47 0.12 . 1 . . . . . . . . 5099 1 98 . 1 1 17 17 LEU CA C 13 53.77 0.12 . 1 . . . . . . . . 5099 1 99 . 1 1 17 17 LEU CB C 13 46.32 0.12 . 1 . . . . . . . . 5099 1 100 . 1 1 17 17 LEU CG C 13 28.28 0.12 . 1 . . . . . . . . 5099 1 101 . 1 1 17 17 LEU CD1 C 13 25.9 0.12 . 2 . . . . . . . . 5099 1 102 . 1 1 17 17 LEU N N 15 116.47 0.12 . 1 . . . . . . . . 5099 1 103 . 1 1 18 18 VAL H H 1 8.21 0.01 . 1 . . . . . . . . 5099 1 104 . 1 1 18 18 VAL HA H 1 5.01 0.01 . 1 . . . . . . . . 5099 1 105 . 1 1 18 18 VAL HB H 1 1.85 0.01 . 1 . . . . . . . . 5099 1 106 . 1 1 18 18 VAL HG11 H 1 0.97 0.01 . 1 . . . . . . . . 5099 1 107 . 1 1 18 18 VAL HG12 H 1 0.97 0.01 . 1 . . . . . . . . 5099 1 108 . 1 1 18 18 VAL HG13 H 1 0.97 0.01 . 1 . . . . . . . . 5099 1 109 . 1 1 18 18 VAL HG21 H 1 0.65 0.01 . 1 . . . . . . . . 5099 1 110 . 1 1 18 18 VAL HG22 H 1 0.65 0.01 . 1 . . . . . . . . 5099 1 111 . 1 1 18 18 VAL HG23 H 1 0.65 0.01 . 1 . . . . . . . . 5099 1 112 . 1 1 18 18 VAL C C 13 175.98 0.12 . 1 . . . . . . . . 5099 1 113 . 1 1 18 18 VAL CA C 13 61.94 0.12 . 1 . . . . . . . . 5099 1 114 . 1 1 18 18 VAL CB C 13 33.06 0.12 . 1 . . . . . . . . 5099 1 115 . 1 1 18 18 VAL CG1 C 13 22.71 0.12 . 1 . . . . . . . . 5099 1 116 . 1 1 18 18 VAL CG2 C 13 20.86 0.12 . 1 . . . . . . . . 5099 1 117 . 1 1 18 18 VAL N N 15 121.97 0.12 . 1 . . . . . . . . 5099 1 118 . 1 1 19 19 ILE H H 1 9.27 0.01 . 1 . . . . . . . . 5099 1 119 . 1 1 19 19 ILE HA H 1 5.02 0.01 . 1 . . . . . . . . 5099 1 120 . 1 1 19 19 ILE HB H 1 1.85 0.01 . 1 . . . . . . . . 5099 1 121 . 1 1 19 19 ILE HG21 H 1 0.73 0.01 . 1 . . . . . . . . 5099 1 122 . 1 1 19 19 ILE HG22 H 1 0.73 0.01 . 1 . . . . . . . . 5099 1 123 . 1 1 19 19 ILE HG23 H 1 0.73 0.01 . 1 . . . . . . . . 5099 1 124 . 1 1 19 19 ILE HD11 H 1 0.23 0.01 . 1 . . . . . . . . 5099 1 125 . 1 1 19 19 ILE HD12 H 1 0.23 0.01 . 1 . . . . . . . . 5099 1 126 . 1 1 19 19 ILE HD13 H 1 0.23 0.01 . 1 . . . . . . . . 5099 1 127 . 1 1 19 19 ILE C C 13 173.50 0.12 . 1 . . . . . . . . 5099 1 128 . 1 1 19 19 ILE CA C 13 59.21 0.12 . 1 . . . . . . . . 5099 1 129 . 1 1 19 19 ILE CB C 13 42.34 0.12 . 1 . . . . . . . . 5099 1 130 . 1 1 19 19 ILE CG2 C 13 18.74 0.12 . 1 . . . . . . . . 5099 1 131 . 1 1 19 19 ILE CD1 C 13 14.01 0.12 . 1 . . . . . . . . 5099 1 132 . 1 1 19 19 ILE N N 15 121.85 0.12 . 1 . . . . . . . . 5099 1 133 . 1 1 20 20 ARG H H 1 8.87 0.01 . 1 . . . . . . . . 5099 1 134 . 1 1 20 20 ARG HA H 1 5.42 0.01 . 1 . . . . . . . . 5099 1 135 . 1 1 20 20 ARG HB2 H 1 0.99 0.01 . 2 . . . . . . . . 5099 1 136 . 1 1 20 20 ARG HB3 H 1 1.55 0.01 . 2 . . . . . . . . 5099 1 137 . 1 1 20 20 ARG HG2 H 1 1.02 0.01 . 2 . . . . . . . . 5099 1 138 . 1 1 20 20 ARG HD2 H 1 1.40 0.01 . 2 . . . . . . . . 5099 1 139 . 1 1 20 20 ARG HD3 H 1 1.66 0.01 . 2 . . . . . . . . 5099 1 140 . 1 1 20 20 ARG C C 13 176.4 0.12 . 1 . . . . . . . . 5099 1 141 . 1 1 20 20 ARG CA C 13 54.53 0.12 . 1 . . . . . . . . 5099 1 142 . 1 1 20 20 ARG CB C 13 33.85 0.12 . 1 . . . . . . . . 5099 1 143 . 1 1 20 20 ARG CG C 13 26.43 0.12 . 1 . . . . . . . . 5099 1 144 . 1 1 20 20 ARG CD C 13 43.93 0.12 . 1 . . . . . . . . 5099 1 145 . 1 1 20 20 ARG N N 15 121.59 0.12 . 1 . . . . . . . . 5099 1 146 . 1 1 21 21 ALA H H 1 9.49 0.01 . 1 . . . . . . . . 5099 1 147 . 1 1 21 21 ALA HA H 1 4.96 0.01 . 1 . . . . . . . . 5099 1 148 . 1 1 21 21 ALA HB1 H 1 0.73 0.01 . 1 . . . . . . . . 5099 1 149 . 1 1 21 21 ALA HB2 H 1 0.73 0.01 . 1 . . . . . . . . 5099 1 150 . 1 1 21 21 ALA HB3 H 1 0.73 0.01 . 1 . . . . . . . . 5099 1 151 . 1 1 21 21 ALA C C 13 175.74 0.12 . 1 . . . . . . . . 5099 1 152 . 1 1 21 21 ALA CA C 13 51.56 0.12 . 1 . . . . . . . . 5099 1 153 . 1 1 21 21 ALA CB C 13 24.3 0.12 . 1 . . . . . . . . 5099 1 154 . 1 1 21 21 ALA N N 15 124.83 0.12 . 1 . . . . . . . . 5099 1 155 . 1 1 22 22 LYS H H 1 8.32 0.01 . 1 . . . . . . . . 5099 1 156 . 1 1 22 22 LYS HA H 1 4.79 0.01 . 1 . . . . . . . . 5099 1 157 . 1 1 22 22 LYS HB2 H 1 1.19 0.01 . 2 . . . . . . . . 5099 1 158 . 1 1 22 22 LYS HG2 H 1 1.09 0.01 . 2 . . . . . . . . 5099 1 159 . 1 1 22 22 LYS HD2 H 1 1.71 0.01 . 9 . . . . . . . . 5099 1 160 . 1 1 22 22 LYS HE2 H 1 2.62 0.01 . 2 . . . . . . . . 5099 1 161 . 1 1 22 22 LYS HE3 H 1 2.67 0.01 . 2 . . . . . . . . 5099 1 162 . 1 1 22 22 LYS C C 13 176.41 0.12 . 1 . . . . . . . . 5099 1 163 . 1 1 22 22 LYS CA C 13 55.24 0.12 . 1 . . . . . . . . 5099 1 164 . 1 1 22 22 LYS CB C 13 34.91 0.12 . 1 . . . . . . . . 5099 1 165 . 1 1 22 22 LYS CG C 13 25.9 0.12 . 1 . . . . . . . . 5099 1 166 . 1 1 22 22 LYS N N 15 119.18 0.12 . 1 . . . . . . . . 5099 1 167 . 1 1 23 23 PHE H H 1 9.56 0.01 . 1 . . . . . . . . 5099 1 168 . 1 1 23 23 PHE HA H 1 4.18 0.01 . 1 . . . . . . . . 5099 1 169 . 1 1 23 23 PHE HB2 H 1 2.40 0.01 . 2 . . . . . . . . 5099 1 170 . 1 1 23 23 PHE C C 13 176.68 0.01 . 1 . . . . . . . . 5099 1 171 . 1 1 23 23 PHE CA C 13 58.78 0.12 . 1 . . . . . . . . 5099 1 172 . 1 1 23 23 PHE N N 15 124.86 0.12 . 1 . . . . . . . . 5099 1 173 . 1 1 24 24 VAL H H 1 7.98 0.01 . 1 . . . . . . . . 5099 1 174 . 1 1 24 24 VAL HA H 1 4.11 0.01 . 1 . . . . . . . . 5099 1 175 . 1 1 24 24 VAL HB H 1 1.83 0.01 . 1 . . . . . . . . 5099 1 176 . 1 1 24 24 VAL HG11 H 1 0.58 0.01 . 1 . . . . . . . . 5099 1 177 . 1 1 24 24 VAL HG12 H 1 0.58 0.01 . 1 . . . . . . . . 5099 1 178 . 1 1 24 24 VAL HG13 H 1 0.58 0.01 . 1 . . . . . . . . 5099 1 179 . 1 1 24 24 VAL HG21 H 1 0.35 0.01 . 1 . . . . . . . . 5099 1 180 . 1 1 24 24 VAL HG22 H 1 0.35 0.01 . 1 . . . . . . . . 5099 1 181 . 1 1 24 24 VAL HG23 H 1 0.35 0.01 . 1 . . . . . . . . 5099 1 182 . 1 1 24 24 VAL C C 13 176.10 0.12 . 1 . . . . . . . . 5099 1 183 . 1 1 24 24 VAL CA C 13 62.28 0.12 . 1 . . . . . . . . 5099 1 184 . 1 1 24 24 VAL CB C 13 32.79 0.12 . 1 . . . . . . . . 5099 1 185 . 1 1 24 24 VAL CG1 C 13 21.12 0.12 . 1 . . . . . . . . 5099 1 186 . 1 1 24 24 VAL CG2 C 13 19.00 0.12 . 1 . . . . . . . . 5099 1 187 . 1 1 24 24 VAL N N 15 118.7 0.12 . 1 . . . . . . . . 5099 1 188 . 1 1 25 25 GLY H H 1 8.20 0.01 . 1 . . . . . . . . 5099 1 189 . 1 1 25 25 GLY HA2 H 1 4.19 0.01 . 2 . . . . . . . . 5099 1 190 . 1 1 25 25 GLY HA3 H 1 3.96 0.01 . 2 . . . . . . . . 5099 1 191 . 1 1 25 25 GLY C C 13 173.59 0.12 . 1 . . . . . . . . 5099 1 192 . 1 1 25 25 GLY CA C 13 45.57 0.12 . 1 . . . . . . . . 5099 1 193 . 1 1 25 25 GLY N N 15 109.84 0.12 . 1 . . . . . . . . 5099 1 194 . 1 1 26 26 THR H H 1 8.31 0.01 . 1 . . . . . . . . 5099 1 195 . 1 1 26 26 THR HA H 1 4.47 0.01 . 1 . . . . . . . . 5099 1 196 . 1 1 26 26 THR HB H 1 4.10 0.01 . 1 . . . . . . . . 5099 1 197 . 1 1 26 26 THR HG21 H 1 1.1 0.01 . 1 . . . . . . . . 5099 1 198 . 1 1 26 26 THR HG22 H 1 1.1 0.01 . 1 . . . . . . . . 5099 1 199 . 1 1 26 26 THR HG23 H 1 1.1 0.01 . 1 . . . . . . . . 5099 1 200 . 1 1 26 26 THR CA C 13 60.04 0.12 . 1 . . . . . . . . 5099 1 201 . 1 1 26 26 THR CB C 13 69.13 0.12 . 1 . . . . . . . . 5099 1 202 . 1 1 26 26 THR CG2 C 13 21.12 0.12 . 1 . . . . . . . . 5099 1 203 . 1 1 26 26 THR N N 15 116.56 0.12 . 1 . . . . . . . . 5099 1 204 . 1 1 27 27 PRO HA H 1 4.13 0.01 . 1 . . . . . . . . 5099 1 205 . 1 1 27 27 PRO C C 13 176.86 0.12 . 1 . . . . . . . . 5099 1 206 . 1 1 27 27 PRO CA C 13 63.19 0.12 . 1 . . . . . . . . 5099 1 207 . 1 1 28 28 GLU H H 1 8.41 0.01 . 1 . . . . . . . . 5099 1 208 . 1 1 28 28 GLU HA H 1 4.38 0.01 . 1 . . . . . . . . 5099 1 209 . 1 1 28 28 GLU HB2 H 1 1.73 0.01 . 2 . . . . . . . . 5099 1 210 . 1 1 28 28 GLU HB3 H 1 1.67 0.01 . 2 . . . . . . . . 5099 1 211 . 1 1 28 28 GLU HG2 H 1 2.06 0.01 . 2 . . . . . . . . 5099 1 212 . 1 1 28 28 GLU HG3 H 1 1.85 0.01 . 2 . . . . . . . . 5099 1 213 . 1 1 28 28 GLU CA C 13 54.93 0.12 . 1 . . . . . . . . 5099 1 214 . 1 1 28 28 GLU CB C 13 31.75 0.12 . 1 . . . . . . . . 5099 1 215 . 1 1 28 28 GLU CG C 13 35.82 0.12 . 1 . . . . . . . . 5099 1 216 . 1 1 28 28 GLU N N 15 121.59 0.12 . 1 . . . . . . . . 5099 1 217 . 1 1 29 29 VAL H H 1 8.85 0.01 . 1 . . . . . . . . 5099 1 218 . 1 1 29 29 VAL C C 13 172.99 0.12 . 1 . . . . . . . . 5099 1 219 . 1 1 29 29 VAL N N 15 127.76 0.12 . 1 . . . . . . . . 5099 1 220 . 1 1 30 30 ASN H H 1 8.69 0.01 . 1 . . . . . . . . 5099 1 221 . 1 1 30 30 ASN HA H 1 4.73 0.01 . 1 . . . . . . . . 5099 1 222 . 1 1 30 30 ASN HB2 H 1 2.58 0.01 . 9 . . . . . . . . 5099 1 223 . 1 1 30 30 ASN CA C 13 52.26 0.12 . 1 . . . . . . . . 5099 1 224 . 1 1 30 30 ASN N N 15 128.89 0.12 . 1 . . . . . . . . 5099 1 225 . 1 1 31 31 GLN H H 1 9.64 0.01 . 1 . . . . . . . . 5099 1 226 . 1 1 31 31 GLN HB2 H 1 2.04 0.01 . 9 . . . . . . . . 5099 1 227 . 1 1 31 31 GLN HB3 H 1 1.81 0.01 . 2 . . . . . . . . 5099 1 228 . 1 1 31 31 GLN CB C 13 28.28 0.12 . 9 . . . . . . . . 5099 1 229 . 1 1 31 31 GLN N N 15 120.63 0.12 . 1 . . . . . . . . 5099 1 230 . 1 1 32 32 THR H H 1 8.89 0.01 . 1 . . . . . . . . 5099 1 231 . 1 1 32 32 THR CA C 13 64.95 0.12 . 1 . . . . . . . . 5099 1 232 . 1 1 32 32 THR N N 15 115.8 0.12 . 1 . . . . . . . . 5099 1 233 . 1 1 33 33 THR H H 1 7.60 0.01 . 1 . . . . . . . . 5099 1 234 . 1 1 33 33 THR N N 15 112.07 0.12 . 1 . . . . . . . . 5099 1 235 . 1 1 34 34 LEU H H 1 8.19 0.01 . 1 . . . . . . . . 5099 1 236 . 1 1 34 34 LEU N N 15 116.56 0.12 . 1 . . . . . . . . 5099 1 237 . 1 1 35 35 TYR H H 1 7.91 0.01 . 1 . . . . . . . . 5099 1 238 . 1 1 35 35 TYR C C 13 175.16 0.12 . 1 . . . . . . . . 5099 1 239 . 1 1 35 35 TYR CA C 13 58.51 0.12 . 1 . . . . . . . . 5099 1 240 . 1 1 35 35 TYR N N 15 118.83 0.12 . 1 . . . . . . . . 5099 1 241 . 1 1 36 36 GLN H H 1 9.85 0.01 . 1 . . . . . . . . 5099 1 242 . 1 1 36 36 GLN HA H 1 5.16 0.01 . 1 . . . . . . . . 5099 1 243 . 1 1 36 36 GLN C C 13 172.91 0.12 . 1 . . . . . . . . 5099 1 244 . 1 1 36 36 GLN CA C 13 52.87 0.12 . 1 . . . . . . . . 5099 1 245 . 1 1 36 36 GLN N N 15 119.96 0.12 . 1 . . . . . . . . 5099 1 246 . 1 1 37 37 ARG H H 1 8.34 0.01 . 1 . . . . . . . . 5099 1 247 . 1 1 37 37 ARG HA H 1 5.19 0.01 . 1 . . . . . . . . 5099 1 248 . 1 1 37 37 ARG HB2 H 1 0.73 0.01 . 2 . . . . . . . . 5099 1 249 . 1 1 37 37 ARG HB3 H 1 1.01 0.01 . 2 . . . . . . . . 5099 1 250 . 1 1 37 37 ARG HG2 H 1 0.63 0.01 . 2 . . . . . . . . 5099 1 251 . 1 1 37 37 ARG HG3 H 1 1.20 0.01 . 9 . . . . . . . . 5099 1 252 . 1 1 37 37 ARG HD2 H 1 1.5 0.01 . 2 . . . . . . . . 5099 1 253 . 1 1 37 37 ARG HD3 H 1 2.34 0.01 . 2 . . . . . . . . 5099 1 254 . 1 1 37 37 ARG C C 13 174.52 0.12 . 1 . . . . . . . . 5099 1 255 . 1 1 37 37 ARG CA C 13 53.26 0.12 . 1 . . . . . . . . 5099 1 256 . 1 1 37 37 ARG CD C 13 43.47 0.12 . 1 . . . . . . . . 5099 1 257 . 1 1 37 37 ARG N N 15 118.58 0.12 . 1 . . . . . . . . 5099 1 258 . 1 1 38 38 TYR H H 1 9.07 0.01 . 1 . . . . . . . . 5099 1 259 . 1 1 38 38 TYR C C 13 175.24 0.12 . 1 . . . . . . . . 5099 1 260 . 1 1 38 38 TYR CA C 13 56.9 0.12 . 1 . . . . . . . . 5099 1 261 . 1 1 38 38 TYR N N 15 122.09 0.12 . 1 . . . . . . . . 5099 1 262 . 1 1 39 39 GLU H H 1 8.93 0.01 . 1 . . . . . . . . 5099 1 263 . 1 1 39 39 GLU HA H 1 4.35 0.01 . 1 . . . . . . . . 5099 1 264 . 1 1 39 39 GLU HB2 H 1 1.68 0.01 . 2 . . . . . . . . 5099 1 265 . 1 1 39 39 GLU HB3 H 1 1.60 0.01 . 2 . . . . . . . . 5099 1 266 . 1 1 39 39 GLU HG2 H 1 1.74 0.01 . 2 . . . . . . . . 5099 1 267 . 1 1 39 39 GLU C C 13 175.91 0.12 . 1 . . . . . . . . 5099 1 268 . 1 1 39 39 GLU CA C 13 56.24 0.12 . 1 . . . . . . . . 5099 1 269 . 1 1 39 39 GLU N N 15 125.99 0.12 . 1 . . . . . . . . 5099 1 270 . 1 1 40 40 ILE H H 1 8.32 0.01 . 1 . . . . . . . . 5099 1 271 . 1 1 40 40 ILE HA H 1 4.88 0.01 . 1 . . . . . . . . 5099 1 272 . 1 1 40 40 ILE HB H 1 0.90 0.01 . 1 . . . . . . . . 5099 1 273 . 1 1 40 40 ILE HG12 H 1 0.77 0.01 . 2 . . . . . . . . 5099 1 274 . 1 1 40 40 ILE HG21 H 1 -0.36 0.01 . 1 . . . . . . . . 5099 1 275 . 1 1 40 40 ILE HG22 H 1 -0.36 0.01 . 1 . . . . . . . . 5099 1 276 . 1 1 40 40 ILE HG23 H 1 -0.36 0.01 . 1 . . . . . . . . 5099 1 277 . 1 1 40 40 ILE HD11 H 1 -0.02 0.01 . 1 . . . . . . . . 5099 1 278 . 1 1 40 40 ILE HD12 H 1 -0.02 0.01 . 1 . . . . . . . . 5099 1 279 . 1 1 40 40 ILE HD13 H 1 -0.02 0.01 . 1 . . . . . . . . 5099 1 280 . 1 1 40 40 ILE C C 13 175.04 0.12 . 1 . . . . . . . . 5099 1 281 . 1 1 40 40 ILE CA C 13 58.73 0.12 . 1 . . . . . . . . 5099 1 282 . 1 1 40 40 ILE CB C 13 43.15 0.12 . 1 . . . . . . . . 5099 1 283 . 1 1 40 40 ILE CG1 C 13 24.84 0.12 . 9 . . . . . . . . 5099 1 284 . 1 1 40 40 ILE CG2 C 13 16.88 0.12 . 1 . . . . . . . . 5099 1 285 . 1 1 40 40 ILE CD1 C 13 14.76 0.12 . 1 . . . . . . . . 5099 1 286 . 1 1 40 40 ILE N N 15 121.21 0.12 . 1 . . . . . . . . 5099 1 287 . 1 1 41 41 LYS H H 1 8.56 0.01 . 1 . . . . . . . . 5099 1 288 . 1 1 41 41 LYS C C 13 175.79 0.12 . 1 . . . . . . . . 5099 1 289 . 1 1 41 41 LYS CA C 13 54.20 0.12 . 1 . . . . . . . . 5099 1 290 . 1 1 41 41 LYS N N 15 121.21 0.12 . 1 . . . . . . . . 5099 1 291 . 1 1 42 42 MET H H 1 9.30 0.12 . 1 . . . . . . . . 5099 1 292 . 1 1 42 42 MET C C 13 176.28 0.12 . 1 . . . . . . . . 5099 1 293 . 1 1 42 42 MET CA C 13 56.92 0.12 . 1 . . . . . . . . 5099 1 294 . 1 1 42 42 MET N N 15 128.64 0.12 . 1 . . . . . . . . 5099 1 295 . 1 1 43 43 THR H H 1 9.19 0.01 . 1 . . . . . . . . 5099 1 296 . 1 1 43 43 THR HA H 1 4.14 0.01 . 1 . . . . . . . . 5099 1 297 . 1 1 43 43 THR HB H 1 3.82 0.01 . 1 . . . . . . . . 5099 1 298 . 1 1 43 43 THR HG21 H 1 0.78 0.01 . 1 . . . . . . . . 5099 1 299 . 1 1 43 43 THR HG22 H 1 0.78 0.01 . 1 . . . . . . . . 5099 1 300 . 1 1 43 43 THR HG23 H 1 0.78 0.01 . 1 . . . . . . . . 5099 1 301 . 1 1 43 43 THR C C 13 175.64 0.12 . 1 . . . . . . . . 5099 1 302 . 1 1 43 43 THR CA C 13 62.24 0.12 . 1 . . . . . . . . 5099 1 303 . 1 1 43 43 THR CB C 13 68.54 0.12 . 1 . . . . . . . . 5099 1 304 . 1 1 43 43 THR CG2 C 13 22.64 0.12 . 1 . . . . . . . . 5099 1 305 . 1 1 43 43 THR N N 15 119.96 0.12 . 1 . . . . . . . . 5099 1 306 . 1 1 44 44 LYS H H 1 7.30 0.01 . 1 . . . . . . . . 5099 1 307 . 1 1 44 44 LYS HA H 1 4.03 0.01 . 1 . . . . . . . . 5099 1 308 . 1 1 44 44 LYS HB2 H 1 1.19 0.01 . 2 . . . . . . . . 5099 1 309 . 1 1 44 44 LYS HB3 H 1 0.76 0.01 . 2 . . . . . . . . 5099 1 310 . 1 1 44 44 LYS HG2 H 1 0.55 0.01 . 2 . . . . . . . . 5099 1 311 . 1 1 44 44 LYS HG3 H 1 0.67 0.01 . 2 . . . . . . . . 5099 1 312 . 1 1 44 44 LYS HD2 H 1 1.34 0.01 . 2 . . . . . . . . 5099 1 313 . 1 1 44 44 LYS HE2 H 1 2.68 0.01 . 2 . . . . . . . . 5099 1 314 . 1 1 44 44 LYS HE3 H 1 2.60 0.01 . 2 . . . . . . . . 5099 1 315 . 1 1 44 44 LYS C C 13 173.35 0.12 . 1 . . . . . . . . 5099 1 316 . 1 1 44 44 LYS CA C 13 55.85 0.12 . 1 . . . . . . . . 5099 1 317 . 1 1 44 44 LYS CB C 13 36.15 0.12 . 1 . . . . . . . . 5099 1 318 . 1 1 44 44 LYS CG C 13 24.27 0.12 . 1 . . . . . . . . 5099 1 319 . 1 1 44 44 LYS CD C 13 28.01 0.12 . 1 . . . . . . . . 5099 1 320 . 1 1 44 44 LYS CE C 13 42.17 0.12 . 1 . . . . . . . . 5099 1 321 . 1 1 44 44 LYS N N 15 121.59 0.12 . 1 . . . . . . . . 5099 1 322 . 1 1 45 45 MET H H 1 8.60 0.01 . 1 . . . . . . . . 5099 1 323 . 1 1 45 45 MET CA C 13 55.61 0.12 . 1 . . . . . . . . 5099 1 324 . 1 1 45 45 MET N N 15 125.11 0.12 . 1 . . . . . . . . 5099 1 325 . 1 1 46 46 TYR H H 1 8.63 0.01 . 1 . . . . . . . . 5099 1 326 . 1 1 46 46 TYR HA H 1 4.88 0.01 . 1 . . . . . . . . 5099 1 327 . 1 1 46 46 TYR HB2 H 1 3.75 0.01 . 9 . . . . . . . . 5099 1 328 . 1 1 46 46 TYR C C 13 175.63 0.12 . 1 . . . . . . . . 5099 1 329 . 1 1 46 46 TYR CA C 13 58.60 0.12 . 1 . . . . . . . . 5099 1 330 . 1 1 46 46 TYR N N 15 123.58 0.12 . 1 . . . . . . . . 5099 1 331 . 1 1 47 47 LYS H H 1 7.94 0.01 . 1 . . . . . . . . 5099 1 332 . 1 1 47 47 LYS CA C 13 57.2 0.12 . 1 . . . . . . . . 5099 1 333 . 1 1 47 47 LYS N N 15 121.34 0.12 . 1 . . . . . . . . 5099 1 334 . 1 1 48 48 GLY H H 1 8.69 0.01 . 1 . . . . . . . . 5099 1 335 . 1 1 48 48 GLY C C 13 173.43 0.12 . 1 . . . . . . . . 5099 1 336 . 1 1 48 48 GLY CA C 13 45.76 0.12 . 1 . . . . . . . . 5099 1 337 . 1 1 48 48 GLY N N 15 114.29 0.12 . 1 . . . . . . . . 5099 1 338 . 1 1 49 49 PHE H H 1 7.49 0.01 . 1 . . . . . . . . 5099 1 339 . 1 1 49 49 PHE HA H 1 4.01 0.01 . 1 . . . . . . . . 5099 1 340 . 1 1 49 49 PHE HB2 H 1 2.79 0.01 . 2 . . . . . . . . 5099 1 341 . 1 1 49 49 PHE HB3 H 1 3.06 0.01 . 2 . . . . . . . . 5099 1 342 . 1 1 49 49 PHE C C 13 177.11 0.12 . 1 . . . . . . . . 5099 1 343 . 1 1 49 49 PHE CA C 13 60.07 0.12 . 1 . . . . . . . . 5099 1 344 . 1 1 49 49 PHE CB C 13 39.24 0.12 . 1 . . . . . . . . 5099 1 345 . 1 1 49 49 PHE N N 15 119.51 0.12 . 1 . . . . . . . . 5099 1 346 . 1 1 50 50 GLN H H 1 8.72 0.01 . 1 . . . . . . . . 5099 1 347 . 1 1 50 50 GLN CA C 13 57.92 0.12 . 1 . . . . . . . . 5099 1 348 . 1 1 50 50 GLN N N 15 118.14 0.12 . 1 . . . . . . . . 5099 1 349 . 1 1 51 51 ALA H H 1 7.68 0.01 . 1 . . . . . . . . 5099 1 350 . 1 1 51 51 ALA HA H 1 4.08 0.01 . 1 . . . . . . . . 5099 1 351 . 1 1 51 51 ALA HB1 H 1 1.18 0.01 . 1 . . . . . . . . 5099 1 352 . 1 1 51 51 ALA HB2 H 1 1.18 0.01 . 1 . . . . . . . . 5099 1 353 . 1 1 51 51 ALA HB3 H 1 1.18 0.01 . 1 . . . . . . . . 5099 1 354 . 1 1 51 51 ALA CA C 13 53.68 0.12 . 1 . . . . . . . . 5099 1 355 . 1 1 51 51 ALA CB C 13 19.27 0.12 . 1 . . . . . . . . 5099 1 356 . 1 1 51 51 ALA N N 15 122.47 0.12 . 1 . . . . . . . . 5099 1 357 . 1 1 52 52 LEU H H 1 7.64 0.01 . 1 . . . . . . . . 5099 1 358 . 1 1 52 52 LEU HA H 1 4.16 0.01 . 1 . . . . . . . . 5099 1 359 . 1 1 52 52 LEU HB2 H 1 1.45 0.01 . 2 . . . . . . . . 5099 1 360 . 1 1 52 52 LEU HG H 1 1.40 0.01 . 1 . . . . . . . . 5099 1 361 . 1 1 52 52 LEU HD11 H 1 0.63 0.01 . 1 . . . . . . . . 5099 1 362 . 1 1 52 52 LEU HD12 H 1 0.63 0.01 . 1 . . . . . . . . 5099 1 363 . 1 1 52 52 LEU HD13 H 1 0.63 0.01 . 1 . . . . . . . . 5099 1 364 . 1 1 52 52 LEU HD21 H 1 0.69 0.01 . 1 . . . . . . . . 5099 1 365 . 1 1 52 52 LEU HD22 H 1 0.69 0.01 . 1 . . . . . . . . 5099 1 366 . 1 1 52 52 LEU HD23 H 1 0.69 0.01 . 1 . . . . . . . . 5099 1 367 . 1 1 52 52 LEU C C 13 178.01 0.12 . 1 . . . . . . . . 5099 1 368 . 1 1 52 52 LEU CA C 13 55.35 0.12 . 1 . . . . . . . . 5099 1 369 . 1 1 52 52 LEU CB C 13 42.34 0.12 . 1 . . . . . . . . 5099 1 370 . 1 1 52 52 LEU CG C 13 26.96 0.12 . 1 . . . . . . . . 5099 1 371 . 1 1 52 52 LEU CD1 C 13 23.24 0.12 . 1 . . . . . . . . 5099 1 372 . 1 1 52 52 LEU CD2 C 13 25.37 0.12 . 1 . . . . . . . . 5099 1 373 . 1 1 52 52 LEU N N 15 116.69 0.12 . 1 . . . . . . . . 5099 1 374 . 1 1 53 53 GLY H H 1 7.90 0.01 . 1 . . . . . . . . 5099 1 375 . 1 1 53 53 GLY HA2 H 1 3.99 0.01 . 2 . . . . . . . . 5099 1 376 . 1 1 53 53 GLY HA3 H 1 3.65 0.01 . 2 . . . . . . . . 5099 1 377 . 1 1 53 53 GLY C C 13 174.22 0.12 . 1 . . . . . . . . 5099 1 378 . 1 1 53 53 GLY CA C 13 45.88 0.12 . 1 . . . . . . . . 5099 1 379 . 1 1 53 53 GLY N N 15 108.88 0.12 . 1 . . . . . . . . 5099 1 380 . 1 1 54 54 ASP H H 1 8.24 0.01 . 1 . . . . . . . . 5099 1 381 . 1 1 54 54 ASP C C 13 176.48 0.12 . 1 . . . . . . . . 5099 1 382 . 1 1 54 54 ASP CA C 13 55.29 0.12 . 1 . . . . . . . . 5099 1 383 . 1 1 54 54 ASP N N 15 120.95 0.12 . 1 . . . . . . . . 5099 1 384 . 1 1 55 55 ALA H H 1 8.09 0.01 . 1 . . . . . . . . 5099 1 385 . 1 1 55 55 ALA HA H 1 4.09 0.01 . 1 . . . . . . . . 5099 1 386 . 1 1 55 55 ALA HB1 H 1 1.18 0.01 . 1 . . . . . . . . 5099 1 387 . 1 1 55 55 ALA HB2 H 1 1.18 0.01 . 1 . . . . . . . . 5099 1 388 . 1 1 55 55 ALA HB3 H 1 1.18 0.01 . 1 . . . . . . . . 5099 1 389 . 1 1 55 55 ALA C C 13 176.98 0.12 . 1 . . . . . . . . 5099 1 390 . 1 1 55 55 ALA CA C 13 52.41 0.12 . 1 . . . . . . . . 5099 1 391 . 1 1 55 55 ALA CB C 13 19.27 0.12 . 1 . . . . . . . . 5099 1 392 . 1 1 55 55 ALA N N 15 123.86 0.12 . 1 . . . . . . . . 5099 1 393 . 1 1 56 56 ALA H H 1 7.70 0.01 . 1 . . . . . . . . 5099 1 394 . 1 1 56 56 ALA HA H 1 4.07 0.01 . 1 . . . . . . . . 5099 1 395 . 1 1 56 56 ALA HB1 H 1 1.12 0.01 . 1 . . . . . . . . 5099 1 396 . 1 1 56 56 ALA HB2 H 1 1.12 0.01 . 1 . . . . . . . . 5099 1 397 . 1 1 56 56 ALA HB3 H 1 1.12 0.01 . 1 . . . . . . . . 5099 1 398 . 1 1 56 56 ALA C C 13 176.69 0.12 . 1 . . . . . . . . 5099 1 399 . 1 1 56 56 ALA CA C 13 52.71 0.12 . 1 . . . . . . . . 5099 1 400 . 1 1 56 56 ALA CB C 13 19.27 0.12 . 1 . . . . . . . . 5099 1 401 . 1 1 56 56 ALA N N 15 121.91 0.12 . 1 . . . . . . . . 5099 1 402 . 1 1 57 57 ASP H H 1 8.01 0.01 . 1 . . . . . . . . 5099 1 403 . 1 1 57 57 ASP HA H 1 4.44 0.01 . 1 . . . . . . . . 5099 1 404 . 1 1 57 57 ASP HB2 H 1 2.51 0.01 . 2 . . . . . . . . 5099 1 405 . 1 1 57 57 ASP HB3 H 1 2.37 0.01 . 2 . . . . . . . . 5099 1 406 . 1 1 57 57 ASP C C 13 175.37 0.12 . 1 . . . . . . . . 5099 1 407 . 1 1 57 57 ASP CA C 13 54.24 0.12 . 1 . . . . . . . . 5099 1 408 . 1 1 57 57 ASP CB C 13 41.54 0.12 . 1 . . . . . . . . 5099 1 409 . 1 1 57 57 ASP N N 15 119.07 0.12 . 1 . . . . . . . . 5099 1 410 . 1 1 58 58 ILE H H 1 7.58 0.01 . 1 . . . . . . . . 5099 1 411 . 1 1 58 58 ILE HA H 1 3.97 0.01 . 1 . . . . . . . . 5099 1 412 . 1 1 58 58 ILE HB H 1 1.64 0.01 . 1 . . . . . . . . 5099 1 413 . 1 1 58 58 ILE HG12 H 1 1.19 0.01 . 2 . . . . . . . . 5099 1 414 . 1 1 58 58 ILE HG13 H 1 1.03 0.01 . 2 . . . . . . . . 5099 1 415 . 1 1 58 58 ILE HG21 H 1 0.64 0.01 . 1 . . . . . . . . 5099 1 416 . 1 1 58 58 ILE HG22 H 1 0.64 0.01 . 1 . . . . . . . . 5099 1 417 . 1 1 58 58 ILE HG23 H 1 0.64 0.01 . 1 . . . . . . . . 5099 1 418 . 1 1 58 58 ILE HD11 H 1 0.55 0.01 . 1 . . . . . . . . 5099 1 419 . 1 1 58 58 ILE HD12 H 1 0.55 0.01 . 1 . . . . . . . . 5099 1 420 . 1 1 58 58 ILE HD13 H 1 0.55 0.01 . 1 . . . . . . . . 5099 1 421 . 1 1 58 58 ILE C C 13 175.04 0.12 . 1 . . . . . . . . 5099 1 422 . 1 1 58 58 ILE CA C 13 61.21 0.12 . 1 . . . . . . . . 5099 1 423 . 1 1 58 58 ILE CB C 13 37.57 0.12 . 1 . . . . . . . . 5099 1 424 . 1 1 58 58 ILE CG1 C 13 26.96 0.12 . 1 . . . . . . . . 5099 1 425 . 1 1 58 58 ILE CG2 C 13 18.03 0.12 . 1 . . . . . . . . 5099 1 426 . 1 1 58 58 ILE N N 15 123.65 0.12 . 1 . . . . . . . . 5099 1 427 . 1 1 59 59 ARG H H 1 8.47 0.01 . 1 . . . . . . . . 5099 1 428 . 1 1 59 59 ARG HA H 1 4.13 0.01 . 1 . . . . . . . . 5099 1 429 . 1 1 59 59 ARG HB2 H 1 1.26 0.01 . 2 . . . . . . . . 5099 1 430 . 1 1 59 59 ARG HG2 H 1 1.00 0.01 . 2 . . . . . . . . 5099 1 431 . 1 1 59 59 ARG HG3 H 1 1.18 0.01 . 2 . . . . . . . . 5099 1 432 . 1 1 59 59 ARG HD2 H 1 2.86 0.01 . 2 . . . . . . . . 5099 1 433 . 1 1 59 59 ARG C C 13 174.36 0.12 . 1 . . . . . . . . 5099 1 434 . 1 1 59 59 ARG CA C 13 56.02 0.12 . 1 . . . . . . . . 5099 1 435 . 1 1 59 59 ARG CB C 13 32.57 0.12 . 1 . . . . . . . . 5099 1 436 . 1 1 59 59 ARG CG C 13 27.36 0.12 . 1 . . . . . . . . 5099 1 437 . 1 1 59 59 ARG CD C 13 43.31 0.12 . 1 . . . . . . . . 5099 1 438 . 1 1 59 59 ARG N N 15 124.87 0.12 . 1 . . . . . . . . 5099 1 439 . 1 1 60 60 PHE H H 1 7.14 0.01 . 1 . . . . . . . . 5099 1 440 . 1 1 60 60 PHE HA H 1 5.45 0.01 . 1 . . . . . . . . 5099 1 441 . 1 1 60 60 PHE HB2 H 1 2.48 0.01 . 2 . . . . . . . . 5099 1 442 . 1 1 60 60 PHE HB3 H 1 2.26 0.01 . 2 . . . . . . . . 5099 1 443 . 1 1 60 60 PHE C C 13 174.98 0.12 . 1 . . . . . . . . 5099 1 444 . 1 1 60 60 PHE CA C 13 56.21 0.12 . 1 . . . . . . . . 5099 1 445 . 1 1 60 60 PHE CB C 13 45.26 0.12 . 1 . . . . . . . . 5099 1 446 . 1 1 60 60 PHE N N 15 114.16 0.12 . 1 . . . . . . . . 5099 1 447 . 1 1 61 61 VAL H H 1 8.58 0.01 . 1 . . . . . . . . 5099 1 448 . 1 1 61 61 VAL HA H 1 4.67 0.01 . 1 . . . . . . . . 5099 1 449 . 1 1 61 61 VAL HB H 1 1.53 0.01 . 1 . . . . . . . . 5099 1 450 . 1 1 61 61 VAL HG11 H 1 0.56 0.01 . 1 . . . . . . . . 5099 1 451 . 1 1 61 61 VAL HG12 H 1 0.56 0.01 . 1 . . . . . . . . 5099 1 452 . 1 1 61 61 VAL HG13 H 1 0.56 0.01 . 1 . . . . . . . . 5099 1 453 . 1 1 61 61 VAL C C 13 173.61 0.12 . 1 . . . . . . . . 5099 1 454 . 1 1 61 61 VAL CA C 13 60.06 0.12 . 1 . . . . . . . . 5099 1 455 . 1 1 61 61 VAL CB C 13 34.65 0.12 . 1 . . . . . . . . 5099 1 456 . 1 1 61 61 VAL CG1 C 13 21.92 0.12 . 1 . . . . . . . . 5099 1 457 . 1 1 61 61 VAL N N 15 116.72 0.12 . 1 . . . . . . . . 5099 1 458 . 1 1 62 62 TYR H H 1 9.25 0.01 . 1 . . . . . . . . 5099 1 459 . 1 1 62 62 TYR HA H 1 5.06 0.01 . 1 . . . . . . . . 5099 1 460 . 1 1 62 62 TYR C C 13 175.32 0.12 . 1 . . . . . . . . 5099 1 461 . 1 1 62 62 TYR CA C 13 57.89 0.12 . 1 . . . . . . . . 5099 1 462 . 1 1 62 62 TYR N N 15 125.83 0.12 . 1 . . . . . . . . 5099 1 463 . 1 1 63 63 THR H H 1 9.04 0.01 . 1 . . . . . . . . 5099 1 464 . 1 1 63 63 THR HA H 1 5.30 0.01 . 9 . . . . . . . . 5099 1 465 . 1 1 63 63 THR HG21 H 1 1.42 0.01 . 1 . . . . . . . . 5099 1 466 . 1 1 63 63 THR HG22 H 1 1.42 0.01 . 1 . . . . . . . . 5099 1 467 . 1 1 63 63 THR HG23 H 1 1.42 0.01 . 1 . . . . . . . . 5099 1 468 . 1 1 63 63 THR CA C 13 60.06 0.12 . 1 . . . . . . . . 5099 1 469 . 1 1 63 63 THR CG2 C 13 20.06 0.12 . 1 . . . . . . . . 5099 1 470 . 1 1 63 63 THR N N 15 114.78 0.12 . 1 . . . . . . . . 5099 1 471 . 1 1 65 65 ALA HA H 1 3.74 0.01 . 1 . . . . . . . . 5099 1 472 . 1 1 65 65 ALA HB1 H 1 0.91 0.01 . 1 . . . . . . . . 5099 1 473 . 1 1 65 65 ALA HB2 H 1 0.91 0.01 . 1 . . . . . . . . 5099 1 474 . 1 1 65 65 ALA HB3 H 1 0.91 0.01 . 1 . . . . . . . . 5099 1 475 . 1 1 65 65 ALA CA C 13 53.21 0.12 . 9 . . . . . . . . 5099 1 476 . 1 1 65 65 ALA CB C 13 19.00 0.12 . 1 . . . . . . . . 5099 1 477 . 1 1 66 66 MET HB2 H 1 2.10 0.01 . 2 . . . . . . . . 5099 1 478 . 1 1 68 68 SER HA H 1 5.02 0.01 . 1 . . . . . . . . 5099 1 479 . 1 1 68 68 SER HB2 H 1 3.72 0.01 . 2 . . . . . . . . 5099 1 480 . 1 1 69 69 VAL HA H 1 4.40 0.01 . 1 . . . . . . . . 5099 1 481 . 1 1 69 69 VAL HB H 1 2.57 0.01 . 1 . . . . . . . . 5099 1 482 . 1 1 69 69 VAL HG11 H 1 0.04 0.01 . 1 . . . . . . . . 5099 1 483 . 1 1 69 69 VAL HG12 H 1 0.04 0.01 . 1 . . . . . . . . 5099 1 484 . 1 1 69 69 VAL HG13 H 1 0.04 0.01 . 1 . . . . . . . . 5099 1 485 . 1 1 69 69 VAL HG21 H 1 -0.39 0.01 . 1 . . . . . . . . 5099 1 486 . 1 1 69 69 VAL HG22 H 1 -0.39 0.01 . 1 . . . . . . . . 5099 1 487 . 1 1 69 69 VAL HG23 H 1 -0.39 0.01 . 1 . . . . . . . . 5099 1 488 . 1 1 69 69 VAL C C 13 174.05 0.12 . 1 . . . . . . . . 5099 1 489 . 1 1 70 70 CYS H H 1 7.83 0.01 . 1 . . . . . . . . 5099 1 490 . 1 1 70 70 CYS C C 13 176.43 0.12 . 1 . . . . . . . . 5099 1 491 . 1 1 70 70 CYS N N 15 109.91 0.12 . 1 . . . . . . . . 5099 1 492 . 1 1 71 71 GLY H H 1 8.15 0.01 . 1 . . . . . . . . 5099 1 493 . 1 1 71 71 GLY C C 13 172.45 0.12 . 1 . . . . . . . . 5099 1 494 . 1 1 71 71 GLY N N 15 110.41 0.12 . 1 . . . . . . . . 5099 1 495 . 1 1 72 72 TYR H H 1 8.85 0.01 . 1 . . . . . . . . 5099 1 496 . 1 1 72 72 TYR C C 13 174.19 0.12 . 1 . . . . . . . . 5099 1 497 . 1 1 72 72 TYR CA C 13 58.76 0.12 . 1 . . . . . . . . 5099 1 498 . 1 1 72 72 TYR N N 15 124.99 0.12 . 1 . . . . . . . . 5099 1 499 . 1 1 73 73 PHE H H 1 8.00 0.01 . 1 . . . . . . . . 5099 1 500 . 1 1 73 73 PHE C C 13 173.27 0.12 . 1 . . . . . . . . 5099 1 501 . 1 1 73 73 PHE CA C 13 56.86 0.12 . 1 . . . . . . . . 5099 1 502 . 1 1 73 73 PHE N N 15 130.72 0.12 . 1 . . . . . . . . 5099 1 503 . 1 1 74 74 HIS H H 1 7.28 0.01 . 1 . . . . . . . . 5099 1 504 . 1 1 74 74 HIS HA H 1 3.30 0.01 . 1 . . . . . . . . 5099 1 505 . 1 1 74 74 HIS HB2 H 1 1.67 0.01 . 2 . . . . . . . . 5099 1 506 . 1 1 74 74 HIS HB3 H 1 2.53 0.01 . 2 . . . . . . . . 5099 1 507 . 1 1 74 74 HIS C C 13 176.02 0.12 . 1 . . . . . . . . 5099 1 508 . 1 1 74 74 HIS CA C 13 56.90 0.12 . 1 . . . . . . . . 5099 1 509 . 1 1 74 74 HIS CB C 13 32.57 0.12 . 1 . . . . . . . . 5099 1 510 . 1 1 74 74 HIS N N 15 125.52 0.12 . 1 . . . . . . . . 5099 1 511 . 1 1 75 75 ARG H H 1 7.81 0.01 . 1 . . . . . . . . 5099 1 512 . 1 1 75 75 ARG HA H 1 3.98 0.01 . 1 . . . . . . . . 5099 1 513 . 1 1 75 75 ARG HB2 H 1 1.56 0.01 . 2 . . . . . . . . 5099 1 514 . 1 1 75 75 ARG HB3 H 1 1.52 0.01 . 2 . . . . . . . . 5099 1 515 . 1 1 75 75 ARG HG2 H 1 1.29 0.01 . 2 . . . . . . . . 5099 1 516 . 1 1 75 75 ARG HG3 H 1 1.23 0.01 . 2 . . . . . . . . 5099 1 517 . 1 1 75 75 ARG HD2 H 1 2.89 0.01 . 2 . . . . . . . . 5099 1 518 . 1 1 75 75 ARG C C 13 175.37 0.12 . 1 . . . . . . . . 5099 1 519 . 1 1 75 75 ARG CA C 13 55.96 0.12 . 1 . . . . . . . . 5099 1 520 . 1 1 75 75 ARG CB C 13 30.45 0.12 . 1 . . . . . . . . 5099 1 521 . 1 1 75 75 ARG CG C 13 27.03 0.12 . 1 . . . . . . . . 5099 1 522 . 1 1 75 75 ARG CD C 13 43.14 0.12 . 1 . . . . . . . . 5099 1 523 . 1 1 75 75 ARG N N 15 126.88 0.12 . 1 . . . . . . . . 5099 1 524 . 1 1 76 76 SER H H 1 6.61 0.01 . 1 . . . . . . . . 5099 1 525 . 1 1 76 76 SER HA H 1 4.13 0.01 . 1 . . . . . . . . 5099 1 526 . 1 1 76 76 SER HB2 H 1 3.62 0.01 . 2 . . . . . . . . 5099 1 527 . 1 1 76 76 SER HB3 H 1 3.17 0.01 . 2 . . . . . . . . 5099 1 528 . 1 1 76 76 SER CB C 13 63.82 0.12 . 1 . . . . . . . . 5099 1 529 . 1 1 76 76 SER N N 15 113.48 0.12 . 1 . . . . . . . . 5099 1 530 . 1 1 77 77 HIS CA C 13 55.69 0.12 . 1 . . . . . . . . 5099 1 531 . 1 1 78 78 ASN H H 1 8.18 0.01 . 1 . . . . . . . . 5099 1 532 . 1 1 78 78 ASN HA H 1 4.71 0.01 . 1 . . . . . . . . 5099 1 533 . 1 1 78 78 ASN HB2 H 1 2.85 0.01 . 2 . . . . . . . . 5099 1 534 . 1 1 78 78 ASN HB3 H 1 2.59 0.01 . 2 . . . . . . . . 5099 1 535 . 1 1 78 78 ASN CA C 13 52.67 0.12 . 1 . . . . . . . . 5099 1 536 . 1 1 78 78 ASN CB C 13 38.63 0.12 . 1 . . . . . . . . 5099 1 537 . 1 1 78 78 ASN N N 15 119.22 0.12 . 1 . . . . . . . . 5099 1 538 . 1 1 79 79 ARG H H 1 8.83 0.01 . 1 . . . . . . . . 5099 1 539 . 1 1 79 79 ARG HA H 1 4.18 0.01 . 1 . . . . . . . . 5099 1 540 . 1 1 79 79 ARG HB2 H 1 1.84 0.01 . 2 . . . . . . . . 5099 1 541 . 1 1 79 79 ARG HB3 H 1 1.74 0.01 . 2 . . . . . . . . 5099 1 542 . 1 1 79 79 ARG HG2 H 1 1.62 0.01 . 2 . . . . . . . . 5099 1 543 . 1 1 79 79 ARG HD2 H 1 3.06 0.01 . 2 . . . . . . . . 5099 1 544 . 1 1 79 79 ARG C C 13 177.97 0.12 . 1 . . . . . . . . 5099 1 545 . 1 1 79 79 ARG CA C 13 58.78 0.12 . 1 . . . . . . . . 5099 1 546 . 1 1 79 79 ARG CB C 13 29.87 0.12 . 1 . . . . . . . . 5099 1 547 . 1 1 79 79 ARG CD C 13 43.40 0.12 . 1 . . . . . . . . 5099 1 548 . 1 1 79 79 ARG N N 15 124.97 0.12 . 1 . . . . . . . . 5099 1 549 . 1 1 80 80 SER H H 1 8.28 0.01 . 1 . . . . . . . . 5099 1 550 . 1 1 80 80 SER HA H 1 4.26 0.01 . 1 . . . . . . . . 5099 1 551 . 1 1 80 80 SER HB2 H 1 3.78 0.01 . 2 . . . . . . . . 5099 1 552 . 1 1 80 80 SER C C 13 174.15 0.12 . 1 . . . . . . . . 5099 1 553 . 1 1 80 80 SER CA C 13 59.39 0.12 . 1 . . . . . . . . 5099 1 554 . 1 1 80 80 SER CB C 13 64.09 0.12 . 1 . . . . . . . . 5099 1 555 . 1 1 80 80 SER N N 15 114.42 0.12 . 1 . . . . . . . . 5099 1 556 . 1 1 81 81 GLU H H 1 7.49 0.01 . 1 . . . . . . . . 5099 1 557 . 1 1 81 81 GLU HA H 1 4.01 0.01 . 1 . . . . . . . . 5099 1 558 . 1 1 81 81 GLU HB2 H 1 2.11 0.01 . 2 . . . . . . . . 5099 1 559 . 1 1 81 81 GLU HB3 H 1 2.03 0.01 . 2 . . . . . . . . 5099 1 560 . 1 1 81 81 GLU HG2 H 1 1.92 0.01 . 2 . . . . . . . . 5099 1 561 . 1 1 81 81 GLU C C 13 176.25 0.12 . 1 . . . . . . . . 5099 1 562 . 1 1 81 81 GLU CA C 13 57.05 0.12 . 1 . . . . . . . . 5099 1 563 . 1 1 81 81 GLU CG C 13 35.98 0.12 . 1 . . . . . . . . 5099 1 564 . 1 1 81 81 GLU N N 15 123.35 0.12 . 1 . . . . . . . . 5099 1 565 . 1 1 82 82 GLU H H 1 8.88 0.01 . 1 . . . . . . . . 5099 1 566 . 1 1 82 82 GLU HG2 H 1 2.10 0.01 . 2 . . . . . . . . 5099 1 567 . 1 1 82 82 GLU HG3 H 1 1.65 0.01 . 2 . . . . . . . . 5099 1 568 . 1 1 82 82 GLU C C 13 177.27 0.12 . 1 . . . . . . . . 5099 1 569 . 1 1 82 82 GLU CA C 13 56.96 0.12 . 1 . . . . . . . . 5099 1 570 . 1 1 82 82 GLU CG C 13 37.94 0.12 . 1 . . . . . . . . 5099 1 571 . 1 1 82 82 GLU N N 15 124.36 0.12 . 1 . . . . . . . . 5099 1 572 . 1 1 83 83 PHE H H 1 9.90 0.01 . 1 . . . . . . . . 5099 1 573 . 1 1 83 83 PHE C C 13 173.85 0.12 . 1 . . . . . . . . 5099 1 574 . 1 1 83 83 PHE CA C 13 58.04 0.12 . 1 . . . . . . . . 5099 1 575 . 1 1 83 83 PHE N N 15 125.24 0.12 . 1 . . . . . . . . 5099 1 576 . 1 1 84 84 LEU H H 1 9.60 0.01 . 1 . . . . . . . . 5099 1 577 . 1 1 84 84 LEU HA H 1 4.91 0.01 . 1 . . . . . . . . 5099 1 578 . 1 1 84 84 LEU HB2 H 1 1.50 0.01 . 2 . . . . . . . . 5099 1 579 . 1 1 84 84 LEU HD21 H 1 0.41 0.01 . 1 . . . . . . . . 5099 1 580 . 1 1 84 84 LEU HD22 H 1 0.41 0.01 . 1 . . . . . . . . 5099 1 581 . 1 1 84 84 LEU HD23 H 1 0.41 0.01 . 1 . . . . . . . . 5099 1 582 . 1 1 84 84 LEU C C 13 175.67 0.12 . 1 . . . . . . . . 5099 1 583 . 1 1 84 84 LEU CA C 13 52.80 0.12 . 1 . . . . . . . . 5099 1 584 . 1 1 84 84 LEU CD2 C 13 23.61 0.12 . 1 . . . . . . . . 5099 1 585 . 1 1 84 84 LEU N N 15 126.37 0.12 . 1 . . . . . . . . 5099 1 586 . 1 1 85 85 ILE H H 1 9.31 0.01 . 1 . . . . . . . . 5099 1 587 . 1 1 85 85 ILE C C 13 173.27 0.12 . 1 . . . . . . . . 5099 1 588 . 1 1 85 85 ILE CA C 13 61.64 0.12 . 1 . . . . . . . . 5099 1 589 . 1 1 85 85 ILE N N 15 124.99 0.12 . 1 . . . . . . . . 5099 1 590 . 1 1 86 86 ALA H H 1 7.98 0.01 . 1 . . . . . . . . 5099 1 591 . 1 1 86 86 ALA HA H 1 5.33 0.01 . 1 . . . . . . . . 5099 1 592 . 1 1 86 86 ALA HB1 H 1 1.42 0.01 . 1 . . . . . . . . 5099 1 593 . 1 1 86 86 ALA HB2 H 1 1.42 0.01 . 1 . . . . . . . . 5099 1 594 . 1 1 86 86 ALA HB3 H 1 1.42 0.01 . 1 . . . . . . . . 5099 1 595 . 1 1 86 86 ALA C C 13 176.41 0.12 . 1 . . . . . . . . 5099 1 596 . 1 1 86 86 ALA CA C 13 50.8 0.12 . 1 . . . . . . . . 5099 1 597 . 1 1 86 86 ALA CB C 13 20.06 0.12 . 1 . . . . . . . . 5099 1 598 . 1 1 86 86 ALA N N 15 132.66 0.12 . 1 . . . . . . . . 5099 1 599 . 1 1 87 87 GLY H H 1 8.55 0.01 . 1 . . . . . . . . 5099 1 600 . 1 1 87 87 GLY HA2 H 1 4.97 0.01 . 1 . . . . . . . . 5099 1 601 . 1 1 87 87 GLY HA3 H 1 3.43 0.01 . 1 . . . . . . . . 5099 1 602 . 1 1 87 87 GLY C C 13 172.97 0.12 . 1 . . . . . . . . 5099 1 603 . 1 1 87 87 GLY CA C 13 44.99 0.12 . 1 . . . . . . . . 5099 1 604 . 1 1 87 87 GLY N N 15 106.74 0.12 . 1 . . . . . . . . 5099 1 605 . 1 1 88 88 LYS H H 1 8.50 0.01 . 1 . . . . . . . . 5099 1 606 . 1 1 88 88 LYS HA H 1 4.70 0.01 . 1 . . . . . . . . 5099 1 607 . 1 1 88 88 LYS HB2 H 1 1.60 0.01 . 2 . . . . . . . . 5099 1 608 . 1 1 88 88 LYS HG2 H 1 1.37 0.01 . 2 . . . . . . . . 5099 1 609 . 1 1 88 88 LYS HG3 H 1 1.39 0.01 . 2 . . . . . . . . 5099 1 610 . 1 1 88 88 LYS HD2 H 1 1.58 0.01 . 2 . . . . . . . . 5099 1 611 . 1 1 88 88 LYS HE2 H 1 2.87 0.01 . 2 . . . . . . . . 5099 1 612 . 1 1 88 88 LYS C C 13 175.36 0.12 . 1 . . . . . . . . 5099 1 613 . 1 1 88 88 LYS CA C 13 54.48 0.12 . 1 . . . . . . . . 5099 1 614 . 1 1 88 88 LYS CB C 13 35.66 0.12 . 1 . . . . . . . . 5099 1 615 . 1 1 88 88 LYS CG C 13 24.84 0.12 . 1 . . . . . . . . 5099 1 616 . 1 1 88 88 LYS CD C 13 28.55 0.12 . 1 . . . . . . . . 5099 1 617 . 1 1 88 88 LYS CE C 13 42.01 0.12 . 1 . . . . . . . . 5099 1 618 . 1 1 88 88 LYS N N 15 120.84 0.12 . 1 . . . . . . . . 5099 1 619 . 1 1 89 89 LEU H H 1 9.83 0.01 . 1 . . . . . . . . 5099 1 620 . 1 1 89 89 LEU HA H 1 4.92 0.01 . 1 . . . . . . . . 5099 1 621 . 1 1 89 89 LEU HB2 H 1 1.30 0.01 . 2 . . . . . . . . 5099 1 622 . 1 1 89 89 LEU HG H 1 1.21 0.01 . 1 . . . . . . . . 5099 1 623 . 1 1 89 89 LEU HD11 H 1 0.49 0.01 . 1 . . . . . . . . 5099 1 624 . 1 1 89 89 LEU HD12 H 1 0.49 0.01 . 1 . . . . . . . . 5099 1 625 . 1 1 89 89 LEU HD13 H 1 0.49 0.01 . 1 . . . . . . . . 5099 1 626 . 1 1 89 89 LEU HD21 H 1 0.55 0.01 . 1 . . . . . . . . 5099 1 627 . 1 1 89 89 LEU HD22 H 1 0.55 0.01 . 1 . . . . . . . . 5099 1 628 . 1 1 89 89 LEU HD23 H 1 0.55 0.01 . 1 . . . . . . . . 5099 1 629 . 1 1 89 89 LEU C C 13 177.27 0.12 . 1 . . . . . . . . 5099 1 630 . 1 1 89 89 LEU CA C 13 54.17 0.12 . 1 . . . . . . . . 5099 1 631 . 1 1 89 89 LEU CB C 13 43.40 0.12 . 1 . . . . . . . . 5099 1 632 . 1 1 89 89 LEU CD1 C 13 23.77 0.12 . 1 . . . . . . . . 5099 1 633 . 1 1 89 89 LEU CD2 C 13 24.83 0.12 . 1 . . . . . . . . 5099 1 634 . 1 1 89 89 LEU N N 15 125.37 0.12 . 1 . . . . . . . . 5099 1 635 . 1 1 90 90 GLN H H 1 9.21 0.01 . 1 . . . . . . . . 5099 1 636 . 1 1 90 90 GLN HA H 1 4.31 0.01 . 1 . . . . . . . . 5099 1 637 . 1 1 90 90 GLN HB2 H 1 1.34 0.01 . 2 . . . . . . . . 5099 1 638 . 1 1 90 90 GLN HG2 H 1 1.74 0.01 . 1 . . . . . . . . 5099 1 639 . 1 1 90 90 GLN C C 13 175.55 0.12 . 1 . . . . . . . . 5099 1 640 . 1 1 90 90 GLN CA C 13 55.30 0.12 . 1 . . . . . . . . 5099 1 641 . 1 1 90 90 GLN CB C 13 30.4 0.12 . 1 . . . . . . . . 5099 1 642 . 1 1 90 90 GLN CG C 13 33.22 0.12 . 1 . . . . . . . . 5099 1 643 . 1 1 90 90 GLN N N 15 125.24 0.12 . 1 . . . . . . . . 5099 1 644 . 1 1 91 91 ASP H H 1 9.30 0.01 . 1 . . . . . . . . 5099 1 645 . 1 1 91 91 ASP HA H 1 4.18 0.01 . 1 . . . . . . . . 5099 1 646 . 1 1 91 91 ASP HB2 H 1 2.62 0.01 . 2 . . . . . . . . 5099 1 647 . 1 1 91 91 ASP HB3 H 1 2.36 0.01 . 2 . . . . . . . . 5099 1 648 . 1 1 91 91 ASP C C 13 175.70 0.12 . 1 . . . . . . . . 5099 1 649 . 1 1 91 91 ASP CA C 13 55.85 0.12 . 1 . . . . . . . . 5099 1 650 . 1 1 91 91 ASP CB C 13 39.89 0.12 . 1 . . . . . . . . 5099 1 651 . 1 1 91 91 ASP N N 15 128.64 0.12 . 1 . . . . . . . . 5099 1 652 . 1 1 92 92 GLY H H 1 8.35 0.01 . 1 . . . . . . . . 5099 1 653 . 1 1 92 92 GLY HA2 H 1 3.89 0.01 . 2 . . . . . . . . 5099 1 654 . 1 1 92 92 GLY HA3 H 1 3.28 0.01 . 2 . . . . . . . . 5099 1 655 . 1 1 92 92 GLY C C 13 173.03 0.12 . 1 . . . . . . . . 5099 1 656 . 1 1 92 92 GLY CA C 13 45.63 0.12 . 1 . . . . . . . . 5099 1 657 . 1 1 92 92 GLY N N 15 102.72 0.12 . 1 . . . . . . . . 5099 1 658 . 1 1 93 93 LEU H H 1 7.66 0.01 . 1 . . . . . . . . 5099 1 659 . 1 1 93 93 LEU HA H 1 4.47 0.01 . 1 . . . . . . . . 5099 1 660 . 1 1 93 93 LEU HB2 H 1 1.37 0.01 . 2 . . . . . . . . 5099 1 661 . 1 1 93 93 LEU HB3 H 1 0.87 0.01 . 2 . . . . . . . . 5099 1 662 . 1 1 93 93 LEU HG H 1 1.26 0.01 . 1 . . . . . . . . 5099 1 663 . 1 1 93 93 LEU HD11 H 1 0.49 0.01 . 1 . . . . . . . . 5099 1 664 . 1 1 93 93 LEU HD12 H 1 0.49 0.01 . 1 . . . . . . . . 5099 1 665 . 1 1 93 93 LEU HD13 H 1 0.49 0.01 . 1 . . . . . . . . 5099 1 666 . 1 1 93 93 LEU HD21 H 1 -0.01 0.01 . 1 . . . . . . . . 5099 1 667 . 1 1 93 93 LEU HD22 H 1 -0.01 0.01 . 1 . . . . . . . . 5099 1 668 . 1 1 93 93 LEU HD23 H 1 -0.01 0.01 . 1 . . . . . . . . 5099 1 669 . 1 1 93 93 LEU CA C 13 53.40 0.12 . 1 . . . . . . . . 5099 1 670 . 1 1 93 93 LEU CG C 13 25.90 0.12 . 1 . . . . . . . . 5099 1 671 . 1 1 93 93 LEU CD1 C 13 21.92 0.12 . 1 . . . . . . . . 5099 1 672 . 1 1 93 93 LEU CD2 C 13 23.51 0.12 . 1 . . . . . . . . 5099 1 673 . 1 1 93 93 LEU N N 15 121.34 0.12 . 1 . . . . . . . . 5099 1 674 . 1 1 94 94 LEU H H 1 9.46 0.01 . 1 . . . . . . . . 5099 1 675 . 1 1 94 94 LEU HA H 1 4.53 0.01 . 9 . . . . . . . . 5099 1 676 . 1 1 94 94 LEU HB2 H 1 1.06 0.01 . 9 . . . . . . . . 5099 1 677 . 1 1 94 94 LEU HB3 H 1 1.00 0.01 . 9 . . . . . . . . 5099 1 678 . 1 1 94 94 LEU HG H 1 1.30 0.01 . 1 . . . . . . . . 5099 1 679 . 1 1 94 94 LEU HD11 H 1 0.66 0.01 . 1 . . . . . . . . 5099 1 680 . 1 1 94 94 LEU HD12 H 1 0.66 0.01 . 1 . . . . . . . . 5099 1 681 . 1 1 94 94 LEU HD13 H 1 0.66 0.01 . 1 . . . . . . . . 5099 1 682 . 1 1 94 94 LEU HD21 H 1 0.53 0.01 . 1 . . . . . . . . 5099 1 683 . 1 1 94 94 LEU HD22 H 1 0.53 0.01 . 1 . . . . . . . . 5099 1 684 . 1 1 94 94 LEU HD23 H 1 0.53 0.01 . 1 . . . . . . . . 5099 1 685 . 1 1 94 94 LEU C C 13 174.54 0.12 . 1 . . . . . . . . 5099 1 686 . 1 1 94 94 LEU CA C 13 55.81 0.12 . 1 . . . . . . . . 5099 1 687 . 1 1 94 94 LEU CG C 13 27.55 0.12 . 1 . . . . . . . . 5099 1 688 . 1 1 94 94 LEU CD1 C 13 23.51 0.12 . 1 . . . . . . . . 5099 1 689 . 1 1 94 94 LEU CD2 C 13 25.90 0.12 . 1 . . . . . . . . 5099 1 690 . 1 1 94 94 LEU N N 15 126.75 0.12 . 1 . . . . . . . . 5099 1 691 . 1 1 95 95 HIS H H 1 9.78 0.01 . 1 . . . . . . . . 5099 1 692 . 1 1 95 95 HIS HA H 1 5.49 0.01 . 1 . . . . . . . . 5099 1 693 . 1 1 95 95 HIS HB2 H 1 3.00 0.01 . 2 . . . . . . . . 5099 1 694 . 1 1 95 95 HIS C C 13 176.80 0.12 . 1 . . . . . . . . 5099 1 695 . 1 1 95 95 HIS CA C 13 56.35 0.12 . 1 . . . . . . . . 5099 1 696 . 1 1 95 95 HIS N N 15 129.14 0.12 . 1 . . . . . . . . 5099 1 697 . 1 1 96 96 ILE H H 1 9.02 0.01 . 1 . . . . . . . . 5099 1 698 . 1 1 96 96 ILE HA H 1 4.99 0.01 . 1 . . . . . . . . 5099 1 699 . 1 1 96 96 ILE HB H 1 1.75 0.01 . 1 . . . . . . . . 5099 1 700 . 1 1 96 96 ILE C C 13 177.07 0.12 . 1 . . . . . . . . 5099 1 701 . 1 1 96 96 ILE CA C 13 60.04 0.12 . 1 . . . . . . . . 5099 1 702 . 1 1 96 96 ILE N N 15 113.66 0.12 . 1 . . . . . . . . 5099 1 703 . 1 1 97 97 THR H H 1 9.62 0.01 . 1 . . . . . . . . 5099 1 704 . 1 1 97 97 THR C C 13 176.66 0.12 . 1 . . . . . . . . 5099 1 705 . 1 1 97 97 THR CA C 13 61.71 0.12 . 1 . . . . . . . . 5099 1 706 . 1 1 97 97 THR N N 15 114.67 0.12 . 1 . . . . . . . . 5099 1 707 . 1 1 98 98 THR H H 1 8.91 0.01 . 1 . . . . . . . . 5099 1 708 . 1 1 98 98 THR C C 13 172.88 0.12 . 1 . . . . . . . . 5099 1 709 . 1 1 98 98 THR CA C 13 66.36 0.12 . 1 . . . . . . . . 5099 1 710 . 1 1 98 98 THR N N 15 116.56 0.12 . 1 . . . . . . . . 5099 1 711 . 1 1 99 99 CYS H H 1 8.48 0.01 . 1 . . . . . . . . 5099 1 712 . 1 1 99 99 CYS C C 13 176.08 0.12 . 1 . . . . . . . . 5099 1 713 . 1 1 99 99 CYS N N 15 114.32 0.12 . 1 . . . . . . . . 5099 1 714 . 1 1 100 100 SER H H 1 7.84 0.01 . 1 . . . . . . . . 5099 1 715 . 1 1 100 100 SER C C 13 172.93 0.12 . 1 . . . . . . . . 5099 1 716 . 1 1 100 100 SER CA C 13 59.71 0.12 . 1 . . . . . . . . 5099 1 717 . 1 1 100 100 SER N N 15 119.09 0.12 . 1 . . . . . . . . 5099 1 718 . 1 1 101 101 PHE H H 1 9.72 0.01 . 1 . . . . . . . . 5099 1 719 . 1 1 101 101 PHE C C 13 172.37 0.12 . 1 . . . . . . . . 5099 1 720 . 1 1 101 101 PHE CA C 13 59.88 0.12 . 1 . . . . . . . . 5099 1 721 . 1 1 101 101 PHE N N 15 127.63 0.12 . 1 . . . . . . . . 5099 1 722 . 1 1 102 102 VAL H H 1 7.01 0.01 . 1 . . . . . . . . 5099 1 723 . 1 1 102 102 VAL HA H 1 4.93 0.01 . 1 . . . . . . . . 5099 1 724 . 1 1 102 102 VAL HB H 1 1.61 0.01 . 1 . . . . . . . . 5099 1 725 . 1 1 102 102 VAL HG11 H 1 0.52 0.01 . 1 . . . . . . . . 5099 1 726 . 1 1 102 102 VAL HG12 H 1 0.52 0.01 . 1 . . . . . . . . 5099 1 727 . 1 1 102 102 VAL HG13 H 1 0.52 0.01 . 1 . . . . . . . . 5099 1 728 . 1 1 102 102 VAL HG21 H 1 0.40 0.01 . 1 . . . . . . . . 5099 1 729 . 1 1 102 102 VAL HG22 H 1 0.40 0.01 . 1 . . . . . . . . 5099 1 730 . 1 1 102 102 VAL HG23 H 1 0.40 0.01 . 1 . . . . . . . . 5099 1 731 . 1 1 102 102 VAL C C 13 176.12 0.12 . 1 . . . . . . . . 5099 1 732 . 1 1 102 102 VAL CA C 13 61.05 0.12 . 1 . . . . . . . . 5099 1 733 . 1 1 102 102 VAL CB C 13 34.91 0.12 . 1 . . . . . . . . 5099 1 734 . 1 1 102 102 VAL CG1 C 13 20.59 0.12 . 1 . . . . . . . . 5099 1 735 . 1 1 102 102 VAL CG2 C 13 21.39 0.12 . 1 . . . . . . . . 5099 1 736 . 1 1 102 102 VAL N N 15 129.27 0.12 . 1 . . . . . . . . 5099 1 737 . 1 1 103 103 ALA H H 1 8.75 0.01 . 1 . . . . . . . . 5099 1 738 . 1 1 103 103 ALA HA H 1 4.83 0.01 . 1 . . . . . . . . 5099 1 739 . 1 1 103 103 ALA HB1 H 1 0.85 0.01 . 1 . . . . . . . . 5099 1 740 . 1 1 103 103 ALA HB2 H 1 0.85 0.01 . 1 . . . . . . . . 5099 1 741 . 1 1 103 103 ALA HB3 H 1 0.85 0.01 . 1 . . . . . . . . 5099 1 742 . 1 1 103 103 ALA CA C 13 50.27 0.12 . 1 . . . . . . . . 5099 1 743 . 1 1 103 103 ALA CB C 13 21.65 0.12 . 1 . . . . . . . . 5099 1 744 . 1 1 103 103 ALA N N 15 128.26 0.12 . 1 . . . . . . . . 5099 1 745 . 1 1 104 104 PRO C C 13 178.93 0.12 . 1 . . . . . . . . 5099 1 746 . 1 1 104 104 PRO CA C 13 62.84 0.12 . 1 . . . . . . . . 5099 1 747 . 1 1 105 105 TRP H H 1 8.99 0.01 . 1 . . . . . . . . 5099 1 748 . 1 1 105 105 TRP C C 13 177.12 0.12 . 1 . . . . . . . . 5099 1 749 . 1 1 105 105 TRP CA C 13 60.47 0.12 . 1 . . . . . . . . 5099 1 750 . 1 1 105 105 TRP N N 15 131.15 0.12 . 1 . . . . . . . . 5099 1 751 . 1 1 106 106 ASN H H 1 9.06 0.01 . 1 . . . . . . . . 5099 1 752 . 1 1 106 106 ASN HA H 1 4.16 0.01 . 1 . . . . . . . . 5099 1 753 . 1 1 106 106 ASN HB2 H 1 2.55 0.01 . 2 . . . . . . . . 5099 1 754 . 1 1 106 106 ASN HB3 H 1 2.68 0.01 . 2 . . . . . . . . 5099 1 755 . 1 1 106 106 ASN C C 13 176.00 0.12 . 1 . . . . . . . . 5099 1 756 . 1 1 106 106 ASN CA C 13 54.78 0.12 . 1 . . . . . . . . 5099 1 757 . 1 1 106 106 ASN CB C 13 37.61 0.12 . 1 . . . . . . . . 5099 1 758 . 1 1 106 106 ASN N N 15 112.66 0.12 . 1 . . . . . . . . 5099 1 759 . 1 1 107 107 SER H H 1 7.58 0.01 . 1 . . . . . . . . 5099 1 760 . 1 1 107 107 SER HA H 1 4.22 0.01 . 1 . . . . . . . . 5099 1 761 . 1 1 107 107 SER HB2 H 1 3.67 0.01 . 2 . . . . . . . . 5099 1 762 . 1 1 107 107 SER HB3 H 1 3.79 0.01 . 2 . . . . . . . . 5099 1 763 . 1 1 107 107 SER C C 13 174.47 0.12 . 1 . . . . . . . . 5099 1 764 . 1 1 107 107 SER CA C 13 59.41 0.12 . 1 . . . . . . . . 5099 1 765 . 1 1 107 107 SER CB C 13 64.09 0.12 . 1 . . . . . . . . 5099 1 766 . 1 1 107 107 SER N N 15 113.92 0.12 . 1 . . . . . . . . 5099 1 767 . 1 1 108 108 LEU H H 1 7.12 0.01 . 1 . . . . . . . . 5099 1 768 . 1 1 108 108 LEU HA H 1 4.26 0.01 . 1 . . . . . . . . 5099 1 769 . 1 1 108 108 LEU HG H 1 1.72 0.01 . 1 . . . . . . . . 5099 1 770 . 1 1 108 108 LEU HD11 H 1 0.76 0.01 . 1 . . . . . . . . 5099 1 771 . 1 1 108 108 LEU HD12 H 1 0.76 0.01 . 1 . . . . . . . . 5099 1 772 . 1 1 108 108 LEU HD13 H 1 0.76 0.01 . 1 . . . . . . . . 5099 1 773 . 1 1 108 108 LEU HD21 H 1 0.61 0.01 . 1 . . . . . . . . 5099 1 774 . 1 1 108 108 LEU HD22 H 1 0.61 0.01 . 1 . . . . . . . . 5099 1 775 . 1 1 108 108 LEU HD23 H 1 0.61 0.01 . 1 . . . . . . . . 5099 1 776 . 1 1 108 108 LEU C C 13 177.93 0.12 . 1 . . . . . . . . 5099 1 777 . 1 1 108 108 LEU CA C 13 54.57 0.12 . 1 . . . . . . . . 5099 1 778 . 1 1 108 108 LEU CG C 13 26.43 0.12 . 1 . . . . . . . . 5099 1 779 . 1 1 108 108 LEU CD1 C 13 22.71 0.12 . 1 . . . . . . . . 5099 1 780 . 1 1 108 108 LEU CD2 C 13 27.22 0.12 . 1 . . . . . . . . 5099 1 781 . 1 1 108 108 LEU N N 15 123.48 0.12 . 1 . . . . . . . . 5099 1 782 . 1 1 109 109 SER H H 1 8.61 0.01 . 1 . . . . . . . . 5099 1 783 . 1 1 109 109 SER C C 13 175.14 0.12 . 1 . . . . . . . . 5099 1 784 . 1 1 109 109 SER CA C 13 57.33 0.12 . 1 . . . . . . . . 5099 1 785 . 1 1 109 109 SER N N 15 119.96 0.12 . 1 . . . . . . . . 5099 1 786 . 1 1 110 110 LEU H H 1 8.75 0.01 . 1 . . . . . . . . 5099 1 787 . 1 1 110 110 LEU HA H 1 3.62 0.01 . 1 . . . . . . . . 5099 1 788 . 1 1 110 110 LEU HB2 H 1 1.44 0.01 . 2 . . . . . . . . 5099 1 789 . 1 1 110 110 LEU HG H 1 1.38 0.01 . 1 . . . . . . . . 5099 1 790 . 1 1 110 110 LEU HD11 H 1 0.71 0.01 . 1 . . . . . . . . 5099 1 791 . 1 1 110 110 LEU HD12 H 1 0.71 0.01 . 1 . . . . . . . . 5099 1 792 . 1 1 110 110 LEU HD13 H 1 0.71 0.01 . 1 . . . . . . . . 5099 1 793 . 1 1 110 110 LEU HD21 H 1 0.63 0.01 . 1 . . . . . . . . 5099 1 794 . 1 1 110 110 LEU HD22 H 1 0.63 0.01 . 1 . . . . . . . . 5099 1 795 . 1 1 110 110 LEU HD23 H 1 0.63 0.01 . 1 . . . . . . . . 5099 1 796 . 1 1 110 110 LEU C C 13 179.34 0.12 . 1 . . . . . . . . 5099 1 797 . 1 1 110 110 LEU CA C 13 59.12 0.12 . 1 . . . . . . . . 5099 1 798 . 1 1 110 110 LEU CB C 13 41.03 0.12 . 1 . . . . . . . . 5099 1 799 . 1 1 110 110 LEU CG C 13 27.03 0.12 . 1 . . . . . . . . 5099 1 800 . 1 1 110 110 LEU CD1 C 13 24.27 0.12 . 1 . . . . . . . . 5099 1 801 . 1 1 110 110 LEU CD2 C 13 23.90 0.12 . 1 . . . . . . . . 5099 1 802 . 1 1 110 110 LEU N N 15 123.23 0.12 . 1 . . . . . . . . 5099 1 803 . 1 1 111 111 ALA H H 1 8.29 0.01 . 1 . . . . . . . . 5099 1 804 . 1 1 111 111 ALA HA H 1 3.71 0.01 . 1 . . . . . . . . 5099 1 805 . 1 1 111 111 ALA HB1 H 1 1.13 0.01 . 1 . . . . . . . . 5099 1 806 . 1 1 111 111 ALA HB2 H 1 1.13 0.01 . 1 . . . . . . . . 5099 1 807 . 1 1 111 111 ALA HB3 H 1 1.13 0.01 . 1 . . . . . . . . 5099 1 808 . 1 1 111 111 ALA C C 13 181.26 0.12 . 1 . . . . . . . . 5099 1 809 . 1 1 111 111 ALA CA C 13 55.42 0.12 . 1 . . . . . . . . 5099 1 810 . 1 1 111 111 ALA CB C 13 18.24 0.12 . 1 . . . . . . . . 5099 1 811 . 1 1 111 111 ALA N N 15 120.47 0.12 . 1 . . . . . . . . 5099 1 812 . 1 1 112 112 GLN H H 1 7.58 0.01 . 1 . . . . . . . . 5099 1 813 . 1 1 112 112 GLN C C 13 178.31 0.12 . 1 . . . . . . . . 5099 1 814 . 1 1 112 112 GLN CA C 13 58.21 0.12 . 1 . . . . . . . . 5099 1 815 . 1 1 112 112 GLN N N 15 119.33 0.12 . 1 . . . . . . . . 5099 1 816 . 1 1 113 113 ARG H H 1 8.34 0.01 . 1 . . . . . . . . 5099 1 817 . 1 1 113 113 ARG C C 13 179.85 0.12 . 1 . . . . . . . . 5099 1 818 . 1 1 113 113 ARG CA C 13 60.95 0.12 . 1 . . . . . . . . 5099 1 819 . 1 1 113 113 ARG N N 15 119.58 0.12 . 1 . . . . . . . . 5099 1 820 . 1 1 114 114 ARG H H 1 8.30 0.01 . 1 . . . . . . . . 5099 1 821 . 1 1 114 114 ARG HA H 1 3.74 0.01 . 1 . . . . . . . . 5099 1 822 . 1 1 114 114 ARG HB2 H 1 1.50 0.01 . 2 . . . . . . . . 5099 1 823 . 1 1 114 114 ARG HG2 H 1 1.49 0.01 . 2 . . . . . . . . 5099 1 824 . 1 1 114 114 ARG HG3 H 1 1.38 0.01 . 2 . . . . . . . . 5099 1 825 . 1 1 114 114 ARG HD2 H 1 2.86 0.01 . 9 . . . . . . . . 5099 1 826 . 1 1 114 114 ARG C C 13 178.63 0.12 . 1 . . . . . . . . 5099 1 827 . 1 1 114 114 ARG CA C 13 59.02 0.12 . 1 . . . . . . . . 5099 1 828 . 1 1 114 114 ARG CB C 13 29.64 0.12 . 1 . . . . . . . . 5099 1 829 . 1 1 114 114 ARG CG C 13 27.52 0.12 . 1 . . . . . . . . 5099 1 830 . 1 1 114 114 ARG CD C 13 43.31 0.01 . 1 . . . . . . . . 5099 1 831 . 1 1 114 114 ARG N N 15 120.71 0.12 . 1 . . . . . . . . 5099 1 832 . 1 1 115 115 GLY H H 1 7.49 0.01 . 1 . . . . . . . . 5099 1 833 . 1 1 115 115 GLY C C 13 176.21 0.12 . 1 . . . . . . . . 5099 1 834 . 1 1 115 115 GLY CA C 13 44.96 0.12 . 1 . . . . . . . . 5099 1 835 . 1 1 115 115 GLY N N 15 111.65 0.12 . 1 . . . . . . . . 5099 1 836 . 1 1 116 116 PHE H H 1 7.71 0.01 . 1 . . . . . . . . 5099 1 837 . 1 1 116 116 PHE C C 13 175.47 0.12 . 1 . . . . . . . . 5099 1 838 . 1 1 116 116 PHE CA C 13 63.19 0.12 . 1 . . . . . . . . 5099 1 839 . 1 1 116 116 PHE N N 15 120.08 0.12 . 1 . . . . . . . . 5099 1 840 . 1 1 117 117 THR H H 1 7.56 0.01 . 1 . . . . . . . . 5099 1 841 . 1 1 117 117 THR HA H 1 3.77 0.01 . 1 . . . . . . . . 5099 1 842 . 1 1 117 117 THR HB H 1 4.04 0.01 . 1 . . . . . . . . 5099 1 843 . 1 1 117 117 THR HG21 H 1 1.17 0.01 . 1 . . . . . . . . 5099 1 844 . 1 1 117 117 THR HG22 H 1 1.17 0.01 . 1 . . . . . . . . 5099 1 845 . 1 1 117 117 THR HG23 H 1 1.17 0.01 . 1 . . . . . . . . 5099 1 846 . 1 1 117 117 THR C C 13 175.60 0.12 . 1 . . . . . . . . 5099 1 847 . 1 1 117 117 THR CA C 13 64.74 0.12 . 1 . . . . . . . . 5099 1 848 . 1 1 117 117 THR CB C 13 69.51 0.12 . 1 . . . . . . . . 5099 1 849 . 1 1 117 117 THR CG2 C 13 21.99 0.12 . 1 . . . . . . . . 5099 1 850 . 1 1 117 117 THR N N 15 107.12 0.12 . 1 . . . . . . . . 5099 1 851 . 1 1 118 118 LYS H H 1 7.90 0.01 . 1 . . . . . . . . 5099 1 852 . 1 1 118 118 LYS HA H 1 4.38 0.01 . 1 . . . . . . . . 5099 1 853 . 1 1 118 118 LYS HB2 H 1 1.62 0.01 . 2 . . . . . . . . 5099 1 854 . 1 1 118 118 LYS HB3 H 1 1.57 0.01 . 2 . . . . . . . . 5099 1 855 . 1 1 118 118 LYS HG2 H 1 1.16 0.01 . 2 . . . . . . . . 5099 1 856 . 1 1 118 118 LYS HG3 H 1 1.11 0.01 . 2 . . . . . . . . 5099 1 857 . 1 1 118 118 LYS HD2 H 1 1.45 0.01 . 2 . . . . . . . . 5099 1 858 . 1 1 118 118 LYS C C 13 177.10 0.12 . 1 . . . . . . . . 5099 1 859 . 1 1 118 118 LYS CA C 13 59.41 0.12 . 1 . . . . . . . . 5099 1 860 . 1 1 118 118 LYS N N 15 120.21 0.12 . 1 . . . . . . . . 5099 1 861 . 1 1 119 119 THR H H 1 8.09 0.01 . 1 . . . . . . . . 5099 1 862 . 1 1 119 119 THR HA H 1 3.98 0.01 . 1 . . . . . . . . 5099 1 863 . 1 1 119 119 THR HG21 H 1 0.84 0.01 . 1 . . . . . . . . 5099 1 864 . 1 1 119 119 THR HG22 H 1 0.84 0.01 . 1 . . . . . . . . 5099 1 865 . 1 1 119 119 THR HG23 H 1 0.84 0.01 . 1 . . . . . . . . 5099 1 866 . 1 1 119 119 THR C C 13 177.72 0.12 . 1 . . . . . . . . 5099 1 867 . 1 1 119 119 THR CA C 13 65.44 0.12 . 1 . . . . . . . . 5099 1 868 . 1 1 119 119 THR N N 15 111.40 0.12 . 1 . . . . . . . . 5099 1 869 . 1 1 120 120 TYR H H 1 9.29 0.01 . 1 . . . . . . . . 5099 1 870 . 1 1 120 120 TYR C C 13 178.81 0.12 . 1 . . . . . . . . 5099 1 871 . 1 1 120 120 TYR CA C 13 56.94 0.12 . 1 . . . . . . . . 5099 1 872 . 1 1 120 120 TYR N N 15 124.23 0.12 . 1 . . . . . . . . 5099 1 873 . 1 1 121 121 THR H H 1 7.95 0.01 . 1 . . . . . . . . 5099 1 874 . 1 1 121 121 THR HA H 1 3.97 0.01 . 1 . . . . . . . . 5099 1 875 . 1 1 121 121 THR HB H 1 4.07 0.01 . 1 . . . . . . . . 5099 1 876 . 1 1 121 121 THR HG21 H 1 1.14 0.01 . 1 . . . . . . . . 5099 1 877 . 1 1 121 121 THR HG22 H 1 1.14 0.01 . 1 . . . . . . . . 5099 1 878 . 1 1 121 121 THR HG23 H 1 1.14 0.01 . 1 . . . . . . . . 5099 1 879 . 1 1 121 121 THR C C 13 176.04 0.12 . 1 . . . . . . . . 5099 1 880 . 1 1 121 121 THR CA C 13 65.24 0.12 . 1 . . . . . . . . 5099 1 881 . 1 1 121 121 THR CB C 13 68.70 0.12 . 1 . . . . . . . . 5099 1 882 . 1 1 121 121 THR CG2 C 13 21.39 0.12 . 1 . . . . . . . . 5099 1 883 . 1 1 121 121 THR N N 15 112.91 0.12 . 1 . . . . . . . . 5099 1 884 . 1 1 122 122 VAL H H 1 7.01 0.01 . 1 . . . . . . . . 5099 1 885 . 1 1 122 122 VAL HA H 1 3.92 0.01 . 1 . . . . . . . . 5099 1 886 . 1 1 122 122 VAL HB H 1 2.04 0.01 . 1 . . . . . . . . 5099 1 887 . 1 1 122 122 VAL HG11 H 1 0.78 0.01 . 1 . . . . . . . . 5099 1 888 . 1 1 122 122 VAL HG12 H 1 0.78 0.01 . 1 . . . . . . . . 5099 1 889 . 1 1 122 122 VAL HG13 H 1 0.78 0.01 . 1 . . . . . . . . 5099 1 890 . 1 1 122 122 VAL C C 13 177.53 0.12 . 1 . . . . . . . . 5099 1 891 . 1 1 122 122 VAL CA C 13 63.81 0.12 . 1 . . . . . . . . 5099 1 892 . 1 1 122 122 VAL CB C 13 31.47 0.12 . 1 . . . . . . . . 5099 1 893 . 1 1 122 122 VAL CG1 C 13 20.86 0.12 . 1 . . . . . . . . 5099 1 894 . 1 1 122 122 VAL N N 15 118.32 0.12 . 1 . . . . . . . . 5099 1 895 . 1 1 123 123 GLY H H 1 7.86 0.01 . 1 . . . . . . . . 5099 1 896 . 1 1 123 123 GLY HA2 H 1 3.61 0.01 . 2 . . . . . . . . 5099 1 897 . 1 1 123 123 GLY HA3 H 1 4.01 0.01 . 2 . . . . . . . . 5099 1 898 . 1 1 123 123 GLY C C 13 175.12 0.01 . 1 . . . . . . . . 5099 1 899 . 1 1 123 123 GLY CA C 13 45.61 0.12 . 1 . . . . . . . . 5099 1 900 . 1 1 123 123 GLY N N 15 108.63 0.12 . 1 . . . . . . . . 5099 1 901 . 1 1 124 124 CYS H H 1 7.74 0.01 . 1 . . . . . . . . 5099 1 902 . 1 1 124 124 CYS HA H 1 4.64 0.01 . 1 . . . . . . . . 5099 1 903 . 1 1 124 124 CYS HB2 H 1 3.28 0.01 . 2 . . . . . . . . 5099 1 904 . 1 1 124 124 CYS HB3 H 1 2.82 0.01 . 2 . . . . . . . . 5099 1 905 . 1 1 124 124 CYS C C 13 175.25 0.12 . 1 . . . . . . . . 5099 1 906 . 1 1 124 124 CYS CA C 13 54.38 0.12 . 1 . . . . . . . . 5099 1 907 . 1 1 124 124 CYS CB C 13 37.83 0.12 . 1 . . . . . . . . 5099 1 908 . 1 1 124 124 CYS N N 15 118.07 0.12 . 1 . . . . . . . . 5099 1 909 . 1 1 125 125 GLU H H 1 8.31 0.01 . 1 . . . . . . . . 5099 1 910 . 1 1 125 125 GLU HA H 1 4.16 0.01 . 1 . . . . . . . . 5099 1 911 . 1 1 125 125 GLU HB2 H 1 1.79 0.01 . 2 . . . . . . . . 5099 1 912 . 1 1 125 125 GLU HB3 H 1 1.93 0.01 . 2 . . . . . . . . 5099 1 913 . 1 1 125 125 GLU HG2 H 1 2.13 0.01 . 2 . . . . . . . . 5099 1 914 . 1 1 125 125 GLU HG3 H 1 2.08 0.01 . 2 . . . . . . . . 5099 1 915 . 1 1 125 125 GLU C C 13 175.70 0.12 . 1 . . . . . . . . 5099 1 916 . 1 1 125 125 GLU CA C 13 57.02 0.12 . 1 . . . . . . . . 5099 1 917 . 1 1 125 125 GLU CB C 13 30.14 0.12 . 1 . . . . . . . . 5099 1 918 . 1 1 125 125 GLU CG C 13 35.97 0.12 . 1 . . . . . . . . 5099 1 919 . 1 1 125 125 GLU N N 15 122.47 0.12 . 1 . . . . . . . . 5099 1 920 . 1 1 126 126 GLU H H 1 7.94 0.01 . 1 . . . . . . . . 5099 1 921 . 1 1 126 126 GLU HA H 1 3.95 0.01 . 1 . . . . . . . . 5099 1 922 . 1 1 126 126 GLU HB2 H 1 1.71 0.01 . 2 . . . . . . . . 5099 1 923 . 1 1 126 126 GLU HB3 H 1 1.85 0.01 . 2 . . . . . . . . 5099 1 924 . 1 1 126 126 GLU HG2 H 1 2.03 0.01 . 2 . . . . . . . . 5099 1 925 . 1 1 126 126 GLU CA C 13 58.40 0.12 . 1 . . . . . . . . 5099 1 926 . 1 1 126 126 GLU CB C 13 30.94 0.12 . 1 . . . . . . . . 5099 1 927 . 1 1 126 126 GLU CG C 13 36.51 0.12 . 1 . . . . . . . . 5099 1 928 . 1 1 126 126 GLU N N 15 127.50 0.12 . 1 . . . . . . . . 5099 1 stop_ save_