data_16940 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 16940 _Entry.Title ; Backbone 1H, 13C, 15N assignments for hirugen bound PPACKed thrombin ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2010-05-20 _Entry.Accession_date 2010-05-20 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.0.9.13 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _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 Bernhard Lechtenberg . C. . 16940 2 Daniel Johnson . J.D. . 16940 3 Stefan Freund . M. . 16940 4 James Huntington . A. . 16940 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 16940 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 525 16940 '15N chemical shifts' 253 16940 '1H chemical shifts' 253 16940 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 2 . . 2010-08-12 2010-05-20 update BMRB 'Complete entry citation' 16940 1 . . 2010-07-26 2010-05-20 original author 'original release' 16940 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 16940 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 20660315 _Citation.Full_citation . _Citation.Title 'NMR resonance assignments of thrombin reveal the conformational and dynamic effects of ligation.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Proc. Natl. Acad. Sci. U.S.A.' _Citation.Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Citation.Journal_volume 107 _Citation.Journal_issue 32 _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 14087 _Citation.Page_last 14092 _Citation.Year 2010 _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 Bernhard Lechtenberg . C. . 16940 1 2 Daniel Johnson . J.D. . 16940 1 3 Stefan Freund . M.V. . 16940 1 4 James Huntington . A. . 16940 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 16940 _Assembly.ID 1 _Assembly.Name Thrombin _Assembly.BMRB_code . _Assembly.Number_of_components 4 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds yes _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 Thrombin 1 $Thrombin A . yes native no no . . . 16940 1 2 Hirugen 2 $Hirugen B . no native no yes . 'Exosite I binder' . 16940 1 3 PPACK 3 $PPACK C . no native no no . Inhibitor . 16940 1 4 Sodium 4 $NA D . no native no yes . . . 16940 1 stop_ loop_ _Entity_deleted_atom.ID _Entity_deleted_atom.Entity_atom_list_ID _Entity_deleted_atom.Entity_assembly_ID _Entity_deleted_atom.Entity_ID _Entity_deleted_atom.Comp_ID _Entity_deleted_atom.Comp_index_ID _Entity_deleted_atom.Seq_ID _Entity_deleted_atom.Atom_ID _Entity_deleted_atom.Auth_entity_assembly_ID _Entity_deleted_atom.Auth_seq_ID _Entity_deleted_atom.Auth_comp_ID _Entity_deleted_atom.Auth_atom_ID _Entity_deleted_atom.Entry_ID _Entity_deleted_atom.Assembly_ID . . 1 1 SER 241 241 HG . 525 SER HG 16940 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Thrombin _Entity.Sf_category entity _Entity.Sf_framecode Thrombin _Entity.Entry_ID 16940 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Thrombin _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(D) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; TFGSGEADCGLRPLFEKKSL EDKTERELLESYIDGRIVEG SDAEIGMSPWQVMLFRKSPQ ELLCGASLISDRWVLTAAHC LLYPPWDKNFTENDLLVRIG KHSRTRYERNIEKISMLEKI YIHPRYNWRENLDRDIALMK LKKPVAFSDYIHPVCLPDRE TAASLLQAGYKGRVTGWGNL KETWTANVGKGQPSVLQVVN LPIVERPVCKDSTRIRITDN MFCAGYKPDEGKRGDACEGD SGGPFVMKSPFNNRWYQMGI VSWGEGCDRDGKYGFYTHVF RLKKWIQKVIDQFGE ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq 'Prothrombin numbering is used. First residue is T285' _Entity.Polymer_author_seq_details 'Light and heavy chain of thrombin. Cleavage after R320' _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 295 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number 3.4.21.5 _Entity.Calc_isoelectric_point . _Entity.Formula_weight 33810 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 1A2C . "Structure Of Thrombin Inhibited By Aeruginosin298-a From A Blue-green Alga" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 2 no PDB 1A3B . "Complex Of Human Alpha-Thrombin With The Bifunctional Boronate Inhibitor Borolog1" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 3 no PDB 1A3E . "Complex Of Human Alpha-Thrombin With The Bifunctional Boronate Inhibitor Borolog2" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 4 no PDB 1A46 . "Thrombin Complexed With Hirugen And A Beta-Strand Mimetic Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 5 no PDB 1A4W . "Crystal Structures Of Thrombin With Thiazole-Containing Inhibitors: Probes Of The S1' Binding Site" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 6 no PDB 1A5G . "Human Thrombin Complexed With Novel Synthetic Peptide Mimetic Inhibitor And Hirugen" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 7 no PDB 1A61 . "Thrombin Complexed With A Beta-Mimetic Thiazole-Containing Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 8 no PDB 1ABI . "Structure Of The Hirulog 3-Thrombin Complex And Nature Of The S' Subsites Of Substrates And Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 9 no PDB 1ABJ . "Structure Of The Hirulog 3-Thrombin Complex And Nature Of The S' Subsites Of Substrates And Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 10 no PDB 1AD8 . "Complex Of Thrombin With And Inhibitor Containing A Novel P1 Moiety" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 11 no PDB 1AE8 . "Human Alpha-Thrombin Inhibition By Eoc-D-Phe-Pro-Azalys-Onp" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 12 no PDB 1AFE . "Human Alpha-Thrombin Inhibition By Cbz-Pro-Azalys-Onp" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 13 no PDB 1AHT . "Crystal Structure Of Human Alpha-Thrombin Complexed With Hirugen And P-Amidinophenylpyruvate At 1.6 Angstroms Resolution" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 14 no PDB 1AI8 . "Human Alpha-Thrombin Ternary Complex With The Exosite Inhibitor Hirugen And Active Site Inhibitor Phch2oco-D-Dpa-Pro-Borompg" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 15 no PDB 1AIX . "Human Alpha-Thrombin Ternary Complex With Exosite Inhibitor Hirugen And Active Site Inhibitor Phch2oco-D-Dpa-Pro-Boroval" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 16 no PDB 1AWF . "Novel Covalent Thrombin Inhibitor From Plant Extract" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 17 no PDB 1AWH . "Novel Covalent Thrombin Inhibitor From Plant Extract" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 18 no PDB 1AY6 . "Thrombin Inhibitor From Theonalla, Cyclotheanamide-Based Macrocyclic Tripeptide Motif" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 19 no PDB 1B5G . "Human Thrombin Complexed With Novel Synthetic Peptide Mimetic Inhibitor And Hirugen" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 20 no PDB 1B7X . "Structure Of Human Alpha-Thrombin Y225i Mutant Bound To D- Phe-Pro-Arg-Chloromethylketone" . . . . . 87.80 259 99.61 99.61 0.00e+00 . . . . 16940 1 21 no PDB 1BA8 . "Thrombin Inhibitor With A Rigid Tripeptidyl Aldehydes" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 22 no PDB 1BB0 . "Thrombin Inhibitors With Rigid Tripeptidyl Aldehydes" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 23 no PDB 1BCU . "Alpha-Thrombin Complexed With Hirugen And Proflavin" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 24 no PDB 1BMM . "Human Alpha-Thrombin Complexed With [s-(R,R)]-4-[(Aminoiminomethyl) Amino]-N-[[1-[3-Hydroxy-2-[(2-Naphthalenylsulfonyl)amino]-1" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 25 no PDB 1BMN . "Human Alpha-Thrombin Complexed With [s-(R,R)]-1-(Aminoiminomethyl)- N-[[1-[n-[(2-Naphthalenylsulfonyl)-L-Seryl]-Pyrrolidinyl]me" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 26 no PDB 1BTH . "Structure Of Thrombin Complexed With Bovine Pancreatic Trypsin Inhibitor" . . . . . 87.80 259 99.23 99.61 0.00e+00 . . . . 16940 1 27 no PDB 1C1U . "Recruiting Zinc To Mediate Potent, Specific Inhibition Of Serine Proteases" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 28 no PDB 1C1V . "Recruiting Zinc To Mediate Potent, Specific Inhibition Of Serine Proteases" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 29 no PDB 1C1W . "Recruiting Zinc To Mediate Potent, Specific Inhibition Of Serine Proteases" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 30 no PDB 1C4U . "Selective Non Electrophilic Thrombin Inhibitors With Cyclohexyl Moieties." . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 31 no PDB 1C4V . "Selective Non Electrophilic Thrombin Inhibitors With Cyclohexyl Moieties." . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 32 no PDB 1C4Y . "Selective Non-Electrophilic Thrombin Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 33 no PDB 1C5L . "Structural Basis For Selectivity Of A Small Molecule, S1-Binding, Sub- Micromolar Inhibitor Of Urokinase Type Plasminogen Activ" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 34 no PDB 1C5N . "Structural Basis For Selectivity Of A Small Molecule, S1-Binding, Sub- Micromolar Inhibitor Of Urokinase Type Plasminogen Activ" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 35 no PDB 1C5O . "Structural Basis For Selectivity Of A Small Molecule, S1-Binding, Sub- Micromolar Inhibitor Of Urokinase Type Plasminogen Activ" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 36 no PDB 1CA8 . "Thrombin Inhibitors With Rigid Tripeptidyl Aldehydes" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 37 no PDB 1D3D . "Crystal Structure Of Human Alpha Thrombin In Complex With Benzothiophene Inhibitor 4" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 38 no PDB 1D3P . "Crystal Structure Of Human Aplha-Thrombin In Complex With Benzo[b]thiophene Inhibitor 3" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 39 no PDB 1D3Q . "Crystal Structure Of Human Alpha Thrombin In Complex With Benzo[b]thiophene Inhibitor 2" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 40 no PDB 1D3T . "Crystal Structure Of Human Alpha Thrombin In Complex With Benzo[b]thiophene Inhibitor 1" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 41 no PDB 1D4P . "Crystal Structure Of Human Alpha Thrombin In Complex With 5- Amidinoindole-4-benzylpiperidine Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 42 no PDB 1D6W . "Structure Of Thrombin Complexed With Selective Non-Electrophilic Inhibitors Having Cyclohexyl Moieties At P1" . . . . . 97.29 287 100.00 100.00 0.00e+00 . . . . 16940 1 43 no PDB 1D9I . "Structure Of Thrombin Complexed With Selective Non-Electophilic Inhibitors Having Cyclohexyl Moieties At P1" . . . . . 97.63 288 100.00 100.00 0.00e+00 . . . . 16940 1 44 no PDB 1DE7 . "Interaction Of Factor Xiii Activation Peptide With Alpha-Thrombin: Crystal Structure Of The Enzyme-Substrate Complex" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 45 no PDB 1DIT . "Complex Of A Divalent Inhibitor With Thrombin" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 46 no PDB 1DM4 . "Ser195ala Mutant Of Human Thrombin Complexed With Fibrinopeptide A (7- 16)" . . . . . 88.14 260 99.62 100.00 0.00e+00 . . . . 16940 1 47 no PDB 1DOJ . "Crystal Structure Of Human Alpha-ThrombinRwj-51438 Complex At 1.7 A" . . . . . 100.00 295 100.00 100.00 0.00e+00 . . . . 16940 1 48 no PDB 1DWB . "Crystallographic Analysis At 3.0-angstroms Resolution Of The Binding To Human Thrombin Of Four Active Site-directed Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 49 no PDB 1DWC . "Crystallographic Analysis At 3.0-Angstroms Resolution Of The Binding To Human Thrombin Of Four Active Site-Directed Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 50 no PDB 1DWD . "Crystallographic Analysis At 3.0-Angstroms Resolution Of The Binding To Human Thrombin Of Four Active Site-Directed Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 51 no PDB 1DWE . "Crystallographic Analysis At 3.0-Angstroms Resolution Of The Binding To Human Thrombin Of Four Active Site-Directed Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 52 no PDB 1DX5 . "Crystal Structure Of The Thrombin-Thrombomodulin Complex" . . . . . 87.80 259 99.61 99.61 0.00e+00 . . . . 16940 1 53 no PDB 1E0F . "Crystal Structure Of The Human Alpha-Thrombin-Haemadin Complex: An Exosite Ii-Binding Inhibitor" . . . . . 87.80 259 99.61 99.61 0.00e+00 . . . . 16940 1 54 no PDB 1EB1 . "Complex Structure Of Human Thrombin With N-Methyl-Arginine Inhibitor" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 55 no PDB 1EOJ . "Design Of P1' And P3' Residues Of Trivalent Thrombin Inhibitors And Their Crystal Structures" . . . . . 97.97 289 99.65 99.65 0.00e+00 . . . . 16940 1 56 no PDB 1EOL . "Design Of P1' And P3' Residues Of Trivalent Thrombin Inhibitors And Their Crystal Structures" . . . . . 97.97 289 99.65 99.65 0.00e+00 . . . . 16940 1 57 no PDB 1FPC . "Active Site Mimetic Inhibition Of Thrombin" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 58 no PDB 1FPH . "The Interaction Of Thrombin With Fibrinogen: A Structural Basis For Its Specificity" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 59 no PDB 1G30 . "Thrombin Inhibitor Complex" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 60 no PDB 1G32 . "Thrombin Inhibitor Complex" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 61 no PDB 1G37 . "Crystal Structure Of Human Alpha-thrombin Complexed With Bch-10556 And Exosite-directed Peptide" . . . . . 97.29 287 100.00 100.00 0.00e+00 . . . . 16940 1 62 no PDB 1GHV . "A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network At The Active Site" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 63 no PDB 1GHW . "A Novel Serine Protease Inhibition Motif Involving A Multi-centered Short Hydrogen Bonding Network At The Active Site" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 64 no PDB 1GHX . "A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network At The Active Site" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 65 no PDB 1GHY . "A Novel Serine Protease Inhibition Motif Involving A Multi-Centered Short Hydrogen Bonding Network At The Active Site" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 66 no PDB 1GJ4 . "Selectivity At S1, H2o Displacement, Upa, Tpa, Ser190/ala190 Protease, Structure-based Drug Design" . . . . . 87.46 258 100.00 100.00 0.00e+00 . . . . 16940 1 67 no PDB 1GJ5 . "Selectivity At S1, H2o Displacement, Upa, Tpa, Ser190ALA190 PROTEASE, Structure-Based Drug Design" . . . . . 87.46 258 100.00 100.00 0.00e+00 . . . . 16940 1 68 no PDB 1H8D . "X-Ray Structure Of The Human Alpha-Thrombin Complex With A Tripeptide Phosphonate Inhibitor" . . . . . 87.46 260 97.29 97.29 0.00e+00 . . . . 16940 1 69 no PDB 1H8I . "X-Ray Crystal Structure Of Human Alpha-Thrombin With A Tripeptide Phosphonate Inhibitor" . . . . . 87.80 253 97.68 97.68 0.00e+00 . . . . 16940 1 70 no PDB 1HAG . "The Isomorphous Structures Of Prethrombin2, Hirugen-And Ppack- Thrombin: Changes Accompanying Activation And Exosite Binding To" . . . . . 100.00 295 100.00 100.00 0.00e+00 . . . . 16940 1 71 no PDB 1HAH . "The Isomorphous Structures Of Prethrombin2, Hirugen-And Ppack- Thrombin: Changes Accompanying Activation And Exosite Binding To" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 72 no PDB 1HAI . "The Isomorphous Structures Of Prethrombin2, Hirugen-And Ppack- Thrombin: Changes Accompanying Activation And Exosite Binding To" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 73 no PDB 1HAO . "Complex Of Human Alpha-thrombin With A 15mer Oligonucleotide Ggttggtgtggttgg (based On Nmr Model Of Dna)" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 74 no PDB 1HAP . "Complex Of Human Alpha-Thrombin With A 15mer Oligonucleotide Ggttggtgtggttgg (Based On X-Ray Model Of Dna)" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 75 no PDB 1HBT . "Human Alpha-Thrombin Complexed With A Peptidyl Pyridinium Methyl Ketone Containing Bivalent Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 76 no PDB 1HDT . "Structure Of A Retro-Binding Peptide Inhibitor Complexed With Human Alpha-Thrombin" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 77 no PDB 1HGT . "Structure Of The Hirugen And Hirulog 1 Complexes Of Alpha- Thrombin" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 78 no PDB 1HLT . "The Structure Of A Nonadecapeptide Of The Fifth Egf Domain Of Thrombomodulin Complexed With Thrombin" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 79 no PDB 1HUT . "The Structure Of Alpha-Thrombin Inhibited By A 15-Mer Single-Stranded Dna Aptamer" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 80 no PDB 1HXE . "Serine Protease" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 81 no PDB 1HXF . "Human Thrombin Complex With Hirudin Variant" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 82 no PDB 1IHS . "Crystal Structure Of The Complex Of Human Alpha-thrombin And Non- Hydrolyzable Bifunctional Inhibitors, Hirutonin-2 And Hiruton" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 83 no PDB 1IHT . "Crystal Structure Of The Complex Of Human Alpha-Thrombin And Non- Hydrolyzable Bifunctional Inhibitors, Hirutonin-2 And Hiruton" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 84 no PDB 1JMO . "Crystal Structure Of The Heparin Cofactor Ii-S195a Thrombin Complex" . . . . . 88.14 260 99.62 100.00 0.00e+00 . . . . 16940 1 85 no PDB 1JOU . "Crystal Structure Of Native S195a Thrombin With An Unoccupied Active Site" . . . . . 87.80 259 99.61 100.00 0.00e+00 . . . . 16940 1 86 no PDB 1JWT . "Crystal Structure Of Thrombin In Complex With A Novel Bicyclic Lactam Inhibitor" . . . . . 100.00 305 100.00 100.00 0.00e+00 . . . . 16940 1 87 no PDB 1K21 . "Human Thrombin-Inhibitor Complex" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 88 no PDB 1K22 . "Human Thrombin-inhibitor Complex" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 89 no PDB 1KTS . "Thrombin Inhibitor Complex" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 90 no PDB 1KTT . "Thrombin Inhibitor Complex" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 91 no PDB 1LHC . "Human Alpha-Thrombin Complexed With Ac-(D)phe-Pro-Boroarg-Oh" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 92 no PDB 1LHD . "Human Alpha-thrombin Complexed With Ac-(d)phe-pro-borolys-oh" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 93 no PDB 1LHE . "Human Alpha-Thrombin Complexed With Ac-(D)phe-Pro-Boro-N- Butyl-Amidino-Glycine-Oh" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 94 no PDB 1LHF . "Human Alpha-Thrombin Complexed With Ac-(D)phe-Pro-Boro- Homolys-Oh" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 95 no PDB 1LHG . "Human Alpha-Thrombin Complexed With Ac-(D)phe-Pro- Boroornithine-Oh" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 96 no PDB 1MH0 . "Crystal Structure Of The Anticoagulant Slow Form Of Thrombin" . . . . . 97.29 287 99.65 99.65 0.00e+00 . . . . 16940 1 97 no PDB 1MU6 . "Crystal Structure Of Thrombin In Complex With L-378,622" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 98 no PDB 1MU8 . Thrombin-Hirugen_l-378,650 . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 99 no PDB 1MUE . Thrombin-Hirugen-L405,426 . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 100 no PDB 1NM6 . "Thrombin In Complex With Selective Macrocyclic Inhibitor At 1.8a" . . . . . 97.29 287 100.00 100.00 0.00e+00 . . . . 16940 1 101 no PDB 1NO9 . "Design Of Weakly Basic Thrombin Inhibitors Incorporating Novel P1 Binding Functions: Molecular And X-Ray Crystallographic Studi" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 102 no PDB 1NRN . "Crystallographic Structures Of Thrombin Complexed With Thrombin Receptor Peptides: Existence Of Expected And Novel Binding Mode" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 103 no PDB 1NRO . "Crystallographic Structures Of Thrombin Complexed With Thrombin Receptor Peptides: Existence Of Expected And Novel Binding Mode" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 104 no PDB 1NRP . "Crystallographic Structures Of Thrombin Complexed With Thrombin Receptor Peptides: Existence Of Expected And Novel Binding Mode" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 105 no PDB 1NRQ . "Crystallographic Structures Of Thrombin Complexed With Thrombin Receptor Peptides: Existence Of Expected And Novel Binding Mode" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 106 no PDB 1NRR . "Crystallographic Structures Of Thrombin Complexed With Thrombin Receptor Peptides: Existence Of Expected And Novel Binding Mode" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 107 no PDB 1NRS . "Crystallographic Structures Of Thrombin Complexed With Thrombin Receptor Peptides: Existence Of Expected And Novel Binding Mode" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 108 no PDB 1NT1 . "Thrombin In Complex With Selective Macrocyclic Inhibitor" . . . . . 97.29 287 100.00 100.00 0.00e+00 . . . . 16940 1 109 no PDB 1NU7 . "Staphylocoagulase-Thrombin Complex" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 110 no PDB 1NU9 . "Staphylocoagulase-prethrombin-2 Complex" . . . . . 98.64 291 100.00 100.00 0.00e+00 . . . . 16940 1 111 no PDB 1NY2 . "Human Alpha Thrombin Inhibited By Rppgf And Hirugen" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 112 no PDB 1NZQ . "D-Phe-Pro-Arg-Type Thrombin Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 113 no PDB 1O0D . "Human Thrombin Complexed With A D-Phe-Pro-Arg-Type Inhibitor And A C- Terminal Hirudin Derived Exo-Site Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 114 no PDB 1O2G . "Elaborate Manifold Of Short Hydrogen Bond Arrays Mediating Binding Of Active Site-Directed Serine Protease Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 115 no PDB 1O5G . "Dissecting And Designing Inhibitor Selectivity Determinants At The S1 Site Using An Artificial Ala190 Protease (Ala190 Upa)" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 116 no PDB 1OOK . "Crystal Structure Of The Complex Of Platelet Receptor Gpib-alpha And Human Alpha-thrombin" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 117 no PDB 1OYT . "Complex Of Recombinant Human Thrombin With A Designed Fluorinated Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 118 no PDB 1P8V . "Crystal Structure Of The Complex Of Platelet Receptor Gpib-alpha And Alpha-thrombin At 2.6a" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 119 no PDB 1PPB . "The Refined 1.9 Angstroms Crystal Structure Of Human Alpha-Thrombin: Interaction With D-Phe-Pro-Arg Chloromethylketone And Sign" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 120 no PDB 1QBV . "Crystal Structure Of Thrombin Complexed With An Guanidine-Mimetic Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 121 no PDB 1QHR . "Novel Covalent Active Site Thrombin Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 122 no PDB 1QJ1 . "Novel Covalent Active Site Thrombin Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 123 no PDB 1QJ6 . "Novel Covalent Active Site Thrombin Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 124 no PDB 1QJ7 . "Novel Covalent Active Site Thrombin Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 125 no PDB 1QUR . "Human Alpha-Thrombin In Complex With Bivalent, Benzamidine-Based Synthetic Inhibitor" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 126 no PDB 1RD3 . "2.5a Structure Of Anticoagulant Thrombin Variant E217k" . . . . . 87.80 259 99.61 100.00 0.00e+00 . . . . 16940 1 127 no PDB 1SB1 . "Novel Non-Covalent Thrombin Inhibitors Incorporating P1 4,5,6,7- Tetrahydrobenzothiazole Arginine Side Chain Mimetics" . . . . . 87.46 258 100.00 100.00 0.00e+00 . . . . 16940 1 128 no PDB 1SFQ . "Fast Form Of Thrombin Mutant R(77a)a Bound To Ppack" . . . . . 87.80 259 99.61 99.61 0.00e+00 . . . . 16940 1 129 no PDB 1SG8 . "Crystal Structure Of The Procoagulant Fast Form Of Thrombin" . . . . . 87.80 259 99.61 99.61 0.00e+00 . . . . 16940 1 130 no PDB 1SGI . "Crystal Structure Of The Anticoagulant Slow Form Of Thrombin" . . . . . 87.80 259 99.61 99.61 0.00e+00 . . . . 16940 1 131 no PDB 1SHH . "Slow Form Of Thrombin Bound With Ppack" . . . . . 87.80 259 99.61 99.61 0.00e+00 . . . . 16940 1 132 no PDB 1SL3 . "Crystal Structue Of Thrombin In Complex With A Potent P1 Heterocycle- Aryl Based Inhibitor" . . . . . 97.29 287 100.00 100.00 0.00e+00 . . . . 16940 1 133 no PDB 1SR5 . "Antithrombin-anhydrothrombin-heparin Ternary Complex Structure" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 134 no PDB 1T4U . "Crystal Structure Analysis Of A Novel Oxyguanidine Bound To Thrombin" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 135 no PDB 1T4V . "Crystal Structure Analysis Of A Novel Oxyguanidine Bound To Thrombin" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 136 no PDB 1TA2 . "Crystal Structure Of Thrombin In Complex With Compound 1" . . . . . 97.29 287 100.00 100.00 0.00e+00 . . . . 16940 1 137 no PDB 1TA6 . "Crystal Structure Of Thrombin In Complex With Compound 14b" . . . . . 97.29 287 100.00 100.00 0.00e+00 . . . . 16940 1 138 no PDB 1TB6 . "2.5a Crystal Structure Of The Antithrombin-Thrombin-Heparin Ternary Complex" . . . . . 87.80 259 99.61 100.00 0.00e+00 . . . . 16940 1 139 no PDB 1TBZ . "Human Thrombin With Active Site N-Methyl-D Phenylalanyl-N-[5- (Aminoiminomethyl)amino]-1-{{benzothiazolyl)carbonyl] Butyl]-L- P" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 140 no PDB 1THP . "Structure Of Human Alpha-Thrombin Y225p Mutant Bound To D-Phe-Pro-Arg- Chloromethylketone" . . . . . 87.80 259 99.61 99.61 0.00e+00 . . . . 16940 1 141 no PDB 1THR . "Structures Of Thrombin Complexes With A Designed And A Natural Exosite Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 142 no PDB 1THS . "Structures Of Thrombin Complexes With A Designed And A Natural Exosite Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 143 no PDB 1TMB . "Molecular Basis For The Inhibition Of Human Alpha-thrombin By The Macrocyclic Peptide Cyclotheonamide A" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 144 no PDB 1TMT . "Changes In Interactions In Complexes Of Hirudin Derivatives And Human Alpha-Thrombin Due To Different Crystal Forms" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 145 no PDB 1TMU . "Changes In Interactions In Complexes Of Hirudin Derivatives And Human Alpha-Thrombin Due To Different Crystal Forms" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 146 no PDB 1TOM . "Alpha-Thrombin Complexed With Hirugen" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 147 no PDB 1TQ0 . "Crystal Structure Of The Potent Anticoagulant Thrombin Mutant W215aE217A IN FREE FORM" . . . . . 87.12 257 99.22 99.22 0.00e+00 . . . . 16940 1 148 no PDB 1TQ7 . "Crystal Structure Of The Anticoagulant Thrombin Mutant W215aE217A Bound To Ppack" . . . . . 87.12 257 99.22 99.22 0.00e+00 . . . . 16940 1 149 no PDB 1TWX . "Crystal Structure Of The Thrombin Mutant D221a/d222k" . . . . . 87.80 259 99.23 99.23 0.00e+00 . . . . 16940 1 150 no PDB 1UMA . "Alpha-Thrombin (Hirugen) Complexed With Na-(N,N-Dimethylcarbamoyl)- Alpha-Azalysine" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 151 no PDB 1UVS . "Bovine Thrombin--Bm51.1011 Complex" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 152 no PDB 1VR1 . "Specifity For Plasminogen Activator Inhibitor-1" . . . . . 88.47 261 96.93 97.32 0.00e+00 . . . . 16940 1 153 no PDB 1W7G . "Alpha-Thrombin Complex With Sulfated Hirudin (Residues 54-65) And L- Arginine Template Inhibitor Cs107" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 154 no PDB 1WAY . "Active Site Thrombin Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 155 no PDB 1WBG . "Active Site Thrombin Inhibitors" . . . . . 87.80 259 99.23 99.23 0.00e+00 . . . . 16940 1 156 no PDB 1XM1 . "Nonbasic Thrombin Inhibitor Complex" . . . . . 100.00 295 100.00 100.00 0.00e+00 . . . . 16940 1 157 no PDB 1XMN . "Crystal Structure Of Thrombin Bound To Heparin" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 158 no PDB 1YPE . "Thrombin Inhibitor Complex" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 159 no PDB 1YPG . "Thrombin Inhibitor Complex" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 160 no PDB 1YPJ . "Thrombin Inhibitor Complex" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 161 no PDB 1YPK . "Thrombin Inhibitor Complex" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 162 no PDB 1YPL . "X-ray Crystal Structure Of Thrombin Inhibited By Synthetic Cyanopeptide Analogue Ra-1008" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 163 no PDB 1YPM . "X-ray Crystal Structure Of Thrombin Inhibited By Synthetic Cyanopeptide Analogue Ra-1014" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 164 no PDB 1Z71 . "Thrombin And P2 Pyridine N-oxide Inhibitor Complex Structure" . . . . . 97.29 287 100.00 100.00 0.00e+00 . . . . 16940 1 165 no PDB 1Z8I . "Crystal Structure Of The Thrombin Mutant G193a Bound To Ppack" . . . . . 87.80 259 99.61 99.61 0.00e+00 . . . . 16940 1 166 no PDB 1Z8J . "Crystal Structure Of The Thrombin Mutant G193p Bound To Ppack" . . . . . 87.80 259 99.61 99.61 0.00e+00 . . . . 16940 1 167 no PDB 1ZGI . "Thrombin In Complex With An Oxazolopyridine Inhibitor 21" . . . . . 97.29 287 100.00 100.00 0.00e+00 . . . . 16940 1 168 no PDB 1ZGV . "Thrombin In Complex With An Oxazolopyridine Inhibitor 2" . . . . . 97.29 287 100.00 100.00 0.00e+00 . . . . 16940 1 169 no PDB 1ZRB . "Thrombin In Complex With An Azafluorenyl Inhibitor 23b" . . . . . 97.29 287 100.00 100.00 0.00e+00 . . . . 16940 1 170 no PDB 2A0Q . "Structure Of Thrombin In 400 Mm Potassium Chloride" . . . . . 87.12 257 99.61 99.61 0.00e+00 . . . . 16940 1 171 no PDB 2A2X . "Orally Active Thrombin Inhibitors In Complex With Thrombin Inh12" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 172 no PDB 2A45 . 'Crystal Structure Of The Complex Between Thrombin And The Central "e" Region Of Fibrin' . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 173 no PDB 2AFQ . "1.9 Angstrom Crytal Structure Of Wild-Type Human Thrombin In The Sodium Free State" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 174 no PDB 2ANK . "Orally Active Thrombin Inhibitors In Complex With Thrombin And An Exosite Decapeptide" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 175 no PDB 2ANM . "Ternary Complex Of An Orally Active Thrombin Inhibitor With Human Thrombin And A C-Terminal Hirudin Derived Exo-Sit Inhibitor" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 176 no PDB 2B5T . "2.1 Angstrom Structure Of A Nonproductive Complex Between Antithrombin, Synthetic Heparin Mimetic Sr123781 And Two S195a Thromb" . . . . . 87.80 259 99.61 100.00 0.00e+00 . . . . 16940 1 177 no PDB 2BDY . "Thrombin In Complex With Inhibitor" . . . . . 97.97 289 100.00 100.00 0.00e+00 . . . . 16940 1 178 no PDB 2BVR . "Human Thrombin Complexed With Fragment-based Small Molecules Occupying The S1 Pocket" . . . . . 87.80 252 97.30 97.30 0.00e+00 . . . . 16940 1 179 no PDB 2BVS . "Human Thrombin Complexed With Fragment-Based Small Molecules Occupying The S1 Pocket" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 180 no PDB 2BVX . "Design And Discovery Of Novel, Potent Thrombin Inhibitors With A Solubilizing Cationic P1-P2-Linker" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 181 no PDB 2BXT . "Design And Discovery Of Novel, Potent Thrombin Inhibitors With A Solubilizing Cationic P1-p2-linker" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 182 no PDB 2BXU . "Design And Discovery Of Novel, Potent Thrombin Inhibitors With A Solubilizing Cationic P1-p2-linker" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 183 no PDB 2C8W . "Thrombin Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 184 no PDB 2C8X . "Thrombin Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 185 no PDB 2C8Y . "Thrombin Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 186 no PDB 2C8Z . "Thrombin Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 187 no PDB 2C90 . "Thrombin Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 188 no PDB 2C93 . "Thrombin Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 189 no PDB 2CF8 . "Complex Of Recombinant Human Thrombin With A Inhibitor" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 190 no PDB 2CF9 . "Complex Of Recombinant Human Thrombin With A Inhibitor" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 191 no PDB 2CN0 . "Complex Of Recombinant Human Thrombin With A Designed Inhibitor" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 192 no PDB 2FEQ . "Orally Active Thrombin Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 193 no PDB 2FES . "Orally Active Thrombin Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 194 no PDB 2GDE . "Thrombin In Complex With Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 195 no PDB 2GP9 . "Crystal Structure Of The Slow Form Of Thrombin In A Self- Inhibited Conformation" . . . . . 87.80 259 99.61 100.00 0.00e+00 . . . . 16940 1 196 no PDB 2H9T . "Crystal Structure Of Human Alpha-Thrombin In Complex With Suramin" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 197 no PDB 2HGT . "Structure Of The Hirugen And Hirulog 1 Complexes Of Alpha-Thrombin" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 198 no PDB 2HPP . "Structures Of The Noncovalent Complexes Of Human And Bovine Prothrombin Fragment 2 With Human Ppack-Thrombin" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 199 no PDB 2HPQ . "Structures Of The Noncovalent Complexes Of Human And Bovine Prothrombin Fragment 2 With Human Ppack-thrombin" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 200 no PDB 2HWL . "Crystal Structure Of Thrombin In Complex With Fibrinogen Gamma' Peptide" . . . . . 87.80 259 99.61 99.61 0.00e+00 . . . . 16940 1 201 no PDB 2JH0 . "Human Thrombin Hirugen Inhibitor Complex" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 202 no PDB 2JH5 . "Human Thrombin Hirugen Inhibitor Complex" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 203 no PDB 2JH6 . "Human Thrombin Hirugen Inhibitor Complex" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 204 no PDB 2OD3 . "Human Thrombin Chimera With Human Residues 184a, 186, 186a, 186b, 186c And 222 Replaced By Murine Thrombin Equivalents" . . . . . 87.80 259 97.68 98.84 0.00e+00 . . . . 16940 1 205 no PDB 2PGB . "Inhibitor-Free Human Thrombin Mutant C191a-C220a" . . . . . 87.80 259 99.23 99.23 0.00e+00 . . . . 16940 1 206 no PDB 2PGQ . "Human Thrombin Mutant C191a-c220a In Complex With The Inhibitor Ppack" . . . . . 87.80 259 99.23 99.23 0.00e+00 . . . . 16940 1 207 no PDB 2PW8 . "Crystal Structure Of Sulfo-Hirudin Complexed To Thrombin" . . . . . 87.46 258 100.00 100.00 0.00e+00 . . . . 16940 1 208 no PDB 2R2M . "2-(2-chloro-6-fluorophenyl)acetamides As Potent Thrombin Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 209 no PDB 2THF . "Structure Of Human Alpha-thrombin Y225f Mutant Bound To D-phe-pro-arg- Chloromethylketone" . . . . . 87.80 259 99.61 100.00 0.00e+00 . . . . 16940 1 210 no PDB 2UUF . "Thrombin-hirugen Binary Complex At 1.26a Resolution" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 211 no PDB 2UUJ . "Thrombin-hirugen-gw473178 Ternary Complex At 1.32a Resolution" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 212 no PDB 2UUK . "Thrombin-hirugen-gw420128 Ternary Complex At 1.39a Resolution" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 213 no PDB 2V3H . "Thrombin With 3-cycle No F" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 214 no PDB 2V3O . "Thrombin With 3-cycle With F" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 215 no PDB 2ZC9 . "Thrombin In Complex With Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 216 no PDB 2ZDA . "Exploring Thrombin S1 Pocket" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 217 no PDB 2ZDV . "Exploring Thrombin S1 Pocket" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 218 no PDB 2ZF0 . "Exploring Thrombin S1 Pocket" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 219 no PDB 2ZFF . "Exploring Thrombin S1-pocket" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 220 no PDB 2ZFP . "Thrombin Inibition" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 221 no PDB 2ZFQ . "Exploring Thrombin S3 Pocket" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 222 no PDB 2ZFR . "Exploring Thrombin S3 Pocket" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 223 no PDB 2ZG0 . "Exploring Thrombin S3 Pocket" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 224 no PDB 2ZGB . "Thrombin Inhibition" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 225 no PDB 2ZGX . "Thrombin Inhibition" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 226 no PDB 2ZHE . "Exploring Thrombin S3 Pocket" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 227 no PDB 2ZHF . "Exploring Thrombin S3 Pocket" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 228 no PDB 2ZHQ . "Thrombin Inhibition" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 229 no PDB 2ZHW . "Exploring Thrombin S3 Pocket" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 230 no PDB 2ZI2 . "Thrombin Inhibition" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 231 no PDB 2ZIQ . "Thrombin Inhibition" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 232 no PDB 2ZNK . "Thrombin Inhibition" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 233 no PDB 2ZO3 . "Bisphenylic Thrombin Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 234 no PDB 3B23 . "Crystal Structure Of Thrombin-Variegin Complex: Insights Of A Novel Mechanism Of Inhibition And Design Of Tunable Thrombin Inhi" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 235 no PDB 3B9F . "1.6 A Structure Of The Pci-Thrombin-Heparin Complex" . . . . . 87.80 259 99.61 100.00 0.00e+00 . . . . 16940 1 236 no PDB 3BEF . "Crystal Structure Of Thrombin Bound To The Extracellular Fragment Of Par1" . . . . . 87.80 259 99.61 100.00 0.00e+00 . . . . 16940 1 237 no PDB 3BEI . "Crystal Structure Of The Slow Form Of Thrombin In A Self_inhibited Conformation" . . . . . 87.80 259 99.61 100.00 0.00e+00 . . . . 16940 1 238 no PDB 3BF6 . "Thrombin:suramin Complex" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 239 no PDB 3BIU . "Human Thrombin-In Complex With Ub-Thr10" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 240 no PDB 3BIV . "Human Thrombin-In Complex With Ub-Thr11" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 241 no PDB 3BV9 . "Structure Of Thrombin Bound To The Inhibitor Fm19" . . . . . 87.80 259 99.61 99.61 0.00e+00 . . . . 16940 1 242 no PDB 3C1K . "Crystal Structure Of Thrombin In Complex With Inhibitor 15" . . . . . 97.29 287 100.00 100.00 0.00e+00 . . . . 16940 1 243 no PDB 3C27 . "Cyanofluorophenylacetamides As Orally Efficacious Thrombin Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 244 no PDB 3D49 . "Thrombin Inhibition" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 245 no PDB 3DA9 . "Crystal Structure Of Thrombin In Complex With Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 246 no PDB 3DD2 . "Crystal Structure Of An Rna Aptamer Bound To Human Thrombin" . . . . . 87.46 258 100.00 100.00 0.00e+00 . . . . 16940 1 247 no PDB 3DHK . "Bisphenylic Thrombin Inhibitors" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 248 no PDB 3DT0 . "Understanding Thrombin Inhibition" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 249 no PDB 3DUX . "Understanding Thrombin Inhibition" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 250 no PDB 3E6P . "Crystal Structure Of Human Meizothrombin Desf1" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 251 no PDB 3EE0 . "Crystal Structure Of The W215aE217A MUTANT OF HUMAN Thrombin (Space Group P2(1)2(1)2(1))" . . . . . 87.80 259 99.23 99.23 0.00e+00 . . . . 16940 1 252 no PDB 3EGK . "Knoble Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 253 no PDB 3EQ0 . "Thrombin Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 254 no PDB 3F68 . "Thrombin Inhibition" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 255 no PDB 3GIS . "Crystal Structure Of Na-Free Thrombin In Complex With Thrombomodulin" . . . . . 87.80 259 99.61 100.00 0.00e+00 . . . . 16940 1 256 no PDB 3HAT . "Active Site Mimetic Inhibition Of Thrombin" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 257 no PDB 3HKJ . "Crystal Structure Of Human Thrombin Mutant W215aE217A IN COMPLEX WITH The Extracellular Fragment Of Human Par1" . . . . . 87.80 259 99.23 99.23 0.00e+00 . . . . 16940 1 258 no PDB 3HTC . "The Structure Of A Complex Of Recombinant Hirudin And Human Alpha-Thrombin" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 259 no PDB 3JZ1 . "Crystal Structure Of Human Thrombin Mutant N143p In E:na+ Form" . . . . . 87.80 259 99.61 99.61 0.00e+00 . . . . 16940 1 260 no PDB 3JZ2 . "Crystal Structure Of Human Thrombin Mutant N143p In E Form" . . . . . 87.80 259 99.61 99.61 0.00e+00 . . . . 16940 1 261 no PDB 3K65 . "Crystal Structure Of Prethombin-2/fragment-2 Complex" . . . . . 100.00 308 99.66 100.00 0.00e+00 . . . . 16940 1 262 no PDB 3LDX . "Discovery And Clinical Evaluation Of Rwj-671818, A Thrombin Inhibitor With An Oxyguanidine P1 Motif" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 263 no PDB 3LU9 . "Crystal Structure Of Human Thrombin Mutant S195a In Complex Extracellular Fragment Of Human Par1" . . . . . 87.80 259 99.61 100.00 0.00e+00 . . . . 16940 1 264 no PDB 3NXP . "Crystal Structure Of Human Prethrombin-1" . . . . . 100.00 424 100.00 100.00 0.00e+00 . . . . 16940 1 265 no PDB 3P17 . "Thrombin Inhibition By Pyridin Derivatives" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 266 no PDB 3P6Z . "Structural Basis Of Thrombin Mediated Factor V Activation: Essential Role Of The Hirudin-Like Sequence Glu666-Glu672 For Proces" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 267 no PDB 3P70 . "Structural Basis Of Thrombin-Mediated Factor V Activation: Essential Role Of The Hirudin-Like Sequence Glu666-Glu672 For Proces" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 268 no PDB 3PMH . "Mechanism Of Sulfotyrosine-Mediated Glycoprotein Ib Interaction With Two Distinct Alpha-Thrombin Sites" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 269 no PDB 3QDZ . "Crystal Structure Of The Human Thrombin Mutant D102n In Complex With The Extracellular Fragment Of Human Par4." . . . . . 87.80 259 99.61 100.00 0.00e+00 . . . . 16940 1 270 no PDB 3QGN . "The Allosteric E-E Equilibrium Is A Key Property Of The Trypsin Fold" . . . . . 87.80 259 99.61 99.61 0.00e+00 . . . . 16940 1 271 no PDB 3QLP . "X-Ray Structure Of The Complex Between Human Alpha Thrombin And A Modified Thrombin Binding Aptamer (Mtba)" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 272 no PDB 3QTO . "Thrombin Inhibition By Pyridin Derivatives" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 273 no PDB 3QTV . "Thrombin Inhibition By Pyridin Derivatives" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 274 no PDB 3QWC . "Thrombin Inhibition By Pyridin Derivatives" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 275 no PDB 3QX5 . "Thrombin Inhibition By Pyridin Derivatives" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 276 no PDB 3R3G . "Structure Of Human Thrombin With Residues 145-150 Of Murine Thrombin" . . . . . 87.80 259 97.68 98.84 0.00e+00 . . . . 16940 1 277 no PDB 3RLW . "Human Thrombin In Complex With Mi328" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 278 no PDB 3RLY . "Human Thrombin In Complex With Mi329" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 279 no PDB 3RM0 . "Human Thrombin In Complex With Mi354" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 280 no PDB 3RM2 . "Human Thrombin In Complex With Mi003" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 281 no PDB 3RML . "Human Thrombin In Complex With Mi331" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 282 no PDB 3RMM . "Human Thrombin In Complex With Mi332" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 283 no PDB 3RMN . "Human Thrombin In Complex With Mi341" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 284 no PDB 3RMO . "Human Thrombin In Complex With Mi004" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 285 no PDB 3S7H . "Structure Of Thrombin Mutant Y225p In The E Form" . . . . . 87.80 259 99.61 99.61 0.00e+00 . . . . 16940 1 286 no PDB 3S7K . "Structure Of Thrombin Mutant Y225p In The E Form" . . . . . 87.80 259 99.61 99.61 0.00e+00 . . . . 16940 1 287 no PDB 3SHA . "Human Thrombin In Complex With Ubthr97" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 288 no PDB 3SHC . "Human Thrombin In Complex With Ubthr101" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 289 no PDB 3SI3 . "Human Thrombin In Complex With Ubthr103" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 290 no PDB 3SI4 . "Human Thrombin In Complex With Ubthr104" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 291 no PDB 3SQE . "Crystal Structure Of Prethrombin-2 Mutant S195a In The Alternative Form" . . . . . 98.31 290 99.66 100.00 0.00e+00 . . . . 16940 1 292 no PDB 3SQH . "Crystal Structure Of Prethrombin-2 Mutant S195a In The The Open Form" . . . . . 98.31 290 99.66 100.00 0.00e+00 . . . . 16940 1 293 no PDB 3SV2 . "Human Thrombin In Complex With Ubthr105" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 294 no PDB 3T5F . "Human Thrombin In Complex With Mi340" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 295 no PDB 3TU7 . "Human Alpha-Thrombin Complexed With N-(Methylsulfonyl)-D-Phenylalanyl- N-((1-Carbamimidoyl-4-Piperidinyl)methyl)-L-Prolinamide " . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 296 no PDB 3U69 . "Unliganded Wild-Type Human Thrombin" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 297 no PDB 3U8O . "Human Thrombin Complexed With D-phe-pro-d-arg-d-thr" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 298 no PDB 3U8R . "Human Thrombin Complexed With D-phe-pro-d-arg-ile" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 299 no PDB 3U8T . "Human Thrombin Complexed With D-phe-pro-d-arg-cys" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 300 no PDB 3U98 . "Human Thrombin In Complex With Mi001" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 301 no PDB 3U9A . "Human Thrombin In Complex With Mi330" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 302 no PDB 3UTU . "High Affinity Inhibitor Of Human Thrombin" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 303 no PDB 3UWJ . "Human Thrombin In Complex With Mi353" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 304 no PDB 3VXE . "Human Alpha-thrombin-bivalirudin Complex At Pd5.0" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 305 no PDB 3VXF . "X/n Joint Refinement Of Human Alpha-thrombin-bivalirudin Complex Pd5" . . . . . 87.46 259 100.00 100.00 0.00e+00 . . . . 16940 1 306 no PDB 4AX9 . "Human Thrombin Complexed With Napsagatran, Ro0466240" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 307 no PDB 4AYV . "Human Thrombin - Inhibitor Complex" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 308 no PDB 4AYY . "Human Thrombin - Inhibitor Complex" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 309 no PDB 4AZ2 . "Human Thrombin - Inhibitor Complex" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 310 no PDB 4BAH . "Thrombin In Complex With Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 311 no PDB 4BAK . "Thrombin In Complex With Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 312 no PDB 4BAM . "Thrombin In Complex With Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 313 no PDB 4BAN . "Thrombin In Complex With Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 314 no PDB 4BAO . "Thrombin In Complex With Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 315 no PDB 4BAQ . "Thrombin In Complex With Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 316 no PDB 4BOH . "Madanins (merops I53) Are Cleaved By Thrombin And Factor Xa" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 317 no PDB 4CH2 . "Low-salt Crystal Structure Of A Thrombin-gpibalpha Peptide Complex" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 318 no PDB 4CH8 . "High-salt Crystal Structure Of A Thrombin-gpibalpha Peptide Complex" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 319 no PDB 4DIH . "X-Ray Structure Of The Complex Between Human Alpha Thrombin And Thrombin Binding Aptamer In The Presence Of Sodium Ions" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 320 no PDB 4DII . "X-Ray Structure Of The Complex Between Human Alpha Thrombin And Thrombin Binding Aptamer In The Presence Of Potassium Ions" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 321 no PDB 4DT7 . "Crystal Structure Of Thrombin Bound To The Activation Domain Qedqvdprlidgkmtrrgds Of Protein C" . . . . . 87.80 259 99.61 100.00 0.00e+00 . . . . 16940 1 322 no PDB 4DY7 . "Crystal Structures Of Protease Nexin-1 In Complex With S195a Thrombin" . . . . . 87.80 259 99.61 100.00 0.00e+00 . . . . 16940 1 323 no PDB 4E05 . "Anophelin From The Malaria Vector Inhibits Thrombin Through A Novel Reverse-Binding Mechanism" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 324 no PDB 4E06 . "Anophelin From The Malaria Vector Inhibits Thrombin Through A Novel Reverse-Binding Mechanism" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 325 no PDB 4E7R . "Thrombin In Complex With 3-Amidinophenylalanine Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 326 no PDB 4H6S . "Crystal Structure Of Thrombin Mutant E14ea/d14la/e18a/s195a" . . . . . 87.80 259 99.23 99.61 0.00e+00 . . . . 16940 1 327 no PDB 4H6T . "Crystal Structure Of Prethrombin-2 Mutant E14ea/d14la/e18a/s195a" . . . . . 100.00 306 98.64 98.98 0.00e+00 . . . . 16940 1 328 no PDB 4HFP . "Structure Of Thrombin Mutant S195a Bound To The Active Site Inhibitor Argatroban" . . . . . 87.80 259 99.61 100.00 0.00e+00 . . . . 16940 1 329 no PDB 4HTC . "The Refined Structure Of The Hirudin-Thrombin Complex" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 330 no PDB 4HZH . "Structure Of Recombinant Gla-domainless Prothrombin Mutant S525a" . . . . . 100.00 533 99.66 100.00 0.00e+00 . . . . 16940 1 331 no PDB 4I7Y . "Crystal Structure Of Human Alpha Thrombin In Complex With A 27-mer Aptamer Bound To Exosite Ii" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 332 no PDB 4LOY . "Crystal Structure Analysis Of Thrombin In Complex With Compound D57, 5-chlorothiophene-2-carboxylic Acid [(s)-2-[2-methyl-3-(2-" . . . . . 87.12 257 100.00 100.00 0.00e+00 . . . . 16940 1 333 no PDB 4LXB . "Crystal Structure Analysis Of Thrombin In Complex With Compound D58" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 334 no PDB 4LZ1 . "X-ray Structure Of The Complex Between Human Thrombin And The Tba Deletion Mutant Lacking Thymine 12 Nucleobase" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 335 no PDB 4LZ4 . "X-ray Structure Of The Complex Between Human Thrombin And The Tba Deletion Mutant Lacking Thymine 3 Nucleobase" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 336 no PDB 4MLF . "Crystal Structure For The Complex Of Thrombin Mutant D102n And Hirudin" . . . . . 87.80 259 99.61 100.00 0.00e+00 . . . . 16940 1 337 no PDB 4N3L . "Crystal Structure Of Thrombin In Complex With A Novel Glucose- Conjugated Potent Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 338 no PDB 4NZE . "Crystal Structure Of Thrombin In Complex With A Novel Tetra-o-acetyl- Glucopyranoside-conjugated Potent Inhibitor" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 339 no PDB 4NZQ . "Crystal Structure Of Ca2+-free Prothrombin Deletion Mutant Residues 146-167" . . . . . 100.00 557 100.00 100.00 0.00e+00 . . . . 16940 1 340 no PDB 4O03 . "Crystal Structure Of Ca2+ Bound Prothrombin Deletion Mutant Residues 146-167" . . . . . 100.00 557 100.00 100.00 0.00e+00 . . . . 16940 1 341 no PDB 4RKJ . "Crystal Structure Of Thrombin Mutant S195t (free Form)" . . . . . 87.80 259 99.61 100.00 0.00e+00 . . . . 16940 1 342 no PDB 4RKO . "Crystal Structure Of Thrombin Mutant S195t Bound With Ppack" . . . . . 87.80 259 99.61 100.00 0.00e+00 . . . . 16940 1 343 no PDB 4RN6 . "Structure Of Prethrombin-2 Mutant S195a Bound To The Active Site Inhibitor Argatroban" . . . . . 98.31 290 99.66 100.00 0.00e+00 . . . . 16940 1 344 no PDB 4THN . "The Crystal Structure Of Alpha-Thrombin-Hirunorm Iv Complex Reveals A Novel Specificity Site Recognition Mode." . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 345 no PDB 4UD9 . "Thrombin In Complex With 5-chlorothiophene-2-carboxamide" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 346 no PDB 4UDW . "Thrombin In Complex With 1-(2r)-2-amino-3-phenyl-propanoyl- N-(2,5dichlorophenyl)methylpyrrolidine-2-carboxamide" . . . . . 87.46 258 100.00 100.00 0.00e+00 . . . . 16940 1 347 no PDB 4UE7 . "Thrombin In Complex With 1-amidinopiperidine" . . . . . 87.46 258 100.00 100.00 0.00e+00 . . . . 16940 1 348 no PDB 4UEH . "Thrombin In Complex With Benzamidine" . . . . . 87.46 258 100.00 100.00 0.00e+00 . . . . 16940 1 349 no PDB 4YES . "Thrombin In Complex With (s)-(4-chloro-2-((1-(5-methyl-1h-pyrrole-2- Carbonyl)pyrrolidine-2-carboxamido)methyl)phenyl)methanami" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 350 no PDB 5AF9 . "Thrombin In Complex With 4-methoxy-n-(2-pyridinyl)benzamide" . . . . . 87.46 258 100.00 100.00 0.00e+00 . . . . 16940 1 351 no PDB 5AFY . "Thrombin In Complex With 3-chloro-benzamide" . . . . . 87.46 258 100.00 100.00 0.00e+00 . . . . 16940 1 352 no PDB 5AFZ . "Thrombin In Complex With (2r)-2-(benzylsulfonylamino)-n-(2-((4-carbamimidoylphenyl)methylamino)-2-oxo-propyl)-3-phenyl- Propana" . . . . . 87.46 258 100.00 100.00 0.00e+00 . . . . 16940 1 353 no PDB 5AHG . "Thrombin In Complex With ((4-chlorophenyl)sulfamoyl)) Diemethylamine" . . . . . 87.46 258 100.00 100.00 0.00e+00 . . . . 16940 1 354 no PDB 5GDS . "Hirunorms Are True Hirudin Mimetics. The Crystal Structure Of Human Alpha-Thrombin:hirunorm V Complex" . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 355 no PDB 7KME . "Crystal Structure Of Human Alpha-Thrombin Inhibited With Sel2711." . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 356 no PDB 8KME . "Crystal Structure Of Human Alpha-thrombin Inhibited With Sel2770." . . . . . 87.80 259 100.00 100.00 0.00e+00 . . . . 16940 1 357 no DBJ BAD96495 . "coagulation factor II precursor variant [Homo sapiens]" . . . . . 100.00 622 99.66 99.66 0.00e+00 . . . . 16940 1 358 no DBJ BAD96497 . "coagulation factor II precursor variant [Homo sapiens]" . . . . . 100.00 622 100.00 100.00 0.00e+00 . . . . 16940 1 359 no DBJ BAG35804 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 622 100.00 100.00 0.00e+00 . . . . 16940 1 360 no DBJ BAG56844 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 471 100.00 100.00 0.00e+00 . . . . 16940 1 361 no DBJ BAG64719 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 605 100.00 100.00 0.00e+00 . . . . 16940 1 362 no EMBL CAA23842 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 615 100.00 100.00 0.00e+00 . . . . 16940 1 363 no EMBL CAH93129 . "hypothetical protein [Pongo abelii]" . . . . . 100.00 623 98.98 99.32 0.00e+00 . . . . 16940 1 364 no EMBL CAJ01369 . "prothrombin [Homo sapiens]" . . . . . 100.00 622 100.00 100.00 0.00e+00 . . . . 16940 1 365 no GB AAC63054 . "prothrombin [Homo sapiens]" . . . . . 100.00 622 100.00 100.00 0.00e+00 . . . . 16940 1 366 no GB AAH51332 . "Coagulation factor II (thrombin) [Homo sapiens]" . . . . . 100.00 622 100.00 100.00 0.00e+00 . . . . 16940 1 367 no GB AAL77436 . "coagulation factor II (thrombin) [Homo sapiens]" . . . . . 100.00 622 100.00 100.00 0.00e+00 . . . . 16940 1 368 no GB AAR08142 . "prothrombin [Homo sapiens]" . . . . . 100.00 295 99.32 99.32 0.00e+00 . . . . 16940 1 369 no GB AAR08143 . "prothrombin B-chain [Homo sapiens]" . . . . . 87.80 259 99.23 99.23 0.00e+00 . . . . 16940 1 370 no REF NP_000497 . "prothrombin isoform 1 preproprotein [Homo sapiens]" . . . . . 100.00 622 100.00 100.00 0.00e+00 . . . . 16940 1 371 no REF NP_001126851 . "prothrombin precursor [Pongo abelii]" . . . . . 100.00 623 98.98 99.32 0.00e+00 . . . . 16940 1 372 no REF NP_001298186 . "prothrombin isoform 2 [Homo sapiens]" . . . . . 100.00 606 100.00 100.00 0.00e+00 . . . . 16940 1 373 no REF XP_001165233 . "PREDICTED: prothrombin isoform X1 [Pan troglodytes]" . . . . . 100.00 622 100.00 100.00 0.00e+00 . . . . 16940 1 374 no REF XP_003815248 . "PREDICTED: prothrombin [Pan paniscus]" . . . . . 100.00 622 100.00 100.00 0.00e+00 . . . . 16940 1 375 no SP P00734 . "RecName: Full=Prothrombin; AltName: Full=Coagulation factor II; Contains: RecName: Full=Activation peptide fragment 1; Contains" . . . . . 100.00 622 100.00 100.00 0.00e+00 . . . . 16940 1 376 no SP Q5R537 . "RecName: Full=Prothrombin; AltName: Full=Coagulation factor II; Contains: RecName: Full=Activation peptide fragment 1; Contains" . . . . . 100.00 623 98.98 99.32 0.00e+00 . . . . 16940 1 stop_ loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'Thrombin is the main protease of the blood coagulation system' 16940 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 1 285 THR . 16940 1 2 286 PHE . 16940 1 3 287 GLY . 16940 1 4 288 SER . 16940 1 5 289 GLY . 16940 1 6 290 GLU . 16940 1 7 291 ALA . 16940 1 8 292 ASP . 16940 1 9 293 CYS . 16940 1 10 294 GLY . 16940 1 11 295 LEU . 16940 1 12 296 ARG . 16940 1 13 297 PRO . 16940 1 14 298 LEU . 16940 1 15 299 PHE . 16940 1 16 300 GLU . 16940 1 17 301 LYS . 16940 1 18 302 LYS . 16940 1 19 303 SER . 16940 1 20 304 LEU . 16940 1 21 305 GLU . 16940 1 22 306 ASP . 16940 1 23 307 LYS . 16940 1 24 308 THR . 16940 1 25 309 GLU . 16940 1 26 310 ARG . 16940 1 27 311 GLU . 16940 1 28 312 LEU . 16940 1 29 313 LEU . 16940 1 30 314 GLU . 16940 1 31 315 SER . 16940 1 32 316 TYR . 16940 1 33 317 ILE . 16940 1 34 318 ASP . 16940 1 35 319 GLY . 16940 1 36 320 ARG . 16940 1 37 321 ILE . 16940 1 38 322 VAL . 16940 1 39 323 GLU . 16940 1 40 324 GLY . 16940 1 41 325 SER . 16940 1 42 326 ASP . 16940 1 43 327 ALA . 16940 1 44 328 GLU . 16940 1 45 329 ILE . 16940 1 46 330 GLY . 16940 1 47 331 MET . 16940 1 48 332 SER . 16940 1 49 333 PRO . 16940 1 50 334 TRP . 16940 1 51 335 GLN . 16940 1 52 336 VAL . 16940 1 53 337 MET . 16940 1 54 338 LEU . 16940 1 55 339 PHE . 16940 1 56 340 ARG . 16940 1 57 341 LYS . 16940 1 58 342 SER . 16940 1 59 343 PRO . 16940 1 60 344 GLN . 16940 1 61 345 GLU . 16940 1 62 346 LEU . 16940 1 63 347 LEU . 16940 1 64 348 CYS . 16940 1 65 349 GLY . 16940 1 66 350 ALA . 16940 1 67 351 SER . 16940 1 68 352 LEU . 16940 1 69 353 ILE . 16940 1 70 354 SER . 16940 1 71 355 ASP . 16940 1 72 356 ARG . 16940 1 73 357 TRP . 16940 1 74 358 VAL . 16940 1 75 359 LEU . 16940 1 76 360 THR . 16940 1 77 361 ALA . 16940 1 78 362 ALA . 16940 1 79 363 HIS . 16940 1 80 364 CYS . 16940 1 81 365 LEU . 16940 1 82 366 LEU . 16940 1 83 367 TYR . 16940 1 84 368 PRO . 16940 1 85 369 PRO . 16940 1 86 370 TRP . 16940 1 87 371 ASP . 16940 1 88 372 LYS . 16940 1 89 373 ASN . 16940 1 90 374 PHE . 16940 1 91 375 THR . 16940 1 92 376 GLU . 16940 1 93 377 ASN . 16940 1 94 378 ASP . 16940 1 95 379 LEU . 16940 1 96 380 LEU . 16940 1 97 381 VAL . 16940 1 98 382 ARG . 16940 1 99 383 ILE . 16940 1 100 384 GLY . 16940 1 101 385 LYS . 16940 1 102 386 HIS . 16940 1 103 387 SER . 16940 1 104 388 ARG . 16940 1 105 389 THR . 16940 1 106 390 ARG . 16940 1 107 391 TYR . 16940 1 108 392 GLU . 16940 1 109 393 ARG . 16940 1 110 394 ASN . 16940 1 111 395 ILE . 16940 1 112 396 GLU . 16940 1 113 397 LYS . 16940 1 114 398 ILE . 16940 1 115 399 SER . 16940 1 116 400 MET . 16940 1 117 401 LEU . 16940 1 118 402 GLU . 16940 1 119 403 LYS . 16940 1 120 404 ILE . 16940 1 121 405 TYR . 16940 1 122 406 ILE . 16940 1 123 407 HIS . 16940 1 124 408 PRO . 16940 1 125 409 ARG . 16940 1 126 410 TYR . 16940 1 127 411 ASN . 16940 1 128 412 TRP . 16940 1 129 413 ARG . 16940 1 130 414 GLU . 16940 1 131 415 ASN . 16940 1 132 416 LEU . 16940 1 133 417 ASP . 16940 1 134 418 ARG . 16940 1 135 419 ASP . 16940 1 136 420 ILE . 16940 1 137 421 ALA . 16940 1 138 422 LEU . 16940 1 139 423 MET . 16940 1 140 424 LYS . 16940 1 141 425 LEU . 16940 1 142 426 LYS . 16940 1 143 427 LYS . 16940 1 144 428 PRO . 16940 1 145 429 VAL . 16940 1 146 430 ALA . 16940 1 147 431 PHE . 16940 1 148 432 SER . 16940 1 149 433 ASP . 16940 1 150 434 TYR . 16940 1 151 435 ILE . 16940 1 152 436 HIS . 16940 1 153 437 PRO . 16940 1 154 438 VAL . 16940 1 155 439 CYS . 16940 1 156 440 LEU . 16940 1 157 441 PRO . 16940 1 158 442 ASP . 16940 1 159 443 ARG . 16940 1 160 444 GLU . 16940 1 161 445 THR . 16940 1 162 446 ALA . 16940 1 163 447 ALA . 16940 1 164 448 SER . 16940 1 165 449 LEU . 16940 1 166 450 LEU . 16940 1 167 451 GLN . 16940 1 168 452 ALA . 16940 1 169 453 GLY . 16940 1 170 454 TYR . 16940 1 171 455 LYS . 16940 1 172 456 GLY . 16940 1 173 457 ARG . 16940 1 174 458 VAL . 16940 1 175 459 THR . 16940 1 176 460 GLY . 16940 1 177 461 TRP . 16940 1 178 462 GLY . 16940 1 179 463 ASN . 16940 1 180 464 LEU . 16940 1 181 465 LYS . 16940 1 182 466 GLU . 16940 1 183 467 THR . 16940 1 184 468 TRP . 16940 1 185 469 THR . 16940 1 186 470 ALA . 16940 1 187 471 ASN . 16940 1 188 472 VAL . 16940 1 189 473 GLY . 16940 1 190 474 LYS . 16940 1 191 475 GLY . 16940 1 192 476 GLN . 16940 1 193 477 PRO . 16940 1 194 478 SER . 16940 1 195 479 VAL . 16940 1 196 480 LEU . 16940 1 197 481 GLN . 16940 1 198 482 VAL . 16940 1 199 483 VAL . 16940 1 200 484 ASN . 16940 1 201 485 LEU . 16940 1 202 486 PRO . 16940 1 203 487 ILE . 16940 1 204 488 VAL . 16940 1 205 489 GLU . 16940 1 206 490 ARG . 16940 1 207 491 PRO . 16940 1 208 492 VAL . 16940 1 209 493 CYS . 16940 1 210 494 LYS . 16940 1 211 495 ASP . 16940 1 212 496 SER . 16940 1 213 497 THR . 16940 1 214 498 ARG . 16940 1 215 499 ILE . 16940 1 216 500 ARG . 16940 1 217 501 ILE . 16940 1 218 502 THR . 16940 1 219 503 ASP . 16940 1 220 504 ASN . 16940 1 221 505 MET . 16940 1 222 506 PHE . 16940 1 223 507 CYS . 16940 1 224 508 ALA . 16940 1 225 509 GLY . 16940 1 226 510 TYR . 16940 1 227 511 LYS . 16940 1 228 512 PRO . 16940 1 229 513 ASP . 16940 1 230 514 GLU . 16940 1 231 515 GLY . 16940 1 232 516 LYS . 16940 1 233 517 ARG . 16940 1 234 518 GLY . 16940 1 235 519 ASP . 16940 1 236 520 ALA . 16940 1 237 521 CYS . 16940 1 238 522 GLU . 16940 1 239 523 GLY . 16940 1 240 524 ASP . 16940 1 241 525 SER . 16940 1 242 526 GLY . 16940 1 243 527 GLY . 16940 1 244 528 PRO . 16940 1 245 529 PHE . 16940 1 246 530 VAL . 16940 1 247 531 MET . 16940 1 248 532 LYS . 16940 1 249 533 SER . 16940 1 250 534 PRO . 16940 1 251 535 PHE . 16940 1 252 536 ASN . 16940 1 253 537 ASN . 16940 1 254 538 ARG . 16940 1 255 539 TRP . 16940 1 256 540 TYR . 16940 1 257 541 GLN . 16940 1 258 542 MET . 16940 1 259 543 GLY . 16940 1 260 544 ILE . 16940 1 261 545 VAL . 16940 1 262 546 SER . 16940 1 263 547 TRP . 16940 1 264 548 GLY . 16940 1 265 549 GLU . 16940 1 266 550 GLY . 16940 1 267 551 CYS . 16940 1 268 552 ASP . 16940 1 269 553 ARG . 16940 1 270 554 ASP . 16940 1 271 555 GLY . 16940 1 272 556 LYS . 16940 1 273 557 TYR . 16940 1 274 558 GLY . 16940 1 275 559 PHE . 16940 1 276 560 TYR . 16940 1 277 561 THR . 16940 1 278 562 HIS . 16940 1 279 563 VAL . 16940 1 280 564 PHE . 16940 1 281 565 ARG . 16940 1 282 566 LEU . 16940 1 283 567 LYS . 16940 1 284 568 LYS . 16940 1 285 569 TRP . 16940 1 286 570 ILE . 16940 1 287 571 GLN . 16940 1 288 572 LYS . 16940 1 289 573 VAL . 16940 1 290 574 ILE . 16940 1 291 575 ASP . 16940 1 292 576 GLN . 16940 1 293 577 PHE . 16940 1 294 578 GLY . 16940 1 295 579 GLU . 16940 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 . THR 1 1 16940 1 . PHE 2 2 16940 1 . GLY 3 3 16940 1 . SER 4 4 16940 1 . GLY 5 5 16940 1 . GLU 6 6 16940 1 . ALA 7 7 16940 1 . ASP 8 8 16940 1 . CYS 9 9 16940 1 . GLY 10 10 16940 1 . LEU 11 11 16940 1 . ARG 12 12 16940 1 . PRO 13 13 16940 1 . LEU 14 14 16940 1 . PHE 15 15 16940 1 . GLU 16 16 16940 1 . LYS 17 17 16940 1 . LYS 18 18 16940 1 . SER 19 19 16940 1 . LEU 20 20 16940 1 . GLU 21 21 16940 1 . ASP 22 22 16940 1 . LYS 23 23 16940 1 . THR 24 24 16940 1 . GLU 25 25 16940 1 . ARG 26 26 16940 1 . GLU 27 27 16940 1 . LEU 28 28 16940 1 . LEU 29 29 16940 1 . GLU 30 30 16940 1 . SER 31 31 16940 1 . TYR 32 32 16940 1 . ILE 33 33 16940 1 . ASP 34 34 16940 1 . GLY 35 35 16940 1 . ARG 36 36 16940 1 . ILE 37 37 16940 1 . VAL 38 38 16940 1 . GLU 39 39 16940 1 . GLY 40 40 16940 1 . SER 41 41 16940 1 . ASP 42 42 16940 1 . ALA 43 43 16940 1 . GLU 44 44 16940 1 . ILE 45 45 16940 1 . GLY 46 46 16940 1 . MET 47 47 16940 1 . SER 48 48 16940 1 . PRO 49 49 16940 1 . TRP 50 50 16940 1 . GLN 51 51 16940 1 . VAL 52 52 16940 1 . MET 53 53 16940 1 . LEU 54 54 16940 1 . PHE 55 55 16940 1 . ARG 56 56 16940 1 . LYS 57 57 16940 1 . SER 58 58 16940 1 . PRO 59 59 16940 1 . GLN 60 60 16940 1 . GLU 61 61 16940 1 . LEU 62 62 16940 1 . LEU 63 63 16940 1 . CYS 64 64 16940 1 . GLY 65 65 16940 1 . ALA 66 66 16940 1 . SER 67 67 16940 1 . LEU 68 68 16940 1 . ILE 69 69 16940 1 . SER 70 70 16940 1 . ASP 71 71 16940 1 . ARG 72 72 16940 1 . TRP 73 73 16940 1 . VAL 74 74 16940 1 . LEU 75 75 16940 1 . THR 76 76 16940 1 . ALA 77 77 16940 1 . ALA 78 78 16940 1 . HIS 79 79 16940 1 . CYS 80 80 16940 1 . LEU 81 81 16940 1 . LEU 82 82 16940 1 . TYR 83 83 16940 1 . PRO 84 84 16940 1 . PRO 85 85 16940 1 . TRP 86 86 16940 1 . ASP 87 87 16940 1 . LYS 88 88 16940 1 . ASN 89 89 16940 1 . PHE 90 90 16940 1 . THR 91 91 16940 1 . GLU 92 92 16940 1 . ASN 93 93 16940 1 . ASP 94 94 16940 1 . LEU 95 95 16940 1 . LEU 96 96 16940 1 . VAL 97 97 16940 1 . ARG 98 98 16940 1 . ILE 99 99 16940 1 . GLY 100 100 16940 1 . LYS 101 101 16940 1 . HIS 102 102 16940 1 . SER 103 103 16940 1 . ARG 104 104 16940 1 . THR 105 105 16940 1 . ARG 106 106 16940 1 . TYR 107 107 16940 1 . GLU 108 108 16940 1 . ARG 109 109 16940 1 . ASN 110 110 16940 1 . ILE 111 111 16940 1 . GLU 112 112 16940 1 . LYS 113 113 16940 1 . ILE 114 114 16940 1 . SER 115 115 16940 1 . MET 116 116 16940 1 . LEU 117 117 16940 1 . GLU 118 118 16940 1 . LYS 119 119 16940 1 . ILE 120 120 16940 1 . TYR 121 121 16940 1 . ILE 122 122 16940 1 . HIS 123 123 16940 1 . PRO 124 124 16940 1 . ARG 125 125 16940 1 . TYR 126 126 16940 1 . ASN 127 127 16940 1 . TRP 128 128 16940 1 . ARG 129 129 16940 1 . GLU 130 130 16940 1 . ASN 131 131 16940 1 . LEU 132 132 16940 1 . ASP 133 133 16940 1 . ARG 134 134 16940 1 . ASP 135 135 16940 1 . ILE 136 136 16940 1 . ALA 137 137 16940 1 . LEU 138 138 16940 1 . MET 139 139 16940 1 . LYS 140 140 16940 1 . LEU 141 141 16940 1 . LYS 142 142 16940 1 . LYS 143 143 16940 1 . PRO 144 144 16940 1 . VAL 145 145 16940 1 . ALA 146 146 16940 1 . PHE 147 147 16940 1 . SER 148 148 16940 1 . ASP 149 149 16940 1 . TYR 150 150 16940 1 . ILE 151 151 16940 1 . HIS 152 152 16940 1 . PRO 153 153 16940 1 . VAL 154 154 16940 1 . CYS 155 155 16940 1 . LEU 156 156 16940 1 . PRO 157 157 16940 1 . ASP 158 158 16940 1 . ARG 159 159 16940 1 . GLU 160 160 16940 1 . THR 161 161 16940 1 . ALA 162 162 16940 1 . ALA 163 163 16940 1 . SER 164 164 16940 1 . LEU 165 165 16940 1 . LEU 166 166 16940 1 . GLN 167 167 16940 1 . ALA 168 168 16940 1 . GLY 169 169 16940 1 . TYR 170 170 16940 1 . LYS 171 171 16940 1 . GLY 172 172 16940 1 . ARG 173 173 16940 1 . VAL 174 174 16940 1 . THR 175 175 16940 1 . GLY 176 176 16940 1 . TRP 177 177 16940 1 . GLY 178 178 16940 1 . ASN 179 179 16940 1 . LEU 180 180 16940 1 . LYS 181 181 16940 1 . GLU 182 182 16940 1 . THR 183 183 16940 1 . TRP 184 184 16940 1 . THR 185 185 16940 1 . ALA 186 186 16940 1 . ASN 187 187 16940 1 . VAL 188 188 16940 1 . GLY 189 189 16940 1 . LYS 190 190 16940 1 . GLY 191 191 16940 1 . GLN 192 192 16940 1 . PRO 193 193 16940 1 . SER 194 194 16940 1 . VAL 195 195 16940 1 . LEU 196 196 16940 1 . GLN 197 197 16940 1 . VAL 198 198 16940 1 . VAL 199 199 16940 1 . ASN 200 200 16940 1 . LEU 201 201 16940 1 . PRO 202 202 16940 1 . ILE 203 203 16940 1 . VAL 204 204 16940 1 . GLU 205 205 16940 1 . ARG 206 206 16940 1 . PRO 207 207 16940 1 . VAL 208 208 16940 1 . CYS 209 209 16940 1 . LYS 210 210 16940 1 . ASP 211 211 16940 1 . SER 212 212 16940 1 . THR 213 213 16940 1 . ARG 214 214 16940 1 . ILE 215 215 16940 1 . ARG 216 216 16940 1 . ILE 217 217 16940 1 . THR 218 218 16940 1 . ASP 219 219 16940 1 . ASN 220 220 16940 1 . MET 221 221 16940 1 . PHE 222 222 16940 1 . CYS 223 223 16940 1 . ALA 224 224 16940 1 . GLY 225 225 16940 1 . TYR 226 226 16940 1 . LYS 227 227 16940 1 . PRO 228 228 16940 1 . ASP 229 229 16940 1 . GLU 230 230 16940 1 . GLY 231 231 16940 1 . LYS 232 232 16940 1 . ARG 233 233 16940 1 . GLY 234 234 16940 1 . ASP 235 235 16940 1 . ALA 236 236 16940 1 . CYS 237 237 16940 1 . GLU 238 238 16940 1 . GLY 239 239 16940 1 . ASP 240 240 16940 1 . SER 241 241 16940 1 . GLY 242 242 16940 1 . GLY 243 243 16940 1 . PRO 244 244 16940 1 . PHE 245 245 16940 1 . VAL 246 246 16940 1 . MET 247 247 16940 1 . LYS 248 248 16940 1 . SER 249 249 16940 1 . PRO 250 250 16940 1 . PHE 251 251 16940 1 . ASN 252 252 16940 1 . ASN 253 253 16940 1 . ARG 254 254 16940 1 . TRP 255 255 16940 1 . TYR 256 256 16940 1 . GLN 257 257 16940 1 . MET 258 258 16940 1 . GLY 259 259 16940 1 . ILE 260 260 16940 1 . VAL 261 261 16940 1 . SER 262 262 16940 1 . TRP 263 263 16940 1 . GLY 264 264 16940 1 . GLU 265 265 16940 1 . GLY 266 266 16940 1 . CYS 267 267 16940 1 . ASP 268 268 16940 1 . ARG 269 269 16940 1 . ASP 270 270 16940 1 . GLY 271 271 16940 1 . LYS 272 272 16940 1 . TYR 273 273 16940 1 . GLY 274 274 16940 1 . PHE 275 275 16940 1 . TYR 276 276 16940 1 . THR 277 277 16940 1 . HIS 278 278 16940 1 . VAL 279 279 16940 1 . PHE 280 280 16940 1 . ARG 281 281 16940 1 . LEU 282 282 16940 1 . LYS 283 283 16940 1 . LYS 284 284 16940 1 . TRP 285 285 16940 1 . ILE 286 286 16940 1 . GLN 287 287 16940 1 . LYS 288 288 16940 1 . VAL 289 289 16940 1 . ILE 290 290 16940 1 . ASP 291 291 16940 1 . GLN 292 292 16940 1 . PHE 293 293 16940 1 . GLY 294 294 16940 1 . GLU 295 295 16940 1 stop_ save_ save_Hirugen _Entity.Sf_category entity _Entity.Sf_framecode Hirugen _Entity.Entry_ID 16940 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name Hirugen _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 GDFEEIPEEYLQ _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details 'C-terminal peptide of thrombin inhibitor Hirudin' _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 12 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 1468 _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 . GLY . 16940 2 2 . ASP . 16940 2 3 . PHE . 16940 2 4 . GLU . 16940 2 5 . GLU . 16940 2 6 . ILE . 16940 2 7 . PRO . 16940 2 8 . GLU . 16940 2 9 . GLU . 16940 2 10 . TYR . 16940 2 11 . LEU . 16940 2 12 . GLN . 16940 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 . GLY 1 1 16940 2 . ASP 2 2 16940 2 . PHE 3 3 16940 2 . GLU 4 4 16940 2 . GLU 5 5 16940 2 . ILE 6 6 16940 2 . PRO 7 7 16940 2 . GLU 8 8 16940 2 . GLU 9 9 16940 2 . TYR 10 10 16940 2 . LEU 11 11 16940 2 . GLN 12 12 16940 2 stop_ save_ save_PPACK _Entity.Sf_category entity _Entity.Sf_framecode PPACK _Entity.Entry_ID 16940 _Entity.ID 3 _Entity.BMRB_code . _Entity.Name PPACK _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 FPRX _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 yes _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 4 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details Inhibitor _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 . PHE . 16940 3 2 . PRO . 16940 3 3 . ARG . 16940 3 4 . CHM . 16940 3 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 16940 3 . PRO 2 2 16940 3 . ARG 3 3 16940 3 . CHM 4 4 16940 3 stop_ save_ save_NA _Entity.Sf_category entity _Entity.Sf_framecode NA _Entity.Entry_ID 16940 _Entity.ID 4 _Entity.BMRB_code . _Entity.Name NA _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 NA _Entity.Nonpolymer_comp_label $chem_comp_NA _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _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 . NA . 16940 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 16940 _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 $Thrombin . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 16940 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 16940 _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 $Thrombin . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pET23a . . . 'Expressed as prethrombin-2 in inclusion bodies and refolded.' . . 16940 1 2 2 $Hirugen . 'obtained from a vendor' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 16940 1 3 3 $PPACK . 'obtained from a vendor' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 16940 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_NA _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_NA _Chem_comp.Entry_ID 16940 _Chem_comp.ID NA _Chem_comp.Provenance . _Chem_comp.Name 'SODIUM ION' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code NA _Chem_comp.Ambiguous_flag . _Chem_comp.Initial_date . _Chem_comp.Modified_date . _Chem_comp.Release_status . _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code NA _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 1 _Chem_comp.Paramagnetic no _Chem_comp.Aromatic no _Chem_comp.Formula Na _Chem_comp.Formula_weight 22.990 _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 Tue Jun 9 15:20:12 2009 ; _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 FKNQFGJONOIPTF-UHFFFAOYAZ InChIKey InChI 1.02b 16940 NA InChI=1/Na/q+1 InChI InChI 1.02b 16940 NA [Na+] SMILES ACDLabs 10.04 16940 NA [Na+] SMILES CACTVS 3.341 16940 NA [Na+] SMILES 'OpenEye OEToolkits' 1.5.0 16940 NA [Na+] SMILES_CANONICAL CACTVS 3.341 16940 NA [Na+] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 16940 NA 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 sodium 'SYSTEMATIC NAME' ACDLabs 10.04 16940 NA 'sodium(+1) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 16940 NA 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 NA . NA . . NA . . N 1 . . . . . . . . . . 0.000 . 0.000 . 0.000 . 0.000 0.000 0.000 . . 16940 NA stop_ save_ save_chem_comp_CHM _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_CHM _Chem_comp.Entry_ID 16940 _Chem_comp.ID CHM _Chem_comp.Provenance . _Chem_comp.Name 1,3-DICHLORO-PROPAN-2-ONE _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code CHM _Chem_comp.Ambiguous_flag . _Chem_comp.Initial_date . _Chem_comp.Modified_date . _Chem_comp.Release_status . _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code CHM _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic no _Chem_comp.Aromatic no _Chem_comp.Formula 'C3 H4 Cl2 O' _Chem_comp.Formula_weight 126.969 _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 yes _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 Tue Jun 9 13:27:26 2009 ; _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 C(C(=O)CCl)Cl SMILES 'OpenEye OEToolkits' 1.5.0 16940 CHM C(C(=O)CCl)Cl SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 16940 CHM ClCC(=O)CCl SMILES CACTVS 2.87 16940 CHM ClCC(=O)CCl SMILES_CANONICAL CACTVS 2.87 16940 CHM InChI=1/C3H4Cl2O/c4-1-3(6)2-5/h1-2H2 INCHI InChi 1 16940 CHM 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 1,3-dichloropropan-2-one 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 16940 CHM 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 C1 . C1 . . C . . N 0 . . . . . . . . . . . . . . . . -0.952 0.000 -1.305 . . 16940 CHM C2 . C2 . . C . . N 0 . . . . . . . . . . . . . . . . -0.199 0.000 0.000 . . 16940 CHM C3 . C3 . . C . . N 0 . . . . . . . . . . . . . . . . -0.952 0.000 1.305 . . 16940 CHM CL1 . CL1 . . CL . . N 0 . . . . . . . . . . . . . . . . 0.218 0.000 -2.675 . . 16940 CHM CL3 . CL3 . . CL . . N 0 . . . . . . . . . . . . . . . . 0.218 0.000 2.675 . . 16940 CHM H11 . H11 . . H . . N 0 . . . . . . . . . . . . . . . . -1.579 0.890 -1.362 . . 16940 CHM H12 . H12 . . H . . N 0 . . . . . . . . . . . . . . . . -1.579 -0.890 -1.362 . . 16940 CHM H31 . H31 . . H . . N 0 . . . . . . . . . . . . . . . . -1.579 0.890 1.362 . . 16940 CHM H32 . H32 . . H . . N 0 . . . . . . . . . . . . . . . . -1.579 -0.890 1.362 . . 16940 CHM O . O . . O . . N 0 . . . . . . . . . . . . . . . . 1.008 0.000 0.000 . . 16940 CHM stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING C1 C2 . . . . 16940 CHM 2 . SING C1 CL1 . . . . 16940 CHM 3 . SING C1 H11 . . . . 16940 CHM 4 . SING C1 H12 . . . . 16940 CHM 5 . SING C2 C3 . . . . 16940 CHM 6 . DOUB C2 O . . . . 16940 CHM 7 . SING C3 CL3 . . . . 16940 CHM 8 . SING C3 H31 . . . . 16940 CHM 9 . SING C3 H32 . . . . 16940 CHM stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 16940 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '95% H2O/5% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 Thrombin '[U-13C; U-15N; U-2H]' . . 1 $Thrombin . . 100 . . uM . . . . 16940 1 2 Hirugen 'natural abundance' . . 2 $Hirugen . . 110 . . uM . . . . 16940 1 3 PPACK 'natural abundance' . . 3 $PPACK . . 100 . . uM . . . . 16940 1 4 'sodium phosphate' 'natural abundance' . . . . . . 50 . . mM . . . . 16940 1 5 H2O 'natural abundance' . . . . . . 95 . . % . . . . 16940 1 6 D2O 'natural abundance' . . . . . . 5 . . % . . . . 16940 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 16940 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 150 . mM 16940 1 pH 7.4 . pH 16940 1 pressure 1 . atm 16940 1 temperature 310 . K 16940 1 stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Software.Sf_category software _Software.Sf_framecode TOPSPIN _Software.Entry_ID 16940 _Software.ID 1 _Software.Name TOPSPIN _Software.Version 2.1 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 16940 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 16940 1 processing 16940 1 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 16940 _Software.ID 2 _Software.Name SPARKY _Software.Version 3.110 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 16940 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 16940 2 'data analysis' 16940 2 'peak picking' 16940 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 16940 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 700 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 16940 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 900 save_ save_spectrometer_3 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_3 _NMR_spectrometer.Entry_ID 16940 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 16940 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker Avance . 700 . . . 16940 1 2 spectrometer_2 Bruker Avance . 900 . . . 16940 1 3 spectrometer_3 Bruker Avance . 800 . . . 16940 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 16940 _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 1H-15N TROSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 16940 1 2 '3D TROSY HN(CO)CACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 16940 1 3 '3D TROSY HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 16940 1 4 '3D TROSY HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 16940 1 5 '3D HN(CA)NNH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 16940 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 16940 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 water protons . . . . ppm 4.75 internal indirect 0.25144953 . . . . . . . . . 16940 1 H 1 water protons . . . . ppm 4.75 internal direct 1 . . . . . . . . . 16940 1 N 15 water protons . . . . ppm 4.75 internal indirect 0.101329118 . . . . . . . . . 16940 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 16940 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err 0.05 _Assigned_chem_shift_list.Chem_shift_13C_err 0.3 _Assigned_chem_shift_list.Chem_shift_15N_err 0.3 _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-15N TROSY' . . . 16940 1 2 '3D TROSY HN(CO)CACB' . . . 16940 1 3 '3D TROSY HNCACB' . . . 16940 1 4 '3D TROSY HNCA' . . . 16940 1 5 '3D HN(CA)NNH' . . . 16940 1 stop_ loop_ _Chem_shift_software.Software_ID _Chem_shift_software.Software_label _Chem_shift_software.Method_ID _Chem_shift_software.Method_label _Chem_shift_software.Entry_ID _Chem_shift_software.Assigned_chem_shift_list_ID 2 $SPARKY . . 16940 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 8 8 ASP CA C 13 50.46 0.30 . 1 . . . . 292 ASP CA . 16940 1 2 . 1 1 8 8 ASP CB C 13 37.77 0.30 . 1 . . . . 292 ASP CB . 16940 1 3 . 1 1 9 9 CYS H H 1 7.78 0.05 . 1 . . . . 293 CYS H . 16940 1 4 . 1 1 9 9 CYS CA C 13 52.17 0.30 . 1 . . . . 293 CYS CA . 16940 1 5 . 1 1 9 9 CYS CB C 13 39.56 0.30 . 1 . . . . 293 CYS CB . 16940 1 6 . 1 1 9 9 CYS N N 15 117.65 0.30 . 1 . . . . 293 CYS N . 16940 1 7 . 1 1 10 10 GLY H H 1 9.14 0.05 . 1 . . . . 294 GLY H . 16940 1 8 . 1 1 10 10 GLY CA C 13 45.32 0.30 . 1 . . . . 294 GLY CA . 16940 1 9 . 1 1 10 10 GLY N N 15 104.65 0.30 . 1 . . . . 294 GLY N . 16940 1 10 . 1 1 11 11 LEU H H 1 7.33 0.05 . 1 . . . . 295 LEU H . 16940 1 11 . 1 1 11 11 LEU CA C 13 50.12 0.30 . 1 . . . . 295 LEU CA . 16940 1 12 . 1 1 11 11 LEU CB C 13 39.89 0.30 . 1 . . . . 295 LEU CB . 16940 1 13 . 1 1 11 11 LEU N N 15 120.23 0.30 . 1 . . . . 295 LEU N . 16940 1 14 . 1 1 12 12 ARG H H 1 8.64 0.05 . 1 . . . . 296 ARG H . 16940 1 15 . 1 1 12 12 ARG CA C 13 51.69 0.30 . 1 . . . . 296 ARG CA . 16940 1 16 . 1 1 12 12 ARG CB C 13 26.58 0.30 . 1 . . . . 296 ARG CB . 16940 1 17 . 1 1 12 12 ARG N N 15 120.65 0.30 . 1 . . . . 296 ARG N . 16940 1 18 . 1 1 13 13 PRO CA C 13 62.33 0.30 . 1 . . . . 297 PRO CA . 16940 1 19 . 1 1 13 13 PRO CB C 13 30.41 0.30 . 1 . . . . 297 PRO CB . 16940 1 20 . 1 1 14 14 LEU H H 1 7.75 0.05 . 1 . . . . 298 LEU H . 16940 1 21 . 1 1 14 14 LEU CA C 13 51.49 0.30 . 1 . . . . 298 LEU CA . 16940 1 22 . 1 1 14 14 LEU CB C 13 37.39 0.30 . 1 . . . . 298 LEU CB . 16940 1 23 . 1 1 14 14 LEU N N 15 109.83 0.30 . 1 . . . . 298 LEU N . 16940 1 24 . 1 1 15 15 PHE H H 1 7.07 0.05 . 1 . . . . 299 PHE H . 16940 1 25 . 1 1 15 15 PHE CA C 13 56.23 0.30 . 1 . . . . 299 PHE CA . 16940 1 26 . 1 1 15 15 PHE CB C 13 36.82 0.30 . 1 . . . . 299 PHE CB . 16940 1 27 . 1 1 15 15 PHE N N 15 113.57 0.30 . 1 . . . . 299 PHE N . 16940 1 28 . 1 1 16 16 GLU H H 1 9.01 0.05 . 1 . . . . 300 GLU H . 16940 1 29 . 1 1 16 16 GLU CA C 13 60.41 0.30 . 1 . . . . 300 GLU CA . 16940 1 30 . 1 1 16 16 GLU CB C 13 25.86 0.30 . 1 . . . . 300 GLU CB . 16940 1 31 . 1 1 16 16 GLU N N 15 125.88 0.30 . 1 . . . . 300 GLU N . 16940 1 32 . 1 1 17 17 LYS H H 1 7.76 0.05 . 1 . . . . 301 LYS H . 16940 1 33 . 1 1 17 17 LYS CA C 13 55.91 0.30 . 1 . . . . 301 LYS CA . 16940 1 34 . 1 1 17 17 LYS CB C 13 27.80 0.30 . 1 . . . . 301 LYS CB . 16940 1 35 . 1 1 17 17 LYS N N 15 113.83 0.30 . 1 . . . . 301 LYS N . 16940 1 36 . 1 1 18 18 LYS H H 1 7.22 0.05 . 1 . . . . 302 LYS H . 16940 1 37 . 1 1 18 18 LYS CA C 13 52.27 0.30 . 1 . . . . 302 LYS CA . 16940 1 38 . 1 1 18 18 LYS CB C 13 29.89 0.30 . 1 . . . . 302 LYS CB . 16940 1 39 . 1 1 18 18 LYS N N 15 117.02 0.30 . 1 . . . . 302 LYS N . 16940 1 40 . 1 1 19 19 SER H H 1 7.68 0.05 . 1 . . . . 303 SER H . 16940 1 41 . 1 1 19 19 SER CA C 13 56.25 0.30 . 1 . . . . 303 SER CA . 16940 1 42 . 1 1 19 19 SER CB C 13 61.77 0.30 . 1 . . . . 303 SER CB . 16940 1 43 . 1 1 19 19 SER N N 15 112.52 0.30 . 1 . . . . 303 SER N . 16940 1 44 . 1 1 20 20 LEU H H 1 7.84 0.05 . 1 . . . . 304 LEU H . 16940 1 45 . 1 1 20 20 LEU CA C 13 50.34 0.30 . 1 . . . . 304 LEU CA . 16940 1 46 . 1 1 20 20 LEU CB C 13 41.30 0.30 . 1 . . . . 304 LEU CB . 16940 1 47 . 1 1 20 20 LEU N N 15 120.49 0.30 . 1 . . . . 304 LEU N . 16940 1 48 . 1 1 21 21 GLU H H 1 8.36 0.05 . 1 . . . . 305 GLU H . 16940 1 49 . 1 1 21 21 GLU CA C 13 51.89 0.30 . 1 . . . . 305 GLU CA . 16940 1 50 . 1 1 21 21 GLU CB C 13 28.92 0.30 . 1 . . . . 305 GLU CB . 16940 1 51 . 1 1 21 21 GLU N N 15 121.99 0.30 . 1 . . . . 305 GLU N . 16940 1 52 . 1 1 22 22 ASP H H 1 9.70 0.05 . 1 . . . . 306 ASP H . 16940 1 53 . 1 1 22 22 ASP CA C 13 50.58 0.30 . 1 . . . . 306 ASP CA . 16940 1 54 . 1 1 22 22 ASP CB C 13 37.68 0.30 . 1 . . . . 306 ASP CB . 16940 1 55 . 1 1 22 22 ASP N N 15 125.37 0.30 . 1 . . . . 306 ASP N . 16940 1 56 . 1 1 23 23 LYS H H 1 9.97 0.05 . 1 . . . . 307 LYS H . 16940 1 57 . 1 1 23 23 LYS CA C 13 56.73 0.30 . 1 . . . . 307 LYS CA . 16940 1 58 . 1 1 23 23 LYS CB C 13 29.90 0.30 . 1 . . . . 307 LYS CB . 16940 1 59 . 1 1 23 23 LYS N N 15 117.58 0.30 . 1 . . . . 307 LYS N . 16940 1 60 . 1 1 24 24 THR H H 1 8.09 0.05 . 1 . . . . 308 THR H . 16940 1 61 . 1 1 24 24 THR CA C 13 58.14 0.30 . 1 . . . . 308 THR CA . 16940 1 62 . 1 1 24 24 THR CB C 13 67.05 0.30 . 1 . . . . 308 THR CB . 16940 1 63 . 1 1 24 24 THR N N 15 104.28 0.30 . 1 . . . . 308 THR N . 16940 1 64 . 1 1 25 25 GLU H H 1 8.04 0.05 . 1 . . . . 309 GLU H . 16940 1 65 . 1 1 25 25 GLU CA C 13 57.27 0.30 . 1 . . . . 309 GLU CA . 16940 1 66 . 1 1 25 25 GLU CB C 13 26.34 0.30 . 1 . . . . 309 GLU CB . 16940 1 67 . 1 1 25 25 GLU N N 15 123.41 0.30 . 1 . . . . 309 GLU N . 16940 1 68 . 1 1 26 26 ARG H H 1 8.87 0.05 . 1 . . . . 310 ARG H . 16940 1 69 . 1 1 26 26 ARG CA C 13 56.21 0.30 . 1 . . . . 310 ARG CA . 16940 1 70 . 1 1 26 26 ARG CB C 13 25.23 0.30 . 1 . . . . 310 ARG CB . 16940 1 71 . 1 1 26 26 ARG N N 15 122.65 0.30 . 1 . . . . 310 ARG N . 16940 1 72 . 1 1 27 27 GLU H H 1 7.55 0.05 . 1 . . . . 311 GLU H . 16940 1 73 . 1 1 27 27 GLU CA C 13 55.51 0.30 . 1 . . . . 311 GLU CA . 16940 1 74 . 1 1 27 27 GLU CB C 13 25.71 0.30 . 1 . . . . 311 GLU CB . 16940 1 75 . 1 1 27 27 GLU N N 15 118.67 0.30 . 1 . . . . 311 GLU N . 16940 1 76 . 1 1 28 28 LEU H H 1 7.09 0.05 . 1 . . . . 312 LEU H . 16940 1 77 . 1 1 28 28 LEU CA C 13 54.91 0.30 . 1 . . . . 312 LEU CA . 16940 1 78 . 1 1 28 28 LEU CB C 13 39.29 0.30 . 1 . . . . 312 LEU CB . 16940 1 79 . 1 1 28 28 LEU N N 15 117.77 0.30 . 1 . . . . 312 LEU N . 16940 1 80 . 1 1 29 29 LEU H H 1 7.15 0.05 . 1 . . . . 313 LEU H . 16940 1 81 . 1 1 29 29 LEU CA C 13 54.55 0.30 . 1 . . . . 313 LEU CA . 16940 1 82 . 1 1 29 29 LEU CB C 13 37.41 0.30 . 1 . . . . 313 LEU CB . 16940 1 83 . 1 1 29 29 LEU N N 15 120.35 0.30 . 1 . . . . 313 LEU N . 16940 1 84 . 1 1 30 30 GLU H H 1 8.34 0.05 . 1 . . . . 314 GLU H . 16940 1 85 . 1 1 30 30 GLU CA C 13 55.16 0.30 . 1 . . . . 314 GLU CA . 16940 1 86 . 1 1 30 30 GLU CB C 13 25.84 0.30 . 1 . . . . 314 GLU CB . 16940 1 87 . 1 1 30 30 GLU N N 15 116.95 0.30 . 1 . . . . 314 GLU N . 16940 1 88 . 1 1 31 31 SER H H 1 7.20 0.05 . 1 . . . . 315 SER H . 16940 1 89 . 1 1 31 31 SER CA C 13 56.99 0.30 . 1 . . . . 315 SER CA . 16940 1 90 . 1 1 31 31 SER CB C 13 60.49 0.30 . 1 . . . . 315 SER CB . 16940 1 91 . 1 1 31 31 SER N N 15 114.85 0.30 . 1 . . . . 315 SER N . 16940 1 92 . 1 1 32 32 TYR H H 1 6.59 0.05 . 1 . . . . 316 TYR H . 16940 1 93 . 1 1 32 32 TYR CA C 13 50.67 0.30 . 1 . . . . 316 TYR CA . 16940 1 94 . 1 1 32 32 TYR CB C 13 35.27 0.30 . 1 . . . . 316 TYR CB . 16940 1 95 . 1 1 32 32 TYR N N 15 121.67 0.30 . 1 . . . . 316 TYR N . 16940 1 96 . 1 1 33 33 ILE H H 1 7.10 0.05 . 1 . . . . 317 ILE H . 16940 1 97 . 1 1 33 33 ILE CA C 13 58.60 0.30 . 1 . . . . 317 ILE CA . 16940 1 98 . 1 1 33 33 ILE CB C 13 35.72 0.30 . 1 . . . . 317 ILE CB . 16940 1 99 . 1 1 33 33 ILE N N 15 118.40 0.30 . 1 . . . . 317 ILE N . 16940 1 100 . 1 1 34 34 ASP H H 1 8.06 0.05 . 1 . . . . 318 ASP H . 16940 1 101 . 1 1 34 34 ASP CA C 13 52.03 0.30 . 1 . . . . 318 ASP CA . 16940 1 102 . 1 1 34 34 ASP CB C 13 37.69 0.30 . 1 . . . . 318 ASP CB . 16940 1 103 . 1 1 34 34 ASP N N 15 128.04 0.30 . 1 . . . . 318 ASP N . 16940 1 104 . 1 1 35 35 GLY H H 1 8.30 0.05 . 1 . . . . 319 GLY H . 16940 1 105 . 1 1 35 35 GLY CA C 13 42.87 0.30 . 1 . . . . 319 GLY CA . 16940 1 106 . 1 1 35 35 GLY N N 15 110.55 0.30 . 1 . . . . 319 GLY N . 16940 1 107 . 1 1 36 36 ARG H H 1 7.73 0.05 . 1 . . . . 320 ARG H . 16940 1 108 . 1 1 36 36 ARG CA C 13 54.52 0.30 . 1 . . . . 320 ARG CA . 16940 1 109 . 1 1 36 36 ARG CB C 13 27.77 0.30 . 1 . . . . 320 ARG CB . 16940 1 110 . 1 1 36 36 ARG N N 15 126.13 0.30 . 1 . . . . 320 ARG N . 16940 1 111 . 1 1 37 37 ILE CA C 13 54.26 0.30 . 1 . . . . 321 ILE CA . 16940 1 112 . 1 1 37 37 ILE CB C 13 33.74 0.30 . 1 . . . . 321 ILE CB . 16940 1 113 . 1 1 38 38 VAL H H 1 9.08 0.05 . 1 . . . . 322 VAL H . 16940 1 114 . 1 1 38 38 VAL CA C 13 57.64 0.30 . 1 . . . . 322 VAL CA . 16940 1 115 . 1 1 38 38 VAL CB C 13 30.18 0.30 . 1 . . . . 322 VAL CB . 16940 1 116 . 1 1 38 38 VAL N N 15 130.67 0.30 . 1 . . . . 322 VAL N . 16940 1 117 . 1 1 39 39 GLU H H 1 9.26 0.05 . 1 . . . . 323 GLU H . 16940 1 118 . 1 1 39 39 GLU CA C 13 54.58 0.30 . 1 . . . . 323 GLU CA . 16940 1 119 . 1 1 39 39 GLU CB C 13 26.21 0.30 . 1 . . . . 323 GLU CB . 16940 1 120 . 1 1 39 39 GLU N N 15 120.69 0.30 . 1 . . . . 323 GLU N . 16940 1 121 . 1 1 40 40 GLY H H 1 7.90 0.05 . 1 . . . . 324 GLY H . 16940 1 122 . 1 1 40 40 GLY CA C 13 41.23 0.30 . 1 . . . . 324 GLY CA . 16940 1 123 . 1 1 40 40 GLY N N 15 106.22 0.30 . 1 . . . . 324 GLY N . 16940 1 124 . 1 1 41 41 SER H H 1 8.44 0.05 . 1 . . . . 325 SER H . 16940 1 125 . 1 1 41 41 SER CA C 13 53.52 0.30 . 1 . . . . 325 SER CA . 16940 1 126 . 1 1 41 41 SER CB C 13 63.09 0.30 . 1 . . . . 325 SER CB . 16940 1 127 . 1 1 41 41 SER N N 15 112.94 0.30 . 1 . . . . 325 SER N . 16940 1 128 . 1 1 42 42 ASP H H 1 8.37 0.05 . 1 . . . . 326 ASP H . 16940 1 129 . 1 1 42 42 ASP CA C 13 51.95 0.30 . 1 . . . . 326 ASP CA . 16940 1 130 . 1 1 42 42 ASP CB C 13 36.92 0.30 . 1 . . . . 326 ASP CB . 16940 1 131 . 1 1 42 42 ASP N N 15 121.23 0.30 . 1 . . . . 326 ASP N . 16940 1 132 . 1 1 43 43 ALA H H 1 8.86 0.05 . 1 . . . . 327 ALA H . 16940 1 133 . 1 1 43 43 ALA CA C 13 48.84 0.30 . 1 . . . . 327 ALA CA . 16940 1 134 . 1 1 43 43 ALA CB C 13 15.50 0.30 . 1 . . . . 327 ALA CB . 16940 1 135 . 1 1 43 43 ALA N N 15 125.81 0.30 . 1 . . . . 327 ALA N . 16940 1 136 . 1 1 44 44 GLU H H 1 7.23 0.05 . 1 . . . . 328 GLU H . 16940 1 137 . 1 1 44 44 GLU CA C 13 53.21 0.30 . 1 . . . . 328 GLU CA . 16940 1 138 . 1 1 44 44 GLU CB C 13 28.85 0.30 . 1 . . . . 328 GLU CB . 16940 1 139 . 1 1 44 44 GLU N N 15 121.01 0.30 . 1 . . . . 328 GLU N . 16940 1 140 . 1 1 45 45 ILE H H 1 8.56 0.05 . 1 . . . . 329 ILE H . 16940 1 141 . 1 1 45 45 ILE CA C 13 59.53 0.30 . 1 . . . . 329 ILE CA . 16940 1 142 . 1 1 45 45 ILE CB C 13 32.87 0.30 . 1 . . . . 329 ILE CB . 16940 1 143 . 1 1 45 45 ILE N N 15 125.26 0.30 . 1 . . . . 329 ILE N . 16940 1 144 . 1 1 46 46 GLY H H 1 9.08 0.05 . 1 . . . . 330 GLY H . 16940 1 145 . 1 1 46 46 GLY CA C 13 42.63 0.30 . 1 . . . . 330 GLY CA . 16940 1 146 . 1 1 46 46 GLY N N 15 113.47 0.30 . 1 . . . . 330 GLY N . 16940 1 147 . 1 1 47 47 MET H H 1 7.61 0.05 . 1 . . . . 331 MET H . 16940 1 148 . 1 1 47 47 MET CA C 13 54.08 0.30 . 1 . . . . 331 MET CA . 16940 1 149 . 1 1 47 47 MET CB C 13 30.91 0.30 . 1 . . . . 331 MET CB . 16940 1 150 . 1 1 47 47 MET N N 15 117.60 0.30 . 1 . . . . 331 MET N . 16940 1 151 . 1 1 48 48 SER H H 1 8.89 0.05 . 1 . . . . 332 SER H . 16940 1 152 . 1 1 48 48 SER CA C 13 54.23 0.30 . 1 . . . . 332 SER CA . 16940 1 153 . 1 1 48 48 SER CB C 13 59.60 0.30 . 1 . . . . 332 SER CB . 16940 1 154 . 1 1 48 48 SER N N 15 115.35 0.30 . 1 . . . . 332 SER N . 16940 1 155 . 1 1 49 49 PRO CA C 13 62.49 0.30 . 1 . . . . 333 PRO CA . 16940 1 156 . 1 1 49 49 PRO CB C 13 30.06 0.30 . 1 . . . . 333 PRO CB . 16940 1 157 . 1 1 50 50 TRP H H 1 5.80 0.05 . 1 . . . . 334 TRP H . 16940 1 158 . 1 1 50 50 TRP CA C 13 51.39 0.30 . 1 . . . . 334 TRP CA . 16940 1 159 . 1 1 50 50 TRP CB C 13 24.80 0.30 . 1 . . . . 334 TRP CB . 16940 1 160 . 1 1 50 50 TRP N N 15 117.93 0.30 . 1 . . . . 334 TRP N . 16940 1 161 . 1 1 51 51 GLN H H 1 8.19 0.05 . 1 . . . . 335 GLN H . 16940 1 162 . 1 1 51 51 GLN CA C 13 54.92 0.30 . 1 . . . . 335 GLN CA . 16940 1 163 . 1 1 51 51 GLN CB C 13 23.45 0.30 . 1 . . . . 335 GLN CB . 16940 1 164 . 1 1 51 51 GLN N N 15 125.37 0.30 . 1 . . . . 335 GLN N . 16940 1 165 . 1 1 52 52 VAL H H 1 8.77 0.05 . 1 . . . . 336 VAL H . 16940 1 166 . 1 1 52 52 VAL CA C 13 58.53 0.30 . 1 . . . . 336 VAL CA . 16940 1 167 . 1 1 52 52 VAL CB C 13 31.55 0.30 . 1 . . . . 336 VAL CB . 16940 1 168 . 1 1 52 52 VAL N N 15 131.18 0.30 . 1 . . . . 336 VAL N . 16940 1 169 . 1 1 53 53 MET H H 1 8.95 0.05 . 1 . . . . 337 MET H . 16940 1 170 . 1 1 53 53 MET CA C 13 52.20 0.30 . 1 . . . . 337 MET CA . 16940 1 171 . 1 1 53 53 MET CB C 13 33.43 0.30 . 1 . . . . 337 MET CB . 16940 1 172 . 1 1 53 53 MET N N 15 126.63 0.30 . 1 . . . . 337 MET N . 16940 1 173 . 1 1 54 54 LEU H H 1 8.91 0.05 . 1 . . . . 338 LEU H . 16940 1 174 . 1 1 54 54 LEU CA C 13 52.11 0.30 . 1 . . . . 338 LEU CA . 16940 1 175 . 1 1 54 54 LEU CB C 13 38.69 0.30 . 1 . . . . 338 LEU CB . 16940 1 176 . 1 1 54 54 LEU N N 15 128.75 0.30 . 1 . . . . 338 LEU N . 16940 1 177 . 1 1 55 55 PHE H H 1 9.03 0.05 . 1 . . . . 339 PHE H . 16940 1 178 . 1 1 55 55 PHE CA C 13 53.48 0.30 . 1 . . . . 339 PHE CA . 16940 1 179 . 1 1 55 55 PHE CB C 13 41.53 0.30 . 1 . . . . 339 PHE CB . 16940 1 180 . 1 1 55 55 PHE N N 15 131.87 0.30 . 1 . . . . 339 PHE N . 16940 1 181 . 1 1 56 56 ARG H H 1 8.37 0.05 . 1 . . . . 340 ARG H . 16940 1 182 . 1 1 56 56 ARG CA C 13 53.37 0.30 . 1 . . . . 340 ARG CA . 16940 1 183 . 1 1 56 56 ARG CB C 13 28.78 0.30 . 1 . . . . 340 ARG CB . 16940 1 184 . 1 1 56 56 ARG N N 15 130.10 0.30 . 1 . . . . 340 ARG N . 16940 1 185 . 1 1 57 57 LYS H H 1 7.21 0.05 . 1 . . . . 341 LYS H . 16940 1 186 . 1 1 57 57 LYS CA C 13 56.96 0.30 . 1 . . . . 341 LYS CA . 16940 1 187 . 1 1 57 57 LYS CB C 13 30.10 0.30 . 1 . . . . 341 LYS CB . 16940 1 188 . 1 1 57 57 LYS N N 15 120.39 0.30 . 1 . . . . 341 LYS N . 16940 1 189 . 1 1 58 58 SER H H 1 7.71 0.05 . 1 . . . . 342 SER H . 16940 1 190 . 1 1 58 58 SER CA C 13 51.94 0.30 . 1 . . . . 342 SER CA . 16940 1 191 . 1 1 58 58 SER CB C 13 60.99 0.30 . 1 . . . . 342 SER CB . 16940 1 192 . 1 1 58 58 SER N N 15 110.46 0.30 . 1 . . . . 342 SER N . 16940 1 193 . 1 1 59 59 PRO CA C 13 59.86 0.30 . 1 . . . . 343 PRO CA . 16940 1 194 . 1 1 59 59 PRO CB C 13 30.65 0.30 . 1 . . . . 343 PRO CB . 16940 1 195 . 1 1 60 60 GLN H H 1 7.88 0.05 . 1 . . . . 344 GLN H . 16940 1 196 . 1 1 60 60 GLN CA C 13 53.30 0.30 . 1 . . . . 344 GLN CA . 16940 1 197 . 1 1 60 60 GLN CB C 13 24.49 0.30 . 1 . . . . 344 GLN CB . 16940 1 198 . 1 1 60 60 GLN N N 15 116.81 0.30 . 1 . . . . 344 GLN N . 16940 1 199 . 1 1 61 61 GLU H H 1 6.15 0.05 . 1 . . . . 345 GLU H . 16940 1 200 . 1 1 61 61 GLU CA C 13 51.74 0.30 . 1 . . . . 345 GLU CA . 16940 1 201 . 1 1 61 61 GLU CB C 13 29.56 0.30 . 1 . . . . 345 GLU CB . 16940 1 202 . 1 1 61 61 GLU N N 15 120.24 0.30 . 1 . . . . 345 GLU N . 16940 1 203 . 1 1 62 62 LEU H H 1 7.85 0.05 . 1 . . . . 346 LEU H . 16940 1 204 . 1 1 62 62 LEU CA C 13 53.41 0.30 . 1 . . . . 346 LEU CA . 16940 1 205 . 1 1 62 62 LEU CB C 13 38.86 0.30 . 1 . . . . 346 LEU CB . 16940 1 206 . 1 1 62 62 LEU N N 15 124.89 0.30 . 1 . . . . 346 LEU N . 16940 1 207 . 1 1 63 63 LEU H H 1 8.35 0.05 . 1 . . . . 347 LEU H . 16940 1 208 . 1 1 63 63 LEU CA C 13 52.62 0.30 . 1 . . . . 347 LEU CA . 16940 1 209 . 1 1 63 63 LEU CB C 13 40.68 0.30 . 1 . . . . 347 LEU CB . 16940 1 210 . 1 1 63 63 LEU N N 15 125.27 0.30 . 1 . . . . 347 LEU N . 16940 1 211 . 1 1 64 64 CYS H H 1 7.71 0.05 . 1 . . . . 348 CYS H . 16940 1 212 . 1 1 64 64 CYS CA C 13 52.87 0.30 . 1 . . . . 348 CYS CA . 16940 1 213 . 1 1 64 64 CYS CB C 13 51.62 0.30 . 1 . . . . 348 CYS CB . 16940 1 214 . 1 1 64 64 CYS N N 15 116.20 0.30 . 1 . . . . 348 CYS N . 16940 1 215 . 1 1 65 65 GLY H H 1 8.89 0.05 . 1 . . . . 349 GLY H . 16940 1 216 . 1 1 65 65 GLY CA C 13 44.07 0.30 . 1 . . . . 349 GLY CA . 16940 1 217 . 1 1 65 65 GLY N N 15 106.62 0.30 . 1 . . . . 349 GLY N . 16940 1 218 . 1 1 66 66 ALA H H 1 7.97 0.05 . 1 . . . . 350 ALA H . 16940 1 219 . 1 1 66 66 ALA CA C 13 48.47 0.30 . 1 . . . . 350 ALA CA . 16940 1 220 . 1 1 66 66 ALA CB C 13 17.40 0.30 . 1 . . . . 350 ALA CB . 16940 1 221 . 1 1 66 66 ALA N N 15 117.39 0.30 . 1 . . . . 350 ALA N . 16940 1 222 . 1 1 67 67 SER H H 1 9.77 0.05 . 1 . . . . 351 SER H . 16940 1 223 . 1 1 67 67 SER CA C 13 53.10 0.30 . 1 . . . . 351 SER CA . 16940 1 224 . 1 1 67 67 SER CB C 13 63.16 0.30 . 1 . . . . 351 SER CB . 16940 1 225 . 1 1 67 67 SER N N 15 114.86 0.30 . 1 . . . . 351 SER N . 16940 1 226 . 1 1 68 68 LEU H H 1 9.36 0.05 . 1 . . . . 352 LEU H . 16940 1 227 . 1 1 68 68 LEU CA C 13 51.99 0.30 . 1 . . . . 352 LEU CA . 16940 1 228 . 1 1 68 68 LEU CB C 13 41.38 0.30 . 1 . . . . 352 LEU CB . 16940 1 229 . 1 1 68 68 LEU N N 15 126.70 0.30 . 1 . . . . 352 LEU N . 16940 1 230 . 1 1 69 69 ILE H H 1 8.08 0.05 . 1 . . . . 353 ILE H . 16940 1 231 . 1 1 69 69 ILE CA C 13 58.49 0.30 . 1 . . . . 353 ILE CA . 16940 1 232 . 1 1 69 69 ILE CB C 13 35.83 0.30 . 1 . . . . 353 ILE CB . 16940 1 233 . 1 1 69 69 ILE N N 15 118.32 0.30 . 1 . . . . 353 ILE N . 16940 1 234 . 1 1 70 70 SER H H 1 8.43 0.05 . 1 . . . . 354 SER H . 16940 1 235 . 1 1 70 70 SER CA C 13 54.62 0.30 . 1 . . . . 354 SER CA . 16940 1 236 . 1 1 70 70 SER CB C 13 60.52 0.30 . 1 . . . . 354 SER CB . 16940 1 237 . 1 1 70 70 SER N N 15 116.96 0.30 . 1 . . . . 354 SER N . 16940 1 238 . 1 1 71 71 ASP H H 1 8.91 0.05 . 1 . . . . 355 ASP H . 16940 1 239 . 1 1 71 71 ASP CA C 13 52.96 0.30 . 1 . . . . 355 ASP CA . 16940 1 240 . 1 1 71 71 ASP CB C 13 36.69 0.30 . 1 . . . . 355 ASP CB . 16940 1 241 . 1 1 71 71 ASP N N 15 115.83 0.30 . 1 . . . . 355 ASP N . 16940 1 242 . 1 1 72 72 ARG H H 1 7.79 0.05 . 1 . . . . 356 ARG H . 16940 1 243 . 1 1 72 72 ARG CA C 13 51.38 0.30 . 1 . . . . 356 ARG CA . 16940 1 244 . 1 1 72 72 ARG CB C 13 29.53 0.30 . 1 . . . . 356 ARG CB . 16940 1 245 . 1 1 72 72 ARG N N 15 114.31 0.30 . 1 . . . . 356 ARG N . 16940 1 246 . 1 1 73 73 TRP H H 1 7.19 0.05 . 1 . . . . 357 TRP H . 16940 1 247 . 1 1 73 73 TRP CA C 13 53.84 0.30 . 1 . . . . 357 TRP CA . 16940 1 248 . 1 1 73 73 TRP CB C 13 29.50 0.30 . 1 . . . . 357 TRP CB . 16940 1 249 . 1 1 73 73 TRP N N 15 118.34 0.30 . 1 . . . . 357 TRP N . 16940 1 250 . 1 1 74 74 VAL H H 1 9.12 0.05 . 1 . . . . 358 VAL H . 16940 1 251 . 1 1 74 74 VAL CA C 13 56.63 0.30 . 1 . . . . 358 VAL CA . 16940 1 252 . 1 1 74 74 VAL CB C 13 32.25 0.30 . 1 . . . . 358 VAL CB . 16940 1 253 . 1 1 74 74 VAL N N 15 121.09 0.30 . 1 . . . . 358 VAL N . 16940 1 254 . 1 1 75 75 LEU H H 1 9.56 0.05 . 1 . . . . 359 LEU H . 16940 1 255 . 1 1 75 75 LEU CA C 13 50.77 0.30 . 1 . . . . 359 LEU CA . 16940 1 256 . 1 1 75 75 LEU CB C 13 42.78 0.30 . 1 . . . . 359 LEU CB . 16940 1 257 . 1 1 75 75 LEU N N 15 129.92 0.30 . 1 . . . . 359 LEU N . 16940 1 258 . 1 1 76 76 THR H H 1 9.19 0.05 . 1 . . . . 360 THR H . 16940 1 259 . 1 1 76 76 THR CA C 13 57.78 0.30 . 1 . . . . 360 THR CA . 16940 1 260 . 1 1 76 76 THR CB C 13 67.07 0.30 . 1 . . . . 360 THR CB . 16940 1 261 . 1 1 76 76 THR N N 15 120.87 0.30 . 1 . . . . 360 THR N . 16940 1 262 . 1 1 77 77 ALA H H 1 8.02 0.05 . 1 . . . . 361 ALA H . 16940 1 263 . 1 1 77 77 ALA CA C 13 47.60 0.30 . 1 . . . . 361 ALA CA . 16940 1 264 . 1 1 77 77 ALA CB C 13 15.51 0.30 . 1 . . . . 361 ALA CB . 16940 1 265 . 1 1 77 77 ALA N N 15 123.33 0.30 . 1 . . . . 361 ALA N . 16940 1 266 . 1 1 78 78 ALA H H 1 6.47 0.05 . 1 . . . . 362 ALA H . 16940 1 267 . 1 1 78 78 ALA CA C 13 53.07 0.30 . 1 . . . . 362 ALA CA . 16940 1 268 . 1 1 78 78 ALA CB C 13 12.87 0.30 . 1 . . . . 362 ALA CB . 16940 1 269 . 1 1 78 78 ALA N N 15 127.79 0.30 . 1 . . . . 362 ALA N . 16940 1 270 . 1 1 79 79 HIS H H 1 10.46 0.05 . 1 . . . . 363 HIS H . 16940 1 271 . 1 1 79 79 HIS CA C 13 55.63 0.30 . 1 . . . . 363 HIS CA . 16940 1 272 . 1 1 79 79 HIS CB C 13 27.05 0.30 . 1 . . . . 363 HIS CB . 16940 1 273 . 1 1 79 79 HIS N N 15 116.50 0.30 . 1 . . . . 363 HIS N . 16940 1 274 . 1 1 80 80 CYS H H 1 6.85 0.05 . 1 . . . . 364 CYS H . 16940 1 275 . 1 1 80 80 CYS CA C 13 56.61 0.30 . 1 . . . . 364 CYS CA . 16940 1 276 . 1 1 80 80 CYS CB C 13 41.00 0.30 . 1 . . . . 364 CYS CB . 16940 1 277 . 1 1 80 80 CYS N N 15 116.63 0.30 . 1 . . . . 364 CYS N . 16940 1 278 . 1 1 81 81 LEU H H 1 7.38 0.05 . 1 . . . . 365 LEU H . 16940 1 279 . 1 1 81 81 LEU CA C 13 52.16 0.30 . 1 . . . . 365 LEU CA . 16940 1 280 . 1 1 81 81 LEU CB C 13 39.46 0.30 . 1 . . . . 365 LEU CB . 16940 1 281 . 1 1 81 81 LEU N N 15 116.68 0.30 . 1 . . . . 365 LEU N . 16940 1 282 . 1 1 82 82 LEU H H 1 8.10 0.05 . 1 . . . . 366 LEU H . 16940 1 283 . 1 1 82 82 LEU CA C 13 50.84 0.30 . 1 . . . . 366 LEU CA . 16940 1 284 . 1 1 82 82 LEU CB C 13 40.39 0.30 . 1 . . . . 366 LEU CB . 16940 1 285 . 1 1 82 82 LEU N N 15 119.80 0.30 . 1 . . . . 366 LEU N . 16940 1 286 . 1 1 83 83 TYR H H 1 9.21 0.05 . 1 . . . . 367 TYR H . 16940 1 287 . 1 1 83 83 TYR CA C 13 55.30 0.30 . 1 . . . . 367 TYR CA . 16940 1 288 . 1 1 83 83 TYR CB C 13 33.94 0.30 . 1 . . . . 367 TYR CB . 16940 1 289 . 1 1 83 83 TYR N N 15 125.83 0.30 . 1 . . . . 367 TYR N . 16940 1 290 . 1 1 85 85 PRO CA C 13 62.80 0.30 . 1 . . . . 369 PRO CA . 16940 1 291 . 1 1 85 85 PRO CB C 13 26.91 0.30 . 1 . . . . 369 PRO CB . 16940 1 292 . 1 1 86 86 TRP H H 1 7.02 0.05 . 1 . . . . 370 TRP H . 16940 1 293 . 1 1 86 86 TRP CA C 13 50.09 0.30 . 1 . . . . 370 TRP CA . 16940 1 294 . 1 1 86 86 TRP CB C 13 27.31 0.30 . 1 . . . . 370 TRP CB . 16940 1 295 . 1 1 86 86 TRP N N 15 113.50 0.30 . 1 . . . . 370 TRP N . 16940 1 296 . 1 1 87 87 ASP H H 1 8.58 0.05 . 1 . . . . 371 ASP H . 16940 1 297 . 1 1 87 87 ASP CA C 13 52.43 0.30 . 1 . . . . 371 ASP CA . 16940 1 298 . 1 1 87 87 ASP CB C 13 36.29 0.30 . 1 . . . . 371 ASP CB . 16940 1 299 . 1 1 87 87 ASP N N 15 119.30 0.30 . 1 . . . . 371 ASP N . 16940 1 300 . 1 1 88 88 LYS H H 1 6.71 0.05 . 1 . . . . 372 LYS H . 16940 1 301 . 1 1 88 88 LYS CA C 13 51.23 0.30 . 1 . . . . 372 LYS CA . 16940 1 302 . 1 1 88 88 LYS CB C 13 28.68 0.30 . 1 . . . . 372 LYS CB . 16940 1 303 . 1 1 88 88 LYS N N 15 115.85 0.30 . 1 . . . . 372 LYS N . 16940 1 304 . 1 1 89 89 ASN CA C 13 49.86 0.30 . 1 . . . . 373 ASN CA . 16940 1 305 . 1 1 89 89 ASN CB C 13 34.78 0.30 . 1 . . . . 373 ASN CB . 16940 1 306 . 1 1 90 90 PHE H H 1 8.63 0.05 . 1 . . . . 374 PHE H . 16940 1 307 . 1 1 90 90 PHE CA C 13 55.26 0.30 . 1 . . . . 374 PHE CA . 16940 1 308 . 1 1 90 90 PHE CB C 13 38.19 0.30 . 1 . . . . 374 PHE CB . 16940 1 309 . 1 1 90 90 PHE N N 15 122.39 0.30 . 1 . . . . 374 PHE N . 16940 1 310 . 1 1 91 91 THR H H 1 9.19 0.05 . 1 . . . . 375 THR H . 16940 1 311 . 1 1 91 91 THR CA C 13 57.00 0.30 . 1 . . . . 375 THR CA . 16940 1 312 . 1 1 91 91 THR CB C 13 68.96 0.30 . 1 . . . . 375 THR CB . 16940 1 313 . 1 1 91 91 THR N N 15 111.76 0.30 . 1 . . . . 375 THR N . 16940 1 314 . 1 1 92 92 GLU H H 1 10.18 0.05 . 1 . . . . 376 GLU H . 16940 1 315 . 1 1 92 92 GLU CA C 13 58.20 0.30 . 1 . . . . 376 GLU CA . 16940 1 316 . 1 1 92 92 GLU CB C 13 24.74 0.30 . 1 . . . . 376 GLU CB . 16940 1 317 . 1 1 92 92 GLU N N 15 119.20 0.30 . 1 . . . . 376 GLU N . 16940 1 318 . 1 1 93 93 ASN H H 1 8.01 0.05 . 1 . . . . 377 ASN H . 16940 1 319 . 1 1 93 93 ASN CA C 13 51.40 0.30 . 1 . . . . 377 ASN CA . 16940 1 320 . 1 1 93 93 ASN CB C 13 35.82 0.30 . 1 . . . . 377 ASN CB . 16940 1 321 . 1 1 93 93 ASN N N 15 113.89 0.30 . 1 . . . . 377 ASN N . 16940 1 322 . 1 1 94 94 ASP H H 1 7.82 0.05 . 1 . . . . 378 ASP H . 16940 1 323 . 1 1 94 94 ASP CA C 13 53.16 0.30 . 1 . . . . 378 ASP CA . 16940 1 324 . 1 1 94 94 ASP CB C 13 40.83 0.30 . 1 . . . . 378 ASP CB . 16940 1 325 . 1 1 94 94 ASP N N 15 116.13 0.30 . 1 . . . . 378 ASP N . 16940 1 326 . 1 1 95 95 LEU H H 1 6.96 0.05 . 1 . . . . 379 LEU H . 16940 1 327 . 1 1 95 95 LEU CA C 13 51.17 0.30 . 1 . . . . 379 LEU CA . 16940 1 328 . 1 1 95 95 LEU CB C 13 43.23 0.30 . 1 . . . . 379 LEU CB . 16940 1 329 . 1 1 95 95 LEU N N 15 117.20 0.30 . 1 . . . . 379 LEU N . 16940 1 330 . 1 1 96 96 LEU H H 1 8.97 0.05 . 1 . . . . 380 LEU H . 16940 1 331 . 1 1 96 96 LEU CA C 13 50.45 0.30 . 1 . . . . 380 LEU CA . 16940 1 332 . 1 1 96 96 LEU CB C 13 43.20 0.30 . 1 . . . . 380 LEU CB . 16940 1 333 . 1 1 96 96 LEU N N 15 117.81 0.30 . 1 . . . . 380 LEU N . 16940 1 334 . 1 1 97 97 VAL H H 1 8.27 0.05 . 1 . . . . 381 VAL H . 16940 1 335 . 1 1 97 97 VAL CA C 13 56.60 0.30 . 1 . . . . 381 VAL CA . 16940 1 336 . 1 1 97 97 VAL CB C 13 29.88 0.30 . 1 . . . . 381 VAL CB . 16940 1 337 . 1 1 97 97 VAL N N 15 114.35 0.30 . 1 . . . . 381 VAL N . 16940 1 338 . 1 1 98 98 ARG H H 1 8.71 0.05 . 1 . . . . 382 ARG H . 16940 1 339 . 1 1 98 98 ARG CA C 13 52.06 0.30 . 1 . . . . 382 ARG CA . 16940 1 340 . 1 1 98 98 ARG CB C 13 28.69 0.30 . 1 . . . . 382 ARG CB . 16940 1 341 . 1 1 98 98 ARG N N 15 120.95 0.30 . 1 . . . . 382 ARG N . 16940 1 342 . 1 1 99 99 ILE H H 1 9.83 0.05 . 1 . . . . 383 ILE H . 16940 1 343 . 1 1 99 99 ILE CA C 13 59.63 0.30 . 1 . . . . 383 ILE CA . 16940 1 344 . 1 1 99 99 ILE CB C 13 37.00 0.30 . 1 . . . . 383 ILE CB . 16940 1 345 . 1 1 99 99 ILE N N 15 130.55 0.30 . 1 . . . . 383 ILE N . 16940 1 346 . 1 1 100 100 GLY H H 1 8.81 0.05 . 1 . . . . 384 GLY H . 16940 1 347 . 1 1 100 100 GLY CA C 13 43.12 0.30 . 1 . . . . 384 GLY CA . 16940 1 348 . 1 1 100 100 GLY N N 15 117.10 0.30 . 1 . . . . 384 GLY N . 16940 1 349 . 1 1 101 101 LYS H H 1 8.22 0.05 . 1 . . . . 385 LYS H . 16940 1 350 . 1 1 101 101 LYS CA C 13 54.85 0.30 . 1 . . . . 385 LYS CA . 16940 1 351 . 1 1 101 101 LYS CB C 13 28.25 0.30 . 1 . . . . 385 LYS CB . 16940 1 352 . 1 1 101 101 LYS N N 15 114.17 0.30 . 1 . . . . 385 LYS N . 16940 1 353 . 1 1 102 102 HIS H H 1 10.12 0.05 . 1 . . . . 386 HIS H . 16940 1 354 . 1 1 102 102 HIS CA C 13 56.98 0.30 . 1 . . . . 386 HIS CA . 16940 1 355 . 1 1 102 102 HIS CB C 13 31.72 0.30 . 1 . . . . 386 HIS CB . 16940 1 356 . 1 1 102 102 HIS N N 15 121.03 0.30 . 1 . . . . 386 HIS N . 16940 1 357 . 1 1 103 103 SER H H 1 9.64 0.05 . 1 . . . . 387 SER H . 16940 1 358 . 1 1 103 103 SER CA C 13 55.44 0.30 . 1 . . . . 387 SER CA . 16940 1 359 . 1 1 103 103 SER CB C 13 60.56 0.30 . 1 . . . . 387 SER CB . 16940 1 360 . 1 1 103 103 SER N N 15 117.91 0.30 . 1 . . . . 387 SER N . 16940 1 361 . 1 1 104 104 ARG H H 1 8.19 0.05 . 1 . . . . 388 ARG H . 16940 1 362 . 1 1 104 104 ARG CA C 13 56.16 0.30 . 1 . . . . 388 ARG CA . 16940 1 363 . 1 1 104 104 ARG CB C 13 29.08 0.30 . 1 . . . . 388 ARG CB . 16940 1 364 . 1 1 104 104 ARG N N 15 124.74 0.30 . 1 . . . . 388 ARG N . 16940 1 365 . 1 1 105 105 THR H H 1 7.06 0.05 . 1 . . . . 389 THR H . 16940 1 366 . 1 1 105 105 THR CA C 13 58.82 0.30 . 1 . . . . 389 THR CA . 16940 1 367 . 1 1 105 105 THR CB C 13 66.95 0.30 . 1 . . . . 389 THR CB . 16940 1 368 . 1 1 105 105 THR N N 15 97.73 0.30 . 1 . . . . 389 THR N . 16940 1 369 . 1 1 106 106 ARG H H 1 7.89 0.05 . 1 . . . . 390 ARG H . 16940 1 370 . 1 1 106 106 ARG CA C 13 53.54 0.30 . 1 . . . . 390 ARG CA . 16940 1 371 . 1 1 106 106 ARG CB C 13 27.23 0.30 . 1 . . . . 390 ARG CB . 16940 1 372 . 1 1 106 106 ARG N N 15 124.75 0.30 . 1 . . . . 390 ARG N . 16940 1 373 . 1 1 107 107 TYR H H 1 9.31 0.05 . 1 . . . . 391 TYR H . 16940 1 374 . 1 1 107 107 TYR CA C 13 53.40 0.30 . 1 . . . . 391 TYR CA . 16940 1 375 . 1 1 107 107 TYR CB C 13 33.06 0.30 . 1 . . . . 391 TYR CB . 16940 1 376 . 1 1 107 107 TYR N N 15 124.23 0.30 . 1 . . . . 391 TYR N . 16940 1 377 . 1 1 108 108 GLU H H 1 9.50 0.05 . 1 . . . . 392 GLU H . 16940 1 378 . 1 1 108 108 GLU CA C 13 52.00 0.30 . 1 . . . . 392 GLU CA . 16940 1 379 . 1 1 108 108 GLU CB C 13 24.63 0.30 . 1 . . . . 392 GLU CB . 16940 1 380 . 1 1 108 108 GLU N N 15 133.81 0.30 . 1 . . . . 392 GLU N . 16940 1 381 . 1 1 109 109 ARG H H 1 6.93 0.05 . 1 . . . . 393 ARG H . 16940 1 382 . 1 1 109 109 ARG CA C 13 54.97 0.30 . 1 . . . . 393 ARG CA . 16940 1 383 . 1 1 109 109 ARG CB C 13 27.12 0.30 . 1 . . . . 393 ARG CB . 16940 1 384 . 1 1 109 109 ARG N N 15 125.54 0.30 . 1 . . . . 393 ARG N . 16940 1 385 . 1 1 111 111 ILE H H 1 7.78 0.05 . 1 . . . . 395 ILE H . 16940 1 386 . 1 1 111 111 ILE CA C 13 60.16 0.30 . 1 . . . . 395 ILE CA . 16940 1 387 . 1 1 111 111 ILE CB C 13 36.50 0.30 . 1 . . . . 395 ILE CB . 16940 1 388 . 1 1 111 111 ILE N N 15 121.75 0.30 . 1 . . . . 395 ILE N . 16940 1 389 . 1 1 112 112 GLU H H 1 8.03 0.05 . 1 . . . . 396 GLU H . 16940 1 390 . 1 1 112 112 GLU CA C 13 51.89 0.30 . 1 . . . . 396 GLU CA . 16940 1 391 . 1 1 112 112 GLU CB C 13 30.08 0.30 . 1 . . . . 396 GLU CB . 16940 1 392 . 1 1 112 112 GLU N N 15 115.69 0.30 . 1 . . . . 396 GLU N . 16940 1 393 . 1 1 113 113 LYS H H 1 9.01 0.05 . 1 . . . . 397 LYS H . 16940 1 394 . 1 1 113 113 LYS CA C 13 50.59 0.30 . 1 . . . . 397 LYS CA . 16940 1 395 . 1 1 113 113 LYS CB C 13 32.28 0.30 . 1 . . . . 397 LYS CB . 16940 1 396 . 1 1 113 113 LYS N N 15 119.94 0.30 . 1 . . . . 397 LYS N . 16940 1 397 . 1 1 114 114 ILE H H 1 8.02 0.05 . 1 . . . . 398 ILE H . 16940 1 398 . 1 1 114 114 ILE CA C 13 57.61 0.30 . 1 . . . . 398 ILE CA . 16940 1 399 . 1 1 114 114 ILE CB C 13 33.92 0.30 . 1 . . . . 398 ILE CB . 16940 1 400 . 1 1 114 114 ILE N N 15 123.86 0.30 . 1 . . . . 398 ILE N . 16940 1 401 . 1 1 115 115 SER H H 1 8.84 0.05 . 1 . . . . 399 SER H . 16940 1 402 . 1 1 115 115 SER CA C 13 54.83 0.30 . 1 . . . . 399 SER CA . 16940 1 403 . 1 1 115 115 SER CB C 13 62.84 0.30 . 1 . . . . 399 SER CB . 16940 1 404 . 1 1 115 115 SER N N 15 120.51 0.30 . 1 . . . . 399 SER N . 16940 1 405 . 1 1 116 116 MET H H 1 8.63 0.05 . 1 . . . . 400 MET H . 16940 1 406 . 1 1 116 116 MET CA C 13 52.23 0.30 . 1 . . . . 400 MET CA . 16940 1 407 . 1 1 116 116 MET CB C 13 30.96 0.30 . 1 . . . . 400 MET CB . 16940 1 408 . 1 1 116 116 MET N N 15 122.78 0.30 . 1 . . . . 400 MET N . 16940 1 409 . 1 1 117 117 LEU H H 1 9.34 0.05 . 1 . . . . 401 LEU H . 16940 1 410 . 1 1 117 117 LEU CA C 13 51.20 0.30 . 1 . . . . 401 LEU CA . 16940 1 411 . 1 1 117 117 LEU CB C 13 39.35 0.30 . 1 . . . . 401 LEU CB . 16940 1 412 . 1 1 117 117 LEU N N 15 122.33 0.30 . 1 . . . . 401 LEU N . 16940 1 413 . 1 1 118 118 GLU H H 1 9.21 0.05 . 1 . . . . 402 GLU H . 16940 1 414 . 1 1 118 118 GLU CA C 13 54.13 0.30 . 1 . . . . 402 GLU CA . 16940 1 415 . 1 1 118 118 GLU CB C 13 28.48 0.30 . 1 . . . . 402 GLU CB . 16940 1 416 . 1 1 118 118 GLU N N 15 122.30 0.30 . 1 . . . . 402 GLU N . 16940 1 417 . 1 1 119 119 LYS H H 1 7.09 0.05 . 1 . . . . 403 LYS H . 16940 1 418 . 1 1 119 119 LYS CA C 13 52.11 0.30 . 1 . . . . 403 LYS CA . 16940 1 419 . 1 1 119 119 LYS CB C 13 33.39 0.30 . 1 . . . . 403 LYS CB . 16940 1 420 . 1 1 119 119 LYS N N 15 114.58 0.30 . 1 . . . . 403 LYS N . 16940 1 421 . 1 1 120 120 ILE H H 1 8.32 0.05 . 1 . . . . 404 ILE H . 16940 1 422 . 1 1 120 120 ILE CA C 13 57.83 0.30 . 1 . . . . 404 ILE CA . 16940 1 423 . 1 1 120 120 ILE CB C 13 37.32 0.30 . 1 . . . . 404 ILE CB . 16940 1 424 . 1 1 120 120 ILE N N 15 123.69 0.30 . 1 . . . . 404 ILE N . 16940 1 425 . 1 1 121 121 TYR H H 1 9.42 0.05 . 1 . . . . 405 TYR H . 16940 1 426 . 1 1 121 121 TYR CA C 13 54.37 0.30 . 1 . . . . 405 TYR CA . 16940 1 427 . 1 1 121 121 TYR CB C 13 36.86 0.30 . 1 . . . . 405 TYR CB . 16940 1 428 . 1 1 121 121 TYR N N 15 125.58 0.30 . 1 . . . . 405 TYR N . 16940 1 429 . 1 1 122 122 ILE H H 1 8.98 0.05 . 1 . . . . 406 ILE H . 16940 1 430 . 1 1 122 122 ILE CA C 13 57.61 0.30 . 1 . . . . 406 ILE CA . 16940 1 431 . 1 1 122 122 ILE CB C 13 35.60 0.30 . 1 . . . . 406 ILE CB . 16940 1 432 . 1 1 122 122 ILE N N 15 125.95 0.30 . 1 . . . . 406 ILE N . 16940 1 433 . 1 1 123 123 HIS H H 1 6.92 0.05 . 1 . . . . 407 HIS H . 16940 1 434 . 1 1 123 123 HIS CA C 13 54.95 0.30 . 1 . . . . 407 HIS CA . 16940 1 435 . 1 1 123 123 HIS CB C 13 27.34 0.30 . 1 . . . . 407 HIS CB . 16940 1 436 . 1 1 123 123 HIS N N 15 129.91 0.30 . 1 . . . . 407 HIS N . 16940 1 437 . 1 1 124 124 PRO CA C 13 61.54 0.30 . 1 . . . . 408 PRO CA . 16940 1 438 . 1 1 124 124 PRO CB C 13 29.00 0.30 . 1 . . . . 408 PRO CB . 16940 1 439 . 1 1 125 125 ARG H H 1 11.21 0.05 . 1 . . . . 409 ARG H . 16940 1 440 . 1 1 125 125 ARG CA C 13 51.19 0.30 . 1 . . . . 409 ARG CA . 16940 1 441 . 1 1 125 125 ARG CB C 13 26.13 0.30 . 1 . . . . 409 ARG CB . 16940 1 442 . 1 1 125 125 ARG N N 15 121.35 0.30 . 1 . . . . 409 ARG N . 16940 1 443 . 1 1 126 126 TYR H H 1 7.54 0.05 . 1 . . . . 410 TYR H . 16940 1 444 . 1 1 126 126 TYR CA C 13 53.97 0.30 . 1 . . . . 410 TYR CA . 16940 1 445 . 1 1 126 126 TYR CB C 13 35.33 0.30 . 1 . . . . 410 TYR CB . 16940 1 446 . 1 1 126 126 TYR N N 15 124.30 0.30 . 1 . . . . 410 TYR N . 16940 1 447 . 1 1 127 127 ASN H H 1 8.77 0.05 . 1 . . . . 411 ASN H . 16940 1 448 . 1 1 127 127 ASN CA C 13 47.47 0.30 . 1 . . . . 411 ASN CA . 16940 1 449 . 1 1 127 127 ASN CB C 13 35.43 0.30 . 1 . . . . 411 ASN CB . 16940 1 450 . 1 1 127 127 ASN N N 15 131.91 0.30 . 1 . . . . 411 ASN N . 16940 1 451 . 1 1 128 128 TRP H H 1 6.37 0.05 . 1 . . . . 412 TRP H . 16940 1 452 . 1 1 128 128 TRP CA C 13 53.08 0.30 . 1 . . . . 412 TRP CA . 16940 1 453 . 1 1 128 128 TRP CB C 13 24.67 0.30 . 1 . . . . 412 TRP CB . 16940 1 454 . 1 1 128 128 TRP N N 15 118.92 0.30 . 1 . . . . 412 TRP N . 16940 1 455 . 1 1 129 129 ARG H H 1 6.87 0.05 . 1 . . . . 413 ARG H . 16940 1 456 . 1 1 129 129 ARG CA C 13 55.71 0.30 . 1 . . . . 413 ARG CA . 16940 1 457 . 1 1 129 129 ARG CB C 13 26.93 0.30 . 1 . . . . 413 ARG CB . 16940 1 458 . 1 1 129 129 ARG N N 15 120.68 0.30 . 1 . . . . 413 ARG N . 16940 1 459 . 1 1 130 130 GLU H H 1 7.14 0.05 . 1 . . . . 414 GLU H . 16940 1 460 . 1 1 130 130 GLU CA C 13 54.18 0.30 . 1 . . . . 414 GLU CA . 16940 1 461 . 1 1 130 130 GLU CB C 13 28.26 0.30 . 1 . . . . 414 GLU CB . 16940 1 462 . 1 1 130 130 GLU N N 15 115.98 0.30 . 1 . . . . 414 GLU N . 16940 1 463 . 1 1 131 131 ASN H H 1 7.22 0.05 . 1 . . . . 415 ASN H . 16940 1 464 . 1 1 131 131 ASN CA C 13 49.46 0.30 . 1 . . . . 415 ASN CA . 16940 1 465 . 1 1 131 131 ASN CB C 13 35.62 0.30 . 1 . . . . 415 ASN CB . 16940 1 466 . 1 1 131 131 ASN N N 15 113.40 0.30 . 1 . . . . 415 ASN N . 16940 1 467 . 1 1 132 132 LEU H H 1 7.72 0.05 . 1 . . . . 416 LEU H . 16940 1 468 . 1 1 132 132 LEU CA C 13 52.70 0.30 . 1 . . . . 416 LEU CA . 16940 1 469 . 1 1 132 132 LEU CB C 13 39.60 0.30 . 1 . . . . 416 LEU CB . 16940 1 470 . 1 1 132 132 LEU N N 15 110.95 0.30 . 1 . . . . 416 LEU N . 16940 1 471 . 1 1 133 133 ASP H H 1 7.14 0.05 . 1 . . . . 417 ASP H . 16940 1 472 . 1 1 133 133 ASP CA C 13 52.95 0.30 . 1 . . . . 417 ASP CA . 16940 1 473 . 1 1 133 133 ASP CB C 13 38.74 0.30 . 1 . . . . 417 ASP CB . 16940 1 474 . 1 1 133 133 ASP N N 15 116.89 0.30 . 1 . . . . 417 ASP N . 16940 1 475 . 1 1 134 134 ARG H H 1 8.70 0.05 . 1 . . . . 418 ARG H . 16940 1 476 . 1 1 134 134 ARG CA C 13 54.63 0.30 . 1 . . . . 418 ARG CA . 16940 1 477 . 1 1 134 134 ARG CB C 13 25.38 0.30 . 1 . . . . 418 ARG CB . 16940 1 478 . 1 1 134 134 ARG N N 15 119.22 0.30 . 1 . . . . 418 ARG N . 16940 1 479 . 1 1 135 135 ASP H H 1 6.89 0.05 . 1 . . . . 419 ASP H . 16940 1 480 . 1 1 135 135 ASP CA C 13 50.35 0.30 . 1 . . . . 419 ASP CA . 16940 1 481 . 1 1 135 135 ASP CB C 13 37.73 0.30 . 1 . . . . 419 ASP CB . 16940 1 482 . 1 1 135 135 ASP N N 15 114.53 0.30 . 1 . . . . 419 ASP N . 16940 1 483 . 1 1 136 136 ILE H H 1 8.31 0.05 . 1 . . . . 420 ILE H . 16940 1 484 . 1 1 136 136 ILE CA C 13 57.84 0.30 . 1 . . . . 420 ILE CA . 16940 1 485 . 1 1 136 136 ILE CB C 13 38.53 0.30 . 1 . . . . 420 ILE CB . 16940 1 486 . 1 1 136 136 ILE N N 15 126.81 0.30 . 1 . . . . 420 ILE N . 16940 1 487 . 1 1 137 137 ALA H H 1 8.29 0.05 . 1 . . . . 421 ALA H . 16940 1 488 . 1 1 137 137 ALA CA C 13 47.91 0.30 . 1 . . . . 421 ALA CA . 16940 1 489 . 1 1 137 137 ALA CB C 13 20.46 0.30 . 1 . . . . 421 ALA CB . 16940 1 490 . 1 1 137 137 ALA N N 15 127.35 0.30 . 1 . . . . 421 ALA N . 16940 1 491 . 1 1 138 138 LEU H H 1 9.49 0.05 . 1 . . . . 422 LEU H . 16940 1 492 . 1 1 138 138 LEU CA C 13 50.25 0.30 . 1 . . . . 422 LEU CA . 16940 1 493 . 1 1 138 138 LEU CB C 13 44.39 0.30 . 1 . . . . 422 LEU CB . 16940 1 494 . 1 1 138 138 LEU N N 15 121.92 0.30 . 1 . . . . 422 LEU N . 16940 1 495 . 1 1 139 139 MET H H 1 9.61 0.05 . 1 . . . . 423 MET H . 16940 1 496 . 1 1 139 139 MET CA C 13 51.27 0.30 . 1 . . . . 423 MET CA . 16940 1 497 . 1 1 139 139 MET CB C 13 32.24 0.30 . 1 . . . . 423 MET CB . 16940 1 498 . 1 1 139 139 MET N N 15 118.46 0.30 . 1 . . . . 423 MET N . 16940 1 499 . 1 1 140 140 LYS H H 1 8.71 0.05 . 1 . . . . 424 LYS H . 16940 1 500 . 1 1 140 140 LYS CA C 13 50.97 0.30 . 1 . . . . 424 LYS CA . 16940 1 501 . 1 1 140 140 LYS CB C 13 31.18 0.30 . 1 . . . . 424 LYS CB . 16940 1 502 . 1 1 140 140 LYS N N 15 126.36 0.30 . 1 . . . . 424 LYS N . 16940 1 503 . 1 1 141 141 LEU H H 1 8.68 0.05 . 1 . . . . 425 LEU H . 16940 1 504 . 1 1 141 141 LEU CA C 13 51.94 0.30 . 1 . . . . 425 LEU CA . 16940 1 505 . 1 1 141 141 LEU CB C 13 38.58 0.30 . 1 . . . . 425 LEU CB . 16940 1 506 . 1 1 141 141 LEU N N 15 128.03 0.30 . 1 . . . . 425 LEU N . 16940 1 507 . 1 1 142 142 LYS H H 1 8.10 0.05 . 1 . . . . 426 LYS H . 16940 1 508 . 1 1 142 142 LYS CA C 13 56.37 0.30 . 1 . . . . 426 LYS CA . 16940 1 509 . 1 1 142 142 LYS CB C 13 29.81 0.30 . 1 . . . . 426 LYS CB . 16940 1 510 . 1 1 142 142 LYS N N 15 120.54 0.30 . 1 . . . . 426 LYS N . 16940 1 511 . 1 1 143 143 LYS H H 1 7.33 0.05 . 1 . . . . 427 LYS H . 16940 1 512 . 1 1 143 143 LYS CA C 13 49.80 0.30 . 1 . . . . 427 LYS CA . 16940 1 513 . 1 1 143 143 LYS CB C 13 31.02 0.30 . 1 . . . . 427 LYS CB . 16940 1 514 . 1 1 143 143 LYS N N 15 114.95 0.30 . 1 . . . . 427 LYS N . 16940 1 515 . 1 1 144 144 PRO CA C 13 59.26 0.30 . 1 . . . . 428 PRO CA . 16940 1 516 . 1 1 144 144 PRO CB C 13 28.52 0.30 . 1 . . . . 428 PRO CB . 16940 1 517 . 1 1 145 145 VAL H H 1 8.70 0.05 . 1 . . . . 429 VAL H . 16940 1 518 . 1 1 145 145 VAL CA C 13 56.87 0.30 . 1 . . . . 429 VAL CA . 16940 1 519 . 1 1 145 145 VAL CB C 13 30.17 0.30 . 1 . . . . 429 VAL CB . 16940 1 520 . 1 1 145 145 VAL N N 15 122.17 0.30 . 1 . . . . 429 VAL N . 16940 1 521 . 1 1 146 146 ALA H H 1 7.87 0.05 . 1 . . . . 430 ALA H . 16940 1 522 . 1 1 146 146 ALA CA C 13 48.03 0.30 . 1 . . . . 430 ALA CA . 16940 1 523 . 1 1 146 146 ALA CB C 13 15.58 0.30 . 1 . . . . 430 ALA CB . 16940 1 524 . 1 1 146 146 ALA N N 15 127.66 0.30 . 1 . . . . 430 ALA N . 16940 1 525 . 1 1 147 147 PHE H H 1 7.81 0.05 . 1 . . . . 431 PHE H . 16940 1 526 . 1 1 147 147 PHE CA C 13 51.68 0.30 . 1 . . . . 431 PHE CA . 16940 1 527 . 1 1 147 147 PHE CB C 13 34.21 0.30 . 1 . . . . 431 PHE CB . 16940 1 528 . 1 1 147 147 PHE N N 15 122.19 0.30 . 1 . . . . 431 PHE N . 16940 1 529 . 1 1 148 148 SER H H 1 9.75 0.05 . 1 . . . . 432 SER H . 16940 1 530 . 1 1 148 148 SER CA C 13 54.34 0.30 . 1 . . . . 432 SER CA . 16940 1 531 . 1 1 148 148 SER CB C 13 63.74 0.30 . 1 . . . . 432 SER CB . 16940 1 532 . 1 1 148 148 SER N N 15 118.63 0.30 . 1 . . . . 432 SER N . 16940 1 533 . 1 1 149 149 ASP H H 1 8.54 0.05 . 1 . . . . 433 ASP H . 16940 1 534 . 1 1 149 149 ASP CA C 13 53.82 0.30 . 1 . . . . 433 ASP CA . 16940 1 535 . 1 1 149 149 ASP CB C 13 36.19 0.30 . 1 . . . . 433 ASP CB . 16940 1 536 . 1 1 149 149 ASP N N 15 118.97 0.30 . 1 . . . . 433 ASP N . 16940 1 537 . 1 1 150 150 TYR H H 1 7.70 0.05 . 1 . . . . 434 TYR H . 16940 1 538 . 1 1 150 150 TYR CA C 13 53.40 0.30 . 1 . . . . 434 TYR CA . 16940 1 539 . 1 1 150 150 TYR CB C 13 37.26 0.30 . 1 . . . . 434 TYR CB . 16940 1 540 . 1 1 150 150 TYR N N 15 113.03 0.30 . 1 . . . . 434 TYR N . 16940 1 541 . 1 1 151 151 ILE H H 1 6.96 0.05 . 1 . . . . 435 ILE H . 16940 1 542 . 1 1 151 151 ILE CA C 13 58.27 0.30 . 1 . . . . 435 ILE CA . 16940 1 543 . 1 1 151 151 ILE CB C 13 37.25 0.30 . 1 . . . . 435 ILE CB . 16940 1 544 . 1 1 151 151 ILE N N 15 118.97 0.30 . 1 . . . . 435 ILE N . 16940 1 545 . 1 1 152 152 HIS H H 1 7.53 0.05 . 1 . . . . 436 HIS H . 16940 1 546 . 1 1 152 152 HIS CA C 13 52.32 0.30 . 1 . . . . 436 HIS CA . 16940 1 547 . 1 1 152 152 HIS CB C 13 31.84 0.30 . 1 . . . . 436 HIS CB . 16940 1 548 . 1 1 152 152 HIS N N 15 126.26 0.30 . 1 . . . . 436 HIS N . 16940 1 549 . 1 1 153 153 PRO CA C 13 59.73 0.30 . 1 . . . . 437 PRO CA . 16940 1 550 . 1 1 153 153 PRO CB C 13 28.92 0.30 . 1 . . . . 437 PRO CB . 16940 1 551 . 1 1 154 154 VAL H H 1 8.08 0.05 . 1 . . . . 438 VAL H . 16940 1 552 . 1 1 154 154 VAL CA C 13 57.10 0.30 . 1 . . . . 438 VAL CA . 16940 1 553 . 1 1 154 154 VAL CB C 13 29.33 0.30 . 1 . . . . 438 VAL CB . 16940 1 554 . 1 1 154 154 VAL N N 15 122.69 0.30 . 1 . . . . 438 VAL N . 16940 1 555 . 1 1 155 155 CYS H H 1 6.79 0.05 . 1 . . . . 439 CYS H . 16940 1 556 . 1 1 155 155 CYS CA C 13 50.82 0.30 . 1 . . . . 439 CYS CA . 16940 1 557 . 1 1 155 155 CYS CB C 13 38.09 0.30 . 1 . . . . 439 CYS CB . 16940 1 558 . 1 1 155 155 CYS N N 15 119.97 0.30 . 1 . . . . 439 CYS N . 16940 1 559 . 1 1 156 156 LEU H H 1 9.11 0.05 . 1 . . . . 440 LEU H . 16940 1 560 . 1 1 156 156 LEU CA C 13 48.92 0.30 . 1 . . . . 440 LEU CA . 16940 1 561 . 1 1 156 156 LEU CB C 13 37.75 0.30 . 1 . . . . 440 LEU CB . 16940 1 562 . 1 1 156 156 LEU N N 15 122.38 0.30 . 1 . . . . 440 LEU N . 16940 1 563 . 1 1 157 157 PRO CA C 13 60.47 0.30 . 1 . . . . 441 PRO CA . 16940 1 564 . 1 1 157 157 PRO CB C 13 28.61 0.30 . 1 . . . . 441 PRO CB . 16940 1 565 . 1 1 158 158 ASP H H 1 7.12 0.05 . 1 . . . . 442 ASP H . 16940 1 566 . 1 1 158 158 ASP CA C 13 48.75 0.30 . 1 . . . . 442 ASP CA . 16940 1 567 . 1 1 158 158 ASP CB C 13 39.24 0.30 . 1 . . . . 442 ASP CB . 16940 1 568 . 1 1 158 158 ASP N N 15 118.20 0.30 . 1 . . . . 442 ASP N . 16940 1 569 . 1 1 159 159 ARG CA C 13 56.82 0.30 . 1 . . . . 443 ARG CA . 16940 1 570 . 1 1 159 159 ARG CB C 13 26.42 0.30 . 1 . . . . 443 ARG CB . 16940 1 571 . 1 1 160 160 GLU H H 1 8.39 0.05 . 1 . . . . 444 GLU H . 16940 1 572 . 1 1 160 160 GLU CA C 13 56.60 0.30 . 1 . . . . 444 GLU CA . 16940 1 573 . 1 1 160 160 GLU CB C 13 25.36 0.30 . 1 . . . . 444 GLU CB . 16940 1 574 . 1 1 160 160 GLU N N 15 119.33 0.30 . 1 . . . . 444 GLU N . 16940 1 575 . 1 1 161 161 THR H H 1 7.90 0.05 . 1 . . . . 445 THR H . 16940 1 576 . 1 1 161 161 THR CA C 13 64.05 0.30 . 1 . . . . 445 THR CA . 16940 1 577 . 1 1 161 161 THR CB C 13 64.53 0.30 . 1 . . . . 445 THR CB . 16940 1 578 . 1 1 161 161 THR N N 15 119.20 0.30 . 1 . . . . 445 THR N . 16940 1 579 . 1 1 162 162 ALA H H 1 7.84 0.05 . 1 . . . . 446 ALA H . 16940 1 580 . 1 1 162 162 ALA CA C 13 52.37 0.30 . 1 . . . . 446 ALA CA . 16940 1 581 . 1 1 162 162 ALA CB C 13 13.94 0.30 . 1 . . . . 446 ALA CB . 16940 1 582 . 1 1 162 162 ALA N N 15 121.77 0.30 . 1 . . . . 446 ALA N . 16940 1 583 . 1 1 163 163 ALA H H 1 7.78 0.05 . 1 . . . . 447 ALA H . 16940 1 584 . 1 1 163 163 ALA CA C 13 51.42 0.30 . 1 . . . . 447 ALA CA . 16940 1 585 . 1 1 163 163 ALA CB C 13 14.76 0.30 . 1 . . . . 447 ALA CB . 16940 1 586 . 1 1 163 163 ALA N N 15 118.49 0.30 . 1 . . . . 447 ALA N . 16940 1 587 . 1 1 164 164 SER H H 1 7.54 0.05 . 1 . . . . 448 SER H . 16940 1 588 . 1 1 164 164 SER CA C 13 58.20 0.30 . 1 . . . . 448 SER CA . 16940 1 589 . 1 1 164 164 SER CB C 13 60.55 0.30 . 1 . . . . 448 SER CB . 16940 1 590 . 1 1 164 164 SER N N 15 110.76 0.30 . 1 . . . . 448 SER N . 16940 1 591 . 1 1 165 165 LEU H H 1 7.55 0.05 . 1 . . . . 449 LEU H . 16940 1 592 . 1 1 165 165 LEU CA C 13 52.58 0.30 . 1 . . . . 449 LEU CA . 16940 1 593 . 1 1 165 165 LEU CB C 13 38.83 0.30 . 1 . . . . 449 LEU CB . 16940 1 594 . 1 1 165 165 LEU N N 15 116.44 0.30 . 1 . . . . 449 LEU N . 16940 1 595 . 1 1 166 166 LEU H H 1 7.23 0.05 . 1 . . . . 450 LEU H . 16940 1 596 . 1 1 166 166 LEU CA C 13 50.36 0.30 . 1 . . . . 450 LEU CA . 16940 1 597 . 1 1 166 166 LEU CB C 13 38.72 0.30 . 1 . . . . 450 LEU CB . 16940 1 598 . 1 1 166 166 LEU N N 15 118.99 0.30 . 1 . . . . 450 LEU N . 16940 1 599 . 1 1 167 167 GLN H H 1 7.29 0.05 . 1 . . . . 451 GLN H . 16940 1 600 . 1 1 167 167 GLN CA C 13 50.20 0.30 . 1 . . . . 451 GLN CA . 16940 1 601 . 1 1 167 167 GLN CB C 13 27.23 0.30 . 1 . . . . 451 GLN CB . 16940 1 602 . 1 1 167 167 GLN N N 15 123.00 0.30 . 1 . . . . 451 GLN N . 16940 1 603 . 1 1 168 168 ALA H H 1 8.18 0.05 . 1 . . . . 452 ALA H . 16940 1 604 . 1 1 168 168 ALA CA C 13 50.36 0.30 . 1 . . . . 452 ALA CA . 16940 1 605 . 1 1 168 168 ALA CB C 13 14.58 0.30 . 1 . . . . 452 ALA CB . 16940 1 606 . 1 1 168 168 ALA N N 15 123.36 0.30 . 1 . . . . 452 ALA N . 16940 1 607 . 1 1 169 169 GLY H H 1 8.96 0.05 . 1 . . . . 453 GLY H . 16940 1 608 . 1 1 169 169 GLY CA C 13 42.22 0.30 . 1 . . . . 453 GLY CA . 16940 1 609 . 1 1 169 169 GLY N N 15 111.31 0.30 . 1 . . . . 453 GLY N . 16940 1 610 . 1 1 170 170 TYR H H 1 8.07 0.05 . 1 . . . . 454 TYR H . 16940 1 611 . 1 1 170 170 TYR CA C 13 53.30 0.30 . 1 . . . . 454 TYR CA . 16940 1 612 . 1 1 170 170 TYR CB C 13 33.30 0.30 . 1 . . . . 454 TYR CB . 16940 1 613 . 1 1 170 170 TYR N N 15 123.87 0.30 . 1 . . . . 454 TYR N . 16940 1 614 . 1 1 171 171 LYS H H 1 8.95 0.05 . 1 . . . . 455 LYS H . 16940 1 615 . 1 1 171 171 LYS CA C 13 53.08 0.30 . 1 . . . . 455 LYS CA . 16940 1 616 . 1 1 171 171 LYS CB C 13 33.05 0.30 . 1 . . . . 455 LYS CB . 16940 1 617 . 1 1 171 171 LYS N N 15 119.77 0.30 . 1 . . . . 455 LYS N . 16940 1 618 . 1 1 172 172 GLY H H 1 8.44 0.05 . 1 . . . . 456 GLY H . 16940 1 619 . 1 1 172 172 GLY CA C 13 40.95 0.30 . 1 . . . . 456 GLY CA . 16940 1 620 . 1 1 172 172 GLY N N 15 107.61 0.30 . 1 . . . . 456 GLY N . 16940 1 621 . 1 1 173 173 ARG H H 1 8.59 0.05 . 1 . . . . 457 ARG H . 16940 1 622 . 1 1 173 173 ARG CA C 13 51.30 0.30 . 1 . . . . 457 ARG CA . 16940 1 623 . 1 1 173 173 ARG CB C 13 31.62 0.30 . 1 . . . . 457 ARG CB . 16940 1 624 . 1 1 173 173 ARG N N 15 120.19 0.30 . 1 . . . . 457 ARG N . 16940 1 625 . 1 1 174 174 VAL H H 1 9.29 0.05 . 1 . . . . 458 VAL H . 16940 1 626 . 1 1 174 174 VAL CA C 13 58.01 0.30 . 1 . . . . 458 VAL CA . 16940 1 627 . 1 1 174 174 VAL CB C 13 31.47 0.30 . 1 . . . . 458 VAL CB . 16940 1 628 . 1 1 174 174 VAL N N 15 128.35 0.30 . 1 . . . . 458 VAL N . 16940 1 629 . 1 1 175 175 THR H H 1 6.73 0.05 . 1 . . . . 459 THR H . 16940 1 630 . 1 1 175 175 THR CA C 13 53.93 0.30 . 1 . . . . 459 THR CA . 16940 1 631 . 1 1 175 175 THR CB C 13 68.73 0.30 . 1 . . . . 459 THR CB . 16940 1 632 . 1 1 175 175 THR N N 15 111.84 0.30 . 1 . . . . 459 THR N . 16940 1 633 . 1 1 176 176 GLY H H 1 7.95 0.05 . 1 . . . . 460 GLY H . 16940 1 634 . 1 1 176 176 GLY CA C 13 43.83 0.30 . 1 . . . . 460 GLY CA . 16940 1 635 . 1 1 176 176 GLY N N 15 105.81 0.30 . 1 . . . . 460 GLY N . 16940 1 636 . 1 1 177 177 TRP H H 1 9.56 0.05 . 1 . . . . 461 TRP H . 16940 1 637 . 1 1 177 177 TRP CA C 13 55.70 0.30 . 1 . . . . 461 TRP CA . 16940 1 638 . 1 1 177 177 TRP CB C 13 26.21 0.30 . 1 . . . . 461 TRP CB . 16940 1 639 . 1 1 177 177 TRP N N 15 122.73 0.30 . 1 . . . . 461 TRP N . 16940 1 640 . 1 1 178 178 GLY H H 1 8.72 0.05 . 1 . . . . 462 GLY H . 16940 1 641 . 1 1 178 178 GLY CA C 13 40.76 0.30 . 1 . . . . 462 GLY CA . 16940 1 642 . 1 1 178 178 GLY N N 15 107.80 0.30 . 1 . . . . 462 GLY N . 16940 1 643 . 1 1 179 179 ASN H H 1 8.20 0.05 . 1 . . . . 463 ASN H . 16940 1 644 . 1 1 179 179 ASN CA C 13 51.28 0.30 . 1 . . . . 463 ASN CA . 16940 1 645 . 1 1 179 179 ASN CB C 13 35.80 0.30 . 1 . . . . 463 ASN CB . 16940 1 646 . 1 1 179 179 ASN N N 15 116.01 0.30 . 1 . . . . 463 ASN N . 16940 1 647 . 1 1 180 180 LEU H H 1 8.26 0.05 . 1 . . . . 464 LEU H . 16940 1 648 . 1 1 180 180 LEU CA C 13 52.09 0.30 . 1 . . . . 464 LEU CA . 16940 1 649 . 1 1 180 180 LEU CB C 13 40.42 0.30 . 1 . . . . 464 LEU CB . 16940 1 650 . 1 1 180 180 LEU N N 15 120.08 0.30 . 1 . . . . 464 LEU N . 16940 1 651 . 1 1 181 181 LYS H H 1 7.50 0.05 . 1 . . . . 465 LYS H . 16940 1 652 . 1 1 181 181 LYS CA C 13 51.10 0.30 . 1 . . . . 465 LYS CA . 16940 1 653 . 1 1 181 181 LYS CB C 13 34.09 0.30 . 1 . . . . 465 LYS CB . 16940 1 654 . 1 1 181 181 LYS N N 15 113.71 0.30 . 1 . . . . 465 LYS N . 16940 1 655 . 1 1 182 182 GLU H H 1 9.07 0.05 . 1 . . . . 466 GLU H . 16940 1 656 . 1 1 182 182 GLU CA C 13 56.43 0.30 . 1 . . . . 466 GLU CA . 16940 1 657 . 1 1 182 182 GLU CB C 13 27.03 0.30 . 1 . . . . 466 GLU CB . 16940 1 658 . 1 1 182 182 GLU N N 15 121.47 0.30 . 1 . . . . 466 GLU N . 16940 1 659 . 1 1 183 183 THR H H 1 7.80 0.05 . 1 . . . . 467 THR H . 16940 1 660 . 1 1 183 183 THR CA C 13 58.09 0.30 . 1 . . . . 467 THR CA . 16940 1 661 . 1 1 183 183 THR N N 15 111.65 0.30 . 1 . . . . 467 THR N . 16940 1 662 . 1 1 194 194 SER CA C 13 57.07 0.30 . 1 . . . . 478 SER CA . 16940 1 663 . 1 1 194 194 SER CB C 13 60.18 0.30 . 1 . . . . 478 SER CB . 16940 1 664 . 1 1 195 195 VAL H H 1 7.55 0.05 . 1 . . . . 479 VAL H . 16940 1 665 . 1 1 195 195 VAL CA C 13 55.26 0.30 . 1 . . . . 479 VAL CA . 16940 1 666 . 1 1 195 195 VAL CB C 13 32.55 0.30 . 1 . . . . 479 VAL CB . 16940 1 667 . 1 1 195 195 VAL N N 15 113.02 0.30 . 1 . . . . 479 VAL N . 16940 1 668 . 1 1 196 196 LEU H H 1 7.09 0.05 . 1 . . . . 480 LEU H . 16940 1 669 . 1 1 196 196 LEU CA C 13 53.37 0.30 . 1 . . . . 480 LEU CA . 16940 1 670 . 1 1 196 196 LEU CB C 13 38.64 0.30 . 1 . . . . 480 LEU CB . 16940 1 671 . 1 1 196 196 LEU N N 15 122.28 0.30 . 1 . . . . 480 LEU N . 16940 1 672 . 1 1 197 197 GLN H H 1 7.15 0.05 . 1 . . . . 481 GLN H . 16940 1 673 . 1 1 197 197 GLN CA C 13 49.77 0.30 . 1 . . . . 481 GLN CA . 16940 1 674 . 1 1 197 197 GLN CB C 13 30.55 0.30 . 1 . . . . 481 GLN CB . 16940 1 675 . 1 1 197 197 GLN N N 15 122.75 0.30 . 1 . . . . 481 GLN N . 16940 1 676 . 1 1 198 198 VAL H H 1 8.97 0.05 . 1 . . . . 482 VAL H . 16940 1 677 . 1 1 198 198 VAL CA C 13 56.01 0.30 . 1 . . . . 482 VAL CA . 16940 1 678 . 1 1 198 198 VAL CB C 13 32.63 0.30 . 1 . . . . 482 VAL CB . 16940 1 679 . 1 1 198 198 VAL N N 15 118.82 0.30 . 1 . . . . 482 VAL N . 16940 1 680 . 1 1 199 199 VAL H H 1 8.72 0.05 . 1 . . . . 483 VAL H . 16940 1 681 . 1 1 199 199 VAL CA C 13 57.86 0.30 . 1 . . . . 483 VAL CA . 16940 1 682 . 1 1 199 199 VAL CB C 13 32.30 0.30 . 1 . . . . 483 VAL CB . 16940 1 683 . 1 1 199 199 VAL N N 15 126.15 0.30 . 1 . . . . 483 VAL N . 16940 1 684 . 1 1 200 200 ASN H H 1 8.59 0.05 . 1 . . . . 484 ASN H . 16940 1 685 . 1 1 200 200 ASN CA C 13 48.38 0.30 . 1 . . . . 484 ASN CA . 16940 1 686 . 1 1 200 200 ASN CB C 13 36.47 0.30 . 1 . . . . 484 ASN CB . 16940 1 687 . 1 1 200 200 ASN N N 15 126.45 0.30 . 1 . . . . 484 ASN N . 16940 1 688 . 1 1 201 201 LEU H H 1 8.95 0.05 . 1 . . . . 485 LEU H . 16940 1 689 . 1 1 201 201 LEU CA C 13 48.57 0.30 . 1 . . . . 485 LEU CA . 16940 1 690 . 1 1 201 201 LEU CB C 13 43.99 0.30 . 1 . . . . 485 LEU CB . 16940 1 691 . 1 1 201 201 LEU N N 15 121.39 0.30 . 1 . . . . 485 LEU N . 16940 1 692 . 1 1 202 202 PRO CA C 13 58.28 0.30 . 1 . . . . 486 PRO CA . 16940 1 693 . 1 1 202 202 PRO CB C 13 28.10 0.30 . 1 . . . . 486 PRO CB . 16940 1 694 . 1 1 203 203 ILE H H 1 8.60 0.05 . 1 . . . . 487 ILE H . 16940 1 695 . 1 1 203 203 ILE CA C 13 59.80 0.30 . 1 . . . . 487 ILE CA . 16940 1 696 . 1 1 203 203 ILE CB C 13 33.97 0.30 . 1 . . . . 487 ILE CB . 16940 1 697 . 1 1 203 203 ILE N N 15 122.37 0.30 . 1 . . . . 487 ILE N . 16940 1 698 . 1 1 204 204 VAL H H 1 7.88 0.05 . 1 . . . . 488 VAL H . 16940 1 699 . 1 1 204 204 VAL CA C 13 59.12 0.30 . 1 . . . . 488 VAL CA . 16940 1 700 . 1 1 204 204 VAL CB C 13 30.14 0.30 . 1 . . . . 488 VAL CB . 16940 1 701 . 1 1 204 204 VAL N N 15 133.56 0.30 . 1 . . . . 488 VAL N . 16940 1 702 . 1 1 205 205 GLU H H 1 9.56 0.05 . 1 . . . . 489 GLU H . 16940 1 703 . 1 1 205 205 GLU CA C 13 54.27 0.30 . 1 . . . . 489 GLU CA . 16940 1 704 . 1 1 205 205 GLU CB C 13 26.38 0.30 . 1 . . . . 489 GLU CB . 16940 1 705 . 1 1 205 205 GLU N N 15 126.33 0.30 . 1 . . . . 489 GLU N . 16940 1 706 . 1 1 206 206 ARG H H 1 8.83 0.05 . 1 . . . . 490 ARG H . 16940 1 707 . 1 1 206 206 ARG CA C 13 59.12 0.30 . 1 . . . . 490 ARG CA . 16940 1 708 . 1 1 206 206 ARG N N 15 124.40 0.30 . 1 . . . . 490 ARG N . 16940 1 709 . 1 1 207 207 PRO CA C 13 63.24 0.30 . 1 . . . . 491 PRO CA . 16940 1 710 . 1 1 207 207 PRO CB C 13 27.78 0.30 . 1 . . . . 491 PRO CB . 16940 1 711 . 1 1 208 208 VAL H H 1 6.73 0.05 . 1 . . . . 492 VAL H . 16940 1 712 . 1 1 208 208 VAL CA C 13 62.43 0.30 . 1 . . . . 492 VAL CA . 16940 1 713 . 1 1 208 208 VAL CB C 13 27.35 0.30 . 1 . . . . 492 VAL CB . 16940 1 714 . 1 1 208 208 VAL N N 15 117.57 0.30 . 1 . . . . 492 VAL N . 16940 1 715 . 1 1 209 209 CYS H H 1 7.67 0.05 . 1 . . . . 493 CYS H . 16940 1 716 . 1 1 209 209 CYS CA C 13 54.10 0.30 . 1 . . . . 493 CYS CA . 16940 1 717 . 1 1 209 209 CYS CB C 13 35.04 0.30 . 1 . . . . 493 CYS CB . 16940 1 718 . 1 1 209 209 CYS N N 15 118.47 0.30 . 1 . . . . 493 CYS N . 16940 1 719 . 1 1 210 210 LYS H H 1 8.68 0.05 . 1 . . . . 494 LYS H . 16940 1 720 . 1 1 210 210 LYS CA C 13 56.89 0.30 . 1 . . . . 494 LYS CA . 16940 1 721 . 1 1 210 210 LYS CB C 13 29.13 0.30 . 1 . . . . 494 LYS CB . 16940 1 722 . 1 1 210 210 LYS N N 15 121.59 0.30 . 1 . . . . 494 LYS N . 16940 1 723 . 1 1 211 211 ASP H H 1 7.74 0.05 . 1 . . . . 495 ASP H . 16940 1 724 . 1 1 211 211 ASP CA C 13 53.00 0.30 . 1 . . . . 495 ASP CA . 16940 1 725 . 1 1 211 211 ASP CB C 13 37.59 0.30 . 1 . . . . 495 ASP CB . 16940 1 726 . 1 1 211 211 ASP N N 15 116.25 0.30 . 1 . . . . 495 ASP N . 16940 1 727 . 1 1 212 212 SER H H 1 7.80 0.05 . 1 . . . . 496 SER H . 16940 1 728 . 1 1 212 212 SER CA C 13 57.35 0.30 . 1 . . . . 496 SER CA . 16940 1 729 . 1 1 212 212 SER CB C 13 61.91 0.30 . 1 . . . . 496 SER CB . 16940 1 730 . 1 1 212 212 SER N N 15 114.01 0.30 . 1 . . . . 496 SER N . 16940 1 731 . 1 1 213 213 THR H H 1 7.54 0.05 . 1 . . . . 497 THR H . 16940 1 732 . 1 1 213 213 THR CA C 13 57.05 0.30 . 1 . . . . 497 THR CA . 16940 1 733 . 1 1 213 213 THR CB C 13 66.50 0.30 . 1 . . . . 497 THR CB . 16940 1 734 . 1 1 213 213 THR N N 15 118.27 0.30 . 1 . . . . 497 THR N . 16940 1 735 . 1 1 214 214 ARG H H 1 8.73 0.05 . 1 . . . . 498 ARG H . 16940 1 736 . 1 1 214 214 ARG CA C 13 52.62 0.30 . 1 . . . . 498 ARG CA . 16940 1 737 . 1 1 214 214 ARG CB C 13 26.72 0.30 . 1 . . . . 498 ARG CB . 16940 1 738 . 1 1 214 214 ARG N N 15 124.14 0.30 . 1 . . . . 498 ARG N . 16940 1 739 . 1 1 215 215 ILE H H 1 8.14 0.05 . 1 . . . . 499 ILE H . 16940 1 740 . 1 1 215 215 ILE CA C 13 58.81 0.30 . 1 . . . . 499 ILE CA . 16940 1 741 . 1 1 215 215 ILE CB C 13 32.86 0.30 . 1 . . . . 499 ILE CB . 16940 1 742 . 1 1 215 215 ILE N N 15 126.96 0.30 . 1 . . . . 499 ILE N . 16940 1 743 . 1 1 216 216 ARG H H 1 8.13 0.05 . 1 . . . . 500 ARG H . 16940 1 744 . 1 1 216 216 ARG CA C 13 53.53 0.30 . 1 . . . . 500 ARG CA . 16940 1 745 . 1 1 216 216 ARG CB C 13 26.63 0.30 . 1 . . . . 500 ARG CB . 16940 1 746 . 1 1 216 216 ARG N N 15 127.58 0.30 . 1 . . . . 500 ARG N . 16940 1 747 . 1 1 217 217 ILE H H 1 7.70 0.05 . 1 . . . . 501 ILE H . 16940 1 748 . 1 1 217 217 ILE CA C 13 57.16 0.30 . 1 . . . . 501 ILE CA . 16940 1 749 . 1 1 217 217 ILE CB C 13 35.88 0.30 . 1 . . . . 501 ILE CB . 16940 1 750 . 1 1 217 217 ILE N N 15 123.67 0.30 . 1 . . . . 501 ILE N . 16940 1 751 . 1 1 218 218 THR H H 1 7.23 0.05 . 1 . . . . 502 THR H . 16940 1 752 . 1 1 218 218 THR CA C 13 56.13 0.30 . 1 . . . . 502 THR CA . 16940 1 753 . 1 1 218 218 THR CB C 13 69.12 0.30 . 1 . . . . 502 THR CB . 16940 1 754 . 1 1 218 218 THR N N 15 110.86 0.30 . 1 . . . . 502 THR N . 16940 1 755 . 1 1 219 219 ASP CA C 13 52.82 0.30 . 1 . . . . 503 ASP CA . 16940 1 756 . 1 1 219 219 ASP CB C 13 36.97 0.30 . 1 . . . . 503 ASP CB . 16940 1 757 . 1 1 220 220 ASN H H 1 8.08 0.05 . 1 . . . . 504 ASN H . 16940 1 758 . 1 1 220 220 ASN CA C 13 51.15 0.30 . 1 . . . . 504 ASN CA . 16940 1 759 . 1 1 220 220 ASN CB C 13 34.80 0.30 . 1 . . . . 504 ASN CB . 16940 1 760 . 1 1 220 220 ASN N N 15 112.55 0.30 . 1 . . . . 504 ASN N . 16940 1 761 . 1 1 221 221 MET H H 1 8.23 0.05 . 1 . . . . 505 MET H . 16940 1 762 . 1 1 221 221 MET CA C 13 51.77 0.30 . 1 . . . . 505 MET CA . 16940 1 763 . 1 1 221 221 MET CB C 13 33.58 0.30 . 1 . . . . 505 MET CB . 16940 1 764 . 1 1 221 221 MET N N 15 124.17 0.30 . 1 . . . . 505 MET N . 16940 1 765 . 1 1 222 222 PHE H H 1 8.90 0.05 . 1 . . . . 506 PHE H . 16940 1 766 . 1 1 222 222 PHE CA C 13 53.91 0.30 . 1 . . . . 506 PHE CA . 16940 1 767 . 1 1 222 222 PHE CB C 13 37.72 0.30 . 1 . . . . 506 PHE CB . 16940 1 768 . 1 1 222 222 PHE N N 15 117.13 0.30 . 1 . . . . 506 PHE N . 16940 1 769 . 1 1 223 223 CYS H H 1 8.74 0.05 . 1 . . . . 507 CYS H . 16940 1 770 . 1 1 223 223 CYS CA C 13 52.36 0.30 . 1 . . . . 507 CYS CA . 16940 1 771 . 1 1 223 223 CYS CB C 13 38.52 0.30 . 1 . . . . 507 CYS CB . 16940 1 772 . 1 1 223 223 CYS N N 15 121.08 0.30 . 1 . . . . 507 CYS N . 16940 1 773 . 1 1 224 224 ALA H H 1 8.52 0.05 . 1 . . . . 508 ALA H . 16940 1 774 . 1 1 224 224 ALA CA C 13 48.52 0.30 . 1 . . . . 508 ALA CA . 16940 1 775 . 1 1 224 224 ALA CB C 13 20.41 0.30 . 1 . . . . 508 ALA CB . 16940 1 776 . 1 1 224 224 ALA N N 15 120.93 0.30 . 1 . . . . 508 ALA N . 16940 1 777 . 1 1 225 225 GLY H H 1 8.73 0.05 . 1 . . . . 509 GLY H . 16940 1 778 . 1 1 225 225 GLY CA C 13 41.46 0.30 . 1 . . . . 509 GLY CA . 16940 1 779 . 1 1 225 225 GLY N N 15 110.03 0.30 . 1 . . . . 509 GLY N . 16940 1 780 . 1 1 226 226 TYR H H 1 9.52 0.05 . 1 . . . . 510 TYR H . 16940 1 781 . 1 1 226 226 TYR CA C 13 56.80 0.30 . 1 . . . . 510 TYR CA . 16940 1 782 . 1 1 226 226 TYR CB C 13 35.83 0.30 . 1 . . . . 510 TYR CB . 16940 1 783 . 1 1 226 226 TYR N N 15 118.87 0.30 . 1 . . . . 510 TYR N . 16940 1 784 . 1 1 227 227 LYS H H 1 10.01 0.05 . 1 . . . . 511 LYS H . 16940 1 785 . 1 1 227 227 LYS CA C 13 52.21 0.30 . 1 . . . . 511 LYS CA . 16940 1 786 . 1 1 227 227 LYS CB C 13 28.33 0.30 . 1 . . . . 511 LYS CB . 16940 1 787 . 1 1 227 227 LYS N N 15 124.64 0.30 . 1 . . . . 511 LYS N . 16940 1 788 . 1 1 228 228 PRO CA C 13 62.59 0.30 . 1 . . . . 512 PRO CA . 16940 1 789 . 1 1 228 228 PRO CB C 13 28.48 0.30 . 1 . . . . 512 PRO CB . 16940 1 790 . 1 1 229 229 ASP H H 1 8.40 0.05 . 1 . . . . 513 ASP H . 16940 1 791 . 1 1 229 229 ASP CA C 13 51.50 0.30 . 1 . . . . 513 ASP CA . 16940 1 792 . 1 1 229 229 ASP CB C 13 36.75 0.30 . 1 . . . . 513 ASP CB . 16940 1 793 . 1 1 229 229 ASP N N 15 113.67 0.30 . 1 . . . . 513 ASP N . 16940 1 794 . 1 1 230 230 GLU H H 1 7.73 0.05 . 1 . . . . 514 GLU H . 16940 1 795 . 1 1 230 230 GLU CA C 13 55.05 0.30 . 1 . . . . 514 GLU CA . 16940 1 796 . 1 1 230 230 GLU CB C 13 27.97 0.30 . 1 . . . . 514 GLU CB . 16940 1 797 . 1 1 230 230 GLU N N 15 118.06 0.30 . 1 . . . . 514 GLU N . 16940 1 798 . 1 1 231 231 GLY H H 1 8.03 0.05 . 1 . . . . 515 GLY H . 16940 1 799 . 1 1 231 231 GLY CA C 13 43.67 0.30 . 1 . . . . 515 GLY CA . 16940 1 800 . 1 1 231 231 GLY N N 15 107.58 0.30 . 1 . . . . 515 GLY N . 16940 1 801 . 1 1 232 232 LYS H H 1 6.68 0.05 . 1 . . . . 516 LYS H . 16940 1 802 . 1 1 232 232 LYS CA C 13 51.97 0.30 . 1 . . . . 516 LYS CA . 16940 1 803 . 1 1 232 232 LYS CB C 13 30.79 0.30 . 1 . . . . 516 LYS CB . 16940 1 804 . 1 1 232 232 LYS N N 15 119.42 0.30 . 1 . . . . 516 LYS N . 16940 1 805 . 1 1 233 233 ARG H H 1 7.95 0.05 . 1 . . . . 517 ARG H . 16940 1 806 . 1 1 233 233 ARG CA C 13 51.68 0.30 . 1 . . . . 517 ARG CA . 16940 1 807 . 1 1 233 233 ARG CB C 13 29.10 0.30 . 1 . . . . 517 ARG CB . 16940 1 808 . 1 1 233 233 ARG N N 15 118.28 0.30 . 1 . . . . 517 ARG N . 16940 1 809 . 1 1 234 234 GLY H H 1 8.60 0.05 . 1 . . . . 518 GLY H . 16940 1 810 . 1 1 234 234 GLY CA C 13 41.62 0.30 . 1 . . . . 518 GLY CA . 16940 1 811 . 1 1 234 234 GLY N N 15 107.21 0.30 . 1 . . . . 518 GLY N . 16940 1 812 . 1 1 235 235 ASP H H 1 8.25 0.05 . 1 . . . . 519 ASP H . 16940 1 813 . 1 1 235 235 ASP CA C 13 50.11 0.30 . 1 . . . . 519 ASP CA . 16940 1 814 . 1 1 235 235 ASP CB C 13 41.01 0.30 . 1 . . . . 519 ASP CB . 16940 1 815 . 1 1 235 235 ASP N N 15 117.86 0.30 . 1 . . . . 519 ASP N . 16940 1 816 . 1 1 236 236 ALA H H 1 8.80 0.05 . 1 . . . . 520 ALA H . 16940 1 817 . 1 1 236 236 ALA CA C 13 49.13 0.30 . 1 . . . . 520 ALA CA . 16940 1 818 . 1 1 236 236 ALA CB C 13 17.75 0.30 . 1 . . . . 520 ALA CB . 16940 1 819 . 1 1 236 236 ALA N N 15 124.49 0.30 . 1 . . . . 520 ALA N . 16940 1 820 . 1 1 237 237 CYS H H 1 9.55 0.05 . 1 . . . . 521 CYS H . 16940 1 821 . 1 1 237 237 CYS CA C 13 51.35 0.30 . 1 . . . . 521 CYS CA . 16940 1 822 . 1 1 237 237 CYS CB C 13 33.91 0.30 . 1 . . . . 521 CYS CB . 16940 1 823 . 1 1 237 237 CYS N N 15 115.23 0.30 . 1 . . . . 521 CYS N . 16940 1 824 . 1 1 238 238 GLU H H 1 8.14 0.05 . 1 . . . . 522 GLU H . 16940 1 825 . 1 1 238 238 GLU CA C 13 57.85 0.30 . 1 . . . . 522 GLU CA . 16940 1 826 . 1 1 238 238 GLU CB C 13 25.30 0.30 . 1 . . . . 522 GLU CB . 16940 1 827 . 1 1 238 238 GLU N N 15 123.07 0.30 . 1 . . . . 522 GLU N . 16940 1 828 . 1 1 241 241 SER CA C 13 55.74 0.30 . 1 . . . . 525 SER CA . 16940 1 829 . 1 1 241 241 SER CB C 13 59.49 0.30 . 1 . . . . 525 SER CB . 16940 1 830 . 1 1 242 242 GLY H H 1 8.98 0.05 . 1 . . . . 526 GLY H . 16940 1 831 . 1 1 242 242 GLY CA C 13 43.14 0.30 . 1 . . . . 526 GLY CA . 16940 1 832 . 1 1 242 242 GLY N N 15 110.67 0.30 . 1 . . . . 526 GLY N . 16940 1 833 . 1 1 243 243 GLY H H 1 8.07 0.05 . 1 . . . . 527 GLY H . 16940 1 834 . 1 1 243 243 GLY CA C 13 41.14 0.30 . 1 . . . . 527 GLY CA . 16940 1 835 . 1 1 243 243 GLY N N 15 105.11 0.30 . 1 . . . . 527 GLY N . 16940 1 836 . 1 1 244 244 PRO CA C 13 60.12 0.30 . 1 . . . . 528 PRO CA . 16940 1 837 . 1 1 244 244 PRO CB C 13 27.84 0.30 . 1 . . . . 528 PRO CB . 16940 1 838 . 1 1 245 245 PHE H H 1 7.93 0.05 . 1 . . . . 529 PHE H . 16940 1 839 . 1 1 245 245 PHE CA C 13 53.19 0.30 . 1 . . . . 529 PHE CA . 16940 1 840 . 1 1 245 245 PHE CB C 13 36.95 0.30 . 1 . . . . 529 PHE CB . 16940 1 841 . 1 1 245 245 PHE N N 15 123.88 0.30 . 1 . . . . 529 PHE N . 16940 1 842 . 1 1 246 246 VAL H H 1 9.58 0.05 . 1 . . . . 530 VAL H . 16940 1 843 . 1 1 246 246 VAL CA C 13 55.89 0.30 . 1 . . . . 530 VAL CA . 16940 1 844 . 1 1 246 246 VAL CB C 13 31.84 0.30 . 1 . . . . 530 VAL CB . 16940 1 845 . 1 1 246 246 VAL N N 15 122.83 0.30 . 1 . . . . 530 VAL N . 16940 1 846 . 1 1 247 247 MET H H 1 9.18 0.05 . 1 . . . . 531 MET H . 16940 1 847 . 1 1 247 247 MET CA C 13 52.36 0.30 . 1 . . . . 531 MET CA . 16940 1 848 . 1 1 247 247 MET CB C 13 35.86 0.30 . 1 . . . . 531 MET CB . 16940 1 849 . 1 1 247 247 MET N N 15 118.55 0.30 . 1 . . . . 531 MET N . 16940 1 850 . 1 1 248 248 LYS H H 1 6.77 0.05 . 1 . . . . 532 LYS H . 16940 1 851 . 1 1 248 248 LYS CA C 13 51.35 0.30 . 1 . . . . 532 LYS CA . 16940 1 852 . 1 1 248 248 LYS CB C 13 28.35 0.30 . 1 . . . . 532 LYS CB . 16940 1 853 . 1 1 248 248 LYS N N 15 123.29 0.30 . 1 . . . . 532 LYS N . 16940 1 854 . 1 1 249 249 SER H H 1 8.85 0.05 . 1 . . . . 533 SER H . 16940 1 855 . 1 1 249 249 SER CA C 13 51.67 0.30 . 1 . . . . 533 SER CA . 16940 1 856 . 1 1 249 249 SER CB C 13 61.66 0.30 . 1 . . . . 533 SER CB . 16940 1 857 . 1 1 249 249 SER N N 15 120.70 0.30 . 1 . . . . 533 SER N . 16940 1 858 . 1 1 250 250 PRO CA C 13 59.89 0.30 . 1 . . . . 534 PRO CA . 16940 1 859 . 1 1 250 250 PRO CB C 13 28.08 0.30 . 1 . . . . 534 PRO CB . 16940 1 860 . 1 1 251 251 PHE H H 1 7.61 0.05 . 1 . . . . 535 PHE H . 16940 1 861 . 1 1 251 251 PHE CA C 13 55.44 0.30 . 1 . . . . 535 PHE CA . 16940 1 862 . 1 1 251 251 PHE CB C 13 35.44 0.30 . 1 . . . . 535 PHE CB . 16940 1 863 . 1 1 251 251 PHE N N 15 118.52 0.30 . 1 . . . . 535 PHE N . 16940 1 864 . 1 1 252 252 ASN H H 1 7.17 0.05 . 1 . . . . 536 ASN H . 16940 1 865 . 1 1 252 252 ASN CA C 13 48.95 0.30 . 1 . . . . 536 ASN CA . 16940 1 866 . 1 1 252 252 ASN CB C 13 35.77 0.30 . 1 . . . . 536 ASN CB . 16940 1 867 . 1 1 252 252 ASN N N 15 113.30 0.30 . 1 . . . . 536 ASN N . 16940 1 868 . 1 1 253 253 ASN H H 1 7.77 0.05 . 1 . . . . 537 ASN H . 16940 1 869 . 1 1 253 253 ASN CA C 13 52.16 0.30 . 1 . . . . 537 ASN CA . 16940 1 870 . 1 1 253 253 ASN CB C 13 35.40 0.30 . 1 . . . . 537 ASN CB . 16940 1 871 . 1 1 253 253 ASN N N 15 114.20 0.30 . 1 . . . . 537 ASN N . 16940 1 872 . 1 1 254 254 ARG H H 1 7.39 0.05 . 1 . . . . 538 ARG H . 16940 1 873 . 1 1 254 254 ARG CA C 13 52.14 0.30 . 1 . . . . 538 ARG CA . 16940 1 874 . 1 1 254 254 ARG CB C 13 29.29 0.30 . 1 . . . . 538 ARG CB . 16940 1 875 . 1 1 254 254 ARG N N 15 112.84 0.30 . 1 . . . . 538 ARG N . 16940 1 876 . 1 1 255 255 TRP H H 1 8.69 0.05 . 1 . . . . 539 TRP H . 16940 1 877 . 1 1 255 255 TRP CA C 13 54.02 0.30 . 1 . . . . 539 TRP CA . 16940 1 878 . 1 1 255 255 TRP CB C 13 27.70 0.30 . 1 . . . . 539 TRP CB . 16940 1 879 . 1 1 255 255 TRP N N 15 120.62 0.30 . 1 . . . . 539 TRP N . 16940 1 880 . 1 1 256 256 TYR H H 1 8.97 0.05 . 1 . . . . 540 TYR H . 16940 1 881 . 1 1 256 256 TYR CA C 13 53.42 0.30 . 1 . . . . 540 TYR CA . 16940 1 882 . 1 1 256 256 TYR CB C 13 40.06 0.30 . 1 . . . . 540 TYR CB . 16940 1 883 . 1 1 256 256 TYR N N 15 118.44 0.30 . 1 . . . . 540 TYR N . 16940 1 884 . 1 1 257 257 GLN H H 1 8.93 0.05 . 1 . . . . 541 GLN H . 16940 1 885 . 1 1 257 257 GLN CA C 13 52.88 0.30 . 1 . . . . 541 GLN CA . 16940 1 886 . 1 1 257 257 GLN CB C 13 23.47 0.30 . 1 . . . . 541 GLN CB . 16940 1 887 . 1 1 257 257 GLN N N 15 121.67 0.30 . 1 . . . . 541 GLN N . 16940 1 888 . 1 1 258 258 MET H H 1 8.42 0.05 . 1 . . . . 542 MET H . 16940 1 889 . 1 1 258 258 MET CA C 13 50.74 0.30 . 1 . . . . 542 MET CA . 16940 1 890 . 1 1 258 258 MET CB C 13 28.94 0.30 . 1 . . . . 542 MET CB . 16940 1 891 . 1 1 258 258 MET N N 15 121.71 0.30 . 1 . . . . 542 MET N . 16940 1 892 . 1 1 259 259 GLY H H 1 8.88 0.05 . 1 . . . . 543 GLY H . 16940 1 893 . 1 1 259 259 GLY CA C 13 42.30 0.30 . 1 . . . . 543 GLY CA . 16940 1 894 . 1 1 259 259 GLY N N 15 104.77 0.30 . 1 . . . . 543 GLY N . 16940 1 895 . 1 1 260 260 ILE H H 1 7.88 0.05 . 1 . . . . 544 ILE H . 16940 1 896 . 1 1 260 260 ILE CA C 13 57.54 0.30 . 1 . . . . 544 ILE CA . 16940 1 897 . 1 1 260 260 ILE CB C 13 38.66 0.30 . 1 . . . . 544 ILE CB . 16940 1 898 . 1 1 260 260 ILE N N 15 122.29 0.30 . 1 . . . . 544 ILE N . 16940 1 899 . 1 1 261 261 VAL H H 1 9.31 0.05 . 1 . . . . 545 VAL H . 16940 1 900 . 1 1 261 261 VAL CA C 13 62.77 0.30 . 1 . . . . 545 VAL CA . 16940 1 901 . 1 1 261 261 VAL CB C 13 28.51 0.30 . 1 . . . . 545 VAL CB . 16940 1 902 . 1 1 261 261 VAL N N 15 127.29 0.30 . 1 . . . . 545 VAL N . 16940 1 903 . 1 1 262 262 SER H H 1 7.57 0.05 . 1 . . . . 546 SER H . 16940 1 904 . 1 1 262 262 SER CA C 13 56.95 0.30 . 1 . . . . 546 SER CA . 16940 1 905 . 1 1 262 262 SER CB C 13 60.70 0.30 . 1 . . . . 546 SER CB . 16940 1 906 . 1 1 262 262 SER N N 15 122.73 0.30 . 1 . . . . 546 SER N . 16940 1 907 . 1 1 263 263 TRP H H 1 7.91 0.05 . 1 . . . . 547 TRP H . 16940 1 908 . 1 1 263 263 TRP CA C 13 53.59 0.30 . 1 . . . . 547 TRP CA . 16940 1 909 . 1 1 263 263 TRP CB C 13 29.51 0.30 . 1 . . . . 547 TRP CB . 16940 1 910 . 1 1 263 263 TRP N N 15 114.33 0.30 . 1 . . . . 547 TRP N . 16940 1 911 . 1 1 264 264 GLY H H 1 8.88 0.05 . 1 . . . . 548 GLY H . 16940 1 912 . 1 1 264 264 GLY CA C 13 42.36 0.30 . 1 . . . . 548 GLY CA . 16940 1 913 . 1 1 264 264 GLY N N 15 107.18 0.30 . 1 . . . . 548 GLY N . 16940 1 914 . 1 1 265 265 GLU H H 1 9.52 0.05 . 1 . . . . 549 GLU H . 16940 1 915 . 1 1 265 265 GLU CA C 13 53.50 0.30 . 1 . . . . 549 GLU CA . 16940 1 916 . 1 1 265 265 GLU CB C 13 27.94 0.30 . 1 . . . . 549 GLU CB . 16940 1 917 . 1 1 265 265 GLU N N 15 125.27 0.30 . 1 . . . . 549 GLU N . 16940 1 918 . 1 1 266 266 GLY H H 1 8.52 0.05 . 1 . . . . 550 GLY H . 16940 1 919 . 1 1 266 266 GLY CA C 13 41.23 0.30 . 1 . . . . 550 GLY CA . 16940 1 920 . 1 1 266 266 GLY N N 15 113.58 0.30 . 1 . . . . 550 GLY N . 16940 1 921 . 1 1 267 267 CYS H H 1 9.06 0.05 . 1 . . . . 551 CYS H . 16940 1 922 . 1 1 267 267 CYS CA C 13 52.59 0.30 . 1 . . . . 551 CYS CA . 16940 1 923 . 1 1 267 267 CYS CB C 13 42.48 0.30 . 1 . . . . 551 CYS CB . 16940 1 924 . 1 1 267 267 CYS N N 15 117.76 0.30 . 1 . . . . 551 CYS N . 16940 1 925 . 1 1 268 268 ASP H H 1 10.70 0.05 . 1 . . . . 552 ASP H . 16940 1 926 . 1 1 268 268 ASP CA C 13 52.62 0.30 . 1 . . . . 552 ASP CA . 16940 1 927 . 1 1 268 268 ASP CB C 13 39.92 0.30 . 1 . . . . 552 ASP CB . 16940 1 928 . 1 1 268 268 ASP N N 15 126.90 0.30 . 1 . . . . 552 ASP N . 16940 1 929 . 1 1 269 269 ARG H H 1 8.32 0.05 . 1 . . . . 553 ARG H . 16940 1 930 . 1 1 269 269 ARG CA C 13 53.06 0.30 . 1 . . . . 553 ARG CA . 16940 1 931 . 1 1 269 269 ARG CB C 13 27.43 0.30 . 1 . . . . 553 ARG CB . 16940 1 932 . 1 1 269 269 ARG N N 15 117.36 0.30 . 1 . . . . 553 ARG N . 16940 1 933 . 1 1 270 270 ASP H H 1 8.92 0.05 . 1 . . . . 554 ASP H . 16940 1 934 . 1 1 270 270 ASP CA C 13 52.72 0.30 . 1 . . . . 554 ASP CA . 16940 1 935 . 1 1 270 270 ASP CB C 13 36.81 0.30 . 1 . . . . 554 ASP CB . 16940 1 936 . 1 1 270 270 ASP N N 15 124.89 0.30 . 1 . . . . 554 ASP N . 16940 1 937 . 1 1 271 271 GLY H H 1 9.07 0.05 . 1 . . . . 555 GLY H . 16940 1 938 . 1 1 271 271 GLY CA C 13 42.42 0.30 . 1 . . . . 555 GLY CA . 16940 1 939 . 1 1 271 271 GLY N N 15 112.26 0.30 . 1 . . . . 555 GLY N . 16940 1 940 . 1 1 272 272 LYS H H 1 7.01 0.05 . 1 . . . . 556 LYS H . 16940 1 941 . 1 1 272 272 LYS CA C 13 52.43 0.30 . 1 . . . . 556 LYS CA . 16940 1 942 . 1 1 272 272 LYS CB C 13 30.42 0.30 . 1 . . . . 556 LYS CB . 16940 1 943 . 1 1 272 272 LYS N N 15 116.98 0.30 . 1 . . . . 556 LYS N . 16940 1 944 . 1 1 273 273 TYR H H 1 8.99 0.05 . 1 . . . . 557 TYR H . 16940 1 945 . 1 1 273 273 TYR CA C 13 54.51 0.30 . 1 . . . . 557 TYR CA . 16940 1 946 . 1 1 273 273 TYR CB C 13 40.24 0.30 . 1 . . . . 557 TYR CB . 16940 1 947 . 1 1 273 273 TYR N N 15 118.77 0.30 . 1 . . . . 557 TYR N . 16940 1 948 . 1 1 274 274 GLY H H 1 7.62 0.05 . 1 . . . . 558 GLY H . 16940 1 949 . 1 1 274 274 GLY CA C 13 42.98 0.30 . 1 . . . . 558 GLY CA . 16940 1 950 . 1 1 274 274 GLY N N 15 108.84 0.30 . 1 . . . . 558 GLY N . 16940 1 951 . 1 1 275 275 PHE H H 1 8.60 0.05 . 1 . . . . 559 PHE H . 16940 1 952 . 1 1 275 275 PHE CA C 13 54.93 0.30 . 1 . . . . 559 PHE CA . 16940 1 953 . 1 1 275 275 PHE CB C 13 36.86 0.30 . 1 . . . . 559 PHE CB . 16940 1 954 . 1 1 275 275 PHE N N 15 118.71 0.30 . 1 . . . . 559 PHE N . 16940 1 955 . 1 1 276 276 TYR H H 1 8.79 0.05 . 1 . . . . 560 TYR H . 16940 1 956 . 1 1 276 276 TYR CA C 13 53.20 0.30 . 1 . . . . 560 TYR CA . 16940 1 957 . 1 1 276 276 TYR CB C 13 37.66 0.30 . 1 . . . . 560 TYR CB . 16940 1 958 . 1 1 276 276 TYR N N 15 122.65 0.30 . 1 . . . . 560 TYR N . 16940 1 959 . 1 1 277 277 THR H H 1 9.18 0.05 . 1 . . . . 561 THR H . 16940 1 960 . 1 1 277 277 THR CA C 13 60.72 0.30 . 1 . . . . 561 THR CA . 16940 1 961 . 1 1 277 277 THR CB C 13 65.80 0.30 . 1 . . . . 561 THR CB . 16940 1 962 . 1 1 277 277 THR N N 15 120.63 0.30 . 1 . . . . 561 THR N . 16940 1 963 . 1 1 278 278 HIS H H 1 8.50 0.05 . 1 . . . . 562 HIS H . 16940 1 964 . 1 1 278 278 HIS CA C 13 53.22 0.30 . 1 . . . . 562 HIS CA . 16940 1 965 . 1 1 278 278 HIS CB C 13 28.74 0.30 . 1 . . . . 562 HIS CB . 16940 1 966 . 1 1 278 278 HIS N N 15 130.62 0.30 . 1 . . . . 562 HIS N . 16940 1 967 . 1 1 279 279 VAL H H 1 7.76 0.05 . 1 . . . . 563 VAL H . 16940 1 968 . 1 1 279 279 VAL CA C 13 65.13 0.30 . 1 . . . . 563 VAL CA . 16940 1 969 . 1 1 279 279 VAL CB C 13 28.34 0.30 . 1 . . . . 563 VAL CB . 16940 1 970 . 1 1 279 279 VAL N N 15 126.20 0.30 . 1 . . . . 563 VAL N . 16940 1 971 . 1 1 280 280 PHE H H 1 9.85 0.05 . 1 . . . . 564 PHE H . 16940 1 972 . 1 1 280 280 PHE CA C 13 59.76 0.30 . 1 . . . . 564 PHE CA . 16940 1 973 . 1 1 280 280 PHE CB C 13 35.96 0.30 . 1 . . . . 564 PHE CB . 16940 1 974 . 1 1 280 280 PHE N N 15 118.98 0.30 . 1 . . . . 564 PHE N . 16940 1 975 . 1 1 281 281 ARG H H 1 8.31 0.05 . 1 . . . . 565 ARG H . 16940 1 976 . 1 1 281 281 ARG CA C 13 55.66 0.30 . 1 . . . . 565 ARG CA . 16940 1 977 . 1 1 281 281 ARG CB C 13 25.45 0.30 . 1 . . . . 565 ARG CB . 16940 1 978 . 1 1 281 281 ARG N N 15 119.34 0.30 . 1 . . . . 565 ARG N . 16940 1 979 . 1 1 282 282 LEU H H 1 7.31 0.05 . 1 . . . . 566 LEU H . 16940 1 980 . 1 1 282 282 LEU CA C 13 50.73 0.30 . 1 . . . . 566 LEU CA . 16940 1 981 . 1 1 282 282 LEU CB C 13 38.43 0.30 . 1 . . . . 566 LEU CB . 16940 1 982 . 1 1 282 282 LEU N N 15 119.80 0.30 . 1 . . . . 566 LEU N . 16940 1 983 . 1 1 283 283 LYS H H 1 7.62 0.05 . 1 . . . . 567 LYS H . 16940 1 984 . 1 1 283 283 LYS CA C 13 56.84 0.30 . 1 . . . . 567 LYS CA . 16940 1 985 . 1 1 283 283 LYS CB C 13 29.46 0.30 . 1 . . . . 567 LYS CB . 16940 1 986 . 1 1 283 283 LYS N N 15 123.60 0.30 . 1 . . . . 567 LYS N . 16940 1 987 . 1 1 284 284 LYS CA C 13 60.08 0.30 . 1 . . . . 568 LYS CA . 16940 1 988 . 1 1 284 284 LYS CB C 13 27.91 0.30 . 1 . . . . 568 LYS CB . 16940 1 989 . 1 1 285 285 TRP H H 1 7.58 0.05 . 1 . . . . 569 TRP H . 16940 1 990 . 1 1 285 285 TRP CA C 13 59.27 0.30 . 1 . . . . 569 TRP CA . 16940 1 991 . 1 1 285 285 TRP CB C 13 24.14 0.30 . 1 . . . . 569 TRP CB . 16940 1 992 . 1 1 285 285 TRP N N 15 121.04 0.30 . 1 . . . . 569 TRP N . 16940 1 993 . 1 1 286 286 ILE H H 1 7.56 0.05 . 1 . . . . 570 ILE H . 16940 1 994 . 1 1 286 286 ILE CA C 13 61.63 0.30 . 1 . . . . 570 ILE CA . 16940 1 995 . 1 1 286 286 ILE CB C 13 35.05 0.30 . 1 . . . . 570 ILE CB . 16940 1 996 . 1 1 286 286 ILE N N 15 117.59 0.30 . 1 . . . . 570 ILE N . 16940 1 997 . 1 1 287 287 GLN H H 1 8.25 0.05 . 1 . . . . 571 GLN H . 16940 1 998 . 1 1 287 287 GLN CA C 13 55.02 0.30 . 1 . . . . 571 GLN CA . 16940 1 999 . 1 1 287 287 GLN CB C 13 25.56 0.30 . 1 . . . . 571 GLN CB . 16940 1 1000 . 1 1 287 287 GLN N N 15 114.50 0.30 . 1 . . . . 571 GLN N . 16940 1 1001 . 1 1 288 288 LYS H H 1 7.36 0.05 . 1 . . . . 572 LYS H . 16940 1 1002 . 1 1 288 288 LYS CA C 13 55.91 0.30 . 1 . . . . 572 LYS CA . 16940 1 1003 . 1 1 288 288 LYS CB C 13 28.32 0.30 . 1 . . . . 572 LYS CB . 16940 1 1004 . 1 1 288 288 LYS N N 15 119.46 0.30 . 1 . . . . 572 LYS N . 16940 1 1005 . 1 1 289 289 VAL H H 1 7.24 0.05 . 1 . . . . 573 VAL H . 16940 1 1006 . 1 1 289 289 VAL CA C 13 63.17 0.30 . 1 . . . . 573 VAL CA . 16940 1 1007 . 1 1 289 289 VAL CB C 13 27.11 0.30 . 1 . . . . 573 VAL CB . 16940 1 1008 . 1 1 289 289 VAL N N 15 120.39 0.30 . 1 . . . . 573 VAL N . 16940 1 1009 . 1 1 290 290 ILE H H 1 7.17 0.05 . 1 . . . . 574 ILE H . 16940 1 1010 . 1 1 290 290 ILE CA C 13 61.85 0.30 . 1 . . . . 574 ILE CA . 16940 1 1011 . 1 1 290 290 ILE CB C 13 33.80 0.30 . 1 . . . . 574 ILE CB . 16940 1 1012 . 1 1 290 290 ILE N N 15 117.53 0.30 . 1 . . . . 574 ILE N . 16940 1 1013 . 1 1 291 291 ASP H H 1 8.07 0.05 . 1 . . . . 575 ASP H . 16940 1 1014 . 1 1 291 291 ASP CA C 13 53.41 0.30 . 1 . . . . 575 ASP CA . 16940 1 1015 . 1 1 291 291 ASP CB C 13 37.49 0.30 . 1 . . . . 575 ASP CB . 16940 1 1016 . 1 1 291 291 ASP N N 15 119.64 0.30 . 1 . . . . 575 ASP N . 16940 1 1017 . 1 1 292 292 GLN H H 1 7.66 0.05 . 1 . . . . 576 GLN H . 16940 1 1018 . 1 1 292 292 GLN CA C 13 54.55 0.30 . 1 . . . . 576 GLN CA . 16940 1 1019 . 1 1 292 292 GLN CB C 13 25.49 0.30 . 1 . . . . 576 GLN CB . 16940 1 1020 . 1 1 292 292 GLN N N 15 117.97 0.30 . 1 . . . . 576 GLN N . 16940 1 1021 . 1 1 293 293 PHE H H 1 8.05 0.05 . 1 . . . . 577 PHE H . 16940 1 1022 . 1 1 293 293 PHE CA C 13 55.03 0.30 . 1 . . . . 577 PHE CA . 16940 1 1023 . 1 1 293 293 PHE CB C 13 35.85 0.30 . 1 . . . . 577 PHE CB . 16940 1 1024 . 1 1 293 293 PHE N N 15 117.78 0.30 . 1 . . . . 577 PHE N . 16940 1 1025 . 1 1 294 294 GLY H H 1 7.99 0.05 . 1 . . . . 578 GLY H . 16940 1 1026 . 1 1 294 294 GLY CA C 13 43.18 0.30 . 1 . . . . 578 GLY CA . 16940 1 1027 . 1 1 294 294 GLY N N 15 110.38 0.30 . 1 . . . . 578 GLY N . 16940 1 1028 . 1 1 295 295 GLU H H 1 7.84 0.05 . 1 . . . . 579 GLU H . 16940 1 1029 . 1 1 295 295 GLU CA C 13 54.40 0.30 . 1 . . . . 579 GLU CA . 16940 1 1030 . 1 1 295 295 GLU CB C 13 27.81 0.30 . 1 . . . . 579 GLU CB . 16940 1 1031 . 1 1 295 295 GLU N N 15 125.93 0.30 . 1 . . . . 579 GLU N . 16940 1 stop_ save_