data_18028 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18028 _Entry.Title ; Solution NMR structure of CaM bound to the eNOS CaM binding domain peptide ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2011-10-29 _Entry.Accession_date 2011-10-29 _Entry.Last_release_date 2012-05-15 _Entry.Original_release_date 2012-05-15 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype 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 Michael Piazza . . . 18028 2 Kathryn Futrega . . . 18028 3 Donald Spratt . E. . 18028 4 J. Guillemette . Guy . 18028 5 Thorsten Dieckmann . . . 18028 stop_ loop_ _SG_project.SG_project_ID _SG_project.Project_name _SG_project.Full_name_of_center _SG_project.Initial_of_center _SG_project.Entry_ID 1 'not applicable' 'not applicable' . 18028 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID Protein . 18028 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18028 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 144 18028 '15N chemical shifts' 145 18028 '1H chemical shifts' 861 18028 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2012-05-15 2011-10-29 original author . 18028 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 18027 'CaM bound to iNOS peptides' 18028 PDB 2LL7 'BMRB Entry Tracking System' 18028 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 18028 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 22486744 _Citation.Full_citation . _Citation.Title 'Structure and Dynamics of Calmodulin (CaM) Bound to Nitric Oxide Synthase Peptides: Effects of a Phosphomimetic CaM Mutation' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 51 _Citation.Journal_issue 17 _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 3651 _Citation.Page_last 3661 _Citation.Year 2012 _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 Michael Piazza . . . 18028 1 2 Kathryn Futrega . . . 18028 1 3 Donald Spratt . E. . 18028 1 4 Thorsten Dieckmann . . . 18028 1 5 J. Guillemette . Guy . 18028 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18028 _Assembly.ID 1 _Assembly.Name 'CaM bound to NOS peptides' _Assembly.BMRB_code . _Assembly.Number_of_components 2 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _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 CaM 1 $CaM A . yes native no no . . . 18028 1 2 eNOS 2 $eNOS B . no native no no . . . 18028 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_CaM _Entity.Sf_category entity _Entity.Sf_framecode CaM _Entity.Entry_ID 18028 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name CaM _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEE FVQMMTAK ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 148 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 16721.465 _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 BMRB 15184 . calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 2 no BMRB 15185 . calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 3 no BMRB 15186 . calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 4 no BMRB 15187 . calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 5 no BMRB 15188 . calmodulin . . . . . 100.00 148 99.32 100.00 9.77e-100 . . . . 18028 1 6 no BMRB 15191 . Calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 7 no BMRB 15470 . calmodulin . . . . . 100.00 148 99.32 100.00 2.01e-99 . . . . 18028 1 8 no BMRB 15624 . Calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 9 no BMRB 15650 . calmodulin . . . . . 100.00 148 99.32 100.00 3.32e-99 . . . . 18028 1 10 no BMRB 15852 . calmodulin . . . . . 100.00 148 99.32 100.00 3.32e-99 . . . . 18028 1 11 no BMRB 1634 . calmodulin . . . . . 100.00 148 97.30 99.32 2.54e-97 . . . . 18028 1 12 no BMRB 16418 . apoCaM . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 13 no BMRB 16465 . entity_1 . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 14 no BMRB 1648 . calmodulin . . . . . 100.00 148 97.30 99.32 2.54e-97 . . . . 18028 1 15 no BMRB 16764 . CALMODULIN . . . . . 100.00 150 100.00 100.00 5.25e-100 . . . . 18028 1 16 no BMRB 17264 . calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 17 no BMRB 17360 . entity_1 . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 18 no BMRB 17771 . Calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 19 no BMRB 17807 . Calmodulin . . . . . 99.32 147 100.00 100.00 2.55e-99 . . . . 18028 1 20 no BMRB 18027 . CaM . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 21 no BMRB 18556 . Calmodulin . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18028 1 22 no BMRB 19036 . calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 23 no BMRB 19238 . Calmodulin_prototypical_calcium_sensor . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 24 no BMRB 19586 . entity_1 . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 25 no BMRB 19604 . calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 26 no BMRB 25253 . CaM . . . . . 100.00 148 98.65 99.32 1.22e-97 . . . . 18028 1 27 no BMRB 25257 . CaM . . . . . 100.00 148 98.65 99.32 1.22e-97 . . . . 18028 1 28 no BMRB 26503 . Calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 29 no BMRB 26626 . CaM . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 30 no BMRB 26627 . CaM . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 31 no BMRB 4056 . calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 32 no BMRB 4270 . calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 33 no BMRB 4284 . Calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 34 no BMRB 4310 . calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 35 no PDB 1A29 . "Calmodulin Complexed With Trifluoperazine (1:2 Complex)" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 36 no PDB 1CFC . "Calcium-Free Calmodulin" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 37 no PDB 1CFD . "Calcium-Free Calmodulin" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 38 no PDB 1CFF . "Nmr Solution Structure Of A Complex Of Calmodulin With A Binding Peptide Of The Ca2+-Pump" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 39 no PDB 1CKK . "CalmodulinRAT CA2+CALMODULIN DEPENDENT PROTEIN KINASE Fragment" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 40 no PDB 1CLL . "Calmodulin Structure Refined At 1.7 Angstroms Resolution" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 41 no PDB 1CM1 . "Motions Of Calmodulin-Single-Conformer Refinement" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 42 no PDB 1CM4 . "Motions Of Calmodulin-four-conformer Refinement" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 43 no PDB 1CTR . "Drug Binding By Calmodulin: Crystal Structure Of A Calmodulin-Trifluoperazine Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 44 no PDB 1DMO . "Calmodulin, Nmr, 30 Structures" . . . . . 100.00 148 99.32 100.00 2.01e-99 . . . . 18028 1 45 no PDB 1G4Y . "1.60 A Crystal Structure Of The Gating Domain From Small Conductance Potassium Channel Complexed With Calcium-Calmodulin" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 46 no PDB 1IQ5 . "CalmodulinNEMATODE CA2+CALMODULIN DEPENDENT KINASE KINASE Fragment" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 47 no PDB 1IWQ . "Crystal Structure Of Marcks Calmodulin Binding Domain Peptide Complexed With Ca2+CALMODULIN" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 48 no PDB 1K90 . "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3' Deoxy-Atp" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 49 no PDB 1K93 . "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin" . . . . . 97.30 144 100.00 100.00 4.42e-97 . . . . 18028 1 50 no PDB 1L7Z . "Crystal Structure Of Ca2+/calmodulin Complexed With Myristoylated Cap-23/nap-22 Peptide" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 51 no PDB 1LIN . "Calmodulin Complexed With Trifluoperazine (1:4 Complex)" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 52 no PDB 1LVC . "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 2' Deoxy, 3' Anthr" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 53 no PDB 1MUX . "Solution Nmr Structure Of CalmodulinW-7 Complex: The Basis Of Diversity In Molecular Recognition, 30 Structures" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 54 no PDB 1MXE . "Structure Of The Complex Of Calmodulin With The Target Sequence Of Camki" . . . . . 100.00 148 97.97 99.32 6.77e-98 . . . . 18028 1 55 no PDB 1NWD . "Solution Structure Of Ca2+CALMODULIN BOUND TO THE C- Terminal Domain Of Petunia Glutamate Decarboxylase" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 56 no PDB 1OOJ . "Structural Genomics Of Caenorhabditis Elegans : Calmodulin" . . . . . 100.00 149 97.97 98.65 1.28e-97 . . . . 18028 1 57 no PDB 1PRW . "Crystal Structure Of Bovine Brain Ca++ Calmodulin In A Compact Form" . . . . . 100.00 149 99.32 99.32 4.27e-99 . . . . 18028 1 58 no PDB 1QIV . "Calmodulin Complexed With N-(3,3,-Diphenylpropyl)-N'-[1-R-( 3,4-Bis-Butoxyphenyl)-Ethyl]-Propylenediamine (Dpd), 1:2 Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 59 no PDB 1QIW . "Calmodulin Complexed With N-(3,3,-Diphenylpropyl)-N'-[1-R-( 3,4-Bis-Butoxyphenyl)-Ethyl]-Propylenediamine (Dpd)" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 60 no PDB 1QX5 . "Crystal Structure Of Apocalmodulin" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 61 no PDB 1S26 . "Structure Of Anthrax Edema Factor-calmodulin-alpha,beta- Methyleneadenosine 5'-triphosphate Complex Reveals An Alternative Mode" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 62 no PDB 1SK6 . "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin, 3',5' Cyclic Amp (Cam" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 63 no PDB 1SY9 . "Structure Of Calmodulin Complexed With A Fragment Of The Olfactory Cng Channel" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 64 no PDB 1UP5 . "Chicken Calmodulin" . . . . . 100.00 148 99.32 99.32 4.13e-99 . . . . 18028 1 65 no PDB 1WRZ . "Calmodulin Complexed With A Peptide From A Human Death-Associated Protein Kinase" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 66 no PDB 1X02 . "Solution Structure Of Stereo Array Isotope Labeled (Sail) Calmodulin" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 67 no PDB 1XA5 . "Structure Of Calmodulin In Complex With Kar-2, A Bis-Indol Alkaloid" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 68 no PDB 1XFU . "Crystal Structure Of Anthrax Edema Factor (ef) Truncation Mutant, Ef-delta 64 In Complex With Calmodulin" . . . . . 100.00 149 99.32 100.00 1.22e-99 . . . . 18028 1 69 no PDB 1XFV . "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3' Deoxy-Atp" . . . . . 100.00 149 99.32 100.00 1.22e-99 . . . . 18028 1 70 no PDB 1XFW . "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3'5' Cyclic Amp (Camp)" . . . . . 100.00 149 99.32 100.00 1.22e-99 . . . . 18028 1 71 no PDB 1XFY . "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin" . . . . . 100.00 149 99.32 100.00 1.22e-99 . . . . 18028 1 72 no PDB 1XFZ . "Crystal Structure Of Anthrax Edema Factor (ef) In Complex With Calmodulin In The Presence Of 1 Millimolar Exogenously Added Cal" . . . . . 100.00 149 99.32 100.00 1.22e-99 . . . . 18028 1 73 no PDB 1Y0V . "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And Pyrophosphate" . . . . . 97.30 146 100.00 100.00 3.80e-97 . . . . 18028 1 74 no PDB 1YR5 . "1.7-A Structure Of Calmodulin Bound To A Peptide From Dap Kinase" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 75 no PDB 2BBM . "Solution Structure Of A Calmodulin-Target Peptide Complex By Multidimensional Nmr" . . . . . 100.00 148 97.97 99.32 6.77e-98 . . . . 18028 1 76 no PDB 2BBN . "Solution Structure Of A Calmodulin-Target Peptide Complex By Multidimensional Nmr" . . . . . 100.00 148 97.97 99.32 6.77e-98 . . . . 18028 1 77 no PDB 2BCX . "Crystal Structure Of Calmodulin In Complex With A Ryanodine Receptor Peptide" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 78 no PDB 2BKH . "Myosin Vi Nucleotide-Free (Mdinsert2) Crystal Structure" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 18028 1 79 no PDB 2BKI . "Myosin Vi Nucleotide-free (mdinsert2-iq) Crystal Structure" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 80 no PDB 2DFS . "3-D Structure Of Myosin-V Inhibited State" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 81 no PDB 2F2O . "Structure Of Calmodulin Bound To A Calcineurin Peptide: A New Way Of Making An Old Binding Mode" . . . . . 100.00 179 100.00 100.00 7.91e-100 . . . . 18028 1 82 no PDB 2F2P . "Structure Of Calmodulin Bound To A Calcineurin Peptide: A New Way Of Making An Old Binding Mode" . . . . . 100.00 179 100.00 100.00 7.91e-100 . . . . 18028 1 83 no PDB 2F3Y . "CalmodulinIQ DOMAIN COMPLEX" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 84 no PDB 2F3Z . "CalmodulinIQ-Aa Domain Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 85 no PDB 2FOT . "Crystal Structure Of The Complex Between Calmodulin And Alphaii-Spectrin" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 86 no PDB 2HQW . "Crystal Structure Of Ca2+CALMODULIN BOUND TO NMDA RECEPTOR NR1C1 Peptide" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 87 no PDB 2JZI . "Structure Of Calmodulin Complexed With The Calmodulin Binding Domain Of Calcineurin" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 88 no PDB 2K0E . "A Coupled Equilibrium Shift Mechanism In Calmodulin- Mediated Signal Transduction" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 89 no PDB 2K0F . "Calmodulin Complexed With Calmodulin-Binding Peptide From Smooth Muscle Myosin Light Chain Kinase" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 90 no PDB 2K0J . "Solution Structure Of Cam Complexed To Drp1p" . . . . . 100.00 148 99.32 100.00 3.32e-99 . . . . 18028 1 91 no PDB 2K61 . "Solution Structure Of Cam Complexed To Dapk Peptide" . . . . . 100.00 148 99.32 100.00 3.32e-99 . . . . 18028 1 92 no PDB 2KDU . "Structural Basis Of The Munc13-1CA2+-Calmodulin Interaction: A Novel 1-26 Calmodulin Binding Motif With A Bipartite Binding Mod" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 93 no PDB 2KNE . "Calmodulin Wraps Around Its Binding Domain In The Plasma Membrane Ca2+ Pump Anchored By A Novel 18-1 Motif" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 94 no PDB 2L53 . "Solution Nmr Structure Of Apo-Calmodulin In Complex With The Iq Motif Of Human Cardiac Sodium Channel Nav1.5" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 95 no PDB 2L7L . "Solution Structure Of Ca2+CALMODULIN COMPLEXED WITH A PEPTIDE Representing The Calmodulin-Binding Domain Of Calmodulin Kinase I" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 96 no PDB 2LGF . "Solution Structure Of Ca2+CALMODULIN COMPLEXED WITH A PEPTIDE Representing The Calmodulin-Binding Domain Of L-Selectin" . . . . . 98.65 146 100.00 100.00 1.07e-98 . . . . 18028 1 97 no PDB 2LL6 . "Solution Nmr Structure Of Cam Bound To Inos Cam Binding Domain Peptide" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 98 no PDB 2LL7 . "Solution Nmr Structure Of Cam Bound To The Enos Cam Binding Domain Peptide" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 99 no PDB 2LV6 . "The Complex Between Ca-calmodulin And Skeletal Muscle Myosin Light Chain Kinase From Combination Of Nmr And Aqueous And Contras" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18028 1 100 no PDB 2M0J . "3d Structure Of Calmodulin And Calmodulin Binding Domain Of Olfactory Cyclic Nucleotide-gated Ion Channel Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 101 no PDB 2M0K . "3d Structure Of Calmodulin And Calmodulin Binding Domain Of Rat Olfactory Cyclic Nucleotide-gated Ion Channel" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 102 no PDB 2M55 . "Nmr Structure Of The Complex Of An N-terminally Acetylated Alpha- Synuclein Peptide With Calmodulin" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 103 no PDB 2MG5 . "Solution Structure Of Calmodulin Bound To The Target Peptide Of Endothelial Nitrogen Oxide Synthase Phosphorylated At Thr495" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 104 no PDB 2MGU . "Structure Of The Complex Between Calmodulin And The Binding Domain Of Hiv-1 Matrix Protein" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 105 no PDB 2O5G . "Calmodulin-Smooth Muscle Light Chain Kinase Peptide Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 106 no PDB 2O60 . "Calmodulin Bound To Peptide From Neuronal Nitric Oxide Synthase" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 107 no PDB 2R28 . "The Complex Structure Of Calmodulin Bound To A Calcineurin Peptide" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 108 no PDB 2V01 . "Recombinant Vertebrate Calmodulin Complexed With Pb" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 109 no PDB 2V02 . "Recombinant Vertebrate Calmodulin Complexed With Ba" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 110 no PDB 2VAS . "Myosin Vi (Md-Insert2-Cam, Delta-Insert1) Post-Rigor State" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 18028 1 111 no PDB 2VAY . "Calmodulin Complexed With Cav1.1 Iq Peptide" . . . . . 98.65 146 100.00 100.00 1.07e-98 . . . . 18028 1 112 no PDB 2VB6 . "Myosin Vi (Md-Insert2-Cam, Delta Insert1) Post-Rigor State ( Crystal Form 2)" . . . . . 100.00 149 97.30 99.32 1.25e-97 . . . . 18028 1 113 no PDB 2W73 . "High-Resolution Structure Of The Complex Between Calmodulin And A Peptide From Calcineurin A" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 114 no PDB 2WEL . "Crystal Structure Of Su6656-Bound CalciumCALMODULIN- Dependent Protein Kinase Ii Delta In Complex With Calmodulin" . . . . . 100.00 150 100.00 100.00 4.76e-100 . . . . 18028 1 115 no PDB 2X0G . "X-ray Structure Of A Dap-kinase Calmodulin Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 116 no PDB 2X51 . "M6 Delta Insert1" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 18028 1 117 no PDB 2Y4V . "Crystal Structure Of Human Calmodulin In Complex With A Dap Kinase-1 Mutant (W305y) Peptide" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 118 no PDB 2YGG . "Complex Of Cambr And Cam" . . . . . 100.00 150 100.00 100.00 5.60e-100 . . . . 18028 1 119 no PDB 3BXK . "Crystal Structure Of The PQ-Type Calcium Channel (Cav2.1) Iq Domain And Ca2+calmodulin Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 120 no PDB 3BXL . "Crystal Structure Of The R-Type Calcium Channel (Cav2.3) Iq Domain And Ca2+calmodulin Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 121 no PDB 3BYA . "Structure Of A Calmodulin Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 122 no PDB 3CLN . "Structure Of Calmodulin Refined At 2.2 Angstroms Resolution" . . . . . 100.00 148 99.32 100.00 2.01e-99 . . . . 18028 1 123 no PDB 3DVE . "Crystal Structure Of Ca2+CAM-Cav2.2 Iq Domain Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 124 no PDB 3DVJ . "Crystal Structure Of Ca2+CAM-Cav2.2 Iq Domain (Without Cloning Artifact, Hm To Tv) Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 125 no PDB 3DVK . "Crystal Structure Of Ca2+CAM-Cav2.3 Iq Domain Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 126 no PDB 3DVM . "Crystal Structure Of Ca2+CAM-Cav2.1 Iq Domain Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 127 no PDB 3EK4 . "Calcium-saturated Gcamp2 Monomer" . . . . . 99.32 449 100.00 100.00 9.40e-96 . . . . 18028 1 128 no PDB 3EK7 . "Calcium-Saturated Gcamp2 Dimer" . . . . . 99.32 449 100.00 100.00 9.40e-96 . . . . 18028 1 129 no PDB 3EK8 . "Calcium-Saturated Gcamp2 T116vG87R MUTANT MONOMER" . . . . . 99.32 449 100.00 100.00 1.33e-95 . . . . 18028 1 130 no PDB 3EKH . "Calcium-Saturated Gcamp2 T116vK378W MUTANT MONOMER" . . . . . 99.32 449 99.32 99.32 9.09e-95 . . . . 18028 1 131 no PDB 3EVU . "Crystal Structure Of Calcium Bound Dimeric Gcamp2, (#1)" . . . . . 99.32 449 100.00 100.00 9.40e-96 . . . . 18028 1 132 no PDB 3EVV . "Crystal Structure Of Calcium Bound Dimeric Gcamp2 (#2)" . . . . . 99.32 449 100.00 100.00 9.40e-96 . . . . 18028 1 133 no PDB 3EWT . "Crystal Structure Of Calmodulin Complexed With A Peptide" . . . . . 100.00 154 100.00 100.00 2.06e-100 . . . . 18028 1 134 no PDB 3EWV . "Crystal Structure Of Calmodulin Complexed With A Peptide" . . . . . 100.00 154 100.00 100.00 2.06e-100 . . . . 18028 1 135 no PDB 3G43 . "Crystal Structure Of The Calmodulin-Bound Cav1.2 C-Terminal Regulatory Domain Dimer" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 136 no PDB 3GN4 . "Myosin Lever Arm" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 18028 1 137 no PDB 3GOF . "Calmodulin Bound To Peptide From Macrophage Nitric Oxide Synthase" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 138 no PDB 3HR4 . "Human Inos Reductase And Calmodulin Complex" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 139 no PDB 3IF7 . "Structure Of Calmodulin Complexed With Its First Endogenous Inhibitor, Sphingosylphosphorylcholine" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 140 no PDB 3J41 . "Pseudo-atomic Model Of The Aquaporin-0/calmodulin Complex Derived From Electron Microscopy" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 141 no PDB 3L9I . "Myosin Vi Nucleotide-Free (Mdinsert2) L310g Mutant Crystal Structure" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 18028 1 142 no PDB 3O77 . "The Structure Of Ca2+ Sensor (Case-16)" . . . . . 99.32 415 100.00 100.00 4.22e-96 . . . . 18028 1 143 no PDB 3O78 . "The Structure Of Ca2+ Sensor (Case-12)" . . . . . 99.32 415 100.00 100.00 4.65e-96 . . . . 18028 1 144 no PDB 3OXQ . "Crystal Structure Of Ca2+CAM-Cav1.2 Pre-IqIQ DOMAIN COMPLEX" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 145 no PDB 3SG2 . "Crystal Structure Of Gcamp2-t116v,d381y" . . . . . 99.32 449 99.32 99.32 1.34e-94 . . . . 18028 1 146 no PDB 3SG3 . "Crystal Structure Of Gcamp3-d380y" . . . . . 99.32 449 98.64 99.32 1.70e-93 . . . . 18028 1 147 no PDB 3SG4 . "Crystal Structure Of Gcamp3-d380y, Lp(linker 2)" . . . . . 100.00 448 97.97 98.65 1.17e-93 . . . . 18028 1 148 no PDB 3SG5 . "Crystal Structure Of Dimeric Gcamp3-d380y, Qp(linker 1), Lp(linker 2)" . . . . . 100.00 448 97.97 98.65 9.63e-94 . . . . 18028 1 149 no PDB 3SG6 . "Crystal Structure Of Dimeric Gcamp2-lia(linker 1)" . . . . . 99.32 450 100.00 100.00 1.20e-95 . . . . 18028 1 150 no PDB 3SG7 . "Crystal Structure Of Gcamp3-kf(linker 1)" . . . . . 99.32 448 99.32 100.00 8.02e-95 . . . . 18028 1 151 no PDB 3SJQ . "Crystal Structure Of A Small Conductance Potassium Channel Splice Variant Complexed With Calcium-Calmodulin" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 152 no PDB 3SUI . "Crystal Structure Of Ca2+-Calmodulin In Complex With A Trpv1 C- Terminal Peptide" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 153 no PDB 3U0K . "Crystal Structure Of The Genetically Encoded Calcium Indicator Rcamp" . . . . . 99.32 440 98.64 99.32 2.87e-94 . . . . 18028 1 154 no PDB 3WFN . "Crystal Structure Of Nav1.6 Iq Motif In Complex With Apo-cam" . . . . . 100.00 182 100.00 100.00 5.91e-100 . . . . 18028 1 155 no PDB 4ANJ . "Myosin Vi (Mdinsert2-Gfp Fusion) Pre-Powerstroke State (Mg.Adp.Alf4)" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 18028 1 156 no PDB 4BW7 . "Calmodulin In Complex With Strontium" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 157 no PDB 4BW8 . "Calmodulin With Small Bend In Central Helix" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 158 no PDB 4BYF . "Crystal Structure Of Human Myosin 1c In Complex With Calmodulin In The Pre-power Stroke State" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 159 no PDB 4CLN . "Structure Of A Recombinant Calmodulin From Drosophila Melanogaster Refined At 2.2-Angstroms Resolution" . . . . . 100.00 148 97.97 99.32 6.77e-98 . . . . 18028 1 160 no PDB 4DBP . "Myosin Vi Nucleotide-free (mdinsert2) D179y Crystal Structure" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 18028 1 161 no PDB 4DBQ . "Myosin Vi D179y (md-insert2-cam, Delta-insert1) Post-rigor State" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 18028 1 162 no PDB 4DCK . "Crystal Structure Of The C-Terminus Of Voltage-Gated Sodium Channel In Complex With Fgf13 And Cam" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 163 no PDB 4DJC . "1.35 A Crystal Structure Of The Nav1.5 Diii-Iv-CaCAM COMPLEX" . . . . . 100.00 152 100.00 100.00 3.59e-100 . . . . 18028 1 164 no PDB 4E50 . "Calmodulin And Ng Peptide Complex" . . . . . 100.00 185 100.00 100.00 2.67e-100 . . . . 18028 1 165 no PDB 4EHQ . "Crystal Structure Of Calmodulin Binding Domain Of Orai1 In Complex With Ca2+CALMODULIN DISPLAYS A UNIQUE BINDING MODE" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 166 no PDB 4G27 . "Calcium-Calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And P" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 167 no PDB 4G28 . "Calcium-Calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And E" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 168 no PDB 4HEX . "A Novel Conformation Of Calmodulin" . . . . . 100.00 156 100.00 100.00 2.20e-100 . . . . 18028 1 169 no PDB 4IK1 . "High Resolution Structure Of Gcampj At Ph 8.5" . . . . . 99.32 448 98.64 99.32 1.47e-93 . . . . 18028 1 170 no PDB 4IK3 . "High Resolution Structure Of Gcamp3 At Ph 8.5" . . . . . 99.32 448 99.32 100.00 9.53e-95 . . . . 18028 1 171 no PDB 4IK4 . "High Resolution Structure Of Gcamp3 At Ph 5.0" . . . . . 99.32 448 99.32 100.00 9.53e-95 . . . . 18028 1 172 no PDB 4IK5 . "High Resolution Structure Of Delta-rest-gcamp3" . . . . . 99.32 414 99.32 100.00 3.73e-95 . . . . 18028 1 173 no PDB 4IK8 . "High Resolution Structure Of Gcamp3 Dimer Form 1 At Ph 7.5" . . . . . 99.32 448 99.32 100.00 9.53e-95 . . . . 18028 1 174 no PDB 4IK9 . "High Resolution Structure Of Gcamp3 Dimer Form 2 At Ph 7.5" . . . . . 99.32 448 99.32 100.00 9.53e-95 . . . . 18028 1 175 no PDB 4J9Y . "Calcium-calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 176 no PDB 4J9Z . "Calcium-calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And N" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 177 no PDB 4JPZ . "Voltage-gated Sodium Channel 1.2 C-terminal Domain In Complex With Fgf13u And Ca2+/calmodulin" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 178 no PDB 4JQ0 . "Voltage-gated Sodium Channel 1.5 C-terminal Domain In Complex With Fgf12b And Ca2+/calmodulin" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 179 no PDB 4L79 . "Crystal Structure Of Nucleotide-free Myosin 1b Residues 1-728 With Bound Calmodulin" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 180 no PDB 4LZX . "Complex Of Iqcg And Ca2+-free Cam" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 181 no PDB 4M1L . "Complex Of Iqcg And Ca2+-bound Cam" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 182 no PDB 4PJJ . "Myosin Vi (md-insert2-cam, Delta-insert1) Post-rigor State - Long Soaking With Po4" . . . . . 100.00 149 97.30 99.32 1.25e-97 . . . . 18028 1 183 no PDB 4Q5U . "Structure Of Calmodulin Bound To Its Recognition Site From Calcineurin" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 184 no PDB 4QNH . "Calcium-calmodulin (t79d) Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Sk2-a" . . . . . 100.00 149 99.32 99.32 6.26e-99 . . . . 18028 1 185 no PDB 4R8G . "Crystal Structure Of Myosin-1c Tail In Complex With Calmodulin" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 186 no PDB 4UMO . "Crystal Structure Of The Kv7.1 Proximal C-terminal Domain In Complex With Calmodulin" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 187 no PDB 4UPU . "Crystal Structure Of Ip3 3-k Calmodulin Binding Region In Complex With Calmodulin" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 188 no PDB 4V0C . "Crystal Structure Of The Kv7.1 Proximal C-terminal Domain In Complex With Calmodulin" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 189 no DBJ BAA08302 . "calmodulin [Homo sapiens]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 190 no DBJ BAA11896 . "calmodulin [Anas platyrhynchos]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 191 no DBJ BAA19786 . "calmodulin [Branchiostoma lanceolatum]" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 18028 1 192 no DBJ BAA19787 . "calmodulin [Branchiostoma floridae]" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 18028 1 193 no DBJ BAA19788 . "calmodulin [Halocynthia roretzi]" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 18028 1 194 no EMBL CAA10601 . "calmodulin [Caenorhabditis elegans]" . . . . . 100.00 149 97.97 98.65 1.28e-97 . . . . 18028 1 195 no EMBL CAA32050 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 196 no EMBL CAA32062 . "calmodulin II [Rattus norvegicus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 197 no EMBL CAA32119 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 198 no EMBL CAA32120 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 199 no GB AAA35635 . "calmodulin [Homo sapiens]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 200 no GB AAA35641 . "calmodulin [Homo sapiens]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 201 no GB AAA37365 . "calmodulin synthesis [Mus musculus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 202 no GB AAA40862 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 203 no GB AAA40863 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 204 no PIR JC1305 . "calmodulin - Japanese medaka" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 205 no PIR MCON . "calmodulin - salmon" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 18028 1 206 no PRF 0409298A . "troponin C-like protein" . . . . . 100.00 148 97.30 100.00 2.53e-98 . . . . 18028 1 207 no PRF 0608335A . calmodulin . . . . . 100.00 148 97.97 99.32 3.48e-97 . . . . 18028 1 208 no REF NP_001008160 . "calmodulin [Xenopus (Silurana) tropicalis]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 209 no REF NP_001009759 . "calmodulin [Ovis aries]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 210 no REF NP_001027633 . "calmodulin [Ciona intestinalis]" . . . . . 100.00 149 97.30 98.65 3.34e-97 . . . . 18028 1 211 no REF NP_001039714 . "calmodulin [Bos taurus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 212 no REF NP_001040234 . "calmodulin [Bombyx mori]" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 18028 1 213 no SP O02367 . "RecName: Full=Calmodulin; Short=CaM; AltName: Full=Ci-CaM" . . . . . 100.00 149 97.30 98.65 3.34e-97 . . . . 18028 1 214 no SP O16305 . "RecName: Full=Calmodulin; Short=CaM" . . . . . 100.00 149 97.97 98.65 1.28e-97 . . . . 18028 1 215 no SP O96081 . "RecName: Full=Calmodulin-B; Short=CaM B" . . . . . 100.00 149 97.30 98.65 3.76e-97 . . . . 18028 1 216 no SP P02594 . "RecName: Full=Calmodulin; Short=CaM" . . . . . 100.00 149 99.32 100.00 1.65e-99 . . . . 18028 1 217 no SP P05932 . "RecName: Full=Calmodulin-beta; Short=Cam B" . . . . . 93.24 138 97.10 99.28 5.25e-90 . . . . 18028 1 218 no TPG DAA13808 . "TPA: calmodulin 2-like [Bos taurus]" . . . . . 100.00 216 98.65 98.65 2.49e-98 . . . . 18028 1 219 no TPG DAA18029 . "TPA: calmodulin [Bos taurus]" . . . . . 100.00 149 98.65 99.32 7.54e-99 . . . . 18028 1 220 no TPG DAA19590 . "TPA: calmodulin 3 [Bos taurus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 221 no TPG DAA24777 . "TPA: calmodulin 2-like [Bos taurus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 1 222 no TPG DAA24988 . "TPA: calmodulin 2-like isoform 1 [Bos taurus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 18028 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 . ALA . 18028 1 2 . ASP . 18028 1 3 . GLN . 18028 1 4 . LEU . 18028 1 5 . THR . 18028 1 6 . GLU . 18028 1 7 . GLU . 18028 1 8 . GLN . 18028 1 9 . ILE . 18028 1 10 . ALA . 18028 1 11 . GLU . 18028 1 12 . PHE . 18028 1 13 . LYS . 18028 1 14 . GLU . 18028 1 15 . ALA . 18028 1 16 . PHE . 18028 1 17 . SER . 18028 1 18 . LEU . 18028 1 19 . PHE . 18028 1 20 . ASP . 18028 1 21 . LYS . 18028 1 22 . ASP . 18028 1 23 . GLY . 18028 1 24 . ASP . 18028 1 25 . GLY . 18028 1 26 . THR . 18028 1 27 . ILE . 18028 1 28 . THR . 18028 1 29 . THR . 18028 1 30 . LYS . 18028 1 31 . GLU . 18028 1 32 . LEU . 18028 1 33 . GLY . 18028 1 34 . THR . 18028 1 35 . VAL . 18028 1 36 . MET . 18028 1 37 . ARG . 18028 1 38 . SER . 18028 1 39 . LEU . 18028 1 40 . GLY . 18028 1 41 . GLN . 18028 1 42 . ASN . 18028 1 43 . PRO . 18028 1 44 . THR . 18028 1 45 . GLU . 18028 1 46 . ALA . 18028 1 47 . GLU . 18028 1 48 . LEU . 18028 1 49 . GLN . 18028 1 50 . ASP . 18028 1 51 . MET . 18028 1 52 . ILE . 18028 1 53 . ASN . 18028 1 54 . GLU . 18028 1 55 . VAL . 18028 1 56 . ASP . 18028 1 57 . ALA . 18028 1 58 . ASP . 18028 1 59 . GLY . 18028 1 60 . ASN . 18028 1 61 . GLY . 18028 1 62 . THR . 18028 1 63 . ILE . 18028 1 64 . ASP . 18028 1 65 . PHE . 18028 1 66 . PRO . 18028 1 67 . GLU . 18028 1 68 . PHE . 18028 1 69 . LEU . 18028 1 70 . THR . 18028 1 71 . MET . 18028 1 72 . MET . 18028 1 73 . ALA . 18028 1 74 . ARG . 18028 1 75 . LYS . 18028 1 76 . MET . 18028 1 77 . LYS . 18028 1 78 . ASP . 18028 1 79 . THR . 18028 1 80 . ASP . 18028 1 81 . SER . 18028 1 82 . GLU . 18028 1 83 . GLU . 18028 1 84 . GLU . 18028 1 85 . ILE . 18028 1 86 . ARG . 18028 1 87 . GLU . 18028 1 88 . ALA . 18028 1 89 . PHE . 18028 1 90 . ARG . 18028 1 91 . VAL . 18028 1 92 . PHE . 18028 1 93 . ASP . 18028 1 94 . LYS . 18028 1 95 . ASP . 18028 1 96 . GLY . 18028 1 97 . ASN . 18028 1 98 . GLY . 18028 1 99 . TYR . 18028 1 100 . ILE . 18028 1 101 . SER . 18028 1 102 . ALA . 18028 1 103 . ALA . 18028 1 104 . GLU . 18028 1 105 . LEU . 18028 1 106 . ARG . 18028 1 107 . HIS . 18028 1 108 . VAL . 18028 1 109 . MET . 18028 1 110 . THR . 18028 1 111 . ASN . 18028 1 112 . LEU . 18028 1 113 . GLY . 18028 1 114 . GLU . 18028 1 115 . LYS . 18028 1 116 . LEU . 18028 1 117 . THR . 18028 1 118 . ASP . 18028 1 119 . GLU . 18028 1 120 . GLU . 18028 1 121 . VAL . 18028 1 122 . ASP . 18028 1 123 . GLU . 18028 1 124 . MET . 18028 1 125 . ILE . 18028 1 126 . ARG . 18028 1 127 . GLU . 18028 1 128 . ALA . 18028 1 129 . ASP . 18028 1 130 . ILE . 18028 1 131 . ASP . 18028 1 132 . GLY . 18028 1 133 . ASP . 18028 1 134 . GLY . 18028 1 135 . GLN . 18028 1 136 . VAL . 18028 1 137 . ASN . 18028 1 138 . TYR . 18028 1 139 . GLU . 18028 1 140 . GLU . 18028 1 141 . PHE . 18028 1 142 . VAL . 18028 1 143 . GLN . 18028 1 144 . MET . 18028 1 145 . MET . 18028 1 146 . THR . 18028 1 147 . ALA . 18028 1 148 . LYS . 18028 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 . ALA 1 1 18028 1 . ASP 2 2 18028 1 . GLN 3 3 18028 1 . LEU 4 4 18028 1 . THR 5 5 18028 1 . GLU 6 6 18028 1 . GLU 7 7 18028 1 . GLN 8 8 18028 1 . ILE 9 9 18028 1 . ALA 10 10 18028 1 . GLU 11 11 18028 1 . PHE 12 12 18028 1 . LYS 13 13 18028 1 . GLU 14 14 18028 1 . ALA 15 15 18028 1 . PHE 16 16 18028 1 . SER 17 17 18028 1 . LEU 18 18 18028 1 . PHE 19 19 18028 1 . ASP 20 20 18028 1 . LYS 21 21 18028 1 . ASP 22 22 18028 1 . GLY 23 23 18028 1 . ASP 24 24 18028 1 . GLY 25 25 18028 1 . THR 26 26 18028 1 . ILE 27 27 18028 1 . THR 28 28 18028 1 . THR 29 29 18028 1 . LYS 30 30 18028 1 . GLU 31 31 18028 1 . LEU 32 32 18028 1 . GLY 33 33 18028 1 . THR 34 34 18028 1 . VAL 35 35 18028 1 . MET 36 36 18028 1 . ARG 37 37 18028 1 . SER 38 38 18028 1 . LEU 39 39 18028 1 . GLY 40 40 18028 1 . GLN 41 41 18028 1 . ASN 42 42 18028 1 . PRO 43 43 18028 1 . THR 44 44 18028 1 . GLU 45 45 18028 1 . ALA 46 46 18028 1 . GLU 47 47 18028 1 . LEU 48 48 18028 1 . GLN 49 49 18028 1 . ASP 50 50 18028 1 . MET 51 51 18028 1 . ILE 52 52 18028 1 . ASN 53 53 18028 1 . GLU 54 54 18028 1 . VAL 55 55 18028 1 . ASP 56 56 18028 1 . ALA 57 57 18028 1 . ASP 58 58 18028 1 . GLY 59 59 18028 1 . ASN 60 60 18028 1 . GLY 61 61 18028 1 . THR 62 62 18028 1 . ILE 63 63 18028 1 . ASP 64 64 18028 1 . PHE 65 65 18028 1 . PRO 66 66 18028 1 . GLU 67 67 18028 1 . PHE 68 68 18028 1 . LEU 69 69 18028 1 . THR 70 70 18028 1 . MET 71 71 18028 1 . MET 72 72 18028 1 . ALA 73 73 18028 1 . ARG 74 74 18028 1 . LYS 75 75 18028 1 . MET 76 76 18028 1 . LYS 77 77 18028 1 . ASP 78 78 18028 1 . THR 79 79 18028 1 . ASP 80 80 18028 1 . SER 81 81 18028 1 . GLU 82 82 18028 1 . GLU 83 83 18028 1 . GLU 84 84 18028 1 . ILE 85 85 18028 1 . ARG 86 86 18028 1 . GLU 87 87 18028 1 . ALA 88 88 18028 1 . PHE 89 89 18028 1 . ARG 90 90 18028 1 . VAL 91 91 18028 1 . PHE 92 92 18028 1 . ASP 93 93 18028 1 . LYS 94 94 18028 1 . ASP 95 95 18028 1 . GLY 96 96 18028 1 . ASN 97 97 18028 1 . GLY 98 98 18028 1 . TYR 99 99 18028 1 . ILE 100 100 18028 1 . SER 101 101 18028 1 . ALA 102 102 18028 1 . ALA 103 103 18028 1 . GLU 104 104 18028 1 . LEU 105 105 18028 1 . ARG 106 106 18028 1 . HIS 107 107 18028 1 . VAL 108 108 18028 1 . MET 109 109 18028 1 . THR 110 110 18028 1 . ASN 111 111 18028 1 . LEU 112 112 18028 1 . GLY 113 113 18028 1 . GLU 114 114 18028 1 . LYS 115 115 18028 1 . LEU 116 116 18028 1 . THR 117 117 18028 1 . ASP 118 118 18028 1 . GLU 119 119 18028 1 . GLU 120 120 18028 1 . VAL 121 121 18028 1 . ASP 122 122 18028 1 . GLU 123 123 18028 1 . MET 124 124 18028 1 . ILE 125 125 18028 1 . ARG 126 126 18028 1 . GLU 127 127 18028 1 . ALA 128 128 18028 1 . ASP 129 129 18028 1 . ILE 130 130 18028 1 . ASP 131 131 18028 1 . GLY 132 132 18028 1 . ASP 133 133 18028 1 . GLY 134 134 18028 1 . GLN 135 135 18028 1 . VAL 136 136 18028 1 . ASN 137 137 18028 1 . TYR 138 138 18028 1 . GLU 139 139 18028 1 . GLU 140 140 18028 1 . PHE 141 141 18028 1 . VAL 142 142 18028 1 . GLN 143 143 18028 1 . MET 144 144 18028 1 . MET 145 145 18028 1 . THR 146 146 18028 1 . ALA 147 147 18028 1 . LYS 148 148 18028 1 stop_ save_ save_eNOS _Entity.Sf_category entity _Entity.Sf_framecode eNOS _Entity.Entry_ID 18028 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name eNOS _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID B _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code KKTFKEVANAVKISASL _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 17 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 1838.215 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-30 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 15185 . eNOSp . . . . . 100.00 20 100.00 100.00 8.54e-01 . . . . 18028 2 2 no PDB 1NIW . "Crystal Structure Of Endothelial Nitric Oxide Synthase Peptide Bound To Calmodulin" . . . . . 100.00 20 100.00 100.00 8.54e-01 . . . . 18028 2 3 no PDB 2LL7 . "Solution Nmr Structure Of Cam Bound To The Enos Cam Binding Domain Peptide" . . . . . 100.00 17 100.00 100.00 1.15e+00 . . . . 18028 2 4 no DBJ BAA05652 . "endothelial nitric oxide synthase [Homo sapiens]" . . . . . 100.00 1204 100.00 100.00 1.37e+00 . . . . 18028 2 5 no DBJ BAD15356 . "nitric oxide synthase 3 [Rattus norvegicus]" . . . . . 100.00 1202 100.00 100.00 1.37e+00 . . . . 18028 2 6 no DBJ BAD97356 . "nitric oxide synthase 3 (endothelial cell) variant [Homo sapiens]" . . . . . 100.00 1203 100.00 100.00 1.37e+00 . . . . 18028 2 7 no DBJ BAF85617 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 1203 100.00 100.00 1.37e+00 . . . . 18028 2 8 no DBJ BAG37648 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 1203 100.00 100.00 1.37e+00 . . . . 18028 2 9 no EMBL CAA53950 . "endothelial nitric oxide synthase [Homo sapiens]" . . . . . 100.00 1203 100.00 100.00 1.37e+00 . . . . 18028 2 10 no EMBL CAI10801 . "endothelial nitric oxide synthase [Mesocricetus auratus]" . . . . . 100.00 122 100.00 100.00 6.25e+00 . . . . 18028 2 11 no GB AAA30494 . "nitric oxide synthase [Bos taurus]" . . . . . 100.00 1205 100.00 100.00 1.37e+00 . . . . 18028 2 12 no GB AAA30667 . "nitric oxide synthase [Bos taurus]" . . . . . 100.00 1205 100.00 100.00 1.37e+00 . . . . 18028 2 13 no GB AAA30669 . "nitric oxide synthase [Bos taurus]" . . . . . 100.00 1205 100.00 100.00 1.37e+00 . . . . 18028 2 14 no GB AAA36364 . "nitric oxide synthase [Homo sapiens]" . . . . . 100.00 1203 100.00 100.00 1.37e+00 . . . . 18028 2 15 no GB AAA36365 . "nitric oxide synthase [Homo sapiens]" . . . . . 100.00 1203 100.00 100.00 1.37e+00 . . . . 18028 2 16 no PRF 2011304A . "NO synthase" . . . . . 100.00 1205 100.00 100.00 1.37e+00 . . . . 18028 2 17 no REF NP_000594 . "nitric oxide synthase, endothelial isoform 1 [Homo sapiens]" . . . . . 100.00 1203 100.00 100.00 1.37e+00 . . . . 18028 2 18 no REF NP_001003158 . "nitric oxide synthase, endothelial [Canis lupus familiaris]" . . . . . 100.00 1205 100.00 100.00 1.37e+00 . . . . 18028 2 19 no REF NP_001076202 . "nitric oxide synthase, endothelial [Oryctolagus cuniculus]" . . . . . 100.00 1209 100.00 100.00 1.37e+00 . . . . 18028 2 20 no REF NP_001123373 . "nitric oxide synthase, endothelial [Ovis aries]" . . . . . 100.00 1205 100.00 100.00 1.37e+00 . . . . 18028 2 21 no REF NP_001153581 . "nitric oxide synthase, endothelial isoform 2 [Homo sapiens]" . . . . . 100.00 596 100.00 100.00 1.21e+00 . . . . 18028 2 22 no SP P29473 . "RecName: Full=Nitric oxide synthase, endothelial; AltName: Full=Constitutive NOS; Short=cNOS; AltName: Full=EC-NOS; AltName: Fu" . . . . . 100.00 1205 100.00 100.00 1.37e+00 . . . . 18028 2 23 no SP P29474 . "RecName: Full=Nitric oxide synthase, endothelial; AltName: Full=Constitutive NOS; Short=cNOS; AltName: Full=EC-NOS; AltName: Fu" . . . . . 100.00 1203 100.00 100.00 1.37e+00 . . . . 18028 2 24 no SP P70313 . "RecName: Full=Nitric oxide synthase, endothelial; AltName: Full=Constitutive NOS; Short=cNOS; AltName: Full=EC-NOS; AltName: Fu" . . . . . 100.00 1202 100.00 100.00 1.37e+00 . . . . 18028 2 25 no SP Q28969 . "RecName: Full=Nitric oxide synthase, endothelial; AltName: Full=Constitutive NOS; Short=cNOS; AltName: Full=EC-NOS; AltName: Fu" . . . . . 100.00 1205 100.00 100.00 1.37e+00 . . . . 18028 2 26 no SP Q62600 . "RecName: Full=Nitric oxide synthase, endothelial; AltName: Full=Constitutive NOS; Short=cNOS; AltName: Full=EC-NOS; AltName: Fu" . . . . . 100.00 1202 100.00 100.00 1.37e+00 . . . . 18028 2 27 no TPG DAA30266 . "TPA: nitric oxide synthase, endothelial [Bos taurus]" . . . . . 100.00 1205 100.00 100.00 1.37e+00 . . . . 18028 2 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . LYS . 18028 2 2 . LYS . 18028 2 3 . THR . 18028 2 4 . PHE . 18028 2 5 . LYS . 18028 2 6 . GLU . 18028 2 7 . VAL . 18028 2 8 . ALA . 18028 2 9 . ASN . 18028 2 10 . ALA . 18028 2 11 . VAL . 18028 2 12 . LYS . 18028 2 13 . ILE . 18028 2 14 . SER . 18028 2 15 . ALA . 18028 2 16 . SER . 18028 2 17 . LEU . 18028 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 . LYS 1 1 18028 2 . LYS 2 2 18028 2 . THR 3 3 18028 2 . PHE 4 4 18028 2 . LYS 5 5 18028 2 . GLU 6 6 18028 2 . VAL 7 7 18028 2 . ALA 8 8 18028 2 . ASN 9 9 18028 2 . ALA 10 10 18028 2 . VAL 11 11 18028 2 . LYS 12 12 18028 2 . ILE 13 13 18028 2 . SER 14 14 18028 2 . ALA 15 15 18028 2 . SER 16 16 18028 2 . LEU 17 17 18028 2 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 18028 _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 $CaM . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 18028 1 2 2 $eNOS . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 18028 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 18028 _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 $CaM . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pET9dCaM . . . . . . 18028 1 2 2 $eNOS . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . N/A . . . . . . 18028 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 18028 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% 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 CaM '[U-99% 13C; U-99% 15N]' . . 1 $CaM . . 1.0 . . mM . . . . 18028 1 2 entity_2 'natural abundance' . . 2 $eNOS . . 1.0 . . mM . . . . 18028 1 3 'potassium chloride' 'natural abundance' . . . . . . 100 . . mM . . . . 18028 1 4 'calcium chloride' 'natural abundance' . . . . . . 10 . . mM . . . . 18028 1 5 'sodium azide' 'natural abundance' . . . . . . 0.2 . . mM . . . . 18028 1 6 H2O 'natural abundance' . . . . . . 90 . . % . . . . 18028 1 7 D2O 'natural abundance' . . . . . . 10 . . % . . . . 18028 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 18028 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 6.0 . pH 18028 1 pressure 1 . atm 18028 1 temperature 298 . K 18028 1 stop_ save_ ############################ # Computer software used # ############################ save_CNSSOLVE _Software.Sf_category software _Software.Sf_framecode CNSSOLVE _Software.Entry_ID 18028 _Software.ID 1 _Software.Name CNSSOLVE _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Brunger, Adams, Clore, Gros, Nilges and Read' . . 18028 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 18028 1 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 18028 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 18028 _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 DRX . 600 . . . 18028 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 18028 _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 HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18028 1 2 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18028 1 3 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18028 1 4 '3D HCCH-TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18028 1 5 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18028 1 6 '3D 1H-13C NOESY aliphatic' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18028 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 18028 _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 TMS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 18028 1 H 1 TMS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 18028 1 N 15 TMS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 18028 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 18028 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-15N HSQC' . . . 18028 1 2 '3D CBCA(CO)NH' . . . 18028 1 3 '3D HNCA' . . . 18028 1 4 '3D HCCH-TOCSY' . . . 18028 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 2 2 ASP H H 1 8.502 0.020 . 1 . . . A 2 ASP H . 18028 1 2 . 1 1 2 2 ASP HA H 1 4.585 0.020 . 1 . . . A 2 ASP HA . 18028 1 3 . 1 1 2 2 ASP CA C 13 51.960 0.3 . 1 . . . A 2 ASP CA . 18028 1 4 . 1 1 2 2 ASP N N 15 120.349 0.3 . 1 . . . A 2 ASP N . 18028 1 5 . 1 1 3 3 GLN H H 1 8.200 0.020 . 1 . . . A 3 GLN H . 18028 1 6 . 1 1 3 3 GLN HA H 1 4.212 0.020 . 1 . . . A 3 GLN HA . 18028 1 7 . 1 1 3 3 GLN CA C 13 52.735 0.3 . 1 . . . A 3 GLN CA . 18028 1 8 . 1 1 3 3 GLN N N 15 119.648 0.3 . 1 . . . A 3 GLN N . 18028 1 9 . 1 1 4 4 LEU H H 1 8.181 0.020 . 1 . . . A 4 LEU H . 18028 1 10 . 1 1 4 4 LEU HA H 1 4.540 0.020 . 1 . . . A 4 LEU HA . 18028 1 11 . 1 1 4 4 LEU HB2 H 1 1.584 0.020 . 1 . . . A 4 LEU HB2 . 18028 1 12 . 1 1 4 4 LEU HB3 H 1 1.584 0.020 . 1 . . . A 4 LEU HB3 . 18028 1 13 . 1 1 4 4 LEU HD11 H 1 0.751 0.020 . 1 . . . A 4 LEU HD11 . 18028 1 14 . 1 1 4 4 LEU HD12 H 1 0.751 0.020 . 1 . . . A 4 LEU HD12 . 18028 1 15 . 1 1 4 4 LEU HD13 H 1 0.751 0.020 . 1 . . . A 4 LEU HD13 . 18028 1 16 . 1 1 4 4 LEU HD21 H 1 0.751 0.020 . 1 . . . A 4 LEU HD21 . 18028 1 17 . 1 1 4 4 LEU HD22 H 1 0.751 0.020 . 1 . . . A 4 LEU HD22 . 18028 1 18 . 1 1 4 4 LEU HD23 H 1 0.751 0.020 . 1 . . . A 4 LEU HD23 . 18028 1 19 . 1 1 4 4 LEU CA C 13 51.658 0.3 . 1 . . . A 4 LEU CA . 18028 1 20 . 1 1 4 4 LEU N N 15 123.025 0.3 . 1 . . . A 4 LEU N . 18028 1 21 . 1 1 5 5 THR H H 1 8.615 0.020 . 1 . . . A 5 THR H . 18028 1 22 . 1 1 5 5 THR HA H 1 4.271 0.020 . 1 . . . A 5 THR HA . 18028 1 23 . 1 1 5 5 THR HG21 H 1 1.169 0.020 . 1 . . . A 5 THR HG21 . 18028 1 24 . 1 1 5 5 THR HG22 H 1 1.169 0.020 . 1 . . . A 5 THR HG22 . 18028 1 25 . 1 1 5 5 THR HG23 H 1 1.169 0.020 . 1 . . . A 5 THR HG23 . 18028 1 26 . 1 1 5 5 THR CA C 13 57.687 0.3 . 1 . . . A 5 THR CA . 18028 1 27 . 1 1 5 5 THR N N 15 112.894 0.3 . 1 . . . A 5 THR N . 18028 1 28 . 1 1 6 6 GLU H H 1 8.882 0.020 . 1 . . . A 6 GLU H . 18028 1 29 . 1 1 6 6 GLU HA H 1 3.797 0.020 . 1 . . . A 6 GLU HA . 18028 1 30 . 1 1 6 6 GLU HB2 H 1 1.880 0.020 . 1 . . . A 6 GLU HB2 . 18028 1 31 . 1 1 6 6 GLU HB3 H 1 1.880 0.020 . 1 . . . A 6 GLU HB3 . 18028 1 32 . 1 1 6 6 GLU HG2 H 1 2.219 0.020 . 1 . . . A 6 GLU HG2 . 18028 1 33 . 1 1 6 6 GLU HG3 H 1 2.219 0.020 . 1 . . . A 6 GLU HG3 . 18028 1 34 . 1 1 6 6 GLU CA C 13 57.247 0.3 . 1 . . . A 6 GLU CA . 18028 1 35 . 1 1 6 6 GLU N N 15 120.209 0.3 . 1 . . . A 6 GLU N . 18028 1 36 . 1 1 7 7 GLU H H 1 8.545 0.020 . 1 . . . A 7 GLU H . 18028 1 37 . 1 1 7 7 GLU HA H 1 3.861 0.020 . 1 . . . A 7 GLU HA . 18028 1 38 . 1 1 7 7 GLU HB2 H 1 1.846 0.020 . 1 . . . A 7 GLU HB2 . 18028 1 39 . 1 1 7 7 GLU HB3 H 1 1.846 0.020 . 1 . . . A 7 GLU HB3 . 18028 1 40 . 1 1 7 7 GLU HG2 H 1 2.178 0.020 . 1 . . . A 7 GLU HG2 . 18028 1 41 . 1 1 7 7 GLU HG3 H 1 2.178 0.020 . 1 . . . A 7 GLU HG3 . 18028 1 42 . 1 1 7 7 GLU CA C 13 57.198 0.3 . 1 . . . A 7 GLU CA . 18028 1 43 . 1 1 7 7 GLU N N 15 119.415 0.3 . 1 . . . A 7 GLU N . 18028 1 44 . 1 1 8 8 GLN H H 1 7.587 0.020 . 1 . . . A 8 GLN H . 18028 1 45 . 1 1 8 8 GLN HA H 1 3.861 0.020 . 1 . . . A 8 GLN HA . 18028 1 46 . 1 1 8 8 GLN HB2 H 1 1.781 0.020 . 1 . . . A 8 GLN HB2 . 18028 1 47 . 1 1 8 8 GLN HB3 H 1 1.781 0.020 . 1 . . . A 8 GLN HB3 . 18028 1 48 . 1 1 8 8 GLN HG2 H 1 2.175 0.020 . 1 . . . A 8 GLN HG2 . 18028 1 49 . 1 1 8 8 GLN HG3 H 1 2.175 0.020 . 1 . . . A 8 GLN HG3 . 18028 1 50 . 1 1 8 8 GLN CA C 13 55.976 0.3 . 1 . . . A 8 GLN CA . 18028 1 51 . 1 1 8 8 GLN N N 15 119.809 0.3 . 1 . . . A 8 GLN N . 18028 1 52 . 1 1 9 9 ILE H H 1 8.268 0.020 . 1 . . . A 9 ILE H . 18028 1 53 . 1 1 9 9 ILE HA H 1 3.712 0.020 . 1 . . . A 9 ILE HA . 18028 1 54 . 1 1 9 9 ILE HB H 1 1.773 0.020 . 1 . . . A 9 ILE HB . 18028 1 55 . 1 1 9 9 ILE HG12 H 1 0.943 0.020 . 1 . . . A 9 ILE HG12 . 18028 1 56 . 1 1 9 9 ILE HG13 H 1 0.943 0.020 . 1 . . . A 9 ILE HG13 . 18028 1 57 . 1 1 9 9 ILE HD11 H 1 0.708 0.020 . 1 . . . A 9 ILE HD11 . 18028 1 58 . 1 1 9 9 ILE HD12 H 1 0.708 0.020 . 1 . . . A 9 ILE HD12 . 18028 1 59 . 1 1 9 9 ILE HD13 H 1 0.708 0.020 . 1 . . . A 9 ILE HD13 . 18028 1 60 . 1 1 9 9 ILE CA C 13 63.796 0.3 . 1 . . . A 9 ILE CA . 18028 1 61 . 1 1 9 9 ILE N N 15 119.415 0.3 . 1 . . . A 9 ILE N . 18028 1 62 . 1 1 10 10 ALA H H 1 7.840 0.020 . 1 . . . A 10 ALA H . 18028 1 63 . 1 1 10 10 ALA HA H 1 3.925 0.020 . 1 . . . A 10 ALA HA . 18028 1 64 . 1 1 10 10 ALA HB1 H 1 1.347 0.020 . 1 . . . A 10 ALA HB1 . 18028 1 65 . 1 1 10 10 ALA HB2 H 1 1.347 0.020 . 1 . . . A 10 ALA HB2 . 18028 1 66 . 1 1 10 10 ALA HB3 H 1 1.347 0.020 . 1 . . . A 10 ALA HB3 . 18028 1 67 . 1 1 10 10 ALA CA C 13 52.702 0.3 . 1 . . . A 10 ALA CA . 18028 1 68 . 1 1 10 10 ALA N N 15 121.044 0.3 . 1 . . . A 10 ALA N . 18028 1 69 . 1 1 11 11 GLU H H 1 7.635 0.020 . 1 . . . A 11 GLU H . 18028 1 70 . 1 1 11 11 GLU HA H 1 3.949 0.020 . 1 . . . A 11 GLU HA . 18028 1 71 . 1 1 11 11 GLU HB2 H 1 1.808 0.020 . 1 . . . A 11 GLU HB2 . 18028 1 72 . 1 1 11 11 GLU HB3 H 1 1.808 0.020 . 1 . . . A 11 GLU HB3 . 18028 1 73 . 1 1 11 11 GLU HG2 H 1 2.175 0.020 . 1 . . . A 11 GLU HG2 . 18028 1 74 . 1 1 11 11 GLU HG3 H 1 2.175 0.020 . 1 . . . A 11 GLU HG3 . 18028 1 75 . 1 1 11 11 GLU CA C 13 56.563 0.3 . 1 . . . A 11 GLU CA . 18028 1 76 . 1 1 11 11 GLU N N 15 119.113 0.3 . 1 . . . A 11 GLU N . 18028 1 77 . 1 1 12 12 PHE H H 1 8.446 0.020 . 1 . . . A 12 PHE H . 18028 1 78 . 1 1 12 12 PHE HA H 1 4.777 0.020 . 1 . . . A 12 PHE HA . 18028 1 79 . 1 1 12 12 PHE HB2 H 1 3.350 0.020 . 1 . . . A 12 PHE HB2 . 18028 1 80 . 1 1 12 12 PHE CA C 13 56.954 0.3 . 1 . . . A 12 PHE CA . 18028 1 81 . 1 1 12 12 PHE N N 15 119.662 0.3 . 1 . . . A 12 PHE N . 18028 1 82 . 1 1 13 13 LYS H H 1 9.107 0.020 . 1 . . . A 13 LYS H . 18028 1 83 . 1 1 13 13 LYS HA H 1 3.903 0.020 . 1 . . . A 13 LYS HA . 18028 1 84 . 1 1 13 13 LYS HB2 H 1 1.752 0.020 . 1 . . . A 13 LYS HB2 . 18028 1 85 . 1 1 13 13 LYS HB3 H 1 1.752 0.020 . 1 . . . A 13 LYS HB3 . 18028 1 86 . 1 1 13 13 LYS CA C 13 57.296 0.3 . 1 . . . A 13 LYS CA . 18028 1 87 . 1 1 13 13 LYS N N 15 123.557 0.3 . 1 . . . A 13 LYS N . 18028 1 88 . 1 1 14 14 GLU H H 1 7.652 0.020 . 1 . . . A 14 GLU H . 18028 1 89 . 1 1 14 14 GLU HA H 1 3.949 0.020 . 1 . . . A 14 GLU HA . 18028 1 90 . 1 1 14 14 GLU HB2 H 1 1.803 0.020 . 1 . . . A 14 GLU HB2 . 18028 1 91 . 1 1 14 14 GLU HB3 H 1 1.803 0.020 . 1 . . . A 14 GLU HB3 . 18028 1 92 . 1 1 14 14 GLU HG2 H 1 2.175 0.020 . 1 . . . A 14 GLU HG2 . 18028 1 93 . 1 1 14 14 GLU HG3 H 1 2.175 0.020 . 1 . . . A 14 GLU HG3 . 18028 1 94 . 1 1 14 14 GLU CA C 13 56.465 0.3 . 1 . . . A 14 GLU CA . 18028 1 95 . 1 1 14 14 GLU N N 15 119.239 0.3 . 1 . . . A 14 GLU N . 18028 1 96 . 1 1 15 15 ALA H H 1 7.781 0.020 . 1 . . . A 15 ALA H . 18028 1 97 . 1 1 15 15 ALA HA H 1 3.993 0.020 . 1 . . . A 15 ALA HA . 18028 1 98 . 1 1 15 15 ALA HB1 H 1 1.728 0.020 . 1 . . . A 15 ALA HB1 . 18028 1 99 . 1 1 15 15 ALA HB2 H 1 1.728 0.020 . 1 . . . A 15 ALA HB2 . 18028 1 100 . 1 1 15 15 ALA HB3 H 1 1.728 0.020 . 1 . . . A 15 ALA HB3 . 18028 1 101 . 1 1 15 15 ALA CA C 13 52.751 0.3 . 1 . . . A 15 ALA CA . 18028 1 102 . 1 1 15 15 ALA N N 15 122.048 0.3 . 1 . . . A 15 ALA N . 18028 1 103 . 1 1 16 16 PHE H H 1 8.767 0.020 . 1 . . . A 16 PHE H . 18028 1 104 . 1 1 16 16 PHE HA H 1 3.095 0.020 . 1 . . . A 16 PHE HA . 18028 1 105 . 1 1 16 16 PHE HB2 H 1 2.669 0.020 . 1 . . . A 16 PHE HB2 . 18028 1 106 . 1 1 16 16 PHE HB3 H 1 2.669 0.020 . 1 . . . A 16 PHE HB3 . 18028 1 107 . 1 1 16 16 PHE HD1 H 1 6.477 0.020 . 1 . . . A 16 PHE HD1 . 18028 1 108 . 1 1 16 16 PHE HD2 H 1 6.477 0.020 . 1 . . . A 16 PHE HD2 . 18028 1 109 . 1 1 16 16 PHE HE1 H 1 6.903 0.020 . 1 . . . A 16 PHE HE1 . 18028 1 110 . 1 1 16 16 PHE HE2 H 1 6.903 0.020 . 1 . . . A 16 PHE HE2 . 18028 1 111 . 1 1 16 16 PHE HZ H 1 7.035 0.020 . 1 . . . A 16 PHE HZ . 18028 1 112 . 1 1 16 16 PHE CA C 13 59.544 0.3 . 1 . . . A 16 PHE CA . 18028 1 113 . 1 1 16 16 PHE N N 15 118.962 0.3 . 1 . . . A 16 PHE N . 18028 1 114 . 1 1 17 17 SER H H 1 7.828 0.020 . 1 . . . A 17 SER H . 18028 1 115 . 1 1 17 17 SER HA H 1 3.883 0.020 . 1 . . . A 17 SER HA . 18028 1 116 . 1 1 17 17 SER HB2 H 1 3.883 0.020 . 1 . . . A 17 SER HB2 . 18028 1 117 . 1 1 17 17 SER HB3 H 1 3.883 0.020 . 1 . . . A 17 SER HB3 . 18028 1 118 . 1 1 17 17 SER CA C 13 58.567 0.3 . 1 . . . A 17 SER CA . 18028 1 119 . 1 1 17 17 SER N N 15 111.534 0.3 . 1 . . . A 17 SER N . 18028 1 120 . 1 1 18 18 LEU H H 1 7.240 0.020 . 1 . . . A 18 LEU H . 18028 1 121 . 1 1 18 18 LEU HA H 1 3.861 0.020 . 1 . . . A 18 LEU HA . 18028 1 122 . 1 1 18 18 LEU HB2 H 1 1.449 0.020 . 1 . . . A 18 LEU HB2 . 18028 1 123 . 1 1 18 18 LEU HB3 H 1 1.449 0.020 . 1 . . . A 18 LEU HB3 . 18028 1 124 . 1 1 18 18 LEU HG H 1 1.454 0.020 . 1 . . . A 18 LEU HG . 18028 1 125 . 1 1 18 18 LEU HD11 H 1 0.495 0.020 . 1 . . . A 18 LEU HD11 . 18028 1 126 . 1 1 18 18 LEU HD12 H 1 0.495 0.020 . 1 . . . A 18 LEU HD12 . 18028 1 127 . 1 1 18 18 LEU HD13 H 1 0.495 0.020 . 1 . . . A 18 LEU HD13 . 18028 1 128 . 1 1 18 18 LEU HD21 H 1 0.644 0.020 . 1 . . . A 18 LEU HD21 . 18028 1 129 . 1 1 18 18 LEU HD22 H 1 0.644 0.020 . 1 . . . A 18 LEU HD22 . 18028 1 130 . 1 1 18 18 LEU HD23 H 1 0.644 0.020 . 1 . . . A 18 LEU HD23 . 18028 1 131 . 1 1 18 18 LEU CA C 13 54.608 0.3 . 1 . . . A 18 LEU CA . 18028 1 132 . 1 1 18 18 LEU N N 15 121.260 0.3 . 1 . . . A 18 LEU N . 18028 1 133 . 1 1 19 19 PHE H H 1 7.070 0.020 . 1 . . . A 19 PHE H . 18028 1 134 . 1 1 19 19 PHE HA H 1 3.963 0.020 . 1 . . . A 19 PHE HA . 18028 1 135 . 1 1 19 19 PHE HB2 H 1 2.493 0.020 . 1 . . . A 19 PHE HB2 . 18028 1 136 . 1 1 19 19 PHE HB3 H 1 2.493 0.020 . 1 . . . A 19 PHE HB3 . 18028 1 137 . 1 1 19 19 PHE HD1 H 1 6.977 0.020 . 1 . . . A 19 PHE HD1 . 18028 1 138 . 1 1 19 19 PHE HD2 H 1 6.977 0.020 . 1 . . . A 19 PHE HD2 . 18028 1 139 . 1 1 19 19 PHE CA C 13 57.247 0.3 . 1 . . . A 19 PHE CA . 18028 1 140 . 1 1 19 19 PHE N N 15 114.235 0.3 . 1 . . . A 19 PHE N . 18028 1 141 . 1 1 20 20 ASP H H 1 7.667 0.020 . 1 . . . A 20 ASP H . 18028 1 142 . 1 1 20 20 ASP HA H 1 4.343 0.020 . 1 . . . A 20 ASP HA . 18028 1 143 . 1 1 20 20 ASP HB2 H 1 2.482 0.020 . 1 . . . A 20 ASP HB2 . 18028 1 144 . 1 1 20 20 ASP HB3 H 1 2.482 0.020 . 1 . . . A 20 ASP HB3 . 18028 1 145 . 1 1 20 20 ASP CA C 13 49.476 0.3 . 1 . . . A 20 ASP CA . 18028 1 146 . 1 1 20 20 ASP N N 15 115.761 0.3 . 1 . . . A 20 ASP N . 18028 1 147 . 1 1 21 21 LYS H H 1 7.548 0.020 . 1 . . . A 21 LYS H . 18028 1 148 . 1 1 21 21 LYS HA H 1 3.786 0.020 . 1 . . . A 21 LYS HA . 18028 1 149 . 1 1 21 21 LYS HB2 H 1 1.688 0.020 . 1 . . . A 21 LYS HB2 . 18028 1 150 . 1 1 21 21 LYS HB3 H 1 1.688 0.020 . 1 . . . A 21 LYS HB3 . 18028 1 151 . 1 1 21 21 LYS HG2 H 1 1.369 0.020 . 2 . . . A 21 LYS HG2 . 18028 1 152 . 1 1 21 21 LYS HG3 H 1 1.283 0.020 . 2 . . . A 21 LYS HG3 . 18028 1 153 . 1 1 21 21 LYS HD2 H 1 1.560 0.020 . 1 . . . A 21 LYS HD2 . 18028 1 154 . 1 1 21 21 LYS HD3 H 1 1.560 0.020 . 1 . . . A 21 LYS HD3 . 18028 1 155 . 1 1 21 21 LYS HE2 H 1 2.881 0.020 . 1 . . . A 21 LYS HE2 . 18028 1 156 . 1 1 21 21 LYS HE3 H 1 2.881 0.020 . 1 . . . A 21 LYS HE3 . 18028 1 157 . 1 1 21 21 LYS CA C 13 56.025 0.3 . 1 . . . A 21 LYS CA . 18028 1 158 . 1 1 21 21 LYS N N 15 124.906 0.3 . 1 . . . A 21 LYS N . 18028 1 159 . 1 1 22 22 ASP H H 1 7.952 0.020 . 1 . . . A 22 ASP H . 18028 1 160 . 1 1 22 22 ASP HA H 1 4.431 0.020 . 1 . . . A 22 ASP HA . 18028 1 161 . 1 1 22 22 ASP HB2 H 1 2.482 0.020 . 1 . . . A 22 ASP HB2 . 18028 1 162 . 1 1 22 22 ASP HB3 H 1 2.898 0.020 . 2 . . . A 22 ASP HB3 . 18028 1 163 . 1 1 22 22 ASP CA C 13 49.965 0.3 . 1 . . . A 22 ASP CA . 18028 1 164 . 1 1 22 22 ASP N N 15 113.609 0.3 . 1 . . . A 22 ASP N . 18028 1 165 . 1 1 23 23 GLY H H 1 7.602 0.020 . 1 . . . A 23 GLY H . 18028 1 166 . 1 1 23 23 GLY HA2 H 1 3.686 0.020 . 1 . . . A 23 GLY HA2 . 18028 1 167 . 1 1 23 23 GLY HA3 H 1 3.686 0.020 . 1 . . . A 23 GLY HA3 . 18028 1 168 . 1 1 23 23 GLY CA C 13 44.442 0.3 . 1 . . . A 23 GLY CA . 18028 1 169 . 1 1 23 23 GLY N N 15 109.369 0.3 . 1 . . . A 23 GLY N . 18028 1 170 . 1 1 24 24 ASP H H 1 8.266 0.020 . 1 . . . A 24 ASP H . 18028 1 171 . 1 1 24 24 ASP HA H 1 4.329 0.020 . 1 . . . A 24 ASP HA . 18028 1 172 . 1 1 24 24 ASP HB2 H 1 2.881 0.020 . 1 . . . A 24 ASP HB2 . 18028 1 173 . 1 1 24 24 ASP HB3 H 1 2.881 0.020 . 1 . . . A 24 ASP HB3 . 18028 1 174 . 1 1 24 24 ASP CA C 13 51.040 0.3 . 1 . . . A 24 ASP CA . 18028 1 175 . 1 1 24 24 ASP N N 15 120.643 0.3 . 1 . . . A 24 ASP N . 18028 1 176 . 1 1 25 25 GLY H H 1 10.543 0.020 . 1 . . . A 25 GLY H . 18028 1 177 . 1 1 25 25 GLY HA2 H 1 3.541 0.020 . 1 . . . A 25 GLY HA2 . 18028 1 178 . 1 1 25 25 GLY HA3 H 1 3.541 0.020 . 2 . . . A 25 GLY HA3 . 18028 1 179 . 1 1 25 25 GLY CA C 13 42.683 0.3 . 1 . . . A 25 GLY CA . 18028 1 180 . 1 1 25 25 GLY N N 15 113.205 0.3 . 1 . . . A 25 GLY N . 18028 1 181 . 1 1 26 26 THR H H 1 8.020 0.020 . 1 . . . A 26 THR H . 18028 1 182 . 1 1 26 26 THR HA H 1 5.140 0.020 . 1 . . . A 26 THR HA . 18028 1 183 . 1 1 26 26 THR HB H 1 3.688 0.020 . 1 . . . A 26 THR HB . 18028 1 184 . 1 1 26 26 THR HG21 H 1 0.861 0.020 . 1 . . . A 26 THR HG21 . 18028 1 185 . 1 1 26 26 THR HG22 H 1 0.861 0.020 . 1 . . . A 26 THR HG22 . 18028 1 186 . 1 1 26 26 THR HG23 H 1 0.861 0.020 . 1 . . . A 26 THR HG23 . 18028 1 187 . 1 1 26 26 THR CA C 13 56.954 0.3 . 1 . . . A 26 THR CA . 18028 1 188 . 1 1 26 26 THR N N 15 112.852 0.3 . 1 . . . A 26 THR N . 18028 1 189 . 1 1 27 27 ILE H H 1 9.689 0.020 . 1 . . . A 27 ILE H . 18028 1 190 . 1 1 27 27 ILE HA H 1 4.670 0.020 . 1 . . . A 27 ILE HA . 18028 1 191 . 1 1 27 27 ILE HB H 1 1.859 0.020 . 1 . . . A 27 ILE HB . 18028 1 192 . 1 1 27 27 ILE HG12 H 1 0.890 0.020 . 1 . . . A 27 ILE HG12 . 18028 1 193 . 1 1 27 27 ILE HG13 H 1 0.890 0.020 . 1 . . . A 27 ILE HG13 . 18028 1 194 . 1 1 27 27 ILE HD11 H 1 0.655 0.020 . 1 . . . A 27 ILE HD11 . 18028 1 195 . 1 1 27 27 ILE HD12 H 1 0.655 0.020 . 1 . . . A 27 ILE HD12 . 18028 1 196 . 1 1 27 27 ILE HD13 H 1 0.655 0.020 . 1 . . . A 27 ILE HD13 . 18028 1 197 . 1 1 27 27 ILE CA C 13 57.931 0.3 . 1 . . . A 27 ILE CA . 18028 1 198 . 1 1 27 27 ILE N N 15 127.005 0.3 . 1 . . . A 27 ILE N . 18028 1 199 . 1 1 28 28 THR H H 1 8.275 0.020 . 1 . . . A 28 THR H . 18028 1 200 . 1 1 28 28 THR HA H 1 4.713 0.020 . 1 . . . A 28 THR HA . 18028 1 201 . 1 1 28 28 THR HB H 1 3.840 0.020 . 1 . . . A 28 THR HB . 18028 1 202 . 1 1 28 28 THR HG21 H 1 0.718 0.020 . 1 . . . A 28 THR HG21 . 18028 1 203 . 1 1 28 28 THR HG22 H 1 0.718 0.020 . 1 . . . A 28 THR HG22 . 18028 1 204 . 1 1 28 28 THR HG23 H 1 0.718 0.020 . 1 . . . A 28 THR HG23 . 18028 1 205 . 1 1 28 28 THR CA C 13 56.612 0.3 . 1 . . . A 28 THR CA . 18028 1 206 . 1 1 28 28 THR N N 15 116.439 0.3 . 1 . . . A 28 THR N . 18028 1 207 . 1 1 29 29 THR H H 1 9.057 0.020 . 1 . . . A 29 THR H . 18028 1 208 . 1 1 29 29 THR HA H 1 3.612 0.020 . 1 . . . A 29 THR HA . 18028 1 209 . 1 1 29 29 THR HB H 1 4.015 0.020 . 1 . . . A 29 THR HB . 18028 1 210 . 1 1 29 29 THR HG21 H 1 1.102 0.020 . 1 . . . A 29 THR HG21 . 18028 1 211 . 1 1 29 29 THR HG22 H 1 1.102 0.020 . 1 . . . A 29 THR HG22 . 18028 1 212 . 1 1 29 29 THR HG23 H 1 1.102 0.020 . 1 . . . A 29 THR HG23 . 18028 1 213 . 1 1 29 29 THR CA C 13 63.845 0.3 . 1 . . . A 29 THR CA . 18028 1 214 . 1 1 29 29 THR N N 15 113.258 0.3 . 1 . . . A 29 THR N . 18028 1 215 . 1 1 30 30 LYS H H 1 7.578 0.020 . 1 . . . A 30 LYS H . 18028 1 216 . 1 1 30 30 LYS HA H 1 4.003 0.020 . 1 . . . A 30 LYS HA . 18028 1 217 . 1 1 30 30 LYS HB2 H 1 1.662 0.020 . 1 . . . A 30 LYS HB2 . 18028 1 218 . 1 1 30 30 LYS HB3 H 1 1.662 0.020 . 1 . . . A 30 LYS HB3 . 18028 1 219 . 1 1 30 30 LYS HG2 H 1 1.211 0.020 . 1 . . . A 30 LYS HG2 . 18028 1 220 . 1 1 30 30 LYS HG3 H 1 1.211 0.020 . 1 . . . A 30 LYS HG3 . 18028 1 221 . 1 1 30 30 LYS CA C 13 56.465 0.3 . 1 . . . A 30 LYS CA . 18028 1 222 . 1 1 30 30 LYS N N 15 121.230 0.3 . 1 . . . A 30 LYS N . 18028 1 223 . 1 1 31 31 GLU H H 1 7.712 0.020 . 1 . . . A 31 GLU H . 18028 1 224 . 1 1 31 31 GLU HA H 1 3.840 0.020 . 1 . . . A 31 GLU HA . 18028 1 225 . 1 1 31 31 GLU HB2 H 1 1.530 0.020 . 1 . . . A 31 GLU HB2 . 18028 1 226 . 1 1 31 31 GLU HB3 H 1 1.920 0.020 . 2 . . . A 31 GLU HB3 . 18028 1 227 . 1 1 31 31 GLU HG2 H 1 2.175 0.020 . 1 . . . A 31 GLU HG2 . 18028 1 228 . 1 1 31 31 GLU HG3 H 1 2.175 0.020 . 1 . . . A 31 GLU HG3 . 18028 1 229 . 1 1 31 31 GLU CA C 13 57.149 0.3 . 1 . . . A 31 GLU CA . 18028 1 230 . 1 1 31 31 GLU N N 15 122.002 0.3 . 1 . . . A 31 GLU N . 18028 1 231 . 1 1 32 32 LEU H H 1 8.520 0.020 . 1 . . . A 32 LEU H . 18028 1 232 . 1 1 32 32 LEU HA H 1 3.925 0.020 . 1 . . . A 32 LEU HA . 18028 1 233 . 1 1 32 32 LEU HB2 H 1 1.837 0.020 . 1 . . . A 32 LEU HB2 . 18028 1 234 . 1 1 32 32 LEU HB3 H 1 1.837 0.020 . 1 . . . A 32 LEU HB3 . 18028 1 235 . 1 1 32 32 LEU HG H 1 1.386 0.020 . 1 . . . A 32 LEU HG . 18028 1 236 . 1 1 32 32 LEU CA C 13 55.529 0.3 . 1 . . . A 32 LEU CA . 18028 1 237 . 1 1 32 32 LEU N N 15 119.182 0.3 . 1 . . . A 32 LEU N . 18028 1 238 . 1 1 33 33 GLY H H 1 8.384 0.020 . 1 . . . A 33 GLY H . 18028 1 239 . 1 1 33 33 GLY HA2 H 1 3.818 0.020 . 1 . . . A 33 GLY HA2 . 18028 1 240 . 1 1 33 33 GLY HA3 H 1 3.392 0.020 . 2 . . . A 33 GLY HA3 . 18028 1 241 . 1 1 33 33 GLY CA C 13 45.664 0.3 . 1 . . . A 33 GLY CA . 18028 1 242 . 1 1 33 33 GLY N N 15 103.688 0.3 . 1 . . . A 33 GLY N . 18028 1 243 . 1 1 34 34 THR H H 1 7.928 0.020 . 1 . . . A 34 THR H . 18028 1 244 . 1 1 34 34 THR HA H 1 3.816 0.020 . 1 . . . A 34 THR HA . 18028 1 245 . 1 1 34 34 THR HB H 1 4.158 0.020 . 1 . . . A 34 THR HB . 18028 1 246 . 1 1 34 34 THR HG21 H 1 1.124 0.020 . 1 . . . A 34 THR HG21 . 18028 1 247 . 1 1 34 34 THR HG22 H 1 1.124 0.020 . 1 . . . A 34 THR HG22 . 18028 1 248 . 1 1 34 34 THR HG23 H 1 1.124 0.020 . 1 . . . A 34 THR HG23 . 18028 1 249 . 1 1 34 34 THR CA C 13 64.285 0.3 . 1 . . . A 34 THR CA . 18028 1 250 . 1 1 34 34 THR N N 15 117.399 0.3 . 1 . . . A 34 THR N . 18028 1 251 . 1 1 35 35 VAL H H 1 7.091 0.020 . 1 . . . A 35 VAL H . 18028 1 252 . 1 1 35 35 VAL N N 15 120.256 0.3 . 1 . . . A 35 VAL N . 18028 1 253 . 1 1 36 36 MET H H 1 8.321 0.020 . 1 . . . A 36 MET H . 18028 1 254 . 1 1 36 36 MET HA H 1 3.861 0.020 . 1 . . . A 36 MET HA . 18028 1 255 . 1 1 36 36 MET HB2 H 1 1.715 0.020 . 1 . . . A 36 MET HB2 . 18028 1 256 . 1 1 36 36 MET HB3 H 1 1.715 0.020 . 1 . . . A 36 MET HB3 . 18028 1 257 . 1 1 36 36 MET HG2 H 1 1.978 0.020 . 1 . . . A 36 MET HG2 . 18028 1 258 . 1 1 36 36 MET HG3 H 1 1.978 0.020 . 1 . . . A 36 MET HG3 . 18028 1 259 . 1 1 36 36 MET CA C 13 57.101 0.3 . 1 . . . A 36 MET CA . 18028 1 260 . 1 1 36 36 MET N N 15 117.757 0.3 . 1 . . . A 36 MET N . 18028 1 261 . 1 1 37 37 ARG H H 1 8.236 0.020 . 1 . . . A 37 ARG H . 18028 1 262 . 1 1 37 37 ARG HA H 1 4.654 0.020 . 1 . . . A 37 ARG HA . 18028 1 263 . 1 1 37 37 ARG HB2 H 1 1.752 0.020 . 1 . . . A 37 ARG HB2 . 18028 1 264 . 1 1 37 37 ARG HB3 H 1 1.752 0.020 . 1 . . . A 37 ARG HB3 . 18028 1 265 . 1 1 37 37 ARG HG2 H 1 1.846 0.020 . 1 . . . A 37 ARG HG2 . 18028 1 266 . 1 1 37 37 ARG HG3 H 1 1.846 0.020 . 1 . . . A 37 ARG HG3 . 18028 1 267 . 1 1 37 37 ARG CA C 13 56.172 0.3 . 1 . . . A 37 ARG CA . 18028 1 268 . 1 1 37 37 ARG N N 15 117.647 0.3 . 1 . . . A 37 ARG N . 18028 1 269 . 1 1 38 38 SER H H 1 7.874 0.020 . 1 . . . A 38 SER H . 18028 1 270 . 1 1 38 38 SER HA H 1 4.074 0.020 . 1 . . . A 38 SER HA . 18028 1 271 . 1 1 38 38 SER HB2 H 1 3.581 0.020 . 1 . . . A 38 SER HB2 . 18028 1 272 . 1 1 38 38 SER HB3 H 1 3.581 0.020 . 1 . . . A 38 SER HB3 . 18028 1 273 . 1 1 38 38 SER CA C 13 59.251 0.3 . 1 . . . A 38 SER CA . 18028 1 274 . 1 1 38 38 SER N N 15 118.974 0.3 . 1 . . . A 38 SER N . 18028 1 275 . 1 1 39 39 LEU H H 1 7.258 0.020 . 1 . . . A 39 LEU H . 18028 1 276 . 1 1 39 39 LEU HA H 1 4.074 0.020 . 1 . . . A 39 LEU HA . 18028 1 277 . 1 1 39 39 LEU HB2 H 1 1.667 0.020 . 1 . . . A 39 LEU HB2 . 18028 1 278 . 1 1 39 39 LEU HB3 H 1 1.667 0.020 . 1 . . . A 39 LEU HB3 . 18028 1 279 . 1 1 39 39 LEU HG H 1 1.584 0.020 . 1 . . . A 39 LEU HG . 18028 1 280 . 1 1 39 39 LEU HD11 H 1 0.517 0.020 . 1 . . . A 39 LEU HD11 . 18028 1 281 . 1 1 39 39 LEU HD12 H 1 0.517 0.020 . 1 . . . A 39 LEU HD12 . 18028 1 282 . 1 1 39 39 LEU HD13 H 1 0.517 0.020 . 1 . . . A 39 LEU HD13 . 18028 1 283 . 1 1 39 39 LEU HD21 H 1 0.517 0.020 . 1 . . . A 39 LEU HD21 . 18028 1 284 . 1 1 39 39 LEU HD22 H 1 0.517 0.020 . 1 . . . A 39 LEU HD22 . 18028 1 285 . 1 1 39 39 LEU HD23 H 1 0.517 0.020 . 1 . . . A 39 LEU HD23 . 18028 1 286 . 1 1 39 39 LEU CA C 13 51.333 0.3 . 1 . . . A 39 LEU CA . 18028 1 287 . 1 1 39 39 LEU N N 15 118.804 0.3 . 1 . . . A 39 LEU N . 18028 1 288 . 1 1 40 40 GLY H H 1 7.462 0.020 . 1 . . . A 40 GLY H . 18028 1 289 . 1 1 40 40 GLY HA2 H 1 4.082 0.020 . 1 . . . A 40 GLY HA2 . 18028 1 290 . 1 1 40 40 GLY HA3 H 1 4.082 0.020 . 2 . . . A 40 GLY HA3 . 18028 1 291 . 1 1 40 40 GLY CA C 13 42.878 0.3 . 1 . . . A 40 GLY CA . 18028 1 292 . 1 1 40 40 GLY N N 15 104.887 0.3 . 1 . . . A 40 GLY N . 18028 1 293 . 1 1 41 41 GLN H H 1 7.860 0.020 . 1 . . . A 41 GLN H . 18028 1 294 . 1 1 41 41 GLN HA H 1 4.390 0.020 . 1 . . . A 41 GLN HA . 18028 1 295 . 1 1 41 41 GLN HB2 H 1 1.455 0.020 . 1 . . . A 41 GLN HB2 . 18028 1 296 . 1 1 41 41 GLN HB3 H 1 1.455 0.020 . 1 . . . A 41 GLN HB3 . 18028 1 297 . 1 1 41 41 GLN HG2 H 1 1.781 0.020 . 1 . . . A 41 GLN HG2 . 18028 1 298 . 1 1 41 41 GLN HG3 H 1 1.781 0.020 . 1 . . . A 41 GLN HG3 . 18028 1 299 . 1 1 41 41 GLN CA C 13 51.187 0.3 . 1 . . . A 41 GLN CA . 18028 1 300 . 1 1 41 41 GLN N N 15 118.032 0.3 . 1 . . . A 41 GLN N . 18028 1 301 . 1 1 42 42 ASN H H 1 8.566 0.020 . 1 . . . A 42 ASN H . 18028 1 302 . 1 1 42 42 ASN HA H 1 5.054 0.020 . 1 . . . A 42 ASN HA . 18028 1 303 . 1 1 42 42 ASN HB2 H 1 2.348 0.020 . 1 . . . A 42 ASN HB2 . 18028 1 304 . 1 1 42 42 ASN HB3 H 1 2.348 0.020 . 2 . . . A 42 ASN HB3 . 18028 1 305 . 1 1 42 42 ASN CA C 13 48.694 0.3 . 1 . . . A 42 ASN CA . 18028 1 306 . 1 1 42 42 ASN N N 15 115.627 0.3 . 1 . . . A 42 ASN N . 18028 1 307 . 1 1 43 43 PRO HD2 H 1 3.448 0.020 . 1 . . . A 43 PRO HD2 . 18028 1 308 . 1 1 44 44 THR H H 1 8.907 0.020 . 1 . . . A 44 THR H . 18028 1 309 . 1 1 44 44 THR HA H 1 4.321 0.020 . 1 . . . A 44 THR HA . 18028 1 310 . 1 1 44 44 THR HB H 1 4.595 0.020 . 1 . . . A 44 THR HB . 18028 1 311 . 1 1 44 44 THR HG21 H 1 1.162 0.020 . 1 . . . A 44 THR HG21 . 18028 1 312 . 1 1 44 44 THR HG22 H 1 1.162 0.020 . 1 . . . A 44 THR HG22 . 18028 1 313 . 1 1 44 44 THR HG23 H 1 1.162 0.020 . 1 . . . A 44 THR HG23 . 18028 1 314 . 1 1 44 44 THR CA C 13 57.638 0.3 . 1 . . . A 44 THR CA . 18028 1 315 . 1 1 44 44 THR N N 15 113.553 0.3 . 1 . . . A 44 THR N . 18028 1 316 . 1 1 45 45 GLU H H 1 8.654 0.020 . 1 . . . A 45 GLU H . 18028 1 317 . 1 1 45 45 GLU HA H 1 3.817 0.020 . 1 . . . A 45 GLU HA . 18028 1 318 . 1 1 45 45 GLU HB2 H 1 1.868 0.020 . 1 . . . A 45 GLU HB2 . 18028 1 319 . 1 1 45 45 GLU HB3 H 1 1.868 0.020 . 1 . . . A 45 GLU HB3 . 18028 1 320 . 1 1 45 45 GLU HG2 H 1 2.175 0.020 . 1 . . . A 45 GLU HG2 . 18028 1 321 . 1 1 45 45 GLU HG3 H 1 2.175 0.020 . 1 . . . A 45 GLU HG3 . 18028 1 322 . 1 1 45 45 GLU CA C 13 57.101 0.3 . 1 . . . A 45 GLU CA . 18028 1 323 . 1 1 45 45 GLU N N 15 120.447 0.3 . 1 . . . A 45 GLU N . 18028 1 324 . 1 1 46 46 ALA H H 1 8.137 0.020 . 1 . . . A 46 ALA H . 18028 1 325 . 1 1 46 46 ALA HA H 1 3.925 0.020 . 1 . . . A 46 ALA HA . 18028 1 326 . 1 1 46 46 ALA HB1 H 1 1.220 0.020 . 1 . . . A 46 ALA HB1 . 18028 1 327 . 1 1 46 46 ALA HB2 H 1 1.220 0.020 . 1 . . . A 46 ALA HB2 . 18028 1 328 . 1 1 46 46 ALA HB3 H 1 1.220 0.020 . 1 . . . A 46 ALA HB3 . 18028 1 329 . 1 1 46 46 ALA CA C 13 52.311 0.3 . 1 . . . A 46 ALA CA . 18028 1 330 . 1 1 46 46 ALA N N 15 120.615 0.3 . 1 . . . A 46 ALA N . 18028 1 331 . 1 1 47 47 GLU H H 1 7.589 0.020 . 1 . . . A 47 GLU H . 18028 1 332 . 1 1 47 47 GLU HA H 1 3.876 0.020 . 1 . . . A 47 GLU HA . 18028 1 333 . 1 1 47 47 GLU HB2 H 1 1.720 0.020 . 1 . . . A 47 GLU HB2 . 18028 1 334 . 1 1 47 47 GLU HB3 H 1 1.720 0.020 . 1 . . . A 47 GLU HB3 . 18028 1 335 . 1 1 47 47 GLU HG2 H 1 2.189 0.020 . 1 . . . A 47 GLU HG2 . 18028 1 336 . 1 1 47 47 GLU HG3 H 1 2.189 0.020 . 1 . . . A 47 GLU HG3 . 18028 1 337 . 1 1 47 47 GLU CA C 13 56.270 0.3 . 1 . . . A 47 GLU CA . 18028 1 338 . 1 1 47 47 GLU N N 15 118.078 0.3 . 1 . . . A 47 GLU N . 18028 1 339 . 1 1 48 48 LEU H H 1 7.868 0.020 . 1 . . . A 48 LEU H . 18028 1 340 . 1 1 48 48 LEU HA H 1 3.927 0.020 . 1 . . . A 48 LEU HA . 18028 1 341 . 1 1 48 48 LEU HB2 H 1 1.636 0.020 . 1 . . . A 48 LEU HB2 . 18028 1 342 . 1 1 48 48 LEU HB3 H 1 1.636 0.020 . 1 . . . A 48 LEU HB3 . 18028 1 343 . 1 1 48 48 LEU HG H 1 1.602 0.020 . 1 . . . A 48 LEU HG . 18028 1 344 . 1 1 48 48 LEU HD11 H 1 0.696 0.020 . 1 . . . A 48 LEU HD11 . 18028 1 345 . 1 1 48 48 LEU HD12 H 1 0.696 0.020 . 1 . . . A 48 LEU HD12 . 18028 1 346 . 1 1 48 48 LEU HD13 H 1 0.696 0.020 . 1 . . . A 48 LEU HD13 . 18028 1 347 . 1 1 48 48 LEU HD21 H 1 1.277 0.020 . 1 . . . A 48 LEU HD21 . 18028 1 348 . 1 1 48 48 LEU HD22 H 1 1.277 0.020 . 1 . . . A 48 LEU HD22 . 18028 1 349 . 1 1 48 48 LEU HD23 H 1 1.277 0.020 . 1 . . . A 48 LEU HD23 . 18028 1 350 . 1 1 48 48 LEU CA C 13 55.048 0.3 . 1 . . . A 48 LEU CA . 18028 1 351 . 1 1 48 48 LEU N N 15 120.241 0.3 . 1 . . . A 48 LEU N . 18028 1 352 . 1 1 49 49 GLN H H 1 8.031 0.020 . 1 . . . A 49 GLN H . 18028 1 353 . 1 1 49 49 GLN HA H 1 3.901 0.020 . 1 . . . A 49 GLN HA . 18028 1 354 . 1 1 49 49 GLN HB2 H 1 1.978 0.020 . 1 . . . A 49 GLN HB2 . 18028 1 355 . 1 1 49 49 GLN HB3 H 1 1.978 0.020 . 1 . . . A 49 GLN HB3 . 18028 1 356 . 1 1 49 49 GLN HG2 H 1 2.219 0.020 . 1 . . . A 49 GLN HG2 . 18028 1 357 . 1 1 49 49 GLN HG3 H 1 2.219 0.020 . 1 . . . A 49 GLN HG3 . 18028 1 358 . 1 1 49 49 GLN CA C 13 55.732 0.3 . 1 . . . A 49 GLN CA . 18028 1 359 . 1 1 49 49 GLN N N 15 117.939 0.3 . 1 . . . A 49 GLN N . 18028 1 360 . 1 1 50 50 ASP H H 1 8.010 0.020 . 1 . . . A 50 ASP H . 18028 1 361 . 1 1 50 50 ASP HA H 1 4.179 0.020 . 1 . . . A 50 ASP HA . 18028 1 362 . 1 1 50 50 ASP HB2 H 1 2.555 0.020 . 1 . . . A 50 ASP HB2 . 18028 1 363 . 1 1 50 50 ASP HB3 H 1 2.555 0.020 . 1 . . . A 50 ASP HB3 . 18028 1 364 . 1 1 50 50 ASP CA C 13 54.706 0.3 . 1 . . . A 50 ASP CA . 18028 1 365 . 1 1 50 50 ASP N N 15 119.284 0.3 . 1 . . . A 50 ASP N . 18028 1 366 . 1 1 51 51 MET H H 1 7.609 0.020 . 1 . . . A 51 MET H . 18028 1 367 . 1 1 51 51 MET HA H 1 3.923 0.020 . 1 . . . A 51 MET HA . 18028 1 368 . 1 1 51 51 MET HB2 H 1 1.829 0.020 . 1 . . . A 51 MET HB2 . 18028 1 369 . 1 1 51 51 MET HB3 H 1 1.829 0.020 . 1 . . . A 51 MET HB3 . 18028 1 370 . 1 1 51 51 MET CA C 13 56.563 0.3 . 1 . . . A 51 MET CA . 18028 1 371 . 1 1 51 51 MET N N 15 119.253 0.3 . 1 . . . A 51 MET N . 18028 1 372 . 1 1 52 52 ILE H H 1 7.514 0.020 . 1 . . . A 52 ILE H . 18028 1 373 . 1 1 52 52 ILE HA H 1 3.328 0.020 . 1 . . . A 52 ILE HA . 18028 1 374 . 1 1 52 52 ILE HB H 1 1.786 0.020 . 1 . . . A 52 ILE HB . 18028 1 375 . 1 1 52 52 ILE HG21 H 1 0.905 0.020 . 1 . . . A 52 ILE HG21 . 18028 1 376 . 1 1 52 52 ILE HG22 H 1 0.905 0.020 . 1 . . . A 52 ILE HG22 . 18028 1 377 . 1 1 52 52 ILE HG23 H 1 0.905 0.020 . 1 . . . A 52 ILE HG23 . 18028 1 378 . 1 1 52 52 ILE HD11 H 1 0.554 0.020 . 1 . . . A 52 ILE HD11 . 18028 1 379 . 1 1 52 52 ILE HD12 H 1 0.554 0.020 . 1 . . . A 52 ILE HD12 . 18028 1 380 . 1 1 52 52 ILE HD13 H 1 0.554 0.020 . 1 . . . A 52 ILE HD13 . 18028 1 381 . 1 1 52 52 ILE CA C 13 61.890 0.3 . 1 . . . A 52 ILE CA . 18028 1 382 . 1 1 52 52 ILE N N 15 117.584 0.3 . 1 . . . A 52 ILE N . 18028 1 383 . 1 1 53 53 ASN H H 1 8.418 0.020 . 1 . . . A 53 ASN H . 18028 1 384 . 1 1 53 53 ASN HA H 1 4.222 0.020 . 1 . . . A 53 ASN HA . 18028 1 385 . 1 1 53 53 ASN HB2 H 1 2.769 0.020 . 1 . . . A 53 ASN HB2 . 18028 1 386 . 1 1 53 53 ASN HB3 H 1 2.769 0.020 . 1 . . . A 53 ASN HB3 . 18028 1 387 . 1 1 53 53 ASN CA C 13 53.093 0.3 . 1 . . . A 53 ASN CA . 18028 1 388 . 1 1 53 53 ASN N N 15 117.126 0.3 . 1 . . . A 53 ASN N . 18028 1 389 . 1 1 54 54 GLU H H 1 7.460 0.020 . 1 . . . A 54 GLU H . 18028 1 390 . 1 1 54 54 GLU HA H 1 3.861 0.020 . 1 . . . A 54 GLU HA . 18028 1 391 . 1 1 54 54 GLU HB2 H 1 1.956 0.020 . 1 . . . A 54 GLU HB2 . 18028 1 392 . 1 1 54 54 GLU HB3 H 1 1.956 0.020 . 1 . . . A 54 GLU HB3 . 18028 1 393 . 1 1 54 54 GLU HG2 H 1 2.241 0.020 . 1 . . . A 54 GLU HG2 . 18028 1 394 . 1 1 54 54 GLU HG3 H 1 2.241 0.020 . 1 . . . A 54 GLU HG3 . 18028 1 395 . 1 1 54 54 GLU CA C 13 56.123 0.3 . 1 . . . A 54 GLU CA . 18028 1 396 . 1 1 54 54 GLU N N 15 116.395 0.3 . 1 . . . A 54 GLU N . 18028 1 397 . 1 1 55 55 VAL H H 1 7.044 0.020 . 1 . . . A 55 VAL H . 18028 1 398 . 1 1 55 55 VAL HA H 1 3.905 0.020 . 1 . . . A 55 VAL HA . 18028 1 399 . 1 1 55 55 VAL HB H 1 1.912 0.020 . 1 . . . A 55 VAL HB . 18028 1 400 . 1 1 55 55 VAL HG11 H 1 0.729 0.020 . 1 . . . A 55 VAL HG11 . 18028 1 401 . 1 1 55 55 VAL HG12 H 1 0.729 0.020 . 1 . . . A 55 VAL HG12 . 18028 1 402 . 1 1 55 55 VAL HG13 H 1 0.729 0.020 . 1 . . . A 55 VAL HG13 . 18028 1 403 . 1 1 55 55 VAL HG21 H 1 0.729 0.020 . 1 . . . A 55 VAL HG21 . 18028 1 404 . 1 1 55 55 VAL HG22 H 1 0.729 0.020 . 1 . . . A 55 VAL HG22 . 18028 1 405 . 1 1 55 55 VAL HG23 H 1 0.729 0.020 . 1 . . . A 55 VAL HG23 . 18028 1 406 . 1 1 55 55 VAL CA C 13 58.176 0.3 . 1 . . . A 55 VAL CA . 18028 1 407 . 1 1 55 55 VAL N N 15 108.622 0.3 . 1 . . . A 55 VAL N . 18028 1 408 . 1 1 56 56 ASP H H 1 7.560 0.020 . 1 . . . A 56 ASP H . 18028 1 409 . 1 1 56 56 ASP HA H 1 4.463 0.020 . 1 . . . A 56 ASP HA . 18028 1 410 . 1 1 56 56 ASP HB2 H 1 2.503 0.020 . 1 . . . A 56 ASP HB2 . 18028 1 411 . 1 1 56 56 ASP HB3 H 1 2.503 0.020 . 1 . . . A 56 ASP HB3 . 18028 1 412 . 1 1 56 56 ASP CA C 13 50.991 0.3 . 1 . . . A 56 ASP CA . 18028 1 413 . 1 1 56 56 ASP N N 15 121.492 0.3 . 1 . . . A 56 ASP N . 18028 1 414 . 1 1 57 57 ALA H H 1 8.359 0.020 . 1 . . . A 57 ALA H . 18028 1 415 . 1 1 57 57 ALA HA H 1 4.053 0.020 . 1 . . . A 57 ALA HA . 18028 1 416 . 1 1 57 57 ALA HB1 H 1 1.369 0.020 . 1 . . . A 57 ALA HB1 . 18028 1 417 . 1 1 57 57 ALA HB2 H 1 1.369 0.020 . 1 . . . A 57 ALA HB2 . 18028 1 418 . 1 1 57 57 ALA HB3 H 1 1.369 0.020 . 1 . . . A 57 ALA HB3 . 18028 1 419 . 1 1 57 57 ALA CA C 13 51.480 0.3 . 1 . . . A 57 ALA CA . 18028 1 420 . 1 1 57 57 ALA N N 15 131.811 0.3 . 1 . . . A 57 ALA N . 18028 1 421 . 1 1 58 58 ASP H H 1 7.978 0.020 . 1 . . . A 58 ASP H . 18028 1 422 . 1 1 58 58 ASP HA H 1 4.453 0.020 . 1 . . . A 58 ASP HA . 18028 1 423 . 1 1 58 58 ASP HB2 H 1 2.876 0.020 . 1 . . . A 58 ASP HB2 . 18028 1 424 . 1 1 58 58 ASP HB3 H 1 2.460 0.020 . 2 . . . A 58 ASP HB3 . 18028 1 425 . 1 1 58 58 ASP CA C 13 49.916 0.3 . 1 . . . A 58 ASP CA . 18028 1 426 . 1 1 58 58 ASP N N 15 113.609 0.3 . 1 . . . A 58 ASP N . 18028 1 427 . 1 1 59 59 GLY H H 1 7.424 0.020 . 1 . . . A 59 GLY H . 18028 1 428 . 1 1 59 59 GLY HA2 H 1 3.664 0.020 . 1 . . . A 59 GLY HA2 . 18028 1 429 . 1 1 59 59 GLY HA3 H 1 3.664 0.020 . 1 . . . A 59 GLY HA3 . 18028 1 430 . 1 1 59 59 GLY CA C 13 44.491 0.3 . 1 . . . A 59 GLY CA . 18028 1 431 . 1 1 59 59 GLY N N 15 108.143 0.3 . 1 . . . A 59 GLY N . 18028 1 432 . 1 1 60 60 ASN H H 1 7.916 0.020 . 1 . . . A 60 ASN H . 18028 1 433 . 1 1 60 60 ASN HA H 1 4.492 0.020 . 1 . . . A 60 ASN HA . 18028 1 434 . 1 1 60 60 ASN HB2 H 1 2.482 0.020 . 1 . . . A 60 ASN HB2 . 18028 1 435 . 1 1 60 60 ASN HB3 H 1 2.482 0.020 . 1 . . . A 60 ASN HB3 . 18028 1 436 . 1 1 60 60 ASN CA C 13 49.769 0.3 . 1 . . . A 60 ASN CA . 18028 1 437 . 1 1 60 60 ASN N N 15 118.109 0.3 . 1 . . . A 60 ASN N . 18028 1 438 . 1 1 61 61 GLY H H 1 10.485 0.020 . 1 . . . A 61 GLY H . 18028 1 439 . 1 1 61 61 GLY HA2 H 1 4.031 0.020 . 1 . . . A 61 GLY HA2 . 18028 1 440 . 1 1 61 61 GLY HA3 H 1 4.031 0.020 . 2 . . . A 61 GLY HA3 . 18028 1 441 . 1 1 61 61 GLY CA C 13 42.878 0.3 . 1 . . . A 61 GLY CA . 18028 1 442 . 1 1 61 61 GLY N N 15 113.247 0.3 . 1 . . . A 61 GLY N . 18028 1 443 . 1 1 62 62 THR H H 1 7.511 0.020 . 1 . . . A 62 THR H . 18028 1 444 . 1 1 62 62 THR HA H 1 4.606 0.020 . 1 . . . A 62 THR HA . 18028 1 445 . 1 1 62 62 THR HB H 1 3.788 0.020 . 1 . . . A 62 THR HB . 18028 1 446 . 1 1 62 62 THR HG21 H 1 0.948 0.020 . 1 . . . A 62 THR HG21 . 18028 1 447 . 1 1 62 62 THR HG22 H 1 0.948 0.020 . 1 . . . A 62 THR HG22 . 18028 1 448 . 1 1 62 62 THR HG23 H 1 0.948 0.020 . 1 . . . A 62 THR HG23 . 18028 1 449 . 1 1 62 62 THR CA C 13 56.661 0.3 . 1 . . . A 62 THR CA . 18028 1 450 . 1 1 62 62 THR N N 15 108.699 0.3 . 1 . . . A 62 THR N . 18028 1 451 . 1 1 63 63 ILE H H 1 8.732 0.020 . 1 . . . A 63 ILE H . 18028 1 452 . 1 1 63 63 ILE HA H 1 4.606 0.020 . 1 . . . A 63 ILE HA . 18028 1 453 . 1 1 63 63 ILE HB H 1 1.859 0.020 . 1 . . . A 63 ILE HB . 18028 1 454 . 1 1 63 63 ILE HG12 H 1 1.059 0.020 . 1 . . . A 63 ILE HG12 . 18028 1 455 . 1 1 63 63 ILE HG13 H 1 1.059 0.020 . 1 . . . A 63 ILE HG13 . 18028 1 456 . 1 1 63 63 ILE HG21 H 1 0.910 0.020 . 1 . . . A 63 ILE HG21 . 18028 1 457 . 1 1 63 63 ILE HG22 H 1 0.910 0.020 . 1 . . . A 63 ILE HG22 . 18028 1 458 . 1 1 63 63 ILE HG23 H 1 0.910 0.020 . 1 . . . A 63 ILE HG23 . 18028 1 459 . 1 1 63 63 ILE HD11 H 1 0.590 0.020 . 1 . . . A 63 ILE HD11 . 18028 1 460 . 1 1 63 63 ILE HD12 H 1 0.590 0.020 . 1 . . . A 63 ILE HD12 . 18028 1 461 . 1 1 63 63 ILE HD13 H 1 0.590 0.020 . 1 . . . A 63 ILE HD13 . 18028 1 462 . 1 1 63 63 ILE CA C 13 57.101 0.3 . 1 . . . A 63 ILE CA . 18028 1 463 . 1 1 63 63 ILE N N 15 122.717 0.3 . 1 . . . A 63 ILE N . 18028 1 464 . 1 1 64 64 ASP H H 1 8.707 0.020 . 1 . . . A 64 ASP H . 18028 1 465 . 1 1 64 64 ASP HA H 1 5.075 0.020 . 1 . . . A 64 ASP HA . 18028 1 466 . 1 1 64 64 ASP HB2 H 1 2.668 0.020 . 1 . . . A 64 ASP HB2 . 18028 1 467 . 1 1 64 64 ASP HB3 H 1 2.945 0.020 . 2 . . . A 64 ASP HB3 . 18028 1 468 . 1 1 64 64 ASP CA C 13 49.378 0.3 . 1 . . . A 64 ASP CA . 18028 1 469 . 1 1 64 64 ASP N N 15 127.818 0.3 . 1 . . . A 64 ASP N . 18028 1 470 . 1 1 65 65 PHE H H 1 8.847 0.020 . 1 . . . A 65 PHE H . 18028 1 471 . 1 1 65 65 PHE HA H 1 3.861 0.020 . 1 . . . A 65 PHE HA . 18028 1 472 . 1 1 65 65 PHE HB2 H 1 1.824 0.020 . 1 . . . A 65 PHE HB2 . 18028 1 473 . 1 1 65 65 PHE HB3 H 1 1.824 0.020 . 1 . . . A 65 PHE HB3 . 18028 1 474 . 1 1 65 65 PHE HD1 H 1 6.590 0.020 . 1 . . . A 65 PHE HD1 . 18028 1 475 . 1 1 65 65 PHE HD2 H 1 6.590 0.020 . 1 . . . A 65 PHE HD2 . 18028 1 476 . 1 1 65 65 PHE HZ H 1 7.035 0.020 . 1 . . . A 65 PHE HZ . 18028 1 477 . 1 1 65 65 PHE CA C 13 60.717 0.3 . 1 . . . A 65 PHE CA . 18028 1 478 . 1 1 65 65 PHE N N 15 118.653 0.3 . 1 . . . A 65 PHE N . 18028 1 479 . 1 1 67 67 GLU H H 1 7.948 0.020 . 1 . . . A 67 GLU H . 18028 1 480 . 1 1 67 67 GLU HA H 1 3.861 0.020 . 1 . . . A 67 GLU HA . 18028 1 481 . 1 1 67 67 GLU HB2 H 1 1.868 0.020 . 1 . . . A 67 GLU HB2 . 18028 1 482 . 1 1 67 67 GLU HB3 H 1 1.868 0.020 . 1 . . . A 67 GLU HB3 . 18028 1 483 . 1 1 67 67 GLU HG2 H 1 2.394 0.020 . 1 . . . A 67 GLU HG2 . 18028 1 484 . 1 1 67 67 GLU HG3 H 1 2.394 0.020 . 1 . . . A 67 GLU HG3 . 18028 1 485 . 1 1 67 67 GLU CA C 13 56.337 0.3 . 1 . . . A 67 GLU CA . 18028 1 486 . 1 1 67 67 GLU N N 15 117.690 0.3 . 1 . . . A 67 GLU N . 18028 1 487 . 1 1 68 68 PHE H H 1 8.760 0.020 . 1 . . . A 68 PHE H . 18028 1 488 . 1 1 68 68 PHE HA H 1 3.840 0.020 . 1 . . . A 68 PHE HA . 18028 1 489 . 1 1 68 68 PHE HB2 H 1 3.371 0.020 . 1 . . . A 68 PHE HB2 . 18028 1 490 . 1 1 68 68 PHE HB3 H 1 3.371 0.020 . 1 . . . A 68 PHE HB3 . 18028 1 491 . 1 1 68 68 PHE HD1 H 1 6.844 0.020 . 1 . . . A 68 PHE HD1 . 18028 1 492 . 1 1 68 68 PHE HD2 H 1 6.844 0.020 . 1 . . . A 68 PHE HD2 . 18028 1 493 . 1 1 68 68 PHE HE1 H 1 6.502 0.020 . 1 . . . A 68 PHE HE1 . 18028 1 494 . 1 1 68 68 PHE HE2 H 1 6.502 0.020 . 1 . . . A 68 PHE HE2 . 18028 1 495 . 1 1 68 68 PHE HZ H 1 7.001 0.020 . 1 . . . A 68 PHE HZ . 18028 1 496 . 1 1 68 68 PHE CA C 13 58.727 0.3 . 1 . . . A 68 PHE CA . 18028 1 497 . 1 1 68 68 PHE N N 15 123.348 0.3 . 1 . . . A 68 PHE N . 18028 1 498 . 1 1 69 69 LEU H H 1 8.400 0.020 . 1 . . . A 69 LEU H . 18028 1 499 . 1 1 69 69 LEU HA H 1 3.801 0.020 . 1 . . . A 69 LEU HA . 18028 1 500 . 1 1 69 69 LEU HB2 H 1 1.361 0.020 . 1 . . . A 69 LEU HB2 . 18028 1 501 . 1 1 69 69 LEU HB3 H 1 1.361 0.020 . 1 . . . A 69 LEU HB3 . 18028 1 502 . 1 1 69 69 LEU HG H 1 1.361 0.020 . 1 . . . A 69 LEU HG . 18028 1 503 . 1 1 69 69 LEU HD11 H 1 0.992 0.020 . 1 . . . A 69 LEU HD11 . 18028 1 504 . 1 1 69 69 LEU HD12 H 1 0.992 0.020 . 1 . . . A 69 LEU HD12 . 18028 1 505 . 1 1 69 69 LEU HD13 H 1 0.992 0.020 . 1 . . . A 69 LEU HD13 . 18028 1 506 . 1 1 69 69 LEU HD21 H 1 0.992 0.020 . 1 . . . A 69 LEU HD21 . 18028 1 507 . 1 1 69 69 LEU HD22 H 1 0.992 0.020 . 1 . . . A 69 LEU HD22 . 18028 1 508 . 1 1 69 69 LEU HD23 H 1 0.992 0.020 . 1 . . . A 69 LEU HD23 . 18028 1 509 . 1 1 69 69 LEU CA C 13 55.158 0.3 . 1 . . . A 69 LEU CA . 18028 1 510 . 1 1 69 69 LEU N N 15 118.822 0.3 . 1 . . . A 69 LEU N . 18028 1 511 . 1 1 70 70 THR H H 1 7.540 0.020 . 1 . . . A 70 THR H . 18028 1 512 . 1 1 70 70 THR HA H 1 3.641 0.020 . 1 . . . A 70 THR HA . 18028 1 513 . 1 1 70 70 THR HB H 1 4.168 0.020 . 1 . . . A 70 THR HB . 18028 1 514 . 1 1 70 70 THR HG21 H 1 1.036 0.020 . 1 . . . A 70 THR HG21 . 18028 1 515 . 1 1 70 70 THR HG22 H 1 1.036 0.020 . 1 . . . A 70 THR HG22 . 18028 1 516 . 1 1 70 70 THR HG23 H 1 1.036 0.020 . 1 . . . A 70 THR HG23 . 18028 1 517 . 1 1 70 70 THR CA C 13 63.843 0.3 . 1 . . . A 70 THR CA . 18028 1 518 . 1 1 70 70 THR N N 15 116.379 0.3 . 1 . . . A 70 THR N . 18028 1 519 . 1 1 71 71 MET H H 1 7.721 0.020 . 1 . . . A 71 MET H . 18028 1 520 . 1 1 71 71 MET HA H 1 3.752 0.020 . 1 . . . A 71 MET HA . 18028 1 521 . 1 1 71 71 MET HB2 H 1 1.671 0.020 . 1 . . . A 71 MET HB2 . 18028 1 522 . 1 1 71 71 MET HB3 H 1 1.671 0.020 . 1 . . . A 71 MET HB3 . 18028 1 523 . 1 1 71 71 MET HG2 H 1 2.197 0.020 . 1 . . . A 71 MET HG2 . 18028 1 524 . 1 1 71 71 MET HG3 H 1 2.197 0.020 . 1 . . . A 71 MET HG3 . 18028 1 525 . 1 1 71 71 MET CA C 13 56.303 0.3 . 1 . . . A 71 MET CA . 18028 1 526 . 1 1 71 71 MET N N 15 121.678 0.3 . 1 . . . A 71 MET N . 18028 1 527 . 1 1 72 72 MET H H 1 7.969 0.020 . 1 . . . A 72 MET H . 18028 1 528 . 1 1 72 72 MET HA H 1 3.774 0.020 . 1 . . . A 72 MET HA . 18028 1 529 . 1 1 72 72 MET HB2 H 1 1.890 0.020 . 1 . . . A 72 MET HB2 . 18028 1 530 . 1 1 72 72 MET HB3 H 1 1.890 0.020 . 1 . . . A 72 MET HB3 . 18028 1 531 . 1 1 72 72 MET HG2 H 1 2.065 0.020 . 1 . . . A 72 MET HG2 . 18028 1 532 . 1 1 72 72 MET HG3 H 1 2.065 0.020 . 1 . . . A 72 MET HG3 . 18028 1 533 . 1 1 72 72 MET CA C 13 53.307 0.3 . 1 . . . A 72 MET CA . 18028 1 534 . 1 1 72 72 MET N N 15 116.476 0.3 . 1 . . . A 72 MET N . 18028 1 535 . 1 1 73 73 ALA H H 1 8.059 0.020 . 1 . . . A 73 ALA H . 18028 1 536 . 1 1 73 73 ALA HA H 1 3.880 0.020 . 1 . . . A 73 ALA HA . 18028 1 537 . 1 1 73 73 ALA HB1 H 1 1.252 0.020 . 1 . . . A 73 ALA HB1 . 18028 1 538 . 1 1 73 73 ALA HB2 H 1 1.252 0.020 . 1 . . . A 73 ALA HB2 . 18028 1 539 . 1 1 73 73 ALA HB3 H 1 1.252 0.020 . 1 . . . A 73 ALA HB3 . 18028 1 540 . 1 1 73 73 ALA CA C 13 52.095 0.3 . 1 . . . A 73 ALA CA . 18028 1 541 . 1 1 73 73 ALA N N 15 121.540 0.3 . 1 . . . A 73 ALA N . 18028 1 542 . 1 1 74 74 ARG H H 1 7.353 0.020 . 1 . . . A 74 ARG H . 18028 1 543 . 1 1 74 74 ARG HA H 1 3.883 0.020 . 1 . . . A 74 ARG HA . 18028 1 544 . 1 1 74 74 ARG HB2 H 1 1.671 0.020 . 1 . . . A 74 ARG HB2 . 18028 1 545 . 1 1 74 74 ARG HB3 H 1 1.671 0.020 . 1 . . . A 74 ARG HB3 . 18028 1 546 . 1 1 74 74 ARG HD2 H 1 2.963 0.020 . 1 . . . A 74 ARG HD2 . 18028 1 547 . 1 1 74 74 ARG HD3 H 1 2.963 0.020 . 1 . . . A 74 ARG HD3 . 18028 1 548 . 1 1 74 74 ARG CA C 13 55.731 0.3 . 1 . . . A 74 ARG CA . 18028 1 549 . 1 1 74 74 ARG N N 15 115.761 0.3 . 1 . . . A 74 ARG N . 18028 1 550 . 1 1 75 75 LYS H H 1 7.621 0.020 . 1 . . . A 75 LYS H . 18028 1 551 . 1 1 75 75 LYS HA H 1 3.905 0.020 . 1 . . . A 75 LYS HA . 18028 1 552 . 1 1 75 75 LYS HB2 H 1 1.693 0.020 . 1 . . . A 75 LYS HB2 . 18028 1 553 . 1 1 75 75 LYS HB3 H 1 1.693 0.020 . 1 . . . A 75 LYS HB3 . 18028 1 554 . 1 1 75 75 LYS HG2 H 1 1.277 0.020 . 1 . . . A 75 LYS HG2 . 18028 1 555 . 1 1 75 75 LYS HG3 H 1 1.277 0.020 . 1 . . . A 75 LYS HG3 . 18028 1 556 . 1 1 75 75 LYS HD2 H 1 1.540 0.020 . 1 . . . A 75 LYS HD2 . 18028 1 557 . 1 1 75 75 LYS HD3 H 1 1.540 0.020 . 1 . . . A 75 LYS HD3 . 18028 1 558 . 1 1 75 75 LYS HE2 H 1 2.898 0.020 . 1 . . . A 75 LYS HE2 . 18028 1 559 . 1 1 75 75 LYS HE3 H 1 2.898 0.020 . 1 . . . A 75 LYS HE3 . 18028 1 560 . 1 1 75 75 LYS CA C 13 53.947 0.3 . 1 . . . A 75 LYS CA . 18028 1 561 . 1 1 75 75 LYS N N 15 117.213 0.3 . 1 . . . A 75 LYS N . 18028 1 562 . 1 1 76 76 MET H H 1 7.779 0.020 . 1 . . . A 76 MET H . 18028 1 563 . 1 1 76 76 MET HA H 1 4.212 0.020 . 1 . . . A 76 MET HA . 18028 1 564 . 1 1 76 76 MET HB2 H 1 2.483 0.020 . 1 . . . A 76 MET HB2 . 18028 1 565 . 1 1 76 76 MET HB3 H 1 2.483 0.020 . 1 . . . A 76 MET HB3 . 18028 1 566 . 1 1 76 76 MET HG2 H 1 2.591 0.020 . 1 . . . A 76 MET HG2 . 18028 1 567 . 1 1 76 76 MET HG3 H 1 2.591 0.020 . 1 . . . A 76 MET HG3 . 18028 1 568 . 1 1 76 76 MET CA C 13 53.947 0.3 . 1 . . . A 76 MET CA . 18028 1 569 . 1 1 76 76 MET N N 15 117.986 0.3 . 1 . . . A 76 MET N . 18028 1 570 . 1 1 77 77 LYS H H 1 7.646 0.020 . 1 . . . A 77 LYS H . 18028 1 571 . 1 1 77 77 LYS HA H 1 4.212 0.020 . 1 . . . A 77 LYS HA . 18028 1 572 . 1 1 77 77 LYS HB2 H 1 1.364 0.020 . 1 . . . A 77 LYS HB2 . 18028 1 573 . 1 1 77 77 LYS HB3 H 1 1.364 0.020 . 1 . . . A 77 LYS HB3 . 18028 1 574 . 1 1 77 77 LYS HG2 H 1 1.277 0.020 . 1 . . . A 77 LYS HG2 . 18028 1 575 . 1 1 77 77 LYS HG3 H 1 1.277 0.020 . 1 . . . A 77 LYS HG3 . 18028 1 576 . 1 1 77 77 LYS HD2 H 1 1.693 0.020 . 1 . . . A 77 LYS HD2 . 18028 1 577 . 1 1 77 77 LYS HD3 H 1 1.693 0.020 . 1 . . . A 77 LYS HD3 . 18028 1 578 . 1 1 77 77 LYS CA C 13 54.283 0.3 . 1 . . . A 77 LYS CA . 18028 1 579 . 1 1 77 77 LYS N N 15 119.979 0.3 . 1 . . . A 77 LYS N . 18028 1 580 . 1 1 78 78 ASP H H 1 8.007 0.020 . 1 . . . A 78 ASP H . 18028 1 581 . 1 1 78 78 ASP HA H 1 4.562 0.020 . 1 . . . A 78 ASP HA . 18028 1 582 . 1 1 78 78 ASP HB2 H 1 2.547 0.020 . 1 . . . A 78 ASP HB2 . 18028 1 583 . 1 1 78 78 ASP HB3 H 1 2.547 0.020 . 1 . . . A 78 ASP HB3 . 18028 1 584 . 1 1 78 78 ASP CA C 13 52.061 0.3 . 1 . . . A 78 ASP CA . 18028 1 585 . 1 1 78 78 ASP N N 15 119.333 0.3 . 1 . . . A 78 ASP N . 18028 1 586 . 1 1 79 79 THR H H 1 7.590 0.020 . 1 . . . A 79 THR H . 18028 1 587 . 1 1 79 79 THR HA H 1 4.625 0.020 . 1 . . . A 79 THR HA . 18028 1 588 . 1 1 79 79 THR HB H 1 4.168 0.020 . 1 . . . A 79 THR HB . 18028 1 589 . 1 1 79 79 THR HG21 H 1 1.080 0.020 . 1 . . . A 79 THR HG21 . 18028 1 590 . 1 1 79 79 THR HG22 H 1 1.080 0.020 . 1 . . . A 79 THR HG22 . 18028 1 591 . 1 1 79 79 THR HG23 H 1 1.080 0.020 . 1 . . . A 79 THR HG23 . 18028 1 592 . 1 1 79 79 THR CA C 13 59.030 0.3 . 1 . . . A 79 THR CA . 18028 1 593 . 1 1 79 79 THR N N 15 112.721 0.3 . 1 . . . A 79 THR N . 18028 1 594 . 1 1 80 80 ASP H H 1 8.349 0.020 . 1 . . . A 80 ASP H . 18028 1 595 . 1 1 80 80 ASP HA H 1 4.180 0.020 . 1 . . . A 80 ASP HA . 18028 1 596 . 1 1 80 80 ASP HB2 H 1 2.585 0.020 . 1 . . . A 80 ASP HB2 . 18028 1 597 . 1 1 80 80 ASP HB3 H 1 2.585 0.020 . 1 . . . A 80 ASP HB3 . 18028 1 598 . 1 1 80 80 ASP CA C 13 50.850 0.3 . 1 . . . A 80 ASP CA . 18028 1 599 . 1 1 80 80 ASP N N 15 122.829 0.3 . 1 . . . A 80 ASP N . 18028 1 600 . 1 1 81 81 SER H H 1 8.235 0.020 . 1 . . . A 81 SER H . 18028 1 601 . 1 1 81 81 SER HA H 1 3.861 0.020 . 1 . . . A 81 SER HA . 18028 1 602 . 1 1 81 81 SER HB2 H 1 3.796 0.020 . 1 . . . A 81 SER HB2 . 18028 1 603 . 1 1 81 81 SER HB3 H 1 3.796 0.020 . 1 . . . A 81 SER HB3 . 18028 1 604 . 1 1 81 81 SER CA C 13 57.717 0.3 . 1 . . . A 81 SER CA . 18028 1 605 . 1 1 81 81 SER N N 15 117.571 0.3 . 1 . . . A 81 SER N . 18028 1 606 . 1 1 82 82 GLU H H 1 8.372 0.020 . 1 . . . A 82 GLU H . 18028 1 607 . 1 1 82 82 GLU HA H 1 3.883 0.020 . 1 . . . A 82 GLU HA . 18028 1 608 . 1 1 82 82 GLU HB2 H 1 1.965 0.020 . 1 . . . A 82 GLU HB2 . 18028 1 609 . 1 1 82 82 GLU HG2 H 1 2.175 0.020 . 1 . . . A 82 GLU HG2 . 18028 1 610 . 1 1 82 82 GLU CA C 13 56.707 0.3 . 1 . . . A 82 GLU CA . 18028 1 611 . 1 1 82 82 GLU N N 15 121.904 0.3 . 1 . . . A 82 GLU N . 18028 1 612 . 1 1 83 83 GLU H H 1 8.036 0.020 . 1 . . . A 83 GLU H . 18028 1 613 . 1 1 83 83 GLU HA H 1 3.883 0.020 . 1 . . . A 83 GLU HA . 18028 1 614 . 1 1 83 83 GLU HB2 H 1 1.956 0.020 . 1 . . . A 83 GLU HB2 . 18028 1 615 . 1 1 83 83 GLU HB3 H 1 1.956 0.020 . 1 . . . A 83 GLU HB3 . 18028 1 616 . 1 1 83 83 GLU HG2 H 1 2.219 0.020 . 1 . . . A 83 GLU HG2 . 18028 1 617 . 1 1 83 83 GLU HG3 H 1 2.219 0.020 . 1 . . . A 83 GLU HG3 . 18028 1 618 . 1 1 83 83 GLU CA C 13 56.606 0.3 . 1 . . . A 83 GLU CA . 18028 1 619 . 1 1 83 83 GLU N N 15 119.340 0.3 . 1 . . . A 83 GLU N . 18028 1 620 . 1 1 84 84 GLU H H 1 8.153 0.020 . 1 . . . A 84 GLU H . 18028 1 621 . 1 1 84 84 GLU HA H 1 3.871 0.020 . 1 . . . A 84 GLU HA . 18028 1 622 . 1 1 84 84 GLU HB2 H 1 1.917 0.020 . 1 . . . A 84 GLU HB2 . 18028 1 623 . 1 1 84 84 GLU HB3 H 1 1.917 0.020 . 1 . . . A 84 GLU HB3 . 18028 1 624 . 1 1 84 84 GLU HG2 H 1 2.226 0.020 . 1 . . . A 84 GLU HG2 . 18028 1 625 . 1 1 84 84 GLU HG3 H 1 2.226 0.020 . 1 . . . A 84 GLU HG3 . 18028 1 626 . 1 1 84 84 GLU CA C 13 56.606 0.3 . 1 . . . A 84 GLU CA . 18028 1 627 . 1 1 84 84 GLU N N 15 118.279 0.3 . 1 . . . A 84 GLU N . 18028 1 628 . 1 1 85 85 ILE H H 1 7.910 0.020 . 1 . . . A 85 ILE H . 18028 1 629 . 1 1 85 85 ILE HA H 1 3.584 0.020 . 1 . . . A 85 ILE HA . 18028 1 630 . 1 1 85 85 ILE HB H 1 1.759 0.020 . 1 . . . A 85 ILE HB . 18028 1 631 . 1 1 85 85 ILE HG12 H 1 0.970 0.020 . 1 . . . A 85 ILE HG12 . 18028 1 632 . 1 1 85 85 ILE HG13 H 1 0.970 0.020 . 1 . . . A 85 ILE HG13 . 18028 1 633 . 1 1 85 85 ILE HG21 H 1 1.562 0.020 . 1 . . . A 85 ILE HG21 . 18028 1 634 . 1 1 85 85 ILE HG22 H 1 1.562 0.020 . 1 . . . A 85 ILE HG22 . 18028 1 635 . 1 1 85 85 ILE HG23 H 1 1.562 0.020 . 1 . . . A 85 ILE HG23 . 18028 1 636 . 1 1 85 85 ILE HD11 H 1 0.686 0.020 . 1 . . . A 85 ILE HD11 . 18028 1 637 . 1 1 85 85 ILE HD12 H 1 0.686 0.020 . 1 . . . A 85 ILE HD12 . 18028 1 638 . 1 1 85 85 ILE HD13 H 1 0.686 0.020 . 1 . . . A 85 ILE HD13 . 18028 1 639 . 1 1 85 85 ILE CA C 13 63.439 0.3 . 1 . . . A 85 ILE CA . 18028 1 640 . 1 1 85 85 ILE N N 15 120.905 0.3 . 1 . . . A 85 ILE N . 18028 1 641 . 1 1 86 86 ARG H H 1 8.227 0.020 . 1 . . . A 86 ARG H . 18028 1 642 . 1 1 86 86 ARG HA H 1 3.927 0.020 . 1 . . . A 86 ARG HA . 18028 1 643 . 1 1 86 86 ARG HB2 H 1 1.781 0.020 . 1 . . . A 86 ARG HB2 . 18028 1 644 . 1 1 86 86 ARG HB3 H 1 1.781 0.020 . 1 . . . A 86 ARG HB3 . 18028 1 645 . 1 1 86 86 ARG HG2 H 1 1.496 0.020 . 1 . . . A 86 ARG HG2 . 18028 1 646 . 1 1 86 86 ARG HG3 H 1 1.496 0.020 . 1 . . . A 86 ARG HG3 . 18028 1 647 . 1 1 86 86 ARG HD2 H 1 2.810 0.020 . 1 . . . A 86 ARG HD2 . 18028 1 648 . 1 1 86 86 ARG HD3 H 1 2.810 0.020 . 1 . . . A 86 ARG HD3 . 18028 1 649 . 1 1 86 86 ARG CA C 13 57.515 0.3 . 1 . . . A 86 ARG CA . 18028 1 650 . 1 1 86 86 ARG N N 15 121.722 0.3 . 1 . . . A 86 ARG N . 18028 1 651 . 1 1 87 87 GLU H H 1 8.156 0.020 . 1 . . . A 87 GLU H . 18028 1 652 . 1 1 87 87 GLU HA H 1 3.861 0.020 . 1 . . . A 87 GLU HA . 18028 1 653 . 1 1 87 87 GLU HB2 H 1 1.890 0.020 . 1 . . . A 87 GLU HB2 . 18028 1 654 . 1 1 87 87 GLU HB3 H 1 1.890 0.020 . 1 . . . A 87 GLU HB3 . 18028 1 655 . 1 1 87 87 GLU HG2 H 1 2.175 0.020 . 1 . . . A 87 GLU HG2 . 18028 1 656 . 1 1 87 87 GLU HG3 H 1 2.175 0.020 . 1 . . . A 87 GLU HG3 . 18028 1 657 . 1 1 87 87 GLU CA C 13 56.606 0.3 . 1 . . . A 87 GLU CA . 18028 1 658 . 1 1 87 87 GLU N N 15 118.369 0.3 . 1 . . . A 87 GLU N . 18028 1 659 . 1 1 88 88 ALA H H 1 7.884 0.020 . 1 . . . A 88 ALA H . 18028 1 660 . 1 1 88 88 ALA HA H 1 3.949 0.020 . 1 . . . A 88 ALA HA . 18028 1 661 . 1 1 88 88 ALA HB1 H 1 1.605 0.020 . 1 . . . A 88 ALA HB1 . 18028 1 662 . 1 1 88 88 ALA HB2 H 1 1.605 0.020 . 1 . . . A 88 ALA HB2 . 18028 1 663 . 1 1 88 88 ALA HB3 H 1 1.605 0.020 . 1 . . . A 88 ALA HB3 . 18028 1 664 . 1 1 88 88 ALA CA C 13 52.263 0.3 . 1 . . . A 88 ALA CA . 18028 1 665 . 1 1 88 88 ALA N N 15 120.389 0.3 . 1 . . . A 88 ALA N . 18028 1 666 . 1 1 89 89 PHE H H 1 8.446 0.020 . 1 . . . A 89 PHE H . 18028 1 667 . 1 1 89 89 PHE HA H 1 3.115 0.020 . 1 . . . A 89 PHE HA . 18028 1 668 . 1 1 89 89 PHE HB2 H 1 1.917 0.020 . 1 . . . A 89 PHE HB2 . 18028 1 669 . 1 1 89 89 PHE HB3 H 1 1.917 0.020 . 1 . . . A 89 PHE HB3 . 18028 1 670 . 1 1 89 89 PHE HD1 H 1 6.613 0.020 . 1 . . . A 89 PHE HD1 . 18028 1 671 . 1 1 89 89 PHE HD2 H 1 6.613 0.020 . 1 . . . A 89 PHE HD2 . 18028 1 672 . 1 1 89 89 PHE HE1 H 1 6.921 0.020 . 1 . . . A 89 PHE HE1 . 18028 1 673 . 1 1 89 89 PHE HE2 H 1 6.921 0.020 . 1 . . . A 89 PHE HE2 . 18028 1 674 . 1 1 89 89 PHE CA C 13 59.703 0.3 . 1 . . . A 89 PHE CA . 18028 1 675 . 1 1 89 89 PHE N N 15 118.191 0.3 . 1 . . . A 89 PHE N . 18028 1 676 . 1 1 90 90 ARG H H 1 7.762 0.020 . 1 . . . A 90 ARG H . 18028 1 677 . 1 1 90 90 ARG HA H 1 3.905 0.020 . 1 . . . A 90 ARG HA . 18028 1 678 . 1 1 90 90 ARG HB2 H 1 1.803 0.020 . 1 . . . A 90 ARG HB2 . 18028 1 679 . 1 1 90 90 ARG HB3 H 1 1.803 0.020 . 1 . . . A 90 ARG HB3 . 18028 1 680 . 1 1 90 90 ARG HG2 H 1 1.562 0.020 . 1 . . . A 90 ARG HG2 . 18028 1 681 . 1 1 90 90 ARG HG3 H 1 1.562 0.020 . 1 . . . A 90 ARG HG3 . 18028 1 682 . 1 1 90 90 ARG HD2 H 1 3.073 0.020 . 1 . . . A 90 ARG HD2 . 18028 1 683 . 1 1 90 90 ARG HD3 H 1 3.073 0.020 . 1 . . . A 90 ARG HD3 . 18028 1 684 . 1 1 90 90 ARG CA C 13 56.168 0.3 . 1 . . . A 90 ARG CA . 18028 1 685 . 1 1 90 90 ARG N N 15 116.070 0.3 . 1 . . . A 90 ARG N . 18028 1 686 . 1 1 91 91 VAL H H 1 7.229 0.020 . 1 . . . A 91 VAL H . 18028 1 687 . 1 1 91 91 VAL HA H 1 3.243 0.020 . 1 . . . A 91 VAL HA . 18028 1 688 . 1 1 91 91 VAL HB H 1 1.901 0.020 . 1 . . . A 91 VAL HB . 18028 1 689 . 1 1 91 91 VAL HG11 H 1 0.346 0.020 . 1 . . . A 91 VAL HG11 . 18028 1 690 . 1 1 91 91 VAL HG12 H 1 0.346 0.020 . 1 . . . A 91 VAL HG12 . 18028 1 691 . 1 1 91 91 VAL HG13 H 1 0.346 0.020 . 1 . . . A 91 VAL HG13 . 18028 1 692 . 1 1 91 91 VAL HG21 H 1 0.815 0.020 . 1 . . . A 91 VAL HG21 . 18028 1 693 . 1 1 91 91 VAL HG22 H 1 0.815 0.020 . 1 . . . A 91 VAL HG22 . 18028 1 694 . 1 1 91 91 VAL HG23 H 1 0.815 0.020 . 1 . . . A 91 VAL HG23 . 18028 1 695 . 1 1 91 91 VAL CA C 13 63.357 0.3 . 1 . . . A 91 VAL CA . 18028 1 696 . 1 1 91 91 VAL N N 15 118.202 0.3 . 1 . . . A 91 VAL N . 18028 1 697 . 1 1 92 92 PHE H H 1 6.690 0.020 . 1 . . . A 92 PHE H . 18028 1 698 . 1 1 92 92 PHE HA H 1 3.967 0.020 . 1 . . . A 92 PHE HA . 18028 1 699 . 1 1 92 92 PHE HD1 H 1 6.373 0.020 . 1 . . . A 92 PHE HD1 . 18028 1 700 . 1 1 92 92 PHE HD2 H 1 6.373 0.020 . 1 . . . A 92 PHE HD2 . 18028 1 701 . 1 1 92 92 PHE CA C 13 58.029 0.3 . 1 . . . A 92 PHE CA . 18028 1 702 . 1 1 92 92 PHE N N 15 113.143 0.3 . 1 . . . A 92 PHE N . 18028 1 703 . 1 1 93 93 ASP H H 1 7.860 0.020 . 1 . . . A 93 ASP H . 18028 1 704 . 1 1 93 93 ASP HA H 1 4.436 0.020 . 1 . . . A 93 ASP HA . 18028 1 705 . 1 1 93 93 ASP HB2 H 1 2.547 0.020 . 1 . . . A 93 ASP HB2 . 18028 1 706 . 1 1 93 93 ASP HB3 H 1 2.547 0.020 . 1 . . . A 93 ASP HB3 . 18028 1 707 . 1 1 93 93 ASP CA C 13 49.525 0.3 . 1 . . . A 93 ASP CA . 18028 1 708 . 1 1 93 93 ASP N N 15 116.549 0.3 . 1 . . . A 93 ASP N . 18028 1 709 . 1 1 94 94 LYS H H 1 7.595 0.020 . 1 . . . A 94 LYS H . 18028 1 710 . 1 1 94 94 LYS HA H 1 3.776 0.020 . 1 . . . A 94 LYS HA . 18028 1 711 . 1 1 94 94 LYS HB2 H 1 1.667 0.020 . 1 . . . A 94 LYS HB2 . 18028 1 712 . 1 1 94 94 LYS HB3 H 1 1.667 0.020 . 1 . . . A 94 LYS HB3 . 18028 1 713 . 1 1 94 94 LYS HG2 H 1 1.369 0.020 . 2 . . . A 94 LYS HG2 . 18028 1 714 . 1 1 94 94 LYS HG3 H 1 1.283 0.020 . 2 . . . A 94 LYS HG3 . 18028 1 715 . 1 1 94 94 LYS HD2 H 1 1.560 0.020 . 1 . . . A 94 LYS HD2 . 18028 1 716 . 1 1 94 94 LYS HD3 H 1 1.560 0.020 . 1 . . . A 94 LYS HD3 . 18028 1 717 . 1 1 94 94 LYS CA C 13 55.976 0.3 . 1 . . . A 94 LYS CA . 18028 1 718 . 1 1 94 94 LYS N N 15 125.339 0.3 . 1 . . . A 94 LYS N . 18028 1 719 . 1 1 95 95 ASP H H 1 8.091 0.020 . 1 . . . A 95 ASP H . 18028 1 720 . 1 1 95 95 ASP HA H 1 4.415 0.020 . 1 . . . A 95 ASP HA . 18028 1 721 . 1 1 95 95 ASP HB2 H 1 2.924 0.020 . 1 . . . A 95 ASP HB2 . 18028 1 722 . 1 1 95 95 ASP HB3 H 1 2.498 0.020 . 2 . . . A 95 ASP HB3 . 18028 1 723 . 1 1 95 95 ASP CA C 13 50.307 0.3 . 1 . . . A 95 ASP CA . 18028 1 724 . 1 1 95 95 ASP N N 15 114.015 0.3 . 1 . . . A 95 ASP N . 18028 1 725 . 1 1 96 96 GLY H H 1 7.659 0.020 . 1 . . . A 96 GLY H . 18028 1 726 . 1 1 96 96 GLY HA2 H 1 3.686 0.020 . 1 . . . A 96 GLY HA2 . 18028 1 727 . 1 1 96 96 GLY HA3 H 1 3.686 0.020 . 1 . . . A 96 GLY HA3 . 18028 1 728 . 1 1 96 96 GLY CA C 13 44.344 0.3 . 1 . . . A 96 GLY CA . 18028 1 729 . 1 1 96 96 GLY N N 15 109.044 0.3 . 1 . . . A 96 GLY N . 18028 1 730 . 1 1 97 97 ASN H H 1 8.243 0.020 . 1 . . . A 97 ASN H . 18028 1 731 . 1 1 97 97 ASN HA H 1 4.500 0.020 . 1 . . . A 97 ASN HA . 18028 1 732 . 1 1 97 97 ASN HB2 H 1 3.271 0.020 . 1 . . . A 97 ASN HB2 . 18028 1 733 . 1 1 97 97 ASN HB3 H 1 3.271 0.020 . 1 . . . A 97 ASN HB3 . 18028 1 734 . 1 1 97 97 ASN CA C 13 49.916 0.3 . 1 . . . A 97 ASN CA . 18028 1 735 . 1 1 97 97 ASN N N 15 119.575 0.3 . 1 . . . A 97 ASN N . 18028 1 736 . 1 1 98 98 GLY H H 1 10.445 0.020 . 1 . . . A 98 GLY H . 18028 1 737 . 1 1 98 98 GLY HA2 H 1 3.967 0.020 . 1 . . . A 98 GLY HA2 . 18028 1 738 . 1 1 98 98 GLY HA3 H 1 3.967 0.020 . 2 . . . A 98 GLY HA3 . 18028 1 739 . 1 1 98 98 GLY CA C 13 42.292 0.3 . 1 . . . A 98 GLY CA . 18028 1 740 . 1 1 98 98 GLY N N 15 112.392 0.3 . 1 . . . A 98 GLY N . 18028 1 741 . 1 1 99 99 TYR H H 1 7.568 0.020 . 1 . . . A 99 TYR H . 18028 1 742 . 1 1 99 99 TYR HA H 1 4.841 0.020 . 1 . . . A 99 TYR HA . 18028 1 743 . 1 1 99 99 TYR HB2 H 1 2.412 0.020 . 1 . . . A 99 TYR HB2 . 18028 1 744 . 1 1 99 99 TYR HB3 H 1 2.412 0.020 . 1 . . . A 99 TYR HB3 . 18028 1 745 . 1 1 99 99 TYR HD1 H 1 6.736 0.020 . 1 . . . A 99 TYR HD1 . 18028 1 746 . 1 1 99 99 TYR HD2 H 1 6.736 0.020 . 1 . . . A 99 TYR HD2 . 18028 1 747 . 1 1 99 99 TYR CA C 13 53.582 0.3 . 1 . . . A 99 TYR CA . 18028 1 748 . 1 1 99 99 TYR N N 15 116.256 0.3 . 1 . . . A 99 TYR N . 18028 1 749 . 1 1 100 100 ILE H H 1 9.957 0.020 . 1 . . . A 100 ILE H . 18028 1 750 . 1 1 100 100 ILE HA H 1 4.457 0.020 . 1 . . . A 100 ILE HA . 18028 1 751 . 1 1 100 100 ILE HB H 1 1.731 0.020 . 1 . . . A 100 ILE HB . 18028 1 752 . 1 1 100 100 ILE HG21 H 1 0.751 0.020 . 1 . . . A 100 ILE HG21 . 18028 1 753 . 1 1 100 100 ILE HG22 H 1 0.751 0.020 . 1 . . . A 100 ILE HG22 . 18028 1 754 . 1 1 100 100 ILE HG23 H 1 0.751 0.020 . 1 . . . A 100 ILE HG23 . 18028 1 755 . 1 1 100 100 ILE HD11 H 1 1.197 0.020 . 1 . . . A 100 ILE HD11 . 18028 1 756 . 1 1 100 100 ILE HD12 H 1 1.197 0.020 . 1 . . . A 100 ILE HD12 . 18028 1 757 . 1 1 100 100 ILE HD13 H 1 1.197 0.020 . 1 . . . A 100 ILE HD13 . 18028 1 758 . 1 1 100 100 ILE CA C 13 58.616 0.3 . 1 . . . A 100 ILE CA . 18028 1 759 . 1 1 100 100 ILE N N 15 127.103 0.3 . 1 . . . A 100 ILE N . 18028 1 760 . 1 1 101 101 SER H H 1 8.845 0.020 . 1 . . . A 101 SER H . 18028 1 761 . 1 1 101 101 SER HA H 1 4.711 0.020 . 1 . . . A 101 SER HA . 18028 1 762 . 1 1 101 101 SER HB2 H 1 3.818 0.020 . 1 . . . A 101 SER HB2 . 18028 1 763 . 1 1 101 101 SER HB3 H 1 3.818 0.020 . 1 . . . A 101 SER HB3 . 18028 1 764 . 1 1 101 101 SER CA C 13 52.897 0.3 . 1 . . . A 101 SER CA . 18028 1 765 . 1 1 101 101 SER N N 15 123.768 0.3 . 1 . . . A 101 SER N . 18028 1 766 . 1 1 102 102 ALA H H 1 9.185 0.020 . 1 . . . A 102 ALA H . 18028 1 767 . 1 1 102 102 ALA HA H 1 3.733 0.020 . 1 . . . A 102 ALA HA . 18028 1 768 . 1 1 102 102 ALA HB1 H 1 1.305 0.020 . 1 . . . A 102 ALA HB1 . 18028 1 769 . 1 1 102 102 ALA HB2 H 1 1.305 0.020 . 1 . . . A 102 ALA HB2 . 18028 1 770 . 1 1 102 102 ALA HB3 H 1 1.305 0.020 . 1 . . . A 102 ALA HB3 . 18028 1 771 . 1 1 102 102 ALA CA C 13 53.093 0.3 . 1 . . . A 102 ALA CA . 18028 1 772 . 1 1 102 102 ALA N N 15 122.940 0.3 . 1 . . . A 102 ALA N . 18028 1 773 . 1 1 103 103 ALA H H 1 8.132 0.020 . 1 . . . A 103 ALA H . 18028 1 774 . 1 1 103 103 ALA HA H 1 3.861 0.020 . 1 . . . A 103 ALA HA . 18028 1 775 . 1 1 103 103 ALA HB1 H 1 1.262 0.020 . 1 . . . A 103 ALA HB1 . 18028 1 776 . 1 1 103 103 ALA HB2 H 1 1.262 0.020 . 1 . . . A 103 ALA HB2 . 18028 1 777 . 1 1 103 103 ALA HB3 H 1 1.262 0.020 . 1 . . . A 103 ALA HB3 . 18028 1 778 . 1 1 103 103 ALA CA C 13 52.409 0.3 . 1 . . . A 103 ALA CA . 18028 1 779 . 1 1 103 103 ALA N N 15 118.443 0.3 . 1 . . . A 103 ALA N . 18028 1 780 . 1 1 104 104 GLU H H 1 7.782 0.020 . 1 . . . A 104 GLU H . 18028 1 781 . 1 1 104 104 GLU HA H 1 3.839 0.020 . 1 . . . A 104 GLU HA . 18028 1 782 . 1 1 104 104 GLU HB2 H 1 1.917 0.020 . 1 . . . A 104 GLU HB2 . 18028 1 783 . 1 1 104 104 GLU HB3 H 1 1.917 0.020 . 1 . . . A 104 GLU HB3 . 18028 1 784 . 1 1 104 104 GLU HG2 H 1 2.260 0.020 . 1 . . . A 104 GLU HG2 . 18028 1 785 . 1 1 104 104 GLU HG3 H 1 2.260 0.020 . 1 . . . A 104 GLU HG3 . 18028 1 786 . 1 1 104 104 GLU CA C 13 56.563 0.3 . 1 . . . A 104 GLU CA . 18028 1 787 . 1 1 104 104 GLU N N 15 120.268 0.3 . 1 . . . A 104 GLU N . 18028 1 788 . 1 1 105 105 LEU H H 1 8.231 0.020 . 1 . . . A 105 LEU H . 18028 1 789 . 1 1 105 105 LEU HA H 1 3.962 0.020 . 1 . . . A 105 LEU HA . 18028 1 790 . 1 1 105 105 LEU HB2 H 1 1.743 0.020 . 1 . . . A 105 LEU HB2 . 18028 1 791 . 1 1 105 105 LEU HB3 H 1 1.743 0.020 . 1 . . . A 105 LEU HB3 . 18028 1 792 . 1 1 105 105 LEU HG H 1 1.577 0.020 . 1 . . . A 105 LEU HG . 18028 1 793 . 1 1 105 105 LEU HD11 H 1 0.773 0.020 . 1 . . . A 105 LEU HD11 . 18028 1 794 . 1 1 105 105 LEU HD12 H 1 0.773 0.020 . 1 . . . A 105 LEU HD12 . 18028 1 795 . 1 1 105 105 LEU HD13 H 1 0.773 0.020 . 1 . . . A 105 LEU HD13 . 18028 1 796 . 1 1 105 105 LEU HD21 H 1 1.036 0.020 . 1 . . . A 105 LEU HD21 . 18028 1 797 . 1 1 105 105 LEU HD22 H 1 1.036 0.020 . 1 . . . A 105 LEU HD22 . 18028 1 798 . 1 1 105 105 LEU HD23 H 1 1.036 0.020 . 1 . . . A 105 LEU HD23 . 18028 1 799 . 1 1 105 105 LEU CA C 13 55.732 0.3 . 1 . . . A 105 LEU CA . 18028 1 800 . 1 1 105 105 LEU N N 15 121.501 0.3 . 1 . . . A 105 LEU N . 18028 1 801 . 1 1 106 106 ARG H H 1 8.774 0.020 . 1 . . . A 106 ARG H . 18028 1 802 . 1 1 106 106 ARG HA H 1 3.861 0.020 . 1 . . . A 106 ARG HA . 18028 1 803 . 1 1 106 106 ARG HB2 H 1 1.803 0.020 . 1 . . . A 106 ARG HB2 . 18028 1 804 . 1 1 106 106 ARG HB3 H 1 1.803 0.020 . 1 . . . A 106 ARG HB3 . 18028 1 805 . 1 1 106 106 ARG HG2 H 1 1.452 0.020 . 1 . . . A 106 ARG HG2 . 18028 1 806 . 1 1 106 106 ARG HG3 H 1 1.452 0.020 . 1 . . . A 106 ARG HG3 . 18028 1 807 . 1 1 106 106 ARG HD2 H 1 3.076 0.020 . 1 . . . A 106 ARG HD2 . 18028 1 808 . 1 1 106 106 ARG HD3 H 1 3.076 0.020 . 2 . . . A 106 ARG HD3 . 18028 1 809 . 1 1 106 106 ARG CA C 13 57.345 0.3 . 1 . . . A 106 ARG CA . 18028 1 810 . 1 1 106 106 ARG N N 15 118.625 0.3 . 1 . . . A 106 ARG N . 18028 1 811 . 1 1 107 107 HIS H H 1 7.946 0.020 . 1 . . . A 107 HIS H . 18028 1 812 . 1 1 107 107 HIS HA H 1 3.876 0.020 . 1 . . . A 107 HIS HA . 18028 1 813 . 1 1 107 107 HIS HB2 H 1 1.837 0.020 . 1 . . . A 107 HIS HB2 . 18028 1 814 . 1 1 107 107 HIS HB3 H 1 1.837 0.020 . 1 . . . A 107 HIS HB3 . 18028 1 815 . 1 1 107 107 HIS CA C 13 56.807 0.3 . 1 . . . A 107 HIS CA . 18028 1 816 . 1 1 107 107 HIS N N 15 119.052 0.3 . 1 . . . A 107 HIS N . 18028 1 817 . 1 1 108 108 VAL H H 1 7.713 0.020 . 1 . . . A 108 VAL H . 18028 1 818 . 1 1 108 108 VAL HA H 1 3.442 0.020 . 1 . . . A 108 VAL HA . 18028 1 819 . 1 1 108 108 VAL HB H 1 1.978 0.020 . 1 . . . A 108 VAL HB . 18028 1 820 . 1 1 108 108 VAL HG11 H 1 0.466 0.020 . 1 . . . A 108 VAL HG11 . 18028 1 821 . 1 1 108 108 VAL HG12 H 1 0.466 0.020 . 1 . . . A 108 VAL HG12 . 18028 1 822 . 1 1 108 108 VAL HG13 H 1 0.466 0.020 . 1 . . . A 108 VAL HG13 . 18028 1 823 . 1 1 108 108 VAL HG21 H 1 0.861 0.020 . 1 . . . A 108 VAL HG21 . 18028 1 824 . 1 1 108 108 VAL HG22 H 1 0.861 0.020 . 1 . . . A 108 VAL HG22 . 18028 1 825 . 1 1 108 108 VAL HG23 H 1 0.861 0.020 . 1 . . . A 108 VAL HG23 . 18028 1 826 . 1 1 108 108 VAL CA C 13 64.285 0.3 . 1 . . . A 108 VAL CA . 18028 1 827 . 1 1 108 108 VAL N N 15 119.160 0.3 . 1 . . . A 108 VAL N . 18028 1 828 . 1 1 109 109 MET H H 1 8.130 0.020 . 1 . . . A 109 MET H . 18028 1 829 . 1 1 109 109 MET HA H 1 4.139 0.020 . 1 . . . A 109 MET HA . 18028 1 830 . 1 1 109 109 MET HB2 H 1 1.781 0.020 . 1 . . . A 109 MET HB2 . 18028 1 831 . 1 1 109 109 MET HB3 H 1 1.781 0.020 . 1 . . . A 109 MET HB3 . 18028 1 832 . 1 1 109 109 MET HG2 H 1 2.038 0.020 . 1 . . . A 109 MET HG2 . 18028 1 833 . 1 1 109 109 MET HG3 H 1 2.038 0.020 . 1 . . . A 109 MET HG3 . 18028 1 834 . 1 1 109 109 MET CA C 13 54.461 0.3 . 1 . . . A 109 MET CA . 18028 1 835 . 1 1 109 109 MET N N 15 115.318 0.3 . 1 . . . A 109 MET N . 18028 1 836 . 1 1 110 110 THR H H 1 8.515 0.020 . 1 . . . A 110 THR H . 18028 1 837 . 1 1 110 110 THR HA H 1 3.879 0.020 . 1 . . . A 110 THR HA . 18028 1 838 . 1 1 110 110 THR HB H 1 4.168 0.020 . 1 . . . A 110 THR HB . 18028 1 839 . 1 1 110 110 THR HG21 H 1 1.080 0.020 . 1 . . . A 110 THR HG21 . 18028 1 840 . 1 1 110 110 THR HG22 H 1 1.080 0.020 . 1 . . . A 110 THR HG22 . 18028 1 841 . 1 1 110 110 THR HG23 H 1 1.080 0.020 . 1 . . . A 110 THR HG23 . 18028 1 842 . 1 1 110 110 THR CA C 13 63.845 0.3 . 1 . . . A 110 THR CA . 18028 1 843 . 1 1 110 110 THR N N 15 116.846 0.3 . 1 . . . A 110 THR N . 18028 1 844 . 1 1 111 111 ASN H H 1 7.877 0.020 . 1 . . . A 111 ASN H . 18028 1 845 . 1 1 111 111 ASN HA H 1 4.202 0.020 . 1 . . . A 111 ASN HA . 18028 1 846 . 1 1 111 111 ASN HB2 H 1 2.689 0.020 . 1 . . . A 111 ASN HB2 . 18028 1 847 . 1 1 111 111 ASN HB3 H 1 2.881 0.020 . 2 . . . A 111 ASN HB3 . 18028 1 848 . 1 1 111 111 ASN CA C 13 53.093 0.3 . 1 . . . A 111 ASN CA . 18028 1 849 . 1 1 111 111 ASN N N 15 123.887 0.3 . 1 . . . A 111 ASN N . 18028 1 850 . 1 1 112 112 LEU H H 1 7.672 0.020 . 1 . . . A 112 LEU H . 18028 1 851 . 1 1 112 112 LEU HA H 1 4.124 0.020 . 1 . . . A 112 LEU HA . 18028 1 852 . 1 1 112 112 LEU HB2 H 1 1.671 0.020 . 1 . . . A 112 LEU HB2 . 18028 1 853 . 1 1 112 112 LEU HB3 H 1 1.671 0.020 . 1 . . . A 112 LEU HB3 . 18028 1 854 . 1 1 112 112 LEU HD11 H 1 0.576 0.020 . 1 . . . A 112 LEU HD11 . 18028 1 855 . 1 1 112 112 LEU HD12 H 1 0.576 0.020 . 1 . . . A 112 LEU HD12 . 18028 1 856 . 1 1 112 112 LEU HD13 H 1 0.576 0.020 . 1 . . . A 112 LEU HD13 . 18028 1 857 . 1 1 112 112 LEU HD21 H 1 0.576 0.020 . 1 . . . A 112 LEU HD21 . 18028 1 858 . 1 1 112 112 LEU HD22 H 1 0.576 0.020 . 1 . . . A 112 LEU HD22 . 18028 1 859 . 1 1 112 112 LEU HD23 H 1 0.576 0.020 . 1 . . . A 112 LEU HD23 . 18028 1 860 . 1 1 112 112 LEU CA C 13 52.653 0.3 . 1 . . . A 112 LEU CA . 18028 1 861 . 1 1 112 112 LEU N N 15 118.372 0.3 . 1 . . . A 112 LEU N . 18028 1 862 . 1 1 113 113 GLY H H 1 7.704 0.020 . 1 . . . A 113 GLY H . 18028 1 863 . 1 1 113 113 GLY HA2 H 1 4.124 0.020 . 1 . . . A 113 GLY HA2 . 18028 1 864 . 1 1 113 113 GLY HA3 H 1 4.124 0.020 . 2 . . . A 113 GLY HA3 . 18028 1 865 . 1 1 113 113 GLY CA C 13 42.536 0.3 . 1 . . . A 113 GLY CA . 18028 1 866 . 1 1 113 113 GLY N N 15 106.860 0.3 . 1 . . . A 113 GLY N . 18028 1 867 . 1 1 114 114 GLU H H 1 7.871 0.020 . 1 . . . A 114 GLU H . 18028 1 868 . 1 1 114 114 GLU HA H 1 4.168 0.020 . 1 . . . A 114 GLU HA . 18028 1 869 . 1 1 114 114 GLU HB2 H 1 1.518 0.020 . 1 . . . A 114 GLU HB2 . 18028 1 870 . 1 1 114 114 GLU HB3 H 1 1.518 0.020 . 1 . . . A 114 GLU HB3 . 18028 1 871 . 1 1 114 114 GLU HG2 H 1 1.803 0.020 . 1 . . . A 114 GLU HG2 . 18028 1 872 . 1 1 114 114 GLU HG3 H 1 1.803 0.020 . 1 . . . A 114 GLU HG3 . 18028 1 873 . 1 1 114 114 GLU CA C 13 52.067 0.3 . 1 . . . A 114 GLU CA . 18028 1 874 . 1 1 114 114 GLU N N 15 120.133 0.3 . 1 . . . A 114 GLU N . 18028 1 875 . 1 1 115 115 LYS H H 1 8.494 0.020 . 1 . . . A 115 LYS H . 18028 1 876 . 1 1 115 115 LYS HA H 1 4.223 0.020 . 1 . . . A 115 LYS HA . 18028 1 877 . 1 1 115 115 LYS HB2 H 1 1.773 0.020 . 1 . . . A 115 LYS HB2 . 18028 1 878 . 1 1 115 115 LYS HB3 H 1 1.773 0.020 . 1 . . . A 115 LYS HB3 . 18028 1 879 . 1 1 115 115 LYS HG2 H 1 1.198 0.020 . 1 . . . A 115 LYS HG2 . 18028 1 880 . 1 1 115 115 LYS HG3 H 1 1.198 0.020 . 2 . . . A 115 LYS HG3 . 18028 1 881 . 1 1 115 115 LYS HD2 H 1 1.496 0.020 . 1 . . . A 115 LYS HD2 . 18028 1 882 . 1 1 115 115 LYS HD3 H 1 1.496 0.020 . 1 . . . A 115 LYS HD3 . 18028 1 883 . 1 1 115 115 LYS CA C 13 52.848 0.3 . 1 . . . A 115 LYS CA . 18028 1 884 . 1 1 115 115 LYS N N 15 124.987 0.3 . 1 . . . A 115 LYS N . 18028 1 885 . 1 1 116 116 LEU H H 1 7.978 0.020 . 1 . . . A 116 LEU H . 18028 1 886 . 1 1 116 116 LEU HA H 1 4.244 0.020 . 1 . . . A 116 LEU HA . 18028 1 887 . 1 1 116 116 LEU HB2 H 1 1.518 0.020 . 1 . . . A 116 LEU HB2 . 18028 1 888 . 1 1 116 116 LEU HB3 H 1 1.518 0.020 . 1 . . . A 116 LEU HB3 . 18028 1 889 . 1 1 116 116 LEU HG H 1 1.433 0.020 . 1 . . . A 116 LEU HG . 18028 1 890 . 1 1 116 116 LEU HD11 H 1 0.657 0.020 . 1 . . . A 116 LEU HD11 . 18028 1 891 . 1 1 116 116 LEU HD12 H 1 0.657 0.020 . 1 . . . A 116 LEU HD12 . 18028 1 892 . 1 1 116 116 LEU HD13 H 1 0.657 0.020 . 1 . . . A 116 LEU HD13 . 18028 1 893 . 1 1 116 116 LEU HD21 H 1 0.657 0.020 . 1 . . . A 116 LEU HD21 . 18028 1 894 . 1 1 116 116 LEU HD22 H 1 0.657 0.020 . 1 . . . A 116 LEU HD22 . 18028 1 895 . 1 1 116 116 LEU HD23 H 1 0.657 0.020 . 1 . . . A 116 LEU HD23 . 18028 1 896 . 1 1 116 116 LEU CA C 13 51.089 0.3 . 1 . . . A 116 LEU CA . 18028 1 897 . 1 1 116 116 LEU N N 15 124.868 0.3 . 1 . . . A 116 LEU N . 18028 1 898 . 1 1 117 117 THR H H 1 9.129 0.020 . 1 . . . A 117 THR H . 18028 1 899 . 1 1 117 117 THR HA H 1 4.611 0.020 . 1 . . . A 117 THR HA . 18028 1 900 . 1 1 117 117 THR HB H 1 4.304 0.020 . 1 . . . A 117 THR HB . 18028 1 901 . 1 1 117 117 THR HG21 H 1 0.668 0.020 . 1 . . . A 117 THR HG21 . 18028 1 902 . 1 1 117 117 THR HG22 H 1 0.668 0.020 . 1 . . . A 117 THR HG22 . 18028 1 903 . 1 1 117 117 THR HG23 H 1 0.668 0.020 . 1 . . . A 117 THR HG23 . 18028 1 904 . 1 1 117 117 THR CA C 13 57.834 0.3 . 1 . . . A 117 THR CA . 18028 1 905 . 1 1 117 117 THR N N 15 114.337 0.3 . 1 . . . A 117 THR N . 18028 1 906 . 1 1 118 118 ASP H H 1 8.767 0.020 . 1 . . . A 118 ASP H . 18028 1 907 . 1 1 118 118 ASP HA H 1 4.031 0.020 . 1 . . . A 118 ASP HA . 18028 1 908 . 1 1 118 118 ASP HB2 H 1 2.412 0.020 . 1 . . . A 118 ASP HB2 . 18028 1 909 . 1 1 118 118 ASP HB3 H 1 2.412 0.020 . 2 . . . A 118 ASP HB3 . 18028 1 910 . 1 1 118 118 ASP CA C 13 55.243 0.3 . 1 . . . A 118 ASP CA . 18028 1 911 . 1 1 118 118 ASP N N 15 120.881 0.3 . 1 . . . A 118 ASP N . 18028 1 912 . 1 1 119 119 GLU H H 1 8.521 0.020 . 1 . . . A 119 GLU H . 18028 1 913 . 1 1 119 119 GLU HA H 1 3.927 0.020 . 1 . . . A 119 GLU HA . 18028 1 914 . 1 1 119 119 GLU HB2 H 1 1.837 0.020 . 1 . . . A 119 GLU HB2 . 18028 1 915 . 1 1 119 119 GLU HB3 H 1 1.837 0.020 . 1 . . . A 119 GLU HB3 . 18028 1 916 . 1 1 119 119 GLU HG2 H 1 2.203 0.020 . 1 . . . A 119 GLU HG2 . 18028 1 917 . 1 1 119 119 GLU HG3 H 1 2.203 0.020 . 1 . . . A 119 GLU HG3 . 18028 1 918 . 1 1 119 119 GLU CA C 13 57.149 0.3 . 1 . . . A 119 GLU CA . 18028 1 919 . 1 1 119 119 GLU N N 15 119.298 0.3 . 1 . . . A 119 GLU N . 18028 1 920 . 1 1 120 120 GLU H H 1 7.577 0.020 . 1 . . . A 120 GLU H . 18028 1 921 . 1 1 120 120 GLU HA H 1 3.847 0.020 . 1 . . . A 120 GLU HA . 18028 1 922 . 1 1 120 120 GLU HB2 H 1 2.218 0.020 . 1 . . . A 120 GLU HB2 . 18028 1 923 . 1 1 120 120 GLU HB3 H 1 2.218 0.020 . 1 . . . A 120 GLU HB3 . 18028 1 924 . 1 1 120 120 GLU CA C 13 56.319 0.3 . 1 . . . A 120 GLU CA . 18028 1 925 . 1 1 120 120 GLU N N 15 120.118 0.3 . 1 . . . A 120 GLU N . 18028 1 926 . 1 1 121 121 VAL H H 1 7.852 0.020 . 1 . . . A 121 VAL H . 18028 1 927 . 1 1 121 121 VAL HA H 1 3.423 0.020 . 1 . . . A 121 VAL HA . 18028 1 928 . 1 1 121 121 VAL HB H 1 1.868 0.020 . 1 . . . A 121 VAL HB . 18028 1 929 . 1 1 121 121 VAL HG11 H 1 0.729 0.020 . 1 . . . A 121 VAL HG11 . 18028 1 930 . 1 1 121 121 VAL HG12 H 1 0.729 0.020 . 1 . . . A 121 VAL HG12 . 18028 1 931 . 1 1 121 121 VAL HG13 H 1 0.729 0.020 . 1 . . . A 121 VAL HG13 . 18028 1 932 . 1 1 121 121 VAL HG21 H 1 0.204 0.020 . 1 . . . A 121 VAL HG21 . 18028 1 933 . 1 1 121 121 VAL HG22 H 1 0.204 0.020 . 1 . . . A 121 VAL HG22 . 18028 1 934 . 1 1 121 121 VAL HG23 H 1 0.204 0.020 . 1 . . . A 121 VAL HG23 . 18028 1 935 . 1 1 121 121 VAL CA C 13 64.090 0.3 . 1 . . . A 121 VAL CA . 18028 1 936 . 1 1 121 121 VAL N N 15 122.079 0.3 . 1 . . . A 121 VAL N . 18028 1 937 . 1 1 122 122 ASP H H 1 7.882 0.020 . 1 . . . A 122 ASP H . 18028 1 938 . 1 1 122 122 ASP HA H 1 4.170 0.020 . 1 . . . A 122 ASP HA . 18028 1 939 . 1 1 122 122 ASP HB2 H 1 2.585 0.020 . 1 . . . A 122 ASP HB2 . 18028 1 940 . 1 1 122 122 ASP HB3 H 1 2.585 0.020 . 1 . . . A 122 ASP HB3 . 18028 1 941 . 1 1 122 122 ASP CA C 13 54.901 0.3 . 1 . . . A 122 ASP CA . 18028 1 942 . 1 1 122 122 ASP N N 15 120.225 0.3 . 1 . . . A 122 ASP N . 18028 1 943 . 1 1 123 123 GLU H H 1 7.814 0.020 . 1 . . . A 123 GLU H . 18028 1 944 . 1 1 123 123 GLU HA H 1 3.796 0.020 . 1 . . . A 123 GLU HA . 18028 1 945 . 1 1 123 123 GLU HB2 H 1 1.978 0.020 . 1 . . . A 123 GLU HB2 . 18028 1 946 . 1 1 123 123 GLU HB3 H 1 1.978 0.020 . 1 . . . A 123 GLU HB3 . 18028 1 947 . 1 1 123 123 GLU HG2 H 1 2.175 0.020 . 1 . . . A 123 GLU HG2 . 18028 1 948 . 1 1 123 123 GLU HG3 H 1 2.175 0.020 . 1 . . . A 123 GLU HG3 . 18028 1 949 . 1 1 123 123 GLU CA C 13 56.612 0.3 . 1 . . . A 123 GLU CA . 18028 1 950 . 1 1 123 123 GLU N N 15 119.175 0.3 . 1 . . . A 123 GLU N . 18028 1 951 . 1 1 124 124 MET H H 1 7.431 0.020 . 1 . . . A 124 MET H . 18028 1 952 . 1 1 124 124 MET HA H 1 3.818 0.020 . 1 . . . A 124 MET HA . 18028 1 953 . 1 1 124 124 MET HB2 H 1 1.605 0.020 . 1 . . . A 124 MET HB2 . 18028 1 954 . 1 1 124 124 MET HB3 H 1 1.605 0.020 . 1 . . . A 124 MET HB3 . 18028 1 955 . 1 1 124 124 MET HG2 H 1 2.109 0.020 . 1 . . . A 124 MET HG2 . 18028 1 956 . 1 1 124 124 MET HG3 H 1 2.109 0.020 . 1 . . . A 124 MET HG3 . 18028 1 957 . 1 1 124 124 MET CA C 13 56.905 0.3 . 1 . . . A 124 MET CA . 18028 1 958 . 1 1 124 124 MET N N 15 119.067 0.3 . 1 . . . A 124 MET N . 18028 1 959 . 1 1 125 125 ILE H H 1 7.710 0.020 . 1 . . . A 125 ILE H . 18028 1 960 . 1 1 125 125 ILE HA H 1 3.380 0.020 . 1 . . . A 125 ILE HA . 18028 1 961 . 1 1 125 125 ILE HB H 1 2.087 0.020 . 1 . . . A 125 ILE HB . 18028 1 962 . 1 1 125 125 ILE HG12 H 1 0.554 0.020 . 1 . . . A 125 ILE HG12 . 18028 1 963 . 1 1 125 125 ILE HG13 H 1 0.554 0.020 . 1 . . . A 125 ILE HG13 . 18028 1 964 . 1 1 125 125 ILE HG21 H 1 1.233 0.020 . 1 . . . A 125 ILE HG21 . 18028 1 965 . 1 1 125 125 ILE HG22 H 1 1.233 0.020 . 1 . . . A 125 ILE HG22 . 18028 1 966 . 1 1 125 125 ILE HG23 H 1 1.233 0.020 . 1 . . . A 125 ILE HG23 . 18028 1 967 . 1 1 125 125 ILE HD11 H 1 0.426 0.020 . 1 . . . A 125 ILE HD11 . 18028 1 968 . 1 1 125 125 ILE HD12 H 1 0.426 0.020 . 1 . . . A 125 ILE HD12 . 18028 1 969 . 1 1 125 125 ILE HD13 H 1 0.426 0.020 . 1 . . . A 125 ILE HD13 . 18028 1 970 . 1 1 125 125 ILE CA C 13 60.131 0.3 . 1 . . . A 125 ILE CA . 18028 1 971 . 1 1 125 125 ILE N N 15 118.171 0.3 . 1 . . . A 125 ILE N . 18028 1 972 . 1 1 126 126 ARG H H 1 7.951 0.020 . 1 . . . A 126 ARG H . 18028 1 973 . 1 1 126 126 ARG HA H 1 3.883 0.020 . 1 . . . A 126 ARG HA . 18028 1 974 . 1 1 126 126 ARG HB2 H 1 1.803 0.020 . 1 . . . A 126 ARG HB2 . 18028 1 975 . 1 1 126 126 ARG HB3 H 1 1.803 0.020 . 1 . . . A 126 ARG HB3 . 18028 1 976 . 1 1 126 126 ARG CA C 13 56.673 0.3 . 1 . . . A 126 ARG CA . 18028 1 977 . 1 1 126 126 ARG N N 15 117.910 0.3 . 1 . . . A 126 ARG N . 18028 1 978 . 1 1 127 127 GLU H H 1 7.600 0.020 . 1 . . . A 127 GLU H . 18028 1 979 . 1 1 127 127 GLU HA H 1 3.861 0.020 . 1 . . . A 127 GLU HA . 18028 1 980 . 1 1 127 127 GLU HB2 H 1 1.737 0.020 . 1 . . . A 127 GLU HB2 . 18028 1 981 . 1 1 127 127 GLU HB3 H 1 1.737 0.020 . 1 . . . A 127 GLU HB3 . 18028 1 982 . 1 1 127 127 GLU HG2 H 1 2.175 0.020 . 1 . . . A 127 GLU HG2 . 18028 1 983 . 1 1 127 127 GLU HG3 H 1 2.175 0.020 . 1 . . . A 127 GLU HG3 . 18028 1 984 . 1 1 127 127 GLU CA C 13 56.319 0.3 . 1 . . . A 127 GLU CA . 18028 1 985 . 1 1 127 127 GLU N N 15 117.507 0.3 . 1 . . . A 127 GLU N . 18028 1 986 . 1 1 128 128 ALA H H 1 7.171 0.020 . 1 . . . A 128 ALA H . 18028 1 987 . 1 1 128 128 ALA HA H 1 4.500 0.020 . 1 . . . A 128 ALA HA . 18028 1 988 . 1 1 128 128 ALA HB1 H 1 1.337 0.020 . 1 . . . A 128 ALA HB1 . 18028 1 989 . 1 1 128 128 ALA HB2 H 1 1.337 0.020 . 1 . . . A 128 ALA HB2 . 18028 1 990 . 1 1 128 128 ALA HB3 H 1 1.337 0.020 . 1 . . . A 128 ALA HB3 . 18028 1 991 . 1 1 128 128 ALA CA C 13 48.205 0.3 . 1 . . . A 128 ALA CA . 18028 1 992 . 1 1 128 128 ALA N N 15 116.595 0.3 . 1 . . . A 128 ALA N . 18028 1 993 . 1 1 129 129 ASP H H 1 7.830 0.020 . 1 . . . A 129 ASP H . 18028 1 994 . 1 1 129 129 ASP HA H 1 4.351 0.020 . 1 . . . A 129 ASP HA . 18028 1 995 . 1 1 129 129 ASP HB2 H 1 2.219 0.020 . 1 . . . A 129 ASP HB2 . 18028 1 996 . 1 1 129 129 ASP HB3 H 1 2.219 0.020 . 1 . . . A 129 ASP HB3 . 18028 1 997 . 1 1 129 129 ASP CA C 13 51.822 0.3 . 1 . . . A 129 ASP CA . 18028 1 998 . 1 1 129 129 ASP N N 15 118.048 0.3 . 1 . . . A 129 ASP N . 18028 1 999 . 1 1 130 130 ILE H H 1 8.140 0.020 . 1 . . . A 130 ILE H . 18028 1 1000 . 1 1 130 130 ILE HA H 1 3.797 0.020 . 1 . . . A 130 ILE HA . 18028 1 1001 . 1 1 130 130 ILE HB H 1 1.837 0.020 . 1 . . . A 130 ILE HB . 18028 1 1002 . 1 1 130 130 ILE HG12 H 1 0.751 0.020 . 1 . . . A 130 ILE HG12 . 18028 1 1003 . 1 1 130 130 ILE HG13 H 1 0.751 0.020 . 1 . . . A 130 ILE HG13 . 18028 1 1004 . 1 1 130 130 ILE HG21 H 1 1.518 0.020 . 1 . . . A 130 ILE HG21 . 18028 1 1005 . 1 1 130 130 ILE HG22 H 1 1.518 0.020 . 1 . . . A 130 ILE HG22 . 18028 1 1006 . 1 1 130 130 ILE HG23 H 1 1.518 0.020 . 1 . . . A 130 ILE HG23 . 18028 1 1007 . 1 1 130 130 ILE HD11 H 1 0.708 0.020 . 1 . . . A 130 ILE HD11 . 18028 1 1008 . 1 1 130 130 ILE HD12 H 1 0.708 0.020 . 1 . . . A 130 ILE HD12 . 18028 1 1009 . 1 1 130 130 ILE HD13 H 1 0.708 0.020 . 1 . . . A 130 ILE HD13 . 18028 1 1010 . 1 1 130 130 ILE CA C 13 60.522 0.3 . 1 . . . A 130 ILE CA . 18028 1 1011 . 1 1 130 130 ILE N N 15 128.000 0.3 . 1 . . . A 130 ILE N . 18028 1 1012 . 1 1 131 131 ASP H H 1 8.188 0.020 . 1 . . . A 131 ASP H . 18028 1 1013 . 1 1 131 131 ASP HA H 1 4.343 0.020 . 1 . . . A 131 ASP HA . 18028 1 1014 . 1 1 131 131 ASP HB2 H 1 2.197 0.020 . 1 . . . A 131 ASP HB2 . 18028 1 1015 . 1 1 131 131 ASP HB3 H 1 2.197 0.020 . 1 . . . A 131 ASP HB3 . 18028 1 1016 . 1 1 131 131 ASP CA C 13 51.187 0.3 . 1 . . . A 131 ASP CA . 18028 1 1017 . 1 1 131 131 ASP N N 15 116.678 0.3 . 1 . . . A 131 ASP N . 18028 1 1018 . 1 1 132 132 GLY H H 1 7.551 0.020 . 1 . . . A 132 GLY H . 18028 1 1019 . 1 1 132 132 GLY HA2 H 1 3.690 0.020 . 1 . . . A 132 GLY HA2 . 18028 1 1020 . 1 1 132 132 GLY HA3 H 1 3.690 0.020 . 1 . . . A 132 GLY HA3 . 18028 1 1021 . 1 1 132 132 GLY CA C 13 44.638 0.3 . 1 . . . A 132 GLY CA . 18028 1 1022 . 1 1 132 132 GLY N N 15 108.469 0.3 . 1 . . . A 132 GLY N . 18028 1 1023 . 1 1 133 133 ASP H H 1 8.211 0.020 . 1 . . . A 133 ASP H . 18028 1 1024 . 1 1 133 133 ASP HA H 1 4.329 0.020 . 1 . . . A 133 ASP HA . 18028 1 1025 . 1 1 133 133 ASP HB2 H 1 2.838 0.020 . 1 . . . A 133 ASP HB2 . 18028 1 1026 . 1 1 133 133 ASP HB3 H 1 2.838 0.020 . 1 . . . A 133 ASP HB3 . 18028 1 1027 . 1 1 133 133 ASP CA C 13 50.942 0.3 . 1 . . . A 133 ASP CA . 18028 1 1028 . 1 1 133 133 ASP N N 15 120.377 0.3 . 1 . . . A 133 ASP N . 18028 1 1029 . 1 1 134 134 GLY H H 1 9.933 0.020 . 1 . . . A 134 GLY H . 18028 1 1030 . 1 1 134 134 GLY HA2 H 1 3.253 0.020 . 1 . . . A 134 GLY HA2 . 18028 1 1031 . 1 1 134 134 GLY HA3 H 1 3.253 0.020 . 2 . . . A 134 GLY HA3 . 18028 1 1032 . 1 1 134 134 GLY CA C 13 43.122 0.3 . 1 . . . A 134 GLY CA . 18028 1 1033 . 1 1 134 134 GLY N N 15 112.182 0.3 . 1 . . . A 134 GLY N . 18028 1 1034 . 1 1 135 135 GLN H H 1 7.840 0.020 . 1 . . . A 135 GLN H . 18028 1 1035 . 1 1 135 135 GLN HA H 1 4.844 0.020 . 1 . . . A 135 GLN HA . 18028 1 1036 . 1 1 135 135 GLN HB2 H 1 1.617 0.020 . 1 . . . A 135 GLN HB2 . 18028 1 1037 . 1 1 135 135 GLN HB3 H 1 1.617 0.020 . 1 . . . A 135 GLN HB3 . 18028 1 1038 . 1 1 135 135 GLN HG2 H 1 1.808 0.020 . 1 . . . A 135 GLN HG2 . 18028 1 1039 . 1 1 135 135 GLN HG3 H 1 1.808 0.020 . 1 . . . A 135 GLN HG3 . 18028 1 1040 . 1 1 135 135 GLN CA C 13 50.454 0.3 . 1 . . . A 135 GLN CA . 18028 1 1041 . 1 1 135 135 GLN N N 15 115.288 0.3 . 1 . . . A 135 GLN N . 18028 1 1042 . 1 1 136 136 VAL H H 1 8.977 0.020 . 1 . . . A 136 VAL H . 18028 1 1043 . 1 1 136 136 VAL HA H 1 5.139 0.020 . 1 . . . A 136 VAL HA . 18028 1 1044 . 1 1 136 136 VAL HB H 1 2.168 0.020 . 1 . . . A 136 VAL HB . 18028 1 1045 . 1 1 136 136 VAL HG11 H 1 0.948 0.020 . 1 . . . A 136 VAL HG11 . 18028 1 1046 . 1 1 136 136 VAL HG12 H 1 0.948 0.020 . 1 . . . A 136 VAL HG12 . 18028 1 1047 . 1 1 136 136 VAL HG13 H 1 0.948 0.020 . 1 . . . A 136 VAL HG13 . 18028 1 1048 . 1 1 136 136 VAL HG21 H 1 0.358 0.020 . 1 . . . A 136 VAL HG21 . 18028 1 1049 . 1 1 136 136 VAL HG22 H 1 0.358 0.020 . 1 . . . A 136 VAL HG22 . 18028 1 1050 . 1 1 136 136 VAL HG23 H 1 0.358 0.020 . 1 . . . A 136 VAL HG23 . 18028 1 1051 . 1 1 136 136 VAL CA C 13 58.713 0.3 . 1 . . . A 136 VAL CA . 18028 1 1052 . 1 1 136 136 VAL N N 15 125.238 0.3 . 1 . . . A 136 VAL N . 18028 1 1053 . 1 1 137 137 ASN H H 1 9.391 0.020 . 1 . . . A 137 ASN H . 18028 1 1054 . 1 1 137 137 ASN HA H 1 5.156 0.020 . 1 . . . A 137 ASN HA . 18028 1 1055 . 1 1 137 137 ASN HB2 H 1 2.829 0.020 . 1 . . . A 137 ASN HB2 . 18028 1 1056 . 1 1 137 137 ASN HB3 H 1 2.829 0.020 . 1 . . . A 137 ASN HB3 . 18028 1 1057 . 1 1 137 137 ASN CA C 13 48.352 0.3 . 1 . . . A 137 ASN CA . 18028 1 1058 . 1 1 137 137 ASN N N 15 129.014 0.3 . 1 . . . A 137 ASN N . 18028 1 1059 . 1 1 138 138 TYR H H 1 8.153 0.020 . 1 . . . A 138 TYR H . 18028 1 1060 . 1 1 138 138 TYR HA H 1 4.277 0.020 . 1 . . . A 138 TYR HA . 18028 1 1061 . 1 1 138 138 TYR HB2 H 1 3.160 0.020 . 1 . . . A 138 TYR HB2 . 18028 1 1062 . 1 1 138 138 TYR HB3 H 1 3.160 0.020 . 1 . . . A 138 TYR HB3 . 18028 1 1063 . 1 1 138 138 TYR HD1 H 1 6.865 0.020 . 1 . . . A 138 TYR HD1 . 18028 1 1064 . 1 1 138 138 TYR HD2 H 1 6.865 0.020 . 1 . . . A 138 TYR HD2 . 18028 1 1065 . 1 1 138 138 TYR CA C 13 59.669 0.3 . 1 . . . A 138 TYR CA . 18028 1 1066 . 1 1 138 138 TYR N N 15 118.562 0.3 . 1 . . . A 138 TYR N . 18028 1 1067 . 1 1 139 139 GLU H H 1 7.985 0.020 . 1 . . . A 139 GLU H . 18028 1 1068 . 1 1 139 139 GLU HA H 1 3.511 0.020 . 1 . . . A 139 GLU HA . 18028 1 1069 . 1 1 139 139 GLU HB2 H 1 1.890 0.020 . 1 . . . A 139 GLU HB2 . 18028 1 1070 . 1 1 139 139 GLU HB3 H 1 1.890 0.020 . 1 . . . A 139 GLU HB3 . 18028 1 1071 . 1 1 139 139 GLU HG2 H 1 2.219 0.020 . 1 . . . A 139 GLU HG2 . 18028 1 1072 . 1 1 139 139 GLU HG3 H 1 2.219 0.020 . 1 . . . A 139 GLU HG3 . 18028 1 1073 . 1 1 139 139 GLU CA C 13 57.540 0.3 . 1 . . . A 139 GLU CA . 18028 1 1074 . 1 1 139 139 GLU N N 15 118.555 0.3 . 1 . . . A 139 GLU N . 18028 1 1075 . 1 1 140 140 GLU H H 1 8.665 0.020 . 1 . . . A 140 GLU H . 18028 1 1076 . 1 1 140 140 GLU HA H 1 3.774 0.020 . 1 . . . A 140 GLU HA . 18028 1 1077 . 1 1 140 140 GLU HB2 H 1 1.846 0.020 . 1 . . . A 140 GLU HB2 . 18028 1 1078 . 1 1 140 140 GLU HB3 H 1 1.846 0.020 . 1 . . . A 140 GLU HB3 . 18028 1 1079 . 1 1 140 140 GLU HG2 H 1 2.197 0.020 . 1 . . . A 140 GLU HG2 . 18028 1 1080 . 1 1 140 140 GLU HG3 H 1 2.197 0.020 . 1 . . . A 140 GLU HG3 . 18028 1 1081 . 1 1 140 140 GLU CA C 13 56.025 0.3 . 1 . . . A 140 GLU CA . 18028 1 1082 . 1 1 140 140 GLU N N 15 119.774 0.3 . 1 . . . A 140 GLU N . 18028 1 1083 . 1 1 141 141 PHE H H 1 8.520 0.020 . 1 . . . A 141 PHE H . 18028 1 1084 . 1 1 141 141 PHE HA H 1 3.627 0.020 . 1 . . . A 141 PHE HA . 18028 1 1085 . 1 1 141 141 PHE HB2 H 1 3.147 0.020 . 1 . . . A 141 PHE HB2 . 18028 1 1086 . 1 1 141 141 PHE HB3 H 1 2.945 0.020 . 2 . . . A 141 PHE HB3 . 18028 1 1087 . 1 1 141 141 PHE HD1 H 1 6.630 0.020 . 1 . . . A 141 PHE HD1 . 18028 1 1088 . 1 1 141 141 PHE HD2 H 1 6.630 0.020 . 1 . . . A 141 PHE HD2 . 18028 1 1089 . 1 1 141 141 PHE HE1 H 1 6.990 0.020 . 1 . . . A 141 PHE HE1 . 18028 1 1090 . 1 1 141 141 PHE HE2 H 1 6.990 0.020 . 1 . . . A 141 PHE HE2 . 18028 1 1091 . 1 1 141 141 PHE HZ H 1 6.390 0.020 . 1 . . . A 141 PHE HZ . 18028 1 1092 . 1 1 141 141 PHE CA C 13 59.447 0.3 . 1 . . . A 141 PHE CA . 18028 1 1093 . 1 1 141 141 PHE N N 15 124.147 0.3 . 1 . . . A 141 PHE N . 18028 1 1094 . 1 1 142 142 VAL H H 1 8.642 0.020 . 1 . . . A 142 VAL H . 18028 1 1095 . 1 1 142 142 VAL HA H 1 2.947 0.020 . 1 . . . A 142 VAL HA . 18028 1 1096 . 1 1 142 142 VAL HG11 H 1 0.576 0.020 . 1 . . . A 142 VAL HG11 . 18028 1 1097 . 1 1 142 142 VAL HG12 H 1 0.576 0.020 . 1 . . . A 142 VAL HG12 . 18028 1 1098 . 1 1 142 142 VAL HG13 H 1 0.576 0.020 . 1 . . . A 142 VAL HG13 . 18028 1 1099 . 1 1 142 142 VAL HG21 H 1 0.291 0.020 . 1 . . . A 142 VAL HG21 . 18028 1 1100 . 1 1 142 142 VAL HG22 H 1 0.291 0.020 . 1 . . . A 142 VAL HG22 . 18028 1 1101 . 1 1 142 142 VAL HG23 H 1 0.291 0.020 . 1 . . . A 142 VAL HG23 . 18028 1 1102 . 1 1 142 142 VAL CA C 13 64.432 0.3 . 1 . . . A 142 VAL CA . 18028 1 1103 . 1 1 142 142 VAL N N 15 119.144 0.3 . 1 . . . A 142 VAL N . 18028 1 1104 . 1 1 143 143 GLN H H 1 7.795 0.020 . 1 . . . A 143 GLN H . 18028 1 1105 . 1 1 143 143 GLN HA H 1 3.726 0.020 . 1 . . . A 143 GLN HA . 18028 1 1106 . 1 1 143 143 GLN HB2 H 1 1.912 0.020 . 1 . . . A 143 GLN HB2 . 18028 1 1107 . 1 1 143 143 GLN HB3 H 1 1.912 0.020 . 1 . . . A 143 GLN HB3 . 18028 1 1108 . 1 1 143 143 GLN HG2 H 1 2.219 0.020 . 1 . . . A 143 GLN HG2 . 18028 1 1109 . 1 1 143 143 GLN HG3 H 1 2.219 0.020 . 1 . . . A 143 GLN HG3 . 18028 1 1110 . 1 1 143 143 GLN CA C 13 56.514 0.3 . 1 . . . A 143 GLN CA . 18028 1 1111 . 1 1 143 143 GLN N N 15 120.173 0.3 . 1 . . . A 143 GLN N . 18028 1 1112 . 1 1 144 144 MET H H 1 7.401 0.020 . 1 . . . A 144 MET H . 18028 1 1113 . 1 1 144 144 MET HA H 1 3.832 0.020 . 1 . . . A 144 MET HA . 18028 1 1114 . 1 1 144 144 MET HB2 H 1 1.781 0.020 . 1 . . . A 144 MET HB2 . 18028 1 1115 . 1 1 144 144 MET HB3 H 1 1.781 0.020 . 1 . . . A 144 MET HB3 . 18028 1 1116 . 1 1 144 144 MET HG2 H 1 1.781 0.020 . 1 . . . A 144 MET HG2 . 18028 1 1117 . 1 1 144 144 MET HG3 H 1 1.781 0.020 . 1 . . . A 144 MET HG3 . 18028 1 1118 . 1 1 144 144 MET CA C 13 55.683 0.3 . 1 . . . A 144 MET CA . 18028 1 1119 . 1 1 144 144 MET N N 15 118.573 0.3 . 1 . . . A 144 MET N . 18028 1 1120 . 1 1 145 145 MET H H 1 7.531 0.020 . 1 . . . A 145 MET H . 18028 1 1121 . 1 1 145 145 MET HA H 1 3.905 0.020 . 1 . . . A 145 MET HA . 18028 1 1122 . 1 1 145 145 MET HB2 H 1 1.672 0.020 . 1 . . . A 145 MET HB2 . 18028 1 1123 . 1 1 145 145 MET HB3 H 1 1.672 0.020 . 1 . . . A 145 MET HB3 . 18028 1 1124 . 1 1 145 145 MET HG2 H 1 1.672 0.020 . 1 . . . A 145 MET HG2 . 18028 1 1125 . 1 1 145 145 MET HG3 H 1 1.672 0.020 . 1 . . . A 145 MET HG3 . 18028 1 1126 . 1 1 145 145 MET CA C 13 53.630 0.3 . 1 . . . A 145 MET CA . 18028 1 1127 . 1 1 145 145 MET N N 15 114.177 0.3 . 1 . . . A 145 MET N . 18028 1 1128 . 1 1 146 146 THR H H 1 7.587 0.020 . 1 . . . A 146 THR H . 18028 1 1129 . 1 1 146 146 THR HA H 1 4.587 0.020 . 1 . . . A 146 THR HA . 18028 1 1130 . 1 1 146 146 THR HB H 1 4.103 0.020 . 1 . . . A 146 THR HB . 18028 1 1131 . 1 1 146 146 THR HG21 H 1 0.964 0.020 . 1 . . . A 146 THR HG21 . 18028 1 1132 . 1 1 146 146 THR HG22 H 1 0.964 0.020 . 1 . . . A 146 THR HG22 . 18028 1 1133 . 1 1 146 146 THR HG23 H 1 0.964 0.020 . 1 . . . A 146 THR HG23 . 18028 1 1134 . 1 1 146 146 THR CA C 13 59.251 0.3 . 1 . . . A 146 THR CA . 18028 1 1135 . 1 1 146 146 THR N N 15 109.158 0.3 . 1 . . . A 146 THR N . 18028 1 1136 . 1 1 147 147 ALA H H 1 7.381 0.020 . 1 . . . A 147 ALA H . 18028 1 1137 . 1 1 147 147 ALA HA H 1 4.095 0.020 . 1 . . . A 147 ALA HA . 18028 1 1138 . 1 1 147 147 ALA HB1 H 1 1.241 0.020 . 1 . . . A 147 ALA HB1 . 18028 1 1139 . 1 1 147 147 ALA HB2 H 1 1.241 0.020 . 1 . . . A 147 ALA HB2 . 18028 1 1140 . 1 1 147 147 ALA HB3 H 1 1.241 0.020 . 1 . . . A 147 ALA HB3 . 18028 1 1141 . 1 1 147 147 ALA CA C 13 50.307 0.3 . 1 . . . A 147 ALA CA . 18028 1 1142 . 1 1 147 147 ALA N N 15 126.868 0.3 . 1 . . . A 147 ALA N . 18028 1 1143 . 1 1 148 148 LYS H H 1 7.854 0.020 . 1 . . . A 148 LYS H . 18028 1 1144 . 1 1 148 148 LYS HA H 1 4.080 0.020 . 1 . . . A 148 LYS HA . 18028 1 1145 . 1 1 148 148 LYS HB2 H 1 1.560 0.020 . 1 . . . A 148 LYS HB2 . 18028 1 1146 . 1 1 148 148 LYS HB3 H 1 1.560 0.020 . 1 . . . A 148 LYS HB3 . 18028 1 1147 . 1 1 148 148 LYS HG2 H 1 1.220 0.020 . 1 . . . A 148 LYS HG2 . 18028 1 1148 . 1 1 148 148 LYS HG3 H 1 1.220 0.020 . 1 . . . A 148 LYS HG3 . 18028 1 1149 . 1 1 148 148 LYS CA C 13 54.803 0.3 . 1 . . . A 148 LYS CA . 18028 1 1150 . 1 1 148 148 LYS N N 15 126.436 0.3 . 1 . . . A 148 LYS N . 18028 1 stop_ save_