data_5227 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5227 _Entry.Title ; Dissection of the Pathway of Molecular Recognition by Calmodulin ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2001-12-10 _Entry.Accession_date 2001-12-10 _Entry.Last_release_date 2002-06-13 _Entry.Original_release_date 2002-06-13 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 James Kranz . K. . 5227 2 Peter Flynn . F. . 5227 3 Ernesto Fuentes . J. . 5227 4 A. Wand . Joshua . 5227 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5227 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 135 5227 '13C chemical shifts' 87 5227 '15N chemical shifts' 25 5227 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 . . 2002-06-13 2001-12-10 original author . 5227 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 5286 'CaM:CaMKIp(299-320) complex' 5227 BMRB 5287 'CaM:CaMKI(1-320) complex' 5227 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5227 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 21840684 _Citation.DOI . _Citation.PubMed_ID 11851407 _Citation.Full_citation . _Citation.Title 'Dissection of the Pathway of Molecular Recognition by Calmodulin' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 41 _Citation.Journal_issue 8 _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 2599 _Citation.Page_last 2608 _Citation.Year 2002 _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 James Kranz . K. . 5227 1 2 Peter Flynn . F. . 5227 1 3 Ernesto Fuentes . J. . 5227 1 4 A. Wand . Joshua . 5227 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_smMLCK_CaM _Assembly.Sf_category assembly _Assembly.Sf_framecode system_smMLCK_CaM _Assembly.Entry_ID 5227 _Assembly.ID 1 _Assembly.Name 'smMLCK:CaM complex' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'not present' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID complex 5227 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'smMLCKp peptide' 1 $smMLCKp . . . native . . . . . 5227 1 2 calmodulin 2 $CaM . . . native . . . . . 5227 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'smMLCK:CaM complex' system 5227 1 CaM abbreviation 5227 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_smMLCKp _Entity.Sf_category entity _Entity.Sf_framecode smMLCKp _Entity.Entry_ID 5227 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Calmodulin recognition element from smooth muscle myosin light chain kinase' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; GSARRKWQKTGHAVRAIGRL S ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 21 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 2336 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 15183 . calmodulin . . . . . 100.00 149 98.65 100.00 2.21e-99 . . . . 5227 1 2 no BMRB 15184 . calmodulin . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 3 no BMRB 15185 . calmodulin . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 4 no BMRB 15186 . calmodulin . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 5 no BMRB 15187 . calmodulin . . . . . 100.00 149 98.65 100.00 2.21e-99 . . . . 5227 1 6 no BMRB 15188 . calmodulin . . . . . 100.00 148 99.32 100.00 6.65e-100 . . . . 5227 1 7 no BMRB 15191 . Calmodulin . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 8 no BMRB 15470 . calmodulin . . . . . 100.00 148 99.32 100.00 1.37e-99 . . . . 5227 1 9 no BMRB 15624 . Calmodulin . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 10 no BMRB 15650 . calmodulin . . . . . 100.00 148 99.32 100.00 2.26e-99 . . . . 5227 1 11 no BMRB 15852 . calmodulin . . . . . 100.00 148 99.32 100.00 2.26e-99 . . . . 5227 1 12 no BMRB 1634 . calmodulin . . . . . 100.00 148 97.30 99.32 1.73e-97 . . . . 5227 1 13 no BMRB 16418 . apoCaM . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 14 no BMRB 16465 . entity_1 . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 15 no BMRB 1648 . calmodulin . . . . . 100.00 148 97.30 99.32 1.73e-97 . . . . 5227 1 16 no BMRB 16764 . CALMODULIN . . . . . 100.00 150 100.00 100.00 3.57e-100 . . . . 5227 1 17 no BMRB 17264 . calmodulin . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 18 no BMRB 17360 . entity_1 . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 19 no BMRB 17771 . Calmodulin . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 20 no BMRB 17807 . Calmodulin . . . . . 99.32 147 100.00 100.00 1.74e-99 . . . . 5227 1 21 no BMRB 18027 . CaM . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 22 no BMRB 18028 . CaM . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 23 no BMRB 18556 . Calmodulin . . . . . 100.00 148 98.65 99.32 1.80e-98 . . . . 5227 1 24 no BMRB 19036 . calmodulin . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 25 no BMRB 19238 . Calmodulin_prototypical_calcium_sensor . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 26 no BMRB 19586 . entity_1 . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 27 no BMRB 19604 . calmodulin . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 28 no BMRB 26503 . Calmodulin . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 29 no BMRB 4056 . calmodulin . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 30 no BMRB 547 . calmodulin . . . . . 100.00 148 97.30 99.32 1.73e-97 . . . . 5227 1 31 no BMRB 6541 . calmodulin . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 32 no BMRB 6778 . calmodulin . . . . . 100.00 148 97.30 99.32 1.73e-97 . . . . 5227 1 33 no BMRB 6798 . calmodulin . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 34 no BMRB 6802 . calmodulin . . . . . 100.00 148 98.65 99.32 2.39e-98 . . . . 5227 1 35 no BMRB 6825 . calmodulin . . . . . 100.00 148 98.65 99.32 2.39e-98 . . . . 5227 1 36 no BMRB 6830 . calmodulin . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 37 no BMRB 6831 . calmodulin . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 38 no BMRB 7018 . calmodulin . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 39 no BMRB 7028 . calmodulin . . . . . 100.00 148 98.65 99.32 2.39e-98 . . . . 5227 1 40 no BMRB 7029 . calmodulin . . . . . 100.00 148 98.65 99.32 2.39e-98 . . . . 5227 1 41 no BMRB 7030 . calmodulin . . . . . 100.00 148 98.65 99.32 2.39e-98 . . . . 5227 1 42 no BMRB 7031 . calmodulin . . . . . 100.00 148 98.65 99.32 2.39e-98 . . . . 5227 1 43 no BMRB 7416 . calmodulin . . . . . 100.00 148 99.32 100.00 2.26e-99 . . . . 5227 1 44 no BMRB 7417 . calmodulin . . . . . 100.00 148 99.32 100.00 2.26e-99 . . . . 5227 1 45 no BMRB 7418 . calmodulin . . . . . 100.00 148 99.32 100.00 2.26e-99 . . . . 5227 1 46 no BMRB 7423 . calmodulin . . . . . 100.00 148 99.32 100.00 2.26e-99 . . . . 5227 1 47 no BMRB 7424 . calmodulin . . . . . 100.00 148 99.32 100.00 2.26e-99 . . . . 5227 1 48 no BMRB 7425 . calmodulin . . . . . 100.00 148 99.32 100.00 2.26e-99 . . . . 5227 1 49 no PDB 1A29 . "Calmodulin Complexed With Trifluoperazine (1:2 Complex)" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 50 no PDB 1CFC . "Calcium-Free Calmodulin" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 51 no PDB 1CFD . "Calcium-Free Calmodulin" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 52 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 3.34e-100 . . . . 5227 1 53 no PDB 1CKK . "CalmodulinRAT CA2+CALMODULIN DEPENDENT PROTEIN KINASE Fragment" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 54 no PDB 1CLL . "Calmodulin Structure Refined At 1.7 Angstroms Resolution" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 55 no PDB 1CM1 . "Motions Of Calmodulin-Single-Conformer Refinement" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 56 no PDB 1CM4 . "Motions Of Calmodulin-four-conformer Refinement" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 57 no PDB 1CTR . "Drug Binding By Calmodulin: Crystal Structure Of A Calmodulin-Trifluoperazine Complex" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 58 no PDB 1DMO . "Calmodulin, Nmr, 30 Structures" . . . . . 100.00 148 99.32 100.00 1.37e-99 . . . . 5227 1 59 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 3.34e-100 . . . . 5227 1 60 no PDB 1IQ5 . "CalmodulinNEMATODE CA2+CALMODULIN DEPENDENT KINASE KINASE Fragment" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 61 no PDB 1IWQ . "Crystal Structure Of Marcks Calmodulin Binding Domain Peptide Complexed With Ca2+CALMODULIN" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 62 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 3.34e-100 . . . . 5227 1 63 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 3.01e-97 . . . . 5227 1 64 no PDB 1L7Z . "Crystal Structure Of Ca2+/calmodulin Complexed With Myristoylated Cap-23/nap-22 Peptide" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 65 no PDB 1LIN . "Calmodulin Complexed With Trifluoperazine (1:4 Complex)" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 66 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 3.49e-100 . . . . 5227 1 67 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 3.34e-100 . . . . 5227 1 68 no PDB 1MXE . "Structure Of The Complex Of Calmodulin With The Target Sequence Of Camki" . . . . . 100.00 148 97.97 99.32 4.61e-98 . . . . 5227 1 69 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 3.34e-100 . . . . 5227 1 70 no PDB 1OOJ . "Structural Genomics Of Caenorhabditis Elegans : Calmodulin" . . . . . 100.00 149 97.97 98.65 8.69e-98 . . . . 5227 1 71 no PDB 1PRW . "Crystal Structure Of Bovine Brain Ca++ Calmodulin In A Compact Form" . . . . . 100.00 149 99.32 99.32 2.91e-99 . . . . 5227 1 72 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 3.34e-100 . . . . 5227 1 73 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 3.34e-100 . . . . 5227 1 74 no PDB 1QX5 . "Crystal Structure Of Apocalmodulin" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 75 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 3.34e-100 . . . . 5227 1 76 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 3.34e-100 . . . . 5227 1 77 no PDB 1SY9 . "Structure Of Calmodulin Complexed With A Fragment Of The Olfactory Cng Channel" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 78 no PDB 1UP5 . "Chicken Calmodulin" . . . . . 100.00 148 99.32 99.32 2.81e-99 . . . . 5227 1 79 no PDB 1WRZ . "Calmodulin Complexed With A Peptide From A Human Death-Associated Protein Kinase" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 80 no PDB 1X02 . "Solution Structure Of Stereo Array Isotope Labeled (Sail) Calmodulin" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 81 no PDB 1XA5 . "Structure Of Calmodulin In Complex With Kar-2, A Bis-Indol Alkaloid" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 82 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 8.28e-100 . . . . 5227 1 83 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 8.28e-100 . . . . 5227 1 84 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 8.28e-100 . . . . 5227 1 85 no PDB 1XFY . "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin" . . . . . 100.00 149 99.32 100.00 8.28e-100 . . . . 5227 1 86 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 8.28e-100 . . . . 5227 1 87 no PDB 1Y0V . "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And Pyrophosphate" . . . . . 97.30 146 100.00 100.00 2.59e-97 . . . . 5227 1 88 no PDB 1YR5 . "1.7-A Structure Of Calmodulin Bound To A Peptide From Dap Kinase" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 89 no PDB 2BBM . "Solution Structure Of A Calmodulin-Target Peptide Complex By Multidimensional Nmr" . . . . . 100.00 148 97.97 99.32 4.61e-98 . . . . 5227 1 90 no PDB 2BBN . "Solution Structure Of A Calmodulin-Target Peptide Complex By Multidimensional Nmr" . . . . . 100.00 148 97.97 99.32 4.61e-98 . . . . 5227 1 91 no PDB 2BCX . "Crystal Structure Of Calmodulin In Complex With A Ryanodine Receptor Peptide" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 92 no PDB 2BKH . "Myosin Vi Nucleotide-Free (Mdinsert2) Crystal Structure" . . . . . 100.00 149 97.97 99.32 3.51e-98 . . . . 5227 1 93 no PDB 2BKI . "Myosin Vi Nucleotide-Free (Mdinsert2-Iq) Crystal Structure" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 94 no PDB 2DFS . "3-D Structure Of Myosin-V Inhibited State" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 95 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 5.38e-100 . . . . 5227 1 96 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 5.38e-100 . . . . 5227 1 97 no PDB 2F3Y . "CalmodulinIQ DOMAIN COMPLEX" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 98 no PDB 2F3Z . "CalmodulinIQ-Aa Domain Complex" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 99 no PDB 2FOT . "Crystal Structure Of The Complex Between Calmodulin And Alphaii-Spectrin" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 100 no PDB 2HQW . "Crystal Structure Of Ca2+CALMODULIN BOUND TO NMDA RECEPTOR NR1C1 Peptide" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 101 no PDB 2JZI . "Structure Of Calmodulin Complexed With The Calmodulin Binding Domain Of Calcineurin" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 102 no PDB 2K0E . "A Coupled Equilibrium Shift Mechanism In Calmodulin- Mediated Signal Transduction" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 103 no PDB 2K0F . "Calmodulin Complexed With Calmodulin-Binding Peptide From Smooth Muscle Myosin Light Chain Kinase" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 104 no PDB 2K0J . "Solution Structure Of Cam Complexed To Drp1p" . . . . . 100.00 148 99.32 100.00 2.26e-99 . . . . 5227 1 105 no PDB 2K61 . "Solution Structure Of Cam Complexed To Dapk Peptide" . . . . . 100.00 148 99.32 100.00 2.26e-99 . . . . 5227 1 106 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 3.34e-100 . . . . 5227 1 107 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 3.34e-100 . . . . 5227 1 108 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 3.34e-100 . . . . 5227 1 109 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 3.34e-100 . . . . 5227 1 110 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 7.26e-99 . . . . 5227 1 111 no PDB 2LL6 . "Solution Nmr Structure Of Cam Bound To Inos Cam Binding Domain Peptide" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 112 no PDB 2LL7 . "Solution Nmr Structure Of Cam Bound To The Enos Cam Binding Domain Peptide" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 113 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 1.80e-98 . . . . 5227 1 114 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 3.34e-100 . . . . 5227 1 115 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 3.34e-100 . . . . 5227 1 116 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 3.34e-100 . . . . 5227 1 117 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 3.34e-100 . . . . 5227 1 118 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 3.34e-100 . . . . 5227 1 119 no PDB 2O5G . "Calmodulin-Smooth Muscle Light Chain Kinase Peptide Complex" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 120 no PDB 2O60 . "Calmodulin Bound To Peptide From Neuronal Nitric Oxide Synthase" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 121 no PDB 2R28 . "The Complex Structure Of Calmodulin Bound To A Calcineurin Peptide" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 122 no PDB 2V01 . "Recombinant Vertebrate Calmodulin Complexed With Pb" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 123 no PDB 2V02 . "Recombinant Vertebrate Calmodulin Complexed With Ba" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 124 no PDB 2VAS . "Myosin Vi (Md-Insert2-Cam, Delta-Insert1) Post-Rigor State" . . . . . 100.00 149 97.97 99.32 3.51e-98 . . . . 5227 1 125 no PDB 2VAY . "Calmodulin Complexed With Cav1.1 Iq Peptide" . . . . . 98.65 146 100.00 100.00 7.26e-99 . . . . 5227 1 126 no PDB 2VB6 . "Myosin Vi (Md-Insert2-Cam, Delta Insert1) Post-Rigor State ( Crystal Form 2)" . . . . . 100.00 149 97.30 99.32 8.50e-98 . . . . 5227 1 127 no PDB 2W73 . "High-Resolution Structure Of The Complex Between Calmodulin And A Peptide From Calcineurin A" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 128 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 3.24e-100 . . . . 5227 1 129 no PDB 2X0G . "X-ray Structure Of A Dap-kinase Calmodulin Complex" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 130 no PDB 2X51 . "M6 Delta Insert1" . . . . . 100.00 149 97.97 99.32 3.51e-98 . . . . 5227 1 131 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 3.49e-100 . . . . 5227 1 132 no PDB 2YGG . "Complex Of Cambr And Cam" . . . . . 100.00 150 100.00 100.00 3.81e-100 . . . . 5227 1 133 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 3.34e-100 . . . . 5227 1 134 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 3.34e-100 . . . . 5227 1 135 no PDB 3BYA . "Structure Of A Calmodulin Complex" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 136 no PDB 3CLN . "Structure Of Calmodulin Refined At 2.2 Angstroms Resolution" . . . . . 100.00 148 99.32 100.00 1.37e-99 . . . . 5227 1 137 no PDB 3DVE . "Crystal Structure Of Ca2+CAM-Cav2.2 Iq Domain Complex" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 138 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 3.34e-100 . . . . 5227 1 139 no PDB 3DVK . "Crystal Structure Of Ca2+CAM-Cav2.3 Iq Domain Complex" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 140 no PDB 3DVM . "Crystal Structure Of Ca2+CAM-Cav2.1 Iq Domain Complex" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 141 no PDB 3EK4 . "Calcium-saturated Gcamp2 Monomer" . . . . . 99.32 449 100.00 100.00 6.40e-96 . . . . 5227 1 142 no PDB 3EK7 . "Calcium-Saturated Gcamp2 Dimer" . . . . . 99.32 449 100.00 100.00 6.40e-96 . . . . 5227 1 143 no PDB 3EK8 . "Calcium-Saturated Gcamp2 T116vG87R MUTANT MONOMER" . . . . . 99.32 449 100.00 100.00 9.04e-96 . . . . 5227 1 144 no PDB 3EKH . "Calcium-Saturated Gcamp2 T116vK378W MUTANT MONOMER" . . . . . 99.32 449 99.32 99.32 6.19e-95 . . . . 5227 1 145 no PDB 3EVU . "Crystal Structure Of Calcium Bound Dimeric Gcamp2, (#1)" . . . . . 99.32 449 100.00 100.00 6.40e-96 . . . . 5227 1 146 no PDB 3EVV . "Crystal Structure Of Calcium Bound Dimeric Gcamp2 (#2)" . . . . . 99.32 449 100.00 100.00 6.40e-96 . . . . 5227 1 147 no PDB 3EWT . "Crystal Structure Of Calmodulin Complexed With A Peptide" . . . . . 100.00 154 100.00 100.00 1.40e-100 . . . . 5227 1 148 no PDB 3EWV . "Crystal Structure Of Calmodulin Complexed With A Peptide" . . . . . 100.00 154 100.00 100.00 1.40e-100 . . . . 5227 1 149 no PDB 3G43 . "Crystal Structure Of The Calmodulin-Bound Cav1.2 C-Terminal Regulatory Domain Dimer" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 150 no PDB 3GN4 . "Myosin Lever Arm" . . . . . 100.00 149 97.97 99.32 3.51e-98 . . . . 5227 1 151 no PDB 3GOF . "Calmodulin Bound To Peptide From Macrophage Nitric Oxide Synthase" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 152 no PDB 3HR4 . "Human Inos Reductase And Calmodulin Complex" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 153 no PDB 3IF7 . "Structure Of Calmodulin Complexed With Its First Endogenous Inhibitor, Sphingosylphosphorylcholine" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 154 no PDB 3J41 . "Pseudo-atomic Model Of The Aquaporin-0/calmodulin Complex Derived From Electron Microscopy" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 155 no PDB 3L9I . "Myosin Vi Nucleotide-Free (Mdinsert2) L310g Mutant Crystal Structure" . . . . . 100.00 149 97.97 99.32 3.51e-98 . . . . 5227 1 156 no PDB 3O77 . "The Structure Of Ca2+ Sensor (Case-16)" . . . . . 99.32 415 100.00 100.00 2.87e-96 . . . . 5227 1 157 no PDB 3O78 . "The Structure Of Ca2+ Sensor (Case-12)" . . . . . 99.32 415 100.00 100.00 3.16e-96 . . . . 5227 1 158 no PDB 3OXQ . "Crystal Structure Of Ca2+CAM-Cav1.2 Pre-IqIQ DOMAIN COMPLEX" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 159 no PDB 3SG2 . "Crystal Structure Of Gcamp2-t116v,d381y" . . . . . 99.32 449 99.32 99.32 9.13e-95 . . . . 5227 1 160 no PDB 3SG3 . "Crystal Structure Of Gcamp3-d380y" . . . . . 99.32 449 98.64 99.32 1.16e-93 . . . . 5227 1 161 no PDB 3SG4 . "Crystal Structure Of Gcamp3-d380y, Lp(linker 2)" . . . . . 100.00 448 97.97 98.65 7.96e-94 . . . . 5227 1 162 no PDB 3SG5 . "Crystal Structure Of Dimeric Gcamp3-d380y, Qp(linker 1), Lp(linker 2)" . . . . . 100.00 448 97.97 98.65 6.55e-94 . . . . 5227 1 163 no PDB 3SG6 . "Crystal Structure Of Dimeric Gcamp2-lia(linker 1)" . . . . . 99.32 450 100.00 100.00 8.17e-96 . . . . 5227 1 164 no PDB 3SG7 . "Crystal Structure Of Gcamp3-kf(linker 1)" . . . . . 99.32 448 99.32 100.00 5.46e-95 . . . . 5227 1 165 no PDB 3SJQ . "Crystal Structure Of A Small Conductance Potassium Channel Splice Variant Complexed With Calcium-Calmodulin" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 166 no PDB 3SUI . "Crystal Structure Of Ca2+-Calmodulin In Complex With A Trpv1 C- Terminal Peptide" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 167 no PDB 3U0K . "Crystal Structure Of The Genetically Encoded Calcium Indicator Rcamp" . . . . . 99.32 440 98.64 99.32 1.95e-94 . . . . 5227 1 168 no PDB 3WFN . "Crystal Structure Of Nav1.6 Iq Motif In Complex With Apo-cam" . . . . . 100.00 182 100.00 100.00 4.02e-100 . . . . 5227 1 169 no PDB 4ANJ . "Myosin Vi (Mdinsert2-Gfp Fusion) Pre-Powerstroke State (Mg.Adp.Alf4)" . . . . . 100.00 149 97.97 99.32 3.51e-98 . . . . 5227 1 170 no PDB 4BW7 . "Calmodulin In Complex With Strontium" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 171 no PDB 4BW8 . "Calmodulin With Small Bend In Central Helix" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 172 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 3.49e-100 . . . . 5227 1 173 no PDB 4CLN . "Structure Of A Recombinant Calmodulin From Drosophila Melanogaster Refined At 2.2-Angstroms Resolution" . . . . . 100.00 148 97.97 99.32 4.61e-98 . . . . 5227 1 174 no PDB 4DBP . "Myosin Vi Nucleotide-free (mdinsert2) D179y Crystal Structure" . . . . . 100.00 149 97.97 99.32 3.51e-98 . . . . 5227 1 175 no PDB 4DBQ . "Myosin Vi D179y (md-insert2-cam, Delta-insert1) Post-rigor State" . . . . . 100.00 149 97.97 99.32 3.51e-98 . . . . 5227 1 176 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 3.49e-100 . . . . 5227 1 177 no PDB 4DJC . "1.35 A Crystal Structure Of The Nav1.5 Diii-Iv-CaCAM COMPLEX" . . . . . 100.00 152 100.00 100.00 2.44e-100 . . . . 5227 1 178 no PDB 4E50 . "Calmodulin And Ng Peptide Complex" . . . . . 100.00 185 100.00 100.00 1.82e-100 . . . . 5227 1 179 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 3.34e-100 . . . . 5227 1 180 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 3.49e-100 . . . . 5227 1 181 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 3.49e-100 . . . . 5227 1 182 no PDB 4HEX . "A Novel Conformation Of Calmodulin" . . . . . 100.00 156 100.00 100.00 1.50e-100 . . . . 5227 1 183 no PDB 4IK1 . "High Resolution Structure Of Gcampj At Ph 8.5" . . . . . 99.32 448 98.64 99.32 9.99e-94 . . . . 5227 1 184 no PDB 4IK3 . "High Resolution Structure Of Gcamp3 At Ph 8.5" . . . . . 99.32 448 99.32 100.00 6.49e-95 . . . . 5227 1 185 no PDB 4IK4 . "High Resolution Structure Of Gcamp3 At Ph 5.0" . . . . . 99.32 448 99.32 100.00 6.49e-95 . . . . 5227 1 186 no PDB 4IK5 . "High Resolution Structure Of Delta-rest-gcamp3" . . . . . 99.32 414 99.32 100.00 2.54e-95 . . . . 5227 1 187 no PDB 4IK8 . "High Resolution Structure Of Gcamp3 Dimer Form 1 At Ph 7.5" . . . . . 99.32 448 99.32 100.00 6.49e-95 . . . . 5227 1 188 no PDB 4IK9 . "High Resolution Structure Of Gcamp3 Dimer Form 2 At Ph 7.5" . . . . . 99.32 448 99.32 100.00 6.49e-95 . . . . 5227 1 189 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 3.49e-100 . . . . 5227 1 190 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 3.49e-100 . . . . 5227 1 191 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 3.49e-100 . . . . 5227 1 192 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 3.49e-100 . . . . 5227 1 193 no PDB 4L79 . "Crystal Structure Of Nucleotide-free Myosin 1b Residues 1-728 With Bound Calmodulin" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 194 no PDB 4LZX . "Complex Of Iqcg And Ca2+-free Cam" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 195 no PDB 4M1L . "Complex Of Iqcg And Ca2+-bound Cam" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 196 no PDB 4Q5U . "Structure Of Calmodulin Bound To Its Recognition Site From Calcineurin" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 197 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 4.26e-99 . . . . 5227 1 198 no PDB 4R8G . "Crystal Structure Of Myosin-1c Tail In Complex With Calmodulin" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 199 no PDB 4UMO . "Crystal Structure Of The Kv7.1 Proximal C-terminal Domain In Complex With Calmodulin" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 200 no PDB 4UPU . "Crystal Structure Of Ip3 3-k Calmodulin Binding Region In Complex With Calmodulin" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 201 no PDB 4V0C . "Crystal Structure Of The Kv7.1 Proximal C-terminal Domain In Complex With Calmodulin" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 202 no DBJ BAA08302 . "calmodulin [Homo sapiens]" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 203 no DBJ BAA11896 . "calmodulin [Anas platyrhynchos]" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 204 no DBJ BAA19786 . "calmodulin [Branchiostoma lanceolatum]" . . . . . 100.00 149 97.97 99.32 3.51e-98 . . . . 5227 1 205 no DBJ BAA19787 . "calmodulin [Branchiostoma floridae]" . . . . . 100.00 149 97.97 99.32 3.51e-98 . . . . 5227 1 206 no DBJ BAA19788 . "calmodulin [Halocynthia roretzi]" . . . . . 100.00 149 97.97 99.32 3.51e-98 . . . . 5227 1 207 no EMBL CAA10601 . "calmodulin [Caenorhabditis elegans]" . . . . . 100.00 149 97.97 98.65 8.69e-98 . . . . 5227 1 208 no EMBL CAA32050 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 209 no EMBL CAA32062 . "calmodulin II [Rattus norvegicus]" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 210 no EMBL CAA32119 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 211 no EMBL CAA32120 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 212 no GB AAA35635 . "calmodulin [Homo sapiens]" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 213 no GB AAA35641 . "calmodulin [Homo sapiens]" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 214 no GB AAA37365 . "calmodulin synthesis [Mus musculus]" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 215 no GB AAA40862 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 216 no GB AAA40863 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 217 no PIR JC1305 . "calmodulin - Japanese medaka" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 218 no PIR MCON . "calmodulin - salmon" . . . . . 100.00 148 100.00 100.00 3.34e-100 . . . . 5227 1 219 no PRF 0409298A . "troponin C-like protein" . . . . . 100.00 148 97.30 100.00 1.72e-98 . . . . 5227 1 220 no PRF 0608335A . calmodulin . . . . . 100.00 148 97.97 99.32 2.37e-97 . . . . 5227 1 221 no REF NP_001008160 . "calmodulin 2 (phosphorylase kinase, delta) [Xenopus (Silurana) tropicalis]" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 222 no REF NP_001009759 . "calmodulin [Ovis aries]" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 223 no REF NP_001027633 . "calmodulin [Ciona intestinalis]" . . . . . 100.00 149 97.30 98.65 2.27e-97 . . . . 5227 1 224 no REF NP_001039714 . "calmodulin [Bos taurus]" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 225 no REF NP_001040234 . "calmodulin [Bombyx mori]" . . . . . 100.00 149 97.97 99.32 3.51e-98 . . . . 5227 1 226 no SP O02367 . "RecName: Full=Calmodulin; Short=CaM; AltName: Full=Ci-CaM [Ciona intestinalis]" . . . . . 100.00 149 97.30 98.65 2.27e-97 . . . . 5227 1 227 no SP O16305 . "RecName: Full=Calmodulin; Short=CaM [Caenorhabditis elegans]" . . . . . 100.00 149 97.97 98.65 8.69e-98 . . . . 5227 1 228 no SP O96081 . "RecName: Full=Calmodulin-B; Short=CaM B [Halocynthia roretzi]" . . . . . 100.00 149 97.30 98.65 2.56e-97 . . . . 5227 1 229 no SP P02594 . "RecName: Full=Calmodulin; Short=CaM [Electrophorus electricus]" . . . . . 100.00 149 99.32 100.00 1.12e-99 . . . . 5227 1 230 no SP P05932 . "RecName: Full=Calmodulin-beta; Short=Cam B, partial [Arbacia punctulata]" . . . . . 93.24 138 97.10 99.28 3.58e-90 . . . . 5227 1 231 no TPG DAA13808 . "TPA: calmodulin 2-like [Bos taurus]" . . . . . 100.00 216 98.65 98.65 1.70e-98 . . . . 5227 1 232 no TPG DAA18029 . "TPA: calmodulin [Bos taurus]" . . . . . 100.00 149 98.65 99.32 5.13e-99 . . . . 5227 1 233 no TPG DAA19590 . "TPA: calmodulin 3 [Bos taurus]" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 234 no TPG DAA24777 . "TPA: calmodulin 2-like [Bos taurus]" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 235 no TPG DAA24988 . "TPA: calmodulin 2-like isoform 1 [Bos taurus]" . . . . . 100.00 149 100.00 100.00 3.49e-100 . . . . 5227 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Calmodulin recognition element from smooth muscle myosin light chain kinase' common 5227 1 smMLCKp abbreviation 5227 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 . GLY . 5227 1 2 . SER . 5227 1 3 . ALA . 5227 1 4 . ARG . 5227 1 5 . ARG . 5227 1 6 . LYS . 5227 1 7 . TRP . 5227 1 8 . GLN . 5227 1 9 . LYS . 5227 1 10 . THR . 5227 1 11 . GLY . 5227 1 12 . HIS . 5227 1 13 . ALA . 5227 1 14 . VAL . 5227 1 15 . ARG . 5227 1 16 . ALA . 5227 1 17 . ILE . 5227 1 18 . GLY . 5227 1 19 . ARG . 5227 1 20 . LEU . 5227 1 21 . SER . 5227 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 . GLY 1 1 5227 1 . SER 2 2 5227 1 . ALA 3 3 5227 1 . ARG 4 4 5227 1 . ARG 5 5 5227 1 . LYS 6 6 5227 1 . TRP 7 7 5227 1 . GLN 8 8 5227 1 . LYS 9 9 5227 1 . THR 10 10 5227 1 . GLY 11 11 5227 1 . HIS 12 12 5227 1 . ALA 13 13 5227 1 . VAL 14 14 5227 1 . ARG 15 15 5227 1 . ALA 16 16 5227 1 . ILE 17 17 5227 1 . GLY 18 18 5227 1 . ARG 19 19 5227 1 . LEU 20 20 5227 1 . SER 21 21 5227 1 stop_ save_ save_CaM _Entity.Sf_category entity _Entity.Sf_framecode CaM _Entity.Entry_ID 5227 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name 'calmodulin (chicken)' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; 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 . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 148 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 16700 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID . . SWISS-PROT P62149 . 'Calmodulin (CaM)' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . SWISS-PROT P62151 . 'Calmodulin (CaM)' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . SWISS-PROT P21251 . 'Calmodulin (CaM)' . . . . . 100.00 149 98.65 99.32 3.66e-78 . . . . 5227 2 . . SWISS-PROT P62144 . 'Calmodulin (CaM)' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . REF NP_001084025 . 'cam [Xenopus laevis]' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . SWISS-PROT P02594 . 'Calmodulin (CaM)' . . . . . 100.00 149 99.32 100.00 9.56e-79 . . . . 5227 2 . . REF NP_001039714 . 'calmodulin 3 [Bos taurus]' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . REF NP_001080864 . 'calmodulin 2 [Xenopus laevis]' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . REF NP_001008160 . 'calmodulin 2 (phosphorylase kinase, delta) [Xenopus tropicalis]' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . REF NP_001009759 . 'calmodulin 2 [Ovis aries]' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . PIR JC1305 . 'calmodulin - Japanese medaka' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . PIR MCON . 'calmodulin - salmon' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . GenBank AAA40862 . calmodulin . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . GenBank AAA40863 . calmodulin . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . GenBank AAA35641 . calmodulin . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . GenBank AAA37365 . 'calmodulin synthesis' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . EMBL CAA32478 . 'calmodulin III [Rattus norvegicus]' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . GenBank AAA35635 . calmodulin . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . EMBL CAA32119 . 'calmodulin [Rattus norvegicus]' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . EMBL CAA32120 . 'calmodulin [Rattus norvegicus]' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . EMBL CAA32050 . 'calmodulin [Rattus norvegicus]' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . EMBL CAA32062 . 'calmodulin II [Rattus norvegicus]' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . DBJ BAB28116 . 'unnamed protein product [Mus musculus]' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . DBJ BAB28319 . 'unnamed protein product [Mus musculus]' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . DBJ BAA11896 . 'calmodulin [Anas platyrhynchos]' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . DBJ BAB23462 . 'unnamed protein product [Mus musculus]' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . PDB 3CLN . 'Structure Of Calmodulin Refined At 2.2 Angstroms Resolution' . . . . . 100.00 148 99.32 100.00 1.14e-78 . . . . 5227 2 . . DBJ BAA08302 . 'calmodulin [Homo sapiens]' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . 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 3.88e-79 . . . . 5227 2 . . 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 3.88e-79 . . . . 5227 2 . . PDB 2V01 . 'Recombinant Vertebrate Calmodulin Complexed With Pb' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . PDB 2V02 . 'Recombinant Vertebrate Calmodulin Complexed With Ba' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . PDB 2O60 . 'Calmodulin Bound To Peptide From Neuronal Nitric Oxide Synthase' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 2R28 . 'The Complex Structure Of Calmodulin Bound To A Calcineurin Peptide' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . PDB 2K0F . 'Calmodulin Complexed With Calmodulin-Binding Peptide From Smooth Muscle Myosin Light Chain Kinase' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 2O5G . 'Calmodulin-Smooth Muscle Light Chain Kinase Peptide Complex' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 2HQW . 'Crystal Structure Of Ca2+CALMODULIN BOUND TO NMDA RECEPTOR Nr1c1 Peptide' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 2K0E . 'A Coupled Equilibrium Shift Mechanism In Calmodulin- Mediated Signal Transduction' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 2F3Z . 'CalmodulinIQ-Aa Domain Complex' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 2FOT . 'Crystal Structure Of The Complex Between Calmodulin And Alphaii-Spectrin' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . 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 2.13e-79 . . . . 5227 2 . . PDB 2F3Y . 'CalmodulinIQ DOMAIN COMPLEX' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 2DFS . '3-D Structure Of Myosin-V Inhibited State' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . 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 2.13e-79 . . . . 5227 2 . . PDB 2BCX . 'Crystal Structure Of Calmodulin In Complex With A Ryanodine Receptor Peptide' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 2BKI . 'Myosin Vi Nucleotide-Free (Mdinsert2-Iq) Crystal Structure' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . PDB 1XFZ . 'Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin In The Presence Of 1 Millimolar Exogenously Added Calcium Chloride' . . . . . 100.00 149 99.32 100.00 7.57e-79 . . . . 5227 2 . . PDB 1YR5 . '1.7-A Structure Of Calmodulin Bound To A Peptide From Dap Kinase' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . 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 7.57e-79 . . . . 5227 2 . . PDB 1XFY . 'Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin' . . . . . 100.00 149 99.32 100.00 7.57e-79 . . . . 5227 2 . . 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 7.57e-79 . . . . 5227 2 . . PDB 1XFV . "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3' Deoxy-Atp" . . . . . 100.00 149 99.32 100.00 7.57e-79 . . . . 5227 2 . . PDB 1X02 . 'Solution Structure Of Stereo Array Isotope Labeled (Sail) Calmodulin' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 1XA5 . 'Structure Of Calmodulin In Complex With Kar-2, A Bis-Indol Alkaloid' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 1UP5 . 'Chicken Calmodulin' . . . . . 100.00 148 99.32 99.32 1.98e-78 . . . . 5227 2 . . PDB 1WRZ . 'Calmodulin Complexed With A Peptide From A Human Death- Associated Protein Kinase' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . PDB 1SK6 . "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin, 3',5' Cyclic Amp (Camp), And Pyrophosphate" . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 1SY9 . 'Structure Of Calmodulin Complexed With A Fragment Of The Olfactory Cng Channel' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 1QX5 . 'Crystal Structure Of Apocalmodulin' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 1S26 . 'Structure Of Anthrax Edema Factor-Calmodulin-Alpha,Beta- Methyleneadenosine 5'-Triphosphate Complex Reveals An Alternative Mode Of Atp Binding To The Catalytic Site' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . 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 3.88e-79 . . . . 5227 2 . . 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 3.88e-79 . . . . 5227 2 . . PDB 1NWD . 'Solution Structure Of Ca2+CALMODULIN BOUND TO THE C- Terminal Domain Of Petunia Glutamate Decarboxylase' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 1PRW . 'Crystal Structure Of Bovine Brain Ca++ Calmodulin In A Compact Form' . . . . . 100.00 148 99.32 99.32 1.98e-78 . . . . 5227 2 . . PDB 1LVC . "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 2' Deoxy, 3' Anthraniloyl Atp" . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . 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 3.88e-79 . . . . 5227 2 . . PDB 1L7Z . 'Crystal Structure Of Ca2+CALMODULIN COMPLEXED WITH Myristoylated Cap-23NAP-22 Peptide' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 1LIN . 'Calmodulin Complexed With Trifluoperazine (1:4 Complex)' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 1IWQ . 'Crystal Structure Of Marcks Calmodulin Binding Domain Peptide Complexed With Ca2+CALMODULIN' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . 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 3.88e-79 . . . . 5227 2 . . 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 3.88e-79 . . . . 5227 2 . . PDB 1IQ5 . 'CalmodulinNEMATODE CA2+CALMODULIN DEPENDENT KINASE KINASE Fragment' . . . . . 100.00 149 100.00 100.00 3.91e-79 . . . . 5227 2 . . PDB 1CTR . 'Drug Binding By Calmodulin: Crystal Structure Of A Calmodulin-Trifluoperazine Complex' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 1DMO . 'Calmodulin, Nmr, 30 Structures' . . . . . 100.00 148 99.32 100.00 1.14e-78 . . . . 5227 2 . . PDB 1CM1 . 'Motions Of Calmodulin-Single-Conformer Refinement' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 1CM4 . 'Motions Of Calmodulin-Four-Conformer Refinement' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 1CKK . 'CalmodulinRAT CA2+CALMODULIN DEPENDENT PROTEIN KINASE Fragment' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 1CLL . 'Calmodulin Structure Refined At 1.7 Angstroms Resolution' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 1CFD . 'Calcium-Free Calmodulin' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . 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 3.88e-79 . . . . 5227 2 . . PDB 1A29 . 'Calmodulin Complexed With Trifluoperazine (1:2 Complex)' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . PDB 1CFC . 'Calcium-Free Calmodulin' . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . BMRB 6023 . Calmodulin . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . BMRB 6541 . calmodulin . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . BMRB 5480 . Calmodulin . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . BMRB 5770 . Calmodulin . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . BMRB 5286 . calmodulin . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . BMRB 5287 . calmodulin . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . BMRB 4310 . calmodulin . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . BMRB 4970 . Calmodulin . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . BMRB 4270 . calmodulin . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . BMRB 4284 . Calmodulin . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . BMRB 15191 . Calmodulin . . . . . 100.00 148 98.65 100.00 1.51e-78 . . . . 5227 2 . . BMRB 4056 . calmodulin . . . . . 100.00 148 100.00 100.00 3.88e-79 . . . . 5227 2 . . BMRB 15187 . calmodulin . . . . . 100.00 149 98.65 100.00 1.60e-78 . . . . 5227 2 . . BMRB 15188 . calmodulin . . . . . 100.00 148 98.65 100.00 1.51e-78 . . . . 5227 2 . . BMRB 15185 . calmodulin . . . . . 100.00 148 98.65 100.00 1.51e-78 . . . . 5227 2 . . BMRB 15186 . calmodulin . . . . . 100.00 148 98.65 100.00 1.51e-78 . . . . 5227 2 . . BMRB 15183 . calmodulin . . . . . 100.00 149 98.65 100.00 1.60e-78 . . . . 5227 2 . . BMRB 15184 . calmodulin . . . . . 100.00 148 98.65 100.00 1.51e-78 . . . . 5227 2 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'calmodulin (chicken)' common 5227 2 CaM abbreviation 5227 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 . ALA . 5227 2 2 . ASP . 5227 2 3 . GLN . 5227 2 4 . LEU . 5227 2 5 . THR . 5227 2 6 . GLU . 5227 2 7 . GLU . 5227 2 8 . GLN . 5227 2 9 . ILE . 5227 2 10 . ALA . 5227 2 11 . GLU . 5227 2 12 . PHE . 5227 2 13 . LYS . 5227 2 14 . GLU . 5227 2 15 . ALA . 5227 2 16 . PHE . 5227 2 17 . SER . 5227 2 18 . LEU . 5227 2 19 . PHE . 5227 2 20 . ASP . 5227 2 21 . LYS . 5227 2 22 . ASP . 5227 2 23 . GLY . 5227 2 24 . ASP . 5227 2 25 . GLY . 5227 2 26 . THR . 5227 2 27 . ILE . 5227 2 28 . THR . 5227 2 29 . THR . 5227 2 30 . LYS . 5227 2 31 . GLU . 5227 2 32 . LEU . 5227 2 33 . GLY . 5227 2 34 . THR . 5227 2 35 . VAL . 5227 2 36 . MET . 5227 2 37 . ARG . 5227 2 38 . SER . 5227 2 39 . LEU . 5227 2 40 . GLY . 5227 2 41 . GLN . 5227 2 42 . ASN . 5227 2 43 . PRO . 5227 2 44 . THR . 5227 2 45 . GLU . 5227 2 46 . ALA . 5227 2 47 . GLU . 5227 2 48 . LEU . 5227 2 49 . GLN . 5227 2 50 . ASP . 5227 2 51 . MET . 5227 2 52 . ILE . 5227 2 53 . ASN . 5227 2 54 . GLU . 5227 2 55 . VAL . 5227 2 56 . ASP . 5227 2 57 . ALA . 5227 2 58 . ASP . 5227 2 59 . GLY . 5227 2 60 . ASN . 5227 2 61 . GLY . 5227 2 62 . THR . 5227 2 63 . ILE . 5227 2 64 . ASP . 5227 2 65 . PHE . 5227 2 66 . PRO . 5227 2 67 . GLU . 5227 2 68 . PHE . 5227 2 69 . LEU . 5227 2 70 . THR . 5227 2 71 . MET . 5227 2 72 . MET . 5227 2 73 . ALA . 5227 2 74 . ARG . 5227 2 75 . LYS . 5227 2 76 . MET . 5227 2 77 . LYS . 5227 2 78 . ASP . 5227 2 79 . THR . 5227 2 80 . ASP . 5227 2 81 . SER . 5227 2 82 . GLU . 5227 2 83 . GLU . 5227 2 84 . GLU . 5227 2 85 . ILE . 5227 2 86 . ARG . 5227 2 87 . GLU . 5227 2 88 . ALA . 5227 2 89 . PHE . 5227 2 90 . ARG . 5227 2 91 . VAL . 5227 2 92 . PHE . 5227 2 93 . ASP . 5227 2 94 . LYS . 5227 2 95 . ASP . 5227 2 96 . GLY . 5227 2 97 . ASN . 5227 2 98 . GLY . 5227 2 99 . TYR . 5227 2 100 . ILE . 5227 2 101 . SER . 5227 2 102 . ALA . 5227 2 103 . ALA . 5227 2 104 . GLU . 5227 2 105 . LEU . 5227 2 106 . ARG . 5227 2 107 . HIS . 5227 2 108 . VAL . 5227 2 109 . MET . 5227 2 110 . THR . 5227 2 111 . ASN . 5227 2 112 . LEU . 5227 2 113 . GLY . 5227 2 114 . GLU . 5227 2 115 . LYS . 5227 2 116 . LEU . 5227 2 117 . THR . 5227 2 118 . ASP . 5227 2 119 . GLU . 5227 2 120 . GLU . 5227 2 121 . VAL . 5227 2 122 . ASP . 5227 2 123 . GLU . 5227 2 124 . MET . 5227 2 125 . ILE . 5227 2 126 . ARG . 5227 2 127 . GLU . 5227 2 128 . ALA . 5227 2 129 . ASP . 5227 2 130 . ILE . 5227 2 131 . ASP . 5227 2 132 . GLY . 5227 2 133 . ASP . 5227 2 134 . GLY . 5227 2 135 . GLN . 5227 2 136 . VAL . 5227 2 137 . ASN . 5227 2 138 . TYR . 5227 2 139 . GLU . 5227 2 140 . GLU . 5227 2 141 . PHE . 5227 2 142 . VAL . 5227 2 143 . GLN . 5227 2 144 . MET . 5227 2 145 . MET . 5227 2 146 . THR . 5227 2 147 . ALA . 5227 2 148 . LYS . 5227 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 . ALA 1 1 5227 2 . ASP 2 2 5227 2 . GLN 3 3 5227 2 . LEU 4 4 5227 2 . THR 5 5 5227 2 . GLU 6 6 5227 2 . GLU 7 7 5227 2 . GLN 8 8 5227 2 . ILE 9 9 5227 2 . ALA 10 10 5227 2 . GLU 11 11 5227 2 . PHE 12 12 5227 2 . LYS 13 13 5227 2 . GLU 14 14 5227 2 . ALA 15 15 5227 2 . PHE 16 16 5227 2 . SER 17 17 5227 2 . LEU 18 18 5227 2 . PHE 19 19 5227 2 . ASP 20 20 5227 2 . LYS 21 21 5227 2 . ASP 22 22 5227 2 . GLY 23 23 5227 2 . ASP 24 24 5227 2 . GLY 25 25 5227 2 . THR 26 26 5227 2 . ILE 27 27 5227 2 . THR 28 28 5227 2 . THR 29 29 5227 2 . LYS 30 30 5227 2 . GLU 31 31 5227 2 . LEU 32 32 5227 2 . GLY 33 33 5227 2 . THR 34 34 5227 2 . VAL 35 35 5227 2 . MET 36 36 5227 2 . ARG 37 37 5227 2 . SER 38 38 5227 2 . LEU 39 39 5227 2 . GLY 40 40 5227 2 . GLN 41 41 5227 2 . ASN 42 42 5227 2 . PRO 43 43 5227 2 . THR 44 44 5227 2 . GLU 45 45 5227 2 . ALA 46 46 5227 2 . GLU 47 47 5227 2 . LEU 48 48 5227 2 . GLN 49 49 5227 2 . ASP 50 50 5227 2 . MET 51 51 5227 2 . ILE 52 52 5227 2 . ASN 53 53 5227 2 . GLU 54 54 5227 2 . VAL 55 55 5227 2 . ASP 56 56 5227 2 . ALA 57 57 5227 2 . ASP 58 58 5227 2 . GLY 59 59 5227 2 . ASN 60 60 5227 2 . GLY 61 61 5227 2 . THR 62 62 5227 2 . ILE 63 63 5227 2 . ASP 64 64 5227 2 . PHE 65 65 5227 2 . PRO 66 66 5227 2 . GLU 67 67 5227 2 . PHE 68 68 5227 2 . LEU 69 69 5227 2 . THR 70 70 5227 2 . MET 71 71 5227 2 . MET 72 72 5227 2 . ALA 73 73 5227 2 . ARG 74 74 5227 2 . LYS 75 75 5227 2 . MET 76 76 5227 2 . LYS 77 77 5227 2 . ASP 78 78 5227 2 . THR 79 79 5227 2 . ASP 80 80 5227 2 . SER 81 81 5227 2 . GLU 82 82 5227 2 . GLU 83 83 5227 2 . GLU 84 84 5227 2 . ILE 85 85 5227 2 . ARG 86 86 5227 2 . GLU 87 87 5227 2 . ALA 88 88 5227 2 . PHE 89 89 5227 2 . ARG 90 90 5227 2 . VAL 91 91 5227 2 . PHE 92 92 5227 2 . ASP 93 93 5227 2 . LYS 94 94 5227 2 . ASP 95 95 5227 2 . GLY 96 96 5227 2 . ASN 97 97 5227 2 . GLY 98 98 5227 2 . TYR 99 99 5227 2 . ILE 100 100 5227 2 . SER 101 101 5227 2 . ALA 102 102 5227 2 . ALA 103 103 5227 2 . GLU 104 104 5227 2 . LEU 105 105 5227 2 . ARG 106 106 5227 2 . HIS 107 107 5227 2 . VAL 108 108 5227 2 . MET 109 109 5227 2 . THR 110 110 5227 2 . ASN 111 111 5227 2 . LEU 112 112 5227 2 . GLY 113 113 5227 2 . GLU 114 114 5227 2 . LYS 115 115 5227 2 . LEU 116 116 5227 2 . THR 117 117 5227 2 . ASP 118 118 5227 2 . GLU 119 119 5227 2 . GLU 120 120 5227 2 . VAL 121 121 5227 2 . ASP 122 122 5227 2 . GLU 123 123 5227 2 . MET 124 124 5227 2 . ILE 125 125 5227 2 . ARG 126 126 5227 2 . GLU 127 127 5227 2 . ALA 128 128 5227 2 . ASP 129 129 5227 2 . ILE 130 130 5227 2 . ASP 131 131 5227 2 . GLY 132 132 5227 2 . ASP 133 133 5227 2 . GLY 134 134 5227 2 . GLN 135 135 5227 2 . VAL 136 136 5227 2 . ASN 137 137 5227 2 . TYR 138 138 5227 2 . GLU 139 139 5227 2 . GLU 140 140 5227 2 . PHE 141 141 5227 2 . VAL 142 142 5227 2 . GLN 143 143 5227 2 . MET 144 144 5227 2 . MET 145 145 5227 2 . THR 146 146 5227 2 . ALA 147 147 5227 2 . LYS 148 148 5227 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 5227 _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 $smMLCKp . 9031 . . 'Gallus gallus' Chicken . . Eukaryota Metazoa Gallus gallus . . . . . . . . . . . . . . . . . . . . . 5227 1 2 2 $CaM . 9031 . . 'Gallus gallus' Chicken . . Eukaryota Metazoa Gallus gallus . . . . . . . . . . . . . . . . . . . . . 5227 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 5227 _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 $smMLCKp . 'recombinant technology' . 'E. coli' . . . . . . . . . . . . . . . . . . . . . . . . ; Peptide is produced in an E. coli overexpression system (described in the associated Biochemistry paper) and therfore is unmodified at the terminii. Often, studies of the smMLCKp peptide interacting with calmodulin are performed using chemically synthesized peptide. ; . . 5227 1 2 2 $CaM . 'recombinant technology' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5227 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5227 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'Calmodulin recognition element from smooth muscle myosin light chain kinase' '[U-99% 13C; U-99% 15N]' . . 1 $smMLCKp . . 2.00 . . mM . . . . 5227 1 2 'calmodulin (chicken)' . . . 2 $CaM . . 2.25 . . mM . . . . 5227 1 3 CaCl2 . . . . . . . 20 . . mM . . . . 5227 1 4 KCl . . . . . . . 100 . . mM . . . . 5227 1 5 Bis-tris . . . . . . . 20 . . mM . . . . 5227 1 6 NaN3 . . . . . . . 0.02 . . % . . . . 5227 1 7 D2O . . . . . . . 7 . . % . . . . 5227 1 stop_ save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-cond_1 _Sample_condition_list.Entry_ID 5227 _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 0.1 na 5227 1 temperature 303 1.5 K 5227 1 'ionic strength' 0.16 0.02 M 5227 1 stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Software.Sf_category software _Software.Sf_framecode FELIX _Software.Entry_ID 5227 _Software.ID 1 _Software.Name FELIX _Software.Version 98.0 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 5227 1 'peak picking' 5227 1 assignments 5227 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 5227 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5227 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer Varian INOVA . 750 . . . 5227 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 5227 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '1H-15N HSQC' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5227 1 2 '1H-13C CT-HSQC' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5227 1 3 CBCA(CO)NH . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5227 1 4 HNCACB . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5227 1 5 HNCO . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5227 1 6 HN(CA)CO . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5227 1 7 HBHACONH . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5227 1 8 HCCHTOCSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5227 1 9 'CH3-filtered (1H13C13C) HCCHTOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5227 1 10 'CCC TOCSY NNH' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5227 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 5227 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '1H-15N HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 5227 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '1H-13C CT-HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 5227 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name CBCA(CO)NH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 5227 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name HNCACB _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 5227 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name HNCO _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 5227 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name HN(CA)CO _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_7 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7 _NMR_spec_expt.Entry_ID 5227 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name HBHACONH _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_8 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_8 _NMR_spec_expt.Entry_ID 5227 _NMR_spec_expt.ID 8 _NMR_spec_expt.Name HCCHTOCSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_9 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_9 _NMR_spec_expt.Entry_ID 5227 _NMR_spec_expt.ID 9 _NMR_spec_expt.Name 'CH3-filtered (1H13C13C) HCCHTOCSY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_10 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_10 _NMR_spec_expt.Entry_ID 5227 _NMR_spec_expt.ID 10 _NMR_spec_expt.Name 'CCC TOCSY NNH' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5227 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.000000000 . . . . . . . . . 5227 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5227 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5227 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_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 5227 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-cond_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '1H-15N HSQC' 1 $sample_1 . 5227 1 2 '1H-13C CT-HSQC' 1 $sample_1 . 5227 1 3 CBCA(CO)NH 1 $sample_1 . 5227 1 4 HNCACB 1 $sample_1 . 5227 1 5 HNCO 1 $sample_1 . 5227 1 6 HN(CA)CO 1 $sample_1 . 5227 1 7 HBHACONH 1 $sample_1 . 5227 1 8 HCCHTOCSY 1 $sample_1 . 5227 1 9 'CH3-filtered (1H13C13C) HCCHTOCSY' 1 $sample_1 . 5227 1 10 'CCC TOCSY NNH' 1 $sample_1 . 5227 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 GLY HA2 H 1 4.033 0.019 . 2 . . . . . . . . 5227 1 2 . 1 1 1 1 GLY HA3 H 1 3.983 0.019 . 2 . . . . . . . . 5227 1 3 . 1 1 1 1 GLY CA C 13 43.59 0.042 . 1 . . . . . . . . 5227 1 4 . 1 1 2 2 SER HA H 1 4.510 0.030 . 2 . . . . . . . . 5227 1 5 . 1 1 2 2 SER HB2 H 1 4.121 0.032 . 2 . . . . . . . . 5227 1 6 . 1 1 2 2 SER HB3 H 1 3.986 0.032 . 2 . . . . . . . . 5227 1 7 . 1 1 2 2 SER C C 13 175.71 0.100 . 1 . . . . . . . . 5227 1 8 . 1 1 2 2 SER CA C 13 59.13 0.040 . 1 . . . . . . . . 5227 1 9 . 1 1 2 2 SER CB C 13 63.56 0.040 . 1 . . . . . . . . 5227 1 10 . 1 1 3 3 ALA H H 1 8.923 0.060 . 1 . . . . . . . . 5227 1 11 . 1 1 3 3 ALA HA H 1 4.176 0.033 . 1 . . . . . . . . 5227 1 12 . 1 1 3 3 ALA HB1 H 1 1.516 0.028 . 1 . . . . . . . . 5227 1 13 . 1 1 3 3 ALA HB2 H 1 1.516 0.028 . 1 . . . . . . . . 5227 1 14 . 1 1 3 3 ALA HB3 H 1 1.516 0.028 . 1 . . . . . . . . 5227 1 15 . 1 1 3 3 ALA C C 13 179.32 0.100 . 1 . . . . . . . . 5227 1 16 . 1 1 3 3 ALA CA C 13 55.17 0.042 . 1 . . . . . . . . 5227 1 17 . 1 1 3 3 ALA CB C 13 19.15 0.042 . 1 . . . . . . . . 5227 1 18 . 1 1 3 3 ALA N N 15 125.27 0.125 . 1 . . . . . . . . 5227 1 19 . 1 1 4 4 ARG H H 1 8.412 0.060 . 1 . . . . . . . . 5227 1 20 . 1 1 4 4 ARG HA H 1 4.232 0.033 . 1 . . . . . . . . 5227 1 21 . 1 1 4 4 ARG HB2 H 1 2.029 0.030 . 2 . . . . . . . . 5227 1 22 . 1 1 4 4 ARG HB3 H 1 1.932 0.030 . 2 . . . . . . . . 5227 1 23 . 1 1 4 4 ARG HG2 H 1 1.771 0.032 . 2 . . . . . . . . 5227 1 24 . 1 1 4 4 ARG HG3 H 1 1.642 0.030 . 2 . . . . . . . . 5227 1 25 . 1 1 4 4 ARG HD2 H 1 3.271 0.031 . 1 . . . . . . . . 5227 1 26 . 1 1 4 4 ARG HE H 1 7.472 0.060 . 1 . . . . . . . . 5227 1 27 . 1 1 4 4 ARG C C 13 178.29 0.100 . 1 . . . . . . . . 5227 1 28 . 1 1 4 4 ARG CA C 13 60.23 0.043 . 1 . . . . . . . . 5227 1 29 . 1 1 4 4 ARG CB C 13 29.77 0.042 . 1 . . . . . . . . 5227 1 30 . 1 1 4 4 ARG CG C 13 28.05 0.041 . 1 . . . . . . . . 5227 1 31 . 1 1 4 4 ARG CD C 13 43.20 0.042 . 1 . . . . . . . . 5227 1 32 . 1 1 4 4 ARG CZ C 13 159.53 0.100 . 1 . . . . . . . . 5227 1 33 . 1 1 4 4 ARG N N 15 118.45 0.125 . 1 . . . . . . . . 5227 1 34 . 1 1 4 4 ARG NE N 15 97.79 0.125 . 1 . . . . . . . . 5227 1 35 . 1 1 5 5 ARG H H 1 7.957 0.060 . 1 . . . . . . . . 5227 1 36 . 1 1 5 5 ARG HA H 1 4.252 0.032 . 1 . . . . . . . . 5227 1 37 . 1 1 5 5 ARG HB2 H 1 2.043 0.024 . 2 . . . . . . . . 5227 1 38 . 1 1 5 5 ARG HB3 H 1 2.021 0.027 . 2 . . . . . . . . 5227 1 39 . 1 1 5 5 ARG HG2 H 1 1.803 0.031 . 1 . . . . . . . . 5227 1 40 . 1 1 5 5 ARG HD2 H 1 3.330 0.031 . 1 . . . . . . . . 5227 1 41 . 1 1 5 5 ARG HE H 1 7.811 0.060 . 1 . . . . . . . . 5227 1 42 . 1 1 5 5 ARG C C 13 178.94 0.100 . 1 . . . . . . . . 5227 1 43 . 1 1 5 5 ARG CA C 13 58.72 0.043 . 1 . . . . . . . . 5227 1 44 . 1 1 5 5 ARG CB C 13 29.59 0.048 . 1 . . . . . . . . 5227 1 45 . 1 1 5 5 ARG CG C 13 27.54 0.040 . 1 . . . . . . . . 5227 1 46 . 1 1 5 5 ARG CD C 13 43.01 0.042 . 1 . . . . . . . . 5227 1 47 . 1 1 5 5 ARG CZ C 13 159.86 0.100 . 1 . . . . . . . . 5227 1 48 . 1 1 5 5 ARG N N 15 118.42 0.125 . 1 . . . . . . . . 5227 1 49 . 1 1 5 5 ARG NE N 15 98.00 0.125 . 1 . . . . . . . . 5227 1 50 . 1 1 6 6 LYS H H 1 7.862 0.060 . 1 . . . . . . . . 5227 1 51 . 1 1 6 6 LYS HA H 1 4.083 0.026 . 1 . . . . . . . . 5227 1 52 . 1 1 6 6 LYS HB2 H 1 2.000 0.031 . 2 . . . . . . . . 5227 1 53 . 1 1 6 6 LYS HB3 H 1 1.759 0.028 . 2 . . . . . . . . 5227 1 54 . 1 1 6 6 LYS HG2 H 1 1.666 0.032 . 2 . . . . . . . . 5227 1 55 . 1 1 6 6 LYS HG3 H 1 1.449 0.031 . 2 . . . . . . . . 5227 1 56 . 1 1 6 6 LYS HD2 H 1 1.671 0.032 . 2 . . . . . . . . 5227 1 57 . 1 1 6 6 LYS HD3 H 1 1.572 0.030 . 2 . . . . . . . . 5227 1 58 . 1 1 6 6 LYS HE2 H 1 2.899 0.030 . 2 . . . . . . . . 5227 1 59 . 1 1 6 6 LYS C C 13 180.38 0.100 . 1 . . . . . . . . 5227 1 60 . 1 1 6 6 LYS CA C 13 60.17 0.043 . 1 . . . . . . . . 5227 1 61 . 1 1 6 6 LYS CB C 13 33.10 0.036 . 1 . . . . . . . . 5227 1 62 . 1 1 6 6 LYS CG C 13 26.07 0.041 . 1 . . . . . . . . 5227 1 63 . 1 1 6 6 LYS CD C 13 29.49 0.040 . 1 . . . . . . . . 5227 1 64 . 1 1 6 6 LYS CE C 13 42.15 0.041 . 1 . . . . . . . . 5227 1 65 . 1 1 6 6 LYS N N 15 119.09 0.125 . 1 . . . . . . . . 5227 1 66 . 1 1 7 7 TRP H H 1 8.190 0.060 . 1 . . . . . . . . 5227 1 67 . 1 1 7 7 TRP HA H 1 4.147 0.031 . 1 . . . . . . . . 5227 1 68 . 1 1 7 7 TRP HB2 H 1 3.574 0.032 . 2 . . . . . . . . 5227 1 69 . 1 1 7 7 TRP HB3 H 1 2.998 0.032 . 2 . . . . . . . . 5227 1 70 . 1 1 7 7 TRP HE1 H 1 10.304 0.080 . 1 . . . . . . . . 5227 1 71 . 1 1 7 7 TRP C C 13 178.57 0.100 . 1 . . . . . . . . 5227 1 72 . 1 1 7 7 TRP CA C 13 61.25 0.044 . 1 . . . . . . . . 5227 1 73 . 1 1 7 7 TRP CB C 13 30.06 0.067 . 1 . . . . . . . . 5227 1 74 . 1 1 7 7 TRP N N 15 121.22 0.125 . 1 . . . . . . . . 5227 1 75 . 1 1 7 7 TRP NE1 N 15 128.00 0.125 . 1 . . . . . . . . 5227 1 76 . 1 1 8 8 GLN H H 1 8.26 0.060 . 1 . . . . . . . . 5227 1 77 . 1 1 8 8 GLN HA H 1 3.848 0.030 . 1 . . . . . . . . 5227 1 78 . 1 1 8 8 GLN HB2 H 1 2.155 0.029 . 2 . . . . . . . . 5227 1 79 . 1 1 8 8 GLN HB3 H 1 1.830 0.024 . 2 . . . . . . . . 5227 1 80 . 1 1 8 8 GLN HG2 H 1 2.559 0.033 . 2 . . . . . . . . 5227 1 81 . 1 1 8 8 GLN HG3 H 1 2.416 0.032 . 2 . . . . . . . . 5227 1 82 . 1 1 8 8 GLN HE21 H 1 7.214 0.060 . 2 . . . . . . . . 5227 1 83 . 1 1 8 8 GLN HE22 H 1 6.724 0.060 . 2 . . . . . . . . 5227 1 84 . 1 1 8 8 GLN C C 13 177.26 0.100 . 1 . . . . . . . . 5227 1 85 . 1 1 8 8 GLN CA C 13 59.05 0.043 . 1 . . . . . . . . 5227 1 86 . 1 1 8 8 GLN CB C 13 28.13 0.041 . 1 . . . . . . . . 5227 1 87 . 1 1 8 8 GLN CG C 13 34.31 0.041 . 1 . . . . . . . . 5227 1 88 . 1 1 8 8 GLN N N 15 117.00 0.125 . 1 . . . . . . . . 5227 1 89 . 1 1 8 8 GLN NE2 N 15 110.62 0.125 . 1 . . . . . . . . 5227 1 90 . 1 1 9 9 LYS H H 1 8.495 0.060 . 1 . . . . . . . . 5227 1 91 . 1 1 9 9 LYS HA H 1 4.129 0.026 . 1 . . . . . . . . 5227 1 92 . 1 1 9 9 LYS HB2 H 1 2.035 0.029 . 2 . . . . . . . . 5227 1 93 . 1 1 9 9 LYS HB3 H 1 1.991 0.018 . 2 . . . . . . . . 5227 1 94 . 1 1 9 9 LYS HG2 H 1 1.557 0.029 . 2 . . . . . . . . 5227 1 95 . 1 1 9 9 LYS HG3 H 1 1.399 0.029 . 2 . . . . . . . . 5227 1 96 . 1 1 9 9 LYS HD2 H 1 1.733 0.032 . 2 . . . . . . . . 5227 1 97 . 1 1 9 9 LYS HE2 H 1 2.858 0.031 . 2 . . . . . . . . 5227 1 98 . 1 1 9 9 LYS HE3 H 1 2.802 0.030 . 2 . . . . . . . . 5227 1 99 . 1 1 9 9 LYS C C 13 177.73 0.100 . 1 . . . . . . . . 5227 1 100 . 1 1 9 9 LYS CA C 13 60.17 0.043 . 1 . . . . . . . . 5227 1 101 . 1 1 9 9 LYS CB C 13 32.87 0.041 . 1 . . . . . . . . 5227 1 102 . 1 1 9 9 LYS CG C 13 24.67 0.040 . 1 . . . . . . . . 5227 1 103 . 1 1 9 9 LYS CD C 13 30.42 0.041 . 1 . . . . . . . . 5227 1 104 . 1 1 9 9 LYS CE C 13 41.92 0.041 . 1 . . . . . . . . 5227 1 105 . 1 1 9 9 LYS N N 15 118.50 0.125 . 1 . . . . . . . . 5227 1 106 . 1 1 10 10 THR H H 1 7.495 0.060 . 1 . . . . . . . . 5227 1 107 . 1 1 10 10 THR HA H 1 3.872 0.031 . 1 . . . . . . . . 5227 1 108 . 1 1 10 10 THR HB H 1 4.208 0.028 . 1 . . . . . . . . 5227 1 109 . 1 1 10 10 THR HG21 H 1 1.285 0.026 . 1 . . . . . . . . 5227 1 110 . 1 1 10 10 THR HG22 H 1 1.285 0.026 . 1 . . . . . . . . 5227 1 111 . 1 1 10 10 THR HG23 H 1 1.285 0.026 . 1 . . . . . . . . 5227 1 112 . 1 1 10 10 THR C C 13 176.92 0.100 . 1 . . . . . . . . 5227 1 113 . 1 1 10 10 THR CA C 13 66.97 0.041 . 1 . . . . . . . . 5227 1 114 . 1 1 10 10 THR CB C 13 68.64 0.040 . 1 . . . . . . . . 5227 1 115 . 1 1 10 10 THR CG2 C 13 22.34 0.039 . 1 . . . . . . . . 5227 1 116 . 1 1 10 10 THR N N 15 113.10 0.125 . 1 . . . . . . . . 5227 1 117 . 1 1 11 11 GLY H H 1 8.992 0.060 . 1 . . . . . . . . 5227 1 118 . 1 1 11 11 GLY HA2 H 1 4.182 0.032 . 2 . . . . . . . . 5227 1 119 . 1 1 11 11 GLY HA3 H 1 3.918 0.018 . 2 . . . . . . . . 5227 1 120 . 1 1 11 11 GLY C C 13 176.38 0.100 . 1 . . . . . . . . 5227 1 121 . 1 1 11 11 GLY CA C 13 48.10 0.044 . 1 . . . . . . . . 5227 1 122 . 1 1 11 11 GLY N N 15 110.24 0.125 . 1 . . . . . . . . 5227 1 123 . 1 1 12 12 HIS H H 1 8.947 0.060 . 1 . . . . . . . . 5227 1 124 . 1 1 12 12 HIS HA H 1 4.838 0.077 . 1 . . . . . . . . 5227 1 125 . 1 1 12 12 HIS HB2 H 1 3.655 0.030 . 2 . . . . . . . . 5227 1 126 . 1 1 12 12 HIS HB3 H 1 3.127 0.030 . 2 . . . . . . . . 5227 1 127 . 1 1 12 12 HIS C C 13 178.48 0.100 . 1 . . . . . . . . 5227 1 128 . 1 1 12 12 HIS CA C 13 58.74 0.071 . 1 . . . . . . . . 5227 1 129 . 1 1 12 12 HIS CB C 13 31.12 0.049 . 1 . . . . . . . . 5227 1 130 . 1 1 12 12 HIS N N 15 119.74 0.125 . 1 . . . . . . . . 5227 1 131 . 1 1 13 13 ALA H H 1 8.018 0.060 . 1 . . . . . . . . 5227 1 132 . 1 1 13 13 ALA HA H 1 4.554 0.031 . 1 . . . . . . . . 5227 1 133 . 1 1 13 13 ALA HB1 H 1 1.745 0.029 . 1 . . . . . . . . 5227 1 134 . 1 1 13 13 ALA HB2 H 1 1.745 0.029 . 1 . . . . . . . . 5227 1 135 . 1 1 13 13 ALA HB3 H 1 1.745 0.029 . 1 . . . . . . . . 5227 1 136 . 1 1 13 13 ALA C C 13 178.85 0.100 . 1 . . . . . . . . 5227 1 137 . 1 1 13 13 ALA CA C 13 56.25 0.043 . 1 . . . . . . . . 5227 1 138 . 1 1 13 13 ALA CB C 13 19.08 0.042 . 1 . . . . . . . . 5227 1 139 . 1 1 13 13 ALA N N 15 121.09 0.125 . 1 . . . . . . . . 5227 1 140 . 1 1 14 14 VAL H H 1 8.436 0.060 . 1 . . . . . . . . 5227 1 141 . 1 1 14 14 VAL HA H 1 3.754 0.032 . 1 . . . . . . . . 5227 1 142 . 1 1 14 14 VAL HB H 1 2.468 0.033 . 1 . . . . . . . . 5227 1 143 . 1 1 14 14 VAL HG11 H 1 1.232 0.028 . 2 . . . . . . . . 5227 1 144 . 1 1 14 14 VAL HG12 H 1 1.232 0.028 . 2 . . . . . . . . 5227 1 145 . 1 1 14 14 VAL HG13 H 1 1.232 0.028 . 2 . . . . . . . . 5227 1 146 . 1 1 14 14 VAL HG21 H 1 1.109 0.027 . 2 . . . . . . . . 5227 1 147 . 1 1 14 14 VAL HG22 H 1 1.109 0.027 . 2 . . . . . . . . 5227 1 148 . 1 1 14 14 VAL HG23 H 1 1.109 0.027 . 2 . . . . . . . . 5227 1 149 . 1 1 14 14 VAL C C 13 179.78 0.100 . 1 . . . . . . . . 5227 1 150 . 1 1 14 14 VAL CA C 13 67.362 0.041 . 1 . . . . . . . . 5227 1 151 . 1 1 14 14 VAL CB C 13 32.168 0.039 . 1 . . . . . . . . 5227 1 152 . 1 1 14 14 VAL CG1 C 13 22.843 0.041 . 2 . . . . . . . . 5227 1 153 . 1 1 14 14 VAL CG2 C 13 23.191 0.041 . 2 . . . . . . . . 5227 1 154 . 1 1 14 14 VAL N N 15 116.25 0.125 . 1 . . . . . . . . 5227 1 155 . 1 1 15 15 ARG H H 1 8.972 0.060 . 1 . . . . . . . . 5227 1 156 . 1 1 15 15 ARG HA H 1 4.431 0.033 . 1 . . . . . . . . 5227 1 157 . 1 1 15 15 ARG HB2 H 1 2.155 0.030 . 2 . . . . . . . . 5227 1 158 . 1 1 15 15 ARG HB3 H 1 1.967 0.026 . 2 . . . . . . . . 5227 1 159 . 1 1 15 15 ARG HG2 H 1 2.281 0.032 . 2 . . . . . . . . 5227 1 160 . 1 1 15 15 ARG HG3 H 1 1.557 0.034 . 2 . . . . . . . . 5227 1 161 . 1 1 15 15 ARG HD2 H 1 3.344 0.028 . 2 . . . . . . . . 5227 1 162 . 1 1 15 15 ARG HD3 H 1 3.233 0.031 . 2 . . . . . . . . 5227 1 163 . 1 1 15 15 ARG HE H 1 8.031 0.060 . 1 . . . . . . . . 5227 1 164 . 1 1 15 15 ARG C C 13 178.99 0.100 . 1 . . . . . . . . 5227 1 165 . 1 1 15 15 ARG CA C 13 59.63 0.043 . 1 . . . . . . . . 5227 1 166 . 1 1 15 15 ARG CB C 13 30.38 0.042 . 1 . . . . . . . . 5227 1 167 . 1 1 15 15 ARG CG C 13 29.22 0.041 . 1 . . . . . . . . 5227 1 168 . 1 1 15 15 ARG CD C 13 43.63 0.039 . 1 . . . . . . . . 5227 1 169 . 1 1 15 15 ARG CZ C 13 160.42 0.100 . 1 . . . . . . . . 5227 1 170 . 1 1 15 15 ARG N N 15 120.83 0.125 . 1 . . . . . . . . 5227 1 171 . 1 1 15 15 ARG NE N 15 96.867 0.125 . 1 . . . . . . . . 5227 1 172 . 1 1 16 16 ALA H H 1 8.666 0.060 . 1 . . . . . . . . 5227 1 173 . 1 1 16 16 ALA HA H 1 3.986 0.032 . 1 . . . . . . . . 5227 1 174 . 1 1 16 16 ALA HB1 H 1 1.748 0.030 . 1 . . . . . . . . 5227 1 175 . 1 1 16 16 ALA HB2 H 1 1.748 0.030 . 1 . . . . . . . . 5227 1 176 . 1 1 16 16 ALA HB3 H 1 1.748 0.030 . 1 . . . . . . . . 5227 1 177 . 1 1 16 16 ALA C C 13 179.32 0.100 . 1 . . . . . . . . 5227 1 178 . 1 1 16 16 ALA CA C 13 55.98 0.041 . 1 . . . . . . . . 5227 1 179 . 1 1 16 16 ALA CB C 13 18.77 0.042 . 1 . . . . . . . . 5227 1 180 . 1 1 16 16 ALA N N 15 122.65 0.125 . 1 . . . . . . . . 5227 1 181 . 1 1 17 17 ILE H H 1 7.714 0.060 . 1 . . . . . . . . 5227 1 182 . 1 1 17 17 ILE HA H 1 3.716 0.033 . 1 . . . . . . . . 5227 1 183 . 1 1 17 17 ILE HB H 1 2.263 0.032 . 1 . . . . . . . . 5227 1 184 . 1 1 17 17 ILE HG12 H 1 2.055 0.030 . 2 . . . . . . . . 5227 1 185 . 1 1 17 17 ILE HG13 H 1 1.422 0.032 . 2 . . . . . . . . 5227 1 186 . 1 1 17 17 ILE HG21 H 1 1.030 0.026 . 1 . . . . . . . . 5227 1 187 . 1 1 17 17 ILE HG22 H 1 1.030 0.026 . 1 . . . . . . . . 5227 1 188 . 1 1 17 17 ILE HG23 H 1 1.030 0.026 . 1 . . . . . . . . 5227 1 189 . 1 1 17 17 ILE HD11 H 1 0.933 0.029 . 1 . . . . . . . . 5227 1 190 . 1 1 17 17 ILE HD12 H 1 0.933 0.029 . 1 . . . . . . . . 5227 1 191 . 1 1 17 17 ILE HD13 H 1 0.933 0.029 . 1 . . . . . . . . 5227 1 192 . 1 1 17 17 ILE C C 13 179.13 0.100 . 1 . . . . . . . . 5227 1 193 . 1 1 17 17 ILE CA C 13 65.11 0.041 . 1 . . . . . . . . 5227 1 194 . 1 1 17 17 ILE CB C 13 37.61 0.039 . 1 . . . . . . . . 5227 1 195 . 1 1 17 17 ILE CG1 C 13 28.94 0.041 . 1 . . . . . . . . 5227 1 196 . 1 1 17 17 ILE CG2 C 13 17.56 0.041 . 1 . . . . . . . . 5227 1 197 . 1 1 17 17 ILE CD1 C 13 13.76 0.041 . 1 . . . . . . . . 5227 1 198 . 1 1 17 17 ILE N N 15 115.41 0.125 . 1 . . . . . . . . 5227 1 199 . 1 1 18 18 GLY H H 1 7.835 0.060 . 1 . . . . . . . . 5227 1 200 . 1 1 18 18 GLY HA2 H 1 4.110 0.028 . 2 . . . . . . . . 5227 1 201 . 1 1 18 18 GLY HA3 H 1 4.015 0.031 . 2 . . . . . . . . 5227 1 202 . 1 1 18 18 GLY C C 13 176.29 0.100 . 1 . . . . . . . . 5227 1 203 . 1 1 18 18 GLY CA C 13 47.23 0.045 . 1 . . . . . . . . 5227 1 204 . 1 1 18 18 GLY N N 15 108.24 0.125 . 1 . . . . . . . . 5227 1 205 . 1 1 19 19 ARG H H 1 8.300 0.060 . 1 . . . . . . . . 5227 1 206 . 1 1 19 19 ARG HA H 1 4.305 0.030 . 1 . . . . . . . . 5227 1 207 . 1 1 19 19 ARG HB2 H 1 2.002 0.033 . 2 . . . . . . . . 5227 1 208 . 1 1 19 19 ARG HB3 H 1 1.759 0.033 . 2 . . . . . . . . 5227 1 209 . 1 1 19 19 ARG HG2 H 1 2.020 0.033 . 2 . . . . . . . . 5227 1 210 . 1 1 19 19 ARG HG3 H 1 1.625 0.033 . 2 . . . . . . . . 5227 1 211 . 1 1 19 19 ARG HD2 H 1 3.078 0.033 . 2 . . . . . . . . 5227 1 212 . 1 1 19 19 ARG HD3 H 1 2.984 0.033 . 2 . . . . . . . . 5227 1 213 . 1 1 19 19 ARG HE H 1 9.102 0.060 . 1 . . . . . . . . 5227 1 214 . 1 1 19 19 ARG C C 13 178.10 0.100 . 1 . . . . . . . . 5227 1 215 . 1 1 19 19 ARG CA C 13 58.97 0.045 . 1 . . . . . . . . 5227 1 216 . 1 1 19 19 ARG CB C 13 30.56 0.046 . 1 . . . . . . . . 5227 1 217 . 1 1 19 19 ARG CG C 13 28.98 0.043 . 1 . . . . . . . . 5227 1 218 . 1 1 19 19 ARG CD C 13 44.21 0.043 . 1 . . . . . . . . 5227 1 219 . 1 1 19 19 ARG CZ C 13 159.43 0.100 . 1 . . . . . . . . 5227 1 220 . 1 1 19 19 ARG N N 15 121.49 0.125 . 1 . . . . . . . . 5227 1 221 . 1 1 19 19 ARG NE N 15 85.98 0.125 . 1 . . . . . . . . 5227 1 222 . 1 1 20 20 LEU H H 1 7.884 0.060 . 1 . . . . . . . . 5227 1 223 . 1 1 20 20 LEU HA H 1 4.247 0.032 . 1 . . . . . . . . 5227 1 224 . 1 1 20 20 LEU HB2 H 1 1.906 0.029 . 2 . . . . . . . . 5227 1 225 . 1 1 20 20 LEU HB3 H 1 1.493 0.030 . 2 . . . . . . . . 5227 1 226 . 1 1 20 20 LEU HG H 1 1.841 0.028 . 1 . . . . . . . . 5227 1 227 . 1 1 20 20 LEU HD11 H 1 0.807 0.027 . 2 . . . . . . . . 5227 1 228 . 1 1 20 20 LEU HD12 H 1 0.807 0.027 . 2 . . . . . . . . 5227 1 229 . 1 1 20 20 LEU HD13 H 1 0.807 0.027 . 2 . . . . . . . . 5227 1 230 . 1 1 20 20 LEU HD21 H 1 0.696 0.028 . 2 . . . . . . . . 5227 1 231 . 1 1 20 20 LEU HD22 H 1 0.696 0.028 . 2 . . . . . . . . 5227 1 232 . 1 1 20 20 LEU HD23 H 1 0.696 0.028 . 2 . . . . . . . . 5227 1 233 . 1 1 20 20 LEU C C 13 176.66 0.100 . 1 . . . . . . . . 5227 1 234 . 1 1 20 20 LEU CA C 13 56.07 0.043 . 1 . . . . . . . . 5227 1 235 . 1 1 20 20 LEU CB C 13 44.13 0.042 . 1 . . . . . . . . 5227 1 236 . 1 1 20 20 LEU CG C 13 26.88 0.040 . 1 . . . . . . . . 5227 1 237 . 1 1 20 20 LEU CD1 C 13 24.71 0.041 . 2 . . . . . . . . 5227 1 238 . 1 1 20 20 LEU CD2 C 13 26.03 0.040 . 2 . . . . . . . . 5227 1 239 . 1 1 20 20 LEU N N 15 119.90 0.125 . 1 . . . . . . . . 5227 1 240 . 1 1 21 21 SER H H 1 7.557 0.060 . 1 . . . . . . . . 5227 1 241 . 1 1 21 21 SER HA H 1 4.383 0.029 . 1 . . . . . . . . 5227 1 242 . 1 1 21 21 SER HB2 H 1 4.045 0.032 . 2 . . . . . . . . 5227 1 243 . 1 1 21 21 SER HB3 H 1 3.902 0.032 . 2 . . . . . . . . 5227 1 244 . 1 1 21 21 SER C C 13 178.88 0.100 . 1 . . . . . . . . 5227 1 245 . 1 1 21 21 SER CA C 13 59.85 0.042 . 1 . . . . . . . . 5227 1 246 . 1 1 21 21 SER CB C 13 65.72 0.041 . 1 . . . . . . . . 5227 1 247 . 1 1 21 21 SER N N 15 117.68 0.125 . 1 . . . . . . . . 5227 1 stop_ save_