data_15185 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 15185 _Entry.Title ; backbone and side chain methly order parameters and correlation times for calmodulin in complex with the eNOS peptide ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2007-03-19 _Entry.Accession_date 2007-03-19 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version . _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Kendra Frederick . K. . 15185 2 Michael Marlow . S. . 15185 3 Kathleen Valentine . G. . 15185 4 Joshua Wand . . . 15185 stop_ loop_ _Entry_src.ID _Entry_src.Project_name _Entry_src.Organization_full_name _Entry_src.Organization_initials _Entry_src.Entry_ID 1 . 'Wand group, University of Pennsylvania' . 15185 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID order_parameters 2 15185 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID 'order parameters' 195 15185 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 3 . . 2011-03-28 2007-03-28 update BMRB ; tags for Tau f and s units added atom nomenclature for THR residues corrected in methyl side chain order parameter save frame ; 15185 2 . . 2009-02-03 2007-03-19 update BMRB 'correction of residue codes' 15185 1 . . 2007-10-05 2007-03-19 original author 'original release' 15185 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 15183 CaM/CaMKKap 15185 BMRB 15184 CaM/CaMK1p 15185 BMRB 15186 Cam/smMLCKp 15185 BMRB 15187 CaM/PDEs 15185 BMRB 15188 calmodulin 15185 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 15185 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 17637663 _Citation.Full_citation . _Citation.Title 'Conformational entropy in molecular recognition by proteins' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Nature _Citation.Journal_name_full . _Citation.Journal_volume 448 _Citation.Journal_issue 7151 _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 325 _Citation.Page_last 329 _Citation.Year 2007 _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 Kendra Frederick . K. . 15185 1 2 Michael Marlow . S. . 15185 1 3 Kathleen Valentine . G. . 15185 1 4 Joshua Wand . . . 15185 1 stop_ save_ save_entry_citation_2 _Citation.Sf_category citations _Citation.Sf_framecode entry_citation_2 _Citation.Entry_ID 15185 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title 'Characterization of the backbone and side chain dynamics of the CaM:eNOSp complex reveals microscopic contributions to protein conformational entropy' _Citation.Status 'in preparation' _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Kendra Frederick . K. . 15185 2 2 Nicholas Warischalk . . . 15185 2 3 Kathleen Valentine . G. . 15185 2 4 Joshua Wand . . . 15185 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 15185 _Assembly.ID 1 _Assembly.Name CaM/eNOSp _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 . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 calmodulin 1 $calmodulin A . yes native no no . . . 15185 1 2 eNOSp 2 $eNOSp A . no native no no . . . 15185 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID yes PDB 1NIW . . X-ray 2.05 . . 15185 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_calmodulin _Entity.Sf_category entity _Entity.Sf_framecode calmodulin _Entity.Entry_ID 15185 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name calmodulin _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 no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 148 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-26 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 15184 . calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 2 no BMRB 15186 . calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 3 no BMRB 15187 . calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 4 no BMRB 15188 . calmodulin . . . . . 100.00 148 99.32 100.00 9.77e-100 . . . . 15185 1 5 no BMRB 15191 . Calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 6 no BMRB 15470 . calmodulin . . . . . 100.00 148 99.32 100.00 2.01e-99 . . . . 15185 1 7 no BMRB 15624 . Calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 8 no BMRB 15650 . calmodulin . . . . . 100.00 148 99.32 100.00 3.32e-99 . . . . 15185 1 9 no BMRB 15852 . calmodulin . . . . . 100.00 148 99.32 100.00 3.32e-99 . . . . 15185 1 10 no BMRB 1634 . calmodulin . . . . . 100.00 148 97.30 99.32 2.54e-97 . . . . 15185 1 11 no BMRB 16418 . apoCaM . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 12 no BMRB 16465 . entity_1 . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 13 no BMRB 1648 . calmodulin . . . . . 100.00 148 97.30 99.32 2.54e-97 . . . . 15185 1 14 no BMRB 16764 . CALMODULIN . . . . . 100.00 150 100.00 100.00 5.25e-100 . . . . 15185 1 15 no BMRB 17264 . calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 16 no BMRB 17360 . entity_1 . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 17 no BMRB 17771 . Calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 18 no BMRB 17807 . Calmodulin . . . . . 99.32 147 100.00 100.00 2.55e-99 . . . . 15185 1 19 no BMRB 18027 . CaM . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 20 no BMRB 18028 . CaM . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 21 no BMRB 18556 . Calmodulin . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 15185 1 22 no BMRB 19036 . calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 23 no BMRB 19238 . Calmodulin_prototypical_calcium_sensor . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 24 no BMRB 19586 . entity_1 . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 25 no BMRB 19604 . calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 26 no BMRB 25253 . CaM . . . . . 100.00 148 98.65 99.32 1.22e-97 . . . . 15185 1 27 no BMRB 25257 . CaM . . . . . 100.00 148 98.65 99.32 1.22e-97 . . . . 15185 1 28 no BMRB 26503 . Calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 29 no BMRB 26626 . CaM . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 30 no BMRB 26627 . CaM . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 31 no BMRB 4056 . calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 32 no BMRB 4270 . calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 33 no BMRB 4284 . Calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 34 no BMRB 4310 . calmodulin . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 35 no PDB 1A29 . "Calmodulin Complexed With Trifluoperazine (1:2 Complex)" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 36 no PDB 1CFC . "Calcium-Free Calmodulin" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 37 no PDB 1CFD . "Calcium-Free Calmodulin" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 38 no PDB 1CFF . "Nmr Solution Structure Of A Complex Of Calmodulin With A Binding Peptide Of The Ca2+-Pump" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 39 no PDB 1CKK . "CalmodulinRAT CA2+CALMODULIN DEPENDENT PROTEIN KINASE Fragment" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 40 no PDB 1CLL . "Calmodulin Structure Refined At 1.7 Angstroms Resolution" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 41 no PDB 1CM1 . "Motions Of Calmodulin-Single-Conformer Refinement" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 42 no PDB 1CM4 . "Motions Of Calmodulin-four-conformer Refinement" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 43 no PDB 1CTR . "Drug Binding By Calmodulin: Crystal Structure Of A Calmodulin-Trifluoperazine Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 44 no PDB 1DMO . "Calmodulin, Nmr, 30 Structures" . . . . . 100.00 148 99.32 100.00 2.01e-99 . . . . 15185 1 45 no PDB 1G4Y . "1.60 A Crystal Structure Of The Gating Domain From Small Conductance Potassium Channel Complexed With Calcium-Calmodulin" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 46 no PDB 1IQ5 . "CalmodulinNEMATODE CA2+CALMODULIN DEPENDENT KINASE KINASE Fragment" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 47 no PDB 1IWQ . "Crystal Structure Of Marcks Calmodulin Binding Domain Peptide Complexed With Ca2+CALMODULIN" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 48 no PDB 1K90 . "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3' Deoxy-Atp" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 49 no PDB 1K93 . "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin" . . . . . 97.30 144 100.00 100.00 4.42e-97 . . . . 15185 1 50 no PDB 1L7Z . "Crystal Structure Of Ca2+/calmodulin Complexed With Myristoylated Cap-23/nap-22 Peptide" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 51 no PDB 1LIN . "Calmodulin Complexed With Trifluoperazine (1:4 Complex)" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 52 no PDB 1LVC . "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 2' Deoxy, 3' Anthr" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 53 no PDB 1MUX . "Solution Nmr Structure Of CalmodulinW-7 Complex: The Basis Of Diversity In Molecular Recognition, 30 Structures" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 54 no PDB 1MXE . "Structure Of The Complex Of Calmodulin With The Target Sequence Of Camki" . . . . . 100.00 148 97.97 99.32 6.77e-98 . . . . 15185 1 55 no PDB 1NWD . "Solution Structure Of Ca2+CALMODULIN BOUND TO THE C- Terminal Domain Of Petunia Glutamate Decarboxylase" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 56 no PDB 1OOJ . "Structural Genomics Of Caenorhabditis Elegans : Calmodulin" . . . . . 100.00 149 97.97 98.65 1.28e-97 . . . . 15185 1 57 no PDB 1PRW . "Crystal Structure Of Bovine Brain Ca++ Calmodulin In A Compact Form" . . . . . 100.00 149 99.32 99.32 4.27e-99 . . . . 15185 1 58 no PDB 1QIV . "Calmodulin Complexed With N-(3,3,-Diphenylpropyl)-N'-[1-R-( 3,4-Bis-Butoxyphenyl)-Ethyl]-Propylenediamine (Dpd), 1:2 Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 59 no PDB 1QIW . "Calmodulin Complexed With N-(3,3,-Diphenylpropyl)-N'-[1-R-( 3,4-Bis-Butoxyphenyl)-Ethyl]-Propylenediamine (Dpd)" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 60 no PDB 1QX5 . "Crystal Structure Of Apocalmodulin" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 61 no PDB 1S26 . "Structure Of Anthrax Edema Factor-calmodulin-alpha,beta- Methyleneadenosine 5'-triphosphate Complex Reveals An Alternative Mode" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 62 no PDB 1SK6 . "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin, 3',5' Cyclic Amp (Cam" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 63 no PDB 1SY9 . "Structure Of Calmodulin Complexed With A Fragment Of The Olfactory Cng Channel" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 64 no PDB 1UP5 . "Chicken Calmodulin" . . . . . 100.00 148 99.32 99.32 4.13e-99 . . . . 15185 1 65 no PDB 1WRZ . "Calmodulin Complexed With A Peptide From A Human Death-Associated Protein Kinase" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 66 no PDB 1X02 . "Solution Structure Of Stereo Array Isotope Labeled (Sail) Calmodulin" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 67 no PDB 1XA5 . "Structure Of Calmodulin In Complex With Kar-2, A Bis-Indol Alkaloid" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 68 no PDB 1XFU . "Crystal Structure Of Anthrax Edema Factor (ef) Truncation Mutant, Ef-delta 64 In Complex With Calmodulin" . . . . . 100.00 149 99.32 100.00 1.22e-99 . . . . 15185 1 69 no PDB 1XFV . "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3' Deoxy-Atp" . . . . . 100.00 149 99.32 100.00 1.22e-99 . . . . 15185 1 70 no PDB 1XFW . "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3'5' Cyclic Amp (Camp)" . . . . . 100.00 149 99.32 100.00 1.22e-99 . . . . 15185 1 71 no PDB 1XFY . "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin" . . . . . 100.00 149 99.32 100.00 1.22e-99 . . . . 15185 1 72 no PDB 1XFZ . "Crystal Structure Of Anthrax Edema Factor (ef) In Complex With Calmodulin In The Presence Of 1 Millimolar Exogenously Added Cal" . . . . . 100.00 149 99.32 100.00 1.22e-99 . . . . 15185 1 73 no PDB 1Y0V . "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And Pyrophosphate" . . . . . 97.30 146 100.00 100.00 3.80e-97 . . . . 15185 1 74 no PDB 1YR5 . "1.7-A Structure Of Calmodulin Bound To A Peptide From Dap Kinase" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 75 no PDB 2BBM . "Solution Structure Of A Calmodulin-Target Peptide Complex By Multidimensional Nmr" . . . . . 100.00 148 97.97 99.32 6.77e-98 . . . . 15185 1 76 no PDB 2BBN . "Solution Structure Of A Calmodulin-Target Peptide Complex By Multidimensional Nmr" . . . . . 100.00 148 97.97 99.32 6.77e-98 . . . . 15185 1 77 no PDB 2BCX . "Crystal Structure Of Calmodulin In Complex With A Ryanodine Receptor Peptide" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 78 no PDB 2BKH . "Myosin Vi Nucleotide-Free (Mdinsert2) Crystal Structure" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 15185 1 79 no PDB 2BKI . "Myosin Vi Nucleotide-free (mdinsert2-iq) Crystal Structure" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 80 no PDB 2DFS . "3-D Structure Of Myosin-V Inhibited State" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 81 no PDB 2F2O . "Structure Of Calmodulin Bound To A Calcineurin Peptide: A New Way Of Making An Old Binding Mode" . . . . . 100.00 179 100.00 100.00 7.91e-100 . . . . 15185 1 82 no PDB 2F2P . "Structure Of Calmodulin Bound To A Calcineurin Peptide: A New Way Of Making An Old Binding Mode" . . . . . 100.00 179 100.00 100.00 7.91e-100 . . . . 15185 1 83 no PDB 2F3Y . "CalmodulinIQ DOMAIN COMPLEX" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 84 no PDB 2F3Z . "CalmodulinIQ-Aa Domain Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 85 no PDB 2FOT . "Crystal Structure Of The Complex Between Calmodulin And Alphaii-Spectrin" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 86 no PDB 2HQW . "Crystal Structure Of Ca2+CALMODULIN BOUND TO NMDA RECEPTOR NR1C1 Peptide" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 87 no PDB 2JZI . "Structure Of Calmodulin Complexed With The Calmodulin Binding Domain Of Calcineurin" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 88 no PDB 2K0E . "A Coupled Equilibrium Shift Mechanism In Calmodulin- Mediated Signal Transduction" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 89 no PDB 2K0F . "Calmodulin Complexed With Calmodulin-Binding Peptide From Smooth Muscle Myosin Light Chain Kinase" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 90 no PDB 2K0J . "Solution Structure Of Cam Complexed To Drp1p" . . . . . 100.00 148 99.32 100.00 3.32e-99 . . . . 15185 1 91 no PDB 2K61 . "Solution Structure Of Cam Complexed To Dapk Peptide" . . . . . 100.00 148 99.32 100.00 3.32e-99 . . . . 15185 1 92 no PDB 2KDU . "Structural Basis Of The Munc13-1CA2+-Calmodulin Interaction: A Novel 1-26 Calmodulin Binding Motif With A Bipartite Binding Mod" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 93 no PDB 2KNE . "Calmodulin Wraps Around Its Binding Domain In The Plasma Membrane Ca2+ Pump Anchored By A Novel 18-1 Motif" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 94 no PDB 2L53 . "Solution Nmr Structure Of Apo-Calmodulin In Complex With The Iq Motif Of Human Cardiac Sodium Channel Nav1.5" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 95 no PDB 2L7L . "Solution Structure Of Ca2+CALMODULIN COMPLEXED WITH A PEPTIDE Representing The Calmodulin-Binding Domain Of Calmodulin Kinase I" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 96 no PDB 2LGF . "Solution Structure Of Ca2+CALMODULIN COMPLEXED WITH A PEPTIDE Representing The Calmodulin-Binding Domain Of L-Selectin" . . . . . 98.65 146 100.00 100.00 1.07e-98 . . . . 15185 1 97 no PDB 2LL6 . "Solution Nmr Structure Of Cam Bound To Inos Cam Binding Domain Peptide" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 98 no PDB 2LL7 . "Solution Nmr Structure Of Cam Bound To The Enos Cam Binding Domain Peptide" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 99 no PDB 2LV6 . "The Complex Between Ca-calmodulin And Skeletal Muscle Myosin Light Chain Kinase From Combination Of Nmr And Aqueous And Contras" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 15185 1 100 no PDB 2M0J . "3d Structure Of Calmodulin And Calmodulin Binding Domain Of Olfactory Cyclic Nucleotide-gated Ion Channel Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 101 no PDB 2M0K . "3d Structure Of Calmodulin And Calmodulin Binding Domain Of Rat Olfactory Cyclic Nucleotide-gated Ion Channel" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 102 no PDB 2M55 . "Nmr Structure Of The Complex Of An N-terminally Acetylated Alpha- Synuclein Peptide With Calmodulin" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 103 no PDB 2MG5 . "Solution Structure Of Calmodulin Bound To The Target Peptide Of Endothelial Nitrogen Oxide Synthase Phosphorylated At Thr495" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 104 no PDB 2MGU . "Structure Of The Complex Between Calmodulin And The Binding Domain Of Hiv-1 Matrix Protein" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 105 no PDB 2O5G . "Calmodulin-Smooth Muscle Light Chain Kinase Peptide Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 106 no PDB 2O60 . "Calmodulin Bound To Peptide From Neuronal Nitric Oxide Synthase" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 107 no PDB 2R28 . "The Complex Structure Of Calmodulin Bound To A Calcineurin Peptide" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 108 no PDB 2V01 . "Recombinant Vertebrate Calmodulin Complexed With Pb" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 109 no PDB 2V02 . "Recombinant Vertebrate Calmodulin Complexed With Ba" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 110 no PDB 2VAS . "Myosin Vi (Md-Insert2-Cam, Delta-Insert1) Post-Rigor State" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 15185 1 111 no PDB 2VAY . "Calmodulin Complexed With Cav1.1 Iq Peptide" . . . . . 98.65 146 100.00 100.00 1.07e-98 . . . . 15185 1 112 no PDB 2VB6 . "Myosin Vi (Md-Insert2-Cam, Delta Insert1) Post-Rigor State ( Crystal Form 2)" . . . . . 100.00 149 97.30 99.32 1.25e-97 . . . . 15185 1 113 no PDB 2W73 . "High-Resolution Structure Of The Complex Between Calmodulin And A Peptide From Calcineurin A" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 114 no PDB 2WEL . "Crystal Structure Of Su6656-Bound CalciumCALMODULIN- Dependent Protein Kinase Ii Delta In Complex With Calmodulin" . . . . . 100.00 150 100.00 100.00 4.76e-100 . . . . 15185 1 115 no PDB 2X0G . "X-ray Structure Of A Dap-kinase Calmodulin Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 116 no PDB 2X51 . "M6 Delta Insert1" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 15185 1 117 no PDB 2Y4V . "Crystal Structure Of Human Calmodulin In Complex With A Dap Kinase-1 Mutant (W305y) Peptide" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 118 no PDB 2YGG . "Complex Of Cambr And Cam" . . . . . 100.00 150 100.00 100.00 5.60e-100 . . . . 15185 1 119 no PDB 3BXK . "Crystal Structure Of The PQ-Type Calcium Channel (Cav2.1) Iq Domain And Ca2+calmodulin Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 120 no PDB 3BXL . "Crystal Structure Of The R-Type Calcium Channel (Cav2.3) Iq Domain And Ca2+calmodulin Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 121 no PDB 3BYA . "Structure Of A Calmodulin Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 122 no PDB 3CLN . "Structure Of Calmodulin Refined At 2.2 Angstroms Resolution" . . . . . 100.00 148 99.32 100.00 2.01e-99 . . . . 15185 1 123 no PDB 3DVE . "Crystal Structure Of Ca2+CAM-Cav2.2 Iq Domain Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 124 no PDB 3DVJ . "Crystal Structure Of Ca2+CAM-Cav2.2 Iq Domain (Without Cloning Artifact, Hm To Tv) Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 125 no PDB 3DVK . "Crystal Structure Of Ca2+CAM-Cav2.3 Iq Domain Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 126 no PDB 3DVM . "Crystal Structure Of Ca2+CAM-Cav2.1 Iq Domain Complex" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 127 no PDB 3EK4 . "Calcium-saturated Gcamp2 Monomer" . . . . . 99.32 449 100.00 100.00 9.40e-96 . . . . 15185 1 128 no PDB 3EK7 . "Calcium-Saturated Gcamp2 Dimer" . . . . . 99.32 449 100.00 100.00 9.40e-96 . . . . 15185 1 129 no PDB 3EK8 . "Calcium-Saturated Gcamp2 T116vG87R MUTANT MONOMER" . . . . . 99.32 449 100.00 100.00 1.33e-95 . . . . 15185 1 130 no PDB 3EKH . "Calcium-Saturated Gcamp2 T116vK378W MUTANT MONOMER" . . . . . 99.32 449 99.32 99.32 9.09e-95 . . . . 15185 1 131 no PDB 3EVU . "Crystal Structure Of Calcium Bound Dimeric Gcamp2, (#1)" . . . . . 99.32 449 100.00 100.00 9.40e-96 . . . . 15185 1 132 no PDB 3EVV . "Crystal Structure Of Calcium Bound Dimeric Gcamp2 (#2)" . . . . . 99.32 449 100.00 100.00 9.40e-96 . . . . 15185 1 133 no PDB 3EWT . "Crystal Structure Of Calmodulin Complexed With A Peptide" . . . . . 100.00 154 100.00 100.00 2.06e-100 . . . . 15185 1 134 no PDB 3EWV . "Crystal Structure Of Calmodulin Complexed With A Peptide" . . . . . 100.00 154 100.00 100.00 2.06e-100 . . . . 15185 1 135 no PDB 3G43 . "Crystal Structure Of The Calmodulin-Bound Cav1.2 C-Terminal Regulatory Domain Dimer" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 136 no PDB 3GN4 . "Myosin Lever Arm" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 15185 1 137 no PDB 3GOF . "Calmodulin Bound To Peptide From Macrophage Nitric Oxide Synthase" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 138 no PDB 3HR4 . "Human Inos Reductase And Calmodulin Complex" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 139 no PDB 3IF7 . "Structure Of Calmodulin Complexed With Its First Endogenous Inhibitor, Sphingosylphosphorylcholine" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 140 no PDB 3J41 . "Pseudo-atomic Model Of The Aquaporin-0/calmodulin Complex Derived From Electron Microscopy" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 141 no PDB 3L9I . "Myosin Vi Nucleotide-Free (Mdinsert2) L310g Mutant Crystal Structure" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 15185 1 142 no PDB 3O77 . "The Structure Of Ca2+ Sensor (Case-16)" . . . . . 99.32 415 100.00 100.00 4.22e-96 . . . . 15185 1 143 no PDB 3O78 . "The Structure Of Ca2+ Sensor (Case-12)" . . . . . 99.32 415 100.00 100.00 4.65e-96 . . . . 15185 1 144 no PDB 3OXQ . "Crystal Structure Of Ca2+CAM-Cav1.2 Pre-IqIQ DOMAIN COMPLEX" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 145 no PDB 3SG2 . "Crystal Structure Of Gcamp2-t116v,d381y" . . . . . 99.32 449 99.32 99.32 1.34e-94 . . . . 15185 1 146 no PDB 3SG3 . "Crystal Structure Of Gcamp3-d380y" . . . . . 99.32 449 98.64 99.32 1.70e-93 . . . . 15185 1 147 no PDB 3SG4 . "Crystal Structure Of Gcamp3-d380y, Lp(linker 2)" . . . . . 100.00 448 97.97 98.65 1.17e-93 . . . . 15185 1 148 no PDB 3SG5 . "Crystal Structure Of Dimeric Gcamp3-d380y, Qp(linker 1), Lp(linker 2)" . . . . . 100.00 448 97.97 98.65 9.63e-94 . . . . 15185 1 149 no PDB 3SG6 . "Crystal Structure Of Dimeric Gcamp2-lia(linker 1)" . . . . . 99.32 450 100.00 100.00 1.20e-95 . . . . 15185 1 150 no PDB 3SG7 . "Crystal Structure Of Gcamp3-kf(linker 1)" . . . . . 99.32 448 99.32 100.00 8.02e-95 . . . . 15185 1 151 no PDB 3SJQ . "Crystal Structure Of A Small Conductance Potassium Channel Splice Variant Complexed With Calcium-Calmodulin" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 152 no PDB 3SUI . "Crystal Structure Of Ca2+-Calmodulin In Complex With A Trpv1 C- Terminal Peptide" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 153 no PDB 3U0K . "Crystal Structure Of The Genetically Encoded Calcium Indicator Rcamp" . . . . . 99.32 440 98.64 99.32 2.87e-94 . . . . 15185 1 154 no PDB 3WFN . "Crystal Structure Of Nav1.6 Iq Motif In Complex With Apo-cam" . . . . . 100.00 182 100.00 100.00 5.91e-100 . . . . 15185 1 155 no PDB 4ANJ . "Myosin Vi (Mdinsert2-Gfp Fusion) Pre-Powerstroke State (Mg.Adp.Alf4)" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 15185 1 156 no PDB 4BW7 . "Calmodulin In Complex With Strontium" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 157 no PDB 4BW8 . "Calmodulin With Small Bend In Central Helix" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 158 no PDB 4BYF . "Crystal Structure Of Human Myosin 1c In Complex With Calmodulin In The Pre-power Stroke State" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 159 no PDB 4CLN . "Structure Of A Recombinant Calmodulin From Drosophila Melanogaster Refined At 2.2-Angstroms Resolution" . . . . . 100.00 148 97.97 99.32 6.77e-98 . . . . 15185 1 160 no PDB 4DBP . "Myosin Vi Nucleotide-free (mdinsert2) D179y Crystal Structure" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 15185 1 161 no PDB 4DBQ . "Myosin Vi D179y (md-insert2-cam, Delta-insert1) Post-rigor State" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 15185 1 162 no PDB 4DCK . "Crystal Structure Of The C-Terminus Of Voltage-Gated Sodium Channel In Complex With Fgf13 And Cam" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 163 no PDB 4DJC . "1.35 A Crystal Structure Of The Nav1.5 Diii-Iv-CaCAM COMPLEX" . . . . . 100.00 152 100.00 100.00 3.59e-100 . . . . 15185 1 164 no PDB 4E50 . "Calmodulin And Ng Peptide Complex" . . . . . 100.00 185 100.00 100.00 2.67e-100 . . . . 15185 1 165 no PDB 4EHQ . "Crystal Structure Of Calmodulin Binding Domain Of Orai1 In Complex With Ca2+CALMODULIN DISPLAYS A UNIQUE BINDING MODE" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 166 no PDB 4G27 . "Calcium-Calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And P" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 167 no PDB 4G28 . "Calcium-Calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And E" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 168 no PDB 4HEX . "A Novel Conformation Of Calmodulin" . . . . . 100.00 156 100.00 100.00 2.20e-100 . . . . 15185 1 169 no PDB 4IK1 . "High Resolution Structure Of Gcampj At Ph 8.5" . . . . . 99.32 448 98.64 99.32 1.47e-93 . . . . 15185 1 170 no PDB 4IK3 . "High Resolution Structure Of Gcamp3 At Ph 8.5" . . . . . 99.32 448 99.32 100.00 9.53e-95 . . . . 15185 1 171 no PDB 4IK4 . "High Resolution Structure Of Gcamp3 At Ph 5.0" . . . . . 99.32 448 99.32 100.00 9.53e-95 . . . . 15185 1 172 no PDB 4IK5 . "High Resolution Structure Of Delta-rest-gcamp3" . . . . . 99.32 414 99.32 100.00 3.73e-95 . . . . 15185 1 173 no PDB 4IK8 . "High Resolution Structure Of Gcamp3 Dimer Form 1 At Ph 7.5" . . . . . 99.32 448 99.32 100.00 9.53e-95 . . . . 15185 1 174 no PDB 4IK9 . "High Resolution Structure Of Gcamp3 Dimer Form 2 At Ph 7.5" . . . . . 99.32 448 99.32 100.00 9.53e-95 . . . . 15185 1 175 no PDB 4J9Y . "Calcium-calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 176 no PDB 4J9Z . "Calcium-calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And N" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 177 no PDB 4JPZ . "Voltage-gated Sodium Channel 1.2 C-terminal Domain In Complex With Fgf13u And Ca2+/calmodulin" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 178 no PDB 4JQ0 . "Voltage-gated Sodium Channel 1.5 C-terminal Domain In Complex With Fgf12b And Ca2+/calmodulin" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 179 no PDB 4L79 . "Crystal Structure Of Nucleotide-free Myosin 1b Residues 1-728 With Bound Calmodulin" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 180 no PDB 4LZX . "Complex Of Iqcg And Ca2+-free Cam" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 181 no PDB 4M1L . "Complex Of Iqcg And Ca2+-bound Cam" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 182 no PDB 4PJJ . "Myosin Vi (md-insert2-cam, Delta-insert1) Post-rigor State - Long Soaking With Po4" . . . . . 100.00 149 97.30 99.32 1.25e-97 . . . . 15185 1 183 no PDB 4Q5U . "Structure Of Calmodulin Bound To Its Recognition Site From Calcineurin" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 184 no PDB 4QNH . "Calcium-calmodulin (t79d) Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Sk2-a" . . . . . 100.00 149 99.32 99.32 6.26e-99 . . . . 15185 1 185 no PDB 4R8G . "Crystal Structure Of Myosin-1c Tail In Complex With Calmodulin" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 186 no PDB 4UMO . "Crystal Structure Of The Kv7.1 Proximal C-terminal Domain In Complex With Calmodulin" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 187 no PDB 4UPU . "Crystal Structure Of Ip3 3-k Calmodulin Binding Region In Complex With Calmodulin" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 188 no PDB 4V0C . "Crystal Structure Of The Kv7.1 Proximal C-terminal Domain In Complex With Calmodulin" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 189 no DBJ BAA08302 . "calmodulin [Homo sapiens]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 190 no DBJ BAA11896 . "calmodulin [Anas platyrhynchos]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 191 no DBJ BAA19786 . "calmodulin [Branchiostoma lanceolatum]" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 15185 1 192 no DBJ BAA19787 . "calmodulin [Branchiostoma floridae]" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 15185 1 193 no DBJ BAA19788 . "calmodulin [Halocynthia roretzi]" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 15185 1 194 no EMBL CAA10601 . "calmodulin [Caenorhabditis elegans]" . . . . . 100.00 149 97.97 98.65 1.28e-97 . . . . 15185 1 195 no EMBL CAA32050 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 196 no EMBL CAA32062 . "calmodulin II [Rattus norvegicus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 197 no EMBL CAA32119 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 198 no EMBL CAA32120 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 199 no GB AAA35635 . "calmodulin [Homo sapiens]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 200 no GB AAA35641 . "calmodulin [Homo sapiens]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 201 no GB AAA37365 . "calmodulin synthesis [Mus musculus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 202 no GB AAA40862 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 203 no GB AAA40863 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 204 no PIR JC1305 . "calmodulin - Japanese medaka" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 205 no PIR MCON . "calmodulin - salmon" . . . . . 100.00 148 100.00 100.00 4.91e-100 . . . . 15185 1 206 no PRF 0409298A . "troponin C-like protein" . . . . . 100.00 148 97.30 100.00 2.53e-98 . . . . 15185 1 207 no PRF 0608335A . calmodulin . . . . . 100.00 148 97.97 99.32 3.48e-97 . . . . 15185 1 208 no REF NP_001008160 . "calmodulin [Xenopus (Silurana) tropicalis]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 209 no REF NP_001009759 . "calmodulin [Ovis aries]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 210 no REF NP_001027633 . "calmodulin [Ciona intestinalis]" . . . . . 100.00 149 97.30 98.65 3.34e-97 . . . . 15185 1 211 no REF NP_001039714 . "calmodulin [Bos taurus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 212 no REF NP_001040234 . "calmodulin [Bombyx mori]" . . . . . 100.00 149 97.97 99.32 5.16e-98 . . . . 15185 1 213 no SP O02367 . "RecName: Full=Calmodulin; Short=CaM; AltName: Full=Ci-CaM" . . . . . 100.00 149 97.30 98.65 3.34e-97 . . . . 15185 1 214 no SP O16305 . "RecName: Full=Calmodulin; Short=CaM" . . . . . 100.00 149 97.97 98.65 1.28e-97 . . . . 15185 1 215 no SP O96081 . "RecName: Full=Calmodulin-B; Short=CaM B" . . . . . 100.00 149 97.30 98.65 3.76e-97 . . . . 15185 1 216 no SP P02594 . "RecName: Full=Calmodulin; Short=CaM" . . . . . 100.00 149 99.32 100.00 1.65e-99 . . . . 15185 1 217 no SP P05932 . "RecName: Full=Calmodulin-beta; Short=Cam B" . . . . . 93.24 138 97.10 99.28 5.25e-90 . . . . 15185 1 218 no TPG DAA13808 . "TPA: calmodulin 2-like [Bos taurus]" . . . . . 100.00 216 98.65 98.65 2.49e-98 . . . . 15185 1 219 no TPG DAA18029 . "TPA: calmodulin [Bos taurus]" . . . . . 100.00 149 98.65 99.32 7.54e-99 . . . . 15185 1 220 no TPG DAA19590 . "TPA: calmodulin 3 [Bos taurus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 221 no TPG DAA24777 . "TPA: calmodulin 2-like [Bos taurus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 222 no TPG DAA24988 . "TPA: calmodulin 2-like isoform 1 [Bos taurus]" . . . . . 100.00 149 100.00 100.00 5.13e-100 . . . . 15185 1 stop_ loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'Ca2+-binding protein' 15185 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . ALA . 15185 1 2 . ASP . 15185 1 3 . GLN . 15185 1 4 . LEU . 15185 1 5 . THR . 15185 1 6 . GLU . 15185 1 7 . GLU . 15185 1 8 . GLN . 15185 1 9 . ILE . 15185 1 10 . ALA . 15185 1 11 . GLU . 15185 1 12 . PHE . 15185 1 13 . LYS . 15185 1 14 . GLU . 15185 1 15 . ALA . 15185 1 16 . PHE . 15185 1 17 . SER . 15185 1 18 . LEU . 15185 1 19 . PHE . 15185 1 20 . ASP . 15185 1 21 . LYS . 15185 1 22 . ASP . 15185 1 23 . GLY . 15185 1 24 . ASP . 15185 1 25 . GLY . 15185 1 26 . THR . 15185 1 27 . ILE . 15185 1 28 . THR . 15185 1 29 . THR . 15185 1 30 . LYS . 15185 1 31 . GLU . 15185 1 32 . LEU . 15185 1 33 . GLY . 15185 1 34 . THR . 15185 1 35 . VAL . 15185 1 36 . MET . 15185 1 37 . ARG . 15185 1 38 . SER . 15185 1 39 . LEU . 15185 1 40 . GLY . 15185 1 41 . GLN . 15185 1 42 . ASN . 15185 1 43 . PRO . 15185 1 44 . THR . 15185 1 45 . GLU . 15185 1 46 . ALA . 15185 1 47 . GLU . 15185 1 48 . LEU . 15185 1 49 . GLN . 15185 1 50 . ASP . 15185 1 51 . MET . 15185 1 52 . ILE . 15185 1 53 . ASN . 15185 1 54 . GLU . 15185 1 55 . VAL . 15185 1 56 . ASP . 15185 1 57 . ALA . 15185 1 58 . ASP . 15185 1 59 . GLY . 15185 1 60 . ASN . 15185 1 61 . GLY . 15185 1 62 . THR . 15185 1 63 . ILE . 15185 1 64 . ASP . 15185 1 65 . PHE . 15185 1 66 . PRO . 15185 1 67 . GLU . 15185 1 68 . PHE . 15185 1 69 . LEU . 15185 1 70 . THR . 15185 1 71 . MET . 15185 1 72 . MET . 15185 1 73 . ALA . 15185 1 74 . ARG . 15185 1 75 . LYS . 15185 1 76 . MET . 15185 1 77 . LYS . 15185 1 78 . ASP . 15185 1 79 . THR . 15185 1 80 . ASP . 15185 1 81 . SER . 15185 1 82 . GLU . 15185 1 83 . GLU . 15185 1 84 . GLU . 15185 1 85 . ILE . 15185 1 86 . ARG . 15185 1 87 . GLU . 15185 1 88 . ALA . 15185 1 89 . PHE . 15185 1 90 . ARG . 15185 1 91 . VAL . 15185 1 92 . PHE . 15185 1 93 . ASP . 15185 1 94 . LYS . 15185 1 95 . ASP . 15185 1 96 . GLY . 15185 1 97 . ASN . 15185 1 98 . GLY . 15185 1 99 . TYR . 15185 1 100 . ILE . 15185 1 101 . SER . 15185 1 102 . ALA . 15185 1 103 . ALA . 15185 1 104 . GLU . 15185 1 105 . LEU . 15185 1 106 . ARG . 15185 1 107 . HIS . 15185 1 108 . VAL . 15185 1 109 . MET . 15185 1 110 . THR . 15185 1 111 . ASN . 15185 1 112 . LEU . 15185 1 113 . GLY . 15185 1 114 . GLU . 15185 1 115 . LYS . 15185 1 116 . LEU . 15185 1 117 . THR . 15185 1 118 . ASP . 15185 1 119 . GLU . 15185 1 120 . GLU . 15185 1 121 . VAL . 15185 1 122 . ASP . 15185 1 123 . GLU . 15185 1 124 . MET . 15185 1 125 . ILE . 15185 1 126 . ARG . 15185 1 127 . GLU . 15185 1 128 . ALA . 15185 1 129 . ASP . 15185 1 130 . ILE . 15185 1 131 . ASP . 15185 1 132 . GLY . 15185 1 133 . ASP . 15185 1 134 . GLY . 15185 1 135 . GLN . 15185 1 136 . VAL . 15185 1 137 . ASN . 15185 1 138 . TYR . 15185 1 139 . GLU . 15185 1 140 . GLU . 15185 1 141 . PHE . 15185 1 142 . VAL . 15185 1 143 . GLN . 15185 1 144 . MET . 15185 1 145 . MET . 15185 1 146 . THR . 15185 1 147 . ALA . 15185 1 148 . LYS . 15185 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . ALA 1 1 15185 1 . ASP 2 2 15185 1 . GLN 3 3 15185 1 . LEU 4 4 15185 1 . THR 5 5 15185 1 . GLU 6 6 15185 1 . GLU 7 7 15185 1 . GLN 8 8 15185 1 . ILE 9 9 15185 1 . ALA 10 10 15185 1 . GLU 11 11 15185 1 . PHE 12 12 15185 1 . LYS 13 13 15185 1 . GLU 14 14 15185 1 . ALA 15 15 15185 1 . PHE 16 16 15185 1 . SER 17 17 15185 1 . LEU 18 18 15185 1 . PHE 19 19 15185 1 . ASP 20 20 15185 1 . LYS 21 21 15185 1 . ASP 22 22 15185 1 . GLY 23 23 15185 1 . ASP 24 24 15185 1 . GLY 25 25 15185 1 . THR 26 26 15185 1 . ILE 27 27 15185 1 . THR 28 28 15185 1 . THR 29 29 15185 1 . LYS 30 30 15185 1 . GLU 31 31 15185 1 . LEU 32 32 15185 1 . GLY 33 33 15185 1 . THR 34 34 15185 1 . VAL 35 35 15185 1 . MET 36 36 15185 1 . ARG 37 37 15185 1 . SER 38 38 15185 1 . LEU 39 39 15185 1 . GLY 40 40 15185 1 . GLN 41 41 15185 1 . ASN 42 42 15185 1 . PRO 43 43 15185 1 . THR 44 44 15185 1 . GLU 45 45 15185 1 . ALA 46 46 15185 1 . GLU 47 47 15185 1 . LEU 48 48 15185 1 . GLN 49 49 15185 1 . ASP 50 50 15185 1 . MET 51 51 15185 1 . ILE 52 52 15185 1 . ASN 53 53 15185 1 . GLU 54 54 15185 1 . VAL 55 55 15185 1 . ASP 56 56 15185 1 . ALA 57 57 15185 1 . ASP 58 58 15185 1 . GLY 59 59 15185 1 . ASN 60 60 15185 1 . GLY 61 61 15185 1 . THR 62 62 15185 1 . ILE 63 63 15185 1 . ASP 64 64 15185 1 . PHE 65 65 15185 1 . PRO 66 66 15185 1 . GLU 67 67 15185 1 . PHE 68 68 15185 1 . LEU 69 69 15185 1 . THR 70 70 15185 1 . MET 71 71 15185 1 . MET 72 72 15185 1 . ALA 73 73 15185 1 . ARG 74 74 15185 1 . LYS 75 75 15185 1 . MET 76 76 15185 1 . LYS 77 77 15185 1 . ASP 78 78 15185 1 . THR 79 79 15185 1 . ASP 80 80 15185 1 . SER 81 81 15185 1 . GLU 82 82 15185 1 . GLU 83 83 15185 1 . GLU 84 84 15185 1 . ILE 85 85 15185 1 . ARG 86 86 15185 1 . GLU 87 87 15185 1 . ALA 88 88 15185 1 . PHE 89 89 15185 1 . ARG 90 90 15185 1 . VAL 91 91 15185 1 . PHE 92 92 15185 1 . ASP 93 93 15185 1 . LYS 94 94 15185 1 . ASP 95 95 15185 1 . GLY 96 96 15185 1 . ASN 97 97 15185 1 . GLY 98 98 15185 1 . TYR 99 99 15185 1 . ILE 100 100 15185 1 . SER 101 101 15185 1 . ALA 102 102 15185 1 . ALA 103 103 15185 1 . GLU 104 104 15185 1 . LEU 105 105 15185 1 . ARG 106 106 15185 1 . HIS 107 107 15185 1 . VAL 108 108 15185 1 . MET 109 109 15185 1 . THR 110 110 15185 1 . ASN 111 111 15185 1 . LEU 112 112 15185 1 . GLY 113 113 15185 1 . GLU 114 114 15185 1 . LYS 115 115 15185 1 . LEU 116 116 15185 1 . THR 117 117 15185 1 . ASP 118 118 15185 1 . GLU 119 119 15185 1 . GLU 120 120 15185 1 . VAL 121 121 15185 1 . ASP 122 122 15185 1 . GLU 123 123 15185 1 . MET 124 124 15185 1 . ILE 125 125 15185 1 . ARG 126 126 15185 1 . GLU 127 127 15185 1 . ALA 128 128 15185 1 . ASP 129 129 15185 1 . ILE 130 130 15185 1 . ASP 131 131 15185 1 . GLY 132 132 15185 1 . ASP 133 133 15185 1 . GLY 134 134 15185 1 . GLN 135 135 15185 1 . VAL 136 136 15185 1 . ASN 137 137 15185 1 . TYR 138 138 15185 1 . GLU 139 139 15185 1 . GLU 140 140 15185 1 . PHE 141 141 15185 1 . VAL 142 142 15185 1 . GLN 143 143 15185 1 . MET 144 144 15185 1 . MET 145 145 15185 1 . THR 146 146 15185 1 . ALA 147 147 15185 1 . LYS 148 148 15185 1 stop_ save_ save_eNOSp _Entity.Sf_category entity _Entity.Sf_framecode eNOSp _Entity.Entry_ID 15185 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name eNOSp _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 ; RKKTFKEVANAVKISASLMG ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details 'derived from the CaM binding region of the human endothelial nitric oxide synthase' _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 20 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-31 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 18028 . eNOS . . . . . 85.00 17 100.00 100.00 1.00e+00 . . . . 15185 2 2 no BMRB 19586 . entity_2 . . . . . 80.00 16 100.00 100.00 1.91e+00 . . . . 15185 2 3 no PDB 1NIW . "Crystal Structure Of Endothelial Nitric Oxide Synthase Peptide Bound To Calmodulin" . . . . . 100.00 20 100.00 100.00 2.14e-03 . . . . 15185 2 4 no PDB 2LL7 . "Solution Nmr Structure Of Cam Bound To The Enos Cam Binding Domain Peptide" . . . . . 85.00 17 100.00 100.00 1.00e+00 . . . . 15185 2 5 no DBJ BAA05652 . "endothelial nitric oxide synthase [Homo sapiens]" . . . . . 100.00 1204 100.00 100.00 6.97e-03 . . . . 15185 2 6 no DBJ BAD15356 . "nitric oxide synthase 3 [Rattus norvegicus]" . . . . . 100.00 1202 100.00 100.00 6.97e-03 . . . . 15185 2 7 no DBJ BAD97356 . "nitric oxide synthase 3 (endothelial cell) variant [Homo sapiens]" . . . . . 100.00 1203 100.00 100.00 6.97e-03 . . . . 15185 2 8 no DBJ BAF85617 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 1203 100.00 100.00 6.97e-03 . . . . 15185 2 9 no DBJ BAG37648 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 1203 100.00 100.00 6.97e-03 . . . . 15185 2 10 no EMBL CAA09493 . "endothelial nitric oxide synthase [Rattus norvegicus]" . . . . . 100.00 200 100.00 100.00 6.30e-03 . . . . 15185 2 11 no EMBL CAA53950 . "endothelial nitric oxide synthase [Homo sapiens]" . . . . . 100.00 1203 100.00 100.00 6.97e-03 . . . . 15185 2 12 no EMBL CAI10801 . "endothelial nitric oxide synthase [Mesocricetus auratus]" . . . . . 100.00 122 100.00 100.00 2.15e-03 . . . . 15185 2 13 no GB AAA30494 . "nitric oxide synthase [Bos taurus]" . . . . . 100.00 1205 100.00 100.00 6.98e-03 . . . . 15185 2 14 no GB AAA30667 . "nitric oxide synthase [Bos taurus]" . . . . . 100.00 1205 100.00 100.00 6.98e-03 . . . . 15185 2 15 no GB AAA30669 . "nitric oxide synthase [Bos taurus]" . . . . . 100.00 1205 100.00 100.00 6.98e-03 . . . . 15185 2 16 no GB AAA36364 . "nitric oxide synthase [Homo sapiens]" . . . . . 100.00 1203 100.00 100.00 6.97e-03 . . . . 15185 2 17 no GB AAA36365 . "nitric oxide synthase [Homo sapiens]" . . . . . 100.00 1203 100.00 100.00 6.97e-03 . . . . 15185 2 18 no PRF 2011304A . "NO synthase" . . . . . 100.00 1205 100.00 100.00 6.98e-03 . . . . 15185 2 19 no REF NP_000594 . "nitric oxide synthase, endothelial isoform 1 [Homo sapiens]" . . . . . 100.00 1203 100.00 100.00 6.97e-03 . . . . 15185 2 20 no REF NP_001003158 . "nitric oxide synthase, endothelial [Canis lupus familiaris]" . . . . . 100.00 1205 100.00 100.00 6.98e-03 . . . . 15185 2 21 no REF NP_001076202 . "nitric oxide synthase, endothelial [Oryctolagus cuniculus]" . . . . . 100.00 1209 100.00 100.00 6.98e-03 . . . . 15185 2 22 no REF NP_001123373 . "nitric oxide synthase, endothelial [Ovis aries]" . . . . . 100.00 1205 100.00 100.00 6.98e-03 . . . . 15185 2 23 no REF NP_001153581 . "nitric oxide synthase, endothelial isoform 2 [Homo sapiens]" . . . . . 100.00 596 100.00 100.00 5.88e-03 . . . . 15185 2 24 no SP P29473 . "RecName: Full=Nitric oxide synthase, endothelial; AltName: Full=Constitutive NOS; Short=cNOS; AltName: Full=EC-NOS; AltName: Fu" . . . . . 100.00 1205 100.00 100.00 6.98e-03 . . . . 15185 2 25 no SP P29474 . "RecName: Full=Nitric oxide synthase, endothelial; AltName: Full=Constitutive NOS; Short=cNOS; AltName: Full=EC-NOS; AltName: Fu" . . . . . 100.00 1203 100.00 100.00 6.97e-03 . . . . 15185 2 26 no SP P70313 . "RecName: Full=Nitric oxide synthase, endothelial; AltName: Full=Constitutive NOS; Short=cNOS; AltName: Full=EC-NOS; AltName: Fu" . . . . . 100.00 1202 100.00 100.00 6.97e-03 . . . . 15185 2 27 no SP Q62600 . "RecName: Full=Nitric oxide synthase, endothelial; AltName: Full=Constitutive NOS; Short=cNOS; AltName: Full=EC-NOS; AltName: Fu" . . . . . 100.00 1202 100.00 100.00 6.97e-03 . . . . 15185 2 28 no SP Q9TUX8 . "RecName: Full=Nitric oxide synthase, endothelial; AltName: Full=Constitutive NOS; Short=cNOS; AltName: Full=EC-NOS; AltName: Fu" . . . . . 100.00 1205 100.00 100.00 6.98e-03 . . . . 15185 2 29 no TPG DAA30266 . "TPA: nitric oxide synthase, endothelial [Bos taurus]" . . . . . 100.00 1205 100.00 100.00 6.98e-03 . . . . 15185 2 stop_ loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'CaM-binding peptide' 15185 2 'Nitric Oxide Synthase' 15185 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 . ARG . 15185 2 2 . LYS . 15185 2 3 . LYS . 15185 2 4 . THR . 15185 2 5 . PHE . 15185 2 6 . LYS . 15185 2 7 . GLU . 15185 2 8 . VAL . 15185 2 9 . ALA . 15185 2 10 . ASN . 15185 2 11 . ALA . 15185 2 12 . VAL . 15185 2 13 . LYS . 15185 2 14 . ILE . 15185 2 15 . SER . 15185 2 16 . ALA . 15185 2 17 . SER . 15185 2 18 . LEU . 15185 2 19 . MET . 15185 2 20 . GLY . 15185 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 . ARG 1 1 15185 2 . LYS 2 2 15185 2 . LYS 3 3 15185 2 . THR 4 4 15185 2 . PHE 5 5 15185 2 . LYS 6 6 15185 2 . GLU 7 7 15185 2 . VAL 8 8 15185 2 . ALA 9 9 15185 2 . ASN 10 10 15185 2 . ALA 11 11 15185 2 . VAL 12 12 15185 2 . LYS 13 13 15185 2 . ILE 14 14 15185 2 . SER 15 15 15185 2 . ALA 16 16 15185 2 . SER 17 17 15185 2 . LEU 18 18 15185 2 . MET 19 19 15185 2 . GLY 20 20 15185 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 15185 _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 $calmodulin . 9031 organism . 'Gallus gallus' chicken . . Eukaryota Metazoa Gallus gallus . . . . . . . . . . . . . . . . . . . . . 15185 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 15185 _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 $calmodulin . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pET . . . . . . 15185 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 15185 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details 'Uniform 15N labeled CaM for backbone relaxation experiments' _Sample.Aggregate_sample_number . _Sample.Solvent_system '95% H2O/5% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 calmodulin '[U-100% 15N]' . . 1 $calmodulin . . 1 . . mM . . . . 15185 1 2 eNOSp 'natural abundance' . . 2 $eNOSp . . 1.2 . . mM 0.1 . . . 15185 1 3 'potassium chloride' 'natural abundance' . . . . . . 100 . . mM . . . . 15185 1 4 imidazole 'natural abundance' . . . . . . 20 . . mM . . . . 15185 1 5 CaCl2 'natural abundance' . . . . . . 6 . . mM . . . . 15185 1 6 'sodium azide' 'natural abundance' . . . . . . 3 . . mM . . . . 15185 1 7 H2O 'natural abundance' . . . . . . 95 . . % . . . . 15185 1 8 D2O 'natural abundance' . . . . . . 5 . . % . . . . 15185 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 15185 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details 'Uniform 15N/13C;55% 2H labeled CaM for methyl relaxation experiments' _Sample.Aggregate_sample_number . _Sample.Solvent_system '95% H2O/5% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 calmodulin '[U-100% 13C; U-100% 15N; 55% 2H]' . . 1 $calmodulin . . 1 . . mM . . . . 15185 2 2 eNOSp 'natural abundance' . . 2 $eNOSp . . 1.2 . . mM 0.1 . . . 15185 2 3 'potassium chloride' 'natural abundance' . . . . . . 100 . . mM . . . . 15185 2 4 imidazole 'natural abundance' . . . . . . 20 . . mM . . . . 15185 2 5 CaCl2 'natural abundance' . . . . . . 6 . . mM . . . . 15185 2 6 'sodium azide' 'natural abundance' . . . . . . 3 . . mM . . . . 15185 2 7 H2O 'natural abundance' . . . . . . 95 . . % . . . . 15185 2 8 D2O 'natural abundance' . . . . . . 5 . . % . . . . 15185 2 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 15185 _Sample_condition_list.ID 1 _Sample_condition_list.Details '20mM imidazole, pH 6.5, 100mM KCl, 6mM CaCl2, 3 mM Na_azide' 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 6.5 . pH 15185 1 pressure 1 . atm 15185 1 temperature 308 . K 15185 1 stop_ save_ ############################ # Computer software used # ############################ save_Felix _Software.Sf_category software _Software.Sf_framecode Felix _Software.Entry_ID 15185 _Software.ID 1 _Software.Name FELIX _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Accelrys Software Inc.' . . 15185 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 15185 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 15185 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 15185 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 15185 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Varian INOVA . 500 . . . 15185 1 2 spectrometer_2 Varian INOVA . 600 cryo-probe . . 15185 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 15185 _Experiment_list.ID 1 _Experiment_list.Details ; Backbone amide relation experiments T1, T2, NOE recorded as 1H-15N HSQCs. Methyl relaxation experiments IzCzDz, IzCzDy, and IzCz recorded as 1H-13C HSQCs ; loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15185 1 2 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15185 1 3 '2D 1H-13C HSQC' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15185 1 4 '2D 1H-13C HSQC' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15185 1 stop_ save_ save_2D_1H-15N_HSQC _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode 2D_1H-15N_HSQC _NMR_spec_expt.Entry_ID 15185 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '2D 1H-15N HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units uL _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $spectrometer_1 _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID 1 _NMR_spec_expt.Software_label $Felix _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details 'T1 and T2 experiments were collected as 12 HSQC - 9 delay times, 3 of which were collected in duplicate.' save_ save_2D_1H-13C_HSQC _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode 2D_1H-13C_HSQC _NMR_spec_expt.Entry_ID 15185 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '2D 1H-13C HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units uL _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $spectrometer_1 _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID 1 _NMR_spec_expt.Software_label $Felix _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details 'methyl relaxation experiments were collected as 11 HSQC - 9 delay times, 2 of which were collected in duplicate.' save_ ###################### # Order parameters # ###################### save_backbone_order_parameters _Order_parameter_list.Sf_category order_parameters _Order_parameter_list.Sf_framecode backbone_order_parameters _Order_parameter_list.Entry_ID 15185 _Order_parameter_list.ID 1 _Order_parameter_list.Sample_condition_list_ID 1 _Order_parameter_list.Sample_condition_list_label $sample_conditions_1 _Order_parameter_list.Tau_e_val_units s _Order_parameter_list.Tau_f_val_units s _Order_parameter_list.Tau_s_val_units s _Order_parameter_list.Rex_field_strength . _Order_parameter_list.Rex_val_units . _Order_parameter_list.Details 'NMR derived backbone N-H bond vector model-free squared generalized order parameters for CaM in complex with eNOSp determined at 500 and 600 MHz (1H)' _Order_parameter_list.Text_data_format . _Order_parameter_list.Text_data . loop_ _Order_parameter_experiment.Experiment_ID _Order_parameter_experiment.Experiment_name _Order_parameter_experiment.Sample_ID _Order_parameter_experiment.Sample_label _Order_parameter_experiment.Sample_state _Order_parameter_experiment.Entry_ID _Order_parameter_experiment.Order_parameter_list_ID 1 '2D 1H-15N HSQC' . . . 15185 1 stop_ loop_ _Order_parameter_software.Software_ID _Order_parameter_software.Software_label _Order_parameter_software.Method_ID _Order_parameter_software.Method_label _Order_parameter_software.Entry_ID _Order_parameter_software.Order_parameter_list_ID 1 $Felix . . 15185 1 stop_ loop_ _Order_param.ID _Order_param.Assembly_atom_ID _Order_param.Entity_assembly_ID _Order_param.Entity_ID _Order_param.Comp_index_ID _Order_param.Seq_ID _Order_param.Comp_ID _Order_param.Atom_ID _Order_param.Atom_type _Order_param.Atom_isotope_number _Order_param.Order_param_val _Order_param.Order_param_val_fit_err _Order_param.Tau_e_val _Order_param.Tau_e_val_fit_err _Order_param.Tau_f_val _Order_param.Tau_f_val_fit_err _Order_param.Tau_s_val _Order_param.Tau_s_val_fit_err _Order_param.Rex_val _Order_param.Rex_val_fit_err _Order_param.Model_free_sum_squared_errs _Order_param.Model_fit _Order_param.Sf2_val _Order_param.Sf2_val_fit_err _Order_param.Ss2_val _Order_param.Ss2_val_fit_err _Order_param.SH2_val _Order_param.SH2_val_fit_err _Order_param.SN2_val _Order_param.SN2_val_fit_err _Order_param.Resonance_ID _Order_param.Auth_entity_assembly_ID _Order_param.Auth_seq_ID _Order_param.Auth_comp_ID _Order_param.Auth_atom_ID _Order_param.Entry_ID _Order_param.Order_parameter_list_ID 1 . 1 1 3 3 GLN N N 15 0.594 0.01 5.00E-14 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15185 1 2 . 1 1 4 4 LEU N N 15 0.598 0.005 1.08E-10 4.42E-12 . . . . . . . . . . . . . . . . . . . . . 15185 1 3 . 1 1 5 5 THR N N 15 0.849 0.017 6.46E-11 2.14E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 4 . 1 1 6 6 GLU N N 15 0.896 0.012 1.23E-10 3.82E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 5 . 1 1 7 7 GLU N N 15 0.905 0.007 1.12E-10 3.21E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 6 . 1 1 8 8 GLN N N 15 0.882 0.009 7.64E-11 1.88E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 7 . 1 1 9 9 ILE N N 15 0.91 0.008 5.88E-11 2.21E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 8 . 1 1 10 10 ALA N N 15 0.924 0.008 7.05E-11 1.33E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 9 . 1 1 11 11 GLU N N 15 0.929 0.005 7.83E-11 1.94E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 10 . 1 1 12 12 PHE N N 15 0.92 0.007 1.08E-10 2.12E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 11 . 1 1 13 13 LYS N N 15 0.948 0.005 6.46E-11 5.03E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 12 . 1 1 14 14 GLU N N 15 0.972 0.003 2.02E-10 6.98E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 13 . 1 1 16 16 PHE N N 15 0.967 0.008 8.61E-11 9.38E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 14 . 1 1 17 17 SER N N 15 0.986 0.004 2.72E-10 8.22E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 15 . 1 1 18 18 LEU N N 15 0.972 0.004 2.39E-10 9.00E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 16 . 1 1 19 19 PHE N N 15 0.91 0.011 3.92E-11 2.28E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 17 . 1 1 20 20 ASP N N 15 0.976 0.011 1.43E-10 1.22E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 18 . 1 1 21 21 LYS N N 15 0.915 0.012 6.07E-11 2.76E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 19 . 1 1 22 22 ASP N N 15 0.957 0.012 1.00E-09 3.12E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 20 . 1 1 23 23 GLY N N 15 0.972 0.013 9.01E-11 1.78E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 21 . 1 1 24 24 ASP N N 15 0.962 0.016 6.07E-11 1.49E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 22 . 1 1 25 25 GLY N N 15 0.915 0.021 4.70E-11 4.42E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 23 . 1 1 26 26 THR N N 15 0.981 0.012 3.92E-11 1.44E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 24 . 1 1 27 27 ILE N N 15 0.872 0.02 3.14E-11 2.28E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 25 . 1 1 28 28 THR N N 15 0.995 0.016 1.45E-10 1.08E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 26 . 1 1 29 29 THR N N 15 0.943 0.022 5.00E-14 2.71E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 27 . 1 1 30 30 LYS N N 15 0.953 0.006 6.66E-11 5.98E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 28 . 1 1 31 31 GLU N N 15 0.962 0.012 5.68E-11 7.71E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 29 . 1 1 32 32 LEU N N 15 0.972 0.008 7.83E-11 8.47E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 30 . 1 1 33 33 GLY N N 15 1 0.017 1.00E-09 6.85E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 31 . 1 1 34 34 THR N N 15 0.943 0.013 7.25E-11 2.85E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 32 . 1 1 35 35 VAL N N 15 0.981 0.011 1.96E-11 1.16E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 33 . 1 1 36 36 MET N N 15 0.948 0.011 3.14E-11 3.99E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 34 . 1 1 37 37 ARG N N 15 0.976 0.011 9.92E-10 4.22E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 35 . 1 1 38 38 SER N N 15 0.915 0.012 4.51E-11 2.03E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 36 . 1 1 39 39 LEU N N 15 0.924 0.014 3.96E-12 1.90E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 37 . 1 1 40 40 GLY N N 15 0.972 0.005 4.09E-10 8.88E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 38 . 1 1 42 42 ASN N N 15 0.858 0.019 5.68E-11 2.23E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 39 . 1 1 44 44 THR N N 15 0.868 0.021 5.09E-11 9.81E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 40 . 1 1 45 45 GLU N N 15 0.981 0.013 7.25E-11 1.17E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 41 . 1 1 46 46 ALA N N 15 0.924 0.008 7.44E-11 2.41E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 42 . 1 1 47 47 GLU N N 15 0.948 0.011 2.55E-11 3.26E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 43 . 1 1 48 48 LEU N N 15 0.972 0.012 5.00E-14 3.28E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 44 . 1 1 49 49 GLN N N 15 0.962 0.006 2.05E-10 7.87E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 45 . 1 1 50 50 ASP N N 15 0.972 0.006 8.81E-11 6.42E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 46 . 1 1 51 51 MET N N 15 0.924 0.006 1.02E-10 2.65E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 47 . 1 1 52 52 ILE N N 15 0.981 0.005 1.60E-10 8.88E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 48 . 1 1 53 53 ASN N N 15 0.962 0.003 3.09E-10 4.91E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 49 . 1 1 54 54 GLU N N 15 0.972 0.006 3.96E-12 3.72E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 50 . 1 1 55 55 VAL N N 15 0.976 0.016 1.96E-10 4.54E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 51 . 1 1 56 56 ASP N N 15 0.915 0.012 5.09E-11 2.95E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 52 . 1 1 57 57 ALA N N 15 0.745 0.011 2.74E-11 5.49E-12 . . . . . . . . . . . . . . . . . . . . . 15185 1 53 . 1 1 58 58 ASP N N 15 0.887 0.011 6.27E-11 1.60E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 54 . 1 1 59 59 GLY N N 15 0.877 0.017 2.74E-11 1.30E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 55 . 1 1 60 60 ASN N N 15 0.934 0.015 4.31E-11 1.35E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 56 . 1 1 61 61 GLY N N 15 0.943 0.021 1.33E-10 1.02E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 57 . 1 1 62 62 THR N N 15 0.962 0.013 5.88E-11 2.10E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 58 . 1 1 63 63 ILE N N 15 0.981 0.018 2.35E-11 1.49E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 59 . 1 1 64 64 ASP N N 15 0.939 0.015 1.12E-10 7.96E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 60 . 1 1 65 65 PHE N N 15 0.948 0.014 8.61E-11 8.18E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 61 . 1 1 68 68 PHE N N 15 0.972 0.009 1.10E-10 1.26E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 62 . 1 1 69 69 LEU N N 15 0.986 0.005 3.33E-10 1.27E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 63 . 1 1 70 70 THR N N 15 0.953 0.01 2.16E-11 3.44E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 64 . 1 1 71 71 MET N N 15 0.957 0.01 1.02E-10 8.52E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 65 . 1 1 72 72 MET N N 15 0.991 0.01 5.00E-14 1.95E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 66 . 1 1 73 73 ALA N N 15 0.976 0.005 2.23E-10 7.89E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 67 . 1 1 74 74 ARG N N 15 0.934 0.006 1.12E-10 3.62E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 68 . 1 1 75 75 LYS N N 15 0.901 0.005 1.21E-10 1.90E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 69 . 1 1 76 76 MET N N 15 0.754 0.007 1.00E-09 1.47E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 70 . 1 1 78 78 ASP N N 15 0.721 0.006 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15185 1 71 . 1 1 79 79 THR N N 15 0.698 0.005 9.90E-10 2.80E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 72 . 1 1 80 80 ASP N N 15 0.731 0.005 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15185 1 73 . 1 1 81 81 SER N N 15 0.839 0.008 1.00E-09 5.61E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 74 . 1 1 82 82 GLU N N 15 0.915 0.005 4.66E-10 1.36E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 75 . 1 1 84 84 GLU N N 15 0.991 0.006 1.39E-10 9.98E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 76 . 1 1 85 85 ILE N N 15 0.976 0.002 2.98E-10 7.32E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 77 . 1 1 86 86 ARG N N 15 0.962 0.008 5.48E-11 5.93E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 78 . 1 1 87 87 GLU N N 15 0.972 0.005 9.98E-11 6.85E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 79 . 1 1 88 88 ALA N N 15 0.953 0.007 7.25E-11 4.50E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 80 . 1 1 89 89 PHE N N 15 0.939 0.01 1.21E-10 5.70E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 81 . 1 1 90 90 ARG N N 15 0.981 0.005 2.31E-10 8.47E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 82 . 1 1 91 91 VAL N N 15 0.967 0.007 2.55E-11 5.17E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 83 . 1 1 92 92 PHE N N 15 0.953 0.011 4.31E-11 5.43E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 84 . 1 1 93 93 ASP N N 15 0.924 0.013 5.48E-11 3.86E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 85 . 1 1 94 94 LYS N N 15 0.887 0.011 3.33E-11 1.32E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 86 . 1 1 95 95 ASP N N 15 0.924 0.008 6.46E-11 1.58E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 87 . 1 1 96 96 GLY N N 15 0.877 0.011 6.07E-11 1.50E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 88 . 1 1 99 99 TYR N N 15 0.976 0.011 1.12E-10 1.12E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 89 . 1 1 100 100 ILE N N 15 0.92 0.023 2.16E-11 4.85E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 90 . 1 1 101 101 SER N N 15 1 0.02 5.00E-14 4.94E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 91 . 1 1 102 102 ALA N N 15 0.981 0.006 2.53E-10 9.68E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 92 . 1 1 103 103 ALA N N 15 0.957 0.008 3.53E-11 3.34E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 93 . 1 1 105 105 LEU N N 15 0.929 0.008 9.79E-11 4.44E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 94 . 1 1 106 106 ARG N N 15 0.957 0.009 2.55E-11 4.03E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 95 . 1 1 107 107 HIS N N 15 0.976 0.009 1.43E-10 4.67E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 96 . 1 1 109 109 MET N N 15 0.939 0.012 4.90E-11 4.61E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 97 . 1 1 110 110 THR N N 15 0.943 0.016 3.14E-11 5.48E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 98 . 1 1 111 111 ASN N N 15 0.962 0.012 3.96E-12 4.73E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 99 . 1 1 112 112 LEU N N 15 0.896 0.011 2.16E-11 1.38E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 100 . 1 1 113 113 GLY N N 15 0.887 0.012 5.29E-11 1.89E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 101 . 1 1 114 114 GLU N N 15 0.891 0.007 5.48E-11 1.27E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 102 . 1 1 115 115 LYS N N 15 0.66 0.008 7.25E-11 5.58E-12 . . . . . . . . . . . . . . . . . . . . . 15185 1 103 . 1 1 116 116 LEU N N 15 0.636 0.006 6.85E-11 3.74E-12 . . . . . . . . . . . . . . . . . . . . . 15185 1 104 . 1 1 117 117 THR N N 15 0.844 0.017 6.66E-11 2.13E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 105 . 1 1 118 118 ASP N N 15 0.939 0.02 1.00E-09 6.02E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 106 . 1 1 119 119 GLU N N 15 0.901 0.005 4.90E-11 9.80E-12 . . . . . . . . . . . . . . . . . . . . . 15185 1 107 . 1 1 120 120 GLU N N 15 0.957 0.002 2.54E-10 5.93E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 108 . 1 1 122 122 ASP N N 15 0.929 0.006 8.42E-11 2.53E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 109 . 1 1 123 123 GLU N N 15 0.934 0.006 9.40E-11 4.00E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 110 . 1 1 124 124 MET N N 15 0.972 0.005 2.56E-10 7.54E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 111 . 1 1 125 125 ILE N N 15 0.967 0.005 1.06E-10 6.96E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 112 . 1 1 127 127 GLU N N 15 0.924 0.008 9.40E-11 3.69E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 113 . 1 1 128 128 ALA N N 15 0.967 0.004 2.96E-10 9.28E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 114 . 1 1 129 129 ASP N N 15 0.92 0.01 3.92E-11 2.33E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 115 . 1 1 130 130 ILE N N 15 0.66 0.01 2.35E-11 3.39E-12 . . . . . . . . . . . . . . . . . . . . . 15185 1 116 . 1 1 131 131 ASP N N 15 0.948 0.01 3.72E-11 2.58E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 117 . 1 1 132 132 GLY N N 15 0.901 0.018 1.77E-11 1.51E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 118 . 1 1 133 133 ASP N N 15 0.934 0.015 3.14E-11 1.40E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 119 . 1 1 134 134 GLY N N 15 0.948 0.02 1.57E-11 4.77E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 120 . 1 1 135 135 GLN N N 15 0.981 0.011 5.00E-14 9.45E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 121 . 1 1 136 136 VAL N N 15 0.924 0.014 4.51E-11 3.35E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 122 . 1 1 137 137 ASN N N 15 0.981 0.013 1.21E-10 1.17E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 123 . 1 1 138 138 TYR N N 15 0.929 0.012 2.94E-11 2.91E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 124 . 1 1 139 139 GLU N N 15 0.92 0.006 4.70E-11 1.61E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 125 . 1 1 140 140 GLU N N 15 0.957 0.009 1.68E-10 1.48E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 126 . 1 1 141 141 PHE N N 15 0.957 0.011 3.33E-11 5.55E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 127 . 1 1 142 142 VAL N N 15 0.953 0.009 9.83E-12 2.74E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 128 . 1 1 143 143 GLN N N 15 0.995 0.005 5.00E-14 1.16E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 129 . 1 1 144 144 MET N N 15 0.948 0.003 3.09E-10 6.96E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 130 . 1 1 145 145 MET N N 15 0.976 0.009 6.27E-11 9.29E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 131 . 1 1 146 146 THR N N 15 0.891 0.012 4.31E-11 1.47E-11 . . . . . . . . . . . . . . . . . . . . . 15185 1 132 . 1 1 147 147 ALA N N 15 0.773 0.015 1.00E-09 4.74E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 133 . 1 1 148 148 LYS N N 15 0.646 0.092 5.00E-14 2.46E-10 . . . . . . . . . . . . . . . . . . . . . 15185 1 stop_ save_ save_Methyl_order_parameters _Order_parameter_list.Sf_category order_parameters _Order_parameter_list.Sf_framecode Methyl_order_parameters _Order_parameter_list.Entry_ID 15185 _Order_parameter_list.ID 2 _Order_parameter_list.Sample_condition_list_ID 1 _Order_parameter_list.Sample_condition_list_label $sample_conditions_1 _Order_parameter_list.Tau_e_val_units s _Order_parameter_list.Tau_f_val_units s _Order_parameter_list.Tau_s_val_units s _Order_parameter_list.Rex_field_strength . _Order_parameter_list.Rex_val_units . _Order_parameter_list.Details ; NMR derived side-chain model-free squared generalized order parameters for the symmetry axis of methyl groups of CaM in complex with eNOSp determined with relaxation data obtained at 500 and 600 MHz (1H). ; _Order_parameter_list.Text_data_format . _Order_parameter_list.Text_data . loop_ _Order_parameter_experiment.Experiment_ID _Order_parameter_experiment.Experiment_name _Order_parameter_experiment.Sample_ID _Order_parameter_experiment.Sample_label _Order_parameter_experiment.Sample_state _Order_parameter_experiment.Entry_ID _Order_parameter_experiment.Order_parameter_list_ID 3 '2D 1H-13C HSQC' . . . 15185 2 stop_ loop_ _Order_parameter_software.Software_ID _Order_parameter_software.Software_label _Order_parameter_software.Method_ID _Order_parameter_software.Method_label _Order_parameter_software.Entry_ID _Order_parameter_software.Order_parameter_list_ID 1 $Felix . . 15185 2 stop_ loop_ _Order_param.ID _Order_param.Assembly_atom_ID _Order_param.Entity_assembly_ID _Order_param.Entity_ID _Order_param.Comp_index_ID _Order_param.Seq_ID _Order_param.Comp_ID _Order_param.Atom_ID _Order_param.Atom_type _Order_param.Atom_isotope_number _Order_param.Order_param_val _Order_param.Order_param_val_fit_err _Order_param.Tau_e_val _Order_param.Tau_e_val_fit_err _Order_param.Tau_f_val _Order_param.Tau_f_val_fit_err _Order_param.Tau_s_val _Order_param.Tau_s_val_fit_err _Order_param.Rex_val _Order_param.Rex_val_fit_err _Order_param.Model_free_sum_squared_errs _Order_param.Model_fit _Order_param.Sf2_val _Order_param.Sf2_val_fit_err _Order_param.Ss2_val _Order_param.Ss2_val_fit_err _Order_param.SH2_val _Order_param.SH2_val_fit_err _Order_param.SN2_val _Order_param.SN2_val_fit_err _Order_param.Resonance_ID _Order_param.Auth_entity_assembly_ID _Order_param.Auth_seq_ID _Order_param.Auth_comp_ID _Order_param.Auth_atom_ID _Order_param.Entry_ID _Order_param.Order_parameter_list_ID 1 . 1 1 4 4 LEU CD1 C 13 0.39 0.011 5.28E-11 2.70E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 2 . 1 1 4 4 LEU CD2 C 13 0.525 0.006 3.90E-11 8.27E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 3 . 1 1 9 9 ILE CG2 C 13 0.694 0.01 3.02E-11 8.87E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 4 . 1 1 10 10 ALA CB C 13 0.836 0.013 3.40E-11 9.67E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 5 . 1 1 15 15 ALA CB C 13 0.793 0.022 4.40E-11 2.64E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 6 . 1 1 18 18 LEU CD1 C 13 0.178 0.002 3.65E-11 6.66E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 7 . 1 1 18 18 LEU CD2 C 13 0.178 0.003 4.03E-11 6.82E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 8 . 1 1 26 26 THR CG2 C 13 0.489 0.007 9.30E-11 2.47E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 9 . 1 1 27 27 ILE CD1 C 13 0.602 0.022 4.53E-11 3.07E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 10 . 1 1 27 27 ILE CG2 C 13 0.715 0.019 3.65E-11 1.72E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 11 . 1 1 29 29 THR CG5 C 13 0.348 0.004 5.97E-11 7.88E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 12 . 1 1 32 32 LEU CD1 C 13 0.44 0.012 4.28E-11 2.13E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 13 . 1 1 32 32 LEU CD2 C 13 0.44 0.018 5.15E-11 4.36E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 14 . 1 1 34 34 THR CG2 C 13 0.673 0.011 5.22E-11 1.53E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 15 . 1 1 35 35 VAL CG1 C 13 0.666 0.014 6.16E-11 2.27E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 16 . 1 1 39 39 LEU CD1 C 13 0.723 0.117 4.15E-11 2.65E-11 . . . . . . . . . . . . . . . . . . . . . 15185 2 17 . 1 1 39 39 LEU CD2 C 13 0.56 0.021 3.02E-11 2.44E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 18 . 1 1 46 46 ALA CB C 13 0.772 0.011 4.28E-11 1.19E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 19 . 1 1 48 48 LEU CD1 C 13 0.588 0.04 6.53E-11 6.11E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 20 . 1 1 48 48 LEU CD2 C 13 0.511 0.008 3.59E-11 1.06E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 21 . 1 1 52 52 ILE CD1 C 13 0.242 0.005 2.14E-11 5.82E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 22 . 1 1 52 52 ILE CG2 C 13 0.68 0.011 4.34E-11 1.30E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 23 . 1 1 55 55 VAL CG1 C 13 0.567 0.009 4.84E-11 1.41E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 24 . 1 1 55 55 VAL CG2 C 13 0.581 0.009 3.65E-11 1.21E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 25 . 1 1 57 57 ALA CB C 13 0.08 0 3.09E-11 2.57E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 26 . 1 1 62 62 THR CG2 C 13 0.779 0.02 1.12E-10 6.61E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 27 . 1 1 63 63 ILE CD1 C 13 0.518 0.007 2.46E-11 6.28E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 28 . 1 1 63 63 ILE CG2 C 13 0.617 0.01 3.21E-11 1.18E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 29 . 1 1 69 69 LEU CD1 C 13 0.433 0.015 4.28E-11 2.75E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 30 . 1 1 69 69 LEU CD2 C 13 0.496 0.018 4.34E-11 3.71E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 31 . 1 1 70 70 THR CG2 C 13 0.624 0.01 5.03E-11 1.25E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 32 . 1 1 71 71 MET CE C 13 0.15 0.004 1.33E-11 1.71E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 33 . 1 1 72 72 MET CE C 13 0.482 0.004 2.14E-11 4.96E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 34 . 1 1 73 73 ALA CB C 13 0.723 0.011 3.46E-11 9.75E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 35 . 1 1 76 76 MET CE C 13 0.143 0 1.45E-11 2.24E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 36 . 1 1 85 85 ILE CG2 C 13 0.765 0.014 2.33E-11 1.10E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 37 . 1 1 88 88 ALA CB C 13 0.871 0.025 7.23E-11 3.63E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 38 . 1 1 91 91 VAL CG1 C 13 0.758 0.019 7.67E-11 3.62E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 39 . 1 1 100 100 ILE CD1 C 13 0.885 0.033 3.71E-11 2.99E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 40 . 1 1 100 100 ILE CG2 C 13 0.864 0.023 2.52E-11 1.63E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 41 . 1 1 102 102 ALA CB C 13 0.906 0.017 3.59E-11 1.22E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 42 . 1 1 105 105 LEU CD1 C 13 0.489 0.009 4.34E-11 1.64E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 43 . 1 1 105 105 LEU CD2 C 13 0.44 0.016 3.77E-11 2.88E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 44 . 1 1 108 108 VAL CG1 C 13 0.723 0.016 4.97E-11 1.95E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 45 . 1 1 108 108 VAL CG2 C 13 0.723 0.013 2.33E-11 1.06E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 46 . 1 1 109 109 MET CE C 13 0.383 0.004 1.64E-11 3.17E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 47 . 1 1 110 110 THR CG2 C 13 0.327 0.005 6.98E-11 1.41E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 48 . 1 1 112 112 LEU CD1 C 13 0.398 0.02 6.47E-11 6.03E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 49 . 1 1 121 121 VAL CG1 C 13 0.595 0.006 4.47E-11 8.63E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 50 . 1 1 121 121 VAL CG2 C 13 0.652 0.012 2.33E-11 1.08E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 51 . 1 1 125 125 ILE CD1 C 13 0.341 0.005 2.90E-11 7.03E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 52 . 1 1 125 125 ILE CG2 C 13 0.701 0.013 4.15E-11 1.31E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 53 . 1 1 128 128 ALA CB C 13 0.878 0.021 6.79E-11 2.95E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 54 . 1 1 130 130 ILE CD1 C 13 0.313 0.004 2.83E-11 6.21E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 55 . 1 1 130 130 ILE CG2 C 13 0.532 0.006 4.15E-11 6.84E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 56 . 1 1 136 136 VAL CG2 C 13 0.765 0.018 3.21E-11 1.61E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 57 . 1 1 142 142 VAL CG1 C 13 0.56 0.007 6.35E-11 1.59E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 58 . 1 1 142 142 VAL CG2 C 13 0.539 0.007 2.71E-11 8.29E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 59 . 1 1 144 144 MET CE C 13 0.553 0.006 1.52E-11 4.63E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 60 . 1 1 145 145 MET CE C 13 0.383 0.003 1.58E-11 3.91E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 61 . 1 1 146 146 THR CG2 C 13 0.588 0.008 4.78E-11 1.09E-12 . . . . . . . . . . . . . . . . . . . . . 15185 2 62 . 1 1 147 147 ALA CB C 13 0.461 0.004 3.96E-11 5.63E-13 . . . . . . . . . . . . . . . . . . . . . 15185 2 stop_ save_