data_15183 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 15183 _Entry.Title ; Backbone and side-chain methyl order parameters and effective correlation times for calmodulin in complex with CaMKKalpha peptide ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2007-03-18 _Entry.Accession_date 2007-03-18 _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 Michael Marlow . S. . 15183 2 Joshua Wand . . . 15183 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' . 15183 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID order_parameters 2 15183 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID 'order parameters' 205 15183 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 4 . . 2011-03-31 2007-03-18 update BMRB 'Residues corrected in backbone order parameter save frame' 15183 3 . . 2011-03-28 2007-03-18 update BMRB ; comp_index_ID values corrected in the order parameter save frames MET residue removed from sequence ; 15183 2 . . 2009-01-29 2007-03-18 update BMRB 'correction of entity ID in data table' 15183 1 . . 2007-10-05 2007-03-18 original author 'original release' 15183 stop_ save_ ############### # Citations # ############### save_primary_citation _Citation.Sf_category citations _Citation.Sf_framecode primary_citation _Citation.Entry_ID 15183 _Citation.ID 1 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 16846216 _Citation.Full_citation . _Citation.Title 'Conformational dynamics of calmodulin in complex with the calmodulin-dependent kinase kinase alpha calmodulin-binding domain.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 45 _Citation.Journal_issue 29 _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 8732 _Citation.Page_last 8741 _Citation.Year 2006 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Michael Marlow . S. . 15183 1 2 'A. Joshua' Wand . . . 15183 1 stop_ save_ save_citation_2 _Citation.Sf_category citations _Citation.Sf_framecode citation_2 _Citation.Entry_ID 15183 _Citation.ID 2 _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. . 15183 2 2 Michael Marlow . S. . 15183 2 3 Kathy Valentine . G. . 15183 2 4 'A. Joshua' Wand . . . 15183 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 15183 _Assembly.ID 1 _Assembly.Name CaM/CaMKKap _Assembly.BMRB_code . _Assembly.Number_of_components 2 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds no _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass 19997.4 _Assembly.Enzyme_commission_number . _Assembly.Details 'full length calmodulin bound to the calmodulin binding domain of calmodulin dependant kinase kinase alpha' _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 2 $calmodulin A . yes native no no . . . 15183 1 2 CaMKKalpha 1 $CaMKKalpha B . no native no no . . . 15183 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 BMRB 4270 . . 'solution NMR' . assignments . 15183 1 yes PDB 1IQ5 . . X-ray 1.8 'related structure' 'CaMKK beta isoform' 15183 1 yes PDB CKK1 . . 'solution NMR' . 'structure used in analysis' 'CaMKK alpha isoform' 15183 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'regulation of kinase activity' 15183 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_CaMKKalpha _Entity.Sf_category entity _Entity.Sf_framecode CaMKKalpha _Entity.Entry_ID 15183 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name CaMKKalpha _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 ; GSVKLIPSWTTVILVKSMLR KRSFGNPF ; _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 28 _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 yes GB AAC31608 . calmodulin . . . . . . . . . . . . . . 15183 1 2 no PDB 1CKK . "CalmodulinRAT CA2+CALMODULIN DEPENDENT PROTEIN KINASE Fragment" . . . . . 92.86 26 100.00 100.00 4.31e-08 . . . . 15183 1 3 no DBJ BAA75246 . "Ca/calmodulin-dependent protein kinase kinase alpha, CaM-kinase kinase alpha [Rattus norvegicus]" . . . . . 96.43 505 100.00 100.00 6.26e-09 . . . . 15183 1 4 no GB AAB46910 . "Ca2+/calmodulin-dependent protein kinase IV kinase isoform [Rattus sp.]" . . . . . 96.43 505 100.00 100.00 6.26e-09 . . . . 15183 1 5 no GB AAC42070 . "Ca2+/calmodulin-dependent protein kinase kinase [Rattus norvegicus]" . . . . . 96.43 505 100.00 100.00 5.90e-09 . . . . 15183 1 6 no GB EDM05132 . "calcium/calmodulin-dependent protein kinase kinase 1, alpha [Rattus norvegicus]" . . . . . 96.43 505 100.00 100.00 6.08e-09 . . . . 15183 1 7 no GB EGW04580 . "Calcium/calmodulin-dependent protein kinase kinase 1 [Cricetulus griseus]" . . . . . 96.43 505 100.00 100.00 5.90e-09 . . . . 15183 1 8 no GB EHB05791 . "Calcium/calmodulin-dependent protein kinase kinase 1 [Heterocephalus glaber]" . . . . . 96.43 531 100.00 100.00 7.97e-09 . . . . 15183 1 9 no PRF 2120334A . "Ca/calmodulin-dependent protein kinase kinase" . . . . . 96.43 505 100.00 100.00 5.90e-09 . . . . 15183 1 10 no REF NP_113850 . "calcium/calmodulin-dependent protein kinase kinase 1 [Rattus norvegicus]" . . . . . 96.43 505 100.00 100.00 6.26e-09 . . . . 15183 1 11 no REF XP_002718907 . "PREDICTED: calcium/calmodulin-dependent protein kinase kinase 1 [Oryctolagus cuniculus]" . . . . . 96.43 505 100.00 100.00 6.45e-09 . . . . 15183 1 12 no REF XP_003416891 . "PREDICTED: LOW QUALITY PROTEIN: calcium/calmodulin-dependent protein kinase kinase 1 [Loxodonta africana]" . . . . . 96.43 503 100.00 100.00 8.12e-09 . . . . 15183 1 13 no REF XP_003469697 . "PREDICTED: calcium/calmodulin-dependent protein kinase kinase 1 [Cavia porcellus]" . . . . . 96.43 505 100.00 100.00 4.95e-09 . . . . 15183 1 14 no REF XP_003509228 . "PREDICTED: calcium/calmodulin-dependent protein kinase kinase 1 [Cricetulus griseus]" . . . . . 96.43 505 100.00 100.00 5.90e-09 . . . . 15183 1 15 no SP P97756 . "RecName: Full=Calcium/calmodulin-dependent protein kinase kinase 1; Short=CaM-KK 1; Short=CaM-kinase kinase 1; Short=CaMKK 1; A" . . . . . 96.43 505 100.00 100.00 6.26e-09 . . . . 15183 1 stop_ loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'Ca2+-binding protein' 15183 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . GLY . 15183 1 2 . SER . 15183 1 3 . VAL . 15183 1 4 . LYS . 15183 1 5 . LEU . 15183 1 6 . ILE . 15183 1 7 . PRO . 15183 1 8 . SER . 15183 1 9 . TRP . 15183 1 10 . THR . 15183 1 11 . THR . 15183 1 12 . VAL . 15183 1 13 . ILE . 15183 1 14 . LEU . 15183 1 15 . VAL . 15183 1 16 . LYS . 15183 1 17 . SER . 15183 1 18 . MET . 15183 1 19 . LEU . 15183 1 20 . ARG . 15183 1 21 . LYS . 15183 1 22 . ARG . 15183 1 23 . SER . 15183 1 24 . PHE . 15183 1 25 . GLY . 15183 1 26 . ASN . 15183 1 27 . PRO . 15183 1 28 . PHE . 15183 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . GLY 1 1 15183 1 . SER 2 2 15183 1 . VAL 3 3 15183 1 . LYS 4 4 15183 1 . LEU 5 5 15183 1 . ILE 6 6 15183 1 . PRO 7 7 15183 1 . SER 8 8 15183 1 . TRP 9 9 15183 1 . THR 10 10 15183 1 . THR 11 11 15183 1 . VAL 12 12 15183 1 . ILE 13 13 15183 1 . LEU 14 14 15183 1 . VAL 15 15 15183 1 . LYS 16 16 15183 1 . SER 17 17 15183 1 . MET 18 18 15183 1 . LEU 19 19 15183 1 . ARG 20 20 15183 1 . LYS 21 21 15183 1 . ARG 22 22 15183 1 . SER 23 23 15183 1 . PHE 24 24 15183 1 . GLY 25 25 15183 1 . ASN 26 26 15183 1 . PRO 27 27 15183 1 . PHE 28 28 15183 1 stop_ save_ save_calmodulin _Entity.Sf_category entity _Entity.Sf_framecode calmodulin _Entity.Entry_ID 15183 _Entity.ID 2 _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 2015-01-31 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 15184 . calmodulin . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 2 no BMRB 15185 . calmodulin . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 3 no BMRB 15186 . calmodulin . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 4 no BMRB 15187 . calmodulin . . . . . 100.00 149 100.00 100.00 3.29e-101 . . . . 15183 2 5 no BMRB 15188 . calmodulin . . . . . 99.33 148 99.32 100.00 4.93e-100 . . . . 15183 2 6 no BMRB 15191 . Calmodulin . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 7 no BMRB 15470 . calmodulin . . . . . 99.33 148 97.97 100.00 9.74e-99 . . . . 15183 2 8 no BMRB 15624 . Calmodulin . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 9 no BMRB 15650 . calmodulin . . . . . 99.33 148 97.97 100.00 1.54e-98 . . . . 15183 2 10 no BMRB 15852 . calmodulin . . . . . 99.33 148 97.97 100.00 1.54e-98 . . . . 15183 2 11 no BMRB 16418 . apoCaM . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 12 no BMRB 16465 . entity_1 . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 13 no BMRB 16764 . CALMODULIN . . . . . 99.33 150 98.65 100.00 2.38e-99 . . . . 15183 2 14 no BMRB 17264 . calmodulin . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 15 no BMRB 17360 . entity_1 . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 16 no BMRB 17771 . Calmodulin . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 17 no BMRB 17807 . Calmodulin . . . . . 98.66 147 98.64 100.00 1.05e-98 . . . . 15183 2 18 no BMRB 18027 . CaM . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 19 no BMRB 18028 . CaM . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 20 no BMRB 18556 . Calmodulin . . . . . 99.33 148 97.30 99.32 9.76e-98 . . . . 15183 2 21 no BMRB 19036 . calmodulin . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 22 no BMRB 19238 . Calmodulin_prototypical_calcium_sensor . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 23 no BMRB 19586 . entity_1 . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 24 no BMRB 19604 . calmodulin . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 25 no BMRB 26503 . Calmodulin . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 26 no BMRB 4056 . calmodulin . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 27 no BMRB 5227 . CaM . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 28 no BMRB 6541 . calmodulin . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 29 no BMRB 6798 . calmodulin . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 30 no BMRB 6802 . calmodulin . . . . . 99.33 148 97.30 99.32 1.34e-97 . . . . 15183 2 31 no BMRB 6825 . calmodulin . . . . . 99.33 148 97.30 99.32 1.34e-97 . . . . 15183 2 32 no BMRB 6830 . calmodulin . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 33 no BMRB 6831 . calmodulin . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 34 no BMRB 7018 . calmodulin . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 35 no BMRB 7028 . calmodulin . . . . . 99.33 148 97.30 99.32 1.34e-97 . . . . 15183 2 36 no BMRB 7029 . calmodulin . . . . . 99.33 148 97.30 99.32 1.34e-97 . . . . 15183 2 37 no BMRB 7030 . calmodulin . . . . . 99.33 148 97.30 99.32 1.34e-97 . . . . 15183 2 38 no BMRB 7031 . calmodulin . . . . . 99.33 148 97.30 99.32 1.34e-97 . . . . 15183 2 39 no BMRB 7416 . calmodulin . . . . . 99.33 148 97.97 100.00 1.54e-98 . . . . 15183 2 40 no BMRB 7417 . calmodulin . . . . . 99.33 148 97.97 100.00 1.54e-98 . . . . 15183 2 41 no BMRB 7418 . calmodulin . . . . . 99.33 148 97.97 100.00 1.54e-98 . . . . 15183 2 42 no BMRB 7423 . calmodulin . . . . . 99.33 148 97.97 100.00 1.54e-98 . . . . 15183 2 43 no BMRB 7424 . calmodulin . . . . . 99.33 148 97.97 100.00 1.54e-98 . . . . 15183 2 44 no BMRB 7425 . calmodulin . . . . . 99.33 148 97.97 100.00 1.54e-98 . . . . 15183 2 45 no PDB 1A29 . "Calmodulin Complexed With Trifluoperazine (1:2 Complex)" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 46 no PDB 1CFC . "Calcium-Free Calmodulin" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 47 no PDB 1CFD . "Calcium-Free Calmodulin" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 48 no PDB 1CFF . "Nmr Solution Structure Of A Complex Of Calmodulin With A Binding Peptide Of The Ca2+-Pump" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 49 no PDB 1CKK . "CalmodulinRAT CA2+CALMODULIN DEPENDENT PROTEIN KINASE Fragment" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 50 no PDB 1CLL . "Calmodulin Structure Refined At 1.7 Angstroms Resolution" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 51 no PDB 1CM1 . "Motions Of Calmodulin-Single-Conformer Refinement" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 52 no PDB 1CM4 . "Motions Of Calmodulin-four-conformer Refinement" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 53 no PDB 1CTR . "Drug Binding By Calmodulin: Crystal Structure Of A Calmodulin-Trifluoperazine Complex" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 54 no PDB 1DMO . "Calmodulin, Nmr, 30 Structures" . . . . . 99.33 148 97.97 100.00 9.74e-99 . . . . 15183 2 55 no PDB 1G4Y . "1.60 A Crystal Structure Of The Gating Domain From Small Conductance Potassium Channel Complexed With Calcium-Calmodulin" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 56 no PDB 1IQ5 . "CalmodulinNEMATODE CA2+CALMODULIN DEPENDENT KINASE KINASE Fragment" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 57 no PDB 1IWQ . "Crystal Structure Of Marcks Calmodulin Binding Domain Peptide Complexed With Ca2+CALMODULIN" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 58 no PDB 1K90 . "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3' Deoxy-Atp" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 59 no PDB 1K93 . "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin" . . . . . 96.64 144 98.61 100.00 1.76e-96 . . . . 15183 2 60 no PDB 1L7Z . "Crystal Structure Of Ca2+/calmodulin Complexed With Myristoylated Cap-23/nap-22 Peptide" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 61 no PDB 1LIN . "Calmodulin Complexed With Trifluoperazine (1:4 Complex)" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 62 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 98.66 100.00 3.93e-100 . . . . 15183 2 63 no PDB 1MUX . "Solution Nmr Structure Of CalmodulinW-7 Complex: The Basis Of Diversity In Molecular Recognition, 30 Structures" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 64 no PDB 1NWD . "Solution Structure Of Ca2+CALMODULIN BOUND TO THE C- Terminal Domain Of Petunia Glutamate Decarboxylase" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 65 no PDB 1PRW . "Crystal Structure Of Bovine Brain Ca++ Calmodulin In A Compact Form" . . . . . 99.33 149 97.97 99.32 1.84e-98 . . . . 15183 2 66 no PDB 1QIV . "Calmodulin Complexed With N-(3,3,-Diphenylpropyl)-N'-[1-R-( 3,4-Bis-Butoxyphenyl)-Ethyl]-Propylenediamine (Dpd), 1:2 Complex" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 67 no PDB 1QIW . "Calmodulin Complexed With N-(3,3,-Diphenylpropyl)-N'-[1-R-( 3,4-Bis-Butoxyphenyl)-Ethyl]-Propylenediamine (Dpd)" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 68 no PDB 1QX5 . "Crystal Structure Of Apocalmodulin" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 69 no PDB 1S26 . "Structure Of Anthrax Edema Factor-calmodulin-alpha,beta- Methyleneadenosine 5'-triphosphate Complex Reveals An Alternative Mode" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 70 no PDB 1SK6 . "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin, 3',5' Cyclic Amp (Cam" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 71 no PDB 1SY9 . "Structure Of Calmodulin Complexed With A Fragment Of The Olfactory Cng Channel" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 72 no PDB 1UP5 . "Chicken Calmodulin" . . . . . 99.33 148 97.97 99.32 1.78e-98 . . . . 15183 2 73 no PDB 1WRZ . "Calmodulin Complexed With A Peptide From A Human Death-Associated Protein Kinase" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 74 no PDB 1X02 . "Solution Structure Of Stereo Array Isotope Labeled (Sail) Calmodulin" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 75 no PDB 1XA5 . "Structure Of Calmodulin In Complex With Kar-2, A Bis-Indol Alkaloid" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 76 no PDB 1XFU . "Crystal Structure Of Anthrax Edema Factor (ef) Truncation Mutant, Ef-delta 64 In Complex With Calmodulin" . . . . . 100.00 149 97.99 100.00 1.02e-99 . . . . 15183 2 77 no PDB 1XFV . "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3' Deoxy-Atp" . . . . . 100.00 149 97.99 100.00 1.02e-99 . . . . 15183 2 78 no PDB 1XFW . "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3'5' Cyclic Amp (Camp)" . . . . . 100.00 149 97.99 100.00 1.02e-99 . . . . 15183 2 79 no PDB 1XFY . "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin" . . . . . 100.00 149 97.99 100.00 1.02e-99 . . . . 15183 2 80 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 97.99 100.00 1.02e-99 . . . . 15183 2 81 no PDB 1Y0V . "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And Pyrophosphate" . . . . . 96.64 146 98.61 100.00 1.51e-96 . . . . 15183 2 82 no PDB 1YR5 . "1.7-A Structure Of Calmodulin Bound To A Peptide From Dap Kinase" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 83 no PDB 2BCX . "Crystal Structure Of Calmodulin In Complex With A Ryanodine Receptor Peptide" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 84 no PDB 2BKI . "Myosin Vi Nucleotide-Free (Mdinsert2-Iq) Crystal Structure" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 85 no PDB 2DFS . "3-D Structure Of Myosin-V Inhibited State" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 86 no PDB 2F2O . "Structure Of Calmodulin Bound To A Calcineurin Peptide: A New Way Of Making An Old Binding Mode" . . . . . 100.00 179 98.66 100.00 4.55e-100 . . . . 15183 2 87 no PDB 2F2P . "Structure Of Calmodulin Bound To A Calcineurin Peptide: A New Way Of Making An Old Binding Mode" . . . . . 100.00 179 98.66 100.00 4.55e-100 . . . . 15183 2 88 no PDB 2F3Y . "CalmodulinIQ DOMAIN COMPLEX" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 89 no PDB 2F3Z . "CalmodulinIQ-Aa Domain Complex" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 90 no PDB 2FOT . "Crystal Structure Of The Complex Between Calmodulin And Alphaii-Spectrin" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 91 no PDB 2HQW . "Crystal Structure Of Ca2+CALMODULIN BOUND TO NMDA RECEPTOR NR1C1 Peptide" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 92 no PDB 2JZI . "Structure Of Calmodulin Complexed With The Calmodulin Binding Domain Of Calcineurin" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 93 no PDB 2K0E . "A Coupled Equilibrium Shift Mechanism In Calmodulin- Mediated Signal Transduction" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 94 no PDB 2K0F . "Calmodulin Complexed With Calmodulin-Binding Peptide From Smooth Muscle Myosin Light Chain Kinase" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 95 no PDB 2K0J . "Solution Structure Of Cam Complexed To Drp1p" . . . . . 99.33 148 97.97 100.00 1.54e-98 . . . . 15183 2 96 no PDB 2K61 . "Solution Structure Of Cam Complexed To Dapk Peptide" . . . . . 99.33 148 97.97 100.00 1.54e-98 . . . . 15183 2 97 no PDB 2KDU . "Structural Basis Of The Munc13-1CA2+-Calmodulin Interaction: A Novel 1-26 Calmodulin Binding Motif With A Bipartite Binding Mod" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 98 no PDB 2KNE . "Calmodulin Wraps Around Its Binding Domain In The Plasma Membrane Ca2+ Pump Anchored By A Novel 18-1 Motif" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 99 no PDB 2L53 . "Solution Nmr Structure Of Apo-Calmodulin In Complex With The Iq Motif Of Human Cardiac Sodium Channel Nav1.5" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 100 no PDB 2L7L . "Solution Structure Of Ca2+CALMODULIN COMPLEXED WITH A PEPTIDE Representing The Calmodulin-Binding Domain Of Calmodulin Kinase I" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 101 no PDB 2LGF . "Solution Structure Of Ca2+CALMODULIN COMPLEXED WITH A PEPTIDE Representing The Calmodulin-Binding Domain Of L-Selectin" . . . . . 97.99 146 98.63 100.00 5.64e-98 . . . . 15183 2 102 no PDB 2LL6 . "Solution Nmr Structure Of Cam Bound To Inos Cam Binding Domain Peptide" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 103 no PDB 2LL7 . "Solution Nmr Structure Of Cam Bound To The Enos Cam Binding Domain Peptide" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 104 no PDB 2LV6 . "The Complex Between Ca-calmodulin And Skeletal Muscle Myosin Light Chain Kinase From Combination Of Nmr And Aqueous And Contras" . . . . . 99.33 148 97.30 99.32 9.76e-98 . . . . 15183 2 105 no PDB 2M0J . "3d Structure Of Calmodulin And Calmodulin Binding Domain Of Olfactory Cyclic Nucleotide-gated Ion Channel Complex" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 106 no PDB 2M0K . "3d Structure Of Calmodulin And Calmodulin Binding Domain Of Rat Olfactory Cyclic Nucleotide-gated Ion Channel" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 107 no PDB 2M55 . "Nmr Structure Of The Complex Of An N-terminally Acetylated Alpha- Synuclein Peptide With Calmodulin" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 108 no PDB 2MG5 . "Solution Structure Of Calmodulin Bound To The Target Peptide Of Endothelial Nitrogen Oxide Synthase Phosphorylated At Thr495" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 109 no PDB 2MGU . "Structure Of The Complex Between Calmodulin And The Binding Domain Of Hiv-1 Matrix Protein" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 110 no PDB 2O5G . "Calmodulin-Smooth Muscle Light Chain Kinase Peptide Complex" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 111 no PDB 2O60 . "Calmodulin Bound To Peptide From Neuronal Nitric Oxide Synthase" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 112 no PDB 2R28 . "The Complex Structure Of Calmodulin Bound To A Calcineurin Peptide" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 113 no PDB 2V01 . "Recombinant Vertebrate Calmodulin Complexed With Pb" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 114 no PDB 2V02 . "Recombinant Vertebrate Calmodulin Complexed With Ba" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 115 no PDB 2VAY . "Calmodulin Complexed With Cav1.1 Iq Peptide" . . . . . 97.99 146 98.63 100.00 5.64e-98 . . . . 15183 2 116 no PDB 2VB6 . "Myosin Vi (Md-Insert2-Cam, Delta Insert1) Post-Rigor State ( Crystal Form 2)" . . . . . 100.00 149 97.32 99.33 1.43e-98 . . . . 15183 2 117 no PDB 2W73 . "High-Resolution Structure Of The Complex Between Calmodulin And A Peptide From Calcineurin A" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 118 no PDB 2WEL . "Crystal Structure Of Su6656-Bound CalciumCALMODULIN- Dependent Protein Kinase Ii Delta In Complex With Calmodulin" . . . . . 100.00 150 98.66 100.00 2.38e-100 . . . . 15183 2 119 no PDB 2X0G . "X-ray Structure Of A Dap-kinase Calmodulin Complex" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 120 no PDB 2Y4V . "Crystal Structure Of Human Calmodulin In Complex With A Dap Kinase-1 Mutant (W305y) Peptide" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 121 no PDB 2YGG . "Complex Of Cambr And Cam" . . . . . 100.00 150 98.66 100.00 3.37e-100 . . . . 15183 2 122 no PDB 3BXK . "Crystal Structure Of The PQ-Type Calcium Channel (Cav2.1) Iq Domain And Ca2+calmodulin Complex" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 123 no PDB 3BXL . "Crystal Structure Of The R-Type Calcium Channel (Cav2.3) Iq Domain And Ca2+calmodulin Complex" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 124 no PDB 3BYA . "Structure Of A Calmodulin Complex" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 125 no PDB 3CLN . "Structure Of Calmodulin Refined At 2.2 Angstroms Resolution" . . . . . 99.33 148 97.97 100.00 9.74e-99 . . . . 15183 2 126 no PDB 3DVE . "Crystal Structure Of Ca2+CAM-Cav2.2 Iq Domain Complex" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 127 no PDB 3DVJ . "Crystal Structure Of Ca2+CAM-Cav2.2 Iq Domain (Without Cloning Artifact, Hm To Tv) Complex" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 128 no PDB 3DVK . "Crystal Structure Of Ca2+CAM-Cav2.3 Iq Domain Complex" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 129 no PDB 3DVM . "Crystal Structure Of Ca2+CAM-Cav2.1 Iq Domain Complex" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 130 no PDB 3EK4 . "Calcium-saturated Gcamp2 Monomer" . . . . . 98.66 449 98.64 100.00 4.92e-95 . . . . 15183 2 131 no PDB 3EK7 . "Calcium-Saturated Gcamp2 Dimer" . . . . . 98.66 449 98.64 100.00 4.92e-95 . . . . 15183 2 132 no PDB 3EK8 . "Calcium-Saturated Gcamp2 T116vG87R MUTANT MONOMER" . . . . . 98.66 449 98.64 100.00 5.36e-95 . . . . 15183 2 133 no PDB 3EKH . "Calcium-Saturated Gcamp2 T116vK378W MUTANT MONOMER" . . . . . 98.66 449 97.96 99.32 4.86e-94 . . . . 15183 2 134 no PDB 3EVU . "Crystal Structure Of Calcium Bound Dimeric Gcamp2, (#1)" . . . . . 98.66 449 98.64 100.00 4.92e-95 . . . . 15183 2 135 no PDB 3EVV . "Crystal Structure Of Calcium Bound Dimeric Gcamp2 (#2)" . . . . . 98.66 449 98.64 100.00 4.92e-95 . . . . 15183 2 136 no PDB 3EWT . "Crystal Structure Of Calmodulin Complexed With A Peptide" . . . . . 99.33 154 98.65 100.00 8.94e-100 . . . . 15183 2 137 no PDB 3EWV . "Crystal Structure Of Calmodulin Complexed With A Peptide" . . . . . 99.33 154 98.65 100.00 8.94e-100 . . . . 15183 2 138 no PDB 3G43 . "Crystal Structure Of The Calmodulin-Bound Cav1.2 C-Terminal Regulatory Domain Dimer" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 139 no PDB 3GOF . "Calmodulin Bound To Peptide From Macrophage Nitric Oxide Synthase" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 140 no PDB 3HR4 . "Human Inos Reductase And Calmodulin Complex" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 141 no PDB 3IF7 . "Structure Of Calmodulin Complexed With Its First Endogenous Inhibitor, Sphingosylphosphorylcholine" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 142 no PDB 3J41 . "Pseudo-atomic Model Of The Aquaporin-0/calmodulin Complex Derived From Electron Microscopy" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 143 no PDB 3O77 . "The Structure Of Ca2+ Sensor (Case-16)" . . . . . 98.66 415 98.64 100.00 2.72e-95 . . . . 15183 2 144 no PDB 3O78 . "The Structure Of Ca2+ Sensor (Case-12)" . . . . . 98.66 415 98.64 100.00 2.94e-95 . . . . 15183 2 145 no PDB 3OXQ . "Crystal Structure Of Ca2+CAM-Cav1.2 Pre-IqIQ DOMAIN COMPLEX" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 146 no PDB 3SG2 . "Crystal Structure Of Gcamp2-t116v,d381y" . . . . . 98.66 449 97.96 99.32 8.90e-94 . . . . 15183 2 147 no PDB 3SG3 . "Crystal Structure Of Gcamp3-d380y" . . . . . 98.66 449 97.28 99.32 6.42e-93 . . . . 15183 2 148 no PDB 3SG6 . "Crystal Structure Of Dimeric Gcamp2-lia(linker 1)" . . . . . 98.66 450 98.64 100.00 4.44e-95 . . . . 15183 2 149 no PDB 3SG7 . "Crystal Structure Of Gcamp3-kf(linker 1)" . . . . . 98.66 448 97.96 100.00 4.99e-94 . . . . 15183 2 150 no PDB 3SJQ . "Crystal Structure Of A Small Conductance Potassium Channel Splice Variant Complexed With Calcium-Calmodulin" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 151 no PDB 3SUI . "Crystal Structure Of Ca2+-Calmodulin In Complex With A Trpv1 C- Terminal Peptide" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 152 no PDB 3U0K . "Crystal Structure Of The Genetically Encoded Calcium Indicator Rcamp" . . . . . 98.66 440 97.28 99.32 9.85e-94 . . . . 15183 2 153 no PDB 3WFN . "Crystal Structure Of Nav1.6 Iq Motif In Complex With Apo-cam" . . . . . 100.00 182 98.66 100.00 3.71e-100 . . . . 15183 2 154 no PDB 4BW7 . "Calmodulin In Complex With Strontium" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 155 no PDB 4BW8 . "Calmodulin With Small Bend In Central Helix" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 156 no PDB 4BYF . "Crystal Structure Of Human Myosin 1c In Complex With Calmodulin In The Pre-power Stroke State" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 157 no PDB 4DCK . "Crystal Structure Of The C-Terminus Of Voltage-Gated Sodium Channel In Complex With Fgf13 And Cam" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 158 no PDB 4DJC . "1.35 A Crystal Structure Of The Nav1.5 Diii-Iv-CaCAM COMPLEX" . . . . . 100.00 152 98.66 100.00 2.23e-100 . . . . 15183 2 159 no PDB 4E50 . "Calmodulin And Ng Peptide Complex" . . . . . 100.00 185 98.66 100.00 2.00e-100 . . . . 15183 2 160 no PDB 4EHQ . "Crystal Structure Of Calmodulin Binding Domain Of Orai1 In Complex With Ca2+CALMODULIN DISPLAYS A UNIQUE BINDING MODE" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 161 no PDB 4G27 . "Calcium-Calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And P" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 162 no PDB 4G28 . "Calcium-Calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And E" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 163 no PDB 4HEX . "A Novel Conformation Of Calmodulin" . . . . . 100.00 156 98.66 100.00 1.49e-100 . . . . 15183 2 164 no PDB 4IK1 . "High Resolution Structure Of Gcampj At Ph 8.5" . . . . . 98.66 448 97.28 99.32 5.43e-93 . . . . 15183 2 165 no PDB 4IK3 . "High Resolution Structure Of Gcamp3 At Ph 8.5" . . . . . 98.66 448 97.96 100.00 3.93e-94 . . . . 15183 2 166 no PDB 4IK4 . "High Resolution Structure Of Gcamp3 At Ph 5.0" . . . . . 98.66 448 97.96 100.00 3.93e-94 . . . . 15183 2 167 no PDB 4IK5 . "High Resolution Structure Of Delta-rest-gcamp3" . . . . . 98.66 414 97.96 100.00 1.80e-94 . . . . 15183 2 168 no PDB 4IK8 . "High Resolution Structure Of Gcamp3 Dimer Form 1 At Ph 7.5" . . . . . 98.66 448 97.96 100.00 3.93e-94 . . . . 15183 2 169 no PDB 4IK9 . "High Resolution Structure Of Gcamp3 Dimer Form 2 At Ph 7.5" . . . . . 98.66 448 97.96 100.00 3.93e-94 . . . . 15183 2 170 no PDB 4J9Y . "Calcium-calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 171 no PDB 4J9Z . "Calcium-calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And N" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 172 no PDB 4JPZ . "Voltage-gated Sodium Channel 1.2 C-terminal Domain In Complex With Fgf13u And Ca2+/calmodulin" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 173 no PDB 4JQ0 . "Voltage-gated Sodium Channel 1.5 C-terminal Domain In Complex With Fgf12b And Ca2+/calmodulin" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 174 no PDB 4L79 . "Crystal Structure Of Nucleotide-free Myosin 1b Residues 1-728 With Bound Calmodulin" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 175 no PDB 4LZX . "Complex Of Iqcg And Ca2+-free Cam" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 176 no PDB 4M1L . "Complex Of Iqcg And Ca2+-bound Cam" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 177 no PDB 4Q5U . "Structure Of Calmodulin Bound To Its Recognition Site From Calcineurin" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 178 no PDB 4QNH . "Calcium-calmodulin (t79d) Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Sk2-a" . . . . . 100.00 149 97.99 99.33 4.90e-99 . . . . 15183 2 179 no PDB 4R8G . "Crystal Structure Of Myosin-1c Tail In Complex With Calmodulin" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 180 no PDB 4UMO . "Crystal Structure Of The Kv7.1 Proximal C-terminal Domain In Complex With Calmodulin" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 181 no PDB 4UPU . "Crystal Structure Of Ip3 3-k Calmodulin Binding Region In Complex With Calmodulin" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 182 no PDB 4V0C . "Crystal Structure Of The Kv7.1 Proximal C-terminal Domain In Complex With Calmodulin" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 183 no DBJ BAA08302 . "calmodulin [Homo sapiens]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 184 no DBJ BAA11896 . "calmodulin [Anas platyrhynchos]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 185 no DBJ BAB23462 . "unnamed protein product [Mus musculus]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 186 no DBJ BAB28116 . "unnamed protein product [Mus musculus]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 187 no DBJ BAB28319 . "unnamed protein product [Mus musculus]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 188 no EMBL CAA32050 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 189 no EMBL CAA32062 . "calmodulin II [Rattus norvegicus]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 190 no EMBL CAA32119 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 191 no EMBL CAA32120 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 192 no EMBL CAA32478 . "calmodulin III [Rattus norvegicus]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 193 no GB AAA35635 . "calmodulin [Homo sapiens]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 194 no GB AAA35641 . "calmodulin [Homo sapiens]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 195 no GB AAA37365 . "calmodulin synthesis [Mus musculus]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 196 no GB AAA40862 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 197 no GB AAA40863 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 198 no PIR JC1305 . "calmodulin - Japanese medaka" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 199 no PIR MCON . "calmodulin - salmon" . . . . . 99.33 148 98.65 100.00 2.23e-99 . . . . 15183 2 200 no REF NP_001008160 . "calmodulin 2 (phosphorylase kinase, delta) [Xenopus (Silurana) tropicalis]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 201 no REF NP_001009759 . "calmodulin [Ovis aries]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 202 no REF NP_001039714 . "calmodulin [Bos taurus]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 203 no REF NP_001080864 . "calmodulin [Xenopus laevis]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 204 no REF NP_001084025 . "calmodulin [Xenopus laevis]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 205 no SP P02594 . "RecName: Full=Calmodulin; Short=CaM [Electrophorus electricus]" . . . . . 100.00 149 97.99 100.00 1.32e-99 . . . . 15183 2 206 no SP P21251 . "RecName: Full=Calmodulin; Short=CaM [Apostichopus japonicus]" . . . . . 100.00 149 97.32 99.33 8.45e-99 . . . . 15183 2 207 no SP P62144 . "RecName: Full=Calmodulin; Short=CaM [Anas platyrhynchos]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 208 no SP P62149 . "RecName: Full=Calmodulin; Short=CaM [Gallus gallus]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 209 no SP P62151 . "RecName: Full=Calmodulin; Short=CaM [Torpedo californica]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 210 no TPG DAA13808 . "TPA: calmodulin 2-like [Bos taurus]" . . . . . 100.00 216 97.32 98.66 1.80e-98 . . . . 15183 2 211 no TPG DAA18029 . "TPA: calmodulin [Bos taurus]" . . . . . 100.00 149 97.32 99.33 6.43e-99 . . . . 15183 2 212 no TPG DAA19590 . "TPA: calmodulin 3 [Bos taurus]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 213 no TPG DAA24777 . "TPA: calmodulin 2-like [Bos taurus]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 214 no TPG DAA24988 . "TPA: calmodulin 2-like isoform 1 [Bos taurus]" . . . . . 100.00 149 98.66 100.00 3.93e-100 . . . . 15183 2 stop_ loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'Ca2+-binding protein' 15183 2 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . ALA . 15183 2 2 . ASP . 15183 2 3 . GLN . 15183 2 4 . LEU . 15183 2 5 . THR . 15183 2 6 . GLU . 15183 2 7 . GLU . 15183 2 8 . GLN . 15183 2 9 . ILE . 15183 2 10 . ALA . 15183 2 11 . GLU . 15183 2 12 . PHE . 15183 2 13 . LYS . 15183 2 14 . GLU . 15183 2 15 . ALA . 15183 2 16 . PHE . 15183 2 17 . SER . 15183 2 18 . LEU . 15183 2 19 . PHE . 15183 2 20 . ASP . 15183 2 21 . LYS . 15183 2 22 . ASP . 15183 2 23 . GLY . 15183 2 24 . ASP . 15183 2 25 . GLY . 15183 2 26 . THR . 15183 2 27 . ILE . 15183 2 28 . THR . 15183 2 29 . THR . 15183 2 30 . LYS . 15183 2 31 . GLU . 15183 2 32 . LEU . 15183 2 33 . GLY . 15183 2 34 . THR . 15183 2 35 . VAL . 15183 2 36 . MET . 15183 2 37 . ARG . 15183 2 38 . SER . 15183 2 39 . LEU . 15183 2 40 . GLY . 15183 2 41 . GLN . 15183 2 42 . ASN . 15183 2 43 . PRO . 15183 2 44 . THR . 15183 2 45 . GLU . 15183 2 46 . ALA . 15183 2 47 . GLU . 15183 2 48 . LEU . 15183 2 49 . GLN . 15183 2 50 . ASP . 15183 2 51 . MET . 15183 2 52 . ILE . 15183 2 53 . ASN . 15183 2 54 . GLU . 15183 2 55 . VAL . 15183 2 56 . ASP . 15183 2 57 . ALA . 15183 2 58 . ASP . 15183 2 59 . GLY . 15183 2 60 . ASN . 15183 2 61 . GLY . 15183 2 62 . THR . 15183 2 63 . ILE . 15183 2 64 . ASP . 15183 2 65 . PHE . 15183 2 66 . PRO . 15183 2 67 . GLU . 15183 2 68 . PHE . 15183 2 69 . LEU . 15183 2 70 . THR . 15183 2 71 . MET . 15183 2 72 . MET . 15183 2 73 . ALA . 15183 2 74 . ARG . 15183 2 75 . LYS . 15183 2 76 . MET . 15183 2 77 . LYS . 15183 2 78 . ASP . 15183 2 79 . THR . 15183 2 80 . ASP . 15183 2 81 . SER . 15183 2 82 . GLU . 15183 2 83 . GLU . 15183 2 84 . GLU . 15183 2 85 . ILE . 15183 2 86 . ARG . 15183 2 87 . GLU . 15183 2 88 . ALA . 15183 2 89 . PHE . 15183 2 90 . ARG . 15183 2 91 . VAL . 15183 2 92 . PHE . 15183 2 93 . ASP . 15183 2 94 . LYS . 15183 2 95 . ASP . 15183 2 96 . GLY . 15183 2 97 . ASN . 15183 2 98 . GLY . 15183 2 99 . TYR . 15183 2 100 . ILE . 15183 2 101 . SER . 15183 2 102 . ALA . 15183 2 103 . ALA . 15183 2 104 . GLU . 15183 2 105 . LEU . 15183 2 106 . ARG . 15183 2 107 . HIS . 15183 2 108 . VAL . 15183 2 109 . MET . 15183 2 110 . THR . 15183 2 111 . ASN . 15183 2 112 . LEU . 15183 2 113 . GLY . 15183 2 114 . GLU . 15183 2 115 . LYS . 15183 2 116 . LEU . 15183 2 117 . THR . 15183 2 118 . ASP . 15183 2 119 . GLU . 15183 2 120 . GLU . 15183 2 121 . VAL . 15183 2 122 . ASP . 15183 2 123 . GLU . 15183 2 124 . MET . 15183 2 125 . ILE . 15183 2 126 . ARG . 15183 2 127 . GLU . 15183 2 128 . ALA . 15183 2 129 . ASP . 15183 2 130 . ILE . 15183 2 131 . ASP . 15183 2 132 . GLY . 15183 2 133 . ASP . 15183 2 134 . GLY . 15183 2 135 . GLN . 15183 2 136 . VAL . 15183 2 137 . ASN . 15183 2 138 . TYR . 15183 2 139 . GLU . 15183 2 140 . GLU . 15183 2 141 . PHE . 15183 2 142 . VAL . 15183 2 143 . GLN . 15183 2 144 . MET . 15183 2 145 . MET . 15183 2 146 . THR . 15183 2 147 . ALA . 15183 2 148 . LYS . 15183 2 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . ALA 1 1 15183 2 . ASP 2 2 15183 2 . GLN 3 3 15183 2 . LEU 4 4 15183 2 . THR 5 5 15183 2 . GLU 6 6 15183 2 . GLU 7 7 15183 2 . GLN 8 8 15183 2 . ILE 9 9 15183 2 . ALA 10 10 15183 2 . GLU 11 11 15183 2 . PHE 12 12 15183 2 . LYS 13 13 15183 2 . GLU 14 14 15183 2 . ALA 15 15 15183 2 . PHE 16 16 15183 2 . SER 17 17 15183 2 . LEU 18 18 15183 2 . PHE 19 19 15183 2 . ASP 20 20 15183 2 . LYS 21 21 15183 2 . ASP 22 22 15183 2 . GLY 23 23 15183 2 . ASP 24 24 15183 2 . GLY 25 25 15183 2 . THR 26 26 15183 2 . ILE 27 27 15183 2 . THR 28 28 15183 2 . THR 29 29 15183 2 . LYS 30 30 15183 2 . GLU 31 31 15183 2 . LEU 32 32 15183 2 . GLY 33 33 15183 2 . THR 34 34 15183 2 . VAL 35 35 15183 2 . MET 36 36 15183 2 . ARG 37 37 15183 2 . SER 38 38 15183 2 . LEU 39 39 15183 2 . GLY 40 40 15183 2 . GLN 41 41 15183 2 . ASN 42 42 15183 2 . PRO 43 43 15183 2 . THR 44 44 15183 2 . GLU 45 45 15183 2 . ALA 46 46 15183 2 . GLU 47 47 15183 2 . LEU 48 48 15183 2 . GLN 49 49 15183 2 . ASP 50 50 15183 2 . MET 51 51 15183 2 . ILE 52 52 15183 2 . ASN 53 53 15183 2 . GLU 54 54 15183 2 . VAL 55 55 15183 2 . ASP 56 56 15183 2 . ALA 57 57 15183 2 . ASP 58 58 15183 2 . GLY 59 59 15183 2 . ASN 60 60 15183 2 . GLY 61 61 15183 2 . THR 62 62 15183 2 . ILE 63 63 15183 2 . ASP 64 64 15183 2 . PHE 65 65 15183 2 . PRO 66 66 15183 2 . GLU 67 67 15183 2 . PHE 68 68 15183 2 . LEU 69 69 15183 2 . THR 70 70 15183 2 . MET 71 71 15183 2 . MET 72 72 15183 2 . ALA 73 73 15183 2 . ARG 74 74 15183 2 . LYS 75 75 15183 2 . MET 76 76 15183 2 . LYS 77 77 15183 2 . ASP 78 78 15183 2 . THR 79 79 15183 2 . ASP 80 80 15183 2 . SER 81 81 15183 2 . GLU 82 82 15183 2 . GLU 83 83 15183 2 . GLU 84 84 15183 2 . ILE 85 85 15183 2 . ARG 86 86 15183 2 . GLU 87 87 15183 2 . ALA 88 88 15183 2 . PHE 89 89 15183 2 . ARG 90 90 15183 2 . VAL 91 91 15183 2 . PHE 92 92 15183 2 . ASP 93 93 15183 2 . LYS 94 94 15183 2 . ASP 95 95 15183 2 . GLY 96 96 15183 2 . ASN 97 97 15183 2 . GLY 98 98 15183 2 . TYR 99 99 15183 2 . ILE 100 100 15183 2 . SER 101 101 15183 2 . ALA 102 102 15183 2 . ALA 103 103 15183 2 . GLU 104 104 15183 2 . LEU 105 105 15183 2 . ARG 106 106 15183 2 . HIS 107 107 15183 2 . VAL 108 108 15183 2 . MET 109 109 15183 2 . THR 110 110 15183 2 . ASN 111 111 15183 2 . LEU 112 112 15183 2 . GLY 113 113 15183 2 . GLU 114 114 15183 2 . LYS 115 115 15183 2 . LEU 116 116 15183 2 . THR 117 117 15183 2 . ASP 118 118 15183 2 . GLU 119 119 15183 2 . GLU 120 120 15183 2 . VAL 121 121 15183 2 . ASP 122 122 15183 2 . GLU 123 123 15183 2 . MET 124 124 15183 2 . ILE 125 125 15183 2 . ARG 126 126 15183 2 . GLU 127 127 15183 2 . ALA 128 128 15183 2 . ASP 129 129 15183 2 . ILE 130 130 15183 2 . ASP 131 131 15183 2 . GLY 132 132 15183 2 . ASP 133 133 15183 2 . GLY 134 134 15183 2 . GLN 135 135 15183 2 . VAL 136 136 15183 2 . ASN 137 137 15183 2 . TYR 138 138 15183 2 . GLU 139 139 15183 2 . GLU 140 140 15183 2 . PHE 141 141 15183 2 . VAL 142 142 15183 2 . GLN 143 143 15183 2 . MET 144 144 15183 2 . MET 145 145 15183 2 . THR 146 146 15183 2 . ALA 147 147 15183 2 . LYS 148 148 15183 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 15183 _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 2 $calmodulin . 9031 organism . 'Gallus gallus' chicken . . Eukaryota Metazoa Gallus gallus . . . . . . . . . . . . . . . . . . . . . 15183 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 15183 _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 2 $calmodulin . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pET . . . . . . 15183 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 15183 _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 '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 calmodulin '[U-100% 15N]' . . 2 $calmodulin . . 1.0 . . mM . . . . 15183 1 2 CaMKKalpha 'natural abundance' . . 1 $CaMKKalpha . . . 1.1 1.2 mM . . . . 15183 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 15183 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details 'Uniform 15N/13C; 60% 2H CaM for methyl relaxation experiments' _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 calmodulin '[U-100% 13C; U-100% 15N; 60% 2H]' . . 2 $calmodulin . . 1.0 . . mM . . . . 15183 2 2 CaMKKalpha 'natural abundance' . . 1 $CaMKKalpha . . . 1.1 1.2 mM . . . . 15183 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 15183 _Sample_condition_list.ID 1 _Sample_condition_list.Details '10mM imidazole, pH 6.5, 100mM KCl, 6mM CaCl2, 0.04% 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 15183 1 pressure 1 . atm 15183 1 temperature 308 . K 15183 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 15183 _Software.ID 1 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 15183 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 15183 1 stop_ save_ save_NMRDraw _Software.Sf_category software _Software.Sf_framecode NMRDraw _Software.Entry_ID 15183 _Software.ID 2 _Software.Name NMRDraw _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 15183 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'peak picking' 15183 2 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 15183 _Software.ID 3 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 15183 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'peak picking' 15183 3 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 15183 _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 15183 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 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 15183 _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 . . . 15183 1 2 spectrometer_2 Varian INOVA . 750 . . . 15183 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 15183 _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 . . . . . . . . . . . . . . . . 15183 1 2 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 15183 1 3 '2D 1H-13C HSQC' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 15183 1 4 '2D 1H-13C HSQC' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 15183 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 15183 _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 . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details 'Backbone amide T1 & T2 were collected as 12 HSQCs - 9 delay times, 3 of which were collected in duplicate. {1H}-15N NOE collected with and without 5s 1H saturation' 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 15183 _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 . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details 'Methyl IzCzDz,IzCzDy & IzCz experiments were collected as 12 HSQCs - 9 delay times, 3 of which were collected in duplicate.' save_ ###################### # Order parameters # ###################### save_Backbone_amide_order_parmaeters _Order_parameter_list.Sf_category order_parameters _Order_parameter_list.Sf_framecode Backbone_amide_order_parmaeters _Order_parameter_list.Entry_ID 15183 _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 CaMKKalphap determined with relaxation data obtained at 500 and 750 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' . . . 15183 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 2 2 2 ASP N N 15 0.693 0.005 5.00E-14 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 2 . 1 2 3 3 GLN N N 15 0.4 0 2.98E-10 1.23E-12 . . . . . . . . . . . . . . . . . . . . . 15183 1 3 . 1 2 4 4 LEU N N 15 0.882 0.008 6.83E-10 5.46E-11 . . . . . . . . . . . . . . . . . . . . . 15183 1 4 . 1 2 5 5 THR N N 15 0.901 0.001 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 5 . 1 2 6 6 GLU N N 15 0.953 0.014 2.55E-11 4.79E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 6 . 1 2 7 7 GLU N N 15 0.905 0 1.00E-09 2.00E-12 . . . . . . . . . . . . . . . . . . . . . 15183 1 7 . 1 2 8 8 GLN N N 15 0.939 0.007 8.42E-11 1.43E-11 . . . . . . . . . . . . . . . . . . . . . 15183 1 8 . 1 2 9 9 ILE N N 15 0.948 0.003 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 9 . 1 2 10 10 ALA N N 15 0.957 0.004 1.00E-09 7.98E-11 . . . . . . . . . . . . . . . . . . . . . 15183 1 10 . 1 2 11 11 GLU N N 15 0.939 0.003 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 11 . 1 2 12 12 PHE N N 15 0.972 0.002 1.00E-09 8.00E-11 . . . . . . . . . . . . . . . . . . . . . 15183 1 12 . 1 2 13 13 LYS N N 15 0.967 0.003 1.00E-09 8.02E-11 . . . . . . . . . . . . . . . . . . . . . 15183 1 13 . 1 2 14 14 GLU N N 15 0.962 0.002 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 14 . 1 2 15 15 ALA N N 15 0.967 0.005 1.00E-09 2.10E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 15 . 1 2 16 16 PHE N N 15 0.972 0.014 1.00E-09 5.18E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 16 . 1 2 17 17 SER N N 15 0.957 0.001 1.00E-09 7.61E-11 . . . . . . . . . . . . . . . . . . . . . 15183 1 17 . 1 2 18 18 LEU N N 15 0.924 0.02 2.35E-11 4.66E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 18 . 1 2 19 19 PHE N N 15 0.891 0.011 1.96E-11 3.13E-12 . . . . . . . . . . . . . . . . . . . . . 15183 1 19 . 1 2 20 20 ASP N N 15 0.877 0.011 2.35E-11 3.05E-12 . . . . . . . . . . . . . . . . . . . . . 15183 1 20 . 1 2 21 21 LYS N N 15 0.976 0.012 5.00E-14 6.71E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 21 . 1 2 22 22 ASP N N 15 0.962 0 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 22 . 1 2 23 23 GLY N N 15 0.976 0.001 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 23 . 1 2 24 24 ASP N N 15 0.962 0.021 5.00E-14 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 24 . 1 2 25 25 GLY N N 15 0.986 0.008 1.00E-09 2.70E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 25 . 1 2 26 26 THR N N 15 0.901 0.028 1.77E-11 4.10E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 26 . 1 2 27 27 ILE N N 15 0.948 0.006 1.00E-09 8.05E-11 . . . . . . . . . . . . . . . . . . . . . 15183 1 27 . 1 2 28 28 THR N N 15 0.981 0.028 1.00E-09 6.32E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 28 . 1 2 29 29 THR N N 15 0.976 0.008 3.25E-10 1.27E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 29 . 1 2 31 31 GLU N N 15 0.967 0.01 2.55E-11 2.45E-11 . . . . . . . . . . . . . . . . . . . . . 15183 1 30 . 1 2 32 32 LEU N N 15 0.976 0.006 1.00E-09 1.64E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 31 . 1 2 33 33 GLY N N 15 0.957 0.017 7.88E-12 6.65E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 32 . 1 2 35 35 VAL N N 15 0.976 0.009 1.00E-09 3.33E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 33 . 1 2 36 36 MET N N 15 0.967 0.012 5.29E-11 5.07E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 34 . 1 2 37 37 ARG N N 15 0.953 0.001 1.00E-09 1.52E-12 . . . . . . . . . . . . . . . . . . . . . 15183 1 35 . 1 2 38 38 SER N N 15 0.967 0.027 6.81E-10 4.51E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 36 . 1 2 39 39 LEU N N 15 0.934 0.017 1.00E-09 4.32E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 37 . 1 2 40 40 GLY N N 15 0.929 0.009 1.00E-09 2.73E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 38 . 1 2 41 41 GLN N N 15 0.891 0.057 7.47E-10 4.91E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 39 . 1 2 43 43 PRO N N 15 0.91 0.034 1.00E-09 5.38E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 40 . 1 2 44 44 THR N N 15 0.957 0.005 1.00E-09 2.80E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 41 . 1 2 45 45 GLU N N 15 0.948 0.002 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 42 . 1 2 46 46 ALA N N 15 0.962 0.013 1.00E-09 3.32E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 43 . 1 2 47 47 GLU N N 15 0.953 0.003 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 44 . 1 2 49 49 GLN N N 15 0.948 0.003 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 45 . 1 2 50 50 ASP N N 15 0.972 0.007 2.35E-11 2.99E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 46 . 1 2 51 51 MET N N 15 0.943 0.003 1.00E-09 5.37E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 47 . 1 2 52 52 ILE N N 15 0.957 0.002 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 48 . 1 2 54 54 GLU N N 15 0.91 0.003 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 49 . 1 2 55 55 VAL N N 15 0.924 0.011 2.94E-11 1.95E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 50 . 1 2 56 56 ASP N N 15 0.698 0.009 2.55E-11 1.23E-12 . . . . . . . . . . . . . . . . . . . . . 15183 1 51 . 1 2 57 57 ALA N N 15 0.901 0.01 1.96E-11 3.13E-12 . . . . . . . . . . . . . . . . . . . . . 15183 1 52 . 1 2 58 58 ASP N N 15 0.901 0.01 1.18E-11 2.05E-12 . . . . . . . . . . . . . . . . . . . . . 15183 1 53 . 1 2 59 59 GLY N N 15 0.976 0.004 1.00E-09 8.13E-11 . . . . . . . . . . . . . . . . . . . . . 15183 1 54 . 1 2 60 60 ASN N N 15 0.943 0.002 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 55 . 1 2 61 61 GLY N N 15 0.981 0.001 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 56 . 1 2 62 62 THR N N 15 0.976 0.029 1.00E-09 7.01E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 57 . 1 2 63 63 ILE N N 15 0.962 0.006 1.00E-09 1.79E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 58 . 1 2 64 64 ASP N N 15 0.976 0.009 1.00E-09 2.71E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 59 . 1 2 66 66 PRO N N 15 0.962 0.002 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 60 . 1 2 67 67 GLU N N 15 0.967 0.01 3.53E-11 4.33E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 61 . 1 2 68 68 PHE N N 15 0.991 0.008 7.88E-12 4.74E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 62 . 1 2 69 69 LEU N N 15 0.943 0.019 1.57E-11 5.47E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 63 . 1 2 70 70 THR N N 15 0.967 0.003 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 64 . 1 2 71 71 MET N N 15 0.962 0.003 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 65 . 1 2 72 72 MET N N 15 0.962 0.003 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 66 . 1 2 73 73 ALA N N 15 0.92 0.003 9.33E-10 1.90E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 67 . 1 2 74 74 ARG N N 15 0.915 0.003 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 68 . 1 2 75 75 LYS N N 15 0.905 0.002 9.84E-10 8.32E-12 . . . . . . . . . . . . . . . . . . . . . 15183 1 69 . 1 2 76 76 MET N N 15 0.83 0.001 9.88E-10 5.96E-12 . . . . . . . . . . . . . . . . . . . . . 15183 1 70 . 1 2 77 77 LYS N N 15 0.811 0.001 9.39E-10 5.00E-12 . . . . . . . . . . . . . . . . . . . . . 15183 1 71 . 1 2 78 78 ASP N N 15 0.759 0.001 8.26E-10 3.19E-12 . . . . . . . . . . . . . . . . . . . . . 15183 1 72 . 1 2 79 79 THR N N 15 0.957 0.002 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 73 . 1 2 80 80 ASP N N 15 0.792 0.001 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 74 . 1 2 81 81 SER N N 15 0.915 0.002 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 75 . 1 2 82 82 GLU N N 15 0.905 0.003 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 76 . 1 2 83 83 GLU N N 15 0.948 0.002 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 77 . 1 2 84 84 GLU N N 15 0.957 0.003 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 78 . 1 2 85 85 ILE N N 15 0.92 0.002 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 79 . 1 2 86 86 ARG N N 15 0.934 0.002 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 80 . 1 2 87 87 GLU N N 15 0.882 0.004 5.24E-10 2.81E-11 . . . . . . . . . . . . . . . . . . . . . 15183 1 81 . 1 2 88 88 ALA N N 15 0.972 0.001 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 82 . 1 2 89 89 PHE N N 15 0.976 0.003 1.00E-09 8.13E-11 . . . . . . . . . . . . . . . . . . . . . 15183 1 83 . 1 2 90 90 ARG N N 15 0.953 0.001 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 84 . 1 2 91 91 VAL N N 15 0.939 0.023 3.96E-12 6.68E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 85 . 1 2 92 92 PHE N N 15 0.929 0.017 2.16E-11 3.49E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 86 . 1 2 93 93 ASP N N 15 0.905 0.025 3.14E-11 6.25E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 87 . 1 2 94 94 LYS N N 15 0.948 0.019 1.77E-11 6.34E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 88 . 1 2 95 95 ASP N N 15 0.976 0.005 1.00E-09 1.15E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 89 . 1 2 97 97 ASN N N 15 0.986 0.011 5.00E-14 5.73E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 90 . 1 2 98 98 GLY N N 15 0.967 0.012 1.77E-11 2.90E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 91 . 1 2 99 99 TYR N N 15 0.901 0.018 9.83E-12 8.12E-11 . . . . . . . . . . . . . . . . . . . . . 15183 1 92 . 1 2 100 100 ILE N N 15 0.976 0.018 1.57E-11 5.03E-11 . . . . . . . . . . . . . . . . . . . . . 15183 1 93 . 1 2 101 101 SER N N 15 0.972 0.017 7.79E-10 4.31E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 94 . 1 2 102 102 ALA N N 15 0.972 0.009 9.77E-10 3.94E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 95 . 1 2 103 103 ALA N N 15 0.934 0.012 7.88E-12 3.44E-12 . . . . . . . . . . . . . . . . . . . . . 15183 1 96 . 1 2 104 104 GLU N N 15 0.953 0.01 2.35E-11 1.85E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 97 . 1 2 105 105 LEU N N 15 0.948 0.01 5.09E-11 1.77E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 98 . 1 2 106 106 ARG N N 15 0.972 0.011 3.92E-11 3.34E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 99 . 1 2 108 108 VAL N N 15 0.939 0.003 9.55E-10 2.78E-11 . . . . . . . . . . . . . . . . . . . . . 15183 1 100 . 1 2 109 109 MET N N 15 0.939 0.01 6.85E-11 2.17E-11 . . . . . . . . . . . . . . . . . . . . . 15183 1 101 . 1 2 110 110 THR N N 15 0.957 0.011 4.31E-11 2.25E-11 . . . . . . . . . . . . . . . . . . . . . 15183 1 102 . 1 2 111 111 ASN N N 15 0.962 0.005 1.00E-09 7.97E-11 . . . . . . . . . . . . . . . . . . . . . 15183 1 103 . 1 2 113 113 GLY N N 15 0.948 0.002 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 104 . 1 2 114 114 GLU N N 15 0.768 0.009 4.51E-11 2.55E-12 . . . . . . . . . . . . . . . . . . . . . 15183 1 105 . 1 2 115 115 LYS N N 15 0.844 0.009 3.53E-11 3.11E-12 . . . . . . . . . . . . . . . . . . . . . 15183 1 106 . 1 2 116 116 LEU N N 15 0.943 0.014 1.00E-09 1.80E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 107 . 1 2 117 117 THR N N 15 0.981 0.01 1.00E-09 2.90E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 108 . 1 2 118 118 ASP N N 15 0.957 0.001 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 109 . 1 2 119 119 GLU N N 15 0.91 0.001 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 110 . 1 2 120 120 GLU N N 15 0.967 0.001 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 111 . 1 2 121 121 VAL N N 15 0.972 0.003 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 112 . 1 2 122 122 ASP N N 15 0.962 0 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 113 . 1 2 123 123 GLU N N 15 0.953 0 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 114 . 1 2 125 125 ILE N N 15 0.972 0.002 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 115 . 1 2 126 126 ARG N N 15 0.957 0.002 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 116 . 1 2 127 127 GLU N N 15 0.981 0.009 1.00E-09 5.20E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 117 . 1 2 128 128 ALA N N 15 0.953 0.009 1.00E-09 1.80E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 118 . 1 2 129 129 ASP N N 15 0.707 0.008 1.57E-11 1.00E-12 . . . . . . . . . . . . . . . . . . . . . 15183 1 119 . 1 2 130 130 ILE N N 15 0.962 0.009 2.16E-11 1.06E-11 . . . . . . . . . . . . . . . . . . . . . 15183 1 120 . 1 2 131 131 ASP N N 15 0.91 0.01 5.00E-14 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 121 . 1 2 132 132 GLY N N 15 0.972 0.015 2.01E-12 6.99E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 122 . 1 2 133 133 ASP N N 15 0.976 0.003 1.00E-09 8.11E-11 . . . . . . . . . . . . . . . . . . . . . 15183 1 123 . 1 2 134 134 GLY N N 15 0.967 0.005 1.00E-09 1.77E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 124 . 1 2 135 135 GLN N N 15 0.91 0.026 3.14E-11 6.35E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 125 . 1 2 136 136 VAL N N 15 0.976 0.013 1.00E-09 3.42E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 126 . 1 2 139 139 GLU N N 15 0.972 0.007 1.00E-09 3.27E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 127 . 1 2 140 140 GLU N N 15 0.976 0.004 1.00E-09 1.39E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 128 . 1 2 141 141 PHE N N 15 0.981 0.004 1.00E-09 1.40E-10 . . . . . . . . . . . . . . . . . . . . . 15183 1 129 . 1 2 142 142 VAL N N 15 1 0 5.00E-14 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 130 . 1 2 143 143 GLN N N 15 0.957 0.001 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 131 . 1 2 144 144 MET N N 15 0.929 0.002 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 132 . 1 2 145 145 MET N N 15 0.896 0.003 1.00E-09 9.48E-13 . . . . . . . . . . . . . . . . . . . . . 15183 1 133 . 1 2 146 146 THR N N 15 0.787 0.002 1.00E-09 0.00E+00 . . . . . . . . . . . . . . . . . . . . . 15183 1 134 . 1 2 147 147 ALA N N 15 0.641 0.001 5.52E-10 2.60E-12 . . . . . . . . . . . . . . . . . . . . . 15183 1 stop_ save_ save_Side-chain_methyl_order_parameters _Order_parameter_list.Sf_category order_parameters _Order_parameter_list.Sf_framecode Side-chain_methyl_order_parameters _Order_parameter_list.Entry_ID 15183 _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 CaMKK p determined with relaxation data obtained at 500 and 750 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' . . . 15183 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 2 4 4 LEU CD1 C 13 0.341 0.01 4.65E-11 2.08E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 2 . 1 2 4 4 LEU CD2 C 13 0.348 0.007 3.21E-11 9.68E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 3 . 1 2 9 9 ILE CD1 C 13 0.405 0.006 2.02E-11 6.52E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 4 . 1 2 9 9 ILE CG2 C 13 0.708 0.011 2.71E-11 9.01E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 5 . 1 2 10 10 ALA CB C 13 0.871 0.016 3.27E-11 9.90E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 6 . 1 2 15 15 ALA CB C 13 0.899 0.044 7.73E-11 5.13E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 7 . 1 2 18 18 LEU CD1 C 13 0.313 0.006 3.84E-11 1.32E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 8 . 1 2 18 18 LEU CD2 C 13 0.299 0.022 5.91E-11 5.10E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 9 . 1 2 27 27 ILE CD1 C 13 0.751 0.048 2.58E-11 3.44E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 10 . 1 2 27 27 ILE CG2 C 13 0.843 0.034 3.40E-11 2.40E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 11 . 1 2 28 28 THR CG2 C 13 0.829 0.027 1.09E-10 5.52E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 12 . 1 2 29 29 THR CG2 C 13 0.306 0.005 7.54E-11 1.43E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 13 . 1 2 32 32 LEU CD1 C 13 0.666 0.039 4.21E-11 3.86E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 14 . 1 2 32 32 LEU CD2 C 13 0.659 0.051 4.90E-11 5.76E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 15 . 1 2 34 34 THR CG2 C 13 0.595 0.013 5.66E-11 1.64E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 16 . 1 2 35 35 VAL CG1 C 13 0.793 0.028 5.72E-11 2.67E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 17 . 1 2 35 35 VAL CG2 C 13 0.744 0.024 2.52E-11 1.67E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 18 . 1 2 36 36 MET CE C 13 0.39 0.004 1.01E-11 3.85E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 19 . 1 2 39 39 LEU CD1 C 13 0.553 0.027 5.53E-11 4.25E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 20 . 1 2 39 39 LEU CD2 C 13 0.595 0.024 2.83E-11 2.06E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 21 . 1 2 44 44 THR CG2 C 13 0.369 0.006 5.85E-11 1.27E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 22 . 1 2 46 46 ALA CB C 13 0.786 0.011 4.40E-11 1.03E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 23 . 1 2 48 48 LEU CD1 C 13 0.68 0.047 5.91E-11 6.06E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 24 . 1 2 51 51 MET CE C 13 0.652 0.009 1.14E-11 6.52E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 25 . 1 2 52 52 ILE CD1 C 13 0.263 0.006 2.33E-11 1.05E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 26 . 1 2 52 52 ILE CG2 C 13 0.786 0.018 4.03E-11 1.46E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 27 . 1 2 55 55 VAL CG1 C 13 0.602 0.026 3.77E-11 2.10E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 28 . 1 2 55 55 VAL CG2 C 13 0.779 0.03 5.78E-11 3.24E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 29 . 1 2 57 57 ALA CB C 13 0.864 0.016 4.28E-11 1.15E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 30 . 1 2 63 63 ILE CD1 C 13 0.602 0.029 4.28E-11 3.26E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 31 . 1 2 63 63 ILE CG2 C 13 0.786 0.036 2.77E-11 2.40E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 32 . 1 2 69 69 LEU CD1 C 13 0.228 0.012 3.33E-11 2.61E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 33 . 1 2 69 69 LEU CD2 C 13 0.171 0.009 4.47E-11 2.88E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 34 . 1 2 70 70 THR CG2 C 13 0.553 0.008 4.97E-11 1.01E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 35 . 1 2 71 71 MET CE C 13 0.39 0.005 2.14E-11 5.86E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 36 . 1 2 72 72 MET CE C 13 0.383 0.004 1.33E-11 4.93E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 37 . 1 2 73 73 ALA CB C 13 0.864 0.018 3.77E-11 1.30E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 38 . 1 2 76 76 MET CE C 13 0.285 0.004 1.33E-11 3.13E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 39 . 1 2 85 85 ILE CD1 C 13 0.617 0.014 1.64E-11 1.14E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 40 . 1 2 85 85 ILE CG2 C 13 0.8 0.022 2.08E-11 1.34E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 41 . 1 2 91 91 VAL CG2 C 13 0.814 0.022 3.15E-11 1.61E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 42 . 1 2 100 100 ILE CD1 C 13 0.829 0.048 2.14E-11 2.92E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 43 . 1 2 100 100 ILE CG2 C 13 0.836 0.031 3.09E-11 2.06E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 44 . 1 2 102 102 ALA CB C 13 0.885 0.022 4.59E-11 1.57E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 45 . 1 2 103 103 ALA CB C 13 0.885 0.019 4.34E-11 1.36E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 46 . 1 2 105 105 LEU CD1 C 13 0.108 0.004 2.77E-11 6.08E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 47 . 1 2 105 105 LEU CD2 C 13 0.186 0.004 3.71E-11 8.78E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 48 . 1 2 108 108 VAL CG1 C 13 0.313 0.006 5.28E-11 1.26E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 49 . 1 2 108 108 VAL CG2 C 13 0.292 0.004 3.96E-11 8.37E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 50 . 1 2 109 109 MET CE C 13 0.595 0.005 1.52E-11 4.21E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 51 . 1 2 110 110 THR CG2 C 13 0.433 0.004 5.41E-11 7.01E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 52 . 1 2 112 112 LEU CD1 C 13 0.426 0.018 6.53E-11 4.46E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 53 . 1 2 112 112 LEU CD2 C 13 0.398 0.012 4.21E-11 2.36E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 54 . 1 2 116 116 LEU CD1 C 13 0.518 0.013 9.30E-11 3.29E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 55 . 1 2 116 116 LEU CD2 C 13 0.574 0.016 7.73E-11 3.03E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 56 . 1 2 121 121 VAL CG1 C 13 0.758 0.016 2.71E-11 1.18E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 57 . 1 2 121 121 VAL CG2 C 13 0.779 0.023 2.90E-11 1.51E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 58 . 1 2 124 124 MET CE C 13 0.878 0.023 5.12E-12 1.01E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 59 . 1 2 125 125 ILE CD1 C 13 0.277 0.005 2.33E-11 8.00E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 60 . 1 2 125 125 ILE CG2 C 13 0.843 0.018 2.21E-11 1.02E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 61 . 1 2 128 128 ALA CB C 13 0.963 0.045 8.92E-11 5.56E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 62 . 1 2 130 130 ILE CD1 C 13 0.32 0.005 2.58E-11 5.77E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 63 . 1 2 130 130 ILE CG2 C 13 0.525 0.005 3.71E-11 6.17E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 64 . 1 2 136 136 VAL CG1 C 13 0.504 0.013 5.22E-11 2.12E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 65 . 1 2 136 136 VAL CG2 C 13 0.546 0.011 5.59E-11 1.96E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 66 . 1 2 142 142 VAL CG1 C 13 0.532 0.008 6.22E-11 1.16E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 67 . 1 2 142 142 VAL CG2 C 13 0.546 0.009 2.39E-11 8.92E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 68 . 1 2 144 144 MET CE C 13 0.504 0.005 1.20E-11 5.46E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 69 . 1 2 145 145 MET CE C 13 0.348 0.005 2.02E-11 3.37E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 70 . 1 2 146 146 THR CG2 C 13 0.511 0.008 4.97E-11 1.12E-12 . . . . . . . . . . . . . . . . . . . . . 15183 2 71 . 1 2 147 147 ALA CB C 13 0.412 0.005 4.15E-11 4.30E-13 . . . . . . . . . . . . . . . . . . . . . 15183 2 stop_ save_