data_18556 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18556 _Entry.Title ; The complex between Ca-Calmodulin and skeletal muscle myosin light chain kinase from combination of NMR and aqueous and contrast-matched SAXS data ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2012-06-29 _Entry.Accession_date 2012-06-29 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype SOLUTION _Entry.Details ; This entry contains the coordinates of the complex between Ca-bound human calmodulin and skeletal muscle myosin light chain kinase determined by refinement against backbone HN-N residual dipolar couplings from solution NMR and solution X-ray scattering intensity data. The latter include both SAXS data in H2O recorded on a Ca-CAM/MLCK sample and data in 65% aqueous sucrose buffer recorded on the Pb-CaM/MLCK sample in which Ca ions in calmodulin were replaced by Pb ions. The position of the C-terminal relative to the N-terminal domain of calmodulin was optimized via an exhaustive rigid-body translational/orientational grid search with a step size of 1A/2deg while fitting RDCs and the two types of SAXS data. Subsequently, the coordinates of the linker connecting the two domain of calmodulin (residues 76-81) and the interfacial side chains were optimized via molecular dynamics/simulated annealing refinement while keeping the coordinates of the backbone atoms fixed. ; _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 Alexander Grishaev . V. . 18556 2 Nicholas Anthis . J. . 18556 3 'G. Marius' Clore . . . 18556 stop_ loop_ _SG_project.SG_project_ID _SG_project.Project_name _SG_project.Full_name_of_center _SG_project.Initial_of_center _SG_project.Entry_ID 1 'not applicable' 'not applicable' . 18556 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'Ca-Calmodulin, CaM' . 18556 'contrast-matched SAXS' . 18556 NMR . 18556 Pb-substituted . 18556 'protein complex' . 18556 skMLCK . 18556 'X-ray solution scattering' . 18556 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18556 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 144 18556 '1H chemical shifts' 144 18556 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 2 . . 2013-02-20 2012-06-29 update BMRB 'update entry citation' 18556 1 . . 2013-02-01 2012-06-29 original author 'original release' 18556 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 1BBM ; skMLCK peptide coordinates and distance restraints from this entry were used during rigid-body optimization of the geometry of the CaM/MLCK complex. ; 18556 PDB 1MXE ; Backbone coordinates of the N- and C-terminal domains from this entry (residues 5-75 and 82-146, respectively) were used during rigid-body optimization of the geometry of the CaM/MLCK complex. ; 18556 PDB 2LV6 'BMRB Entry Tracking System' 18556 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 18556 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 22908850 _Citation.Full_citation . _Citation.Title 'Contrast-matched small-angle X-ray scattering from a heavy-atom-labeled protein in structure determination: application to a lead-substituted calmodulin-peptide complex.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Am. Chem. Soc.' _Citation.Journal_name_full 'Journal of the American Chemical Society' _Citation.Journal_volume 134 _Citation.Journal_issue 36 _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 14686 _Citation.Page_last 14689 _Citation.Year 2012 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Alexander Grishaev . . . 18556 1 2 Nicholas Anthis . J. . 18556 1 3 'G. Marius' Clore . . . 18556 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18556 _Assembly.ID 1 _Assembly.Name 'complex between Ca-Calmodulin and skeletal muscle myosin light chain kinase' _Assembly.BMRB_code . _Assembly.Number_of_components 6 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 Calmodulin 1 $Calmodulin A . yes native no no . . . 18556 1 2 ssMLCK 2 $ssMLCK B . yes native no no . . . 18556 1 3 'CALCIUM ION_1' 3 $entity_CA C . yes native no no . . . 18556 1 4 'CALCIUM ION_2' 3 $entity_CA D . yes native no no . . . 18556 1 5 'CALCIUM ION_3' 3 $entity_CA E . yes native no no . . . 18556 1 6 'CALCIUM ION_4' 3 $entity_CA F . yes native no no . . . 18556 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Calmodulin _Entity.Sf_category entity _Entity.Sf_framecode Calmodulin _Entity.Entry_ID 18556 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Calmodulin _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGFI SAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEE FVTMMTAK ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 148 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment 'human calmodulin' _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 16678.439 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 15184 . calmodulin . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 2 no BMRB 15185 . calmodulin . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 3 no BMRB 15186 . calmodulin . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 4 no BMRB 15187 . calmodulin . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 5 no BMRB 15188 . calmodulin . . . . . 100.00 148 97.97 99.32 5.38e-98 . . . . 18556 1 6 no BMRB 15191 . Calmodulin . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 7 no BMRB 15470 . calmodulin . . . . . 100.00 148 97.97 99.32 9.29e-98 . . . . 18556 1 8 no BMRB 15624 . Calmodulin . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 9 no BMRB 15650 . calmodulin . . . . . 100.00 148 97.97 99.32 1.73e-97 . . . . 18556 1 10 no BMRB 15852 . calmodulin . . . . . 100.00 148 97.97 99.32 1.73e-97 . . . . 18556 1 11 no BMRB 1634 . calmodulin . . . . . 100.00 148 98.65 100.00 1.65e-98 . . . . 18556 1 12 no BMRB 16418 . apoCaM . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 13 no BMRB 16465 . entity_1 . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 14 no BMRB 1648 . calmodulin . . . . . 100.00 148 98.65 100.00 1.65e-98 . . . . 18556 1 15 no BMRB 16764 . CALMODULIN . . . . . 100.00 150 98.65 99.32 2.83e-98 . . . . 18556 1 16 no BMRB 17264 . calmodulin . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 17 no BMRB 17360 . entity_1 . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 18 no BMRB 17771 . Calmodulin . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 19 no BMRB 17807 . Calmodulin . . . . . 99.32 147 98.64 99.32 1.52e-97 . . . . 18556 1 20 no BMRB 18027 . CaM . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 21 no BMRB 18028 . CaM . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 22 no BMRB 19036 . calmodulin . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 23 no BMRB 19238 . Calmodulin_prototypical_calcium_sensor . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 24 no BMRB 19586 . entity_1 . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 25 no BMRB 19604 . calmodulin . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 26 no BMRB 25253 . CaM . . . . . 100.00 148 97.97 98.65 2.90e-96 . . . . 18556 1 27 no BMRB 25257 . CaM . . . . . 100.00 148 97.97 98.65 2.90e-96 . . . . 18556 1 28 no BMRB 26503 . Calmodulin . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 29 no BMRB 26626 . CaM . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 30 no BMRB 26627 . CaM . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 31 no BMRB 4056 . calmodulin . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 32 no BMRB 4270 . calmodulin . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 33 no BMRB 4284 . Calmodulin . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 34 no BMRB 4310 . calmodulin . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 35 no PDB 1A29 . "Calmodulin Complexed With Trifluoperazine (1:2 Complex)" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 36 no PDB 1AHR . "Calmodulin Mutant With A Two Residue Deletion In The Central Helix" . . . . . 100.00 146 97.97 98.65 1.54e-95 . . . . 18556 1 37 no PDB 1CFC . "Calcium-Free Calmodulin" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 38 no PDB 1CFD . "Calcium-Free Calmodulin" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 39 no PDB 1CFF . "Nmr Solution Structure Of A Complex Of Calmodulin With A Binding Peptide Of The Ca2+-Pump" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 40 no PDB 1CKK . "CalmodulinRAT CA2+CALMODULIN DEPENDENT PROTEIN KINASE Fragment" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 41 no PDB 1CLL . "Calmodulin Structure Refined At 1.7 Angstroms Resolution" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 42 no PDB 1CM1 . "Motions Of Calmodulin-Single-Conformer Refinement" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 43 no PDB 1CM4 . "Motions Of Calmodulin-four-conformer Refinement" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 44 no PDB 1CTR . "Drug Binding By Calmodulin: Crystal Structure Of A Calmodulin-Trifluoperazine Complex" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 45 no PDB 1DMO . "Calmodulin, Nmr, 30 Structures" . . . . . 100.00 148 97.97 99.32 9.29e-98 . . . . 18556 1 46 no PDB 1G4Y . "1.60 A Crystal Structure Of The Gating Domain From Small Conductance Potassium Channel Complexed With Calcium-Calmodulin" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 47 no PDB 1IQ5 . "CalmodulinNEMATODE CA2+CALMODULIN DEPENDENT KINASE KINASE Fragment" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 48 no PDB 1IWQ . "Crystal Structure Of Marcks Calmodulin Binding Domain Peptide Complexed With Ca2+CALMODULIN" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 49 no PDB 1K90 . "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3' Deoxy-Atp" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 50 no PDB 1K93 . "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin" . . . . . 97.30 144 98.61 99.31 2.87e-95 . . . . 18556 1 51 no PDB 1L7Z . "Crystal Structure Of Ca2+/calmodulin Complexed With Myristoylated Cap-23/nap-22 Peptide" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 52 no PDB 1LIN . "Calmodulin Complexed With Trifluoperazine (1:4 Complex)" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 53 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 98.65 99.32 2.20e-98 . . . . 18556 1 54 no PDB 1MUX . "Solution Nmr Structure Of CalmodulinW-7 Complex: The Basis Of Diversity In Molecular Recognition, 30 Structures" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 55 no PDB 1MXE . "Structure Of The Complex Of Calmodulin With The Target Sequence Of Camki" . . . . . 100.00 148 99.32 100.00 5.99e-99 . . . . 18556 1 56 no PDB 1NWD . "Solution Structure Of Ca2+CALMODULIN BOUND TO THE C- Terminal Domain Of Petunia Glutamate Decarboxylase" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 57 no PDB 1OOJ . "Structural Genomics Of Caenorhabditis Elegans : Calmodulin" . . . . . 100.00 149 99.32 99.32 1.22e-98 . . . . 18556 1 58 no PDB 1PRW . "Crystal Structure Of Bovine Brain Ca++ Calmodulin In A Compact Form" . . . . . 100.00 149 97.97 98.65 2.74e-97 . . . . 18556 1 59 no PDB 1QIV . "Calmodulin Complexed With N-(3,3,-Diphenylpropyl)-N'-[1-R-( 3,4-Bis-Butoxyphenyl)-Ethyl]-Propylenediamine (Dpd), 1:2 Complex" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 60 no PDB 1QIW . "Calmodulin Complexed With N-(3,3,-Diphenylpropyl)-N'-[1-R-( 3,4-Bis-Butoxyphenyl)-Ethyl]-Propylenediamine (Dpd)" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 61 no PDB 1QX5 . "Crystal Structure Of Apocalmodulin" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 62 no PDB 1S26 . "Structure Of Anthrax Edema Factor-calmodulin-alpha,beta- Methyleneadenosine 5'-triphosphate Complex Reveals An Alternative Mode" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 63 no PDB 1SK6 . "Crystal Structure Of The Adenylyl Cyclase Domain Of Anthrax Edema Factor (Ef) In Complex With Calmodulin, 3',5' Cyclic Amp (Cam" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 64 no PDB 1SY9 . "Structure Of Calmodulin Complexed With A Fragment Of The Olfactory Cng Channel" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 65 no PDB 1UP5 . "Chicken Calmodulin" . . . . . 100.00 148 97.97 98.65 2.65e-97 . . . . 18556 1 66 no PDB 1WRZ . "Calmodulin Complexed With A Peptide From A Human Death-Associated Protein Kinase" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 67 no PDB 1X02 . "Solution Structure Of Stereo Array Isotope Labeled (Sail) Calmodulin" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 68 no PDB 1XA5 . "Structure Of Calmodulin In Complex With Kar-2, A Bis-Indol Alkaloid" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 69 no PDB 1XFU . "Crystal Structure Of Anthrax Edema Factor (ef) Truncation Mutant, Ef-delta 64 In Complex With Calmodulin" . . . . . 100.00 149 97.97 99.32 7.39e-98 . . . . 18556 1 70 no PDB 1XFV . "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3' Deoxy-Atp" . . . . . 100.00 149 97.97 99.32 7.39e-98 . . . . 18556 1 71 no PDB 1XFW . "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And 3'5' Cyclic Amp (Camp)" . . . . . 100.00 149 97.97 99.32 7.39e-98 . . . . 18556 1 72 no PDB 1XFY . "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin" . . . . . 100.00 149 97.97 99.32 7.39e-98 . . . . 18556 1 73 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 97.97 99.32 7.39e-98 . . . . 18556 1 74 no PDB 1Y0V . "Crystal Structure Of Anthrax Edema Factor (Ef) In Complex With Calmodulin And Pyrophosphate" . . . . . 97.30 146 98.61 99.31 2.31e-95 . . . . 18556 1 75 no PDB 1YR5 . "1.7-A Structure Of Calmodulin Bound To A Peptide From Dap Kinase" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 76 no PDB 2BBM . "Solution Structure Of A Calmodulin-Target Peptide Complex By Multidimensional Nmr" . . . . . 100.00 148 99.32 100.00 5.99e-99 . . . . 18556 1 77 no PDB 2BBN . "Solution Structure Of A Calmodulin-Target Peptide Complex By Multidimensional Nmr" . . . . . 100.00 148 99.32 100.00 5.99e-99 . . . . 18556 1 78 no PDB 2BCX . "Crystal Structure Of Calmodulin In Complex With A Ryanodine Receptor Peptide" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 79 no PDB 2BKH . "Myosin Vi Nucleotide-Free (Mdinsert2) Crystal Structure" . . . . . 100.00 149 99.32 100.00 5.49e-99 . . . . 18556 1 80 no PDB 2BKI . "Myosin Vi Nucleotide-free (mdinsert2-iq) Crystal Structure" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 81 no PDB 2DFS . "3-D Structure Of Myosin-V Inhibited State" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 82 no PDB 2F2O . "Structure Of Calmodulin Bound To A Calcineurin Peptide: A New Way Of Making An Old Binding Mode" . . . . . 100.00 179 98.65 99.32 5.23e-98 . . . . 18556 1 83 no PDB 2F2P . "Structure Of Calmodulin Bound To A Calcineurin Peptide: A New Way Of Making An Old Binding Mode" . . . . . 100.00 179 98.65 99.32 5.23e-98 . . . . 18556 1 84 no PDB 2F3Y . "CalmodulinIQ DOMAIN COMPLEX" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 85 no PDB 2F3Z . "CalmodulinIQ-Aa Domain Complex" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 86 no PDB 2FOT . "Crystal Structure Of The Complex Between Calmodulin And Alphaii-Spectrin" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 87 no PDB 2HQW . "Crystal Structure Of Ca2+CALMODULIN BOUND TO NMDA RECEPTOR NR1C1 Peptide" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 88 no PDB 2JZI . "Structure Of Calmodulin Complexed With The Calmodulin Binding Domain Of Calcineurin" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 89 no PDB 2K0E . "A Coupled Equilibrium Shift Mechanism In Calmodulin- Mediated Signal Transduction" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 90 no PDB 2K0F . "Calmodulin Complexed With Calmodulin-Binding Peptide From Smooth Muscle Myosin Light Chain Kinase" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 91 no PDB 2K0J . "Solution Structure Of Cam Complexed To Drp1p" . . . . . 100.00 148 97.97 99.32 1.73e-97 . . . . 18556 1 92 no PDB 2K61 . "Solution Structure Of Cam Complexed To Dapk Peptide" . . . . . 100.00 148 97.97 99.32 1.73e-97 . . . . 18556 1 93 no PDB 2KDU . "Structural Basis Of The Munc13-1CA2+-Calmodulin Interaction: A Novel 1-26 Calmodulin Binding Motif With A Bipartite Binding Mod" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 94 no PDB 2KNE . "Calmodulin Wraps Around Its Binding Domain In The Plasma Membrane Ca2+ Pump Anchored By A Novel 18-1 Motif" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 95 no PDB 2L53 . "Solution Nmr Structure Of Apo-Calmodulin In Complex With The Iq Motif Of Human Cardiac Sodium Channel Nav1.5" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 96 no PDB 2L7L . "Solution Structure Of Ca2+CALMODULIN COMPLEXED WITH A PEPTIDE Representing The Calmodulin-Binding Domain Of Calmodulin Kinase I" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 97 no PDB 2LGF . "Solution Structure Of Ca2+CALMODULIN COMPLEXED WITH A PEPTIDE Representing The Calmodulin-Binding Domain Of L-Selectin" . . . . . 98.65 146 98.63 99.32 7.08e-97 . . . . 18556 1 98 no PDB 2LL6 . "Solution Nmr Structure Of Cam Bound To Inos Cam Binding Domain Peptide" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 99 no PDB 2LL7 . "Solution Nmr Structure Of Cam Bound To The Enos Cam Binding Domain Peptide" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 100 no PDB 2LV6 . "The Complex Between Ca-calmodulin And Skeletal Muscle Myosin Light Chain Kinase From Combination Of Nmr And Aqueous And Contras" . . . . . 100.00 148 100.00 100.00 2.47e-99 . . . . 18556 1 101 no PDB 2M0J . "3d Structure Of Calmodulin And Calmodulin Binding Domain Of Olfactory Cyclic Nucleotide-gated Ion Channel Complex" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 102 no PDB 2M0K . "3d Structure Of Calmodulin And Calmodulin Binding Domain Of Rat Olfactory Cyclic Nucleotide-gated Ion Channel" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 103 no PDB 2M55 . "Nmr Structure Of The Complex Of An N-terminally Acetylated Alpha- Synuclein Peptide With Calmodulin" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 104 no PDB 2MG5 . "Solution Structure Of Calmodulin Bound To The Target Peptide Of Endothelial Nitrogen Oxide Synthase Phosphorylated At Thr495" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 105 no PDB 2MGU . "Structure Of The Complex Between Calmodulin And The Binding Domain Of Hiv-1 Matrix Protein" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 106 no PDB 2O5G . "Calmodulin-Smooth Muscle Light Chain Kinase Peptide Complex" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 107 no PDB 2O60 . "Calmodulin Bound To Peptide From Neuronal Nitric Oxide Synthase" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 108 no PDB 2R28 . "The Complex Structure Of Calmodulin Bound To A Calcineurin Peptide" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 109 no PDB 2V01 . "Recombinant Vertebrate Calmodulin Complexed With Pb" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 110 no PDB 2V02 . "Recombinant Vertebrate Calmodulin Complexed With Ba" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 111 no PDB 2VAS . "Myosin Vi (Md-Insert2-Cam, Delta-Insert1) Post-Rigor State" . . . . . 100.00 149 99.32 100.00 5.49e-99 . . . . 18556 1 112 no PDB 2VAY . "Calmodulin Complexed With Cav1.1 Iq Peptide" . . . . . 98.65 146 98.63 99.32 7.08e-97 . . . . 18556 1 113 no PDB 2VB6 . "Myosin Vi (Md-Insert2-Cam, Delta Insert1) Post-Rigor State ( Crystal Form 2)" . . . . . 100.00 149 98.65 100.00 1.09e-98 . . . . 18556 1 114 no PDB 2W73 . "High-Resolution Structure Of The Complex Between Calmodulin And A Peptide From Calcineurin A" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 115 no PDB 2WEL . "Crystal Structure Of Su6656-Bound CalciumCALMODULIN- Dependent Protein Kinase Ii Delta In Complex With Calmodulin" . . . . . 100.00 150 98.65 99.32 2.02e-98 . . . . 18556 1 116 no PDB 2X0G . "X-ray Structure Of A Dap-kinase Calmodulin Complex" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 117 no PDB 2X51 . "M6 Delta Insert1" . . . . . 100.00 149 99.32 100.00 5.49e-99 . . . . 18556 1 118 no PDB 2Y4V . "Crystal Structure Of Human Calmodulin In Complex With A Dap Kinase-1 Mutant (W305y) Peptide" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 119 no PDB 2YGG . "Complex Of Cambr And Cam" . . . . . 100.00 150 98.65 99.32 2.18e-98 . . . . 18556 1 120 no PDB 3BXK . "Crystal Structure Of The PQ-Type Calcium Channel (Cav2.1) Iq Domain And Ca2+calmodulin Complex" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 121 no PDB 3BXL . "Crystal Structure Of The R-Type Calcium Channel (Cav2.3) Iq Domain And Ca2+calmodulin Complex" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 122 no PDB 3BYA . "Structure Of A Calmodulin Complex" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 123 no PDB 3CLN . "Structure Of Calmodulin Refined At 2.2 Angstroms Resolution" . . . . . 100.00 148 97.97 99.32 9.29e-98 . . . . 18556 1 124 no PDB 3DVE . "Crystal Structure Of Ca2+CAM-Cav2.2 Iq Domain Complex" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 125 no PDB 3DVJ . "Crystal Structure Of Ca2+CAM-Cav2.2 Iq Domain (Without Cloning Artifact, Hm To Tv) Complex" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 126 no PDB 3DVK . "Crystal Structure Of Ca2+CAM-Cav2.3 Iq Domain Complex" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 127 no PDB 3DVM . "Crystal Structure Of Ca2+CAM-Cav2.1 Iq Domain Complex" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 128 no PDB 3EK4 . "Calcium-saturated Gcamp2 Monomer" . . . . . 99.32 449 98.64 99.32 3.83e-94 . . . . 18556 1 129 no PDB 3EK7 . "Calcium-Saturated Gcamp2 Dimer" . . . . . 99.32 449 98.64 99.32 3.83e-94 . . . . 18556 1 130 no PDB 3EK8 . "Calcium-Saturated Gcamp2 T116vG87R MUTANT MONOMER" . . . . . 99.32 449 98.64 99.32 3.83e-94 . . . . 18556 1 131 no PDB 3EKH . "Calcium-Saturated Gcamp2 T116vK378W MUTANT MONOMER" . . . . . 99.32 449 97.96 98.64 3.78e-93 . . . . 18556 1 132 no PDB 3EVU . "Crystal Structure Of Calcium Bound Dimeric Gcamp2, (#1)" . . . . . 99.32 449 98.64 99.32 3.83e-94 . . . . 18556 1 133 no PDB 3EVV . "Crystal Structure Of Calcium Bound Dimeric Gcamp2 (#2)" . . . . . 99.32 449 98.64 99.32 3.83e-94 . . . . 18556 1 134 no PDB 3EWT . "Crystal Structure Of Calmodulin Complexed With A Peptide" . . . . . 100.00 154 98.65 99.32 9.32e-99 . . . . 18556 1 135 no PDB 3EWV . "Crystal Structure Of Calmodulin Complexed With A Peptide" . . . . . 100.00 154 98.65 99.32 9.32e-99 . . . . 18556 1 136 no PDB 3G43 . "Crystal Structure Of The Calmodulin-Bound Cav1.2 C-Terminal Regulatory Domain Dimer" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 137 no PDB 3GN4 . "Myosin Lever Arm" . . . . . 100.00 149 99.32 100.00 5.49e-99 . . . . 18556 1 138 no PDB 3GOF . "Calmodulin Bound To Peptide From Macrophage Nitric Oxide Synthase" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 139 no PDB 3HR4 . "Human Inos Reductase And Calmodulin Complex" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 140 no PDB 3IF7 . "Structure Of Calmodulin Complexed With Its First Endogenous Inhibitor, Sphingosylphosphorylcholine" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 141 no PDB 3J41 . "Pseudo-atomic Model Of The Aquaporin-0/calmodulin Complex Derived From Electron Microscopy" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 142 no PDB 3L9I . "Myosin Vi Nucleotide-Free (Mdinsert2) L310g Mutant Crystal Structure" . . . . . 100.00 149 99.32 100.00 5.49e-99 . . . . 18556 1 143 no PDB 3O77 . "The Structure Of Ca2+ Sensor (Case-16)" . . . . . 99.32 415 98.64 99.32 1.97e-94 . . . . 18556 1 144 no PDB 3O78 . "The Structure Of Ca2+ Sensor (Case-12)" . . . . . 99.32 415 98.64 99.32 2.27e-94 . . . . 18556 1 145 no PDB 3OXQ . "Crystal Structure Of Ca2+CAM-Cav1.2 Pre-IqIQ DOMAIN COMPLEX" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 146 no PDB 3SG2 . "Crystal Structure Of Gcamp2-t116v,d381y" . . . . . 99.32 449 97.96 98.64 4.95e-93 . . . . 18556 1 147 no PDB 3SG3 . "Crystal Structure Of Gcamp3-d380y" . . . . . 99.32 449 97.28 98.64 3.17e-92 . . . . 18556 1 148 no PDB 3SG6 . "Crystal Structure Of Dimeric Gcamp2-lia(linker 1)" . . . . . 99.32 450 98.64 99.32 3.94e-94 . . . . 18556 1 149 no PDB 3SG7 . "Crystal Structure Of Gcamp3-kf(linker 1)" . . . . . 99.32 448 97.96 99.32 3.26e-93 . . . . 18556 1 150 no PDB 3SJQ . "Crystal Structure Of A Small Conductance Potassium Channel Splice Variant Complexed With Calcium-Calmodulin" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 151 no PDB 3SUI . "Crystal Structure Of Ca2+-Calmodulin In Complex With A Trpv1 C- Terminal Peptide" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 152 no PDB 3U0K . "Crystal Structure Of The Genetically Encoded Calcium Indicator Rcamp" . . . . . 99.32 440 97.28 98.64 1.02e-92 . . . . 18556 1 153 no PDB 3WFN . "Crystal Structure Of Nav1.6 Iq Motif In Complex With Apo-cam" . . . . . 100.00 182 98.65 99.32 3.32e-98 . . . . 18556 1 154 no PDB 4ANJ . "Myosin Vi (Mdinsert2-Gfp Fusion) Pre-Powerstroke State (Mg.Adp.Alf4)" . . . . . 100.00 149 99.32 100.00 5.49e-99 . . . . 18556 1 155 no PDB 4BW7 . "Calmodulin In Complex With Strontium" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 156 no PDB 4BW8 . "Calmodulin With Small Bend In Central Helix" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 157 no PDB 4BYF . "Crystal Structure Of Human Myosin 1c In Complex With Calmodulin In The Pre-power Stroke State" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 158 no PDB 4CLN . "Structure Of A Recombinant Calmodulin From Drosophila Melanogaster Refined At 2.2-Angstroms Resolution" . . . . . 100.00 148 99.32 100.00 5.99e-99 . . . . 18556 1 159 no PDB 4DBP . "Myosin Vi Nucleotide-free (mdinsert2) D179y Crystal Structure" . . . . . 100.00 149 99.32 100.00 5.49e-99 . . . . 18556 1 160 no PDB 4DBQ . "Myosin Vi D179y (md-insert2-cam, Delta-insert1) Post-rigor State" . . . . . 100.00 149 99.32 100.00 5.49e-99 . . . . 18556 1 161 no PDB 4DCK . "Crystal Structure Of The C-Terminus Of Voltage-Gated Sodium Channel In Complex With Fgf13 And Cam" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 162 no PDB 4DJC . "1.35 A Crystal Structure Of The Nav1.5 Diii-Iv-CaCAM COMPLEX" . . . . . 100.00 152 98.65 99.32 2.41e-98 . . . . 18556 1 163 no PDB 4E50 . "Calmodulin And Ng Peptide Complex" . . . . . 100.00 185 98.65 99.32 1.39e-98 . . . . 18556 1 164 no PDB 4EHQ . "Crystal Structure Of Calmodulin Binding Domain Of Orai1 In Complex With Ca2+CALMODULIN DISPLAYS A UNIQUE BINDING MODE" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 165 no PDB 4G27 . "Calcium-Calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And P" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 166 no PDB 4G28 . "Calcium-Calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And E" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 167 no PDB 4HEX . "A Novel Conformation Of Calmodulin" . . . . . 100.00 156 98.65 99.32 1.14e-98 . . . . 18556 1 168 no PDB 4IK1 . "High Resolution Structure Of Gcampj At Ph 8.5" . . . . . 99.32 448 97.28 98.64 3.15e-92 . . . . 18556 1 169 no PDB 4IK3 . "High Resolution Structure Of Gcamp3 At Ph 8.5" . . . . . 99.32 448 97.96 99.32 2.69e-93 . . . . 18556 1 170 no PDB 4IK4 . "High Resolution Structure Of Gcamp3 At Ph 5.0" . . . . . 99.32 448 97.96 99.32 2.69e-93 . . . . 18556 1 171 no PDB 4IK5 . "High Resolution Structure Of Delta-rest-gcamp3" . . . . . 99.32 414 97.96 99.32 1.19e-93 . . . . 18556 1 172 no PDB 4IK8 . "High Resolution Structure Of Gcamp3 Dimer Form 1 At Ph 7.5" . . . . . 99.32 448 97.96 99.32 2.69e-93 . . . . 18556 1 173 no PDB 4IK9 . "High Resolution Structure Of Gcamp3 Dimer Form 2 At Ph 7.5" . . . . . 99.32 448 97.96 99.32 2.69e-93 . . . . 18556 1 174 no PDB 4J9Y . "Calcium-calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 175 no PDB 4J9Z . "Calcium-calmodulin Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Splice Variant And N" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 176 no PDB 4JPZ . "Voltage-gated Sodium Channel 1.2 C-terminal Domain In Complex With Fgf13u And Ca2+/calmodulin" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 177 no PDB 4JQ0 . "Voltage-gated Sodium Channel 1.5 C-terminal Domain In Complex With Fgf12b And Ca2+/calmodulin" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 178 no PDB 4L79 . "Crystal Structure Of Nucleotide-free Myosin 1b Residues 1-728 With Bound Calmodulin" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 179 no PDB 4LZX . "Complex Of Iqcg And Ca2+-free Cam" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 180 no PDB 4M1L . "Complex Of Iqcg And Ca2+-bound Cam" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 181 no PDB 4PJJ . "Myosin Vi (md-insert2-cam, Delta-insert1) Post-rigor State - Long Soaking With Po4" . . . . . 100.00 149 98.65 100.00 1.09e-98 . . . . 18556 1 182 no PDB 4Q5U . "Structure Of Calmodulin Bound To Its Recognition Site From Calcineurin" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 183 no PDB 4QNH . "Calcium-calmodulin (t79d) Complexed With The Calmodulin Binding Domain From A Small Conductance Potassium Channel Sk2-a" . . . . . 100.00 149 97.97 98.65 3.60e-97 . . . . 18556 1 184 no PDB 4R8G . "Crystal Structure Of Myosin-1c Tail In Complex With Calmodulin" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 185 no PDB 4UMO . "Crystal Structure Of The Kv7.1 Proximal C-terminal Domain In Complex With Calmodulin" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 186 no PDB 4UPU . "Crystal Structure Of Ip3 3-k Calmodulin Binding Region In Complex With Calmodulin" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 187 no PDB 4V0C . "Crystal Structure Of The Kv7.1 Proximal C-terminal Domain In Complex With Calmodulin" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 188 no DBJ BAA08302 . "calmodulin [Homo sapiens]" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 189 no DBJ BAA11896 . "calmodulin [Anas platyrhynchos]" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 190 no DBJ BAA19786 . "calmodulin [Branchiostoma lanceolatum]" . . . . . 100.00 149 99.32 100.00 5.49e-99 . . . . 18556 1 191 no DBJ BAA19787 . "calmodulin [Branchiostoma floridae]" . . . . . 100.00 149 99.32 100.00 5.49e-99 . . . . 18556 1 192 no DBJ BAA19788 . "calmodulin [Halocynthia roretzi]" . . . . . 100.00 149 99.32 100.00 5.49e-99 . . . . 18556 1 193 no EMBL CAA10601 . "calmodulin [Caenorhabditis elegans]" . . . . . 100.00 149 99.32 99.32 1.22e-98 . . . . 18556 1 194 no EMBL CAA32050 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 195 no EMBL CAA32062 . "calmodulin II [Rattus norvegicus]" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 196 no EMBL CAA32119 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 197 no EMBL CAA32120 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 198 no GB AAA35635 . "calmodulin [Homo sapiens]" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 199 no GB AAA35641 . "calmodulin [Homo sapiens]" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 200 no GB AAA37365 . "calmodulin synthesis [Mus musculus]" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 201 no GB AAA40862 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 202 no GB AAA40863 . "calmodulin [Rattus norvegicus]" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 203 no PIR JC1305 . "calmodulin - Japanese medaka" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 204 no PIR MCON . "calmodulin - salmon" . . . . . 100.00 148 98.65 99.32 2.65e-98 . . . . 18556 1 205 no PRF 0711223A . calmodulin . . . . . 100.00 148 97.97 100.00 3.80e-97 . . . . 18556 1 206 no REF NP_001008160 . "calmodulin [Xenopus (Silurana) tropicalis]" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 207 no REF NP_001009759 . "calmodulin [Ovis aries]" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 208 no REF NP_001027633 . "calmodulin [Ciona intestinalis]" . . . . . 100.00 149 97.97 98.65 1.62e-97 . . . . 18556 1 209 no REF NP_001039714 . "calmodulin [Bos taurus]" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 210 no REF NP_001040234 . "calmodulin [Bombyx mori]" . . . . . 100.00 149 99.32 100.00 5.49e-99 . . . . 18556 1 211 no SP O02367 . "RecName: Full=Calmodulin; Short=CaM; AltName: Full=Ci-CaM" . . . . . 100.00 149 97.97 98.65 1.62e-97 . . . . 18556 1 212 no SP O16305 . "RecName: Full=Calmodulin; Short=CaM" . . . . . 100.00 149 99.32 99.32 1.22e-98 . . . . 18556 1 213 no SP O96081 . "RecName: Full=Calmodulin-B; Short=CaM B" . . . . . 100.00 149 98.65 99.32 3.19e-98 . . . . 18556 1 214 no SP P02594 . "RecName: Full=Calmodulin; Short=CaM" . . . . . 100.00 149 97.97 99.32 6.78e-98 . . . . 18556 1 215 no SP P02595 . "RecName: Full=Calmodulin; Short=CaM" . . . . . 100.00 149 97.97 100.00 3.81e-97 . . . . 18556 1 216 no TPG DAA13808 . "TPA: calmodulin 2-like [Bos taurus]" . . . . . 100.00 216 97.30 97.97 1.20e-96 . . . . 18556 1 217 no TPG DAA18029 . "TPA: calmodulin [Bos taurus]" . . . . . 100.00 149 97.97 99.32 1.20e-97 . . . . 18556 1 218 no TPG DAA19590 . "TPA: calmodulin 3 [Bos taurus]" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 219 no TPG DAA24777 . "TPA: calmodulin 2-like [Bos taurus]" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 220 no TPG DAA24988 . "TPA: calmodulin 2-like isoform 1 [Bos taurus]" . . . . . 100.00 149 98.65 99.32 2.20e-98 . . . . 18556 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . ALA . 18556 1 2 . ASP . 18556 1 3 . GLN . 18556 1 4 . LEU . 18556 1 5 . THR . 18556 1 6 . GLU . 18556 1 7 . GLU . 18556 1 8 . GLN . 18556 1 9 . ILE . 18556 1 10 . ALA . 18556 1 11 . GLU . 18556 1 12 . PHE . 18556 1 13 . LYS . 18556 1 14 . GLU . 18556 1 15 . ALA . 18556 1 16 . PHE . 18556 1 17 . SER . 18556 1 18 . LEU . 18556 1 19 . PHE . 18556 1 20 . ASP . 18556 1 21 . LYS . 18556 1 22 . ASP . 18556 1 23 . GLY . 18556 1 24 . ASP . 18556 1 25 . GLY . 18556 1 26 . THR . 18556 1 27 . ILE . 18556 1 28 . THR . 18556 1 29 . THR . 18556 1 30 . LYS . 18556 1 31 . GLU . 18556 1 32 . LEU . 18556 1 33 . GLY . 18556 1 34 . THR . 18556 1 35 . VAL . 18556 1 36 . MET . 18556 1 37 . ARG . 18556 1 38 . SER . 18556 1 39 . LEU . 18556 1 40 . GLY . 18556 1 41 . GLN . 18556 1 42 . ASN . 18556 1 43 . PRO . 18556 1 44 . THR . 18556 1 45 . GLU . 18556 1 46 . ALA . 18556 1 47 . GLU . 18556 1 48 . LEU . 18556 1 49 . GLN . 18556 1 50 . ASP . 18556 1 51 . MET . 18556 1 52 . ILE . 18556 1 53 . ASN . 18556 1 54 . GLU . 18556 1 55 . VAL . 18556 1 56 . ASP . 18556 1 57 . ALA . 18556 1 58 . ASP . 18556 1 59 . GLY . 18556 1 60 . ASN . 18556 1 61 . GLY . 18556 1 62 . THR . 18556 1 63 . ILE . 18556 1 64 . ASP . 18556 1 65 . PHE . 18556 1 66 . PRO . 18556 1 67 . GLU . 18556 1 68 . PHE . 18556 1 69 . LEU . 18556 1 70 . THR . 18556 1 71 . MET . 18556 1 72 . MET . 18556 1 73 . ALA . 18556 1 74 . ARG . 18556 1 75 . LYS . 18556 1 76 . MET . 18556 1 77 . LYS . 18556 1 78 . ASP . 18556 1 79 . THR . 18556 1 80 . ASP . 18556 1 81 . SER . 18556 1 82 . GLU . 18556 1 83 . GLU . 18556 1 84 . GLU . 18556 1 85 . ILE . 18556 1 86 . ARG . 18556 1 87 . GLU . 18556 1 88 . ALA . 18556 1 89 . PHE . 18556 1 90 . ARG . 18556 1 91 . VAL . 18556 1 92 . PHE . 18556 1 93 . ASP . 18556 1 94 . LYS . 18556 1 95 . ASP . 18556 1 96 . GLY . 18556 1 97 . ASN . 18556 1 98 . GLY . 18556 1 99 . PHE . 18556 1 100 . ILE . 18556 1 101 . SER . 18556 1 102 . ALA . 18556 1 103 . ALA . 18556 1 104 . GLU . 18556 1 105 . LEU . 18556 1 106 . ARG . 18556 1 107 . HIS . 18556 1 108 . VAL . 18556 1 109 . MET . 18556 1 110 . THR . 18556 1 111 . ASN . 18556 1 112 . LEU . 18556 1 113 . GLY . 18556 1 114 . GLU . 18556 1 115 . LYS . 18556 1 116 . LEU . 18556 1 117 . THR . 18556 1 118 . ASP . 18556 1 119 . GLU . 18556 1 120 . GLU . 18556 1 121 . VAL . 18556 1 122 . ASP . 18556 1 123 . GLU . 18556 1 124 . MET . 18556 1 125 . ILE . 18556 1 126 . ARG . 18556 1 127 . GLU . 18556 1 128 . ALA . 18556 1 129 . ASP . 18556 1 130 . ILE . 18556 1 131 . ASP . 18556 1 132 . GLY . 18556 1 133 . ASP . 18556 1 134 . GLY . 18556 1 135 . GLN . 18556 1 136 . VAL . 18556 1 137 . ASN . 18556 1 138 . TYR . 18556 1 139 . GLU . 18556 1 140 . GLU . 18556 1 141 . PHE . 18556 1 142 . VAL . 18556 1 143 . THR . 18556 1 144 . MET . 18556 1 145 . MET . 18556 1 146 . THR . 18556 1 147 . ALA . 18556 1 148 . LYS . 18556 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . ALA 1 1 18556 1 . ASP 2 2 18556 1 . GLN 3 3 18556 1 . LEU 4 4 18556 1 . THR 5 5 18556 1 . GLU 6 6 18556 1 . GLU 7 7 18556 1 . GLN 8 8 18556 1 . ILE 9 9 18556 1 . ALA 10 10 18556 1 . GLU 11 11 18556 1 . PHE 12 12 18556 1 . LYS 13 13 18556 1 . GLU 14 14 18556 1 . ALA 15 15 18556 1 . PHE 16 16 18556 1 . SER 17 17 18556 1 . LEU 18 18 18556 1 . PHE 19 19 18556 1 . ASP 20 20 18556 1 . LYS 21 21 18556 1 . ASP 22 22 18556 1 . GLY 23 23 18556 1 . ASP 24 24 18556 1 . GLY 25 25 18556 1 . THR 26 26 18556 1 . ILE 27 27 18556 1 . THR 28 28 18556 1 . THR 29 29 18556 1 . LYS 30 30 18556 1 . GLU 31 31 18556 1 . LEU 32 32 18556 1 . GLY 33 33 18556 1 . THR 34 34 18556 1 . VAL 35 35 18556 1 . MET 36 36 18556 1 . ARG 37 37 18556 1 . SER 38 38 18556 1 . LEU 39 39 18556 1 . GLY 40 40 18556 1 . GLN 41 41 18556 1 . ASN 42 42 18556 1 . PRO 43 43 18556 1 . THR 44 44 18556 1 . GLU 45 45 18556 1 . ALA 46 46 18556 1 . GLU 47 47 18556 1 . LEU 48 48 18556 1 . GLN 49 49 18556 1 . ASP 50 50 18556 1 . MET 51 51 18556 1 . ILE 52 52 18556 1 . ASN 53 53 18556 1 . GLU 54 54 18556 1 . VAL 55 55 18556 1 . ASP 56 56 18556 1 . ALA 57 57 18556 1 . ASP 58 58 18556 1 . GLY 59 59 18556 1 . ASN 60 60 18556 1 . GLY 61 61 18556 1 . THR 62 62 18556 1 . ILE 63 63 18556 1 . ASP 64 64 18556 1 . PHE 65 65 18556 1 . PRO 66 66 18556 1 . GLU 67 67 18556 1 . PHE 68 68 18556 1 . LEU 69 69 18556 1 . THR 70 70 18556 1 . MET 71 71 18556 1 . MET 72 72 18556 1 . ALA 73 73 18556 1 . ARG 74 74 18556 1 . LYS 75 75 18556 1 . MET 76 76 18556 1 . LYS 77 77 18556 1 . ASP 78 78 18556 1 . THR 79 79 18556 1 . ASP 80 80 18556 1 . SER 81 81 18556 1 . GLU 82 82 18556 1 . GLU 83 83 18556 1 . GLU 84 84 18556 1 . ILE 85 85 18556 1 . ARG 86 86 18556 1 . GLU 87 87 18556 1 . ALA 88 88 18556 1 . PHE 89 89 18556 1 . ARG 90 90 18556 1 . VAL 91 91 18556 1 . PHE 92 92 18556 1 . ASP 93 93 18556 1 . LYS 94 94 18556 1 . ASP 95 95 18556 1 . GLY 96 96 18556 1 . ASN 97 97 18556 1 . GLY 98 98 18556 1 . PHE 99 99 18556 1 . ILE 100 100 18556 1 . SER 101 101 18556 1 . ALA 102 102 18556 1 . ALA 103 103 18556 1 . GLU 104 104 18556 1 . LEU 105 105 18556 1 . ARG 106 106 18556 1 . HIS 107 107 18556 1 . VAL 108 108 18556 1 . MET 109 109 18556 1 . THR 110 110 18556 1 . ASN 111 111 18556 1 . LEU 112 112 18556 1 . GLY 113 113 18556 1 . GLU 114 114 18556 1 . LYS 115 115 18556 1 . LEU 116 116 18556 1 . THR 117 117 18556 1 . ASP 118 118 18556 1 . GLU 119 119 18556 1 . GLU 120 120 18556 1 . VAL 121 121 18556 1 . ASP 122 122 18556 1 . GLU 123 123 18556 1 . MET 124 124 18556 1 . ILE 125 125 18556 1 . ARG 126 126 18556 1 . GLU 127 127 18556 1 . ALA 128 128 18556 1 . ASP 129 129 18556 1 . ILE 130 130 18556 1 . ASP 131 131 18556 1 . GLY 132 132 18556 1 . ASP 133 133 18556 1 . GLY 134 134 18556 1 . GLN 135 135 18556 1 . VAL 136 136 18556 1 . ASN 137 137 18556 1 . TYR 138 138 18556 1 . GLU 139 139 18556 1 . GLU 140 140 18556 1 . PHE 141 141 18556 1 . VAL 142 142 18556 1 . THR 143 143 18556 1 . MET 144 144 18556 1 . MET 145 145 18556 1 . THR 146 146 18556 1 . ALA 147 147 18556 1 . LYS 148 148 18556 1 stop_ save_ save_ssMLCK _Entity.Sf_category entity _Entity.Sf_framecode ssMLCK _Entity.Entry_ID 18556 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name ssMLCK _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID B _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; KRRWKKNFIAVSAANRFKKI SSSGAL ; _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 26 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment 'skeletal muscle myosin light chain kinase' _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 2972.567 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-30 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 7028 . "WFF peptide" . . . . . 69.23 18 100.00 100.00 6.00e-02 . . . . 18556 2 2 no PDB 2B8K . "12-Subunit Rna Polymerase Ii" . . . . . 100.00 215 100.00 100.00 7.07e-08 . . . . 18556 2 3 no PDB 2BBM . "Solution Structure Of A Calmodulin-Target Peptide Complex By Multidimensional Nmr" . . . . . 100.00 26 100.00 100.00 4.12e-07 . . . . 18556 2 4 no PDB 2BBN . "Solution Structure Of A Calmodulin-Target Peptide Complex By Multidimensional Nmr" . . . . . 100.00 26 100.00 100.00 4.12e-07 . . . . 18556 2 5 no PDB 2LV6 . "The Complex Between Ca-calmodulin And Skeletal Muscle Myosin Light Chain Kinase From Combination Of Nmr And Aqueous And Contras" . . . . . 100.00 26 100.00 100.00 4.12e-07 . . . . 18556 2 6 no PDB 3KF9 . "Crystal Structure Of The SdcenSKMLCK COMPLEX" . . . . . 84.62 22 100.00 100.00 2.74e-04 . . . . 18556 2 7 no PDB 3P9D . "The Crystal Structure Of Yeast Cct Reveals Intrinsic Asymmetry Of Eukaryotic Cytosolic Chaperonins" . . . . . 100.00 590 100.00 100.00 1.51e-07 . . . . 18556 2 8 no PDB 3P9E . "The Crystal Structure Of Yeast Cct Reveals Intrinsic Asymmetry Of Eukaryotic Cytosolic Chaperonins" . . . . . 100.00 590 100.00 100.00 1.51e-07 . . . . 18556 2 9 no PDB 4AOL . "The Crystal Structures Of The Eukaryotic Chaperonin Cct Reveal Its Functional Partitioning" . . . . . 100.00 590 100.00 100.00 1.51e-07 . . . . 18556 2 10 no PDB 4APK . "The Crystal Structures Of The Eukaryotic Chaperonin Cct Reveal Its Functional Partitioning" . . . . . 100.00 590 100.00 100.00 1.51e-07 . . . . 18556 2 11 no PDB 4D8Q . "Molecular Architecture Of The Eukaryotic Chaperonin TricCCT DERIVED By A Combination Of Chemical Crosslinking And Mass-Spectrom" . . . . . 100.00 590 100.00 100.00 1.51e-07 . . . . 18556 2 12 no PDB 4D8R . "Molecular Architecture Of The Eukaryotic Chaperonin TricCCT DERIVED By A Combination Of Chemical Crosslinking And Mass-Spectrom" . . . . . 100.00 590 100.00 100.00 1.51e-07 . . . . 18556 2 13 no PDB 4GWP . "Structure Of The Mediator Head Module From S. Cerevisiae" . . . . . 100.00 407 100.00 100.00 4.09e-06 . . . . 18556 2 14 no PDB 4GWQ . "Structure Of The Mediator Head Module From S. Cerevisiae In Complex With The Carboxy-Terminal Domain (Ctd) Of Rna Polymerase Ii" . . . . . 100.00 407 100.00 100.00 4.09e-06 . . . . 18556 2 15 no PDB 4I43 . "Crystal Structure Of Prp8:aar2 Complex" . . . . . 100.00 1564 100.00 100.00 1.02e-06 . . . . 18556 2 16 no DBJ BAD30083 . "yellow cameleon 2.60 [synthetic construct]" . . . . . 100.00 653 100.00 100.00 6.76e-08 . . . . 18556 2 17 no DBJ BAD30084 . "yellow cameleon 3.60 [synthetic construct]" . . . . . 100.00 653 100.00 100.00 6.76e-08 . . . . 18556 2 18 no DBJ BAD30085 . "yellow cameleon 4.60 [synthetic construct]" . . . . . 100.00 653 100.00 100.00 6.76e-08 . . . . 18556 2 19 no DBJ BAD30086 . "yellow cameleon 3.60-pm [synthetic construct]" . . . . . 100.00 691 100.00 100.00 6.97e-08 . . . . 18556 2 20 no DBJ BAI47180 . "myosin light chain kinase 2 [synthetic construct]" . . . . . 100.00 596 100.00 100.00 1.62e-07 . . . . 18556 2 21 no EMBL CAA46981 . "51aa protein with 3 functional units; keptide unit,Factor X unit, calmodulin binding unit [synthetic construct]" . . . . . 100.00 52 100.00 100.00 2.27e-07 . . . . 18556 2 22 no EMBL CAC81354 . "skeletal muscle-specific myosin light chain kinase [Homo sapiens]" . . . . . 100.00 596 100.00 100.00 1.62e-07 . . . . 18556 2 23 no GB AAA31400 . "myosin light chain kinase (EC 2.7.1.-) [Oryctolagus cuniculus]" . . . . . 100.00 608 100.00 100.00 6.49e-08 . . . . 18556 2 24 no GB AAC71016 . "calmodulin-binding peptide-FLAG epitope fusion protein [Cloning vector pCALnFLAG]" . . . . . 100.00 61 100.00 100.00 2.03e-07 . . . . 18556 2 25 no GB AAH07753 . "MYLK2 protein, partial [Homo sapiens]" . . . . . 100.00 242 100.00 100.00 1.07e-07 . . . . 18556 2 26 no GB AAH19408 . "Mylk2 protein, partial [Mus musculus]" . . . . . 100.00 240 100.00 100.00 8.82e-08 . . . . 18556 2 27 no GB AAH69627 . "Myosin light chain kinase 2 [Homo sapiens]" . . . . . 100.00 596 100.00 100.00 1.62e-07 . . . . 18556 2 28 no PRF 1507147A . "myosin L kinase" . . . . . 100.00 315 100.00 100.00 2.07e-07 . . . . 18556 2 29 no REF NP_001074513 . "myosin light chain kinase 2, skeletal/cardiac muscle [Mus musculus]" . . . . . 100.00 613 100.00 100.00 1.12e-07 . . . . 18556 2 30 no REF NP_001075705 . "myosin light chain kinase 2, skeletal/cardiac muscle [Oryctolagus cuniculus]" . . . . . 100.00 608 100.00 100.00 6.49e-08 . . . . 18556 2 31 no REF NP_001077188 . "myosin light chain kinase 2, skeletal/cardiac muscle [Bos taurus]" . . . . . 100.00 623 100.00 100.00 6.58e-08 . . . . 18556 2 32 no REF NP_149109 . "myosin light chain kinase 2, skeletal/cardiac muscle [Homo sapiens]" . . . . . 100.00 596 100.00 100.00 1.62e-07 . . . . 18556 2 33 no REF XP_001499833 . "PREDICTED: myosin light chain kinase 2, skeletal/cardiac muscle isoformX1 [Equus caballus]" . . . . . 100.00 668 100.00 100.00 6.85e-08 . . . . 18556 2 34 no SP A4IFM7 . "RecName: Full=Myosin light chain kinase 2, skeletal/cardiac muscle; Short=MLCK2 [Bos taurus]" . . . . . 100.00 623 100.00 100.00 6.58e-08 . . . . 18556 2 35 no SP P07313 . "RecName: Full=Myosin light chain kinase 2, skeletal/cardiac muscle; Short=MLCK2 [Oryctolagus cuniculus]" . . . . . 100.00 608 100.00 100.00 6.49e-08 . . . . 18556 2 36 no SP P20689 . "RecName: Full=Myosin light chain kinase 2, skeletal/cardiac muscle; Short=MLCK2 [Rattus norvegicus]" . . . . . 100.00 610 100.00 100.00 6.50e-08 . . . . 18556 2 37 no SP Q8VCR8 . "RecName: Full=Myosin light chain kinase 2, skeletal/cardiac muscle; Short=MLCK2 [Mus musculus]" . . . . . 100.00 613 100.00 100.00 1.12e-07 . . . . 18556 2 38 no SP Q9H1R3 . "RecName: Full=Myosin light chain kinase 2, skeletal/cardiac muscle; Short=MLCK2 [Homo sapiens]" . . . . . 100.00 596 100.00 100.00 1.62e-07 . . . . 18556 2 39 no TPG DAA23271 . "TPA: myosin light chain kinase 2, skeletal/cardiac muscle [Bos taurus]" . . . . . 100.00 623 100.00 100.00 6.58e-08 . . . . 18556 2 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . LYS . 18556 2 2 . ARG . 18556 2 3 . ARG . 18556 2 4 . TRP . 18556 2 5 . LYS . 18556 2 6 . LYS . 18556 2 7 . ASN . 18556 2 8 . PHE . 18556 2 9 . ILE . 18556 2 10 . ALA . 18556 2 11 . VAL . 18556 2 12 . SER . 18556 2 13 . ALA . 18556 2 14 . ALA . 18556 2 15 . ASN . 18556 2 16 . ARG . 18556 2 17 . PHE . 18556 2 18 . LYS . 18556 2 19 . LYS . 18556 2 20 . ILE . 18556 2 21 . SER . 18556 2 22 . SER . 18556 2 23 . SER . 18556 2 24 . GLY . 18556 2 25 . ALA . 18556 2 26 . LEU . 18556 2 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . LYS 1 1 18556 2 . ARG 2 2 18556 2 . ARG 3 3 18556 2 . TRP 4 4 18556 2 . LYS 5 5 18556 2 . LYS 6 6 18556 2 . ASN 7 7 18556 2 . PHE 8 8 18556 2 . ILE 9 9 18556 2 . ALA 10 10 18556 2 . VAL 11 11 18556 2 . SER 12 12 18556 2 . ALA 13 13 18556 2 . ALA 14 14 18556 2 . ASN 15 15 18556 2 . ARG 16 16 18556 2 . PHE 17 17 18556 2 . LYS 18 18 18556 2 . LYS 19 19 18556 2 . ILE 20 20 18556 2 . SER 21 21 18556 2 . SER 22 22 18556 2 . SER 23 23 18556 2 . GLY 24 24 18556 2 . ALA 25 25 18556 2 . LEU 26 26 18556 2 stop_ save_ save_entity_CA _Entity.Sf_category entity _Entity.Sf_framecode entity_CA _Entity.Entry_ID 18556 _Entity.ID 3 _Entity.BMRB_code CA _Entity.Name entity_CA _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID CA _Entity.Nonpolymer_comp_label $chem_comp_CA _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components 1 _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 3 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 40.078 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'CALCIUM ION' BMRB 18556 3 stop_ loop_ _Entity_systematic_name.Name _Entity_systematic_name.Naming_system _Entity_systematic_name.Entry_ID _Entity_systematic_name.Entity_ID 'CALCIUM ION' BMRB 18556 3 CA 'Three letter code' 18556 3 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 1 CA $chem_comp_CA 18556 3 stop_ loop_ _Entity_atom_list.ID _Entity_atom_list.Comp_index_ID _Entity_atom_list.Comp_ID _Entity_atom_list.Atom_ID _Entity_atom_list.Entry_ID _Entity_atom_list.Entity_ID 1 1 CA CA 18556 3 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 18556 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $Calmodulin . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 18556 1 2 2 $ssMLCK . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 18556 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 18556 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $Calmodulin . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli BL21 'codon-plus (DE3) RIPL' . . . . . . . . . . . . . . pET21a . . . . . . 18556 1 2 2 $ssMLCK . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 18556 1 3 3 $entity_CA . 'obtained from a vendor' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 18556 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_CA _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_CA _Chem_comp.Entry_ID 18556 _Chem_comp.ID CA _Chem_comp.Provenance PDB _Chem_comp.Name 'CALCIUM ION' _Chem_comp.Type NON-POLYMER _Chem_comp.BMRB_code CA _Chem_comp.PDB_code CA _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 2012-11-20 _Chem_comp.Modified_date 2012-11-20 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code CA _Chem_comp.Number_atoms_all 1 _Chem_comp.Number_atoms_nh 1 _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code InChI=1S/Ca/q+2 _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 2 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula Ca _Chem_comp.Formula_weight 40.078 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details . _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID BHPQYMZQTOCNFJ-UHFFFAOYSA-N InChIKey InChI 1.03 18556 CA [Ca++] SMILES CACTVS 3.341 18556 CA [Ca++] SMILES_CANONICAL CACTVS 3.341 18556 CA [Ca+2] SMILES ACDLabs 10.04 18556 CA [Ca+2] SMILES 'OpenEye OEToolkits' 1.5.0 18556 CA [Ca+2] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 18556 CA InChI=1S/Ca/q+2 InChI InChI 1.03 18556 CA stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID calcium 'SYSTEMATIC NAME' ACDLabs 10.04 18556 CA 'calcium(+2) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 18556 CA stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID CA CA CA CA . CA . . N 2 . . . 0 no no . . . . 0.000 . 0.000 . 0.000 . 0.000 0.000 0.000 1 . 18556 CA stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 18556 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '95% H2O/5% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 Calmodulin '[U-13C; U-15N; U-2H]' . . 1 $Calmodulin . . 0.3 . . mM . . . . 18556 1 2 ssMLCK 'natural abundance' . . 2 $ssMLCK . . 0.3 . . mM . . . . 18556 1 3 CaCl2 'natural abundance' . . 3 $entity_CA . . 3 . . mM . . . . 18556 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 18556 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '65% w/v sucrose/H2O' _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-13C; U-15N; U-2H]' . . 1 $Calmodulin . . . 0.06 0.25 mM . . . . 18556 2 2 ssMLCK 'natural abundance' . . 2 $ssMLCK . . . 0.06 0.25 mM . . . . 18556 2 3 CaCl2 'natural abundance' . . 3 $entity_CA . . 3 . . mM . . . . 18556 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 18556 _Sample_condition_list.ID 1 _Sample_condition_list.Details ; CaM/MLCK in aqueous buffer with 3mM CaCl2 ; loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.1 . M 18556 1 pH 6.5 . pH 18556 1 pressure 1 . atm 18556 1 temperature 273 . K 18556 1 stop_ save_ save_sample_conditions_2 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_2 _Sample_condition_list.Entry_ID 18556 _Sample_condition_list.ID 2 _Sample_condition_list.Details 'CaM/MLCK in 65% sucrose buffer with 3uM PbCl2' loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.15 . M 18556 2 pH 6.5 . pH 18556 2 pressure 1 . atm 18556 2 temperature 273 . K 18556 2 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 18556 _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' . . 18556 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 18556 1 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 18556 _Software.ID 2 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 18556 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 18556 2 stop_ save_ save_Custom _Software.Sf_category software _Software.Sf_framecode Custom _Software.Entry_ID 18556 _Software.ID 3 _Software.Name Custom _Software.Version . _Software.Details 'Grid search procedure for rigid-body optimization of the relative domain positions against RDC and SAXS data' loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Grishaev . . 18556 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 18556 3 stop_ save_ save_CNS _Software.Sf_category software _Software.Sf_framecode CNS _Software.Entry_ID 18556 _Software.ID 4 _Software.Name CNS _Software.Version 1.0 _Software.Details 'used for optimization of the linker ends connecting N- and C-terminal domains of calmodulin int he complex with MLCK' loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Brunger, Adams, Clore, Gros, Nilges and Read' . . 18556 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 18556 4 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 18556 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 18556 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Bruker DRX . 600 . . . 18556 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 18556 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N HSQC' no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18556 1 2 '2D 1H-15N HSQC' no 1 $NMR_spectrometer_expt . . . . . . . . 1 $sample_1 anisotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18556 1 stop_ save_ save_NMR_spectrometer_expt _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spectrometer_expt _NMR_spec_expt.Entry_ID 18556 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name . _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $spectrometer_1 _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 18556 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 water protons . . . . ppm 4.754 internal direct 1.0 . . . . . . . . . 18556 1 N 15 'protein backbone amides' nitrogen . . . . ppm 0.0 internal indirect 0.101329118 . . . . . . . . . 18556 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 18556 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-15N HSQC' . . . 18556 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 3 3 GLN H H 1 8.347 . . 1 . . . A 3 GLN H . 18556 1 2 . 1 1 3 3 GLN N N 15 120.996 . . 1 . . . A 3 GLN N . 18556 1 3 . 1 1 4 4 LEU H H 1 8.254 . . 1 . . . A 4 LEU H . 18556 1 4 . 1 1 4 4 LEU N N 15 124.429 . . 1 . . . A 4 LEU N . 18556 1 5 . 1 1 5 5 THR H H 1 8.768 . . 1 . . . A 5 THR H . 18556 1 6 . 1 1 5 5 THR N N 15 113.937 . . 1 . . . A 5 THR N . 18556 1 7 . 1 1 6 6 GLU H H 1 8.929 . . 1 . . . A 6 GLU H . 18556 1 8 . 1 1 6 6 GLU N N 15 120.853 . . 1 . . . A 6 GLU N . 18556 1 9 . 1 1 7 7 GLU H H 1 8.473 . . 1 . . . A 7 GLU H . 18556 1 10 . 1 1 7 7 GLU N N 15 120.555 . . 1 . . . A 7 GLU N . 18556 1 11 . 1 1 8 8 GLN H H 1 7.717 . . 1 . . . A 8 GLN H . 18556 1 12 . 1 1 8 8 GLN N N 15 119.379 . . 1 . . . A 8 GLN N . 18556 1 13 . 1 1 9 9 ILE H H 1 8.485 . . 1 . . . A 9 ILE H . 18556 1 14 . 1 1 9 9 ILE N N 15 120.599 . . 1 . . . A 9 ILE N . 18556 1 15 . 1 1 10 10 ALA H H 1 7.981 . . 1 . . . A 10 ALA H . 18556 1 16 . 1 1 10 10 ALA N N 15 122.315 . . 1 . . . A 10 ALA N . 18556 1 17 . 1 1 11 11 GLU H H 1 7.834 . . 1 . . . A 11 GLU H . 18556 1 18 . 1 1 11 11 GLU N N 15 119.078 . . 1 . . . A 11 GLU N . 18556 1 19 . 1 1 12 12 PHE H H 1 8.238 . . 1 . . . A 12 PHE H . 18556 1 20 . 1 1 12 12 PHE N N 15 117.646 . . 1 . . . A 12 PHE N . 18556 1 21 . 1 1 13 13 LYS H H 1 9.164 . . 1 . . . A 13 LYS H . 18556 1 22 . 1 1 13 13 LYS N N 15 123.393 . . 1 . . . A 13 LYS N . 18556 1 23 . 1 1 14 14 GLU H H 1 8.188 . . 1 . . . A 14 GLU H . 18556 1 24 . 1 1 14 14 GLU N N 15 120.423 . . 1 . . . A 14 GLU N . 18556 1 25 . 1 1 15 15 ALA H H 1 8.144 . . 1 . . . A 15 ALA H . 18556 1 26 . 1 1 15 15 ALA N N 15 123.615 . . 1 . . . A 15 ALA N . 18556 1 27 . 1 1 16 16 PHE H H 1 8.843 . . 1 . . . A 16 PHE H . 18556 1 28 . 1 1 16 16 PHE N N 15 119.734 . . 1 . . . A 16 PHE N . 18556 1 29 . 1 1 17 17 SER H H 1 8.009 . . 1 . . . A 17 SER H . 18556 1 30 . 1 1 17 17 SER N N 15 114.963 . . 1 . . . A 17 SER N . 18556 1 31 . 1 1 18 18 LEU H H 1 7.410 . . 1 . . . A 18 LEU H . 18556 1 32 . 1 1 18 18 LEU N N 15 120.314 . . 1 . . . A 18 LEU N . 18556 1 33 . 1 1 19 19 PHE H H 1 7.226 . . 1 . . . A 19 PHE H . 18556 1 34 . 1 1 19 19 PHE N N 15 115.206 . . 1 . . . A 19 PHE N . 18556 1 35 . 1 1 20 20 ASP H H 1 7.644 . . 1 . . . A 20 ASP H . 18556 1 36 . 1 1 20 20 ASP N N 15 117.467 . . 1 . . . A 20 ASP N . 18556 1 37 . 1 1 21 21 LYS H H 1 7.485 . . 1 . . . A 21 LYS H . 18556 1 38 . 1 1 21 21 LYS N N 15 123.678 . . 1 . . . A 21 LYS N . 18556 1 39 . 1 1 22 22 ASP H H 1 8.013 . . 1 . . . A 22 ASP H . 18556 1 40 . 1 1 22 22 ASP N N 15 114.531 . . 1 . . . A 22 ASP N . 18556 1 41 . 1 1 23 23 GLY H H 1 7.637 . . 1 . . . A 23 GLY H . 18556 1 42 . 1 1 23 23 GLY N N 15 110.174 . . 1 . . . A 23 GLY N . 18556 1 43 . 1 1 24 24 ASP H H 1 8.452 . . 1 . . . A 24 ASP H . 18556 1 44 . 1 1 24 24 ASP N N 15 121.917 . . 1 . . . A 24 ASP N . 18556 1 45 . 1 1 25 25 GLY H H 1 10.557 . . 1 . . . A 25 GLY H . 18556 1 46 . 1 1 25 25 GLY N N 15 113.602 . . 1 . . . A 25 GLY N . 18556 1 47 . 1 1 26 26 THR H H 1 8.128 . . 1 . . . A 26 THR H . 18556 1 48 . 1 1 26 26 THR N N 15 112.486 . . 1 . . . A 26 THR N . 18556 1 49 . 1 1 27 27 ILE H H 1 9.975 . . 1 . . . A 27 ILE H . 18556 1 50 . 1 1 27 27 ILE N N 15 127.198 . . 1 . . . A 27 ILE N . 18556 1 51 . 1 1 28 28 THR H H 1 8.382 . . 1 . . . A 28 THR H . 18556 1 52 . 1 1 28 28 THR N N 15 116.943 . . 1 . . . A 28 THR N . 18556 1 53 . 1 1 29 29 THR H H 1 9.065 . . 1 . . . A 29 THR H . 18556 1 54 . 1 1 29 29 THR N N 15 113.249 . . 1 . . . A 29 THR N . 18556 1 55 . 1 1 30 30 LYS H H 1 7.520 . . 1 . . . A 30 LYS H . 18556 1 56 . 1 1 30 30 LYS N N 15 121.355 . . 1 . . . A 30 LYS N . 18556 1 57 . 1 1 31 31 GLU H H 1 7.654 . . 1 . . . A 31 GLU H . 18556 1 58 . 1 1 31 31 GLU N N 15 122.574 . . 1 . . . A 31 GLU N . 18556 1 59 . 1 1 32 32 LEU H H 1 8.669 . . 1 . . . A 32 LEU H . 18556 1 60 . 1 1 32 32 LEU N N 15 121.075 . . 1 . . . A 32 LEU N . 18556 1 61 . 1 1 33 33 GLY H H 1 8.647 . . 1 . . . A 33 GLY H . 18556 1 62 . 1 1 33 33 GLY N N 15 106.479 . . 1 . . . A 33 GLY N . 18556 1 63 . 1 1 34 34 THR H H 1 7.845 . . 1 . . . A 34 THR H . 18556 1 64 . 1 1 34 34 THR N N 15 118.569 . . 1 . . . A 34 THR N . 18556 1 65 . 1 1 35 35 VAL H H 1 7.550 . . 1 . . . A 35 VAL H . 18556 1 66 . 1 1 35 35 VAL N N 15 123.149 . . 1 . . . A 35 VAL N . 18556 1 67 . 1 1 36 36 MET H H 1 8.476 . . 1 . . . A 36 MET H . 18556 1 68 . 1 1 36 36 MET N N 15 117.276 . . 1 . . . A 36 MET N . 18556 1 69 . 1 1 37 37 ARG H H 1 8.539 . . 1 . . . A 37 ARG H . 18556 1 70 . 1 1 37 37 ARG N N 15 118.981 . . 1 . . . A 37 ARG N . 18556 1 71 . 1 1 38 38 SER H H 1 7.972 . . 1 . . . A 38 SER H . 18556 1 72 . 1 1 38 38 SER N N 15 120.097 . . 1 . . . A 38 SER N . 18556 1 73 . 1 1 39 39 LEU H H 1 7.298 . . 1 . . . A 39 LEU H . 18556 1 74 . 1 1 39 39 LEU N N 15 119.469 . . 1 . . . A 39 LEU N . 18556 1 75 . 1 1 40 40 GLY H H 1 7.775 . . 1 . . . A 40 GLY H . 18556 1 76 . 1 1 40 40 GLY N N 15 107.845 . . 1 . . . A 40 GLY N . 18556 1 77 . 1 1 41 41 GLN H H 1 7.945 . . 1 . . . A 41 GLN H . 18556 1 78 . 1 1 41 41 GLN N N 15 119.289 . . 1 . . . A 41 GLN N . 18556 1 79 . 1 1 42 42 ASN H H 1 8.652 . . 1 . . . A 42 ASN H . 18556 1 80 . 1 1 42 42 ASN N N 15 116.758 . . 1 . . . A 42 ASN N . 18556 1 81 . 1 1 44 44 THR H H 1 8.821 . . 1 . . . A 44 THR H . 18556 1 82 . 1 1 44 44 THR N N 15 113.911 . . 1 . . . A 44 THR N . 18556 1 83 . 1 1 45 45 GLU H H 1 8.744 . . 1 . . . A 45 GLU H . 18556 1 84 . 1 1 45 45 GLU N N 15 120.879 . . 1 . . . A 45 GLU N . 18556 1 85 . 1 1 46 46 ALA H H 1 8.214 . . 1 . . . A 46 ALA H . 18556 1 86 . 1 1 46 46 ALA N N 15 121.605 . . 1 . . . A 46 ALA N . 18556 1 87 . 1 1 47 47 GLU H H 1 7.659 . . 1 . . . A 47 GLU H . 18556 1 88 . 1 1 47 47 GLU N N 15 119.501 . . 1 . . . A 47 GLU N . 18556 1 89 . 1 1 48 48 LEU H H 1 8.177 . . 1 . . . A 48 LEU H . 18556 1 90 . 1 1 48 48 LEU N N 15 120.480 . . 1 . . . A 48 LEU N . 18556 1 91 . 1 1 49 49 GLN H H 1 7.997 . . 1 . . . A 49 GLN H . 18556 1 92 . 1 1 49 49 GLN N N 15 118.369 . . 1 . . . A 49 GLN N . 18556 1 93 . 1 1 50 50 ASP H H 1 7.900 . . 1 . . . A 50 ASP H . 18556 1 94 . 1 1 50 50 ASP N N 15 120.856 . . 1 . . . A 50 ASP N . 18556 1 95 . 1 1 51 51 MET H H 1 8.038 . . 1 . . . A 51 MET H . 18556 1 96 . 1 1 51 51 MET N N 15 119.982 . . 1 . . . A 51 MET N . 18556 1 97 . 1 1 52 52 ILE H H 1 7.478 . . 1 . . . A 52 ILE H . 18556 1 98 . 1 1 52 52 ILE N N 15 116.643 . . 1 . . . A 52 ILE N . 18556 1 99 . 1 1 53 53 ASN H H 1 8.646 . . 1 . . . A 53 ASN H . 18556 1 100 . 1 1 53 53 ASN N N 15 117.435 . . 1 . . . A 53 ASN N . 18556 1 101 . 1 1 54 54 GLU H H 1 7.555 . . 1 . . . A 54 GLU H . 18556 1 102 . 1 1 54 54 GLU N N 15 116.901 . . 1 . . . A 54 GLU N . 18556 1 103 . 1 1 55 55 VAL H H 1 7.074 . . 1 . . . A 55 VAL H . 18556 1 104 . 1 1 55 55 VAL N N 15 112.988 . . 1 . . . A 55 VAL N . 18556 1 105 . 1 1 56 56 ASP H H 1 7.763 . . 1 . . . A 56 ASP H . 18556 1 106 . 1 1 56 56 ASP N N 15 122.343 . . 1 . . . A 56 ASP N . 18556 1 107 . 1 1 57 57 ALA H H 1 7.967 . . 1 . . . A 57 ALA H . 18556 1 108 . 1 1 57 57 ALA N N 15 131.834 . . 1 . . . A 57 ALA N . 18556 1 109 . 1 1 58 58 ASP H H 1 8.177 . . 1 . . . A 58 ASP H . 18556 1 110 . 1 1 58 58 ASP N N 15 114.591 . . 1 . . . A 58 ASP N . 18556 1 111 . 1 1 59 59 GLY H H 1 7.547 . . 1 . . . A 59 GLY H . 18556 1 112 . 1 1 59 59 GLY N N 15 109.453 . . 1 . . . A 59 GLY N . 18556 1 113 . 1 1 60 60 ASN H H 1 8.146 . . 1 . . . A 60 ASN H . 18556 1 114 . 1 1 60 60 ASN N N 15 119.709 . . 1 . . . A 60 ASN N . 18556 1 115 . 1 1 61 61 GLY H H 1 10.568 . . 1 . . . A 61 GLY H . 18556 1 116 . 1 1 61 61 GLY N N 15 114.187 . . 1 . . . A 61 GLY N . 18556 1 117 . 1 1 62 62 THR H H 1 7.565 . . 1 . . . A 62 THR H . 18556 1 118 . 1 1 62 62 THR N N 15 108.935 . . 1 . . . A 62 THR N . 18556 1 119 . 1 1 63 63 ILE H H 1 8.702 . . 1 . . . A 63 ILE H . 18556 1 120 . 1 1 63 63 ILE N N 15 124.173 . . 1 . . . A 63 ILE N . 18556 1 121 . 1 1 64 64 ASP H H 1 9.023 . . 1 . . . A 64 ASP H . 18556 1 122 . 1 1 64 64 ASP N N 15 129.411 . . 1 . . . A 64 ASP N . 18556 1 123 . 1 1 65 65 PHE H H 1 8.854 . . 1 . . . A 65 PHE H . 18556 1 124 . 1 1 65 65 PHE N N 15 118.894 . . 1 . . . A 65 PHE N . 18556 1 125 . 1 1 67 67 GLU H H 1 8.328 . . 1 . . . A 67 GLU H . 18556 1 126 . 1 1 67 67 GLU N N 15 118.803 . . 1 . . . A 67 GLU N . 18556 1 127 . 1 1 68 68 PHE H H 1 8.561 . . 1 . . . A 68 PHE H . 18556 1 128 . 1 1 68 68 PHE N N 15 125.025 . . 1 . . . A 68 PHE N . 18556 1 129 . 1 1 69 69 LEU H H 1 8.675 . . 1 . . . A 69 LEU H . 18556 1 130 . 1 1 69 69 LEU N N 15 120.532 . . 1 . . . A 69 LEU N . 18556 1 131 . 1 1 70 70 THR H H 1 7.889 . . 1 . . . A 70 THR H . 18556 1 132 . 1 1 70 70 THR N N 15 116.007 . . 1 . . . A 70 THR N . 18556 1 133 . 1 1 71 71 MET H H 1 7.395 . . 1 . . . A 71 MET H . 18556 1 134 . 1 1 71 71 MET N N 15 121.214 . . 1 . . . A 71 MET N . 18556 1 135 . 1 1 72 72 MET H H 1 7.435 . . 1 . . . A 72 MET H . 18556 1 136 . 1 1 72 72 MET N N 15 115.320 . . 1 . . . A 72 MET N . 18556 1 137 . 1 1 73 73 ALA H H 1 7.816 . . 1 . . . A 73 ALA H . 18556 1 138 . 1 1 73 73 ALA N N 15 122.137 . . 1 . . . A 73 ALA N . 18556 1 139 . 1 1 74 74 ARG H H 1 6.984 . . 1 . . . A 74 ARG H . 18556 1 140 . 1 1 74 74 ARG N N 15 119.503 . . 1 . . . A 74 ARG N . 18556 1 141 . 1 1 75 75 LYS H H 1 8.492 . . 1 . . . A 75 LYS H . 18556 1 142 . 1 1 75 75 LYS N N 15 125.011 . . 1 . . . A 75 LYS N . 18556 1 143 . 1 1 76 76 MET H H 1 8.622 . . 1 . . . A 76 MET H . 18556 1 144 . 1 1 76 76 MET N N 15 124.810 . . 1 . . . A 76 MET N . 18556 1 145 . 1 1 77 77 LYS H H 1 8.651 . . 1 . . . A 77 LYS H . 18556 1 146 . 1 1 77 77 LYS N N 15 123.044 . . 1 . . . A 77 LYS N . 18556 1 147 . 1 1 78 78 ASP H H 1 8.583 . . 1 . . . A 78 ASP H . 18556 1 148 . 1 1 78 78 ASP N N 15 121.067 . . 1 . . . A 78 ASP N . 18556 1 149 . 1 1 79 79 THR H H 1 7.708 . . 1 . . . A 79 THR H . 18556 1 150 . 1 1 79 79 THR N N 15 113.719 . . 1 . . . A 79 THR N . 18556 1 151 . 1 1 80 80 ASP H H 1 8.135 . . 1 . . . A 80 ASP H . 18556 1 152 . 1 1 80 80 ASP N N 15 124.596 . . 1 . . . A 80 ASP N . 18556 1 153 . 1 1 81 81 SER H H 1 8.500 . . 1 . . . A 81 SER H . 18556 1 154 . 1 1 81 81 SER N N 15 117.936 . . 1 . . . A 81 SER N . 18556 1 155 . 1 1 82 82 GLU H H 1 8.290 . . 1 . . . A 82 GLU H . 18556 1 156 . 1 1 82 82 GLU N N 15 122.349 . . 1 . . . A 82 GLU N . 18556 1 157 . 1 1 83 83 GLU H H 1 7.924 . . 1 . . . A 83 GLU H . 18556 1 158 . 1 1 83 83 GLU N N 15 120.441 . . 1 . . . A 83 GLU N . 18556 1 159 . 1 1 84 84 GLU H H 1 8.045 . . 1 . . . A 84 GLU H . 18556 1 160 . 1 1 84 84 GLU N N 15 118.776 . . 1 . . . A 84 GLU N . 18556 1 161 . 1 1 85 85 ILE H H 1 8.112 . . 1 . . . A 85 ILE H . 18556 1 162 . 1 1 85 85 ILE N N 15 122.610 . . 1 . . . A 85 ILE N . 18556 1 163 . 1 1 86 86 ARG H H 1 8.366 . . 1 . . . A 86 ARG H . 18556 1 164 . 1 1 86 86 ARG N N 15 123.293 . . 1 . . . A 86 ARG N . 18556 1 165 . 1 1 87 87 GLU H H 1 8.587 . . 1 . . . A 87 GLU H . 18556 1 166 . 1 1 87 87 GLU N N 15 118.855 . . 1 . . . A 87 GLU N . 18556 1 167 . 1 1 88 88 ALA H H 1 8.017 . . 1 . . . A 88 ALA H . 18556 1 168 . 1 1 88 88 ALA N N 15 122.022 . . 1 . . . A 88 ALA N . 18556 1 169 . 1 1 89 89 PHE H H 1 8.902 . . 1 . . . A 89 PHE H . 18556 1 170 . 1 1 89 89 PHE N N 15 120.927 . . 1 . . . A 89 PHE N . 18556 1 171 . 1 1 90 90 ARG H H 1 7.937 . . 1 . . . A 90 ARG H . 18556 1 172 . 1 1 90 90 ARG N N 15 115.931 . . 1 . . . A 90 ARG N . 18556 1 173 . 1 1 91 91 VAL H H 1 7.236 . . 1 . . . A 91 VAL H . 18556 1 174 . 1 1 91 91 VAL N N 15 118.340 . . 1 . . . A 91 VAL N . 18556 1 175 . 1 1 92 92 PHE H H 1 7.051 . . 1 . . . A 92 PHE H . 18556 1 176 . 1 1 92 92 PHE N N 15 115.491 . . 1 . . . A 92 PHE N . 18556 1 177 . 1 1 93 93 ASP H H 1 7.970 . . 1 . . . A 93 ASP H . 18556 1 178 . 1 1 93 93 ASP N N 15 116.797 . . 1 . . . A 93 ASP N . 18556 1 179 . 1 1 94 94 LYS H H 1 7.384 . . 1 . . . A 94 LYS H . 18556 1 180 . 1 1 94 94 LYS N N 15 125.790 . . 1 . . . A 94 LYS N . 18556 1 181 . 1 1 95 95 ASP H H 1 8.262 . . 1 . . . A 95 ASP H . 18556 1 182 . 1 1 95 95 ASP N N 15 114.644 . . 1 . . . A 95 ASP N . 18556 1 183 . 1 1 96 96 GLY H H 1 7.812 . . 1 . . . A 96 GLY H . 18556 1 184 . 1 1 96 96 GLY N N 15 110.192 . . 1 . . . A 96 GLY N . 18556 1 185 . 1 1 97 97 ASN H H 1 8.343 . . 1 . . . A 97 ASN H . 18556 1 186 . 1 1 97 97 ASN N N 15 120.536 . . 1 . . . A 97 ASN N . 18556 1 187 . 1 1 98 98 GLY H H 1 10.642 . . 1 . . . A 98 GLY H . 18556 1 188 . 1 1 98 98 GLY N N 15 113.490 . . 1 . . . A 98 GLY N . 18556 1 189 . 1 1 99 99 PHE H H 1 7.634 . . 1 . . . A 99 PHE H . 18556 1 190 . 1 1 99 99 PHE N N 15 117.067 . . 1 . . . A 99 PHE N . 18556 1 191 . 1 1 100 100 ILE H H 1 10.178 . . 1 . . . A 100 ILE H . 18556 1 192 . 1 1 100 100 ILE N N 15 127.928 . . 1 . . . A 100 ILE N . 18556 1 193 . 1 1 101 101 SER H H 1 8.909 . . 1 . . . A 101 SER H . 18556 1 194 . 1 1 101 101 SER N N 15 124.410 . . 1 . . . A 101 SER N . 18556 1 195 . 1 1 102 102 ALA H H 1 9.250 . . 1 . . . A 102 ALA H . 18556 1 196 . 1 1 102 102 ALA N N 15 123.613 . . 1 . . . A 102 ALA N . 18556 1 197 . 1 1 103 103 ALA H H 1 8.248 . . 1 . . . A 103 ALA H . 18556 1 198 . 1 1 103 103 ALA N N 15 118.961 . . 1 . . . A 103 ALA N . 18556 1 199 . 1 1 104 104 GLU H H 1 7.909 . . 1 . . . A 104 GLU H . 18556 1 200 . 1 1 104 104 GLU N N 15 121.176 . . 1 . . . A 104 GLU N . 18556 1 201 . 1 1 105 105 LEU H H 1 8.528 . . 1 . . . A 105 LEU H . 18556 1 202 . 1 1 105 105 LEU N N 15 122.109 . . 1 . . . A 105 LEU N . 18556 1 203 . 1 1 106 106 ARG H H 1 8.668 . . 1 . . . A 106 ARG H . 18556 1 204 . 1 1 106 106 ARG N N 15 118.097 . . 1 . . . A 106 ARG N . 18556 1 205 . 1 1 107 107 HIS H H 1 8.052 . . 1 . . . A 107 HIS H . 18556 1 206 . 1 1 107 107 HIS N N 15 120.650 . . 1 . . . A 107 HIS N . 18556 1 207 . 1 1 108 108 VAL H H 1 7.857 . . 1 . . . A 108 VAL H . 18556 1 208 . 1 1 108 108 VAL N N 15 119.062 . . 1 . . . A 108 VAL N . 18556 1 209 . 1 1 109 109 MET H H 1 8.031 . . 1 . . . A 109 MET H . 18556 1 210 . 1 1 109 109 MET N N 15 116.585 . . 1 . . . A 109 MET N . 18556 1 211 . 1 1 110 110 THR H H 1 8.427 . . 1 . . . A 110 THR H . 18556 1 212 . 1 1 110 110 THR N N 15 115.483 . . 1 . . . A 110 THR N . 18556 1 213 . 1 1 111 111 ASN H H 1 7.929 . . 1 . . . A 111 ASN H . 18556 1 214 . 1 1 111 111 ASN N N 15 124.320 . . 1 . . . A 111 ASN N . 18556 1 215 . 1 1 112 112 LEU H H 1 7.675 . . 1 . . . A 112 LEU H . 18556 1 216 . 1 1 112 112 LEU N N 15 119.170 . . 1 . . . A 112 LEU N . 18556 1 217 . 1 1 113 113 GLY H H 1 7.498 . . 1 . . . A 113 GLY H . 18556 1 218 . 1 1 113 113 GLY N N 15 104.913 . . 1 . . . A 113 GLY N . 18556 1 219 . 1 1 114 114 GLU H H 1 8.044 . . 1 . . . A 114 GLU H . 18556 1 220 . 1 1 114 114 GLU N N 15 121.948 . . 1 . . . A 114 GLU N . 18556 1 221 . 1 1 115 115 LYS H H 1 8.437 . . 1 . . . A 115 LYS H . 18556 1 222 . 1 1 115 115 LYS N N 15 125.351 . . 1 . . . A 115 LYS N . 18556 1 223 . 1 1 116 116 LEU H H 1 8.099 . . 1 . . . A 116 LEU H . 18556 1 224 . 1 1 116 116 LEU N N 15 126.107 . . 1 . . . A 116 LEU N . 18556 1 225 . 1 1 117 117 THR H H 1 8.737 . . 1 . . . A 117 THR H . 18556 1 226 . 1 1 117 117 THR N N 15 113.725 . . 1 . . . A 117 THR N . 18556 1 227 . 1 1 118 118 ASP H H 1 8.844 . . 1 . . . A 118 ASP H . 18556 1 228 . 1 1 118 118 ASP N N 15 121.675 . . 1 . . . A 118 ASP N . 18556 1 229 . 1 1 119 119 GLU H H 1 8.638 . . 1 . . . A 119 GLU H . 18556 1 230 . 1 1 119 119 GLU N N 15 120.054 . . 1 . . . A 119 GLU N . 18556 1 231 . 1 1 120 120 GLU H H 1 7.631 . . 1 . . . A 120 GLU H . 18556 1 232 . 1 1 120 120 GLU N N 15 120.904 . . 1 . . . A 120 GLU N . 18556 1 233 . 1 1 121 121 VAL H H 1 7.821 . . 1 . . . A 121 VAL H . 18556 1 234 . 1 1 121 121 VAL N N 15 121.716 . . 1 . . . A 121 VAL N . 18556 1 235 . 1 1 122 122 ASP H H 1 7.995 . . 1 . . . A 122 ASP H . 18556 1 236 . 1 1 122 122 ASP N N 15 120.410 . . 1 . . . A 122 ASP N . 18556 1 237 . 1 1 123 123 GLU H H 1 8.050 . . 1 . . . A 123 GLU H . 18556 1 238 . 1 1 123 123 GLU N N 15 119.960 . . 1 . . . A 123 GLU N . 18556 1 239 . 1 1 124 124 MET H H 1 7.611 . . 1 . . . A 124 MET H . 18556 1 240 . 1 1 124 124 MET N N 15 120.154 . . 1 . . . A 124 MET N . 18556 1 241 . 1 1 125 125 ILE H H 1 8.108 . . 1 . . . A 125 ILE H . 18556 1 242 . 1 1 125 125 ILE N N 15 121.465 . . 1 . . . A 125 ILE N . 18556 1 243 . 1 1 126 126 ARG H H 1 8.385 . . 1 . . . A 126 ARG H . 18556 1 244 . 1 1 126 126 ARG N N 15 118.324 . . 1 . . . A 126 ARG N . 18556 1 245 . 1 1 127 127 GLU H H 1 7.969 . . 1 . . . A 127 GLU H . 18556 1 246 . 1 1 127 127 GLU N N 15 117.616 . . 1 . . . A 127 GLU N . 18556 1 247 . 1 1 128 128 ALA H H 1 7.112 . . 1 . . . A 128 ALA H . 18556 1 248 . 1 1 128 128 ALA N N 15 117.785 . . 1 . . . A 128 ALA N . 18556 1 249 . 1 1 129 129 ASP H H 1 7.924 . . 1 . . . A 129 ASP H . 18556 1 250 . 1 1 129 129 ASP N N 15 118.689 . . 1 . . . A 129 ASP N . 18556 1 251 . 1 1 130 130 ILE H H 1 8.171 . . 1 . . . A 130 ILE H . 18556 1 252 . 1 1 130 130 ILE N N 15 128.653 . . 1 . . . A 130 ILE N . 18556 1 253 . 1 1 131 131 ASP H H 1 8.315 . . 1 . . . A 131 ASP H . 18556 1 254 . 1 1 131 131 ASP N N 15 117.198 . . 1 . . . A 131 ASP N . 18556 1 255 . 1 1 132 132 GLY H H 1 7.572 . . 1 . . . A 132 GLY H . 18556 1 256 . 1 1 132 132 GLY N N 15 109.424 . . 1 . . . A 132 GLY N . 18556 1 257 . 1 1 133 133 ASP H H 1 8.327 . . 1 . . . A 133 ASP H . 18556 1 258 . 1 1 133 133 ASP N N 15 121.692 . . 1 . . . A 133 ASP N . 18556 1 259 . 1 1 134 134 GLY H H 1 10.239 . . 1 . . . A 134 GLY H . 18556 1 260 . 1 1 134 134 GLY N N 15 113.412 . . 1 . . . A 134 GLY N . 18556 1 261 . 1 1 135 135 GLN H H 1 7.914 . . 1 . . . A 135 GLN H . 18556 1 262 . 1 1 135 135 GLN N N 15 115.680 . . 1 . . . A 135 GLN N . 18556 1 263 . 1 1 136 136 VAL H H 1 9.104 . . 1 . . . A 136 VAL H . 18556 1 264 . 1 1 136 136 VAL N N 15 126.116 . . 1 . . . A 136 VAL N . 18556 1 265 . 1 1 137 137 ASN H H 1 9.520 . . 1 . . . A 137 ASN H . 18556 1 266 . 1 1 137 137 ASN N N 15 129.845 . . 1 . . . A 137 ASN N . 18556 1 267 . 1 1 138 138 TYR H H 1 8.239 . . 1 . . . A 138 TYR H . 18556 1 268 . 1 1 138 138 TYR N N 15 119.110 . . 1 . . . A 138 TYR N . 18556 1 269 . 1 1 139 139 GLU H H 1 8.002 . . 1 . . . A 139 GLU H . 18556 1 270 . 1 1 139 139 GLU N N 15 119.239 . . 1 . . . A 139 GLU N . 18556 1 271 . 1 1 140 140 GLU H H 1 8.661 . . 1 . . . A 140 GLU H . 18556 1 272 . 1 1 140 140 GLU N N 15 120.537 . . 1 . . . A 140 GLU N . 18556 1 273 . 1 1 141 141 PHE H H 1 8.390 . . 1 . . . A 141 PHE H . 18556 1 274 . 1 1 141 141 PHE N N 15 124.460 . . 1 . . . A 141 PHE N . 18556 1 275 . 1 1 142 142 VAL H H 1 8.631 . . 1 . . . A 142 VAL H . 18556 1 276 . 1 1 142 142 VAL N N 15 119.726 . . 1 . . . A 142 VAL N . 18556 1 277 . 1 1 143 143 THR H H 1 7.741 . . 1 . . . A 143 THR H . 18556 1 278 . 1 1 143 143 THR N N 15 120.005 . . 1 . . . A 143 THR N . 18556 1 279 . 1 1 144 144 MET H H 1 7.251 . . 1 . . . A 144 MET H . 18556 1 280 . 1 1 144 144 MET N N 15 117.270 . . 1 . . . A 144 MET N . 18556 1 281 . 1 1 145 145 MET H H 1 7.345 . . 1 . . . A 145 MET H . 18556 1 282 . 1 1 145 145 MET N N 15 113.128 . . 1 . . . A 145 MET N . 18556 1 283 . 1 1 146 146 THR H H 1 7.425 . . 1 . . . A 146 THR H . 18556 1 284 . 1 1 146 146 THR N N 15 109.194 . . 1 . . . A 146 THR N . 18556 1 285 . 1 1 147 147 ALA H H 1 7.454 . . 1 . . . A 147 ALA H . 18556 1 286 . 1 1 147 147 ALA N N 15 127.217 . . 1 . . . A 147 ALA N . 18556 1 287 . 1 1 148 148 LYS H H 1 7.980 . . 1 . . . A 148 LYS H . 18556 1 288 . 1 1 148 148 LYS N N 15 127.522 . . 1 . . . A 148 LYS N . 18556 1 stop_ save_