data_25569 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 25569 _Entry.Title ; PIN1 WW domain in complex with a phosphorylated CPEB1 derived peptide ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2015-04-13 _Entry.Accession_date 2015-04-13 _Entry.Last_release_date 2015-10-26 _Entry.Original_release_date 2015-10-26 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.81 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype SOLUTION _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Constanze Schelhorn . . . 25569 2 'Maria J.' Macias . . . 25569 3 Pau Martin-Malpartida . . . 25569 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' . 25569 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID CPEB1 . 25569 PIN1 . 25569 Phosphorylation . 25569 WW . 25569 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 25569 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 235 25569 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2015-10-26 . original BMRB . 25569 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2N1O 'BMRB Entry Tracking System' 25569 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 25569 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 26456073 _Citation.Full_citation . _Citation.Title ; Structural Analysis of the Pin1-CPEB1 interaction and its potential role in CPEB1 degradation ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Sci. Rep.' _Citation.Journal_name_full . _Citation.Journal_volume 5 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 14990 _Citation.Page_last 14990 _Citation.Year 2015 _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 Constanze Schelhorn . . . 25569 1 2 Pau Martin-Malpartida . . . 25569 1 3 David Sunol . . . 25569 1 4 'Maria J.' Macias . . . 25569 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 25569 _Assembly.ID 1 _Assembly.Name 'PIN1 WW domain in complex with a phosphorylated CPEB1 derived peptide' _Assembly.BMRB_code . _Assembly.Number_of_components 2 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds no _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _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 Pin1 1 $Pin1 A . yes native no no . . . 25569 1 2 CPEB1 2 $CPEB1 B . yes native no no . . . 25569 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Pin1 _Entity.Sf_category entity _Entity.Sf_framecode Pin1 _Entity.Entry_ID 25569 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Pin1 _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 ; LPPGWEKRMSRSSGRVYYFN HITNASQWERPSG ; _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 33 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 3901.367 _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 yes UNP Q13526 . PIN1 . . . . . . . . . . . . . . 25569 1 2 no BMRB 16070 . Pin1_WW . . . . . 100.00 36 100.00 100.00 6.01e-15 . . . . 25569 1 3 no BMRB 16088 . Pin1_WW . . . . . 100.00 36 100.00 100.00 6.01e-15 . . . . 25569 1 4 no BMRB 17545 . "first domain of human PIN1" . . . . . 100.00 36 100.00 100.00 5.94e-15 . . . . 25569 1 5 no BMRB 19258 . entity . . . . . 100.00 43 100.00 100.00 3.62e-15 . . . . 25569 1 6 no BMRB 19259 . Pin1 . . . . . 100.00 43 96.97 96.97 1.22e-14 . . . . 25569 1 7 no PDB 1F8A . "Structural Basis For The Phosphoserine-proline Recognition By Group Iv Ww Domains" . . . . . 100.00 167 100.00 100.00 5.36e-15 . . . . 25569 1 8 no PDB 1I6C . "Solution Structure Of Pin1 Ww Domain" . . . . . 100.00 39 100.00 100.00 5.00e-15 . . . . 25569 1 9 no PDB 1I8G . "Solution Structure Of Pin1 Ww Domain Complexed With Cdc25 Phosphothreonine Peptide" . . . . . 100.00 39 100.00 100.00 5.00e-15 . . . . 25569 1 10 no PDB 1I8H . "Solution Structure Of Pin1 Ww Domain Complexed With Human Tau Phosphothreonine Peptide" . . . . . 100.00 39 100.00 100.00 5.00e-15 . . . . 25569 1 11 no PDB 1NMV . "Solution Structure Of Human Pin1" . . . . . 100.00 163 100.00 100.00 5.07e-15 . . . . 25569 1 12 no PDB 1PIN . "Pin1 Peptidyl-prolyl Cis-trans Isomerase From Homo Sapiens" . . . . . 100.00 163 100.00 100.00 5.07e-15 . . . . 25569 1 13 no PDB 2ITK . "Human Pin1 Bound To D-Peptide" . . . . . 100.00 167 96.97 96.97 4.48e-14 . . . . 25569 1 14 no PDB 2KCF . "The Nmr Solution Structure Of The Isolated Apo Pin1 Ww Domain" . . . . . 100.00 36 100.00 100.00 6.01e-15 . . . . 25569 1 15 no PDB 2LB3 . "Structure Of The Ww Domain Of Pin1 In Complex With A Human Phosphorylated Smad3 Derived Peptide" . . . . . 100.00 36 100.00 100.00 5.94e-15 . . . . 25569 1 16 no PDB 2M8I . "Structure Of Pin1 Ww Domain" . . . . . 100.00 43 100.00 100.00 3.62e-15 . . . . 25569 1 17 no PDB 2M8J . "Structure Of Pin1 Ww Domain Phospho-mimic S16e" . . . . . 100.00 43 96.97 96.97 1.22e-14 . . . . 25569 1 18 no PDB 2Q5A . "Human Pin1 Bound To L-Peptide" . . . . . 100.00 167 96.97 96.97 4.48e-14 . . . . 25569 1 19 no PDB 2XP3 . "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" . . . . . 100.00 167 96.97 96.97 4.48e-14 . . . . 25569 1 20 no PDB 2XP4 . "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" . . . . . 100.00 167 96.97 96.97 4.48e-14 . . . . 25569 1 21 no PDB 2XP5 . "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" . . . . . 100.00 167 96.97 96.97 4.48e-14 . . . . 25569 1 22 no PDB 2XP6 . "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" . . . . . 100.00 167 96.97 96.97 4.21e-14 . . . . 25569 1 23 no PDB 2XP7 . "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" . . . . . 100.00 167 96.97 96.97 4.48e-14 . . . . 25569 1 24 no PDB 2XP8 . "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" . . . . . 100.00 167 96.97 96.97 4.48e-14 . . . . 25569 1 25 no PDB 2XP9 . "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" . . . . . 100.00 167 96.97 96.97 4.48e-14 . . . . 25569 1 26 no PDB 2XPA . "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" . . . . . 100.00 167 96.97 96.97 4.48e-14 . . . . 25569 1 27 no PDB 2XPB . "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" . . . . . 100.00 167 96.97 96.97 4.48e-14 . . . . 25569 1 28 no PDB 2ZQS . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 100.00 100.00 4.43e-15 . . . . 25569 1 29 no PDB 2ZQT . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 100.00 100.00 4.97e-15 . . . . 25569 1 30 no PDB 2ZQU . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 96.97 96.97 1.03e-13 . . . . 25569 1 31 no PDB 2ZQV . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 96.97 96.97 7.43e-14 . . . . 25569 1 32 no PDB 2ZR4 . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 96.97 100.00 1.10e-14 . . . . 25569 1 33 no PDB 2ZR5 . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 100.00 100.00 5.07e-15 . . . . 25569 1 34 no PDB 2ZR6 . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 96.97 96.97 4.22e-14 . . . . 25569 1 35 no PDB 3KAB . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 96.97 96.97 4.48e-14 . . . . 25569 1 36 no PDB 3KAD . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 96.97 96.97 4.21e-14 . . . . 25569 1 37 no PDB 3KAF . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 96.97 96.97 4.21e-14 . . . . 25569 1 38 no PDB 3KAG . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 96.97 96.97 4.48e-14 . . . . 25569 1 39 no PDB 3KAH . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 96.97 96.97 4.48e-14 . . . . 25569 1 40 no PDB 3KAI . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 96.97 96.97 4.48e-14 . . . . 25569 1 41 no PDB 3KCE . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 96.97 96.97 4.48e-14 . . . . 25569 1 42 no PDB 3NTP . "Human Pin1 Complexed With Reduced Amide Inhibitor" . . . . . 100.00 167 96.97 96.97 4.48e-14 . . . . 25569 1 43 no PDB 3ODK . "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" . . . . . 100.00 167 96.97 96.97 4.48e-14 . . . . 25569 1 44 no PDB 3OOB . "Structural And Functional Insights Of Directly Targeting Pin1 By Epigallocatechin-3-Gallate" . . . . . 100.00 163 96.97 96.97 4.22e-14 . . . . 25569 1 45 no PDB 3TC5 . "Selective Targeting Of Disease-Relevant Protein Binding Domains By O- Phosphorylated Natural Product Derivatives" . . . . . 100.00 166 96.97 96.97 4.25e-14 . . . . 25569 1 46 no PDB 3TCZ . "Human Pin1 Bound To Cis Peptidomimetic Inhibitor" . . . . . 100.00 158 96.97 96.97 4.38e-14 . . . . 25569 1 47 no PDB 3TDB . "Human Pin1 Bound To Trans Peptidomimetic Inhibitor" . . . . . 100.00 158 96.97 96.97 4.38e-14 . . . . 25569 1 48 no PDB 3WH0 . "Structure Of Pin1 Complex With 18-crown-6" . . . . . 100.00 163 96.97 96.97 4.22e-14 . . . . 25569 1 49 no PDB 4GWT . "Structure Of Racemic Pin1 Ww Domain Cocrystallized With Dl-malic Acid" . . . . . 100.00 36 100.00 100.00 6.01e-15 . . . . 25569 1 50 no PDB 4GWV . "Structure Of Racemic Pin1 Ww Domain Cocrystallized With Tri-ammonium Citrate" . . . . . 100.00 36 100.00 100.00 6.01e-15 . . . . 25569 1 51 no PDB 4QIB . "Oxidation-mediated Inhibition Of The Peptidyl-prolyl Isomerase Pin1" . . . . . 100.00 159 96.97 96.97 4.53e-14 . . . . 25569 1 52 no PDB 4U84 . "Human Pin1 With S-hydroxyl-cysteine 113" . . . . . 100.00 181 96.97 96.97 6.41e-14 . . . . 25569 1 53 no PDB 4U85 . "Human Pin1 With Cysteine Sulfinic Acid 113" . . . . . 100.00 181 96.97 96.97 6.41e-14 . . . . 25569 1 54 no PDB 4U86 . "Human Pin1 With Cysteine Sulfonic Acid 113" . . . . . 100.00 181 96.97 96.97 6.41e-14 . . . . 25569 1 55 no DBJ BAA87037 . "PIN1 [Mus sp.]" . . . . . 100.00 165 100.00 100.00 5.44e-15 . . . . 25569 1 56 no DBJ BAA87038 . "PIN1 [Mus sp.]" . . . . . 100.00 165 100.00 100.00 5.44e-15 . . . . 25569 1 57 no DBJ BAB22270 . "unnamed protein product [Mus musculus]" . . . . . 100.00 165 100.00 100.00 5.44e-15 . . . . 25569 1 58 no DBJ BAB22743 . "unnamed protein product [Mus musculus]" . . . . . 100.00 165 100.00 100.00 5.44e-15 . . . . 25569 1 59 no DBJ BAC35631 . "unnamed protein product [Mus musculus]" . . . . . 100.00 165 100.00 100.00 5.44e-15 . . . . 25569 1 60 no EMBL CAG28582 . "UBL5 [Homo sapiens]" . . . . . 100.00 163 100.00 100.00 5.07e-15 . . . . 25569 1 61 no GB AAC50492 . "Pin1 [Homo sapiens]" . . . . . 100.00 163 100.00 100.00 5.07e-15 . . . . 25569 1 62 no GB AAH02899 . "Peptidylprolyl cis/trans isomerase, NIMA-interacting 1 [Homo sapiens]" . . . . . 100.00 163 100.00 100.00 5.07e-15 . . . . 25569 1 63 no GB AAH38254 . "Protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1 [Mus musculus]" . . . . . 100.00 165 100.00 100.00 5.44e-15 . . . . 25569 1 64 no GB AAH59553 . "Protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1 [Danio rerio]" . . . . . 100.00 159 96.97 96.97 4.00e-14 . . . . 25569 1 65 no GB AAI12584 . "Peptidylprolyl cis/trans isomerase, NIMA-interacting 1 [Bos taurus]" . . . . . 100.00 163 100.00 100.00 4.97e-15 . . . . 25569 1 66 no PRF 2209428A . "peptidyl-Pro isomerase" . . . . . 100.00 163 100.00 100.00 5.07e-15 . . . . 25569 1 67 no REF NP_001029804 . "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Bos taurus]" . . . . . 100.00 163 100.00 100.00 4.97e-15 . . . . 25569 1 68 no REF NP_001100171 . "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Rattus norvegicus]" . . . . . 100.00 165 96.97 96.97 5.43e-14 . . . . 25569 1 69 no REF NP_001231300 . "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Sus scrofa]" . . . . . 100.00 163 100.00 100.00 5.34e-15 . . . . 25569 1 70 no REF NP_001270625 . "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Macaca fascicularis]" . . . . . 100.00 163 96.97 96.97 3.93e-14 . . . . 25569 1 71 no REF NP_006212 . "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Homo sapiens]" . . . . . 100.00 163 100.00 100.00 5.07e-15 . . . . 25569 1 72 no SP Q13526 . "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" . . . . . 100.00 163 100.00 100.00 5.07e-15 . . . . 25569 1 73 no SP Q4R383 . "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" . . . . . 100.00 163 96.97 96.97 3.93e-14 . . . . 25569 1 74 no SP Q5BIN5 . "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" . . . . . 100.00 163 100.00 100.00 4.97e-15 . . . . 25569 1 75 no SP Q9QUR7 . "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" . . . . . 100.00 165 100.00 100.00 5.44e-15 . . . . 25569 1 76 no TPG DAA28013 . "TPA: peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Bos taurus]" . . . . . 100.00 163 100.00 100.00 4.97e-15 . . . . 25569 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 7 LEU . 25569 1 2 8 PRO . 25569 1 3 9 PRO . 25569 1 4 10 GLY . 25569 1 5 11 TRP . 25569 1 6 12 GLU . 25569 1 7 13 LYS . 25569 1 8 14 ARG . 25569 1 9 15 MET . 25569 1 10 16 SER . 25569 1 11 17 ARG . 25569 1 12 18 SER . 25569 1 13 19 SER . 25569 1 14 20 GLY . 25569 1 15 21 ARG . 25569 1 16 22 VAL . 25569 1 17 23 TYR . 25569 1 18 24 TYR . 25569 1 19 25 PHE . 25569 1 20 26 ASN . 25569 1 21 27 HIS . 25569 1 22 28 ILE . 25569 1 23 29 THR . 25569 1 24 30 ASN . 25569 1 25 31 ALA . 25569 1 26 32 SER . 25569 1 27 33 GLN . 25569 1 28 34 TRP . 25569 1 29 35 GLU . 25569 1 30 36 ARG . 25569 1 31 37 PRO . 25569 1 32 38 SER . 25569 1 33 39 GLY . 25569 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 . LEU 1 1 25569 1 . PRO 2 2 25569 1 . PRO 3 3 25569 1 . GLY 4 4 25569 1 . TRP 5 5 25569 1 . GLU 6 6 25569 1 . LYS 7 7 25569 1 . ARG 8 8 25569 1 . MET 9 9 25569 1 . SER 10 10 25569 1 . ARG 11 11 25569 1 . SER 12 12 25569 1 . SER 13 13 25569 1 . GLY 14 14 25569 1 . ARG 15 15 25569 1 . VAL 16 16 25569 1 . TYR 17 17 25569 1 . TYR 18 18 25569 1 . PHE 19 19 25569 1 . ASN 20 20 25569 1 . HIS 21 21 25569 1 . ILE 22 22 25569 1 . THR 23 23 25569 1 . ASN 24 24 25569 1 . ALA 25 25 25569 1 . SER 26 26 25569 1 . GLN 27 27 25569 1 . TRP 28 28 25569 1 . GLU 29 29 25569 1 . ARG 30 30 25569 1 . PRO 31 31 25569 1 . SER 32 32 25569 1 . GLY 33 33 25569 1 stop_ save_ save_CPEB1 _Entity.Sf_category entity _Entity.Sf_framecode CPEB1 _Entity.Entry_ID 25569 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name CPEB1 _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 ; RIXPPLPF ; _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 yes _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 8 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 1007.111 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . 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 . yes UNP Q91572 . CPEB1 . . . . . . . . . . . . . . 25569 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 1 208 ARG . 25569 2 2 209 ILE . 25569 2 3 210 SEP . 25569 2 4 211 PRO . 25569 2 5 212 PRO . 25569 2 6 213 LEU . 25569 2 7 214 PRO . 25569 2 8 215 PHE . 25569 2 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . ARG 1 1 25569 2 . ILE 2 2 25569 2 . SEP 3 3 25569 2 . PRO 4 4 25569 2 . PRO 5 5 25569 2 . LEU 6 6 25569 2 . PRO 7 7 25569 2 . PHE 8 8 25569 2 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 25569 _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.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.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $Pin1 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . 25569 1 2 2 $CPEB1 . 8355 organism . 'Xenopus laevis' 'African clawed frog' . . Eukaryota Metazoa Xenopus laevis . . . . . . . . . . . . . 25569 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 25569 _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_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.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $Pin1 . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . pETM30 . . . 25569 1 2 2 $CPEB1 . 'chemical synthesis' . . . . . . . . . . . . . . . . 25569 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_SEP _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_SEP _Chem_comp.Entry_ID 25569 _Chem_comp.ID SEP _Chem_comp.Provenance PDB _Chem_comp.Name PHOSPHOSERINE _Chem_comp.Type 'L-PEPTIDE LINKING' _Chem_comp.BMRB_code SEP _Chem_comp.PDB_code SEP _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 S _Chem_comp.Three_letter_code SEP _Chem_comp.Number_atoms_all 19 _Chem_comp.Number_atoms_nh 11 _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code InChI=1S/C3H8NO6P/c4-2(3(5)6)1-10-11(7,8)9/h2H,1,4H2,(H,5,6)(H2,7,8,9)/t2-/m0/s1 _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 SER _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 PHOSPHONOSERINE _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula 'C3 H8 N O6 P' _Chem_comp.Formula_weight 185.072 _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 1BX6 _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 BZQFBWGGLXLEPQ-REOHCLBHSA-N InChIKey InChI 1.03 25569 SEP C(C(C(=O)O)N)OP(=O)(O)O SMILES 'OpenEye OEToolkits' 1.5.0 25569 SEP C([C@@H](C(=O)O)N)OP(=O)(O)O SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 25569 SEP InChI=1S/C3H8NO6P/c4-2(3(5)6)1-10-11(7,8)9/h2H,1,4H2,(H,5,6)(H2,7,8,9)/t2-/m0/s1 InChI InChI 1.03 25569 SEP N[C@@H](CO[P](O)(O)=O)C(O)=O SMILES_CANONICAL CACTVS 3.341 25569 SEP N[CH](CO[P](O)(O)=O)C(O)=O SMILES CACTVS 3.341 25569 SEP O=P(O)(O)OCC(C(=O)O)N SMILES ACDLabs 10.04 25569 SEP 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 '(2S)-2-amino-3-phosphonooxy-propanoic acid' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 25569 SEP O-phosphono-L-serine 'SYSTEMATIC NAME' ACDLabs 10.04 25569 SEP 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 N N N N . N . . N 0 . . . 1 no no . . . . 12.751 . 44.134 . -4.949 . 1.855 0.421 1.751 1 . 25569 SEP CA CA CA CA . C . . S 0 . . . 1 no no . . . . 12.373 . 44.600 . -6.265 . 0.401 0.620 1.687 2 . 25569 SEP CB CB CB CB . C . . N 0 . . . 1 no no . . . . 11.077 . 45.353 . -6.305 . -0.139 0.015 0.391 3 . 25569 SEP OG OG OG OG . O . . N 0 . . . 1 no no . . . . 10.895 . 45.809 . -7.608 . 0.477 0.655 -0.727 4 . 25569 SEP C C C C . C . . N 0 . . . 1 no no . . . . 13.435 . 45.364 . -6.941 . -0.249 -0.053 2.867 5 . 25569 SEP O O O O . O . . N 0 . . . 1 no no . . . . 14.373 . 45.871 . -6.303 . 0.254 -1.038 3.354 6 . 25569 SEP OXT OXT OXT OXT . O . . N 0 . . . 1 no yes . . . . 13.281 . 45.410 . -8.244 . -1.389 0.439 3.377 7 . 25569 SEP P P P P . P . . N 0 . . . 1 no no . . . . 9.607 . 45.328 . -8.384 . -0.135 -0.027 -2.050 8 . 25569 SEP O1P O1P O1P O1P . O . . N 0 . . . 1 no no . . . . 9.500 . 46.086 . -9.633 . -1.601 0.172 -2.074 9 . 25569 SEP O2P O2P O2P O2P . O . . N 0 . . . 1 no no . . . . 9.829 . 43.907 . -8.669 . 0.520 0.649 -3.356 10 . 25569 SEP O3P O3P O3P O3P . O . . N 0 . . . 1 no no . . . . 8.402 . 45.541 . -7.535 . 0.191 -1.603 -2.041 11 . 25569 SEP H H H H . H . . N 0 . . . 1 no no . . . . 13.632 . 43.621 . -4.921 . 2.237 0.796 0.895 12 . 25569 SEP H2 H2 H2 2HN . H . . N 0 . . . 1 no yes . . . . 12.001 . 43.575 . -4.540 . 2.013 -0.574 1.727 13 . 25569 SEP HA HA HA HA . H . . N 0 . . . 1 no no . . . . 12.213 . 43.656 . -6.837 . 0.179 1.687 1.711 14 . 25569 SEP HB2 HB2 HB2 1HB . H . . N 0 . . . 1 no no . . . . 10.214 . 44.753 . -5.930 . 0.082 -1.051 0.367 15 . 25569 SEP HB3 HB3 HB3 2HB . H . . N 0 . . . 1 no no . . . . 11.026 . 46.170 . -5.548 . -1.218 0.163 0.344 16 . 25569 SEP HXT HXT HXT HXT . H . . N 0 . . . 1 no yes . . . . 13.966 . 45.902 . -8.680 . -1.807 0.006 4.134 17 . 25569 SEP HOP2 HOP2 HOP2 2HOP . H . . N 0 . . . 0 no no . . . . 9.054 . 43.617 . -9.135 . 0.127 0.212 -4.124 18 . 25569 SEP HOP3 HOP3 HOP3 3HOP . H . . N 0 . . . 0 no no . . . . 7.627 . 45.251 . -8.001 . 1.154 -1.689 -2.025 19 . 25569 SEP stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING N CA no N 1 . 25569 SEP 2 . SING N H no N 2 . 25569 SEP 3 . SING N H2 no N 3 . 25569 SEP 4 . SING CA CB no N 4 . 25569 SEP 5 . SING CA C no N 5 . 25569 SEP 6 . SING CA HA no N 6 . 25569 SEP 7 . SING CB OG no N 7 . 25569 SEP 8 . SING CB HB2 no N 8 . 25569 SEP 9 . SING CB HB3 no N 9 . 25569 SEP 10 . SING OG P no N 10 . 25569 SEP 11 . DOUB C O no N 11 . 25569 SEP 12 . SING C OXT no N 12 . 25569 SEP 13 . SING OXT HXT no N 13 . 25569 SEP 14 . DOUB P O1P no N 14 . 25569 SEP 15 . SING P O2P no N 15 . 25569 SEP 16 . SING P O3P no N 16 . 25569 SEP 17 . SING O2P HOP2 no N 17 . 25569 SEP 18 . SING O3P HOP3 no N 18 . 25569 SEP stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 25569 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 Pin1 'natural abundance' . . 1 $Pin1 . . 1 . . mM . . . . 25569 1 2 CPEB1 'natural abundance' . . 2 $CPEB1 . . 3 . . mM . . . . 25569 1 3 D2O '[U-100% 2H]' . . . . . . 10 . . % . . . . 25569 1 4 TRIS '[U-100% 2H]' . . . . . . 20 . . mM . . . . 25569 1 5 'sodium chloride' 'natural abundance' . . . . . . 130 . . mM . . . . 25569 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 25569 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 7 . pH 25569 1 pressure 1 . atm 25569 1 temperature 285 . K 25569 1 stop_ save_ ############################ # Computer software used # ############################ save_CNSSOLVE _Software.Sf_category software _Software.Sf_framecode CNSSOLVE _Software.Entry_ID 25569 _Software.ID 1 _Software.Name CNSSOLVE _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Brunger, Adams, Clore, Gros, Nilges and Read' . . 25569 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 25569 1 stop_ save_ save_XEASY _Software.Sf_category software _Software.Sf_framecode XEASY _Software.Entry_ID 25569 _Software.ID 2 _Software.Name XEASY _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bartels et al.' . . 25569 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 25569 2 stop_ save_ save_TOPSPIN _Software.Sf_category software _Software.Sf_framecode TOPSPIN _Software.Entry_ID 25569 _Software.ID 3 _Software.Name TOPSPIN _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 25569 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 25569 3 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 25569 _Software.ID 4 _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' . . 25569 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 25569 4 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_Blanquito _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode Blanquito _NMR_spectrometer.Entry_ID 25569 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _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 25569 _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 Blanquito Bruker Avance . 600 . . . 25569 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 25569 _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-1H NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $Blanquito . . . . . . . . . . . . . . . . 25569 1 2 '2D 1H-1H TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $Blanquito . . . . . . . . . . . . . . . . 25569 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 25569 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 25569 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 25569 _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 0.01 _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-1H NOESY' . . . 25569 1 2 '2D 1H-1H TOCSY' . . . 25569 1 stop_ loop_ _Chem_shift_software.Software_ID _Chem_shift_software.Software_label _Chem_shift_software.Method_ID _Chem_shift_software.Method_label _Chem_shift_software.Entry_ID _Chem_shift_software.Assigned_chem_shift_list_ID 2 $XEASY . . 25569 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 LEU HA H 1 4.390 0.001 . 1 . . . A 7 LEU HA . 25569 1 2 . 1 1 1 1 LEU HB2 H 1 1.607 0.001 . 2 . . . A 7 LEU HB2 . 25569 1 3 . 1 1 1 1 LEU HB3 H 1 1.555 0.01 . 2 . . . A 7 LEU HB3 . 25569 1 4 . 1 1 1 1 LEU HG H 1 1.196 0.01 . 1 . . . A 7 LEU HG . 25569 1 5 . 1 1 1 1 LEU HD11 H 1 0.869 0.002 . 2 . . . A 7 LEU HD11 . 25569 1 6 . 1 1 1 1 LEU HD12 H 1 0.869 0.002 . 2 . . . A 7 LEU HD11 . 25569 1 7 . 1 1 1 1 LEU HD13 H 1 0.869 0.002 . 2 . . . A 7 LEU HD11 . 25569 1 8 . 1 1 1 1 LEU HD21 H 1 0.560 0.002 . 2 . . . A 7 LEU HD21 . 25569 1 9 . 1 1 1 1 LEU HD22 H 1 0.560 0.002 . 2 . . . A 7 LEU HD21 . 25569 1 10 . 1 1 1 1 LEU HD23 H 1 0.560 0.002 . 2 . . . A 7 LEU HD21 . 25569 1 11 . 1 1 2 2 PRO HA H 1 4.610 0.01 . 1 . . . A 8 PRO HA . 25569 1 12 . 1 1 2 2 PRO HB2 H 1 2.366 0.001 . 2 . . . A 8 PRO HB2 . 25569 1 13 . 1 1 2 2 PRO HB3 H 1 1.556 0.01 . 2 . . . A 8 PRO HB3 . 25569 1 14 . 1 1 2 2 PRO HG2 H 1 1.399 0.01 . 2 . . . A 8 PRO HG2 . 25569 1 15 . 1 1 2 2 PRO HD2 H 1 3.454 0.01 . 2 . . . A 8 PRO HD2 . 25569 1 16 . 1 1 2 2 PRO HD3 H 1 2.794 0.001 . 2 . . . A 8 PRO HD3 . 25569 1 17 . 1 1 3 3 PRO HA H 1 4.158 0.002 . 1 . . . A 9 PRO HA . 25569 1 18 . 1 1 3 3 PRO HB2 H 1 1.930 0.01 . 2 . . . A 9 PRO HB2 . 25569 1 19 . 1 1 3 3 PRO HB3 H 1 1.828 0.01 . 2 . . . A 9 PRO HB3 . 25569 1 20 . 1 1 3 3 PRO HG2 H 1 1.645 0.01 . 2 . . . A 9 PRO HG2 . 25569 1 21 . 1 1 3 3 PRO HD2 H 1 3.695 0.01 . 2 . . . A 9 PRO HD2 . 25569 1 22 . 1 1 3 3 PRO HD3 H 1 3.420 0.01 . 2 . . . A 9 PRO HD3 . 25569 1 23 . 1 1 4 4 GLY HA2 H 1 3.064 0.01 . 2 . . . A 10 GLY HA2 . 25569 1 24 . 1 1 4 4 GLY HA3 H 1 3.777 0.002 . 2 . . . A 10 GLY HA3 . 25569 1 25 . 1 1 5 5 TRP H H 1 7.151 0.01 . 1 . . . A 11 TRP H . 25569 1 26 . 1 1 5 5 TRP HA H 1 5.095 0.002 . 1 . . . A 11 TRP HA . 25569 1 27 . 1 1 5 5 TRP HB2 H 1 3.041 0.01 . 2 . . . A 11 TRP HB2 . 25569 1 28 . 1 1 5 5 TRP HB3 H 1 2.754 0.01 . 2 . . . A 11 TRP HB3 . 25569 1 29 . 1 1 5 5 TRP HD1 H 1 6.754 0.01 . 1 . . . A 11 TRP HD1 . 25569 1 30 . 1 1 5 5 TRP HE3 H 1 7.189 0.01 . 1 . . . A 11 TRP HE3 . 25569 1 31 . 1 1 5 5 TRP HZ2 H 1 7.213 0.001 . 1 . . . A 11 TRP HZ2 . 25569 1 32 . 1 1 5 5 TRP HZ3 H 1 6.689 0.001 . 1 . . . A 11 TRP HZ3 . 25569 1 33 . 1 1 5 5 TRP HH2 H 1 6.776 0.01 . 1 . . . A 11 TRP HH2 . 25569 1 34 . 1 1 6 6 GLU HA H 1 4.641 0.01 . 1 . . . A 12 GLU HA . 25569 1 35 . 1 1 6 6 GLU HB2 H 1 2.033 0.002 . 2 . . . A 12 GLU HB2 . 25569 1 36 . 1 1 6 6 GLU HB3 H 1 1.996 0.01 . 2 . . . A 12 GLU HB3 . 25569 1 37 . 1 1 6 6 GLU HG2 H 1 2.333 0.01 . 2 . . . A 12 GLU HG2 . 25569 1 38 . 1 1 6 6 GLU HG3 H 1 2.293 0.01 . 2 . . . A 12 GLU HG3 . 25569 1 39 . 1 1 7 7 LYS HA H 1 4.318 0.01 . 1 . . . A 13 LYS HA . 25569 1 40 . 1 1 7 7 LYS HB2 H 1 1.479 0.01 . 2 . . . A 13 LYS HB2 . 25569 1 41 . 1 1 7 7 LYS HB3 H 1 1.412 0.001 . 2 . . . A 13 LYS HB3 . 25569 1 42 . 1 1 7 7 LYS HG2 H 1 0.864 0.001 . 2 . . . A 13 LYS HG2 . 25569 1 43 . 1 1 7 7 LYS HD2 H 1 1.009 0.001 . 2 . . . A 13 LYS HD2 . 25569 1 44 . 1 1 7 7 LYS HE2 H 1 2.737 0.001 . 2 . . . A 13 LYS HE2 . 25569 1 45 . 1 1 8 8 ARG HA H 1 4.104 0.01 . 1 . . . A 14 ARG HA . 25569 1 46 . 1 1 8 8 ARG HB2 H 1 1.141 0.001 . 2 . . . A 14 ARG HB2 . 25569 1 47 . 1 1 8 8 ARG HB3 H 1 1.008 0.001 . 2 . . . A 14 ARG HB3 . 25569 1 48 . 1 1 8 8 ARG HG2 H 1 -0.154 0.01 . 2 . . . A 14 ARG HG2 . 25569 1 49 . 1 1 8 8 ARG HG3 H 1 -0.178 0.004 . 2 . . . A 14 ARG HG3 . 25569 1 50 . 1 1 8 8 ARG HD2 H 1 2.612 0.01 . 2 . . . A 14 ARG HD2 . 25569 1 51 . 1 1 8 8 ARG HD3 H 1 2.473 0.01 . 2 . . . A 14 ARG HD3 . 25569 1 52 . 1 1 8 8 ARG HE H 1 6.657 0.01 . 1 . . . A 14 ARG HE . 25569 1 53 . 1 1 8 8 ARG HH21 H 1 6.213 0.004 . 2 . . . A 14 ARG HH21 . 25569 1 54 . 1 1 9 9 MET HA H 1 4.674 0.01 . 1 . . . A 15 MET HA . 25569 1 55 . 1 1 9 9 MET HB2 H 1 1.518 0.162 . 2 . . . A 15 MET HB2 . 25569 1 56 . 1 1 9 9 MET HB3 H 1 0.986 0.01 . 2 . . . A 15 MET HB3 . 25569 1 57 . 1 1 9 9 MET HG2 H 1 2.224 0.01 . 2 . . . A 15 MET HG2 . 25569 1 58 . 1 1 9 9 MET HG3 H 1 1.749 0.01 . 2 . . . A 15 MET HG3 . 25569 1 59 . 1 1 10 10 SER HA H 1 4.856 0.002 . 1 . . . A 16 SER HA . 25569 1 60 . 1 1 10 10 SER HB2 H 1 4.133 0.003 . 2 . . . A 16 SER HB2 . 25569 1 61 . 1 1 10 10 SER HB3 H 1 4.123 0.01 . 2 . . . A 16 SER HB3 . 25569 1 62 . 1 1 11 11 ARG HA H 1 4.002 0.01 . 1 . . . A 17 ARG HA . 25569 1 63 . 1 1 11 11 ARG HB2 H 1 1.758 0.002 . 2 . . . A 17 ARG HB2 . 25569 1 64 . 1 1 11 11 ARG HB3 H 1 1.721 0.001 . 2 . . . A 17 ARG HB3 . 25569 1 65 . 1 1 11 11 ARG HG2 H 1 1.617 0.01 . 2 . . . A 17 ARG HG2 . 25569 1 66 . 1 1 11 11 ARG HD2 H 1 3.063 0.01 . 2 . . . A 17 ARG HD2 . 25569 1 67 . 1 1 11 11 ARG HD3 H 1 2.941 0.004 . 2 . . . A 17 ARG HD3 . 25569 1 68 . 1 1 12 12 SER HA H 1 4.526 0.01 . 1 . . . A 18 SER HA . 25569 1 69 . 1 1 12 12 SER HB2 H 1 3.734 0.01 . 2 . . . A 18 SER HB2 . 25569 1 70 . 1 1 12 12 SER HB3 H 1 3.610 0.01 . 2 . . . A 18 SER HB3 . 25569 1 71 . 1 1 13 13 SER HA H 1 4.163 0.002 . 1 . . . A 19 SER HA . 25569 1 72 . 1 1 13 13 SER HB2 H 1 3.697 0.001 . 2 . . . A 19 SER HB2 . 25569 1 73 . 1 1 13 13 SER HB3 H 1 3.675 0.002 . 2 . . . A 19 SER HB3 . 25569 1 74 . 1 1 14 14 GLY HA2 H 1 3.734 0.01 . 2 . . . A 20 GLY HA2 . 25569 1 75 . 1 1 14 14 GLY HA3 H 1 3.900 0.002 . 2 . . . A 20 GLY HA3 . 25569 1 76 . 1 1 15 15 ARG HA H 1 4.229 0.01 . 1 . . . A 21 ARG HA . 25569 1 77 . 1 1 15 15 ARG HB2 H 1 1.509 0.01 . 2 . . . A 21 ARG HB2 . 25569 1 78 . 1 1 15 15 ARG HB3 H 1 1.351 0.01 . 2 . . . A 21 ARG HB3 . 25569 1 79 . 1 1 15 15 ARG HG2 H 1 1.686 0.01 . 2 . . . A 21 ARG HG2 . 25569 1 80 . 1 1 15 15 ARG HD2 H 1 2.422 0.01 . 2 . . . A 21 ARG HD2 . 25569 1 81 . 1 1 15 15 ARG HD3 H 1 2.214 0.01 . 2 . . . A 21 ARG HD3 . 25569 1 82 . 1 1 15 15 ARG HE H 1 6.731 0.01 . 1 . . . A 21 ARG HE . 25569 1 83 . 1 1 15 15 ARG HH22 H 1 6.899 0.01 . 2 . . . A 21 ARG HH22 . 25569 1 84 . 1 1 16 16 VAL HA H 1 4.461 0.01 . 1 . . . A 22 VAL HA . 25569 1 85 . 1 1 16 16 VAL HB H 1 1.765 0.001 . 1 . . . A 22 VAL HB . 25569 1 86 . 1 1 16 16 VAL HG11 H 1 0.804 0.01 . 2 . . . A 22 VAL HG11 . 25569 1 87 . 1 1 16 16 VAL HG12 H 1 0.804 0.01 . 2 . . . A 22 VAL HG11 . 25569 1 88 . 1 1 16 16 VAL HG13 H 1 0.804 0.01 . 2 . . . A 22 VAL HG11 . 25569 1 89 . 1 1 16 16 VAL HG21 H 1 0.590 0.001 . 2 . . . A 22 VAL HG21 . 25569 1 90 . 1 1 16 16 VAL HG22 H 1 0.590 0.001 . 2 . . . A 22 VAL HG21 . 25569 1 91 . 1 1 16 16 VAL HG23 H 1 0.590 0.001 . 2 . . . A 22 VAL HG21 . 25569 1 92 . 1 1 17 17 TYR HA H 1 4.661 0.003 . 1 . . . A 23 TYR HA . 25569 1 93 . 1 1 17 17 TYR HB2 H 1 2.613 0.001 . 2 . . . A 23 TYR HB2 . 25569 1 94 . 1 1 17 17 TYR HB3 H 1 2.270 0.002 . 2 . . . A 23 TYR HB3 . 25569 1 95 . 1 1 17 17 TYR HD1 H 1 6.608 0.01 . 3 . . . A 23 TYR HD1 . 25569 1 96 . 1 1 17 17 TYR HE1 H 1 6.204 0.01 . 3 . . . A 23 TYR HE1 . 25569 1 97 . 1 1 18 18 TYR HA H 1 5.082 0.001 . 1 . . . A 24 TYR HA . 25569 1 98 . 1 1 18 18 TYR HB2 H 1 2.744 0.01 . 2 . . . A 24 TYR HB2 . 25569 1 99 . 1 1 18 18 TYR HB3 H 1 2.465 0.003 . 2 . . . A 24 TYR HB3 . 25569 1 100 . 1 1 18 18 TYR HD2 H 1 6.637 0.01 . 3 . . . A 24 TYR HD2 . 25569 1 101 . 1 1 18 18 TYR HE2 H 1 6.552 0.01 . 3 . . . A 24 TYR HE2 . 25569 1 102 . 1 1 19 19 PHE HA H 1 5.386 0.001 . 1 . . . A 25 PHE HA . 25569 1 103 . 1 1 19 19 PHE HB2 H 1 2.700 0.001 . 2 . . . A 25 PHE HB2 . 25569 1 104 . 1 1 19 19 PHE HB3 H 1 2.360 0.01 . 2 . . . A 25 PHE HB3 . 25569 1 105 . 1 1 19 19 PHE HD1 H 1 6.683 0.01 . 3 . . . A 25 PHE HD1 . 25569 1 106 . 1 1 19 19 PHE HE1 H 1 6.750 0.01 . 3 . . . A 25 PHE HE1 . 25569 1 107 . 1 1 19 19 PHE HZ H 1 7.069 0.01 . 1 . . . A 25 PHE HZ . 25569 1 108 . 1 1 20 20 ASN H H 1 7.910 0.01 . 1 . . . A 26 ASN H . 25569 1 109 . 1 1 20 20 ASN HA H 1 4.167 0.002 . 1 . . . A 26 ASN HA . 25569 1 110 . 1 1 20 20 ASN HB2 H 1 1.758 0.005 . 2 . . . A 26 ASN HB2 . 25569 1 111 . 1 1 20 20 ASN HB3 H 1 -0.919 0.001 . 2 . . . A 26 ASN HB3 . 25569 1 112 . 1 1 20 20 ASN HD22 H 1 3.944 0.01 . 2 . . . A 26 ASN HD22 . 25569 1 113 . 1 1 21 21 HIS HA H 1 3.854 0.001 . 1 . . . A 27 HIS HA . 25569 1 114 . 1 1 21 21 HIS HB2 H 1 3.049 0.001 . 2 . . . A 27 HIS HB2 . 25569 1 115 . 1 1 21 21 HIS HB3 H 1 2.799 0.01 . 2 . . . A 27 HIS HB3 . 25569 1 116 . 1 1 21 21 HIS HD2 H 1 6.742 0.002 . 1 . . . A 27 HIS HD2 . 25569 1 117 . 1 1 21 21 HIS HE1 H 1 7.612 0.002 . 1 . . . A 27 HIS HE1 . 25569 1 118 . 1 1 22 22 ILE HA H 1 3.603 0.01 . 1 . . . A 28 ILE HA . 25569 1 119 . 1 1 22 22 ILE HB H 1 1.778 0.01 . 1 . . . A 28 ILE HB . 25569 1 120 . 1 1 22 22 ILE HG12 H 1 1.063 0.01 . 2 . . . A 28 ILE HG12 . 25569 1 121 . 1 1 22 22 ILE HG13 H 1 0.760 0.01 . 2 . . . A 28 ILE HG13 . 25569 1 122 . 1 1 22 22 ILE HG21 H 1 0.503 0.001 . 1 . . . A 28 ILE HG21 . 25569 1 123 . 1 1 22 22 ILE HG22 H 1 0.503 0.001 . 1 . . . A 28 ILE HG21 . 25569 1 124 . 1 1 22 22 ILE HG23 H 1 0.503 0.001 . 1 . . . A 28 ILE HG21 . 25569 1 125 . 1 1 22 22 ILE HD11 H 1 0.543 0.01 . 1 . . . A 28 ILE HD11 . 25569 1 126 . 1 1 22 22 ILE HD12 H 1 0.543 0.01 . 1 . . . A 28 ILE HD11 . 25569 1 127 . 1 1 22 22 ILE HD13 H 1 0.543 0.01 . 1 . . . A 28 ILE HD11 . 25569 1 128 . 1 1 23 23 THR H H 1 7.179 0.01 . 1 . . . A 29 THR H . 25569 1 129 . 1 1 23 23 THR HA H 1 3.859 0.001 . 1 . . . A 29 THR HA . 25569 1 130 . 1 1 23 23 THR HB H 1 3.998 0.001 . 1 . . . A 29 THR HB . 25569 1 131 . 1 1 23 23 THR HG1 H 1 1.287 0.01 . 1 . . . A 29 THR HG1 . 25569 1 132 . 1 1 23 23 THR HG21 H 1 0.702 0.002 . 1 . . . A 29 THR HG21 . 25569 1 133 . 1 1 23 23 THR HG22 H 1 0.702 0.002 . 1 . . . A 29 THR HG21 . 25569 1 134 . 1 1 23 23 THR HG23 H 1 0.702 0.002 . 1 . . . A 29 THR HG21 . 25569 1 135 . 1 1 24 24 ASN HA H 1 3.910 0.01 . 1 . . . A 30 ASN HA . 25569 1 136 . 1 1 24 24 ASN HB2 H 1 2.862 0.01 . 2 . . . A 30 ASN HB2 . 25569 1 137 . 1 1 24 24 ASN HB3 H 1 2.695 0.01 . 2 . . . A 30 ASN HB3 . 25569 1 138 . 1 1 24 24 ASN HD21 H 1 7.224 0.01 . 2 . . . A 30 ASN HD21 . 25569 1 139 . 1 1 24 24 ASN HD22 H 1 6.618 0.001 . 2 . . . A 30 ASN HD22 . 25569 1 140 . 1 1 25 25 ALA HA H 1 4.181 0.001 . 1 . . . A 31 ALA HA . 25569 1 141 . 1 1 25 25 ALA HB1 H 1 1.005 0.002 . 1 . . . A 31 ALA HB1 . 25569 1 142 . 1 1 25 25 ALA HB2 H 1 1.005 0.002 . 1 . . . A 31 ALA HB1 . 25569 1 143 . 1 1 25 25 ALA HB3 H 1 1.005 0.002 . 1 . . . A 31 ALA HB1 . 25569 1 144 . 1 1 26 26 SER H H 1 8.063 0.01 . 1 . . . A 32 SER H . 25569 1 145 . 1 1 26 26 SER HA H 1 5.762 0.001 . 1 . . . A 32 SER HA . 25569 1 146 . 1 1 26 26 SER HB2 H 1 3.708 0.01 . 2 . . . A 32 SER HB2 . 25569 1 147 . 1 1 26 26 SER HB3 H 1 3.568 0.01 . 2 . . . A 32 SER HB3 . 25569 1 148 . 1 1 27 27 GLN HA H 1 4.667 0.01 . 1 . . . A 33 GLN HA . 25569 1 149 . 1 1 27 27 GLN HB2 H 1 2.037 0.002 . 2 . . . A 33 GLN HB2 . 25569 1 150 . 1 1 27 27 GLN HG2 H 1 2.501 0.01 . 2 . . . A 33 GLN HG2 . 25569 1 151 . 1 1 27 27 GLN HG3 H 1 2.753 0.946 . 2 . . . A 33 GLN HG3 . 25569 1 152 . 1 1 28 28 TRP HA H 1 4.664 0.01 . 1 . . . A 34 TRP HA . 25569 1 153 . 1 1 28 28 TRP HB2 H 1 3.375 0.001 . 2 . . . A 34 TRP HB2 . 25569 1 154 . 1 1 28 28 TRP HB3 H 1 2.964 0.01 . 2 . . . A 34 TRP HB3 . 25569 1 155 . 1 1 28 28 TRP HD1 H 1 7.242 0.01 . 1 . . . A 34 TRP HD1 . 25569 1 156 . 1 1 28 28 TRP HE3 H 1 8.010 0.01 . 1 . . . A 34 TRP HE3 . 25569 1 157 . 1 1 28 28 TRP HZ2 H 1 7.099 0.01 . 1 . . . A 34 TRP HZ2 . 25569 1 158 . 1 1 28 28 TRP HZ3 H 1 6.726 0.001 . 1 . . . A 34 TRP HZ3 . 25569 1 159 . 1 1 28 28 TRP HH2 H 1 6.901 0.01 . 1 . . . A 34 TRP HH2 . 25569 1 160 . 1 1 29 29 GLU HA H 1 4.125 0.01 . 1 . . . A 35 GLU HA . 25569 1 161 . 1 1 29 29 GLU HB2 H 1 1.684 0.01 . 2 . . . A 35 GLU HB2 . 25569 1 162 . 1 1 29 29 GLU HB3 H 1 1.602 0.01 . 2 . . . A 35 GLU HB3 . 25569 1 163 . 1 1 29 29 GLU HG2 H 1 2.123 0.01 . 2 . . . A 35 GLU HG2 . 25569 1 164 . 1 1 29 29 GLU HG3 H 1 2.053 0.01 . 2 . . . A 35 GLU HG3 . 25569 1 165 . 1 1 30 30 ARG HA H 1 2.466 0.01 . 1 . . . A 36 ARG HA . 25569 1 166 . 1 1 30 30 ARG HB2 H 1 1.136 0.001 . 2 . . . A 36 ARG HB2 . 25569 1 167 . 1 1 30 30 ARG HB3 H 1 0.965 0.01 . 2 . . . A 36 ARG HB3 . 25569 1 168 . 1 1 30 30 ARG HG2 H 1 0.671 0.01 . 2 . . . A 36 ARG HG2 . 25569 1 169 . 1 1 30 30 ARG HG3 H 1 0.553 0.01 . 2 . . . A 36 ARG HG3 . 25569 1 170 . 1 1 30 30 ARG HD2 H 1 2.770 0.01 . 2 . . . A 36 ARG HD2 . 25569 1 171 . 1 1 30 30 ARG HE H 1 7.058 0.01 . 1 . . . A 36 ARG HE . 25569 1 172 . 1 1 31 31 PRO HA H 1 3.666 0.01 . 1 . . . A 37 PRO HA . 25569 1 173 . 1 1 31 31 PRO HB2 H 1 0.565 0.01 . 2 . . . A 37 PRO HB2 . 25569 1 174 . 1 1 31 31 PRO HB3 H 1 0.467 0.01 . 2 . . . A 37 PRO HB3 . 25569 1 175 . 1 1 31 31 PRO HG2 H 1 0.313 0.01 . 2 . . . A 37 PRO HG2 . 25569 1 176 . 1 1 31 31 PRO HG3 H 1 -0.323 0.01 . 2 . . . A 37 PRO HG3 . 25569 1 177 . 1 1 31 31 PRO HD2 H 1 2.264 0.01 . 2 . . . A 37 PRO HD2 . 25569 1 178 . 1 1 31 31 PRO HD3 H 1 2.051 0.001 . 2 . . . A 37 PRO HD3 . 25569 1 179 . 1 1 32 32 SER HA H 1 4.098 0.01 . 1 . . . A 38 SER HA . 25569 1 180 . 1 1 32 32 SER HB2 H 1 3.575 0.01 . 2 . . . A 38 SER HB2 . 25569 1 181 . 1 1 32 32 SER HB3 H 1 3.473 0.011 . 2 . . . A 38 SER HB3 . 25569 1 182 . 2 2 1 1 ARG HA H 1 4.220 0.003 . 1 . . . . 208 ARG HA . 25569 1 183 . 2 2 1 1 ARG HB2 H 1 1.866 0.003 . 2 . . . . 208 ARG HB2 . 25569 1 184 . 2 2 1 1 ARG HB3 H 1 1.809 0.001 . 2 . . . . 208 ARG HB3 . 25569 1 185 . 2 2 1 1 ARG HG2 H 1 1.720 0.001 . 2 . . . . 208 ARG HG2 . 25569 1 186 . 2 2 1 1 ARG HD2 H 1 2.404 0.001 . 2 . . . . 208 ARG HD2 . 25569 1 187 . 2 2 1 1 ARG HD3 H 1 2.336 0.001 . 2 . . . . 208 ARG HD3 . 25569 1 188 . 2 2 2 2 ILE HA H 1 4.010 0.01 . 1 . . . . 209 ILE HA . 25569 1 189 . 2 2 2 2 ILE HB H 1 1.597 0.002 . 1 . . . . 209 ILE HB . 25569 1 190 . 2 2 2 2 ILE HG12 H 1 1.227 0.01 . 2 . . . . 209 ILE HG12 . 25569 1 191 . 2 2 2 2 ILE HG13 H 1 0.925 0.01 . 2 . . . . 209 ILE HG13 . 25569 1 192 . 2 2 2 2 ILE HG21 H 1 0.646 0.01 . 1 . . . . 209 ILE HG22 . 25569 1 193 . 2 2 2 2 ILE HG22 H 1 0.646 0.01 . 1 . . . . 209 ILE HG22 . 25569 1 194 . 2 2 2 2 ILE HG23 H 1 0.646 0.01 . 1 . . . . 209 ILE HG22 . 25569 1 195 . 2 2 2 2 ILE HD11 H 1 0.594 0.01 . 1 . . . . 209 ILE HD12 . 25569 1 196 . 2 2 2 2 ILE HD12 H 1 0.594 0.01 . 1 . . . . 209 ILE HD12 . 25569 1 197 . 2 2 2 2 ILE HD13 H 1 0.594 0.01 . 1 . . . . 209 ILE HD12 . 25569 1 198 . 2 2 3 3 SEP HA H 1 4.344 0.001 . 1 . . . . 210 SEP HA . 25569 1 199 . 2 2 3 3 SEP HB2 H 1 3.742 0.002 . 2 . . . . 210 SEP HB2 . 25569 1 200 . 2 2 3 3 SEP HB3 H 1 3.627 0.003 . 2 . . . . 210 SEP HB3 . 25569 1 201 . 2 2 4 4 PRO HA H 1 4.419 0.001 . 1 . . . . 211 PRO HA . 25569 1 202 . 2 2 4 4 PRO HB2 H 1 2.063 0.01 . 2 . . . . 211 PRO HB2 . 25569 1 203 . 2 2 4 4 PRO HB3 H 1 1.643 0.002 . 2 . . . . 211 PRO HB3 . 25569 1 204 . 2 2 4 4 PRO HG2 H 1 1.557 0.001 . 2 . . . . 211 PRO HG2 . 25569 1 205 . 2 2 4 4 PRO HG3 H 1 1.734 0.002 . 2 . . . . 211 PRO HG3 . 25569 1 206 . 2 2 4 4 PRO HD2 H 1 3.581 0.001 . 2 . . . . 211 PRO HD2 . 25569 1 207 . 2 2 4 4 PRO HD3 H 1 3.382 0.001 . 2 . . . . 211 PRO HD3 . 25569 1 208 . 2 2 5 5 PRO HA H 1 4.193 0.001 . 1 . . . . 212 PRO HA . 25569 1 209 . 2 2 5 5 PRO HB2 H 1 2.063 0.01 . 2 . . . . 212 PRO HB2 . 25569 1 210 . 2 2 5 5 PRO HB3 H 1 1.776 0.001 . 2 . . . . 212 PRO HB3 . 25569 1 211 . 2 2 5 5 PRO HG2 H 1 1.785 0.01 . 2 . . . . 212 PRO HG2 . 25569 1 212 . 2 2 5 5 PRO HG3 H 1 1.577 0.01 . 2 . . . . 212 PRO HG3 . 25569 1 213 . 2 2 5 5 PRO HD2 H 1 3.577 0.01 . 2 . . . . 212 PRO HD2 . 25569 1 214 . 2 2 5 5 PRO HD3 H 1 3.386 0.005 . 2 . . . . 212 PRO HD3 . 25569 1 215 . 2 2 6 6 LEU HA H 1 4.335 0.001 . 1 . . . . 213 LEU HA . 25569 1 216 . 2 2 6 6 LEU HB2 H 1 1.486 0.012 . 2 . . . . 213 LEU HB2 . 25569 1 217 . 2 2 6 6 LEU HB3 H 1 1.344 0.005 . 2 . . . . 213 LEU HB3 . 25569 1 218 . 2 2 6 6 LEU HG H 1 1.260 0.003 . 1 . . . . 213 LEU HG . 25569 1 219 . 2 2 6 6 LEU HD11 H 1 0.696 0.007 . 2 . . . . 213 LEU HD12 . 25569 1 220 . 2 2 6 6 LEU HD12 H 1 0.696 0.007 . 2 . . . . 213 LEU HD12 . 25569 1 221 . 2 2 6 6 LEU HD13 H 1 0.696 0.007 . 2 . . . . 213 LEU HD12 . 25569 1 222 . 2 2 6 6 LEU HD21 H 1 0.674 0.01 . 2 . . . . 213 LEU HD22 . 25569 1 223 . 2 2 6 6 LEU HD22 H 1 0.674 0.01 . 2 . . . . 213 LEU HD22 . 25569 1 224 . 2 2 6 6 LEU HD23 H 1 0.674 0.01 . 2 . . . . 213 LEU HD22 . 25569 1 225 . 2 2 7 7 PRO HA H 1 4.113 0.01 . 1 . . . . 214 PRO HA . 25569 1 226 . 2 2 7 7 PRO HB2 H 1 1.971 0.001 . 2 . . . . 214 PRO HB2 . 25569 1 227 . 2 2 7 7 PRO HG2 H 1 1.748 0.001 . 2 . . . . 214 PRO HG2 . 25569 1 228 . 2 2 7 7 PRO HG3 H 1 1.541 0.002 . 2 . . . . 214 PRO HG3 . 25569 1 229 . 2 2 7 7 PRO HD2 H 1 3.581 0.001 . 2 . . . . 214 PRO HD2 . 25569 1 230 . 2 2 7 7 PRO HD3 H 1 3.384 0.001 . 2 . . . . 214 PRO HD3 . 25569 1 231 . 2 2 8 8 PHE HA H 1 4.268 0.003 . 1 . . . . 215 PHE HA . 25569 1 232 . 2 2 8 8 PHE HB2 H 1 2.909 0.01 . 2 . . . . 215 PHE HB2 . 25569 1 233 . 2 2 8 8 PHE HB3 H 1 2.869 0.01 . 2 . . . . 215 PHE HB3 . 25569 1 234 . 2 2 8 8 PHE HD2 H 1 7.037 0.001 . 3 . . . . 215 PHE HD2 . 25569 1 235 . 2 2 8 8 PHE HE2 H 1 7.145 0.01 . 3 . . . . 215 PHE HE2 . 25569 1 stop_ save_