data_5248 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5248 _Entry.Title ; NMR Solution Structure of the Isolated Apo Pin1 WW Domain: Comparison to the X-Ray Crystal Structures of Pin 1 ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2002-01-03 _Entry.Accession_date 2002-01-04 _Entry.Last_release_date 2002-02-05 _Entry.Original_release_date 2002-02-05 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Jennifer Kowalski . A. . 5248 2 Kai Liu . . . 5248 3 Jeffery Kelly . W. . 5248 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5248 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 196 5248 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2002-02-05 2002-01-03 original author . 5248 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5248 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11786999 _Citation.Full_citation . _Citation.Title ; NMR Solution Structure of the Isolated Apo Pin1 WW Domain: Comaprison to the X-Ray Crystal Structures of Pin 1 ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biopolymers _Citation.Journal_name_full . _Citation.Journal_volume 63 _Citation.Journal_issue 2 _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 111 _Citation.Page_last 121 _Citation.Year 2002 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Jennifer Kowalski . A. . 5248 1 2 Kai Liu . . . 5248 1 3 Jeffery Kelly . W. . 5248 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'WW Domain' 5248 1 'Pin 1' 5248 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_WW_domain _Assembly.Sf_category assembly _Assembly.Sf_framecode system_WW_domain _Assembly.Entry_ID 5248 _Assembly.ID 1 _Assembly.Name 'Pin1 N-terminal WW domain' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'not present' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5248 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'Pin1 N-terminal WW Domain' 1 $Pin1_WW_Domain . . . native . . . . . 5248 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Pin1 N-terminal WW domain' system 5248 1 'WW domain' abbreviation 5248 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_Pin1_WW_Domain _Entity.Sf_category entity _Entity.Sf_framecode Pin1_WW_Domain _Entity.Entry_ID 5248 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Pin1 WW domain' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; MADEEKLPPGWEKRMSRSSG RVYYFNHITNASQWERPSG ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 39 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 16070 . Pin1_WW . . . . . 87.18 36 100.00 100.00 5.82e-16 . . . . 5248 1 2 no BMRB 16088 . Pin1_WW . . . . . 87.18 36 100.00 100.00 5.82e-16 . . . . 5248 1 3 no BMRB 17545 . "first domain of human PIN1" . . . . . 87.18 36 100.00 100.00 5.11e-16 . . . . 5248 1 4 no BMRB 19258 . entity . . . . . 100.00 43 100.00 100.00 6.32e-20 . . . . 5248 1 5 no BMRB 19259 . Pin1 . . . . . 100.00 43 97.44 97.44 2.96e-19 . . . . 5248 1 6 no BMRB 4882 . WW_domain . . . . . 87.18 39 100.00 100.00 4.35e-16 . . . . 5248 1 7 no BMRB 5305 . Pin1 . . . . . 100.00 183 100.00 100.00 1.28e-19 . . . . 5248 1 8 no PDB 1F8A . "Structural Basis For The Phosphoserine-proline Recognition By Group Iv Ww Domains" . . . . . 100.00 167 100.00 100.00 9.76e-20 . . . . 5248 1 9 no PDB 1I6C . "Solution Structure Of Pin1 Ww Domain" . . . . . 87.18 39 100.00 100.00 4.35e-16 . . . . 5248 1 10 no PDB 1I8G . "Solution Structure Of Pin1 Ww Domain Complexed With Cdc25 Phosphothreonine Peptide" . . . . . 87.18 39 100.00 100.00 4.35e-16 . . . . 5248 1 11 no PDB 1I8H . "Solution Structure Of Pin1 Ww Domain Complexed With Human Tau Phosphothreonine Peptide" . . . . . 87.18 39 100.00 100.00 4.35e-16 . . . . 5248 1 12 no PDB 1NMV . "Solution Structure Of Human Pin1" . . . . . 100.00 163 100.00 100.00 9.53e-20 . . . . 5248 1 13 no PDB 1PIN . "Pin1 Peptidyl-prolyl Cis-trans Isomerase From Homo Sapiens" . . . . . 100.00 163 100.00 100.00 9.53e-20 . . . . 5248 1 14 no PDB 2ITK . "Human Pin1 Bound To D-Peptide" . . . . . 100.00 167 97.44 97.44 8.46e-19 . . . . 5248 1 15 no PDB 2KCF . "The Nmr Solution Structure Of The Isolated Apo Pin1 Ww Domain" . . . . . 87.18 36 100.00 100.00 5.82e-16 . . . . 5248 1 16 no PDB 2LB3 . "Structure Of The Ww Domain Of Pin1 In Complex With A Human Phosphorylated Smad3 Derived Peptide" . . . . . 87.18 36 100.00 100.00 5.11e-16 . . . . 5248 1 17 no PDB 2M8I . "Structure Of Pin1 Ww Domain" . . . . . 100.00 43 100.00 100.00 6.32e-20 . . . . 5248 1 18 no PDB 2M8J . "Structure Of Pin1 Ww Domain Phospho-mimic S16e" . . . . . 100.00 43 97.44 97.44 2.96e-19 . . . . 5248 1 19 no PDB 2Q5A . "Human Pin1 Bound To L-Peptide" . . . . . 100.00 167 97.44 97.44 8.46e-19 . . . . 5248 1 20 no PDB 2XP3 . "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" . . . . . 100.00 167 97.44 97.44 8.46e-19 . . . . 5248 1 21 no PDB 2XP4 . "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" . . . . . 100.00 167 97.44 97.44 8.46e-19 . . . . 5248 1 22 no PDB 2XP5 . "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" . . . . . 100.00 167 97.44 97.44 8.46e-19 . . . . 5248 1 23 no PDB 2XP6 . "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" . . . . . 100.00 167 97.44 97.44 8.73e-19 . . . . 5248 1 24 no PDB 2XP7 . "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" . . . . . 100.00 167 97.44 97.44 8.46e-19 . . . . 5248 1 25 no PDB 2XP8 . "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" . . . . . 100.00 167 97.44 97.44 8.46e-19 . . . . 5248 1 26 no PDB 2XP9 . "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" . . . . . 100.00 167 97.44 97.44 8.46e-19 . . . . 5248 1 27 no PDB 2XPA . "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" . . . . . 100.00 167 97.44 97.44 8.46e-19 . . . . 5248 1 28 no PDB 2XPB . "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" . . . . . 100.00 167 97.44 97.44 8.46e-19 . . . . 5248 1 29 no PDB 2ZQS . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 100.00 100.00 8.40e-20 . . . . 5248 1 30 no PDB 2ZQT . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 100.00 100.00 8.49e-20 . . . . 5248 1 31 no PDB 2ZQU . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 97.44 97.44 2.05e-18 . . . . 5248 1 32 no PDB 2ZQV . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 97.44 97.44 1.53e-18 . . . . 5248 1 33 no PDB 2ZR4 . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 97.44 100.00 2.17e-19 . . . . 5248 1 34 no PDB 2ZR5 . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 100.00 100.00 9.04e-20 . . . . 5248 1 35 no PDB 2ZR6 . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 97.44 97.44 8.20e-19 . . . . 5248 1 36 no PDB 3KAB . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 97.44 97.44 8.46e-19 . . . . 5248 1 37 no PDB 3KAD . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 97.44 97.44 8.73e-19 . . . . 5248 1 38 no PDB 3KAF . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 97.44 97.44 8.73e-19 . . . . 5248 1 39 no PDB 3KAG . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 97.44 97.44 8.46e-19 . . . . 5248 1 40 no PDB 3KAH . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 97.44 97.44 8.46e-19 . . . . 5248 1 41 no PDB 3KAI . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 97.44 97.44 8.46e-19 . . . . 5248 1 42 no PDB 3KCE . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 97.44 97.44 8.46e-19 . . . . 5248 1 43 no PDB 3NTP . "Human Pin1 Complexed With Reduced Amide Inhibitor" . . . . . 100.00 167 97.44 97.44 8.46e-19 . . . . 5248 1 44 no PDB 3ODK . "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" . . . . . 100.00 167 97.44 97.44 8.46e-19 . . . . 5248 1 45 no PDB 3OOB . "Structural And Functional Insights Of Directly Targeting Pin1 By Epigallocatechin-3-Gallate" . . . . . 100.00 163 97.44 97.44 8.20e-19 . . . . 5248 1 46 no PDB 3TC5 . "Selective Targeting Of Disease-Relevant Protein Binding Domains By O- Phosphorylated Natural Product Derivatives" . . . . . 100.00 166 97.44 97.44 8.66e-19 . . . . 5248 1 47 no PDB 3TCZ . "Human Pin1 Bound To Cis Peptidomimetic Inhibitor" . . . . . 87.18 158 97.06 97.06 5.01e-15 . . . . 5248 1 48 no PDB 3TDB . "Human Pin1 Bound To Trans Peptidomimetic Inhibitor" . . . . . 87.18 158 97.06 97.06 5.01e-15 . . . . 5248 1 49 no PDB 3WH0 . "Structure Of Pin1 Complex With 18-crown-6" . . . . . 100.00 163 97.44 97.44 8.20e-19 . . . . 5248 1 50 no PDB 4GWT . "Structure Of Racemic Pin1 Ww Domain Cocrystallized With Dl-malic Acid" . . . . . 87.18 36 100.00 100.00 5.82e-16 . . . . 5248 1 51 no PDB 4GWV . "Structure Of Racemic Pin1 Ww Domain Cocrystallized With Tri-ammonium Citrate" . . . . . 87.18 36 100.00 100.00 5.82e-16 . . . . 5248 1 52 no DBJ BAA87037 . "PIN1 [Mus sp.]" . . . . . 100.00 165 100.00 100.00 9.70e-20 . . . . 5248 1 53 no DBJ BAA87038 . "PIN1 [Mus sp.]" . . . . . 100.00 165 100.00 100.00 9.70e-20 . . . . 5248 1 54 no DBJ BAB22270 . "unnamed protein product [Mus musculus]" . . . . . 100.00 165 100.00 100.00 9.70e-20 . . . . 5248 1 55 no DBJ BAB22743 . "unnamed protein product [Mus musculus]" . . . . . 100.00 165 100.00 100.00 9.70e-20 . . . . 5248 1 56 no DBJ BAC35631 . "unnamed protein product [Mus musculus]" . . . . . 100.00 165 100.00 100.00 9.70e-20 . . . . 5248 1 57 no EMBL CAG28582 . "UBL5 [Homo sapiens]" . . . . . 100.00 163 100.00 100.00 9.53e-20 . . . . 5248 1 58 no GB AAC50492 . "Pin1 [Homo sapiens]" . . . . . 100.00 163 100.00 100.00 9.53e-20 . . . . 5248 1 59 no GB AAF43897 . "prolyl isomerase Pin1 [Xenopus laevis]" . . . . . 94.87 159 97.30 100.00 8.40e-18 . . . . 5248 1 60 no GB AAH02899 . "Peptidylprolyl cis/trans isomerase, NIMA-interacting 1 [Homo sapiens]" . . . . . 100.00 163 100.00 100.00 9.53e-20 . . . . 5248 1 61 no GB AAH38254 . "Protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1 [Mus musculus]" . . . . . 100.00 165 100.00 100.00 9.70e-20 . . . . 5248 1 62 no GB AAH77447 . "Unknown (protein for IMAGE:4058360), partial [Xenopus laevis]" . . . . . 92.31 158 97.22 100.00 6.06e-17 . . . . 5248 1 63 no PRF 2209428A . "peptidyl-Pro isomerase" . . . . . 100.00 163 100.00 100.00 9.53e-20 . . . . 5248 1 64 no REF NP_001029804 . "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Bos taurus]" . . . . . 100.00 163 100.00 100.00 9.04e-20 . . . . 5248 1 65 no REF NP_001084236 . "prolyl isomerase Pin1 b [Xenopus laevis]" . . . . . 94.87 159 97.30 100.00 8.40e-18 . . . . 5248 1 66 no REF NP_001100171 . "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Rattus norvegicus]" . . . . . 100.00 165 97.44 97.44 1.07e-18 . . . . 5248 1 67 no REF NP_001231300 . "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Sus scrofa]" . . . . . 100.00 163 100.00 100.00 9.64e-20 . . . . 5248 1 68 no REF NP_001270625 . "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Macaca fascicularis]" . . . . . 100.00 163 97.44 97.44 9.60e-19 . . . . 5248 1 69 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 9.53e-20 . . . . 5248 1 70 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 97.44 97.44 9.60e-19 . . . . 5248 1 71 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 9.04e-20 . . . . 5248 1 72 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 9.70e-20 . . . . 5248 1 73 no TPG DAA28013 . "TPA: peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Bos taurus]" . . . . . 100.00 163 100.00 100.00 9.04e-20 . . . . 5248 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Pin1 WW domain' common 5248 1 'Pin1 WW Domain' abbreviation 5248 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 -3 MET . 5248 1 2 -2 ALA . 5248 1 3 -1 ASP . 5248 1 4 1 GLU . 5248 1 5 2 GLU . 5248 1 6 3 LYS . 5248 1 7 4 LEU . 5248 1 8 5 PRO . 5248 1 9 6 PRO . 5248 1 10 7 GLY . 5248 1 11 8 TRP . 5248 1 12 9 GLU . 5248 1 13 10 LYS . 5248 1 14 11 ARG . 5248 1 15 12 MET . 5248 1 16 13 SER . 5248 1 17 14 ARG . 5248 1 18 15 SER . 5248 1 19 16 SER . 5248 1 20 17 GLY . 5248 1 21 18 ARG . 5248 1 22 19 VAL . 5248 1 23 20 TYR . 5248 1 24 21 TYR . 5248 1 25 22 PHE . 5248 1 26 23 ASN . 5248 1 27 24 HIS . 5248 1 28 25 ILE . 5248 1 29 26 THR . 5248 1 30 27 ASN . 5248 1 31 28 ALA . 5248 1 32 29 SER . 5248 1 33 30 GLN . 5248 1 34 31 TRP . 5248 1 35 32 GLU . 5248 1 36 33 ARG . 5248 1 37 34 PRO . 5248 1 38 35 SER . 5248 1 39 36 GLY . 5248 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 . MET 1 1 5248 1 . ALA 2 2 5248 1 . ASP 3 3 5248 1 . GLU 4 4 5248 1 . GLU 5 5 5248 1 . LYS 6 6 5248 1 . LEU 7 7 5248 1 . PRO 8 8 5248 1 . PRO 9 9 5248 1 . GLY 10 10 5248 1 . TRP 11 11 5248 1 . GLU 12 12 5248 1 . LYS 13 13 5248 1 . ARG 14 14 5248 1 . MET 15 15 5248 1 . SER 16 16 5248 1 . ARG 17 17 5248 1 . SER 18 18 5248 1 . SER 19 19 5248 1 . GLY 20 20 5248 1 . ARG 21 21 5248 1 . VAL 22 22 5248 1 . TYR 23 23 5248 1 . TYR 24 24 5248 1 . PHE 25 25 5248 1 . ASN 26 26 5248 1 . HIS 27 27 5248 1 . ILE 28 28 5248 1 . THR 29 29 5248 1 . ASN 30 30 5248 1 . ALA 31 31 5248 1 . SER 32 32 5248 1 . GLN 33 33 5248 1 . TRP 34 34 5248 1 . GLU 35 35 5248 1 . ARG 36 36 5248 1 . PRO 37 37 5248 1 . SER 38 38 5248 1 . GLY 39 39 5248 1 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 5248 _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 $Pin1_WW_Domain . 9606 . . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 5248 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 5248 _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 $Pin1_WW_Domain . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5248 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5248 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'Pin1 WW domain' . . . 1 $Pin1_WW_Domain . . . 1 1.2 mM . . . . 5248 1 stop_ save_ ####################### # Sample conditions # ####################### save_Only_Conditions _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Only_Conditions _Sample_condition_list.Entry_ID 5248 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 6.2 0.1 na 5248 1 temperature 278 1 K 5248 1 stop_ save_ ############################ # Computer software used # ############################ save_PROSA _Software.Sf_category software _Software.Sf_framecode PROSA _Software.Entry_ID 5248 _Software.ID 1 _Software.Name PROSA _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data processing' 5248 1 stop_ save_ save_xeasy _Software.Sf_category software _Software.Sf_framecode xeasy _Software.Entry_ID 5248 _Software.ID 2 _Software.Name xeasy _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data display' 5248 2 'data analysis' 5248 2 stop_ save_ save_GARANT _Software.Sf_category software _Software.Sf_framecode GARANT _Software.Entry_ID 5248 _Software.ID 3 _Software.Name GARANT _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'automated peak assignments' 5248 3 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 5248 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer BRUKER _NMR_spectrometer.Model AMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 5248 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer BRUKER _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5248 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer_1 BRUKER AMX . 600 . . . 5248 1 2 NMR_spectrometer_2 BRUKER DMX . 750 . . . 5248 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 5248 _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 DQF-COSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5248 1 2 NOESY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5248 1 3 TOCSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5248 1 4 D2O-NOESY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5248 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 5248 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name DQF-COSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 5248 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name NOESY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 5248 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name TOCSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 5248 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name D2O-NOESY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5248 _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 1.00000000 internal . . . . . . . . 5248 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_Pin1_WW_shifts _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode Pin1_WW_shifts _Assigned_chem_shift_list.Entry_ID 5248 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Only_Conditions _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 DQF-COSY 1 $sample_1 . 5248 1 2 NOESY 1 $sample_1 . 5248 1 3 TOCSY 1 $sample_1 . 5248 1 4 D2O-NOESY 1 $sample_1 . 5248 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 7 7 LEU H H 1 8.811 0.060 . . . . . . . . . . 5248 1 2 . 1 1 7 7 LEU HA H 1 4.574 0.043 . . . . . . . . . . 5248 1 3 . 1 1 7 7 LEU HG H 1 1.452 0.010 . . . . . . . . . . 5248 1 4 . 1 1 7 7 LEU HD11 H 1 0.825 0.004 . 1 . . . . . . . . 5248 1 5 . 1 1 7 7 LEU HD12 H 1 0.825 0.004 . 1 . . . . . . . . 5248 1 6 . 1 1 7 7 LEU HD13 H 1 0.825 0.004 . 1 . . . . . . . . 5248 1 7 . 1 1 7 7 LEU HD21 H 1 1.110 0.005 . 1 . . . . . . . . 5248 1 8 . 1 1 7 7 LEU HD22 H 1 1.110 0.005 . 1 . . . . . . . . 5248 1 9 . 1 1 7 7 LEU HD23 H 1 1.110 0.005 . 1 . . . . . . . . 5248 1 10 . 1 1 8 8 PRO HA H 1 4.891 0.006 . . . . . . . . . . 5248 1 11 . 1 1 8 8 PRO HB2 H 1 2.039 0.006 . . . . . . . . . . 5248 1 12 . 1 1 8 8 PRO HB3 H 1 2.647 0.003 . . . . . . . . . . 5248 1 13 . 1 1 8 8 PRO HG2 H 1 1.682 0.006 . . . . . . . . . . 5248 1 14 . 1 1 8 8 PRO HG3 H 1 1.818 0.004 . . . . . . . . . . 5248 1 15 . 1 1 8 8 PRO HD2 H 1 3.057 0.012 . . . . . . . . . . 5248 1 16 . 1 1 8 8 PRO HD3 H 1 3.726 0.014 . . . . . . . . . . 5248 1 17 . 1 1 9 9 PRO HA H 1 4.392 0.007 . . . . . . . . . . 5248 1 18 . 1 1 9 9 PRO HB2 H 1 1.901 0.005 . . . . . . . . . . 5248 1 19 . 1 1 9 9 PRO HB3 H 1 2.370 0.006 . . . . . . . . . . 5248 1 20 . 1 1 9 9 PRO HG2 H 1 2.090 0.010 . . . . . . . . . . 5248 1 21 . 1 1 9 9 PRO HG3 H 1 2.192 0.008 . . . . . . . . . . 5248 1 22 . 1 1 9 9 PRO HD2 H 1 3.676 0.010 . . . . . . . . . . 5248 1 23 . 1 1 9 9 PRO HD3 H 1 3.962 0.005 . . . . . . . . . . 5248 1 24 . 1 1 10 10 GLY H H 1 8.900 0.007 . . . . . . . . . . 5248 1 25 . 1 1 10 10 GLY HA2 H 1 3.288 0.010 . . . . . . . . . . 5248 1 26 . 1 1 10 10 GLY HA3 H 1 4.070 0.009 . . . . . . . . . . 5248 1 27 . 1 1 11 11 TRP H H 1 7.411 0.011 . . . . . . . . . . 5248 1 28 . 1 1 11 11 TRP HA H 1 5.274 0.009 . . . . . . . . . . 5248 1 29 . 1 1 11 11 TRP HB2 H 1 3.286 0.006 . . . . . . . . . . 5248 1 30 . 1 1 11 11 TRP HB3 H 1 2.996 0.010 . . . . . . . . . . 5248 1 31 . 1 1 11 11 TRP HD1 H 1 6.993 0.007 . . . . . . . . . . 5248 1 32 . 1 1 11 11 TRP HE3 H 1 7.408 0.008 . . . . . . . . . . 5248 1 33 . 1 1 11 11 TRP HE1 H 1 10.714 0.005 . . . . . . . . . . 5248 1 34 . 1 1 11 11 TRP HZ3 H 1 6.981 0.009 . . . . . . . . . . 5248 1 35 . 1 1 11 11 TRP HZ2 H 1 7.469 0.009 . . . . . . . . . . 5248 1 36 . 1 1 11 11 TRP HH2 H 1 7.037 0.010 . . . . . . . . . . 5248 1 37 . 1 1 12 12 GLU H H 1 9.849 0.003 . . . . . . . . . . 5248 1 38 . 1 1 12 12 GLU HA H 1 4.875 0.009 . . . . . . . . . . 5248 1 39 . 1 1 12 12 GLU HG2 H 1 2.352 0.007 . . . . . . . . . . 5248 1 40 . 1 1 12 12 GLU HG3 H 1 2.574 0.004 . . . . . . . . . . 5248 1 41 . 1 1 13 13 LYS H H 1 9.066 0.009 . . . . . . . . . . 5248 1 42 . 1 1 13 13 LYS HA H 1 4.413 0.023 . . . . . . . . . . 5248 1 43 . 1 1 14 14 ARG H H 1 8.953 0.007 . . . . . . . . . . 5248 1 44 . 1 1 14 14 ARG HA H 1 4.464 0.002 . . . . . . . . . . 5248 1 45 . 1 1 14 14 ARG HB2 H 1 0.110 0.006 . . . . . . . . . . 5248 1 46 . 1 1 14 14 ARG HB3 H 1 1.319 0.004 . . . . . . . . . . 5248 1 47 . 1 1 14 14 ARG HG2 H 1 1.267 0.003 . . . . . . . . . . 5248 1 48 . 1 1 14 14 ARG HG3 H 1 1.413 0.013 . . . . . . . . . . 5248 1 49 . 1 1 14 14 ARG HD2 H 1 2.665 0.009 . . . . . . . . . . 5248 1 50 . 1 1 14 14 ARG HD3 H 1 2.913 0.005 . . . . . . . . . . 5248 1 51 . 1 1 14 14 ARG HE H 1 7.017 0.008 . . . . . . . . . . 5248 1 52 . 1 1 14 14 ARG HH11 H 1 6.233 0.006 . . . . . . . . . . 5248 1 53 . 1 1 14 14 ARG HH21 H 1 6.367 0.007 . . . . . . . . . . 5248 1 54 . 1 1 15 15 MET H H 1 8.342 0.004 . . . . . . . . . . 5248 1 55 . 1 1 15 15 MET HA H 1 4.993 0.005 . . . . . . . . . . 5248 1 56 . 1 1 15 15 MET HG2 H 1 2.277 0.007 . . . . . . . . . . 5248 1 57 . 1 1 15 15 MET HG3 H 1 2.458 0.007 . . . . . . . . . . 5248 1 58 . 1 1 16 16 SER H H 1 9.131 0.005 . . . . . . . . . . 5248 1 59 . 1 1 16 16 SER HA H 1 4.887 0.002 . . . . . . . . . . 5248 1 60 . 1 1 16 16 SER HB2 H 1 4.310 0.011 . . . . . . . . . . 5248 1 61 . 1 1 16 16 SER HB3 H 1 4.228 0.009 . . . . . . . . . . 5248 1 62 . 1 1 17 17 ARG H H 1 10.000 0.040 . . . . . . . . . . 5248 1 63 . 1 1 17 17 ARG HA H 1 4.162 0.009 . . . . . . . . . . 5248 1 64 . 1 1 17 17 ARG HE H 1 7.765 0.029 . . . . . . . . . . 5248 1 65 . 1 1 18 18 SER H H 1 8.784 0.012 . . . . . . . . . . 5248 1 66 . 1 1 18 18 SER HA H 1 4.374 0.013 . . . . . . . . . . 5248 1 67 . 1 1 18 18 SER HB3 H 1 3.939 0.005 . . . . . . . . . . 5248 1 68 . 1 1 19 19 SER H H 1 8.333 0.005 . . . . . . . . . . 5248 1 69 . 1 1 19 19 SER HA H 1 4.312 0.005 . . . . . . . . . . 5248 1 70 . 1 1 19 19 SER HB2 H 1 3.753 0.012 . . . . . . . . . . 5248 1 71 . 1 1 19 19 SER HB3 H 1 3.823 0.007 . . . . . . . . . . 5248 1 72 . 1 1 20 20 GLY H H 1 8.146 0.015 . . . . . . . . . . 5248 1 73 . 1 1 20 20 GLY HA2 H 1 4.152 0.007 . . . . . . . . . . 5248 1 74 . 1 1 20 20 GLY HA3 H 1 3.978 0.009 . . . . . . . . . . 5248 1 75 . 1 1 21 21 ARG H H 1 7.743 0.003 . . . . . . . . . . 5248 1 76 . 1 1 21 21 ARG HA H 1 4.486 0.010 . . . . . . . . . . 5248 1 77 . 1 1 21 21 ARG HB2 H 1 1.774 0.005 . . . . . . . . . . 5248 1 78 . 1 1 21 21 ARG HB3 H 1 2.007 0.008 . . . . . . . . . . 5248 1 79 . 1 1 21 21 ARG HD2 H 1 2.511 0.010 . . . . . . . . . . 5248 1 80 . 1 1 21 21 ARG HD3 H 1 2.853 0.009 . . . . . . . . . . 5248 1 81 . 1 1 21 21 ARG HE H 1 6.816 0.010 . . . . . . . . . . 5248 1 82 . 1 1 21 21 ARG HH11 H 1 6.007 0.004 . . . . . . . . . . 5248 1 83 . 1 1 21 21 ARG HH21 H 1 6.127 0.004 . . . . . . . . . . 5248 1 84 . 1 1 22 22 VAL H H 1 8.681 0.006 . . . . . . . . . . 5248 1 85 . 1 1 22 22 VAL HA H 1 4.708 0.007 . . . . . . . . . . 5248 1 86 . 1 1 22 22 VAL HB H 1 2.026 0.003 . . . . . . . . . . 5248 1 87 . 1 1 22 22 VAL HG11 H 1 0.841 0.006 . 1 . . . . . . . . 5248 1 88 . 1 1 22 22 VAL HG12 H 1 0.841 0.006 . 1 . . . . . . . . 5248 1 89 . 1 1 22 22 VAL HG13 H 1 0.841 0.006 . 1 . . . . . . . . 5248 1 90 . 1 1 22 22 VAL HG21 H 1 1.089 0.008 . 1 . . . . . . . . 5248 1 91 . 1 1 22 22 VAL HG22 H 1 1.089 0.008 . 1 . . . . . . . . 5248 1 92 . 1 1 22 22 VAL HG23 H 1 1.089 0.008 . 1 . . . . . . . . 5248 1 93 . 1 1 23 23 TYR H H 1 8.761 0.008 . . . . . . . . . . 5248 1 94 . 1 1 23 23 TYR HA H 1 4.936 0.006 . . . . . . . . . . 5248 1 95 . 1 1 23 23 TYR HB2 H 1 2.569 0.004 . . . . . . . . . . 5248 1 96 . 1 1 23 23 TYR HB3 H 1 3.013 0.014 . . . . . . . . . . 5248 1 97 . 1 1 23 23 TYR HD1 H 1 6.924 0.006 . . . . . . . . . . 5248 1 98 . 1 1 23 23 TYR HE1 H 1 6.468 0.004 . . . . . . . . . . 5248 1 99 . 1 1 23 23 TYR HE2 H 1 6.939 0.011 . . . . . . . . . . 5248 1 100 . 1 1 23 23 TYR HD2 H 1 8.199 0.002 . . . . . . . . . . 5248 1 101 . 1 1 24 24 TYR H H 1 9.100 0.006 . . . . . . . . . . 5248 1 102 . 1 1 24 24 TYR HA H 1 5.302 0.007 . . . . . . . . . . 5248 1 103 . 1 1 24 24 TYR HB2 H 1 2.921 0.007 . . . . . . . . . . 5248 1 104 . 1 1 24 24 TYR HB3 H 1 2.678 0.012 . . . . . . . . . . 5248 1 105 . 1 1 24 24 TYR HD1 H 1 6.853 0.007 . . . . . . . . . . 5248 1 106 . 1 1 24 24 TYR HE1 H 1 6.790 0.006 . . . . . . . . . . 5248 1 107 . 1 1 24 24 TYR HE2 H 1 7.529 0.000 . . . . . . . . . . 5248 1 108 . 1 1 25 25 PHE H H 1 9.451 0.009 . . . . . . . . . . 5248 1 109 . 1 1 25 25 PHE HA H 1 5.687 0.009 . . . . . . . . . . 5248 1 110 . 1 1 25 25 PHE HB2 H 1 2.593 0.009 . . . . . . . . . . 5248 1 111 . 1 1 25 25 PHE HB3 H 1 2.955 0.005 . . . . . . . . . . 5248 1 112 . 1 1 25 25 PHE HZ H 1 7.340 0.009 . . . . . . . . . . 5248 1 113 . 1 1 26 26 ASN H H 1 8.267 0.009 . . . . . . . . . . 5248 1 114 . 1 1 26 26 ASN HA H 1 4.392 0.006 . . . . . . . . . . 5248 1 115 . 1 1 26 26 ASN HB2 H 1 2.026 0.009 . . . . . . . . . . 5248 1 116 . 1 1 26 26 ASN HB3 H 1 -0.682 0.010 . . . . . . . . . . 5248 1 117 . 1 1 26 26 ASN HD21 H 1 6.668 0.004 . . . . . . . . . . 5248 1 118 . 1 1 26 26 ASN HD22 H 1 4.223 0.002 . . . . . . . . . . 5248 1 119 . 1 1 27 27 HIS H H 1 8.238 0.004 . . . . . . . . . . 5248 1 120 . 1 1 27 27 HIS HA H 1 4.174 0.014 . . . . . . . . . . 5248 1 121 . 1 1 27 27 HIS HB2 H 1 3.415 0.020 . . . . . . . . . . 5248 1 122 . 1 1 27 27 HIS HB3 H 1 3.158 0.009 . . . . . . . . . . 5248 1 123 . 1 1 27 27 HIS HD1 H 1 7.168 0.011 . . . . . . . . . . 5248 1 124 . 1 1 27 27 HIS HD2 H 1 7.129 0.056 . . . . . . . . . . 5248 1 125 . 1 1 27 27 HIS HE1 H 1 8.299 0.038 . . . . . . . . . . 5248 1 126 . 1 1 28 28 ILE H H 1 8.415 0.007 . . . . . . . . . . 5248 1 127 . 1 1 28 28 ILE HA H 1 3.864 0.009 . . . . . . . . . . 5248 1 128 . 1 1 28 28 ILE HB H 1 2.029 0.006 . . . . . . . . . . 5248 1 129 . 1 1 28 28 ILE HG21 H 1 0.790 0.006 . 1 . . . . . . . . 5248 1 130 . 1 1 28 28 ILE HG22 H 1 0.790 0.006 . 1 . . . . . . . . 5248 1 131 . 1 1 28 28 ILE HG23 H 1 0.790 0.006 . 1 . . . . . . . . 5248 1 132 . 1 1 28 28 ILE HG12 H 1 1.286 0.004 . . . . . . . . . . 5248 1 133 . 1 1 28 28 ILE HG13 H 1 0.988 0.010 . . . . . . . . . . 5248 1 134 . 1 1 28 28 ILE HD11 H 1 0.753 0.007 . 1 . . . . . . . . 5248 1 135 . 1 1 28 28 ILE HD12 H 1 0.753 0.007 . 1 . . . . . . . . 5248 1 136 . 1 1 28 28 ILE HD13 H 1 0.753 0.007 . 1 . . . . . . . . 5248 1 137 . 1 1 29 29 THR H H 1 7.372 0.005 . . . . . . . . . . 5248 1 138 . 1 1 29 29 THR HA H 1 4.117 0.007 . . . . . . . . . . 5248 1 139 . 1 1 29 29 THR HB H 1 4.261 0.008 . . . . . . . . . . 5248 1 140 . 1 1 29 29 THR HG21 H 1 0.959 0.004 . 1 . . . . . . . . 5248 1 141 . 1 1 29 29 THR HG22 H 1 0.959 0.004 . 1 . . . . . . . . 5248 1 142 . 1 1 29 29 THR HG23 H 1 0.959 0.004 . 1 . . . . . . . . 5248 1 143 . 1 1 30 30 ASN H H 1 8.111 0.007 . . . . . . . . . . 5248 1 144 . 1 1 30 30 ASN HA H 1 4.157 0.007 . . . . . . . . . . 5248 1 145 . 1 1 30 30 ASN HB2 H 1 2.943 0.007 . . . . . . . . . . 5248 1 146 . 1 1 30 30 ASN HB3 H 1 3.161 0.009 . . . . . . . . . . 5248 1 147 . 1 1 30 30 ASN HD21 H 1 6.947 0.000 . . . . . . . . . . 5248 1 148 . 1 1 30 30 ASN HD22 H 1 7.583 0.000 . . . . . . . . . . 5248 1 149 . 1 1 31 31 ALA H H 1 7.173 0.006 . . . . . . . . . . 5248 1 150 . 1 1 31 31 ALA HA H 1 4.460 0.009 . . . . . . . . . . 5248 1 151 . 1 1 31 31 ALA HB1 H 1 1.267 0.005 . 1 . . . . . . . . 5248 1 152 . 1 1 31 31 ALA HB2 H 1 1.267 0.005 . 1 . . . . . . . . 5248 1 153 . 1 1 31 31 ALA HB3 H 1 1.267 0.005 . 1 . . . . . . . . 5248 1 154 . 1 1 32 32 SER H H 1 8.440 0.006 . . . . . . . . . . 5248 1 155 . 1 1 32 32 SER HA H 1 6.071 0.004 . . . . . . . . . . 5248 1 156 . 1 1 32 32 SER HB2 H 1 3.742 0.003 . . . . . . . . . . 5248 1 157 . 1 1 32 32 SER HB3 H 1 3.838 0.009 . . . . . . . . . . 5248 1 158 . 1 1 33 33 GLN H H 1 9.428 0.006 . . . . . . . . . . 5248 1 159 . 1 1 33 33 GLN HA H 1 4.865 0.011 . . . . . . . . . . 5248 1 160 . 1 1 33 33 GLN HB2 H 1 2.234 0.006 . . . . . . . . . . 5248 1 161 . 1 1 33 33 GLN HB3 H 1 2.536 0.011 . . . . . . . . . . 5248 1 162 . 1 1 33 33 GLN HE21 H 1 6.788 0.001 . . . . . . . . . . 5248 1 163 . 1 1 33 33 GLN HE22 H 1 7.517 0.000 . . . . . . . . . . 5248 1 164 . 1 1 34 34 TRP H H 1 8.494 0.014 . . . . . . . . . . 5248 1 165 . 1 1 34 34 TRP HA H 1 5.002 0.007 . . . . . . . . . . 5248 1 166 . 1 1 34 34 TRP HB2 H 1 3.217 0.006 . . . . . . . . . . 5248 1 167 . 1 1 34 34 TRP HB3 H 1 3.642 0.007 . . . . . . . . . . 5248 1 168 . 1 1 34 34 TRP HD1 H 1 7.504 0.005 . . . . . . . . . . 5248 1 169 . 1 1 34 34 TRP HE3 H 1 8.198 0.004 . . . . . . . . . . 5248 1 170 . 1 1 34 34 TRP HE1 H 1 10.211 0.004 . . . . . . . . . . 5248 1 171 . 1 1 34 34 TRP HZ3 H 1 6.938 0.007 . . . . . . . . . . 5248 1 172 . 1 1 34 34 TRP HZ2 H 1 7.399 0.004 . . . . . . . . . . 5248 1 173 . 1 1 34 34 TRP HH2 H 1 7.114 0.006 . . . . . . . . . . 5248 1 174 . 1 1 35 35 GLU H H 1 8.156 0.005 . . . . . . . . . . 5248 1 175 . 1 1 35 35 GLU HA H 1 4.422 0.013 . . . . . . . . . . 5248 1 176 . 1 1 35 35 GLU HG2 H 1 2.272 0.008 . . . . . . . . . . 5248 1 177 . 1 1 35 35 GLU HG3 H 1 2.349 0.014 . . . . . . . . . . 5248 1 178 . 1 1 36 36 ARG H H 1 8.677 0.003 . . . . . . . . . . 5248 1 179 . 1 1 36 36 ARG HA H 1 2.627 0.009 . . . . . . . . . . 5248 1 180 . 1 1 36 36 ARG HG2 H 1 0.914 0.018 . . . . . . . . . . 5248 1 181 . 1 1 36 36 ARG HG3 H 1 1.224 0.008 . . . . . . . . . . 5248 1 182 . 1 1 36 36 ARG HE H 1 7.465 0.021 . . . . . . . . . . 5248 1 183 . 1 1 37 37 PRO HA H 1 3.938 0.009 . . . . . . . . . . 5248 1 184 . 1 1 37 37 PRO HB2 H 1 0.789 0.008 . . . . . . . . . . 5248 1 185 . 1 1 37 37 PRO HB3 H 1 0.897 0.014 . . . . . . . . . . 5248 1 186 . 1 1 37 37 PRO HG2 H 1 -0.070 0.003 . . . . . . . . . . 5248 1 187 . 1 1 37 37 PRO HG3 H 1 0.567 0.045 . . . . . . . . . . 5248 1 188 . 1 1 37 37 PRO HD2 H 1 2.515 0.009 . . . . . . . . . . 5248 1 189 . 1 1 37 37 PRO HD3 H 1 2.300 0.010 . . . . . . . . . . 5248 1 190 . 1 1 38 38 SER H H 1 8.070 0.005 . . . . . . . . . . 5248 1 191 . 1 1 38 38 SER HA H 1 4.711 0.005 . . . . . . . . . . 5248 1 192 . 1 1 38 38 SER HB2 H 1 3.894 0.016 . . . . . . . . . . 5248 1 193 . 1 1 38 38 SER HB3 H 1 4.019 0.007 . . . . . . . . . . 5248 1 194 . 1 1 39 39 GLY H H 1 8.059 0.009 . . . . . . . . . . 5248 1 195 . 1 1 39 39 GLY HA2 H 1 3.830 0.016 . . . . . . . . . . 5248 1 196 . 1 1 39 39 GLY HA3 H 1 3.745 0.007 . . . . . . . . . . 5248 1 stop_ save_