data_4882 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4882 _Entry.Title ; 1H NMR Study on the Binding of Pin1 Trp-trp domain with Phosphothreonine Peptides ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2000-10-25 _Entry.Accession_date 2000-10-25 _Entry.Last_release_date 2001-07-11 _Entry.Original_release_date 2001-07-11 _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 Rene Wintjens . . . 4882 2 Jean-Michel Wieruszeski . . . 4882 3 Herve Drobecq . . . 4882 4 Pierre Rousselot-Pailley . . . 4882 5 Guy Lippens . . . 4882 6 Isabelle Landrieu . . . 4882 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4882 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 260 4882 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 . . 2001-07-11 2000-10-25 original author . 4882 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4882 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 21326075 _Citation.DOI . _Citation.PubMed_ID 11313338 _Citation.Full_citation . _Citation.Title '1H NMR Study on the Binding of Pin1 Trp-trp domain with Phosphothreonine Peptides' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full . _Citation.Journal_volume 276 _Citation.Journal_issue 27 _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 25150 _Citation.Page_last 25156 _Citation.Year 2001 _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 Rene Wintjens . . . 4882 1 2 Jean-Michel Wieruszeski . . . 4882 1 3 Herve Drobecq . . . 4882 1 4 Pierre Rousselot-Pailley . . . 4882 1 5 L. Buee . . . 4882 1 6 Guy Lippens . . . 4882 1 7 Isabelle Landrieu . . . 4882 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_WW_domain _Assembly.Sf_category assembly _Assembly.Sf_framecode system_WW_domain _Assembly.Entry_ID 4882 _Assembly.ID 1 _Assembly.Name 'Pin1 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 4882 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 'WW domain' 1 $WW_domain . . . native . . . . . 4882 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Pin1 WW domain' system 4882 1 'WW domain' abbreviation 4882 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_WW_domain _Entity.Sf_category entity _Entity.Sf_framecode WW_domain _Entity.Entry_ID 4882 _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 ; KLPPGWEKRMSRSSGRVYYF NHITNASQWERPSGNSSSG ; _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 2015-01-29 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 7.70e-16 . . . . 4882 1 2 no BMRB 16088 . Pin1_WW . . . . . 87.18 36 100.00 100.00 7.70e-16 . . . . 4882 1 3 no BMRB 17545 . "first domain of human PIN1" . . . . . 92.31 36 100.00 100.00 3.89e-17 . . . . 4882 1 4 no BMRB 19258 . entity . . . . . 87.18 43 100.00 100.00 4.74e-16 . . . . 4882 1 5 no BMRB 19259 . Pin1 . . . . . 87.18 43 97.06 97.06 1.42e-15 . . . . 4882 1 6 no BMRB 5248 . Pin1_WW_Domain . . . . . 87.18 39 100.00 100.00 4.35e-16 . . . . 4882 1 7 no BMRB 5305 . Pin1 . . . . . 100.00 183 100.00 100.00 1.14e-18 . . . . 4882 1 8 no PDB 1F8A . "Structural Basis For The Phosphoserine-proline Recognition By Group Iv Ww Domains" . . . . . 100.00 167 100.00 100.00 7.94e-19 . . . . 4882 1 9 no PDB 1I6C . "Solution Structure Of Pin1 Ww Domain" . . . . . 100.00 39 100.00 100.00 7.73e-19 . . . . 4882 1 10 no PDB 1I8G . "Solution Structure Of Pin1 Ww Domain Complexed With Cdc25 Phosphothreonine Peptide" . . . . . 100.00 39 100.00 100.00 7.73e-19 . . . . 4882 1 11 no PDB 1I8H . "Solution Structure Of Pin1 Ww Domain Complexed With Human Tau Phosphothreonine Peptide" . . . . . 100.00 39 100.00 100.00 7.73e-19 . . . . 4882 1 12 no PDB 1NMV . "Solution Structure Of Human Pin1" . . . . . 100.00 163 100.00 100.00 6.93e-19 . . . . 4882 1 13 no PDB 1PIN . "Pin1 Peptidyl-prolyl Cis-trans Isomerase From Homo Sapiens" . . . . . 100.00 163 100.00 100.00 6.93e-19 . . . . 4882 1 14 no PDB 2ITK . "Human Pin1 Bound To D-Peptide" . . . . . 100.00 167 97.44 97.44 6.83e-18 . . . . 4882 1 15 no PDB 2KCF . "The Nmr Solution Structure Of The Isolated Apo Pin1 Ww Domain" . . . . . 87.18 36 100.00 100.00 7.70e-16 . . . . 4882 1 16 no PDB 2LB3 . "Structure Of The Ww Domain Of Pin1 In Complex With A Human Phosphorylated Smad3 Derived Peptide" . . . . . 92.31 36 100.00 100.00 3.89e-17 . . . . 4882 1 17 no PDB 2M8I . "Structure Of Pin1 Ww Domain" . . . . . 87.18 43 100.00 100.00 4.74e-16 . . . . 4882 1 18 no PDB 2M8J . "Structure Of Pin1 Ww Domain Phospho-mimic S16e" . . . . . 87.18 43 97.06 97.06 1.42e-15 . . . . 4882 1 19 no PDB 2Q5A . "Human Pin1 Bound To L-Peptide" . . . . . 100.00 167 97.44 97.44 6.83e-18 . . . . 4882 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 6.83e-18 . . . . 4882 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 6.83e-18 . . . . 4882 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 6.83e-18 . . . . 4882 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 6.28e-18 . . . . 4882 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 6.83e-18 . . . . 4882 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 6.83e-18 . . . . 4882 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 6.83e-18 . . . . 4882 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 6.83e-18 . . . . 4882 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 6.83e-18 . . . . 4882 1 29 no PDB 2ZQS . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 100.00 100.00 6.37e-19 . . . . 4882 1 30 no PDB 2ZQT . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 100.00 100.00 6.44e-19 . . . . 4882 1 31 no PDB 2ZQU . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 97.44 97.44 1.51e-17 . . . . 4882 1 32 no PDB 2ZQV . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 97.44 97.44 1.15e-17 . . . . 4882 1 33 no PDB 2ZR4 . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 97.44 100.00 1.32e-18 . . . . 4882 1 34 no PDB 2ZR5 . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 100.00 100.00 6.78e-19 . . . . 4882 1 35 no PDB 2ZR6 . "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" . . . . . 100.00 163 97.44 97.44 5.98e-18 . . . . 4882 1 36 no PDB 3KAB . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 97.44 97.44 6.83e-18 . . . . 4882 1 37 no PDB 3KAD . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 97.44 97.44 6.28e-18 . . . . 4882 1 38 no PDB 3KAF . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 97.44 97.44 6.28e-18 . . . . 4882 1 39 no PDB 3KAG . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 97.44 97.44 6.83e-18 . . . . 4882 1 40 no PDB 3KAH . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 97.44 97.44 6.83e-18 . . . . 4882 1 41 no PDB 3KAI . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 97.44 97.44 6.83e-18 . . . . 4882 1 42 no PDB 3KCE . "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" . . . . . 100.00 167 97.44 97.44 6.83e-18 . . . . 4882 1 43 no PDB 3NTP . "Human Pin1 Complexed With Reduced Amide Inhibitor" . . . . . 100.00 167 97.44 97.44 6.83e-18 . . . . 4882 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 6.83e-18 . . . . 4882 1 45 no PDB 3OOB . "Structural And Functional Insights Of Directly Targeting Pin1 By Epigallocatechin-3-Gallate" . . . . . 100.00 163 97.44 97.44 5.98e-18 . . . . 4882 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 6.44e-18 . . . . 4882 1 47 no PDB 3TCZ . "Human Pin1 Bound To Cis Peptidomimetic Inhibitor" . . . . . 100.00 158 97.44 97.44 6.41e-18 . . . . 4882 1 48 no PDB 3TDB . "Human Pin1 Bound To Trans Peptidomimetic Inhibitor" . . . . . 100.00 158 97.44 97.44 6.41e-18 . . . . 4882 1 49 no PDB 3WH0 . "Structure Of Pin1 Complex With 18-crown-6" . . . . . 100.00 163 97.44 97.44 5.98e-18 . . . . 4882 1 50 no PDB 4GWT . "Structure Of Racemic Pin1 Ww Domain Cocrystallized With Dl-malic Acid" . . . . . 87.18 36 100.00 100.00 7.70e-16 . . . . 4882 1 51 no PDB 4GWV . "Structure Of Racemic Pin1 Ww Domain Cocrystallized With Tri-ammonium Citrate" . . . . . 87.18 36 100.00 100.00 7.70e-16 . . . . 4882 1 52 no DBJ BAA87037 . "PIN1 [Mus sp.]" . . . . . 82.05 165 100.00 100.00 1.43e-14 . . . . 4882 1 53 no DBJ BAA87038 . "PIN1 [Mus sp.]" . . . . . 82.05 165 100.00 100.00 1.43e-14 . . . . 4882 1 54 no DBJ BAB22270 . "unnamed protein product [Mus musculus]" . . . . . 82.05 165 100.00 100.00 1.43e-14 . . . . 4882 1 55 no DBJ BAB22743 . "unnamed protein product [Mus musculus]" . . . . . 82.05 165 100.00 100.00 1.43e-14 . . . . 4882 1 56 no DBJ BAC35631 . "unnamed protein product [Mus musculus]" . . . . . 82.05 165 100.00 100.00 1.43e-14 . . . . 4882 1 57 no EMBL CAG28582 . "UBL5 [Homo sapiens]" . . . . . 100.00 163 100.00 100.00 6.93e-19 . . . . 4882 1 58 no GB AAC50492 . "Pin1 [Homo sapiens]" . . . . . 100.00 163 100.00 100.00 6.93e-19 . . . . 4882 1 59 no GB AAH02899 . "Peptidylprolyl cis/trans isomerase, NIMA-interacting 1 [Homo sapiens]" . . . . . 100.00 163 100.00 100.00 6.93e-19 . . . . 4882 1 60 no GB AAH38254 . "Protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1 [Mus musculus]" . . . . . 82.05 165 100.00 100.00 1.43e-14 . . . . 4882 1 61 no GB AAI12584 . "Peptidylprolyl cis/trans isomerase, NIMA-interacting 1 [Bos taurus]" . . . . . 94.87 163 100.00 100.00 1.22e-17 . . . . 4882 1 62 no GB AAV38138 . "protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1 [Homo sapiens]" . . . . . 100.00 163 100.00 100.00 6.93e-19 . . . . 4882 1 63 no PRF 2209428A . "peptidyl-Pro isomerase" . . . . . 100.00 163 100.00 100.00 6.93e-19 . . . . 4882 1 64 no REF NP_001029804 . "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Bos taurus]" . . . . . 94.87 163 100.00 100.00 1.22e-17 . . . . 4882 1 65 no REF NP_001231300 . "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Sus scrofa]" . . . . . 100.00 163 97.44 97.44 2.81e-18 . . . . 4882 1 66 no REF NP_001270625 . "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Macaca fascicularis]" . . . . . 100.00 163 97.44 97.44 4.85e-18 . . . . 4882 1 67 no REF NP_006212 . "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Homo sapiens]" . . . . . 100.00 163 100.00 100.00 6.93e-19 . . . . 4882 1 68 no REF NP_075860 . "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Mus musculus]" . . . . . 82.05 165 100.00 100.00 1.43e-14 . . . . 4882 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 6.93e-19 . . . . 4882 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 4.85e-18 . . . . 4882 1 71 no SP Q5BIN5 . "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" . . . . . 94.87 163 100.00 100.00 1.22e-17 . . . . 4882 1 72 no SP Q9QUR7 . "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" . . . . . 82.05 165 100.00 100.00 1.43e-14 . . . . 4882 1 73 no TPG DAA28013 . "TPA: peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Bos taurus]" . . . . . 94.87 163 100.00 100.00 1.22e-17 . . . . 4882 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 4882 1 'WW domain' abbreviation 4882 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 . LYS . 4882 1 2 . LEU . 4882 1 3 . PRO . 4882 1 4 . PRO . 4882 1 5 . GLY . 4882 1 6 . TRP . 4882 1 7 . GLU . 4882 1 8 . LYS . 4882 1 9 . ARG . 4882 1 10 . MET . 4882 1 11 . SER . 4882 1 12 . ARG . 4882 1 13 . SER . 4882 1 14 . SER . 4882 1 15 . GLY . 4882 1 16 . ARG . 4882 1 17 . VAL . 4882 1 18 . TYR . 4882 1 19 . TYR . 4882 1 20 . PHE . 4882 1 21 . ASN . 4882 1 22 . HIS . 4882 1 23 . ILE . 4882 1 24 . THR . 4882 1 25 . ASN . 4882 1 26 . ALA . 4882 1 27 . SER . 4882 1 28 . GLN . 4882 1 29 . TRP . 4882 1 30 . GLU . 4882 1 31 . ARG . 4882 1 32 . PRO . 4882 1 33 . SER . 4882 1 34 . GLY . 4882 1 35 . ASN . 4882 1 36 . SER . 4882 1 37 . SER . 4882 1 38 . SER . 4882 1 39 . GLY . 4882 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 . LYS 1 1 4882 1 . LEU 2 2 4882 1 . PRO 3 3 4882 1 . PRO 4 4 4882 1 . GLY 5 5 4882 1 . TRP 6 6 4882 1 . GLU 7 7 4882 1 . LYS 8 8 4882 1 . ARG 9 9 4882 1 . MET 10 10 4882 1 . SER 11 11 4882 1 . ARG 12 12 4882 1 . SER 13 13 4882 1 . SER 14 14 4882 1 . GLY 15 15 4882 1 . ARG 16 16 4882 1 . VAL 17 17 4882 1 . TYR 18 18 4882 1 . TYR 19 19 4882 1 . PHE 20 20 4882 1 . ASN 21 21 4882 1 . HIS 22 22 4882 1 . ILE 23 23 4882 1 . THR 24 24 4882 1 . ASN 25 25 4882 1 . ALA 26 26 4882 1 . SER 27 27 4882 1 . GLN 28 28 4882 1 . TRP 29 29 4882 1 . GLU 30 30 4882 1 . ARG 31 31 4882 1 . PRO 32 32 4882 1 . SER 33 33 4882 1 . GLY 34 34 4882 1 . ASN 35 35 4882 1 . SER 36 36 4882 1 . SER 37 37 4882 1 . SER 38 38 4882 1 . GLY 39 39 4882 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 4882 _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 $WW_domain . 9606 . . 'Homo sapiens' human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 4882 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 4882 _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 $WW_domain . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4882 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4882 _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 $WW_domain . . 1.0 . . mM . . . . 4882 1 stop_ save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-cond_1 _Sample_condition_list.Entry_ID 4882 _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 pD 6.4 0.1 n/a 4882 1 temperature 285 1 K 4882 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 4882 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4882 _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 Bruker DMX . 600 . . . 4882 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 4882 _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 '1H TOCY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4882 1 2 '1H NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4882 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 4882 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '1H TOCY' _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 4882 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '1H 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 4882 _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 TSP 'methyl protons' . . . . ppm 0.00 internal direct . internal cylindrical . . . . . . . 4882 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_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode set_1 _Assigned_chem_shift_list.Entry_ID 4882 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-cond_1 _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 '1H TOCY' 1 $sample_1 . 4882 1 2 '1H NOESY' 1 $sample_1 . 4882 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 LYS HA H 1 4.18 0.02 . 1 . . . . . . . . 4882 1 2 . 1 1 1 1 LYS HB2 H 1 1.99 0.02 . 1 . . . . . . . . 4882 1 3 . 1 1 1 1 LYS HB3 H 1 1.99 0.02 . 1 . . . . . . . . 4882 1 4 . 1 1 1 1 LYS HG2 H 1 1.54 0.02 . 1 . . . . . . . . 4882 1 5 . 1 1 1 1 LYS HG3 H 1 1.61 0.02 . 1 . . . . . . . . 4882 1 6 . 1 1 1 1 LYS HD2 H 1 1.80 0.02 . 1 . . . . . . . . 4882 1 7 . 1 1 1 1 LYS HD3 H 1 1.80 0.02 . 1 . . . . . . . . 4882 1 8 . 1 1 1 1 LYS HE2 H 1 3.10 0.02 . 1 . . . . . . . . 4882 1 9 . 1 1 1 1 LYS HE3 H 1 3.10 0.02 . 1 . . . . . . . . 4882 1 10 . 1 1 2 2 LEU H H 1 8.86 0.02 . 1 . . . . . . . . 4882 1 11 . 1 1 2 2 LEU HA H 1 4.67 0.02 . 1 . . . . . . . . 4882 1 12 . 1 1 2 2 LEU HB2 H 1 1.89 0.02 . 1 . . . . . . . . 4882 1 13 . 1 1 2 2 LEU HB3 H 1 1.49 0.02 . 1 . . . . . . . . 4882 1 14 . 1 1 2 2 LEU HG H 1 2.00 0.02 . 1 . . . . . . . . 4882 1 15 . 1 1 2 2 LEU HD11 H 1 1.13 0.02 . 1 . . . . . . . . 4882 1 16 . 1 1 2 2 LEU HD12 H 1 1.13 0.02 . 1 . . . . . . . . 4882 1 17 . 1 1 2 2 LEU HD13 H 1 1.13 0.02 . 1 . . . . . . . . 4882 1 18 . 1 1 2 2 LEU HD21 H 1 0.86 0.02 . 1 . . . . . . . . 4882 1 19 . 1 1 2 2 LEU HD22 H 1 0.86 0.02 . 1 . . . . . . . . 4882 1 20 . 1 1 2 2 LEU HD23 H 1 0.86 0.02 . 1 . . . . . . . . 4882 1 21 . 1 1 3 3 PRO HA H 1 4.66 0.02 . 1 . . . . . . . . 4882 1 22 . 1 1 3 3 PRO HB2 H 1 2.67 0.02 . 1 . . . . . . . . 4882 1 23 . 1 1 3 3 PRO HB3 H 1 2.67 0.02 . 1 . . . . . . . . 4882 1 24 . 1 1 3 3 PRO HG2 H 1 1.86 0.02 . 1 . . . . . . . . 4882 1 25 . 1 1 3 3 PRO HG3 H 1 1.72 0.02 . 1 . . . . . . . . 4882 1 26 . 1 1 3 3 PRO HD2 H 1 3.75 0.02 . 1 . . . . . . . . 4882 1 27 . 1 1 3 3 PRO HD3 H 1 3.09 0.02 . 1 . . . . . . . . 4882 1 28 . 1 1 4 4 PRO HA H 1 4.42 0.02 . 1 . . . . . . . . 4882 1 29 . 1 1 4 4 PRO HB2 H 1 2.39 0.02 . 1 . . . . . . . . 4882 1 30 . 1 1 4 4 PRO HB3 H 1 1.91 0.02 . 1 . . . . . . . . 4882 1 31 . 1 1 4 4 PRO HG2 H 1 2.10 0.02 . 1 . . . . . . . . 4882 1 32 . 1 1 4 4 PRO HG3 H 1 2.20 0.02 . 1 . . . . . . . . 4882 1 33 . 1 1 4 4 PRO HD2 H 1 3.71 0.02 . 1 . . . . . . . . 4882 1 34 . 1 1 4 4 PRO HD3 H 1 3.99 0.02 . 1 . . . . . . . . 4882 1 35 . 1 1 5 5 GLY H H 1 8.83 0.02 . 1 . . . . . . . . 4882 1 36 . 1 1 5 5 GLY HA2 H 1 4.09 0.02 . 1 . . . . . . . . 4882 1 37 . 1 1 5 5 GLY HA3 H 1 3.23 0.02 . 1 . . . . . . . . 4882 1 38 . 1 1 6 6 TRP H H 1 7.44 0.02 . 1 . . . . . . . . 4882 1 39 . 1 1 6 6 TRP HA H 1 5.24 0.02 . 1 . . . . . . . . 4882 1 40 . 1 1 6 6 TRP HB2 H 1 3.00 0.02 . 1 . . . . . . . . 4882 1 41 . 1 1 6 6 TRP HB3 H 1 3.28 0.02 . 1 . . . . . . . . 4882 1 42 . 1 1 6 6 TRP HD1 H 1 7.01 0.02 . 1 . . . . . . . . 4882 1 43 . 1 1 6 6 TRP HE1 H 1 10.57 0.02 . 1 . . . . . . . . 4882 1 44 . 1 1 6 6 TRP HE3 H 1 7.42 0.02 . 1 . . . . . . . . 4882 1 45 . 1 1 6 6 TRP HZ2 H 1 7.47 0.02 . 1 . . . . . . . . 4882 1 46 . 1 1 6 6 TRP HZ3 H 1 7.03 0.02 . 1 . . . . . . . . 4882 1 47 . 1 1 6 6 TRP HH2 H 1 7.05 0.02 . 1 . . . . . . . . 4882 1 48 . 1 1 7 7 GLU H H 1 9.83 0.02 . 1 . . . . . . . . 4882 1 49 . 1 1 7 7 GLU HA H 1 4.91 0.02 . 1 . . . . . . . . 4882 1 50 . 1 1 7 7 GLU HB2 H 1 2.28 0.02 . 1 . . . . . . . . 4882 1 51 . 1 1 7 7 GLU HB3 H 1 2.37 0.02 . 1 . . . . . . . . 4882 1 52 . 1 1 7 7 GLU HG2 H 1 2.62 0.02 . 1 . . . . . . . . 4882 1 53 . 1 1 7 7 GLU HG3 H 1 2.62 0.02 . 1 . . . . . . . . 4882 1 54 . 1 1 8 8 LYS H H 1 8.98 0.02 . 1 . . . . . . . . 4882 1 55 . 1 1 8 8 LYS HA H 1 4.45 0.02 . 1 . . . . . . . . 4882 1 56 . 1 1 8 8 LYS HB2 H 1 1.83 0.02 . 1 . . . . . . . . 4882 1 57 . 1 1 8 8 LYS HB3 H 1 1.83 0.02 . 1 . . . . . . . . 4882 1 58 . 1 1 8 8 LYS HG2 H 1 1.13 0.02 . 1 . . . . . . . . 4882 1 59 . 1 1 8 8 LYS HG3 H 1 1.13 0.02 . 1 . . . . . . . . 4882 1 60 . 1 1 8 8 LYS HD2 H 1 1.69 0.02 . 1 . . . . . . . . 4882 1 61 . 1 1 8 8 LYS HD3 H 1 1.69 0.02 . 1 . . . . . . . . 4882 1 62 . 1 1 8 8 LYS HE2 H 1 3.01 0.02 . 1 . . . . . . . . 4882 1 63 . 1 1 8 8 LYS HE3 H 1 3.01 0.02 . 1 . . . . . . . . 4882 1 64 . 1 1 9 9 ARG H H 1 8.90 0.02 . 1 . . . . . . . . 4882 1 65 . 1 1 9 9 ARG HA H 1 4.45 0.02 . 1 . . . . . . . . 4882 1 66 . 1 1 9 9 ARG HB2 H 1 0.10 0.02 . 1 . . . . . . . . 4882 1 67 . 1 1 9 9 ARG HB3 H 1 0.10 0.02 . 1 . . . . . . . . 4882 1 68 . 1 1 9 9 ARG HG2 H 1 1.29 0.02 . 1 . . . . . . . . 4882 1 69 . 1 1 9 9 ARG HG3 H 1 1.47 0.02 . 1 . . . . . . . . 4882 1 70 . 1 1 9 9 ARG HD2 H 1 2.98 0.02 . 1 . . . . . . . . 4882 1 71 . 1 1 9 9 ARG HD3 H 1 2.69 0.02 . 1 . . . . . . . . 4882 1 72 . 1 1 9 9 ARG HE H 1 7.02 0.02 . 1 . . . . . . . . 4882 1 73 . 1 1 10 10 MET H H 1 8.28 0.02 . 1 . . . . . . . . 4882 1 74 . 1 1 10 10 MET HA H 1 5.00 0.02 . 1 . . . . . . . . 4882 1 75 . 1 1 10 10 MET HB2 H 1 2.33 0.02 . 1 . . . . . . . . 4882 1 76 . 1 1 10 10 MET HB3 H 1 2.33 0.02 . 1 . . . . . . . . 4882 1 77 . 1 1 10 10 MET HG2 H 1 2.49 0.02 . 1 . . . . . . . . 4882 1 78 . 1 1 10 10 MET HG3 H 1 2.49 0.02 . 1 . . . . . . . . 4882 1 79 . 1 1 10 10 MET HE1 H 1 1.92 0.02 . 1 . . . . . . . . 4882 1 80 . 1 1 10 10 MET HE2 H 1 1.92 0.02 . 1 . . . . . . . . 4882 1 81 . 1 1 10 10 MET HE3 H 1 1.92 0.02 . 1 . . . . . . . . 4882 1 82 . 1 1 11 11 SER H H 1 9.12 0.02 . 1 . . . . . . . . 4882 1 83 . 1 1 11 11 SER HA H 1 4.78 0.02 . 1 . . . . . . . . 4882 1 84 . 1 1 11 11 SER HB2 H 1 4.33 0.02 . 1 . . . . . . . . 4882 1 85 . 1 1 11 11 SER HB3 H 1 4.22 0.02 . 1 . . . . . . . . 4882 1 86 . 1 1 12 12 ARG H H 1 9.27 0.02 . 1 . . . . . . . . 4882 1 87 . 1 1 12 12 ARG HA H 1 4.20 0.02 . 1 . . . . . . . . 4882 1 88 . 1 1 12 12 ARG HB2 H 1 1.85 0.02 . 1 . . . . . . . . 4882 1 89 . 1 1 12 12 ARG HB3 H 1 1.78 0.02 . 1 . . . . . . . . 4882 1 90 . 1 1 12 12 ARG HG2 H 1 1.98 0.02 . 1 . . . . . . . . 4882 1 91 . 1 1 12 12 ARG HG3 H 1 1.98 0.02 . 1 . . . . . . . . 4882 1 92 . 1 1 12 12 ARG HD2 H 1 3.27 0.02 . 1 . . . . . . . . 4882 1 93 . 1 1 12 12 ARG HD3 H 1 3.27 0.02 . 1 . . . . . . . . 4882 1 94 . 1 1 12 12 ARG HE H 1 7.30 0.02 . 1 . . . . . . . . 4882 1 95 . 1 1 13 13 SER H H 1 8.48 0.02 . 1 . . . . . . . . 4882 1 96 . 1 1 13 13 SER HA H 1 4.43 0.02 . 1 . . . . . . . . 4882 1 97 . 1 1 13 13 SER HB2 H 1 3.98 0.02 . 1 . . . . . . . . 4882 1 98 . 1 1 13 13 SER HB3 H 1 3.98 0.02 . 1 . . . . . . . . 4882 1 99 . 1 1 14 14 SER H H 1 7.95 0.02 . 1 . . . . . . . . 4882 1 100 . 1 1 14 14 SER HA H 1 4.62 0.02 . 1 . . . . . . . . 4882 1 101 . 1 1 14 14 SER HB2 H 1 3.32 0.02 . 1 . . . . . . . . 4882 1 102 . 1 1 14 14 SER HB3 H 1 3.27 0.02 . 1 . . . . . . . . 4882 1 103 . 1 1 15 15 GLY H H 1 8.19 0.02 . 1 . . . . . . . . 4882 1 104 . 1 1 15 15 GLY HA2 H 1 3.99 0.02 . 1 . . . . . . . . 4882 1 105 . 1 1 15 15 GLY HA3 H 1 4.16 0.02 . 1 . . . . . . . . 4882 1 106 . 1 1 16 16 ARG H H 1 7.75 0.02 . 1 . . . . . . . . 4882 1 107 . 1 1 16 16 ARG HA H 1 4.50 0.02 . 1 . . . . . . . . 4882 1 108 . 1 1 16 16 ARG HB2 H 1 2.00 0.02 . 1 . . . . . . . . 4882 1 109 . 1 1 16 16 ARG HB3 H 1 1.78 0.02 . 2 . . . . . . . . 4882 1 110 . 1 1 16 16 ARG HG2 H 1 1.78 0.02 . 2 . . . . . . . . 4882 1 111 . 1 1 16 16 ARG HG3 H 1 1.73 0.02 . 1 . . . . . . . . 4882 1 112 . 1 1 16 16 ARG HD2 H 1 2.88 0.02 . 1 . . . . . . . . 4882 1 113 . 1 1 16 16 ARG HD3 H 1 2.53 0.02 . 1 . . . . . . . . 4882 1 114 . 1 1 16 16 ARG HE H 1 6.80 0.02 . 1 . . . . . . . . 4882 1 115 . 1 1 17 17 VAL H H 1 8.64 0.02 . 1 . . . . . . . . 4882 1 116 . 1 1 17 17 VAL HA H 1 4.73 0.02 . 1 . . . . . . . . 4882 1 117 . 1 1 17 17 VAL HB H 1 2.04 0.02 . 1 . . . . . . . . 4882 1 118 . 1 1 17 17 VAL HG11 H 1 1.08 0.02 . 1 . . . . . . . . 4882 1 119 . 1 1 17 17 VAL HG12 H 1 1.08 0.02 . 1 . . . . . . . . 4882 1 120 . 1 1 17 17 VAL HG13 H 1 1.08 0.02 . 1 . . . . . . . . 4882 1 121 . 1 1 17 17 VAL HG21 H 1 0.84 0.02 . 1 . . . . . . . . 4882 1 122 . 1 1 17 17 VAL HG22 H 1 0.84 0.02 . 1 . . . . . . . . 4882 1 123 . 1 1 17 17 VAL HG23 H 1 0.84 0.02 . 1 . . . . . . . . 4882 1 124 . 1 1 18 18 TYR H H 1 8.74 0.02 . 1 . . . . . . . . 4882 1 125 . 1 1 18 18 TYR HA H 1 4.96 0.02 . 1 . . . . . . . . 4882 1 126 . 1 1 18 18 TYR HB2 H 1 2.98 0.02 . 1 . . . . . . . . 4882 1 127 . 1 1 18 18 TYR HB3 H 1 2.56 0.02 . 1 . . . . . . . . 4882 1 128 . 1 1 18 18 TYR HD1 H 1 6.93 0.02 . 1 . . . . . . . . 4882 1 129 . 1 1 18 18 TYR HD2 H 1 6.93 0.02 . 1 . . . . . . . . 4882 1 130 . 1 1 18 18 TYR HE1 H 1 6.46 0.02 . 1 . . . . . . . . 4882 1 131 . 1 1 18 18 TYR HE2 H 1 6.46 0.02 . 1 . . . . . . . . 4882 1 132 . 1 1 19 19 TYR H H 1 9.06 0.02 . 1 . . . . . . . . 4882 1 133 . 1 1 19 19 TYR HA H 1 5.33 0.02 . 1 . . . . . . . . 4882 1 134 . 1 1 19 19 TYR HB2 H 1 2.98 0.02 . 1 . . . . . . . . 4882 1 135 . 1 1 19 19 TYR HB3 H 1 2.71 0.02 . 1 . . . . . . . . 4882 1 136 . 1 1 19 19 TYR HD1 H 1 6.88 0.02 . 1 . . . . . . . . 4882 1 137 . 1 1 19 19 TYR HD2 H 1 6.88 0.02 . 1 . . . . . . . . 4882 1 138 . 1 1 19 19 TYR HE1 H 1 6.80 0.02 . 1 . . . . . . . . 4882 1 139 . 1 1 19 19 TYR HE2 H 1 6.80 0.02 . 1 . . . . . . . . 4882 1 140 . 1 1 20 20 PHE H H 1 9.43 0.02 . 1 . . . . . . . . 4882 1 141 . 1 1 20 20 PHE HA H 1 5.70 0.02 . 1 . . . . . . . . 4882 1 142 . 1 1 20 20 PHE HB2 H 1 2.97 0.02 . 1 . . . . . . . . 4882 1 143 . 1 1 20 20 PHE HB3 H 1 2.57 0.02 . 1 . . . . . . . . 4882 1 144 . 1 1 20 20 PHE HD1 H 1 7.01 0.02 . 1 . . . . . . . . 4882 1 145 . 1 1 20 20 PHE HD2 H 1 7.01 0.02 . 1 . . . . . . . . 4882 1 146 . 1 1 20 20 PHE HE1 H 1 7.06 0.02 . 1 . . . . . . . . 4882 1 147 . 1 1 20 20 PHE HE2 H 1 7.06 0.02 . 1 . . . . . . . . 4882 1 148 . 1 1 20 20 PHE HZ H 1 7.37 0.02 . 1 . . . . . . . . 4882 1 149 . 1 1 21 21 ASN H H 1 8.23 0.02 . 1 . . . . . . . . 4882 1 150 . 1 1 21 21 ASN HA H 1 4.39 0.02 . 1 . . . . . . . . 4882 1 151 . 1 1 21 21 ASN HB2 H 1 -0.64 0.02 . 1 . . . . . . . . 4882 1 152 . 1 1 21 21 ASN HB3 H 1 2.05 0.02 . 1 . . . . . . . . 4882 1 153 . 1 1 21 21 ASN HD21 H 1 6.70 0.02 . 1 . . . . . . . . 4882 1 154 . 1 1 21 21 ASN HD22 H 1 4.23 0.02 . 1 . . . . . . . . 4882 1 155 . 1 1 22 22 HIS H H 1 8.23 0.02 . 1 . . . . . . . . 4882 1 156 . 1 1 22 22 HIS HA H 1 4.24 0.02 . 1 . . . . . . . . 4882 1 157 . 1 1 22 22 HIS HB2 H 1 3.23 0.02 . 1 . . . . . . . . 4882 1 158 . 1 1 22 22 HIS HB3 H 1 3.55 0.02 . 1 . . . . . . . . 4882 1 159 . 1 1 22 22 HIS HD2 H 1 7.04 0.02 . 1 . . . . . . . . 4882 1 160 . 1 1 22 22 HIS HE1 H 1 7.71 0.02 . 1 . . . . . . . . 4882 1 161 . 1 1 23 23 ILE H H 1 8.35 0.02 . 1 . . . . . . . . 4882 1 162 . 1 1 23 23 ILE HA H 1 3.92 0.02 . 1 . . . . . . . . 4882 1 163 . 1 1 23 23 ILE HB H 1 2.04 0.02 . 1 . . . . . . . . 4882 1 164 . 1 1 23 23 ILE HG12 H 1 1.00 0.02 . 1 . . . . . . . . 4882 1 165 . 1 1 23 23 ILE HG13 H 1 1.27 0.02 . 1 . . . . . . . . 4882 1 166 . 1 1 23 23 ILE HG21 H 1 0.79 0.02 . 4 . . . . . . . . 4882 1 167 . 1 1 23 23 ILE HG22 H 1 0.79 0.02 . 4 . . . . . . . . 4882 1 168 . 1 1 23 23 ILE HG23 H 1 0.79 0.02 . 4 . . . . . . . . 4882 1 169 . 1 1 23 23 ILE HD11 H 1 0.79 0.02 . 4 . . . . . . . . 4882 1 170 . 1 1 23 23 ILE HD12 H 1 0.79 0.02 . 4 . . . . . . . . 4882 1 171 . 1 1 23 23 ILE HD13 H 1 0.79 0.02 . 4 . . . . . . . . 4882 1 172 . 1 1 24 24 THR H H 1 7.35 0.02 . 1 . . . . . . . . 4882 1 173 . 1 1 24 24 THR HA H 1 4.29 0.02 . 1 . . . . . . . . 4882 1 174 . 1 1 24 24 THR HB H 1 4.14 0.02 . 1 . . . . . . . . 4882 1 175 . 1 1 24 24 THR HG21 H 1 0.98 0.02 . 1 . . . . . . . . 4882 1 176 . 1 1 24 24 THR HG22 H 1 0.98 0.02 . 1 . . . . . . . . 4882 1 177 . 1 1 24 24 THR HG23 H 1 0.98 0.02 . 1 . . . . . . . . 4882 1 178 . 1 1 25 25 ASN H H 1 8.10 0.02 . 1 . . . . . . . . 4882 1 179 . 1 1 25 25 ASN HA H 1 4.16 0.02 . 1 . . . . . . . . 4882 1 180 . 1 1 25 25 ASN HB2 H 1 3.17 0.02 . 1 . . . . . . . . 4882 1 181 . 1 1 25 25 ASN HB3 H 1 2.96 0.02 . 1 . . . . . . . . 4882 1 182 . 1 1 25 25 ASN HD21 H 1 7.52 0.02 . 1 . . . . . . . . 4882 1 183 . 1 1 25 25 ASN HD22 H 1 6.90 0.02 . 1 . . . . . . . . 4882 1 184 . 1 1 26 26 ALA H H 1 7.16 0.02 . 1 . . . . . . . . 4882 1 185 . 1 1 26 26 ALA HA H 1 4.48 0.02 . 1 . . . . . . . . 4882 1 186 . 1 1 26 26 ALA HB1 H 1 1.29 0.02 . 1 . . . . . . . . 4882 1 187 . 1 1 26 26 ALA HB2 H 1 1.29 0.02 . 1 . . . . . . . . 4882 1 188 . 1 1 26 26 ALA HB3 H 1 1.29 0.02 . 1 . . . . . . . . 4882 1 189 . 1 1 27 27 SER H H 1 8.37 0.02 . 1 . . . . . . . . 4882 1 190 . 1 1 27 27 SER HA H 1 6.05 0.02 . 1 . . . . . . . . 4882 1 191 . 1 1 27 27 SER HB2 H 1 3.77 0.02 . 1 . . . . . . . . 4882 1 192 . 1 1 27 27 SER HB3 H 1 3.85 0.02 . 1 . . . . . . . . 4882 1 193 . 1 1 28 28 GLN H H 1 9.41 0.02 . 1 . . . . . . . . 4882 1 194 . 1 1 28 28 GLN HA H 1 4.89 0.02 . 1 . . . . . . . . 4882 1 195 . 1 1 28 28 GLN HB2 H 1 2.56 0.02 . 1 . . . . . . . . 4882 1 196 . 1 1 28 28 GLN HB3 H 1 2.56 0.02 . 1 . . . . . . . . 4882 1 197 . 1 1 28 28 GLN HG2 H 1 2.65 0.02 . 1 . . . . . . . . 4882 1 198 . 1 1 28 28 GLN HG3 H 1 2.65 0.02 . 1 . . . . . . . . 4882 1 199 . 1 1 28 28 GLN HE21 H 1 6.75 0.02 . 1 . . . . . . . . 4882 1 200 . 1 1 28 28 GLN HE22 H 1 7.51 0.02 . 1 . . . . . . . . 4882 1 201 . 1 1 29 29 TRP H H 1 8.54 0.02 . 1 . . . . . . . . 4882 1 202 . 1 1 29 29 TRP HA H 1 5.00 0.02 . 1 . . . . . . . . 4882 1 203 . 1 1 29 29 TRP HB2 H 1 3.25 0.02 . 1 . . . . . . . . 4882 1 204 . 1 1 29 29 TRP HB3 H 1 3.67 0.02 . 1 . . . . . . . . 4882 1 205 . 1 1 29 29 TRP HD1 H 1 7.51 0.02 . 1 . . . . . . . . 4882 1 206 . 1 1 29 29 TRP HE1 H 1 10.16 0.02 . 1 . . . . . . . . 4882 1 207 . 1 1 29 29 TRP HE3 H 1 8.20 0.02 . 1 . . . . . . . . 4882 1 208 . 1 1 29 29 TRP HZ2 H 1 7.41 0.02 . 1 . . . . . . . . 4882 1 209 . 1 1 29 29 TRP HZ3 H 1 6.94 0.02 . 1 . . . . . . . . 4882 1 210 . 1 1 29 29 TRP HH2 H 1 7.15 0.02 . 1 . . . . . . . . 4882 1 211 . 1 1 30 30 GLU H H 1 8.14 0.02 . 1 . . . . . . . . 4882 1 212 . 1 1 30 30 GLU HA H 1 4.45 0.02 . 1 . . . . . . . . 4882 1 213 . 1 1 30 30 GLU HB2 H 1 1.93 0.02 . 1 . . . . . . . . 4882 1 214 . 1 1 30 30 GLU HB3 H 1 1.93 0.02 . 1 . . . . . . . . 4882 1 215 . 1 1 30 30 GLU HG2 H 1 2.27 0.02 . 1 . . . . . . . . 4882 1 216 . 1 1 30 30 GLU HG3 H 1 2.37 0.02 . 1 . . . . . . . . 4882 1 217 . 1 1 31 31 ARG H H 1 8.60 0.02 . 1 . . . . . . . . 4882 1 218 . 1 1 31 31 ARG HA H 1 2.68 0.02 . 1 . . . . . . . . 4882 1 219 . 1 1 31 31 ARG HB2 H 1 1.43 0.02 . 1 . . . . . . . . 4882 1 220 . 1 1 31 31 ARG HB3 H 1 1.43 0.02 . 1 . . . . . . . . 4882 1 221 . 1 1 31 31 ARG HG2 H 1 1.01 0.02 . 1 . . . . . . . . 4882 1 222 . 1 1 31 31 ARG HG3 H 1 1.24 0.02 . 1 . . . . . . . . 4882 1 223 . 1 1 31 31 ARG HD2 H 1 3.10 0.02 . 1 . . . . . . . . 4882 1 224 . 1 1 31 31 ARG HD3 H 1 3.10 0.02 . 1 . . . . . . . . 4882 1 225 . 1 1 31 31 ARG HE H 1 7.22 0.02 . 1 . . . . . . . . 4882 1 226 . 1 1 32 32 PRO HA H 1 3.95 0.02 . 1 . . . . . . . . 4882 1 227 . 1 1 32 32 PRO HB2 H 1 0.03 0.02 . 1 . . . . . . . . 4882 1 228 . 1 1 32 32 PRO HB3 H 1 0.62 0.02 . 1 . . . . . . . . 4882 1 229 . 1 1 32 32 PRO HG2 H 1 0.79 0.02 . 1 . . . . . . . . 4882 1 230 . 1 1 32 32 PRO HG3 H 1 0.87 0.02 . 1 . . . . . . . . 4882 1 231 . 1 1 32 32 PRO HD2 H 1 2.34 0.02 . 1 . . . . . . . . 4882 1 232 . 1 1 32 32 PRO HD3 H 1 2.56 0.02 . 1 . . . . . . . . 4882 1 233 . 1 1 33 33 SER H H 1 8.26 0.02 . 1 . . . . . . . . 4882 1 234 . 1 1 33 33 SER HA H 1 4.37 0.02 . 1 . . . . . . . . 4882 1 235 . 1 1 33 33 SER HB2 H 1 3.77 0.02 . 1 . . . . . . . . 4882 1 236 . 1 1 33 33 SER HB3 H 1 3.85 0.02 . 1 . . . . . . . . 4882 1 237 . 1 1 34 34 GLY H H 1 8.55 0.02 . 1 . . . . . . . . 4882 1 238 . 1 1 34 34 GLY HA2 H 1 4.01 0.02 . 1 . . . . . . . . 4882 1 239 . 1 1 34 34 GLY HA3 H 1 4.01 0.02 . 1 . . . . . . . . 4882 1 240 . 1 1 35 35 ASN H H 1 8.50 0.02 . 1 . . . . . . . . 4882 1 241 . 1 1 35 35 ASN HA H 1 4.84 0.02 . 1 . . . . . . . . 4882 1 242 . 1 1 35 35 ASN HB2 H 1 2.92 0.02 . 1 . . . . . . . . 4882 1 243 . 1 1 35 35 ASN HB3 H 1 2.83 0.02 . 1 . . . . . . . . 4882 1 244 . 1 1 35 35 ASN HD21 H 1 7.56 0.02 . 1 . . . . . . . . 4882 1 245 . 1 1 35 35 ASN HD22 H 1 7.23 0.02 . 1 . . . . . . . . 4882 1 246 . 1 1 36 36 SER H H 1 8.53 0.02 . 1 . . . . . . . . 4882 1 247 . 1 1 36 36 SER HA H 1 4.53 0.02 . 1 . . . . . . . . 4882 1 248 . 1 1 36 36 SER HB2 H 1 3.94 0.02 . 1 . . . . . . . . 4882 1 249 . 1 1 36 36 SER HB3 H 1 3.94 0.02 . 1 . . . . . . . . 4882 1 250 . 1 1 37 37 SER H H 1 8.47 0.02 . 1 . . . . . . . . 4882 1 251 . 1 1 37 37 SER HA H 1 4.53 0.02 . 1 . . . . . . . . 4882 1 252 . 1 1 37 37 SER HB2 H 1 3.98 0.02 . 1 . . . . . . . . 4882 1 253 . 1 1 37 37 SER HB3 H 1 3.98 0.02 . 1 . . . . . . . . 4882 1 254 . 1 1 38 38 SER H H 1 8.58 0.02 . 1 . . . . . . . . 4882 1 255 . 1 1 38 38 SER HA H 1 4.56 0.02 . 1 . . . . . . . . 4882 1 256 . 1 1 38 38 SER HB2 H 1 3.97 0.02 . 1 . . . . . . . . 4882 1 257 . 1 1 38 38 SER HB3 H 1 3.97 0.02 . 1 . . . . . . . . 4882 1 258 . 1 1 39 39 GLY H H 1 8.86 0.02 . 1 . . . . . . . . 4882 1 259 . 1 1 39 39 GLY HA2 H 1 4.98 0.02 . 1 . . . . . . . . 4882 1 260 . 1 1 39 39 GLY HA3 H 1 4.98 0.02 . 1 . . . . . . . . 4882 1 stop_ save_