data_1658 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 1658 _Entry.Title ; Two-dimensional 1H, 15N-NMR investigation of uniformly 15N-labeled ribonuclease T1 (Complete assignment of 15N resonances) ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1995-07-31 _Entry.Accession_date 1996-03-25 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination BMRB _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 Jurgen Schmidt . M. . 1658 2 Harald Thuring . . . 1658 3 Angela Werner . . . 1658 4 Heinz Ruterjans . . . 1658 5 Rainer Quaas . . . 1658 6 Ulrich Hahn . . . 1658 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 1658 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 120 1658 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 5 . . 2010-06-15 . revision BMRB 'Complete natural source information' 1658 4 . . 2009-02-19 . revision author 'update residue sequence: 18 TYR ==> THR, 50 SER ==> PHE' 1658 3 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1658 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1658 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 1658 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 1658 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Schmidt, Jurgen M., Thuring, Harald, Werner, Angela, Ruterjans, Heinz, Quaas, Rainer, Hahn, Ulrich, "Two-dimensional 1H, 15N-NMR investigation of uniformly 15N-labeled ribonuclease T1 (Complete assignment of 15N resonances)," Eur. J. Biochem. 197, 643-653 (1991). ; _Citation.Title ; Two-dimensional 1H, 15N-NMR investigation of uniformly 15N-labeled ribonuclease T1 (Complete assignment of 15N resonances) ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Eur. J. Biochem.' _Citation.Journal_name_full . _Citation.Journal_volume 197 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 643 _Citation.Page_last 653 _Citation.Year 1991 _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 Jurgen Schmidt . M. . 1658 1 2 Harald Thuring . . . 1658 1 3 Angela Werner . . . 1658 1 4 Heinz Ruterjans . . . 1658 1 5 Rainer Quaas . . . 1658 1 6 Ulrich Hahn . . . 1658 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_ribonuclease_T1 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_ribonuclease_T1 _Assembly.Entry_ID 1658 _Assembly.ID 1 _Assembly.Name 'ribonuclease T1' _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 . _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'ribonuclease T1' 1 $ribonuclease_T1 . . . . . . . . . 1658 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'ribonuclease T1' system 1658 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_ribonuclease_T1 _Entity.Sf_category entity _Entity.Sf_framecode ribonuclease_T1 _Entity.Entry_ID 1658 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'ribonuclease T1' _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 ; ACDYTCGSNCYSSSDVSTAQ AAGYKLHEDGETVGSNSYPH KYNNYEGFDFSVSSPYYEWP ILSSGDVYSGGSPGADRVVF NENNQLAGVITHTGASGNNF VECT ; _Entity.Polymer_seq_one_letter_code ; ACDYTCGSNCYSSSDVSTAQ AAGYKLHEDGETVGSNSYPH KYNNYEGFDFSVSSPYYEWP ILSSGDVYSGGSPGADRVVF NENNQLAGVITHTGASGNNF VECT ; _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 104 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number 3.1.27.3 _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 15905 . RNase_T1 . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 2 no BMRB 16469 . RNase_T1 . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 3 no BMRB 16580 . RNase_T1 . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 4 no PDB 1B2M . "Three-Dimensional Structure Of Ribonulcease T1 Complexed With An Isosteric Phosphonate Analogue Of Gpu: Alternate Substrate Bin" . . . . . 100.00 104 99.04 100.00 1.20e-67 . . . . 1658 1 5 no PDB 1BIR . "Ribonuclease T1, Phe 100 To Ala Mutant Complexed With 2' Gmp" . . . . . 100.00 104 99.04 99.04 4.96e-67 . . . . 1658 1 6 no PDB 1BU4 . "Ribonuclease 1 Complex With 2'gmp" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 7 no PDB 1BVI . "Ribonuclease T1 (Wildtype) Complexed With 2'gmp" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 8 no PDB 1DET . "Ribonuclease T1 Carboxymethylated At Glu 58 In Complex With 2'gmp" . . . . . 100.00 104 98.08 99.04 1.12e-66 . . . . 1658 1 9 no PDB 1FYS . "Ribonuclease T1 V16c Mutant" . . . . . 100.00 104 99.04 99.04 3.50e-67 . . . . 1658 1 10 no PDB 1FZU . "Rnase T1 V78a Mutant" . . . . . 100.00 104 99.04 99.04 1.34e-67 . . . . 1658 1 11 no PDB 1G02 . "Ribonuclease T1 V16s Mutant" . . . . . 100.00 104 99.04 99.04 2.81e-67 . . . . 1658 1 12 no PDB 1GSP . "Ribonuclease T1 Complexed With 2',3'-Cgps, 1 Day" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 13 no PDB 1HYF . "Ribonuclease T1 V16a Mutant In Complex With Sr2+" . . . . . 100.00 104 99.04 99.04 1.34e-67 . . . . 1658 1 14 no PDB 1HZ1 . "Ribonuclease T1 V16a Mutant In Complex With Mg2+" . . . . . 100.00 104 99.04 99.04 1.34e-67 . . . . 1658 1 15 no PDB 1I0V . "Ribonuclease T1 In Complex With 2'gmp (Form I Crystal)" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 16 no PDB 1I0X . "Ribonuclease T1 In Complex With 2'gmp (Form Ii Crystal)" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 17 no PDB 1I2E . "Ribonuclease T1 V16a Mutant, Form I" . . . . . 100.00 104 99.04 99.04 1.34e-67 . . . . 1658 1 18 no PDB 1I2F . "Ribonuclease T1 V16a Mutant, Form Ii" . . . . . 100.00 104 99.04 99.04 1.34e-67 . . . . 1658 1 19 no PDB 1I2G . "Ribonuclease T1 V16t Mutant" . . . . . 100.00 104 99.04 99.04 1.37e-67 . . . . 1658 1 20 no PDB 1I3F . "Ribonuclease T1 V89s Mutant" . . . . . 100.00 104 99.04 99.04 2.81e-67 . . . . 1658 1 21 no PDB 1I3I . "Ribonuclease T1 V78t Mutant" . . . . . 100.00 104 99.04 99.04 1.37e-67 . . . . 1658 1 22 no PDB 1IYY . "Nmr Structure Of Gln25-Ribonuclease T1, 24 Structures" . . . . . 100.00 104 99.04 100.00 1.20e-67 . . . . 1658 1 23 no PDB 1LOV . "X-ray Structure Of The E58a Mutant Of Ribonuclease T1 Complexed With 3'-guanosine Monophosphate" . . . . . 100.00 104 99.04 99.04 2.26e-67 . . . . 1658 1 24 no PDB 1LOW . "X-ray Structure Of The H40a Mutant Of Ribonuclease T1 Complexed With 3'-guanosine Monophosphate" . . . . . 100.00 104 99.04 99.04 6.03e-67 . . . . 1658 1 25 no PDB 1LOY . "X-Ray Structure Of The H40aE58A MUTANT OF RIBONUCLEASE T1 Complexed With 3'-Guanosine Monophosphate" . . . . . 100.00 104 98.08 98.08 3.38e-66 . . . . 1658 1 26 no PDB 1LRA . "Crystallographic Study Of Glu 58 Ala Rnase T1(Asterisk)2'-Guanosine Monophosphate At 1.9 Angstroms Resolution" . . . . . 100.00 104 99.04 99.04 2.26e-67 . . . . 1658 1 27 no PDB 1RGA . "Crystal Structure Of Rnase T1 With 3'-Gmp And Guanosine: A Product Complex" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 28 no PDB 1RGC . "The Complex Between Ribonuclease T1 And 3'-guanylic Acid Suggests Geometry Of Enzymatic Reaction Path. An X-ray Study" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 29 no PDB 1RGK . "Rnase T1 Mutant Glu46gln Binds The Inhibitors 2'gmp And 2'amp At The 3' Subsite" . . . . . 100.00 104 99.04 100.00 8.65e-68 . . . . 1658 1 30 no PDB 1RGL . "Rnase T1 Mutant Glu46gln Binds The Inhibitors 2'gmp And 2'amp At The 3' Subsite" . . . . . 100.00 104 99.04 100.00 8.65e-68 . . . . 1658 1 31 no PDB 1RHL . "Ribonuclease T1 Complexed With 2'gmpG23A MUTANT" . . . . . 100.00 104 99.04 99.04 1.72e-67 . . . . 1658 1 32 no PDB 1RLS . "Crystal Structure Of Rnase T1 Complexed With The Product Nucleotide 3'-Gmp. Structural Evidence For Direct Interaction Of Histi" . . . . . 100.00 104 99.04 100.00 1.20e-67 . . . . 1658 1 33 no PDB 1RN1 . "Three-Dimensional Structure Of Gln 25-Ribonuclease T1 At 1.84 Angstroms Resolution: Structural Variations At The Base Recogniti" . . . . . 100.00 104 99.04 100.00 1.20e-67 . . . . 1658 1 34 no PDB 1RN4 . "His92ala Mutation In Ribonuclease T1 Induces Segmental Flexibility. An X-Ray Study" . . . . . 100.00 104 99.04 99.04 6.03e-67 . . . . 1658 1 35 no PDB 1RNT . "Restrained Least-Squares Refinement Of The Crystal Structure Of The Ribonuclease T1(Asterisk)2(Prime)- Guanylic Acid Complex At" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 36 no PDB 1TRP . "X-ray Crystallographic And Calorimeric Studies Of The Effects Of The Mutation Trp 59 Tyr In Ribonuclease T1" . . . . . 100.00 104 98.08 100.00 3.45e-66 . . . . 1658 1 37 no PDB 1TRQ . "X-ray Crystallographic And Calorimeric Studies Of The Effects Of The Mutation Trp 59 Tyr In Ribonuclease T1" . . . . . 100.00 104 99.04 100.00 4.80e-67 . . . . 1658 1 38 no PDB 1YGW . "Nmr Structure Of Ribonuclease T1, 34 Structures" . . . . . 99.04 104 100.00 100.00 1.72e-67 . . . . 1658 1 39 no PDB 2AAD . "The Role Of Histidine-40 In Ribonuclease T1 Catalysis: Three-Dimensional Structures Of The Partially Active His40lys Mutant" . . . . . 100.00 104 99.04 99.04 3.94e-67 . . . . 1658 1 40 no PDB 2AAE . "The Role Of Histidine-40 In Ribonuclease T1 Catalysis: Three-Dimensional Structures Of The Partially Active His40lys Mutant" . . . . . 100.00 104 99.04 99.04 3.94e-67 . . . . 1658 1 41 no PDB 2BIR . "Additivity Of Substrate Binding In Ribonuclease T1 (Y42a Mutant)" . . . . . 100.00 104 98.08 98.08 3.45e-66 . . . . 1658 1 42 no PDB 2BU4 . "Ribonuclease T1 Complex With 2'gmp" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 43 no PDB 2GSP . "Ribonuclease T12',3'-Cgps And 3'-Gmp, 2 Days" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 44 no PDB 2HOH . "Ribonuclease T1 (n9a Mutant) Complexed With 2'gmp" . . . . . 100.00 104 99.04 99.04 2.72e-67 . . . . 1658 1 45 no PDB 2RNT . "Three-Dimensional Structure Of Ribonuclease T1 Complexed With Guanylyl-2(Prime),5(Prime)-Guanosine At 1.8 Angstroms Resolution" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 46 no PDB 3BIR . "Disecting Histidine Interactions In Ribonuclease T1 By Asn And Gln Substitutions" . . . . . 100.00 104 99.04 100.00 3.53e-67 . . . . 1658 1 47 no PDB 3BU4 . "Ribonuclease T1 Complex With 2'gmp" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 48 no PDB 3GSP . "Ribonuclease T1 Complexed With 2',3'-Cgps + 3'-Gmp, 4 Days" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 49 no PDB 3HOH . "Ribonuclease T1 (Thr93gln Mutant) Complexed With 2'gmp" . . . . . 100.00 104 99.04 99.04 1.84e-67 . . . . 1658 1 50 no PDB 3RNT . "Crystal Structure Of Guanosine-Free Ribonuclease T1, Complexed With Vanadate(V), Suggests Conformational Change Upon Substrate " . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 51 no PDB 3SYU . "Re-Refined Coordinates For Pdb Entry 1det - Ribonuclease T1 Carboxymethylated At Glu 58 In Complex With 2'gmp" . . . . . 100.00 104 98.08 99.04 1.12e-66 . . . . 1658 1 52 no PDB 3URP . "Re-refinement Of Pdb Entry 5rnt - Ribonuclease T1 With Guanosine-3', 5'-diphosphate And Phosphate Ion Bound" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 53 no PDB 4BIR . "Ribonuclease T1: Free His92gln Mutant" . . . . . 100.00 104 99.04 99.04 2.66e-67 . . . . 1658 1 54 no PDB 4BU4 . "Ribonuclease T1 Complex With 2'gmp" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 55 no PDB 4GSP . "Ribonuclease T1 Complexed With 2',3'-Cgps + 3'-Gmp, 7 Days" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 56 no PDB 4HOH . "Ribonuclease T1 (Thr93ala Mutant) Complexed With 2'gmp" . . . . . 100.00 104 99.04 99.04 1.70e-67 . . . . 1658 1 57 no PDB 4RNT . "His 92 Ala Mutation In Ribonuclease T1 Induces Segmental Flexibility. An X-Ray Study" . . . . . 100.00 104 99.04 99.04 6.03e-67 . . . . 1658 1 58 no PDB 5BIR . "Disecting Histidine Interactions In Ribonuclease T1 Using Asn And Gln Mutations" . . . . . 100.00 104 99.04 99.04 2.66e-67 . . . . 1658 1 59 no PDB 5BU4 . "Ribonuclease T1 Complex With 2'gmp" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 60 no PDB 5GSP . "Ribonuclease T13'-Gmp, 9 Weeks" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 61 no PDB 5HOH . "Ribonuclease T1 (Asn9alaTHR93ALA DOUBLEMUTANT) COMPLEXED With 2'gmp" . . . . . 100.00 104 98.08 98.08 1.28e-66 . . . . 1658 1 62 no PDB 5RNT . "X-Ray Analysis Of Cubic Crystals Of The Complex Formed Between Ribonuclease T1 And Guanosine-3',5'-Bisphosphate" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 63 no PDB 6GSP . "Ribonuclease T1/3'-gmp, 15 Weeks" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 64 no PDB 6RNT . "Crystal Structure Of Ribonuclease T1 Complexed With Adenosine 2'-monophosphate At 1.8-angstroms Resolution" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 65 no PDB 7GSP . "Ribonuclease T12',3'-Cgps, Non-Productive" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 66 no PDB 7RNT . "Crystal Structure Of The Tyr45trp Mutant Of Ribonuclease T1 In A Complex With 2'-Adenylic Acid" . . . . . 100.00 104 99.04 100.00 1.48e-67 . . . . 1658 1 67 no PDB 8RNT . "Structure Of Ribonuclease T1 Complexed With Zinc(Ii) At 1.8 Angstroms Resolution: A Zn2+.6h2o.Carboxylate Clathrate" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 68 no PDB 9RNT . "Ribonuclease T1 With Free Recognition And Catalytic Site: Crystal Structure Analysis At 1.5 Angstroms Resolution" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 69 no DBJ BAA05707 . "ribonuclease T1 [Aspergillus oryzae]" . . . . . 100.00 130 99.04 100.00 1.81e-68 . . . . 1658 1 70 no DBJ BAA08407 . "ribonuclease T1 [Aspergillus oryzae]" . . . . . 100.00 130 99.04 100.00 1.81e-68 . . . . 1658 1 71 no DBJ BAE64671 . "unnamed protein product [Aspergillus oryzae RIB40]" . . . . . 100.00 130 99.04 100.00 1.81e-68 . . . . 1658 1 72 no EMBL CAA30560 . "unnamed protein product [Aspergillus oryzae]" . . . . . 100.00 104 100.00 100.00 3.54e-68 . . . . 1658 1 73 no GB AAA72541 . "RNase T1 [synthetic construct]" . . . . . 100.00 105 99.04 100.00 1.25e-67 . . . . 1658 1 74 no GB AAA72994 . "fusion gene containing ompA-signal peptide/RNase T1 [synthetic construct]" . . . . . 100.00 125 100.00 100.00 3.19e-69 . . . . 1658 1 75 no GB EED52238 . "extracellular guanyl-specific ribonuclease RntA [Aspergillus flavus NRRL3357]" . . . . . 100.00 130 99.04 100.00 1.81e-68 . . . . 1658 1 76 no GB EIT74451 . "guanyl-specific ribonuclease T1 [Aspergillus oryzae 3.042]" . . . . . 100.00 130 99.04 100.00 1.81e-68 . . . . 1658 1 77 no GB KDE77875 . "guanyl-specific ribonuclease T1 [Aspergillus oryzae 100-8]" . . . . . 100.00 130 99.04 100.00 1.81e-68 . . . . 1658 1 78 no REF XP_001825804 . "guanyl-specific ribonuclease T1 [Aspergillus oryzae RIB40]" . . . . . 100.00 130 99.04 100.00 1.81e-68 . . . . 1658 1 79 no REF XP_002377402 . "extracellular guanyl-specific ribonuclease RntA [Aspergillus flavus NRRL3357]" . . . . . 100.00 130 99.04 100.00 1.81e-68 . . . . 1658 1 80 no SP P00651 . "RecName: Full=Guanyl-specific ribonuclease T1; Short=RNase T1; Flags: Precursor" . . . . . 100.00 130 99.04 100.00 1.81e-68 . . . . 1658 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'ribonuclease T1' common 1658 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . ALA . 1658 1 2 . CYS . 1658 1 3 . ASP . 1658 1 4 . TYR . 1658 1 5 . THR . 1658 1 6 . CYS . 1658 1 7 . GLY . 1658 1 8 . SER . 1658 1 9 . ASN . 1658 1 10 . CYS . 1658 1 11 . TYR . 1658 1 12 . SER . 1658 1 13 . SER . 1658 1 14 . SER . 1658 1 15 . ASP . 1658 1 16 . VAL . 1658 1 17 . SER . 1658 1 18 . THR . 1658 1 19 . ALA . 1658 1 20 . GLN . 1658 1 21 . ALA . 1658 1 22 . ALA . 1658 1 23 . GLY . 1658 1 24 . TYR . 1658 1 25 . LYS . 1658 1 26 . LEU . 1658 1 27 . HIS . 1658 1 28 . GLU . 1658 1 29 . ASP . 1658 1 30 . GLY . 1658 1 31 . GLU . 1658 1 32 . THR . 1658 1 33 . VAL . 1658 1 34 . GLY . 1658 1 35 . SER . 1658 1 36 . ASN . 1658 1 37 . SER . 1658 1 38 . TYR . 1658 1 39 . PRO . 1658 1 40 . HIS . 1658 1 41 . LYS . 1658 1 42 . TYR . 1658 1 43 . ASN . 1658 1 44 . ASN . 1658 1 45 . TYR . 1658 1 46 . GLU . 1658 1 47 . GLY . 1658 1 48 . PHE . 1658 1 49 . ASP . 1658 1 50 . PHE . 1658 1 51 . SER . 1658 1 52 . VAL . 1658 1 53 . SER . 1658 1 54 . SER . 1658 1 55 . PRO . 1658 1 56 . TYR . 1658 1 57 . TYR . 1658 1 58 . GLU . 1658 1 59 . TRP . 1658 1 60 . PRO . 1658 1 61 . ILE . 1658 1 62 . LEU . 1658 1 63 . SER . 1658 1 64 . SER . 1658 1 65 . GLY . 1658 1 66 . ASP . 1658 1 67 . VAL . 1658 1 68 . TYR . 1658 1 69 . SER . 1658 1 70 . GLY . 1658 1 71 . GLY . 1658 1 72 . SER . 1658 1 73 . PRO . 1658 1 74 . GLY . 1658 1 75 . ALA . 1658 1 76 . ASP . 1658 1 77 . ARG . 1658 1 78 . VAL . 1658 1 79 . VAL . 1658 1 80 . PHE . 1658 1 81 . ASN . 1658 1 82 . GLU . 1658 1 83 . ASN . 1658 1 84 . ASN . 1658 1 85 . GLN . 1658 1 86 . LEU . 1658 1 87 . ALA . 1658 1 88 . GLY . 1658 1 89 . VAL . 1658 1 90 . ILE . 1658 1 91 . THR . 1658 1 92 . HIS . 1658 1 93 . THR . 1658 1 94 . GLY . 1658 1 95 . ALA . 1658 1 96 . SER . 1658 1 97 . GLY . 1658 1 98 . ASN . 1658 1 99 . ASN . 1658 1 100 . PHE . 1658 1 101 . VAL . 1658 1 102 . GLU . 1658 1 103 . CYS . 1658 1 104 . THR . 1658 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . ALA 1 1 1658 1 . CYS 2 2 1658 1 . ASP 3 3 1658 1 . TYR 4 4 1658 1 . THR 5 5 1658 1 . CYS 6 6 1658 1 . GLY 7 7 1658 1 . SER 8 8 1658 1 . ASN 9 9 1658 1 . CYS 10 10 1658 1 . TYR 11 11 1658 1 . SER 12 12 1658 1 . SER 13 13 1658 1 . SER 14 14 1658 1 . ASP 15 15 1658 1 . VAL 16 16 1658 1 . SER 17 17 1658 1 . THR 18 18 1658 1 . ALA 19 19 1658 1 . GLN 20 20 1658 1 . ALA 21 21 1658 1 . ALA 22 22 1658 1 . GLY 23 23 1658 1 . TYR 24 24 1658 1 . LYS 25 25 1658 1 . LEU 26 26 1658 1 . HIS 27 27 1658 1 . GLU 28 28 1658 1 . ASP 29 29 1658 1 . GLY 30 30 1658 1 . GLU 31 31 1658 1 . THR 32 32 1658 1 . VAL 33 33 1658 1 . GLY 34 34 1658 1 . SER 35 35 1658 1 . ASN 36 36 1658 1 . SER 37 37 1658 1 . TYR 38 38 1658 1 . PRO 39 39 1658 1 . HIS 40 40 1658 1 . LYS 41 41 1658 1 . TYR 42 42 1658 1 . ASN 43 43 1658 1 . ASN 44 44 1658 1 . TYR 45 45 1658 1 . GLU 46 46 1658 1 . GLY 47 47 1658 1 . PHE 48 48 1658 1 . ASP 49 49 1658 1 . PHE 50 50 1658 1 . SER 51 51 1658 1 . VAL 52 52 1658 1 . SER 53 53 1658 1 . SER 54 54 1658 1 . PRO 55 55 1658 1 . TYR 56 56 1658 1 . TYR 57 57 1658 1 . GLU 58 58 1658 1 . TRP 59 59 1658 1 . PRO 60 60 1658 1 . ILE 61 61 1658 1 . LEU 62 62 1658 1 . SER 63 63 1658 1 . SER 64 64 1658 1 . GLY 65 65 1658 1 . ASP 66 66 1658 1 . VAL 67 67 1658 1 . TYR 68 68 1658 1 . SER 69 69 1658 1 . GLY 70 70 1658 1 . GLY 71 71 1658 1 . SER 72 72 1658 1 . PRO 73 73 1658 1 . GLY 74 74 1658 1 . ALA 75 75 1658 1 . ASP 76 76 1658 1 . ARG 77 77 1658 1 . VAL 78 78 1658 1 . VAL 79 79 1658 1 . PHE 80 80 1658 1 . ASN 81 81 1658 1 . GLU 82 82 1658 1 . ASN 83 83 1658 1 . ASN 84 84 1658 1 . GLN 85 85 1658 1 . LEU 86 86 1658 1 . ALA 87 87 1658 1 . GLY 88 88 1658 1 . VAL 89 89 1658 1 . ILE 90 90 1658 1 . THR 91 91 1658 1 . HIS 92 92 1658 1 . THR 93 93 1658 1 . GLY 94 94 1658 1 . ALA 95 95 1658 1 . SER 96 96 1658 1 . GLY 97 97 1658 1 . ASN 98 98 1658 1 . ASN 99 99 1658 1 . PHE 100 100 1658 1 . VAL 101 101 1658 1 . GLU 102 102 1658 1 . CYS 103 103 1658 1 . THR 104 104 1658 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 1658 _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 $ribonuclease_T1 . 5062 organism . 'Aspergillus oryzae' . . . Eukaryota Fungi Aspergillus oryzae generic . . . . . . . . . . . . . . . . . . . . 1658 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 1658 _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 $ribonuclease_T1 . 'not available' 'Escherichia coli' . . . Escherichia coli DH5alpha . . . . . . . . . . . . . . . . . . . . . . 1658 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 1658 _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 . save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_condition_set_one _Sample_condition_list.Entry_ID 1658 _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 5.5 . na 1658 1 temperature 313 . K 1658 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 1658 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 1658 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 unknown unknown . 0 'spectrometer information not available' . . 1658 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 1658 _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 . . . . . . . . . . . . 1 $sample_one . . . 1 $sample_condition_set_one . . . 1 $spectrometer_list . . . . . . . . . . . . . . . . 1658 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_par_set_one _Chem_shift_reference.Entry_ID 1658 _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 N . 'liquid NH3' . . . . . ppm 0 . . . . . . 1 $entry_citation . . 1 $entry_citation 1658 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_chemical_shift_assignment_data_set_one _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode 'chemical_shift_assignment_data_set_one' _Assigned_chem_shift_list.Entry_ID 1658 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_condition_set_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_par_set_one _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 $sample_one . 1658 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 ALA N N 15 40.5 . . 1 . . . . . . . . 1658 1 2 . 1 1 3 3 ASP N N 15 128.4 . . 1 . . . . . . . . 1658 1 3 . 1 1 4 4 TYR N N 15 115.4 . . 1 . . . . . . . . 1658 1 4 . 1 1 5 5 THR N N 15 120.6 . . 1 . . . . . . . . 1658 1 5 . 1 1 6 6 CYS N N 15 126.9 . . 1 . . . . . . . . 1658 1 6 . 1 1 7 7 GLY N N 15 117.4 . . 1 . . . . . . . . 1658 1 7 . 1 1 8 8 SER N N 15 123.6 . . 1 . . . . . . . . 1658 1 8 . 1 1 9 9 ASN ND2 N 15 116.9 . . 1 . . . . . . . . 1658 1 9 . 1 1 9 9 ASN N N 15 121.7 . . 1 . . . . . . . . 1658 1 10 . 1 1 10 10 CYS N N 15 124.3 . . 1 . . . . . . . . 1658 1 11 . 1 1 11 11 TYR N N 15 126.4 . . 1 . . . . . . . . 1658 1 12 . 1 1 12 12 SER N N 15 119.8 . . 1 . . . . . . . . 1658 1 13 . 1 1 13 13 SER N N 15 119.5 . . 1 . . . . . . . . 1658 1 14 . 1 1 14 14 SER N N 15 117.8 . . 1 . . . . . . . . 1658 1 15 . 1 1 15 15 ASP N N 15 126.2 . . 1 . . . . . . . . 1658 1 16 . 1 1 16 16 VAL N N 15 121.7 . . 1 . . . . . . . . 1658 1 17 . 1 1 17 17 SER N N 15 116.1 . . 1 . . . . . . . . 1658 1 18 . 1 1 18 18 THR N N 15 120.4 . . 1 . . . . . . . . 1658 1 19 . 1 1 19 19 ALA N N 15 124.4 . . 1 . . . . . . . . 1658 1 20 . 1 1 20 20 GLN NE2 N 15 106.1 . . 1 . . . . . . . . 1658 1 21 . 1 1 20 20 GLN N N 15 118.3 . . 1 . . . . . . . . 1658 1 22 . 1 1 21 21 ALA N N 15 119 . . 1 . . . . . . . . 1658 1 23 . 1 1 22 22 ALA N N 15 120.4 . . 1 . . . . . . . . 1658 1 24 . 1 1 23 23 GLY N N 15 105.3 . . 1 . . . . . . . . 1658 1 25 . 1 1 24 24 TYR N N 15 123.7 . . 1 . . . . . . . . 1658 1 26 . 1 1 25 25 LYS NZ N 15 33 . . 1 . . . . . . . . 1658 1 27 . 1 1 25 25 LYS N N 15 119.3 . . 1 . . . . . . . . 1658 1 28 . 1 1 26 26 LEU N N 15 117.8 . . 1 . . . . . . . . 1658 1 29 . 1 1 27 27 HIS ND1 N 15 177.2 . . 1 . . . . . . . . 1658 1 30 . 1 1 27 27 HIS NE2 N 15 177 . . 1 . . . . . . . . 1658 1 31 . 1 1 27 27 HIS N N 15 116.2 . . 1 . . . . . . . . 1658 1 32 . 1 1 28 28 GLU N N 15 120.9 . . 1 . . . . . . . . 1658 1 33 . 1 1 29 29 ASP N N 15 117.9 . . 1 . . . . . . . . 1658 1 34 . 1 1 30 30 GLY N N 15 109.9 . . 1 . . . . . . . . 1658 1 35 . 1 1 31 31 GLU N N 15 120 . . 1 . . . . . . . . 1658 1 36 . 1 1 32 32 THR N N 15 109 . . 1 . . . . . . . . 1658 1 37 . 1 1 33 33 VAL N N 15 115.1 . . 1 . . . . . . . . 1658 1 38 . 1 1 34 34 GLY N N 15 109.5 . . 1 . . . . . . . . 1658 1 39 . 1 1 36 36 ASN ND2 N 15 112.5 . . 1 . . . . . . . . 1658 1 40 . 1 1 36 36 ASN N N 15 122.7 . . 1 . . . . . . . . 1658 1 41 . 1 1 37 37 SER N N 15 112 . . 1 . . . . . . . . 1658 1 42 . 1 1 38 38 TYR N N 15 121.1 . . 1 . . . . . . . . 1658 1 43 . 1 1 39 39 PRO N N 15 132.9 . . 1 . . . . . . . . 1658 1 44 . 1 1 40 40 HIS ND1 N 15 176.7 . . 1 . . . . . . . . 1658 1 45 . 1 1 40 40 HIS NE2 N 15 175.7 . . 1 . . . . . . . . 1658 1 46 . 1 1 40 40 HIS N N 15 114.5 . . 1 . . . . . . . . 1658 1 47 . 1 1 41 41 LYS NZ N 15 33 . . 1 . . . . . . . . 1658 1 48 . 1 1 41 41 LYS N N 15 125.6 . . 1 . . . . . . . . 1658 1 49 . 1 1 42 42 TYR N N 15 128 . . 1 . . . . . . . . 1658 1 50 . 1 1 43 43 ASN ND2 N 15 112.8 . . 1 . . . . . . . . 1658 1 51 . 1 1 43 43 ASN N N 15 125.5 . . 1 . . . . . . . . 1658 1 52 . 1 1 44 44 ASN ND2 N 15 105.7 . . 1 . . . . . . . . 1658 1 53 . 1 1 44 44 ASN N N 15 114.3 . . 1 . . . . . . . . 1658 1 54 . 1 1 45 45 TYR N N 15 121.6 . . 1 . . . . . . . . 1658 1 55 . 1 1 46 46 GLU N N 15 118.5 . . 1 . . . . . . . . 1658 1 56 . 1 1 47 47 GLY N N 15 107.3 . . 1 . . . . . . . . 1658 1 57 . 1 1 48 48 PHE N N 15 121.5 . . 1 . . . . . . . . 1658 1 58 . 1 1 49 49 ASP N N 15 124 . . 1 . . . . . . . . 1658 1 59 . 1 1 50 50 PHE N N 15 122.5 . . 1 . . . . . . . . 1658 1 60 . 1 1 51 51 SER N N 15 117 . . 1 . . . . . . . . 1658 1 61 . 1 1 52 52 VAL N N 15 111.7 . . 1 . . . . . . . . 1658 1 62 . 1 1 53 53 SER N N 15 119.5 . . 1 . . . . . . . . 1658 1 63 . 1 1 54 54 SER N N 15 119.3 . . 1 . . . . . . . . 1658 1 64 . 1 1 55 55 PRO N N 15 135.3 . . 1 . . . . . . . . 1658 1 65 . 1 1 56 56 TYR N N 15 117.4 . . 1 . . . . . . . . 1658 1 66 . 1 1 57 57 TYR N N 15 118.6 . . 1 . . . . . . . . 1658 1 67 . 1 1 58 58 GLU N N 15 117.4 . . 1 . . . . . . . . 1658 1 68 . 1 1 59 59 TRP NE1 N 15 130.9 . . 1 . . . . . . . . 1658 1 69 . 1 1 59 59 TRP N N 15 124.1 . . 1 . . . . . . . . 1658 1 70 . 1 1 60 60 PRO N N 15 141.2 . . 1 . . . . . . . . 1658 1 71 . 1 1 61 61 ILE N N 15 121 . . 1 . . . . . . . . 1658 1 72 . 1 1 62 62 LEU N N 15 125.2 . . 1 . . . . . . . . 1658 1 73 . 1 1 63 63 SER N N 15 120.8 . . 1 . . . . . . . . 1658 1 74 . 1 1 64 64 SER N N 15 114.3 . . 1 . . . . . . . . 1658 1 75 . 1 1 65 65 GLY N N 15 110.2 . . 1 . . . . . . . . 1658 1 76 . 1 1 66 66 ASP N N 15 120 . . 1 . . . . . . . . 1658 1 77 . 1 1 67 67 VAL N N 15 121.2 . . 1 . . . . . . . . 1658 1 78 . 1 1 68 68 TYR N N 15 129.3 . . 1 . . . . . . . . 1658 1 79 . 1 1 69 69 SER N N 15 118.7 . . 1 . . . . . . . . 1658 1 80 . 1 1 70 70 GLY N N 15 105.9 . . 1 . . . . . . . . 1658 1 81 . 1 1 73 73 PRO N N 15 139.5 . . 1 . . . . . . . . 1658 1 82 . 1 1 74 74 GLY N N 15 106.7 . . 1 . . . . . . . . 1658 1 83 . 1 1 75 75 ALA N N 15 125.2 . . 1 . . . . . . . . 1658 1 84 . 1 1 76 76 ASP N N 15 118.7 . . 1 . . . . . . . . 1658 1 85 . 1 1 77 77 ARG NE N 15 86 . . 1 . . . . . . . . 1658 1 86 . 1 1 77 77 ARG NH1 N 15 71 . . 1 . . . . . . . . 1658 1 87 . 1 1 77 77 ARG NH2 N 15 72 . . 1 . . . . . . . . 1658 1 88 . 1 1 77 77 ARG N N 15 122 . . 1 . . . . . . . . 1658 1 89 . 1 1 78 78 VAL N N 15 116.9 . . 1 . . . . . . . . 1658 1 90 . 1 1 79 79 VAL N N 15 123.9 . . 1 . . . . . . . . 1658 1 91 . 1 1 80 80 PHE N N 15 123.7 . . 1 . . . . . . . . 1658 1 92 . 1 1 81 81 ASN ND2 N 15 113.6 . . 1 . . . . . . . . 1658 1 93 . 1 1 81 81 ASN N N 15 121.4 . . 1 . . . . . . . . 1658 1 94 . 1 1 82 82 GLU N N 15 116.5 . . 1 . . . . . . . . 1658 1 95 . 1 1 83 83 ASN ND2 N 15 111.7 . . 1 . . . . . . . . 1658 1 96 . 1 1 83 83 ASN N N 15 115 . . 1 . . . . . . . . 1658 1 97 . 1 1 84 84 ASN N N 15 116.2 . . 1 . . . . . . . . 1658 1 98 . 1 1 85 85 GLN NE2 N 15 113.8 . . 1 . . . . . . . . 1658 1 99 . 1 1 85 85 GLN N N 15 114.4 . . 1 . . . . . . . . 1658 1 100 . 1 1 86 86 LEU N N 15 124.8 . . 1 . . . . . . . . 1658 1 101 . 1 1 87 87 ALA N N 15 131.2 . . 1 . . . . . . . . 1658 1 102 . 1 1 88 88 GLY N N 15 101.3 . . 1 . . . . . . . . 1658 1 103 . 1 1 89 89 VAL N N 15 121.5 . . 1 . . . . . . . . 1658 1 104 . 1 1 90 90 ILE N N 15 119.7 . . 1 . . . . . . . . 1658 1 105 . 1 1 91 91 THR N N 15 113.1 . . 1 . . . . . . . . 1658 1 106 . 1 1 92 92 HIS ND1 N 15 172.2 . . 1 . . . . . . . . 1658 1 107 . 1 1 92 92 HIS NE2 N 15 174.3 . . 1 . . . . . . . . 1658 1 108 . 1 1 92 92 HIS N N 15 124.6 . . 1 . . . . . . . . 1658 1 109 . 1 1 93 93 THR N N 15 124.1 . . 1 . . . . . . . . 1658 1 110 . 1 1 94 94 GLY N N 15 115.2 . . 1 . . . . . . . . 1658 1 111 . 1 1 95 95 ALA N N 15 123.7 . . 1 . . . . . . . . 1658 1 112 . 1 1 96 96 SER N N 15 115.5 . . 1 . . . . . . . . 1658 1 113 . 1 1 97 97 GLY N N 15 111.8 . . 1 . . . . . . . . 1658 1 114 . 1 1 99 99 ASN ND2 N 15 113.1 . . 1 . . . . . . . . 1658 1 115 . 1 1 99 99 ASN N N 15 118 . . 1 . . . . . . . . 1658 1 116 . 1 1 100 100 PHE N N 15 119.6 . . 1 . . . . . . . . 1658 1 117 . 1 1 101 101 VAL N N 15 113.7 . . 1 . . . . . . . . 1658 1 118 . 1 1 102 102 GLU N N 15 121.1 . . 1 . . . . . . . . 1658 1 119 . 1 1 103 103 CYS N N 15 121.9 . . 1 . . . . . . . . 1658 1 120 . 1 1 104 104 THR N N 15 120.1 . . 1 . . . . . . . . 1658 1 stop_ save_