data_4424 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Structure of the N-terminal Domain of Saccharomyces cerevisiae RNase HI Reveals a Fold with a Strong Resemblance to the N-terminal Domain of Ribosomal Protein L9 ; _BMRB_accession_number 4424 _BMRB_flat_file_name bmr4424.str _Entry_type original _Submission_date 1999-09-29 _Accession_date 1999-09-30 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Evans S. P. . 2 Bycroft M. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 311 "13C chemical shifts" 190 "15N chemical shifts" 58 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-12-23 original author . stop_ _Original_release_date 1999-12-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR Structure of the N-terminal Domain of Saccharomyces cerevisiae RNase HI Reveals a Fold with a Strong Resemblance to the N-terminal Domain of Ribosomal Protein L ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99380410 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Evans S. P. . 2 Bycroft M. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 291 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 661 _Page_last 669 _Year 1999 _Details . loop_ _Keyword 'Ribonuclease HI N-terminal domain' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full . _Citation_title 'The non-RNase H domain of Saccharomyces cerevisiae RNase H1 binds double-stranded RNA: magnesium modulates the switch between double-stranded RNA binding and RNase H activity.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 7489497 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cerritelli 'S. M.' M. . 2 Crouch 'R. J.' J. . stop_ _Journal_abbreviation RNA _Journal_name_full 'RNA (New York, N.Y.)' _Journal_volume 1 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 246 _Page_last 259 _Year 1995 _Details ; Eukaryotic ribonucleases H of known sequence are composed of an RNase H domain similar in size and sequence to that of Escherichia coli RNase HI and additional domains of unknown function. The RNase H1 of Saccharomyces cerevisiae has such an RNase H domain at its C-terminus. Here we show that the N-terminal non-RNase H portion of the yeast RNase H1 binds tightly to double-stranded RNA (dsRNA) and RNA-DNA hybrids even in the absence of the RNase H domain. Two copies of a sequence with limited similarity to the dsRNA-binding motif are present in this N-terminus. When the first of these sequences is altered, the protein no longer binds tightly to dsRNA and exhibits an increase in RNase H activity. Unlike other dsRNA-binding proteins, increasing the Mg2+ concentration from 0.5 mM to 5 mM inhibits binding of RNase H1 to dsRNA; yet a protein missing the RNase H domain binds strongly to dsRNA even at the higher Mg2+ concentration. These results suggest that binding to dsRNA and RNase H activity are mutually exclusive, and the Mg2+ concentration is critical for switching between the activities. Changes in the Mg2+ concentration or proteolytic severing of the dsRNA-binding domain could alter the activity or location of the RNase H and may govern access of the enzyme to the substrate. Sequences similar to the dsRNA-binding motif are present in other eukaryotic RNases H and the transactivating protein of cauliflower mosaic virus, suggesting that these proteins may also bind to dsRNA. ; save_ save_ref_2 _Saveframe_category citation _Citation_full . _Citation_title 'Selective cloning of genes encoding RNase H from Salmonella typhimurium, Saccharomyces cerevisiae and Escherichia coli rnh mutant.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 1650910 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Itaya M. . . 2 McKelvin D. . . 3 Chatterjie 'S. K.' K. . 4 Crouch 'R. J.' J. . stop_ _Journal_abbreviation 'Mol. Gen. Genet.' _Journal_name_full 'Molecular & general genetics : MGG' _Journal_volume 227 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 438 _Page_last 445 _Year 1991 _Details ; We have cloned genes encoding RNase H from Escherichia coli rnh mutants, Salmonella typhimurium and Saccharomyces cerevisiae. Selection was accomplished by suppression of the temperature-sensitive growth phenotype of Escherichia coli strains containing the rnh-339::cat and either recB270 (Ts) or recC271 (Ts) mutations. RNases H from E. coli and S. typhimurium contained 155 amino acid residues and differed at only 11 positions. The S. cerevisiae and E. coli RNases H were about 30% homologous. A comparison of the amino acid sequences of several RNases H from cellular and retroviral sources revealed some strongly conserved regions as well as variable regions; the carboxyl-terminus was particularly variable. The overlapping, divergent promoter gene organization found in E. coli was observed to be present in S. typhimurium. ; save_ ################################## # Molecular system description # ################################## save_system_RNase_HI _Saveframe_category molecular_system _Mol_system_name 'ribonuclease HI' _Abbreviation_common 'RNase HI' _Enzyme_commission_number 3.1.26.4 loop_ _Mol_system_component_name _Mol_label 'RNase HI' $RNase_HI stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'fully reduced' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_RNase_HI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'ribonuclease HI' _Abbreviation_common 'RNase HI' _Molecular_mass . _Mol_thiol_state 'fully reduced' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 63 _Mol_residue_sequence ; GSARQGNFYAVRKGRETGIY NTWNECKNQVDGYGGAIYKK FNSYEQAKSFLGQPNTTSNY GSS ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 ALA 4 ARG 5 GLN 6 GLY 7 ASN 8 PHE 9 TYR 10 ALA 11 VAL 12 ARG 13 LYS 14 GLY 15 ARG 16 GLU 17 THR 18 GLY 19 ILE 20 TYR 21 ASN 22 THR 23 TRP 24 ASN 25 GLU 26 CYS 27 LYS 28 ASN 29 GLN 30 VAL 31 ASP 32 GLY 33 TYR 34 GLY 35 GLY 36 ALA 37 ILE 38 TYR 39 LYS 40 LYS 41 PHE 42 ASN 43 SER 44 TYR 45 GLU 46 GLN 47 ALA 48 LYS 49 SER 50 PHE 51 LEU 52 GLY 53 GLN 54 PRO 55 ASN 56 THR 57 THR 58 SER 59 ASN 60 TYR 61 GLY 62 SER 63 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1QHK "N-Terminal Domain Of Saccharomyces Cerevisiae Rnase Hi Reveals A Fold With A Resemblance To The N-Terminal Domain Of Ribosomal " 73.02 47 100.00 100.00 2.98e-24 DBJ GAA25685 "K7_Rnh1p [Saccharomyces cerevisiae Kyokai no. 7]" 96.83 348 100.00 100.00 6.57e-34 EMBL CAA90205 "Rnh1p [Saccharomyces cerevisiae]" 96.83 348 100.00 100.00 6.99e-34 EMBL CAY82065 "Rnh1p [Saccharomyces cerevisiae EC1118]" 96.83 348 100.00 100.00 6.99e-34 GB AHY76689 "Rnh1p [Saccharomyces cerevisiae YJM993]" 96.83 348 100.00 100.00 6.99e-34 GB AJP40928 "Rnh1p [Saccharomyces cerevisiae YJM1078]" 96.83 348 100.00 100.00 6.99e-34 GB AJS62100 "Rnh1p [Saccharomyces cerevisiae YJM189]" 96.83 348 100.00 100.00 6.99e-34 GB AJS62535 "Rnh1p [Saccharomyces cerevisiae YJM193]" 96.83 348 98.36 98.36 3.41e-33 GB AJS62973 "Rnh1p [Saccharomyces cerevisiae YJM195]" 96.83 348 100.00 100.00 6.57e-34 REF NP_013961 "Rnh1p [Saccharomyces cerevisiae S288c]" 96.83 348 100.00 100.00 6.99e-34 SP Q04740 "RecName: Full=Ribonuclease H; Short=RNase H" 96.83 348 100.00 100.00 6.99e-34 TPG DAA10134 "TPA: Rnh1p [Saccharomyces cerevisiae S288c]" 96.83 348 100.00 100.00 6.99e-34 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $RNase_HI 'Baker's yeast' 4932 Eukaryota Fungi Saccharomyces cerevisiae stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $RNase_HI 'recombinant technology' 'Escherichia coli' Escherichia coli BL21(DE3)C41 . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $RNase_HI . mM 1.0 3.0 '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 2.3 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_1 save_ save_COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _Sample_label $sample_1 save_ save_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_1 save_ save_HBHA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label $sample_1 save_ save_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_HCCH-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_1 save_ save_HNHA_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label $sample_1 save_ save_HNHB_9 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.6 0.2 n/a temperature 298 0.3 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_ref _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio TSP H 1 'methyl protons' ppm 0.00 internal direct . internal . . DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chem_shift_ref _Mol_system_component_name 'RNase HI' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 GLY H H 8.72 . 1 2 . 1 GLY HA2 H 3.58 . 1 3 . 1 GLY HA3 H 3.58 . 1 4 . 1 GLY CA C 41.46 . 1 5 . 1 GLY N N 121.52 . 1 6 . 2 SER H H 8.65 . 1 7 . 2 SER HA H 4.41 . 1 8 . 2 SER HB2 H 3.76 . 1 9 . 2 SER HB3 H 3.76 . 1 10 . 2 SER CA C 55.63 . 1 11 . 2 SER CB C 61.70 . 1 12 . 2 SER N N 117.89 . 1 13 . 3 ALA H H 8.53 . 1 14 . 3 ALA HA H 4.27 . 1 15 . 3 ALA HB H 1.27 . 1 16 . 3 ALA CA C 50.16 . 1 17 . 3 ALA CB C 17.05 . 1 18 . 3 ALA N N 128.53 . 1 19 . 4 ARG H H 8.45 . 1 20 . 4 ARG HA H 4.25 . 1 21 . 4 ARG HB2 H 1.65 . 2 22 . 4 ARG HB3 H 1.71 . 2 23 . 4 ARG HG2 H 1.48 . 1 24 . 4 ARG HG3 H 1.48 . 1 25 . 4 ARG HD2 H 3.06 . 1 26 . 4 ARG HD3 H 3.06 . 1 27 . 4 ARG CA C 53.57 . 1 28 . 4 ARG CB C 28.59 . 1 29 . 4 ARG CG C 24.67 . 1 30 . 4 ARG CD C 41.34 . 1 31 . 4 ARG N N 123.00 . 1 32 . 5 GLN H H 8.47 . 1 33 . 5 GLN HA H 4.50 . 1 34 . 5 GLN HB2 H 2.03 . 1 35 . 5 GLN HB3 H 1.92 . 1 36 . 5 GLN HG2 H 2.28 . 1 37 . 5 GLN HG3 H 2.28 . 1 38 . 5 GLN CA C 53.49 . 1 39 . 5 GLN CB C 27.78 . 1 40 . 5 GLN CG C 31.56 . 1 41 . 5 GLN N N 124.48 . 1 42 . 6 GLY H H 8.42 . 1 43 . 6 GLY HA2 H 3.90 . 2 44 . 6 GLY HA3 H 3.70 . 2 45 . 6 GLY CA C 42.70 . 1 46 . 6 GLY N N 112.56 . 1 47 . 7 ASN H H 7.88 . 1 48 . 7 ASN HA H 4.79 . 1 49 . 7 ASN HB2 H 2.10 . 1 50 . 7 ASN HB3 H 2.44 . 1 51 . 7 ASN CA C 50.14 . 1 52 . 7 ASN CB C 39.34 . 1 53 . 7 ASN N N 119.56 . 1 54 . 8 PHE H H 8.34 . 1 55 . 8 PHE HA H 4.80 . 1 56 . 8 PHE HB2 H 2.50 . 1 57 . 8 PHE HB3 H 2.50 . 1 58 . 8 PHE HD1 H 6.97 . 1 59 . 8 PHE HD2 H 6.97 . 1 60 . 8 PHE HE1 H 7.32 . 1 61 . 8 PHE HE2 H 7.32 . 1 62 . 8 PHE CA C 54.20 . 1 63 . 8 PHE CB C 39.35 . 1 64 . 8 PHE CD1 C 129.97 . 1 65 . 8 PHE CD2 C 129.97 . 1 66 . 8 PHE CE1 C 130.72 . 1 67 . 8 PHE CE2 C 130.72 . 1 68 . 8 PHE N N 119.07 . 1 69 . 9 TYR H H 9.68 . 1 70 . 9 TYR HA H 4.86 . 1 71 . 9 TYR HB2 H 2.98 . 1 72 . 9 TYR HB3 H 2.98 . 1 73 . 9 TYR HD1 H 7.04 . 1 74 . 9 TYR HD2 H 7.04 . 1 75 . 9 TYR HE1 H 6.77 . 1 76 . 9 TYR HE2 H 6.77 . 1 77 . 9 TYR CA C 55.37 . 1 78 . 9 TYR CB C 37.07 . 1 79 . 9 TYR CD1 C 131.21 . 1 80 . 9 TYR CD2 C 131.21 . 1 81 . 9 TYR CE1 C 115.72 . 1 82 . 9 TYR CE2 C 115.72 . 1 83 . 9 TYR N N 124.58 . 1 84 . 10 ALA H H 9.40 . 1 85 . 10 ALA HA H 5.16 . 1 86 . 10 ALA HB H 1.60 . 1 87 . 10 ALA CA C 48.57 . 1 88 . 10 ALA CB C 19.81 . 1 89 . 10 ALA N N 130.08 . 1 90 . 11 VAL H H 9.57 . 1 91 . 11 VAL HA H 4.52 . 1 92 . 11 VAL HB H 2.30 . 1 93 . 11 VAL HG2 H 0.66 . 2 94 . 11 VAL HG1 H 0.95 . 2 95 . 11 VAL CA C 59.78 . 1 96 . 11 VAL CB C 31.10 . 1 97 . 11 VAL CG1 C 19.28 . 1 98 . 11 VAL CG2 C 21.20 . 1 99 . 11 VAL N N 126.87 . 1 100 . 12 ARG H H 8.41 . 1 101 . 12 ARG HA H 4.33 . 1 102 . 12 ARG HB2 H 1.48 . 1 103 . 12 ARG HB3 H 1.48 . 1 104 . 12 ARG CA C 53.50 . 1 105 . 12 ARG CB C 28.34 . 1 106 . 12 ARG N N 128.51 . 1 107 . 15 ARG CA C 58.63 . 1 108 . 15 ARG CB C 27.20 . 1 109 . 16 GLU H H 7.09 . 1 110 . 16 GLU HA H 4.39 . 1 111 . 16 GLU HB2 H 1.62 . 2 112 . 16 GLU HB3 H 1.81 . 2 113 . 16 GLU HG2 H 2.20 . 2 114 . 16 GLU HG3 H 2.29 . 2 115 . 16 GLU CA C 52.27 . 1 116 . 16 GLU CB C 28.19 . 1 117 . 16 GLU N N 117.06 . 1 118 . 17 THR CA C 58.53 . 1 119 . 17 THR CB C 68.25 . 1 120 . 18 GLY H H 8.28 . 1 121 . 18 GLY HA2 H 4.19 . 2 122 . 18 GLY HA3 H 3.61 . 2 123 . 18 GLY CA C 42.11 . 1 124 . 18 GLY N N 108.63 . 1 125 . 19 ILE H H 8.04 . 1 126 . 19 ILE HA H 4.77 . 1 127 . 19 ILE HB H 1.48 . 1 128 . 19 ILE HG12 H 0.52 . 1 129 . 19 ILE HG13 H 0.52 . 1 130 . 19 ILE HG2 H 0.84 . 1 131 . 19 ILE HD1 H 0.33 . 1 132 . 19 ILE CA C 57.86 . 1 133 . 19 ILE CB C 37.18 . 1 134 . 19 ILE CG1 C 27.05 . 1 135 . 19 ILE CG2 C 16.74 . 1 136 . 19 ILE CD1 C 11.17 . 1 137 . 19 ILE N N 121.26 . 1 138 . 20 TYR H H 9.46 . 1 139 . 20 TYR HA H 4.90 . 1 140 . 20 TYR HB2 H 3.19 . 1 141 . 20 TYR HB3 H 2.48 . 1 142 . 20 TYR HD1 H 7.04 . 1 143 . 20 TYR HD2 H 7.04 . 1 144 . 20 TYR HE1 H 6.52 . 1 145 . 20 TYR HE2 H 6.52 . 1 146 . 20 TYR CA C 54.41 . 1 147 . 20 TYR CB C 39.65 . 1 148 . 20 TYR CD1 C 131.48 . 1 149 . 20 TYR CD2 C 131.48 . 1 150 . 20 TYR CE1 C 115.33 . 1 151 . 20 TYR CE2 C 115.33 . 1 152 . 20 TYR N N 128.54 . 1 153 . 21 ASN H H 9.43 . 1 154 . 21 ASN HA H 5.17 . 1 155 . 21 ASN HB2 H 2.88 . 1 156 . 21 ASN HB3 H 2.88 . 1 157 . 21 ASN CA C 51.59 . 1 158 . 21 ASN CB C 37.67 . 1 159 . 21 ASN N N 121.37 . 1 160 . 22 THR H H 7.42 . 1 161 . 22 THR HA H 4.81 . 1 162 . 22 THR HB H 4.41 . 1 163 . 22 THR HG2 H 1.15 . 1 164 . 22 THR CA C 56.58 . 1 165 . 22 THR CB C 70.36 . 1 166 . 22 THR CG2 C 19.58 . 1 167 . 22 THR N N 107.61 . 1 168 . 23 TRP H H 9.05 . 1 169 . 23 TRP HA H 3.59 . 1 170 . 23 TRP HB2 H 3.18 . 2 171 . 23 TRP HB3 H 2.84 . 2 172 . 23 TRP HZ2 H 7.36 . 1 173 . 23 TRP HH2 H 6.89 . 1 174 . 23 TRP CA C 55.63 . 1 175 . 23 TRP CB C 26.96 . 1 176 . 23 TRP CZ2 C 112.44 . 1 177 . 23 TRP CH2 C 121.80 . 1 178 . 23 TRP N N 125.95 . 1 179 . 24 ASN H H 8.56 . 1 180 . 24 ASN HA H 3.53 . 1 181 . 24 ASN HB2 H 2.44 . 1 182 . 24 ASN HB3 H 2.44 . 1 183 . 24 ASN CA C 53.85 . 1 184 . 24 ASN CB C 35.31 . 1 185 . 24 ASN N N 117.83 . 1 186 . 25 GLU H H 7.22 . 1 187 . 25 GLU HA H 3.65 . 1 188 . 25 GLU HB2 H 1.90 . 1 189 . 25 GLU HB3 H 1.90 . 1 190 . 25 GLU HG2 H 2.14 . 1 191 . 25 GLU HG3 H 2.14 . 1 192 . 25 GLU CA C 55.83 . 1 193 . 25 GLU CB C 28.17 . 1 194 . 25 GLU CG C 34.72 . 1 195 . 25 GLU N N 117.50 . 1 196 . 26 CYS H H 7.03 . 1 197 . 26 CYS HA H 3.02 . 1 198 . 26 CYS HB2 H 2.34 . 2 199 . 26 CYS HB3 H 1.93 . 2 200 . 26 CYS CA C 59.54 . 1 201 . 26 CYS CB C 24.02 . 1 202 . 26 CYS N N 120.91 . 1 203 . 27 LYS H H 8.39 . 1 204 . 27 LYS HA H 2.80 . 1 205 . 27 LYS HB2 H 0.15 . 1 206 . 27 LYS HB3 H 0.67 . 1 207 . 27 LYS HG2 H 0.77 . 1 208 . 27 LYS HG3 H 0.77 . 1 209 . 27 LYS HD2 H 1.29 . 1 210 . 27 LYS HD3 H 1.29 . 1 211 . 27 LYS CA C 56.45 . 1 212 . 27 LYS CB C 28.47 . 1 213 . 27 LYS CG C 22.42 . 1 214 . 27 LYS CD C 26.86 . 1 215 . 27 LYS CE C 39.55 . 1 216 . 27 LYS N N 122.00 . 1 217 . 28 ASN H H 6.93 . 1 218 . 28 ASN HA H 4.16 . 1 219 . 28 ASN HB2 H 2.47 . 1 220 . 28 ASN HB3 H 2.47 . 1 221 . 28 ASN CA C 52.86 . 1 222 . 28 ASN CB C 35.29 . 1 223 . 28 ASN N N 117.01 . 1 224 . 29 GLN H H 7.60 . 1 225 . 29 GLN HA H 4.51 . 1 226 . 29 GLN HB2 H 2.02 . 2 227 . 29 GLN HB3 H 1.67 . 2 228 . 29 GLN HG2 H 2.42 . 1 229 . 29 GLN HG3 H 2.42 . 1 230 . 29 GLN CA C 52.10 . 1 231 . 29 GLN CB C 26.10 . 1 232 . 29 GLN CG C 28.00 . 1 233 . 29 GLN N N 115.89 . 1 234 . 30 VAL H H 7.06 . 1 235 . 30 VAL HA H 4.44 . 1 236 . 30 VAL HB H 2.03 . 1 237 . 30 VAL HG2 H 0.71 . 2 238 . 30 VAL HG1 H 0.32 . 2 239 . 30 VAL CA C 58.89 . 1 240 . 30 VAL CB C 31.31 . 1 241 . 30 VAL CG1 C 20.11 . 1 242 . 30 VAL CG2 C 15.38 . 1 243 . 30 VAL N N 109.31 . 1 244 . 31 ASP H H 8.61 . 1 245 . 31 ASP HA H 4.40 . 1 246 . 31 ASP HB2 H 2.47 . 1 247 . 31 ASP HB3 H 2.47 . 1 248 . 31 ASP CA C 53.83 . 1 249 . 31 ASP CB C 38.06 . 1 250 . 31 ASP N N 126.87 . 1 251 . 32 GLY H H 9.24 . 1 252 . 32 GLY HA2 H 3.98 . 2 253 . 32 GLY HA3 H 3.68 . 2 254 . 32 GLY CA C 43.80 . 1 255 . 32 GLY N N 117.79 . 1 256 . 33 TYR H H 7.78 . 1 257 . 33 TYR HA H 4.36 . 1 258 . 33 TYR HB2 H 3.18 . 2 259 . 33 TYR HB3 H 2.15 . 2 260 . 33 TYR HD1 H 6.77 . 1 261 . 33 TYR HD2 H 6.77 . 1 262 . 33 TYR HE1 H 6.58 . 1 263 . 33 TYR HE2 H 6.58 . 1 264 . 33 TYR CA C 54.40 . 1 265 . 33 TYR CB C 37.07 . 1 266 . 33 TYR CD1 C 131.50 . 1 267 . 33 TYR CD2 C 131.50 . 1 268 . 33 TYR CE1 C 115.63 . 1 269 . 33 TYR CE2 C 115.63 . 1 270 . 33 TYR N N 125.02 . 1 271 . 34 GLY H H 8.52 . 1 272 . 34 GLY HA2 H 3.77 . 2 273 . 34 GLY HA3 H 3.41 . 2 274 . 34 GLY CA C 44.37 . 1 275 . 34 GLY N N 120.21 . 1 276 . 35 GLY H H 8.92 . 1 277 . 35 GLY HA2 H 3.82 . 2 278 . 35 GLY HA3 H 3.73 . 2 279 . 35 GLY CA C 43.40 . 1 280 . 35 GLY N N 115.03 . 1 281 . 36 ALA H H 7.61 . 1 282 . 36 ALA HA H 4.08 . 1 283 . 36 ALA HB H 1.76 . 1 284 . 36 ALA CA C 50.67 . 1 285 . 36 ALA CB C 17.77 . 1 286 . 36 ALA N N 121.38 . 1 287 . 37 ILE H H 9.02 . 1 288 . 37 ILE HA H 4.62 . 1 289 . 37 ILE HB H 1.61 . 1 290 . 37 ILE HG12 H 1.17 . 1 291 . 37 ILE HG13 H 1.17 . 1 292 . 37 ILE HG2 H 0.94 . 1 293 . 37 ILE HD1 H 0.83 . 1 294 . 37 ILE CA C 58.12 . 1 295 . 37 ILE CB C 39.43 . 1 296 . 37 ILE CG1 C 23.89 . 1 297 . 37 ILE CG2 C 15.48 . 1 298 . 37 ILE CD1 C 11.07 . 1 299 . 37 ILE N N 122.41 . 1 300 . 38 TYR H H 8.74 . 1 301 . 38 TYR HA H 6.10 . 1 302 . 38 TYR HB2 H 3.01 . 2 303 . 38 TYR HB3 H 2.92 . 2 304 . 38 TYR HD1 H 6.89 . 1 305 . 38 TYR HD2 H 6.89 . 1 306 . 38 TYR HE1 H 6.95 . 1 307 . 38 TYR HE2 H 6.95 . 1 308 . 38 TYR CA C 53.32 . 1 309 . 38 TYR CB C 40.38 . 1 310 . 38 TYR CD1 C 131.38 . 1 311 . 38 TYR CD2 C 131.38 . 1 312 . 38 TYR CE1 C 116.19 . 1 313 . 38 TYR CE2 C 116.19 . 1 314 . 38 TYR N N 127.69 . 1 315 . 39 LYS H H 8.72 . 1 316 . 39 LYS HA H 4.00 . 1 317 . 39 LYS HB2 H 0.88 . 1 318 . 39 LYS HB3 H 0.47 . 1 319 . 39 LYS HG2 H 0.27 . 1 320 . 39 LYS HG3 H 0.27 . 1 321 . 39 LYS HD2 H 0.74 . 1 322 . 39 LYS HD3 H 0.74 . 1 323 . 39 LYS CA C 54.25 . 1 324 . 39 LYS CB C 34.73 . 1 325 . 39 LYS CG C 23.04 . 1 326 . 39 LYS CD C 28.60 . 1 327 . 39 LYS CE C 39.91 . 1 328 . 39 LYS N N 123.09 . 1 329 . 40 LYS H H 8.07 . 1 330 . 40 LYS HA H 4.52 . 1 331 . 40 LYS HB2 H 1.29 . 1 332 . 40 LYS HB3 H 1.29 . 1 333 . 40 LYS HG2 H 0.27 . 1 334 . 40 LYS HG3 H 0.27 . 1 335 . 40 LYS HD2 H 0.72 . 1 336 . 40 LYS HD3 H 0.72 . 1 337 . 40 LYS CA C 53.24 . 1 338 . 40 LYS CB C 32.22 . 1 339 . 40 LYS CG C 22.21 . 1 340 . 40 LYS CD C 28.60 . 1 341 . 40 LYS CE C 39.67 . 1 342 . 40 LYS N N 127.43 . 1 343 . 41 PHE H H 9.17 . 1 344 . 41 PHE HA H 4.73 . 1 345 . 41 PHE HB2 H 3.31 . 2 346 . 41 PHE HB3 H 2.59 . 2 347 . 41 PHE HD1 H 7.13 . 1 348 . 41 PHE HD2 H 7.13 . 1 349 . 41 PHE HE1 H 6.87 . 1 350 . 41 PHE HE2 H 6.87 . 1 351 . 41 PHE CA C 54.71 . 1 352 . 41 PHE CB C 42.59 . 1 353 . 41 PHE CD1 C 130.04 . 1 354 . 41 PHE CD2 C 130.04 . 1 355 . 41 PHE CE1 C 128.80 . 1 356 . 41 PHE CE2 C 128.80 . 1 357 . 41 PHE N N 124.96 . 1 358 . 42 ASN H H 9.11 . 1 359 . 42 ASN HA H 5.30 . 1 360 . 42 ASN HB2 H 2.90 . 1 361 . 42 ASN HB3 H 2.90 . 1 362 . 42 ASN CA C 50.74 . 1 363 . 42 ASN CB C 37.06 . 1 364 . 42 ASN N N 119.50 . 1 365 . 43 SER H H 7.37 . 1 366 . 43 SER HA H 4.72 . 1 367 . 43 SER HB2 H 4.01 . 2 368 . 43 SER HB3 H 3.72 . 2 369 . 43 SER CA C 53.61 . 1 370 . 43 SER CB C 63.48 . 1 371 . 43 SER N N 112.89 . 1 372 . 44 TYR H H 8.61 . 1 373 . 44 TYR HA H 2.86 . 1 374 . 44 TYR HB2 H 2.37 . 2 375 . 44 TYR HB3 H 2.14 . 2 376 . 44 TYR HD1 H 6.64 . 1 377 . 44 TYR HD2 H 6.64 . 1 378 . 44 TYR HE1 H 6.63 . 1 379 . 44 TYR HE2 H 6.63 . 1 380 . 44 TYR CA C 59.22 . 1 381 . 44 TYR CB C 35.92 . 1 382 . 44 TYR CD1 C 130.80 . 1 383 . 44 TYR CD2 C 130.80 . 1 384 . 44 TYR CE1 C 115.86 . 1 385 . 44 TYR CE2 C 115.86 . 1 386 . 44 TYR N N 130.00 . 1 387 . 45 GLU H H 8.68 . 1 388 . 45 GLU HA H 3.54 . 1 389 . 45 GLU HB2 H 1.78 . 1 390 . 45 GLU HB3 H 1.78 . 1 391 . 45 GLU HG2 H 2.20 . 1 392 . 45 GLU HG3 H 2.20 . 1 393 . 45 GLU CA C 57.43 . 1 394 . 45 GLU CB C 26.06 . 1 395 . 45 GLU CG C 32.62 . 1 396 . 45 GLU N N 118.98 . 1 397 . 46 GLN H H 7.31 . 1 398 . 46 GLN HA H 3.65 . 1 399 . 46 GLN HB2 H 1.72 . 1 400 . 46 GLN HB3 H 1.72 . 1 401 . 46 GLN HG2 H 2.20 . 1 402 . 46 GLN HG3 H 2.20 . 1 403 . 46 GLN CA C 56.04 . 1 404 . 46 GLN CB C 26.96 . 1 405 . 46 GLN CG C 32.37 . 1 406 . 46 GLN N N 119.92 . 1 407 . 47 ALA H H 6.92 . 1 408 . 47 ALA HA H 3.11 . 1 409 . 47 ALA HB H 1.10 . 1 410 . 47 ALA CA C 51.82 . 1 411 . 47 ALA CB C 15.84 . 1 412 . 47 ALA N N 124.75 . 1 413 . 48 LYS H H 8.17 . 1 414 . 48 LYS HA H 3.45 . 1 415 . 48 LYS HB2 H 1.43 . 2 416 . 48 LYS HB3 H 1.13 . 2 417 . 48 LYS HG2 H 1.02 . 1 418 . 48 LYS HG3 H 1.02 . 1 419 . 48 LYS HD2 H 0.32 . 1 420 . 48 LYS HD3 H 0.32 . 1 421 . 48 LYS CA C 57.74 . 1 422 . 48 LYS CB C 29.31 . 1 423 . 48 LYS CG C 26.35 . 1 424 . 48 LYS CD C 33.65 . 1 425 . 48 LYS CE C 36.36 . 1 426 . 48 LYS N N 119.86 . 1 427 . 49 SER H H 7.76 . 1 428 . 49 SER HA H 3.97 . 1 429 . 49 SER HB2 H 3.65 . 1 430 . 49 SER HB3 H 3.65 . 1 431 . 49 SER CA C 56.75 . 1 432 . 49 SER CB C 60.82 . 1 433 . 49 SER N N 117.13 . 1 434 . 50 PHE H H 7.42 . 1 435 . 50 PHE HA H 4.15 . 1 436 . 50 PHE HB2 H 3.00 . 2 437 . 50 PHE HB3 H 2.84 . 2 438 . 50 PHE HD1 H 7.29 . 1 439 . 50 PHE HD2 H 7.29 . 1 440 . 50 PHE HE1 H 7.18 . 1 441 . 50 PHE HE2 H 7.18 . 1 442 . 50 PHE HZ H 7.32 . 1 443 . 50 PHE CA C 58.28 . 1 444 . 50 PHE CB C 37.83 . 1 445 . 50 PHE CD1 C 129.45 . 1 446 . 50 PHE CD2 C 129.45 . 1 447 . 50 PHE CE1 C 129.90 . 1 448 . 50 PHE CE2 C 129.90 . 1 449 . 50 PHE CZ C 130.72 . 1 450 . 50 PHE N N 124.17 . 1 451 . 51 LEU H H 7.52 . 1 452 . 51 LEU HA H 3.72 . 1 453 . 51 LEU HB2 H 1.57 . 1 454 . 51 LEU HB3 H 1.65 . 1 455 . 51 LEU HG H 1.77 . 1 456 . 51 LEU HD1 H 0.76 . 2 457 . 51 LEU HD2 H 0.73 . 2 458 . 51 LEU CA C 54.14 . 1 459 . 51 LEU CB C 39.41 . 1 460 . 51 LEU CG C 24.73 . 1 461 . 51 LEU CD1 C 23.16 . 1 462 . 51 LEU CD2 C 21.26 . 1 463 . 51 LEU N N 118.71 . 1 464 . 52 GLY H H 7.53 . 1 465 . 52 GLY HA2 H 3.86 . 2 466 . 52 GLY HA3 H 3.67 . 2 467 . 52 GLY CA C 42.82 . 1 468 . 52 GLY N N 106.66 . 1 469 . 53 GLN H H 7.70 . 1 470 . 53 GLN HA H 4.45 . 1 471 . 53 GLN HB2 H 1.92 . 1 472 . 53 GLN HB3 H 1.73 . 1 473 . 53 GLN HG2 H 2.31 . 1 474 . 53 GLN HG3 H 2.31 . 1 475 . 53 GLN CA C 51.28 . 1 476 . 53 GLN CB C 26.34 . 1 477 . 53 GLN CG C 31.14 . 1 478 . 53 GLN N N 122.66 . 1 479 . 54 PRO HA H 4.53 . 1 480 . 54 PRO HB2 H 2.10 . 2 481 . 54 PRO HB3 H 1.80 . 2 482 . 54 PRO HG2 H 1.89 . 1 483 . 54 PRO HG3 H 1.89 . 1 484 . 54 PRO HD2 H 3.65 . 2 485 . 54 PRO HD3 H 3.53 . 2 486 . 54 PRO CA C 60.93 . 1 487 . 54 PRO CB C 30.05 . 1 488 . 54 PRO CG C 25.03 . 1 489 . 54 PRO CD C 48.32 . 1 490 . 55 ASN H H 8.55 . 1 491 . 55 ASN HA H 4.62 . 1 492 . 55 ASN HB2 H 2.73 . 2 493 . 55 ASN HB3 H 2.68 . 2 494 . 55 ASN CA C 51.01 . 1 495 . 55 ASN CB C 36.50 . 1 496 . 55 ASN N N 120.67 . 1 497 . 56 THR H H 8.13 . 1 498 . 56 THR HA H 4.36 . 1 499 . 56 THR HB H 4.23 . 1 500 . 56 THR HG2 H 1.24 . 1 501 . 56 THR CA C 59.03 . 1 502 . 56 THR CB C 67.28 . 1 503 . 56 THR CG2 C 19.37 . 1 504 . 56 THR N N 115.82 . 1 505 . 57 THR H H 8.22 . 1 506 . 57 THR HA H 4.31 . 1 507 . 57 THR HB H 4.18 . 1 508 . 57 THR HG2 H 1.04 . 1 509 . 57 THR CA C 60.25 . 1 510 . 57 THR CB C 68.25 . 1 511 . 57 THR CG2 C 19.48 . 1 512 . 57 THR N N 116.78 . 1 513 . 58 SER H H 8.30 . 1 514 . 58 SER HA H 4.32 . 1 515 . 58 SER HB2 H 3.69 . 1 516 . 58 SER HB3 H 3.69 . 1 517 . 58 SER CA C 55.64 . 1 518 . 58 SER CB C 61.35 . 1 519 . 58 SER N N 119.92 . 1 520 . 59 ASN H H 8.41 . 1 521 . 59 ASN HA H 4.62 . 1 522 . 59 ASN HB2 H 2.65 . 2 523 . 59 ASN HB3 H 2.59 . 2 524 . 59 ASN CA C 51.03 . 1 525 . 59 ASN CB C 36.29 . 1 526 . 59 ASN N N 122.75 . 1 527 . 60 TYR H H 8.20 . 1 528 . 60 TYR HA H 4.44 . 1 529 . 60 TYR HB2 H 3.00 . 2 530 . 60 TYR HB3 H 2.84 . 2 531 . 60 TYR HD1 H 7.10 . 1 532 . 60 TYR HD2 H 7.10 . 1 533 . 60 TYR HE1 H 6.80 . 1 534 . 60 TYR HE2 H 6.80 . 1 535 . 60 TYR CA C 56.00 . 1 536 . 60 TYR CB C 36.29 . 1 537 . 60 TYR CD1 C 131.19 . 1 538 . 60 TYR CD2 C 131.19 . 1 539 . 60 TYR CE1 C 116.07 . 1 540 . 60 TYR CE2 C 116.07 . 1 541 . 60 TYR N N 122.90 . 1 542 . 61 GLY H H 8.31 . 1 543 . 61 GLY HA2 H 3.82 . 1 544 . 61 GLY HA3 H 3.82 . 1 545 . 61 GLY CA C 42.90 . 1 546 . 61 GLY N N 112.94 . 1 547 . 62 SER H H 8.14 . 1 548 . 62 SER HA H 4.43 . 1 549 . 62 SER HB2 H 3.78 . 1 550 . 62 SER HB3 H 3.78 . 1 551 . 62 SER CA C 56.28 . 1 552 . 62 SER CB C 62.43 . 1 553 . 62 SER N N 117.90 . 1 554 . 63 SER H H 8.12 . 1 555 . 63 SER HA H 4.40 . 1 556 . 63 SER HB2 H 2.91 . 1 557 . 63 SER HB3 H 2.91 . 1 558 . 63 SER CA C 57.48 . 1 559 . 63 SER N N 124.09 . 1 stop_ save_