data_6005 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structural Basis for Recognition of the mRNA Class II AU-Rich Element by the Tandem Zinc Finger Domain of TIS11d ; _BMRB_accession_number 6005 _BMRB_flat_file_name bmr6005.str _Entry_type original _Submission_date 2003-11-13 _Accession_date 2003-11-14 _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 Hudson Brian P. . 2 Martinez-Yamout Maria A. . 3 Dyson H. Jane . 4 Wright Peter E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 443 "13C chemical shifts" 282 "15N chemical shifts" 70 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-11-14 original author . stop_ _Original_release_date 2005-11-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Recognition of the mRNA AU-Rich Element by the Zinc Finger Domain of TIS11d ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14981510 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hudson Brian P. . 2 Martinez-Yamout Maria A. . 3 Dyson H. Jane . 4 Wright Peter E. . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_volume 11 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 257 _Page_last 264 _Year 2004 _Details . loop_ _Keyword butyrate complex 'degradation ARE UTR Nup475' ERF intercalate intercalation 'response factor' single-stranded TIS11 'TTP tristetraprolin RNA' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_reference_6 _Saveframe_category citation _Citation_full ; 1: Nie XF, Maclean KN, Kumar V, McKay IA, Bustin SA. Gene. 1995 Jan 23;152(2):285-6. ; _Citation_title 'ERF-2, the human homologue of the murine Tis11d early response gene.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 7835719 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nie 'X. F.' F. . 2 Maclean 'K. N.' N. . 3 Kumar V. . . 4 McKay 'I. A.' A. . 5 Bustin 'S. A.' A. . stop_ _Journal_abbreviation Gene _Journal_name_full Gene _Journal_volume 152 _Journal_issue 2 _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 285 _Page_last 286 _Year 1995 _Details ; A human cDNA specifying a member of the Tis11 early response gene family was cloned and sequenced. The human gene differs from its mouse homologue by encoding an additional 97 amino acids at its C-terminal end. The sequence has transactivation-like motifs, an unusual Cys-Ser-Ala-rich motif and displays sequence similarity at the extreme C-terminal end with another Tis11 family member, ERF-1. ; save_ save_reference_22 _Saveframe_category citation _Citation_full ; Nie XF, Maclean KN, Kumar V, McKay IA, Bustin SA. Gene. 1995 Jan 23;152(2):285-6. ; _Citation_title 'Characteristics of the interaction of a synthetic human tristetraprolin tandem zinc finger peptide with AU-rich element-containing RNA substrates.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12639954 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Blackshear 'Perry J.' J. . 2 Lai 'Wi S.' S. . 3 Kennington 'Elizabeth A.' A. . 4 Brewer Gary . . 5 Wilson 'Gerald M.' M. . 6 Guan Xiaoju . . 7 Zhou Pei . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 278 _Journal_issue 22 _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 19947 _Page_last 19955 _Year 2003 _Details ; Tristetraprolin (TTP) and its two known mammalian family members are tandem CCCH zinc finger proteins that can bind to AU-rich elements (AREs) in cellular mRNAs and destabilize those transcripts, apparently by initiating their deadenylation. Previous studies have shown that the approximately 70-amino acid tandem zinc finger domain of TTP is required and sufficient for RNA binding, and that the integrity of both zinc fingers is also required. However, little is known about the kinetics or structure of the peptide-RNA interaction, in part because of difficulties in obtaining soluble recombinant protein or peptides. We characterized the binding of a synthetic 73-amino acid peptide from human TTP to the tumor necrosis factor (TNF) ARE by gel mobility shift analyses and fluorescence anisotropy experiments. Both types of studies yielded a peptide-RNA dissociation constant of approximately 10 nM. Surprisingly, we found that the "footprint" from the TNF ARE required for peptide binding was only approximately 9 bases and that two molecules of peptide could bind to probes containing as little as 19 bases. An identical recombinant peptide exhibited gel shift characteristics similar to those of the synthetic peptide. NMR analysis of the 15N-labeled recombinant peptide suggested that its first zinc finger was structured in solution but that the second was not. The titration of oligonucleotides representing 17, 13, and even 9 bases of the TNF ARE caused an essentially identical, dramatic shift of existing resonances, and the appearance of new resonances in the peptide spectra, so that all amino acids could be assigned. These data suggest that this TTP peptide-RNA complex is structured in solution and might be amenable to NMR structure determination. ; save_ ################################## # Molecular system description # ################################## save_system_TIS11d _Saveframe_category molecular_system _Mol_system_name "TIS11d TZF/ 5'-UUAUUUAUU-3' complex" _Abbreviation_common TIS11d _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'TIS11d TZF' $TIS11d 5'-UUAUUUAUU-3' $UUAUUUAUU 'ZINC (II) ION 1' $ZN 'ZINC (II) ION 2' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all other bound' loop_ _Biological_function 'mRNA degradation' 'single-stranded RNA binding' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TIS11d _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'TIS11d TZF' _Abbreviation_common TIS11d _Molecular_mass 8298 _Mol_thiol_state 'all other bound' _Details 'Contains two CCCH (CX8CX5CX3H) zinc fingers separated by an 18-aa linker' ############################## # Polymer residue sequence # ############################## _Residue_count 70 _Mol_residue_sequence ; STRYKTELCRPFEESGTCKY GEKCQFAHGFHELRSLTRHP KYKTELCRTFHTIGFCPYGP RCHFIHNADE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 151 SER 2 152 THR 3 153 ARG 4 154 TYR 5 155 LYS 6 156 THR 7 157 GLU 8 158 LEU 9 159 CYS 10 160 ARG 11 161 PRO 12 162 PHE 13 163 GLU 14 164 GLU 15 165 SER 16 166 GLY 17 167 THR 18 168 CYS 19 169 LYS 20 170 TYR 21 171 GLY 22 172 GLU 23 173 LYS 24 174 CYS 25 175 GLN 26 176 PHE 27 177 ALA 28 178 HIS 29 179 GLY 30 180 PHE 31 181 HIS 32 182 GLU 33 183 LEU 34 184 ARG 35 185 SER 36 186 LEU 37 187 THR 38 188 ARG 39 189 HIS 40 190 PRO 41 191 LYS 42 192 TYR 43 193 LYS 44 194 THR 45 195 GLU 46 196 LEU 47 197 CYS 48 198 ARG 49 199 THR 50 200 PHE 51 201 HIS 52 202 THR 53 203 ILE 54 204 GLY 55 205 PHE 56 206 CYS 57 207 PRO 58 208 TYR 59 209 GLY 60 210 PRO 61 211 ARG 62 212 CYS 63 213 HIS 64 214 PHE 65 215 ILE 66 216 HIS 67 217 ASN 68 218 ALA 69 219 ASP 70 220 GLU stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 1RGO 'Structural Basis For Recognition Of The Mrna Class Ii Au- Rich Element By The Tandem Zinc Finger Domain Of Tis11d' 100.00 70 100.00 100.00 2.45e-33 stop_ save_ save_UUAUUUAUU _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class RNA _Name_common 5'-UUAUUUAUU-3' _Abbreviation_common UUAUUUAUU _Molecular_mass 2830 _Mol_thiol_state 'not present' _Details . _Residue_count 7 _Mol_residue_sequence UUAUUUAUU loop_ _Residue_seq_code _Residue_label 1 U 2 U 3 A 4 U 5 U 6 U 7 A 8 U 9 U stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jul 25 12:26:23 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ $TIS11d Human 9606 Eukaryota Metazoa Homo sapiens liver $UUAUUUAUU Human 9606 Eukaryota Metazoa Homo sapiens . stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $TIS11d 'recombinant technology' 'E. coli' . . BL21(DE3) plasmid pET21a . $UUAUUUAUU vendor . . . . . . 'synthesized by Dharmacon, Inc.' 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 _Isotopic_labeling $TIS11d 0.5 mM [U-15N] $UUAUUUAUU 0.5 mM . TrisHCl 10 mM . KCl 20 mM . DTT 2.5 mM . ZnSO4 25 uM . H20 95 % . D2O 5 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TIS11d 0.5 mM '[U-13C; U-15N]' $UUAUUUAUU 0.5 mM . TrisHCl 10 mM . KCl 20 mM . DTT 2.5 mM . ZnSO4 25 uM . H20 95 % . D2O 5 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TIS11d 0.5 mM '[U-13C; U-15N]' $UUAUUUAUU 0.5 mM . Tris-HCl 10 mM . KCl 20 mM . DTT 2.5 mM . ZnSO4 25 uM . D2O 100 % . stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type d_bicell_solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TIS11d 0.5 mM '[U-13C; U-15N]' $UUAUUUAUU 0.5 mM . TrisHCl 10 mM . KCl 20 mM . DTT 2.5 mM . ZnSO4 25 uM . 'Pf1 filamentous phage' 12 mg/mL . D2O 100 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 2.1 loop_ _Task 'data collection' stop_ _Details Bruker save_ save_NMRpipe _Saveframe_category software _Name NMRPipe _Version 2.1 loop_ _Task 'data processing' stop_ _Details ; Delaglio, F., Grzesiek, S., Vuister, G.W., Guang, Z., Pfeifer, J. and Bax, A. (1995) J. Biomol. NMR 6, 277-293 ; save_ save_NMRVIEW _Saveframe_category software _Name NMRView _Version 5.0 loop_ _Task 'data analysis' stop_ _Details ; Johnson, B.A. and Blevins, R.A. (1994) J. Biomol. NMR 4, 603-614 ; save_ save_SANE _Saveframe_category software _Name SANE _Version n/a loop_ _Task 'automatic NOE assignment' stop_ _Details ; Duggan, B.M., Legge, G.B., Dyson, H.J., & Wright, P.E. (2001) J. Biomol. NMR 19, 321-329 In-house developed software ; save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'structure determination' stop_ _Details ; Gunter, P., Mumenthaler, C. and Wuthrich, K. (1997) J. Mol. Biol. 273, 283-298 ; save_ save_AMBER _Saveframe_category software _Name AMBER _Version 8.0 loop_ _Task 'structure refinement' stop_ _Details ; Case, D.A., Pearlman, D.A., Caldwell, J.W., Cheatham III, T.E., Wang, J., Ross, W.S. Simmerling, C., Darden, T., Merz, K.M., Stanton, R.V., Cheng, A., Vincent, J.J. Crowley, M., Tsui, V., Gohlke, H., Radmer, R., et al. and Kollman, P.A. (1999) University of California, San Francisco. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_1H-15N-HMQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-15N-HMQC _Sample_label . save_ save_1H-13C-HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-13C-HSQC _Sample_label . save_ save_1H-13C-CT-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-13C-CT-HSQC _Sample_label . save_ save_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCO_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_C(CO)NH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH-TOCSY _Sample_label . save_ save_H(CCO)NH-TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH-TOCSY _Sample_label . save_ save_CCH-COSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name CCH-COSY _Sample_label . save_ save_CCH-TOCSY_11 _Saveframe_category NMR_applied_experiment _Experiment_name CCH-TOCSY _Sample_label . save_ save_H(C)CH-COSY_12 _Saveframe_category NMR_applied_experiment _Experiment_name H(C)CH-COSY _Sample_label . save_ save_H(C)CH-TOCSY_13 _Saveframe_category NMR_applied_experiment _Experiment_name H(C)CH-TOCSY _Sample_label . save_ save_(HB)CB(CGCD)HD_14 _Saveframe_category NMR_applied_experiment _Experiment_name (HB)CB(CGCD)HD _Sample_label . save_ save_(HB)CB(CGCDCE)HE_15 _Saveframe_category NMR_applied_experiment _Experiment_name (HB)CB(CGCDCE)HE _Sample_label . save_ save_3D_15N-separated_NOESY_16 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_3D_13C-separated_NOESY_17 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _Sample_label . save_ save_3D_13C_F1-edited,_F3-separated_NOESY_18 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C F1-edited, F3-separated NOESY' _Sample_label . save_ save_2D_13C_double-half-filtered_NOESY_19 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C double-half-filtered NOESY' _Sample_label . save_ save_2D_13C_double-half-filtered_TOCSY_20 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 13C double-half-filtered TOCSY' _Sample_label . save_ save_HNHA_21 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_HNHB_22 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _Sample_label . save_ save_HACAHB-COSY_23 _Saveframe_category NMR_applied_experiment _Experiment_name HACAHB-COSY _Sample_label . save_ save_13C-{13CO}_spin-echo_difference_CT-HSQC_24 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-{13CO} spin-echo difference CT-HSQC' _Sample_label . save_ save_13C-{15N}_spin-echo_difference_CT-HSQC_25 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-{15N} spin-echo difference CT-HSQC' _Sample_label . save_ save_IPAP-[1H,15N]-HSQC_26 _Saveframe_category NMR_applied_experiment _Experiment_name IPAP-[1H,15N]-HSQC _Sample_label . save_ save_IPAP-HNCO_27 _Saveframe_category NMR_applied_experiment _Experiment_name IPAP-HNCO _Sample_label . save_ ####################### # Sample conditions # ####################### save_Conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.02 . M pH 6.2 0.1 pH temperature 298 0.5 K stop_ save_ save_Conditions_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.02 . M pH 6.2 0.1 pH temperature 298 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 DSS C 13 'methyl protons' ppm 0.00 external direct . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 external direct . . . 1.00000 DSS N 15 'methyl protons' ppm 0.00 external direct . . . 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_protein_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_3 stop_ _Sample_conditions_label $Conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'TIS11d TZF' _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 . 2 THR CA C 62.281 0.08 1 2 . 2 THR CB C 69.097 0.08 1 3 . 2 THR CG2 C 21.384 0.08 1 4 . 2 THR HA H 4.368 0.02 1 5 . 2 THR HB H 4.257 0.02 1 6 . 2 THR HG2 H 1.243 0.02 1 7 . 2 THR C C 176.609 0.08 1 8 . 3 ARG CG C 27.565 0.08 1 9 . 3 ARG H H 8.368 0.02 1 10 . 3 ARG HA H 4.100 0.02 1 11 . 3 ARG HB3 H 1.482 0.02 2 12 . 3 ARG HB2 H 1.250 0.02 2 13 . 3 ARG HD3 H 3.223 0.02 2 14 . 3 ARG HD2 H 3.128 0.02 2 15 . 3 ARG HE H 7.075 0.02 1 16 . 3 ARG HG3 H 1.606 0.02 2 17 . 3 ARG HG2 H 1.474 0.02 2 18 . 3 ARG N N 120.796 0.07 1 19 . 3 ARG NE N 115.589 0.07 1 20 . 3 ARG CA C 55.266 0.08 1 21 . 3 ARG CB C 29.490 0.08 1 22 . 3 ARG CD C 42.808 0.08 1 23 . 3 ARG C C 175.917 0.08 1 24 . 4 TYR CA C 59.056 0.08 1 25 . 4 TYR CB C 39.186 0.08 1 26 . 4 TYR CD1 C 132.617 0.08 3 27 . 4 TYR CE1 C 117.293 0.08 3 28 . 4 TYR H H 7.329 0.02 1 29 . 4 TYR HA H 3.910 0.02 1 30 . 4 TYR HB2 H 3.058 0.02 1 31 . 4 TYR HB3 H 2.587 0.02 1 32 . 4 TYR N N 123.822 0.07 1 33 . 4 TYR HD1 H 6.935 0.02 1 34 . 4 TYR HD2 H 6.935 0.02 1 35 . 4 TYR HE1 H 6.671 0.02 1 36 . 4 TYR HE2 H 6.671 0.02 1 37 . 4 TYR C C 173.884 0.08 1 38 . 5 LYS CA C 58.859 0.08 1 39 . 5 LYS CB C 29.822 0.08 1 40 . 5 LYS CD C 29.992 0.08 1 41 . 5 LYS CE C 42.369 0.08 1 42 . 5 LYS CG C 26.560 0.08 1 43 . 5 LYS H H 8.168 0.02 1 44 . 5 LYS HA H 3.251 0.02 1 45 . 5 LYS HB3 H 1.073 0.02 2 46 . 5 LYS HB2 H 0.975 0.02 2 47 . 5 LYS HE3 H 2.881 0.02 2 48 . 5 LYS HE2 H 2.477 0.02 2 49 . 5 LYS HG3 H -0.280 0.02 2 50 . 5 LYS HG2 H -0.475 0.02 2 51 . 5 LYS N N 122.688 0.07 1 52 . 5 LYS HD3 H 1.726 0.02 1 53 . 5 LYS HD2 H 1.726 0.02 1 54 . 5 LYS C C 173.383 0.08 1 55 . 6 THR CA C 61.880 0.08 1 56 . 6 THR CB C 70.477 0.08 1 57 . 6 THR CG2 C 29.870 0.08 1 58 . 6 THR H H 7.501 0.02 1 59 . 6 THR HA H 4.614 0.02 1 60 . 6 THR HB H 4.265 0.02 1 61 . 6 THR N N 106.465 0.07 1 62 . 6 THR HG2 H 0.924 0.02 1 63 . 6 THR C C 174.637 0.08 1 64 . 7 GLU CA C 54.611 0.08 1 65 . 7 GLU CB C 34.692 0.08 1 66 . 7 GLU CG C 37.240 0.08 1 67 . 7 GLU H H 9.025 0.02 1 68 . 7 GLU HA H 4.680 0.02 1 69 . 7 GLU HG3 H 2.534 0.02 2 70 . 7 GLU HG2 H 2.472 0.02 2 71 . 7 GLU N N 126.389 0.07 1 72 . 7 GLU HB3 H 2.166 0.02 1 73 . 7 GLU HB2 H 2.166 0.02 1 74 . 7 GLU C C 175.273 0.08 1 75 . 8 LEU CA C 55.653 0.08 1 76 . 8 LEU CB C 41.905 0.08 1 77 . 8 LEU CD1 C 25.711 0.08 2 78 . 8 LEU CD2 C 22.155 0.08 2 79 . 8 LEU CG C 26.862 0.08 1 80 . 8 LEU H H 8.882 0.02 1 81 . 8 LEU HA H 4.383 0.02 1 82 . 8 LEU HB2 H 1.800 0.02 1 83 . 8 LEU HB3 H 1.468 0.02 1 84 . 8 LEU HG H 1.787 0.02 1 85 . 8 LEU N N 125.966 0.07 1 86 . 8 LEU HD1 H 0.915 0.02 4 87 . 8 LEU HD2 H 0.642 0.02 4 88 . 8 LEU C C 177.058 0.08 1 89 . 9 CYS CA C 59.313 0.08 1 90 . 9 CYS CB C 31.864 0.08 1 91 . 9 CYS H H 9.672 0.02 1 92 . 9 CYS HA H 4.761 0.02 1 93 . 9 CYS HB2 H 3.243 0.02 1 94 . 9 CYS HB3 H 2.801 0.02 1 95 . 9 CYS N N 128.914 0.07 1 96 . 9 CYS C C 176.962 0.08 1 97 . 10 ARG HG3 H 1.785 0.02 2 98 . 10 ARG HG2 H 1.739 0.02 2 99 . 10 ARG N N 106.073 0.07 1 100 . 10 ARG NE N 114.400 0.07 1 101 . 10 ARG CA C 60.739 0.08 1 102 . 10 ARG CB C 27.938 0.08 1 103 . 10 ARG CD C 42.982 0.08 1 104 . 10 ARG CG C 27.118 0.08 1 105 . 10 ARG H H 10.880 0.02 1 106 . 10 ARG HA H 4.380 0.02 1 107 . 10 ARG HB3 H 1.775 0.02 2 108 . 10 ARG HB2 H 1.561 0.02 2 109 . 10 ARG HD3 H 3.117 0.02 2 110 . 10 ARG HD2 H 2.988 0.02 2 111 . 10 ARG HE H 7.150 0.02 1 112 . 11 PRO CA C 66.518 0.08 1 113 . 11 PRO CB C 31.471 0.08 1 114 . 11 PRO CD C 50.198 0.08 1 115 . 11 PRO CG C 28.773 0.08 1 116 . 11 PRO HA H 4.454 0.02 1 117 . 11 PRO HB3 H 2.480 0.02 2 118 . 11 PRO HB2 H 2.199 0.02 2 119 . 11 PRO HD3 H 5.197 0.02 2 120 . 11 PRO HD2 H 3.525 0.02 2 121 . 11 PRO HG3 H 2.696 0.02 2 122 . 11 PRO HG2 H 2.048 0.02 2 123 . 11 PRO C C 180.037 0.08 1 124 . 12 PHE CA C 62.581 0.08 1 125 . 12 PHE CB C 37.933 0.08 1 126 . 12 PHE CD1 C 130.170 0.08 3 127 . 12 PHE CE1 C 130.436 0.08 3 128 . 12 PHE H H 8.964 0.02 1 129 . 12 PHE HA H 3.813 0.02 1 130 . 12 PHE HB2 H 3.213 0.02 1 131 . 12 PHE HB3 H 3.283 0.02 1 132 . 12 PHE HZ H 6.057 0.02 1 133 . 12 PHE N N 123.039 0.07 1 134 . 12 PHE HD1 H 6.752 0.02 1 135 . 12 PHE HD2 H 6.752 0.02 1 136 . 12 PHE HE1 H 7.111 0.02 1 137 . 12 PHE HE2 H 7.111 0.02 1 138 . 12 PHE C C 179.630 0.08 1 139 . 13 GLU CA C 58.777 0.08 1 140 . 13 GLU CB C 30.224 0.08 1 141 . 13 GLU CG C 36.423 0.08 1 142 . 13 GLU H H 8.648 0.02 1 143 . 13 GLU HA H 4.017 0.02 1 144 . 13 GLU HB3 H 2.370 0.02 2 145 . 13 GLU HB2 H 2.248 0.02 2 146 . 13 GLU HG3 H 2.584 0.02 2 147 . 13 GLU HG2 H 2.388 0.02 2 148 . 13 GLU N N 122.341 0.07 1 149 . 13 GLU C C 178.737 0.08 1 150 . 14 GLU CA C 58.437 0.08 1 151 . 14 GLU CB C 30.396 0.08 1 152 . 14 GLU CG C 36.319 0.08 1 153 . 14 GLU H H 8.469 0.02 1 154 . 14 GLU HA H 4.125 0.02 1 155 . 14 GLU HB2 H 2.037 0.02 1 156 . 14 GLU HB3 H 2.118 0.02 1 157 . 14 GLU HG3 H 2.443 0.02 2 158 . 14 GLU HG2 H 2.254 0.02 2 159 . 14 GLU N N 117.440 0.07 1 160 . 14 GLU C C 178.704 0.08 1 161 . 15 SER CA C 58.638 0.08 1 162 . 15 SER CB C 67.009 0.08 1 163 . 15 SER H H 8.494 0.02 1 164 . 15 SER HA H 4.764 0.02 1 165 . 15 SER HB3 H 3.966 0.02 2 166 . 15 SER HB2 H 3.837 0.02 2 167 . 15 SER N N 112.152 0.07 1 168 . 15 SER C C 175.519 0.08 1 169 . 16 GLY CA C 45.076 0.08 1 170 . 16 GLY H H 8.352 0.02 1 171 . 16 GLY HA3 H 3.787 0.02 2 172 . 16 GLY HA2 H 2.777 0.02 2 173 . 16 GLY N N 114.082 0.07 1 174 . 16 GLY C C 172.377 0.08 1 175 . 17 THR CA C 59.819 0.08 1 176 . 17 THR CB C 70.802 0.08 1 177 . 17 THR CG2 C 20.222 0.08 1 178 . 17 THR H H 7.487 0.02 1 179 . 17 THR HA H 4.454 0.02 1 180 . 17 THR HB H 3.940 0.02 1 181 . 17 THR N N 112.660 0.07 1 182 . 17 THR HG2 H 0.993 0.02 1 183 . 17 THR C C 170.910 0.08 1 184 . 18 CYS CA C 58.742 0.08 1 185 . 18 CYS CB C 32.885 0.08 1 186 . 18 CYS H H 8.269 0.02 1 187 . 18 CYS HA H 4.676 0.02 1 188 . 18 CYS HB2 H 2.998 0.02 1 189 . 18 CYS HB3 H 2.745 0.02 1 190 . 18 CYS N N 124.318 0.07 1 191 . 18 CYS C C 177.363 0.08 1 192 . 19 LYS CA C 58.544 0.08 1 193 . 19 LYS CB C 31.867 0.08 1 194 . 19 LYS CD C 29.428 0.08 1 195 . 19 LYS CE C 41.941 0.08 1 196 . 19 LYS CG C 24.099 0.08 1 197 . 19 LYS H H 9.216 0.02 1 198 . 19 LYS HA H 4.245 0.02 1 199 . 19 LYS HB2 H 1.885 0.02 1 200 . 19 LYS HB3 H 1.800 0.02 1 201 . 19 LYS HD3 H 1.610 0.02 2 202 . 19 LYS HD2 H 1.562 0.02 2 203 . 19 LYS HE3 H 2.959 0.02 2 204 . 19 LYS HE2 H 2.786 0.02 2 205 . 19 LYS HG3 H 1.483 0.02 2 206 . 19 LYS HG2 H 0.835 0.02 2 207 . 19 LYS N N 131.637 0.07 1 208 . 19 LYS C C 177.272 0.08 1 209 . 20 TYR CA C 60.458 0.08 1 210 . 20 TYR CB C 38.333 0.08 1 211 . 20 TYR CD1 C 132.155 0.08 3 212 . 20 TYR CE1 C 117.616 0.08 3 213 . 20 TYR H H 9.289 0.02 1 214 . 20 TYR HA H 4.345 0.02 1 215 . 20 TYR HB2 H 3.230 0.02 1 216 . 20 TYR HB3 H 2.637 0.02 1 217 . 20 TYR N N 122.448 0.07 1 218 . 20 TYR HD1 H 7.143 0.02 1 219 . 20 TYR HD2 H 7.143 0.02 1 220 . 20 TYR HE1 H 6.783 0.02 1 221 . 20 TYR HE2 H 6.783 0.02 1 222 . 20 TYR C C 178.074 0.08 1 223 . 21 GLY CA C 47.575 0.08 1 224 . 21 GLY H H 8.018 0.02 1 225 . 21 GLY N N 111.028 0.07 1 226 . 21 GLY HA2 H 4.073 0.02 1 227 . 21 GLY HA3 H 4.073 0.02 1 228 . 21 GLY C C 176.807 0.08 1 229 . 22 GLU CA C 58.072 0.08 1 230 . 22 GLU CB C 29.104 0.08 1 231 . 22 GLU CG C 36.222 0.08 1 232 . 22 GLU H H 9.599 0.02 1 233 . 22 GLU HA H 4.301 0.02 1 234 . 22 GLU HB2 H 2.141 0.02 1 235 . 22 GLU HB3 H 2.275 0.02 1 236 . 22 GLU N N 128.536 0.07 1 237 . 22 GLU HG3 H 2.427 0.02 1 238 . 22 GLU HG2 H 2.427 0.02 1 239 . 22 GLU C C 177.208 0.08 1 240 . 23 LYS CA C 55.769 0.08 1 241 . 23 LYS CB C 32.127 0.08 1 242 . 23 LYS CD C 29.025 0.08 1 243 . 23 LYS CE C 42.043 0.08 1 244 . 23 LYS CG C 25.631 0.08 1 245 . 23 LYS H H 8.555 0.02 1 246 . 23 LYS HA H 4.498 0.02 1 247 . 23 LYS HG3 H 1.673 0.02 2 248 . 23 LYS HG2 H 1.556 0.02 2 249 . 23 LYS N N 119.618 0.07 1 250 . 23 LYS HB3 H 2.233 0.02 1 251 . 23 LYS HB2 H 2.233 0.02 1 252 . 23 LYS HD3 H 1.863 0.02 1 253 . 23 LYS HD2 H 1.863 0.02 1 254 . 23 LYS HE3 H 3.116 0.02 1 255 . 23 LYS HE2 H 3.116 0.02 1 256 . 23 LYS C C 176.244 0.08 1 257 . 24 CYS CA C 61.628 0.08 1 258 . 24 CYS CB C 31.512 0.08 1 259 . 24 CYS H H 7.509 0.02 1 260 . 24 CYS HA H 4.065 0.02 1 261 . 24 CYS HB2 H 3.189 0.02 1 262 . 24 CYS HB3 H 2.498 0.02 1 263 . 24 CYS N N 125.255 0.07 1 264 . 24 CYS C C 177.250 0.08 1 265 . 25 GLN CA C 55.042 0.08 1 266 . 25 GLN CB C 28.768 0.08 1 267 . 25 GLN CG C 34.432 0.08 1 268 . 25 GLN H H 8.945 0.02 1 269 . 25 GLN HA H 4.254 0.02 1 270 . 25 GLN HB2 H 1.421 0.02 1 271 . 25 GLN HB3 H 2.519 0.02 1 272 . 25 GLN HE22 H 7.202 0.02 2 273 . 25 GLN HE21 H 7.083 0.02 2 274 . 25 GLN HG3 H 2.638 0.02 2 275 . 25 GLN HG2 H 2.518 0.02 2 276 . 25 GLN N N 125.948 0.07 1 277 . 25 GLN NE2 N 115.549 0.07 1 278 . 25 GLN C C 175.081 0.08 1 279 . 26 PHE CA C 56.909 0.08 1 280 . 26 PHE CB C 39.299 0.08 1 281 . 26 PHE CZ C 125.985 0.08 1 282 . 26 PHE H H 9.513 0.02 1 283 . 26 PHE HA H 4.780 0.02 1 284 . 26 PHE HZ H 5.746 0.02 1 285 . 26 PHE N N 127.986 0.07 1 286 . 26 PHE HB3 H 2.861 0.02 1 287 . 26 PHE HB2 H 2.861 0.02 1 288 . 26 PHE HD1 H 6.567 0.02 1 289 . 26 PHE HD2 H 6.567 0.02 1 290 . 26 PHE C C 175.111 0.08 1 291 . 27 ALA CA C 52.901 0.08 1 292 . 27 ALA CB C 19.053 0.08 1 293 . 27 ALA H H 9.066 0.02 1 294 . 27 ALA HA H 3.633 0.02 1 295 . 27 ALA N N 125.133 0.07 1 296 . 27 ALA HB H 1.045 0.02 1 297 . 27 ALA C C 176.731 0.08 1 298 . 28 HIS CA C 52.819 0.08 1 299 . 28 HIS CB C 25.051 0.08 1 300 . 28 HIS CD2 C 123.909 0.08 1 301 . 28 HIS CE1 C 137.461 0.08 1 302 . 28 HIS H H 9.425 0.02 1 303 . 28 HIS HA H 4.378 0.02 1 304 . 28 HIS HB2 H 2.541 0.02 1 305 . 28 HIS HB3 H 0.962 0.02 1 306 . 28 HIS HD2 H 6.404 0.02 1 307 . 28 HIS HE1 H 7.926 0.02 1 308 . 28 HIS N N 129.137 0.07 1 309 . 28 HIS C C 174.046 0.08 1 310 . 29 GLY CA C 44.109 0.08 1 311 . 29 GLY H H 8.017 0.02 1 312 . 29 GLY HA3 H 4.491 0.02 2 313 . 29 GLY HA2 H 3.983 0.02 2 314 . 29 GLY N N 111.582 0.07 1 315 . 29 GLY C C 174.654 0.08 1 316 . 30 PHE CA C 60.711 0.08 1 317 . 30 PHE CB C 38.948 0.08 1 318 . 30 PHE CD1 C 130.883 0.08 3 319 . 30 PHE CE1 C 130.805 0.08 3 320 . 30 PHE H H 8.446 0.02 1 321 . 30 PHE HA H 4.054 0.02 1 322 . 30 PHE HB2 H 3.199 0.02 1 323 . 30 PHE HB3 H 3.093 0.02 1 324 . 30 PHE N N 118.886 0.07 1 325 . 30 PHE HD1 H 7.216 0.02 1 326 . 30 PHE HD2 H 7.216 0.02 1 327 . 30 PHE HE1 H 7.364 0.02 1 328 . 30 PHE HE2 H 7.364 0.02 1 329 . 31 HIS CA C 57.978 0.08 1 330 . 31 HIS CB C 28.258 0.08 1 331 . 31 HIS HA H 4.356 0.02 1 332 . 31 HIS HB3 H 3.238 0.02 2 333 . 31 HIS HB2 H 3.152 0.02 2 334 . 31 HIS C C 179.379 0.08 1 335 . 32 GLU CA C 56.028 0.08 1 336 . 32 GLU CB C 31.697 0.08 1 337 . 32 GLU CG C 36.676 0.08 1 338 . 32 GLU H H 7.184 0.02 1 339 . 32 GLU HA H 4.115 0.02 1 340 . 32 GLU HB2 H 1.598 0.02 1 341 . 32 GLU HB3 H 1.981 0.02 1 342 . 32 GLU HG3 H 2.053 0.02 2 343 . 32 GLU HG2 H 1.927 0.02 2 344 . 32 GLU N N 117.760 0.07 1 345 . 32 GLU C C 176.185 0.08 1 346 . 33 LEU CA C 55.808 0.08 1 347 . 33 LEU CB C 42.502 0.08 1 348 . 33 LEU CD1 C 25.254 0.08 2 349 . 33 LEU CD2 C 24.276 0.08 2 350 . 33 LEU CG C 26.811 0.08 1 351 . 33 LEU H H 7.016 0.02 1 352 . 33 LEU HA H 4.074 0.02 1 353 . 33 LEU HG H 1.325 0.02 1 354 . 33 LEU N N 120.446 0.07 1 355 . 33 LEU HB3 H 1.426 0.02 2 356 . 33 LEU HD1 H 0.784 0.02 4 357 . 33 LEU HD2 H 0.665 0.02 4 358 . 33 LEU C C 177.551 0.08 1 359 . 34 ARG CA C 54.474 0.08 1 360 . 34 ARG CB C 31.317 0.08 1 361 . 34 ARG CD C 43.326 0.08 1 362 . 34 ARG H H 8.683 0.02 1 363 . 34 ARG HA H 4.397 0.02 1 364 . 34 ARG HB2 H 1.441 0.02 1 365 . 34 ARG HB3 H 1.790 0.02 1 366 . 34 ARG HE H 7.390 0.02 1 367 . 34 ARG HG3 H 1.782 0.02 2 368 . 34 ARG HG2 H 1.546 0.02 2 369 . 34 ARG N N 127.726 0.07 1 370 . 34 ARG NE N 116.668 0.07 1 371 . 34 ARG HD3 H 3.160 0.02 1 372 . 34 ARG HD2 H 3.160 0.02 1 373 . 34 ARG C C 175.850 0.08 1 374 . 35 SER CB C 63.855 0.08 1 375 . 35 SER H H 8.368 0.02 1 376 . 35 SER HA H 4.306 0.02 1 377 . 35 SER N N 116.876 0.07 1 378 . 35 SER HB3 H 3.744 0.02 1 379 . 35 SER HB2 H 3.744 0.02 1 380 . 35 SER C C 173.892 0.08 1 381 . 36 LEU CA C 53.861 0.08 1 382 . 36 LEU CB C 44.154 0.08 1 383 . 36 LEU CD1 C 24.631 0.08 2 384 . 36 LEU H H 8.398 0.02 1 385 . 36 LEU HA H 4.472 0.02 1 386 . 36 LEU HB2 H 1.405 0.02 1 387 . 36 LEU HB3 H 1.480 0.02 1 388 . 36 LEU N N 125.958 0.07 1 389 . 36 LEU HD1 H 0.847 0.02 4 390 . 36 LEU C C 177.210 0.08 1 391 . 37 THR CA C 62.448 0.08 1 392 . 37 THR CB C 68.892 0.08 1 393 . 37 THR CG2 C 21.569 0.08 1 394 . 37 THR H H 8.413 0.02 1 395 . 37 THR HA H 4.113 0.02 1 396 . 37 THR HB H 3.955 0.02 1 397 . 37 THR N N 120.898 0.07 1 398 . 37 THR HG2 H 1.129 0.02 1 399 . 37 THR C C 174.251 0.08 1 400 . 38 ARG CA C 53.374 0.08 1 401 . 38 ARG CB C 31.935 0.08 1 402 . 38 ARG CD C 42.460 0.08 1 403 . 38 ARG CG C 26.164 0.08 1 404 . 38 ARG H H 8.595 0.02 1 405 . 38 ARG HA H 4.156 0.02 1 406 . 38 ARG HB2 H 1.424 0.02 1 407 . 38 ARG HB3 H 1.288 0.02 1 408 . 38 ARG HD3 H 2.147 0.02 2 409 . 38 ARG HD2 H 1.824 0.02 2 410 . 38 ARG HE H 6.886 0.02 1 411 . 38 ARG HG3 H 1.188 0.02 2 412 . 38 ARG HG2 H 1.049 0.02 2 413 . 38 ARG N N 127.045 0.07 1 414 . 38 ARG NE N 115.765 0.07 1 415 . 38 ARG C C 174.723 0.08 1 416 . 39 HIS CA C 56.301 0.08 1 417 . 39 HIS CB C 31.889 0.08 1 418 . 39 HIS CD2 C 117.889 0.08 1 419 . 39 HIS CE1 C 137.449 0.08 1 420 . 39 HIS H H 8.556 0.02 1 421 . 39 HIS HA H 4.360 0.02 1 422 . 39 HIS HB2 H 3.192 0.02 1 423 . 39 HIS HB3 H 2.654 0.02 1 424 . 39 HIS HD2 H 7.160 0.02 1 425 . 39 HIS HE1 H 7.536 0.02 1 426 . 39 HIS N N 125.578 0.07 1 427 . 40 PRO CA C 65.076 0.08 1 428 . 40 PRO CB C 32.129 0.08 1 429 . 40 PRO CD C 50.260 0.08 1 430 . 40 PRO CG C 27.325 0.08 1 431 . 40 PRO HA H 4.292 0.02 1 432 . 40 PRO HB3 H 2.295 0.02 2 433 . 40 PRO HB2 H 1.796 0.02 2 434 . 40 PRO HD3 H 3.431 0.02 2 435 . 40 PRO HD2 H 2.271 0.02 2 436 . 40 PRO HG3 H 1.809 0.02 2 437 . 40 PRO HG2 H 1.718 0.02 2 438 . 40 PRO C C 178.501 0.08 1 439 . 41 LYS CA C 54.950 0.08 1 440 . 41 LYS CB C 31.617 0.08 1 441 . 41 LYS CD C 29.006 0.08 1 442 . 41 LYS CE C 42.001 0.08 1 443 . 41 LYS CG C 26.056 0.08 1 444 . 41 LYS H H 0.316 0.02 1 445 . 41 LYS HA H 4.260 0.02 1 446 . 41 LYS HB3 H 1.672 0.02 2 447 . 41 LYS HB2 H 1.539 0.02 2 448 . 41 LYS HD3 H 1.820 0.02 2 449 . 41 LYS HD2 H 1.730 0.02 2 450 . 41 LYS HE3 H 3.044 0.02 2 451 . 41 LYS HE2 H 3.019 0.02 2 452 . 41 LYS HG3 H 1.561 0.02 2 453 . 41 LYS HG2 H 1.301 0.02 2 454 . 41 LYS C C 176.058 0.08 1 455 . 42 TYR CA C 59.681 0.08 1 456 . 42 TYR CB C 39.479 0.08 1 457 . 42 TYR CD1 C 132.556 0.08 3 458 . 42 TYR CE1 C 117.373 0.08 3 459 . 42 TYR H H 7.932 0.02 1 460 . 42 TYR HA H 3.660 0.02 1 461 . 42 TYR HB2 H 3.201 0.02 1 462 . 42 TYR HB3 H 2.691 0.02 1 463 . 42 TYR N N 123.501 0.07 1 464 . 42 TYR HD1 H 6.822 0.02 1 465 . 42 TYR HD2 H 6.822 0.02 1 466 . 42 TYR HE1 H 6.584 0.02 1 467 . 42 TYR HE2 H 6.584 0.02 1 468 . 42 TYR C C 174.188 0.08 1 469 . 43 LYS CA C 57.828 0.08 1 470 . 43 LYS CB C 29.948 0.08 1 471 . 43 LYS CD C 28.968 0.08 1 472 . 43 LYS CE C 42.050 0.08 1 473 . 43 LYS CG C 25.308 0.08 1 474 . 43 LYS H H 7.909 0.02 1 475 . 43 LYS HA H 3.106 0.02 1 476 . 43 LYS HB2 H 1.262 0.02 1 477 . 43 LYS HB3 H 1.406 0.02 1 478 . 43 LYS HD3 H 1.186 0.02 2 479 . 43 LYS HD2 H 0.969 0.02 2 480 . 43 LYS HE3 H 2.877 0.02 2 481 . 43 LYS HE2 H 2.737 0.02 2 482 . 43 LYS HG3 H -0.027 0.02 2 483 . 43 LYS HG2 H -0.350 0.02 2 484 . 43 LYS N N 121.795 0.07 1 485 . 43 LYS C C 173.663 0.08 1 486 . 44 THR CA C 62.235 0.08 1 487 . 44 THR CB C 71.454 0.08 1 488 . 44 THR CG2 C 21.186 0.08 1 489 . 44 THR H H 7.717 0.02 1 490 . 44 THR HA H 4.569 0.02 1 491 . 44 THR HB H 4.173 0.02 1 492 . 44 THR N N 106.267 0.07 1 493 . 44 THR HG2 H 1.035 0.02 1 494 . 44 THR C C 175.400 0.08 1 495 . 45 GLU CA C 54.087 0.08 1 496 . 45 GLU CB C 33.182 0.08 1 497 . 45 GLU CG C 35.859 0.08 1 498 . 45 GLU H H 9.241 0.02 1 499 . 45 GLU HA H 4.881 0.02 1 500 . 45 GLU HB2 H 2.062 0.02 1 501 . 45 GLU HB3 H 2.265 0.02 1 502 . 45 GLU N N 125.411 0.07 1 503 . 45 GLU HG3 H 2.508 0.02 1 504 . 45 GLU HG2 H 2.508 0.02 1 505 . 45 GLU C C 175.637 0.08 1 506 . 46 LEU CA C 56.112 0.08 1 507 . 46 LEU CB C 41.171 0.08 1 508 . 46 LEU CD1 C 24.689 0.08 2 509 . 46 LEU CD2 C 22.359 0.08 2 510 . 46 LEU CG C 26.809 0.08 1 511 . 46 LEU H H 8.937 0.02 1 512 . 46 LEU HA H 4.224 0.02 1 513 . 46 LEU HB2 H 1.657 0.02 1 514 . 46 LEU HB3 H 1.123 0.02 1 515 . 46 LEU HG H 1.667 0.02 1 516 . 46 LEU N N 123.263 0.07 1 517 . 46 LEU HD1 H 0.631 0.02 4 518 . 46 LEU HD2 H 0.538 0.02 4 519 . 46 LEU C C 177.604 0.08 1 520 . 47 CYS CA C 59.535 0.08 1 521 . 47 CYS CB C 31.697 0.08 1 522 . 47 CYS H H 9.577 0.02 1 523 . 47 CYS HA H 4.799 0.02 1 524 . 47 CYS HB3 H 3.412 0.02 2 525 . 47 CYS HB2 H 3.026 0.02 2 526 . 47 CYS N N 127.490 0.07 1 527 . 47 CYS C C 177.428 0.08 1 528 . 48 ARG CA C 58.842 0.08 1 529 . 48 ARG CB C 30.178 0.08 1 530 . 48 ARG CD C 43.269 0.08 1 531 . 48 ARG CG C 27.379 0.08 1 532 . 48 ARG H H 11.330 0.02 1 533 . 48 ARG HA H 4.279 0.02 1 534 . 48 ARG HB3 H 1.704 0.02 2 535 . 48 ARG HB2 H 1.650 0.02 2 536 . 48 ARG HE H 6.784 0.02 1 537 . 48 ARG HG3 H 1.577 0.02 2 538 . 48 ARG HG2 H 1.313 0.02 2 539 . 48 ARG N N 106.718 0.07 1 540 . 48 ARG NE N 113.999 0.07 1 541 . 48 ARG HD3 H 2.634 0.02 1 542 . 48 ARG HD2 H 2.634 0.02 1 543 . 48 ARG C C 177.834 0.08 1 544 . 49 THR CA C 65.291 0.08 1 545 . 49 THR CB C 68.473 0.08 1 546 . 49 THR CG2 C 23.631 0.08 1 547 . 49 THR H H 8.187 0.02 1 548 . 49 THR HA H 4.069 0.02 1 549 . 49 THR HB H 4.464 0.02 1 550 . 49 THR N N 121.260 0.07 1 551 . 49 THR HG2 H 1.555 0.02 1 552 . 49 THR C C 176.455 0.08 1 553 . 50 PHE CA C 62.117 0.08 1 554 . 50 PHE CB C 39.225 0.08 1 555 . 50 PHE H H 9.803 0.02 1 556 . 50 PHE HA H 3.419 0.02 1 557 . 50 PHE HB2 H 2.909 0.02 1 558 . 50 PHE HB3 H 2.829 0.02 1 559 . 50 PHE N N 126.830 0.07 1 560 . 50 PHE HD1 H 6.053 0.02 1 561 . 50 PHE HD2 H 6.053 0.02 1 562 . 50 PHE C C 178.083 0.08 1 563 . 51 HIS CA C 58.362 0.08 1 564 . 51 HIS CB C 29.140 0.08 1 565 . 51 HIS CD2 C 119.851 0.08 1 566 . 51 HIS H H 8.055 0.02 1 567 . 51 HIS HA H 4.327 0.02 1 568 . 51 HIS HB3 H 3.285 0.02 2 569 . 51 HIS HB2 H 3.486 0.02 2 570 . 51 HIS HD2 H 7.944 0.02 1 571 . 51 HIS N N 112.512 0.07 1 572 . 51 HIS C C 175.133 0.08 1 573 . 52 THR CA C 63.960 0.08 1 574 . 52 THR CB C 69.776 0.08 1 575 . 52 THR CG2 C 21.476 0.08 1 576 . 52 THR H H 7.644 0.02 1 577 . 52 THR HA H 4.402 0.02 1 578 . 52 THR HB H 4.206 0.02 1 579 . 52 THR N N 112.630 0.07 1 580 . 52 THR HG2 H 1.312 0.02 1 581 . 52 THR C C 175.921 0.08 1 582 . 53 ILE CA C 61.111 0.08 1 583 . 53 ILE CB C 39.207 0.08 1 584 . 53 ILE CD1 C 13.145 0.08 1 585 . 53 ILE CG1 C 27.183 0.08 1 586 . 53 ILE CG2 C 17.686 0.08 1 587 . 53 ILE H H 8.246 0.02 1 588 . 53 ILE HA H 4.482 0.02 1 589 . 53 ILE HB H 2.174 0.02 1 590 . 53 ILE HG13 H 1.417 0.02 2 591 . 53 ILE HG12 H 1.295 0.02 2 592 . 53 ILE N N 116.589 0.07 1 593 . 53 ILE HD1 H 0.801 0.02 1 594 . 53 ILE HG2 H 0.911 0.02 1 595 . 53 ILE C C 177.196 0.08 1 596 . 54 GLY CA C 45.144 0.08 1 597 . 54 GLY H H 7.322 0.02 1 598 . 54 GLY HA3 H 3.911 0.02 2 599 . 54 GLY HA2 H 3.156 0.02 2 600 . 54 GLY N N 109.837 0.07 1 601 . 54 GLY C C 172.279 0.08 1 602 . 55 PHE CA C 56.116 0.08 1 603 . 55 PHE CB C 41.792 0.08 1 604 . 55 PHE CD1 C 131.143 0.08 3 605 . 55 PHE CE1 C 129.143 0.08 3 606 . 55 PHE H H 7.026 0.02 1 607 . 55 PHE HA H 4.448 0.02 1 608 . 55 PHE HB3 H 2.616 0.02 2 609 . 55 PHE HB2 H 3.108 0.02 2 610 . 55 PHE N N 117.835 0.07 1 611 . 55 PHE HD1 H 7.091 0.02 1 612 . 55 PHE HD2 H 7.091 0.02 1 613 . 55 PHE HE1 H 7.308 0.02 1 614 . 55 PHE HE2 H 7.308 0.02 1 615 . 56 CYS CA C 54.867 0.08 1 616 . 56 CYS CB C 33.800 0.08 1 617 . 56 CYS H H 8.083 0.02 1 618 . 56 CYS HA H 4.909 0.02 1 619 . 56 CYS HB2 H 2.682 0.02 1 620 . 56 CYS HB3 H 2.814 0.02 1 621 . 56 CYS N N 125.869 0.07 1 622 . 57 PRO CA C 64.294 0.08 1 623 . 57 PRO CB C 31.622 0.08 1 624 . 57 PRO CD C 52.210 0.08 1 625 . 57 PRO CG C 26.800 0.08 1 626 . 57 PRO HA H 4.465 0.02 1 627 . 57 PRO HB3 H 2.385 0.02 2 628 . 57 PRO HB2 H 2.262 0.02 2 629 . 57 PRO HD3 H 4.366 0.02 2 630 . 57 PRO HD2 H 3.724 0.02 2 631 . 57 PRO HG3 H 2.191 0.02 2 632 . 57 PRO HG2 H 1.858 0.02 2 633 . 57 PRO C C 177.831 0.08 1 634 . 58 TYR CA C 60.539 0.08 1 635 . 58 TYR CB C 38.046 0.08 1 636 . 58 TYR CD1 C 131.495 0.08 3 637 . 58 TYR CE1 C 117.782 0.08 3 638 . 58 TYR H H 9.066 0.02 1 639 . 58 TYR HA H 4.441 0.02 1 640 . 58 TYR HB2 H 3.342 0.02 1 641 . 58 TYR HB3 H 2.539 0.02 1 642 . 58 TYR N N 122.055 0.07 1 643 . 58 TYR HD1 H 6.928 0.02 1 644 . 58 TYR HD2 H 6.928 0.02 1 645 . 58 TYR HE1 H 6.715 0.02 1 646 . 58 TYR HE2 H 6.715 0.02 1 647 . 58 TYR C C 177.872 0.08 1 648 . 59 GLY CA C 45.756 0.08 1 649 . 59 GLY H H 7.943 0.02 1 650 . 59 GLY HA3 H 4.446 0.02 2 651 . 59 GLY HA2 H 3.968 0.02 2 652 . 59 GLY N N 110.422 0.07 1 653 . 60 PRO CA C 63.945 0.08 1 654 . 60 PRO CB C 32.329 0.08 1 655 . 60 PRO CD C 51.660 0.08 1 656 . 60 PRO CG C 26.893 0.08 1 657 . 60 PRO HA H 4.648 0.02 1 658 . 60 PRO HB3 H 2.500 0.02 2 659 . 60 PRO HB2 H 2.245 0.02 2 660 . 60 PRO HD3 H 4.186 0.02 2 661 . 60 PRO HD2 H 3.945 0.02 2 662 . 60 PRO HG3 H 2.209 0.02 2 663 . 60 PRO HG2 H 2.153 0.02 2 664 . 60 PRO C C 177.630 0.08 1 665 . 61 ARG CA C 56.467 0.08 1 666 . 61 ARG CB C 29.990 0.08 1 667 . 61 ARG CD C 43.375 0.08 1 668 . 61 ARG CG C 28.120 0.08 1 669 . 61 ARG H H 8.473 0.02 1 670 . 61 ARG HA H 4.583 0.02 1 671 . 61 ARG HD3 H 3.765 0.02 2 672 . 61 ARG HD2 H 3.481 0.02 2 673 . 61 ARG HE H 8.846 0.02 1 674 . 61 ARG HG3 H 1.972 0.02 2 675 . 61 ARG HG2 H 1.908 0.02 2 676 . 61 ARG N N 118.597 0.07 1 677 . 61 ARG NE N 117.181 0.07 1 678 . 61 ARG HB3 H 2.383 0.02 1 679 . 61 ARG HB2 H 2.383 0.02 1 680 . 61 ARG C C 175.814 0.08 1 681 . 62 CYS CA C 61.330 0.08 1 682 . 62 CYS CB C 31.090 0.08 1 683 . 62 CYS H H 7.573 0.02 1 684 . 62 CYS HA H 3.998 0.02 1 685 . 62 CYS HB2 H 2.987 0.02 1 686 . 62 CYS HB3 H 2.351 0.02 1 687 . 62 CYS N N 124.656 0.07 1 688 . 62 CYS C C 177.347 0.08 1 689 . 63 HIS CA C 54.959 0.08 1 690 . 63 HIS CB C 29.418 0.08 1 691 . 63 HIS H H 9.008 0.02 1 692 . 63 HIS HA H 4.589 0.02 1 693 . 63 HIS HB2 H 2.345 0.02 1 694 . 63 HIS HB3 H 3.496 0.02 1 695 . 63 HIS N N 126.973 0.07 1 696 . 63 HIS C C 174.359 0.08 1 697 . 64 PHE CA C 56.933 0.08 1 698 . 64 PHE CB C 39.245 0.08 1 699 . 64 PHE CD1 C 130.248 0.08 3 700 . 64 PHE CE1 C 128.524 0.08 3 701 . 64 PHE CZ C 125.608 0.08 1 702 . 64 PHE H H 9.176 0.02 1 703 . 64 PHE HA H 4.774 0.02 1 704 . 64 PHE HB3 H 2.939 0.02 2 705 . 64 PHE HB2 H 2.839 0.02 2 706 . 64 PHE HZ H 5.766 0.02 1 707 . 64 PHE N N 127.853 0.07 1 708 . 64 PHE HD1 H 6.554 0.02 1 709 . 64 PHE HD2 H 6.554 0.02 1 710 . 64 PHE HE1 H 6.132 0.02 1 711 . 64 PHE HE2 H 6.132 0.02 1 712 . 64 PHE C C 174.433 0.08 1 713 . 65 ILE CA C 63.915 0.08 1 714 . 65 ILE CB C 40.047 0.08 1 715 . 65 ILE CD1 C 14.063 0.08 1 716 . 65 ILE CG1 C 28.388 0.08 1 717 . 65 ILE CG2 C 16.161 0.08 1 718 . 65 ILE H H 9.209 0.02 1 719 . 65 ILE HA H 3.373 0.02 1 720 . 65 ILE HB H 1.531 0.02 1 721 . 65 ILE HG13 H 1.101 0.02 2 722 . 65 ILE HG12 H 0.573 0.02 2 723 . 65 ILE N N 120.680 0.07 1 724 . 65 ILE HD1 H 0.506 0.02 1 725 . 65 ILE HG2 H 0.756 0.02 1 726 . 65 ILE C C 178.130 0.08 1 727 . 66 HIS CA C 53.474 0.08 1 728 . 66 HIS CB C 26.411 0.08 1 729 . 66 HIS CD2 C 122.791 0.08 1 730 . 66 HIS CE1 C 138.333 0.08 1 731 . 66 HIS H H 9.070 0.02 1 732 . 66 HIS HA H 4.396 0.02 1 733 . 66 HIS HB2 H 2.870 0.02 1 734 . 66 HIS HB3 H 1.246 0.02 1 735 . 66 HIS HD2 H 6.484 0.02 1 736 . 66 HIS HE1 H 7.913 0.02 1 737 . 66 HIS N N 130.462 0.07 1 738 . 66 HIS C C 172.885 0.08 1 739 . 67 ASN CA C 55.986 0.08 1 740 . 67 ASN H H 7.900 0.02 1 741 . 67 ASN HA H 4.816 0.02 1 742 . 67 ASN HD22 H 7.841 0.02 2 743 . 67 ASN HD21 H 7.200 0.02 2 744 . 67 ASN N N 120.206 0.07 1 745 . 67 ASN ND2 N 114.294 0.07 1 746 . 67 ASN HB3 H 2.924 0.02 1 747 . 67 ASN HB2 H 2.924 0.02 1 748 . 67 ASN C C 175.390 0.08 1 749 . 68 ALA CA C 53.196 0.08 1 750 . 68 ALA CB C 18.826 0.08 1 751 . 68 ALA H H 8.625 0.02 1 752 . 68 ALA HA H 4.205 0.02 1 753 . 68 ALA N N 125.121 0.07 1 754 . 68 ALA HB H 1.426 0.02 1 755 . 68 ALA C C 177.549 0.08 1 756 . 69 ASP CA C 54.134 0.08 1 757 . 69 ASP CB C 40.880 0.08 1 758 . 69 ASP H H 8.385 0.02 1 759 . 69 ASP HA H 4.635 0.02 1 760 . 69 ASP HB2 H 2.675 0.02 1 761 . 69 ASP HB3 H 2.758 0.02 1 762 . 69 ASP N N 118.885 0.07 1 763 . 69 ASP C C 175.363 0.08 1 764 . 70 GLU CA C 58.063 0.08 1 765 . 70 GLU CB C 31.384 0.08 1 766 . 70 GLU H H 7.727 0.02 1 767 . 70 GLU HA H 4.135 0.02 1 768 . 70 GLU HB3 H 2.032 0.02 2 769 . 70 GLU HB2 H 1.938 0.02 2 770 . 70 GLU N N 126.287 0.07 1 771 . 70 GLU HG3 H 2.222 0.02 1 772 . 70 GLU HG2 H 2.222 0.02 1 stop_ save_ save_rna_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_3 stop_ _Sample_conditions_label $Conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 5'-UUAUUUAUU-3' _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 U H1' H 6.024 0.02 1 2 . 2 U H6 H 7.616 0.02 1 3 . 3 A H2 H 8.165 0.02 1 4 . 3 A H3' H 4.855 0.02 1 5 . 3 A H8 H 8.393 0.02 1 6 . 4 U H1' H 5.152 0.02 1 7 . 4 U H5 H 6.128 0.02 1 8 . 4 U H6 H 7.994 0.02 1 9 . 5 U H1' H 6.372 0.02 1 10 . 5 U H5 H 5.731 0.02 1 11 . 5 U H6 H 7.678 0.02 1 12 . 6 U H1' H 5.534 0.02 1 13 . 6 U H6 H 7.715 0.02 1 14 . 7 A H1' H 5.962 0.02 1 15 . 7 A H2 H 8.129 0.02 1 16 . 7 A H8 H 8.556 0.02 1 17 . 8 U H1' H 5.666 0.02 1 18 . 8 U H5 H 6.186 0.02 1 19 . 8 U H6 H 8.040 0.02 1 20 . 9 U H1' H 6.096 0.02 1 21 . 9 U H2' H 4.398 0.02 1 22 . 9 U H5 H 5.751 0.02 1 23 . 9 U H6 H 7.727 0.02 1 stop_ save_