data_7307 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignment and RDCs of L11 in complex with RNA ; _BMRB_accession_number 7307 _BMRB_flat_file_name bmr7307.str _Entry_type original _Submission_date 2006-09-28 _Accession_date 2006-09-28 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone 1H, 13C, and 15N chemical shift assignment and Residual Dipolar Coupling data of L11 from Thermotoga maritima in complex with its cognate RNA' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jonker Henry . . 2 Ilin Serge . . 3 Grimm Steffen . . 4 Wohnert Jens . . 5 Schwalbe Harald . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 residual_dipolar_couplings 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 127 "13C chemical shifts" 256 "15N chemical shifts" 127 "residual dipolar couplings" 127 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-17 update BMRB 'complete entry citation' 2006-12-20 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'L11 domain rearrangement upon binding to RNA and thiostrepton studied by NMR spectroscopy.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17169991 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jonker Henry R. . 2 Ilin Serge . . 3 Grimm Steffen K. . 4 Wohnert Jens . . 5 Schwalbe Harald . . stop_ _Journal_abbreviation 'Nucleic Acids Res.' _Journal_volume 35 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 441 _Page_last 454 _Year 2007 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'L11-RNA complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'L11 protein' $L11 'GAR RNA' $RNA stop_ _System_molecular_weight 34346 _System_physical_state native _System_oligomer_state 'protein-RNA complex' _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details 'Complex between the ribosomal protein L11 and its cognate RNA binding domain' save_ ######################## # Monomeric polymers # ######################## save_L11 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'ribosomal L11 protein' _Molecular_mass 15088 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 141 _Mol_residue_sequence ; MAKKVAAQIKLQLPAGKATP APPVGPALGQHGVNIMEFCK RFNAETADKAGMILPVVITV YEDKSFTFIIKTPPASFLLK KAAGIEKGSSEPKRKIVGKV TRKQIEEIAKTKMPDLNANS LEAAMKIIEGTAKSMGIEVV D ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 LYS 4 LYS 5 VAL 6 ALA 7 ALA 8 GLN 9 ILE 10 LYS 11 LEU 12 GLN 13 LEU 14 PRO 15 ALA 16 GLY 17 LYS 18 ALA 19 THR 20 PRO 21 ALA 22 PRO 23 PRO 24 VAL 25 GLY 26 PRO 27 ALA 28 LEU 29 GLY 30 GLN 31 HIS 32 GLY 33 VAL 34 ASN 35 ILE 36 MET 37 GLU 38 PHE 39 CYS 40 LYS 41 ARG 42 PHE 43 ASN 44 ALA 45 GLU 46 THR 47 ALA 48 ASP 49 LYS 50 ALA 51 GLY 52 MET 53 ILE 54 LEU 55 PRO 56 VAL 57 VAL 58 ILE 59 THR 60 VAL 61 TYR 62 GLU 63 ASP 64 LYS 65 SER 66 PHE 67 THR 68 PHE 69 ILE 70 ILE 71 LYS 72 THR 73 PRO 74 PRO 75 ALA 76 SER 77 PHE 78 LEU 79 LEU 80 LYS 81 LYS 82 ALA 83 ALA 84 GLY 85 ILE 86 GLU 87 LYS 88 GLY 89 SER 90 SER 91 GLU 92 PRO 93 LYS 94 ARG 95 LYS 96 ILE 97 VAL 98 GLY 99 LYS 100 VAL 101 THR 102 ARG 103 LYS 104 GLN 105 ILE 106 GLU 107 GLU 108 ILE 109 ALA 110 LYS 111 THR 112 LYS 113 MET 114 PRO 115 ASP 116 LEU 117 ASN 118 ALA 119 ASN 120 SER 121 LEU 122 GLU 123 ALA 124 ALA 125 MET 126 LYS 127 ILE 128 ILE 129 GLU 130 GLY 131 THR 132 ALA 133 LYS 134 SER 135 MET 136 GLY 137 ILE 138 GLU 139 VAL 140 VAL 141 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 BMRB 5513 L11_monomer 100.00 141 100.00 100.00 4.02e-94 PDB 1EG0 "Fitting Of Components With Known Structure Into An 11.5 A Cryo-Em Map Of The E.Coli 70s Ribosome" 99.29 140 100.00 100.00 3.50e-93 PDB 1GIY "Crystal Structure Of The Ribosome At 5.5 A Resolution. This File, 1giy, Contains The 50s Ribosome Subunit. The 30s Ribosome Sub" 100.00 141 100.00 100.00 4.02e-94 PDB 1JQM "Fitting Of L11 Protein And Elongation Factor G (Ef-G) In The Cryo-Em Map Of E. Coli 70s Ribosome Bound With Ef-G, Gdp And Fusid" 98.58 139 100.00 100.00 2.69e-92 PDB 1JQS "Fitting Of L11 Protein And Elongation Factor G (Domain G' And V) In The Cryo-Em Map Of E. Coli 70s Ribosome Bound With Ef-G And" 98.58 139 100.00 100.00 2.69e-92 PDB 1JQT "Fitting Of L11 Protein In The Low Resolution Cryo-Em Map Of E.Coli 70s Ribosome" 98.58 139 100.00 100.00 2.69e-92 PDB 1MJ1 "Fitting The Ternary Complex Of Ef-TuTRNAGTP AND RIBOSOMAL PROTEINS Into A 13 A Cryo-Em Map Of The Coli 70s Ribosome" 100.00 141 100.00 100.00 4.02e-94 PDB 1ML5 "Structure Of The E. Coli Ribosomal Termination Complex With Release Factor 2" 100.00 141 100.00 100.00 4.02e-94 PDB 1MMS "Crystal Structure Of The Ribosomal Protein L11-Rna Complex" 99.29 140 100.00 100.00 2.55e-93 PDB 1MVR "Decoding Center & Peptidyl Transferase Center From The X-Ray Structure Of The Thermus Thermophilus 70s Ribosome, Aligned To The" 99.29 140 100.00 100.00 2.55e-93 PDB 1OLN "Model For Thiostrepton Antibiotic Binding To L11 Substrate From 50s Ribosomal Rna" 99.29 140 100.00 100.00 2.55e-93 PDB 1PN7 "Coordinates Of S12, L11 Proteins And P-Trna, From The 70s X- Ray Structure Aligned To The 70s Cryo-Em Map Of E.Coli Ribosome" 94.33 133 100.00 100.00 1.39e-88 PDB 1PN8 "Coordinates Of S12, L11 Proteins And E-Site Trna From 70s Crystal Structure Separately Fitted Into The Cryo-Em Map Of E.Coli 70" 94.33 133 100.00 100.00 1.39e-88 PDB 1R2W "Coordinates Of L11 With 58nts Of 23s Rrna Fitted Into The Cryo-Em Map Of The 70s Ribosome" 100.00 141 99.29 99.29 1.76e-91 PDB 1R2X "Coordinates Of L11 With 58nts Of 23s Rrna Fitted Into The Cryo-em Map Of Ef-tu Ternary Complex (gdp.kirromycin) Bound 70s Ribos" 100.00 141 99.29 99.29 1.76e-91 PDB 1YL3 "Crystal Structure Of 70s Ribosome With Thrs Operator And Trnas. Large Subunit. The Coordinates For The Small Subunit Are In The" 100.00 141 100.00 100.00 4.02e-94 PDB 2B66 "50s Ribosomal Subunit From A Crystal Structure Of Release Factor Rf1, Trnas And Mrna Bound To The Ribosome. This File Contains " 100.00 141 100.00 100.00 4.02e-94 PDB 2B9N "50s Ribosomal Subunit From A Crystal Structure Of Release Factor Rf2, Trnas And Mrna Bound To The Ribosome. This File Contains " 100.00 141 100.00 100.00 4.02e-94 PDB 2B9P "50s Ribosomal Subunit From A Crystal Structure Of The Ribosome In Complex With Trnas And Mrna With A Stop Codon In The A-Site. " 100.00 141 100.00 100.00 4.02e-94 PDB 2JQ7 "Model For Thiostrepton Binding To The Ribosomal L11-Rna" 100.00 141 100.00 100.00 4.02e-94 PDB 2K3F "Ribosomal Protein L11 From Thermotoga Maritima" 100.00 141 100.00 100.00 4.02e-94 PDB 487D "Seven Ribosomal Proteins Fitted To A Cryo-Electron Microscopic Map Of The Large 50s Subunit At 7.5 Angstroms Resolution" 94.33 133 100.00 100.00 1.39e-88 EMBL CAA77859 "ribosomal protein L11 [Thermotoga maritima MSB8]" 100.00 141 100.00 100.00 4.02e-94 GB AAD35537 "ribosomal protein L11 [Thermotoga maritima MSB8]" 100.00 141 100.00 100.00 4.02e-94 GB ABQ46490 "LSU ribosomal protein L11P [Thermotoga petrophila RKU-1]" 100.00 141 97.16 98.58 4.66e-92 GB ACB08837 "ribosomal protein L11 [Thermotoga sp. RQ2]" 100.00 141 100.00 100.00 4.02e-94 GB ADA66341 "ribosomal protein L11 [Thermotoga naphthophila RKU-10]" 100.00 141 97.16 98.58 4.66e-92 GB AGL49376 "LSU ribosomal protein L11p (L12e) [Thermotoga maritima MSB8]" 100.00 141 100.00 100.00 4.02e-94 REF NP_228264 "50S ribosomal protein L11 [Thermotoga maritima MSB8]" 100.00 141 100.00 100.00 4.02e-94 REF WP_004081512 "MULTISPECIES: 50S ribosomal protein L11 [Thermotoga]" 100.00 141 100.00 100.00 4.02e-94 REF WP_011943108 "MULTISPECIES: 50S ribosomal protein L11 [Thermotoga]" 100.00 141 97.16 98.58 4.66e-92 REF WP_038033608 "MULTISPECIES: 50S ribosomal protein L11 [Thermotoga]" 100.00 141 97.87 99.29 1.15e-92 REF YP_001244066 "50S ribosomal protein L11 [Thermotoga petrophila RKU-1]" 100.00 141 97.16 98.58 4.66e-92 SP A5IJW7 "RecName: Full=50S ribosomal protein L11 [Thermotoga petrophila RKU-1]" 100.00 141 97.16 98.58 4.66e-92 SP B1L939 "RecName: Full=50S ribosomal protein L11 [Thermotoga sp. RQ2]" 100.00 141 100.00 100.00 4.02e-94 SP P29395 "RecName: Full=50S ribosomal protein L11 [Thermotoga maritima MSB8]" 100.00 141 100.00 100.00 4.02e-94 stop_ save_ save_RNA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class RNA _Name_common '23S GAR RNA' _Molecular_mass 19258 _Mol_thiol_state 'not present' _Details . _Residue_count 60 _Mol_residue_sequence ; GGGCAGGAUGUAGGCUUAGA AGCAGCCAUCAUUUAAAGAA AGCGUAAUAGCUCACUGCCC ; loop_ _Residue_seq_code _Residue_label 1 G 2 G 3 G 4 C 5 A 6 G 7 G 8 A 9 U 10 G 11 U 12 A 13 G 14 G 15 C 16 U 17 U 18 A 19 G 20 A 21 A 22 G 23 C 24 A 25 G 26 C 27 C 28 A 29 U 30 C 31 A 32 U 33 U 34 U 35 A 36 A 37 A 38 G 39 A 40 A 41 A 42 G 43 C 44 G 45 U 46 A 47 A 48 U 49 A 50 G 51 C 52 U 53 C 54 A 55 C 56 U 57 G 58 C 59 C 60 C stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $L11 'Thermotoga maritima' 2336 Bacteria . Thermotoga maritima $RNA 'Escherichia coli' 562 Bacteria . Escherichia coli 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 $L11 'recombinant technology' E.Coli . . . . $RNA 'in vitro transcription' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_L11+RNA _Saveframe_category sample _Sample_type solution _Details 'binary complex' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $L11 0.3 mM '[U->95% 2D; U->98% 15N; U->98% 13C]' $RNA 0.5 mM . 'potassium phosphate' 20 mM . 'potassium chloride' 200 mM . complete . mM . superase . mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio et al.' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3 loop_ _Vendor _Address _Electronic_address 'Goddard et al.' . . stop_ loop_ _Task 'analysis & assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details 'Cryoprobe TXI z-gradient' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'TXI xyz-gradient' save_ ############################# # NMR applied experiments # ############################# save_2D_(1H,15N)HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D (1H,15N)HSQC' _Sample_label $L11+RNA save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $L11+RNA save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $L11+RNA save_ ####################### # Sample conditions # ####################### save_25C _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.1 0.05 pH temperature 298 0.1 K stop_ save_ save_35C _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.1 0.05 pH temperature 308 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 _Indirect_shift_ratio_citation_label _Reference_correction_type _Correction_value_citation_label H2O C 13 protons ppm 4.7 internal indirect . . . 0.251449530 $1 temperature $1 H2O H 1 protons ppm 4.7 internal direct . . . 1.000000000 $1 temperature $1 H2O N 15 protons ppm 4.7 internal indirect . . . 0.101329118 $1 temperature $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_chem_shift_LR _Saveframe_category assigned_chemical_shifts _Details L11+RNA loop_ _Experiment_label 2D_(1H,15N)HSQC 3D_HNCO 3D_HNCA stop_ loop_ _Sample_label $L11+RNA stop_ _Sample_conditions_label $35C _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'L11 protein' _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 2 ALA C C 171.1 . 1 2 2 2 ALA CA C 48.7 . 1 3 3 3 LYS H H 8.35 . 1 4 3 3 LYS C C 173.3 . 1 5 3 3 LYS CA C 53.2 . 1 6 3 3 LYS N N 121.4 . 1 7 4 4 LYS H H 8.79 . 1 8 4 4 LYS C C 173.8 . 1 9 4 4 LYS CA C 53.2 . 1 10 4 4 LYS N N 124.1 . 1 11 5 5 VAL H H 8.59 . 1 12 5 5 VAL C C 173.0 . 1 13 5 5 VAL CA C 61.2 . 1 14 5 5 VAL N N 126.2 . 1 15 6 6 ALA H H 9.46 . 1 16 6 6 ALA C C 174.6 . 1 17 6 6 ALA CA C 49.6 . 1 18 6 6 ALA N N 131.4 . 1 19 7 7 ALA H H 7.82 . 1 20 7 7 ALA C C 172.0 . 1 21 7 7 ALA CA C 48.8 . 1 22 7 7 ALA N N 118.8 . 1 23 8 8 GLN H H 8.14 . 1 24 8 8 GLN C C 172.2 . 1 25 8 8 GLN CA C 51.9 . 1 26 8 8 GLN N N 118.8 . 1 27 9 9 ILE H H 9.08 . 1 28 9 9 ILE C C 171.3 . 1 29 9 9 ILE CA C 57.2 . 1 30 9 9 ILE N N 125.6 . 1 31 10 10 LYS H H 8.66 . 1 32 10 10 LYS C C 172.9 . 1 33 10 10 LYS CA C 52.3 . 1 34 10 10 LYS N N 128.4 . 1 35 11 11 LEU H H 8.75 . 1 36 11 11 LEU C C 172.7 . 1 37 11 11 LEU CA C 50.5 . 1 38 11 11 LEU N N 124.2 . 1 39 12 12 GLN H H 8.44 . 1 40 12 12 GLN C C 172.8 . 1 41 12 12 GLN CA C 52.2 . 1 42 12 12 GLN N N 120.3 . 1 43 13 13 LEU H H 8.43 . 1 44 13 13 LEU CA C 50.2 . 1 45 13 13 LEU N N 123.2 . 1 46 14 14 PRO C C 173.9 . 1 47 14 14 PRO CA C 58.5 . 1 48 15 15 ALA H H 8.33 . 1 49 15 15 ALA C C 176.5 . 1 50 15 15 ALA CA C 50.3 . 1 51 15 15 ALA N N 127.7 . 1 52 16 16 GLY H H 8.32 . 1 53 16 16 GLY C C 171.2 . 1 54 16 16 GLY CA C 42.7 . 1 55 16 16 GLY N N 109.5 . 1 56 17 17 LYS H H 7.62 . 1 57 17 17 LYS C C 173.3 . 1 58 17 17 LYS CA C 51.7 . 1 59 17 17 LYS N N 120.3 . 1 60 18 18 ALA H H 9.91 . 1 61 18 18 ALA C C 175.2 . 1 62 18 18 ALA CA C 50.7 . 1 63 18 18 ALA N N 126.0 . 1 64 19 19 THR H H 7.87 . 1 65 19 19 THR CA C 56.9 . 1 66 19 19 THR N N 115.0 . 1 67 20 20 PRO C C 173.6 . 1 68 20 20 PRO CA C 60.4 . 1 69 21 21 ALA H H 7.28 . 1 70 21 21 ALA CA C 48.2 . 1 71 21 21 ALA N N 121.5 . 1 72 23 23 PRO C C 174.1 . 1 73 23 23 PRO CA C 61.1 . 1 74 24 24 VAL H H 8.01 . 1 75 24 24 VAL C C 174.7 . 1 76 24 24 VAL CA C 64.2 . 1 77 24 24 VAL N N 127.4 . 1 78 25 25 GLY H H 6.76 . 1 79 25 25 GLY CA C 45.9 . 1 80 25 25 GLY N N 103.9 . 1 81 26 26 PRO C C 176.1 . 1 82 26 26 PRO CA C 61.5 . 1 83 27 27 ALA H H 6.92 . 1 84 27 27 ALA C C 176.5 . 1 85 27 27 ALA CA C 51.6 . 1 86 27 27 ALA N N 117.7 . 1 87 28 28 LEU H H 7.88 . 1 88 28 28 LEU C C 177.5 . 1 89 28 28 LEU CA C 54.0 . 1 90 28 28 LEU N N 114.8 . 1 91 29 29 GLY H H 8.64 . 1 92 29 29 GLY C C 174.9 . 1 93 29 29 GLY CA C 44.1 . 1 94 29 29 GLY N N 110.6 . 1 95 30 30 GLN H H 7.38 . 1 96 30 30 GLN C C 173.4 . 1 97 30 30 GLN CA C 54.5 . 1 98 30 30 GLN N N 118.9 . 1 99 31 31 HIS H H 7.03 . 1 100 31 31 HIS C C 172.5 . 1 101 31 31 HIS CA C 52.7 . 1 102 31 31 HIS N N 114.7 . 1 103 32 32 GLY H H 7.68 . 1 104 32 32 GLY C C 171.2 . 1 105 32 32 GLY CA C 43.3 . 1 106 32 32 GLY N N 107.2 . 1 107 33 33 VAL H H 6.83 . 1 108 33 33 VAL C C 172.3 . 1 109 33 33 VAL CA C 58.5 . 1 110 33 33 VAL N N 117.6 . 1 111 34 34 ASN H H 8.71 . 1 112 34 34 ASN C C 171.9 . 1 113 34 34 ASN CA C 50.5 . 1 114 34 34 ASN N N 124.2 . 1 115 35 35 ILE H H 7.98 . 1 116 35 35 ILE C C 175.4 . 1 117 35 35 ILE CA C 61.9 . 1 118 35 35 ILE N N 129.7 . 1 119 36 36 MET H H 8.32 . 1 120 36 36 MET C C 176.4 . 1 121 36 36 MET CA C 54.9 . 1 122 36 36 MET N N 119.8 . 1 123 37 37 GLU H H 7.88 . 1 124 37 37 GLU C C 176.5 . 1 125 37 37 GLU CA C 56.0 . 1 126 37 37 GLU N N 121.7 . 1 127 38 38 PHE H H 7.95 . 1 128 38 38 PHE C C 173.3 . 1 129 38 38 PHE CA C 59.7 . 1 130 38 38 PHE N N 119.0 . 1 131 39 39 CYS H H 8.27 . 1 132 39 39 CYS C C 173.1 . 1 133 39 39 CYS CA C 61.7 . 1 134 39 39 CYS N N 117.2 . 1 135 40 40 LYS H H 8.07 . 1 136 40 40 LYS C C 177.3 . 1 137 40 40 LYS CA C 56.7 . 1 138 40 40 LYS N N 118.6 . 1 139 41 41 ARG H H 7.98 . 1 140 41 41 ARG C C 176.1 . 1 141 41 41 ARG CA C 56.4 . 1 142 41 41 ARG N N 119.7 . 1 143 42 42 PHE H H 8.74 . 1 144 42 42 PHE C C 176.6 . 1 145 42 42 PHE CA C 59.1 . 1 146 42 42 PHE N N 120.7 . 1 147 43 43 ASN H H 8.81 . 1 148 43 43 ASN C C 174.7 . 1 149 43 43 ASN CA C 52.9 . 1 150 43 43 ASN N N 121.6 . 1 151 44 44 ALA H H 7.65 . 1 152 44 44 ALA C C 177.9 . 1 153 44 44 ALA CA C 51.8 . 1 154 44 44 ALA N N 121.9 . 1 155 45 45 GLU H H 7.62 . 1 156 45 45 GLU C C 175.3 . 1 157 45 45 GLU CA C 55.0 . 1 158 45 45 GLU N N 115.9 . 1 159 46 46 THR H H 7.28 . 1 160 46 46 THR C C 172.6 . 1 161 46 46 THR CA C 58.4 . 1 162 46 46 THR N N 105.0 . 1 163 47 47 ALA H H 7.15 . 1 164 47 47 ALA C C 176.2 . 1 165 47 47 ALA CA C 52.6 . 1 166 47 47 ALA N N 126.1 . 1 167 48 48 ASP H H 8.46 . 1 168 48 48 ASP C C 174.0 . 1 169 48 48 ASP CA C 51.8 . 1 170 48 48 ASP N N 114.6 . 1 171 49 49 LYS H H 7.66 . 1 172 49 49 LYS C C 171.4 . 1 173 49 49 LYS CA C 51.8 . 1 174 49 49 LYS N N 121.4 . 1 175 50 50 ALA H H 6.87 . 1 176 50 50 ALA C C 175.2 . 1 177 50 50 ALA CA C 51.2 . 1 178 50 50 ALA N N 120.5 . 1 179 51 51 GLY H H 9.04 . 1 180 51 51 GLY C C 172.3 . 1 181 51 51 GLY CA C 41.7 . 1 182 51 51 GLY N N 112.5 . 1 183 52 52 MET H H 8.00 . 1 184 52 52 MET CA C 51.9 . 1 185 52 52 MET N N 118.7 . 1 186 55 55 PRO C C 172.9 . 1 187 55 55 PRO CA C 58.3 . 1 188 56 56 VAL H H 9.11 . 1 189 56 56 VAL C C 172.1 . 1 190 56 56 VAL CA C 56.0 . 1 191 56 56 VAL N N 122.6 . 1 192 57 57 VAL H H 8.64 . 1 193 57 57 VAL C C 174.3 . 1 194 57 57 VAL CA C 58.4 . 1 195 57 57 VAL N N 125.8 . 1 196 58 58 ILE H H 9.92 . 1 197 58 58 ILE C C 172.5 . 1 198 58 58 ILE CA C 57.8 . 1 199 58 58 ILE N N 133.1 . 1 200 59 59 THR H H 9.36 . 1 201 59 59 THR C C 169.3 . 1 202 59 59 THR CA C 60.0 . 1 203 59 59 THR N N 126.4 . 1 204 60 60 VAL H H 8.65 . 1 205 60 60 VAL C C 173.2 . 1 206 60 60 VAL CA C 57.4 . 1 207 60 60 VAL N N 126.1 . 1 208 61 61 TYR H H 8.83 . 1 209 61 61 TYR C C 175.6 . 1 210 61 61 TYR CA C 55.4 . 1 211 61 61 TYR N N 127.1 . 1 212 62 62 GLU H H 8.82 . 1 213 62 62 GLU C C 173.1 . 1 214 62 62 GLU CA C 56.1 . 1 215 62 62 GLU N N 120.8 . 1 216 63 63 ASP H H 7.76 . 1 217 63 63 ASP C C 174.1 . 1 218 63 63 ASP CA C 50.3 . 1 219 63 63 ASP N N 117.4 . 1 220 64 64 LYS H H 8.34 . 1 221 64 64 LYS C C 173.0 . 1 222 64 64 LYS CA C 56.0 . 1 223 64 64 LYS N N 113.4 . 1 224 65 65 SER H H 8.05 . 1 225 65 65 SER C C 170.1 . 1 226 65 65 SER CA C 56.1 . 1 227 65 65 SER N N 115.2 . 1 228 66 66 PHE H H 8.14 . 1 229 66 66 PHE C C 172.3 . 1 230 66 66 PHE CA C 53.4 . 1 231 66 66 PHE N N 112.7 . 1 232 67 67 THR H H 9.19 . 1 233 67 67 THR C C 170.3 . 1 234 67 67 THR CA C 57.2 . 1 235 67 67 THR N N 113.3 . 1 236 68 68 PHE H H 8.49 . 1 237 68 68 PHE C C 170.5 . 1 238 68 68 PHE CA C 53.3 . 1 239 68 68 PHE N N 116.2 . 1 240 69 69 ILE H H 8.52 . 1 241 69 69 ILE C C 171.7 . 1 242 69 69 ILE CA C 56.2 . 1 243 69 69 ILE N N 117.9 . 1 244 70 70 ILE H H 8.66 . 1 245 70 70 ILE C C 173.9 . 1 246 70 70 ILE CA C 57.1 . 1 247 70 70 ILE N N 125.2 . 1 248 71 71 LYS H H 8.53 . 1 249 71 71 LYS C C 173.0 . 1 250 71 71 LYS CA C 51.5 . 1 251 71 71 LYS N N 128.0 . 1 252 72 72 THR H H 8.45 . 1 253 72 72 THR CA C 57.9 . 1 254 72 72 THR N N 111.7 . 1 255 74 74 PRO C C 174.9 . 1 256 74 74 PRO CA C 59.2 . 1 257 75 75 ALA H H 9.83 . 1 258 75 75 ALA C C 177.1 . 1 259 75 75 ALA CA C 53.4 . 1 260 75 75 ALA N N 128.5 . 1 261 76 76 SER H H 10.26 . 1 262 76 76 SER C C 173.5 . 1 263 76 76 SER CA C 57.5 . 1 264 76 76 SER N N 114.0 . 1 265 77 77 PHE H H 6.79 . 1 266 77 77 PHE C C 174.5 . 1 267 77 77 PHE CA C 58.3 . 1 268 77 77 PHE N N 123.9 . 1 269 78 78 LEU H H 8.11 . 1 270 78 78 LEU C C 178.1 . 1 271 78 78 LEU CA C 54.3 . 1 272 78 78 LEU N N 119.4 . 1 273 79 79 LEU H H 8.65 . 1 274 79 79 LEU C C 175.4 . 1 275 79 79 LEU CA C 55.3 . 1 276 79 79 LEU N N 121.9 . 1 277 80 80 LYS H H 7.57 . 1 278 80 80 LYS C C 176.1 . 1 279 80 80 LYS CA C 57.6 . 1 280 80 80 LYS N N 119.3 . 1 281 81 81 LYS H H 7.39 . 1 282 81 81 LYS C C 177.3 . 1 283 81 81 LYS CA C 54.7 . 1 284 81 81 LYS N N 117.0 . 1 285 82 82 ALA H H 7.89 . 1 286 82 82 ALA C C 175.8 . 1 287 82 82 ALA CA C 51.6 . 1 288 82 82 ALA N N 122.8 . 1 289 83 83 ALA H H 8.03 . 1 290 83 83 ALA C C 175.1 . 1 291 83 83 ALA CA C 49.0 . 1 292 83 83 ALA N N 117.9 . 1 293 84 84 GLY H H 7.82 . 1 294 84 84 GLY C C 172.3 . 1 295 84 84 GLY CA C 43.5 . 1 296 84 84 GLY N N 109.2 . 1 297 85 85 ILE H H 7.73 . 1 298 85 85 ILE C C 172.2 . 1 299 85 85 ILE CA C 56.1 . 1 300 85 85 ILE N N 112.0 . 1 301 86 86 GLU H H 8.46 . 1 302 86 86 GLU C C 174.2 . 1 303 86 86 GLU CA C 53.8 . 1 304 86 86 GLU N N 119.0 . 1 305 87 87 LYS H H 7.35 . 1 306 87 87 LYS C C 173.7 . 1 307 87 87 LYS CA C 50.8 . 1 308 87 87 LYS N N 117.3 . 1 309 88 88 GLY H H 8.89 . 1 310 88 88 GLY C C 169.5 . 1 311 88 88 GLY CA C 40.7 . 1 312 88 88 GLY N N 106.8 . 1 313 89 89 SER H H 7.86 . 1 314 89 89 SER C C 174.2 . 1 315 89 89 SER CA C 54.7 . 1 316 89 89 SER N N 110.0 . 1 317 90 90 SER H H 8.51 . 1 318 90 90 SER CA C 57.0 . 1 319 90 90 SER N N 122.1 . 1 320 91 91 GLU H H 8.20 . 1 321 91 91 GLU N N 120.0 . 1 322 92 92 PRO C C 171.3 . 1 323 93 93 LYS H H 8.55 . 1 324 93 93 LYS C C 174.6 . 1 325 93 93 LYS CA C 52.2 . 1 326 93 93 LYS N N 128.1 . 1 327 94 94 ARG H H 7.94 . 1 328 94 94 ARG C C 174.1 . 1 329 94 94 ARG CA C 54.9 . 1 330 94 94 ARG N N 119.5 . 1 331 95 95 LYS H H 8.54 . 1 332 95 95 LYS C C 172.1 . 1 333 95 95 LYS CA C 52.2 . 1 334 95 95 LYS N N 120.3 . 1 335 96 96 ILE H H 8.70 . 1 336 96 96 ILE C C 175.6 . 1 337 96 96 ILE CA C 55.3 . 1 338 96 96 ILE N N 129.4 . 1 339 97 97 VAL H H 9.01 . 1 340 97 97 VAL C C 172.8 . 1 341 97 97 VAL CA C 57.7 . 1 342 97 97 VAL N N 119.4 . 1 343 98 98 GLY H H 7.55 . 1 344 98 98 GLY C C 167.2 . 1 345 98 98 GLY CA C 42.2 . 1 346 98 98 GLY N N 107.8 . 1 347 99 99 LYS H H 8.79 . 1 348 99 99 LYS C C 172.2 . 1 349 99 99 LYS CA C 51.7 . 1 350 99 99 LYS N N 119.1 . 1 351 100 100 VAL H H 8.58 . 1 352 100 100 VAL C C 171.9 . 1 353 100 100 VAL CA C 55.3 . 1 354 100 100 VAL N N 114.0 . 1 355 101 101 THR H H 8.90 . 1 356 101 101 THR C C 174.8 . 1 357 101 101 THR CA C 56.7 . 1 358 101 101 THR N N 112.4 . 1 359 102 102 ARG H H 8.61 . 1 360 102 102 ARG C C 176.2 . 1 361 102 102 ARG CA C 56.7 . 1 362 102 102 ARG N N 121.8 . 1 363 103 103 LYS H H 8.20 . 1 364 103 103 LYS C C 176.5 . 1 365 103 103 LYS CA C 55.6 . 1 366 103 103 LYS N N 120.3 . 1 367 104 104 GLN H H 7.78 . 1 368 104 104 GLN C C 177.0 . 1 369 104 104 GLN CA C 56.4 . 1 370 104 104 GLN N N 119.9 . 1 371 105 105 ILE H H 8.13 . 1 372 105 105 ILE C C 174.9 . 1 373 105 105 ILE CA C 59.9 . 1 374 105 105 ILE N N 120.3 . 1 375 106 106 GLU H H 8.43 . 1 376 106 106 GLU C C 175.1 . 1 377 106 106 GLU CA C 57.3 . 1 378 106 106 GLU N N 122.9 . 1 379 107 107 GLU H H 7.88 . 1 380 107 107 GLU C C 177.4 . 1 381 107 107 GLU CA C 56.4 . 1 382 107 107 GLU N N 118.7 . 1 383 108 108 ILE H H 8.26 . 1 384 108 108 ILE C C 174.8 . 1 385 108 108 ILE CA C 62.8 . 1 386 108 108 ILE N N 122.5 . 1 387 109 109 ALA H H 8.92 . 1 388 109 109 ALA C C 176.0 . 1 389 109 109 ALA CA C 52.7 . 1 390 109 109 ALA N N 123.2 . 1 391 110 110 LYS H H 8.32 . 1 392 110 110 LYS C C 177.2 . 1 393 110 110 LYS CA C 57.3 . 1 394 110 110 LYS N N 115.8 . 1 395 111 111 THR H H 8.01 . 1 396 111 111 THR CA C 63.6 . 1 397 111 111 THR N N 117.6 . 1 398 112 112 LYS H H 8.22 . 1 399 112 112 LYS C C 174.0 . 1 400 112 112 LYS CA C 51.9 . 1 401 112 112 LYS N N 115.7 . 1 402 113 113 MET H H 7.56 . 1 403 113 113 MET CA C 57.1 . 1 404 113 113 MET N N 121.2 . 1 405 114 114 PRO C C 174.7 . 1 406 115 115 ASP H H 8.45 . 1 407 115 115 ASP C C 172.8 . 1 408 115 115 ASP CA C 51.3 . 1 409 115 115 ASP N N 114.9 . 1 410 116 116 LEU H H 7.80 . 1 411 116 116 LEU C C 173.8 . 1 412 116 116 LEU CA C 49.8 . 1 413 116 116 LEU N N 118.3 . 1 414 117 117 ASN H H 7.78 . 1 415 117 117 ASN C C 172.3 . 1 416 117 117 ASN CA C 48.7 . 1 417 117 117 ASN N N 116.7 . 1 418 118 118 ALA H H 6.21 . 1 419 118 118 ALA C C 174.1 . 1 420 118 118 ALA CA C 49.0 . 1 421 118 118 ALA N N 119.8 . 1 422 119 119 ASN H H 8.91 . 1 423 119 119 ASN C C 171.9 . 1 424 119 119 ASN CA C 49.6 . 1 425 119 119 ASN N N 116.9 . 1 426 120 120 SER H H 7.33 . 1 427 120 120 SER C C 171.4 . 1 428 120 120 SER CA C 53.5 . 1 429 120 120 SER N N 111.5 . 1 430 121 121 LEU H H 8.94 . 1 431 121 121 LEU C C 175.7 . 1 432 121 121 LEU CA C 54.6 . 1 433 121 121 LEU N N 125.2 . 1 434 122 122 GLU H H 8.94 . 1 435 122 122 GLU C C 176.5 . 1 436 122 122 GLU CA C 57.4 . 1 437 122 122 GLU N N 119.4 . 1 438 123 123 ALA H H 7.53 . 1 439 123 123 ALA C C 176.5 . 1 440 123 123 ALA CA C 51.9 . 1 441 123 123 ALA N N 121.7 . 1 442 124 124 ALA H H 7.84 . 1 443 124 124 ALA C C 176.9 . 1 444 124 124 ALA CA C 51.7 . 1 445 124 124 ALA N N 120.2 . 1 446 125 125 MET H H 8.62 . 1 447 125 125 MET C C 175.4 . 1 448 125 125 MET CA C 57.5 . 1 449 125 125 MET N N 116.9 . 1 450 126 126 LYS H H 7.29 . 1 451 126 126 LYS CA C 57.3 . 1 452 126 126 LYS N N 119.2 . 1 453 127 127 ILE H H 7.57 . 1 454 127 127 ILE CA C 62.2 . 1 455 127 127 ILE N N 121.6 . 1 456 128 128 ILE H H 7.86 . 1 457 128 128 ILE C C 177.0 . 1 458 128 128 ILE CA C 58.9 . 1 459 128 128 ILE N N 119.7 . 1 460 129 129 GLU H H 8.85 . 1 461 129 129 GLU C C 175.8 . 1 462 129 129 GLU CA C 57.0 . 1 463 129 129 GLU N N 121.2 . 1 464 130 130 GLY H H 7.96 . 1 465 130 130 GLY C C 175.9 . 1 466 130 130 GLY CA C 44.7 . 1 467 130 130 GLY N N 108.5 . 1 468 131 131 THR H H 7.77 . 1 469 131 131 THR C C 175.5 . 1 470 131 131 THR CA C 63.6 . 1 471 131 131 THR N N 122.3 . 1 472 132 132 ALA H H 8.36 . 1 473 132 132 ALA C C 176.5 . 1 474 132 132 ALA CA C 54.1 . 1 475 132 132 ALA N N 129.7 . 1 476 133 133 LYS H H 8.17 . 1 477 133 133 LYS C C 176.6 . 1 478 133 133 LYS CA C 56.4 . 1 479 133 133 LYS N N 117.2 . 1 480 134 134 SER H H 7.43 . 1 481 134 134 SER C C 170.1 . 1 482 134 134 SER CA C 57.5 . 1 483 134 134 SER N N 116.7 . 1 484 135 135 MET H H 7.33 . 1 485 135 135 MET C C 174.0 . 1 486 135 135 MET CA C 51.9 . 1 487 135 135 MET N N 113.3 . 1 488 136 136 GLY H H 7.81 . 1 489 136 136 GLY C C 170.3 . 1 490 136 136 GLY CA C 44.0 . 1 491 136 136 GLY N N 108.0 . 1 492 137 137 ILE H H 7.40 . 1 493 137 137 ILE C C 172.4 . 1 494 137 137 ILE CA C 56.5 . 1 495 137 137 ILE N N 119.0 . 1 496 138 138 GLU H H 8.40 . 1 497 138 138 GLU C C 171.7 . 1 498 138 138 GLU CA C 51.9 . 1 499 138 138 GLU N N 128.4 . 1 500 139 139 VAL H H 8.24 . 1 501 139 139 VAL C C 174.0 . 1 502 139 139 VAL CA C 58.2 . 1 503 139 139 VAL N N 124.5 . 1 504 140 140 VAL H H 8.85 . 1 505 140 140 VAL C C 171.8 . 1 506 140 140 VAL CA C 56.9 . 1 507 140 140 VAL N N 125.1 . 1 508 141 141 ASP H H 7.92 . 1 509 141 141 ASP CA C 54.0 . 1 510 141 141 ASP N N 126.1 . 1 stop_ save_ save_RDC_list_LR _Saveframe_category residual_dipolar_couplings loop_ _Sample_label $L11+RNA $L11+RNA stop_ loop_ _Residual_dipolar_coupling_ID _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name _Residual_dipolar_coupling_value _Atom_one_mol_system_component_name _Atom_two_mol_system_component_name _Residual_dipolar_coupling_min_value _Residual_dipolar_coupling_max_value _Residual_dipolar_coupling_value_error 1DHNN 3 LYS H 3 LYS N 4.86 ? ? . . 2 1DHNN 4 LYS H 4 LYS N -6.87 ? ? . . 2 1DHNN 5 VAL H 5 VAL N 5.64 ? ? . . 2 1DHNN 6 ALA H 6 ALA N 14.47 ? ? . . 2 1DHNN 7 ALA H 7 ALA N -4.49 ? ? . . 2 1DHNN 8 GLN H 8 GLN N -6.57 ? ? . . 2 1DHNN 9 ILE H 9 ILE N -10.58 ? ? . . 2 1DHNN 10 LYS H 10 LYS N -2.73 ? ? . . 2 1DHNN 11 LEU H 11 LEU N -2.98 ? ? . . 2 1DHNN 12 GLN H 12 GLN N 2.74 ? ? . . 2 1DHNN 13 LEU H 13 LEU N -2.98 ? ? . . 2 1DHNN 15 ALA H 15 ALA N -22.50 ? ? . . 2 1DHNN 16 GLY H 16 GLY N 10.03 ? ? . . 2 1DHNN 17 LYS H 17 LYS N -8.88 ? ? . . 2 1DHNN 18 ALA H 18 ALA N -1.95 ? ? . . 2 1DHNN 19 THR H 19 THR N -3.34 ? ? . . 2 1DHNN 21 ALA H 21 ALA N 7.66 ? ? . . 2 1DHNN 24 VAL H 24 VAL N 11.73 ? ? . . 2 1DHNN 25 GLY H 25 GLY N 11.06 ? ? . . 2 1DHNN 27 ALA H 27 ALA N 9.24 ? ? . . 2 1DHNN 28 LEU H 28 LEU N -4.44 ? ? . . 2 1DHNN 29 GLY H 29 GLY N 4.98 ? ? . . 2 1DHNN 30 GLN H 30 GLN N 5.23 ? ? . . 2 1DHNN 31 HIS H 31 HIS N 8.45 ? ? . . 2 1DHNN 32 GLY H 32 GLY N -1.16 ? ? . . 2 1DHNN 33 VAL H 33 VAL N -17.88 ? ? . . 2 1DHNN 34 ASN H 34 ASN N 4.50 ? ? . . 2 1DHNN 35 ILE H 35 ILE N 13.01 ? ? . . 2 1DHNN 36 MET H 36 MET N 6.98 ? ? . . 2 1DHNN 37 GLU H 37 GLU N 19.76 ? ? . . 2 1DHNN 38 PHE H 38 PHE N 8.94 ? ? . . 2 1DHNN 39 CYS H 39 CYS N 5.73 ? ? . . 2 1DHNN 40 LYS H 40 LYS N 6.56 ? ? . . 2 1DHNN 41 ARG H 41 ARG N 11.12 ? ? . . 2 1DHNN 42 PHE H 42 PHE N 8.03 ? ? . . 2 1DHNN 43 ASN H 43 ASN N 0.31 ? ? . . 2 1DHNN 44 ALA H 44 ALA N 8.88 ? ? . . 2 1DHNN 45 GLU H 45 GLU N 9.30 ? ? . . 2 1DHNN 46 THR H 46 THR N 4.99 ? ? . . 2 1DHNN 47 ALA H 47 ALA N -5.83 ? ? . . 2 1DHNN 48 ASP H 48 ASP N 10.46 ? ? . . 2 1DHNN 49 LYS H 49 LYS N 3.29 ? ? . . 2 1DHNN 50 ALA H 50 ALA N -15.62 ? ? . . 2 1DHNN 51 GLY H 51 GLY N -1.58 ? ? . . 2 1DHNN 52 MET H 52 MET N -0.05 ? ? . . 2 1DHNN 56 VAL H 56 VAL N 1.46 ? ? . . 2 1DHNN 57 VAL H 57 VAL N 1.22 ? ? . . 2 1DHNN 58 ILE H 58 ILE N -8.75 ? ? . . 2 1DHNN 59 THR H 59 THR N -5.00 ? ? . . 2 1DHNN 60 VAL H 60 VAL N 8.82 ? ? . . 2 1DHNN 61 TYR H 61 TYR N -1.21 ? ? . . 2 1DHNN 62 GLU H 62 GLU N 13.92 ? ? . . 2 1DHNN 63 ASP H 63 ASP N 7.36 ? ? . . 2 1DHNN 64 LYS H 64 LYS N -6.80 ? ? . . 2 1DHNN 65 SER H 65 SER N 10.82 ? ? . . 2 1DHNN 66 PHE H 66 PHE N -6.93 ? ? . . 2 1DHNN 67 THR H 67 THR N -8.02 ? ? . . 2 1DHNN 68 PHE H 68 PHE N -3.96 ? ? . . 2 1DHNN 69 ILE H 69 ILE N -5.47 ? ? . . 2 1DHNN 70 ILE H 70 ILE N -3.52 ? ? . . 2 1DHNN 71 LYS H 71 LYS N 10.03 ? ? . . 2 1DHNN 72 THR H 72 THR N 20.52 ? ? . . 2 1DHNN 75 ALA H 75 ALA N 12.28 ? ? . . 2 1DHNN 76 SER H 76 SER N 7.11 ? ? . . 2 1DHNN 77 PHE H 77 PHE N 9.12 ? ? . . 2 1DHNN 78 LEU H 78 LEU N 19.20 ? ? . . 2 1DHNN 79 LEU H 79 LEU N 6.63 ? ? . . 2 1DHNN 80 LYS H 80 LYS N -5.53 ? ? . . 2 1DHNN 81 LYS H 81 LYS N 6.09 ? ? . . 2 1DHNN 82 ALA H 82 ALA N 21.03 ? ? . . 2 1DHNN 83 ALA H 83 ALA N 13.50 ? ? . . 2 1DHNN 84 GLY H 84 GLY N -5.84 ? ? . . 2 1DHNN 85 ILE H 85 ILE N 10.10 ? ? . . 2 1DHNN 86 GLU H 86 GLU N -4.25 ? ? . . 2 1DHNN 87 LYS H 87 LYS N 2.22 ? ? . . 2 1DHNN 88 GLY H 88 GLY N -1.71 ? ? . . 2 1DHNN 89 SER H 89 SER N 12.40 ? ? . . 2 1DHNN 90 SER H 90 SER N 15.93 ? ? . . 2 1DHNN 91 GLU H 91 GLU N -1.69 ? ? . . 2 1DHNN 93 LYS H 93 LYS N 12.70 ? ? . . 2 1DHNN 94 ARG H 94 ARG N 7.30 ? ? . . 2 1DHNN 95 LYS H 95 LYS N -2.38 ? ? . . 2 1DHNN 96 ILE H 96 ILE N -13.68 ? ? . . 2 1DHNN 97 VAL H 97 VAL N 12.34 ? ? . . 2 1DHNN 98 GLY H 98 GLY N 7.66 ? ? . . 2 1DHNN 99 LYS H 99 LYS N 6.02 ? ? . . 2 1DHNN 100 VAL H 100 VAL N -3.53 ? ? . . 2 1DHNN 101 THR H 101 THR N -13.08 ? ? . . 2 1DHNN 102 ARG H 102 ARG N -16.17 ? ? . . 2 1DHNN 103 LYS H 103 LYS N -1.14 ? ? . . 2 1DHNN 104 GLN H 104 GLN N -2.67 ? ? . . 2 1DHNN 105 ILE H 105 ILE N -5.52 ? ? . . 2 1DHNN 106 GLU H 106 GLU N 3.95 ? ? . . 2 1DHNN 107 GLU H 107 GLU N -6.88 ? ? . . 2 1DHNN 108 ILE H 108 ILE N -13.44 ? ? . . 2 1DHNN 109 ALA H 109 ALA N -11.80 ? ? . . 2 1DHNN 110 LYS H 110 LYS N 4.86 ? ? . . 2 1DHNN 111 THR H 111 THR N -8.02 ? ? . . 2 1DHNN 112 LYS H 112 LYS N -13.06 ? ? . . 2 1DHNN 113 MET H 113 MET N 5.42 ? ? . . 2 1DHNN 115 ASP H 115 ASP N 11.55 ? ? . . 2 1DHNN 116 LEU H 116 LEU N -0.92 ? ? . . 2 1DHNN 117 ASN H 117 ASN N 0.55 ? ? . . 2 1DHNN 118 ALA H 118 ALA N 13.62 ? ? . . 2 1DHNN 119 ASN H 119 ASN N -20.80 ? ? . . 2 1DHNN 120 SER H 120 SER N -8.20 ? ? . . 2 1DHNN 121 LEU H 121 LEU N -1.27 ? ? . . 2 1DHNN 122 GLU H 122 GLU N 6.99 ? ? . . 2 1DHNN 123 ALA H 123 ALA N -1.94 ? ? . . 2 1DHNN 124 ALA H 124 ALA N 0.36 ? ? . . 2 1DHNN 125 MET H 125 MET N 6.37 ? ? . . 2 1DHNN 126 LYS H 126 LYS N 10.10 ? ? . . 2 1DHNN 127 ILE H 127 ILE N 1.95 ? ? . . 2 1DHNN 128 ILE H 128 ILE N 0.61 ? ? . . 2 1DHNN 129 GLU H 129 GLU N 9.66 ? ? . . 2 1DHNN 130 GLY H 130 GLY N 0.30 ? ? . . 2 1DHNN 131 THR H 131 THR N -1.21 ? ? . . 2 1DHNN 132 ALA H 132 ALA N 11.07 ? ? . . 2 1DHNN 133 LYS H 133 LYS N 9.66 ? ? . . 2 1DHNN 134 SER H 134 SER N -12.78 ? ? . . 2 1DHNN 135 MET H 135 MET N 4.93 ? ? . . 2 1DHNN 136 GLY H 136 GLY N 18.91 ? ? . . 2 1DHNN 137 ILE H 137 ILE N 1.40 ? ? . . 2 1DHNN 138 GLU H 138 GLU N 19.27 ? ? . . 2 1DHNN 139 VAL H 139 VAL N -1.94 ? ? . . 2 1DHNN 140 VAL H 140 VAL N -14.89 ? ? . . 2 1DHNN 141 ASP H 141 ASP N -17.93 ? ? . . 2 stop_ _Details L11+RNA _Sample_conditions_label $25C _Spectrometer_frequency_1H 600 _Text_data_format . _Text_data . save_