data_4134 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Assignments for Denatured LysN ; _BMRB_accession_number 4134 _BMRB_flat_file_name bmr4134.str _Entry_type original _Submission_date 1998-04-16 _Accession_date 1998-04-16 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; NMR assignments for the N-terminal anticodon binding domain of lysyl-tRNA synthesase in its denatured form (pH 2.8, 3M urea, 11 oC). The aim of this study is to determine if residual structure is conserved in the denatured states of three proteins (LysN, cold shock protein A [BMRB 4107 & 4108], microccocal nuclease) that share a similar native state OB-fold, in spite of no detectable sequence homology. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Alexandrescu Andrei T. . 2 Jaravine Viktor A. . 3 Lamour Francois P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 372 "13C chemical shifts" 219 "15N chemical shifts" 115 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-06-17 revision author 'comments added to chemical shift saveframe' stop_ loop_ _Related_BMRB_accession_number _Relationship 4107 'denatured state assignments of a protein belonging to the OB-fold superfamily' 4108 'denatured state assignments of a protein belonging to the OB-fold superfamily' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Alexandrescu, A. T., Jaravine, Viktor A., and Lamour, F. P., "NMR Assignments for Denatured LysN," ; _Citation_title 'NMR Assignments for denatured LysN' _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Alexandrescu Andrei T. . 2 Jaravine Viktor A. . 3 Lamour Francois P. . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 1999 _Details . loop_ _Keyword 'denatured state' 'lysyl-tRNA synthetase' OB-fold 'protein folding' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Wishart D. S., Bigam C .G., Yao J., Abildgaard F., Dyson H. J., Oldfield E., Markley J. L., Sykes B. D. , '1H, 13C and 15N chemical shift referencing in biomolecular NMR,' J. Biomol. NMR 6, 135-140 (1995). ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _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 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_den-LysN _Saveframe_category molecular_system _Mol_system_name den-LysN _Abbreviation_common den-LysN _Enzyme_commission_number 'EC 6.1.1.6' loop_ _Mol_system_component_name _Mol_label den-LysN $den-LysN stop_ _System_molecular_weight 13526 _System_physical_state denatured _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'LysN is the N-terminal anticodon binding domain of the lysyl-tRNA synthetase' stop_ _Database_query_date . _Details ; NMR structures of native LysN ; save_ ######################## # Monomeric polymers # ######################## save_den-LysN _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common lysl-tRNA_synthetase _Abbreviation_common den-LysN _Molecular_mass . _Mol_thiol_state . loop_ _Biological_function 'LysN is the N-terminal anticodon binding domain of the lysyl-tRNA synthetase' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 120 _Mol_residue_sequence ; AEQGIAFPNDFRRDHTSDQL HAEFDGKENEELEALNIEVA VAGRMMTRRIMGKASFVTLQ DVGGRIQLYVARDDLPEGVY NEQFKKWDLGDILGAKGKLF KTKTGELSIHCTELRLLTKA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ALA 2 31 GLU 3 32 GLN 4 33 GLY 5 34 ILE 6 35 ALA 7 36 PHE 8 37 PRO 9 38 ASN 10 39 ASP 11 40 PHE 12 41 ARG 13 42 ARG 14 43 ASP 15 44 HIS 16 45 THR 17 46 SER 18 47 ASP 19 48 GLN 20 49 LEU 21 50 HIS 22 51 ALA 23 52 GLU 24 53 PHE 25 54 ASP 26 55 GLY 27 56 LYS 28 57 GLU 29 58 ASN 30 59 GLU 31 60 GLU 32 61 LEU 33 62 GLU 34 63 ALA 35 64 LEU 36 65 ASN 37 66 ILE 38 67 GLU 39 68 VAL 40 69 ALA 41 70 VAL 42 71 ALA 43 72 GLY 44 73 ARG 45 74 MET 46 75 MET 47 76 THR 48 77 ARG 49 78 ARG 50 79 ILE 51 80 MET 52 81 GLY 53 82 LYS 54 83 ALA 55 84 SER 56 85 PHE 57 86 VAL 58 87 THR 59 88 LEU 60 89 GLN 61 90 ASP 62 91 VAL 63 92 GLY 64 93 GLY 65 94 ARG 66 95 ILE 67 96 GLN 68 97 LEU 69 98 TYR 70 99 VAL 71 100 ALA 72 101 ARG 73 102 ASP 74 103 ASP 75 104 LEU 76 105 PRO 77 106 GLU 78 107 GLY 79 108 VAL 80 109 TYR 81 110 ASN 82 111 GLU 83 112 GLN 84 113 PHE 85 114 LYS 86 115 LYS 87 116 TRP 88 117 ASP 89 118 LEU 90 119 GLY 91 120 ASP 92 121 ILE 93 122 LEU 94 123 GLY 95 124 ALA 96 125 LYS 97 126 GLY 98 127 LYS 99 128 LEU 100 129 PHE 101 130 LYS 102 131 THR 103 132 LYS 104 133 THR 105 134 GLY 106 135 GLU 107 136 LEU 108 137 SER 109 138 ILE 110 139 HIS 111 140 CYS 112 141 THR 113 142 GLU 114 143 LEU 115 144 ARG 116 145 LEU 117 146 LEU 118 147 THR 119 148 LYS 120 149 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-03 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 1BBU "Lysyl-Trna Synthetase (Lyss) Complexed With Lysine" 99.17 504 100.00 100.00 6.92e-77 PDB 1BBW "Lysyl-Trna Synthetase (Lyss)" 99.17 504 100.00 100.00 6.92e-77 PDB 1KRS "Solution Structure Of The Anticodon Binding Domain Of Escherichia Coli Lysyl-Trna Synthetase And Studies Of Its Interactions Wi" 100.00 120 100.00 100.00 8.48e-82 PDB 1KRT "Solution Structure Of The Anticodon Binding Domain Of Escherichia Coli Lysyl-Trna Synthetase And Studies Of Its Interactions Wi" 100.00 120 100.00 100.00 8.48e-82 DBJ BAB37185 "lysine tRNA synthetase [Escherichia coli O157:H7 str. Sakai]" 99.17 505 100.00 100.00 7.24e-77 DBJ BAE76955 "lysine tRNA synthetase, constitutive [Escherichia coli str. K12 substr. W3110]" 99.17 505 100.00 100.00 6.79e-77 DBJ BAG78677 "lysyl-tRNA synthase [Escherichia coli SE11]" 99.17 505 100.00 100.00 6.79e-77 DBJ BAI27164 "lysine tRNA synthetase LysS, constitutive [Escherichia coli O26:H11 str. 11368]" 99.17 505 99.16 100.00 1.17e-76 DBJ BAI32202 "lysine tRNA synthetase LysS, constitutive [Escherichia coli O103:H2 str. 12009]" 99.17 505 100.00 100.00 7.72e-77 EMBL CAP77327 "Lysyl-tRNA synthetase [Escherichia coli LF82]" 99.17 505 100.00 100.00 6.79e-77 EMBL CAQ33202 "lysyl tRNA synthetase (LysRSs), constitutive, subunit of lysyl-tRNA synthetase, constitutive [Escherichia coli BL21(DE3)]" 99.17 505 100.00 100.00 6.79e-77 EMBL CAQ90319 "lysine tRNA synthetase, constitutive [Escherichia fergusonii ATCC 35469]" 99.17 505 99.16 100.00 2.59e-76 EMBL CAQ99824 "lysine tRNA synthetase, constitutive [Escherichia coli IAI1]" 99.17 505 100.00 100.00 7.72e-77 EMBL CAR04406 "lysine tRNA synthetase, constitutive [Escherichia coli S88]" 99.17 505 100.00 100.00 6.79e-77 GB AAA23959 "herC protein [Escherichia coli]" 99.17 505 100.00 100.00 6.79e-77 GB AAA83071 "lysyl tRNA synthetase (LysRS), constitutive [Escherichia coli]" 99.17 505 100.00 100.00 6.79e-77 GB AAC75928 "lysine tRNA synthetase, constitutive [Escherichia coli str. K-12 substr. MG1655]" 99.17 505 100.00 100.00 6.79e-77 GB AAG58018 "lysine tRNA synthetase, constitutive; suppressor of ColE1 mutation in primer RNA [Escherichia coli O157:H7 str. EDL933]" 99.17 505 100.00 100.00 7.24e-77 GB AAN44362 "lysine tRNA synthetase [Shigella flexneri 2a str. 301]" 99.17 505 100.00 100.00 7.72e-77 REF NP_311789 "lysyl-tRNA synthetase [Escherichia coli O157:H7 str. Sakai]" 99.17 505 100.00 100.00 7.24e-77 REF NP_417366 "lysine tRNA synthetase, constitutive [Escherichia coli str. K-12 substr. MG1655]" 99.17 505 100.00 100.00 6.79e-77 REF NP_708655 "lysyl-tRNA synthetase [Shigella flexneri 2a str. 301]" 99.17 505 100.00 100.00 7.72e-77 REF WP_000003059 "lysine--tRNA ligase [Escherichia coli]" 99.17 505 99.16 99.16 3.74e-75 REF WP_000003060 "lysine--tRNA ligase [Escherichia coli]" 99.17 505 99.16 100.00 1.21e-76 SP B2U0Q7 "RecName: Full=Lysine--tRNA ligase; AltName: Full=Lysyl-tRNA synthetase; Short=LysRS" 99.17 505 100.00 100.00 7.72e-77 SP P0A8N3 "RecName: Full=Lysine--tRNA ligase; AltName: Full=Lysyl-tRNA synthetase; Short=LysRS" 99.17 505 100.00 100.00 6.79e-77 SP P0A8N4 "RecName: Full=Lysine--tRNA ligase; AltName: Full=Lysyl-tRNA synthetase; Short=LysRS" 99.17 505 100.00 100.00 6.79e-77 SP Q0T106 "RecName: Full=Lysine--tRNA ligase; AltName: Full=Lysyl-tRNA synthetase; Short=LysRS" 99.17 505 100.00 100.00 7.72e-77 SP Q31WF2 "RecName: Full=Lysine--tRNA ligase; AltName: Full=Lysyl-tRNA synthetase; Short=LysRS" 99.17 505 99.16 99.16 2.94e-76 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Variant _Details $den-LysN 'E. coli' 562 Eubacteria . Escherichia coli K12 ; Commans, S.; Plateau,P.; Blanquet, S.; Dardel, F. (1995) "Solution structure of the anticodon-binding domain of Escherichia coli Lysyl-tRNA synthetase and studies of its interaction with tRNALys" J. Mol. Biol. 253:100-113. ; 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 _Vendor_name _Details $den-LysN 'recombinant technology' 'E. coli' Escherichia coli . plasmid pET28a Novagen ; natural (A 374 bp NcoI-BamHI fragment of the pTRc-N? plasmid [Commans, S., Plateau,P., Blanquet, S., Dardel, F. (1995) "Solution structure of the anticodon-binding domain of Escherichia coli Lysyl-tRNA synthetase and studies of its interaction with tRNALys" J. Mol. Biol. 253:100-113.], encoding the gene for LysN was transferred into the NcoI-BamHI sites of the pET28a vector (Novagen) to yield the plasmid pFLI-N. E. coli strain BL21(DE3)pLysS (Novagen) was used for expression) ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $den-LysN 1.5 mM '[U-15N; U-13C]' urea 3 M . H2O 90 % . D2O 10 % . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $den-LysN 1 mM [U-15N] urea 3 M . H2O 90 % . D2O 10 % . stop_ save_ ############################# # Purity of the molecules # ############################# save_mol_purity_list _Saveframe_category sample_mol_purity _Sample_label $sample_one loop_ _Mol_label _Mol_purity_value _Mol_purity_value_units _Mol_purity_measurement_method $den-LysN 95 % SDS-PAGE $den-LysN 95 % SDS-PAGE stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity plus' _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_NMR_spectral_acquisition_parameters_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'NMR spectral acquisition parameters' _Sample_label $sample_two save_ save_t3_H_599.9094119_146ms_._7000Hz_No_1024_complex_._2 _Saveframe_category NMR_applied_experiment _Experiment_name 't3 H 599.9094119 146ms . 7000Hz No 1024 complex .' _Sample_label $sample_two save_ save_t2_C_150.8529083_7.7ms_._8300Hz_No_64_complex_._3 _Saveframe_category NMR_applied_experiment _Experiment_name 't2 C 150.8529083 7.7ms . 8300Hz No 64 complex .' _Sample_label $sample_two save_ save_t1_N_60.7952139_21ms_._1540Hz_No_32_complex_._4 _Saveframe_category NMR_applied_experiment _Experiment_name 't1 N 60.7952139 21ms . 1540Hz No 32 complex .' _Sample_label $sample_two save_ save_NMR_spectral_processing_parameters_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'NMR spectral processing parameters' _Sample_label $sample_two save_ save_D1_H_sine-bell_1024_90_Zero-fill_2048_6 _Saveframe_category NMR_applied_experiment _Experiment_name 'D1 H sine-bell 1024 90 Zero-fill 2048' _Sample_label $sample_two save_ save_D2_C_squared-sine-bell_64_70_Zero-fill_128_7 _Saveframe_category NMR_applied_experiment _Experiment_name 'D2 C squared-sine-bell 64 70 Zero-fill 128' _Sample_label $sample_two save_ save_D3_N_linear_predict_32_to_48_squaredsine-bell_48_70_Zero-fill_64_8 _Saveframe_category NMR_applied_experiment _Experiment_name 'D3 N linear predict 32 to 48 squaredsine-bell 48 70 Zero-fill 64' _Sample_label $sample_two save_ save_46_ms_mix_time_9 _Saveframe_category NMR_applied_experiment _Experiment_name '46 ms mix time' _Sample_label $sample_one save_ save_NMR_spectral_acquisition_parameters_10 _Saveframe_category NMR_applied_experiment _Experiment_name 'NMR spectral acquisition parameters' _Sample_label $sample_one save_ save_t3_H_600.1328206MHz_85ms_46ms_6009.615Hz_No_512_complex_._11 _Saveframe_category NMR_applied_experiment _Experiment_name 't3 H 600.1328206MHz 85ms 46ms 6009.615Hz No 512 complex .' _Sample_label $sample_one save_ save_t2_N_60.8178387MHz_21ms_._1521Hz_No_32_complex_._12 _Saveframe_category NMR_applied_experiment _Experiment_name 't2 N 60.8178387MHz 21ms . 1521Hz No 32 complex .' _Sample_label $sample_one save_ save_t1_H_600.1328206MHz_21ms_._6009.615Hz_No_128_complex_._13 _Saveframe_category NMR_applied_experiment _Experiment_name 't1 H 600.1328206MHz 21ms . 6009.615Hz No 128 complex .' _Sample_label $sample_one save_ save_NMR_spectral_processing_parameters_14 _Saveframe_category NMR_applied_experiment _Experiment_name 'NMR spectral processing parameters' _Sample_label $sample_one save_ save_3D_[1H-15N]_TOCSY-HSQC_15 _Saveframe_category NMR_applied_experiment _Experiment_name '3D [1H-15N] TOCSY-HSQC' _Sample_label $sample_one save_ save_D1_H_gm_-10_0.1_Zero-fill_1024_16 _Saveframe_category NMR_applied_experiment _Experiment_name 'D1 H gm -10 0.1 Zero-fill 1024' _Sample_label $sample_one save_ save_D2_N_lpl_32_to_48_gm_-13_0.1_Zero-fill_64_17 _Saveframe_category NMR_applied_experiment _Experiment_name 'D2 N lpl 32 to 48 gm -13 0.1 Zero-fill 64' _Sample_label $sample_one save_ save_D3_H_gm_-13_0.1_zf_256_18 _Saveframe_category NMR_applied_experiment _Experiment_name 'D3 H gm -13 0.1 zf 256' _Sample_label $sample_one save_ save_200_ms_mix_time_19 _Saveframe_category NMR_applied_experiment _Experiment_name '200 ms mix time' _Sample_label $sample_one save_ save_t3_H_599.9094183MHz_146ms_200ms_7000Hz_No_1024_complex_._20 _Saveframe_category NMR_applied_experiment _Experiment_name 't3 H 599.9094183MHz 146ms 200ms 7000Hz No 1024 complex .' _Sample_label $sample_one save_ save_t2_H_599.9094183MHz_18ms_._7000Hz_No_128_complex_._21 _Saveframe_category NMR_applied_experiment _Experiment_name 't2 H 599.9094183MHz 18ms . 7000Hz No 128 complex .' _Sample_label $sample_one save_ save_t1_N_60.7951139MHz_21ms_._1540Hz_No_32_complex_._22 _Saveframe_category NMR_applied_experiment _Experiment_name 't1 N 60.7951139MHz 21ms . 1540Hz No 32 complex .' _Sample_label $sample_one save_ save_3D_[1H-15N]_NOESY-HSQC_23 _Saveframe_category NMR_applied_experiment _Experiment_name '3D [1H-15N] NOESY-HSQC' _Sample_label $sample_one save_ save_D1_H_gm_-5_0.1_Zero-fill_2048_24 _Saveframe_category NMR_applied_experiment _Experiment_name 'D1 H gm -5 0.1 Zero-fill 2048' _Sample_label $sample_one save_ save_D2_H_gm_-7_0.1_Zero-fill_256_25 _Saveframe_category NMR_applied_experiment _Experiment_name 'D2 H gm -7 0.1 Zero-fill 256' _Sample_label $sample_one save_ save_D3_N_lpl_32_to_48_gm_-15_0.1_Zero-fill_64_26 _Saveframe_category NMR_applied_experiment _Experiment_name 'D3 N lpl 32 to 48 gm -15 0.1 Zero-fill 64' _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.8 . na pressure 1 . atm temperature 284 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 DSS C 13 'methyl protons' ppm 0.000 . indirect . . . 0.251449530 $citation_one DSS H 1 'methyl protons' ppm 0.000 . direct . . . . $citation_one DSS N 15 'methyl protons' ppm 0.000 . indirect . . . 0.101329118 $citation_one 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_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details ; The first 30 residues of the LysS lysyl-tRNA synthetase are missing in LysN, and the construct contains an extra N-terminal Ala (Commans et al., 1995). For consistency with the numbering scheme for LysN of Commans et al (1995), an increment of 29 should be added to the sequence position counter (e.g the second residue in the LysN sequence corresponds to Glu 31, the last residue in the sequence corresponds to Ala149 of the LysS lysyl-tRNA synthetase). Could not distinguish between the spin systems of E60 and Q112, and between L136 and L146. The HA assigned to T45 and S84 could be due to only one of the spin systems. The HA assigned to T45 and S84 could be due to only one of the spin systems. The CB assigned to H44 and H50 could be due to only one of the spin systems. The HA and HB2 assigned to N65 and D103 could be due to only one of the spin systems. Estimates of the uncertainties in reported chemical shifts are: 1HN +/- 0.01 ppm 1Hx +/- 0.03 ppm 13C +/- 0.2 ppm 15N +/- 0.05 ppm ; loop_ _Sample_label $sample_one $sample_two stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name den-LysN _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 ALA HA H 4.14 0.03 1 2 . 1 ALA CA C 51.9 0.2 1 3 . 1 ALA CB C 19.6 0.2 1 4 . 2 GLU H H 8.78 0.01 1 5 . 2 GLU HA H 4.39 0.03 1 6 . 2 GLU HB2 H 2.04 0.03 2 7 . 2 GLU CA C 55.7 0.2 1 8 . 2 GLU CB C 29.1 0.2 1 9 . 2 GLU N N 120.28 0.05 1 10 . 3 GLN H H 8.7 0.01 1 11 . 3 GLN HA H 4.39 0.03 1 12 . 3 GLN CA C 55.7 0.2 1 13 . 3 GLN CB C 29.9 0.2 1 14 . 3 GLN N N 122.64 0.05 1 15 . 4 GLY H H 8.55 0.01 1 16 . 4 GLY HA2 H 4 0.03 2 17 . 4 GLY CA C 45.4 0.2 1 18 . 4 GLY N N 110.62 0.05 1 19 . 5 ILE H H 8.03 0.01 1 20 . 5 ILE HA H 4.15 0.03 1 21 . 5 ILE CA C 60.9 0.2 1 22 . 5 ILE CB C 39 0.2 1 23 . 5 ILE N N 120.08 0.05 1 24 . 6 ALA H H 8.35 0.01 1 25 . 6 ALA HA H 4.31 0.03 1 26 . 6 ALA HB H 1.26 0.03 1 27 . 6 ALA CA C 52.3 0.2 1 28 . 6 ALA CB C 19.6 0.2 1 29 . 6 ALA N N 128.12 0.05 1 30 . 7 PHE H H 8.28 0.01 1 31 . 7 PHE HA H 4.86 0.03 1 32 . 7 PHE HB2 H 2.9 0.03 2 33 . 7 PHE HB3 H 3.14 0.03 2 34 . 7 PHE CA C 55.7 0.2 1 35 . 7 PHE CB C 39 0.2 1 36 . 7 PHE N N 120.32 0.05 1 37 . 8 PRO HA H 4.37 0.03 1 38 . 8 PRO CA C 63.5 0.2 1 39 . 8 PRO CB C 32.1 0.2 1 40 . 9 ASN H H 8.59 0.01 1 41 . 9 ASN HA H 4.62 0.03 1 42 . 9 ASN HB2 H 2.75 0.03 2 43 . 9 ASN CA C 53.6 0.2 1 44 . 9 ASN CB C 38.5 0.2 1 45 . 9 ASN N N 118.53 0.05 1 46 . 10 ASP H H 8.37 0.01 1 47 . 10 ASP HA H 4.7 0.03 1 48 . 10 ASP HB2 H 2.82 0.03 2 49 . 10 ASP CA C 53.2 0.2 1 50 . 10 ASP CB C 38.1 0.2 1 51 . 10 ASP N N 119.09 0.05 1 52 . 11 PHE H H 8.16 0.01 1 53 . 11 PHE HA H 4.54 0.03 1 54 . 11 PHE HB2 H 3.14 0.03 2 55 . 11 PHE CB C 39.4 0.2 1 56 . 11 PHE N N 120.81 0.05 1 57 . 12 ARG H H 8.27 0.01 1 58 . 12 ARG HA H 4.25 0.03 1 59 . 12 ARG HB2 H 1.72 0.03 4 60 . 12 ARG HB3 H 1.55 0.03 4 61 . 12 ARG HG2 H 1.72 0.03 4 62 . 12 ARG HG3 H 1.55 0.03 4 63 . 12 ARG CA C 56.2 0.2 1 64 . 12 ARG CB C 30.8 0.2 1 65 . 12 ARG N N 122.56 0.05 1 66 . 13 ARG H H 8.33 0.01 1 67 . 13 ARG HA H 4.23 0.03 1 68 . 13 ARG HB2 H 1.81 0.03 4 69 . 13 ARG HB3 H 1.73 0.03 4 70 . 13 ARG HG2 H 1.81 0.03 4 71 . 13 ARG HG3 H 1.73 0.03 4 72 . 13 ARG HD2 H 3.29 0.03 2 73 . 13 ARG CA C 56.2 0.2 1 74 . 13 ARG CB C 30.8 0.2 1 75 . 13 ARG N N 121.91 0.05 1 76 . 14 ASP H H 8.49 0.01 1 77 . 14 ASP HA H 4.7 0.03 1 78 . 14 ASP HB2 H 2.82 0.03 2 79 . 14 ASP CA C 53.2 0.2 1 80 . 14 ASP CB C 38.1 0.2 1 81 . 14 ASP N N 119.8 0.05 1 82 . 15 HIS H H 8.58 0.01 1 83 . 15 HIS HA H 4.78 0.03 1 84 . 15 HIS HB2 H 3.21 0.03 2 85 . 15 HIS CA C 55.3 0.2 1 86 . 15 HIS CB C 29.1 0.2 5 87 . 15 HIS N N 119.12 0.05 1 88 . 16 THR H H 8.3 0.01 1 89 . 16 THR HA H 4.38 0.03 5 90 . 16 THR HG2 H 1.22 0.03 1 91 . 16 THR CA C 61.7 0.2 1 92 . 16 THR CB C 69.9 0.2 1 93 . 16 THR N N 115.62 0.05 1 94 . 17 SER H H 8.54 0.01 1 95 . 17 SER HA H 4.47 0.03 1 96 . 17 SER HB2 H 3.92 0.03 2 97 . 17 SER CA C 58.3 0.2 1 98 . 17 SER CB C 63.9 0.2 1 99 . 17 SER N N 117.97 0.05 1 100 . 18 ASP H H 8.61 0.01 1 101 . 18 ASP HA H 4.7 0.03 1 102 . 18 ASP HB2 H 2.9 0.03 2 103 . 18 ASP CA C 53.2 0.2 1 104 . 18 ASP CB C 38.1 0.2 1 105 . 18 ASP N N 121.49 0.05 1 106 . 19 GLN H H 8.39 0.01 1 107 . 19 GLN HA H 4.31 0.03 1 108 . 19 GLN HB2 H 2.04 0.03 2 109 . 19 GLN HG2 H 2.45 0.03 2 110 . 19 GLN CB C 29.5 0.2 1 111 . 19 GLN N N 120.79 0.05 1 112 . 20 LEU H H 8.27 0.01 1 113 . 20 LEU HA H 4.3 0.03 1 114 . 20 LEU HB2 H 1.55 0.03 4 115 . 20 LEU HB3 H 1.55 0.03 4 116 . 20 LEU HG H 1.55 0.03 4 117 . 20 LEU HD1 H 0.9 0.03 2 118 . 20 LEU CA C 55.7 0.2 1 119 . 20 LEU CB C 42.4 0.2 1 120 . 20 LEU N N 123.05 0.05 1 121 . 21 HIS H H 8.57 0.01 1 122 . 21 HIS HA H 4.7 0.03 1 123 . 21 HIS HB2 H 3.21 0.03 2 124 . 21 HIS CA C 55.3 0.2 1 125 . 21 HIS CB C 29.1 0.2 5 126 . 21 HIS N N 119.05 0.05 1 127 . 22 ALA H H 8.41 0.01 1 128 . 22 ALA HA H 4.31 0.03 1 129 . 22 ALA HB H 1.34 0.03 1 130 . 22 ALA CA C 52.7 0.2 1 131 . 22 ALA CB C 19.6 0.2 1 132 . 22 ALA N N 125.22 0.05 1 133 . 23 GLU H H 8.42 0.01 1 134 . 23 GLU HA H 4.31 0.03 1 135 . 23 GLU HB2 H 1.96 0.03 2 136 . 23 GLU CA C 55.7 0.2 1 137 . 23 GLU CB C 29.1 0.2 1 138 . 23 GLU N N 119.98 0.05 1 139 . 24 PHE H H 8.47 0.01 1 140 . 24 PHE HA H 4.7 0.03 1 141 . 24 PHE HB2 H 3.06 0.03 2 142 . 24 PHE CA C 57.9 0.2 1 143 . 24 PHE CB C 39.8 0.2 1 144 . 24 PHE N N 121.67 0.05 1 145 . 25 ASP H H 8.52 0.01 1 146 . 25 ASP HA H 4.7 0.03 1 147 . 25 ASP HB2 H 2.9 0.03 2 148 . 25 ASP CA C 52.7 0.2 1 149 . 25 ASP CB C 38.1 0.2 1 150 . 25 ASP N N 121.89 0.05 1 151 . 26 GLY H H 7.8 0.01 1 152 . 26 GLY HA2 H 3.92 0.03 2 153 . 26 GLY CA C 45.8 0.2 1 154 . 26 GLY N N 108.63 0.05 1 155 . 27 LYS H H 8.14 0.01 1 156 . 27 LYS HA H 4.31 0.03 1 157 . 27 LYS HB2 H 1.86 0.03 2 158 . 27 LYS HB3 H 1.63 0.03 2 159 . 27 LYS HG2 H 1.4 0.03 2 160 . 27 LYS CA C 56.6 0.2 1 161 . 27 LYS CB C 32.9 0.2 1 162 . 27 LYS N N 120.58 0.05 1 163 . 28 GLU H H 8.45 0.01 1 164 . 28 GLU HA H 4.31 0.03 1 165 . 28 GLU HB2 H 2.04 0.03 2 166 . 28 GLU HG2 H 2.45 0.03 2 167 . 28 GLU CA C 56.2 0.2 1 168 . 28 GLU CB C 28.6 0.2 1 169 . 28 GLU N N 121.02 0.05 1 170 . 29 ASN H H 8.55 0.01 1 171 . 29 ASN HA H 4.7 0.03 1 172 . 29 ASN HB2 H 2.82 0.03 2 173 . 29 ASN CA C 53.6 0.2 1 174 . 29 ASN CB C 38.5 0.2 1 175 . 29 ASN N N 119.88 0.05 1 176 . 30 GLU H H 8.44 0.01 1 177 . 30 GLU HA H 4.31 0.03 1 178 . 30 GLU HB2 H 2.04 0.03 2 179 . 30 GLU HG2 H 2.45 0.03 2 180 . 30 GLU CA C 56.6 0.2 1 181 . 30 GLU CB C 28.6 0.2 1 182 . 30 GLU N N 121.08 0.05 1 183 . 31 GLU H H 8.32 0.01 5 184 . 31 GLU HA H 4.15 0.03 5 185 . 31 GLU CA C 56.6 0.2 5 186 . 31 GLU CB C 28.6 0.2 5 187 . 31 GLU N N 120.36 0.05 5 188 . 32 LEU H H 8.21 0.01 1 189 . 32 LEU CA C 55.7 0.2 1 190 . 32 LEU CB C 42.4 0.2 1 191 . 32 LEU N N 122.46 0.05 1 192 . 33 GLU H H 8.29 0.01 1 193 . 33 GLU HA H 4.23 0.03 1 194 . 33 GLU HB2 H 2.04 0.03 2 195 . 33 GLU HG2 H 2.45 0.03 2 196 . 33 GLU CA C 56.2 0.2 1 197 . 33 GLU CB C 28.6 0.2 1 198 . 33 GLU N N 120.67 0.05 1 199 . 34 ALA H H 8.27 0.01 1 200 . 34 ALA HA H 4.23 0.03 1 201 . 34 ALA HB H 1.42 0.03 1 202 . 34 ALA CA C 52.7 0.2 1 203 . 34 ALA CB C 19.2 0.2 1 204 . 34 ALA N N 124.61 0.05 1 205 . 35 LEU H H 8.16 0.01 1 206 . 35 LEU CA C 55.3 0.2 1 207 . 35 LEU CB C 42.4 0.2 1 208 . 35 LEU N N 120.81 0.05 1 209 . 36 ASN H H 8.44 0.01 1 210 . 36 ASN HA H 4.7 0.03 5 211 . 36 ASN HB2 H 2.82 0.03 5 212 . 36 ASN CA C 53.2 0.2 1 213 . 36 ASN CB C 38.5 0.2 1 214 . 36 ASN N N 119.41 0.05 1 215 . 37 ILE H H 8.09 0.01 1 216 . 37 ILE HA H 4.15 0.03 1 217 . 37 ILE HB H 1.9 0.03 1 218 . 37 ILE HG12 H 1.45 0.03 2 219 . 37 ILE HG13 H 1.18 0.03 2 220 . 37 ILE CA C 61.3 0.2 1 221 . 37 ILE CB C 39.2 0.2 1 222 . 37 ILE N N 120.86 0.05 1 223 . 39 VAL H H 8.25 0.01 1 224 . 39 VAL HA H 4.08 0.03 1 225 . 39 VAL HB H 2.04 0.03 1 226 . 39 VAL HG1 H 0.95 0.03 2 227 . 39 VAL CA C 62.2 0.2 1 228 . 39 VAL CB C 32.9 0.2 1 229 . 39 VAL N N 121.82 0.05 1 230 . 40 ALA H H 8.4 0.01 1 231 . 40 ALA HA H 4.39 0.03 1 232 . 40 ALA HB H 1.37 0.03 1 233 . 40 ALA CA C 52.3 0.2 1 234 . 40 ALA CB C 19.6 0.2 1 235 . 40 ALA N N 127.82 0.05 1 236 . 41 VAL H H 8.24 0.01 1 237 . 41 VAL HA H 4.08 0.03 1 238 . 41 VAL HB H 2.04 0.03 1 239 . 41 VAL HG1 H 0.95 0.03 2 240 . 41 VAL CA C 62.6 0.2 1 241 . 41 VAL CB C 32.9 0.2 1 242 . 41 VAL N N 120.28 0.05 1 243 . 42 ALA H H 8.49 0.01 1 244 . 42 ALA HA H 4.31 0.03 1 245 . 42 ALA HB H 1.42 0.03 1 246 . 42 ALA CA C 52.7 0.2 1 247 . 42 ALA CB C 19.2 0.2 1 248 . 42 ALA N N 127.9 0.05 1 249 . 43 GLY H H 8.42 0.01 1 250 . 43 GLY HA2 H 4 0.03 2 251 . 43 GLY CA C 45.4 0.2 1 252 . 43 GLY N N 108.04 0.05 1 253 . 44 ARG H H 8.2 0.01 1 254 . 44 ARG HB2 H 1.8 0.03 4 255 . 44 ARG HB3 H 1.8 0.03 4 256 . 44 ARG HG2 H 1.8 0.03 4 257 . 44 ARG HG3 H 1.8 0.03 4 258 . 44 ARG CB C 31.2 0.2 1 259 . 44 ARG N N 120.59 0.05 1 260 . 45 MET H H 8.55 0.01 1 261 . 45 MET HA H 4.54 0.03 1 262 . 45 MET HB2 H 2.04 0.03 2 263 . 45 MET CA C 55.7 0.2 1 264 . 45 MET CB C 32.9 0.2 1 265 . 45 MET N N 121.8 0.05 1 266 . 46 MET H H 8.59 0.01 1 267 . 46 MET HA H 4.62 0.03 1 268 . 46 MET HB2 H 2.09 0.03 2 269 . 46 MET CA C 55.3 0.2 1 270 . 46 MET CB C 32.9 0.2 1 271 . 46 MET N N 122.64 0.05 1 272 . 47 THR H H 8.28 0.01 1 273 . 47 THR HG2 H 1.22 0.03 1 274 . 47 THR CA C 61.7 0.2 1 275 . 47 THR CB C 69.9 0.2 1 276 . 47 THR N N 116.3 0.05 1 277 . 48 ARG H H 8.49 0.01 1 278 . 48 ARG HA H 4.39 0.03 1 279 . 48 ARG HB2 H 1.81 0.03 4 280 . 48 ARG HB3 H 1.81 0.03 4 281 . 48 ARG HG2 H 1.81 0.03 4 282 . 48 ARG HG3 H 1.81 0.03 4 283 . 48 ARG CA C 56.2 0.2 1 284 . 48 ARG CB C 31.2 0.2 1 285 . 48 ARG N N 124.1 0.05 1 286 . 49 ARG H H 8.55 0.01 1 287 . 49 ARG HA H 4.39 0.03 1 288 . 49 ARG CA C 56.2 0.2 1 289 . 49 ARG CB C 31.2 0.2 1 290 . 49 ARG N N 123.75 0.05 1 291 . 50 ILE H H 8.47 0.01 1 292 . 50 ILE HA H 4.15 0.03 1 293 . 50 ILE CA C 60.9 0.2 1 294 . 50 ILE CB C 38.5 0.2 1 295 . 50 ILE N N 123.65 0.05 1 296 . 51 MET H H 8.65 0.01 1 297 . 51 MET HA H 4.55 0.03 1 298 . 51 MET HB2 H 2.04 0.03 2 299 . 51 MET CA C 55.3 0.2 1 300 . 51 MET CB C 32.9 0.2 1 301 . 51 MET N N 125.78 0.05 1 302 . 52 GLY H H 8.47 0.01 1 303 . 52 GLY HA2 H 4 0.03 2 304 . 52 GLY CA C 45.4 0.2 1 305 . 52 GLY N N 110.39 0.05 1 306 . 53 LYS H H 8.33 0.01 1 307 . 53 LYS HA H 4.31 0.03 1 308 . 53 LYS CA C 56.2 0.2 1 309 . 53 LYS CB C 33.4 0.2 1 310 . 53 LYS N N 121.2 0.05 1 311 . 54 ALA H H 8.51 0.01 1 312 . 54 ALA HA H 4.31 0.03 1 313 . 54 ALA HB H 1.34 0.03 1 314 . 54 ALA CA C 52.7 0.2 1 315 . 54 ALA CB C 19.6 0.2 1 316 . 54 ALA N N 125.76 0.05 1 317 . 55 SER H H 8.32 0.01 1 318 . 55 SER HA H 4.39 0.03 5 319 . 55 SER HB2 H 3.84 0.03 2 320 . 55 SER CA C 58.3 0.2 1 321 . 55 SER CB C 63.9 0.2 1 322 . 55 SER N N 115.44 0.05 1 323 . 56 PHE H H 8.3 0.01 1 324 . 56 PHE HA H 4.7 0.03 1 325 . 56 PHE HB2 H 3.06 0.03 2 326 . 56 PHE CA C 57.9 0.2 1 327 . 56 PHE CB C 39.8 0.2 1 328 . 56 PHE N N 122.24 0.05 1 329 . 57 VAL H H 8.19 0.01 1 330 . 57 VAL HB H 1.99 0.03 1 331 . 57 VAL HG1 H 0.9 0.03 2 332 . 57 VAL CA C 62.2 0.2 1 333 . 57 VAL CB C 33.4 0.2 1 334 . 57 VAL N N 122.26 0.05 1 335 . 58 THR H H 8.3 0.01 1 336 . 58 THR HA H 4.39 0.03 1 337 . 58 THR CA C 61.7 0.2 1 338 . 58 THR CB C 69.9 0.2 1 339 . 58 THR N N 119 0.05 1 340 . 59 LEU H H 8.43 0.01 1 341 . 59 LEU HA H 4.39 0.03 1 342 . 59 LEU HB2 H 1.65 0.03 4 343 . 59 LEU HB3 H 1.65 0.03 4 344 . 59 LEU HG H 1.65 0.03 4 345 . 59 LEU CA C 55.4 0.2 1 346 . 59 LEU CB C 42.4 0.2 1 347 . 59 LEU N N 125.23 0.05 1 348 . 60 GLN H H 8.5 0.01 1 349 . 60 GLN HA H 4.31 0.03 1 350 . 60 GLN HB2 H 1.96 0.03 2 351 . 60 GLN CA C 55.7 0.2 1 352 . 60 GLN CB C 29.9 0.2 1 353 . 60 GLN N N 120.84 0.05 1 354 . 61 ASP H H 8.59 0.01 1 355 . 61 ASP HA H 4.78 0.03 1 356 . 61 ASP HB2 H 2.81 0.03 2 357 . 61 ASP HB3 H 2.9 0.03 2 358 . 61 ASP CA C 52.7 0.2 1 359 . 61 ASP CB C 38.1 0.2 1 360 . 61 ASP N N 120.45 0.05 1 361 . 62 VAL H H 8.25 0.01 1 362 . 62 VAL HA H 4.15 0.03 1 363 . 62 VAL HB H 2.12 0.03 1 364 . 62 VAL HG1 H 0.93 0.03 2 365 . 62 VAL CA C 62.6 0.2 1 366 . 62 VAL CB C 32.9 0.2 1 367 . 62 VAL N N 120.9 0.05 1 368 . 63 GLY H H 8.6 0.01 1 369 . 63 GLY HA2 H 4 0.03 2 370 . 63 GLY CA C 45.4 0.2 1 371 . 63 GLY N N 112.63 0.05 1 372 . 64 GLY H H 8.26 0.01 1 373 . 64 GLY HA2 H 4 0.03 2 374 . 64 GLY CA C 45.4 0.2 1 375 . 64 GLY N N 108.3 0.05 1 376 . 65 ARG H H 8.28 0.01 1 377 . 65 ARG HA H 4.23 0.03 1 378 . 65 ARG HB2 H 1.88 0.03 4 379 . 65 ARG HB3 H 1.88 0.03 4 380 . 65 ARG HG2 H 1.88 0.03 4 381 . 65 ARG HG3 H 1.88 0.03 4 382 . 65 ARG CA C 55.7 0.2 1 383 . 65 ARG CB C 31.2 0.2 1 384 . 65 ARG N N 120.99 0.05 1 385 . 66 ILE H H 8.36 0.01 1 386 . 66 ILE HA H 4.15 0.03 1 387 . 66 ILE HB H 1.9 0.03 1 388 . 66 ILE CA C 60.9 0.2 1 389 . 66 ILE CB C 38.5 0.2 1 390 . 66 ILE N N 123.15 0.05 1 391 . 67 GLN H H 8.59 0.01 1 392 . 67 GLN HA H 4.39 0.03 1 393 . 67 GLN HB2 H 2 0.03 2 394 . 67 GLN CA C 55.3 0.2 1 395 . 67 GLN CB C 29.9 0.2 1 396 . 67 GLN N N 125.62 0.05 1 397 . 68 LEU H H 8.38 0.01 1 398 . 68 LEU HA H 4.31 0.03 1 399 . 68 LEU HB2 H 1.49 0.03 4 400 . 68 LEU HB3 H 1.49 0.03 4 401 . 68 LEU HG H 1.49 0.03 4 402 . 68 LEU HD1 H 0.86 0.03 2 403 . 68 LEU CA C 55.3 0.2 1 404 . 68 LEU CB C 42.4 0.2 1 405 . 68 LEU N N 124.6 0.05 1 406 . 69 TYR H H 8.41 0.01 1 407 . 69 TYR HA H 4.61 0.03 1 408 . 69 TYR HB2 H 2.9 0.03 2 409 . 69 TYR CA C 57.9 0.2 1 410 . 69 TYR CB C 39 0.2 1 411 . 69 TYR N N 121.96 0.05 1 412 . 70 VAL H H 8.04 0.01 1 413 . 70 VAL HA H 4 0.03 1 414 . 70 VAL HB H 1.88 0.03 1 415 . 70 VAL HG1 H 0.86 0.03 2 416 . 70 VAL CA C 61.7 0.2 1 417 . 70 VAL CB C 33.4 0.2 1 418 . 70 VAL N N 124.31 0.05 1 419 . 71 ALA H H 8.38 0.01 1 420 . 71 ALA HA H 4.23 0.03 1 421 . 71 ALA HB H 1.41 0.03 1 422 . 71 ALA CA C 52.3 0.2 1 423 . 71 ALA CB C 19.2 0.2 1 424 . 71 ALA N N 128.51 0.05 1 425 . 72 ARG H H 8.41 0.01 1 426 . 72 ARG HA H 4.32 0.03 1 427 . 72 ARG CA C 56.6 0.2 1 428 . 72 ARG CB C 30.8 0.2 1 429 . 72 ARG N N 120.69 0.05 1 430 . 73 ASP H H 8.53 0.01 1 431 . 73 ASP HA H 4.7 0.03 1 432 . 73 ASP HB2 H 2.9 0.03 2 433 . 73 ASP CA C 52.7 0.2 1 434 . 73 ASP CB C 38.1 0.2 1 435 . 73 ASP N N 119.35 0.05 1 436 . 74 ASP H H 8.43 0.01 1 437 . 74 ASP HA H 4.7 0.03 5 438 . 74 ASP HB2 H 2.82 0.03 5 439 . 74 ASP CB C 38.1 0.2 1 440 . 74 ASP N N 119.42 0.05 1 441 . 75 LEU H H 8.1 0.01 1 442 . 75 LEU HA H 4.62 0.03 1 443 . 75 LEU HB2 H 1.63 0.03 2 444 . 75 LEU HD1 H 0.9 0.03 2 445 . 75 LEU CA C 53.2 0.2 1 446 . 75 LEU CB C 42 0.2 1 447 . 75 LEU N N 123.19 0.05 1 448 . 76 PRO CA C 63 0.2 1 449 . 76 PRO CB C 32.1 0.2 1 450 . 77 GLU H H 8.55 0.01 1 451 . 77 GLU HA H 4.31 0.03 1 452 . 77 GLU HB2 H 2.04 0.03 2 453 . 77 GLU CA C 56.2 0.2 1 454 . 77 GLU CB C 29.1 0.2 1 455 . 77 GLU N N 120.84 0.05 1 456 . 78 GLY H H 8.51 0.01 1 457 . 78 GLY HA2 H 3.99 0.03 2 458 . 78 GLY CA C 45.4 0.2 1 459 . 78 GLY N N 110.04 0.05 1 460 . 79 VAL H H 7.91 0.01 1 461 . 79 VAL HA H 4.08 0.03 1 462 . 79 VAL HB H 2 0.03 1 463 . 79 VAL HG1 H 0.86 0.03 2 464 . 79 VAL CA C 62.6 0.2 1 465 . 79 VAL CB C 32.9 0.2 1 466 . 79 VAL N N 119.28 0.05 1 467 . 80 TYR H H 8.39 0.01 1 468 . 80 TYR CA C 57.9 0.2 1 469 . 80 TYR CB C 39 0.2 1 470 . 80 TYR N N 124.03 0.05 1 471 . 81 ASN CB C 39 0.2 1 472 . 82 GLU H H 8.42 0.01 1 473 . 82 GLU HA H 4.47 0.03 1 474 . 82 GLU CB C 28.6 0.2 1 475 . 82 GLU N N 124.01 0.05 1 476 . 83 GLN H H 8.48 0.01 5 477 . 83 GLN HA H 4.39 0.03 5 478 . 83 GLN CA C 56.2 0.2 5 479 . 83 GLN CB C 29.1 0.2 5 480 . 83 GLN N N 121.57 0.05 5 481 . 84 PHE H H 8.12 0.01 1 482 . 84 PHE HA H 4.55 0.03 1 483 . 84 PHE HB2 H 2.9 0.03 2 484 . 84 PHE HB3 H 3.14 0.03 2 485 . 84 PHE CA C 57.9 0.2 1 486 . 84 PHE CB C 39.4 0.2 1 487 . 84 PHE N N 120.29 0.05 1 488 . 85 LYS H H 8.15 0.01 1 489 . 85 LYS HA H 4.15 0.03 1 490 . 85 LYS CA C 56.2 0.2 1 491 . 85 LYS CB C 32.9 0.2 1 492 . 85 LYS N N 122.66 0.05 1 493 . 86 LYS H H 8.18 0.01 1 494 . 86 LYS HA H 4.15 0.03 1 495 . 86 LYS HB2 H 1.96 0.03 2 496 . 86 LYS HE2 H 3.45 0.03 2 497 . 86 LYS CA C 56.6 0.2 1 498 . 86 LYS CB C 33.4 0.2 1 499 . 86 LYS N N 121.95 0.05 1 500 . 87 TRP H H 8.26 0.01 1 501 . 87 TRP HA H 4.7 0.03 1 502 . 87 TRP HB2 H 3.22 0.03 2 503 . 87 TRP CA C 57 0.2 1 504 . 87 TRP CB C 29.9 0.2 1 505 . 87 TRP N N 122.06 0.05 1 506 . 88 ASP H H 8.37 0.01 1 507 . 88 ASP HA H 4.7 0.03 1 508 . 88 ASP HB2 H 2.75 0.03 2 509 . 88 ASP N N 120.88 0.05 1 510 . 89 LEU H H 8.13 0.01 1 511 . 89 LEU HA H 4.23 0.03 1 512 . 89 LEU HB2 H 1.59 0.03 4 513 . 89 LEU HB3 H 1.59 0.03 4 514 . 89 LEU HG H 1.59 0.03 4 515 . 89 LEU HD1 H 0.9 0.03 2 516 . 89 LEU CA C 55.7 0.2 1 517 . 89 LEU CB C 42 0.2 1 518 . 89 LEU N N 122.4 0.05 1 519 . 90 GLY H H 8.35 0.01 1 520 . 90 GLY HA2 H 3.92 0.03 2 521 . 90 GLY CA C 45.4 0.2 1 522 . 90 GLY N N 108.37 0.05 1 523 . 91 ASP H H 8.23 0.01 1 524 . 91 ASP HA H 4.7 0.03 1 525 . 91 ASP HB2 H 2.82 0.03 2 526 . 91 ASP CA C 53.2 0.2 1 527 . 91 ASP CB C 38.1 0.2 1 528 . 91 ASP N N 118.81 0.05 1 529 . 92 ILE H H 8.16 0.01 1 530 . 92 ILE HA H 4.15 0.03 1 531 . 92 ILE HB H 1.88 0.03 1 532 . 92 ILE CA C 61.3 0.2 1 533 . 92 ILE CB C 38.5 0.2 1 534 . 92 ILE N N 121.56 0.05 1 535 . 93 LEU H H 8.39 0.01 1 536 . 93 LEU HA H 4.31 0.03 1 537 . 93 LEU HB2 H 1.65 0.03 4 538 . 93 LEU HB3 H 1.65 0.03 4 539 . 93 LEU HG H 1.65 0.03 4 540 . 93 LEU HD1 H 0.86 0.03 2 541 . 93 LEU CA C 55.3 0.2 1 542 . 93 LEU CB C 42.4 0.2 1 543 . 93 LEU N N 125.74 0.05 1 544 . 94 GLY H H 8.36 0.01 1 545 . 94 GLY HA2 H 3.92 0.03 2 546 . 94 GLY CA C 45.4 0.2 1 547 . 94 GLY N N 109.64 0.05 1 548 . 95 ALA H H 8.21 0.01 1 549 . 95 ALA HA H 4.31 0.03 1 550 . 95 ALA HB H 1.4 0.03 1 551 . 95 ALA CA C 52.7 0.2 1 552 . 95 ALA CB C 19.6 0.2 1 553 . 95 ALA N N 123.8 0.05 1 554 . 96 LYS H H 8.45 0.01 1 555 . 96 LYS HA H 4.31 0.03 1 556 . 96 LYS HB2 H 1.81 0.03 2 557 . 96 LYS HG2 H 1.4 0.03 2 558 . 96 LYS CA C 56.6 0.2 1 559 . 96 LYS CB C 32.9 0.2 1 560 . 96 LYS N N 120.4 0.05 1 561 . 97 GLY H H 8.39 0.01 1 562 . 97 GLY HA2 H 3.92 0.03 2 563 . 97 GLY CA C 45.4 0.2 1 564 . 97 GLY N N 109.64 0.05 1 565 . 98 LYS H H 8.2 0.01 1 566 . 98 LYS HA H 4.28 0.03 1 567 . 98 LYS CA C 56.2 0.2 1 568 . 98 LYS CB C 33.4 0.2 1 569 . 98 LYS N N 120.88 0.05 1 570 . 99 LEU H H 8.3 0.01 1 571 . 99 LEU HA H 4.39 0.03 1 572 . 99 LEU HB2 H 1.57 0.03 4 573 . 99 LEU HB3 H 1.57 0.03 4 574 . 99 LEU HG H 1.57 0.03 4 575 . 99 LEU CA C 54.9 0.2 1 576 . 99 LEU CB C 42.4 0.2 1 577 . 99 LEU N N 123.23 0.05 1 578 . 100 PHE H H 8.4 0.01 1 579 . 100 PHE HA H 4.62 0.03 1 580 . 100 PHE HB2 H 2.98 0.03 2 581 . 100 PHE CA C 57.4 0.2 1 582 . 100 PHE CB C 39.8 0.2 1 583 . 100 PHE N N 121.96 0.05 1 584 . 101 LYS H H 8.4 0.01 1 585 . 101 LYS HA H 4.39 0.03 1 586 . 101 LYS HB2 H 1.73 0.03 2 587 . 101 LYS CA C 56.2 0.2 1 588 . 101 LYS CB C 33.4 0.2 1 589 . 101 LYS N N 123.81 0.05 1 590 . 102 THR H H 8.29 0.01 1 591 . 102 THR HG2 H 1.22 0.03 1 592 . 102 THR CA C 61.7 0.2 1 593 . 102 THR CB C 69.9 0.2 1 594 . 102 THR N N 116.39 0.05 1 595 . 103 LYS H H 8.6 0.01 1 596 . 103 LYS HA H 4.39 0.03 1 597 . 103 LYS HB2 H 1.81 0.03 2 598 . 103 LYS CA C 56.6 0.2 1 599 . 103 LYS CB C 33.4 0.2 1 600 . 103 LYS N N 124.02 0.05 1 601 . 104 THR H H 8.28 0.01 1 602 . 104 THR HA H 4.31 0.03 1 603 . 104 THR HG2 H 1.22 0.03 1 604 . 104 THR CA C 62.2 0.2 1 605 . 104 THR CB C 69.9 0.2 1 606 . 104 THR N N 115.21 0.05 1 607 . 105 GLY H H 8.49 0.01 1 608 . 105 GLY HA2 H 4 0.03 2 609 . 105 GLY CA C 45.4 0.2 1 610 . 105 GLY N N 111.21 0.05 1 611 . 106 GLU H H 8.27 0.01 1 612 . 106 GLU HA H 4.39 0.03 1 613 . 106 GLU HB2 H 2.04 0.03 2 614 . 106 GLU HG2 H 2.45 0.03 2 615 . 106 GLU CA C 55.7 0.2 1 616 . 106 GLU CB C 29.1 0.2 1 617 . 106 GLU N N 119.91 0.05 1 618 . 107 LEU H H 8.45 0.01 5 619 . 107 LEU HA H 4.31 0.03 5 620 . 107 LEU HB2 H 1.57 0.03 5 621 . 107 LEU HB3 H 1.57 0.03 5 622 . 107 LEU HG H 1.57 0.03 5 623 . 107 LEU CA C 55.3 0.2 5 624 . 107 LEU CB C 42.4 0.2 5 625 . 107 LEU N N 123.81 0.05 5 626 . 108 SER H H 8.43 0.01 1 627 . 108 SER HA H 4.47 0.03 1 628 . 108 SER HB2 H 3.84 0.03 2 629 . 108 SER CA C 57.9 0.2 1 630 . 108 SER CB C 63.9 0.2 1 631 . 108 SER N N 117.18 0.05 1 632 . 109 ILE H H 8.21 0.01 1 633 . 109 ILE HA H 4.18 0.03 1 634 . 109 ILE CA C 61.3 0.2 1 635 . 109 ILE CB C 39 0.2 1 636 . 109 ILE N N 122.46 0.05 1 637 . 110 HIS H H 8.68 0.01 1 638 . 110 HIS HA H 4.78 0.03 1 639 . 110 HIS HB2 H 3.22 0.03 2 640 . 110 HIS CA C 55.3 0.2 1 641 . 110 HIS CB C 29.1 0.2 1 642 . 110 HIS N N 122.43 0.05 1 643 . 111 CYS H H 8.53 0.01 1 644 . 111 CYS HA H 4.68 0.03 1 645 . 111 CYS HB2 H 2.95 0.03 2 646 . 111 CYS CA C 58.7 0.2 1 647 . 111 CYS CB C 28.2 0.2 1 648 . 111 CYS N N 121.73 0.05 1 649 . 112 THR H H 8.51 0.01 1 650 . 112 THR HA H 4.31 0.03 1 651 . 112 THR CA C 62.2 0.2 1 652 . 112 THR CB C 69.5 0.2 1 653 . 112 THR N N 117.75 0.05 1 654 . 113 GLU H H 8.42 0.01 1 655 . 113 GLU HA H 4.39 0.03 1 656 . 113 GLU HB2 H 2.04 0.03 2 657 . 113 GLU CA C 55.7 0.2 1 658 . 113 GLU CB C 29.1 0.2 1 659 . 113 GLU N N 123.24 0.05 1 660 . 114 LEU H H 8.39 0.01 5 661 . 114 LEU HA H 4.31 0.03 5 662 . 114 LEU HB2 H 1.57 0.03 5 663 . 114 LEU HB3 H 1.57 0.03 5 664 . 114 LEU HG H 1.57 0.03 5 665 . 114 LEU CA C 55.3 0.2 5 666 . 114 LEU CB C 42.4 0.2 5 667 . 114 LEU N N 124.3 0.05 5 668 . 115 ARG H H 8.48 0.01 1 669 . 115 ARG HA H 4.31 0.03 1 670 . 115 ARG HB2 H 1.81 0.03 1 671 . 115 ARG HB3 H 1.81 0.03 1 672 . 115 ARG CA C 55.7 0.2 1 673 . 115 ARG CB C 30.8 0.2 1 674 . 115 ARG N N 122.67 0.05 1 675 . 116 LEU H H 8.37 0.01 1 676 . 116 LEU HA H 4.39 0.03 1 677 . 116 LEU HB2 H 1.65 0.03 4 678 . 116 LEU HB3 H 1.65 0.03 4 679 . 116 LEU HG H 1.65 0.03 4 680 . 116 LEU CA C 54.9 0.2 1 681 . 116 LEU CB C 42.4 0.2 1 682 . 116 LEU N N 124.01 0.05 1 683 . 117 LEU H H 8.45 0.01 1 684 . 117 LEU HB2 H 1.63 0.03 4 685 . 117 LEU HB3 H 1.63 0.03 4 686 . 117 LEU HG H 1.63 0.03 4 687 . 117 LEU CA C 54.9 0.2 1 688 . 117 LEU CB C 42.4 0.2 1 689 . 117 LEU N N 123.81 0.05 1 690 . 118 THR H H 8.18 0.01 1 691 . 118 THR HA H 4.31 0.03 1 692 . 118 THR CA C 61.7 0.2 1 693 . 118 THR CB C 69.9 0.2 1 694 . 118 THR N N 115.74 0.05 1 695 . 119 LYS H H 8.45 0.01 1 696 . 119 LYS HA H 4.31 0.03 1 697 . 119 LYS HB2 H 1.81 0.03 2 698 . 119 LYS CA C 56.2 0.2 1 699 . 119 LYS CB C 33.4 0.2 1 700 . 119 LYS N N 124.3 0.05 1 701 . 120 ALA H H 8.54 0.01 1 702 . 120 ALA HA H 4.31 0.03 1 703 . 120 ALA HB H 1.42 0.03 1 704 . 120 ALA CA C 51.9 0.2 1 705 . 120 ALA CB C 19.2 0.2 1 706 . 120 ALA N N 127.72 0.05 1 stop_ save_