data_4134 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Assignments for Denatured LysN ; 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_ _BMRB_accession_number 4134 _BMRB_flat_file_name bmr4134.str _Entry_type new _Submission_date 1998-04-16 _Accession_date 1998-04-16 _Entry_origination author _NMR_STAR_version 2.1 _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_ _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 _MEDLINE_UI_code ? 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 ? _Page_first ? _Page_last ? _Year 1999 loop_ _Keyword 'lysyl-tRNA synthetase' 'protein folding' OB-fold 'denatured state' stop_ 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_type simple _System_paramagnetic no loop_ _Biological_function 'LysN is the N-terminal anticodon binding domain of the lysyl-tRNA synthetase' stop_ _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 _Name_variant . _Abbreviation_common den-LysN loop_ _Biological_function 'LysN is the N-terminal anticodon binding domain of the lysyl-tRNA synthetase' stop_ ############################## # 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 2008-09-24 _Sequence_homology_query_revised_last_date 2008-09-24 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 1.73e-64 PDB 1BBW "Lysyl-Trna Synthetase (Lyss)" 99.17 504 100.00 100.00 1.73e-64 PDB 1KRS "Solution Structure Of The Anticodon Binding Domain Of Escherichia Coli Lysyl-Trna Synthetase And Studies Of Its Interactions With Trna-Lys" 100.00 120 100.00 100.00 1.71e-64 PDB 1KRT "Solution Structure Of The Anticodon Binding Domain Of Escherichia Coli Lysyl-Trna Synthetase And Studies Of Its Interactions With Trna-Lys" 100.00 120 100.00 100.00 1.71e-64 DBJ BAB37185 "lysine tRNA synthetase [Escherichia coli O157:H7 str. Sakai]" 99.17 505 100.00 100.00 1.76e-64 DBJ BAE76955 "lysine tRNA synthetase, constitutive [Escherichia coli W3110]" 99.17 505 100.00 100.00 1.67e-64 GenBank AAA23959 "herC protein" 99.17 505 100.00 100.00 1.67e-64 GenBank AAA83071 "lysyl tRNA synthetase (LysRS), constitutive" 99.17 505 100.00 100.00 1.67e-64 GenBank AAC75928 "lysine tRNA synthetase, constitutive [Escherichia coli str. K-12 substr. MG1655]" 99.17 505 100.00 100.00 1.67e-64 GenBank AAG58018 "lysine tRNA synthetase, constitutive; suppressor of ColE1 mutation in primer RNA [Escherichia coli O157:H7 EDL933]" 99.17 505 100.00 100.00 1.76e-64 GenBank AAN44362 "lysine tRNA synthetase [Shigella flexneri 2a str. 301]" 99.17 505 100.00 100.00 1.85e-64 REF AP_003449 "lysine tRNA synthetase, constitutive [Escherichia coli W3110]" 99.17 505 100.00 100.00 1.67e-64 REF NP_289459 "lysyl-tRNA synthetase [Escherichia coli O157:H7 EDL933]" 99.17 505 100.00 100.00 1.76e-64 REF NP_311789 "lysyl-tRNA synthetase [Escherichia coli O157:H7 str. Sakai]" 99.17 505 100.00 100.00 1.76e-64 REF NP_417366 "lysine tRNA synthetase, constitutive [Escherichia coli str. K-12 substr. MG1655]" 99.17 505 100.00 100.00 1.67e-64 REF NP_708655 "lysyl-tRNA synthetase [Shigella flexneri 2a str. 301]" 99.17 505 100.00 100.00 1.85e-64 SWISS-PROT P0A8N3 "Lysyl-tRNA synthetase (Lysine--tRNA ligase) (LysRS)" 99.17 505 100.00 100.00 1.67e-64 SWISS-PROT P0A8N4 "Lysyl-tRNA synthetase (Lysine--tRNA ligase) (LysRS)" 99.17 505 100.00 100.00 1.67e-64 SWISS-PROT Q0T106 "Lysyl-tRNA synthetase (Lysine--tRNA ligase) (LysRS)" 99.17 505 100.00 100.00 1.85e-64 SWISS-PROT Q31WF2 "Lysyl-tRNA synthetase (Lysine--tRNA ligase) (LysRS)" 99.17 505 99.16 99.16 5.25e-64 SWISS-PROT Q32BV3 "Lysyl-tRNA synthetase (Lysine--tRNA ligase) (LysRS)" 99.17 505 99.16 99.16 5.61e-64 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 _Vector_type _Vector_name _Vendor_name _Gene_source _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 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 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_sample_mol_purity_one _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 stop_ save_ save_sample_mol_purity_two _Saveframe_category sample_mol_purity _Sample_label $sample_two loop_ _Mol_label _Mol_purity_value _Mol_purity_value_units _Mol_purity_measurement_method $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 _Software_version_number 1.2 save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity plus' _Field_strength 600 _Software_version_number 4.2 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment_one _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_two _Details ; NMR spectral acquisition parameters t3 H 599.9094119 146ms . 7000Hz No 1024 complex . t2 C 150.8529083 7.7ms . 8300Hz No 64 complex . t1 N 60.7952139 21ms . 1540Hz No 32 complex . NMR spectral processing parameters D1 H sine-bell 1024 90 Zero-fill 2048 D2 C squared-sine-bell 64 70 Zero-fill 128 D3 N linear predict 32 to 48 squaredsine-bell 48 70 Zero-fill 64 ; save_ save_NMR_applied_experiment_two _Saveframe_category NMR_applied_experiment _Experiment_name '3D[1H-15N]TOCSY-HSQC' _Sample_label $sample_one _Details ; 46 ms mix time NMR spectral acquisition parameters t3 H 600.1328206MHz 85ms 46ms 6009.615Hz No 512 complex . t2 N 60.8178387MHz 21ms . 1521Hz No 32 complex . t1 H 600.1328206MHz 21ms . 6009.615Hz No 128 complex . NMR spectral processing parameters 3D [1H-15N] TOCSY-HSQC D1 H gm -10 0.1 Zero-fill 1024 D2 N lpl 32 to 48 gm -13 0.1 Zero-fill 64 D3 H gm -13 0.1 zf 256 ; save_ save_NMR_applied_experiment_three _Saveframe_category NMR_applied_experiment _Experiment_name '3D[1H-15N]NOESY-HSQC' _Sample_label $sample_one _Details ; 200 ms mix time NMR spectral acquisition parameters t3 H 599.9094183MHz 146ms 200ms 7000Hz No 1024 complex . t2 H 599.9094183MHz 18ms . 7000Hz No 128 complex . t1 N 60.7951139MHz 21ms . 1540Hz No 32 complex . NMR spectral processing parameters 3D [1H-15N] NOESY-HSQC D1 H gm -5 0.1 Zero-fill 2048 D2 H gm -7 0.1 Zero-fill 256 D3 N lpl 32 to 48 gm -15 0.1 Zero-fill 64 ; save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.8 . na temperature 284 . K pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _Indirect_shift_ratio _Indirect_shift_ratio_citation_label DSS H 1 'methyl protons' ppm 0.000 direct . . $citation_one DSS C 13 'methyl protons' ppm 0.000 indirect . 0.251449530 $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 # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 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) # # 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 loop_ _Atom_shift_assign_ID _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_ save_ambiguous_atom_definitions _Saveframe_category ambiguous_chemical_shift_definitions loop_ _Chemical_shift_ambiguity_ID _Mol_system_component_name _Assigned_chemical_shift_label _Atom_shift_assign_ID 1 den-LysN $assigned_chemical_shifts_one 59 1 den-LysN $assigned_chemical_shifts_one 60 1 den-LysN $assigned_chemical_shifts_one 61 1 den-LysN $assigned_chemical_shifts_one 62 2 den-LysN $assigned_chemical_shifts_one 68 2 den-LysN $assigned_chemical_shifts_one 69 2 den-LysN $assigned_chemical_shifts_one 70 2 den-LysN $assigned_chemical_shifts_one 71 3 den-LysN $assigned_chemical_shifts_one 86 3 den-LysN $assigned_chemical_shifts_one 125 4 den-LysN $assigned_chemical_shifts_one 89 4 den-LysN $assigned_chemical_shifts_one 318 5 den-LysN $assigned_chemical_shifts_one 114 5 den-LysN $assigned_chemical_shifts_one 115 5 den-LysN $assigned_chemical_shifts_one 116 6 den-LysN $assigned_chemical_shifts_one 183 6 den-LysN $assigned_chemical_shifts_one 476 7 den-LysN $assigned_chemical_shifts_one 184 7 den-LysN $assigned_chemical_shifts_one 477 8 den-LysN $assigned_chemical_shifts_one 185 8 den-LysN $assigned_chemical_shifts_one 478 9 den-LysN $assigned_chemical_shifts_one 186 9 den-LysN $assigned_chemical_shifts_one 479 10 den-LysN $assigned_chemical_shifts_one 187 10 den-LysN $assigned_chemical_shifts_one 480 11 den-LysN $assigned_chemical_shifts_one 210 11 den-LysN $assigned_chemical_shifts_one 437 12 den-LysN $assigned_chemical_shifts_one 211 12 den-LysN $assigned_chemical_shifts_one 438 13 den-LysN $assigned_chemical_shifts_one 254 13 den-LysN $assigned_chemical_shifts_one 255 13 den-LysN $assigned_chemical_shifts_one 256 13 den-LysN $assigned_chemical_shifts_one 257 14 den-LysN $assigned_chemical_shifts_one 279 14 den-LysN $assigned_chemical_shifts_one 280 14 den-LysN $assigned_chemical_shifts_one 281 14 den-LysN $assigned_chemical_shifts_one 282 15 den-LysN $assigned_chemical_shifts_one 342 15 den-LysN $assigned_chemical_shifts_one 343 15 den-LysN $assigned_chemical_shifts_one 344 16 den-LysN $assigned_chemical_shifts_one 378 16 den-LysN $assigned_chemical_shifts_one 379 16 den-LysN $assigned_chemical_shifts_one 380 16 den-LysN $assigned_chemical_shifts_one 381 17 den-LysN $assigned_chemical_shifts_one 399 17 den-LysN $assigned_chemical_shifts_one 400 17 den-LysN $assigned_chemical_shifts_one 401 18 den-LysN $assigned_chemical_shifts_one 512 18 den-LysN $assigned_chemical_shifts_one 513 18 den-LysN $assigned_chemical_shifts_one 514 19 den-LysN $assigned_chemical_shifts_one 537 19 den-LysN $assigned_chemical_shifts_one 538 19 den-LysN $assigned_chemical_shifts_one 539 20 den-LysN $assigned_chemical_shifts_one 572 20 den-LysN $assigned_chemical_shifts_one 573 20 den-LysN $assigned_chemical_shifts_one 574 21 den-LysN $assigned_chemical_shifts_one 618 21 den-LysN $assigned_chemical_shifts_one 660 22 den-LysN $assigned_chemical_shifts_one 623 22 den-LysN 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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). ; save_