data_15913 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of the IsdC NEAT domain bound to Zinc Protoporphyrin ; _BMRB_accession_number 15913 _BMRB_flat_file_name bmr15913.str _Entry_type new _Submission_date 2008-08-07 _Accession_date 2008-08-07 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Villareal Valerie A. . 2 Pilpa Rosemarie M. . 3 Robson Scott A. . 4 Fadeev Evgeny A. . 5 Clubb Robert T. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 618 "13C chemical shifts" 488 "15N chemical shifts" 130 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-02-27 update BMRB 'complete entry citation' 2008-08-14 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The IsdC protein from Staphylococcus aureus uses a flexible binding pocket to capture heme' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18715872 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Villareal Valerie A. . 2 Pilpa Rosemarie M. . 3 Robson Scott A. . 4 Fadeev Evgeny A. . 5 Clubb Robert T. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 283 _Journal_issue 46 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 31591 _Page_last 31600 _Year 2008 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name IsdC _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label IsdC $IsdC ZNH $ZNH stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_IsdC _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common IsdC _Molecular_mass 14322.988 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 147 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSH MSANAADSGTLNYEVYKYNT NDTSIANDYFNKPAKYIKKN GKLYVQITVNHSHWITGMSI EGHKENIISKNTAKDERTSE FEVSKLNGKIDGKIDVYIDE KVNGKPFKYDHHYNITYKFN GPTDVAG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 4 MET 2 5 GLY 3 6 SER 4 7 SER 5 8 HIS 6 9 HIS 7 10 HIS 8 11 HIS 9 12 HIS 10 13 HIS 11 14 SER 12 15 SER 13 16 GLY 14 17 LEU 15 18 VAL 16 19 PRO 17 20 ARG 18 21 GLY 19 22 SER 20 23 HIS 21 24 MET 22 25 SER 23 26 ALA 24 27 ASN 25 28 ALA 26 29 ALA 27 30 ASP 28 31 SER 29 32 GLY 30 33 THR 31 34 LEU 32 35 ASN 33 36 TYR 34 37 GLU 35 38 VAL 36 39 TYR 37 40 LYS 38 41 TYR 39 42 ASN 40 43 THR 41 44 ASN 42 45 ASP 43 46 THR 44 47 SER 45 48 ILE 46 49 ALA 47 50 ASN 48 51 ASP 49 52 TYR 50 53 PHE 51 54 ASN 52 55 LYS 53 56 PRO 54 57 ALA 55 58 LYS 56 59 TYR 57 60 ILE 58 61 LYS 59 62 LYS 60 63 ASN 61 64 GLY 62 65 LYS 63 66 LEU 64 67 TYR 65 68 VAL 66 69 GLN 67 70 ILE 68 71 THR 69 72 VAL 70 73 ASN 71 74 HIS 72 75 SER 73 76 HIS 74 77 TRP 75 78 ILE 76 79 THR 77 80 GLY 78 81 MET 79 82 SER 80 83 ILE 81 84 GLU 82 85 GLY 83 86 HIS 84 87 LYS 85 88 GLU 86 89 ASN 87 90 ILE 88 91 ILE 89 92 SER 90 93 LYS 91 94 ASN 92 95 THR 93 96 ALA 94 97 LYS 95 98 ASP 96 99 GLU 97 100 ARG 98 101 THR 99 102 SER 100 103 GLU 101 104 PHE 102 105 GLU 103 106 VAL 104 107 SER 105 108 LYS 106 109 LEU 107 110 ASN 108 111 GLY 109 112 LYS 110 113 ILE 111 114 ASP 112 115 GLY 113 116 LYS 114 117 ILE 115 118 ASP 116 119 VAL 117 120 TYR 118 121 ILE 119 122 ASP 120 123 GLU 121 124 LYS 122 125 VAL 123 126 ASN 124 127 GLY 125 128 LYS 126 129 PRO 127 130 PHE 128 131 LYS 129 132 TYR 130 133 ASP 131 134 HIS 132 135 HIS 133 136 TYR 134 137 ASN 135 138 ILE 136 139 THR 137 140 TYR 138 141 LYS 139 142 PHE 140 143 ASN 141 144 GLY 142 145 PRO 143 146 THR 144 147 ASP 145 148 VAL 146 149 ALA 147 150 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-04-25 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 2K78 "Solution Structure Of The Isdc Neat Domain Bound To Zinc Protoporphyrin" 100.00 147 100.00 100.00 2.55e-101 PDB 2O6P "Crystal Structure Of The Heme-isdc Complex" 83.67 161 98.37 99.19 2.35e-81 DBJ BAB42227 "conserved hypothetical protein [Staphylococcus aureus subsp. aureus N315]" 85.71 227 100.00 100.00 2.06e-84 DBJ BAB57293 "conserved hypothetical protein [Staphylococcus aureus subsp. aureus Mu50]" 85.71 227 100.00 100.00 2.06e-84 DBJ BAB94878 "conserved hypothetical protein [Staphylococcus aureus subsp. aureus MW2]" 85.71 227 100.00 100.00 2.06e-84 DBJ BAF67314 "iron-regulated cell surface protein [Staphylococcus aureus subsp. aureus str. Newman]" 85.71 227 100.00 100.00 2.06e-84 DBJ BAF78005 "conserved hypothetical protein [Staphylococcus aureus subsp. aureus Mu3]" 85.71 227 100.00 100.00 2.06e-84 EMBL CAG40106 "putative surface anchored protein [Staphylococcus aureus subsp. aureus MRSA252]" 85.71 227 97.62 99.21 1.12e-82 EMBL CAG42839 "putative surface anchored protein [Staphylococcus aureus subsp. aureus MSSA476]" 85.71 227 100.00 100.00 2.06e-84 EMBL CAI80683 "iron-regulated cell surface protein [Staphylococcus aureus RF122]" 85.71 227 99.21 100.00 3.02e-84 EMBL CAQ49552 "iron-regulated surface determinant protein C (Staphylococcaliron-regulated protein D) [Staphylococcus aureus subsp. aureus ST39" 85.71 228 99.21 99.21 1.46e-83 EMBL CBI49004 "putative surface protein [Staphylococcus aureus subsp. aureus TW20]" 85.71 227 100.00 100.00 2.06e-84 GB AAL33767 "hypothetical protein SirD [Staphylococcus aureus]" 85.71 227 97.62 99.21 1.12e-82 GB AAW38020 "NPQTN cell wall surface anchor protein [Staphylococcus aureus subsp. aureus COL]" 85.71 227 100.00 100.00 2.11e-84 GB ABD20415 "iron transport associated domain protein [Staphylococcus aureus subsp. aureus USA300_FPR3757]" 85.71 227 100.00 100.00 2.06e-84 GB ABD30198 "conserved hypothetical protein [Staphylococcus aureus subsp. aureus NCTC 8325]" 85.71 227 100.00 100.00 2.06e-84 GB ABQ48990 "NEAr transporter [Staphylococcus aureus subsp. aureus JH9]" 85.71 227 100.00 100.00 2.06e-84 REF WP_000789795 "heme transporter IsdC [Staphylococcus aureus]" 85.71 228 99.21 99.21 1.74e-83 REF WP_000789808 "heme transporter IsdC [Staphylococcus aureus]" 85.71 228 99.21 99.21 1.46e-83 REF WP_000789809 "iron-regulated surface determinant protein C [Staphylococcus aureus]" 85.71 227 98.41 99.21 2.31e-83 REF WP_000789810 "iron-regulated surface determinant protein C [Staphylococcus aureus]" 85.71 227 98.41 99.21 2.36e-83 REF WP_000789811 "heme transporter IsdC [Staphylococcus aureus]" 85.71 226 97.62 99.21 1.21e-82 SP A5IS17 "RecName: Full=Iron-regulated surface determinant protein C; AltName: Full=Staphylococcal iron-regulated protein D; Flags: Precu" 85.71 227 100.00 100.00 2.06e-84 SP A6QG32 "RecName: Full=Iron-regulated surface determinant protein C; AltName: Full=Staphylococcal iron-regulated protein D; Flags: Precu" 85.71 227 100.00 100.00 2.06e-84 SP A6U0U8 "RecName: Full=Iron-regulated surface determinant protein C; AltName: Full=Staphylococcal iron-regulated protein D; Flags: Precu" 85.71 227 100.00 100.00 2.06e-84 SP A7X149 "RecName: Full=Iron-regulated surface determinant protein C; AltName: Full=Staphylococcal iron-regulated protein D; Flags: Precu" 85.71 227 100.00 100.00 2.06e-84 SP A8Z1R1 "RecName: Full=Iron-regulated surface determinant protein C; AltName: Full=Staphylococcal iron-regulated protein D; Flags: Precu" 85.71 227 100.00 100.00 2.06e-84 stop_ save_ ############# # Ligands # ############# save_ZNH _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZNH (PROTOPORPHYRIN IX CONTAINING ZN)" _BMRB_code . _PDB_code ZNH _Molecular_mass 626.051 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Feb 15 21:22:10 2008 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN N 0 . ? CHA CHA C N 0 . ? CHB CHB C N 0 . ? CHC CHC C N 0 . ? CHD CHD C N 0 . ? NA NA N N 0 . ? C1A C1A C N 0 . ? C2A C2A C N 0 . ? C3A C3A C N 0 . ? C4A C4A C N 0 . ? CMA CMA C N 0 . ? CAA CAA C N 0 . ? CBA CBA C N 0 . ? CGA CGA C N 0 . ? O1A O1A O N 0 . ? O2A O2A O N 0 . ? NB NB N N 0 . ? C1B C1B C N 0 . ? C2B C2B C N 0 . ? C3B C3B C N 0 . ? C4B C4B C N 0 . ? CMB CMB C N 0 . ? CAB CAB C N 0 . ? CBB CBB C N 0 . ? NC NC N N 0 . ? C1C C1C C N 0 . ? C2C C2C C N 0 . ? C3C C3C C N 0 . ? C4C C4C C N 0 . ? CMC CMC C N 0 . ? CAC CAC C N 0 . ? CBC CBC C N 0 . ? ND ND N N 0 . ? C1D C1D C N 0 . ? C2D C2D C N 0 . ? C3D C3D C N 0 . ? C4D C4D C N 0 . ? CMD CMD C N 0 . ? CAD CAD C N 0 . ? CBD CBD C N 0 . ? CGD CGD C N 0 . ? O1D O1D O N 0 . ? O2D O2D O N 0 . ? HHA HHA H N 0 . ? HHB HHB H N 0 . ? HHC HHC H N 0 . ? HHD HHD H N 0 . ? HMA1 HMA1 H N 0 . ? HMA2 HMA2 H N 0 . ? HMA3 HMA3 H N 0 . ? HAA1 HAA1 H N 0 . ? HAA2 HAA2 H N 0 . ? HBA1 HBA1 H N 0 . ? HBA2 HBA2 H N 0 . ? H2A H2A H N 0 . ? HMB1 HMB1 H N 0 . ? HMB2 HMB2 H N 0 . ? HMB3 HMB3 H N 0 . ? HAB HAB H N 0 . ? HBB1 HBB1 H N 0 . ? HBB2 HBB2 H N 0 . ? HMC1 HMC1 H N 0 . ? HMC2 HMC2 H N 0 . ? HMC3 HMC3 H N 0 . ? HAC HAC H N 0 . ? HBC1 HBC1 H N 0 . ? HBC2 HBC2 H N 0 . ? HMD1 HMD1 H N 0 . ? HMD2 HMD2 H N 0 . ? HMD3 HMD3 H N 0 . ? HAD1 HAD1 H N 0 . ? HAD2 HAD2 H N 0 . ? HBD1 HBD1 H N 0 . ? HBD2 HBD2 H N 0 . ? H2D H2D H N 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING ZN NA ? ? SING ZN NB ? ? SING ZN NC ? ? SING ZN ND ? ? DOUB CHA C1A ? ? SING CHA C4D ? ? SING CHA HHA ? ? DOUB CHB C4A ? ? SING CHB C1B ? ? SING CHB HHB ? ? DOUB CHC C4B ? ? SING CHC C1C ? ? SING CHC HHC ? ? SING CHD C4C ? ? DOUB CHD C1D ? ? SING CHD HHD ? ? SING NA C1A ? ? SING NA C4A ? ? SING C1A C2A ? ? DOUB C2A C3A ? ? SING C2A CAA ? ? SING C3A C4A ? ? SING C3A CMA ? ? SING CMA HMA1 ? ? SING CMA HMA2 ? ? SING CMA HMA3 ? ? SING CAA CBA ? ? SING CAA HAA1 ? ? SING CAA HAA2 ? ? SING CBA CGA ? ? SING CBA HBA1 ? ? SING CBA HBA2 ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING O2A H2A ? ? DOUB NB C1B ? ? SING NB C4B ? ? SING C1B C2B ? ? DOUB C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? SING C3B CAB ? ? SING CMB HMB1 ? ? SING CMB HMB2 ? ? SING CMB HMB3 ? ? DOUB CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB1 ? ? SING CBB HBB2 ? ? SING NC C1C ? ? SING NC C4C ? ? DOUB C1C C2C ? ? SING C2C C3C ? ? SING C2C CMC ? ? DOUB C3C C4C ? ? SING C3C CAC ? ? SING CMC HMC1 ? ? SING CMC HMC2 ? ? SING CMC HMC3 ? ? DOUB CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC1 ? ? SING CBC HBC2 ? ? SING ND C1D ? ? DOUB ND C4D ? ? SING C1D C2D ? ? DOUB C2D C3D ? ? SING C2D CMD ? ? SING C3D C4D ? ? SING C3D CAD ? ? SING CMD HMD1 ? ? SING CMD HMD2 ? ? SING CMD HMD3 ? ? SING CAD CBD ? ? SING CAD HAD1 ? ? SING CAD HAD2 ? ? SING CBD CGD ? ? SING CBD HBD1 ? ? SING CBD HBD2 ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2D H2D ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $IsdC 'Staphylococcus aureus' 1280 Bacteria . Staphylococcus aureus 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 $IsdC 'recombinant technology' . . . . pET15b $ZNH 'obtained from a vendor' . . . . 'not applicable' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling 'sodium phosphate' 50 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' 'sodium azide' 0.01 % 'natural abundance' $IsdC 1.3 mM '[U-100% 13C; U-100% 15N]' $ZNH 2.1 mM 'natural abundance' D2O 7 % '[U-100% 2H]' H2O 93 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling 'sodium phosphate' 50 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' 'sodium azide' 0.01 % 'natural abundance' $IsdC 1.1 mM 'natural abundance' $ZNH 2.3 mM 'natural abundance' D2O 100 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR_NIH _Saveframe_category software _Name X-PLOR_NIH _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_PIPP _Saveframe_category software _Name PIPP _Version . loop_ _Vendor _Address _Electronic_address Garrett . . stop_ loop_ _Task 'peak picking' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_ATNOS/CANDID _Saveframe_category software _Name ATNOS/CANDID _Version . loop_ _Vendor _Address _Electronic_address 'Herrmann, Guntert, Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address Keller . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_2 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNHA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label $sample_1 save_ save_3D_HCCH-COSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-COSY' _Sample_label $sample_2 save_ save_3D_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_2 save_ save_3D_1H-15N_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HNCO_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNHB_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHB' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 302 . K pH 6 . pH pressure 1 . atm 'ionic strength' 150 . mM stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0 external indirect . . . 1.000000000 DSS C 13 'methyl protons' ppm 0 external indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0 external indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D CBCA(CO)NH' '3D HNCACB' '3D HNHA' '3D HCCH-COSY' '3D HCCH-TOCSY' '3D HNCO' '3D HNHB' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name IsdC _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 25 22 SER H H 8.3100 . 1 2 25 22 SER HA H 4.4200 . 1 3 25 22 SER HB2 H 3.7900 . 2 4 25 22 SER C C 173.2300 . 1 5 25 22 SER CA C 58.2300 . 1 6 25 22 SER CB C 63.6100 . 1 7 25 22 SER N N 117.3600 . 1 8 26 23 ALA H H 8.4100 . 1 9 26 23 ALA HA H 4.4130 . 1 10 26 23 ALA HB H 1.4300 . 1 11 26 23 ALA C C 176.3100 . 1 12 26 23 ALA CA C 52.7400 . 1 13 26 23 ALA CB C 19.1800 . 1 14 26 23 ALA N N 126.2000 . 1 15 27 24 ASN H H 8.3400 . 1 16 27 24 ASN HA H 4.7200 . 1 17 27 24 ASN HB2 H 2.9500 . 2 18 27 24 ASN HB3 H 2.8300 . 2 19 27 24 ASN C C 173.9000 . 1 20 27 24 ASN CA C 52.9600 . 1 21 27 24 ASN CB C 38.7100 . 1 22 27 24 ASN N N 117.9300 . 1 23 28 25 ALA H H 8.2300 . 1 24 28 25 ALA HA H 4.2800 . 1 25 28 25 ALA HB H 1.3400 . 1 26 28 25 ALA C C 176.1400 . 1 27 28 25 ALA CA C 52.4500 . 1 28 28 25 ALA CB C 19.3100 . 1 29 28 25 ALA N N 125.0300 . 1 30 29 26 ALA H H 8.2600 . 1 31 29 26 ALA HA H 4.4200 . 1 32 29 26 ALA HB H 1.4300 . 1 33 29 26 ALA C C 176.4800 . 1 34 29 26 ALA CA C 52.2400 . 1 35 29 26 ALA CB C 19.2400 . 1 36 29 26 ALA N N 122.8700 . 1 37 30 27 ASP H H 8.3600 . 1 38 30 27 ASP HA H 4.6500 . 1 39 30 27 ASP HB2 H 2.8700 . 2 40 30 27 ASP HB3 H 2.7800 . 2 41 30 27 ASP C C 173.3600 . 1 42 30 27 ASP CA C 54.7300 . 1 43 30 27 ASP CB C 41.4100 . 1 44 30 27 ASP N N 119.1900 . 1 45 31 28 SER H H 7.5900 . 1 46 31 28 SER HA H 4.5700 . 1 47 31 28 SER HB2 H 3.7300 . 2 48 31 28 SER C C 171.6600 . 1 49 31 28 SER CA C 56.4600 . 1 50 31 28 SER CB C 65.6000 . 1 51 31 28 SER N N 111.6200 . 1 52 32 29 GLY H H 6.9200 . 1 53 32 29 GLY HA2 H 3.7100 . 2 54 32 29 GLY HA3 H 3.9400 . 2 55 32 29 GLY C C 170.8000 . 1 56 32 29 GLY CA C 45.4400 . 1 57 32 29 GLY N N 106.1500 . 1 58 33 30 THR H H 8.4500 . 1 59 33 30 THR HA H 4.8600 . 1 60 33 30 THR HB H 4.1100 . 1 61 33 30 THR HG2 H 1.2200 . 1 62 33 30 THR C C 172.5100 . 1 63 33 30 THR CA C 61.7300 . 1 64 33 30 THR CB C 70.5900 . 1 65 33 30 THR CG2 C 22.0400 . 1 66 33 30 THR N N 113.8300 . 1 67 34 31 LEU H H 8.6600 . 1 68 34 31 LEU HA H 4.8860 . 1 69 34 31 LEU HB2 H 1.6800 . 2 70 34 31 LEU HB3 H 1.4400 . 2 71 34 31 LEU HD1 H 0.5700 . 2 72 34 31 LEU HD2 H 0.8640 . 2 73 34 31 LEU HG H 1.5850 . 1 74 34 31 LEU C C 173.1300 . 1 75 34 31 LEU CA C 53.7400 . 1 76 34 31 LEU CB C 45.1700 . 1 77 34 31 LEU CD1 C 27.1000 . 2 78 34 31 LEU CD2 C 25.7700 . 2 79 34 31 LEU CG C 27.1000 . 1 80 34 31 LEU N N 122.8200 . 1 81 35 32 ASN H H 9.1500 . 1 82 35 32 ASN HA H 5.1200 . 1 83 35 32 ASN HB2 H 2.8830 . 2 84 35 32 ASN HB3 H 2.7860 . 2 85 35 32 ASN C C 172.8400 . 1 86 35 32 ASN CA C 52.8700 . 1 87 35 32 ASN CB C 39.2700 . 1 88 35 32 ASN N N 126.3600 . 1 89 36 33 TYR H H 8.1100 . 1 90 36 33 TYR HA H 5.4060 . 1 91 36 33 TYR HB2 H 2.7000 . 2 92 36 33 TYR HD1 H 6.9400 . 3 93 36 33 TYR HE1 H 6.8500 . 3 94 36 33 TYR C C 170.6300 . 1 95 36 33 TYR CA C 55.7100 . 1 96 36 33 TYR CB C 41.8800 . 1 97 36 33 TYR CD1 C 132.9400 . 3 98 36 33 TYR CE1 C 118.2600 . 3 99 36 33 TYR N N 118.4700 . 1 100 37 34 GLU H H 8.2100 . 1 101 37 34 GLU HA H 4.0400 . 1 102 37 34 GLU HB2 H 1.4400 . 2 103 37 34 GLU HB3 H 1.5900 . 2 104 37 34 GLU HG2 H 1.8840 . 2 105 37 34 GLU C C 172.1600 . 1 106 37 34 GLU CA C 54.8800 . 1 107 37 34 GLU CB C 34.3700 . 1 108 37 34 GLU CG C 36.1000 . 1 109 37 34 GLU N N 116.9800 . 1 110 38 35 VAL H H 7.4000 . 1 111 38 35 VAL HA H 3.9320 . 1 112 38 35 VAL HB H 1.3600 . 1 113 38 35 VAL HG1 H 0.0100 . 2 114 38 35 VAL HG2 H 0.2660 . 2 115 38 35 VAL C C 173.5600 . 1 116 38 35 VAL CA C 62.0900 . 1 117 38 35 VAL CB C 31.9800 . 1 118 38 35 VAL CG1 C 20.3400 . 2 119 38 35 VAL CG2 C 22.3700 . 2 120 38 35 VAL N N 121.0100 . 1 121 39 36 TYR H H 9.6000 . 1 122 39 36 TYR HA H 4.9860 . 1 123 39 36 TYR HB2 H 2.9700 . 1 124 39 36 TYR HB3 H 2.6900 . 1 125 39 36 TYR HD1 H 6.6100 . 3 126 39 36 TYR HE1 H 6.5400 . 3 127 39 36 TYR C C 175.4900 . 1 128 39 36 TYR CA C 53.9800 . 1 129 39 36 TYR CB C 39.4400 . 1 130 39 36 TYR CD1 C 131.9500 . 3 131 39 36 TYR CE1 C 118.0800 . 3 132 39 36 TYR N N 128.4300 . 1 133 40 37 LYS H H 8.5200 . 1 134 40 37 LYS HA H 4.5130 . 1 135 40 37 LYS HB2 H 1.7500 . 2 136 40 37 LYS HB3 H 1.6800 . 2 137 40 37 LYS HE2 H 3.1000 . 2 138 40 37 LYS HE3 H 3.0200 . 2 139 40 37 LYS HG2 H 1.4800 . 2 140 40 37 LYS C C 177.2000 . 1 141 40 37 LYS CA C 56.2200 . 1 142 40 37 LYS CB C 31.6400 . 1 143 40 37 LYS CE C 42.1400 . 1 144 40 37 LYS CG C 24.6800 . 1 145 40 37 LYS N N 122.6100 . 1 146 41 38 TYR H H 9.2400 . 1 147 41 38 TYR HA H 4.4850 . 1 148 41 38 TYR HB2 H 2.9300 . 2 149 41 38 TYR HB3 H 2.8600 . 2 150 41 38 TYR HD1 H 7.0700 . 3 151 41 38 TYR HE1 H 6.8000 . 3 152 41 38 TYR C C 175.1200 . 1 153 41 38 TYR CA C 57.9900 . 1 154 41 38 TYR CB C 39.7600 . 1 155 41 38 TYR CD1 C 133.0700 . 3 156 41 38 TYR CE1 C 118.2900 . 3 157 41 38 TYR N N 129.1300 . 1 158 42 39 ASN H H 8.6800 . 1 159 42 39 ASN HA H 4.1120 . 1 160 42 39 ASN HB2 H 2.9160 . 2 161 42 39 ASN HB3 H 2.0490 . 2 162 42 39 ASN HD21 H 6.4500 . 2 163 42 39 ASN HD22 H 7.1000 . 2 164 42 39 ASN C C 173.1600 . 1 165 42 39 ASN CA C 53.7000 . 1 166 42 39 ASN CB C 37.1100 . 1 167 42 39 ASN N N 120.8000 . 1 168 42 39 ASN ND2 N 110.8600 . 1 169 43 40 THR H H 8.0600 . 1 170 43 40 THR HA H 4.7600 . 1 171 43 40 THR HB H 4.1300 . 1 172 43 40 THR HG2 H 1.0500 . 1 173 43 40 THR C C 172.0200 . 1 174 43 40 THR CA C 60.4700 . 1 175 43 40 THR CB C 72.5500 . 1 176 43 40 THR CG2 C 21.0000 . 1 177 43 40 THR N N 109.2400 . 1 178 44 41 ASN H H 8.1100 . 1 179 44 41 ASN HA H 4.4600 . 1 180 44 41 ASN HB2 H 2.7000 . 2 181 44 41 ASN HB3 H 2.2350 . 2 182 44 41 ASN HD21 H 7.3800 . 2 183 44 41 ASN HD22 H 6.8300 . 2 184 44 41 ASN C C 172.8600 . 1 185 44 41 ASN CA C 51.8900 . 1 186 44 41 ASN CB C 38.7100 . 1 187 44 41 ASN N N 115.7500 . 1 188 44 41 ASN ND2 N 114.7200 . 1 189 45 42 ASP H H 8.4300 . 1 190 45 42 ASP HA H 4.5300 . 1 191 45 42 ASP HB2 H 2.3700 . 2 192 45 42 ASP C C 173.7300 . 1 193 45 42 ASP CA C 52.5600 . 1 194 45 42 ASP CB C 42.4300 . 1 195 45 42 ASP N N 120.4000 . 1 196 46 43 THR H H 8.2200 . 1 197 46 43 THR HA H 3.7900 . 1 198 46 43 THR HB H 3.5400 . 1 199 46 43 THR HG2 H 1.0200 . 1 200 46 43 THR C C 172.8600 . 1 201 46 43 THR CA C 64.3300 . 1 202 46 43 THR CB C 69.0600 . 1 203 46 43 THR CG2 C 22.1900 . 1 204 46 43 THR N N 118.4100 . 1 205 47 44 SER H H 8.6800 . 1 206 47 44 SER HA H 4.4600 . 1 207 47 44 SER HB2 H 3.6000 . 2 208 47 44 SER HB3 H 4.4000 . 2 209 47 44 SER C C 176.7800 . 1 210 47 44 SER CA C 56.2200 . 1 211 47 44 SER CB C 62.9600 . 1 212 47 44 SER N N 120.3600 . 1 213 48 45 ILE H H 8.8300 . 1 214 48 45 ILE HA H 1.9310 . 1 215 48 45 ILE HD1 H -1.9500 . 1 216 48 45 ILE HG12 H -0.7500 . 2 217 48 45 ILE HG13 H -1.0800 . 2 218 48 45 ILE C C 174.4400 . 1 219 48 45 ILE CA C 62.7500 . 1 220 48 45 ILE CB C 34.4300 . 1 221 48 45 ILE CD1 C 9.5700 . 1 222 48 45 ILE CG1 C 27.7400 . 1 223 48 45 ILE CG2 C 9.8500 . 1 224 48 45 ILE N N 105.0300 . 1 225 49 46 ALA H H 7.9900 . 1 226 49 46 ALA HA H 3.5300 . 1 227 49 46 ALA HB H 1.9000 . 1 228 49 46 ALA C C 177.8700 . 1 229 49 46 ALA CA C 52.6300 . 1 230 49 46 ALA CB C 20.0100 . 1 231 49 46 ALA N N 116.4900 . 1 232 50 47 ASN H H 7.2000 . 1 233 50 47 ASN HA H 4.0300 . 1 234 50 47 ASN HB2 H 2.8330 . 2 235 50 47 ASN HB3 H 2.4300 . 2 236 50 47 ASN C C 175.6200 . 1 237 50 47 ASN CA C 57.8600 . 1 238 50 47 ASN CB C 39.7700 . 1 239 50 47 ASN N N 111.9400 . 1 240 51 48 ASP H H 6.8800 . 1 241 51 48 ASP HA H 4.1000 . 1 242 51 48 ASP HB2 H 1.3700 . 1 243 51 48 ASP HB3 H 1.9700 . 1 244 51 48 ASP C C 175.6400 . 1 245 51 48 ASP CA C 55.9800 . 1 246 51 48 ASP CB C 40.1700 . 1 247 51 48 ASP N N 114.1900 . 1 248 53 50 PHE H H 7.3900 . 1 249 53 50 PHE HA H 4.6300 . 1 250 53 50 PHE HB2 H 2.6820 . 2 251 53 50 PHE HB3 H 4.0400 . 2 252 53 50 PHE HD1 H 7.7000 . 3 253 53 50 PHE HD2 H 7.7000 . 3 254 53 50 PHE C C 175.4600 . 1 255 53 50 PHE CA C 57.4700 . 1 256 53 50 PHE CB C 38.2200 . 1 257 53 50 PHE CD1 C 131.7200 . 3 258 53 50 PHE N N 119.8600 . 1 259 54 51 ASN H H 9.2500 . 1 260 54 51 ASN HA H 4.7500 . 1 261 54 51 ASN HB2 H 2.9100 . 2 262 54 51 ASN C C 175.6600 . 1 263 54 51 ASN CA C 52.9600 . 1 264 54 51 ASN CB C 36.5300 . 1 265 54 51 ASN N N 126.5400 . 1 266 55 52 LYS H H 9.3100 . 1 267 55 52 LYS HA H 4.8400 . 1 268 55 52 LYS HB2 H 1.6600 . 2 269 55 52 LYS HB3 H 2.0800 . 2 270 55 52 LYS C C 173.9000 . 1 271 55 52 LYS CA C 53.6300 . 1 272 55 52 LYS CB C 32.6900 . 1 273 55 52 LYS N N 125.9200 . 1 274 56 53 PRO HA H 4.8660 . 1 275 56 53 PRO HB2 H 2.4900 . 2 276 56 53 PRO HD2 H 3.4700 . 2 277 56 53 PRO HD3 H 3.6300 . 2 278 56 53 PRO HG2 H 1.7300 . 2 279 56 53 PRO HG3 H 2.0300 . 2 280 56 53 PRO CA C 63.5000 . 1 281 56 53 PRO CB C 34.9600 . 1 282 56 53 PRO CD C 49.6800 . 1 283 56 53 PRO CG C 24.2000 . 1 284 57 54 ALA H H 8.9400 . 1 285 57 54 ALA HA H 5.1800 . 1 286 57 54 ALA HB H 1.5400 . 1 287 57 54 ALA C C 175.6600 . 1 288 57 54 ALA CA C 51.3900 . 1 289 57 54 ALA CB C 21.5200 . 1 290 57 54 ALA N N 120.3500 . 1 291 58 55 LYS H H 8.1300 . 1 292 58 55 LYS HA H 5.2380 . 1 293 58 55 LYS HB2 H 1.7400 . 2 294 58 55 LYS HB3 H 1.6800 . 2 295 58 55 LYS C C 174.4000 . 1 296 58 55 LYS CA C 54.8400 . 1 297 58 55 LYS CB C 36.0300 . 1 298 58 55 LYS N N 119.6900 . 1 299 59 56 TYR H H 8.7000 . 1 300 59 56 TYR HA H 5.8700 . 1 301 59 56 TYR HB2 H 3.0400 . 2 302 59 56 TYR HB3 H 2.5181 . 2 303 59 56 TYR HD1 H 6.5400 . 3 304 59 56 TYR HE1 H 6.5500 . 3 305 59 56 TYR C C 172.3400 . 1 306 59 56 TYR CA C 55.3601 . 1 307 59 56 TYR CB C 42.6800 . 1 308 59 56 TYR CD1 C 133.1900 . 3 309 59 56 TYR CE1 C 117.0400 . 3 310 59 56 TYR N N 119.4200 . 1 311 60 57 ILE H H 9.1200 . 1 312 60 57 ILE HA H 4.5900 . 1 313 60 57 ILE HB H 1.6100 . 1 314 60 57 ILE HD1 H 0.6500 . 1 315 60 57 ILE HG12 H 1.3300 . 2 316 60 57 ILE HG13 H 0.9000 . 2 317 60 57 ILE HG2 H 0.7400 . 1 318 60 57 ILE C C 172.6600 . 1 319 60 57 ILE CA C 60.6000 . 1 320 60 57 ILE CB C 42.9500 . 1 321 60 57 ILE CD1 C 14.2300 . 1 322 60 57 ILE CG1 C 28.3300 . 1 323 60 57 ILE CG2 C 17.9000 . 1 324 60 57 ILE N N 119.8700 . 1 325 61 58 LYS H H 8.6500 . 1 326 61 58 LYS HA H 5.2950 . 1 327 61 58 LYS HB2 H 1.9090 . 1 328 61 58 LYS HB3 H 1.7070 . 1 329 61 58 LYS HG2 H 1.2560 . 2 330 61 58 LYS C C 174.7700 . 1 331 61 58 LYS CA C 55.1200 . 1 332 61 58 LYS CB C 33.4700 . 1 333 61 58 LYS CG C 24.9900 . 1 334 61 58 LYS N N 126.2200 . 1 335 62 59 LYS H H 8.5900 . 1 336 62 59 LYS HA H 4.6500 . 1 337 62 59 LYS HB2 H 1.7800 . 2 338 62 59 LYS HB3 H 1.5700 . 2 339 62 59 LYS C C 174.4200 . 1 340 62 59 LYS CA C 55.4000 . 1 341 62 59 LYS CB C 34.7100 . 1 342 62 59 LYS N N 122.2000 . 1 343 63 60 ASN H H 9.4200 . 1 344 63 60 ASN HA H 4.3700 . 1 345 63 60 ASN HB2 H 3.0300 . 2 346 63 60 ASN HB3 H 2.8970 . 2 347 63 60 ASN C C 173.8800 . 1 348 63 60 ASN CA C 54.2000 . 1 349 63 60 ASN CB C 37.4500 . 1 350 63 60 ASN N N 120.7200 . 1 351 64 61 GLY H H 8.7500 . 1 352 64 61 GLY HA2 H 4.0700 . 2 353 64 61 GLY HA3 H 3.5800 . 2 354 64 61 GLY C C 172.7000 . 1 355 64 61 GLY CA C 45.6500 . 1 356 64 61 GLY N N 104.8100 . 1 357 65 62 LYS H H 8.1100 . 1 358 65 62 LYS HA H 4.4791 . 1 359 65 62 LYS HB2 H 1.8460 . 1 360 65 62 LYS HB3 H 1.4201 . 1 361 65 62 LYS C C 172.6900 . 1 362 65 62 LYS CA C 54.7300 . 1 363 65 62 LYS CB C 37.0500 . 1 364 65 62 LYS N N 121.9000 . 1 365 66 63 LEU H H 8.2900 . 1 366 66 63 LEU HA H 4.7900 . 1 367 66 63 LEU HB2 H 0.8100 . 1 368 66 63 LEU HB3 H 1.9600 . 1 369 66 63 LEU HD1 H 0.6300 . 2 370 66 63 LEU HD2 H 0.5701 . 2 371 66 63 LEU HG H 1.4701 . 1 372 66 63 LEU C C 173.3900 . 1 373 66 63 LEU CA C 53.4700 . 1 374 66 63 LEU CB C 43.9200 . 1 375 66 63 LEU CD1 C 23.5100 . 2 376 66 63 LEU CD2 C 25.0000 . 2 377 66 63 LEU CG C 26.1600 . 1 378 66 63 LEU N N 121.1300 . 1 379 67 64 TYR H H 8.6300 . 1 380 67 64 TYR HA H 5.5100 . 1 381 67 64 TYR HB2 H 2.7500 . 2 382 67 64 TYR HB3 H 2.6300 . 2 383 67 64 TYR HD1 H 6.5500 . 3 384 67 64 TYR C C 174.8200 . 1 385 67 64 TYR CA C 55.8600 . 1 386 67 64 TYR CB C 41.7800 . 1 387 67 64 TYR CD1 C 133.1200 . 3 388 67 64 TYR N N 116.9100 . 1 389 68 65 VAL H H 9.1500 . 1 390 68 65 VAL HA H 5.2400 . 1 391 68 65 VAL HB H 1.6300 . 1 392 68 65 VAL HG1 H 0.4701 . 2 393 68 65 VAL HG2 H 0.6500 . 2 394 68 65 VAL C C 173.9000 . 1 395 68 65 VAL CA C 58.8500 . 1 396 68 65 VAL CB C 35.2100 . 1 397 68 65 VAL CG1 C 21.9500 . 2 398 68 65 VAL CG2 C 20.1600 . 2 399 68 65 VAL N N 113.7600 . 1 400 69 66 GLN H H 9.1800 . 1 401 69 66 GLN HA H 5.4800 . 1 402 69 66 GLN HB2 H 1.9400 . 1 403 69 66 GLN HB3 H 1.4500 . 1 404 69 66 GLN HG2 H 2.1400 . 2 405 69 66 GLN HG3 H 2.0100 . 2 406 69 66 GLN C C 174.7700 . 1 407 69 66 GLN CA C 54.1300 . 1 408 69 66 GLN CB C 29.4900 . 1 409 69 66 GLN CG C 33.2200 . 1 410 69 66 GLN N N 121.8500 . 1 411 70 67 ILE H H 9.4500 . 1 412 70 67 ILE HA H 4.6300 . 1 413 70 67 ILE HB H 1.9500 . 1 414 70 67 ILE HD1 H 0.5300 . 1 415 70 67 ILE HG12 H 1.4700 . 2 416 70 67 ILE HG13 H 0.9800 . 2 417 70 67 ILE HG2 H 1.3301 . 1 418 70 67 ILE C C 173.0300 . 1 419 70 67 ILE CA C 59.7600 . 1 420 70 67 ILE CB C 43.0100 . 1 421 70 67 ILE CD1 C 13.1000 . 1 422 70 67 ILE CG1 C 28.1700 . 1 423 70 67 ILE CG2 C 17.7900 . 1 424 70 67 ILE N N 128.1500 . 1 425 71 68 THR H H 9.7700 . 1 426 71 68 THR HA H 5.7900 . 1 427 71 68 THR HB H 4.0500 . 1 428 71 68 THR HG2 H 1.0900 . 1 429 71 68 THR C C 172.5600 . 1 430 71 68 THR CA C 60.8700 . 1 431 71 68 THR CB C 70.3700 . 1 432 71 68 THR CG2 C 21.8000 . 1 433 71 68 THR N N 126.2400 . 1 434 72 69 VAL H H 8.7700 . 1 435 72 69 VAL HA H 5.1300 . 1 436 72 69 VAL HB H 2.3200 . 1 437 72 69 VAL HG1 H 0.4100 . 2 438 72 69 VAL HG2 H 0.8400 . 2 439 72 69 VAL C C 174.4000 . 1 440 72 69 VAL CA C 58.2600 . 1 441 72 69 VAL CB C 33.2900 . 1 442 72 69 VAL CG1 C 21.9900 . 2 443 72 69 VAL CG2 C 18.6800 . 2 444 72 69 VAL N N 118.5100 . 1 445 73 70 ASN H H 8.9700 . 1 446 73 70 ASN HA H 5.3400 . 1 447 73 70 ASN HB2 H 3.3700 . 2 448 73 70 ASN HB3 H 2.6400 . 2 449 73 70 ASN C C 172.0200 . 1 450 73 70 ASN CA C 51.5600 . 1 451 73 70 ASN CB C 41.6400 . 1 452 73 70 ASN N N 117.7400 . 1 453 74 71 HIS H H 8.8700 . 1 454 74 71 HIS HA H 4.1200 . 1 455 74 71 HIS C C 175.2700 . 1 456 74 71 HIS CA C 57.5600 . 1 457 74 71 HIS N N 110.1300 . 1 458 75 72 SER H H 8.1500 . 1 459 75 72 SER HA H 3.8100 . 1 460 75 72 SER CA C 61.2200 . 1 461 75 72 SER CB C 62.4600 . 1 462 75 72 SER N N 109.0300 . 1 463 76 73 HIS H H 10.3500 . 1 464 76 73 HIS HA H 4.1300 . 1 465 76 73 HIS C C 175.1200 . 1 466 76 73 HIS CA C 57.7500 . 1 467 76 73 HIS CB C 26.3000 . 1 468 76 73 HIS N N 115.4300 . 1 469 77 74 TRP H H 8.2900 . 1 470 77 74 TRP HA H 5.0600 . 1 471 77 74 TRP HE1 H 10.0600 . 1 472 77 74 TRP C C 174.2600 . 1 473 77 74 TRP CA C 55.3900 . 1 474 77 74 TRP CB C 30.3700 . 1 475 77 74 TRP N N 121.0600 . 1 476 77 74 TRP NE1 N 128.5600 . 1 477 78 75 ILE H H 8.0300 . 1 478 78 75 ILE HA H 4.8750 . 1 479 78 75 ILE HD1 H 1.2100 . 1 480 78 75 ILE HG2 H 1.2100 . 1 481 78 75 ILE C C 176.8300 . 1 482 78 75 ILE CA C 60.7400 . 1 483 78 75 ILE CB C 38.7800 . 1 484 78 75 ILE CD1 C 14.5500 . 1 485 78 75 ILE CG1 C 32.5900 . 1 486 78 75 ILE CG2 C 18.7200 . 1 487 78 75 ILE N N 120.6600 . 1 488 79 76 THR H H 8.5900 . 1 489 79 76 THR HA H 4.2300 . 1 490 79 76 THR HB H 4.2200 . 1 491 79 76 THR HG2 H 1.1700 . 1 492 79 76 THR C C 175.2400 . 1 493 79 76 THR CA C 63.5300 . 1 494 79 76 THR CB C 67.8000 . 1 495 79 76 THR CG2 C 23.9000 . 1 496 79 76 THR N N 121.3000 . 1 497 80 77 GLY H H 7.6200 . 1 498 80 77 GLY HA2 H 4.4200 . 2 499 80 77 GLY HA3 H 4.1600 . 2 500 80 77 GLY C C 170.1000 . 1 501 80 77 GLY CA C 45.9900 . 1 502 80 77 GLY N N 107.8900 . 1 503 81 78 MET H H 7.6000 . 1 504 81 78 MET HA H 5.3200 . 1 505 81 78 MET HB2 H 2.6400 . 2 506 81 78 MET HB3 H 2.2300 . 2 507 81 78 MET HG2 H 2.5800 . 2 508 81 78 MET HG3 H 2.6860 . 2 509 81 78 MET C C 174.0800 . 1 510 81 78 MET CA C 55.9600 . 1 511 81 78 MET CB C 40.6500 . 1 512 81 78 MET CG C 33.2800 . 1 513 81 78 MET N N 118.6700 . 1 514 82 79 SER H H 8.6200 . 1 515 82 79 SER HA H 5.5400 . 1 516 82 79 SER HB2 H 3.7100 . 2 517 82 79 SER HB3 H 3.4600 . 2 518 82 79 SER C C 173.4800 . 1 519 82 79 SER CA C 57.2100 . 1 520 82 79 SER CB C 66.2000 . 1 521 82 79 SER N N 114.1800 . 1 522 83 80 ILE H H 8.7800 . 1 523 83 80 ILE HA H 4.3900 . 1 524 83 80 ILE HB H 1.2500 . 1 525 83 80 ILE HD1 H -0.6800 . 1 526 83 80 ILE HG12 H 0.4600 . 2 527 83 80 ILE HG2 H 0.5901 . 1 528 83 80 ILE C C 174.6000 . 1 529 83 80 ILE CA C 63.5300 . 1 530 83 80 ILE CB C 41.1100 . 1 531 83 80 ILE CD1 C 11.7000 . 1 532 83 80 ILE CG1 C 28.4200 . 1 533 83 80 ILE CG2 C 17.5000 . 1 534 83 80 ILE N N 123.9100 . 1 535 84 81 GLU H H 9.3400 . 1 536 84 81 GLU HA H 3.9500 . 1 537 84 81 GLU HB2 H 2.6200 . 2 538 84 81 GLU HB3 H 1.9420 . 2 539 84 81 GLU HG2 H 2.5100 . 2 540 84 81 GLU HG3 H 2.3600 . 2 541 84 81 GLU C C 174.6200 . 1 542 84 81 GLU CA C 57.2100 . 1 543 84 81 GLU CB C 29.5400 . 1 544 84 81 GLU CG C 38.9900 . 1 545 84 81 GLU N N 129.5800 . 1 546 85 82 GLY H H 9.0000 . 1 547 85 82 GLY HA2 H 3.9100 . 2 548 85 82 GLY HA3 H 3.5600 . 2 549 85 82 GLY C C 173.3900 . 1 550 85 82 GLY CA C 44.9100 . 1 551 85 82 GLY N N 104.3600 . 1 552 86 83 HIS H H 8.3600 . 1 553 86 83 HIS HA H 5.0650 . 1 554 86 83 HIS HB2 H 3.9000 . 1 555 86 83 HIS HB3 H 3.5200 . 1 556 86 83 HIS HD2 H 7.5050 . 1 557 86 83 HIS C C 173.3800 . 1 558 86 83 HIS CA C 53.6700 . 1 559 86 83 HIS CB C 28.9300 . 1 560 86 83 HIS CD2 C 121.5700 . 1 561 86 83 HIS N N 120.0000 . 1 562 87 84 LYS H H 8.9300 . 1 563 87 84 LYS HA H 4.4000 . 1 564 87 84 LYS HB2 H 1.9600 . 2 565 87 84 LYS HB3 H 1.8900 . 2 566 87 84 LYS HD2 H 1.7300 . 2 567 87 84 LYS HE2 H 3.0400 . 2 568 87 84 LYS HG2 H 1.7500 . 2 569 87 84 LYS HG3 H 1.6500 . 2 570 87 84 LYS C C 175.5400 . 1 571 87 84 LYS CA C 56.8500 . 1 572 87 84 LYS CB C 33.3000 . 1 573 87 84 LYS CD C 29.0400 . 1 574 87 84 LYS CE C 42.4600 . 1 575 87 84 LYS CG C 25.2200 . 1 576 87 84 LYS N N 125.8800 . 1 577 88 85 GLU H H 8.0000 . 1 578 88 85 GLU HA H 4.5800 . 1 579 88 85 GLU HB2 H 3.1300 . 2 580 88 85 GLU HB3 H 3.0500 . 2 581 88 85 GLU HG2 H 2.2200 . 2 582 88 85 GLU HG3 H 2.5800 . 2 583 88 85 GLU C C 172.8800 . 1 584 88 85 GLU CA C 56.2200 . 1 585 88 85 GLU CB C 30.0500 . 1 586 88 85 GLU CG C 34.6000 . 1 587 88 85 GLU N N 119.6000 . 1 588 89 86 ASN H H 7.3800 . 1 589 89 86 ASN HA H 4.9430 . 1 590 89 86 ASN HB2 H 2.8100 . 2 591 89 86 ASN HB3 H 2.6900 . 2 592 89 86 ASN HD21 H 6.6500 . 2 593 89 86 ASN HD22 H 7.5900 . 2 594 89 86 ASN C C 173.8700 . 1 595 89 86 ASN CA C 51.2700 . 1 596 89 86 ASN CB C 38.9100 . 1 597 89 86 ASN N N 119.8500 . 1 598 89 86 ASN ND2 N 111.8400 . 1 599 90 87 ILE H H 8.8000 . 1 600 90 87 ILE HA H 4.1400 . 1 601 90 87 ILE HB H 1.6700 . 1 602 90 87 ILE HD1 H 0.7600 . 1 603 90 87 ILE HG2 H 0.7100 . 1 604 90 87 ILE C C 175.5400 . 1 605 90 87 ILE CA C 63.5300 . 1 606 90 87 ILE CB C 37.7600 . 1 607 90 87 ILE CD1 C 13.1900 . 1 608 90 87 ILE CG1 C 26.9000 . 1 609 90 87 ILE CG2 C 17.7000 . 1 610 90 87 ILE N N 126.8700 . 1 611 91 88 ILE H H 9.0400 . 1 612 91 88 ILE HA H 4.2500 . 1 613 91 88 ILE HB H 1.7900 . 1 614 91 88 ILE HD1 H 0.5600 . 1 615 91 88 ILE HG12 H 1.0700 . 2 616 91 88 ILE HG13 H 1.0500 . 2 617 91 88 ILE HG2 H 0.7140 . 1 618 91 88 ILE C C 175.6400 . 1 619 91 88 ILE CA C 60.9800 . 1 620 91 88 ILE CB C 38.5400 . 1 621 91 88 ILE CD1 C 12.0400 . 1 622 91 88 ILE CG1 C 26.5000 . 1 623 91 88 ILE CG2 C 17.5000 . 1 624 91 88 ILE N N 126.6800 . 1 625 92 89 SER H H 7.8500 . 1 626 92 89 SER HA H 4.5000 . 1 627 92 89 SER HB2 H 3.7900 . 2 628 92 89 SER HB3 H 3.5900 . 2 629 92 89 SER C C 170.8000 . 1 630 92 89 SER CA C 57.9900 . 1 631 92 89 SER CB C 64.5900 . 1 632 92 89 SER N N 114.3300 . 1 633 93 90 LYS H H 8.4400 . 1 634 93 90 LYS HA H 4.7000 . 1 635 93 90 LYS HB2 H 1.7800 . 1 636 93 90 LYS HB3 H 1.6700 . 1 637 93 90 LYS HD2 H 1.2100 . 2 638 93 90 LYS HD3 H 1.1200 . 2 639 93 90 LYS HE2 H 2.8400 . 2 640 93 90 LYS HE3 H 2.7600 . 2 641 93 90 LYS HG2 H 1.3300 . 2 642 93 90 LYS HG3 H 1.2800 . 2 643 93 90 LYS C C 173.5600 . 1 644 93 90 LYS CA C 55.9800 . 1 645 93 90 LYS CB C 35.4600 . 1 646 93 90 LYS CD C 29.7700 . 1 647 93 90 LYS CE C 42.4600 . 1 648 93 90 LYS CG C 25.0800 . 1 649 93 90 LYS N N 121.2000 . 1 650 94 91 ASN H H 8.5100 . 1 651 94 91 ASN HA H 4.9900 . 1 652 94 91 ASN HB2 H 2.8600 . 2 653 94 91 ASN HB3 H 2.6200 . 2 654 94 91 ASN HD21 H 7.8000 . 2 655 94 91 ASN HD22 H 6.9100 . 2 656 94 91 ASN C C 175.2900 . 1 657 94 91 ASN CA C 51.1500 . 1 658 94 91 ASN CB C 38.7200 . 1 659 94 91 ASN N N 121.3800 . 1 660 94 91 ASN ND2 N 112.1900 . 1 661 95 92 THR H H 8.8200 . 1 662 95 92 THR HA H 4.1400 . 1 663 95 92 THR HB H 4.2300 . 1 664 95 92 THR HG2 H 1.2400 . 1 665 95 92 THR C C 175.9100 . 1 666 95 92 THR CA C 64.9600 . 1 667 95 92 THR CB C 68.6000 . 1 668 95 92 THR CG2 C 22.4000 . 1 669 95 92 THR N N 119.2300 . 1 670 96 93 ALA H H 8.3400 . 1 671 96 93 ALA HA H 4.1300 . 1 672 96 93 ALA HB H 1.4500 . 1 673 96 93 ALA C C 178.3700 . 1 674 96 93 ALA CA C 54.9300 . 1 675 96 93 ALA CB C 18.0700 . 1 676 96 93 ALA N N 125.8100 . 1 677 97 94 LYS H H 7.1200 . 1 678 97 94 LYS HA H 4.2800 . 1 679 97 94 LYS HB2 H 1.8300 . 2 680 97 94 LYS HB3 H 1.1100 . 2 681 97 94 LYS C C 174.2500 . 1 682 97 94 LYS CA C 54.9600 . 1 683 97 94 LYS CB C 33.2900 . 1 684 97 94 LYS CD C 29.0000 . 1 685 97 94 LYS CE C 41.9000 . 1 686 97 94 LYS CG C 25.4000 . 1 687 97 94 LYS N N 113.8500 . 1 688 98 95 ASP H H 7.9200 . 1 689 98 95 ASP HA H 4.2900 . 1 690 98 95 ASP HB2 H 3.1700 . 2 691 98 95 ASP HB3 H 2.2700 . 2 692 98 95 ASP C C 173.0300 . 1 693 98 95 ASP CA C 54.2200 . 1 694 98 95 ASP CB C 38.5500 . 1 695 98 95 ASP N N 120.4500 . 1 696 99 96 GLU H H 8.0500 . 1 697 99 96 GLU HA H 5.6400 . 1 698 99 96 GLU HB2 H 1.8100 . 1 699 99 96 GLU HB3 H 1.5600 . 1 700 99 96 GLU HG2 H 2.1800 . 2 701 99 96 GLU HG3 H 2.2100 . 2 702 99 96 GLU C C 176.6600 . 1 703 99 96 GLU CA C 53.9800 . 1 704 99 96 GLU CB C 35.4500 . 1 705 99 96 GLU CG C 36.5100 . 1 706 99 96 GLU N N 117.0700 . 1 707 100 97 ARG H H 8.4400 . 1 708 100 97 ARG HA H 5.1100 . 1 709 100 97 ARG HB2 H 1.8100 . 2 710 100 97 ARG C C 171.6700 . 1 711 100 97 ARG CA C 55.7000 . 1 712 100 97 ARG CB C 33.0100 . 1 713 100 97 ARG CG C 31.1000 . 1 714 100 97 ARG N N 118.2300 . 1 715 101 98 THR H H 8.8500 . 1 716 101 98 THR HA H 5.3800 . 1 717 101 98 THR HB H 3.7500 . 1 718 101 98 THR HG2 H 1.0100 . 1 719 101 98 THR C C 172.0200 . 1 720 101 98 THR CA C 61.5300 . 1 721 101 98 THR CB C 70.5200 . 1 722 101 98 THR CG2 C 21.3100 . 1 723 101 98 THR N N 117.7600 . 1 724 102 99 SER H H 9.4800 . 1 725 102 99 SER HA H 5.1400 . 1 726 102 99 SER HB2 H 3.6000 . 1 727 102 99 SER HB3 H 3.2800 . 1 728 102 99 SER C C 169.9600 . 1 729 102 99 SER CA C 57.4800 . 1 730 102 99 SER CB C 67.7000 . 1 731 102 99 SER N N 125.1700 . 1 732 103 100 GLU H H 9.2600 . 1 733 103 100 GLU HA H 5.6400 . 1 734 103 100 GLU HB2 H 1.9900 . 2 735 103 100 GLU HB3 H 1.7800 . 2 736 103 100 GLU HG2 H 2.1500 . 2 737 103 100 GLU HG3 H 2.0800 . 2 738 103 100 GLU C C 174.2500 . 1 739 103 100 GLU CA C 54.0500 . 1 740 103 100 GLU CB C 34.9500 . 1 741 103 100 GLU CG C 39.2900 . 1 742 103 100 GLU N N 124.2700 . 1 743 104 101 PHE H H 9.0800 . 1 744 104 101 PHE HA H 4.9500 . 1 745 104 101 PHE HB2 H 3.0300 . 1 746 104 101 PHE HB3 H 2.5800 . 1 747 104 101 PHE HD1 H 7.2400 . 3 748 104 101 PHE HE1 H 7.0800 . 3 749 104 101 PHE C C 173.3800 . 1 750 104 101 PHE CA C 56.1200 . 1 751 104 101 PHE CB C 42.5100 . 1 752 104 101 PHE CD1 C 133.5000 . 3 753 104 101 PHE CE1 C 130.5300 . 3 754 104 101 PHE N N 122.9800 . 1 755 105 102 GLU H H 8.2700 . 1 756 105 102 GLU HA H 4.2900 . 1 757 105 102 GLU HB2 H 1.5900 . 2 758 105 102 GLU HB3 H 1.1200 . 2 759 105 102 GLU C C 174.2500 . 1 760 105 102 GLU CA C 55.7400 . 1 761 105 102 GLU CB C 29.5400 . 1 762 105 102 GLU CG C 35.8100 . 1 763 105 102 GLU N N 126.6600 . 1 764 106 103 VAL H H 8.2100 . 1 765 106 103 VAL HA H 5.0400 . 1 766 106 103 VAL HB H 2.0400 . 1 767 106 103 VAL HG1 H 0.3400 . 2 768 106 103 VAL HG2 H 0.6700 . 2 769 106 103 VAL C C 175.6400 . 1 770 106 103 VAL CA C 59.1600 . 1 771 106 103 VAL CB C 37.1100 . 1 772 106 103 VAL CG1 C 19.0700 . 2 773 106 103 VAL CG2 C 23.1000 . 2 774 106 103 VAL N N 117.5200 . 1 775 107 104 SER H H 9.9400 . 1 776 107 104 SER HA H 4.0800 . 1 777 107 104 SER HB2 H 3.9500 . 2 778 107 104 SER HB3 H 3.8300 . 2 779 107 104 SER CA C 59.4900 . 1 780 107 104 SER CB C 62.9800 . 1 781 107 104 SER N N 115.9300 . 1 782 108 105 LYS H H 7.3000 . 1 783 108 105 LYS HA H 4.2300 . 1 784 108 105 LYS HB2 H 1.9500 . 2 785 108 105 LYS HB3 H 1.6300 . 2 786 108 105 LYS HD2 H 1.5700 . 2 787 108 105 LYS HE2 H 2.8400 . 2 788 108 105 LYS HE3 H 2.7700 . 2 789 108 105 LYS HG2 H 1.2300 . 2 790 108 105 LYS HG3 H 0.9200 . 2 791 108 105 LYS C C 170.9700 . 1 792 108 105 LYS CA C 54.9600 . 1 793 108 105 LYS CB C 33.8700 . 1 794 108 105 LYS CD C 29.4600 . 1 795 108 105 LYS CE C 42.5500 . 1 796 108 105 LYS CG C 22.3300 . 1 797 108 105 LYS N N 116.5300 . 1 798 109 106 LEU H H 8.0700 . 1 799 109 106 LEU HA H 4.2200 . 1 800 109 106 LEU HB2 H 1.3200 . 1 801 109 106 LEU HB3 H 1.1200 . 1 802 109 106 LEU HD1 H 0.1000 . 2 803 109 106 LEU HD2 H 0.2800 . 2 804 109 106 LEU HG H 1.1800 . 1 805 109 106 LEU C C 173.2100 . 1 806 109 106 LEU CA C 52.7200 . 1 807 109 106 LEU CB C 42.5100 . 1 808 109 106 LEU CD1 C 26.2000 . 2 809 109 106 LEU CD2 C 23.0300 . 2 810 109 106 LEU CG C 25.9000 . 1 811 109 106 LEU N N 112.6800 . 1 812 110 107 ASN H H 6.9500 . 1 813 110 107 ASN HA H 4.7600 . 1 814 110 107 ASN HB2 H 2.4000 . 2 815 110 107 ASN HB3 H 2.1900 . 2 816 110 107 ASN HD21 H 7.0500 . 2 817 110 107 ASN HD22 H 8.2000 . 2 818 110 107 ASN C C 172.6900 . 1 819 110 107 ASN CA C 52.4500 . 1 820 110 107 ASN CB C 41.5400 . 1 821 110 107 ASN N N 116.1700 . 1 822 110 107 ASN ND2 N 114.3700 . 1 823 111 108 GLY H H 8.6600 . 1 824 111 108 GLY HA2 H 4.4200 . 2 825 111 108 GLY HA3 H 3.7500 . 2 826 111 108 GLY C C 170.8000 . 1 827 111 108 GLY CA C 43.6400 . 1 828 111 108 GLY N N 112.4700 . 1 829 112 109 LYS H H 8.3000 . 1 830 112 109 LYS HA H 5.3800 . 1 831 112 109 LYS HB2 H 1.6200 . 2 832 112 109 LYS HB3 H 1.5400 . 2 833 112 109 LYS HE2 H 2.8500 . 2 834 112 109 LYS HE3 H 2.7600 . 2 835 112 109 LYS HG2 H 1.0200 . 2 836 112 109 LYS C C 175.6400 . 1 837 112 109 LYS CA C 55.4200 . 1 838 112 109 LYS CB C 33.8400 . 1 839 112 109 LYS CD C 29.7700 . 1 840 112 109 LYS CE C 42.4700 . 1 841 112 109 LYS CG C 26.2000 . 1 842 112 109 LYS N N 119.3800 . 1 843 113 110 ILE H H 9.0900 . 1 844 113 110 ILE HA H 4.3400 . 1 845 113 110 ILE HB H 1.5300 . 1 846 113 110 ILE HD1 H 0.6900 . 1 847 113 110 ILE HG12 H 1.2500 . 2 848 113 110 ILE HG13 H 0.8500 . 2 849 113 110 ILE HG2 H 0.9300 . 1 850 113 110 ILE C C 173.2100 . 1 851 113 110 ILE CA C 60.4700 . 1 852 113 110 ILE CB C 42.0000 . 1 853 113 110 ILE CD1 C 13.7300 . 1 854 113 110 ILE CG1 C 26.4900 . 1 855 113 110 ILE CG2 C 18.9200 . 1 856 113 110 ILE N N 124.0600 . 1 857 114 111 ASP H H 8.9000 . 1 858 114 111 ASP HA H 5.5400 . 1 859 114 111 ASP HB2 H 3.1300 . 1 860 114 111 ASP HB3 H 2.7500 . 1 861 114 111 ASP C C 174.9400 . 1 862 114 111 ASP CA C 55.2000 . 1 863 114 111 ASP CB C 42.9400 . 1 864 114 111 ASP N N 127.2200 . 1 865 115 112 GLY H H 9.1600 . 1 866 115 112 GLY HA2 H 5.2200 . 2 867 115 112 GLY HA3 H 4.2300 . 2 868 115 112 GLY C C 171.8300 . 1 869 115 112 GLY CA C 45.9000 . 1 870 115 112 GLY N N 106.0900 . 1 871 116 113 LYS H H 8.5800 . 1 872 116 113 LYS HA H 5.5400 . 1 873 116 113 LYS HB2 H 1.8600 . 1 874 116 113 LYS HB3 H 1.6500 . 1 875 116 113 LYS C C 175.4700 . 1 876 116 113 LYS CA C 55.2300 . 1 877 116 113 LYS CB C 37.6600 . 1 878 116 113 LYS CE C 42.7000 . 1 879 116 113 LYS N N 119.1200 . 1 880 117 114 ILE H H 9.3500 . 1 881 117 114 ILE HA H 5.2000 . 1 882 117 114 ILE HB H 2.0000 . 1 883 117 114 ILE HD1 H 1.7400 . 1 884 117 114 ILE HG12 H 1.4600 . 2 885 117 114 ILE HG13 H 2.2300 . 2 886 117 114 ILE HG2 H 1.5300 . 1 887 117 114 ILE C C 169.9300 . 1 888 117 114 ILE CA C 60.5200 . 1 889 117 114 ILE CB C 44.1200 . 1 890 117 114 ILE CD1 C 16.4700 . 1 891 117 114 ILE CG1 C 29.4100 . 1 892 117 114 ILE CG2 C 17.6000 . 1 893 117 114 ILE N N 121.8500 . 1 894 118 115 ASP H H 8.6200 . 1 895 118 115 ASP HA H 5.1100 . 1 896 118 115 ASP HB2 H 2.5000 . 2 897 118 115 ASP HB3 H 2.2700 . 2 898 118 115 ASP C C 172.8600 . 1 899 118 115 ASP CA C 53.2600 . 1 900 118 115 ASP CB C 44.0000 . 1 901 118 115 ASP N N 127.1100 . 1 902 119 116 VAL HA H 4.9100 . 1 903 119 116 VAL HB H 0.7100 . 1 904 119 116 VAL HG1 H 0.2100 . 2 905 119 116 VAL HG2 H 0.5300 . 2 906 119 116 VAL CA C 60.2200 . 1 907 119 116 VAL CB C 34.7500 . 1 908 119 116 VAL CG1 C 21.1000 . 2 909 119 116 VAL CG2 C 20.5800 . 2 910 120 117 TYR H H 9.2300 . 1 911 120 117 TYR HA H 4.9400 . 1 912 120 117 TYR HB2 H 2.7100 . 2 913 120 117 TYR HB3 H 2.5700 . 2 914 120 117 TYR HD1 H 6.7700 . 3 915 120 117 TYR HE1 H 6.6000 . 3 916 120 117 TYR C C 171.8400 . 1 917 120 117 TYR CA C 57.4800 . 1 918 120 117 TYR CB C 41.9300 . 1 919 120 117 TYR CD1 C 133.0200 . 3 920 120 117 TYR CE1 C 118.0000 . 3 921 120 117 TYR N N 130.3600 . 1 922 121 118 ILE H H 8.5700 . 1 923 121 118 ILE HA H 3.7100 . 1 924 121 118 ILE HB H 0.9200 . 1 925 121 118 ILE HD1 H -0.3000 . 1 926 121 118 ILE HG12 H 0.7100 . 2 927 121 118 ILE HG13 H -0.6400 . 2 928 121 118 ILE HG2 H 0.4300 . 1 929 121 118 ILE C C 172.8800 . 1 930 121 118 ILE CA C 59.9600 . 1 931 121 118 ILE CB C 41.4600 . 1 932 121 118 ILE CD1 C 13.8900 . 1 933 121 118 ILE CG1 C 24.9200 . 1 934 121 118 ILE CG2 C 16.8500 . 1 935 121 118 ILE N N 128.2800 . 1 936 122 119 ASP H H 9.1400 . 1 937 122 119 ASP HA H 5.0200 . 1 938 122 119 ASP HB2 H 2.6300 . 1 939 122 119 ASP HB3 H 2.1000 . 1 940 122 119 ASP C C 173.3800 . 1 941 122 119 ASP CA C 53.3000 . 1 942 122 119 ASP CB C 40.5000 . 1 943 122 119 ASP N N 127.1500 . 1 944 123 120 GLU H H 8.1400 . 1 945 123 120 GLU HA H 4.7600 . 1 946 123 120 GLU HB2 H 2.5800 . 1 947 123 120 GLU HB3 H 2.2200 . 1 948 123 120 GLU HG2 H 2.2600 . 2 949 123 120 GLU C C 173.3800 . 1 950 123 120 GLU CA C 54.5900 . 1 951 123 120 GLU CB C 31.1700 . 1 952 123 120 GLU CG C 34.5200 . 1 953 123 120 GLU N N 117.7100 . 1 954 124 121 LYS H H 8.4600 . 1 955 124 121 LYS HA H 4.5500 . 1 956 124 121 LYS HB2 H 1.7900 . 2 957 124 121 LYS HB3 H 1.3400 . 2 958 124 121 LYS HE2 H 2.8700 . 2 959 124 121 LYS HG2 H 1.4600 . 2 960 124 121 LYS HG3 H 0.9500 . 2 961 124 121 LYS C C 175.6600 . 1 962 124 121 LYS CA C 56.9700 . 1 963 124 121 LYS CB C 32.7800 . 1 964 124 121 LYS CE C 41.8000 . 1 965 124 121 LYS CG C 26.2800 . 1 966 124 121 LYS N N 118.6100 . 1 967 125 122 VAL H H 8.9200 . 1 968 125 122 VAL HA H 4.3500 . 1 969 125 122 VAL HB H 1.8500 . 1 970 125 122 VAL HG1 H 1.0600 . 2 971 125 122 VAL HG2 H 1.1800 . 2 972 125 122 VAL C C 175.5900 . 1 973 125 122 VAL CA C 61.8500 . 1 974 125 122 VAL CB C 34.3500 . 1 975 125 122 VAL CG1 C 21.2000 . 2 976 125 122 VAL CG2 C 21.7000 . 2 977 125 122 VAL N N 126.1200 . 1 978 126 123 ASN H H 9.7900 . 1 979 126 123 ASN HA H 4.4300 . 1 980 126 123 ASN HB2 H 3.1300 . 2 981 126 123 ASN HB3 H 2.8500 . 2 982 126 123 ASN HD21 H 7.5900 . 2 983 126 123 ASN HD22 H 6.9700 . 2 984 126 123 ASN C C 174.6200 . 1 985 126 123 ASN CA C 54.4100 . 1 986 126 123 ASN CB C 37.1100 . 1 987 126 123 ASN N N 127.6400 . 1 988 126 123 ASN ND2 N 113.2400 . 1 989 127 124 GLY H H 8.7000 . 1 990 127 124 GLY HA2 H 4.2300 . 2 991 127 124 GLY HA3 H 3.5900 . 2 992 127 124 GLY C C 172.6700 . 1 993 127 124 GLY CA C 45.2400 . 1 994 127 124 GLY N N 102.1600 . 1 995 128 125 LYS H H 7.6500 . 1 996 128 125 LYS HA H 5.0000 . 1 997 128 125 LYS HB2 H 1.8700 . 2 998 128 125 LYS HB3 H 1.7500 . 2 999 128 125 LYS HE2 H 3.0400 . 2 1000 128 125 LYS HG2 H 1.4600 . 2 1001 128 125 LYS HG3 H 1.4200 . 2 1002 128 125 LYS C C 172.3400 . 1 1003 128 125 LYS CA C 52.9200 . 1 1004 128 125 LYS CB C 34.3700 . 1 1005 128 125 LYS CE C 41.8000 . 1 1006 128 125 LYS CG C 24.4100 . 1 1007 128 125 LYS N N 120.7900 . 1 1008 129 126 PRO HA H 4.1100 . 1 1009 129 126 PRO HB2 H 2.1600 . 2 1010 129 126 PRO HB3 H 1.8500 . 2 1011 129 126 PRO HD2 H 3.8500 . 2 1012 129 126 PRO HD3 H 3.6700 . 2 1013 129 126 PRO HG2 H 2.1500 . 2 1014 129 126 PRO HG3 H 1.8900 . 2 1015 129 126 PRO CA C 64.3300 . 1 1016 129 126 PRO CB C 32.0200 . 1 1017 129 126 PRO CD C 51.0600 . 1 1018 129 126 PRO CG C 27.2900 . 1 1019 130 127 PHE H H 8.4600 . 1 1020 130 127 PHE HA H 4.7900 . 1 1021 130 127 PHE HB2 H 3.1200 . 2 1022 130 127 PHE HB3 H 3.0200 . 2 1023 130 127 PHE HD1 H 7.0800 . 3 1024 130 127 PHE C C 171.3500 . 1 1025 130 127 PHE CA C 57.2100 . 1 1026 130 127 PHE CB C 42.3300 . 1 1027 130 127 PHE CD1 C 131.0200 . 3 1028 130 127 PHE N N 127.7500 . 1 1029 131 128 LYS H H 7.3700 . 1 1030 131 128 LYS HA H 4.7500 . 1 1031 131 128 LYS HB2 H 1.3300 . 2 1032 131 128 LYS HB3 H 1.1800 . 2 1033 131 128 LYS HE2 H 2.7300 . 2 1034 131 128 LYS HE3 H 2.6000 . 2 1035 131 128 LYS HG2 H 0.9900 . 2 1036 131 128 LYS HG3 H 0.8800 . 2 1037 131 128 LYS C C 173.0300 . 1 1038 131 128 LYS CA C 53.7000 . 1 1039 131 128 LYS CB C 34.3600 . 1 1040 131 128 LYS CD C 28.0200 . 1 1041 131 128 LYS CE C 42.2000 . 1 1042 131 128 LYS CG C 24.9000 . 1 1043 131 128 LYS N N 127.4400 . 1 1044 132 129 TYR H H 8.2700 . 1 1045 132 129 TYR HA H 3.4200 . 1 1046 132 129 TYR HB2 H 1.6300 . 1 1047 132 129 TYR HB3 H 1.4300 . 1 1048 132 129 TYR HD1 H 7.0100 . 3 1049 132 129 TYR HD2 H 7.0100 . 3 1050 132 129 TYR C C 170.6500 . 1 1051 132 129 TYR CA C 56.5400 . 1 1052 132 129 TYR CB C 42.3500 . 1 1053 132 129 TYR N N 128.8600 . 1 1054 133 130 ASP H H 7.1000 . 1 1055 133 130 ASP HA H 4.4900 . 1 1056 133 130 ASP HB2 H 2.0200 . 2 1057 133 130 ASP HB3 H 1.8600 . 2 1058 133 130 ASP C C 172.8600 . 1 1059 133 130 ASP CA C 51.5500 . 1 1060 133 130 ASP CB C 41.2300 . 1 1061 133 130 ASP N N 127.9700 . 1 1062 134 131 HIS H H 7.5300 . 1 1063 134 131 HIS HA H 3.7400 . 1 1064 134 131 HIS HB2 H 0.8300 . 2 1065 134 131 HIS HB3 H 0.3600 . 2 1066 134 131 HIS C C 169.7600 . 1 1067 134 131 HIS CA C 53.5000 . 1 1068 134 131 HIS CB C 34.8100 . 1 1069 134 131 HIS N N 118.3700 . 1 1070 135 132 HIS H H 7.4500 . 1 1071 135 132 HIS HA H 4.8700 . 1 1072 135 132 HIS HB2 H 2.8900 . 2 1073 135 132 HIS HB3 H 2.7400 . 2 1074 135 132 HIS C C 172.5100 . 1 1075 135 132 HIS CA C 53.8100 . 1 1076 135 132 HIS CB C 29.5800 . 1 1077 135 132 HIS N N 119.1400 . 1 1078 136 133 TYR H H 8.9500 . 1 1079 136 133 TYR HA H 5.0800 . 1 1080 136 133 TYR HB2 H 3.6900 . 1 1081 136 133 TYR HB3 H 2.6300 . 1 1082 136 133 TYR HD1 H 6.8800 . 3 1083 136 133 TYR HD2 H 6.8800 . 3 1084 136 133 TYR C C 175.1400 . 1 1085 136 133 TYR CA C 56.9700 . 1 1086 136 133 TYR CB C 44.0900 . 1 1087 136 133 TYR N N 120.8000 . 1 1088 137 134 ASN H H 9.0200 . 1 1089 137 134 ASN HA H 5.4100 . 1 1090 137 134 ASN HB2 H 1.9600 . 1 1091 137 134 ASN HB3 H 1.8000 . 1 1092 137 134 ASN HD21 H 6.9200 . 2 1093 137 134 ASN HD22 H 6.6700 . 2 1094 137 134 ASN C C 173.3800 . 1 1095 137 134 ASN CA C 52.7500 . 1 1096 137 134 ASN CB C 40.0900 . 1 1097 137 134 ASN N N 119.7500 . 1 1098 137 134 ASN ND2 N 113.9800 . 1 1099 138 135 ILE H H 8.6300 . 1 1100 138 135 ILE HA H 4.7900 . 1 1101 138 135 ILE HB H 1.7100 . 1 1102 138 135 ILE HD1 H 0.7200 . 1 1103 138 135 ILE HG2 H 1.1900 . 1 1104 138 135 ILE C C 172.3400 . 1 1105 138 135 ILE CA C 61.3600 . 1 1106 138 135 ILE CB C 43.5900 . 1 1107 138 135 ILE CD1 C 14.1000 . 1 1108 138 135 ILE CG1 C 25.3800 . 1 1109 138 135 ILE CG2 C 20.7500 . 1 1110 138 135 ILE N N 115.7600 . 1 1111 139 136 THR H H 8.5100 . 1 1112 139 136 THR HA H 5.0300 . 1 1113 139 136 THR HB H 3.7200 . 1 1114 139 136 THR HG2 H 1.1900 . 1 1115 139 136 THR C C 171.3000 . 1 1116 139 136 THR CA C 62.7700 . 1 1117 139 136 THR CB C 72.4400 . 1 1118 139 136 THR CG2 C 22.3000 . 1 1119 139 136 THR N N 118.6100 . 1 1120 140 137 TYR H H 9.6200 . 1 1121 140 137 TYR HA H 4.2900 . 1 1122 140 137 TYR HB2 H 2.6200 . 1 1123 140 137 TYR HB3 H 1.6500 . 1 1124 140 137 TYR HD1 H 6.6200 . 3 1125 140 137 TYR HD2 H 6.6200 . 3 1126 140 137 TYR HE1 H 6.3200 . 3 1127 140 137 TYR C C 173.5800 . 1 1128 140 137 TYR CA C 57.9900 . 1 1129 140 137 TYR CB C 40.4000 . 1 1130 140 137 TYR CD1 C 132.0900 . 3 1131 140 137 TYR CE1 C 117.4800 . 3 1132 140 137 TYR N N 127.1700 . 1 1133 141 138 LYS H H 8.6000 . 1 1134 141 138 LYS HA H 4.5700 . 1 1135 141 138 LYS HB2 H 1.4100 . 2 1136 141 138 LYS HB3 H 0.7700 . 2 1137 141 138 LYS HE2 H 2.8700 . 2 1138 141 138 LYS HG2 H 1.1100 . 2 1139 141 138 LYS HG3 H 0.9600 . 2 1140 141 138 LYS C C 174.3300 . 1 1141 141 138 LYS CA C 54.5100 . 1 1142 141 138 LYS CB C 34.0200 . 1 1143 141 138 LYS CE C 42.0000 . 1 1144 141 138 LYS CG C 25.0900 . 1 1145 141 138 LYS N N 122.3100 . 1 1146 142 139 PHE H H 8.7600 . 1 1147 142 139 PHE HA H 4.8800 . 1 1148 142 139 PHE HB2 H 3.1600 . 1 1149 142 139 PHE HB3 H 2.6500 . 1 1150 142 139 PHE HD1 H 6.9700 . 3 1151 142 139 PHE HE1 H 6.6000 . 3 1152 142 139 PHE C C 175.2900 . 1 1153 142 139 PHE CA C 56.1200 . 1 1154 142 139 PHE CB C 39.7700 . 1 1155 142 139 PHE CD1 C 130.6800 . 3 1156 142 139 PHE CE1 C 130.8400 . 3 1157 142 139 PHE N N 125.2600 . 1 1158 143 140 ASN H H 8.7400 . 1 1159 143 140 ASN HA H 5.3700 . 1 1160 143 140 ASN HB2 H 3.0100 . 1 1161 143 140 ASN HB3 H 2.4700 . 1 1162 143 140 ASN HD21 H 7.1000 . 2 1163 143 140 ASN HD22 H 6.8400 . 2 1164 143 140 ASN C C 174.3000 . 1 1165 143 140 ASN CA C 51.9500 . 1 1166 143 140 ASN CB C 38.7600 . 1 1167 143 140 ASN N N 123.9000 . 1 1168 143 140 ASN ND2 N 111.9400 . 1 1169 144 141 GLY H H 7.9500 . 1 1170 144 141 GLY HA2 H 4.4600 . 2 1171 144 141 GLY HA3 H 3.6400 . 2 1172 144 141 GLY C C 169.7600 . 1 1173 144 141 GLY CA C 45.0900 . 1 1174 144 141 GLY N N 108.9400 . 1 1175 145 142 PRO HA H 4.3300 . 1 1176 145 142 PRO HB2 H 2.2000 . 2 1177 145 142 PRO HB3 H 1.8100 . 2 1178 145 142 PRO HD2 H 3.7500 . 2 1179 145 142 PRO HD3 H 3.6000 . 2 1180 145 142 PRO HG2 H 1.9600 . 2 1181 145 142 PRO HG3 H 1.8800 . 2 1182 145 142 PRO CA C 63.0000 . 1 1183 145 142 PRO CB C 32.0100 . 1 1184 145 142 PRO CD C 50.8900 . 1 1185 145 142 PRO CG C 27.5400 . 1 1186 146 143 THR H H 8.1900 . 1 1187 146 143 THR HA H 4.0900 . 1 1188 146 143 THR HB H 4.2000 . 1 1189 146 143 THR HG2 H 1.0900 . 1 1190 146 143 THR C C 173.3800 . 1 1191 146 143 THR CA C 61.6400 . 1 1192 146 143 THR CB C 69.5000 . 1 1193 146 143 THR CG2 C 21.4400 . 1 1194 146 143 THR N N 112.3700 . 1 1195 147 144 ASP H H 8.2300 . 1 1196 147 144 ASP HA H 4.5800 . 1 1197 147 144 ASP HB2 H 2.5700 . 2 1198 147 144 ASP HB3 H 2.5200 . 2 1199 147 144 ASP C C 174.7200 . 1 1200 147 144 ASP CA C 53.9700 . 1 1201 147 144 ASP CB C 41.1800 . 1 1202 147 144 ASP N N 121.6900 . 1 1203 148 145 VAL H H 7.8600 . 1 1204 148 145 VAL HA H 4.0900 . 1 1205 148 145 VAL HB H 1.9800 . 1 1206 148 145 VAL HG1 H 0.7800 . 2 1207 148 145 VAL HG2 H 0.8000 . 2 1208 148 145 VAL C C 174.2500 . 1 1209 148 145 VAL CA C 61.4300 . 1 1210 148 145 VAL CB C 32.5000 . 1 1211 148 145 VAL CG1 C 20.0500 . 2 1212 148 145 VAL CG2 C 21.6000 . 2 1213 148 145 VAL N N 118.8000 . 1 1214 149 146 ALA H H 8.2600 . 1 1215 149 146 ALA HA H 4.4000 . 1 1216 149 146 ALA HB H 1.4200 . 1 1217 149 146 ALA C C 175.7900 . 1 1218 149 146 ALA CA C 52.4300 . 1 1219 149 146 ALA CB C 19.4700 . 1 1220 149 146 ALA N N 127.7300 . 1 1221 150 147 GLY H H 7.9100 . 1 1222 150 147 GLY HA2 H 3.6500 . 2 1223 150 147 GLY C C 177.8700 . 1 1224 150 147 GLY CA C 45.8000 . 1 1225 150 147 GLY N N 114.6000 . 1 stop_ save_ save_assigned_chem_shift_list_1_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D CBCA(CO)NH' '3D HNCACB' '3D HNHA' '3D HCCH-COSY' '3D HCCH-TOCSY' '3D HNCO' '3D HNHB' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name ZNH _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 1 148 . ZNH HAB H 7.8800 . 9 2 148 . ZNH HAC H 8.4900 . 9 3 148 . ZNH HBC1 H 6.0000 . 9 4 148 . ZNH HHA H 10.0000 . 9 5 148 . ZNH HHC H 9.7800 . 9 6 148 . ZNH HHD H 9.7700 . 9 7 148 . ZNH HMC1 H 2.9600 . 9 8 148 . ZNH HMC3 H 2.9600 . 9 9 148 . ZNH HMD1 H 3.1100 . 9 10 148 . ZNH HMD2 H 3.1100 . 9 11 148 . ZNH HMD3 H 3.1100 . 9 stop_ save_