data_5828 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone and sidechain heteronuclear resonance assignments and hyperfine nuclear magnetic resonance shifts in horse cytochrome c ; _BMRB_accession_number 5828 _BMRB_flat_file_name bmr5828.str _Entry_type original _Submission_date 2003-06-10 _Accession_date 2003-06-11 _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 Liu Weixia . . 2 Rumbley Jon . . 3 Englander S. Walter . 4 Wand A. Joshua . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 442 "13C chemical shifts" 418 "15N chemical shifts" 97 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-09-28 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5827 'cytochrome c reduced state of H26N, H33N mutant' 5829 'cytochrome c reduced state of wild type' 5830 'cytochrome c oxidized state of wild type' stop_ _Original_release_date 2003-09-28 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone and Side-chain Heteronuclear Resonance Assignments and Hyperfine NMR Shifts in Horse Cytochrome c ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22812282 _PubMed_ID 12931009 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liu Weixia . . 2 Rumbley Jon . . 3 Englander S. Walter . 4 Wand A. Joshua . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_volume 12 _Journal_issue 9 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2104 _Page_last 2108 _Year 2003 _Details . save_ ################################## # Molecular system description # ################################## save_system_cyt_c _Saveframe_category molecular_system _Mol_system_name 'Horse cytochrome c' _Abbreviation_common 'cyt c' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'cytochrome c' $cyt_c heme $HEM stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic yes _System_thiol_state 'not reported' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cyt_c _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Horse cytochrome c' _Name_variant 'H26N, H33N' _Abbreviation_common 'cyt c' _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 104 _Mol_residue_sequence ; GDVEKGKKIFVQKCAQCHTV EKGGKNKTGPNLNGLFGRKT GQAPGFTYTDANKNKGITWK EETLMEYLENPKKYIPGTKM IFAGIKKKTEREDLIAYLKK ATNE ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ASP 3 VAL 4 GLU 5 LYS 6 GLY 7 LYS 8 LYS 9 ILE 10 PHE 11 VAL 12 GLN 13 LYS 14 CYS 15 ALA 16 GLN 17 CYS 18 HIS 19 THR 20 VAL 21 GLU 22 LYS 23 GLY 24 GLY 25 LYS 26 ASN 27 LYS 28 THR 29 GLY 30 PRO 31 ASN 32 LEU 33 ASN 34 GLY 35 LEU 36 PHE 37 GLY 38 ARG 39 LYS 40 THR 41 GLY 42 GLN 43 ALA 44 PRO 45 GLY 46 PHE 47 THR 48 TYR 49 THR 50 ASP 51 ALA 52 ASN 53 LYS 54 ASN 55 LYS 56 GLY 57 ILE 58 THR 59 TRP 60 LYS 61 GLU 62 GLU 63 THR 64 LEU 65 MET 66 GLU 67 TYR 68 LEU 69 GLU 70 ASN 71 PRO 72 LYS 73 LYS 74 TYR 75 ILE 76 PRO 77 GLY 78 THR 79 LYS 80 MET 81 ILE 82 PHE 83 ALA 84 GLY 85 ILE 86 LYS 87 LYS 88 LYS 89 THR 90 GLU 91 ARG 92 GLU 93 ASP 94 LEU 95 ILE 96 ALA 97 TYR 98 LEU 99 LYS 100 LYS 101 ALA 102 THR 103 ASN 104 GLU stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PRF 610169A 'cytochrome c' 100.00 104 98.08 100.00 2.67e-52 SWISS-PROT P00004 'Cytochrome c' 100.00 105 98.08 100.00 2.92e-52 PDB 2GIW 'Solution Structure Of Reduced Horse Heart Cytochrome C, Nmr, 40 Structures' 100.00 104 98.08 100.00 2.67e-52 PDB 2PCB 'Crystal Structure Of A Complex Between Electron Transfer Partners, Cytochrome C Peroxidase And Cytochrome C' 100.00 104 98.08 100.00 2.67e-52 PDB 1WEJ 'Igg1 Fab Fragment (Of E8 Antibody) Complexed With Horse Cytochrome C At 1.8 A Resolution' 100.00 104 98.08 100.00 2.67e-52 PDB 2FRC 'Cytochrome C (Reduced) From Equus Caballus, Nmr, Minimized Average Structure' 100.00 104 98.08 100.00 2.67e-52 PDB 1OCD 'Cytochrome C (Oxidized) From Equus Caballus, Nmr, Minimized Average Structure' 100.00 104 98.08 100.00 2.67e-52 PDB 1U75 'Electron Transfer Complex Between Horse Heart Cytochrome C And Zinc-Porphyrin Substituted Cytochrome C Peroxidase' 100.00 104 98.08 100.00 2.67e-52 PDB 1LC2 'Solution Structure Of Reduced Horse Heart Cytochrome C In 30% Acetonitrile Solution, Nmr 30 Structures' 100.00 104 98.08 100.00 2.67e-52 PDB 1M60 'Solution Structure Of Zinc-Substituted Cytochrome C' 100.00 104 98.08 100.00 2.67e-52 PDB 1I5T 'Solution Structure Of Cyanoferricytochrome C' 100.00 104 98.08 100.00 2.67e-52 PDB 1LC1 'Solution Structure Of Reduced Horse Heart Cytochrome C In 30% Acetonitrile Solution, Nmr Minimized Average Structure' 100.00 104 98.08 100.00 2.67e-52 PDB 1GIW 'Solution Structure Of Reduced Horse Heart Cytochrome C, Nmr, Minimized Average Structure' 99.04 104 98.06 100.00 9.17e-52 PDB 1HRC 'High-Resolution Three-Dimensional Structure Of Horse Heart Cytochrome C' 100.00 104 98.08 100.00 2.67e-52 PDB 1FI7 'Solution Structure Of The Imidazole Complex Of Cytochrome C' 100.00 104 98.08 100.00 2.67e-52 PDB 1FI9 'Solution Structure Of The Imidazole Complex Of Cytochrome C' 100.00 104 98.08 100.00 2.67e-52 PDB 1AKK 'Solution Structure Of Oxidized Horse Heart Cytochrome C, Nmr, Minimized Average Structure' 100.00 104 98.08 100.00 2.67e-52 PDB 1CRC 'Cytochrome C At Low Ionic Strength' 100.00 104 98.08 100.00 2.67e-52 BMRB 5829 'Horse cytochrome c' 100.00 104 98.08 100.00 2.67e-52 BMRB 5830 'Horse cytochrome c' 100.00 104 98.08 100.00 2.67e-52 BMRB 5660 'oxidized cytochrome c' 100.00 104 98.08 100.00 2.67e-52 BMRB 5827 'Horse cytochrome c' 100.00 104 100.00 100.00 3.28e-53 BMRB 5026 'cytochrome C' 100.00 104 98.08 100.00 2.67e-52 BMRB 5372 'cytochrome c' 100.00 104 98.08 100.00 2.67e-52 BMRB 4809 'cytochrome c' 100.00 104 98.08 100.00 2.67e-52 BMRB 4810 'ferric cytochrome c' 100.00 104 98.08 100.00 2.67e-52 BMRB 4805 'cytochrome c' 100.00 104 98.08 100.00 2.67e-52 BMRB 4808 'cytochrome c' 100.00 104 98.08 100.00 2.67e-52 BMRB 274 'cytochrome c' 100.00 104 98.08 100.00 2.67e-52 BMRB 4189 'cytochrome c' 100.00 104 98.08 100.00 2.67e-52 BMRB 243 'cytochrome c' 100.00 104 98.08 100.00 2.67e-52 BMRB 244 'cytochrome c' 100.00 104 98.08 100.00 2.67e-52 stop_ save_ ############# # Ligands # ############# save_HEM _Saveframe_category ligand _Mol_type non-polymer _Name_common "HEM (PROTOPORPHYRIN IX CONTAINING FE)" _BMRB_code . _PDB_code HEM _Molecular_mass 616.487 _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 Jun 10 14:10:54 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CHA CHA C . 0 . ? CHB CHB C . 0 . ? CHC CHC C . 0 . ? CHD CHD C . 0 . ? C1A C1A C . 0 . ? C2A C2A C . 0 . ? C3A C3A C . 0 . ? C4A C4A C . 0 . ? CMA CMA C . 0 . ? CAA CAA C . 0 . ? CBA CBA C . 0 . ? CGA CGA C . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? C1B C1B C . 0 . ? C2B C2B C . 0 . ? C3B C3B C . 0 . ? C4B C4B C . 0 . ? CMB CMB C . 0 . ? CAB CAB C . 0 . ? CBB CBB C . 0 . ? C1C C1C C . 0 . ? C2C C2C C . 0 . ? C3C C3C C . 0 . ? C4C C4C C . 0 . ? CMC CMC C . 0 . ? CAC CAC C . 0 . ? CBC CBC C . 0 . ? C1D C1D C . 0 . ? C2D C2D C . 0 . ? C3D C3D C . 0 . ? C4D C4D C . 0 . ? CMD CMD C . 0 . ? CAD CAD C . 0 . ? CBD CBD C . 0 . ? CGD CGD C . 0 . ? O1D O1D O . 0 . ? O2D O2D O . 0 . ? NA NA N . 0 . ? NB NB N . 0 . ? NC NC N . 0 . ? ND ND N . 0 . ? FE FE FE . 0 . ? HHB HHB H . 0 . ? HHC HHC H . 0 . ? HHD HHD H . 0 . ? HMA HMA H . 0 . ? HMAA HMAA H . 0 . ? HMAB HMAB H . 0 . ? HAA HAA H . 0 . ? HAAA HAAA H . 0 . ? HBA HBA H . 0 . ? HBAA HBAA H . 0 . ? HMB HMB H . 0 . ? HMBA HMBA H . 0 . ? HMBB HMBB H . 0 . ? HAB HAB H . 0 . ? HBB HBB H . 0 . ? HBBA HBBA H . 0 . ? HMC HMC H . 0 . ? HMCA HMCA H . 0 . ? HMCB HMCB H . 0 . ? HAC HAC H . 0 . ? HBC HBC H . 0 . ? HBCA HBCA H . 0 . ? HMD HMD H . 0 . ? HMDA HMDA H . 0 . ? HMDB HMDB H . 0 . ? HAD HAD H . 0 . ? HADA HADA H . 0 . ? HBD HBD H . 0 . ? HBDA HBDA H . 0 . ? H2A H2A H . 0 . ? H2D H2D H . 0 . ? HHA HHA H . 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 CHA C1A ? ? DOUB CHA C4D ? ? SING CHA HHA ? ? SING CHB C4A ? ? DOUB CHB C1B ? ? SING CHB HHB ? ? SING CHC C4B ? ? DOUB CHC C1C ? ? SING CHC HHC ? ? DOUB CHD C4C ? ? SING CHD C1D ? ? SING CHD HHD ? ? DOUB C1A C2A ? ? SING C1A NA ? ? SING C2A C3A ? ? SING C2A CAA ? ? DOUB C3A C4A ? ? SING C3A CMA ? ? SING C4A NA ? ? SING CMA HMA ? ? SING CMA HMAA ? ? SING CMA HMAB ? ? SING CAA CBA ? ? SING CAA HAA ? ? SING CAA HAAA ? ? SING CBA CGA ? ? SING CBA HBA ? ? SING CBA HBAA ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING C1B C2B ? ? SING C1B NB ? ? DOUB C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? SING C3B CAB ? ? DOUB C4B NB ? ? SING CMB HMB ? ? SING CMB HMBA ? ? SING CMB HMBB ? ? DOUB CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB ? ? SING CBB HBBA ? ? SING C1C C2C ? ? SING C1C NC ? ? DOUB C2C C3C ? ? SING C2C CMC ? ? SING C3C C4C ? ? SING C3C CAC ? ? SING C4C NC ? ? SING CMC HMC ? ? SING CMC HMCA ? ? SING CMC HMCB ? ? DOUB CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC ? ? SING CBC HBCA ? ? SING C1D C2D ? ? DOUB C1D ND ? ? DOUB C2D C3D ? ? SING C2D CMD ? ? SING C3D C4D ? ? SING C3D CAD ? ? SING C4D ND ? ? SING CMD HMD ? ? SING CMD HMDA ? ? SING CMD HMDB ? ? SING CAD CBD ? ? SING CAD HAD ? ? SING CAD HADA ? ? SING CBD CGD ? ? SING CBD HBD ? ? SING CBD HBDA ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2A H2A ? ? SING O2D H2D ? ? SING FE NA ? ? SING FE NB ? ? SING FE NC ? ? SING FE ND ? ? 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 $cyt_c 9796 Horse Eukaryota Metazoa Equus caballus 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 $cyt_c 'recombinant technology' . . . . . 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 $cyt_c 1.0 mM '[U-15N; U-13C]' stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 98 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_(H)CC(CO)NH_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (H)CC(CO)NH_TOCSY' _Sample_label $sample_1 save_ save_3D_H(CC)(CO)NH_TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CC)(CO)NH_TOCSY' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (H)CC(CO)NH_TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CC)(CO)NH_TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.8 0.05 n/a temperature 293 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation 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_cyt_ox_assignments _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'cytochrome c' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 GLY HA2 H 3.24 0.13 2 2 . 1 GLY HA3 H 3.75 0.13 2 3 . 1 GLY C C 167.97 0.25 1 4 . 1 GLY CA C 42.74 0.42 1 5 . 2 ASP H H 9.41 0.04 1 6 . 2 ASP HA H 4.75 0.13 1 7 . 2 ASP HB2 H 2.67 0.13 2 8 . 2 ASP HB3 H 2.34 0.13 2 9 . 2 ASP C C 175.68 0.25 1 10 . 2 ASP CA C 52.78 0.42 1 11 . 2 ASP CB C 42.79 0.42 1 12 . 2 ASP N N 124.83 0.19 1 13 . 3 VAL H H 8.57 0.04 1 14 . 3 VAL HA H 3.46 0.13 1 15 . 3 VAL HB H 2.10 0.13 1 16 . 3 VAL HG1 H 1.02 0.04 1 17 . 3 VAL HG2 H 0.98 0.04 1 18 . 3 VAL C C 177.39 0.25 1 19 . 3 VAL CA C 66.31 0.42 1 20 . 3 VAL CB C 32.28 0.42 1 21 . 3 VAL CG1 C 22.03 0.16 1 22 . 3 VAL N N 124.14 0.19 1 23 . 4 GLU H H 8.04 0.04 1 24 . 4 GLU HA H 4.03 0.13 1 25 . 4 GLU HB2 H 2.10 0.13 2 26 . 4 GLU HG2 H 2.28 0.13 2 27 . 4 GLU C C 180.21 0.25 1 28 . 4 GLU CA C 59.10 0.42 1 29 . 4 GLU CB C 28.77 0.42 1 30 . 4 GLU CG C 36.18 0.42 1 31 . 4 GLU N N 120.11 0.19 1 32 . 5 LYS H H 8.01 0.04 1 33 . 5 LYS HA H 3.85 0.13 1 34 . 5 LYS HB2 H 1.61 0.13 4 35 . 5 LYS HG2 H 1.23 0.13 4 36 . 5 LYS C C 180.46 0.25 1 37 . 5 LYS CA C 59.53 0.42 1 38 . 5 LYS CB C 32.84 0.42 1 39 . 5 LYS CG C 26.05 0.42 1 40 . 5 LYS CD C 29.04 0.42 1 41 . 5 LYS CE C 42.10 0.42 1 42 . 5 LYS N N 121.00 0.19 1 43 . 6 GLY H H 8.57 0.04 1 44 . 6 GLY HA2 H 3.21 0.13 2 45 . 6 GLY HA3 H 3.90 0.13 2 46 . 6 GLY C C 174.14 0.25 1 47 . 6 GLY CA C 46.51 0.42 1 48 . 6 GLY N N 107.23 0.19 1 49 . 7 LYS H H 8.00 0.04 1 50 . 7 LYS HA H 2.23 0.13 4 51 . 7 LYS HB2 H 1.68 0.13 4 52 . 7 LYS HG2 H 0.87 0.13 4 53 . 7 LYS HD2 H 1.13 0.13 4 54 . 7 LYS HE2 H 2.95 0.13 4 55 . 7 LYS C C 177.49 0.25 1 56 . 7 LYS CA C 59.11 0.42 1 57 . 7 LYS CB C 32.28 0.42 1 58 . 7 LYS CG C 24.42 0.42 1 59 . 7 LYS CD C 29.31 0.42 1 60 . 7 LYS CE C 42.21 0.42 1 61 . 7 LYS N N 124.12 0.19 1 62 . 8 LYS H H 6.87 0.04 1 63 . 8 LYS HA H 3.84 0.13 1 64 . 8 LYS HB2 H 1.80 0.13 4 65 . 8 LYS HG2 H 1.31 0.13 4 66 . 8 LYS HD2 H 1.56 0.13 4 67 . 8 LYS HE2 H 2.89 0.13 4 68 . 8 LYS C C 179.36 0.25 1 69 . 8 LYS CA C 59.53 0.42 1 70 . 8 LYS CB C 32.05 0.42 1 71 . 8 LYS CG C 25.19 0.42 1 72 . 8 LYS CD C 29.06 0.42 1 73 . 8 LYS CE C 41.72 0.42 1 74 . 8 LYS N N 116.95 0.19 1 75 . 9 ILE H H 7.42 0.04 1 76 . 9 ILE HA H 3.47 0.13 1 77 . 9 ILE HB H 1.59 0.13 1 78 . 9 ILE HG12 H 0.81 0.13 1 79 . 9 ILE HG2 H 0.35 0.04 1 80 . 9 ILE HD1 H 0.72 0.04 1 81 . 9 ILE C C 176.93 0.25 1 82 . 9 ILE CA C 64.47 0.42 1 83 . 9 ILE CB C 37.41 0.42 1 84 . 9 ILE CG1 C 27.96 0.42 1 85 . 9 ILE CG2 C 18.11 0.16 1 86 . 9 ILE CD1 C 14.19 0.16 1 87 . 9 ILE N N 119.00 0.19 1 88 . 10 PHE H H 8.35 0.04 1 89 . 10 PHE HA H 3.40 0.13 1 90 . 10 PHE HB2 H 3.11 0.13 2 91 . 10 PHE HB3 H 2.71 0.13 2 92 . 10 PHE C C 178.72 0.25 1 93 . 10 PHE CA C 62.59 0.42 1 94 . 10 PHE CB C 39.74 0.42 1 95 . 10 PHE N N 120.77 0.19 1 96 . 11 VAL H H 8.84 0.04 1 97 . 11 VAL HA H 3.81 0.13 1 98 . 11 VAL HB H 2.19 0.13 1 99 . 11 VAL HG1 H 1.05 0.04 1 100 . 11 VAL HG2 H 1.27 0.04 1 101 . 11 VAL C C 177.66 0.25 1 102 . 11 VAL CA C 66.54 0.42 1 103 . 11 VAL CB C 32.04 0.42 1 104 . 11 VAL CG1 C 21.24 0.16 1 105 . 11 VAL CG2 C 23.03 0.16 1 106 . 11 VAL N N 121.44 0.19 1 107 . 12 GLN H H 7.76 0.04 1 108 . 12 GLN HA H 4.11 0.13 1 109 . 12 GLN HB2 H 2.00 0.13 2 110 . 12 GLN HG2 H 2.24 0.13 2 111 . 12 GLN HG3 H 2.50 0.13 2 112 . 12 GLN C C 178.26 0.25 1 113 . 12 GLN CA C 58.61 0.42 1 114 . 12 GLN CB C 29.71 0.42 1 115 . 12 GLN CG C 34.06 0.42 1 116 . 12 GLN N N 117.32 0.19 1 117 . 13 LYS H H 8.42 0.04 1 118 . 13 LYS HA H 4.32 0.13 1 119 . 13 LYS HB2 H 1.13 0.13 4 120 . 13 LYS HG2 H 0.77 0.13 4 121 . 13 LYS HD2 H 1.09 0.13 4 122 . 13 LYS HE2 H 2.69 0.13 4 123 . 13 LYS C C 176.69 0.25 1 124 . 13 LYS CA C 56.74 0.42 1 125 . 13 LYS CB C 34.84 0.42 1 126 . 13 LYS CG C 25.74 0.42 1 127 . 13 LYS CD C 28.99 0.5 1 128 . 13 LYS CE C 42.23 0.56 1 129 . 13 LYS N N 112.30 0.19 1 130 . 14 CYS H H 8.04 0.04 1 131 . 14 CYS HA H 4.45 0.13 1 132 . 14 CYS HB2 H 2.83 0.13 2 133 . 14 CYS HB3 H 1.60 0.13 2 134 . 14 CYS C C 178.36 0.25 1 135 . 14 CYS CA C 54.66 0.42 1 136 . 14 CYS CB C 37.85 0.42 1 137 . 14 CYS N N 114.99 0.19 1 138 . 15 ALA H H 8.05 0.04 1 139 . 15 ALA HA H 5.94 0.13 1 140 . 15 ALA HB H 2.16 0.04 1 141 . 15 ALA C C 178.64 0.25 1 142 . 15 ALA CA C 55.33 0.42 1 143 . 15 ALA CB C 20.38 0.16 1 144 . 15 ALA N N 123.61 0.19 1 145 . 16 GLN H H 9.87 0.04 1 146 . 16 GLN HA H 4.68 0.13 1 147 . 16 GLN HB2 H 2.65 0.13 4 148 . 16 GLN HG2 H 2.93 0.13 4 149 . 16 GLN HG3 H 2.81 0.13 4 150 . 16 GLN C C 177.35 0.25 1 151 . 16 GLN CA C 59.08 0.42 1 152 . 16 GLN CB C 28.79 0.42 1 153 . 16 GLN CG C 34.00 0.42 1 154 . 16 GLN N N 117.37 0.19 1 155 . 17 CYS H H 9.54 0.04 1 156 . 17 CYS HA H 5.93 0.13 1 157 . 17 CYS HB2 H 7.03 0.13 2 158 . 17 CYS HB3 H 2.06 0.13 2 159 . 17 CYS C C 175.68 0.25 1 160 . 17 CYS CA C 58.16 0.42 1 161 . 17 CYS CB C 35.81 0.42 1 162 . 17 CYS N N 113.99 0.19 1 163 . 18 HIS H H 10.94 0.04 1 164 . 18 HIS C C 177.06 0.25 1 165 . 18 HIS CA C 75.89 0.42 1 166 . 18 HIS CB C 26.68 0.42 1 167 . 18 HIS N N 118.41 0.19 1 168 . 19 THR H H 10.61 0.04 1 169 . 19 THR HA H 6.19 0.13 1 170 . 19 THR HB H 5.50 0.13 1 171 . 19 THR HG2 H 2.18 0.04 1 172 . 19 THR C C 176.19 0.25 1 173 . 19 THR CA C 60.70 0.42 1 174 . 19 THR CB C 72.39 0.42 1 175 . 19 THR CG2 C 22.84 0.16 1 176 . 19 THR N N 113.96 0.19 1 177 . 20 VAL H H 8.86 0.04 1 178 . 20 VAL HA H 4.94 0.13 1 179 . 20 VAL HB H 2.14 0.13 1 180 . 20 VAL HG1 H 0.94 0.04 1 181 . 20 VAL HG2 H 0.98 0.04 1 182 . 20 VAL C C 174.73 0.25 1 183 . 20 VAL CA C 61.90 0.42 1 184 . 20 VAL CB C 34.39 0.42 1 185 . 20 VAL CG1 C 23.08 0.16 1 186 . 20 VAL CG2 C 18.74 0.16 1 187 . 20 VAL N N 111.55 0.19 1 188 . 21 GLU H H 9.68 0.04 1 189 . 21 GLU HA H 4.61 0.13 1 190 . 21 GLU HB2 H 2.23 0.13 2 191 . 21 GLU HG2 H 2.55 0.13 2 192 . 21 GLU C C 178.25 0.25 1 193 . 21 GLU CA C 57.20 0.42 1 194 . 21 GLU CB C 30.40 0.42 1 195 . 21 GLU CG C 36.36 0.42 1 196 . 21 GLU N N 121.49 0.19 1 197 . 22 LYS H H 9.46 0.04 1 198 . 22 LYS HA H 3.93 0.13 1 199 . 22 LYS HB2 H 1.87 0.13 4 200 . 22 LYS HG2 H 1.40 0.13 4 201 . 22 LYS HD2 H 1.75 0.13 4 202 . 22 LYS C C 178.23 0.25 1 203 . 22 LYS CA C 58.62 0.42 1 204 . 22 LYS CB C 31.55 0.42 1 205 . 22 LYS CG C 24.50 0.42 1 206 . 22 LYS CD C 28.98 0.42 1 207 . 22 LYS CE C 42.12 0.42 1 208 . 22 LYS N N 128.23 0.19 1 209 . 23 GLY H H 9.58 0.04 1 210 . 23 GLY HA2 H 3.80 0.13 2 211 . 23 GLY HA3 H 4.15 0.13 2 212 . 23 GLY C C 175.07 0.25 1 213 . 23 GLY CA C 45.54 0.42 1 214 . 23 GLY N N 117.73 0.19 1 215 . 24 GLY H H 8.30 0.04 1 216 . 24 GLY HA2 H 3.71 0.13 2 217 . 24 GLY HA3 H 4.26 0.13 2 218 . 24 GLY C C 173.07 0.25 1 219 . 24 GLY CA C 44.87 0.42 1 220 . 24 GLY N N 107.38 0.19 1 221 . 25 LYS H H 8.87 0.04 1 222 . 25 LYS HA H 4.35 0.13 1 223 . 25 LYS HB2 H 2.01 0.13 4 224 . 25 LYS HG2 H 1.68 0.13 4 225 . 25 LYS HD2 H 1.78 0.13 4 226 . 25 LYS HE2 H 3.09 0.13 4 227 . 25 LYS C C 179.78 0.25 1 228 . 25 LYS CA C 56.52 0.42 1 229 . 25 LYS CB C 33.44 0.42 1 230 . 25 LYS CG C 24.91 0.42 1 231 . 25 LYS CD C 29.02 0.42 1 232 . 25 LYS CE C 42.31 0.42 1 233 . 25 LYS N N 118.66 0.19 1 234 . 26 ASN H H 9.21 0.04 1 235 . 26 ASN HA H 4.70 0.13 1 236 . 26 ASN HB2 H 2.78 0.13 2 237 . 26 ASN HB3 H 2.42 0.13 2 238 . 26 ASN C C 174.34 0.25 1 239 . 26 ASN CA C 53.97 0.42 1 240 . 26 ASN CB C 39.03 0.42 1 241 . 26 ASN N N 121.43 0.19 1 242 . 27 LYS H H 7.94 0.04 1 243 . 27 LYS CA C 55.14 0.42 1 244 . 27 LYS CB C 32.27 0.42 1 245 . 27 LYS CG C 24.91 0.42 1 246 . 28 THR HA H 3.07 0.13 1 247 . 28 THR HG2 H -0.01 0.04 1 248 . 28 THR C C 171.96 0.25 1 249 . 28 THR CA C 66.06 0.42 1 250 . 28 THR CB C 68.82 0.42 1 251 . 28 THR CG2 C 20.23 0.16 1 252 . 29 GLY H H 6.93 0.04 1 253 . 29 GLY CA C 37.44 0.42 1 254 . 29 GLY N N 99.56 0.19 1 255 . 30 PRO HA H 3.38 0.04 1 256 . 30 PRO HB2 H -0.14 0.13 4 257 . 30 PRO HB3 H 1.33 0.13 4 258 . 30 PRO HG2 H -0.67 0.13 4 259 . 30 PRO HD2 H -1.13 0.13 4 260 . 30 PRO C C 177.13 0.25 1 261 . 30 PRO CD C 51.58 0.25 1 262 . 30 PRO CA C 60.03 0.25 1 263 . 30 PRO CB C 30.19 0.42 1 264 . 30 PRO CG C 23.85 0.42 1 265 . 31 ASN H H 8.55 0.04 1 266 . 31 ASN HA H 5.81 0.13 1 267 . 31 ASN HB2 H 2.84 0.13 2 268 . 31 ASN HB3 H 2.53 0.13 2 269 . 31 ASN C C 176.16 0.25 1 270 . 31 ASN CA C 55.79 0.42 1 271 . 31 ASN CB C 40.69 0.42 1 272 . 31 ASN N N 122.75 0.19 1 273 . 32 LEU H H 9.43 0.04 1 274 . 32 LEU HA H 4.95 0.13 1 275 . 32 LEU HB2 H 2.50 0.13 2 276 . 32 LEU HG H 2.29 0.13 1 277 . 32 LEU HD1 H 2.00 0.04 1 278 . 32 LEU HD2 H 1.59 0.04 1 279 . 32 LEU C C 175.85 0.25 1 280 . 32 LEU CA C 53.97 0.42 1 281 . 32 LEU CB C 44.42 0.42 1 282 . 32 LEU CG C 27.54 0.42 1 283 . 32 LEU CD2 C 22.01 0.16 1 284 . 32 LEU N N 120.74 0.19 1 285 . 33 ASN H H 8.13 0.04 1 286 . 33 ASN HA H 4.28 0.13 1 287 . 33 ASN HB2 H 2.96 0.13 2 288 . 33 ASN HB3 H 2.66 0.13 2 289 . 33 ASN C C 176.66 0.25 1 290 . 33 ASN CA C 58.14 0.42 1 291 . 33 ASN CB C 40.67 0.42 1 292 . 33 ASN N N 120.04 0.19 1 293 . 34 GLY H H 9.58 0.04 1 294 . 34 GLY HA2 H 3.95 0.13 2 295 . 34 GLY HA3 H 4.07 0.13 2 296 . 34 GLY C C 174.41 0.25 1 297 . 34 GLY CA C 46.01 0.42 1 298 . 34 GLY N N 113.99 0.19 1 299 . 35 LEU H H 7.17 0.04 1 300 . 35 LEU HA H 3.61 0.13 1 301 . 35 LEU HB2 H 2.19 0.13 2 302 . 35 LEU HG H 1.47 0.13 1 303 . 35 LEU HD1 H 0.42 0.04 1 304 . 35 LEU HD2 H 0.12 0.04 1 305 . 35 LEU C C 177.04 0.25 1 306 . 35 LEU CA C 58.12 0.42 1 307 . 35 LEU CB C 44.40 0.42 1 308 . 35 LEU CD1 C 25.13 0.16 1 309 . 35 LEU CD2 C 26.69 0.16 1 310 . 35 LEU N N 117.32 0.19 1 311 . 36 PHE H H 8.65 0.04 1 312 . 36 PHE HA H 3.76 0.13 1 313 . 36 PHE HB2 H 3.21 0.13 2 314 . 36 PHE HB3 H 2.75 0.13 2 315 . 36 PHE C C 177.74 0.25 1 316 . 36 PHE CA C 60.04 0.42 1 317 . 36 PHE CB C 37.16 0.42 1 318 . 36 PHE N N 112.27 0.19 1 319 . 37 GLY H H 9.29 0.04 1 320 . 37 GLY HA2 H 3.44 0.13 2 321 . 37 GLY HA3 H 4.36 0.13 2 322 . 37 GLY C C 173.28 0.25 1 323 . 37 GLY CA C 44.69 0.42 1 324 . 37 GLY N N 111.53 0.19 1 325 . 38 ARG H H 8.18 0.04 1 326 . 38 ARG HA H 4.66 0.13 1 327 . 38 ARG HB2 H 2.10 0.13 4 328 . 38 ARG HG2 H 1.88 0.13 4 329 . 38 ARG HD2 H 3.11 0.13 4 330 . 38 ARG C C 174.81 0.25 1 331 . 38 ARG CA C 54.91 0.42 1 332 . 38 ARG CB C 33.44 0.42 1 333 . 38 ARG CG C 26.41 0.42 1 334 . 38 ARG CD C 45.32 0.42 1 335 . 38 ARG N N 123.82 0.19 1 336 . 39 LYS H H 8.01 0.04 1 337 . 39 LYS HA H 4.86 0.13 1 338 . 39 LYS HB2 H 1.62 0.13 4 339 . 39 LYS HG2 H 1.32 0.13 4 340 . 39 LYS HD2 H 1.42 0.13 4 341 . 39 LYS HE2 H 2.80 0.13 4 342 . 39 LYS C C 177.33 0.25 1 343 . 39 LYS CA C 55.34 0.42 1 344 . 39 LYS CB C 33.67 0.42 1 345 . 39 LYS CG C 25.16 0.42 1 346 . 39 LYS CD C 29.01 0.42 1 347 . 39 LYS CE C 41.89 0.42 1 348 . 39 LYS N N 121.11 0.19 1 349 . 40 THR H H 7.53 0.04 1 350 . 40 THR HA H 4.17 0.13 1 351 . 40 THR HB H 4.45 0.13 1 352 . 40 THR HG2 H 0.87 0.04 1 353 . 40 THR C C 176.67 0.25 1 354 . 40 THR CA C 61.20 0.42 1 355 . 40 THR CB C 68.65 0.42 1 356 . 40 THR CG2 C 22.80 0.16 1 357 . 40 THR N N 108.62 0.19 1 358 . 41 GLY H H 8.85 0.04 1 359 . 41 GLY HA2 H 1.18 0.13 2 360 . 41 GLY HA3 H 3.12 0.13 2 361 . 41 GLY C C 174.77 0.25 1 362 . 41 GLY CA C 45.82 0.42 1 363 . 41 GLY N N 108.59 0.19 1 364 . 42 GLN H H 7.71 0.04 1 365 . 42 GLN HA H 4.40 0.13 1 366 . 42 GLN HB2 H 2.07 0.13 2 367 . 42 GLN HG2 H 2.12 0.13 2 368 . 42 GLN C C 176.07 0.25 1 369 . 42 GLN CA C 54.65 0.42 1 370 . 42 GLN CB C 30.17 0.42 1 371 . 42 GLN CG C 33.62 0.42 1 372 . 42 GLN N N 113.56 0.19 1 373 . 43 ALA H H 8.22 0.04 1 374 . 43 ALA HB H 1.39 0.04 1 375 . 43 ALA CA C 51.85 0.42 1 376 . 43 ALA CB C 18.98 0.16 1 377 . 43 ALA N N 125.84 0.19 1 378 . 44 PRO HA H 4.34 0.04 1 379 . 44 PRO HB2 H 2.28 0.13 4 380 . 44 PRO HG2 H 2.06 0.13 4 381 . 44 PRO HD2 H 3.84 0.13 4 382 . 44 PRO C C 178.90 0.25 1 383 . 44 PRO CA C 63.06 0.25 1 384 . 44 PRO CB C 32.04 0.42 1 385 . 44 PRO CG C 27.69 0.42 1 386 . 44 PRO CD C 50.95 0.42 1 387 . 45 GLY H H 8.80 0.04 1 388 . 45 GLY HA2 H 3.57 0.13 2 389 . 45 GLY HA3 H 3.85 0.13 2 390 . 45 GLY C C 172.42 0.25 1 391 . 45 GLY CA C 46.01 0.42 1 392 . 45 GLY N N 110.26 0.42 1 393 . 46 PHE H H 6.86 0.19 1 394 . 46 PHE HA H 3.84 0.04 1 395 . 46 PHE HB2 H 1.92 0.13 2 396 . 46 PHE C C 173.35 0.25 1 397 . 46 PHE CA C 57.01 0.42 1 398 . 46 PHE CB C 40.89 0.42 1 399 . 46 PHE N N 119.98 0.19 1 400 . 47 THR H H 6.77 0.04 1 401 . 47 THR HA H 3.79 0.13 1 402 . 47 THR HB H 3.15 0.13 1 403 . 47 THR HG2 H 0.68 0.04 1 404 . 47 THR C C 171.44 0.25 1 405 . 47 THR CA C 60.94 0.42 1 406 . 47 THR CB C 67.25 0.42 1 407 . 47 THR CG2 C 21.24 0.16 1 408 . 47 THR N N 123.82 0.19 1 409 . 48 TYR H H 8.04 0.04 1 410 . 48 TYR HA H 4.08 0.13 1 411 . 48 TYR HB2 H 3.11 0.13 2 412 . 48 TYR HB3 H 2.42 0.13 2 413 . 48 TYR C C 178.78 0.25 1 414 . 48 TYR CA C 57.90 0.42 1 415 . 48 TYR CB C 41.38 0.42 1 416 . 48 TYR N N 126.42 0.19 1 417 . 49 THR H H 9.60 0.04 1 418 . 49 THR HA H 4.13 0.13 1 419 . 49 THR HB H 4.66 0.13 1 420 . 49 THR HG2 H 1.51 0.04 1 421 . 49 THR C C 176.11 0.25 1 422 . 49 THR CA C 62.14 0.42 1 423 . 49 THR CB C 71.21 0.42 1 424 . 49 THR CG2 C 22.33 0.16 1 425 . 49 THR N N 112.62 0.19 1 426 . 50 ASP H H 8.85 0.04 1 427 . 50 ASP HA H 4.22 0.13 1 428 . 50 ASP HB2 H 2.60 0.13 2 429 . 50 ASP C C 178.18 0.25 1 430 . 50 ASP CA C 57.46 0.42 1 431 . 50 ASP CB C 39.52 0.42 1 432 . 50 ASP N N 122.82 0.19 1 433 . 51 ALA H H 8.05 0.04 1 434 . 51 ALA HA H 4.13 0.13 1 435 . 51 ALA HB H 1.60 0.04 1 436 . 51 ALA C C 179.86 0.25 1 437 . 51 ALA CA C 55.11 0.42 1 438 . 51 ALA CB C 19.02 0.16 1 439 . 51 ALA N N 119.44 0.19 1 440 . 52 ASN H H 8.55 0.04 1 441 . 52 ASN HA H 4.71 0.13 1 442 . 52 ASN HB2 H 3.21 0.13 2 443 . 52 ASN HB3 H 3.11 0.13 2 444 . 52 ASN C C 179.18 0.25 1 445 . 52 ASN CA C 55.11 0.42 1 446 . 52 ASN CB C 40.21 0.42 1 447 . 52 ASN N N 116.98 0.19 1 448 . 53 LYS H H 8.74 0.04 1 449 . 53 LYS HA H 3.62 0.13 1 450 . 53 LYS HB2 H 1.78 0.13 4 451 . 53 LYS HG2 H 1.37 0.13 4 452 . 53 LYS HD2 H 1.73 0.13 4 453 . 53 LYS HE2 H 2.93 0.13 4 454 . 53 LYS C C 177.66 0.25 1 455 . 53 LYS CA C 59.56 0.42 1 456 . 53 LYS CB C 32.72 0.42 1 457 . 53 LYS CG C 24.36 0.42 1 458 . 53 LYS CD C 28.89 0.42 1 459 . 53 LYS CE C 41.90 0.42 1 460 . 53 LYS N N 121.70 0.19 1 461 . 54 ASN H H 8.16 0.04 1 462 . 54 ASN HA H 4.72 0.13 1 463 . 54 ASN HB2 H 2.93 0.13 2 464 . 54 ASN HB3 H 2.74 0.13 2 465 . 54 ASN C C 176.09 0.25 1 466 . 54 ASN CA C 53.02 0.42 1 467 . 54 ASN CB C 39.02 0.42 1 468 . 54 ASN N N 112.29 0.19 1 469 . 55 LYS H H 6.98 0.04 1 470 . 55 LYS HA H 4.22 0.13 4 471 . 55 LYS HB2 H 2.20 0.13 4 472 . 55 LYS HG2 H 1.19 0.13 4 473 . 55 LYS C C 177.78 0.25 1 474 . 55 LYS CA C 58.37 0.42 1 475 . 55 LYS CB C 30.66 0.42 1 476 . 55 LYS CG C 25.59 0.42 1 477 . 55 LYS CD C 30.52 0.42 1 478 . 55 LYS CE C 41.89 0.42 1 479 . 55 LYS N N 121.74 0.19 1 480 . 56 GLY H H 7.85 0.04 1 481 . 56 GLY HA2 H 3.71 0.13 2 482 . 56 GLY HA3 H 3.81 0.13 2 483 . 56 GLY C C 174.61 0.25 1 484 . 56 GLY CA C 46.74 0.42 1 485 . 56 GLY N N 103.40 0.19 1 486 . 57 ILE H H 6.55 0.04 1 487 . 57 ILE HA H 4.44 0.13 1 488 . 57 ILE HB H 1.83 0.13 1 489 . 57 ILE HG12 H 1.10 0.13 1 490 . 57 ILE HG2 H 0.77 0.04 1 491 . 57 ILE HD1 H -0.46 0.04 1 492 . 57 ILE C C 174.08 0.25 1 493 . 57 ILE CA C 57.70 0.42 1 494 . 57 ILE CB C 41.14 0.42 1 495 . 57 ILE CG1 C 27.36 0.42 1 496 . 57 ILE CG2 C 21.97 0.16 1 497 . 57 ILE CD1 C 13.84 0.16 1 498 . 57 ILE N N 111.25 0.19 1 499 . 58 THR H H 8.18 0.04 1 500 . 58 THR HA H 4.16 0.13 1 501 . 58 THR HB H 3.71 0.13 1 502 . 58 THR HG2 H 0.91 0.04 1 503 . 58 THR C C 174.81 0.25 1 504 . 58 THR CA C 61.64 0.42 1 505 . 58 THR CB C 69.58 0.42 1 506 . 58 THR CG2 C 21.21 0.16 1 507 . 58 THR N N 115.96 0.19 1 508 . 59 TRP H H 8.67 0.04 1 509 . 59 TRP HA H 4.67 0.13 1 510 . 59 TRP HB2 H 3.58 0.13 2 511 . 59 TRP HB3 H 2.11 0.13 2 512 . 59 TRP C C 173.74 0.25 1 513 . 59 TRP CA C 57.01 0.42 1 514 . 59 TRP CB C 29.72 0.42 1 515 . 59 TRP N N 129.24 0.19 1 516 . 60 LYS H H 7.94 0.04 1 517 . 60 LYS HA H 4.26 0.13 1 518 . 60 LYS HB2 H 2.33 0.13 4 519 . 60 LYS HG2 H 1.60 0.13 4 520 . 60 LYS HD2 H 1.41 0.13 4 521 . 60 LYS HD3 H 1.73 0.13 4 522 . 60 LYS HE2 H 2.93 0.13 4 523 . 60 LYS C C 174.71 0.25 1 524 . 60 LYS CA C 54.66 0.42 1 525 . 60 LYS CB C 34.17 0.42 1 526 . 60 LYS CG C 23.30 0.42 1 527 . 60 LYS CD C 29.45 0.42 1 528 . 60 LYS CE C 42.27 0.42 1 529 . 60 LYS N N 119.74 0.19 1 530 . 61 GLU H H 10.46 0.04 1 531 . 61 GLU HA H 3.62 0.13 1 532 . 61 GLU HB2 H 2.15 0.13 4 533 . 61 GLU HB3 H 2.01 0.13 4 534 . 61 GLU HG2 H 2.42 0.13 4 535 . 61 GLU C C 177.90 0.25 1 536 . 61 GLU CA C 63.50 0.42 1 537 . 61 GLU CB C 28.77 0.42 1 538 . 61 GLU CG C 37.76 0.42 1 539 . 61 GLU N N 122.78 0.19 1 540 . 62 GLU H H 9.53 0.04 1 541 . 62 GLU HA H 3.94 0.13 1 542 . 62 GLU HB2 H 2.01 0.13 4 543 . 62 GLU HG2 H 2.33 0.13 4 544 . 62 GLU C C 179.65 0.25 1 545 . 62 GLU CA C 60.74 0.42 1 546 . 62 GLU CB C 29.71 0.42 1 547 . 62 GLU CG C 36.81 0.42 1 548 . 62 GLU N N 114.61 0.19 1 549 . 63 THR H H 6.99 0.04 1 550 . 63 THR HA H 4.31 0.13 1 551 . 63 THR HB H 4.49 0.13 1 552 . 63 THR HG2 H 1.33 0.04 1 553 . 63 THR C C 177.41 0.25 1 554 . 63 THR CA C 62.83 0.42 1 555 . 63 THR CB C 68.88 0.42 1 556 . 63 THR CG2 C 23.78 0.16 1 557 . 63 THR N N 108.50 0.19 1 558 . 64 LEU H H 8.46 0.04 1 559 . 64 LEU HA H 3.80 0.13 1 560 . 64 LEU HB2 H 1.51 0.13 1 561 . 64 LEU HG H 0.44 0.13 1 562 . 64 LEU HD1 H -0.28 0.04 1 563 . 64 LEU HD2 H -0.60 0.04 1 564 . 64 LEU C C 178.38 0.25 1 565 . 64 LEU CA C 58.17 0.42 1 566 . 64 LEU CB C 42.08 0.42 1 567 . 64 LEU CD1 C 26.61 0.16 1 568 . 64 LEU CD2 C 23.14 0.16 1 569 . 64 LEU N N 122.06 0.19 1 570 . 65 MET H H 8.21 0.04 1 571 . 65 MET HA H 3.62 0.13 1 572 . 65 MET HB2 H 2.51 0.13 4 573 . 65 MET HB3 H 2.36 0.13 4 574 . 65 MET HG2 H 2.11 0.13 4 575 . 65 MET HG3 H 1.92 0.13 4 576 . 65 MET HE H 1.84 0.04 1 577 . 65 MET C C 177.58 0.25 1 578 . 65 MET CA C 57.91 0.42 1 579 . 65 MET CB C 31.04 0.42 1 580 . 65 MET CG C 32.06 0.42 1 581 . 65 MET CE C 16.63 0.16 1 582 . 65 MET N N 118.37 0.19 1 583 . 66 GLU H H 6.60 0.04 1 584 . 66 GLU HA H 4.57 0.13 1 585 . 66 GLU HB2 H 2.38 0.13 4 586 . 66 GLU HB3 H 2.10 0.13 4 587 . 66 GLU HG2 H 1.96 0.13 4 588 . 66 GLU HG3 H 1.74 0.13 4 589 . 66 GLU C C 177.59 0.25 1 590 . 66 GLU CA C 58.37 0.42 1 591 . 66 GLU CB C 30.18 0.42 1 592 . 66 GLU CG C 36.18 0.42 1 593 . 66 GLU N N 117.18 0.19 1 594 . 67 TYR H H 8.05 0.04 1 595 . 67 TYR HA H 3.94 0.13 1 596 . 67 TYR HB2 H 3.24 0.13 2 597 . 67 TYR HB3 H 2.61 0.13 2 598 . 67 TYR C C 176.91 0.25 1 599 . 67 TYR CA C 60.50 0.42 1 600 . 67 TYR CB C 40.46 0.42 1 601 . 67 TYR N N 121.07 0.19 1 602 . 68 LEU H H 8.05 0.04 1 603 . 68 LEU HA H 2.56 0.13 1 604 . 68 LEU HB2 H 0.96 0.13 1 605 . 68 LEU HG H -0.11 0.13 1 606 . 68 LEU HD1 H -0.66 0.04 1 607 . 68 LEU HD2 H -2.93 0.04 1 608 . 68 LEU C C 176.67 0.25 1 609 . 68 LEU CA C 55.56 0.42 1 610 . 68 LEU CB C 40.91 0.42 1 611 . 68 LEU CG C 29.04 0.42 1 612 . 68 LEU CD1 C 24.61 0.16 1 613 . 68 LEU CD2 C 19.68 0.16 1 614 . 68 LEU N N 110.89 0.19 1 615 . 69 GLU H H 6.75 0.04 1 616 . 69 GLU HA H 3.80 0.13 1 617 . 69 GLU HB2 H 1.63 0.13 4 618 . 69 GLU HG2 H 2.15 0.13 4 619 . 69 GLU C C 176.38 0.25 1 620 . 69 GLU CA C 58.83 0.42 1 621 . 69 GLU CB C 29.95 0.42 1 622 . 69 GLU CG C 36.48 0.42 1 623 . 69 GLU N N 118.97 0.19 1 624 . 70 ASN H H 6.63 0.04 1 625 . 70 ASN CA C 52.30 0.42 1 626 . 70 ASN CB C 37.65 0.42 1 627 . 70 ASN N N 105.51 0.19 1 628 . 71 PRO HA H 5.35 0.04 1 629 . 71 PRO HB2 H 5.17 0.13 4 630 . 71 PRO HB3 H 4.94 0.13 4 631 . 71 PRO HG2 H 2.02 0.13 4 632 . 71 PRO HG3 H 3.16 0.13 4 633 . 71 PRO HD2 H 3.84 0.13 4 634 . 71 PRO C C 178.66 0.25 1 635 . 71 PRO CA C 67.93 0.42 1 636 . 71 PRO CB C 33.69 0.42 1 637 . 71 PRO CG C 27.36 0.42 1 638 . 71 PRO CD C 49.69 0.42 1 639 . 72 LYS H H 9.38 0.04 1 640 . 72 LYS HA H 5.22 0.13 1 641 . 72 LYS HB2 H 2.74 0.13 4 642 . 72 LYS HG2 H 2.33 0.13 4 643 . 72 LYS HD2 H 2.57 0.13 4 644 . 72 LYS HE2 H 3.57 0.13 4 645 . 72 LYS C C 178.44 0.25 1 646 . 72 LYS CA C 59.10 0.42 1 647 . 72 LYS CB C 32.77 0.42 1 648 . 72 LYS CG C 25.67 0.42 1 649 . 72 LYS CD C 30.07 0.42 1 650 . 72 LYS CE C 42.24 0.42 1 651 . 72 LYS N N 115.59 0.19 1 652 . 73 LYS H H 7.77 0.04 1 653 . 73 LYS HA H 4.44 0.13 1 654 . 73 LYS HB2 H 2.05 0.13 4 655 . 73 LYS HG2 H 1.64 0.13 4 656 . 73 LYS HD2 H 1.88 0.13 4 657 . 73 LYS HE2 H 3.15 0.13 4 658 . 73 LYS C C 179.12 0.25 1 659 . 73 LYS CA C 58.16 0.42 1 660 . 73 LYS CB C 33.89 0.42 1 661 . 73 LYS CG C 25.26 0.42 1 662 . 73 LYS CD C 29.76 0.42 1 663 . 73 LYS CE C 42.43 0.42 1 664 . 73 LYS N N 119.66 0.19 1 665 . 74 TYR H H 8.08 0.04 1 666 . 74 TYR HA H 4.73 0.13 1 667 . 74 TYR HB2 H 4.08 0.13 2 668 . 74 TYR HB3 H 3.84 0.13 2 669 . 74 TYR C C 176.37 0.25 1 670 . 74 TYR CA C 61.64 0.42 1 671 . 74 TYR CB C 40.67 0.42 1 672 . 74 TYR N N 120.11 0.19 1 673 . 75 ILE H H 9.43 0.04 1 674 . 75 ILE HG2 H 1.30 0.04 1 675 . 75 ILE HD1 H 2.04 0.04 1 676 . 75 ILE CA C 59.53 0.42 1 677 . 75 ILE CB C 38.34 0.42 1 678 . 75 ILE CG1 C 28.64 0.42 1 679 . 75 ILE CG2 C 19.21 0.16 1 680 . 75 ILE CD1 C 13.53 0.16 1 681 . 75 ILE N N 115.00 0.19 1 682 . 76 PRO HA H 5.18 0.04 1 683 . 76 PRO HB2 H 2.29 0.13 4 684 . 76 PRO HG2 H 2.10 0.13 4 685 . 76 PRO HD2 H 3.75 0.13 4 686 . 76 PRO C C 179.18 0.25 1 687 . 76 PRO CA C 64.47 0.42 1 688 . 76 PRO CB C 31.58 0.42 1 689 . 76 PRO CG C 28.01 0.42 1 690 . 76 PRO CD C 50.07 0.42 1 691 . 77 GLY H H 9.32 0.04 1 692 . 77 GLY HA2 H 4.02 0.13 2 693 . 77 GLY HA3 H 4.58 0.13 2 694 . 77 GLY C C 176.27 0.25 1 695 . 77 GLY CA C 44.86 0.42 1 696 . 77 GLY N N 111.55 0.19 1 697 . 78 THR H H 9.04 0.04 1 698 . 78 THR HA H 5.23 0.13 1 699 . 78 THR HB H 5.91 0.13 1 700 . 78 THR HG2 H 0.34 0.04 1 701 . 78 THR C C 173.28 0.25 1 702 . 78 THR CA C 61.85 0.42 1 703 . 78 THR CB C 70.52 0.42 1 704 . 78 THR CG2 C 21.75 0.16 1 705 . 78 THR N N 115.26 0.19 1 706 . 79 LYS H H 8.25 0.04 1 707 . 79 LYS HA H 4.95 0.13 1 708 . 79 LYS HB2 H 1.74 0.13 4 709 . 79 LYS HG2 H 1.14 0.13 4 710 . 79 LYS HD2 H 1.46 0.13 4 711 . 79 LYS HE2 H 2.38 0.13 4 712 . 79 LYS C C 174.88 0.25 1 713 . 79 LYS CA C 55.34 0.42 1 714 . 79 LYS CB C 32.28 0.42 1 715 . 79 LYS CG C 23.81 0.42 1 716 . 79 LYS CD C 28.71 0.42 1 717 . 79 LYS CE C 41.47 0.42 1 718 . 79 LYS N N 123.69 0.19 1 719 . 80 MET H H 9.27 0.04 1 720 . 80 MET HA H 2.93 0.13 1 721 . 80 MET C C 175.34 0.25 1 722 . 80 MET CA C 64.19 0.42 1 723 . 80 MET N N 122.75 0.19 1 724 . 81 ILE H H 8.55 0.04 1 725 . 81 ILE HA H 5.07 0.13 1 726 . 81 ILE HB H 2.11 0.13 1 727 . 81 ILE HG12 H 1.41 0.13 1 728 . 81 ILE HG2 H 1.09 0.04 1 729 . 81 ILE HD1 H 0.92 0.04 1 730 . 81 ILE C C 175.32 0.25 1 731 . 81 ILE CA C 60.93 0.42 1 732 . 81 ILE CB C 35.55 0.42 1 733 . 81 ILE CG1 C 26.47 0.42 1 734 . 81 ILE CG2 C 17.64 0.16 1 735 . 81 ILE CD1 C 11.15 0.16 1 736 . 81 ILE N N 135.37 0.19 1 737 . 82 PHE H H 8.94 0.04 1 738 . 82 PHE HA H 3.53 0.13 1 739 . 82 PHE HB2 H 2.89 0.13 2 740 . 82 PHE C C 174.93 0.25 1 741 . 82 PHE CA C 59.34 0.42 1 742 . 82 PHE CB C 41.37 0.42 1 743 . 82 PHE N N 126.15 0.19 1 744 . 83 ALA H H 8.44 0.04 1 745 . 83 ALA HB H 1.62 0.04 1 746 . 83 ALA CA C 55.09 0.42 1 747 . 83 ALA CB C 19.01 0.16 1 748 . 83 ALA N N 130.93 0.19 1 749 . 84 GLY H H 4.60 0.04 1 750 . 84 GLY HA2 H 4.35 0.13 2 751 . 84 GLY HA3 H 2.83 0.13 2 752 . 84 GLY C C 171.88 0.25 1 753 . 84 GLY CA C 43.01 0.42 1 754 . 84 GLY N N 100.20 0.19 1 755 . 85 ILE H H 7.94 0.04 1 756 . 85 ILE HA H 3.81 0.13 1 757 . 85 ILE HB H 0.77 0.13 1 758 . 85 ILE HG12 H 0.53 0.13 1 759 . 85 ILE HG2 H 0.45 0.04 1 760 . 85 ILE HD1 H -0.33 0.04 1 761 . 85 ILE C C 174.81 0.25 1 762 . 85 ILE CA C 59.25 0.42 1 763 . 85 ILE CB C 39.04 0.42 1 764 . 85 ILE CG1 C 25.97 0.42 1 765 . 85 ILE CG2 C 18.48 0.16 1 766 . 85 ILE CD1 C 13.25 0.16 1 767 . 85 ILE N N 120.97 0.19 1 768 . 86 LYS H H 8.41 0.04 1 769 . 86 LYS HA H 3.93 0.13 1 770 . 86 LYS HB2 H 1.64 0.13 4 771 . 86 LYS HG2 H 1.32 0.13 4 772 . 86 LYS HD2 H 1.54 0.13 4 773 . 86 LYS HE2 H 2.84 0.13 4 774 . 86 LYS C C 178.58 0.25 1 775 . 86 LYS CA C 58.64 0.42 1 776 . 86 LYS CB C 32.53 0.42 1 777 . 86 LYS CG C 24.60 0.42 1 778 . 86 LYS CD C 28.36 0.42 1 779 . 86 LYS CE C 42.17 0.42 1 780 . 86 LYS N N 127.19 0.19 1 781 . 87 LYS H H 8.18 0.04 1 782 . 87 LYS HA H 4.12 0.13 1 783 . 87 LYS HB2 H 1.66 0.13 4 784 . 87 LYS HG2 H 1.45 0.13 4 785 . 87 LYS HD2 H 1.53 0.13 4 786 . 87 LYS HE2 H 2.88 0.13 4 787 . 87 LYS C C 177.33 0.25 1 788 . 87 LYS CA C 57.01 0.42 1 789 . 87 LYS CB C 32.96 0.42 1 790 . 87 LYS CG C 25.55 0.42 1 791 . 87 LYS CD C 29.11 0.42 1 792 . 87 LYS CE C 42.07 0.42 1 793 . 87 LYS N N 120.09 0.19 1 794 . 88 LYS H H 8.91 0.04 1 795 . 88 LYS HA H 3.47 0.13 1 796 . 88 LYS HB2 H 1.74 0.13 4 797 . 88 LYS HG2 H 1.18 0.13 4 798 . 88 LYS HD2 H 1.55 0.13 4 799 . 88 LYS C C 178.12 0.25 1 800 . 88 LYS CA C 60.51 0.42 1 801 . 88 LYS CB C 32.75 0.42 1 802 . 88 LYS CG C 25.05 0.42 1 803 . 88 LYS CD C 29.38 0.42 1 804 . 88 LYS CE C 41.21 0.42 1 805 . 88 LYS N N 128.91 0.19 1 806 . 89 THR H H 8.13 0.04 1 807 . 89 THR HA H 3.90 0.13 1 808 . 89 THR HB H 3.97 0.13 1 809 . 89 THR HG2 H 1.18 0.04 1 810 . 89 THR C C 175.93 0.25 1 811 . 89 THR CA C 64.91 0.42 1 812 . 89 THR CB C 67.71 0.42 1 813 . 89 THR CG2 C 22.21 0.16 1 814 . 89 THR N N 109.83 0.19 1 815 . 90 GLU H H 6.02 0.04 1 816 . 90 GLU HA H 3.94 0.13 1 817 . 90 GLU HB2 H 1.69 0.13 4 818 . 90 GLU HG2 H 2.05 0.13 4 819 . 90 GLU C C 178.50 0.25 1 820 . 90 GLU CA C 58.38 0.42 1 821 . 90 GLU CB C 29.96 0.42 1 822 . 90 GLU CG C 37.00 0.16 1 823 . 90 GLU N N 118.73 0.19 1 824 . 91 ARG H H 7.08 0.04 1 825 . 91 ARG HA H 3.16 0.13 1 826 . 91 ARG HB2 H 1.41 0.13 4 827 . 91 ARG HG2 H 0.59 0.13 4 828 . 91 ARG HD2 H 2.93 0.13 4 829 . 91 ARG C C 177.39 0.25 1 830 . 91 ARG CA C 61.20 0.42 1 831 . 91 ARG CB C 31.11 0.42 1 832 . 91 ARG CD C 43.80 0.42 4 833 . 91 ARG N N 116.98 0.19 1 834 . 92 GLU H H 8.24 0.04 1 835 . 92 GLU HA H 3.53 0.13 1 836 . 92 GLU HB2 H 2.01 0.13 4 837 . 92 GLU HG2 H 2.29 0.13 4 838 . 92 GLU C C 179.94 0.25 1 839 . 92 GLU CA C 59.58 0.42 1 840 . 92 GLU CB C 29.49 0.42 1 841 . 92 GLU CG C 37.02 0.42 1 842 . 92 GLU N N 117.64 0.19 1 843 . 93 ASP H H 8.15 0.04 1 844 . 93 ASP HA H 4.36 0.13 1 845 . 93 ASP HB2 H 2.38 0.13 2 846 . 93 ASP C C 177.47 0.25 1 847 . 93 ASP CA C 58.14 0.42 1 848 . 93 ASP CB C 39.49 0.42 1 849 . 93 ASP N N 122.72 0.19 1 850 . 94 LEU H H 7.91 0.04 1 851 . 94 LEU HA H 3.76 0.13 1 852 . 94 LEU HB2 H 1.41 0.13 1 853 . 94 LEU HB3 H 1.05 0.13 1 854 . 94 LEU HG H 0.72 0.13 1 855 . 94 LEU HD1 H 0.59 0.04 1 856 . 94 LEU HD2 H -0.33 0.04 1 857 . 94 LEU C C 178.13 0.25 1 858 . 94 LEU CA C 57.93 0.42 1 859 . 94 LEU CB C 40.92 0.42 1 860 . 94 LEU CD1 C 23.56 0.16 1 861 . 94 LEU CD2 C 27.43 0.16 1 862 . 94 LEU N N 120.71 0.19 1 863 . 95 ILE H H 8.38 0.04 1 864 . 95 ILE HA H 3.06 0.13 1 865 . 95 ILE HB H 1.60 0.13 1 866 . 95 ILE HG12 H 0.77 0.13 1 867 . 95 ILE HG2 H 0.82 0.04 1 868 . 95 ILE HD1 H 0.43 0.04 1 869 . 95 ILE C C 176.08 0.25 1 870 . 95 ILE CA C 66.29 0.42 1 871 . 95 ILE CB C 37.39 0.42 1 872 . 95 ILE CG1 C 31.61 0.42 1 873 . 95 ILE CG2 C 17.85 0.16 1 874 . 95 ILE CD1 C 14.29 0.16 1 875 . 95 ILE N N 119.35 0.19 1 876 . 96 ALA H H 7.74 0.04 1 877 . 96 ALA HA H 3.89 0.13 1 878 . 96 ALA HB H 1.19 0.04 1 879 . 96 ALA C C 180.70 0.25 1 880 . 96 ALA CA C 54.90 0.42 1 881 . 96 ALA CB C 17.35 0.16 1 882 . 96 ALA N N 122.75 0.19 1 883 . 97 TYR H H 7.88 0.04 1 884 . 97 TYR HA H 4.12 0.13 1 885 . 97 TYR HB2 H 3.48 0.13 2 886 . 97 TYR HB3 H 2.79 0.13 2 887 . 97 TYR C C 176.23 0.25 1 888 . 97 TYR CA C 61.63 0.42 1 889 . 97 TYR CB C 37.40 0.42 1 890 . 97 TYR N N 117.55 0.19 1 891 . 98 LEU H H 8.69 0.04 1 892 . 98 LEU HA H 3.34 0.13 1 893 . 98 LEU HB2 H 1.78 0.13 1 894 . 98 LEU HG H 1.01 0.13 1 895 . 98 LEU HD1 H -0.15 0.04 1 896 . 98 LEU HD2 H 0.41 0.04 1 897 . 98 LEU C C 179.12 0.25 1 898 . 98 LEU CA C 57.47 0.42 1 899 . 98 LEU CB C 41.59 0.42 1 900 . 98 LEU CG C 26.14 0.42 1 901 . 98 LEU CD1 C 24.90 0.16 1 902 . 98 LEU CD2 C 22.80 0.16 1 903 . 98 LEU N N 118.70 0.19 1 904 . 99 LYS H H 8.83 0.04 1 905 . 99 LYS HA H 2.51 0.13 1 906 . 99 LYS HB2 H 1.45 0.13 4 907 . 99 LYS HG2 H 1.10 0.13 4 908 . 99 LYS HD2 H 0.22 0.13 4 909 . 99 LYS HE2 H 0.72 0.13 4 910 . 99 LYS C C 176.85 0.25 1 911 . 99 LYS CA C 59.11 0.42 1 912 . 99 LYS CB C 32.05 0.42 1 913 . 99 LYS CG C 24.66 0.42 1 914 . 99 LYS CD C 29.01 0.42 1 915 . 99 LYS CE C 41.87 0.42 1 916 . 99 LYS N N 123.78 0.19 1 917 . 100 LYS H H 6.71 0.04 1 918 . 100 LYS HA H 4.03 0.13 1 919 . 100 LYS HB2 H 1.69 0.13 4 920 . 100 LYS HG2 H 1.28 0.13 4 921 . 100 LYS HD2 H 1.61 0.13 4 922 . 100 LYS HE2 H 2.97 0.13 4 923 . 100 LYS C C 178.61 0.25 1 924 . 100 LYS CA C 57.94 0.42 1 925 . 100 LYS CB C 33.45 0.42 1 926 . 100 LYS CG C 24.56 0.42 1 927 . 100 LYS CD C 29.37 0.42 1 928 . 100 LYS CE C 42.13 0.42 1 929 . 100 LYS N N 116.98 0.19 1 930 . 101 ALA H H 8.53 0.04 1 931 . 101 ALA HA H 3.94 0.13 1 932 . 101 ALA HB H 0.69 0.04 1 933 . 101 ALA C C 179.66 0.25 1 934 . 101 ALA CA C 54.65 0.42 1 935 . 101 ALA CB C 18.98 0.16 1 936 . 101 ALA N N 118.89 0.19 1 937 . 102 THR H H 7.94 0.04 1 938 . 102 THR HA H 4.67 0.13 1 939 . 102 THR HB H 5.08 0.13 1 940 . 102 THR HG2 H 1.27 0.04 1 941 . 102 THR C C 173.93 0.25 1 942 . 102 THR CA C 62.35 0.42 1 943 . 102 THR CB C 69.80 0.42 1 944 . 102 THR CG2 C 22.14 0.16 1 945 . 102 THR N N 102.12 0.19 1 946 . 103 ASN H H 7.11 0.04 1 947 . 103 ASN HA H 5.08 0.13 1 948 . 103 ASN HB2 H 2.89 0.13 2 949 . 103 ASN HB3 H 2.61 0.13 2 950 . 103 ASN C C 173.67 0.25 1 951 . 103 ASN CA C 53.00 0.42 1 952 . 103 ASN CB C 40.89 0.42 1 953 . 103 ASN N N 119.70 0.19 1 954 . 104 GLU H H 7.36 0.04 1 955 . 104 GLU CA C 57.44 0.42 1 956 . 104 GLU CB C 31.35 0.42 1 957 . 104 GLU N N 124.86 0.19 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 35 34 54,53,52,51,50 67,66,65,64 122,121,120,119 149,148,147 201,200,199 226,225,224,223 259,258,257,256 329,328,327 341,340,339,338 381,380,379 453,452,451,450 472,471,470 522,521,520,519,518 534,533,532 543,542 575,574,573,572 588,587,586,585 618,617 633,632,631,630,629 644,643,642,641 657,656,655,654 685,684,683 711,710,709,708 773,772,771,770 786,785,784,783 798,797,796 818,817 832,828,827,826 837,836 909,908,907,906 922,921,920,910 stop_ save_