data_5005 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone Sequential Resonance Assignments of Yeast iso-2 Cytochrome c, Reduced and Oxidized forms ; _BMRB_accession_number 5005 _BMRB_flat_file_name bmr5005.str _Entry_type original _Submission_date 2001-05-01 _Accession_date 2001-05-01 _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 Benavides-Garcia Maria G. . 2 Rivera Edna V. . 3 Ramos William . . 4 Hinck Andrew P. . 5 Nall Barry T. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 348 "13C chemical shifts" 418 "15N chemical shifts" 104 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-06-26 update author 'Update the chemical shift table.' 2002-04-05 original author 'Original release.' stop_ loop_ _Related_BMRB_accession_number _Relationship 5003 'reduced form' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone Sequential Resonance Assignments of Yeast iso-2 Cytochrome c, Reduced and Oxidized forms ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21882793 _PubMed_ID 11885986 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Benavides-Garcia Maria G. . 2 Rivera Edna V. . 3 Ramos William . . 4 Hinck Andrew P. . 5 Nall Barry T. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 22 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 93 _Page_last 94 _Year 2002 _Details . loop_ _Keyword 'Cytochrome c' 'NMR assignments' 'heme protein' 'yeast iso-2' 'E. coli expression' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_NMRPipe _Saveframe_category citation _Citation_full . _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes' _Citation_status . _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 96088118 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F. . . 2 Grzesiek S. . . 3 Vuister G. W. . 4 Zhu G. . . 5 Pfeifer J. . . 6 Bax A. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full . _Journal_volume 6 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 277 _Page_last 293 _Year 1995 _Details . save_ ################################## # Molecular system description # ################################## save_system_yeast_iso-2_cyt_c _Saveframe_category molecular_system _Mol_system_name 'oxidized yeast iso-2 cytochrome c' _Abbreviation_common 'yeast iso-2 cyt c' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'yeast iso-2 cyt c' $cyt_c 'oxidized heme' $HEC stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic yes _System_thiol_state 'all other bound' loop_ _Biological_function 'electron transfer protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cyt_c _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'yeast iso-2 cytochrome c, oxidized form' _Name_variant K72A _Abbreviation_common 'yeast iso-2 cyt c' _Molecular_mass 12958 _Mol_thiol_state 'all other bound' _Details ; Protein is in its oxidized state, which means that the Iron in the heme group is in the oxidation state +3" It has a K72A mutation ; ############################## # Polymer residue sequence # ############################## _Residue_count 112 _Mol_residue_sequence ; AKESTGFKPGSAKKGATLFK TRCQQCHTIEEGGPNKVGPN LHGIFGRHSGQVKGYSYTDA NINKNVKWDEDSMSEYLTNP AKYIPGTKMAFAGLKKEKDR NDLITYMTKAAK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -9 ALA 2 -8 LYS 3 -7 GLU 4 -6 SER 5 -5 THR 6 -4 GLY 7 -3 PHE 8 -2 LYS 9 -1 PRO 10 1 GLY 11 2 SER 12 3 ALA 13 4 LYS 14 5 LYS 15 6 GLY 16 7 ALA 17 8 THR 18 9 LEU 19 10 PHE 20 11 LYS 21 12 THR 22 13 ARG 23 14 CYS 24 15 GLN 25 16 GLN 26 17 CYS 27 18 HIS 28 19 THR 29 20 ILE 30 21 GLU 31 22 GLU 32 23 GLY 33 24 GLY 34 25 PRO 35 26 ASN 36 27 LYS 37 28 VAL 38 29 GLY 39 30 PRO 40 31 ASN 41 32 LEU 42 33 HIS 43 34 GLY 44 35 ILE 45 36 PHE 46 37 GLY 47 38 ARG 48 39 HIS 49 40 SER 50 41 GLY 51 42 GLN 52 43 VAL 53 44 LYS 54 45 GLY 55 46 TYR 56 47 SER 57 48 TYR 58 49 THR 59 50 ASP 60 51 ALA 61 52 ASN 62 53 ILE 63 54 ASN 64 55 LYS 65 56 ASN 66 57 VAL 67 58 LYS 68 59 TRP 69 60 ASP 70 61 GLU 71 62 ASP 72 63 SER 73 64 MET 74 65 SER 75 66 GLU 76 67 TYR 77 68 LEU 78 69 THR 79 70 ASN 80 71 PRO 81 72 ALA 82 73 LYS 83 74 TYR 84 75 ILE 85 76 PRO 86 77 GLY 87 78 THR 88 79 LYS 89 80 MET 90 81 ALA 91 82 PHE 92 83 ALA 93 84 GLY 94 85 LEU 95 86 LYS 96 87 LYS 97 88 GLU 98 89 LYS 99 90 ASP 100 91 ARG 101 92 ASN 102 93 ASP 103 94 LEU 104 95 ILE 105 96 THR 106 97 TYR 107 98 MET 108 99 THR 109 100 LYS 110 101 ALA 111 102 ALA 112 103 LYS 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 REF NP_010875 'Cytochrome c isoform 2' 100.00 113 99.11 99.11 7.64e-60 SWISS-PROT P00045 'Cytochrome c iso-2' 100.00 113 99.11 99.11 7.64e-60 GenBank AAD13974 'Unknown [Saccharomyces cerevisiae]' 100.00 113 99.11 99.11 7.64e-60 GenBank AAT93051 'YEL039C [Saccharomyces cerevisiae]' 100.00 113 99.11 99.11 7.64e-60 GenBank AAB59339 'iso-2-cytochrome c' 100.00 113 99.11 99.11 7.64e-60 GenBank AAB65003 'Cyc7p: cytochrome c, isoform-2 [Saccharomyces cerevisiae]' 100.00 113 99.11 99.11 7.64e-60 EMBL CAA24606 'unnamed protein product [Saccharomyces cerevisiae]' 100.00 113 99.11 99.11 7.64e-60 GenBank AAA34940 'cytochrome c isozyme' 100.00 113 99.11 99.11 7.64e-60 PDB 1YTC 'Thermodynamic Cycles As Probes Of Structure-Function Relationships In Unfolded Proteins' 100.00 112 98.21 98.21 7.90e-59 PDB 3CXH 'Structure Of Yeast Complex Iii With Isoform-2 Cytochrome C' 100.00 112 99.11 99.11 7.90e-60 BMRB 5003 'yeast iso-2 cytochrome c, reduced form' 100.00 112 100.00 100.00 2.13e-60 PDB 1YEA 'Structure Determination And Analysis Of Yeast Iso-2- Cytochrome C And A Composite Mutant Protein' 100.00 112 99.11 99.11 7.51e-60 stop_ save_ ############# # Ligands # ############# save_HEC _Saveframe_category ligand _Mol_type non-polymer _Name_common "HEC (HEME C)" _BMRB_code . _PDB_code HEC _Molecular_mass 618.503 _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 Wed Jun 8 16:15:05 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons FE FE FE . 0 . ? CHA CHA C . 0 . ? CHB CHB C . 0 . ? CHC CHC C . 0 . ? CHD CHD C . 0 . ? NA NA N . 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 . ? NB NB N . 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 . ? NC NC N . 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 . ? ND ND N . 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 . ? HHA HHA H . 0 . ? HHB HHB H . 0 . ? HHC HHC H . 0 . ? HHD HHD H . 0 . ? HMA1 HMA1 H . 0 . ? HMA2 HMA2 H . 0 . ? HMA3 HMA3 H . 0 . ? HAA1 HAA1 H . 0 . ? HAA2 HAA2 H . 0 . ? HBA1 HBA1 H . 0 . ? HBA2 HBA2 H . 0 . ? H2A H2A H . 0 . ? HMB1 HMB1 H . 0 . ? HMB2 HMB2 H . 0 . ? HMB3 HMB3 H . 0 . ? HAB HAB H . 0 . ? HBB1 HBB1 H . 0 . ? HBB2 HBB2 H . 0 . ? HBB3 HBB3 H . 0 . ? HMC1 HMC1 H . 0 . ? HMC2 HMC2 H . 0 . ? HMC3 HMC3 H . 0 . ? HAC HAC H . 0 . ? HBC1 HBC1 H . 0 . ? HBC2 HBC2 H . 0 . ? HBC3 HBC3 H . 0 . ? HMD1 HMD1 H . 0 . ? HMD2 HMD2 H . 0 . ? HMD3 HMD3 H . 0 . ? HAD1 HAD1 H . 0 . ? HAD2 HAD2 H . 0 . ? HBD1 HBD1 H . 0 . ? HBD2 HBD2 H . 0 . ? H2D H2D 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 FE NA ? ? SING FE NB ? ? SING FE NC ? ? SING FE 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 ? ? DOUB CHD C4C ? ? SING 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 ? ? SING NB C1B ? ? SING NB C4B ? ? DOUB C1B C2B ? ? SING C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? DOUB C3B CAB ? ? SING CMB HMB1 ? ? SING CMB HMB2 ? ? SING CMB HMB3 ? ? SING CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB1 ? ? SING CBB HBB2 ? ? SING CBB HBB3 ? ? SING NC C1C ? ? SING NC C4C ? ? DOUB C1C C2C ? ? SING C2C C3C ? ? SING C2C CMC ? ? SING C3C C4C ? ? DOUB C3C CAC ? ? SING CMC HMC1 ? ? SING CMC HMC2 ? ? SING CMC HMC3 ? ? SING CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC1 ? ? SING CBC HBC2 ? ? SING CBC HBC3 ? ? SING ND C1D ? ? SING ND C4D ? ? DOUB C1D C2D ? ? SING C2D C3D ? ? SING C2D CMD ? ? DOUB 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 $cyt_c 'Baker's yeast' 4932 Eukaryota Fungi Saccharomyces cerevisiae stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name _Details $cyt_c 'recombinant technology' 'E. coli' Escherichia coli K12 BL21(DE3) plasmid pERICYC7 'Succcessful expression required coexpression of cytochrome c heme lyase' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $cyt_c 2.0 mM 1.8 2.2 '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.8 loop_ _Task processing stop_ _Details . _Citation_label $ref_NMRPipe save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_HSQC_COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'HSQC COSY' _Sample_label $sample1 save_ save_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample1 save_ save_C(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _Sample_label $sample1 save_ save_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample1 save_ save_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label $sample1 save_ save_HBHA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label $sample1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'HSQC COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.1 n/a temperature 293 1 K 'ionic strength' 0.13 0.02 M 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 DSS H 1 'methyl protons' ppm 0.00 external direct cylindrical external_to_the_sample parallel_to_Bo 1.0 DSS C 13 'methyl protons' ppm 0.00 external indirect cylindrical external_to_the_sample parallel_to_Bo 0.251449530 DSS N 15 'methyl protons' ppm 0.00 external indirect cylindrical external_to_the_sample parallel_to_Bo 0.10132918 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_csr1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample1 stop_ _Sample_conditions_label $condition1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'yeast iso-2 cyt 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 . 2 LYS C C 176.20 0.40 1 2 . 2 LYS CA C 56.50 0.40 1 3 . 2 LYS CB C 32.70 0.40 1 4 . 2 LYS CG C 24.40 0.40 1 5 . 2 LYS CD C 28.90 0.40 1 6 . 2 LYS CE C 41.90 0.40 1 7 . 3 GLU H H 8.62 0.02 1 8 . 3 GLU HA H 4.24 0.02 1 9 . 3 GLU HB2 H 1.94 0.02 1 10 . 3 GLU HB3 H 1.94 0.02 1 11 . 3 GLU C C 176.50 0.40 1 12 . 3 GLU CA C 56.60 0.40 1 13 . 3 GLU CB C 30.00 0.40 1 14 . 3 GLU CG C 36.00 0.40 1 15 . 3 GLU N N 122.70 0.25 1 16 . 4 SER H H 8.33 0.02 1 17 . 4 SER HA H 3.95 0.02 1 18 . 4 SER HB2 H 0.61 0.02 1 19 . 4 SER HB3 H 0.61 0.02 1 20 . 4 SER C C 174.70 0.40 1 21 . 4 SER CA C 57.60 0.40 1 22 . 4 SER CB C 63.60 0.40 1 23 . 4 SER N N 116.80 0.25 1 24 . 5 THR H H 8.30 0.02 1 25 . 5 THR HA H 4.28 0.02 1 26 . 5 THR C C 174.90 0.40 1 27 . 5 THR CA C 61.40 0.40 1 28 . 5 THR CB C 69.70 0.40 1 29 . 5 THR CG2 C 21.30 0.40 1 30 . 5 THR N N 115.60 0.25 1 31 . 6 GLY H H 8.25 0.02 1 32 . 6 GLY HA2 H 3.90 0.02 1 33 . 6 GLY HA3 H 3.90 0.02 1 34 . 6 GLY C C 173.60 0.40 1 35 . 6 GLY CA C 44.50 0.40 1 36 . 6 GLY N N 111.00 0.25 1 37 . 7 PHE H H 8.66 0.02 1 38 . 7 PHE HA H 4.23 0.02 1 39 . 7 PHE HB2 H 2.67 0.02 1 40 . 7 PHE HB3 H 2.67 0.02 1 41 . 7 PHE C C 175.10 0.40 1 42 . 7 PHE CA C 58.70 0.40 1 43 . 7 PHE CB C 39.40 0.40 1 44 . 7 PHE N N 122.10 0.25 1 45 . 8 LYS H H 6.20 0.02 1 46 . 8 LYS CA C 52.40 0.40 1 47 . 8 LYS CB C 34.10 0.40 1 48 . 8 LYS N N 128.10 0.25 1 49 . 9 PRO HA H 3.66 0.02 1 50 . 9 PRO HB2 H 1.65 0.02 2 51 . 9 PRO HB3 H 2.12 0.02 2 52 . 9 PRO C C 177.30 0.40 1 53 . 9 PRO CA C 63.20 0.40 1 54 . 9 PRO CB C 31.80 0.40 1 55 . 9 PRO CG C 27.20 0.40 1 56 . 9 PRO CD C 49.80 0.40 1 57 . 10 GLY H H 8.24 0.02 1 58 . 10 GLY HA2 H 4.28 0.02 2 59 . 10 GLY HA3 H 3.26 0.02 2 60 . 10 GLY C C 172.90 0.40 1 61 . 10 GLY CA C 43.50 0.40 1 62 . 10 GLY N N 112.70 0.25 1 63 . 11 SER H H 9.41 0.02 1 64 . 11 SER HA H 4.64 0.02 1 65 . 11 SER HB2 H 3.52 0.02 2 66 . 11 SER HB3 H 3.76 0.02 2 67 . 11 SER C C 175.30 0.40 1 68 . 11 SER CA C 55.00 0.40 1 69 . 11 SER CB C 62.80 0.40 1 70 . 11 SER N N 120.70 0.25 1 71 . 12 ALA H H 9.19 0.02 1 72 . 12 ALA HA H 3.87 0.02 1 73 . 12 ALA HB H 1.38 0.02 1 74 . 12 ALA C C 179.70 0.40 1 75 . 12 ALA CA C 54.90 0.40 1 76 . 12 ALA CB C 17.90 0.40 1 77 . 12 ALA N N 132.00 0.25 1 78 . 13 LYS H H 8.13 0.02 1 79 . 13 LYS HA H 3.92 0.02 1 80 . 13 LYS HB2 H 1.60 0.02 1 81 . 13 LYS HB3 H 1.60 0.02 1 82 . 13 LYS C C 179.30 0.40 1 83 . 13 LYS CA C 59.30 0.40 1 84 . 13 LYS CB C 32.30 0.40 1 85 . 13 LYS CG C 24.90 0.40 1 86 . 13 LYS CD C 29.00 0.40 1 87 . 13 LYS CE C 42.30 0.40 1 88 . 13 LYS N N 119.50 0.25 1 89 . 14 LYS H H 7.60 0.02 1 90 . 14 LYS HA H 4.00 0.02 1 91 . 14 LYS HB2 H 1.59 0.02 1 92 . 14 LYS HB3 H 1.59 0.02 1 93 . 14 LYS C C 180.60 0.40 1 94 . 14 LYS CA C 58.00 0.40 1 95 . 14 LYS CB C 31.90 0.40 1 96 . 14 LYS CG C 25.20 0.40 1 97 . 14 LYS CD C 28.20 0.40 1 98 . 14 LYS CE C 41.80 0.40 1 99 . 14 LYS N N 120.00 0.25 1 100 . 15 GLY H H 8.57 0.02 1 101 . 15 GLY HA2 H 3.18 0.02 2 102 . 15 GLY HA3 H 3.95 0.02 2 103 . 15 GLY C C 174.20 0.40 1 104 . 15 GLY CA C 46.80 0.40 1 105 . 15 GLY N N 107.70 0.25 1 106 . 16 ALA H H 7.87 0.02 1 107 . 16 ALA HA H 2.23 0.02 1 108 . 16 ALA HB H 1.09 0.02 1 109 . 16 ALA C C 180.60 0.40 1 110 . 16 ALA CA C 54.50 0.40 1 111 . 16 ALA CB C 18.30 0.40 1 112 . 16 ALA N N 125.30 0.25 1 113 . 17 THR H H 7.02 0.02 1 114 . 17 THR HA H 4.07 0.02 1 115 . 17 THR HB H 3.83 0.02 1 116 . 17 THR C C 177.30 0.40 1 117 . 17 THR CA C 65.80 0.40 1 118 . 17 THR CB C 68.10 0.40 1 119 . 17 THR CG2 C 22.00 0.40 1 120 . 17 THR N N 115.40 0.25 1 121 . 18 LEU H H 7.70 0.02 1 122 . 18 LEU HA H 3.66 0.02 1 123 . 18 LEU HB2 H 1.71 0.02 1 124 . 18 LEU HB3 H 1.71 0.02 1 125 . 18 LEU C C 177.60 0.40 1 126 . 18 LEU CA C 57.70 0.40 1 127 . 18 LEU CB C 42.60 0.40 1 128 . 18 LEU CG C 27.30 0.40 1 129 . 18 LEU CD1 C 23.00 0.40 1 130 . 18 LEU CD2 C 23.00 0.40 1 131 . 18 LEU N N 123.60 0.25 1 132 . 19 PHE H H 8.51 0.02 1 133 . 19 PHE HA H 3.34 0.02 1 134 . 19 PHE HB2 H 2.90 0.02 1 135 . 19 PHE HB3 H 2.90 0.02 1 136 . 19 PHE C C 178.70 0.40 1 137 . 19 PHE CA C 62.80 0.40 1 138 . 19 PHE CB C 39.60 0.40 1 139 . 19 PHE N N 121.00 0.25 1 140 . 20 LYS H H 8.22 0.02 1 141 . 20 LYS HA H 4.29 0.02 1 142 . 20 LYS HB2 H 2.03 0.02 1 143 . 20 LYS HB3 H 2.03 0.02 1 144 . 20 LYS C C 178.10 0.40 1 145 . 20 LYS CA C 59.50 0.40 1 146 . 20 LYS CB C 32.70 0.40 1 147 . 20 LYS CG C 25.00 0.40 1 148 . 20 LYS CD C 29.40 0.40 1 149 . 20 LYS CE C 42.20 0.40 1 150 . 20 LYS N N 120.40 0.25 1 151 . 21 THR H H 7.93 0.02 1 152 . 21 THR HA H 4.23 0.02 1 153 . 21 THR HB H 4.06 0.02 1 154 . 21 THR C C 176.90 0.40 1 155 . 21 THR CA C 63.60 0.40 1 156 . 21 THR CB C 70.30 0.40 1 157 . 21 THR CG2 C 21.70 0.40 1 158 . 21 THR N N 107.10 0.25 1 159 . 22 ARG H H 8.21 0.02 1 160 . 22 ARG HA H 4.40 0.02 1 161 . 22 ARG HB2 H 1.54 0.02 1 162 . 22 ARG HB3 H 1.54 0.02 1 163 . 22 ARG C C 176.80 0.40 1 164 . 22 ARG CA C 54.60 0.40 1 165 . 22 ARG CB C 30.60 0.40 1 166 . 22 ARG CG C 26.40 0.40 1 167 . 22 ARG CD C 41.60 0.40 1 168 . 22 ARG N N 116.00 0.25 1 169 . 23 CYS H H 7.60 0.02 1 170 . 23 CYS HA H 4.39 0.02 1 171 . 23 CYS HB2 H 1.25 0.02 1 172 . 23 CYS HB3 H 1.25 0.02 1 173 . 23 CYS C C 178.60 0.40 1 174 . 23 CYS CA C 54.50 0.40 1 175 . 23 CYS CB C 36.00 0.40 1 176 . 23 CYS N N 114.20 0.25 1 177 . 24 GLN H H 8.28 0.02 1 178 . 24 GLN HA H 6.40 0.02 1 179 . 24 GLN HB2 H 2.79 0.02 1 180 . 24 GLN HB3 H 2.79 0.02 1 181 . 24 GLN C C 177.10 0.40 1 182 . 24 GLN CA C 58.50 0.40 1 183 . 24 GLN CB C 29.90 0.40 1 184 . 24 GLN CG C 34.50 0.40 1 185 . 24 GLN N N 122.10 0.25 1 186 . 25 GLN H H 10.24 0.02 1 187 . 25 GLN HA H 4.70 0.02 1 188 . 25 GLN HB2 H 2.31 0.02 1 189 . 25 GLN HB3 H 2.31 0.02 1 190 . 25 GLN C C 178.30 0.40 1 191 . 25 GLN CA C 59.10 0.40 1 192 . 25 GLN CB C 28.50 0.40 1 193 . 25 GLN CG C 33.80 0.40 1 194 . 25 GLN N N 119.60 0.25 1 195 . 26 CYS H H 9.66 0.02 1 196 . 26 CYS C C 176.50 0.40 1 197 . 26 CYS CA C 58.00 0.40 1 198 . 26 CYS CB C 37.30 0.40 1 199 . 26 CYS N N 114.30 0.25 1 200 . 27 HIS H H 11.44 0.02 1 201 . 27 HIS C C 174.20 0.40 1 202 . 27 HIS CA C 76.90 0.40 1 203 . 27 HIS CB C 26.90 0.40 1 204 . 27 HIS N N 119.60 0.25 1 205 . 28 THR H H 10.76 0.02 1 206 . 28 THR HA H 6.25 0.02 1 207 . 28 THR HB H 5.50 0.02 1 208 . 28 THR C C 175.80 0.40 1 209 . 28 THR CA C 61.10 0.40 1 210 . 28 THR CB C 72.90 0.40 1 211 . 28 THR CG2 C 23.30 0.40 1 212 . 28 THR N N 112.40 0.25 1 213 . 29 ILE H H 9.30 0.02 1 214 . 29 ILE HA H 5.03 0.02 1 215 . 29 ILE HB H 3.41 0.02 1 216 . 29 ILE C C 173.10 0.40 1 217 . 29 ILE CA C 61.50 0.40 1 218 . 29 ILE CB C 43.30 0.40 1 219 . 29 ILE CG2 C 15.40 0.40 1 220 . 29 ILE CD1 C 15.00 0.40 1 221 . 29 ILE N N 119.80 0.25 1 222 . 30 GLU H H 9.50 0.02 1 223 . 30 GLU HA H 4.54 0.02 1 224 . 30 GLU HB2 H 2.19 0.02 1 225 . 30 GLU HB3 H 2.19 0.02 1 226 . 30 GLU C C 177.70 0.40 1 227 . 30 GLU CA C 56.50 0.40 1 228 . 30 GLU CB C 29.70 0.40 1 229 . 30 GLU CG C 36.00 0.40 1 230 . 30 GLU N N 124.10 0.25 1 231 . 31 GLU H H 8.95 0.02 1 232 . 31 GLU HA H 3.38 0.02 1 233 . 31 GLU HB2 H 0.90 0.02 2 234 . 31 GLU HB3 H 1.65 0.02 2 235 . 31 GLU C C 177.30 0.40 1 236 . 31 GLU CA C 58.10 0.40 1 237 . 31 GLU CB C 28.80 0.40 1 238 . 31 GLU CG C 35.40 0.40 1 239 . 31 GLU N N 126.50 0.25 1 240 . 32 GLY H H 9.41 0.02 1 241 . 32 GLY HA2 H 4.05 0.02 2 242 . 32 GLY HA3 H 3.72 0.02 2 243 . 32 GLY C C 174.90 0.40 1 244 . 32 GLY CA C 45.20 0.40 1 245 . 32 GLY N N 117.30 0.25 1 246 . 33 GLY H H 8.11 0.02 1 247 . 33 GLY C C 171.50 0.40 1 248 . 33 GLY CA C 44.50 0.40 1 249 . 33 GLY N N 108.20 0.25 1 250 . 34 PRO HA H 4.68 0.02 1 251 . 34 PRO HB2 H 1.52 0.02 1 252 . 34 PRO HB3 H 1.52 0.02 1 253 . 34 PRO C C 179.70 0.40 1 254 . 34 PRO CA C 62.30 0.40 1 255 . 34 PRO CB C 31.90 0.40 1 256 . 34 PRO CG C 27.30 0.40 1 257 . 35 ASN H H 9.16 0.02 1 258 . 35 ASN C C 174.50 0.40 1 259 . 35 ASN CA C 54.20 0.40 1 260 . 35 ASN CB C 38.20 0.40 1 261 . 35 ASN N N 120.90 0.25 1 262 . 36 LYS H H 8.10 0.02 1 263 . 36 LYS HA H 4.64 0.02 1 264 . 36 LYS HB2 H 2.41 0.02 1 265 . 36 LYS HB3 H 2.41 0.02 1 266 . 36 LYS C C 176.20 0.40 1 267 . 36 LYS CA C 55.10 0.40 1 268 . 36 LYS CB C 32.60 0.40 1 269 . 36 LYS CG C 24.70 0.40 1 270 . 36 LYS CD C 30.00 0.40 1 271 . 36 LYS N N 125.30 0.25 1 272 . 37 VAL H H 7.71 0.02 1 273 . 37 VAL HA H 2.92 0.02 1 274 . 37 VAL HB H 1.37 0.02 1 275 . 37 VAL C C 175.90 0.40 1 276 . 37 VAL CA C 65.70 0.40 1 277 . 37 VAL CB C 32.40 0.40 1 278 . 37 VAL CG1 C 20.00 0.40 1 279 . 37 VAL CG2 C 22.70 0.40 1 280 . 37 VAL N N 123.40 0.25 1 281 . 38 GLY H H 8.01 0.02 1 282 . 38 GLY CA C 38.10 0.40 1 283 . 38 GLY N N 133.00 0.25 1 284 . 39 PRO HA H 3.65 0.02 1 285 . 39 PRO C C 177.10 0.40 1 286 . 39 PRO CA C 60.60 0.40 1 287 . 39 PRO CB C 30.10 0.40 1 288 . 39 PRO CG C 24.30 0.40 1 289 . 40 ASN H H 8.90 0.02 1 290 . 40 ASN HA H 5.92 0.02 1 291 . 40 ASN HB2 H 2.96 0.02 2 292 . 40 ASN HB3 H 3.49 0.02 2 293 . 40 ASN C C 176.30 0.40 1 294 . 40 ASN CA C 56.00 0.40 1 295 . 40 ASN CB C 40.70 0.40 1 296 . 40 ASN N N 123.50 0.25 1 297 . 41 LEU H H 9.60 0.02 1 298 . 41 LEU HA H 4.63 0.02 1 299 . 41 LEU HB2 H 3.91 0.02 1 300 . 41 LEU HB3 H 3.91 0.02 1 301 . 41 LEU C C 176.30 0.40 1 302 . 41 LEU CA C 54.20 0.40 1 303 . 41 LEU CB C 43.80 0.40 1 304 . 41 LEU CG C 26.80 0.40 1 305 . 41 LEU N N 121.10 0.25 1 306 . 42 HIS H H 8.35 0.02 1 307 . 42 HIS HA H 4.04 0.02 1 308 . 42 HIS HB2 H 3.23 0.02 1 309 . 42 HIS HB3 H 3.23 0.02 1 310 . 42 HIS C C 177.60 0.40 1 311 . 42 HIS CA C 60.20 0.40 1 312 . 42 HIS CB C 27.90 0.40 1 313 . 42 HIS N N 120.80 0.25 1 314 . 43 GLY H H 9.17 0.02 1 315 . 43 GLY HA2 H 3.72 0.02 1 316 . 43 GLY HA3 H 3.72 0.02 1 317 . 43 GLY C C 175.50 0.40 1 318 . 43 GLY CA C 46.10 0.40 1 319 . 43 GLY N N 116.80 0.25 1 320 . 44 ILE H H 6.86 0.02 1 321 . 44 ILE HA H 3.53 0.02 1 322 . 44 ILE HB H 1.31 0.02 1 323 . 44 ILE C C 174.00 0.40 1 324 . 44 ILE CA C 60.70 0.40 1 325 . 44 ILE CB C 37.60 0.40 1 326 . 44 ILE CG1 C 29.20 0.40 1 327 . 44 ILE CG2 C 18.30 0.40 1 328 . 44 ILE CD1 C 14.90 0.40 1 329 . 44 ILE N N 115.70 0.25 1 330 . 45 PHE H H 6.90 0.02 1 331 . 45 PHE HA H 3.84 0.02 1 332 . 45 PHE HB2 H 2.51 0.02 1 333 . 45 PHE HB3 H 2.51 0.02 1 334 . 45 PHE C C 176.20 0.40 1 335 . 45 PHE CA C 60.00 0.40 1 336 . 45 PHE CB C 36.50 0.40 1 337 . 45 PHE N N 115.50 0.25 1 338 . 46 GLY H H 8.73 0.02 1 339 . 46 GLY HA2 H 4.15 0.02 2 340 . 46 GLY HA3 H 3.67 0.02 2 341 . 46 GLY C C 173.60 0.40 1 342 . 46 GLY CA C 44.50 0.40 1 343 . 46 GLY N N 111.10 0.25 1 344 . 47 ARG H H 7.72 0.02 1 345 . 47 ARG HA H 4.57 0.02 1 346 . 47 ARG HB2 H 1.77 0.02 2 347 . 47 ARG HB3 H 1.86 0.02 2 348 . 47 ARG C C 175.60 0.40 1 349 . 47 ARG CA C 54.70 0.40 1 350 . 47 ARG CB C 32.40 0.40 1 351 . 47 ARG CG C 27.20 0.40 1 352 . 47 ARG CD C 43.60 0.40 1 353 . 47 ARG N N 121.00 0.25 1 354 . 48 HIS H H 8.20 0.02 1 355 . 48 HIS HA H 4.51 0.02 1 356 . 48 HIS HB2 H 3.77 0.02 1 357 . 48 HIS HB3 H 3.77 0.02 1 358 . 48 HIS C C 176.20 0.40 1 359 . 48 HIS CA C 55.80 0.40 1 360 . 48 HIS CB C 29.90 0.40 1 361 . 48 HIS N N 118.00 0.25 1 362 . 49 SER H H 8.41 0.02 1 363 . 49 SER HA H 4.43 0.02 1 364 . 49 SER HB2 H 3.58 0.02 1 365 . 49 SER HB3 H 3.58 0.02 1 366 . 49 SER C C 175.40 0.40 1 367 . 49 SER CA C 58.40 0.40 1 368 . 49 SER CB C 63.70 0.40 1 369 . 49 SER N N 116.00 0.25 1 370 . 50 GLY H H 8.89 0.02 1 371 . 50 GLY HA2 H 3.03 0.02 2 372 . 50 GLY HA3 H 1.06 0.02 2 373 . 50 GLY C C 174.90 0.40 1 374 . 50 GLY CA C 45.30 0.40 1 375 . 50 GLY N N 110.00 0.25 1 376 . 51 GLN H H 8.02 0.02 1 377 . 51 GLN HA H 4.31 0.02 1 378 . 51 GLN HB2 H 1.60 0.02 2 379 . 51 GLN HB3 H 2.29 0.02 2 380 . 51 GLN C C 176.40 0.40 1 381 . 51 GLN CA C 54.80 0.40 1 382 . 51 GLN CB C 29.90 0.40 1 383 . 51 GLN CG C 33.60 0.40 1 384 . 51 GLN N N 113.70 0.25 1 385 . 52 VAL H H 7.80 0.02 1 386 . 52 VAL HA H 3.70 0.02 1 387 . 52 VAL HB H 1.97 0.02 1 388 . 52 VAL C C 176.90 0.40 1 389 . 52 VAL CA C 65.40 0.40 1 390 . 52 VAL CB C 30.40 0.40 1 391 . 52 VAL CG1 C 21.10 0.40 1 392 . 52 VAL CG2 C 22.70 0.40 1 393 . 52 VAL N N 123.10 0.25 1 394 . 53 LYS H H 8.55 0.02 1 395 . 53 LYS HA H 3.97 0.02 1 396 . 53 LYS HB2 H 1.73 0.02 1 397 . 53 LYS HB3 H 1.73 0.02 1 398 . 53 LYS C C 178.00 0.40 1 399 . 53 LYS CA C 57.30 0.40 1 400 . 53 LYS CB C 32.00 0.40 1 401 . 53 LYS CG C 24.60 0.40 1 402 . 53 LYS CD C 28.80 0.40 1 403 . 53 LYS CE C 42.10 0.40 1 404 . 53 LYS N N 130.30 0.25 1 405 . 54 GLY H H 8.74 0.02 1 406 . 54 GLY HA2 H 3.91 0.02 2 407 . 54 GLY HA3 H 3.46 0.02 2 408 . 54 GLY C C 173.00 0.40 1 409 . 54 GLY CA C 45.10 0.40 1 410 . 54 GLY N N 111.60 0.25 1 411 . 55 TYR H H 7.03 0.02 1 412 . 55 TYR HA H 3.74 0.02 1 413 . 55 TYR HB2 H 1.95 0.02 1 414 . 55 TYR HB3 H 1.95 0.02 1 415 . 55 TYR C C 173.60 0.40 1 416 . 55 TYR CA C 57.20 0.40 1 417 . 55 TYR CB C 39.20 0.40 1 418 . 55 TYR N N 119.90 0.25 1 419 . 56 SER H H 6.47 0.02 1 420 . 56 SER HA H 3.93 0.02 1 421 . 56 SER HB2 H 2.87 0.02 2 422 . 56 SER HB3 H 3.06 0.02 2 423 . 56 SER C C 171.30 0.40 1 424 . 56 SER CA C 55.60 0.40 1 425 . 56 SER CB C 61.10 0.40 1 426 . 56 SER N N 122.50 0.25 1 427 . 57 TYR H H 7.58 0.02 1 428 . 57 TYR HA H 4.03 0.02 1 429 . 57 TYR HB2 H 3.17 0.02 1 430 . 57 TYR HB3 H 3.17 0.02 1 431 . 57 TYR C C 179.30 0.40 1 432 . 57 TYR CA C 58.20 0.40 1 433 . 57 TYR CB C 41.60 0.40 1 434 . 57 TYR N N 124.80 0.25 1 435 . 58 THR H H 9.55 0.02 1 436 . 58 THR HA H 4.53 0.02 1 437 . 58 THR HB H 4.09 0.02 1 438 . 58 THR C C 176.20 0.40 1 439 . 58 THR CA C 61.90 0.40 1 440 . 58 THR CB C 70.80 0.40 1 441 . 58 THR CG2 C 21.80 0.40 1 442 . 58 THR N N 112.50 0.25 1 443 . 59 ASP H H 8.57 0.02 1 444 . 59 ASP HA H 4.20 0.02 1 445 . 59 ASP HB2 H 2.49 0.02 1 446 . 59 ASP HB3 H 2.49 0.02 1 447 . 59 ASP C C 178.60 0.40 1 448 . 59 ASP CA C 56.90 0.40 1 449 . 59 ASP CB C 39.30 0.40 1 450 . 59 ASP N N 121.20 0.25 1 451 . 60 ALA H H 7.98 0.02 1 452 . 60 ALA HA H 4.08 0.02 1 453 . 60 ALA HB H 1.55 0.02 1 454 . 60 ALA C C 179.80 0.40 1 455 . 60 ALA CA C 55.10 0.40 1 456 . 60 ALA CB C 18.60 0.40 1 457 . 60 ALA N N 120.20 0.25 1 458 . 61 ASN H H 8.27 0.02 1 459 . 61 ASN HA H 4.56 0.02 1 460 . 61 ASN HB2 H 2.82 0.02 2 461 . 61 ASN HB3 H 3.02 0.02 2 462 . 61 ASN C C 178.80 0.40 1 463 . 61 ASN CA C 55.80 0.40 1 464 . 61 ASN CB C 40.20 0.40 1 465 . 61 ASN N N 118.00 0.25 1 466 . 62 ILE H H 7.59 0.02 1 467 . 62 ILE HA H 3.44 0.02 1 468 . 62 ILE HB H 1.70 0.02 1 469 . 62 ILE C C 178.20 0.40 1 470 . 62 ILE CA C 65.30 0.40 1 471 . 62 ILE CB C 38.80 0.40 1 472 . 62 ILE CG1 C 28.20 0.40 1 473 . 62 ILE CG2 C 16.90 0.40 1 474 . 62 ILE CD1 C 13.70 0.40 1 475 . 62 ILE N N 121.10 0.25 1 476 . 63 ASN H H 8.91 0.02 1 477 . 63 ASN HA H 4.32 0.02 1 478 . 63 ASN HB2 H 2.71 0.02 1 479 . 63 ASN HB3 H 2.71 0.02 1 480 . 63 ASN C C 176.60 0.40 1 481 . 63 ASN CA C 54.40 0.40 1 482 . 63 ASN CB C 37.90 0.40 1 483 . 63 ASN N N 117.40 0.25 1 484 . 64 LYS H H 7.33 0.02 1 485 . 64 LYS HA H 4.03 0.02 1 486 . 64 LYS HB2 H 1.97 0.02 1 487 . 64 LYS HB3 H 1.97 0.02 1 488 . 64 LYS C C 176.60 0.40 1 489 . 64 LYS CA C 56.80 0.40 1 490 . 64 LYS CB C 31.40 0.40 1 491 . 64 LYS CG C 24.00 0.40 1 492 . 64 LYS CD C 28.30 0.40 1 493 . 64 LYS N N 119.70 0.25 1 494 . 65 ASN H H 7.39 0.02 1 495 . 65 ASN HA H 4.28 0.02 1 496 . 65 ASN HB2 H 2.29 0.02 2 497 . 65 ASN HB3 H 2.95 0.02 2 498 . 65 ASN C C 174.10 0.40 1 499 . 65 ASN CA C 53.60 0.40 1 500 . 65 ASN CB C 37.00 0.40 1 501 . 65 ASN N N 113.20 0.25 1 502 . 66 VAL H H 7.23 0.02 1 503 . 66 VAL HA H 4.00 0.02 1 504 . 66 VAL HB H 1.29 0.02 1 505 . 66 VAL C C 173.60 0.40 1 506 . 66 VAL CA C 59.20 0.40 1 507 . 66 VAL CB C 33.70 0.40 1 508 . 66 VAL CG1 C 17.70 0.40 1 509 . 66 VAL CG2 C 20.50 0.40 1 510 . 66 VAL N N 115.90 0.25 1 511 . 67 LYS H H 8.17 0.02 1 512 . 67 LYS HA H 3.62 0.02 1 513 . 67 LYS HB2 H 0.79 0.02 2 514 . 67 LYS HB3 H 1.50 0.02 2 515 . 67 LYS C C 175.60 0.40 1 516 . 67 LYS CA C 54.60 0.40 1 517 . 67 LYS CB C 31.30 0.40 1 518 . 67 LYS CG C 24.50 0.40 1 519 . 67 LYS CD C 28.90 0.40 1 520 . 67 LYS CE C 41.90 0.40 1 521 . 67 LYS N N 127.30 0.25 1 522 . 68 TRP H H 7.75 0.02 1 523 . 68 TRP HA H 4.42 0.02 1 524 . 68 TRP HB2 H 1.98 0.02 2 525 . 68 TRP HB3 H 3.31 0.02 2 526 . 68 TRP C C 175.80 0.40 1 527 . 68 TRP CA C 57.80 0.40 1 528 . 68 TRP CB C 29.80 0.40 1 529 . 68 TRP N N 127.70 0.25 1 530 . 69 ASP H H 8.21 0.02 1 531 . 69 ASP HA H 4.61 0.02 1 532 . 69 ASP HB2 H 2.88 0.02 1 533 . 69 ASP HB3 H 2.88 0.02 1 534 . 69 ASP C C 174.70 0.40 1 535 . 69 ASP CA C 52.10 0.40 1 536 . 69 ASP CB C 42.00 0.40 1 537 . 69 ASP N N 122.00 0.25 1 538 . 70 GLU H H 10.44 0.02 1 539 . 70 GLU HA H 4.12 0.02 1 540 . 70 GLU HB2 H 3.08 0.02 1 541 . 70 GLU HB3 H 3.08 0.02 1 542 . 70 GLU C C 177.80 0.40 1 543 . 70 GLU CA C 62.70 0.40 1 544 . 70 GLU CB C 28.30 0.40 1 545 . 70 GLU CG C 36.00 0.40 1 546 . 70 GLU N N 120.10 0.25 1 547 . 71 ASP H H 8.04 0.02 1 548 . 71 ASP HA H 4.34 0.02 1 549 . 71 ASP HB2 H 2.62 0.02 1 550 . 71 ASP HB3 H 2.62 0.02 1 551 . 71 ASP C C 179.70 0.40 1 552 . 71 ASP CA C 57.60 0.40 1 553 . 71 ASP CB C 40.60 0.40 1 554 . 71 ASP N N 117.60 0.25 1 555 . 72 SER H H 9.02 0.02 1 556 . 72 SER HA H 4.26 0.02 1 557 . 72 SER HB2 H 4.05 0.02 1 558 . 72 SER HB3 H 4.05 0.02 1 559 . 72 SER C C 177.70 0.40 1 560 . 72 SER CA C 61.10 0.40 1 561 . 72 SER CB C 62.60 0.40 1 562 . 72 SER N N 119.10 0.25 1 563 . 73 MET H H 8.65 0.02 1 564 . 73 MET HA H 4.24 0.02 1 565 . 73 MET HB2 H 1.80 0.02 1 566 . 73 MET HB3 H 1.80 0.02 1 567 . 73 MET C C 177.60 0.40 1 568 . 73 MET CA C 56.20 0.40 1 569 . 73 MET CB C 29.10 0.40 1 570 . 73 MET N N 121.20 0.25 1 571 . 74 SER H H 7.69 0.02 1 572 . 74 SER HA H 3.40 0.02 1 573 . 74 SER C C 177.30 0.40 1 574 . 74 SER CA C 61.40 0.40 1 575 . 74 SER CB C 62.70 0.40 1 576 . 74 SER N N 113.40 0.25 1 577 . 75 GLU H H 7.82 0.02 1 578 . 75 GLU HA H 3.79 0.02 1 579 . 75 GLU HB2 H 1.85 0.02 2 580 . 75 GLU HB3 H 2.02 0.02 2 581 . 75 GLU C C 179.90 0.40 1 582 . 75 GLU CA C 60.10 0.40 1 583 . 75 GLU CB C 29.20 0.40 1 584 . 75 GLU CG C 36.20 0.40 1 585 . 75 GLU N N 121.60 0.25 1 586 . 76 TYR H H 8.43 0.02 1 587 . 76 TYR HA H 4.14 0.02 1 588 . 76 TYR C C 177.30 0.40 1 589 . 76 TYR CA C 60.60 0.40 1 590 . 76 TYR CB C 39.40 0.40 1 591 . 76 TYR N N 122.20 0.25 1 592 . 77 LEU H H 8.04 0.02 1 593 . 77 LEU HA H 2.97 0.02 1 594 . 77 LEU HB2 H 0.96 0.02 1 595 . 77 LEU HB3 H 0.96 0.02 1 596 . 77 LEU C C 177.60 0.40 1 597 . 77 LEU CA C 55.40 0.40 1 598 . 77 LEU CB C 40.90 0.40 1 599 . 77 LEU CG C 25.00 0.40 1 600 . 77 LEU N N 112.50 0.25 1 601 . 78 THR H H 7.36 0.02 1 602 . 78 THR HA H 4.29 0.02 1 603 . 78 THR HB H 3.78 0.02 1 604 . 78 THR C C 174.70 0.40 1 605 . 78 THR CA C 66.30 0.40 1 606 . 78 THR CB C 68.40 0.40 1 607 . 78 THR CG2 C 20.70 0.40 1 608 . 78 THR N N 115.90 0.25 1 609 . 79 ASN H H 6.84 0.02 1 610 . 79 ASN C C 173.90 0.40 1 611 . 79 ASN CA C 52.40 0.40 1 612 . 79 ASN CB C 37.60 0.40 1 613 . 79 ASN N N 108.90 0.25 1 614 . 80 PRO HA H 5.79 0.02 1 615 . 80 PRO HB2 H 5.18 0.02 1 616 . 80 PRO HB3 H 5.18 0.02 1 617 . 80 PRO C C 178.20 0.40 1 618 . 80 PRO CA C 68.80 0.40 1 619 . 80 PRO CB C 31.60 0.40 1 620 . 80 PRO CG C 28.00 0.40 1 621 . 80 PRO CD C 50.30 0.40 1 622 . 81 ALA H H 9.32 0.02 1 623 . 81 ALA HA H 5.21 0.02 1 624 . 81 ALA HB H 2.15 0.02 1 625 . 81 ALA C C 180.00 0.40 1 626 . 81 ALA CA C 51.50 0.40 1 627 . 81 ALA CB C 16.70 0.40 1 628 . 81 ALA N N 117.80 0.25 1 629 . 82 LYS H H 7.86 0.02 1 630 . 82 LYS HA H 4.47 0.02 1 631 . 82 LYS HB2 H 2.04 0.02 1 632 . 82 LYS HB3 H 2.04 0.02 1 633 . 82 LYS C C 177.70 0.40 1 634 . 82 LYS CA C 57.70 0.40 1 635 . 82 LYS CB C 33.70 0.40 1 636 . 82 LYS CG C 25.20 0.40 1 637 . 82 LYS CD C 29.60 0.40 1 638 . 82 LYS CE C 42.10 0.40 1 639 . 82 LYS N N 117.00 0.25 1 640 . 83 TYR H H 8.29 0.02 1 641 . 83 TYR HA H 4.69 0.02 1 642 . 83 TYR HB2 H 2.70 0.02 1 643 . 83 TYR HB3 H 2.70 0.02 1 644 . 83 TYR C C 176.70 0.40 1 645 . 83 TYR CA C 61.70 0.40 1 646 . 83 TYR CB C 40.80 0.40 1 647 . 83 TYR N N 121.00 0.25 1 648 . 84 ILE H H 9.57 0.02 1 649 . 84 ILE C C 176.70 0.40 1 650 . 84 ILE CA C 59.60 0.40 1 651 . 84 ILE CB C 38.30 0.40 1 652 . 84 ILE N N 115.20 0.25 1 653 . 85 PRO HA H 5.15 0.02 1 654 . 85 PRO HB2 H 4.04 0.02 1 655 . 85 PRO HB3 H 4.04 0.02 1 656 . 85 PRO C C 179.30 0.40 1 657 . 85 PRO CA C 64.20 0.40 1 658 . 85 PRO CB C 31.50 0.40 1 659 . 85 PRO CG C 27.90 0.40 1 660 . 85 PRO CD C 49.70 0.40 1 661 . 86 GLY H H 9.51 0.02 1 662 . 86 GLY HA2 H 4.54 0.02 2 663 . 86 GLY HA3 H 3.92 0.02 2 664 . 86 GLY C C 176.50 0.40 1 665 . 86 GLY CA C 44.60 0.40 1 666 . 86 GLY N N 112.40 0.25 1 667 . 87 THR H H 9.11 0.02 1 668 . 87 THR C C 173.50 0.40 1 669 . 87 THR CA C 61.70 0.40 1 670 . 87 THR CB C 70.20 0.40 1 671 . 87 THR CG2 C 21.10 0.40 1 672 . 87 THR N N 115.60 0.25 1 673 . 88 LYS H H 8.01 0.02 1 674 . 88 LYS HA H 4.77 0.02 1 675 . 88 LYS C C 174.90 0.40 1 676 . 88 LYS CA C 54.90 0.40 1 677 . 88 LYS CB C 31.50 0.40 1 678 . 88 LYS CG C 23.30 0.40 1 679 . 88 LYS CD C 28.60 0.40 1 680 . 88 LYS CE C 41.40 0.40 1 681 . 88 LYS N N 122.90 0.25 1 682 . 89 MET H H 8.86 0.02 1 683 . 89 MET C C 174.20 0.40 1 684 . 89 MET CA C 67.40 0.40 1 685 . 89 MET CB C 31.60 0.40 1 686 . 89 MET N N 122.50 0.25 1 687 . 90 ALA H H 7.99 0.02 1 688 . 90 ALA HA H 5.06 0.02 1 689 . 90 ALA HB H 1.13 0.02 1 690 . 90 ALA C C 175.00 0.40 1 691 . 90 ALA CA C 51.50 0.40 1 692 . 90 ALA CB C 16.70 0.40 1 693 . 90 ALA N N 139.50 0.25 1 694 . 91 PHE H H 8.72 0.02 1 695 . 91 PHE C C 174.90 0.40 1 696 . 91 PHE CA C 57.80 0.40 1 697 . 91 PHE CB C 42.70 0.40 1 698 . 91 PHE N N 123.20 0.25 1 699 . 92 ALA H H 8.53 0.02 1 700 . 92 ALA CA C 54.50 0.40 1 701 . 92 ALA CB C 18.80 0.40 1 702 . 92 ALA N N 130.80 0.25 1 703 . 93 GLY HA2 H 4.40 0.02 2 704 . 93 GLY HA3 H 3.12 0.02 2 705 . 93 GLY C C 172.20 0.40 1 706 . 93 GLY CA C 43.30 0.40 1 707 . 94 LEU H H 8.06 0.02 1 708 . 94 LEU HA H 4.26 0.02 1 709 . 94 LEU C C 175.10 0.40 1 710 . 94 LEU CA C 52.60 0.40 1 711 . 94 LEU CB C 42.20 0.40 1 712 . 94 LEU CG C 26.10 0.40 1 713 . 94 LEU CD1 C 24.30 0.40 1 714 . 94 LEU CD2 C 24.30 0.40 1 715 . 94 LEU N N 122.40 0.25 1 716 . 95 LYS H H 8.31 0.02 1 717 . 95 LYS HA H 3.83 0.02 1 718 . 95 LYS HB2 H 1.68 0.02 1 719 . 95 LYS HB3 H 1.68 0.02 1 720 . 95 LYS C C 177.90 0.40 1 721 . 95 LYS CA C 57.60 0.40 1 722 . 95 LYS CB C 32.50 0.40 1 723 . 95 LYS CG C 24.60 0.40 1 724 . 95 LYS CD C 28.30 0.40 1 725 . 95 LYS CE C 48.80 0.40 1 726 . 95 LYS N N 122.70 0.25 1 727 . 96 LYS H H 8.57 0.02 1 728 . 96 LYS HA H 4.24 0.02 1 729 . 96 LYS HB2 H 1.57 0.02 1 730 . 96 LYS HB3 H 1.57 0.02 1 731 . 96 LYS C C 176.80 0.40 1 732 . 96 LYS CA C 55.60 0.40 1 733 . 96 LYS CB C 31.90 0.40 1 734 . 96 LYS CG C 24.70 0.40 1 735 . 96 LYS CD C 28.80 0.40 1 736 . 96 LYS CE C 41.60 0.40 1 737 . 96 LYS N N 119.70 0.25 1 738 . 97 GLU H H 8.85 0.02 1 739 . 97 GLU HA H 3.33 0.02 1 740 . 97 GLU HB2 H 1.74 0.02 1 741 . 97 GLU HB3 H 1.74 0.02 1 742 . 97 GLU C C 176.80 0.40 1 743 . 97 GLU CA C 59.70 0.40 1 744 . 97 GLU CB C 29.40 0.40 1 745 . 97 GLU CG C 35.60 0.40 1 746 . 97 GLU N N 129.10 0.25 1 747 . 98 LYS H H 8.55 0.02 1 748 . 98 LYS HA H 3.73 0.02 1 749 . 98 LYS HB2 H 1.59 0.02 1 750 . 98 LYS HB3 H 1.59 0.02 1 751 . 98 LYS C C 177.80 0.40 1 752 . 98 LYS CA C 59.30 0.40 1 753 . 98 LYS CB C 32.30 0.40 1 754 . 98 LYS CG C 24.40 0.40 1 755 . 98 LYS CD C 28.80 0.40 1 756 . 98 LYS CE C 41.80 0.40 1 757 . 98 LYS N N 116.70 0.25 1 758 . 99 ASP H H 6.16 0.02 1 759 . 99 ASP HA H 3.96 0.02 1 760 . 99 ASP HB2 H 2.54 0.02 1 761 . 99 ASP HB3 H 2.54 0.02 1 762 . 99 ASP C C 177.80 0.40 1 763 . 99 ASP CA C 56.50 0.40 1 764 . 99 ASP CB C 39.90 0.40 1 765 . 99 ASP N N 115.40 0.25 1 766 . 100 ARG H H 7.14 0.02 1 767 . 100 ARG HA H 5.25 0.02 1 768 . 100 ARG HB2 H 3.14 0.02 1 769 . 100 ARG HB3 H 3.14 0.02 1 770 . 100 ARG C C 177.30 0.40 1 771 . 100 ARG CA C 61.00 0.40 1 772 . 100 ARG CB C 30.20 0.40 1 773 . 100 ARG CD C 43.20 0.40 1 774 . 100 ARG N N 117.70 0.25 1 775 . 101 ASN H H 8.53 0.02 1 776 . 101 ASN HA H 4.34 0.02 1 777 . 101 ASN HB2 H 2.49 0.02 1 778 . 101 ASN HB3 H 2.80 0.02 1 779 . 101 ASN C C 179.80 0.40 1 780 . 101 ASN CA C 55.60 0.40 1 781 . 101 ASN CB C 36.60 0.40 1 782 . 101 ASN N N 117.90 0.25 1 783 . 102 ASP H H 8.51 0.02 1 784 . 102 ASP HA H 3.81 0.02 1 785 . 102 ASP HB2 H 2.37 0.02 1 786 . 102 ASP HB3 H 2.37 0.02 1 787 . 102 ASP C C 177.60 0.40 1 788 . 102 ASP CA C 58.70 0.40 1 789 . 102 ASP CB C 39.70 0.40 1 790 . 102 ASP N N 126.00 0.25 1 791 . 103 LEU H H 8.03 0.02 1 792 . 103 LEU HA H 3.74 0.02 1 793 . 103 LEU C C 178.70 0.40 1 794 . 103 LEU CA C 58.50 0.40 1 795 . 103 LEU CB C 41.20 0.40 1 796 . 103 LEU CG C 27.60 0.40 1 797 . 103 LEU CD1 C 24.00 0.40 1 798 . 103 LEU CD2 C 24.00 0.40 1 799 . 103 LEU N N 120.10 0.25 1 800 . 104 ILE H H 8.69 0.02 1 801 . 104 ILE HA H 4.05 0.02 1 802 . 104 ILE HB H 2.99 0.02 1 803 . 104 ILE C C 176.80 0.40 1 804 . 104 ILE CA C 65.60 0.40 1 805 . 104 ILE CB C 37.10 0.40 1 806 . 104 ILE CG1 C 31.00 0.40 1 807 . 104 ILE CG2 C 17.90 0.40 1 808 . 104 ILE CD1 C 12.80 0.40 1 809 . 104 ILE N N 119.70 0.25 1 810 . 105 THR H H 8.03 0.02 1 811 . 105 THR HA H 4.18 0.02 1 812 . 105 THR HB H 3.73 0.02 1 813 . 105 THR C C 176.80 0.40 1 814 . 105 THR CA C 68.00 0.40 1 815 . 105 THR CB C 69.90 0.40 1 816 . 105 THR CG2 C 20.20 0.40 1 817 . 105 THR N N 118.80 0.25 1 818 . 106 TYR H H 7.56 0.02 1 819 . 106 TYR HA H 3.97 0.02 1 820 . 106 TYR HB2 H 3.51 0.02 1 821 . 106 TYR HB3 H 3.51 0.02 1 822 . 106 TYR C C 176.40 0.40 1 823 . 106 TYR CA C 61.30 0.40 1 824 . 106 TYR CB C 37.40 0.40 1 825 . 106 TYR N N 119.80 0.25 1 826 . 107 MET H H 8.67 0.02 1 827 . 107 MET HA H 2.98 0.02 1 828 . 107 MET HB2 H 1.72 0.02 1 829 . 107 MET HB3 H 1.72 0.02 1 830 . 107 MET C C 177.40 0.40 1 831 . 107 MET CA C 59.90 0.40 1 832 . 107 MET CB C 33.90 0.40 1 833 . 107 MET CG C 31.20 0.40 1 834 . 107 MET N N 117.70 0.25 1 835 . 108 THR H H 8.330 0.02 1 836 . 108 THR HA H 3.58 0.02 1 837 . 108 THR HB H 3.39 0.02 1 838 . 108 THR C C 176.20 0.40 1 839 . 108 THR CA C 64.40 0.40 1 840 . 108 THR CB C 68.60 0.40 1 841 . 108 THR CG2 C 20.20 0.40 1 842 . 108 THR N N 109.00 0.25 1 843 . 109 LYS H H 6.59 0.02 1 844 . 109 LYS HA H 4.04 0.02 1 845 . 109 LYS HB2 H 1.72 0.02 1 846 . 109 LYS HB3 H 1.72 0.02 1 847 . 109 LYS C C 178.30 0.40 1 848 . 109 LYS CA C 57.60 0.40 1 849 . 109 LYS CB C 32.30 0.40 1 850 . 109 LYS CG C 24.30 0.40 1 851 . 109 LYS CD C 28.70 0.40 1 852 . 109 LYS CE C 42.10 0.40 1 853 . 109 LYS N N 120.10 0.25 1 854 . 110 ALA H H 8.01 0.02 1 855 . 110 ALA C C 178.60 0.40 1 856 . 110 ALA CA C 53.70 0.40 1 857 . 110 ALA CB C 18.50 0.40 1 858 . 110 ALA N N 120.90 0.25 1 859 . 111 ALA H H 8.25 0.02 1 860 . 111 ALA HA H 4.18 0.02 1 861 . 111 ALA HB H 1.38 0.02 1 862 . 111 ALA C C 176.50 0.40 1 863 . 111 ALA CA C 52.00 0.40 1 864 . 111 ALA CB C 18.80 0.40 1 865 . 111 ALA N N 115.70 0.25 1 866 . 112 LYS H H 6.79 0.02 1 867 . 112 LYS C C 181.10 0.40 1 868 . 112 LYS CA C 58.50 0.40 1 869 . 112 LYS CB C 33.30 0.40 1 870 . 112 LYS N N 124.80 0.25 1 stop_ save_