data_4130 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N, 13C Chemical Shifts of Recombinant Rat Ferrocytochrome b5, A conformation ; _BMRB_accession_number 4130 _BMRB_flat_file_name bmr4130.str _Entry_type original _Submission_date 1998-04-07 _Accession_date 1998-04-07 _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 Dangi Bindi . . 2 Sarma Siddhartha . . 3 Yan Chunhua . . 4 Banville Debra L. . 5 Guiles Ronald D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 434 "13C chemical shifts" 297 "15N chemical shifts" 90 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1998-08-12 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4131 '1H, 13C, and 15N chemical shifts for Rat Ferrocytochrome b5, B conformation' stop_ _Original_release_date 1998-08-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Dangi, B., Sarma, S., Yan, C., Banville, D., Guiles, R.D., "The Origin of Difference in the Physical Properties of the Equilibrium Forms of Cytochrome b5 Revealed Through High Resolution NMR Structures and Backbone Dynamic Analyses," Biochemistry 37, 8289-8302 (1998). ; _Citation_title ; The Origin of Difference in the Physical Properties of the Equilibrium Forms of Cytochrome b5 Revealed Through High Resolution NMR Structures and Backbone Dynamic Analyses ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98285557 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Dangi Bindi . . 2 Sarma Siddhartha . . 3 Yan Chunhua . . 4 Banville Debra L. . 5 Guiles Ronald D. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 37 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 8289 _Page_last 8302 _Year 1998 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full 'Wishart and Sykes, (1994), J.B. NMR, 4 171-18' _Citation_title 'The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8019132 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 4 _Journal_issue 2 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 171 _Page_last 180 _Year 1994 _Details ; A simple technique for identifying protein secondary structures through the analysis of backbone 13C chemical shifts is described. It is based on the Chemical-Shift Index [Wishart et al. (1992) Biochemistry, 31, 1647-1651] which was originally developed for the analysis of 1H(alpha) chemical shifts. By extending the Chemical-Shift Index to include 13C(alpha), 13C(beta) and carbonyl 13C chemical shifts, it is now possible to use four independent chemical-shift measurements to identify and locate protein secondary structures. It is shown that by combining both 1H and 13C chemical-shift indices to produce a 'consensus' estimate of secondary structure, it is possible to achieve a predictive accuracy in excess of 92%. This suggests that the secondary structure of peptides and proteins can be accurately obtained from 1H and 13C chemical shifts, without recourse to NOE measurements. ; save_ ################################## # Molecular system description # ################################## save_system_cytb5_a _Saveframe_category molecular_system _Mol_system_name 'rat ferrocytochrome b5 A form' _Abbreviation_common reduced_cytb5A _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label cytb5_A $cytb5_A heme $entity_HEC stop_ _System_molecular_weight 11210 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cytb5_A _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'cytochrome b5' _Abbreviation_common cytb5 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 94 _Mol_residue_sequence ; DKDVKYYTLEEIQKHKDSKS TWVILHHKVYDLTKFLEEHP GGEEVLREQAGGDATENFED VGHSTDARELSKTYIIGELH PDDRSKIAKPSETL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ASP 2 2 LYS 3 3 ASP 4 4 VAL 5 5 LYS 6 6 TYR 7 7 TYR 8 8 THR 9 9 LEU 10 10 GLU 11 11 GLU 12 12 ILE 13 13 GLN 14 14 LYS 15 15 HIS 16 16 LYS 17 17 ASP 18 18 SER 19 19 LYS 20 20 SER 21 21 THR 22 22 TRP 23 23 VAL 24 24 ILE 25 25 LEU 26 26 HIS 27 27 HIS 28 28 LYS 29 29 VAL 30 30 TYR 31 31 ASP 32 32 LEU 33 33 THR 34 34 LYS 35 35 PHE 36 36 LEU 37 37 GLU 38 38 GLU 39 39 HIS 40 40 PRO 41 41 GLY 42 42 GLY 43 43 GLU 44 44 GLU 45 45 VAL 46 46 LEU 47 47 ARG 48 48 GLU 49 49 GLN 50 50 ALA 51 51 GLY 52 52 GLY 53 53 ASP 54 54 ALA 55 55 THR 56 56 GLU 57 57 ASN 58 58 PHE 59 59 GLU 60 60 ASP 61 61 VAL 62 62 GLY 63 63 HIS 64 64 SER 65 65 THR 66 66 ASP 67 67 ALA 68 68 ARG 69 69 GLU 70 70 LEU 71 71 SER 72 72 LYS 73 73 THR 74 74 TYR 75 75 ILE 76 76 ILE 77 77 GLY 78 78 GLU 79 79 LEU 80 80 HIS 81 81 PRO 82 82 ASP 83 83 ASP 84 84 ARG 85 85 SER 86 86 LYS 87 87 ILE 88 88 ALA 89 89 LYS 90 90 PRO 91 91 SER 92 92 GLU 93 93 THR 94 94 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-25 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 BMRB 4131 "cytochrome b5" 100.00 94 100.00 100.00 4.05e-60 PDB 1AQA "Solution Structure Of Reduced Microsomal Rat Cytochrome B5, Nmr, Minimized Average Structure" 100.00 94 100.00 100.00 4.05e-60 PDB 1AW3 "The Solution Nmr Structure Of Oxidized Rat Microsomal Cytochrome B5, Minimized Average Structure" 98.94 94 100.00 100.00 2.15e-59 PDB 1AXX "The Solution Structure Of Oxidized Rat Microsomal Cytochrome B5, Nmr, 19 Structures" 98.94 94 100.00 100.00 2.15e-59 PDB 1B5A "Rat Ferrocytochrome B5 A Conformation, Nmr, 1 Structure" 98.94 94 100.00 100.00 2.15e-59 PDB 1B5B "Rat Ferrocytochrome B5 B Conformation, Nmr, 1 Structure" 98.94 94 100.00 100.00 2.15e-59 PDB 1BFX "The Solution Nmr Structure Of The B Form Of Oxidized Rat Microsomal Cytochrome B5, Minimized Average Structure" 100.00 99 100.00 100.00 1.75e-60 PDB 1BLV "Solution Structure Of Oxidized Rat Microsomal Cytochrome B5 In The Presence Of 2 M Guanidinium Chloride: Monitoring The Early S" 98.94 94 100.00 100.00 2.15e-59 PDB 1I87 "Solution Structure Of The Water-Soluble Fragment Of Rat Hepatic Apocytochrome B5" 100.00 98 100.00 100.00 2.04e-60 PDB 1I8C "Solution Structure Of The Water-Soluble Fragment Of Rat Hepatic Apocytochrome B5" 100.00 98 100.00 100.00 2.04e-60 PDB 1IB7 "Solution Structure Of F35y Mutant Of Rat Ferro Cytochrome B5, A Conformation, Ensemble Of 20 Structures" 100.00 94 98.94 100.00 1.60e-59 PDB 1IET "Apocytochrome B5, Ph 6.2, 298 K, Nmr, Minimized Average Structure" 100.00 98 100.00 100.00 2.04e-60 PDB 1IEU "Apocytochrome B5, Ph 6.2, 298 K, Nmr, 10 Structures" 100.00 98 100.00 100.00 2.04e-60 PDB 1JEX "Solution Structure Of A67v Mutant Of Rat Ferro Cytochrome B5" 100.00 94 98.94 98.94 2.15e-59 PDB 1MNY "Dimethyl Propionate Ester Heme-Containing Cytochrome B5" 100.00 94 100.00 100.00 4.05e-60 PDB 2AXX "The Solution Structure Of Oxidized Rat Microsomal Cytochrome B5, Nmr, 21 Structures" 100.00 94 100.00 100.00 4.05e-60 DBJ BAA02492 "cytochrome b5 precursor [Rattus norvegicus]" 100.00 134 100.00 100.00 1.01e-60 DBJ BAB22093 "unnamed protein product [Mus musculus]" 100.00 134 98.94 100.00 4.03e-60 DBJ BAB28714 "unnamed protein product [Mus musculus]" 100.00 134 98.94 100.00 4.03e-60 DBJ BAE20982 "unnamed protein product [Mus musculus]" 100.00 134 98.94 100.00 4.03e-60 GB AAA67175 "flavocytochrome b5 chimeric protein [synthetic construct]" 93.62 356 98.86 98.86 2.37e-52 GB AAA72420 "cytochrome b5, partial [synthetic construct]" 92.55 92 100.00 100.00 2.93e-55 GB AAA72421 "cytochrome b5 [synthetic construct]" 93.62 356 98.86 98.86 2.37e-52 GB AAA72557 "cytochrome b(5) [synthetic construct]" 100.00 99 100.00 100.00 1.75e-60 GB AAA99718 "NADH:cytochrome c reductase [synthetic construct]" 93.62 360 98.86 98.86 1.64e-52 REF NP_001268328 "cytochrome b5-like [Mesocricetus auratus]" 100.00 171 97.87 100.00 4.59e-59 REF NP_071581 "cytochrome b5 [Rattus norvegicus]" 100.00 134 100.00 100.00 1.01e-60 REF NP_080073 "cytochrome b5 [Mus musculus]" 100.00 134 98.94 100.00 4.03e-60 REF XP_003512427 "PREDICTED: cytochrome b5 [Cricetulus griseus]" 100.00 134 97.87 100.00 1.35e-59 REF XP_005356388 "PREDICTED: cytochrome b5 [Microtus ochrogaster]" 100.00 134 97.87 100.00 1.27e-59 SP P00173 "RecName: Full=Cytochrome b5" 100.00 134 100.00 100.00 1.01e-60 SP P56395 "RecName: Full=Cytochrome b5" 100.00 134 98.94 100.00 4.03e-60 stop_ save_ ############# # Ligands # ############# save_HEC _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'HEME C' _BMRB_code HEC _PDB_code HEC _Molecular_mass 618.503 _Mol_charge 0 _Mol_paramagnetic no _Mol_aromatic yes _Details . 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 'not present' _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 $cytb5_A rat 10117 Eukaryota Metazoa Rattus rattus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $cytb5_A 'recombinant technology' E.coli Escherichia coli BL21(DE3)PlysS plasmid pET3c stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details '4mM 15N, 13C labeled in 100 mM phosphate pH 7.0' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $cytb5_A 4 mM '[U-15N; U-13C]' phosphate 100 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX600 _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 10 . pH 7.0 0.2 n/a temperature 313 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference _Details ; The 15N and 13C referencing was done using the indirect referencing according to the article Wishart and Sykes, (1994), J. Biomol. NMR 4, 171-180 ; 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 TSP C 13 . ppm 0.00 . indirect . . . TSP H 1 methyl ppm 0.00 . direct . . . TSP N 15 . ppm 0.00 . indirect . . . stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name cytb5_A _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 ASP H H 8.37 . . 2 . 1 ASP HA H 4.62 . . 3 . 1 ASP HB2 H 2.69 . . 4 . 1 ASP HB3 H 2.02 . . 5 . 1 ASP N N 124.8 . . 6 . 2 LYS H H 8.04 . . 7 . 2 LYS HA H 4.14 . . 8 . 2 LYS HB2 H 1.76 . . 9 . 2 LYS HG2 H 1.41 . . 10 . 2 LYS HD2 H 1.66 . . 11 . 2 LYS C C 177 . . 12 . 2 LYS N N 127 . . 13 . 3 ASP H H 8.19 . . 14 . 3 ASP HA H 4.16 . . 15 . 3 ASP HB2 H 2.57 . . 16 . 3 ASP C C 175.34 . . 17 . 3 ASP N N 124.3 . . 18 . 4 VAL H H 7.63 . . 19 . 4 VAL HA H 3.87 . . 20 . 4 VAL HB H 1.64 . . 21 . 4 VAL HG1 H 0.68 . . 22 . 4 VAL HG2 H 0.39 . . 23 . 4 VAL C C 174.34 . . 24 . 4 VAL CA C 61.83 . . 25 . 4 VAL CB C 33.42 . . 26 . 4 VAL CG1 C 21.64 . . 27 . 4 VAL CG2 C 20.8 . . 28 . 4 VAL N N 127.6 . . 29 . 5 LYS H H 8.07 . . 30 . 5 LYS HA H 4.14 . . 31 . 5 LYS HB2 H 1.65 . . 32 . 5 LYS HB3 H 1.52 . . 33 . 5 LYS HG2 H 2.84 . . 34 . 5 LYS HG3 H 2.96 . . 35 . 5 LYS HD2 H 1.21 . . 36 . 5 LYS HD3 H 1.07 . . 37 . 5 LYS HE2 H 3.55 . . 38 . 5 LYS C C 176.35 . . 39 . 5 LYS CA C 54.68 . . 40 . 5 LYS N N 133.3 . . 41 . 6 TYR H H 8.12 . . 42 . 6 TYR HA H 5.76 . . 43 . 6 TYR HB2 H 2.88 . . 44 . 6 TYR HB3 H 2.69 . . 45 . 6 TYR HD1 H 6.92 . . 46 . 6 TYR HD2 H 6.92 . . 47 . 6 TYR HE1 H 6.66 . . 48 . 6 TYR HE2 H 6.66 . . 49 . 6 TYR C C 176.35 . . 50 . 6 TYR CA C 55.1 . . 51 . 6 TYR CB C 40.99 . . 52 . 6 TYR N N 128.1 . . 53 . 7 TYR H H 8.73 . . 54 . 7 TYR HA H 5.21 . . 55 . 7 TYR HB2 H 3.23 . . 56 . 7 TYR HB3 H 2.55 . . 57 . 7 TYR HD1 H 6.98 . . 58 . 7 TYR HD2 H 6.98 . . 59 . 7 TYR HE1 H 6.64 . . 60 . 7 TYR HE2 H 6.64 . . 61 . 7 TYR C C 176.02 . . 62 . 7 TYR CA C 56.99 . . 63 . 7 TYR CB C 43.1 . . 64 . 7 TYR N N 121.6 . . 65 . 8 THR H H 9.19 . . 66 . 8 THR HA H 4.69 . . 67 . 8 THR HB H 4.9 . . 68 . 8 THR C C 175.68 . . 69 . 8 THR CA C 60.36 . . 70 . 8 THR CB C 30.68 . . 71 . 8 THR N N 121.6 . . 72 . 9 LEU H H 9.75 . . 73 . 9 LEU HA H 4.13 . . 74 . 9 LEU HB2 H 1.76 . . 75 . 9 LEU HB3 H 1.57 . . 76 . 9 LEU HD1 H 1.05 . . 77 . 9 LEU C C 178.7 . . 78 . 9 LEU CA C 58.46 . . 79 . 9 LEU CB C 42.05 . . 80 . 9 LEU N N 130.3 . . 81 . 10 GLU H H 8.44 . . 82 . 10 GLU HA H 3.98 . . 83 . 10 GLU HB2 H 2.07 . . 84 . 10 GLU HB3 H 1.99 . . 85 . 10 GLU HG2 H 3.26 . . 86 . 10 GLU C C 178.37 . . 87 . 10 GLU CA C 59.09 . . 88 . 10 GLU CB C 29.63 . . 89 . 10 GLU CG C 38.49 . . 90 . 10 GLU N N 123.6 . . 91 . 11 GLU H H 7.69 . . 92 . 11 GLU HA H 4.12 . . 93 . 11 GLU HB2 H 2.19 . . 94 . 11 GLU HB3 H 2.33 . . 95 . 11 GLU HG2 H 2.4 . . 96 . 11 GLU HG3 H 2.51 . . 97 . 11 GLU C C 179.38 . . 98 . 11 GLU CA C 58.89 . . 99 . 11 GLU CB C 30.12 . . 100 . 11 GLU CG C 36.81 . . 101 . 11 GLU N N 124.9 . . 102 . 12 ILE H H 8.52 . . 103 . 12 ILE HA H 3.79 . . 104 . 12 ILE HB H 2.02 . . 105 . 12 ILE HG12 H 1.41 . . 106 . 12 ILE HG13 H 1.57 . . 107 . 12 ILE HG2 H 1.02 . . 108 . 12 ILE HD1 H 0.97 . . 109 . 12 ILE C C 177.7 . . 110 . 12 ILE CA C 65.67 . . 111 . 12 ILE CB C 38.4 . . 112 . 12 ILE CG2 C 17.65 . . 113 . 12 ILE CD1 C 17.02 . . 114 . 12 ILE N N 128 . . 115 . 13 GLN H H 8.22 . . 116 . 13 GLN HA H 4.4 . . 117 . 13 GLN HB2 H 2.23 . . 118 . 13 GLN HB3 H 2.08 . . 119 . 13 GLN HG2 H 2.65 . . 120 . 13 GLN C C 176.35 . . 121 . 13 GLN CA C 58.04 . . 122 . 13 GLN CB C 34.68 . . 123 . 13 GLN CG C 34.68 . . 124 . 13 GLN N N 121.8 . . 125 . 14 LYS H H 7.32 . . 126 . 14 LYS HA H 4.4 . . 127 . 14 LYS HB2 H 1.67 . . 128 . 14 LYS HB3 H 1.45 . . 129 . 14 LYS HG2 H 1.45 . . 130 . 14 LYS HG3 H 1.32 . . 131 . 14 LYS HD2 H 1.62 . . 132 . 14 LYS HE2 H 2.98 . . 133 . 14 LYS C C 177.7 . . 134 . 14 LYS CA C 54.46 . . 135 . 14 LYS CB C 32.37 . . 136 . 14 LYS N N 121.9 . . 137 . 15 HIS H H 7.73 . . 138 . 15 HIS HA H 4.19 . . 139 . 15 HIS HB2 H 2.53 . . 140 . 15 HIS HB3 H 2.2 . . 141 . 15 HIS C C 173.66 . . 142 . 15 HIS CA C 54.46 . . 143 . 15 HIS CB C 26.47 . . 144 . 15 HIS N N 128 . . 145 . 16 LYS H H 7.46 . . 146 . 16 LYS HA H 4.83 . . 147 . 16 LYS HB2 H 1.78 . . 148 . 16 LYS HB3 H 1.48 . . 149 . 16 LYS HG2 H 1.33 . . 150 . 16 LYS HG3 H 1.24 . . 151 . 16 LYS C C 175.33 . . 152 . 16 LYS CA C 54.7 . . 153 . 16 LYS CB C 33.21 . . 154 . 16 LYS CG C 23.11 . . 155 . 16 LYS CD C 29.63 . . 156 . 16 LYS N N 175.33 . . 157 . 17 ASP H H 8.07 . . 158 . 17 ASP HA H 4.91 . . 159 . 17 ASP HB2 H 3.09 . . 160 . 17 ASP HB3 H 2.61 . . 161 . 17 ASP C C 177.02 . . 162 . 17 ASP CA C 52.99 . . 163 . 17 ASP CB C 43.1 . . 164 . 17 ASP N N 128 . . 165 . 18 SER H H 7.39 . . 166 . 18 SER HA H 4.49 . . 167 . 18 SER HB2 H 3.96 . . 168 . 18 SER C C 174.67 . . 169 . 18 SER CA C 59.09 . . 170 . 18 SER N N 121.8 . . 171 . 19 LYS H H 8.02 . . 172 . 19 LYS HA H 4.23 . . 173 . 19 LYS HB2 H 1.84 . . 174 . 19 LYS HG2 H 1.37 . . 175 . 19 LYS HD2 H 1.65 . . 176 . 19 LYS HE2 H 2.97 . . 177 . 19 LYS C C 177.36 . . 178 . 19 LYS CA C 57.2 . . 179 . 19 LYS CB C 32.37 . . 180 . 19 LYS N N 126 . . 181 . 20 SER H H 7.44 . . 182 . 20 SER HA H 4.99 . . 183 . 20 SER HB2 H 3.89 . . 184 . 20 SER HB3 H 3.79 . . 185 . 20 SER C C 172.99 . . 186 . 20 SER CA C 58.04 . . 187 . 20 SER CB C 63.09 . . 188 . 20 SER N N 119.4 . . 189 . 21 THR H H 8.65 . . 190 . 21 THR HA H 4.54 . . 191 . 21 THR HB H 3.64 . . 192 . 21 THR HG2 H 1 . . 193 . 21 THR C C 172.99 . . 194 . 21 THR CA C 62.67 . . 195 . 21 THR CB C 31.95 . . 196 . 21 THR CG2 C 23.32 . . 197 . 21 THR N N 129.1 . . 198 . 22 TRP H H 8.76 . . 199 . 22 TRP HA H 6.53 . . 200 . 22 TRP HB2 H 3.23 . . 201 . 22 TRP HB3 H 3.04 . . 202 . 22 TRP C C 176.69 . . 203 . 22 TRP CA C 62.67 . . 204 . 22 TRP CB C 33.24 . . 205 . 22 TRP N N 133.4 . . 206 . 23 VAL H H 8.98 . . 207 . 23 VAL HA H 5.12 . . 208 . 23 VAL HB H 2.33 . . 209 . 23 VAL HG1 H 1.13 . . 210 . 23 VAL HG2 H 1.05 . . 211 . 23 VAL C C 173.7 . . 212 . 23 VAL CA C 59.94 . . 213 . 23 VAL CB C 37 . . 214 . 23 VAL CG1 C 22.48 . . 215 . 23 VAL CG2 C 21.01 . . 216 . 23 VAL N N 119.8 . . 217 . 24 ILE H H 8.5 . . 218 . 24 ILE HA H 5.49 . . 219 . 24 ILE HB H 1.68 . . 220 . 24 ILE HG12 H 0.95 . . 221 . 24 ILE HG2 H 0.84 . . 222 . 24 ILE HD1 H 1.81 . . 223 . 24 ILE C C 175.68 . . 224 . 24 ILE CA C 59.73 . . 225 . 24 ILE CG1 C 16.17 . . 226 . 24 ILE CD1 C 40.79 . . 227 . 24 ILE N N 129.2 . . 228 . 25 LEU H H 8.99 . . 229 . 25 LEU HA H 4.88 . . 230 . 25 LEU HB2 H 1.83 . . 231 . 25 LEU HB3 H 0.73 . . 232 . 25 LEU HG H 1.15 . . 233 . 25 LEU HD1 H 0.53 . . 234 . 25 LEU HD2 H -0.3 . . 235 . 25 LEU C C 175.68 . . 236 . 25 LEU CA C 53.83 . . 237 . 25 LEU CB C 44.37 . . 238 . 25 LEU CG C 25.84 . . 239 . 25 LEU CD1 C 25.84 . . 240 . 25 LEU CD2 C 23.74 . . 241 . 25 LEU N N 130.5 . . 242 . 26 HIS H H 9.52 . . 243 . 26 HIS HA H 4.02 . . 244 . 26 HIS HB2 H 4.03 . . 245 . 26 HIS C C 174.67 . . 246 . 26 HIS CA C 56.68 . . 247 . 26 HIS CB C 27.53 . . 248 . 26 HIS N N 131.3 . . 249 . 27 HIS H H 8.77 . . 250 . 27 HIS HA H 4.06 . . 251 . 27 HIS HB2 H 2.69 . . 252 . 27 HIS HB3 H 2.94 . . 253 . 27 HIS C C 173.33 . . 254 . 27 HIS CA C 57 . . 255 . 27 HIS CB C 43.32 . . 256 . 27 HIS N N 114.6 . . 257 . 28 LYS H H 8.46 . . 258 . 28 LYS HA H 4.96 . . 259 . 28 LYS HB2 H 2.33 . . 260 . 28 LYS HG2 H 1.62 . . 261 . 28 LYS HD2 H 1.5 . . 262 . 28 LYS HE2 H 3.07 . . 263 . 28 LYS C C 173.66 . . 264 . 28 LYS CA C 55.73 . . 265 . 28 LYS CB C 34.26 . . 266 . 28 LYS CG C 26.26 . . 267 . 28 LYS CD C 26.26 . . 268 . 28 LYS N N 128.5 . . 269 . 29 VAL H H 8.49 . . 270 . 29 VAL HA H 4.49 . . 271 . 29 VAL HB H 1.24 . . 272 . 29 VAL HG1 H 0.76 . . 273 . 29 VAL HG2 H 0.28 . . 274 . 29 VAL C C 173.66 . . 275 . 29 VAL CA C 62.65 . . 276 . 29 VAL CB C 32.79 . . 277 . 29 VAL CG1 C 22.48 . . 278 . 29 VAL CG2 C 22.48 . . 279 . 29 VAL N N 127.6 . . 280 . 30 TYR H H 9.26 . . 281 . 30 TYR HA H 4.9 . . 282 . 30 TYR HB2 H 3 . . 283 . 30 TYR HB3 H 2.58 . . 284 . 30 TYR C C 175.01 . . 285 . 30 TYR CA C 56.36 . . 286 . 30 TYR CB C 40.36 . . 287 . 30 TYR N N 133.3 . . 288 . 31 ASP H H 8.35 . . 289 . 31 ASP HA H 5.23 . . 290 . 31 ASP HB2 H 3.05 . . 291 . 31 ASP HB3 H 2.55 . . 292 . 31 ASP C C 175.33 . . 293 . 31 ASP CA C 52.99 . . 294 . 31 ASP CB C 42.26 . . 295 . 31 ASP N N 126.5 . . 296 . 32 LEU H H 8.77 . . 297 . 32 LEU HA H 4.07 . . 298 . 32 LEU HB2 H 1.84 . . 299 . 32 LEU HB3 H 1.16 . . 300 . 32 LEU HG H 1.89 . . 301 . 32 LEU HD1 H 1.14 . . 302 . 32 LEU HD2 H 1.02 . . 303 . 32 LEU C C 172.99 . . 304 . 32 LEU CB C 43.52 . . 305 . 32 LEU CG C 26.26 . . 306 . 32 LEU N N 129.9 . . 307 . 33 THR H H 8.63 . . 308 . 33 THR HA H 3.57 . . 309 . 33 THR HB H 4.28 . . 310 . 33 THR HG2 H 1.33 . . 311 . 33 THR C C 176.35 . . 312 . 33 THR CA C 69.19 . . 313 . 33 THR CB C 69.19 . . 314 . 33 THR CG2 C 21.43 . . 315 . 33 THR N N 128.5 . . 316 . 34 LYS H H 8.98 . . 317 . 34 LYS HA H 4.3 . . 318 . 34 LYS HB2 H 1.87 . . 319 . 34 LYS HB3 H 2.12 . . 320 . 34 LYS HG2 H 1.42 . . 321 . 34 LYS HD2 H 1.7 . . 322 . 34 LYS HE2 H 3.02 . . 323 . 34 LYS C C 176.35 . . 324 . 34 LYS CA C 57.42 . . 325 . 34 LYS CB C 31.95 . . 326 . 34 LYS CG C 25.42 . . 327 . 34 LYS N N 123.4 . . 328 . 35 PHE H H 7.71 . . 329 . 35 PHE HA H 4.44 . . 330 . 35 PHE HB2 H 2.4 . . 331 . 35 PHE HB3 H 1.98 . . 332 . 35 PHE HD2 H 6.56 . . 333 . 35 PHE HE1 H 7.12 . . 334 . 35 PHE HZ H 6.32 . . 335 . 35 PHE C C 175.34 . . 336 . 35 PHE CA C 56.68 . . 337 . 35 PHE CB C 41 . . 338 . 35 PHE N N 126.1 . . 339 . 36 LEU H H 7.02 . . 340 . 36 LEU HA H 2.96 . . 341 . 36 LEU HB2 H 1.57 . . 342 . 36 LEU HB3 H 1.06 . . 343 . 36 LEU HG H 1.78 . . 344 . 36 LEU HD1 H 0.76 . . 345 . 36 LEU HD2 H 0.49 . . 346 . 36 LEU C C 177.02 . . 347 . 36 LEU CA C 59.09 . . 348 . 36 LEU CB C 42.26 . . 349 . 36 LEU CG C 26.26 . . 350 . 36 LEU CD1 C 24.16 . . 351 . 36 LEU CD2 C 24.16 . . 352 . 36 LEU N N 124.4 . . 353 . 37 GLU H H 7.62 . . 354 . 37 GLU HA H 3.78 . . 355 . 37 GLU HB2 H 1.89 . . 356 . 37 GLU HB3 H 1.77 . . 357 . 37 GLU HG2 H 2.07 . . 358 . 37 GLU C C 176.02 . . 359 . 37 GLU CA C 57.41 . . 360 . 37 GLU CB C 29.63 . . 361 . 37 GLU CG C 36.58 . . 362 . 37 GLU N N 117.7 . . 363 . 38 GLU H H 7.02 . . 364 . 38 GLU HA H 4 . . 365 . 38 GLU HB2 H 2.07 . . 366 . 38 GLU HB3 H 1.64 . . 367 . 38 GLU C C 176.02 . . 368 . 38 GLU CA C 54.68 . . 369 . 38 GLU CB C 30.9 . . 370 . 38 GLU N N 123.1 . . 371 . 39 HIS H H 6.01 . . 372 . 39 HIS HA H 2.47 . . 373 . 39 HIS HB2 H 0.79 . . 374 . 39 HIS HB3 H 0.38 . . 375 . 39 HIS C C 175.2 . . 376 . 39 HIS CA C 52.15 . . 377 . 39 HIS CB C 27.74 . . 378 . 39 HIS N N 126.1 . . 379 . 40 PRO HA H 3.59 . . 380 . 40 PRO HB2 H 1.63 . . 381 . 40 PRO HG2 H 1.67 . . 382 . 40 PRO HD2 H 3.74 . . 383 . 40 PRO HD3 H 1.28 . . 384 . 40 PRO C C 176.02 . . 385 . 40 PRO CA C 63.83 . . 386 . 40 PRO CB C 32.47 . . 387 . 41 GLY H H 1.04 . . 388 . 41 GLY HA2 H 3.39 . . 389 . 41 GLY HA3 H 0.38 . . 390 . 41 GLY C C 172.32 . . 391 . 41 GLY CA C 44.57 . . 392 . 41 GLY N N 101.9 . . 393 . 42 GLY H H 6.15 . . 394 . 42 GLY HA2 H 3.98 . . 395 . 42 GLY HA3 H 3.4 . . 396 . 42 GLY C C 173.66 . . 397 . 42 GLY CA C 43.73 . . 398 . 42 GLY N N 113.1 . . 399 . 43 GLU H H 8.16 . . 400 . 43 GLU HA H 3.59 . . 401 . 43 GLU HB2 H 1.74 . . 402 . 43 GLU HB3 H 1.62 . . 403 . 43 GLU HG2 H 1.89 . . 404 . 43 GLU C C 177.88 . . 405 . 43 GLU CA C 57.83 . . 406 . 43 GLU CB C 30.68 . . 407 . 43 GLU N N 127.5 . . 408 . 44 GLU H H 8.32 . . 409 . 44 GLU HA H 3.72 . . 410 . 44 GLU HB2 H 1.94 . . 411 . 44 GLU HB3 H 1.63 . . 412 . 44 GLU HG2 H 2.27 . . 413 . 44 GLU HG3 H 2.23 . . 414 . 44 GLU C C 179.38 . . 415 . 44 GLU CA C 61.62 . . 416 . 44 GLU CB C 29.42 . . 417 . 44 GLU CG C 36.58 . . 418 . 44 GLU N N 128.3 . . 419 . 45 VAL H H 8.25 . . 420 . 45 VAL HA H 4.12 . . 421 . 45 VAL HB H 2.55 . . 422 . 45 VAL HG1 H 0.99 . . 423 . 45 VAL HG2 H 0.89 . . 424 . 45 VAL C C 177.02 . . 425 . 45 VAL CA C 63.93 . . 426 . 45 VAL CB C 31.31 . . 427 . 45 VAL CG1 C 21.87 . . 428 . 45 VAL CG2 C 21.01 . . 429 . 45 VAL N N 119.5 . . 430 . 46 LEU H H 6.01 . . 431 . 46 LEU HA H 3.9 . . 432 . 46 LEU HB2 H 1.5 . . 433 . 46 LEU HB3 H 0.62 . . 434 . 46 LEU HG H 0.25 . . 435 . 46 LEU HD1 H -0.67 . . 436 . 46 LEU C C 178.38 . . 437 . 46 LEU CA C 56.36 . . 438 . 46 LEU CB C 41.22 . . 439 . 46 LEU CG C 25.42 . . 440 . 46 LEU CD1 C 25.21 . . 441 . 46 LEU N N 123.1 . . 442 . 47 ARG H H 7.97 . . 443 . 47 ARG HA H 3.78 . . 444 . 47 ARG HB2 H 1.78 . . 445 . 47 ARG HB3 H 1.9 . . 446 . 47 ARG HG2 H 1.49 . . 447 . 47 ARG HE H 3.07 . . 448 . 47 ARG C C 180.05 . . 449 . 47 ARG CA C 59.94 . . 450 . 47 ARG CB C 29.9 . . 451 . 47 ARG N N 124.7 . . 452 . 48 GLU H H 8.07 . . 453 . 48 GLU HA H 4.12 . . 454 . 48 GLU HB2 H 2.37 . . 455 . 48 GLU HB3 H 2.19 . . 456 . 48 GLU HG2 H 2.51 . . 457 . 48 GLU C C 177.7 . . 458 . 48 GLU CA C 58.25 . . 459 . 48 GLU CB C 30.26 . . 460 . 48 GLU CG C 30.26 . . 461 . 48 GLU N N 123.3 . . 462 . 49 GLN H H 7.17 . . 463 . 49 GLN HA H 4.6 . . 464 . 49 GLN HB2 H 1.99 . . 465 . 49 GLN C C 175.33 . . 466 . 49 GLN CA C 54.33 . . 467 . 49 GLN CB C 29.33 . . 468 . 49 GLN N N 120.3 . . 469 . 50 ALA H H 7.22 . . 470 . 50 ALA HA H 4.28 . . 471 . 50 ALA HB H 1.7 . . 472 . 50 ALA C C 178.03 . . 473 . 50 ALA CA C 53.62 . . 474 . 50 ALA CB C 21.01 . . 475 . 50 ALA N N 127.7 . . 476 . 51 GLY H H 9.69 . . 477 . 51 GLY HA2 H 4.05 . . 478 . 51 GLY HA3 H 3.82 . . 479 . 51 GLY C C 173.33 . . 480 . 51 GLY CA C 46.05 . . 481 . 51 GLY N N 116.3 . . 482 . 52 GLY H H 7.79 . . 483 . 52 GLY HA2 H 4.47 . . 484 . 52 GLY HA3 H 3.92 . . 485 . 52 GLY C C 171.99 . . 486 . 52 GLY CA C 44.78 . . 487 . 52 GLY N N 111.5 . . 488 . 53 ASP H H 8.62 . . 489 . 53 ASP HA H 5.25 . . 490 . 53 ASP HB2 H 3.07 . . 491 . 53 ASP HB3 H 2.49 . . 492 . 53 ASP C C 176.35 . . 493 . 53 ASP CA C 54.47 . . 494 . 53 ASP CB C 42.27 . . 495 . 53 ASP N N 124.1 . . 496 . 54 ALA H H 9.24 . . 497 . 54 ALA HA H 5.24 . . 498 . 54 ALA HB H 1.75 . . 499 . 54 ALA C C 176.88 . . 500 . 54 ALA CA C 51.1 . . 501 . 54 ALA CB C 22.06 . . 502 . 54 ALA N N 136.8 . . 503 . 55 THR H H 8.44 . . 504 . 55 THR HA H 3.38 . . 505 . 55 THR HB H 68.14 . . 506 . 55 THR HG2 H 0.47 . . 507 . 55 THR C C 175.33 . . 508 . 55 THR CA C 69.19 . . 509 . 55 THR CB C 68.14 . . 510 . 55 THR CG2 C 20.38 . . 511 . 55 THR N N 124.1 . . 512 . 56 GLU H H 8.79 . . 513 . 56 GLU HA H 3.9 . . 514 . 56 GLU HB2 H 2.33 . . 515 . 56 GLU HB3 H 1.99 . . 516 . 56 GLU HG2 H 2.31 . . 517 . 56 GLU C C 178.37 . . 518 . 56 GLU CA C 59.73 . . 519 . 56 GLU N N 125.8 . . 520 . 57 ASN H H 7.93 . . 521 . 57 ASN HA H 4.43 . . 522 . 57 ASN HB2 H 2.82 . . 523 . 57 ASN HB3 H 2.67 . . 524 . 57 ASN C C 177.02 . . 525 . 57 ASN CA C 56.79 . . 526 . 57 ASN CB C 39.96 . . 527 . 57 ASN N N 123.5 . . 528 . 58 PHE H H 8.66 . . 529 . 58 PHE HA H 3.84 . . 530 . 58 PHE HB2 H 2.87 . . 531 . 58 PHE C C 178.7 . . 532 . 58 PHE CA C 55.11 . . 533 . 58 PHE CB C 39.75 . . 534 . 58 PHE N N 126 . . 535 . 59 GLU H H 8.32 . . 536 . 59 GLU HA H 3.83 . . 537 . 59 GLU HB2 H 1.89 . . 538 . 59 GLU HG2 H 2.69 . . 539 . 59 GLU C C 179.38 . . 540 . 59 GLU CA C 57.63 . . 541 . 59 GLU CB C 32.37 . . 542 . 59 GLU N N 124.8 . . 543 . 60 ASP H H 8.2 . . 544 . 60 ASP HA H 4.23 . . 545 . 60 ASP HB2 H 2.79 . . 546 . 60 ASP HB3 H 2.58 . . 547 . 60 ASP C C 177.7 . . 548 . 60 ASP CA C 56.78 . . 549 . 60 ASP CB C 41 . . 550 . 60 ASP N N 127.8 . . 551 . 61 VAL H H 6.73 . . 552 . 61 VAL HA H 3.3 . . 553 . 61 VAL HB H 0.4 . . 554 . 61 VAL HG1 H 0.78 . . 555 . 61 VAL HG2 H -1.07 . . 556 . 61 VAL C C 176.35 . . 557 . 61 VAL CA C 63.72 . . 558 . 61 VAL CB C 32.16 . . 559 . 61 VAL CG1 C 22.69 . . 560 . 61 VAL CG2 C 18.69 . . 561 . 61 VAL N N 122.8 . . 562 . 62 GLY H H 6.56 . . 563 . 62 GLY HA2 H 3.39 . . 564 . 62 GLY HA3 H 3.2 . . 565 . 62 GLY C C 174 . . 566 . 62 GLY CA C 46.05 . . 567 . 62 GLY N N 112 . . 568 . 63 HIS H H 6.02 . . 569 . 63 HIS HA H 2.59 . . 570 . 63 HIS HB2 H 1.04 . . 571 . 63 HIS HB3 H 0.37 . . 572 . 63 HIS C C 175.68 . . 573 . 63 HIS CA C 57.83 . . 574 . 63 HIS CB C 27.74 . . 575 . 63 HIS N N 122.9 . . 576 . 64 SER H H 9.71 . . 577 . 64 SER HA H 4.07 . . 578 . 64 SER HB2 H 4.27 . . 579 . 64 SER C C 175.34 . . 580 . 64 SER CA C 59.52 . . 581 . 64 SER CB C 64.77 . . 582 . 64 SER N N 128.7 . . 583 . 65 THR H H 8.72 . . 584 . 65 THR HA H 3.83 . . 585 . 65 THR HB H 4.23 . . 586 . 65 THR HG2 H 1.27 . . 587 . 65 THR C C 177.02 . . 588 . 65 THR CA C 68.14 . . 589 . 65 THR CB C 66.59 . . 590 . 65 THR CG2 C 22.48 . . 591 . 65 THR N N 125.8 . . 592 . 66 ASP H H 7.97 . . 593 . 66 ASP HA H 4.5 . . 594 . 66 ASP HB2 H 2.86 . . 595 . 66 ASP C C 179.04 . . 596 . 66 ASP CA C 57.63 . . 597 . 66 ASP CB C 39.1 . . 598 . 66 ASP N N 127.8 . . 599 . 67 ALA H H 8.54 . . 600 . 67 ALA HA H 4.74 . . 601 . 67 ALA HB H 1.23 . . 602 . 67 ALA C C 180.05 . . 603 . 67 ALA CA C 56.15 . . 604 . 67 ALA CB C 19.54 . . 605 . 67 ALA N N 131.7 . . 606 . 68 ARG H H 8.09 . . 607 . 68 ARG HA H 3.67 . . 608 . 68 ARG HB2 H 1.78 . . 609 . 68 ARG C C 181.05 . . 610 . 68 ARG CA C 56.15 . . 611 . 68 ARG N N 123.8 . . 612 . 69 GLU H H 8.62 . . 613 . 69 GLU HA H 4.17 . . 614 . 69 GLU HB2 H 2.51 . . 615 . 69 GLU HG2 H 2.44 . . 616 . 69 GLU C C 179.71 . . 617 . 69 GLU CA C 58.89 . . 618 . 69 GLU CB C 29.33 . . 619 . 69 GLU N N 129.2 . . 620 . 70 LEU H H 8.39 . . 621 . 70 LEU HA H 4.44 . . 622 . 70 LEU HB2 H 2.69 . . 623 . 70 LEU HB3 H 2.03 . . 624 . 70 LEU HG H 1.74 . . 625 . 70 LEU HD1 H 0.91 . . 626 . 70 LEU HD2 H 0.69 . . 627 . 70 LEU C C 180.72 . . 628 . 70 LEU CA C 57.85 . . 629 . 70 LEU CB C 42.65 . . 630 . 70 LEU N N 129.3 . . 631 . 71 SER H H 8.65 . . 632 . 71 SER HA H 4.2 . . 633 . 71 SER HB2 H 3.96 . . 634 . 71 SER C C 175.33 . . 635 . 71 SER CA C 59.52 . . 636 . 71 SER CB C 59.52 . . 637 . 71 SER N N 120.7 . . 638 . 72 LYS H H 7.34 . . 639 . 72 LYS HA H 4.22 . . 640 . 72 LYS HB2 H 2.02 . . 641 . 72 LYS HG2 H 1.8 . . 642 . 72 LYS HD2 H 1.62 . . 643 . 72 LYS HE2 H 3.06 . . 644 . 72 LYS C C 179.04 . . 645 . 72 LYS CA C 59.09 . . 646 . 72 LYS CB C 32.79 . . 647 . 72 LYS N N 127 . . 648 . 73 THR H H 7.94 . . 649 . 73 THR HA H 3.98 . . 650 . 73 THR HB H 3.85 . . 651 . 73 THR HG2 H 0.93 . . 652 . 73 THR C C 175.01 . . 653 . 73 THR CA C 69.19 . . 654 . 73 THR CG2 C 21.64 . . 655 . 73 THR N N 117.9 . . 656 . 74 TYR H H 7.72 . . 657 . 74 TYR HA H 4.73 . . 658 . 74 TYR HB2 H 3.82 . . 659 . 74 TYR HB3 H 2.83 . . 660 . 74 TYR C C 174.67 . . 661 . 74 TYR CA C 58.67 . . 662 . 74 TYR CB C 39.52 . . 663 . 74 TYR N N 124.6 . . 664 . 75 ILE H H 6.98 . . 665 . 75 ILE HA H 3.67 . . 666 . 75 ILE HB H 1.56 . . 667 . 75 ILE HG12 H 0.07 . . 668 . 75 ILE HG13 H -0.02 . . 669 . 75 ILE HG2 H 0.85 . . 670 . 75 ILE HD1 H 0.93 . . 671 . 75 ILE C C 178.03 . . 672 . 75 ILE CA C 62.88 . . 673 . 75 ILE CB C 39.12 . . 674 . 75 ILE CG1 C 30.05 . . 675 . 75 ILE CG2 C 57.84 . . 676 . 75 ILE CD1 C 54.89 . . 677 . 75 ILE N N 127.4 . . 678 . 76 ILE H H 8.84 . . 679 . 76 ILE HA H 4.68 . . 680 . 76 ILE HB H 1.87 . . 681 . 76 ILE HG12 H 0.09 . . 682 . 76 ILE HG13 H 0.32 . . 683 . 76 ILE HG2 H 0.82 . . 684 . 76 ILE HD1 H -1 . . 685 . 76 ILE C C 176.02 . . 686 . 76 ILE CA C 60.78 . . 687 . 76 ILE CB C 39.94 . . 688 . 76 ILE CG1 C 26.05 . . 689 . 76 ILE CG2 C 19.12 . . 690 . 76 ILE N N 126 . . 691 . 77 GLY H H 7.47 . . 692 . 77 GLY HA2 H 4.49 . . 693 . 77 GLY HA3 H 4.17 . . 694 . 77 GLY C C 171.31 . . 695 . 77 GLY CA C 46.05 . . 696 . 77 GLY N N 117 . . 697 . 78 GLU H H 9.1 . . 698 . 78 GLU HA H 5.25 . . 699 . 78 GLU HB2 H 2.26 . . 700 . 78 GLU HB3 H 1.84 . . 701 . 78 GLU HG2 H 2.34 . . 702 . 78 GLU C C 175.34 . . 703 . 78 GLU CA C 54.9 . . 704 . 78 GLU CB C 34.68 . . 705 . 78 GLU CG C 37.02 . . 706 . 78 GLU N N 125.6 . . 707 . 79 LEU H H 8.72 . . 708 . 79 LEU HA H 4.38 . . 709 . 79 LEU HB2 H 2.09 . . 710 . 79 LEU HB3 H 1.98 . . 711 . 79 LEU HG H 2.29 . . 712 . 79 LEU C C 177.02 . . 713 . 79 LEU CA C 54.55 . . 714 . 79 LEU CB C 43.6 . . 715 . 79 LEU N N 124.9 . . 716 . 80 HIS H H 9.07 . . 717 . 80 HIS HA H 3.84 . . 718 . 80 HIS HB2 H 2.64 . . 719 . 80 HIS HB3 H 2.96 . . 720 . 80 HIS C C 174.32 . . 721 . 80 HIS CA C 50.99 . . 722 . 80 HIS CB C 32.37 . . 723 . 80 HIS N N 137 . . 724 . 81 PRO HA H 3.77 . . 725 . 81 PRO HB2 H 2.02 . . 726 . 81 PRO HB3 H 1.76 . . 727 . 81 PRO HG2 H 1.64 . . 728 . 81 PRO HD2 H 2.67 . . 729 . 81 PRO HD3 H 2.34 . . 730 . 81 PRO C C 178.7 . . 731 . 81 PRO CA C 65.61 . . 732 . 81 PRO CB C 29.84 . . 733 . 81 PRO CD C 50.05 . . 734 . 82 ASP H H 10.98 . . 735 . 82 ASP HA H 4.52 . . 736 . 82 ASP HB2 H 2.71 . . 737 . 82 ASP C C 177.7 . . 738 . 82 ASP CA C 56.98 . . 739 . 82 ASP CB C 39.75 . . 740 . 82 ASP N N 127.8 . . 741 . 83 ASP H H 8.22 . . 742 . 83 ASP HA H 4.99 . . 743 . 83 ASP HB2 H 2.73 . . 744 . 83 ASP HB3 H 2.99 . . 745 . 83 ASP C C 177.7 . . 746 . 83 ASP CA C 54.89 . . 747 . 83 ASP CB C 43.1 . . 748 . 83 ASP N N 124.3 . . 749 . 84 ARG H H 7.43 . . 750 . 84 ARG HA H 4.04 . . 751 . 84 ARG HB2 H 1.82 . . 752 . 84 ARG HG2 H 1.59 . . 753 . 84 ARG HD2 H 2.95 . . 754 . 84 ARG CA C 57.31 . . 755 . 84 ARG N N 126.4 . . 756 . 85 SER H H 7.78 . . 757 . 85 SER HA H 3.77 . . 758 . 85 SER HB2 H 3.89 . . 759 . 85 SER C C 177.7 . . 760 . 85 SER CA C 59.52 . . 761 . 85 SER N N 131.6 . . 762 . 86 LYS H H 7.7 . . 763 . 86 LYS HA H 4.31 . . 764 . 86 LYS HB2 H 2.02 . . 765 . 86 LYS HB3 H 1.97 . . 766 . 86 LYS HG2 H 1.59 . . 767 . 86 LYS HE2 H 3.1 . . 768 . 86 LYS C C 177.02 . . 769 . 86 LYS CA C 57.41 . . 770 . 86 LYS N N 127.4 . . 771 . 87 ILE H H 7.37 . . 772 . 87 ILE HA H 4.39 . . 773 . 87 ILE HB H 2.13 . . 774 . 87 ILE HG12 H 1.02 . . 775 . 87 ILE HG2 H 1.02 . . 776 . 87 ILE HD1 H 1.37 . . 777 . 87 ILE C C 176.35 . . 778 . 87 ILE CA C 60.57 . . 779 . 87 ILE CB C 38.89 . . 780 . 87 ILE CG2 C 18.48 . . 781 . 87 ILE N N 122.1 . . 782 . 88 ALA H H 7.87 . . 783 . 88 ALA HA H 4.42 . . 784 . 88 ALA HB H 1.44 . . 785 . 88 ALA C C 178.03 . . 786 . 88 ALA CA C 52.78 . . 787 . 88 ALA CB C 19.75 . . 788 . 88 ALA N N 127.4 . . 789 . 89 LYS H H 8.27 . . 790 . 89 LYS HA H 4.66 . . 791 . 89 LYS HB2 H 3.07 . . 792 . 89 LYS HG2 H 1.55 . . 793 . 89 LYS HG3 H 1.53 . . 794 . 89 LYS C C 174.88 . . 795 . 89 LYS CA C 54.25 . . 796 . 89 LYS N N 128.7 . . 797 . 91 SER H H 8.69 . . 798 . 91 SER HA H 3.76 . . 799 . 91 SER HB2 H 3.36 . . 800 . 91 SER C C 175.68 . . 801 . 92 GLU H H 7.76 . . 802 . 92 GLU HA H 4.18 . . 803 . 92 GLU HB2 H 1.62 . . 804 . 92 GLU HB3 H 1.49 . . 805 . 92 GLU HG2 H 2.8 . . 806 . 92 GLU C C 176.35 . . 807 . 92 GLU CA C 56.71 . . 808 . 92 GLU CB C 29.83 . . 809 . 92 GLU N N 131.6 . . 810 . 93 THR H H 8.13 . . 811 . 93 THR HA H 4.39 . . 812 . 93 THR HB H 4.2 . . 813 . 93 THR HG2 H 1.21 . . 814 . 93 THR C C 173.66 . . 815 . 93 THR CA C 62.04 . . 816 . 93 THR CB C 69.19 . . 817 . 93 THR N N 121.9 . . 818 . 94 LEU H H 7.9 . . 819 . 94 LEU HA H 4.23 . . 820 . 94 LEU CA C 56.99 . . 821 . 94 LEU N N 137.5 . . stop_ save_