data_5030 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N Chemical Shift Assignment of the Honeybee Odorant-binding Protein ASP2 ; _BMRB_accession_number 5030 _BMRB_flat_file_name bmr5030.str _Entry_type original _Submission_date 2001-05-23 _Accession_date 2001-05-23 _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 Lescop Ewen . . 2 Briand Loic . . 3 Pernollet Jean-Claude . . 4 'van Heijenoort' Carine . . 5 Guittet Eric . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 444 "13C chemical shifts" 361 "15N chemical shifts" 119 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-05-30 original BMRB . stop_ _Original_release_date 2001-05-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C and 15N Chemical Shift Assignment of the Honeybee Odorant-binding Protein ASP2 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21584505 _PubMed_ID 11727984 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lescop Ewen . . 2 Briand Loic . . 3 Pernollet Jean-Claude . . 4 'van Heijenoort' Carine . . 5 Guittet Eric . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 21 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 181 _Page_last 182 _Year 2001 _Details . loop_ _Keyword 'apis mellifera L.' insect 'odorant binding protein' olfaction 'resonances assignments' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Briand L, Nespoulous C, Huet JC, Takahashi M, Pernollet JC. Ligand binding and physico-chemical properties of ASP2, a recombinant odorant-binding protein from honeybee (Apis mellifera L.). Eur J Biochem. 2001 Feb;268(3):752-60. ; _Citation_title ; Ligand binding and physico-chemical properties of ASP2, a recombinant odorant-binding protein from honeybee (Apis mellifera L.). ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11168415 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Briand L. . . 2 Nespoulous C. . . 3 Huet 'J. C.' C. . 4 Takahashi M. . . 5 Pernollet 'J. C.' C. . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_name_full 'European journal of biochemistry / FEBS' _Journal_volume 268 _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 752 _Page_last 760 _Year 2001 _Details ; In insects, the transport of airborne, hydrophobic odorants and pheromones through the sensillum lymph is generally thought to be accomplished by odorant-binding proteins (OBPs). We report the structural and functional properties of a honeybee OBP called ASP2, heterologously expressed by the yeast Pichia pastoris. ASP2 disulfide bonds were assigned after classic trypsinolysis followed by ion-spray mass spectrometry combined with microsequencing. The pairing [Cys(I)-Cys(III), Cys(II)-Cys(V), Cys(IV)-Cys(VI)] was found to be identical to that of Bombyx mori OBP, suggesting that this pattern occurs commonly throughout the highly divergent insect OBPs. CD measurements revealed that ASP2 is mainly constituted of alpha helices, like other insect OBPs, but different from lipocalin-like vertebrate OBPs. Gel filtration analysis showed that ASP2 is homodimeric at neutral pH, but monomerizes upon acidification or addition of a chaotropic agent. A general volatile-odorant binding assay allowed us to examine the uptake of some odorants and pheromones by ASP2. Recombinant ASP2 bound all tested molecules, except beta-ionone, which could not interact with it at all. The affinity constants of ASP2 for these ligands, determined at neutral pH by isothermal titration calorimetry, are in the micromolar range, as observed for vertebrate OBP. These results suggest that odorants occupy three binding sites per dimer, probably one in the core of each monomer and another whose location and biological role are questionable. At acidic pH, no binding was observed, in correlation with monomerization and a local conformational change supported by CD experiments. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Briand L, Perez V, Huet JC, Danty E, Masson C, Pernollet JC. Optimization of the production of a honeybee odorant-binding protein by Pichia pastoris. Protein Expr Purif. 1999 Apr;15(3):362-9. ; _Citation_title ; Optimization of the production of a honeybee odorant-binding protein by Pichia pastoris. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10092496 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Briand L. . . 2 Perez V. . . 3 Huet 'J. C.' C. . 4 Danty E. . . 5 Masson C. . . 6 Pernollet 'J. C.' C. . stop_ _Journal_abbreviation 'Protein Expr. Purif.' _Journal_name_full 'Protein expression and purification' _Journal_volume 15 _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 362 _Page_last 369 _Year 1999 _Details ; A honeybee putative general odorant-binding protein ASP2 has been expressed in the methylotrophic yeast Pichia pastoris. It was secreted into the buffered minimal medium using either the alpha-factor preprosequence with and without the Glu-Ala-Glu-Ala spacer peptide of Saccharomyces cerevisiae or its native signal peptide. Whereas ASP2 secreted using the alpha-factor preprosequence with the spacer peptide showed N-terminal heterogeneity, the recombinant protein using the two other secretion peptides was correctly processed. Mass spectrometry showed that the protein secreted using the natural peptide sequence had a mass of 13,695.1 Da, in perfect agreement with the measured molecular mass of the native protein. These data showed a native-like processing and the three disulfide bridges formation confirmed by sulfhydryl titration analysis. After dialysis, the recombinant protein was purified by one-step anion-exchange chromatography in a highly pure form. The final expression yield after 7-day fermentation was approximately 150 mg/liter. To our knowledge, this is the first report of the use of a natural insect leader sequence for secretion with correct processing in P. pastoris. The overproduction of recombinant ASP2 should allow ligand binding and mutational analysis to understand the relationships between structure and biological function of the protein. ; save_ save_ref_3 _Saveframe_category citation _Citation_full ; Danty E, Briand L, Michard-Vanhee C, Perez V, Arnold G, Gaudemer O, Huet D, Huet JC, Ouali C, Masson C, Pernollet JC. Cloning and expression of a queen pheromone-binding protein in the honeybee: an olfactory-specific, developmentally regulated protein. J Neurosci. 1999 Sep 1;19(17):7468-75. ; _Citation_title ; Cloning and expression of a queen pheromone-binding protein in the honeybee: an olfactory-specific, developmentally regulated protein. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10460253 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Danty E. . . 2 Briand L. . . 3 Michard-Vanhee C. . . 4 Perez V. . . 5 Arnold G. . . 6 Gaudemer O. . . 7 Huet D. . . 8 Huet 'J. C.' C. . 9 Ouali C. . . 10 Masson C. . . 11 Pernollet 'J. C.' C. . stop_ _Journal_abbreviation 'J. Neurosci.' _Journal_name_full 'The Journal of neuroscience : the official journal of the Society for Neuroscience' _Journal_volume 19 _Journal_issue 17 _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 7468 _Page_last 7475 _Year 1999 _Details ; Odorant-binding proteins (OBPs) are small abundant extracellular proteins thought to participate in perireceptor events of odor-pheromone detection by carrying, deactivating, and/or selecting odor stimuli. The honeybee queen pheromone is known to play a crucial role in colony organization, in addition to drone sex attraction. We identified, for the first time in a social insect, a binding protein called antennal-specific protein 1 (ASP1), which binds at least one of the major queen pheromone components. ASP1 was characterized by cDNA cloning, expression in Pichia pastoris, and pheromone binding. In situ hybridization showed that it is specifically expressed in the auxiliary cell layer of the antennal olfactory sensilla. The ASP1 sequence revealed it as a divergent member of the insect OBP family. The recombinant protein presented the exact characteristics of the native protein, as shown by mass spectrometry, and N-terminal sequencing and exclusion-diffusion chromatography showed that recombinant ASP1 is dimeric. ASP1 interacts with queen pheromone major components, opposite to another putative honeybee OBP, called ASP2. ASP1 biosynthetic accumulation, followed by nondenaturing electrophoresis during development, starts at day 1 before emergence, in concomitance with the functional maturation of olfactory neurons. The isobar ASP1b isoform appears simultaneously to ASP1a in workers, but only at approximately 2 weeks after emergence in drones. Comparison of in vivo and heterologous expressions suggests that the difference between ASP1 isoforms might be because of dimerization, which might play a physiological role in relation with mate attraction. ; save_ ################################## # Molecular system description # ################################## save_system_ASP2 _Saveframe_category molecular_system _Mol_system_name 'Honeybee antennal specific Protein 2' _Abbreviation_common ASP2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label ASP2 $ASP2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomeric _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'General Odorant-Binding Protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ASP2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ASP2 _Abbreviation_common ASP2 _Molecular_mass 13695 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 123 _Mol_residue_sequence ; IDQDTVVAKYMEYLMPDIMP CADELHISEDIATNIQAAKN GADMSQLGCLKACVMKRIEM LKGTELYVEPVYKMIEVVHA GNADDIQLVKGIANECIENA KGETDECNIGNKYTDCYIEK LFS ; loop_ _Residue_seq_code _Residue_label 1 ILE 2 ASP 3 GLN 4 ASP 5 THR 6 VAL 7 VAL 8 ALA 9 LYS 10 TYR 11 MET 12 GLU 13 TYR 14 LEU 15 MET 16 PRO 17 ASP 18 ILE 19 MET 20 PRO 21 CYS 22 ALA 23 ASP 24 GLU 25 LEU 26 HIS 27 ILE 28 SER 29 GLU 30 ASP 31 ILE 32 ALA 33 THR 34 ASN 35 ILE 36 GLN 37 ALA 38 ALA 39 LYS 40 ASN 41 GLY 42 ALA 43 ASP 44 MET 45 SER 46 GLN 47 LEU 48 GLY 49 CYS 50 LEU 51 LYS 52 ALA 53 CYS 54 VAL 55 MET 56 LYS 57 ARG 58 ILE 59 GLU 60 MET 61 LEU 62 LYS 63 GLY 64 THR 65 GLU 66 LEU 67 TYR 68 VAL 69 GLU 70 PRO 71 VAL 72 TYR 73 LYS 74 MET 75 ILE 76 GLU 77 VAL 78 VAL 79 HIS 80 ALA 81 GLY 82 ASN 83 ALA 84 ASP 85 ASP 86 ILE 87 GLN 88 LEU 89 VAL 90 LYS 91 GLY 92 ILE 93 ALA 94 ASN 95 GLU 96 CYS 97 ILE 98 GLU 99 ASN 100 ALA 101 LYS 102 GLY 103 GLU 104 THR 105 ASP 106 GLU 107 CYS 108 ASN 109 ILE 110 GLY 111 ASN 112 LYS 113 TYR 114 THR 115 ASP 116 CYS 117 TYR 118 ILE 119 GLU 120 LYS 121 LEU 122 PHE 123 SER 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 PDB 1TUJ 'Solution Structure Of The Honey Bee General Odorant Binding Protein Asp2 In Complex With Trimethylsilyl-D4 Propionate' 100.00 123 100.00 100.00 2.35e-65 GenBank AAD51945 'putative odorant-binding protein ASP2 [Apis mellifera]' 100.00 142 100.00 100.00 7.06e-66 GenBank AAL60418 'odorant binding protein ASP2 [Apis mellifera]' 100.00 142 100.00 100.00 7.06e-66 GenBank ABD97844 'odorant binding protein ASP2 [Apis cerana cerana]' 100.00 142 98.37 99.19 1.61e-64 REF NP_001011591 'odorant binding protein ASP2 [Apis mellifera]' 100.00 142 100.00 100.00 7.06e-66 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ _Secretion $ASP2 Honeybee 7460 Eukaryota Metazoa Apis mellifera antennae 'sensillum lymph' 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 $ASP2 'recombinant technology' 'P. pastoris' Pichia pastoris GS115 Muts pHIL-D2 pNatASP2 'The host-vector system used was extremely efficient (around 100mg/L), see ref_2.' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_15N13C_H2O _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $ASP2 . mM 0.7 1.5 '[U-98% 13C; U-98% 15N]' TSP 0.1 mM . . . 'phosphate buffer' 100 mM . . . NaN3 0.1 mM . . . H2O 90 % . . . D2O 10 % . . . stop_ save_ save_15N13C_D2O _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ASP2 1.3 mM '[U-98% 13C; U-98% 15N]' TSP 0.1 mM . 'phosphate buffer' 100 mM . NaN3 0.1 mM . D2O 100 % . stop_ save_ save_15N_H2O _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ASP2 1 mM '[U-98% 15N]' TSP 0.1 mM . 'phosphate buffer' 100 mM . NaN3 0.1 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.6 loop_ _Task acquisition processing stop_ _Details 'Developed by Bruker' save_ save_AURELIA _Saveframe_category software _Name AURELIA _Version 2.8.4 loop_ _Task Analysis stop_ _Details 'Developed by Bruker' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details ; Spectrometer equipped with a 5 mm TXI triple resonance, triple-axis gradient probe. ; save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_1H-15N_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_HNCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HCCH-TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_NOESY-HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY-HSQC _Sample_label . save_ ####################### # Sample conditions # ####################### save_Cond_D2O _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.11 . M pH 7.7 0.1 n/a temperature 308 1 K stop_ save_ save_Cond_H2O _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.11 . M pH 5.7 0.1 n/a temperature 308 1 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 TSP C 13 'methyl protons' ppm 0.00 internal indirect . internal . 0.101329118 TSP H 1 'methyl protons' ppm 0.00 internal direct . internal . 1.0 TSP N 15 'methyl protons' ppm 0.00 internal indirect . internal . 0.251449530 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_ASP2_shift_set _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N NOESY' '1H-15N TOCSY' HNCA HN(CO)CA HNCO HN(CA)CO HNCACB CBCA(CO)NH HCCH-TOCSY NOESY-HSQC stop_ _Sample_conditions_label $Cond_D2O _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name ASP2 _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 ILE HA H 3.77 0.02 1 2 . 1 ILE HB H 2.01 0.02 1 3 . 1 ILE C C 171.70 0.05 1 4 . 1 ILE CA C 59.70 0.20 1 5 . 1 ILE CB C 38.90 0.40 1 6 . 2 ASP H H 8.79 0.01 1 7 . 2 ASP HA H 4.89 0.02 1 8 . 2 ASP HB2 H 2.69 0.02 2 9 . 2 ASP HB3 H 2.92 0.02 2 10 . 2 ASP C C 175.50 0.05 1 11 . 2 ASP CA C 53.20 0.20 1 12 . 2 ASP CB C 41.10 0.40 1 13 . 2 ASP N N 126.70 0.10 1 14 . 3 GLN H H 8.80 0.01 1 15 . 3 GLN HA H 3.81 0.02 1 16 . 3 GLN HB2 H 1.88 0.02 1 17 . 3 GLN HB3 H 1.88 0.02 1 18 . 3 GLN C C 176.70 0.05 1 19 . 3 GLN CA C 59.50 0.20 1 20 . 3 GLN CB C 28.40 0.40 1 21 . 3 GLN N N 125.00 0.10 1 22 . 4 ASP H H 8.51 0.01 1 23 . 4 ASP HA H 4.40 0.02 1 24 . 4 ASP HB2 H 2.70 0.02 2 25 . 4 ASP HB3 H 2.77 0.02 2 26 . 4 ASP C C 178.76 0.05 1 27 . 4 ASP CA C 57.10 0.20 1 28 . 4 ASP CB C 40.40 0.40 1 29 . 4 ASP N N 117.10 0.10 1 30 . 5 THR H H 7.69 0.01 1 31 . 5 THR HA H 4.31 0.02 2 32 . 5 THR HB H 4.29 0.02 2 33 . 5 THR C C 176.50 0.05 1 34 . 5 THR CA C 64.50 0.20 1 35 . 5 THR CB C 69.60 0.40 1 36 . 5 THR N N 113.30 0.10 1 37 . 6 VAL H H 7.94 0.01 1 38 . 6 VAL HA H 3.81 0.02 1 39 . 6 VAL HB H 2.33 0.02 1 40 . 6 VAL C C 177.40 0.05 1 41 . 6 VAL CA C 66.20 0.20 1 42 . 6 VAL CB C 31.80 0.40 1 43 . 6 VAL N N 120.40 0.10 1 44 . 7 VAL H H 8.49 0.01 1 45 . 7 VAL HA H 3.79 0.02 1 46 . 7 VAL HB H 2.21 0.02 1 47 . 7 VAL C C 177.60 0.05 1 48 . 7 VAL CA C 68.00 0.20 1 49 . 7 VAL CB C 32.00 0.40 1 50 . 7 VAL N N 120.60 0.10 1 51 . 8 ALA H H 7.70 0.01 1 52 . 8 ALA HA H 4.16 0.02 1 53 . 8 ALA HB H 1.56 0.02 1 54 . 8 ALA C C 180.70 0.05 1 55 . 8 ALA CA C 55.20 0.20 1 56 . 8 ALA CB C 17.80 0.40 1 57 . 8 ALA N N 120.10 0.10 1 58 . 9 LYS H H 7.79 0.01 1 59 . 9 LYS HA H 4.22 0.02 1 60 . 9 LYS HB2 H 1.78 0.02 2 61 . 9 LYS HB3 H 2.02 0.02 2 62 . 9 LYS C C 180.30 0.05 1 63 . 9 LYS CA C 59.20 0.20 1 64 . 9 LYS CB C 33.00 0.40 1 65 . 9 LYS N N 118.30 0.10 1 66 . 10 TYR H H 8.47 0.01 1 67 . 10 TYR HA H 4.20 0.02 1 68 . 10 TYR HB2 H 2.98 0.02 2 69 . 10 TYR HB3 H 3.29 0.02 2 70 . 10 TYR C C 178.50 0.05 1 71 . 10 TYR CA C 63.20 0.20 1 72 . 10 TYR CB C 38.80 0.40 1 73 . 10 TYR N N 120.20 0.10 1 74 . 11 MET H H 8.57 0.01 1 75 . 11 MET HA H 4.21 0.02 1 76 . 11 MET HB2 H 2.28 0.02 2 77 . 11 MET HB3 H 2.00 0.02 2 78 . 11 MET C C 178.30 0.05 1 79 . 11 MET CA C 58.00 0.20 1 80 . 11 MET CB C 31.50 0.40 1 81 . 11 MET N N 116.70 0.10 1 82 . 12 GLU H H 8.16 0.01 1 83 . 12 GLU HA H 4.02 0.02 1 84 . 12 GLU HB2 H 2.16 0.02 2 85 . 12 GLU HB3 H 2.20 0.02 2 86 . 12 GLU C C 178.80 0.05 1 87 . 12 GLU CA C 59.40 0.20 1 88 . 12 GLU CB C 29.60 0.40 1 89 . 12 GLU N N 118.40 0.10 1 90 . 13 TYR H H 7.79 0.01 1 91 . 13 TYR HA H 4.03 0.02 1 92 . 13 TYR HB2 H 3.31 0.02 2 93 . 13 TYR HB3 H 3.02 0.02 2 94 . 13 TYR C C 177.50 0.05 1 95 . 13 TYR CA C 61.20 0.20 1 96 . 13 TYR CB C 38.90 0.40 1 97 . 13 TYR N N 119.10 0.10 1 98 . 14 LEU H H 8.30 0.01 1 99 . 14 LEU HA H 4.58 0.02 1 100 . 14 LEU HB2 H 1.62 0.02 2 101 . 14 LEU HB3 H 2.06 0.02 2 102 . 14 LEU C C 178.62 0.05 1 103 . 14 LEU CA C 55.00 0.20 1 104 . 14 LEU CB C 43.70 0.40 1 105 . 14 LEU N N 114.50 0.10 1 106 . 15 MET H H 8.30 0.01 1 107 . 15 MET HA H 4.56 0.02 1 108 . 15 MET HB2 H 2.59 0.02 2 109 . 15 MET HB3 H 2.21 0.02 2 110 . 15 MET C C 173.77 0.05 1 111 . 15 MET CA C 59.50 0.20 1 112 . 15 MET CB C 28.20 0.40 1 113 . 15 MET N N 124.20 0.10 1 114 . 16 PRO HA H 4.39 0.02 1 115 . 16 PRO HB2 H 2.31 0.02 2 116 . 16 PRO HB3 H 1.76 0.02 2 117 . 16 PRO C C 176.13 0.05 1 118 . 16 PRO CA C 65.50 0.20 1 119 . 16 PRO CB C 31.00 0.40 1 120 . 17 ASP H H 8.02 0.01 1 121 . 17 ASP HA H 4.84 0.02 1 122 . 17 ASP HB2 H 2.52 0.02 2 123 . 17 ASP HB3 H 2.62 0.02 2 124 . 17 ASP C C 175.95 0.05 1 125 . 17 ASP CA C 55.80 0.20 1 126 . 17 ASP CB C 44.60 0.40 1 127 . 17 ASP N N 113.70 0.10 1 128 . 18 ILE H H 8.42 0.01 1 129 . 18 ILE HA H 3.44 0.02 1 130 . 18 ILE HB H 1.89 0.02 1 131 . 18 ILE C C 177.66 0.05 1 132 . 18 ILE CA C 65.60 0.20 1 133 . 18 ILE CB C 37.90 0.40 1 134 . 18 ILE N N 120.40 0.10 1 135 . 19 MET H H 7.83 0.01 1 136 . 19 MET HA H 4.43 0.02 1 137 . 19 MET HB2 H 2.12 0.02 1 138 . 19 MET HB3 H 2.12 0.02 1 139 . 19 MET C C 175.95 0.05 1 140 . 19 MET CA C 59.60 0.20 1 141 . 19 MET CB C 29.20 0.40 1 142 . 19 MET N N 115.30 0.10 1 143 . 20 PRO HA H 4.48 0.02 1 144 . 20 PRO HB2 H 2.36 0.02 2 145 . 20 PRO HB3 H 1.75 0.02 2 146 . 20 PRO C C 180.30 0.05 1 147 . 20 PRO CA C 65.70 0.20 1 148 . 20 PRO CB C 30.80 0.40 1 149 . 21 CYS H H 6.77 0.01 1 150 . 21 CYS HA H 4.41 0.02 1 151 . 21 CYS HB2 H 2.74 0.02 2 152 . 21 CYS HB3 H 3.24 0.02 2 153 . 21 CYS C C 175.30 0.05 1 154 . 21 CYS CA C 59.70 0.20 1 155 . 21 CYS CB C 41.00 0.40 1 156 . 21 CYS N N 116.60 0.10 1 157 . 22 ALA H H 8.86 0.01 1 158 . 22 ALA HA H 3.84 0.02 1 159 . 22 ALA HB H 1.42 0.02 1 160 . 22 ALA C C 179.30 0.05 1 161 . 22 ALA CA C 55.60 0.20 1 162 . 22 ALA CB C 16.60 0.40 1 163 . 22 ALA N N 123.70 0.10 1 164 . 23 ASP H H 7.95 0.01 1 165 . 23 ASP HA H 4.40 0.02 1 166 . 23 ASP HB2 H 2.74 0.02 2 167 . 23 ASP HB3 H 2.93 0.02 2 168 . 23 ASP C C 179.40 0.05 1 169 . 23 ASP CA C 57.10 0.20 1 170 . 23 ASP CB C 41.10 0.40 1 171 . 23 ASP N N 117.00 0.10 1 172 . 24 GLU H H 8.01 0.01 1 173 . 24 GLU HA H 3.92 0.02 1 174 . 24 GLU HB2 H 2.25 0.02 2 175 . 24 GLU HB3 H 2.10 0.02 2 176 . 24 GLU C C 177.96 0.05 1 177 . 24 GLU CA C 58.90 0.20 1 178 . 24 GLU CB C 29.40 0.40 1 179 . 24 GLU N N 120.20 0.10 1 180 . 25 LEU H H 7.64 0.01 1 181 . 25 LEU HA H 4.22 0.02 1 182 . 25 LEU HB2 H 1.63 0.02 1 183 . 25 LEU HB3 H 1.63 0.02 1 184 . 25 LEU C C 175.80 0.05 1 185 . 25 LEU CA C 54.40 0.20 1 186 . 25 LEU CB C 42.00 0.40 1 187 . 25 LEU N N 116.30 0.10 1 188 . 26 HIS H H 7.75 0.01 1 189 . 26 HIS HA H 4.35 0.02 1 190 . 26 HIS HB2 H 3.35 0.02 2 191 . 26 HIS HB3 H 3.51 0.02 2 192 . 26 HIS C C 174.00 0.05 1 193 . 26 HIS CA C 55.90 0.20 1 194 . 26 HIS CB C 26.00 0.40 1 195 . 26 HIS N N 115.60 0.10 1 196 . 27 ILE H H 8.47 0.01 1 197 . 27 ILE HA H 4.30 0.02 1 198 . 27 ILE HB H 1.53 0.02 1 199 . 27 ILE C C 175.40 0.05 1 200 . 27 ILE CA C 59.80 0.20 1 201 . 27 ILE CB C 39.60 0.40 1 202 . 27 ILE N N 118.90 0.10 1 203 . 28 SER H H 8.36 0.01 1 204 . 28 SER HA H 4.26 0.02 1 205 . 28 SER HB2 H 3.92 0.02 2 206 . 28 SER HB3 H 4.12 0.02 2 207 . 28 SER C C 175.60 0.05 1 208 . 28 SER CA C 58.80 0.20 1 209 . 28 SER CB C 63.70 0.40 1 210 . 28 SER N N 120.70 0.10 1 211 . 29 GLU H H 8.79 0.01 1 212 . 29 GLU HA H 3.91 0.02 1 213 . 29 GLU HB2 H 2.05 0.02 1 214 . 29 GLU C C 177.15 0.05 1 215 . 29 GLU CA C 59.50 0.20 1 216 . 29 GLU CB C 28.90 0.40 1 217 . 29 GLU N N 123.70 0.10 1 218 . 30 ASP H H 8.31 0.01 1 219 . 30 ASP HA H 4.40 0.02 1 220 . 30 ASP HB2 H 2.61 0.02 2 221 . 30 ASP HB3 H 2.70 0.02 2 222 . 30 ASP C C 177.22 0.05 1 223 . 30 ASP CA C 55.70 0.20 1 224 . 30 ASP CB C 39.50 0.40 1 225 . 30 ASP N N 118.20 0.10 1 226 . 31 ILE H H 7.41 0.01 1 227 . 31 ILE HA H 3.92 0.02 1 228 . 31 ILE HB H 1.92 0.02 1 229 . 31 ILE C C 177.14 0.05 1 230 . 31 ILE CA C 62.60 0.20 1 231 . 31 ILE CB C 39.40 0.40 1 232 . 31 ILE N N 119.90 0.10 1 233 . 32 ALA H H 8.02 0.01 1 234 . 32 ALA HA H 3.85 0.02 1 235 . 32 ALA HB H 1.29 0.02 1 236 . 32 ALA C C 176.60 0.05 1 237 . 32 ALA CA C 54.10 0.20 1 238 . 32 ALA CB C 19.70 0.40 1 239 . 32 ALA N N 120.40 0.10 1 240 . 33 THR H H 7.64 0.01 1 241 . 33 THR HA H 4.16 0.02 1 242 . 33 THR HB H 4.24 0.02 1 243 . 33 THR C C 174.16 0.05 1 244 . 33 THR CA C 62.90 0.20 1 245 . 33 THR CB C 70.70 0.40 1 246 . 33 THR N N 118.50 0.10 1 247 . 34 ASN H H 7.42 0.01 1 248 . 34 ASN HA H 4.79 0.02 1 249 . 34 ASN HB2 H 2.89 0.02 2 250 . 34 ASN HB3 H 2.81 0.02 2 251 . 34 ASN C C 175.96 0.05 1 252 . 34 ASN CA C 53.00 0.20 1 253 . 34 ASN CB C 38.90 0.40 1 254 . 34 ASN N N 120.00 0.10 1 255 . 35 ILE H H 8.34 0.01 1 256 . 35 ILE HA H 3.96 0.02 1 257 . 35 ILE HB H 1.92 0.02 1 258 . 35 ILE C C 176.57 0.05 1 259 . 35 ILE CA C 63.10 0.20 1 260 . 35 ILE N N 122.00 0.10 1 261 . 36 GLN H H 8.05 0.01 1 262 . 36 GLN HA H 3.94 0.02 1 263 . 36 GLN HB2 H 2.08 0.02 2 264 . 36 GLN HB3 H 2.23 0.02 2 265 . 36 GLN C C 176.57 0.05 1 266 . 36 GLN CA C 56.70 0.20 1 267 . 36 GLN CB C 29.00 0.40 1 268 . 36 GLN N N 119.80 0.10 1 269 . 37 ALA H H 7.81 0.01 1 270 . 37 ALA HA H 4.20 0.02 1 271 . 37 ALA HB H 1.43 0.02 1 272 . 37 ALA C C 178.43 0.05 1 273 . 37 ALA CA C 53.50 0.20 1 274 . 37 ALA CB C 18.50 0.40 1 275 . 37 ALA N N 122.30 0.10 1 276 . 38 ALA H H 8.06 0.01 1 277 . 38 ALA HA H 4.12 0.02 1 278 . 38 ALA HB H 1.42 0.02 1 279 . 38 ALA C C 178.70 0.05 1 280 . 38 ALA CA C 54.40 0.20 1 281 . 38 ALA CB C 18.50 0.40 1 282 . 38 ALA N N 121.10 0.10 1 283 . 39 LYS H H 7.99 0.01 1 284 . 39 LYS HA H 4.23 0.02 1 285 . 39 LYS HB2 H 1.80 0.02 1 286 . 39 LYS HB3 H 1.80 0.02 1 287 . 39 LYS C C 176.70 0.05 1 288 . 39 LYS CA C 57.20 0.20 1 289 . 39 LYS CB C 32.70 0.40 1 290 . 39 LYS N N 118.30 0.10 1 291 . 40 ASN H H 7.95 0.01 1 292 . 40 ASN HA H 4.75 0.02 1 293 . 40 ASN HB2 H 2.91 0.02 2 294 . 40 ASN HB3 H 2.77 0.02 2 295 . 40 ASN C C 175.70 0.05 1 296 . 40 ASN CA C 53.30 0.20 1 297 . 40 ASN CB C 38.8 0.40 1 298 . 40 ASN N N 117.00 0.10 1 299 . 41 GLY H H 8.10 0.01 1 300 . 41 GLY HA2 H 3.90 0.02 1 301 . 41 GLY HA3 H 4.04 0.02 1 302 . 41 GLY C C 174.30 0.05 1 303 . 41 GLY CA C 45.40 0.20 1 304 . 41 GLY N N 108.30 0.10 1 305 . 42 ALA H H 7.89 0.01 1 306 . 42 ALA HA H 4.30 0.02 1 307 . 42 ALA HB H 1.33 0.02 1 308 . 42 ALA C C 177.21 0.05 1 309 . 42 ALA CA C 52.50 0.20 1 310 . 42 ALA CB C 19.40 0.40 1 311 . 42 ALA N N 123.00 0.10 1 312 . 43 ASP H H 8.32 0.01 1 313 . 43 ASP HA H 4.59 0.02 1 314 . 43 ASP HB2 H 2.71 0.02 2 315 . 43 ASP HB3 H 2.80 0.02 2 316 . 43 ASP C C 176.80 0.05 1 317 . 43 ASP CA C 54.10 0.20 1 318 . 43 ASP CB C 41.20 0.40 1 319 . 43 ASP N N 118.90 0.10 1 320 . 44 MET H H 8.50 0.01 1 321 . 44 MET HA H 4.51 0.02 1 322 . 44 MET HB2 H 2.13 0.02 2 323 . 44 MET HB3 H 2.05 0.02 2 324 . 44 MET C C 178.76 0.05 1 325 . 44 MET CA C 56.10 0.20 1 326 . 44 MET CB C 32.20 0.40 1 327 . 44 MET N N 123.10 0.10 1 328 . 45 SER H H 8.58 0.01 1 329 . 45 SER HA H 4.03 0.02 1 330 . 45 SER HB2 H 4.26 0.02 1 331 . 45 SER HB3 H 4.26 0.02 1 332 . 45 SER C C 176.33 0.05 1 333 . 45 SER CA C 62.60 0.20 1 334 . 45 SER CB C 61.40 0.20 1 335 . 45 SER N N 118.80 0.10 1 336 . 46 GLN H H 8.41 0.01 1 337 . 46 GLN HA H 4.32 0.02 1 338 . 46 GLN HB2 H 2.13 0.02 2 339 . 46 GLN HB3 H 2.22 0.02 2 340 . 46 GLN C C 177.89 0.05 1 341 . 46 GLN CA C 57.60 0.20 1 342 . 46 GLN CB C 28.80 0.40 1 343 . 46 GLN N N 121.00 0.10 1 344 . 47 LEU H H 7.93 0.01 1 345 . 47 LEU HA H 4.35 0.02 1 346 . 47 LEU HB2 H 1.76 0.02 2 347 . 47 LEU HB3 H 1.87 0.02 2 348 . 47 LEU C C 178.70 0.05 1 349 . 47 LEU CA C 56.10 0.20 1 350 . 47 LEU CB C 42.30 0.40 1 351 . 47 LEU N N 119.00 0.10 1 352 . 48 GLY H H 8.29 0.01 1 353 . 48 GLY HA2 H 3.70 0.02 1 354 . 48 GLY HA3 H 4.18 0.02 1 355 . 48 GLY C C 176.42 0.05 1 356 . 48 GLY CA C 48.20 0.20 1 357 . 48 GLY N N 110.30 0.10 1 358 . 49 CYS H H 8.23 0.01 1 359 . 49 CYS HA H 4.29 0.02 1 360 . 49 CYS HB2 H 2.59 0.02 2 361 . 49 CYS HB3 H 2.72 0.02 2 362 . 49 CYS C C 177.90 0.05 1 363 . 49 CYS CA C 58.50 0.20 1 364 . 49 CYS CB C 37.50 0.40 1 365 . 49 CYS N N 120.00 0.10 1 366 . 50 LEU H H 8.03 0.01 1 367 . 50 LEU HA H 4.00 0.02 1 368 . 50 LEU HB2 H 1.54 0.02 2 369 . 50 LEU HB3 H 2.30 0.02 2 370 . 50 LEU C C 177.70 0.05 1 371 . 50 LEU CA C 58.80 0.20 1 372 . 50 LEU CB C 40.50 0.40 1 373 . 50 LEU N N 125.60 0.10 1 374 . 51 LYS H H 8.25 0.01 1 375 . 51 LYS HA H 3.84 0.02 1 376 . 51 LYS HB2 H 1.82 0.02 1 377 . 51 LYS HB3 H 1.82 0.02 1 378 . 51 LYS C C 178.62 0.05 1 379 . 51 LYS CA C 60.30 0.20 1 380 . 51 LYS CB C 29.50 0.40 1 381 . 51 LYS N N 118.90 0.10 1 382 . 52 ALA H H 8.38 0.01 1 383 . 52 ALA HA H 4.10 0.02 1 384 . 52 ALA HB H 1.42 0.02 1 385 . 52 ALA C C 178.50 0.05 1 386 . 52 ALA CA C 54.70 0.20 1 387 . 52 ALA CB C 18.50 0.40 1 388 . 52 ALA N N 119.90 0.10 1 389 . 53 CYS H H 8.07 0.01 1 390 . 53 CYS HA H 4.17 0.02 1 391 . 53 CYS HB2 H 3.52 0.02 2 392 . 53 CYS HB3 H 3.26 0.02 2 393 . 53 CYS C C 177.10 0.05 1 394 . 53 CYS CA C 60.60 0.20 1 395 . 53 CYS CB C 38.20 0.40 1 396 . 53 CYS N N 118.60 0.10 1 397 . 54 VAL H H 8.14 0.01 1 398 . 54 VAL HA H 3.38 0.02 1 399 . 54 VAL HB H 2.31 0.02 1 400 . 54 VAL C C 177.30 0.05 1 401 . 54 VAL CA C 67.00 0.20 1 402 . 54 VAL CB C 31.90 0.40 1 403 . 54 VAL N N 123.30 0.10 1 404 . 55 MET H H 8.26 0.01 1 405 . 55 MET HA H 3.79 0.02 1 406 . 55 MET HB2 H 2.21 0.02 2 407 . 55 MET HB3 H 1.93 0.02 2 408 . 55 MET C C 179.00 0.05 1 409 . 55 MET CA C 59.70 0.20 1 410 . 55 MET CB C 34.00 0.40 1 411 . 55 MET N N 117.40 0.10 1 412 . 56 LYS H H 8.55 0.01 1 413 . 56 LYS HA H 4.53 0.02 1 414 . 56 LYS HB2 H 2.05 0.02 1 415 . 56 LYS HB3 H 2.05 0.02 1 416 . 56 LYS C C 181.00 0.05 1 417 . 56 LYS CA C 59.70 0.20 1 418 . 56 LYS CB C 32.20 0.40 1 419 . 56 LYS N N 120.30 0.10 1 420 . 57 ARG H H 8.21 0.01 1 421 . 57 ARG HA H 4.08 0.02 1 422 . 57 ARG HB2 H 2.04 0.02 2 423 . 57 ARG HB3 H 1.99 0.02 2 424 . 57 ARG C C 179.10 0.05 1 425 . 57 ARG CA C 60.60 0.20 1 426 . 57 ARG CB C 30.60 0.40 1 427 . 57 ARG N N 122.00 0.10 1 428 . 58 ILE H H 7.80 0.01 1 429 . 58 ILE HA H 4.56 0.02 1 430 . 58 ILE HB H 2.34 0.02 1 431 . 58 ILE C C 174.90 0.05 1 432 . 58 ILE CA C 61.40 0.20 1 433 . 58 ILE CB C 37.60 0.40 1 434 . 58 ILE N N 109.80 0.10 1 435 . 59 GLU H H 7.50 0.01 1 436 . 59 GLU HA H 3.78 0.02 1 437 . 59 GLU HB2 H 2.13 0.02 2 438 . 59 GLU HB3 H 2.09 0.02 2 439 . 59 GLU C C 174.50 0.05 1 440 . 59 GLU CA C 58.20 0.20 1 441 . 59 GLU CB C 26.20 0.40 1 442 . 59 GLU N N 111.60 0.10 1 443 . 60 MET H H 8.21 0.01 1 444 . 60 MET HA H 4.84 0.02 1 445 . 60 MET HB2 H 1.68 0.02 2 446 . 60 MET HB3 H 2.23 0.02 2 447 . 60 MET C C 173.20 0.05 1 448 . 60 MET CA C 56.80 0.20 1 449 . 60 MET CB C 34.20 0.40 1 450 . 60 MET N N 116.10 0.10 1 451 . 61 LEU H H 6.67 0.01 1 452 . 61 LEU HA H 5.23 0.02 1 453 . 61 LEU HB2 H 0.96 0.02 2 454 . 61 LEU HB3 H 1.42 0.02 2 455 . 61 LEU C C 175.00 0.05 1 456 . 61 LEU CA C 52.70 0.20 1 457 . 61 LEU CB C 46.00 0.40 1 458 . 61 LEU N N 120.20 0.10 1 459 . 62 LYS H H 8.73 0.01 1 460 . 62 LYS HA H 4.50 0.02 1 461 . 62 LYS HB2 H 1.81 0.02 1 462 . 62 LYS HB3 H 1.81 0.02 1 463 . 62 LYS C C 176.50 0.05 1 464 . 62 LYS CA C 55.70 0.20 1 465 . 62 LYS CB C 33.60 0.40 1 466 . 62 LYS N N 126.50 0.10 1 467 . 63 GLY H H 9.04 0.01 1 468 . 63 GLY HA2 H 4.19 0.02 1 469 . 63 GLY HA3 H 3.67 0.02 1 470 . 63 GLY C C 173.90 0.05 1 471 . 63 GLY CA C 47.00 0.20 1 472 . 63 GLY N N 117.70 0.10 1 473 . 64 THR H H 8.60 0.01 1 474 . 64 THR HA H 4.24 0.02 1 475 . 64 THR HB H 4.58 0.02 1 476 . 64 THR C C 173.00 0.05 1 477 . 64 THR CA C 60.80 0.20 1 478 . 64 THR CB C 68.50 0.40 1 479 . 64 THR N N 116.60 0.10 1 480 . 65 GLU H H 7.98 0.01 1 481 . 65 GLU HA H 4.42 0.02 1 482 . 65 GLU HB2 H 1.88 0.02 2 483 . 65 GLU HB3 H 2.12 0.02 2 484 . 65 GLU C C 174.10 0.05 1 485 . 65 GLU CA C 55.40 0.20 1 486 . 65 GLU CB C 32.20 0.40 1 487 . 65 GLU N N 122.00 0.10 1 488 . 66 LEU H H 7.82 0.01 1 489 . 66 LEU HA H 5.25 0.02 1 490 . 66 LEU HB2 H 0.94 0.02 2 491 . 66 LEU HB3 H 1.58 0.02 2 492 . 66 LEU C C 176.40 0.05 1 493 . 66 LEU CA C 52.90 0.20 1 494 . 66 LEU CB C 45.20 0.40 1 495 . 66 LEU N N 121.60 0.10 1 496 . 67 TYR H H 9.14 0.01 1 497 . 67 TYR HA H 4.55 0.02 1 498 . 67 TYR HB2 H 3.16 0.02 2 499 . 67 TYR HB3 H 2.81 0.02 2 500 . 67 TYR C C 175.00 0.05 1 501 . 67 TYR CA C 56.80 0.20 1 502 . 67 TYR CB C 40.20 0.40 1 503 . 67 TYR N N 122.00 0.10 1 504 . 68 VAL H H 8.07 0.01 1 505 . 68 VAL HA H 3.91 0.02 1 506 . 68 VAL HB H 1.75 0.02 1 507 . 68 VAL C C 177.00 0.05 1 508 . 68 VAL CA C 62.80 0.20 1 509 . 68 VAL CB C 33.30 0.40 1 510 . 68 VAL N N 117.90 0.10 1 511 . 69 GLU H H 8.91 0.01 1 512 . 69 GLU HA H 3.83 0.02 1 513 . 69 GLU HB2 H 2.01 0.02 2 514 . 69 GLU HB3 H 2.19 0.02 2 515 . 69 GLU C C 176.10 0.05 1 516 . 69 GLU CA C 63.00 0.20 1 517 . 69 GLU CB C 26.40 0.40 1 518 . 69 GLU N N 123.90 0.10 1 519 . 70 PRO HA H 4.37 0.02 1 520 . 70 PRO HB2 H 1.52 0.02 2 521 . 70 PRO HB3 H 2.60 0.02 2 522 . 70 PRO C C 179.53 0.05 1 523 . 70 PRO CA C 65.20 0.20 1 524 . 70 PRO CB C 32.40 0.40 1 525 . 71 VAL H H 7.46 0.01 1 526 . 71 VAL HA H 3.82 0.02 1 527 . 71 VAL HB H 2.37 0.02 1 528 . 71 VAL C C 178.06 0.05 1 529 . 71 VAL CA C 65.20 0.20 1 530 . 71 VAL CB C 31.60 0.40 1 531 . 71 VAL N N 117.60 0.10 1 532 . 72 TYR H H 8.28 0.01 1 533 . 72 TYR HA H 4.43 0.02 1 534 . 72 TYR HB2 H 3.67 0.02 2 535 . 72 TYR HB3 H 3.18 0.02 2 536 . 72 TYR C C 177.83 0.05 1 537 . 72 TYR CA C 58.50 0.20 1 538 . 72 TYR CB C 35.60 0.40 1 539 . 72 TYR N N 120.60 0.10 1 540 . 73 LYS H H 7.80 0.01 1 541 . 73 LYS HA H 4.05 0.02 1 542 . 73 LYS HB2 H 1.98 0.02 1 543 . 73 LYS HB3 H 1.98 0.02 1 544 . 73 LYS C C 177.98 0.05 1 545 . 73 LYS CA C 59.80 0.20 1 546 . 73 LYS CB C 32.00 0.40 1 547 . 73 LYS N N 117.20 0.10 1 548 . 74 MET H H 7.14 0.01 1 549 . 74 MET HA H 3.51 0.02 1 550 . 74 MET HB2 H 1.92 0.02 2 551 . 74 MET HB3 H 1.26 0.02 2 552 . 74 MET C C 177.80 0.05 1 553 . 74 MET CA C 58.50 0.20 1 554 . 74 MET CB C 30.00 0.40 1 555 . 74 MET N N 118.40 0.10 1 556 . 75 ILE H H 8.83 0.01 1 557 . 75 ILE HA H 3.63 0.02 1 558 . 75 ILE HB H 2.09 0.02 1 559 . 75 ILE C C 177.25 0.05 1 560 . 75 ILE CA C 65.90 0.20 1 561 . 75 ILE CB C 38.60 0.40 1 562 . 75 ILE N N 121.50 0.10 1 563 . 76 GLU H H 7.98 0.01 1 564 . 76 GLU HA H 3.77 0.02 1 565 . 76 GLU HB2 H 2.21 0.02 2 566 . 76 GLU HB3 H 2.08 0.02 2 567 . 76 GLU C C 177.60 0.05 1 568 . 76 GLU CA C 58.90 0.20 1 569 . 76 GLU CB C 29.20 0.40 1 570 . 76 GLU N N 116.40 0.10 1 571 . 77 VAL H H 7.24 0.01 1 572 . 77 VAL HA H 3.94 0.02 1 573 . 77 VAL HB H 2.14 0.02 1 574 . 77 VAL C C 178.60 0.05 1 575 . 77 VAL CA C 65.50 0.20 1 576 . 77 VAL CB C 32.40 0.20 1 577 . 77 VAL N N 117.10 0.10 1 578 . 78 VAL H H 8.66 0.01 1 579 . 78 VAL HA H 3.33 0.02 1 580 . 78 VAL HB H 1.32 0.02 1 581 . 78 VAL C C 176.80 0.05 1 582 . 78 VAL CA C 66.50 0.20 1 583 . 78 VAL CB C 31.70 0.40 1 584 . 78 VAL N N 120.30 0.10 1 585 . 79 HIS H H 8.29 0.01 1 586 . 79 HIS HA H 4.59 0.02 1 587 . 79 HIS HB2 H 3.03 0.02 2 588 . 79 HIS HB3 H 3.40 0.02 2 589 . 79 HIS C C 172.80 0.05 1 590 . 79 HIS CA C 54.90 0.20 1 591 . 79 HIS CB C 27.10 0.40 1 592 . 79 HIS N N 114.80 0.10 1 593 . 80 ALA H H 6.54 0.01 1 594 . 80 ALA HA H 3.98 0.02 1 595 . 80 ALA HB H 1.53 0.02 1 596 . 80 ALA C C 178.60 0.05 1 597 . 80 ALA CA C 54.10 0.20 1 598 . 80 ALA CB C 19.00 0.40 1 599 . 80 ALA N N 119.90 0.10 1 600 . 81 GLY H H 8.91 0.01 1 601 . 81 GLY HA2 H 3.70 0.02 1 602 . 81 GLY HA3 H 4.34 0.02 1 603 . 81 GLY C C 174.00 0.05 1 604 . 81 GLY CA C 44.80 0.20 1 605 . 81 GLY N N 109.00 0.10 1 606 . 82 ASN H H 7.61 0.01 1 607 . 82 ASN HA H 5.00 0.02 1 608 . 82 ASN HB2 H 2.73 0.02 2 609 . 82 ASN HB3 H 3.14 0.02 2 610 . 82 ASN C C 174.00 0.05 1 611 . 82 ASN CA C 52.20 0.20 1 612 . 82 ASN CB C 39.40 0.40 1 613 . 82 ASN N N 118.70 0.10 1 614 . 83 ALA H H 8.74 0.01 1 615 . 83 ALA HA H 4.00 0.02 1 616 . 83 ALA HB H 1.46 0.02 1 617 . 83 ALA C C 180.00 0.05 1 618 . 83 ALA CA C 55.40 0.20 1 619 . 83 ALA CB C 18.90 0.40 1 620 . 83 ALA N N 127.00 0.10 1 621 . 84 ASP H H 8.26 0.01 1 622 . 84 ASP HA H 4.41 0.02 1 623 . 84 ASP HB2 H 2.71 0.02 2 624 . 84 ASP HB3 H 2.78 0.02 2 625 . 84 ASP C C 178.80 0.05 1 626 . 84 ASP CA C 57.10 0.20 1 627 . 84 ASP CB C 40.00 0.40 1 628 . 84 ASP N N 118.20 0.10 1 629 . 85 ASP H H 7.95 0.01 1 630 . 85 ASP HA H 4.33 0.02 1 631 . 85 ASP HB2 H 2.34 0.02 2 632 . 85 ASP HB3 H 2.87 0.02 2 633 . 85 ASP C C 177.50 0.05 1 634 . 85 ASP CA C 56.70 0.20 1 635 . 85 ASP CB C 39.40 0.40 1 636 . 85 ASP N N 122.20 0.10 1 637 . 86 ILE H H 8.00 0.01 1 638 . 86 ILE HA H 3.17 0.02 1 639 . 86 ILE HB H 1.81 0.02 1 640 . 86 ILE C C 177.00 0.05 1 641 . 86 ILE CA C 66.30 0.20 1 642 . 86 ILE CB C 37.80 0.40 1 643 . 86 ILE N N 119.10 0.10 1 644 . 87 GLN H H 7.57 0.01 1 645 . 87 GLN HA H 3.87 0.02 1 646 . 87 GLN HB2 H 2.15 0.02 1 647 . 87 GLN HB3 H 2.15 0.02 1 648 . 87 GLN C C 178.90 0.05 1 649 . 87 GLN CA C 58.90 0.20 1 650 . 87 GLN CB C 28.70 0.40 1 651 . 87 GLN N N 116.60 0.10 1 652 . 88 LEU H H 7.87 0.01 1 653 . 88 LEU HA H 4.04 0.02 1 654 . 88 LEU HB2 H 1.78 0.02 2 655 . 88 LEU HB3 H 1.89 0.02 2 656 . 88 LEU C C 179.80 0.05 1 657 . 88 LEU CA C 58.10 0.20 1 658 . 88 LEU CB C 42.40 0.40 1 659 . 88 LEU N N 121.80 0.10 1 660 . 89 VAL H H 8.68 0.01 1 661 . 89 VAL HA H 3.44 0.02 1 662 . 89 VAL HB H 1.73 0.02 1 663 . 89 VAL C C 178.30 0.05 1 664 . 89 VAL CA C 66.20 0.20 1 665 . 89 VAL CB C 30.80 0.40 1 666 . 89 VAL N N 120.20 0.10 1 667 . 90 LYS H H 8.49 0.01 1 668 . 90 LYS HA H 3.87 0.02 1 669 . 90 LYS HB2 H 1.76 0.02 2 670 . 90 LYS HB3 H 1.51 0.02 2 671 . 90 LYS C C 179.00 0.05 1 672 . 90 LYS CA C 61.60 0.20 1 673 . 90 LYS CB C 32.40 0.40 1 674 . 90 LYS N N 120.60 0.10 1 675 . 91 GLY H H 7.54 0.01 1 676 . 91 GLY HA2 H 3.98 0.02 1 677 . 91 GLY HA3 H 3.95 0.02 1 678 . 91 GLY C C 176.80 0.05 1 679 . 91 GLY CA C 47.40 0.20 1 680 . 91 GLY N N 105.30 0.10 1 681 . 92 ILE H H 7.60 0.01 1 682 . 92 ILE HA H 3.57 0.02 1 683 . 92 ILE HB H 1.83 0.02 1 684 . 92 ILE C C 177.30 0.05 1 685 . 92 ILE CA C 65.40 0.20 1 686 . 92 ILE CB C 38.00 0.40 1 687 . 92 ILE N N 124.70 0.10 1 688 . 93 ALA H H 8.76 0.01 1 689 . 93 ALA HA H 4.23 0.02 1 690 . 93 ALA HB H 1.75 0.02 1 691 . 93 ALA C C 181.00 0.05 1 692 . 93 ALA CA C 54.50 0.20 1 693 . 93 ALA CB C 18.90 0.40 1 694 . 93 ALA N N 121.00 0.10 1 695 . 94 ASN H H 7.99 0.01 1 696 . 94 ASN HA H 4.62 0.02 1 697 . 94 ASN HB2 H 2.97 0.02 2 698 . 94 ASN HB3 H 3.18 0.02 2 699 . 94 ASN C C 178.20 0.05 1 700 . 94 ASN CA C 56.20 0.20 1 701 . 94 ASN CB C 39.50 0.40 1 702 . 94 ASN N N 114.40 0.10 1 703 . 95 GLU H H 8.60 0.01 1 704 . 95 GLU HA H 4.10 0.02 1 705 . 95 GLU HB2 H 2.01 0.02 2 706 . 95 GLU HB3 H 2.22 0.02 2 707 . 95 GLU C C 180.10 0.05 1 708 . 95 GLU CA C 59.90 0.20 1 709 . 95 GLU CB C 29.50 0.40 1 710 . 95 GLU N N 122.40 0.10 1 711 . 96 CYS H H 8.55 0.01 1 712 . 96 CYS HA H 4.66 0.02 1 713 . 96 CYS HB2 H 2.45 0.02 2 714 . 96 CYS HB3 H 2.67 0.02 2 715 . 96 CYS C C 177.20 0.05 1 716 . 96 CYS CA C 56.20 0.20 1 717 . 96 CYS CB C 37.50 0.40 1 718 . 96 CYS N N 115.10 0.10 1 719 . 97 ILE H H 7.92 0.01 1 720 . 97 ILE HA H 3.89 0.02 1 721 . 97 ILE HB H 2.44 0.02 1 722 . 97 ILE C C 178.30 0.05 1 723 . 97 ILE CA C 65.50 0.20 1 724 . 97 ILE CB C 39.30 0.40 1 725 . 97 ILE N N 123.20 0.10 1 726 . 98 GLU H H 7.47 0.01 1 727 . 98 GLU HA H 4.05 0.02 1 728 . 98 GLU HB2 H 2.22 0.02 1 729 . 98 GLU HB3 H 2.22 0.02 1 730 . 98 GLU C C 178.70 0.05 1 731 . 98 GLU CA C 58.60 0.20 1 732 . 98 GLU CB C 29.30 0.40 1 733 . 98 GLU N N 117.60 0.10 1 734 . 99 ASN H H 7.68 0.01 1 735 . 99 ASN HA H 4.54 0.02 1 736 . 99 ASN HB2 H 2.82 0.02 2 737 . 99 ASN HB3 H 2.86 0.02 2 738 . 99 ASN C C 175.50 0.05 1 739 . 99 ASN CA C 55.20 0.20 1 740 . 99 ASN CB C 39.00 0.40 1 741 . 99 ASN N N 116.00 0.10 1 742 . 100 ALA H H 7.53 0.01 1 743 . 100 ALA HA H 4.39 0.02 1 744 . 100 ALA HB H 1.54 0.02 1 745 . 100 ALA C C 176.40 0.05 1 746 . 100 ALA CA C 51.90 0.20 1 747 . 100 ALA CB C 19.90 0.40 1 748 . 100 ALA N N 119.20 0.10 1 749 . 101 LYS H H 7.32 0.01 1 750 . 101 LYS HA H 4.16 0.02 1 751 . 101 LYS HB2 H 1.96 0.02 2 752 . 101 LYS HB3 H 1.91 0.02 2 753 . 101 LYS C C 177.30 0.05 1 754 . 101 LYS CA C 58.20 0.20 1 755 . 101 LYS CB C 32.40 0.40 1 756 . 101 LYS N N 118.60 0.10 1 757 . 102 GLY H H 8.70 0.01 1 758 . 102 GLY HA2 H 4.18 0.02 1 759 . 102 GLY HA3 H 3.78 0.02 1 760 . 102 GLY C C 174.40 0.05 1 761 . 102 GLY CA C 45.00 0.20 1 762 . 102 GLY N N 111.20 0.10 1 763 . 103 GLU H H 7.50 0.01 1 764 . 103 GLU HA H 4.43 0.02 1 765 . 103 GLU HB2 H 2.00 0.02 2 766 . 103 GLU HB3 H 2.10 0.02 2 767 . 103 GLU C C 176.20 0.05 1 768 . 103 GLU CA C 55.40 0.20 1 769 . 103 GLU CB C 30.80 0.40 1 770 . 103 GLU N N 119.90 0.10 1 771 . 104 THR H H 8.23 0.01 1 772 . 104 THR HA H 4.45 0.02 1 773 . 104 THR HB H 4.38 0.02 1 774 . 104 THR C C 174.00 0.05 1 775 . 104 THR CA C 61.60 0.20 1 776 . 104 THR CB C 70.00 0.40 1 777 . 104 THR N N 112.00 0.10 1 778 . 105 ASP H H 8.42 0.01 1 779 . 105 ASP HA H 4.84 0.02 1 780 . 105 ASP HB2 H 2.61 0.02 2 781 . 105 ASP HB3 H 2.93 0.02 2 782 . 105 ASP C C 177.20 0.05 1 783 . 105 ASP CA C 53.00 0.20 1 784 . 105 ASP CB C 43.00 0.40 1 785 . 105 ASP N N 123.60 0.10 1 786 . 106 GLU H H 9.18 0.01 1 787 . 106 GLU HA H 3.87 0.02 1 788 . 106 GLU HB2 H 2.01 0.02 2 789 . 106 GLU HB3 H 2.20 0.02 2 790 . 106 GLU C C 177.11 0.05 1 791 . 106 GLU CA C 59.00 0.20 1 792 . 106 GLU CB C 29.70 0.40 1 793 . 106 GLU N N 126.10 0.10 1 794 . 107 CYS H H 8.36 0.01 1 795 . 107 CYS HA H 4.22 0.02 1 796 . 107 CYS HB2 H 2.81 0.02 2 797 . 107 CYS HB3 H 3.78 0.02 2 798 . 107 CYS C C 175.86 0.05 1 799 . 107 CYS CA C 60.10 0.20 1 800 . 107 CYS CB C 30.00 0.40 1 801 . 107 CYS N N 117.90 0.10 1 802 . 108 ASN H H 7.82 0.01 1 803 . 108 ASN HA H 4.67 0.02 1 804 . 108 ASN HB2 H 2.81 0.02 2 805 . 108 ASN HB3 H 3.07 0.02 2 806 . 108 ASN C C 178.42 0.05 1 807 . 108 ASN CA C 55.20 0.20 1 808 . 108 ASN CB C 37.70 0.40 1 809 . 108 ASN N N 118.70 0.10 1 810 . 109 ILE H H 8.20 0.01 1 811 . 109 ILE HA H 3.44 0.02 1 812 . 109 ILE HB H 1.99 0.02 1 813 . 109 ILE C C 177.40 0.05 1 814 . 109 ILE CA C 67.10 0.20 1 815 . 109 ILE CB C 37.50 0.40 1 816 . 109 ILE N N 122.00 0.10 1 817 . 110 GLY H H 8.11 0.01 1 818 . 110 GLY HA2 H 3.88 0.02 1 819 . 110 GLY HA3 H 3.83 0.02 1 820 . 110 GLY C C 175.92 0.05 1 821 . 110 GLY CA C 47.50 0.20 1 822 . 110 GLY N N 104.80 0.10 1 823 . 111 ASN H H 7.52 0.01 1 824 . 111 ASN HA H 4.47 0.02 1 825 . 111 ASN HB2 H 2.85 0.02 1 826 . 111 ASN HB3 H 2.85 0.02 1 827 . 111 ASN C C 176.16 0.05 1 828 . 111 ASN CA C 55.90 0.20 1 829 . 111 ASN CB C 38.50 0.40 1 830 . 111 ASN N N 119.50 0.10 1 831 . 112 LYS H H 8.79 0.01 1 832 . 112 LYS HA H 4.07 0.02 1 833 . 112 LYS HB2 H 1.92 0.02 2 834 . 112 LYS HB3 H 1.76 0.02 2 835 . 112 LYS C C 180.18 0.05 1 836 . 112 LYS CA C 59.40 0.20 1 837 . 112 LYS CB C 33.00 0.40 1 838 . 112 LYS N N 119.20 0.10 1 839 . 113 TYR H H 8.85 0.01 1 840 . 113 TYR HA H 3.95 0.02 1 841 . 113 TYR HB2 H 2.79 0.02 2 842 . 113 TYR HB3 H 2.86 0.02 2 843 . 113 TYR C C 176.70 0.05 1 844 . 113 TYR CA C 63.20 0.20 1 845 . 113 TYR CB C 39.50 0.40 1 846 . 113 TYR N N 118.00 0.10 1 847 . 114 THR H H 7.44 0.01 1 848 . 114 THR HA H 3.67 0.02 1 849 . 114 THR HB H 4.35 0.02 1 850 . 114 THR C C 175.62 0.05 1 851 . 114 THR CA C 66.90 0.20 1 852 . 114 THR CB C 68.80 0.40 1 853 . 114 THR N N 111.50 0.10 1 854 . 115 ASP H H 8.54 0.01 1 855 . 115 ASP HA H 4.32 0.02 1 856 . 115 ASP HB2 H 2.56 0.02 2 857 . 115 ASP HB3 H 2.71 0.02 2 858 . 115 ASP C C 178.16 0.05 1 859 . 115 ASP CA C 57.30 0.20 1 860 . 115 ASP CB C 39.50 0.40 1 861 . 115 ASP N N 120.90 0.10 1 862 . 116 CYS H H 7.00 0.01 1 863 . 116 CYS HA H 4.14 0.02 1 864 . 116 CYS HB2 H 3.05 0.02 2 865 . 116 CYS HB3 H 3.27 0.02 2 866 . 116 CYS C C 173.95 0.05 1 867 . 116 CYS CA C 59.30 0.20 1 868 . 116 CYS CB C 36.50 0.40 1 869 . 116 CYS N N 118.40 0.10 1 870 . 117 TYR H H 7.95 0.01 1 871 . 117 TYR HA H 3.52 0.02 1 872 . 117 TYR HB2 H 2.34 0.02 2 873 . 117 TYR HB3 H 3.05 0.02 2 874 . 117 TYR C C 177.35 0.05 1 875 . 117 TYR CA C 61.00 0.20 1 876 . 117 TYR CB C 40.30 0.40 1 877 . 117 TYR N N 123.50 0.10 1 878 . 118 ILE H H 8.44 0.01 1 879 . 118 ILE HA H 3.78 0.02 1 880 . 118 ILE HB H 2.01 0.02 1 881 . 118 ILE C C 178.06 0.05 1 882 . 118 ILE CA C 63.90 0.20 1 883 . 118 ILE CB C 38.50 0.40 1 884 . 118 ILE N N 115.00 0.10 1 885 . 119 GLU H H 7.86 0.01 1 886 . 119 GLU HA H 4.00 0.02 1 887 . 119 GLU HB2 H 2.08 0.02 2 888 . 119 GLU HB3 H 2.14 0.02 2 889 . 119 GLU C C 179.45 0.05 1 890 . 119 GLU CA C 59.20 0.20 1 891 . 119 GLU CB C 29.40 0.40 1 892 . 119 GLU N N 119.50 0.10 1 893 . 120 LYS H H 7.80 0.01 1 894 . 120 LYS HA H 4.01 0.02 1 895 . 120 LYS HB2 H 1.76 0.02 2 896 . 120 LYS HB3 H 1.58 0.02 2 897 . 120 LYS C C 178.77 0.05 1 898 . 120 LYS CA C 58.60 0.20 1 899 . 120 LYS CB C 33.30 0.40 1 900 . 120 LYS N N 116.10 0.10 1 901 . 121 LEU H H 8.14 0.01 1 902 . 121 LEU HA H 3.78 0.02 1 903 . 121 LEU HB2 H 1.14 0.02 2 904 . 121 LEU HB3 H 1.34 0.02 2 905 . 121 LEU C C 177.53 0.05 1 906 . 121 LEU CA C 57.30 0.20 1 907 . 121 LEU CB C 42.60 0.40 1 908 . 121 LEU N N 120.50 0.10 1 909 . 122 PHE H H 7.43 0.01 1 910 . 122 PHE HA H 4.90 0.02 1 911 . 122 PHE HB2 H 2.95 0.02 2 912 . 122 PHE HB3 H 3.50 0.02 2 913 . 122 PHE C C 175.40 0.05 1 914 . 122 PHE CA C 56.20 0.20 1 915 . 122 PHE CB C 38.60 0.40 1 916 . 122 PHE N N 113.50 0.10 1 917 . 123 SER H H 7.35 0.01 1 918 . 123 SER HA H 4.36 0.02 1 919 . 123 SER HB2 H 3.97 0.02 1 920 . 123 SER HB3 H 3.97 0.02 1 921 . 123 SER C C 178.76 0.05 1 922 . 123 SER CA C 60.50 0.20 1 923 . 123 SER CB C 64.80 0.40 1 924 . 123 SER N N 120.90 0.10 1 stop_ save_