data_4455 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Glycan-free mutant adhesion domain of human CD58 (LFA-3) ; _BMRB_accession_number 4455 _BMRB_flat_file_name bmr4455.str _Entry_type original _Submission_date 1999-11-11 _Accession_date 1999-11-11 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sun 'Z. Y.' J. . 2 Dotsch V. . . 3 Kim M. . . 4 Li J. . . 5 Reinherz E. L. . 6 Wagner G. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 517 "13C chemical shifts" 375 "15N chemical shifts" 97 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-12-22 original BMRB . stop_ _Original_release_date 1999-11-11 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Functional Glycan-free Adhesion Domain of Human Cell Surface Receptor CD58: Design, Production, and NMR Studies ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99286218 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sun 'Z. Y.' J. . 2 Dotsch V. . . 3 Kim M. . . 4 Li J. . . 5 Reinherz E. L. . 6 Wagner G. . . stop_ _Journal_abbreviation 'EMBO J.' _Journal_name_full 'EMBO Journal' _Journal_volume 18 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2941 _Page_last 2949 _Year 1999 _Details . loop_ _Keyword 'adhesion glycoprotein' 'cell surface receptor' 'immunoglobulin superfamily V-set domain' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Sun ZY, Dotsch V, Kim M, Li J, Reinherz EL, Wagner G Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studies. EMBO J. 1999 Jun 1;18(11):2941-9. ; _Citation_title ; Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studies. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10357807 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sun 'Z. Y.' Y. . 2 Dotsch V. . . 3 Kim M. . . 4 Li J. . . 5 Reinherz 'E. L.' L. . 6 Wagner G. . . stop_ _Journal_abbreviation 'EMBO J.' _Journal_name_full 'The EMBO journal' _Journal_volume 18 _Journal_issue 11 _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 2941 _Page_last 2949 _Year 1999 _Details ; A general strategy is presented here for producing glycan-free forms of glycoproteins without loss of function by employing apolar-to-polar mutations of surface residues in functionally irrelevant epitopes. The success of this structure-based approach was demonstrated through the expression in Escherichia coli of a soluble 11 kDa adhesion domain extracted from the heavily glycosylated 55 kDa human CD58 ectodomain. The solution structure was subsequently determined and binding to its counter-receptor CD2 studied by NMR. This mutant adhesion domain is functional as determined by several experimental methods, and the size of its binding site has been probed by chemical shift perturbations in NMR titration experiments. The new structural information supports a 'hand-shake' model of CD2-CD58 interaction involving the GFCC'C" faces of both CD2 and CD58 adhesion domains. The region responsible for binding specificity is most likely localized on the C, C' and C" strands and the C-C' and C'-C" loops on CD58. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995). ; _Citation_title . _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart D. . . stop_ _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _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 . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_1dCD58 _Saveframe_category molecular_system _Mol_system_name 'CD58 adhesion domain, 1dCD58' _Abbreviation_common 1dCD58 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 1dCD58 $1dCD58 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details ; Biological_function: CD58 adhesion domain responsible for binding to counter receptor CD2 on T-cell surface. ; save_ ######################## # Monomeric polymers # ######################## save_1dCD58 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 1dCD58 _Name_variant F1S/V9K/V21Q/V58K/T85S/L93G _Abbreviation_common 1dCD58 _Molecular_mass 11200 _Mol_thiol_state 'not present' _Details 'CD58 in human is heavily glycosylated' ############################## # Polymer residue sequence # ############################## _Residue_count 95 _Mol_residue_sequence ; SSQQIYGVKYGNVTFHVPSN QPLKEVLWKKQKDKVAELEN SEFRAFSSFKNRVYLDTKSG SLTIYNLTSSDEDEYEMESP NITDSMKFFLYVGES ; loop_ _Residue_seq_code _Residue_label 1 SER 2 SER 3 GLN 4 GLN 5 ILE 6 TYR 7 GLY 8 VAL 9 LYS 10 TYR 11 GLY 12 ASN 13 VAL 14 THR 15 PHE 16 HIS 17 VAL 18 PRO 19 SER 20 ASN 21 GLN 22 PRO 23 LEU 24 LYS 25 GLU 26 VAL 27 LEU 28 TRP 29 LYS 30 LYS 31 GLN 32 LYS 33 ASP 34 LYS 35 VAL 36 ALA 37 GLU 38 LEU 39 GLU 40 ASN 41 SER 42 GLU 43 PHE 44 ARG 45 ALA 46 PHE 47 SER 48 SER 49 PHE 50 LYS 51 ASN 52 ARG 53 VAL 54 TYR 55 LEU 56 ASP 57 THR 58 LYS 59 SER 60 GLY 61 SER 62 LEU 63 THR 64 ILE 65 TYR 66 ASN 67 LEU 68 THR 69 SER 70 SER 71 ASP 72 GLU 73 ASP 74 GLU 75 TYR 76 GLU 77 MET 78 GLU 79 SER 80 PRO 81 ASN 82 ILE 83 THR 84 ASP 85 SER 86 MET 87 LYS 88 PHE 89 PHE 90 LEU 91 TYR 92 VAL 93 GLY 94 GLU 95 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 1CI5 'Glycan-Free Mutant Adhesion Domain Of Human Cd58 (Lfa-3)' 100.00 95 100.00 100.00 1.63e-48 PDB 1QA9 'Structure Of A Heterophilic Adhesion Complex Between The Human Cd2 And Cd58(Lfa-3) Counter-Receptors' 100.00 95 100.00 100.00 1.63e-48 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Plasmid _Gene_mnemonic $1dCD58 Human 9606 Eukaryota Metazoa Homo sapiens pET11a-1dCD58x6 1dCD58x6 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 $1dCD58 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET11a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $1dCD58 . mM 0.2 0.6 '[U-13C; U-15N]' NaPO4 10 mM . . . D2O 10 % . . . stop_ save_ ############################ # Computer software used # ############################ save_XEASY _Saveframe_category software _Name XEASY _Version . _Details . save_ save_DIANA _Saveframe_category software _Name DIANA _Version . _Details . save_ save_DYANA _Saveframe_category software _Name DYANA _Version . _Details . save_ save_XPLOR _Saveframe_category software _Name XPLOR _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityInova _Field_strength 500 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityInova _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_1 save_ save_NOESY-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY-HSQC _Sample_label $sample_1 save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_HBHA(CBCACO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CBCACO)NH _Sample_label $sample_1 save_ save_HCCH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_1 save_ save_HNHA_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label $sample_1 save_ save_HNHB_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _Sample_label $sample_1 save_ save_HNCO_9 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HN(CA)CO_10 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.01 . M pH 7.5 0.1 n/a pressure 1 . atm temperature 298 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 DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 1dCD58 _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 SER HA H 4.78 . 1 2 . 2 SER HB2 H 3.73 . 2 3 . 2 SER HB3 H 3.67 . 2 4 . 2 SER C C 173.92 . 1 5 . 2 SER CA C 57.39 . 1 6 . 2 SER CB C 64.36 . 1 7 . 3 GLN H H 8.13 . 1 8 . 3 GLN HA H 4.59 . 1 9 . 3 GLN HB2 H 2.12 . 2 10 . 3 GLN HB3 H 1.88 . 2 11 . 3 GLN HG2 H 2.30 . 2 12 . 3 GLN HE21 H 7.53 . 2 13 . 3 GLN HE22 H 7.00 . 2 14 . 3 GLN C C 174.95 . 1 15 . 3 GLN CA C 55.23 . 1 16 . 3 GLN CB C 31.26 . 1 17 . 3 GLN CG C 34.10 . 1 18 . 3 GLN N N 122.48 . 1 19 . 3 GLN NE2 N 112.12 . 1 20 . 4 GLN H H 8.84 . 1 21 . 4 GLN HA H 5.18 . 1 22 . 4 GLN HB2 H 2.37 . 2 23 . 4 GLN HB3 H 2.14 . 2 24 . 4 GLN HG2 H 2.59 . 2 25 . 4 GLN HG3 H 2.54 . 2 26 . 4 GLN HE21 H 7.42 . 2 27 . 4 GLN HE22 H 6.89 . 2 28 . 4 GLN C C 174.56 . 1 29 . 4 GLN CA C 55.80 . 1 30 . 4 GLN CB C 30.37 . 1 31 . 4 GLN CG C 34.62 . 1 32 . 4 GLN N N 123.37 . 1 33 . 4 GLN NE2 N 112.42 . 1 34 . 5 ILE H H 9.44 . 1 35 . 5 ILE HA H 4.61 . 1 36 . 5 ILE HB H 2.00 . 1 37 . 5 ILE HG12 H 1.65 . 2 38 . 5 ILE HG13 H 1.55 . 2 39 . 5 ILE HG2 H 0.96 . 1 40 . 5 ILE HD1 H 1.01 . 1 41 . 5 ILE C C 172.92 . 1 42 . 5 ILE CA C 58.92 . 1 43 . 5 ILE CB C 39.86 . 1 44 . 5 ILE CG1 C 27.46 . 1 45 . 5 ILE CG2 C 18.00 . 1 46 . 5 ILE CD1 C 11.84 . 1 47 . 5 ILE N N 125.53 . 1 48 . 6 TYR H H 8.67 . 1 49 . 6 TYR HA H 5.13 . 1 50 . 6 TYR HB2 H 3.11 . 2 51 . 6 TYR HB3 H 2.88 . 2 52 . 6 TYR HD1 H 7.21 . 3 53 . 6 TYR HE1 H 6.55 . 3 54 . 6 TYR C C 175.70 . 1 55 . 6 TYR CA C 57.72 . 1 56 . 6 TYR CB C 39.02 . 1 57 . 6 TYR N N 125.09 . 1 58 . 7 GLY H H 9.14 . 1 59 . 7 GLY HA2 H 4.66 . 1 60 . 7 GLY HA3 H 3.20 . 1 61 . 7 GLY C C 172.02 . 1 62 . 7 GLY CA C 43.16 . 1 63 . 7 GLY N N 111.96 . 1 64 . 8 VAL H H 8.28 . 1 65 . 8 VAL HA H 4.57 . 1 66 . 8 VAL HB H 1.86 . 1 67 . 8 VAL HG1 H 0.87 . 2 68 . 8 VAL HG2 H 0.82 . 2 69 . 8 VAL C C 174.52 . 1 70 . 8 VAL CA C 59.60 . 1 71 . 8 VAL CB C 35.23 . 1 72 . 8 VAL CG1 C 21.43 . 1 73 . 8 VAL CG2 C 20.18 . 1 74 . 8 VAL N N 117.29 . 1 75 . 9 LYS H H 8.19 . 1 76 . 9 LYS HA H 3.25 . 1 77 . 9 LYS HB2 H 1.37 . 2 78 . 9 LYS HB3 H 1.30 . 2 79 . 9 LYS HG2 H 1.49 . 2 80 . 9 LYS HD2 H 0.98 . 2 81 . 9 LYS HD3 H 0.35 . 2 82 . 9 LYS HE2 H 2.77 . 2 83 . 9 LYS C C 176.60 . 1 84 . 9 LYS CA C 58.35 . 1 85 . 9 LYS CB C 32.32 . 1 86 . 9 LYS CG C 29.57 . 1 87 . 9 LYS CD C 24.96 . 1 88 . 9 LYS CE C 41.52 . 1 89 . 9 LYS N N 124.77 . 1 90 . 10 TYR H H 9.60 . 1 91 . 10 TYR HA H 4.41 . 1 92 . 10 TYR HB2 H 3.35 . 2 93 . 10 TYR HD1 H 7.15 . 3 94 . 10 TYR HE1 H 6.83 . 3 95 . 10 TYR C C 176.05 . 1 96 . 10 TYR CA C 59.57 . 1 97 . 10 TYR CB C 35.95 . 1 98 . 10 TYR N N 119.31 . 1 99 . 11 GLY H H 8.89 . 1 100 . 11 GLY HA2 H 4.47 . 1 101 . 11 GLY HA3 H 3.81 . 1 102 . 11 GLY C C 171.09 . 1 103 . 11 GLY CA C 44.01 . 1 104 . 11 GLY N N 111.17 . 1 105 . 12 ASN H H 8.19 . 1 106 . 12 ASN HA H 5.72 . 1 107 . 12 ASN HB2 H 2.41 . 2 108 . 12 ASN HB3 H 2.23 . 2 109 . 12 ASN HD21 H 7.46 . 2 110 . 12 ASN HD22 H 7.00 . 2 111 . 12 ASN C C 175.13 . 1 112 . 12 ASN CA C 50.75 . 1 113 . 12 ASN CB C 42.37 . 1 114 . 12 ASN N N 112.75 . 1 115 . 12 ASN ND2 N 113.52 . 1 116 . 13 VAL H H 8.35 . 1 117 . 13 VAL HA H 4.44 . 1 118 . 13 VAL HB H 1.74 . 1 119 . 13 VAL HG1 H 0.55 . 2 120 . 13 VAL HG2 H 0.54 . 2 121 . 13 VAL C C 171.71 . 1 122 . 13 VAL CA C 60.20 . 1 123 . 13 VAL CB C 35.65 . 1 124 . 13 VAL CG1 C 21.21 . 1 125 . 13 VAL CG2 C 20.55 . 1 126 . 13 VAL N N 116.49 . 1 127 . 14 THR H H 7.86 . 1 128 . 14 THR HA H 4.80 . 1 129 . 14 THR HB H 3.33 . 1 130 . 14 THR HG2 H 0.38 . 1 131 . 14 THR C C 172.17 . 1 132 . 14 THR CA C 60.80 . 1 133 . 14 THR CB C 71.63 . 1 134 . 14 THR CG2 C 19.96 . 1 135 . 14 THR N N 118.54 . 1 136 . 15 PHE H H 8.80 . 1 137 . 15 PHE HA H 4.35 . 1 138 . 15 PHE HB2 H 2.29 . 2 139 . 15 PHE HB3 H 1.33 . 2 140 . 15 PHE HD1 H 6.20 . 3 141 . 15 PHE HE1 H 6.26 . 3 142 . 15 PHE HZ H 5.99 . 1 143 . 15 PHE C C 173.53 . 1 144 . 15 PHE CA C 52.72 . 1 145 . 15 PHE CB C 37.50 . 1 146 . 15 PHE N N 126.78 . 1 147 . 16 HIS H H 8.50 . 1 148 . 16 HIS HA H 4.44 . 1 149 . 16 HIS HB2 H 3.04 . 2 150 . 16 HIS HB3 H 2.98 . 2 151 . 16 HIS HD2 H 7.03 . 1 152 . 16 HIS HE1 H 7.73 . 1 153 . 16 HIS C C 175.02 . 1 154 . 16 HIS CA C 57.06 . 1 155 . 16 HIS CB C 31.01 . 1 156 . 16 HIS N N 122.43 . 1 157 . 17 VAL H H 8.53 . 1 158 . 17 VAL HA H 4.57 . 1 159 . 17 VAL HB H 2.14 . 1 160 . 17 VAL HG1 H 1.11 . 2 161 . 17 VAL HG2 H 1.19 . 2 162 . 17 VAL C C 174.88 . 1 163 . 17 VAL CA C 59.02 . 1 164 . 17 VAL CB C 33.65 . 1 165 . 17 VAL CG1 C 21.52 . 1 166 . 17 VAL CG2 C 21.52 . 1 167 . 17 VAL N N 125.38 . 1 168 . 18 PRO HA H 4.57 . 1 169 . 18 PRO HB2 H 2.21 . 2 170 . 18 PRO HG2 H 2.10 . 2 171 . 18 PRO HD2 H 3.92 . 2 172 . 18 PRO HD3 H 3.75 . 2 173 . 18 PRO C C 176.44 . 1 174 . 18 PRO CA C 62.62 . 1 175 . 18 PRO CB C 31.05 . 1 176 . 18 PRO CG C 27.47 . 1 177 . 18 PRO CD C 51.19 . 1 178 . 19 SER H H 8.25 . 1 179 . 19 SER HA H 4.47 . 1 180 . 19 SER HB2 H 3.87 . 2 181 . 19 SER C C 174.97 . 1 182 . 19 SER CA C 58.34 . 1 183 . 19 SER CB C 63.95 . 1 184 . 19 SER N N 115.94 . 1 185 . 20 ASN H H 8.77 . 1 186 . 20 ASN HA H 4.75 . 1 187 . 20 ASN HB2 H 2.87 . 2 188 . 20 ASN HD21 H 7.64 . 2 189 . 20 ASN HD22 H 6.94 . 2 190 . 20 ASN C C 174.35 . 1 191 . 20 ASN CA C 53.74 . 1 192 . 20 ASN CB C 38.87 . 1 193 . 20 ASN N N 121.53 . 1 194 . 20 ASN ND2 N 112.17 . 1 195 . 21 GLN H H 7.96 . 1 196 . 21 GLN HA H 4.78 . 1 197 . 21 GLN HB2 H 2.12 . 2 198 . 21 GLN HB3 H 1.91 . 2 199 . 21 GLN HG2 H 2.31 . 2 200 . 21 GLN HE21 H 7.49 . 2 201 . 21 GLN HE22 H 6.89 . 2 202 . 21 GLN C C 172.85 . 1 203 . 21 GLN CA C 53.48 . 1 204 . 21 GLN CB C 29.81 . 1 205 . 21 GLN CG C 33.23 . 1 206 . 21 GLN N N 118.67 . 1 207 . 21 GLN NE2 N 111.78 . 1 208 . 22 PRO HA H 4.43 . 1 209 . 22 PRO HB2 H 2.29 . 2 210 . 22 PRO HB3 H 1.83 . 2 211 . 22 PRO HG2 H 2.11 . 2 212 . 22 PRO HG3 H 1.97 . 2 213 . 22 PRO HD2 H 3.80 . 2 214 . 22 PRO HD3 H 3.63 . 2 215 . 22 PRO C C 176.55 . 1 216 . 22 PRO CA C 63.20 . 1 217 . 22 PRO CB C 31.79 . 1 218 . 22 PRO CG C 27.75 . 1 219 . 22 PRO CD C 50.58 . 1 220 . 23 LEU H H 8.37 . 1 221 . 23 LEU HA H 4.36 . 1 222 . 23 LEU HB2 H 1.53 . 2 223 . 23 LEU HB3 H 1.29 . 2 224 . 23 LEU HG H 1.69 . 1 225 . 23 LEU HD1 H 0.81 . 2 226 . 23 LEU HD2 H 0.77 . 2 227 . 23 LEU C C 176.63 . 1 228 . 23 LEU CA C 54.55 . 1 229 . 23 LEU CB C 42.84 . 1 230 . 23 LEU CG C 26.83 . 1 231 . 23 LEU CD1 C 26.14 . 1 232 . 23 LEU CD2 C 23.93 . 1 233 . 23 LEU N N 123.54 . 1 234 . 24 LYS H H 8.37 . 1 235 . 24 LYS HA H 4.29 . 1 236 . 24 LYS HB2 H 1.92 . 2 237 . 24 LYS HG2 H 1.73 . 2 238 . 24 LYS HD2 H 1.42 . 2 239 . 24 LYS HE2 H 2.99 . 2 240 . 24 LYS C C 175.97 . 1 241 . 24 LYS CA C 57.27 . 1 242 . 24 LYS CB C 33.70 . 1 243 . 24 LYS CG C 29.17 . 1 244 . 24 LYS CD C 25.14 . 1 245 . 24 LYS CE C 42.23 . 1 246 . 24 LYS N N 120.01 . 1 247 . 25 GLU H H 7.80 . 1 248 . 25 GLU HA H 4.96 . 1 249 . 25 GLU HB2 H 2.08 . 2 250 . 25 GLU HB3 H 1.95 . 2 251 . 25 GLU HG2 H 2.30 . 2 252 . 25 GLU C C 174.64 . 1 253 . 25 GLU CA C 55.22 . 1 254 . 25 GLU CB C 32.51 . 1 255 . 25 GLU CG C 36.59 . 1 256 . 25 GLU N N 118.23 . 1 257 . 26 VAL H H 8.53 . 1 258 . 26 VAL HA H 4.68 . 1 259 . 26 VAL HB H 2.12 . 1 260 . 26 VAL HG1 H 1.01 . 2 261 . 26 VAL HG2 H 0.94 . 2 262 . 26 VAL C C 172.17 . 1 263 . 26 VAL CA C 61.02 . 1 264 . 26 VAL CB C 35.88 . 1 265 . 26 VAL CG1 C 22.11 . 1 266 . 26 VAL CG2 C 23.08 . 1 267 . 26 VAL N N 120.39 . 1 268 . 27 LEU H H 8.80 . 1 269 . 27 LEU HA H 5.15 . 1 270 . 27 LEU HB2 H 1.77 . 2 271 . 27 LEU HB3 H 1.68 . 2 272 . 27 LEU HG H 1.44 . 1 273 . 27 LEU HD1 H 1.02 . 2 274 . 27 LEU HD2 H 0.88 . 2 275 . 27 LEU C C 174.05 . 1 276 . 27 LEU CA C 54.58 . 1 277 . 27 LEU CB C 45.24 . 1 278 . 27 LEU CG C 28.05 . 1 279 . 27 LEU CD1 C 23.64 . 1 280 . 27 LEU CD2 C 26.12 . 1 281 . 27 LEU N N 127.12 . 1 282 . 28 TRP H H 9.16 . 1 283 . 28 TRP HA H 5.49 . 1 284 . 28 TRP HB2 H 3.04 . 2 285 . 28 TRP HB3 H 2.91 . 2 286 . 28 TRP HD1 H 6.73 . 1 287 . 28 TRP HE1 H 10.16 . 1 288 . 28 TRP HE3 H 7.28 . 1 289 . 28 TRP HZ2 H 7.47 . 1 290 . 28 TRP HZ3 H 6.48 . 1 291 . 28 TRP HH2 H 6.67 . 1 292 . 28 TRP C C 175.89 . 1 293 . 28 TRP CA C 56.33 . 1 294 . 28 TRP CB C 32.20 . 1 295 . 28 TRP N N 124.08 . 1 296 . 28 TRP NE1 N 127.59 . 1 297 . 29 LYS H H 9.64 . 1 298 . 29 LYS HA H 5.07 . 1 299 . 29 LYS HB2 H 1.65 . 2 300 . 29 LYS HB3 H 1.59 . 2 301 . 29 LYS HG2 H 1.49 . 2 302 . 29 LYS HD2 H 1.28 . 2 303 . 29 LYS HD3 H 1.09 . 2 304 . 29 LYS HE2 H 2.68 . 2 305 . 29 LYS C C 173.77 . 1 306 . 29 LYS CA C 54.73 . 1 307 . 29 LYS CB C 37.19 . 1 308 . 29 LYS CG C 29.33 . 1 309 . 29 LYS CD C 24.96 . 1 310 . 29 LYS CE C 41.49 . 1 311 . 29 LYS N N 122.31 . 1 312 . 30 LYS H H 8.69 . 1 313 . 30 LYS HA H 4.26 . 1 314 . 30 LYS HB2 H 1.44 . 2 315 . 30 LYS HB3 H 1.11 . 2 316 . 30 LYS HG2 H 0.93 . 2 317 . 30 LYS HG3 H 0.24 . 2 318 . 30 LYS HD2 H 1.89 . 2 319 . 30 LYS HD3 H 1.74 . 2 320 . 30 LYS HE2 H 3.38 . 2 321 . 30 LYS HE3 H 2.94 . 2 322 . 30 LYS C C 176.38 . 1 323 . 30 LYS CA C 54.70 . 1 324 . 30 LYS CB C 35.37 . 1 325 . 30 LYS CG C 24.33 . 1 326 . 30 LYS CD C 30.58 . 1 327 . 30 LYS CE C 42.77 . 1 328 . 30 LYS N N 122.73 . 1 329 . 31 GLN H H 8.76 . 1 330 . 31 GLN HA H 3.67 . 1 331 . 31 GLN HB2 H 2.35 . 2 332 . 31 GLN HB3 H 2.25 . 2 333 . 31 GLN HG2 H 2.63 . 2 334 . 31 GLN HG3 H 2.38 . 2 335 . 31 GLN HE21 H 8.78 . 2 336 . 31 GLN HE22 H 6.90 . 2 337 . 31 GLN C C 175.25 . 1 338 . 31 GLN CA C 58.93 . 1 339 . 31 GLN CB C 26.61 . 1 340 . 31 GLN CG C 34.06 . 1 341 . 31 GLN N N 125.09 . 1 342 . 31 GLN NE2 N 114.15 . 1 343 . 32 LYS H H 8.33 . 1 344 . 32 LYS HA H 4.20 . 1 345 . 32 LYS HB2 H 1.98 . 2 346 . 32 LYS HB3 H 1.86 . 2 347 . 32 LYS HG2 H 1.64 . 2 348 . 32 LYS HD2 H 1.46 . 2 349 . 32 LYS HD3 H 1.37 . 2 350 . 32 LYS HE2 H 2.96 . 2 351 . 32 LYS C C 176.19 . 1 352 . 32 LYS CA C 56.48 . 1 353 . 32 LYS CB C 32.17 . 1 354 . 32 LYS CG C 28.79 . 1 355 . 32 LYS CD C 25.14 . 1 356 . 32 LYS CE C 42.23 . 1 357 . 32 LYS N N 118.23 . 1 358 . 33 ASP H H 8.06 . 1 359 . 33 ASP HA H 4.79 . 1 360 . 33 ASP HB2 H 2.71 . 2 361 . 33 ASP C C 175.39 . 1 362 . 33 ASP CA C 53.38 . 1 363 . 33 ASP CB C 42.72 . 1 364 . 33 ASP N N 120.29 . 1 365 . 34 LYS H H 8.38 . 1 366 . 34 LYS HA H 4.04 . 1 367 . 34 LYS HB2 H 1.03 . 2 368 . 34 LYS HG2 H 1.15 . 2 369 . 34 LYS HG3 H 1.05 . 2 370 . 34 LYS HD2 H 1.44 . 2 371 . 34 LYS HD3 H 0.96 . 2 372 . 34 LYS HE2 H 2.51 . 2 373 . 34 LYS HE3 H 2.37 . 2 374 . 34 LYS C C 175.90 . 1 375 . 34 LYS CA C 58.61 . 1 376 . 34 LYS CB C 33.50 . 1 377 . 34 LYS CG C 29.64 . 1 378 . 34 LYS CD C 25.85 . 1 379 . 34 LYS CE C 41.49 . 1 380 . 34 LYS N N 120.83 . 1 381 . 35 VAL H H 9.12 . 1 382 . 35 VAL HA H 4.13 . 1 383 . 35 VAL HB H 1.64 . 1 384 . 35 VAL HG1 H 0.27 . 2 385 . 35 VAL HG2 H 0.56 . 2 386 . 35 VAL C C 175.18 . 1 387 . 35 VAL CA C 63.29 . 1 388 . 35 VAL CB C 33.47 . 1 389 . 35 VAL CG1 C 20.24 . 1 390 . 35 VAL CG2 C 21.80 . 1 391 . 35 VAL N N 120.86 . 1 392 . 36 ALA H H 7.71 . 1 393 . 36 ALA HA H 5.36 . 1 394 . 36 ALA HB H 1.45 . 1 395 . 36 ALA C C 174.49 . 1 396 . 36 ALA CA C 51.48 . 1 397 . 36 ALA CB C 22.32 . 1 398 . 36 ALA N N 115.19 . 1 399 . 37 GLU H H 9.35 . 1 400 . 37 GLU HA H 5.44 . 1 401 . 37 GLU HB2 H 2.24 . 2 402 . 37 GLU HG2 H 2.33 . 2 403 . 37 GLU C C 173.06 . 1 404 . 37 GLU CA C 54.57 . 1 405 . 37 GLU CB C 35.34 . 1 406 . 37 GLU CG C 35.89 . 1 407 . 37 GLU N N 118.62 . 1 408 . 38 LEU H H 9.06 . 1 409 . 38 LEU HA H 5.30 . 1 410 . 38 LEU HB2 H 1.78 . 2 411 . 38 LEU HB3 H 1.40 . 2 412 . 38 LEU HG H 1.55 . 1 413 . 38 LEU HD1 H 0.80 . 1 414 . 38 LEU HD2 H 0.80 . 1 415 . 38 LEU C C 175.62 . 1 416 . 38 LEU CA C 53.63 . 1 417 . 38 LEU CB C 46.49 . 1 418 . 38 LEU CG C 27.46 . 1 419 . 38 LEU CD1 C 23.98 . 1 420 . 38 LEU CD2 C 25.85 . 1 421 . 38 LEU N N 122.83 . 1 422 . 39 GLU H H 8.82 . 1 423 . 39 GLU HA H 4.69 . 1 424 . 39 GLU HB2 H 2.08 . 2 425 . 39 GLU HB3 H 1.95 . 2 426 . 39 GLU HG2 H 2.30 . 2 427 . 39 GLU C C 175.87 . 1 428 . 39 GLU CA C 55.82 . 1 429 . 39 GLU CB C 32.10 . 1 430 . 39 GLU CG C 35.89 . 1 431 . 39 GLU N N 124.93 . 1 432 . 40 ASN H H 9.76 . 1 433 . 40 ASN HA H 4.38 . 1 434 . 40 ASN HB2 H 3.13 . 2 435 . 40 ASN HB3 H 2.82 . 2 436 . 40 ASN HD21 H 7.83 . 2 437 . 40 ASN HD22 H 6.91 . 2 438 . 40 ASN C C 174.72 . 1 439 . 40 ASN CA C 55.09 . 1 440 . 40 ASN CB C 37.21 . 1 441 . 40 ASN N N 126.80 . 1 442 . 40 ASN ND2 N 113.20 . 1 443 . 41 SER H H 8.89 . 1 444 . 41 SER HA H 3.99 . 1 445 . 41 SER HB2 H 4.24 . 2 446 . 41 SER HB3 H 4.10 . 2 447 . 41 SER C C 172.69 . 1 448 . 41 SER CA C 60.43 . 1 449 . 41 SER CB C 62.62 . 1 450 . 41 SER N N 107.11 . 1 451 . 42 GLU H H 8.15 . 1 452 . 42 GLU HA H 4.69 . 1 453 . 42 GLU HB2 H 2.08 . 2 454 . 42 GLU HG2 H 2.34 . 2 455 . 42 GLU HG3 H 2.21 . 2 456 . 42 GLU C C 174.53 . 1 457 . 42 GLU CA C 55.20 . 1 458 . 42 GLU CB C 31.69 . 1 459 . 42 GLU CG C 36.26 . 1 460 . 42 GLU N N 121.34 . 1 461 . 43 PHE H H 8.65 . 1 462 . 43 PHE HA H 5.76 . 1 463 . 43 PHE HB2 H 3.17 . 2 464 . 43 PHE HB3 H 2.83 . 2 465 . 43 PHE HD1 H 7.15 . 3 466 . 43 PHE HE1 H 7.21 . 3 467 . 43 PHE C C 174.44 . 1 468 . 43 PHE CA C 55.22 . 1 469 . 43 PHE CB C 41.91 . 1 470 . 43 PHE N N 123.27 . 1 471 . 44 ARG H H 8.54 . 1 472 . 44 ARG HA H 4.08 . 1 473 . 44 ARG HB2 H 1.47 . 2 474 . 44 ARG HB3 H 1.42 . 2 475 . 44 ARG HG2 H 1.38 . 2 476 . 44 ARG HG3 H 1.31 . 2 477 . 44 ARG HD2 H 3.13 . 2 478 . 44 ARG C C 172.30 . 1 479 . 44 ARG CA C 54.59 . 1 480 . 44 ARG CB C 34.16 . 1 481 . 44 ARG CG C 27.46 . 1 482 . 44 ARG CD C 43.35 . 1 483 . 44 ARG N N 125.09 . 1 484 . 45 ALA H H 7.91 . 1 485 . 45 ALA HA H 4.85 . 1 486 . 45 ALA HB H 1.33 . 1 487 . 45 ALA C C 175.79 . 1 488 . 45 ALA CA C 50.10 . 1 489 . 45 ALA CB C 22.95 . 1 490 . 45 ALA N N 122.03 . 1 491 . 46 PHE H H 7.61 . 1 492 . 46 PHE HA H 4.75 . 1 493 . 46 PHE HB2 H 2.82 . 2 494 . 46 PHE HB3 H 3.22 . 2 495 . 46 PHE HD1 H 6.98 . 3 496 . 46 PHE HE1 H 7.08 . 3 497 . 46 PHE HZ H 7.22 . 1 498 . 46 PHE C C 175.41 . 1 499 . 46 PHE CA C 57.55 . 1 500 . 46 PHE CB C 42.54 . 1 501 . 46 PHE N N 114.74 . 1 502 . 47 SER H H 9.34 . 1 503 . 47 SER HA H 4.06 . 1 504 . 47 SER HB2 H 4.34 . 2 505 . 47 SER HB3 H 4.18 . 2 506 . 47 SER CA C 58.52 . 1 507 . 47 SER CB C 62.14 . 1 508 . 47 SER N N 113.70 . 1 509 . 48 SER HA H 4.34 . 1 510 . 48 SER HB2 H 3.90 . 2 511 . 48 SER HB3 H 3.77 . 2 512 . 48 SER C C 175.03 . 1 513 . 48 SER CA C 60.04 . 1 514 . 48 SER CB C 62.70 . 1 515 . 49 PHE H H 8.62 . 1 516 . 49 PHE HA H 4.28 . 1 517 . 49 PHE HB2 H 3.51 . 2 518 . 49 PHE HB3 H 3.37 . 2 519 . 49 PHE HD1 H 7.22 . 3 520 . 49 PHE HE1 H 7.34 . 3 521 . 49 PHE HZ H 7.50 . 1 522 . 49 PHE C C 175.39 . 1 523 . 49 PHE CA C 59.67 . 1 524 . 49 PHE CB C 38.41 . 1 525 . 49 PHE N N 121.19 . 1 526 . 50 LYS H H 7.05 . 1 527 . 50 LYS HA H 3.76 . 1 528 . 50 LYS HB2 H 1.72 . 2 529 . 50 LYS HB3 H 1.63 . 2 530 . 50 LYS HG2 H 1.71 . 2 531 . 50 LYS HD2 H 1.42 . 2 532 . 50 LYS HD3 H 1.28 . 2 533 . 50 LYS HE2 H 3.03 . 2 534 . 50 LYS CA C 58.94 . 1 535 . 50 LYS CB C 32.40 . 1 536 . 50 LYS CG C 29.33 . 1 537 . 50 LYS CD C 25.14 . 1 538 . 50 LYS CE C 41.85 . 1 539 . 50 LYS N N 119.55 . 1 540 . 51 ASN H H 8.95 . 1 541 . 51 ASN HA H 4.62 . 1 542 . 51 ASN HB2 H 3.03 . 2 543 . 51 ASN HD21 H 7.72 . 2 544 . 51 ASN HD22 H 6.99 . 2 545 . 51 ASN C C 175.43 . 1 546 . 51 ASN CA C 54.67 . 1 547 . 51 ASN CB C 38.39 . 1 548 . 51 ASN N N 115.63 . 1 549 . 51 ASN ND2 N 113.46 . 1 550 . 52 ARG H H 8.20 . 1 551 . 52 ARG HA H 4.89 . 1 552 . 52 ARG HB2 H 1.98 . 2 553 . 52 ARG HG2 H 1.77 . 2 554 . 52 ARG HG3 H 1.60 . 2 555 . 52 ARG HD2 H 3.51 . 2 556 . 52 ARG HD3 H 3.14 . 2 557 . 52 ARG C C 173.43 . 1 558 . 52 ARG CA C 55.84 . 1 559 . 52 ARG CB C 31.61 . 1 560 . 52 ARG CG C 27.77 . 1 561 . 52 ARG CD C 43.70 . 1 562 . 52 ARG N N 115.88 . 1 563 . 53 VAL H H 7.40 . 1 564 . 53 VAL HA H 5.72 . 1 565 . 53 VAL HB H 1.97 . 1 566 . 53 VAL HG1 H 1.11 . 2 567 . 53 VAL HG2 H 0.95 . 2 568 . 53 VAL C C 175.16 . 1 569 . 53 VAL CA C 58.03 . 1 570 . 53 VAL CB C 36.67 . 1 571 . 53 VAL CG1 C 23.99 . 1 572 . 53 VAL CG2 C 19.02 . 1 573 . 53 VAL N N 108.31 . 1 574 . 54 TYR H H 8.77 . 1 575 . 54 TYR HA H 4.43 . 1 576 . 54 TYR HB2 H 3.15 . 2 577 . 54 TYR HB3 H 2.54 . 2 578 . 54 TYR HD1 H 6.50 . 3 579 . 54 TYR HE1 H 6.89 . 3 580 . 54 TYR CA C 57.58 . 1 581 . 54 TYR CB C 42.47 . 1 582 . 54 TYR N N 121.47 . 1 583 . 55 LEU HA H 4.55 . 1 584 . 55 LEU HB2 H 1.05 . 2 585 . 55 LEU HB3 H 0.63 . 2 586 . 55 LEU HG H 1.22 . 1 587 . 55 LEU HD1 H 0.81 . 2 588 . 55 LEU HD2 H 0.72 . 2 589 . 55 LEU C C 173.28 . 1 590 . 55 LEU CA C 52.12 . 1 591 . 55 LEU CB C 44.71 . 1 592 . 55 LEU CG C 27.64 . 1 593 . 55 LEU CD1 C 26.76 . 1 594 . 55 LEU CD2 C 26.83 . 1 595 . 56 ASP H H 8.11 . 1 596 . 56 ASP HA H 4.35 . 1 597 . 56 ASP HB2 H 2.59 . 2 598 . 56 ASP HB3 H 2.92 . 2 599 . 56 ASP C C 177.26 . 1 600 . 56 ASP CA C 53.37 . 1 601 . 56 ASP CB C 42.24 . 1 602 . 56 ASP N N 123.50 . 1 603 . 57 THR H H 8.48 . 1 604 . 57 THR HA H 3.79 . 1 605 . 57 THR HB H 4.37 . 1 606 . 57 THR HG2 H 1.28 . 1 607 . 57 THR C C 174.72 . 1 608 . 57 THR CA C 64.05 . 1 609 . 57 THR CB C 68.26 . 1 610 . 57 THR CG2 C 22.05 . 1 611 . 57 THR N N 119.62 . 1 612 . 58 LYS H H 8.17 . 1 613 . 58 LYS HA H 4.30 . 1 614 . 58 LYS HB2 H 2.01 . 2 615 . 58 LYS HB3 H 1.93 . 2 616 . 58 LYS HG2 H 1.73 . 2 617 . 58 LYS HD2 H 1.52 . 2 618 . 58 LYS HD3 H 1.42 . 2 619 . 58 LYS HE2 H 3.02 . 2 620 . 58 LYS C C 176.68 . 1 621 . 58 LYS CA C 57.72 . 1 622 . 58 LYS CB C 32.31 . 1 623 . 58 LYS CG C 28.80 . 1 624 . 58 LYS CD C 25.14 . 1 625 . 58 LYS CE C 41.85 . 1 626 . 58 LYS N N 118.68 . 1 627 . 59 SER H H 7.59 . 1 628 . 59 SER HA H 4.63 . 1 629 . 59 SER HB2 H 4.30 . 2 630 . 59 SER HB3 H 3.83 . 2 631 . 59 SER C C 173.98 . 1 632 . 59 SER CA C 58.40 . 1 633 . 59 SER CB C 67.07 . 1 634 . 59 SER N N 108.82 . 1 635 . 60 GLY H H 8.53 . 1 636 . 60 GLY HA2 H 3.44 . 1 637 . 60 GLY HA3 H 4.41 . 1 638 . 60 GLY C C 172.53 . 1 639 . 60 GLY CA C 45.30 . 1 640 . 60 GLY N N 109.13 . 1 641 . 61 SER H H 8.03 . 1 642 . 61 SER HA H 4.61 . 1 643 . 61 SER HB2 H 3.72 . 2 644 . 61 SER HB3 H 3.65 . 2 645 . 61 SER C C 172.63 . 1 646 . 61 SER CA C 60.83 . 1 647 . 61 SER CB C 63.36 . 1 648 . 61 SER N N 113.85 . 1 649 . 62 LEU H H 7.21 . 1 650 . 62 LEU HA H 4.56 . 1 651 . 62 LEU HB2 H -0.46 . 2 652 . 62 LEU HB3 H 0.24 . 2 653 . 62 LEU HG H 0.52 . 1 654 . 62 LEU HD1 H 0.17 . 2 655 . 62 LEU HD2 H -0.34 . 2 656 . 62 LEU C C 174.03 . 1 657 . 62 LEU CA C 52.83 . 1 658 . 62 LEU CB C 44.01 . 1 659 . 62 LEU CG C 26.14 . 1 660 . 62 LEU CD1 C 23.08 . 1 661 . 62 LEU CD2 C 24.29 . 1 662 . 62 LEU N N 126.55 . 1 663 . 63 THR H H 9.05 . 1 664 . 63 THR HA H 5.05 . 1 665 . 63 THR HB H 3.70 . 1 666 . 63 THR HG2 H 0.35 . 1 667 . 63 THR C C 172.73 . 1 668 . 63 THR CA C 60.84 . 1 669 . 63 THR CB C 71.06 . 1 670 . 63 THR CG2 C 19.91 . 1 671 . 63 THR N N 123.69 . 1 672 . 64 ILE H H 8.32 . 1 673 . 64 ILE HA H 4.36 . 1 674 . 64 ILE HB H 1.11 . 1 675 . 64 ILE HG12 H 0.85 . 2 676 . 64 ILE HG13 H 0.38 . 2 677 . 64 ILE HG2 H 0.85 . 1 678 . 64 ILE HD1 H 0.16 . 1 679 . 64 ILE C C 174.19 . 1 680 . 64 ILE CA C 60.26 . 1 681 . 64 ILE CB C 40.26 . 1 682 . 64 ILE CG1 C 26.76 . 1 683 . 64 ILE CG2 C 18.29 . 1 684 . 64 ILE CD1 C 13.95 . 1 685 . 64 ILE N N 124.47 . 1 686 . 65 TYR H H 8.41 . 1 687 . 65 TYR HA H 4.74 . 1 688 . 65 TYR HB2 H 2.90 . 2 689 . 65 TYR HB3 H 2.63 . 2 690 . 65 TYR HD1 H 6.88 . 3 691 . 65 TYR HE1 H 6.95 . 3 692 . 65 TYR CA C 56.58 . 1 693 . 65 TYR CB C 40.27 . 1 694 . 65 TYR N N 122.74 . 1 695 . 66 ASN C C 174.10 . 1 696 . 66 ASN CA C 52.84 . 1 697 . 66 ASN CB C 36.61 . 1 698 . 67 LEU H H 8.44 . 1 699 . 67 LEU HA H 4.23 . 1 700 . 67 LEU HB2 H 1.78 . 2 701 . 67 LEU HB3 H 1.01 . 2 702 . 67 LEU HG H 1.65 . 1 703 . 67 LEU HD1 H 0.62 . 2 704 . 67 LEU HD2 H 0.67 . 2 705 . 67 LEU C C 178.40 . 1 706 . 67 LEU CA C 55.28 . 1 707 . 67 LEU CB C 43.37 . 1 708 . 67 LEU CG C 26.81 . 1 709 . 67 LEU CD1 C 26.10 . 1 710 . 67 LEU CD2 C 23.71 . 1 711 . 67 LEU N N 116.02 . 1 712 . 68 THR H H 9.16 . 1 713 . 68 THR HA H 4.57 . 1 714 . 68 THR HB H 4.38 . 1 715 . 68 THR HG2 H 1.23 . 1 716 . 68 THR C C 175.66 . 1 717 . 68 THR CA C 59.54 . 1 718 . 68 THR CB C 72.57 . 1 719 . 68 THR CG2 C 20.90 . 1 720 . 68 THR N N 112.13 . 1 721 . 69 SER H H 8.99 . 1 722 . 69 SER HA H 4.09 . 1 723 . 69 SER HB2 H 3.94 . 2 724 . 69 SER CA C 62.21 . 1 725 . 69 SER CB C 62.22 . 1 726 . 69 SER N N 117.12 . 1 727 . 70 SER H H 7.91 . 1 728 . 70 SER HA H 4.38 . 1 729 . 70 SER HB2 H 3.85 . 2 730 . 70 SER C C 174.04 . 1 731 . 70 SER CA C 60.20 . 1 732 . 70 SER CB C 62.68 . 1 733 . 70 SER N N 115.09 . 1 734 . 71 ASP H H 7.98 . 1 735 . 71 ASP HA H 4.65 . 1 736 . 71 ASP HB2 H 2.87 . 2 737 . 71 ASP HB3 H 2.73 . 2 738 . 71 ASP C C 176.52 . 1 739 . 71 ASP CA C 55.32 . 1 740 . 71 ASP CB C 41.37 . 1 741 . 71 ASP N N 118.67 . 1 742 . 72 GLU H H 7.19 . 1 743 . 72 GLU HA H 4.49 . 1 744 . 72 GLU HB2 H 2.27 . 2 745 . 72 GLU HB3 H 2.14 . 2 746 . 72 GLU HG2 H 3.26 . 2 747 . 72 GLU HG3 H 2.14 . 2 748 . 72 GLU C C 174.46 . 1 749 . 72 GLU CA C 57.01 . 1 750 . 72 GLU CB C 30.21 . 1 751 . 72 GLU CG C 36.23 . 1 752 . 72 GLU N N 120.87 . 1 753 . 73 ASP H H 8.02 . 1 754 . 73 ASP HA H 4.37 . 1 755 . 73 ASP HB2 H 2.48 . 2 756 . 73 ASP HB3 H 2.05 . 2 757 . 73 ASP C C 172.88 . 1 758 . 73 ASP CA C 52.68 . 1 759 . 73 ASP CB C 44.03 . 1 760 . 73 ASP N N 127.54 . 1 761 . 74 GLU H H 9.05 . 1 762 . 74 GLU HA H 4.80 . 1 763 . 74 GLU HB2 H 1.94 . 2 764 . 74 GLU HB3 H 1.88 . 2 765 . 74 GLU HG2 H 2.06 . 2 766 . 74 GLU C C 174.77 . 1 767 . 74 GLU CA C 55.21 . 1 768 . 74 GLU CB C 32.27 . 1 769 . 74 GLU CG C 37.40 . 1 770 . 74 GLU N N 118.34 . 1 771 . 75 TYR H H 9.37 . 1 772 . 75 TYR HA H 5.51 . 1 773 . 75 TYR HB2 H 2.86 . 2 774 . 75 TYR HB3 H 2.68 . 2 775 . 75 TYR HD1 H 6.88 . 3 776 . 75 TYR HE1 H 6.59 . 3 777 . 75 TYR C C 175.54 . 1 778 . 75 TYR CA C 56.35 . 1 779 . 75 TYR CB C 42.34 . 1 780 . 75 TYR N N 124.14 . 1 781 . 76 GLU H H 9.15 . 1 782 . 76 GLU HA H 5.45 . 1 783 . 76 GLU HB2 H 1.84 . 2 784 . 76 GLU HG2 H 2.06 . 2 785 . 76 GLU HG3 H 1.96 . 2 786 . 76 GLU C C 173.11 . 1 787 . 76 GLU CA C 54.54 . 1 788 . 76 GLU CB C 34.77 . 1 789 . 76 GLU CG C 36.59 . 1 790 . 76 GLU N N 120.32 . 1 791 . 77 MET H H 8.58 . 1 792 . 77 MET HA H 4.44 . 1 793 . 77 MET HB2 H 1.33 . 2 794 . 77 MET HB3 H 1.24 . 2 795 . 77 MET HG2 H -0.36 . 2 796 . 77 MET HE H 1.87 . 1 797 . 77 MET C C 174.74 . 1 798 . 77 MET CA C 53.87 . 1 799 . 77 MET CB C 32.87 . 1 800 . 77 MET CG C 33.08 . 1 801 . 77 MET CE C 18.71 . 1 802 . 77 MET N N 126.05 . 1 803 . 78 GLU H H 8.91 . 1 804 . 78 GLU HA H 4.63 . 1 805 . 78 GLU HB2 H 1.87 . 2 806 . 78 GLU HB3 H 1.79 . 2 807 . 78 GLU HG2 H 2.03 . 2 808 . 78 GLU C C 175.22 . 1 809 . 78 GLU CA C 54.24 . 1 810 . 78 GLU CB C 33.69 . 1 811 . 78 GLU CG C 36.60 . 1 812 . 78 GLU N N 123.61 . 1 813 . 79 SER H H 8.56 . 1 814 . 79 SER HA H 5.07 . 1 815 . 79 SER HB2 H 4.25 . 2 816 . 79 SER HB3 H 3.39 . 2 817 . 79 SER C C 173.79 . 1 818 . 79 SER CA C 55.32 . 1 819 . 79 SER CB C 66.51 . 1 820 . 79 SER N N 116.96 . 1 821 . 80 PRO HA H 4.56 . 1 822 . 80 PRO HB2 H 2.37 . 2 823 . 80 PRO HB3 H 1.96 . 2 824 . 80 PRO HG2 H 2.03 . 2 825 . 80 PRO HG3 H 1.96 . 2 826 . 80 PRO HD2 H 3.92 . 2 827 . 80 PRO HD3 H 3.80 . 2 828 . 80 PRO C C 177.03 . 1 829 . 80 PRO CA C 63.93 . 1 830 . 80 PRO CB C 32.26 . 1 831 . 80 PRO CG C 27.16 . 1 832 . 80 PRO CD C 51.53 . 1 833 . 81 ASN H H 8.32 . 1 834 . 81 ASN HA H 4.73 . 1 835 . 81 ASN HB2 H 3.12 . 2 836 . 81 ASN HB3 H 2.60 . 2 837 . 81 ASN HD21 H 7.64 . 2 838 . 81 ASN HD22 H 7.13 . 2 839 . 81 ASN C C 174.05 . 1 840 . 81 ASN CA C 53.92 . 1 841 . 81 ASN CB C 40.30 . 1 842 . 81 ASN N N 113.68 . 1 843 . 81 ASN ND2 N 110.41 . 1 844 . 82 ILE H H 7.49 . 1 845 . 82 ILE HA H 4.61 . 1 846 . 82 ILE HB H 1.97 . 1 847 . 82 ILE HG12 H 1.39 . 2 848 . 82 ILE HG13 H 1.19 . 2 849 . 82 ILE HG2 H 0.92 . 1 850 . 82 ILE HD1 H 0.86 . 1 851 . 82 ILE C C 175.66 . 1 852 . 82 ILE CA C 59.82 . 1 853 . 82 ILE CB C 40.27 . 1 854 . 82 ILE CG1 C 26.09 . 1 855 . 82 ILE CG2 C 18.00 . 1 856 . 82 ILE CD1 C 13.40 . 1 857 . 82 ILE N N 115.86 . 1 858 . 83 THR H H 8.41 . 1 859 . 83 THR HA H 4.16 . 1 860 . 83 THR HB H 4.20 . 1 861 . 83 THR HG2 H 1.21 . 1 862 . 83 THR C C 174.25 . 1 863 . 83 THR CA C 63.92 . 1 864 . 83 THR CB C 68.92 . 1 865 . 83 THR CG2 C 21.70 . 1 866 . 83 THR N N 116.12 . 1 867 . 84 ASP H H 7.68 . 1 868 . 84 ASP HA H 4.81 . 1 869 . 84 ASP HB2 H 2.54 . 2 870 . 84 ASP HB3 H 2.66 . 2 871 . 84 ASP C C 174.94 . 1 872 . 84 ASP CA C 53.38 . 1 873 . 84 ASP CB C 42.86 . 1 874 . 84 ASP N N 119.79 . 1 875 . 85 SER H H 8.36 . 1 876 . 85 SER HA H 4.55 . 1 877 . 85 SER HB2 H 3.88 . 2 878 . 85 SER HB3 H 3.82 . 2 879 . 85 SER C C 174.03 . 1 880 . 85 SER CA C 57.97 . 1 881 . 85 SER CB C 63.83 . 1 882 . 85 SER N N 116.57 . 1 883 . 86 MET H H 8.47 . 1 884 . 86 MET HA H 4.70 . 1 885 . 86 MET HB2 H 2.04 . 2 886 . 86 MET HB3 H 1.95 . 2 887 . 86 MET HG2 H 2.53 . 2 888 . 86 MET HG3 H 2.48 . 2 889 . 86 MET HE H 2.18 . 1 890 . 86 MET C C 174.02 . 1 891 . 86 MET CA C 54.62 . 1 892 . 86 MET CB C 35.21 . 1 893 . 86 MET CG C 32.50 . 1 894 . 86 MET CE C 17.46 . 1 895 . 86 MET N N 121.27 . 1 896 . 87 LYS H H 8.09 . 1 897 . 87 LYS HA H 5.33 . 1 898 . 87 LYS HB2 H 1.73 . 2 899 . 87 LYS HB3 H 1.70 . 2 900 . 87 LYS HG2 H 1.53 . 2 901 . 87 LYS HD2 H 1.34 . 2 902 . 87 LYS HD3 H 1.23 . 2 903 . 87 LYS HE2 H 2.79 . 2 904 . 87 LYS C C 175.72 . 1 905 . 87 LYS CA C 55.21 . 1 906 . 87 LYS CB C 35.60 . 1 907 . 87 LYS CG C 29.33 . 1 908 . 87 LYS CD C 25.80 . 1 909 . 87 LYS CE C 41.85 . 1 910 . 87 LYS N N 121.37 . 1 911 . 88 PHE H H 9.36 . 1 912 . 88 PHE HA H 5.16 . 1 913 . 88 PHE HB2 H 2.35 . 2 914 . 88 PHE HB3 H 2.27 . 2 915 . 88 PHE HD1 H 7.07 . 3 916 . 88 PHE HE1 H 7.39 . 3 917 . 88 PHE C C 173.98 . 1 918 . 88 PHE CA C 55.87 . 1 919 . 88 PHE CB C 42.85 . 1 920 . 88 PHE N N 121.36 . 1 921 . 89 PHE H H 9.23 . 1 922 . 89 PHE HA H 4.85 . 1 923 . 89 PHE HB2 H 3.01 . 2 924 . 89 PHE HB3 H 2.84 . 2 925 . 89 PHE HD1 H 6.65 . 3 926 . 89 PHE HE1 H 6.95 . 3 927 . 89 PHE HZ H 7.12 . 1 928 . 89 PHE C C 172.86 . 1 929 . 89 PHE CA C 57.73 . 1 930 . 89 PHE CB C 41.00 . 1 931 . 89 PHE N N 124.39 . 1 932 . 90 LEU H H 8.13 . 1 933 . 90 LEU HA H 5.03 . 1 934 . 90 LEU HB2 H 2.23 . 2 935 . 90 LEU HB3 H 1.25 . 2 936 . 90 LEU HG H 1.27 . 1 937 . 90 LEU HD1 H 0.75 . 2 938 . 90 LEU HD2 H 0.71 . 2 939 . 90 LEU C C 173.76 . 1 940 . 90 LEU CA C 52.90 . 1 941 . 90 LEU CB C 44.62 . 1 942 . 90 LEU CG C 28.08 . 1 943 . 90 LEU CD1 C 24.65 . 1 944 . 90 LEU CD2 C 25.55 . 1 945 . 90 LEU N N 128.23 . 1 946 . 91 TYR H H 8.78 . 1 947 . 91 TYR HA H 4.74 . 1 948 . 91 TYR HB2 H 2.69 . 2 949 . 91 TYR HB3 H 3.08 . 2 950 . 91 TYR HD1 H 6.86 . 3 951 . 91 TYR HE1 H 6.63 . 3 952 . 91 TYR C C 175.45 . 1 953 . 91 TYR CA C 57.10 . 1 954 . 91 TYR CB C 40.35 . 1 955 . 91 TYR N N 124.29 . 1 956 . 92 VAL H H 9.46 . 1 957 . 92 VAL HA H 4.17 . 1 958 . 92 VAL HB H 1.93 . 1 959 . 92 VAL HG1 H 0.45 . 2 960 . 92 VAL HG2 H 0.73 . 2 961 . 92 VAL C C 175.50 . 1 962 . 92 VAL CA C 61.48 . 1 963 . 92 VAL CB C 32.92 . 1 964 . 92 VAL CG1 C 20.90 . 1 965 . 92 VAL CG2 C 20.90 . 1 966 . 92 VAL N N 122.10 . 1 967 . 93 GLY H H 8.59 . 1 968 . 93 GLY HA2 H 4.61 . 1 969 . 93 GLY HA3 H 3.94 . 1 970 . 93 GLY C C 173.16 . 1 971 . 93 GLY CA C 44.03 . 1 972 . 93 GLY N N 114.61 . 1 973 . 94 GLU H H 8.62 . 1 974 . 94 GLU HA H 4.31 . 1 975 . 94 GLU HB2 H 1.97 . 2 976 . 94 GLU HB3 H 2.17 . 2 977 . 94 GLU HG2 H 2.38 . 2 978 . 94 GLU HG3 H 2.29 . 2 979 . 94 GLU C C 176.03 . 1 980 . 94 GLU CA C 57.01 . 1 981 . 94 GLU CB C 30.98 . 1 982 . 94 GLU CG C 36.63 . 1 983 . 94 GLU N N 118.53 . 1 984 . 95 SER H H 7.90 . 1 985 . 95 SER HA H 4.20 . 1 986 . 95 SER HB2 H 3.89 . 2 987 . 95 SER CA C 59.98 . 1 988 . 95 SER CB C 65.02 . 1 989 . 95 SER N N 118.84 . 1 stop_ save_