data_5049 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N data for the extracellular domain of human IFNAR2 ; _BMRB_accession_number 5049 _BMRB_flat_file_name bmr5049.str _Entry_type original _Submission_date 2001-06-10 _Accession_date 2001-06-11 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chill Jordan H. . 2 Nivasch Rachel . . 3 Levy Rina . . 4 Albeck Shira . . 5 Schreiber Gideon . . 6 Anglister Jacob . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 574 "13C chemical shifts" 573 "15N chemical shifts" 183 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-04-05 original BMRB . stop_ _Original_release_date 2001-06-11 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The Human Interferon Receptor: NMR-based Modeling, Mapping of the IFN-alpha2 Binding Site, and Observed Ligand-Induced Tightening ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21885813 _PubMed_ID 11888273 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chill Jordan H. . 2 Nivasch Rachel . . 3 Levy Rina . . 4 Albeck Shira . . 5 Schreiber Gideon . . 6 Anglister Jacob . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 41 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3575 _Page_last 3585 _Year 2002 _Details . save_ ################################## # Molecular system description # ################################## save_system_IFNAR2-EC _Saveframe_category molecular_system _Mol_system_name 'Extracellular domain of subunit 2 of the human receptor for type I interferons' _Abbreviation_common IFNAR2-EC _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label IFNAR2-EC $IFNAR2-EC stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'receptor for type I interferons' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_IFNAR2-EC _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Extracellular domain of subunit 2 of the Human receptor for type I interferons' _Abbreviation_common IFNAR2-EC _Molecular_mass 24850 _Mol_thiol_state 'all disulfide bound' _Details ; Double immunoglobulin fold highly beta-character (14 b-sheets) ; ############################## # Polymer residue sequence # ############################## _Residue_count 212 _Mol_residue_sequence ; SYDSPDYTDESCTFKISLRN FRSILSWELKNHSIVPTHYT LLYTIMSKPEDLKVVKNCAN TTRSFCDLTDEWRSTHEAYV TVLEGFSGNTTLFSCSHNFW LAIDMSFEPPEFEIVGFTNH INVMVKFPSIVEEELQFDLS LVIEEQSEGIVKKHKPEIKG NMSGNFTYIIDKLIPNTNYC VSVYLEHSDEQAVIKSPLKC TLLPPGQESEFS ; loop_ _Residue_seq_code _Residue_label 1 SER 2 TYR 3 ASP 4 SER 5 PRO 6 ASP 7 TYR 8 THR 9 ASP 10 GLU 11 SER 12 CYS 13 THR 14 PHE 15 LYS 16 ILE 17 SER 18 LEU 19 ARG 20 ASN 21 PHE 22 ARG 23 SER 24 ILE 25 LEU 26 SER 27 TRP 28 GLU 29 LEU 30 LYS 31 ASN 32 HIS 33 SER 34 ILE 35 VAL 36 PRO 37 THR 38 HIS 39 TYR 40 THR 41 LEU 42 LEU 43 TYR 44 THR 45 ILE 46 MET 47 SER 48 LYS 49 PRO 50 GLU 51 ASP 52 LEU 53 LYS 54 VAL 55 VAL 56 LYS 57 ASN 58 CYS 59 ALA 60 ASN 61 THR 62 THR 63 ARG 64 SER 65 PHE 66 CYS 67 ASP 68 LEU 69 THR 70 ASP 71 GLU 72 TRP 73 ARG 74 SER 75 THR 76 HIS 77 GLU 78 ALA 79 TYR 80 VAL 81 THR 82 VAL 83 LEU 84 GLU 85 GLY 86 PHE 87 SER 88 GLY 89 ASN 90 THR 91 THR 92 LEU 93 PHE 94 SER 95 CYS 96 SER 97 HIS 98 ASN 99 PHE 100 TRP 101 LEU 102 ALA 103 ILE 104 ASP 105 MET 106 SER 107 PHE 108 GLU 109 PRO 110 PRO 111 GLU 112 PHE 113 GLU 114 ILE 115 VAL 116 GLY 117 PHE 118 THR 119 ASN 120 HIS 121 ILE 122 ASN 123 VAL 124 MET 125 VAL 126 LYS 127 PHE 128 PRO 129 SER 130 ILE 131 VAL 132 GLU 133 GLU 134 GLU 135 LEU 136 GLN 137 PHE 138 ASP 139 LEU 140 SER 141 LEU 142 VAL 143 ILE 144 GLU 145 GLU 146 GLN 147 SER 148 GLU 149 GLY 150 ILE 151 VAL 152 LYS 153 LYS 154 HIS 155 LYS 156 PRO 157 GLU 158 ILE 159 LYS 160 GLY 161 ASN 162 MET 163 SER 164 GLY 165 ASN 166 PHE 167 THR 168 TYR 169 ILE 170 ILE 171 ASP 172 LYS 173 LEU 174 ILE 175 PRO 176 ASN 177 THR 178 ASN 179 TYR 180 CYS 181 VAL 182 SER 183 VAL 184 TYR 185 LEU 186 GLU 187 HIS 188 SER 189 ASP 190 GLU 191 GLN 192 ALA 193 VAL 194 ILE 195 LYS 196 SER 197 PRO 198 LEU 199 LYS 200 CYS 201 THR 202 LEU 203 LEU 204 PRO 205 PRO 206 GLY 207 GLN 208 GLU 209 SER 210 GLU 211 PHE 212 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 1N6U 'Nmr Structure Of The Interferon-Binding Ectodomain Of The Human Interferon Receptor' 100.00 212 100.00 100.00 2.45e-121 PDB 1N6V 'Average Structure Of The Interferon-Binding Ectodomain Of The Human Type I Interferon Receptor' 100.00 212 100.00 100.00 2.45e-121 PDB 2HYM 'Nmr Based Docking Model Of The Complex Between The Human Type I Interferon Receptor And Human Interferon Alpha-2' 100.00 212 100.00 100.00 2.45e-121 DBJ BAF85748 'unnamed protein product [Homo sapiens]' 99.06 515 100.00 100.00 2.75e-121 EMBL CAA54785 'interferon alpha/beta receptor [Homo sapiens]' 99.06 331 100.00 100.00 3.20e-121 EMBL CAA61914 'interferon alpha /beta receptor [Homo sapiens]' 99.06 515 100.00 100.00 2.35e-121 EMBL CAA61940 'soluble IFN alpha/beta receptor [Homo sapiens]' 100.00 239 100.00 100.00 4.62e-122 EMBL CAG46616 'IFNAR2 [Homo sapiens]' 99.06 331 100.00 100.00 3.54e-121 GenBank AAB46413 'interferon receptor' 99.06 515 100.00 100.00 2.75e-121 GenBank AAB46414 'interferon receptor' 100.00 239 100.00 100.00 5.11e-122 GenBank AAB46415 'interferon receptor' 99.06 331 100.00 100.00 3.54e-121 GenBank AAB46417 'interferon receptor' 99.06 331 100.00 100.00 3.54e-121 GenBank AAB46418 'interferon receptor' 100.00 239 100.00 100.00 5.11e-122 REF NP_000865 'interferon alpha/beta receptor 2 isoform b precursor [Homo sapiens]' 99.06 331 100.00 100.00 3.54e-121 REF NP_997467 'interferon alpha/beta receptor 2 isoform b precursor [Homo sapiens]' 99.06 331 100.00 100.00 3.54e-121 REF NP_997468 'interferon alpha/beta receptor 2 isoform a precursor [Homo sapiens]' 99.06 515 100.00 100.00 2.75e-121 REF XP_001164791 'PREDICTED: interferon alpha/beta receptor 2 isoform 1 [Pan troglodytes]' 100.00 239 98.58 100.00 5.88e-121 REF XP_001164897 'PREDICTED: interferon alpha/beta receptor 2 isoform 2 [Pan troglodytes]' 99.06 516 98.57 100.00 3.94e-120 SWISS-PROT P48551 ; Interferon-alpha/beta receptor beta chain precursor (Interferon alpha/beta receptor 2) (IFN-alpha-REC) (Type I interferon receptor) (IFN-R) ; 99.06 515 100.00 100.00 2.75e-121 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $IFNAR2-EC Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name _Details $IFNAR2-EC 'recombinant technology' 'E. coli' . . . . 'E. Coli TG1 cells' 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 $IFNAR2-EC . mM 0.25 0.4 '[U-97% 13C; U-97% 15N]' NaN3 0.02 % . . . NaCl . mM 0 1 . Tris 25 mM . . [U-2H] stop_ save_ ############################ # Computer software used # ############################ save_AURELIA _Saveframe_category software _Name AURELIA _Version 2.8 loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_15N-separated_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-separated NOESY' _Sample_label . save_ save_HNHA_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_15N,_13C-4D_separated_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '15N, 13C-4D separated NOESY' _Sample_label . save_ save_13C,_13C-4D_separated_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '13C, 13C-4D separated NOESY' _Sample_label . save_ save_1H,_15N-HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '1H, 15N-HSQC' _Sample_label . save_ ####################### # Sample conditions # ####################### save_Cond-1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 8.0 0.2 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 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 TSP H 1 'methyl protons' ppm 0.00 external direct cylindrical external parallel 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HNCO HNCA CBCA(CO)NH HNCACB '15N-separated NOESY' HNHA '15N, 13C-4D separated NOESY' '13C, 13C-4D separated NOESY' '1H, 15N-HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Cond-1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name IFNAR2-EC _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 TYR C C 175.4 0.1 1 2 . 2 TYR HA H 4.50 0.02 1 3 . 2 TYR HB2 H 2.88 0.02 2 4 . 2 TYR HB3 H 3.05 0.02 2 5 . 3 ASP N N 120.93 0.1 1 6 . 3 ASP H H 8.21 0.02 1 7 . 3 ASP C C 175.6 0.1 1 8 . 3 ASP CA C 54.18 0.1 1 9 . 3 ASP HA H 4.59 0.02 1 10 . 3 ASP CB C 41.23 0.1 1 11 . 3 ASP HB2 H 2.53 0.02 2 12 . 4 SER N N 116.33 0.1 1 13 . 4 SER H H 7.93 0.02 1 14 . 4 SER CA C 56.09 0.1 1 15 . 4 SER HA H 4.59 0.02 1 16 . 4 SER CB C 63.69 0.1 1 17 . 5 PRO C C 176.2 0.1 1 18 . 5 PRO CA C 63.31 0.1 1 19 . 5 PRO HA H 4.42 0.02 1 20 . 5 PRO CB C 31.93 0.1 1 21 . 5 PRO HB2 H 1.75 0.02 2 22 . 5 PRO HB3 H 2.18 0.02 2 23 . 6 ASP N N 119.46 0.1 1 24 . 6 ASP H H 8.16 0.02 1 25 . 6 ASP C C 175.8 0.1 1 26 . 6 ASP CA C 54.26 0.1 1 27 . 6 ASP HA H 4.55 0.02 1 28 . 6 ASP CB C 41.20 0.1 1 29 . 6 ASP HB2 H 2.49 0.02 2 30 . 6 ASP HB3 H 2.58 0.02 2 31 . 7 TYR N N 120.42 0.1 1 32 . 7 TYR H H 7.99 0.02 1 33 . 7 TYR C C 175.9 0.1 1 34 . 7 TYR CA C 57.98 0.1 1 35 . 7 TYR HA H 4.62 0.02 1 36 . 7 TYR CB C 38.78 0.1 1 37 . 7 TYR HB2 H 2.98 0.02 2 38 . 7 TYR HB3 H 3.10 0.02 2 39 . 8 THR N N 115.39 0.1 1 40 . 8 THR H H 8.08 0.02 1 41 . 8 THR C C 174.2 0.1 1 42 . 8 THR CA C 61.81 0.1 1 43 . 8 THR HA H 4.37 0.02 1 44 . 8 THR CB C 70.00 0.1 1 45 . 8 THR HB H 4.24 0.02 1 46 . 9 ASP N N 122.41 0.1 1 47 . 9 ASP H H 8.29 0.02 1 48 . 9 ASP C C 176.3 0.1 1 49 . 9 ASP CA C 54.74 0.1 1 50 . 9 ASP HA H 4.67 0.02 1 51 . 9 ASP CB C 41.45 0.1 1 52 . 9 ASP HB2 H 2.67 0.02 2 53 . 9 ASP HB3 H 2.82 0.02 2 54 . 10 GLU N N 120.87 0.1 1 55 . 10 GLU H H 8.30 0.02 1 56 . 10 GLU C C 176.8 0.1 1 57 . 10 GLU CA C 56.47 0.1 1 58 . 10 GLU HA H 4.43 0.02 1 59 . 10 GLU CB C 30.15 0.1 1 60 . 10 GLU HB2 H 2.05 0.02 2 61 . 11 SER N N 115.51 0.1 1 62 . 11 SER H H 8.50 0.02 1 63 . 11 SER C C 173.7 0.1 1 64 . 11 SER CA C 60.28 0.1 1 65 . 11 SER HA H 4.63 0.02 1 66 . 11 SER CB C 64.28 0.1 1 67 . 11 SER HB2 H 3.69 0.02 2 68 . 12 CYS N N 117.77 0.1 1 69 . 12 CYS H H 8.04 0.02 1 70 . 12 CYS C C 172.8 0.1 1 71 . 12 CYS CA C 55.72 0.1 1 72 . 12 CYS HA H 4.88 0.02 1 73 . 12 CYS CB C 43.55 0.1 1 74 . 12 CYS HB2 H 2.40 0.02 2 75 . 12 CYS HB3 H 2.80 0.02 2 76 . 13 THR N N 116.70 0.1 1 77 . 13 THR H H 8.48 0.02 1 78 . 13 THR C C 173.2 0.1 1 79 . 13 THR CA C 61.39 0.1 1 80 . 13 THR HA H 4.49 0.02 1 81 . 13 THR CB C 70.52 0.1 1 82 . 13 THR HB H 3.90 0.02 1 83 . 14 PHE N N 122.81 0.1 1 84 . 14 PHE H H 8.96 0.02 1 85 . 14 PHE C C 175.8 0.1 1 86 . 14 PHE CA C 56.92 0.1 1 87 . 14 PHE HA H 5.61 0.02 1 88 . 14 PHE CB C 44.71 0.1 1 89 . 14 PHE HB2 H 2.58 0.02 2 90 . 14 PHE HB3 H 3.19 0.02 2 91 . 15 LYS N N 120.57 0.1 1 92 . 15 LYS H H 8.89 0.02 1 93 . 15 LYS C C 173.8 0.1 1 94 . 15 LYS CA C 56.01 0.1 1 95 . 15 LYS HA H 4.62 0.02 1 96 . 15 LYS CB C 36.25 0.1 1 97 . 15 LYS HB2 H 1.58 0.02 2 98 . 15 LYS HB3 H 1.70 0.02 2 99 . 16 ILE N N 123.53 0.1 1 100 . 16 ILE H H 8.99 0.02 1 101 . 16 ILE C C 173.2 0.1 1 102 . 16 ILE CA C 57.57 0.1 1 103 . 16 ILE HA H 5.30 0.02 1 104 . 16 ILE CB C 41.41 0.1 1 105 . 16 ILE HB H 1.35 0.02 1 106 . 17 SER N N 121.23 0.1 1 107 . 17 SER H H 8.48 0.02 1 108 . 17 SER C C 171.3 0.1 1 109 . 17 SER CA C 56.28 0.1 1 110 . 17 SER HA H 4.98 0.02 1 111 . 17 SER CB C 66.47 0.1 1 112 . 17 SER HB2 H 3.37 0.02 2 113 . 17 SER HB3 H 3.50 0.02 2 114 . 18 LEU N N 125.20 0.1 1 115 . 18 LEU H H 8.71 0.02 1 116 . 18 LEU C C 176.3 0.1 1 117 . 18 LEU CA C 53.30 0.1 1 118 . 18 LEU HA H 4.99 0.02 1 119 . 18 LEU CB C 42.38 0.1 1 120 . 19 ARG N N 129.84 0.1 1 121 . 19 ARG H H 9.20 0.02 1 122 . 19 ARG CA C 54.95 0.1 1 123 . 19 ARG HA H 4.00 0.02 1 124 . 19 ARG CB C 31.94 0.1 1 125 . 20 ASN C C 174.3 0.1 1 126 . 20 ASN CA C 54.51 0.1 1 127 . 20 ASN CB C 37.48 0.1 1 128 . 20 ASN HB2 H 2.69 0.02 2 129 . 20 ASN HB3 H 3.05 0.02 2 130 . 21 PHE N N 105.38 0.1 1 131 . 21 PHE H H 8.33 0.02 1 132 . 21 PHE C C 173.0 0.1 1 133 . 21 PHE CA C 60.72 0.1 1 134 . 21 PHE CB C 35.36 0.1 1 135 . 21 PHE HB2 H 3.29 0.02 2 136 . 21 PHE HB3 H 3.45 0.02 2 137 . 22 ARG N N 117.39 0.1 1 138 . 22 ARG H H 7.60 0.02 1 139 . 22 ARG C C 176.0 0.1 1 140 . 22 ARG CA C 52.54 0.1 1 141 . 22 ARG HA H 4.91 0.02 1 142 . 22 ARG CB C 30.16 0.1 1 143 . 23 SER N N 121.41 0.1 1 144 . 23 SER H H 8.76 0.02 1 145 . 23 SER C C 171.8 0.1 1 146 . 23 SER CA C 57.22 0.1 1 147 . 23 SER HA H 4.52 0.02 1 148 . 23 SER CB C 62.90 0.1 1 149 . 23 SER HB2 H 3.37 0.02 2 150 . 23 SER HB3 H 3.53 0.02 2 151 . 24 ILE N N 126.19 0.1 1 152 . 24 ILE H H 8.99 0.02 1 153 . 24 ILE C C 175.3 0.1 1 154 . 24 ILE CA C 58.25 0.1 1 155 . 24 ILE HA H 4.50 0.02 1 156 . 24 ILE CB C 37.66 0.1 1 157 . 24 ILE HB H 1.88 0.02 1 158 . 25 LEU N N 132.49 0.1 1 159 . 25 LEU H H 8.67 0.02 1 160 . 25 LEU C C 174.5 0.1 1 161 . 25 LEU CA C 53.28 0.1 1 162 . 25 LEU HA H 5.17 0.02 1 163 . 25 LEU CB C 45.48 0.1 1 164 . 26 SER N N 121.39 0.1 1 165 . 26 SER H H 9.64 0.02 1 166 . 26 SER C C 172.9 0.1 1 167 . 26 SER CA C 56.99 0.1 1 168 . 26 SER HA H 4.87 0.02 1 169 . 26 SER CB C 66.55 0.1 1 170 . 26 SER HB2 H 3.50 0.02 2 171 . 26 SER HB3 H 3.80 0.02 2 172 . 27 TRP N N 115.58 0.1 1 173 . 27 TRP H H 7.26 0.02 1 174 . 27 TRP C C 174.5 0.1 1 175 . 27 TRP CA C 54.48 0.1 1 176 . 27 TRP HA H 5.63 0.02 1 177 . 27 TRP CB C 31.41 0.1 1 178 . 28 GLU N N 117.27 0.1 1 179 . 28 GLU H H 8.23 0.02 1 180 . 28 GLU C C 174.6 0.1 1 181 . 28 GLU CA C 54.42 0.1 1 182 . 28 GLU HA H 4.51 0.02 1 183 . 28 GLU CB C 33.70 0.1 1 184 . 28 GLU HB2 H 1.70 0.02 2 185 . 28 GLU HB3 H 1.87 0.02 2 186 . 29 LEU N N 123.39 0.1 1 187 . 29 LEU H H 8.62 0.02 1 188 . 29 LEU C C 177.2 0.1 1 189 . 29 LEU CA C 53.73 0.1 1 190 . 29 LEU HA H 4.63 0.02 1 191 . 29 LEU CB C 42.16 0.1 1 192 . 30 LYS N N 121.42 0.1 1 193 . 30 LYS H H 8.10 0.02 1 194 . 30 LYS C C 175.8 0.1 1 195 . 30 LYS CA C 56.60 0.1 1 196 . 30 LYS HA H 4.24 0.02 1 197 . 30 LYS CB C 33.25 0.1 1 198 . 30 LYS HB2 H 1.70 0.02 2 199 . 31 ASN N N 116.78 0.1 1 200 . 31 ASN H H 8.18 0.02 1 201 . 31 ASN CA C 53.18 0.1 1 202 . 31 ASN HA H 4.39 0.02 1 203 . 31 ASN CB C 38.43 0.1 1 204 . 33 SER C C 174.1 0.1 1 205 . 33 SER CA C 59.82 0.1 1 206 . 33 SER HA H 4.32 0.02 1 207 . 33 SER CB C 63.57 0.1 1 208 . 33 SER HB2 H 3.86 0.02 2 209 . 34 ILE N N 121.12 0.1 1 210 . 34 ILE H H 7.51 0.02 1 211 . 34 ILE C C 174.6 0.1 1 212 . 34 ILE CA C 60.24 0.1 1 213 . 34 ILE HA H 4.20 0.02 1 214 . 34 ILE CB C 39.19 0.1 1 215 . 34 ILE HB H 1.78 0.02 1 216 . 35 VAL N N 126.49 0.1 1 217 . 35 VAL H H 8.37 0.02 1 218 . 35 VAL CA C 60.03 0.1 1 219 . 35 VAL HA H 4.33 0.02 1 220 . 35 VAL CB C 32.57 0.1 1 221 . 36 PRO C C 177.1 0.1 1 222 . 36 PRO CA C 62.50 0.1 1 223 . 36 PRO HA H 4.24 0.02 1 224 . 36 PRO CB C 32.15 0.1 1 225 . 36 PRO HB2 H 1.97 0.02 2 226 . 37 THR N N 112.03 0.1 1 227 . 37 THR H H 9.40 0.02 1 228 . 37 THR C C 175.3 0.1 1 229 . 37 THR CA C 63.16 0.1 1 230 . 37 THR HA H 4.44 0.02 1 231 . 37 THR CB C 69.71 0.1 1 232 . 37 THR HB H 4.28 0.02 1 233 . 38 HIS N N 115.39 0.1 1 234 . 38 HIS H H 7.28 0.02 1 235 . 38 HIS C C 172.1 0.1 1 236 . 38 HIS CA C 56.32 0.1 1 237 . 38 HIS HA H 4.90 0.02 1 238 . 38 HIS CB C 32.43 0.1 1 239 . 39 TYR N N 116.21 0.1 1 240 . 39 TYR H H 9.23 0.02 1 241 . 39 TYR C C 175.6 0.1 1 242 . 39 TYR CA C 56.39 0.1 1 243 . 39 TYR HA H 5.77 0.02 1 244 . 39 TYR CB C 43.59 0.1 1 245 . 39 TYR HB2 H 2.80 0.02 2 246 . 39 TYR HB3 H 3.02 0.02 2 247 . 40 THR N N 116.47 0.1 1 248 . 40 THR H H 9.11 0.02 1 249 . 40 THR C C 171.1 0.1 1 250 . 40 THR CA C 62.68 0.1 1 251 . 40 THR HA H 5.10 0.02 1 252 . 40 THR CB C 73.29 0.1 1 253 . 41 LEU N N 128.79 0.1 1 254 . 41 LEU H H 8.00 0.02 1 255 . 41 LEU C C 173.9 0.1 1 256 . 41 LEU CA C 53.19 0.1 1 257 . 41 LEU HA H 5.19 0.02 1 258 . 41 LEU CB C 45.83 0.1 1 259 . 42 LEU N N 125.71 0.1 1 260 . 42 LEU H H 9.50 0.02 1 261 . 42 LEU C C 176.4 0.1 1 262 . 42 LEU CA C 54.18 0.1 1 263 . 42 LEU HA H 5.64 0.02 1 264 . 42 LEU CB C 46.36 0.1 1 265 . 42 LEU HB2 H 1.46 0.02 2 266 . 42 LEU HB3 H 1.51 0.02 2 267 . 43 TYR N N 114.84 0.1 1 268 . 43 TYR H H 9.00 0.02 1 269 . 43 TYR C C 173.9 0.1 1 270 . 43 TYR CA C 57.20 0.1 1 271 . 43 TYR HA H 5.98 0.02 1 272 . 43 TYR CB C 42.76 0.1 1 273 . 43 TYR HB2 H 3.58 0.02 2 274 . 44 THR N N 114.03 0.1 1 275 . 44 THR H H 9.14 0.02 1 276 . 44 THR C C 175.5 0.1 1 277 . 44 THR CA C 58.93 0.1 1 278 . 44 THR HA H 4.38 0.02 1 279 . 44 THR CB C 70.67 0.1 1 280 . 44 THR HB H 4.07 0.02 1 281 . 45 ILE N N 118.49 0.1 1 282 . 45 ILE H H 8.42 0.02 1 283 . 45 ILE C C 177.8 0.1 1 284 . 45 ILE CA C 59.99 0.1 1 285 . 45 ILE HA H 4.93 0.02 1 286 . 45 ILE CB C 39.94 0.1 1 287 . 45 ILE HB H 1.80 0.02 1 288 . 46 MET N N 123.20 0.1 1 289 . 46 MET H H 8.36 0.02 1 290 . 46 MET C C 176.6 0.1 1 291 . 46 MET CA C 58.70 0.1 1 292 . 46 MET HA H 3.80 0.02 1 293 . 46 MET CB C 32.77 0.1 1 294 . 47 SER N N 109.49 0.1 1 295 . 47 SER H H 7.90 0.02 1 296 . 47 SER C C 174.6 0.1 1 297 . 47 SER CA C 59.08 0.1 1 298 . 47 SER HA H 4.20 0.02 1 299 . 47 SER CB C 62.68 0.1 1 300 . 47 SER HB2 H 3.89 0.02 2 301 . 47 SER HB3 H 4.01 0.02 2 302 . 48 LYS N N 121.75 0.1 1 303 . 48 LYS H H 7.62 0.02 1 304 . 48 LYS CA C 53.90 0.1 1 305 . 48 LYS HA H 4.83 0.02 1 306 . 48 LYS CB C 33.04 0.1 1 307 . 49 PRO C C 177.1 0.1 1 308 . 49 PRO CA C 64.90 0.1 1 309 . 49 PRO HA H 4.29 0.02 1 310 . 49 PRO CB C 31.63 0.1 1 311 . 49 PRO HB2 H 1.97 0.02 2 312 . 49 PRO HB3 H 2.19 0.02 2 313 . 50 GLU N N 117.77 0.1 1 314 . 50 GLU H H 8.87 0.02 1 315 . 50 GLU C C 176.6 0.1 1 316 . 50 GLU CA C 56.44 0.1 1 317 . 50 GLU HA H 4.33 0.02 1 318 . 50 GLU CB C 29.73 0.1 1 319 . 50 GLU HB2 H 1.92 0.02 2 320 . 50 GLU HB3 H 2.13 0.02 2 321 . 51 ASP N N 121.61 0.1 1 322 . 51 ASP H H 7.52 0.02 1 323 . 51 ASP C C 174.8 0.1 1 324 . 51 ASP CA C 53.72 0.1 1 325 . 51 ASP HA H 4.75 0.02 1 326 . 51 ASP CB C 41.08 0.1 1 327 . 51 ASP HB2 H 2.41 0.02 2 328 . 51 ASP HB3 H 2.79 0.02 2 329 . 52 LEU N N 120.78 0.1 1 330 . 52 LEU H H 7.39 0.02 1 331 . 52 LEU C C 176.6 0.1 1 332 . 52 LEU CA C 56.23 0.1 1 333 . 52 LEU HA H 3.83 0.02 1 334 . 52 LEU CB C 43.04 0.1 1 335 . 52 LEU HB2 H 1.35 0.02 2 336 . 52 LEU HB3 H 1.51 0.02 2 337 . 53 LYS N N 124.86 0.1 1 338 . 53 LYS H H 8.54 0.02 1 339 . 53 LYS C C 175.1 0.1 1 340 . 53 LYS CA C 54.53 0.1 1 341 . 53 LYS HA H 4.58 0.02 1 342 . 53 LYS CB C 34.87 0.1 1 343 . 53 LYS HB2 H 1.55 0.02 2 344 . 54 VAL N N 121.94 0.1 1 345 . 54 VAL H H 8.27 0.02 1 346 . 54 VAL C C 176.6 0.1 1 347 . 54 VAL CA C 62.33 0.1 1 348 . 54 VAL HA H 4.19 0.02 1 349 . 54 VAL CB C 32.98 0.1 1 350 . 54 VAL HB H 1.92 0.02 1 351 . 55 VAL N N 128.35 0.1 1 352 . 55 VAL H H 8.32 0.02 1 353 . 55 VAL CA C 62.55 0.1 1 354 . 55 VAL HA H 4.00 0.02 1 355 . 55 VAL CB C 31.28 0.1 1 356 . 57 ASN C C 175.5 0.1 1 357 . 57 ASN CA C 54.36 0.1 1 358 . 57 ASN HA H 4.76 0.02 1 359 . 57 ASN CB C 37.70 0.1 1 360 . 57 ASN HB2 H 2.97 0.02 2 361 . 58 CYS N N 118.84 0.1 1 362 . 58 CYS H H 8.39 0.02 1 363 . 58 CYS C C 170.4 0.1 1 364 . 58 CYS CA C 52.95 0.1 1 365 . 58 CYS HA H 4.66 0.02 1 366 . 58 CYS CB C 43.74 0.1 1 367 . 59 ALA N N 120.63 0.1 1 368 . 59 ALA H H 7.24 0.02 1 369 . 59 ALA C C 176.8 0.1 1 370 . 59 ALA CA C 51.68 0.1 1 371 . 59 ALA HA H 4.84 0.02 1 372 . 59 ALA CB C 19.98 0.1 1 373 . 59 ALA HB H 1.35 0.02 1 374 . 60 ASN N N 123.39 0.1 1 375 . 60 ASN H H 9.15 0.02 1 376 . 60 ASN C C 174.8 0.1 1 377 . 60 ASN CA C 54.46 0.1 1 378 . 60 ASN HA H 4.17 0.02 1 379 . 60 ASN CB C 36.89 0.1 1 380 . 60 ASN HB2 H 2.58 0.02 2 381 . 60 ASN HB3 H 2.67 0.02 2 382 . 61 THR N N 112.90 0.1 1 383 . 61 THR H H 8.95 0.02 1 384 . 61 THR C C 174.0 0.1 1 385 . 61 THR CA C 59.85 0.1 1 386 . 61 THR HA H 4.94 0.02 1 387 . 61 THR CB C 70.90 0.1 1 388 . 62 THR N N 115.57 0.1 1 389 . 62 THR H H 8.35 0.02 1 390 . 62 THR C C 175.5 0.1 1 391 . 62 THR CA C 61.98 0.1 1 392 . 62 THR HA H 4.72 0.02 1 393 . 62 THR CB C 69.34 0.1 1 394 . 62 THR HB H 4.64 0.02 1 395 . 63 ARG N N 123.16 0.1 1 396 . 63 ARG H H 8.16 0.02 1 397 . 63 ARG C C 174.0 0.1 1 398 . 63 ARG CA C 55.17 0.1 1 399 . 63 ARG HA H 4.37 0.02 1 400 . 63 ARG CB C 31.49 0.1 1 401 . 63 ARG HB2 H 1.31 0.02 2 402 . 63 ARG HB3 H 1.48 0.02 2 403 . 64 SER N N 112.37 0.1 1 404 . 64 SER H H 7.79 0.02 1 405 . 64 SER CA C 55.68 0.1 1 406 . 64 SER HA H 4.22 0.02 1 407 . 64 SER CB C 62.35 0.1 1 408 . 65 PHE N N 112.00 0.1 1 409 . 65 PHE H H 6.15 0.02 1 410 . 65 PHE C C 173.0 0.1 1 411 . 65 PHE CA C 54.96 0.1 1 412 . 65 PHE HA H 4.50 0.02 1 413 . 65 PHE CB C 40.62 0.1 1 414 . 65 PHE HB2 H 2.53 0.02 2 415 . 66 CYS N N 117.12 0.1 1 416 . 66 CYS H H 9.39 0.02 1 417 . 66 CYS C C 172.0 0.1 1 418 . 66 CYS CA C 54.86 0.1 1 419 . 66 CYS HA H 4.68 0.02 1 420 . 66 CYS CB C 44.08 0.1 1 421 . 66 CYS HB2 H 2.71 0.02 2 422 . 67 ASP N N 128.35 0.1 1 423 . 67 ASP H H 8.80 0.02 1 424 . 67 ASP C C 176.1 0.1 1 425 . 67 ASP CA C 53.57 0.1 1 426 . 67 ASP HA H 4.92 0.02 1 427 . 67 ASP CB C 40.76 0.1 1 428 . 67 ASP HB2 H 2.06 0.02 2 429 . 67 ASP HB3 H 2.35 0.02 2 430 . 68 LEU N N 129.83 0.1 1 431 . 68 LEU H H 8.77 0.02 1 432 . 68 LEU C C 177.4 0.1 1 433 . 68 LEU CA C 53.79 0.1 1 434 . 68 LEU HA H 4.14 0.02 1 435 . 68 LEU CB C 41.19 0.1 1 436 . 69 THR N N 120.36 0.1 1 437 . 69 THR H H 8.66 0.02 1 438 . 69 THR C C 174.8 0.1 1 439 . 69 THR CA C 68.05 0.1 1 440 . 69 THR HA H 3.71 0.02 1 441 . 69 THR CB C 69.75 0.1 1 442 . 69 THR HB H 3.93 0.02 1 443 . 70 ASP N N 114.89 0.1 1 444 . 70 ASP H H 8.32 0.02 1 445 . 70 ASP C C 175.8 0.1 1 446 . 70 ASP CA C 55.21 0.1 1 447 . 70 ASP HA H 4.54 0.02 1 448 . 70 ASP CB C 40.84 0.1 1 449 . 70 ASP HB2 H 2.46 0.02 2 450 . 70 ASP HB3 H 2.71 0.02 2 451 . 71 GLU N N 117.65 0.1 1 452 . 71 GLU H H 7.47 0.02 1 453 . 71 GLU C C 176.2 0.1 1 454 . 71 GLU CA C 57.13 0.1 1 455 . 71 GLU HA H 4.37 0.02 1 456 . 71 GLU CB C 31.18 0.1 1 457 . 72 TRP N N 121.45 0.1 1 458 . 72 TRP H H 8.00 0.02 1 459 . 72 TRP C C 175.1 0.1 1 460 . 72 TRP CA C 54.22 0.1 1 461 . 72 TRP HA H 4.89 0.02 1 462 . 72 TRP CB C 27.70 0.1 1 463 . 73 ARG N N 118.84 0.1 1 464 . 73 ARG H H 7.61 0.02 1 465 . 73 ARG C C 176.1 0.1 1 466 . 73 ARG CA C 55.68 0.1 1 467 . 73 ARG HA H 4.36 0.02 1 468 . 73 ARG CB C 30.31 0.1 1 469 . 73 ARG HB2 H 2.05 0.02 2 470 . 74 SER N N 112.11 0.1 1 471 . 74 SER H H 7.84 0.02 1 472 . 74 SER CA C 56.68 0.1 1 473 . 74 SER HA H 3.84 0.02 1 474 . 74 SER CB C 64.40 0.1 1 475 . 76 HIS C C 174.6 0.1 1 476 . 76 HIS CA C 56.65 0.1 1 477 . 76 HIS HA H 4.60 0.02 1 478 . 76 HIS CB C 31.01 0.1 1 479 . 76 HIS HB2 H 2.96 0.02 2 480 . 76 HIS HB3 H 3.17 0.02 2 481 . 77 GLU N N 118.55 0.1 1 482 . 77 GLU H H 6.90 0.02 1 483 . 77 GLU C C 173.4 0.1 1 484 . 77 GLU CA C 54.48 0.1 1 485 . 77 GLU HA H 4.28 0.02 1 486 . 77 GLU CB C 31.95 0.1 1 487 . 77 GLU HB2 H 1.30 0.02 2 488 . 77 GLU HB3 H 1.47 0.02 2 489 . 78 ALA N N 124.84 0.1 1 490 . 78 ALA H H 8.01 0.02 1 491 . 78 ALA C C 176.0 0.1 1 492 . 78 ALA CA C 50.66 0.1 1 493 . 78 ALA HA H 4.35 0.02 1 494 . 78 ALA CB C 18.71 0.1 1 495 . 78 ALA HB H 0.55 0.02 1 496 . 79 TYR N N 120.15 0.1 1 497 . 79 TYR H H 8.36 0.02 1 498 . 79 TYR C C 175.7 0.1 1 499 . 79 TYR CA C 57.95 0.1 1 500 . 79 TYR HA H 4.63 0.02 1 501 . 79 TYR CB C 41.01 0.1 1 502 . 80 VAL N N 125.88 0.1 1 503 . 80 VAL H H 8.77 0.02 1 504 . 80 VAL C C 175.9 0.1 1 505 . 80 VAL CA C 61.88 0.1 1 506 . 80 VAL HA H 4.50 0.02 1 507 . 80 VAL CB C 33.01 0.1 1 508 . 81 THR N N 119.67 0.1 1 509 . 81 THR H H 8.76 0.02 1 510 . 81 THR C C 173.6 0.1 1 511 . 81 THR CA C 61.48 0.1 1 512 . 81 THR HA H 5.28 0.02 1 513 . 81 THR CB C 71.32 0.1 1 514 . 81 THR HB H 4.16 0.02 1 515 . 82 VAL N N 125.26 0.1 1 516 . 82 VAL H H 9.01 0.02 1 517 . 82 VAL C C 172.7 0.1 1 518 . 82 VAL CA C 61.68 0.1 1 519 . 82 VAL HA H 4.64 0.02 1 520 . 82 VAL CB C 35.35 0.1 1 521 . 82 VAL HB H 1.82 0.02 1 522 . 83 LEU N N 128.56 0.1 1 523 . 83 LEU H H 9.22 0.02 1 524 . 83 LEU C C 174.7 0.1 1 525 . 83 LEU CA C 52.66 0.1 1 526 . 83 LEU HA H 5.02 0.02 1 527 . 83 LEU CB C 46.25 0.1 1 528 . 84 GLU N N 125.85 0.1 1 529 . 84 GLU H H 8.93 0.02 1 530 . 84 GLU C C 175.0 0.1 1 531 . 84 GLU CA C 54.45 0.1 1 532 . 84 GLU HA H 4.61 0.02 1 533 . 84 GLU CB C 32.60 0.1 1 534 . 85 GLY N N 106.49 0.1 1 535 . 85 GLY H H 6.76 0.02 1 536 . 85 GLY C C 171.7 0.1 1 537 . 85 GLY CA C 43.44 0.1 1 538 . 85 GLY HA2 H 3.94 0.02 1 539 . 85 GLY HA3 H 3.94 0.02 1 540 . 86 PHE N N 120.05 0.1 1 541 . 86 PHE H H 8.10 0.02 1 542 . 86 PHE C C 175.4 0.1 1 543 . 86 PHE CA C 56.78 0.1 1 544 . 86 PHE HA H 4.99 0.02 1 545 . 86 PHE HB2 H 2.75 0.02 2 546 . 87 SER N N 113.97 0.1 1 547 . 87 SER H H 8.48 0.02 1 548 . 87 SER CA C 56.72 0.1 1 549 . 87 SER HA H 4.88 0.02 1 550 . 87 SER CB C 63.36 0.1 1 551 . 89 ASN C C 175.2 0.1 1 552 . 89 ASN CA C 53.30 0.1 1 553 . 89 ASN HA H 4.72 0.02 1 554 . 89 ASN CB C 38.73 0.1 1 555 . 89 ASN HB2 H 2.75 0.02 2 556 . 89 ASN HB3 H 2.91 0.02 2 557 . 90 THR N N 117.56 0.1 1 558 . 90 THR H H 8.15 0.02 1 559 . 90 THR C C 173.6 0.1 1 560 . 90 THR CA C 62.26 0.1 1 561 . 90 THR HA H 4.41 0.02 1 562 . 90 THR CB C 70.77 0.1 1 563 . 90 THR HB H 4.24 0.02 1 564 . 91 THR N N 124.31 0.1 1 565 . 91 THR H H 8.85 0.02 1 566 . 91 THR C C 173.8 0.1 1 567 . 91 THR CA C 63.50 0.1 1 568 . 91 THR HA H 3.88 0.02 1 569 . 91 THR CB C 68.49 0.1 1 570 . 92 LEU N N 128.27 0.1 1 571 . 92 LEU H H 8.94 0.02 1 572 . 92 LEU C C 176.3 0.1 1 573 . 92 LEU CA C 55.60 0.1 1 574 . 92 LEU HA H 4.25 0.02 1 575 . 92 LEU CB C 44.48 0.1 1 576 . 92 LEU HB2 H 1.18 0.02 2 577 . 92 LEU HB3 H 1.40 0.02 2 578 . 93 PHE N N 110.95 0.1 1 579 . 93 PHE H H 6.88 0.02 1 580 . 93 PHE C C 172.4 0.1 1 581 . 93 PHE CA C 56.30 0.1 1 582 . 93 PHE HA H 4.75 0.02 1 583 . 93 PHE CB C 40.32 0.1 1 584 . 94 SER N N 113.02 0.1 1 585 . 94 SER H H 8.27 0.02 1 586 . 94 SER C C 173.9 0.1 1 587 . 94 SER CA C 56.82 0.1 1 588 . 94 SER HA H 5.31 0.02 1 589 . 94 SER CB C 64.76 0.1 1 590 . 94 SER HB2 H 3.59 0.02 2 591 . 95 CYS N N 123.68 0.1 1 592 . 95 CYS H H 9.63 0.02 1 593 . 95 CYS C C 172.7 0.1 1 594 . 95 CYS CA C 53.96 0.1 1 595 . 95 CYS HA H 5.11 0.02 1 596 . 95 CYS CB C 47.06 0.1 1 597 . 96 SER N N 117.77 0.1 1 598 . 96 SER H H 9.01 0.02 1 599 . 96 SER C C 173.5 0.1 1 600 . 96 SER CA C 56.50 0.1 1 601 . 96 SER HA H 5.83 0.02 1 602 . 96 SER CB C 66.49 0.1 1 603 . 96 SER HB2 H 3.76 0.02 2 604 . 97 HIS N N 122.30 0.1 1 605 . 97 HIS H H 8.58 0.02 1 606 . 97 HIS CA C 56.31 0.1 1 607 . 97 HIS HA H 4.33 0.02 1 608 . 97 HIS CB C 33.95 0.1 1 609 . 98 ASN C C 174.0 0.1 1 610 . 98 ASN CA C 51.30 0.1 1 611 . 98 ASN HA H 5.53 0.02 1 612 . 98 ASN CB C 39.85 0.1 1 613 . 98 ASN HB2 H 2.10 0.02 2 614 . 98 ASN HB3 H 2.40 0.02 2 615 . 99 PHE N N 119.06 0.1 1 616 . 99 PHE H H 8.94 0.02 1 617 . 99 PHE C C 175.0 0.1 1 618 . 99 PHE CA C 57.61 0.1 1 619 . 99 PHE HA H 5.03 0.02 1 620 . 99 PHE CB C 44.19 0.1 1 621 . 99 PHE HB2 H 2.62 0.02 2 622 . 100 TRP N N 124.80 0.1 1 623 . 100 TRP H H 9.62 0.02 1 624 . 100 TRP C C 177.5 0.1 1 625 . 100 TRP CA C 56.29 0.1 1 626 . 100 TRP HA H 4.98 0.02 1 627 . 100 TRP CB C 29.28 0.1 1 628 . 101 LEU N N 125.67 0.1 1 629 . 101 LEU H H 9.38 0.02 1 630 . 101 LEU C C 177.1 0.1 1 631 . 101 LEU CA C 59.83 0.1 1 632 . 101 LEU HA H 3.94 0.02 1 633 . 101 LEU CB C 41.48 0.1 1 634 . 101 LEU HB2 H 1.83 0.02 2 635 . 101 LEU HB3 H 1.92 0.02 2 636 . 102 ALA N N 116.18 0.1 1 637 . 102 ALA H H 8.40 0.02 1 638 . 102 ALA C C 177.6 0.1 1 639 . 102 ALA CA C 54.68 0.1 1 640 . 102 ALA HA H 4.17 0.02 1 641 . 102 ALA CB C 18.65 0.1 1 642 . 102 ALA HB H 1.36 0.02 1 643 . 103 ILE N N 111.72 0.1 1 644 . 103 ILE H H 7.25 0.02 1 645 . 103 ILE C C 177.0 0.1 1 646 . 103 ILE CA C 61.71 0.1 1 647 . 103 ILE HA H 4.41 0.02 1 648 . 103 ILE CB C 40.38 0.1 1 649 . 103 ILE HB H 1.91 0.02 1 650 . 104 ASP N N 118.11 0.1 1 651 . 104 ASP H H 8.56 0.02 1 652 . 104 ASP C C 176.6 0.1 1 653 . 104 ASP CA C 56.58 0.1 1 654 . 104 ASP HA H 4.28 0.02 1 655 . 104 ASP CB C 43.74 0.1 1 656 . 104 ASP HB2 H 1.70 0.02 2 657 . 104 ASP HB3 H 2.05 0.02 2 658 . 105 MET N N 118.82 0.1 1 659 . 105 MET H H 7.64 0.02 1 660 . 105 MET C C 174.9 0.1 1 661 . 105 MET CA C 56.18 0.1 1 662 . 105 MET HA H 4.73 0.02 1 663 . 105 MET CB C 34.08 0.1 1 664 . 105 MET HB2 H 2.48 0.02 2 665 . 105 MET HB3 H 3.02 0.02 2 666 . 106 SER N N 119.13 0.1 1 667 . 106 SER H H 7.63 0.02 1 668 . 106 SER C C 173.5 0.1 1 669 . 106 SER CA C 56.27 0.1 1 670 . 106 SER HA H 4.50 0.02 1 671 . 106 SER CB C 64.49 0.1 1 672 . 106 SER HB2 H 3.79 0.02 2 673 . 107 PHE N N 122.47 0.1 1 674 . 107 PHE H H 9.06 0.02 1 675 . 107 PHE C C 175.7 0.1 1 676 . 107 PHE CA C 56.62 0.1 1 677 . 107 PHE HA H 4.76 0.02 1 678 . 107 PHE CB C 39.21 0.1 1 679 . 108 GLU N N 126.71 0.1 1 680 . 108 GLU H H 8.04 0.02 1 681 . 108 GLU CA C 56.07 0.1 1 682 . 108 GLU CB C 28.36 0.1 1 683 . 110 PRO C C 175.9 0.1 1 684 . 110 PRO CA C 61.57 0.1 1 685 . 110 PRO HA H 4.67 0.02 1 686 . 110 PRO CB C 31.95 0.1 1 687 . 110 PRO HB2 H 1.92 0.02 2 688 . 110 PRO HB3 H 2.05 0.02 2 689 . 111 GLU N N 119.17 0.1 1 690 . 111 GLU H H 8.52 0.02 1 691 . 111 GLU C C 175.5 0.1 1 692 . 111 GLU CA C 56.30 0.1 1 693 . 111 GLU HA H 4.45 0.02 1 694 . 111 GLU CB C 30.83 0.1 1 695 . 111 GLU HB2 H 1.92 0.02 2 696 . 111 GLU HB3 H 2.01 0.02 2 697 . 112 PHE N N 117.12 0.1 1 698 . 112 PHE H H 8.40 0.02 1 699 . 112 PHE C C 172.5 0.1 1 700 . 112 PHE CA C 55.75 0.1 1 701 . 112 PHE HA H 5.66 0.02 1 702 . 112 PHE CB C 42.33 0.1 1 703 . 112 PHE HB2 H 2.80 0.02 2 704 . 112 PHE HB3 H 2.97 0.02 2 705 . 113 GLU N N 119.18 0.1 1 706 . 113 GLU H H 9.10 0.02 1 707 . 113 GLU C C 175.0 0.1 1 708 . 113 GLU CA C 54.28 0.1 1 709 . 113 GLU HA H 4.39 0.02 1 710 . 113 GLU CB C 34.42 0.1 1 711 . 113 GLU HB2 H 1.70 0.02 2 712 . 114 ILE N N 113.51 0.1 1 713 . 114 ILE H H 8.67 0.02 1 714 . 114 ILE C C 174.9 0.1 1 715 . 114 ILE CA C 58.74 0.1 1 716 . 114 ILE HA H 5.69 0.02 1 717 . 114 ILE CB C 42.22 0.1 1 718 . 114 ILE HB H 1.62 0.02 1 719 . 115 VAL N N 121.61 0.1 1 720 . 115 VAL H H 8.43 0.02 1 721 . 115 VAL C C 174.8 0.1 1 722 . 115 VAL CA C 61.93 0.1 1 723 . 115 VAL HA H 4.08 0.02 1 724 . 115 VAL CB C 35.32 0.1 1 725 . 115 VAL HB H 1.93 0.02 1 726 . 116 GLY N N 113.40 0.1 1 727 . 116 GLY H H 8.63 0.02 1 728 . 116 GLY C C 171.4 0.1 1 729 . 116 GLY CA C 45.34 0.1 1 730 . 116 GLY HA2 H 3.44 0.02 1 731 . 116 GLY HA3 H 4.28 0.02 1 732 . 117 PHE N N 124.55 0.1 1 733 . 117 PHE H H 8.48 0.02 1 734 . 117 PHE C C 174.2 0.1 1 735 . 117 PHE CA C 56.74 0.1 1 736 . 117 PHE HA H 4.46 0.02 1 737 . 117 PHE CB C 40.04 0.1 1 738 . 118 THR N N 111.59 0.1 1 739 . 118 THR H H 7.92 0.02 1 740 . 118 THR CA C 66.14 0.1 1 741 . 118 THR CB C 69.30 0.1 1 742 . 119 ASN C C 174.7 0.1 1 743 . 119 ASN CA C 51.65 0.1 1 744 . 119 ASN HA H 4.73 0.02 1 745 . 119 ASN CB C 40.06 0.1 1 746 . 119 ASN HB2 H 2.93 0.02 2 747 . 119 ASN HB3 H 2.97 0.02 2 748 . 120 HIS N N 113.63 0.1 1 749 . 120 HIS H H 7.31 0.02 1 750 . 120 HIS C C 171.6 0.1 1 751 . 120 HIS CA C 55.99 0.1 1 752 . 120 HIS HA H 5.09 0.02 1 753 . 120 HIS CB C 32.07 0.1 1 754 . 121 ILE N N 117.74 0.1 1 755 . 121 ILE H H 8.78 0.02 1 756 . 121 ILE C C 174.6 0.1 1 757 . 121 ILE CA C 59.63 0.1 1 758 . 121 ILE HA H 4.76 0.02 1 759 . 121 ILE CB C 43.79 0.1 1 760 . 121 ILE HB H 1.27 0.02 1 761 . 122 ASN N N 125.72 0.1 1 762 . 122 ASN H H 8.98 0.02 1 763 . 122 ASN C C 174.1 0.1 1 764 . 122 ASN CA C 52.22 0.1 1 765 . 122 ASN HA H 5.06 0.02 1 766 . 122 ASN CB C 39.45 0.1 1 767 . 122 ASN HB2 H 2.63 0.02 2 768 . 122 ASN HB3 H 2.79 0.02 2 769 . 123 VAL N N 126.37 0.1 1 770 . 123 VAL H H 9.34 0.02 1 771 . 123 VAL C C 173.8 0.1 1 772 . 123 VAL CA C 61.48 0.1 1 773 . 123 VAL HA H 4.64 0.02 1 774 . 123 VAL CB C 32.61 0.1 1 775 . 123 VAL HB H 2.67 0.02 1 776 . 124 MET N N 127.72 0.1 1 777 . 124 MET H H 9.14 0.02 1 778 . 124 MET C C 175.1 0.1 1 779 . 124 MET CA C 54.45 0.1 1 780 . 124 MET HA H 5.22 0.02 1 781 . 124 MET CB C 34.25 0.1 1 782 . 124 MET HB2 H 1.92 0.02 2 783 . 125 VAL N N 127.23 0.1 1 784 . 125 VAL H H 9.62 0.02 1 785 . 125 VAL C C 174.7 0.1 1 786 . 125 VAL CA C 62.06 0.1 1 787 . 125 VAL HA H 4.24 0.02 1 788 . 125 VAL CB C 32.90 0.1 1 789 . 126 LYS N N 127.81 0.1 1 790 . 126 LYS H H 8.31 0.02 1 791 . 126 LYS C C 175.8 0.1 1 792 . 126 LYS CA C 55.13 0.1 1 793 . 126 LYS HA H 4.57 0.02 1 794 . 126 LYS CB C 31.35 0.1 1 795 . 126 LYS HB2 H 1.57 0.02 2 796 . 126 LYS HB3 H 1.61 0.02 2 797 . 127 PHE N N 124.18 0.1 1 798 . 127 PHE H H 7.87 0.02 1 799 . 127 PHE CA C 56.27 0.1 1 800 . 127 PHE HA H 4.88 0.02 1 801 . 127 PHE CB C 37.23 0.1 1 802 . 129 SER C C 174.3 0.1 1 803 . 129 SER CA C 59.28 0.1 1 804 . 129 SER HA H 4.69 0.02 1 805 . 129 SER CB C 62.88 0.1 1 806 . 129 SER HB2 H 4.37 0.02 2 807 . 130 ILE N N 121.32 0.1 1 808 . 130 ILE H H 7.76 0.02 1 809 . 130 ILE C C 175.2 0.1 1 810 . 130 ILE CA C 60.01 0.1 1 811 . 130 ILE HA H 4.31 0.02 1 812 . 130 ILE CB C 40.64 0.1 1 813 . 130 ILE HB H 1.74 0.02 1 814 . 131 VAL N N 124.12 0.1 1 815 . 131 VAL H H 8.20 0.02 1 816 . 131 VAL C C 176.3 0.1 1 817 . 131 VAL CA C 61.90 0.1 1 818 . 131 VAL HA H 4.11 0.02 1 819 . 131 VAL CB C 32.56 0.1 1 820 . 131 VAL HB H 1.94 0.02 1 821 . 132 GLU N N 126.28 0.1 1 822 . 132 GLU H H 8.61 0.02 1 823 . 132 GLU C C 175.9 0.1 1 824 . 132 GLU CA C 58.42 0.1 1 825 . 132 GLU HA H 3.97 0.02 1 826 . 132 GLU CB C 29.95 0.1 1 827 . 132 GLU HB2 H 1.94 0.02 2 828 . 133 GLU N N 118.90 0.1 1 829 . 133 GLU H H 8.51 0.02 1 830 . 133 GLU C C 176.4 0.1 1 831 . 133 GLU CA C 57.89 0.1 1 832 . 133 GLU HA H 4.14 0.02 1 833 . 133 GLU CB C 29.86 0.1 1 834 . 133 GLU HB2 H 1.96 0.02 2 835 . 134 GLU N N 118.35 0.1 1 836 . 134 GLU H H 8.08 0.02 1 837 . 134 GLU C C 176.5 0.1 1 838 . 134 GLU CA C 56.35 0.1 1 839 . 134 GLU HA H 4.20 0.02 1 840 . 134 GLU CB C 30.18 0.1 1 841 . 134 GLU HB2 H 1.89 0.02 2 842 . 134 GLU HB3 H 2.06 0.02 2 843 . 135 LEU N N 122.77 0.1 1 844 . 135 LEU H H 7.88 0.02 1 845 . 135 LEU C C 177.4 0.1 1 846 . 135 LEU CA C 55.20 0.1 1 847 . 135 LEU HA H 4.27 0.02 1 848 . 135 LEU CB C 42.50 0.1 1 849 . 135 LEU HB2 H 1.63 0.02 2 850 . 136 GLN N N 121.63 0.1 1 851 . 136 GLN H H 8.75 0.02 1 852 . 136 GLN C C 174.7 0.1 1 853 . 136 GLN CA C 56.11 0.1 1 854 . 136 GLN HA H 4.16 0.02 1 855 . 136 GLN CB C 29.14 0.1 1 856 . 136 GLN HB2 H 1.66 0.02 2 857 . 136 GLN HB3 H 1.86 0.02 2 858 . 137 PHE N N 115.93 0.1 1 859 . 137 PHE H H 7.17 0.02 1 860 . 137 PHE CA C 56.35 0.1 1 861 . 137 PHE HA H 4.61 0.02 1 862 . 137 PHE CB C 41.65 0.1 1 863 . 138 ASP CA C 53.80 0.1 1 864 . 138 ASP CB C 40.28 0.1 1 865 . 139 LEU N N 122.71 0.1 1 866 . 139 LEU H H 7.79 0.02 1 867 . 139 LEU C C 176.2 0.1 1 868 . 139 LEU CA C 53.70 0.1 1 869 . 139 LEU HA H 4.68 0.02 1 870 . 139 LEU CB C 45.27 0.1 1 871 . 139 LEU HB2 H 1.09 0.02 2 872 . 139 LEU HB3 H 1.48 0.02 2 873 . 140 SER N N 115.22 0.1 1 874 . 140 SER H H 8.60 0.02 1 875 . 140 SER C C 172.4 0.1 1 876 . 140 SER CA C 57.13 0.1 1 877 . 140 SER HA H 4.59 0.02 1 878 . 140 SER CB C 64.61 0.1 1 879 . 140 SER HB2 H 3.63 0.02 2 880 . 141 LEU N N 125.84 0.1 1 881 . 141 LEU H H 7.99 0.02 1 882 . 141 LEU C C 174.1 0.1 1 883 . 141 LEU CA C 54.20 0.1 1 884 . 141 LEU HA H 4.65 0.02 1 885 . 141 LEU CB C 44.96 0.1 1 886 . 141 LEU HB2 H 1.66 0.02 2 887 . 142 VAL N N 127.21 0.1 1 888 . 142 VAL H H 8.90 0.02 1 889 . 142 VAL C C 174.0 0.1 1 890 . 142 VAL CA C 60.75 0.1 1 891 . 142 VAL HA H 4.42 0.02 1 892 . 142 VAL CB C 33.20 0.1 1 893 . 143 ILE N N 124.54 0.1 1 894 . 143 ILE H H 8.61 0.02 1 895 . 143 ILE C C 174.4 0.1 1 896 . 143 ILE CA C 59.95 0.1 1 897 . 143 ILE HA H 4.35 0.02 1 898 . 143 ILE CB C 40.49 0.1 1 899 . 143 ILE HB H 1.40 0.02 1 900 . 144 GLU N N 128.99 0.1 1 901 . 144 GLU H H 9.60 0.02 1 902 . 144 GLU C C 174.0 0.1 1 903 . 144 GLU CA C 55.54 0.1 1 904 . 144 GLU HA H 4.95 0.02 1 905 . 144 GLU CB C 32.46 0.1 1 906 . 144 GLU HB2 H 1.97 0.02 2 907 . 145 GLU N N 126.58 0.1 1 908 . 145 GLU H H 9.12 0.02 1 909 . 145 GLU C C 174.8 0.1 1 910 . 145 GLU CA C 54.37 0.1 1 911 . 145 GLU HA H 4.96 0.02 1 912 . 145 GLU CB C 33.03 0.1 1 913 . 146 GLN N N 125.47 0.1 1 914 . 146 GLN H H 9.57 0.02 1 915 . 146 GLN C C 175.4 0.1 1 916 . 146 GLN CA C 54.35 0.1 1 917 . 146 GLN HA H 5.52 0.02 1 918 . 146 GLN CB C 31.41 0.1 1 919 . 146 GLN HB2 H 1.84 0.02 2 920 . 146 GLN HB3 H 2.01 0.02 2 921 . 147 SER N N 117.97 0.1 1 922 . 147 SER H H 8.50 0.02 1 923 . 147 SER C C 174.6 0.1 1 924 . 147 SER CA C 58.11 0.1 1 925 . 147 SER HA H 4.45 0.02 1 926 . 147 SER CB C 64.55 0.1 1 927 . 147 SER HB2 H 3.64 0.02 2 928 . 148 GLU N N 123.61 0.1 1 929 . 148 GLU H H 9.07 0.02 1 930 . 148 GLU C C 176.3 0.1 1 931 . 148 GLU CA C 57.59 0.1 1 932 . 148 GLU HA H 3.90 0.02 1 933 . 148 GLU CB C 28.14 0.1 1 934 . 148 GLU HB2 H 2.00 0.02 2 935 . 148 GLU HB3 H 2.13 0.02 2 936 . 149 GLY N N 106.83 0.1 1 937 . 149 GLY H H 8.56 0.02 1 938 . 149 GLY C C 173.9 0.1 1 939 . 149 GLY CA C 45.50 0.1 1 940 . 149 GLY HA2 H 3.63 0.02 1 941 . 149 GLY HA3 H 4.11 0.02 1 942 . 150 ILE N N 122.50 0.1 1 943 . 150 ILE H H 8.15 0.02 1 944 . 150 ILE C C 175.1 0.1 1 945 . 150 ILE CA C 60.26 0.1 1 946 . 150 ILE HA H 4.33 0.02 1 947 . 150 ILE CB C 39.09 0.1 1 948 . 150 ILE HB H 2.04 0.02 1 949 . 151 VAL N N 126.91 0.1 1 950 . 151 VAL H H 8.30 0.02 1 951 . 151 VAL C C 175.6 0.1 1 952 . 151 VAL CA C 61.51 0.1 1 953 . 151 VAL HA H 4.82 0.02 1 954 . 151 VAL CB C 33.69 0.1 1 955 . 151 VAL HB H 1.90 0.02 1 956 . 152 LYS N N 128.41 0.1 1 957 . 152 LYS H H 9.24 0.02 1 958 . 152 LYS C C 174.5 0.1 1 959 . 152 LYS CA C 55.02 0.1 1 960 . 152 LYS HA H 4.58 0.02 1 961 . 152 LYS CB C 35.47 0.1 1 962 . 152 LYS HB2 H 1.61 0.02 2 963 . 153 LYS N N 122.97 0.1 1 964 . 153 LYS H H 8.55 0.02 1 965 . 153 LYS C C 175.1 0.1 1 966 . 153 LYS CA C 56.09 0.1 1 967 . 153 LYS HA H 4.54 0.02 1 968 . 153 LYS CB C 34.15 0.1 1 969 . 153 LYS HB2 H 1.44 0.02 2 970 . 153 LYS HB3 H 1.67 0.02 2 971 . 154 HIS N N 125.60 0.1 1 972 . 154 HIS H H 9.13 0.02 1 973 . 154 HIS C C 174.6 0.1 1 974 . 154 HIS CA C 55.67 0.1 1 975 . 154 HIS HA H 4.55 0.02 1 976 . 154 HIS CB C 32.60 0.1 1 977 . 155 LYS N N 122.99 0.1 1 978 . 155 LYS H H 8.74 0.02 1 979 . 155 LYS CA C 52.94 0.1 1 980 . 155 LYS HA H 5.21 0.02 1 981 . 155 LYS CB C 32.81 0.1 1 982 . 156 PRO C C 175.9 0.1 1 983 . 156 PRO CA C 63.99 0.1 1 984 . 156 PRO HA H 4.37 0.02 1 985 . 156 PRO CB C 35.01 0.1 1 986 . 157 GLU N N 122.35 0.1 1 987 . 157 GLU H H 8.67 0.02 1 988 . 157 GLU C C 176.2 0.1 1 989 . 157 GLU CA C 57.02 0.1 1 990 . 157 GLU HA H 4.30 0.02 1 991 . 157 GLU CB C 29.94 0.1 1 992 . 157 GLU HB2 H 2.05 0.02 2 993 . 158 ILE N N 122.90 0.1 1 994 . 158 ILE H H 8.15 0.02 1 995 . 158 ILE C C 175.4 0.1 1 996 . 158 ILE CA C 60.27 0.1 1 997 . 158 ILE HA H 4.18 0.02 1 998 . 158 ILE CB C 39.68 0.1 1 999 . 158 ILE HB H 1.53 0.02 1 1000 . 159 LYS N N 125.07 0.1 1 1001 . 159 LYS H H 8.06 0.02 1 1002 . 159 LYS C C 177.5 0.1 1 1003 . 159 LYS CA C 57.48 0.1 1 1004 . 159 LYS HA H 4.11 0.02 1 1005 . 159 LYS CB C 32.00 0.1 1 1006 . 159 LYS HB2 H 1.79 0.02 2 1007 . 160 GLY N N 114.41 0.1 1 1008 . 160 GLY H H 9.28 0.02 1 1009 . 160 GLY C C 174.0 0.1 1 1010 . 160 GLY CA C 45.38 0.1 1 1011 . 160 GLY HA2 H 3.69 0.02 1 1012 . 160 GLY HA3 H 4.07 0.02 1 1013 . 161 ASN N N 118.66 0.1 1 1014 . 161 ASN H H 8.33 0.02 1 1015 . 161 ASN C C 174.8 0.1 1 1016 . 161 ASN CA C 52.62 0.1 1 1017 . 161 ASN HA H 4.91 0.02 1 1018 . 161 ASN CB C 40.09 0.1 1 1019 . 161 ASN HB2 H 2.40 0.02 2 1020 . 161 ASN HB3 H 2.92 0.02 2 1021 . 162 MET N N 121.42 0.1 1 1022 . 162 MET H H 8.12 0.02 1 1023 . 162 MET C C 173.0 0.1 1 1024 . 162 MET CA C 55.38 0.1 1 1025 . 162 MET HA H 3.66 0.02 1 1026 . 162 MET HB2 H 1.22 0.02 2 1027 . 162 MET HB3 H 1.35 0.02 2 1028 . 163 SER N N 111.71 0.1 1 1029 . 163 SER H H 7.33 0.02 1 1030 . 163 SER C C 174.8 0.1 1 1031 . 163 SER CA C 57.01 0.1 1 1032 . 163 SER HA H 3.68 0.02 1 1033 . 163 SER CB C 64.74 0.1 1 1034 . 163 SER HB2 H 3.76 0.02 2 1035 . 164 GLY N N 112.73 0.1 1 1036 . 164 GLY H H 7.84 0.02 1 1037 . 164 GLY C C 172.5 0.1 1 1038 . 164 GLY CA C 45.08 0.1 1 1039 . 164 GLY HA2 H 3.72 0.02 1 1040 . 164 GLY HA3 H 4.10 0.02 1 1041 . 165 ASN N N 117.50 0.1 1 1042 . 165 ASN H H 8.18 0.02 1 1043 . 165 ASN C C 175.1 0.1 1 1044 . 165 ASN CA C 53.27 0.1 1 1045 . 165 ASN HA H 5.15 0.02 1 1046 . 165 ASN CB C 38.85 0.1 1 1047 . 165 ASN HB2 H 2.58 0.02 2 1048 . 165 ASN HB3 H 2.71 0.02 2 1049 . 166 PHE N N 127.77 0.1 1 1050 . 166 PHE H H 9.16 0.02 1 1051 . 166 PHE C C 173.9 0.1 1 1052 . 166 PHE CA C 57.38 0.1 1 1053 . 166 PHE HA H 4.87 0.02 1 1054 . 166 PHE CB C 42.34 0.1 1 1055 . 166 PHE HB2 H 3.02 0.02 2 1056 . 166 PHE HB3 H 3.45 0.02 2 1057 . 167 THR N N 123.43 0.1 1 1058 . 167 THR H H 7.95 0.02 1 1059 . 167 THR C C 172.3 0.1 1 1060 . 167 THR CA C 61.45 0.1 1 1061 . 167 THR HA H 5.18 0.02 1 1062 . 167 THR CB C 70.30 0.1 1 1063 . 167 THR HB H 3.73 0.02 1 1064 . 168 TYR N N 127.77 0.1 1 1065 . 168 TYR H H 9.21 0.02 1 1066 . 168 TYR C C 172.7 0.1 1 1067 . 168 TYR CA C 56.72 0.1 1 1068 . 168 TYR HA H 4.43 0.02 1 1069 . 168 TYR CB C 42.69 0.1 1 1070 . 168 TYR HB2 H 2.74 0.02 2 1071 . 169 ILE N N 127.52 0.1 1 1072 . 169 ILE H H 7.35 0.02 1 1073 . 169 ILE C C 174.8 0.1 1 1074 . 169 ILE CA C 59.89 0.1 1 1075 . 169 ILE HA H 4.51 0.02 1 1076 . 169 ILE CB C 38.79 0.1 1 1077 . 169 ILE HB H 1.35 0.02 1 1078 . 170 ILE N N 127.42 0.1 1 1079 . 170 ILE H H 8.73 0.02 1 1080 . 170 ILE C C 174.2 0.1 1 1081 . 170 ILE CA C 61.25 0.1 1 1082 . 170 ILE HA H 3.77 0.02 1 1083 . 170 ILE CB C 38.14 0.1 1 1084 . 171 ASP N N 125.88 0.1 1 1085 . 171 ASP H H 8.03 0.02 1 1086 . 171 ASP C C 174.0 0.1 1 1087 . 171 ASP CA C 51.73 0.1 1 1088 . 171 ASP HA H 4.93 0.02 1 1089 . 171 ASP CB C 43.04 0.1 1 1090 . 172 LYS N N 112.07 0.1 1 1091 . 172 LYS H H 8.58 0.02 1 1092 . 172 LYS C C 176.1 0.1 1 1093 . 172 LYS CA C 56.85 0.1 1 1094 . 172 LYS HA H 3.82 0.02 1 1095 . 172 LYS CB C 28.63 0.1 1 1096 . 172 LYS HB2 H 1.83 0.02 2 1097 . 172 LYS HB3 H 2.01 0.02 2 1098 . 173 LEU N N 117.67 0.1 1 1099 . 173 LEU H H 7.75 0.02 1 1100 . 173 LEU CA C 52.95 0.1 1 1101 . 173 LEU CB C 41.80 0.1 1 1102 . 174 ILE N N 120.93 0.1 1 1103 . 174 ILE H H 8.02 0.02 1 1104 . 174 ILE CA C 58.07 0.1 1 1105 . 174 ILE CB C 38.84 0.1 1 1106 . 175 PRO C C 178.2 0.1 1 1107 . 175 PRO CA C 62.98 0.1 1 1108 . 175 PRO CB C 32.85 0.1 1 1109 . 176 ASN N N 117.77 0.1 1 1110 . 176 ASN H H 8.06 0.02 1 1111 . 176 ASN C C 173.9 0.1 1 1112 . 176 ASN CA C 53.90 0.1 1 1113 . 176 ASN HA H 4.49 0.02 1 1114 . 176 ASN CB C 38.63 0.1 1 1115 . 176 ASN HB2 H 2.41 0.02 2 1116 . 176 ASN HB3 H 3.22 0.02 2 1117 . 177 THR N N 112.22 0.1 1 1118 . 177 THR H H 7.09 0.02 1 1119 . 177 THR C C 172.2 0.1 1 1120 . 177 THR CA C 61.98 0.1 1 1121 . 177 THR HA H 4.33 0.02 1 1122 . 177 THR CB C 71.10 0.1 1 1123 . 177 THR HB H 4.24 0.02 1 1124 . 178 ASN N N 124.56 0.1 1 1125 . 178 ASN H H 8.57 0.02 1 1126 . 178 ASN C C 174.2 0.1 1 1127 . 178 ASN CA C 53.29 0.1 1 1128 . 178 ASN HA H 5.25 0.02 1 1129 . 178 ASN CB C 40.46 0.1 1 1130 . 178 ASN HB2 H 2.46 0.02 2 1131 . 178 ASN HB3 H 2.58 0.02 2 1132 . 179 TYR N N 124.27 0.1 1 1133 . 179 TYR H H 8.88 0.02 1 1134 . 179 TYR C C 174.4 0.1 1 1135 . 179 TYR CA C 57.91 0.1 1 1136 . 179 TYR HA H 4.98 0.02 1 1137 . 179 TYR CB C 44.14 0.1 1 1138 . 180 CYS N N 116.78 0.1 1 1139 . 180 CYS H H 9.19 0.02 1 1140 . 180 CYS C C 172.7 0.1 1 1141 . 180 CYS CA C 55.09 0.1 1 1142 . 180 CYS HA H 5.55 0.02 1 1143 . 180 CYS CB C 48.66 0.1 1 1144 . 180 CYS HB2 H 2.82 0.02 2 1145 . 181 VAL N N 123.14 0.1 1 1146 . 181 VAL H H 9.56 0.02 1 1147 . 181 VAL C C 174.5 0.1 1 1148 . 181 VAL CA C 60.30 0.1 1 1149 . 181 VAL HA H 5.45 0.02 1 1150 . 181 VAL CB C 36.50 0.1 1 1151 . 181 VAL HB H 2.01 0.02 1 1152 . 182 SER N N 118.98 0.1 1 1153 . 182 SER H H 8.38 0.02 1 1154 . 182 SER C C 172.5 0.1 1 1155 . 182 SER CA C 56.48 0.1 1 1156 . 182 SER HA H 4.57 0.02 1 1157 . 182 SER CB C 66.29 0.1 1 1158 . 182 SER HB2 H 3.52 0.02 2 1159 . 182 SER HB3 H 3.80 0.02 2 1160 . 183 VAL N N 118.53 0.1 1 1161 . 183 VAL H H 8.29 0.02 1 1162 . 183 VAL C C 174.9 0.1 1 1163 . 183 VAL CA C 58.90 0.1 1 1164 . 183 VAL HA H 5.22 0.02 1 1165 . 183 VAL CB C 34.99 0.1 1 1166 . 183 VAL HB H 1.49 0.02 1 1167 . 184 TYR N N 115.07 0.1 1 1168 . 184 TYR H H 8.46 0.02 1 1169 . 184 TYR C C 172.7 0.1 1 1170 . 184 TYR CA C 56.35 0.1 1 1171 . 184 TYR HA H 4.78 0.02 1 1172 . 184 TYR CB C 40.37 0.1 1 1173 . 185 LEU N N 118.76 0.1 1 1174 . 185 LEU H H 9.15 0.02 1 1175 . 185 LEU C C 175.6 0.1 1 1176 . 185 LEU CA C 52.62 0.1 1 1177 . 185 LEU HA H 5.27 0.02 1 1178 . 185 LEU CB C 43.71 0.1 1 1179 . 185 LEU HB2 H 1.62 0.02 2 1180 . 186 GLU N N 121.39 0.1 1 1181 . 186 GLU H H 8.81 0.02 1 1182 . 186 GLU CA C 55.93 0.1 1 1183 . 186 GLU HA H 4.55 0.02 1 1184 . 186 GLU CB C 33.54 0.1 1 1185 . 189 ASP C C 176.8 0.1 1 1186 . 189 ASP CA C 53.97 0.1 1 1187 . 189 ASP HA H 4.71 0.02 1 1188 . 189 ASP CB C 41.27 0.1 1 1189 . 189 ASP HB2 H 2.88 0.02 2 1190 . 190 GLU N N 121.73 0.1 1 1191 . 190 GLU H H 8.50 0.02 1 1192 . 190 GLU C C 177.1 0.1 1 1193 . 190 GLU CA C 58.03 0.1 1 1194 . 190 GLU HA H 4.13 0.02 1 1195 . 190 GLU CB C 29.98 0.1 1 1196 . 190 GLU HB2 H 2.05 0.02 2 1197 . 191 GLN N N 117.57 0.1 1 1198 . 191 GLN H H 7.99 0.02 1 1199 . 191 GLN C C 175.9 0.1 1 1200 . 191 GLN CA C 56.15 0.1 1 1201 . 191 GLN HA H 4.24 0.02 1 1202 . 191 GLN CB C 29.53 0.1 1 1203 . 192 ALA N N 124.16 0.1 1 1204 . 192 ALA H H 8.10 0.02 1 1205 . 192 ALA C C 177.3 0.1 1 1206 . 192 ALA CA C 51.76 0.1 1 1207 . 192 ALA HA H 4.38 0.02 1 1208 . 192 ALA CB C 18.34 0.1 1 1209 . 192 ALA HB H 1.27 0.02 1 1210 . 193 VAL N N 116.86 0.1 1 1211 . 193 VAL H H 7.38 0.02 1 1212 . 193 VAL C C 175.5 0.1 1 1213 . 193 VAL CA C 61.51 0.1 1 1214 . 193 VAL HA H 4.33 0.02 1 1215 . 193 VAL CB C 34.03 0.1 1 1216 . 194 ILE N N 125.63 0.1 1 1217 . 194 ILE H H 8.64 0.02 1 1218 . 194 ILE C C 175.1 0.1 1 1219 . 194 ILE CA C 59.96 0.1 1 1220 . 194 ILE HA H 4.15 0.02 1 1221 . 194 ILE CB C 38.41 0.1 1 1222 . 194 ILE HB H 1.88 0.02 1 1223 . 195 LYS N N 125.33 0.1 1 1224 . 195 LYS H H 8.46 0.02 1 1225 . 195 LYS C C 177.3 0.1 1 1226 . 195 LYS CA C 56.47 0.1 1 1227 . 195 LYS HA H 4.42 0.02 1 1228 . 195 LYS CB C 32.92 0.1 1 1229 . 195 LYS HB2 H 1.79 0.02 2 1230 . 196 SER N N 117.63 0.1 1 1231 . 196 SER H H 8.09 0.02 1 1232 . 196 SER CA C 58.29 0.1 1 1233 . 196 SER CB C 62.67 0.1 1 1234 . 197 PRO C C 176.7 0.1 1 1235 . 197 PRO CA C 63.08 0.1 1 1236 . 197 PRO HA H 4.57 0.02 1 1237 . 197 PRO CB C 31.87 0.1 1 1238 . 197 PRO HB2 H 1.83 0.02 2 1239 . 197 PRO HB3 H 2.47 0.02 2 1240 . 198 LEU N N 123.80 0.1 1 1241 . 198 LEU H H 8.43 0.02 1 1242 . 198 LEU C C 178.4 0.1 1 1243 . 198 LEU CA C 55.26 0.1 1 1244 . 198 LEU HA H 4.69 0.02 1 1245 . 198 LEU CB C 43.58 0.1 1 1246 . 198 LEU HB2 H 1.66 0.02 2 1247 . 199 LYS N N 122.98 0.1 1 1248 . 199 LYS H H 8.98 0.02 1 1249 . 199 LYS C C 175.5 0.1 1 1250 . 199 LYS CA C 56.80 0.1 1 1251 . 199 LYS HA H 4.68 0.02 1 1252 . 199 LYS CB C 35.35 0.1 1 1253 . 200 CYS N N 120.55 0.1 1 1254 . 200 CYS H H 8.71 0.02 1 1255 . 200 CYS C C 173.7 0.1 1 1256 . 200 CYS CA C 55.30 0.1 1 1257 . 200 CYS HA H 5.99 0.02 1 1258 . 200 CYS CB C 49.00 0.1 1 1259 . 200 CYS HB2 H 3.09 0.02 2 1260 . 201 THR N N 117.90 0.1 1 1261 . 201 THR H H 9.38 0.02 1 1262 . 201 THR CA C 61.23 0.1 1 1263 . 201 THR HA H 4.61 0.02 1 1264 . 201 THR CB C 69.76 0.1 1 1265 . 202 LEU N N 128.90 0.1 1 1266 . 202 LEU H H 7.74 0.02 1 1267 . 202 LEU C C 177.1 0.1 1 1268 . 202 LEU CA C 53.58 0.1 1 1269 . 202 LEU HA H 4.78 0.02 1 1270 . 202 LEU CB C 43.05 0.1 1 1271 . 202 LEU HB2 H 1.70 0.02 2 1272 . 203 LEU N N 128.71 0.1 1 1273 . 203 LEU H H 8.33 0.02 1 1274 . 203 LEU CA C 53.96 0.1 1 1275 . 203 LEU CB C 37.96 0.1 1 1276 . 205 PRO C C 177.3 0.1 1 1277 . 205 PRO CA C 62.84 0.1 1 1278 . 205 PRO HA H 4.37 0.02 1 1279 . 205 PRO CB C 32.25 0.1 1 1280 . 205 PRO HB2 H 1.96 0.02 2 1281 . 205 PRO HB3 H 2.23 0.02 2 1282 . 206 GLY N N 107.32 0.1 1 1283 . 206 GLY H H 8.23 0.02 1 1284 . 206 GLY C C 176.5 0.1 1 1285 . 206 GLY CA C 45.07 0.1 1 1286 . 206 GLY HA2 H 3.84 0.02 1 1287 . 206 GLY HA3 H 4.05 0.02 1 1288 . 207 GLN N N 119.64 0.1 1 1289 . 207 GLN H H 8.29 0.02 1 1290 . 207 GLN C C 175.9 0.1 1 1291 . 207 GLN CA C 55.70 0.1 1 1292 . 207 GLN HA H 4.37 0.02 1 1293 . 207 GLN CB C 29.90 0.1 1 1294 . 207 GLN HB2 H 1.97 0.02 2 1295 . 207 GLN HB3 H 2.10 0.02 2 1296 . 208 GLU N N 122.42 0.1 1 1297 . 208 GLU H H 8.64 0.02 1 1298 . 208 GLU C C 176.5 0.1 1 1299 . 208 GLU CA C 56.98 0.1 1 1300 . 208 GLU HA H 4.25 0.02 1 1301 . 208 GLU CB C 29.94 0.1 1 1302 . 208 GLU HB2 H 1.93 0.02 2 1303 . 208 GLU HB3 H 2.05 0.02 2 1304 . 209 SER N N 116.09 0.1 1 1305 . 209 SER H H 8.26 0.02 1 1306 . 209 SER C C 174.3 0.1 1 1307 . 209 SER CA C 58.20 0.1 1 1308 . 209 SER HA H 4.40 0.02 1 1309 . 209 SER CB C 63.86 0.1 1 1310 . 209 SER HB2 H 3.80 0.02 2 1311 . 210 GLU N N 122.55 0.1 1 1312 . 210 GLU H H 8.35 0.02 1 1313 . 210 GLU C C 175.9 0.1 1 1314 . 210 GLU CA C 56.78 0.1 1 1315 . 210 GLU HA H 4.20 0.02 1 1316 . 210 GLU CB C 30.29 0.1 1 1317 . 210 GLU HB2 H 1.79 0.02 2 1318 . 211 PHE N N 120.29 0.1 1 1319 . 211 PHE H H 8.07 0.02 1 1320 . 211 PHE C C 174.9 0.1 1 1321 . 211 PHE CA C 57.30 0.1 1 1322 . 211 PHE HA H 4.72 0.02 1 1323 . 211 PHE CB C 39.64 0.1 1 1324 . 211 PHE HB2 H 2.97 0.02 2 1325 . 211 PHE HB3 H 3.23 0.02 2 1326 . 212 SER N N 122.53 0.1 1 1327 . 212 SER H H 7.76 0.02 1 1328 . 212 SER CA C 60.01 0.1 1 1329 . 212 SER HA H 4.22 0.02 1 1330 . 212 SER CB C 64.98 0.1 1 stop_ save_